data_8OTU
# 
_entry.id   8OTU 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8OTU         pdb_00008otu 10.2210/pdb8otu/pdb 
WWPDB D_1292129515 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_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                        8OTU 
_pdbx_database_status.recvd_initial_deposition_date   2023-04-21 
_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              sander.smits@hhu.de 
_pdbx_contact_author.name_first         Sander 
_pdbx_contact_author.name_last          Smits 
_pdbx_contact_author.name_mi            H.J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0780-9251 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Costanzi, E.'  1 0000-0002-3231-232X 
'Applegate, V.' 2 ?                   
'Smits, S.H.J.' 3 0000-0003-0780-9251 
# 
_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                     'The crystal structure of PET44, a PETase enzyme from Alkalilimnicola ehrlichii' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Costanzi, E.'  1 ? 
primary 'Applegate, V.' 2 ? 
primary 'Smits, S.H.J.' 3 ? 
# 
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 'Dienelactone hydrolase domain-containing protein' 34720.773 2   ? ? ? ? 
2 non-polymer syn 'SODIUM ION'                                       22.990    3   ? ? ? ? 
3 non-polymer syn 1,2-ETHANEDIOL                                     62.068    25  ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                     35.453    3   ? ? ? ? 
5 water       nat water                                              18.015    477 ? ? ? ? 
# 
_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       
;MSSIIKRKLASLFAFSAAMLLSTSVWSMNPGDVPDTCEGDCGYARGPDPTESFLEADSGPYTIATSNVSSLVRGFGGGTI
YYPVNAEGTMAAIVVIPGYMSYQSSISFWGPRLASHGFVVMTIDTNRISDQPPSRRDQIEAALEYLVDQSNSSRSPINGM
VDPNRLGAVGWSMGGGGTLRLAADDGIQAAIGLAPWNTSSLGFRSIETPTLIFACERDSIAPVRSHASPFYNAIPSSTDK
AYFEISGGNHYCANGSNRYDALLGKYGVAWMKLHLDQDQRYAPFLCGPNHERDRQISEHRSTCPFVDKLAAALEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MSSIIKRKLASLFAFSAAMLLSTSVWSMNPGDVPDTCEGDCGYARGPDPTESFLEADSGPYTIATSNVSSLVRGFGGGTI
YYPVNAEGTMAAIVVIPGYMSYQSSISFWGPRLASHGFVVMTIDTNRISDQPPSRRDQIEAALEYLVDQSNSSRSPINGM
VDPNRLGAVGWSMGGGGTLRLAADDGIQAAIGLAPWNTSSLGFRSIETPTLIFACERDSIAPVRSHASPFYNAIPSSTDK
AYFEISGGNHYCANGSNRYDALLGKYGVAWMKLHLDQDQRYAPFLCGPNHERDRQISEHRSTCPFVDKLAAALEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SODIUM ION'   NA  
3 1,2-ETHANEDIOL EDO 
4 'CHLORIDE ION' CL  
5 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   SER n 
1 3   SER n 
1 4   ILE n 
1 5   ILE n 
1 6   LYS n 
1 7   ARG n 
1 8   LYS n 
1 9   LEU n 
1 10  ALA n 
1 11  SER n 
1 12  LEU n 
1 13  PHE n 
1 14  ALA n 
1 15  PHE n 
1 16  SER n 
1 17  ALA n 
1 18  ALA n 
1 19  MET n 
1 20  LEU n 
1 21  LEU n 
1 22  SER n 
1 23  THR n 
1 24  SER n 
1 25  VAL n 
1 26  TRP n 
1 27  SER n 
1 28  MET n 
1 29  ASN n 
1 30  PRO n 
1 31  GLY n 
1 32  ASP n 
1 33  VAL n 
1 34  PRO n 
1 35  ASP n 
1 36  THR n 
1 37  CYS n 
1 38  GLU n 
1 39  GLY n 
1 40  ASP n 
1 41  CYS n 
1 42  GLY n 
1 43  TYR n 
1 44  ALA n 
1 45  ARG n 
1 46  GLY n 
1 47  PRO n 
1 48  ASP n 
1 49  PRO n 
1 50  THR n 
1 51  GLU n 
1 52  SER n 
1 53  PHE n 
1 54  LEU n 
1 55  GLU n 
1 56  ALA n 
1 57  ASP n 
1 58  SER n 
1 59  GLY n 
1 60  PRO n 
1 61  TYR n 
1 62  THR n 
1 63  ILE n 
1 64  ALA n 
1 65  THR n 
1 66  SER n 
1 67  ASN n 
1 68  VAL n 
1 69  SER n 
1 70  SER n 
1 71  LEU n 
1 72  VAL n 
1 73  ARG n 
1 74  GLY n 
1 75  PHE n 
1 76  GLY n 
1 77  GLY n 
1 78  GLY n 
1 79  THR n 
1 80  ILE n 
1 81  TYR n 
1 82  TYR n 
1 83  PRO n 
1 84  VAL n 
1 85  ASN n 
1 86  ALA n 
1 87  GLU n 
1 88  GLY n 
1 89  THR n 
1 90  MET n 
1 91  ALA n 
1 92  ALA n 
1 93  ILE n 
1 94  VAL n 
1 95  VAL n 
1 96  ILE n 
1 97  PRO n 
1 98  GLY n 
1 99  TYR n 
1 100 MET n 
1 101 SER n 
1 102 TYR n 
1 103 GLN n 
1 104 SER n 
1 105 SER n 
1 106 ILE n 
1 107 SER n 
1 108 PHE n 
1 109 TRP n 
1 110 GLY n 
1 111 PRO n 
1 112 ARG n 
1 113 LEU n 
1 114 ALA n 
1 115 SER n 
1 116 HIS n 
1 117 GLY n 
1 118 PHE n 
1 119 VAL n 
1 120 VAL n 
1 121 MET n 
1 122 THR n 
1 123 ILE n 
1 124 ASP n 
1 125 THR n 
1 126 ASN n 
1 127 ARG n 
1 128 ILE n 
1 129 SER n 
1 130 ASP n 
1 131 GLN n 
1 132 PRO n 
1 133 PRO n 
1 134 SER n 
1 135 ARG n 
1 136 ARG n 
1 137 ASP n 
1 138 GLN n 
1 139 ILE n 
1 140 GLU n 
1 141 ALA n 
1 142 ALA n 
1 143 LEU n 
1 144 GLU n 
1 145 TYR n 
1 146 LEU n 
1 147 VAL n 
1 148 ASP n 
1 149 GLN n 
1 150 SER n 
1 151 ASN n 
1 152 SER n 
1 153 SER n 
1 154 ARG n 
1 155 SER n 
1 156 PRO n 
1 157 ILE n 
1 158 ASN n 
1 159 GLY n 
1 160 MET n 
1 161 VAL n 
1 162 ASP n 
1 163 PRO n 
1 164 ASN n 
1 165 ARG n 
1 166 LEU n 
1 167 GLY n 
1 168 ALA n 
1 169 VAL n 
1 170 GLY n 
1 171 TRP n 
1 172 SER n 
1 173 MET n 
1 174 GLY n 
1 175 GLY n 
1 176 GLY n 
1 177 GLY n 
1 178 THR n 
1 179 LEU n 
1 180 ARG n 
1 181 LEU n 
1 182 ALA n 
1 183 ALA n 
1 184 ASP n 
1 185 ASP n 
1 186 GLY n 
1 187 ILE n 
1 188 GLN n 
1 189 ALA n 
1 190 ALA n 
1 191 ILE n 
1 192 GLY n 
1 193 LEU n 
1 194 ALA n 
1 195 PRO n 
1 196 TRP n 
1 197 ASN n 
1 198 THR n 
1 199 SER n 
1 200 SER n 
1 201 LEU n 
1 202 GLY n 
1 203 PHE n 
1 204 ARG n 
1 205 SER n 
1 206 ILE n 
1 207 GLU n 
1 208 THR n 
1 209 PRO n 
1 210 THR n 
1 211 LEU n 
1 212 ILE n 
1 213 PHE n 
1 214 ALA n 
1 215 CYS n 
1 216 GLU n 
1 217 ARG n 
1 218 ASP n 
1 219 SER n 
1 220 ILE n 
1 221 ALA n 
1 222 PRO n 
1 223 VAL n 
1 224 ARG n 
1 225 SER n 
1 226 HIS n 
1 227 ALA n 
1 228 SER n 
1 229 PRO n 
1 230 PHE n 
1 231 TYR n 
1 232 ASN n 
1 233 ALA n 
1 234 ILE n 
1 235 PRO n 
1 236 SER n 
1 237 SER n 
1 238 THR n 
1 239 ASP n 
1 240 LYS n 
1 241 ALA n 
1 242 TYR n 
1 243 PHE n 
1 244 GLU n 
1 245 ILE n 
1 246 SER n 
1 247 GLY n 
1 248 GLY n 
1 249 ASN n 
1 250 HIS n 
1 251 TYR n 
1 252 CYS n 
1 253 ALA n 
1 254 ASN n 
1 255 GLY n 
1 256 SER n 
1 257 ASN n 
1 258 ARG n 
1 259 TYR n 
1 260 ASP n 
1 261 ALA n 
1 262 LEU n 
1 263 LEU n 
1 264 GLY n 
1 265 LYS n 
1 266 TYR n 
1 267 GLY n 
1 268 VAL n 
1 269 ALA n 
1 270 TRP n 
1 271 MET n 
1 272 LYS n 
1 273 LEU n 
1 274 HIS n 
1 275 LEU n 
1 276 ASP n 
1 277 GLN n 
1 278 ASP n 
1 279 GLN n 
1 280 ARG n 
1 281 TYR n 
1 282 ALA n 
1 283 PRO n 
1 284 PHE n 
1 285 LEU n 
1 286 CYS n 
1 287 GLY n 
1 288 PRO n 
1 289 ASN n 
1 290 HIS n 
1 291 GLU n 
1 292 ARG n 
1 293 ASP n 
1 294 ARG n 
1 295 GLN n 
1 296 ILE n 
1 297 SER n 
1 298 GLU n 
1 299 HIS n 
1 300 ARG n 
1 301 SER n 
1 302 THR n 
1 303 CYS n 
1 304 PRO n 
1 305 PHE n 
1 306 VAL n 
1 307 ASP n 
1 308 LYS n 
1 309 LEU n 
1 310 ALA n 
1 311 ALA n 
1 312 ALA n 
1 313 LEU n 
1 314 GLU n 
1 315 HIS n 
1 316 HIS n 
1 317 HIS n 
1 318 HIS n 
1 319 HIS n 
1 320 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                   320 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CAL65_11960 
_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      'Alkalilimnicola ehrlichii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     351052 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                 'C4 H7 N O4'     133.103 
CL  non-polymer         . 'CHLORIDE ION'  ?                 'Cl -1'          35.453  
CYS 'L-peptide linking' y CYSTEINE        ?                 'C3 H7 N O2 S'   121.158 
EDO non-polymer         . 1,2-ETHANEDIOL  'ETHYLENE GLYCOL' 'C2 H6 O2'       62.068  
GLN 'L-peptide linking' y GLUTAMINE       ?                 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                 'C2 H5 N O2'     75.067  
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 
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 
# 
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   SER 2   2   ?   ?   ?   A . n 
A 1 3   SER 3   3   ?   ?   ?   A . n 
A 1 4   ILE 4   4   ?   ?   ?   A . n 
A 1 5   ILE 5   5   ?   ?   ?   A . n 
A 1 6   LYS 6   6   ?   ?   ?   A . n 
A 1 7   ARG 7   7   ?   ?   ?   A . n 
A 1 8   LYS 8   8   ?   ?   ?   A . n 
A 1 9   LEU 9   9   ?   ?   ?   A . n 
A 1 10  ALA 10  10  ?   ?   ?   A . n 
A 1 11  SER 11  11  ?   ?   ?   A . n 
A 1 12  LEU 12  12  ?   ?   ?   A . n 
A 1 13  PHE 13  13  ?   ?   ?   A . n 
A 1 14  ALA 14  14  ?   ?   ?   A . n 
A 1 15  PHE 15  15  ?   ?   ?   A . n 
A 1 16  SER 16  16  ?   ?   ?   A . n 
A 1 17  ALA 17  17  ?   ?   ?   A . n 
A 1 18  ALA 18  18  ?   ?   ?   A . n 
A 1 19  MET 19  19  ?   ?   ?   A . n 
A 1 20  LEU 20  20  ?   ?   ?   A . n 
A 1 21  LEU 21  21  ?   ?   ?   A . n 
A 1 22  SER 22  22  ?   ?   ?   A . n 
A 1 23  THR 23  23  ?   ?   ?   A . n 
A 1 24  SER 24  24  ?   ?   ?   A . n 
A 1 25  VAL 25  25  ?   ?   ?   A . n 
A 1 26  TRP 26  26  ?   ?   ?   A . n 
A 1 27  SER 27  27  ?   ?   ?   A . n 
A 1 28  MET 28  28  ?   ?   ?   A . n 
A 1 29  ASN 29  29  ?   ?   ?   A . n 
A 1 30  PRO 30  30  ?   ?   ?   A . n 
A 1 31  GLY 31  31  ?   ?   ?   A . n 
A 1 32  ASP 32  32  ?   ?   ?   A . n 
A 1 33  VAL 33  33  ?   ?   ?   A . n 
A 1 34  PRO 34  34  ?   ?   ?   A . n 
A 1 35  ASP 35  35  ?   ?   ?   A . n 
A 1 36  THR 36  36  ?   ?   ?   A . n 
A 1 37  CYS 37  37  ?   ?   ?   A . n 
A 1 38  GLU 38  38  ?   ?   ?   A . n 
A 1 39  GLY 39  39  ?   ?   ?   A . n 
A 1 40  ASP 40  40  ?   ?   ?   A . n 
A 1 41  CYS 41  41  ?   ?   ?   A . n 
A 1 42  GLY 42  42  42  GLY GLY A . n 
A 1 43  TYR 43  43  43  TYR TYR A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ARG 45  45  45  ARG ARG A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  PRO 47  47  47  PRO PRO A . n 
A 1 48  ASP 48  48  48  ASP ASP A . n 
A 1 49  PRO 49  49  49  PRO PRO A . n 
A 1 50  THR 50  50  50  THR THR A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLU 55  55  55  GLU GLU A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  TYR 61  61  61  TYR TYR A . n 
A 1 62  THR 62  62  62  THR THR A . n 
A 1 63  ILE 63  63  63  ILE ILE A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  SER 66  66  66  SER SER A . n 
A 1 67  ASN 67  67  67  ASN ASN A . n 
A 1 68  VAL 68  68  68  VAL VAL A . n 
A 1 69  SER 69  69  69  SER SER A . n 
A 1 70  SER 70  70  70  SER SER A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  VAL 72  72  72  VAL VAL A . n 
A 1 73  ARG 73  73  73  ARG ARG A . n 
A 1 74  GLY 74  74  74  GLY GLY A . n 
A 1 75  PHE 75  75  75  PHE PHE A . n 
A 1 76  GLY 76  76  76  GLY GLY A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  THR 79  79  79  THR THR A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  TYR 81  81  81  TYR TYR A . n 
A 1 82  TYR 82  82  82  TYR TYR A . n 
A 1 83  PRO 83  83  83  PRO PRO A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  ASN 85  85  85  ASN ASN A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  GLU 87  87  87  GLU GLU A . n 
A 1 88  GLY 88  88  88  GLY GLY A . n 
A 1 89  THR 89  89  89  THR THR A . n 
A 1 90  MET 90  90  90  MET MET A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ILE 93  93  93  ILE ILE A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  ILE 96  96  96  ILE ILE A . n 
A 1 97  PRO 97  97  97  PRO PRO A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  TYR 99  99  99  TYR TYR A . n 
A 1 100 MET 100 100 100 MET MET A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 GLN 103 103 103 GLN GLN A . n 
A 1 104 SER 104 104 104 SER SER A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 TRP 109 109 109 TRP TRP A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 PRO 111 111 111 PRO PRO A . n 
A 1 112 ARG 112 112 112 ARG ARG A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 SER 115 115 115 SER SER A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 GLY 117 117 117 GLY GLY A . n 
A 1 118 PHE 118 118 118 PHE PHE A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 VAL 120 120 120 VAL VAL A . n 
A 1 121 MET 121 121 121 MET MET A . n 
A 1 122 THR 122 122 122 THR THR A . n 
A 1 123 ILE 123 123 123 ILE ILE A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 THR 125 125 125 THR THR A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 ILE 128 128 128 ILE ILE A . n 
A 1 129 SER 129 129 129 SER SER A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 PRO 132 132 132 PRO PRO A . n 
A 1 133 PRO 133 133 133 PRO PRO A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 ARG 135 135 135 ARG ARG A . n 
A 1 136 ARG 136 136 136 ARG ARG A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 GLN 138 138 138 GLN GLN A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 GLU 140 140 140 GLU GLU A . n 
A 1 141 ALA 141 141 141 ALA ALA A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 LEU 143 143 143 LEU LEU A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 TYR 145 145 145 TYR TYR A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ASP 148 148 148 ASP ASP A . n 
A 1 149 GLN 149 149 149 GLN GLN A . n 
A 1 150 SER 150 150 150 SER SER A . n 
A 1 151 ASN 151 151 151 ASN ASN A . n 
A 1 152 SER 152 152 152 SER SER A . n 
A 1 153 SER 153 153 153 SER SER A . n 
A 1 154 ARG 154 154 154 ARG ARG A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 PRO 156 156 156 PRO PRO A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 ASN 158 158 158 ASN ASN A . n 
A 1 159 GLY 159 159 159 GLY GLY A . n 
A 1 160 MET 160 160 160 MET MET A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 PRO 163 163 163 PRO PRO A . n 
A 1 164 ASN 164 164 164 ASN ASN A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 GLY 167 167 167 GLY GLY A . n 
A 1 168 ALA 168 168 168 ALA ALA A . n 
A 1 169 VAL 169 169 169 VAL VAL A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 TRP 171 171 171 TRP TRP A . n 
A 1 172 SER 172 172 172 SER SER A . n 
A 1 173 MET 173 173 173 MET MET A . n 
A 1 174 GLY 174 174 174 GLY GLY A . n 
A 1 175 GLY 175 175 175 GLY GLY A . n 
A 1 176 GLY 176 176 176 GLY GLY A . n 
A 1 177 GLY 177 177 177 GLY GLY A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 LEU 179 179 179 LEU LEU A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 LEU 181 181 181 LEU LEU A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ALA 183 183 183 ALA ALA A . n 
A 1 184 ASP 184 184 184 ASP ASP A . n 
A 1 185 ASP 185 185 185 ASP ASP A . n 
A 1 186 GLY 186 186 186 GLY GLY A . n 
A 1 187 ILE 187 187 187 ILE ILE A . n 
A 1 188 GLN 188 188 188 GLN GLN A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 ILE 191 191 191 ILE ILE A . n 
A 1 192 GLY 192 192 192 GLY GLY A . n 
A 1 193 LEU 193 193 193 LEU LEU A . n 
A 1 194 ALA 194 194 194 ALA ALA A . n 
A 1 195 PRO 195 195 195 PRO PRO A . n 
A 1 196 TRP 196 196 196 TRP TRP A . n 
A 1 197 ASN 197 197 197 ASN ASN A . n 
A 1 198 THR 198 198 198 THR THR A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 SER 200 200 200 SER SER A . n 
A 1 201 LEU 201 201 201 LEU LEU A . n 
A 1 202 GLY 202 202 202 GLY GLY A . n 
A 1 203 PHE 203 203 203 PHE PHE A . n 
A 1 204 ARG 204 204 204 ARG ARG A . n 
A 1 205 SER 205 205 205 SER SER A . n 
A 1 206 ILE 206 206 206 ILE ILE A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 THR 210 210 210 THR THR A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 ILE 212 212 212 ILE ILE A . n 
A 1 213 PHE 213 213 213 PHE PHE A . n 
A 1 214 ALA 214 214 214 ALA ALA A . n 
A 1 215 CYS 215 215 215 CYS CYS A . n 
A 1 216 GLU 216 216 216 GLU GLU A . n 
A 1 217 ARG 217 217 217 ARG ARG A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 SER 219 219 219 SER SER A . n 
A 1 220 ILE 220 220 220 ILE ILE A . n 
A 1 221 ALA 221 221 221 ALA ALA A . n 
A 1 222 PRO 222 222 222 PRO PRO A . n 
A 1 223 VAL 223 223 223 VAL VAL A . n 
A 1 224 ARG 224 224 224 ARG ARG A . n 
A 1 225 SER 225 225 225 SER SER A . n 
A 1 226 HIS 226 226 226 HIS HIS A . n 
A 1 227 ALA 227 227 227 ALA ALA A . n 
A 1 228 SER 228 228 228 SER SER A . n 
A 1 229 PRO 229 229 229 PRO PRO A . n 
A 1 230 PHE 230 230 230 PHE PHE A . n 
A 1 231 TYR 231 231 231 TYR TYR A . n 
A 1 232 ASN 232 232 232 ASN ASN A . n 
A 1 233 ALA 233 233 233 ALA ALA A . n 
A 1 234 ILE 234 234 234 ILE ILE A . n 
A 1 235 PRO 235 235 235 PRO PRO A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 SER 237 237 237 SER SER A . n 
A 1 238 THR 238 238 238 THR THR A . n 
A 1 239 ASP 239 239 239 ASP ASP A . n 
A 1 240 LYS 240 240 240 LYS LYS A . n 
A 1 241 ALA 241 241 241 ALA ALA A . n 
A 1 242 TYR 242 242 242 TYR TYR A . n 
A 1 243 PHE 243 243 243 PHE PHE A . n 
A 1 244 GLU 244 244 244 GLU GLU A . n 
A 1 245 ILE 245 245 245 ILE ILE A . n 
A 1 246 SER 246 246 246 SER SER A . n 
A 1 247 GLY 247 247 247 GLY GLY A . n 
A 1 248 GLY 248 248 248 GLY GLY A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 TYR 251 251 251 TYR TYR A . n 
A 1 252 CYS 252 252 252 CYS CYS A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 ASN 254 254 254 ASN ASN A . n 
A 1 255 GLY 255 255 255 GLY GLY A . n 
A 1 256 SER 256 256 256 SER SER A . n 
A 1 257 ASN 257 257 257 ASN ASN A . n 
A 1 258 ARG 258 258 258 ARG ARG A . n 
A 1 259 TYR 259 259 259 TYR TYR A . n 
A 1 260 ASP 260 260 260 ASP ASP A . n 
A 1 261 ALA 261 261 261 ALA ALA A . n 
A 1 262 LEU 262 262 262 LEU LEU A . n 
A 1 263 LEU 263 263 263 LEU LEU A . n 
A 1 264 GLY 264 264 264 GLY GLY A . n 
A 1 265 LYS 265 265 265 LYS LYS A . n 
A 1 266 TYR 266 266 266 TYR TYR A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 ALA 269 269 269 ALA ALA A . n 
A 1 270 TRP 270 270 270 TRP TRP A . n 
A 1 271 MET 271 271 271 MET MET A . n 
A 1 272 LYS 272 272 272 LYS LYS A . n 
A 1 273 LEU 273 273 273 LEU LEU A . n 
A 1 274 HIS 274 274 274 HIS HIS A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 ASP 276 276 276 ASP ASP A . n 
A 1 277 GLN 277 277 277 GLN GLN A . n 
A 1 278 ASP 278 278 278 ASP ASP A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 TYR 281 281 281 TYR TYR A . n 
A 1 282 ALA 282 282 282 ALA ALA A . n 
A 1 283 PRO 283 283 283 PRO PRO A . n 
A 1 284 PHE 284 284 284 PHE PHE A . n 
A 1 285 LEU 285 285 285 LEU LEU A . n 
A 1 286 CYS 286 286 286 CYS CYS A . n 
A 1 287 GLY 287 287 287 GLY GLY A . n 
A 1 288 PRO 288 288 288 PRO PRO A . n 
A 1 289 ASN 289 289 289 ASN ASN A . n 
A 1 290 HIS 290 290 290 HIS HIS A . n 
A 1 291 GLU 291 291 291 GLU GLU A . n 
A 1 292 ARG 292 292 292 ARG ARG A . n 
A 1 293 ASP 293 293 293 ASP ASP A . n 
A 1 294 ARG 294 294 294 ARG ARG A . n 
A 1 295 GLN 295 295 295 GLN GLN A . n 
A 1 296 ILE 296 296 296 ILE ILE A . n 
A 1 297 SER 297 297 297 SER SER A . n 
A 1 298 GLU 298 298 298 GLU GLU A . n 
A 1 299 HIS 299 299 299 HIS HIS A . n 
A 1 300 ARG 300 300 300 ARG ARG A . n 
A 1 301 SER 301 301 301 SER SER A . n 
A 1 302 THR 302 302 302 THR THR A . n 
A 1 303 CYS 303 303 303 CYS CYS A . n 
A 1 304 PRO 304 304 304 PRO PRO A . n 
A 1 305 PHE 305 305 305 PHE PHE A . n 
A 1 306 VAL 306 306 ?   ?   ?   A . n 
A 1 307 ASP 307 307 ?   ?   ?   A . n 
A 1 308 LYS 308 308 ?   ?   ?   A . n 
A 1 309 LEU 309 309 ?   ?   ?   A . n 
A 1 310 ALA 310 310 ?   ?   ?   A . n 
A 1 311 ALA 311 311 ?   ?   ?   A . n 
A 1 312 ALA 312 312 ?   ?   ?   A . n 
A 1 313 LEU 313 313 ?   ?   ?   A . n 
A 1 314 GLU 314 314 ?   ?   ?   A . n 
A 1 315 HIS 315 315 ?   ?   ?   A . n 
A 1 316 HIS 316 316 ?   ?   ?   A . n 
A 1 317 HIS 317 317 ?   ?   ?   A . n 
A 1 318 HIS 318 318 ?   ?   ?   A . n 
A 1 319 HIS 319 319 ?   ?   ?   A . n 
A 1 320 HIS 320 320 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   SER 2   2   ?   ?   ?   B . n 
B 1 3   SER 3   3   ?   ?   ?   B . n 
B 1 4   ILE 4   4   ?   ?   ?   B . n 
B 1 5   ILE 5   5   ?   ?   ?   B . n 
B 1 6   LYS 6   6   ?   ?   ?   B . n 
B 1 7   ARG 7   7   ?   ?   ?   B . n 
B 1 8   LYS 8   8   ?   ?   ?   B . n 
B 1 9   LEU 9   9   ?   ?   ?   B . n 
B 1 10  ALA 10  10  ?   ?   ?   B . n 
B 1 11  SER 11  11  ?   ?   ?   B . n 
B 1 12  LEU 12  12  ?   ?   ?   B . n 
B 1 13  PHE 13  13  ?   ?   ?   B . n 
B 1 14  ALA 14  14  ?   ?   ?   B . n 
B 1 15  PHE 15  15  ?   ?   ?   B . n 
B 1 16  SER 16  16  ?   ?   ?   B . n 
B 1 17  ALA 17  17  ?   ?   ?   B . n 
B 1 18  ALA 18  18  ?   ?   ?   B . n 
B 1 19  MET 19  19  ?   ?   ?   B . n 
B 1 20  LEU 20  20  ?   ?   ?   B . n 
B 1 21  LEU 21  21  ?   ?   ?   B . n 
B 1 22  SER 22  22  ?   ?   ?   B . n 
B 1 23  THR 23  23  ?   ?   ?   B . n 
B 1 24  SER 24  24  ?   ?   ?   B . n 
B 1 25  VAL 25  25  ?   ?   ?   B . n 
B 1 26  TRP 26  26  ?   ?   ?   B . n 
B 1 27  SER 27  27  ?   ?   ?   B . n 
B 1 28  MET 28  28  ?   ?   ?   B . n 
B 1 29  ASN 29  29  ?   ?   ?   B . n 
B 1 30  PRO 30  30  ?   ?   ?   B . n 
B 1 31  GLY 31  31  ?   ?   ?   B . n 
B 1 32  ASP 32  32  ?   ?   ?   B . n 
B 1 33  VAL 33  33  ?   ?   ?   B . n 
B 1 34  PRO 34  34  ?   ?   ?   B . n 
B 1 35  ASP 35  35  ?   ?   ?   B . n 
B 1 36  THR 36  36  ?   ?   ?   B . n 
B 1 37  CYS 37  37  ?   ?   ?   B . n 
B 1 38  GLU 38  38  ?   ?   ?   B . n 
B 1 39  GLY 39  39  ?   ?   ?   B . n 
B 1 40  ASP 40  40  ?   ?   ?   B . n 
B 1 41  CYS 41  41  ?   ?   ?   B . n 
B 1 42  GLY 42  42  42  GLY GLY B . n 
B 1 43  TYR 43  43  43  TYR TYR B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  ARG 45  45  45  ARG ARG B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  PRO 47  47  47  PRO PRO B . n 
B 1 48  ASP 48  48  48  ASP ASP B . n 
B 1 49  PRO 49  49  49  PRO PRO B . n 
B 1 50  THR 50  50  50  THR THR B . n 
B 1 51  GLU 51  51  51  GLU GLU B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  PHE 53  53  53  PHE PHE B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  GLU 55  55  55  GLU GLU B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  ASP 57  57  57  ASP ASP B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  GLY 59  59  59  GLY GLY B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  TYR 61  61  61  TYR TYR B . n 
B 1 62  THR 62  62  62  THR THR B . n 
B 1 63  ILE 63  63  63  ILE ILE B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  SER 66  66  66  SER SER B . n 
B 1 67  ASN 67  67  67  ASN ASN B . n 
B 1 68  VAL 68  68  68  VAL VAL B . n 
B 1 69  SER 69  69  69  SER SER B . n 
B 1 70  SER 70  70  70  SER SER B . n 
B 1 71  LEU 71  71  71  LEU LEU B . n 
B 1 72  VAL 72  72  72  VAL VAL B . n 
B 1 73  ARG 73  73  73  ARG ARG B . n 
B 1 74  GLY 74  74  74  GLY GLY B . n 
B 1 75  PHE 75  75  75  PHE PHE B . n 
B 1 76  GLY 76  76  76  GLY GLY B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  THR 79  79  79  THR THR B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  TYR 81  81  81  TYR TYR B . n 
B 1 82  TYR 82  82  82  TYR TYR B . n 
B 1 83  PRO 83  83  83  PRO PRO B . n 
B 1 84  VAL 84  84  84  VAL VAL B . n 
B 1 85  ASN 85  85  85  ASN ASN B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  GLU 87  87  87  GLU GLU B . n 
B 1 88  GLY 88  88  88  GLY GLY B . n 
B 1 89  THR 89  89  89  THR THR B . n 
B 1 90  MET 90  90  90  MET MET B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  ILE 93  93  93  ILE ILE B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  ILE 96  96  96  ILE ILE B . n 
B 1 97  PRO 97  97  97  PRO PRO B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  TYR 99  99  99  TYR TYR B . n 
B 1 100 MET 100 100 100 MET MET B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 TYR 102 102 102 TYR TYR B . n 
B 1 103 GLN 103 103 103 GLN GLN B . n 
B 1 104 SER 104 104 104 SER SER B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 TRP 109 109 109 TRP TRP B . n 
B 1 110 GLY 110 110 110 GLY GLY B . n 
B 1 111 PRO 111 111 111 PRO PRO B . n 
B 1 112 ARG 112 112 112 ARG ARG B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 SER 115 115 115 SER SER B . n 
B 1 116 HIS 116 116 116 HIS HIS B . n 
B 1 117 GLY 117 117 117 GLY GLY B . n 
B 1 118 PHE 118 118 118 PHE PHE B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 VAL 120 120 120 VAL VAL B . n 
B 1 121 MET 121 121 121 MET MET B . n 
B 1 122 THR 122 122 122 THR THR B . n 
B 1 123 ILE 123 123 123 ILE ILE B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 THR 125 125 125 THR THR B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 ARG 127 127 127 ARG ARG B . n 
B 1 128 ILE 128 128 128 ILE ILE B . n 
B 1 129 SER 129 129 129 SER SER B . n 
B 1 130 ASP 130 130 130 ASP ASP B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 PRO 132 132 132 PRO PRO B . n 
B 1 133 PRO 133 133 133 PRO PRO B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 ARG 135 135 135 ARG ARG B . n 
B 1 136 ARG 136 136 136 ARG ARG B . n 
B 1 137 ASP 137 137 137 ASP ASP B . n 
B 1 138 GLN 138 138 138 GLN GLN B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 GLU 140 140 140 GLU GLU B . n 
B 1 141 ALA 141 141 141 ALA ALA B . n 
B 1 142 ALA 142 142 142 ALA ALA B . n 
B 1 143 LEU 143 143 143 LEU LEU B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 TYR 145 145 145 TYR TYR B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ASP 148 148 148 ASP ASP B . n 
B 1 149 GLN 149 149 149 GLN GLN B . n 
B 1 150 SER 150 150 150 SER SER B . n 
B 1 151 ASN 151 151 151 ASN ASN B . n 
B 1 152 SER 152 152 152 SER SER B . n 
B 1 153 SER 153 153 153 SER SER B . n 
B 1 154 ARG 154 154 154 ARG ARG B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 PRO 156 156 156 PRO PRO B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 ASN 158 158 158 ASN ASN B . n 
B 1 159 GLY 159 159 159 GLY GLY B . n 
B 1 160 MET 160 160 160 MET MET B . n 
B 1 161 VAL 161 161 161 VAL VAL B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 PRO 163 163 163 PRO PRO B . n 
B 1 164 ASN 164 164 164 ASN ASN B . n 
B 1 165 ARG 165 165 165 ARG ARG B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 GLY 167 167 167 GLY GLY B . n 
B 1 168 ALA 168 168 168 ALA ALA B . n 
B 1 169 VAL 169 169 169 VAL VAL B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 TRP 171 171 171 TRP TRP B . n 
B 1 172 SER 172 172 172 SER SER B . n 
B 1 173 MET 173 173 173 MET MET B . n 
B 1 174 GLY 174 174 174 GLY GLY B . n 
B 1 175 GLY 175 175 175 GLY GLY B . n 
B 1 176 GLY 176 176 176 GLY GLY B . n 
B 1 177 GLY 177 177 177 GLY GLY B . n 
B 1 178 THR 178 178 178 THR THR B . n 
B 1 179 LEU 179 179 179 LEU LEU B . n 
B 1 180 ARG 180 180 180 ARG ARG B . n 
B 1 181 LEU 181 181 181 LEU LEU B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 ALA 183 183 183 ALA ALA B . n 
B 1 184 ASP 184 184 184 ASP ASP B . n 
B 1 185 ASP 185 185 185 ASP ASP B . n 
B 1 186 GLY 186 186 186 GLY GLY B . n 
B 1 187 ILE 187 187 187 ILE ILE B . n 
B 1 188 GLN 188 188 188 GLN GLN B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 ILE 191 191 191 ILE ILE B . n 
B 1 192 GLY 192 192 192 GLY GLY B . n 
B 1 193 LEU 193 193 193 LEU LEU B . n 
B 1 194 ALA 194 194 194 ALA ALA B . n 
B 1 195 PRO 195 195 195 PRO PRO B . n 
B 1 196 TRP 196 196 196 TRP TRP B . n 
B 1 197 ASN 197 197 197 ASN ASN B . n 
B 1 198 THR 198 198 198 THR THR B . n 
B 1 199 SER 199 199 199 SER SER B . n 
B 1 200 SER 200 200 200 SER SER B . n 
B 1 201 LEU 201 201 201 LEU LEU B . n 
B 1 202 GLY 202 202 202 GLY GLY B . n 
B 1 203 PHE 203 203 203 PHE PHE B . n 
B 1 204 ARG 204 204 204 ARG ARG B . n 
B 1 205 SER 205 205 205 SER SER B . n 
B 1 206 ILE 206 206 206 ILE ILE B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 THR 208 208 208 THR THR B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 THR 210 210 210 THR THR B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 ILE 212 212 212 ILE ILE B . n 
B 1 213 PHE 213 213 213 PHE PHE B . n 
B 1 214 ALA 214 214 214 ALA ALA B . n 
B 1 215 CYS 215 215 215 CYS CYS B . n 
B 1 216 GLU 216 216 216 GLU GLU B . n 
B 1 217 ARG 217 217 217 ARG ARG B . n 
B 1 218 ASP 218 218 218 ASP ASP B . n 
B 1 219 SER 219 219 219 SER SER B . n 
B 1 220 ILE 220 220 220 ILE ILE B . n 
B 1 221 ALA 221 221 221 ALA ALA B . n 
B 1 222 PRO 222 222 222 PRO PRO B . n 
B 1 223 VAL 223 223 223 VAL VAL B . n 
B 1 224 ARG 224 224 224 ARG ARG B . n 
B 1 225 SER 225 225 225 SER SER B . n 
B 1 226 HIS 226 226 226 HIS HIS B . n 
B 1 227 ALA 227 227 227 ALA ALA B . n 
B 1 228 SER 228 228 228 SER SER B . n 
B 1 229 PRO 229 229 229 PRO PRO B . n 
B 1 230 PHE 230 230 230 PHE PHE B . n 
B 1 231 TYR 231 231 231 TYR TYR B . n 
B 1 232 ASN 232 232 232 ASN ASN B . n 
B 1 233 ALA 233 233 233 ALA ALA B . n 
B 1 234 ILE 234 234 234 ILE ILE B . n 
B 1 235 PRO 235 235 235 PRO PRO B . n 
B 1 236 SER 236 236 236 SER SER B . n 
B 1 237 SER 237 237 237 SER SER B . n 
B 1 238 THR 238 238 238 THR THR B . n 
B 1 239 ASP 239 239 239 ASP ASP B . n 
B 1 240 LYS 240 240 240 LYS LYS B . n 
B 1 241 ALA 241 241 241 ALA ALA B . n 
B 1 242 TYR 242 242 242 TYR TYR B . n 
B 1 243 PHE 243 243 243 PHE PHE B . n 
B 1 244 GLU 244 244 244 GLU GLU B . n 
B 1 245 ILE 245 245 245 ILE ILE B . n 
B 1 246 SER 246 246 246 SER SER B . n 
B 1 247 GLY 247 247 247 GLY GLY B . n 
B 1 248 GLY 248 248 248 GLY GLY B . n 
B 1 249 ASN 249 249 249 ASN ASN B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 TYR 251 251 251 TYR TYR B . n 
B 1 252 CYS 252 252 252 CYS CYS B . n 
B 1 253 ALA 253 253 253 ALA ALA B . n 
B 1 254 ASN 254 254 254 ASN ASN B . n 
B 1 255 GLY 255 255 255 GLY GLY B . n 
B 1 256 SER 256 256 256 SER SER B . n 
B 1 257 ASN 257 257 257 ASN ASN B . n 
B 1 258 ARG 258 258 258 ARG ARG B . n 
B 1 259 TYR 259 259 259 TYR TYR B . n 
B 1 260 ASP 260 260 260 ASP ASP B . n 
B 1 261 ALA 261 261 261 ALA ALA B . n 
B 1 262 LEU 262 262 262 LEU LEU B . n 
B 1 263 LEU 263 263 263 LEU LEU B . n 
B 1 264 GLY 264 264 264 GLY GLY B . n 
B 1 265 LYS 265 265 265 LYS LYS B . n 
B 1 266 TYR 266 266 266 TYR TYR B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 ALA 269 269 269 ALA ALA B . n 
B 1 270 TRP 270 270 270 TRP TRP B . n 
B 1 271 MET 271 271 271 MET MET B . n 
B 1 272 LYS 272 272 272 LYS LYS B . n 
B 1 273 LEU 273 273 273 LEU LEU B . n 
B 1 274 HIS 274 274 274 HIS HIS B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 ASP 276 276 276 ASP ASP B . n 
B 1 277 GLN 277 277 277 GLN GLN B . n 
B 1 278 ASP 278 278 278 ASP ASP B . n 
B 1 279 GLN 279 279 279 GLN GLN B . n 
B 1 280 ARG 280 280 280 ARG ARG B . n 
B 1 281 TYR 281 281 281 TYR TYR B . n 
B 1 282 ALA 282 282 282 ALA ALA B . n 
B 1 283 PRO 283 283 283 PRO PRO B . n 
B 1 284 PHE 284 284 284 PHE PHE B . n 
B 1 285 LEU 285 285 285 LEU LEU B . n 
B 1 286 CYS 286 286 286 CYS CYS B . n 
B 1 287 GLY 287 287 287 GLY GLY B . n 
B 1 288 PRO 288 288 288 PRO PRO B . n 
B 1 289 ASN 289 289 289 ASN ASN B . n 
B 1 290 HIS 290 290 290 HIS HIS B . n 
B 1 291 GLU 291 291 291 GLU GLU B . n 
B 1 292 ARG 292 292 292 ARG ARG B . n 
B 1 293 ASP 293 293 293 ASP ASP B . n 
B 1 294 ARG 294 294 294 ARG ARG B . n 
B 1 295 GLN 295 295 295 GLN GLN B . n 
B 1 296 ILE 296 296 296 ILE ILE B . n 
B 1 297 SER 297 297 297 SER SER B . n 
B 1 298 GLU 298 298 298 GLU GLU B . n 
B 1 299 HIS 299 299 299 HIS HIS B . n 
B 1 300 ARG 300 300 300 ARG ARG B . n 
B 1 301 SER 301 301 301 SER SER B . n 
B 1 302 THR 302 302 302 THR THR B . n 
B 1 303 CYS 303 303 303 CYS CYS B . n 
B 1 304 PRO 304 304 304 PRO PRO B . n 
B 1 305 PHE 305 305 305 PHE PHE B . n 
B 1 306 VAL 306 306 306 VAL VAL B . n 
B 1 307 ASP 307 307 307 ASP ASP B . n 
B 1 308 LYS 308 308 ?   ?   ?   B . n 
B 1 309 LEU 309 309 ?   ?   ?   B . n 
B 1 310 ALA 310 310 ?   ?   ?   B . n 
B 1 311 ALA 311 311 ?   ?   ?   B . n 
B 1 312 ALA 312 312 ?   ?   ?   B . n 
B 1 313 LEU 313 313 ?   ?   ?   B . n 
B 1 314 GLU 314 314 ?   ?   ?   B . n 
B 1 315 HIS 315 315 ?   ?   ?   B . n 
B 1 316 HIS 316 316 ?   ?   ?   B . n 
B 1 317 HIS 317 317 ?   ?   ?   B . n 
B 1 318 HIS 318 318 ?   ?   ?   B . n 
B 1 319 HIS 319 319 ?   ?   ?   B . n 
B 1 320 HIS 320 320 ?   ?   ?   B . 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 
C  2 NA  1   401 1   NA  NA  A . 
D  3 EDO 1   402 2   EDO EDO A . 
E  3 EDO 1   403 3   EDO EDO A . 
F  3 EDO 1   404 7   EDO EDO A . 
G  3 EDO 1   405 9   EDO EDO A . 
H  3 EDO 1   406 10  EDO EDO A . 
I  3 EDO 1   407 12  EDO EDO A . 
J  3 EDO 1   408 13  EDO EDO A . 
K  3 EDO 1   409 15  EDO EDO A . 
L  3 EDO 1   410 16  EDO EDO A . 
M  3 EDO 1   411 18  EDO EDO A . 
N  3 EDO 1   412 25  EDO EDO A . 
O  3 EDO 1   413 26  EDO EDO A . 
P  3 EDO 1   414 27  EDO EDO A . 
Q  3 EDO 1   415 29  EDO EDO A . 
R  3 EDO 1   416 30  EDO EDO A . 
S  3 EDO 1   417 31  EDO EDO A . 
T  4 CL  1   418 1   CL  CL  A . 
U  4 CL  1   419 3   CL  CL  A . 
V  2 NA  1   401 2   NA  NA  B . 
W  2 NA  1   402 3   NA  NA  B . 
X  3 EDO 1   403 4   EDO EDO B . 
Y  3 EDO 1   404 5   EDO EDO B . 
Z  3 EDO 1   405 6   EDO EDO B . 
AA 3 EDO 1   406 8   EDO EDO B . 
BA 3 EDO 1   407 20  EDO EDO B . 
CA 3 EDO 1   408 23  EDO EDO B . 
DA 3 EDO 1   409 24  EDO EDO B . 
EA 3 EDO 1   410 28  EDO EDO B . 
FA 3 EDO 1   411 32  EDO EDO B . 
GA 4 CL  1   412 2   CL  CL  B . 
HA 5 HOH 1   501 512 HOH HOH A . 
HA 5 HOH 2   502 416 HOH HOH A . 
HA 5 HOH 3   503 515 HOH HOH A . 
HA 5 HOH 4   504 41  HOH HOH A . 
HA 5 HOH 5   505 565 HOH HOH A . 
HA 5 HOH 6   506 522 HOH HOH A . 
HA 5 HOH 7   507 315 HOH HOH A . 
HA 5 HOH 8   508 490 HOH HOH A . 
HA 5 HOH 9   509 159 HOH HOH A . 
HA 5 HOH 10  510 192 HOH HOH A . 
HA 5 HOH 11  511 99  HOH HOH A . 
HA 5 HOH 12  512 235 HOH HOH A . 
HA 5 HOH 13  513 180 HOH HOH A . 
HA 5 HOH 14  514 178 HOH HOH A . 
HA 5 HOH 15  515 454 HOH HOH A . 
HA 5 HOH 16  516 202 HOH HOH A . 
HA 5 HOH 17  517 22  HOH HOH A . 
HA 5 HOH 18  518 299 HOH HOH A . 
HA 5 HOH 19  519 132 HOH HOH A . 
HA 5 HOH 20  520 197 HOH HOH A . 
HA 5 HOH 21  521 133 HOH HOH A . 
HA 5 HOH 22  522 370 HOH HOH A . 
HA 5 HOH 23  523 64  HOH HOH A . 
HA 5 HOH 24  524 538 HOH HOH A . 
HA 5 HOH 25  525 80  HOH HOH A . 
HA 5 HOH 26  526 243 HOH HOH A . 
HA 5 HOH 27  527 45  HOH HOH A . 
HA 5 HOH 28  528 44  HOH HOH A . 
HA 5 HOH 29  529 6   HOH HOH A . 
HA 5 HOH 30  530 354 HOH HOH A . 
HA 5 HOH 31  531 48  HOH HOH A . 
HA 5 HOH 32  532 362 HOH HOH A . 
HA 5 HOH 33  533 61  HOH HOH A . 
HA 5 HOH 34  534 92  HOH HOH A . 
HA 5 HOH 35  535 21  HOH HOH A . 
HA 5 HOH 36  536 259 HOH HOH A . 
HA 5 HOH 37  537 513 HOH HOH A . 
HA 5 HOH 38  538 253 HOH HOH A . 
HA 5 HOH 39  539 324 HOH HOH A . 
HA 5 HOH 40  540 187 HOH HOH A . 
HA 5 HOH 41  541 75  HOH HOH A . 
HA 5 HOH 42  542 116 HOH HOH A . 
HA 5 HOH 43  543 510 HOH HOH A . 
HA 5 HOH 44  544 129 HOH HOH A . 
HA 5 HOH 45  545 11  HOH HOH A . 
HA 5 HOH 46  546 247 HOH HOH A . 
HA 5 HOH 47  547 105 HOH HOH A . 
HA 5 HOH 48  548 83  HOH HOH A . 
HA 5 HOH 49  549 498 HOH HOH A . 
HA 5 HOH 50  550 82  HOH HOH A . 
HA 5 HOH 51  551 114 HOH HOH A . 
HA 5 HOH 52  552 71  HOH HOH A . 
HA 5 HOH 53  553 127 HOH HOH A . 
HA 5 HOH 54  554 66  HOH HOH A . 
HA 5 HOH 55  555 290 HOH HOH A . 
HA 5 HOH 56  556 306 HOH HOH A . 
HA 5 HOH 57  557 112 HOH HOH A . 
HA 5 HOH 58  558 10  HOH HOH A . 
HA 5 HOH 59  559 274 HOH HOH A . 
HA 5 HOH 60  560 272 HOH HOH A . 
HA 5 HOH 61  561 273 HOH HOH A . 
HA 5 HOH 62  562 136 HOH HOH A . 
HA 5 HOH 63  563 36  HOH HOH A . 
HA 5 HOH 64  564 125 HOH HOH A . 
HA 5 HOH 65  565 201 HOH HOH A . 
HA 5 HOH 66  566 314 HOH HOH A . 
HA 5 HOH 67  567 228 HOH HOH A . 
HA 5 HOH 68  568 9   HOH HOH A . 
HA 5 HOH 69  569 86  HOH HOH A . 
HA 5 HOH 70  570 109 HOH HOH A . 
HA 5 HOH 71  571 185 HOH HOH A . 
HA 5 HOH 72  572 333 HOH HOH A . 
HA 5 HOH 73  573 14  HOH HOH A . 
HA 5 HOH 74  574 19  HOH HOH A . 
HA 5 HOH 75  575 77  HOH HOH A . 
HA 5 HOH 76  576 284 HOH HOH A . 
HA 5 HOH 77  577 359 HOH HOH A . 
HA 5 HOH 78  578 124 HOH HOH A . 
HA 5 HOH 79  579 206 HOH HOH A . 
HA 5 HOH 80  580 122 HOH HOH A . 
HA 5 HOH 81  581 428 HOH HOH A . 
HA 5 HOH 82  582 17  HOH HOH A . 
HA 5 HOH 83  583 25  HOH HOH A . 
HA 5 HOH 84  584 301 HOH HOH A . 
HA 5 HOH 85  585 130 HOH HOH A . 
HA 5 HOH 86  586 67  HOH HOH A . 
HA 5 HOH 87  587 3   HOH HOH A . 
HA 5 HOH 88  588 539 HOH HOH A . 
HA 5 HOH 89  589 76  HOH HOH A . 
HA 5 HOH 90  590 194 HOH HOH A . 
HA 5 HOH 91  591 58  HOH HOH A . 
HA 5 HOH 92  592 23  HOH HOH A . 
HA 5 HOH 93  593 27  HOH HOH A . 
HA 5 HOH 94  594 224 HOH HOH A . 
HA 5 HOH 95  595 456 HOH HOH A . 
HA 5 HOH 96  596 87  HOH HOH A . 
HA 5 HOH 97  597 562 HOH HOH A . 
HA 5 HOH 98  598 162 HOH HOH A . 
HA 5 HOH 99  599 215 HOH HOH A . 
HA 5 HOH 100 600 4   HOH HOH A . 
HA 5 HOH 101 601 176 HOH HOH A . 
HA 5 HOH 102 602 142 HOH HOH A . 
HA 5 HOH 103 603 349 HOH HOH A . 
HA 5 HOH 104 604 335 HOH HOH A . 
HA 5 HOH 105 605 191 HOH HOH A . 
HA 5 HOH 106 606 321 HOH HOH A . 
HA 5 HOH 107 607 221 HOH HOH A . 
HA 5 HOH 108 608 49  HOH HOH A . 
HA 5 HOH 109 609 30  HOH HOH A . 
HA 5 HOH 110 610 233 HOH HOH A . 
HA 5 HOH 111 611 232 HOH HOH A . 
HA 5 HOH 112 612 322 HOH HOH A . 
HA 5 HOH 113 613 167 HOH HOH A . 
HA 5 HOH 114 614 175 HOH HOH A . 
HA 5 HOH 115 615 295 HOH HOH A . 
HA 5 HOH 116 616 518 HOH HOH A . 
HA 5 HOH 117 617 183 HOH HOH A . 
HA 5 HOH 118 618 240 HOH HOH A . 
HA 5 HOH 119 619 113 HOH HOH A . 
HA 5 HOH 120 620 161 HOH HOH A . 
HA 5 HOH 121 621 174 HOH HOH A . 
HA 5 HOH 122 622 316 HOH HOH A . 
HA 5 HOH 123 623 260 HOH HOH A . 
HA 5 HOH 124 624 275 HOH HOH A . 
HA 5 HOH 125 625 13  HOH HOH A . 
HA 5 HOH 126 626 293 HOH HOH A . 
HA 5 HOH 127 627 517 HOH HOH A . 
HA 5 HOH 128 628 318 HOH HOH A . 
HA 5 HOH 129 629 564 HOH HOH A . 
HA 5 HOH 130 630 422 HOH HOH A . 
HA 5 HOH 131 631 139 HOH HOH A . 
HA 5 HOH 132 632 246 HOH HOH A . 
HA 5 HOH 133 633 430 HOH HOH A . 
HA 5 HOH 134 634 488 HOH HOH A . 
HA 5 HOH 135 635 267 HOH HOH A . 
HA 5 HOH 136 636 95  HOH HOH A . 
HA 5 HOH 137 637 226 HOH HOH A . 
HA 5 HOH 138 638 281 HOH HOH A . 
HA 5 HOH 139 639 298 HOH HOH A . 
HA 5 HOH 140 640 59  HOH HOH A . 
HA 5 HOH 141 641 51  HOH HOH A . 
HA 5 HOH 142 642 507 HOH HOH A . 
HA 5 HOH 143 643 289 HOH HOH A . 
HA 5 HOH 144 644 334 HOH HOH A . 
HA 5 HOH 145 645 309 HOH HOH A . 
HA 5 HOH 146 646 63  HOH HOH A . 
HA 5 HOH 147 647 204 HOH HOH A . 
HA 5 HOH 148 648 214 HOH HOH A . 
HA 5 HOH 149 649 393 HOH HOH A . 
HA 5 HOH 150 650 166 HOH HOH A . 
HA 5 HOH 151 651 288 HOH HOH A . 
HA 5 HOH 152 652 212 HOH HOH A . 
HA 5 HOH 153 653 20  HOH HOH A . 
HA 5 HOH 154 654 464 HOH HOH A . 
HA 5 HOH 155 655 186 HOH HOH A . 
HA 5 HOH 156 656 357 HOH HOH A . 
HA 5 HOH 157 657 213 HOH HOH A . 
HA 5 HOH 158 658 33  HOH HOH A . 
HA 5 HOH 159 659 103 HOH HOH A . 
HA 5 HOH 160 660 463 HOH HOH A . 
HA 5 HOH 161 661 302 HOH HOH A . 
HA 5 HOH 162 662 311 HOH HOH A . 
HA 5 HOH 163 663 93  HOH HOH A . 
HA 5 HOH 164 664 236 HOH HOH A . 
HA 5 HOH 165 665 218 HOH HOH A . 
HA 5 HOH 166 666 50  HOH HOH A . 
HA 5 HOH 167 667 208 HOH HOH A . 
HA 5 HOH 168 668 337 HOH HOH A . 
HA 5 HOH 169 669 157 HOH HOH A . 
HA 5 HOH 170 670 145 HOH HOH A . 
HA 5 HOH 171 671 238 HOH HOH A . 
HA 5 HOH 172 672 117 HOH HOH A . 
HA 5 HOH 173 673 78  HOH HOH A . 
HA 5 HOH 174 674 100 HOH HOH A . 
HA 5 HOH 175 675 126 HOH HOH A . 
HA 5 HOH 176 676 220 HOH HOH A . 
HA 5 HOH 177 677 567 HOH HOH A . 
HA 5 HOH 178 678 563 HOH HOH A . 
HA 5 HOH 179 679 285 HOH HOH A . 
HA 5 HOH 180 680 264 HOH HOH A . 
HA 5 HOH 181 681 459 HOH HOH A . 
HA 5 HOH 182 682 403 HOH HOH A . 
HA 5 HOH 183 683 344 HOH HOH A . 
HA 5 HOH 184 684 200 HOH HOH A . 
HA 5 HOH 185 685 555 HOH HOH A . 
HA 5 HOH 186 686 429 HOH HOH A . 
HA 5 HOH 187 687 457 HOH HOH A . 
HA 5 HOH 188 688 414 HOH HOH A . 
HA 5 HOH 189 689 262 HOH HOH A . 
HA 5 HOH 190 690 241 HOH HOH A . 
HA 5 HOH 191 691 458 HOH HOH A . 
HA 5 HOH 192 692 541 HOH HOH A . 
HA 5 HOH 193 693 569 HOH HOH A . 
HA 5 HOH 194 694 519 HOH HOH A . 
HA 5 HOH 195 695 378 HOH HOH A . 
HA 5 HOH 196 696 465 HOH HOH A . 
HA 5 HOH 197 697 423 HOH HOH A . 
HA 5 HOH 198 698 566 HOH HOH A . 
HA 5 HOH 199 699 138 HOH HOH A . 
HA 5 HOH 200 700 329 HOH HOH A . 
HA 5 HOH 201 701 276 HOH HOH A . 
HA 5 HOH 202 702 568 HOH HOH A . 
HA 5 HOH 203 703 433 HOH HOH A . 
HA 5 HOH 204 704 495 HOH HOH A . 
HA 5 HOH 205 705 140 HOH HOH A . 
HA 5 HOH 206 706 377 HOH HOH A . 
HA 5 HOH 207 707 368 HOH HOH A . 
HA 5 HOH 208 708 210 HOH HOH A . 
HA 5 HOH 209 709 431 HOH HOH A . 
HA 5 HOH 210 710 330 HOH HOH A . 
HA 5 HOH 211 711 561 HOH HOH A . 
HA 5 HOH 212 712 453 HOH HOH A . 
HA 5 HOH 213 713 258 HOH HOH A . 
HA 5 HOH 214 714 556 HOH HOH A . 
HA 5 HOH 215 715 342 HOH HOH A . 
HA 5 HOH 216 716 415 HOH HOH A . 
HA 5 HOH 217 717 406 HOH HOH A . 
HA 5 HOH 218 718 254 HOH HOH A . 
HA 5 HOH 219 719 424 HOH HOH A . 
HA 5 HOH 220 720 294 HOH HOH A . 
HA 5 HOH 221 721 397 HOH HOH A . 
HA 5 HOH 222 722 419 HOH HOH A . 
HA 5 HOH 223 723 257 HOH HOH A . 
HA 5 HOH 224 724 84  HOH HOH A . 
HA 5 HOH 225 725 492 HOH HOH A . 
HA 5 HOH 226 726 520 HOH HOH A . 
HA 5 HOH 227 727 385 HOH HOH A . 
HA 5 HOH 228 728 418 HOH HOH A . 
HA 5 HOH 229 729 146 HOH HOH A . 
HA 5 HOH 230 730 405 HOH HOH A . 
HA 5 HOH 231 731 338 HOH HOH A . 
HA 5 HOH 232 732 341 HOH HOH A . 
HA 5 HOH 233 733 420 HOH HOH A . 
HA 5 HOH 234 734 511 HOH HOH A . 
HA 5 HOH 235 735 426 HOH HOH A . 
HA 5 HOH 236 736 227 HOH HOH A . 
HA 5 HOH 237 737 413 HOH HOH A . 
HA 5 HOH 238 738 365 HOH HOH A . 
HA 5 HOH 239 739 345 HOH HOH A . 
HA 5 HOH 240 740 560 HOH HOH A . 
HA 5 HOH 241 741 408 HOH HOH A . 
HA 5 HOH 242 742 521 HOH HOH A . 
HA 5 HOH 243 743 172 HOH HOH A . 
HA 5 HOH 244 744 417 HOH HOH A . 
HA 5 HOH 245 745 356 HOH HOH A . 
HA 5 HOH 246 746 374 HOH HOH A . 
HA 5 HOH 247 747 168 HOH HOH A . 
HA 5 HOH 248 748 502 HOH HOH A . 
IA 5 HOH 1   501 559 HOH HOH B . 
IA 5 HOH 2   502 445 HOH HOH B . 
IA 5 HOH 3   503 250 HOH HOH B . 
IA 5 HOH 4   504 545 HOH HOH B . 
IA 5 HOH 5   505 468 HOH HOH B . 
IA 5 HOH 6   506 65  HOH HOH B . 
IA 5 HOH 7   507 270 HOH HOH B . 
IA 5 HOH 8   508 384 HOH HOH B . 
IA 5 HOH 9   509 149 HOH HOH B . 
IA 5 HOH 10  510 40  HOH HOH B . 
IA 5 HOH 11  511 360 HOH HOH B . 
IA 5 HOH 12  512 68  HOH HOH B . 
IA 5 HOH 13  513 402 HOH HOH B . 
IA 5 HOH 14  514 46  HOH HOH B . 
IA 5 HOH 15  515 473 HOH HOH B . 
IA 5 HOH 16  516 18  HOH HOH B . 
IA 5 HOH 17  517 96  HOH HOH B . 
IA 5 HOH 18  518 203 HOH HOH B . 
IA 5 HOH 19  519 88  HOH HOH B . 
IA 5 HOH 20  520 131 HOH HOH B . 
IA 5 HOH 21  521 443 HOH HOH B . 
IA 5 HOH 22  522 170 HOH HOH B . 
IA 5 HOH 23  523 529 HOH HOH B . 
IA 5 HOH 24  524 118 HOH HOH B . 
IA 5 HOH 25  525 56  HOH HOH B . 
IA 5 HOH 26  526 319 HOH HOH B . 
IA 5 HOH 27  527 296 HOH HOH B . 
IA 5 HOH 28  528 256 HOH HOH B . 
IA 5 HOH 29  529 153 HOH HOH B . 
IA 5 HOH 30  530 144 HOH HOH B . 
IA 5 HOH 31  531 37  HOH HOH B . 
IA 5 HOH 32  532 5   HOH HOH B . 
IA 5 HOH 33  533 57  HOH HOH B . 
IA 5 HOH 34  534 196 HOH HOH B . 
IA 5 HOH 35  535 115 HOH HOH B . 
IA 5 HOH 36  536 91  HOH HOH B . 
IA 5 HOH 37  537 450 HOH HOH B . 
IA 5 HOH 38  538 252 HOH HOH B . 
IA 5 HOH 39  539 90  HOH HOH B . 
IA 5 HOH 40  540 152 HOH HOH B . 
IA 5 HOH 41  541 190 HOH HOH B . 
IA 5 HOH 42  542 7   HOH HOH B . 
IA 5 HOH 43  543 73  HOH HOH B . 
IA 5 HOH 44  544 282 HOH HOH B . 
IA 5 HOH 45  545 52  HOH HOH B . 
IA 5 HOH 46  546 177 HOH HOH B . 
IA 5 HOH 47  547 231 HOH HOH B . 
IA 5 HOH 48  548 217 HOH HOH B . 
IA 5 HOH 49  549 135 HOH HOH B . 
IA 5 HOH 50  550 348 HOH HOH B . 
IA 5 HOH 51  551 16  HOH HOH B . 
IA 5 HOH 52  552 182 HOH HOH B . 
IA 5 HOH 53  553 15  HOH HOH B . 
IA 5 HOH 54  554 263 HOH HOH B . 
IA 5 HOH 55  555 150 HOH HOH B . 
IA 5 HOH 56  556 81  HOH HOH B . 
IA 5 HOH 57  557 173 HOH HOH B . 
IA 5 HOH 58  558 29  HOH HOH B . 
IA 5 HOH 59  559 462 HOH HOH B . 
IA 5 HOH 60  560 198 HOH HOH B . 
IA 5 HOH 61  561 484 HOH HOH B . 
IA 5 HOH 62  562 8   HOH HOH B . 
IA 5 HOH 63  563 43  HOH HOH B . 
IA 5 HOH 64  564 347 HOH HOH B . 
IA 5 HOH 65  565 286 HOH HOH B . 
IA 5 HOH 66  566 432 HOH HOH B . 
IA 5 HOH 67  567 230 HOH HOH B . 
IA 5 HOH 68  568 128 HOH HOH B . 
IA 5 HOH 69  569 31  HOH HOH B . 
IA 5 HOH 70  570 53  HOH HOH B . 
IA 5 HOH 71  571 24  HOH HOH B . 
IA 5 HOH 72  572 12  HOH HOH B . 
IA 5 HOH 73  573 476 HOH HOH B . 
IA 5 HOH 74  574 165 HOH HOH B . 
IA 5 HOH 75  575 32  HOH HOH B . 
IA 5 HOH 76  576 440 HOH HOH B . 
IA 5 HOH 77  577 69  HOH HOH B . 
IA 5 HOH 78  578 42  HOH HOH B . 
IA 5 HOH 79  579 72  HOH HOH B . 
IA 5 HOH 80  580 280 HOH HOH B . 
IA 5 HOH 81  581 35  HOH HOH B . 
IA 5 HOH 82  582 28  HOH HOH B . 
IA 5 HOH 83  583 229 HOH HOH B . 
IA 5 HOH 84  584 70  HOH HOH B . 
IA 5 HOH 85  585 292 HOH HOH B . 
IA 5 HOH 86  586 60  HOH HOH B . 
IA 5 HOH 87  587 269 HOH HOH B . 
IA 5 HOH 88  588 371 HOH HOH B . 
IA 5 HOH 89  589 89  HOH HOH B . 
IA 5 HOH 90  590 325 HOH HOH B . 
IA 5 HOH 91  591 531 HOH HOH B . 
IA 5 HOH 92  592 110 HOH HOH B . 
IA 5 HOH 93  593 171 HOH HOH B . 
IA 5 HOH 94  594 245 HOH HOH B . 
IA 5 HOH 95  595 244 HOH HOH B . 
IA 5 HOH 96  596 199 HOH HOH B . 
IA 5 HOH 97  597 188 HOH HOH B . 
IA 5 HOH 98  598 55  HOH HOH B . 
IA 5 HOH 99  599 101 HOH HOH B . 
IA 5 HOH 100 600 26  HOH HOH B . 
IA 5 HOH 101 601 156 HOH HOH B . 
IA 5 HOH 102 602 189 HOH HOH B . 
IA 5 HOH 103 603 38  HOH HOH B . 
IA 5 HOH 104 604 108 HOH HOH B . 
IA 5 HOH 105 605 155 HOH HOH B . 
IA 5 HOH 106 606 154 HOH HOH B . 
IA 5 HOH 107 607 107 HOH HOH B . 
IA 5 HOH 108 608 332 HOH HOH B . 
IA 5 HOH 109 609 340 HOH HOH B . 
IA 5 HOH 110 610 438 HOH HOH B . 
IA 5 HOH 111 611 304 HOH HOH B . 
IA 5 HOH 112 612 398 HOH HOH B . 
IA 5 HOH 113 613 255 HOH HOH B . 
IA 5 HOH 114 614 265 HOH HOH B . 
IA 5 HOH 115 615 223 HOH HOH B . 
IA 5 HOH 116 616 205 HOH HOH B . 
IA 5 HOH 117 617 225 HOH HOH B . 
IA 5 HOH 118 618 437 HOH HOH B . 
IA 5 HOH 119 619 151 HOH HOH B . 
IA 5 HOH 120 620 554 HOH HOH B . 
IA 5 HOH 121 621 104 HOH HOH B . 
IA 5 HOH 122 622 209 HOH HOH B . 
IA 5 HOH 123 623 39  HOH HOH B . 
IA 5 HOH 124 624 147 HOH HOH B . 
IA 5 HOH 125 625 216 HOH HOH B . 
IA 5 HOH 126 626 352 HOH HOH B . 
IA 5 HOH 127 627 395 HOH HOH B . 
IA 5 HOH 128 628 193 HOH HOH B . 
IA 5 HOH 129 629 123 HOH HOH B . 
IA 5 HOH 130 630 268 HOH HOH B . 
IA 5 HOH 131 631 34  HOH HOH B . 
IA 5 HOH 132 632 234 HOH HOH B . 
IA 5 HOH 133 633 479 HOH HOH B . 
IA 5 HOH 134 634 62  HOH HOH B . 
IA 5 HOH 135 635 291 HOH HOH B . 
IA 5 HOH 136 636 79  HOH HOH B . 
IA 5 HOH 137 637 447 HOH HOH B . 
IA 5 HOH 138 638 491 HOH HOH B . 
IA 5 HOH 139 639 547 HOH HOH B . 
IA 5 HOH 140 640 248 HOH HOH B . 
IA 5 HOH 141 641 489 HOH HOH B . 
IA 5 HOH 142 642 47  HOH HOH B . 
IA 5 HOH 143 643 528 HOH HOH B . 
IA 5 HOH 144 644 552 HOH HOH B . 
IA 5 HOH 145 645 164 HOH HOH B . 
IA 5 HOH 146 646 85  HOH HOH B . 
IA 5 HOH 147 647 148 HOH HOH B . 
IA 5 HOH 148 648 160 HOH HOH B . 
IA 5 HOH 149 649 303 HOH HOH B . 
IA 5 HOH 150 650 137 HOH HOH B . 
IA 5 HOH 151 651 219 HOH HOH B . 
IA 5 HOH 152 652 179 HOH HOH B . 
IA 5 HOH 153 653 134 HOH HOH B . 
IA 5 HOH 154 654 94  HOH HOH B . 
IA 5 HOH 155 655 411 HOH HOH B . 
IA 5 HOH 156 656 307 HOH HOH B . 
IA 5 HOH 157 657 499 HOH HOH B . 
IA 5 HOH 158 658 98  HOH HOH B . 
IA 5 HOH 159 659 549 HOH HOH B . 
IA 5 HOH 160 660 350 HOH HOH B . 
IA 5 HOH 161 661 317 HOH HOH B . 
IA 5 HOH 162 662 361 HOH HOH B . 
IA 5 HOH 163 663 383 HOH HOH B . 
IA 5 HOH 164 664 343 HOH HOH B . 
IA 5 HOH 165 665 367 HOH HOH B . 
IA 5 HOH 166 666 444 HOH HOH B . 
IA 5 HOH 167 667 249 HOH HOH B . 
IA 5 HOH 168 668 211 HOH HOH B . 
IA 5 HOH 169 669 471 HOH HOH B . 
IA 5 HOH 170 670 278 HOH HOH B . 
IA 5 HOH 171 671 379 HOH HOH B . 
IA 5 HOH 172 672 375 HOH HOH B . 
IA 5 HOH 173 673 386 HOH HOH B . 
IA 5 HOH 174 674 195 HOH HOH B . 
IA 5 HOH 175 675 442 HOH HOH B . 
IA 5 HOH 176 676 486 HOH HOH B . 
IA 5 HOH 177 677 237 HOH HOH B . 
IA 5 HOH 178 678 266 HOH HOH B . 
IA 5 HOH 179 679 481 HOH HOH B . 
IA 5 HOH 180 680 312 HOH HOH B . 
IA 5 HOH 181 681 546 HOH HOH B . 
IA 5 HOH 182 682 500 HOH HOH B . 
IA 5 HOH 183 683 472 HOH HOH B . 
IA 5 HOH 184 684 239 HOH HOH B . 
IA 5 HOH 185 685 466 HOH HOH B . 
IA 5 HOH 186 686 470 HOH HOH B . 
IA 5 HOH 187 687 530 HOH HOH B . 
IA 5 HOH 188 688 331 HOH HOH B . 
IA 5 HOH 189 689 496 HOH HOH B . 
IA 5 HOH 190 690 448 HOH HOH B . 
IA 5 HOH 191 691 461 HOH HOH B . 
IA 5 HOH 192 692 535 HOH HOH B . 
IA 5 HOH 193 693 287 HOH HOH B . 
IA 5 HOH 194 694 242 HOH HOH B . 
IA 5 HOH 195 695 207 HOH HOH B . 
IA 5 HOH 196 696 460 HOH HOH B . 
IA 5 HOH 197 697 427 HOH HOH B . 
IA 5 HOH 198 698 487 HOH HOH B . 
IA 5 HOH 199 699 392 HOH HOH B . 
IA 5 HOH 200 700 451 HOH HOH B . 
IA 5 HOH 201 701 446 HOH HOH B . 
IA 5 HOH 202 702 439 HOH HOH B . 
IA 5 HOH 203 703 558 HOH HOH B . 
IA 5 HOH 204 704 54  HOH HOH B . 
IA 5 HOH 205 705 483 HOH HOH B . 
IA 5 HOH 206 706 308 HOH HOH B . 
IA 5 HOH 207 707 279 HOH HOH B . 
IA 5 HOH 208 708 514 HOH HOH B . 
IA 5 HOH 209 709 477 HOH HOH B . 
IA 5 HOH 210 710 401 HOH HOH B . 
IA 5 HOH 211 711 310 HOH HOH B . 
IA 5 HOH 212 712 184 HOH HOH B . 
IA 5 HOH 213 713 387 HOH HOH B . 
IA 5 HOH 214 714 441 HOH HOH B . 
IA 5 HOH 215 715 482 HOH HOH B . 
IA 5 HOH 216 716 497 HOH HOH B . 
IA 5 HOH 217 717 346 HOH HOH B . 
IA 5 HOH 218 718 120 HOH HOH B . 
IA 5 HOH 219 719 435 HOH HOH B . 
IA 5 HOH 220 720 544 HOH HOH B . 
IA 5 HOH 221 721 355 HOH HOH B . 
IA 5 HOH 222 722 501 HOH HOH B . 
IA 5 HOH 223 723 533 HOH HOH B . 
IA 5 HOH 224 724 467 HOH HOH B . 
IA 5 HOH 225 725 493 HOH HOH B . 
IA 5 HOH 226 726 327 HOH HOH B . 
IA 5 HOH 227 727 434 HOH HOH B . 
IA 5 HOH 228 728 380 HOH HOH B . 
IA 5 HOH 229 729 449 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.2_4158 1 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? 1.19.2_4158 2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .           3 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           4 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   97.830 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8OTU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     141.133 
_cell.length_a_esd                 ? 
_cell.length_b                     45.660 
_cell.length_b_esd                 ? 
_cell.length_c                     84.187 
_cell.length_c_esd                 ? 
_cell.volume                       537454.172 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8OTU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            'C 2y' 
_symmetry.space_group_name_H-M             'C 1 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                   8OTU 
_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             1.93 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          36.43 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.1 M HEPES pH 7.5, 10%
(w/v) PEG 8000, 10% ethylene glycol
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            285 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-08-19 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9795 
_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                        'PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'P13 (MX1)' 
_diffrn_source.pdbx_synchrotron_site       'PETRA III, EMBL c/o DESY' 
# 
_reflns.B_iso_Wilson_estimate                          18.15 
_reflns.entry_id                                       8OTU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.40 
_reflns.d_resolution_low                               57.58 
_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                                     100380 
_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                           95.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          21.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   1.000 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.036 
_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                                    1.40 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3171 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.785 
_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                                  0.565 
_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                               25.37 
_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                                 8OTU 
_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                            1.40 
_refine.ls_d_res_low                             50.31 
_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                     100364 
_refine.ls_number_reflns_R_free                  5036 
_refine.ls_number_reflns_R_work                  95328 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.68 
_refine.ls_percent_reflns_R_free                 5.02 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1328 
_refine.ls_R_factor_R_free                       0.1498 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1319 
_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                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 14.8428 
_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                            0.1178 
_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                       1.40 
_refine_hist.d_res_low                        50.31 
_refine_hist.number_atoms_solvent             477 
_refine_hist.number_atoms_total               4624 
_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        4041 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         106 
_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' ? 0.0109  ? 4312 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1565  ? 5834 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0855  ? 609  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0124  ? 778  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 12.3347 ? 1555 ? 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' 1.40 1.42  . . 97  1812 55.80 . . . . 0.2856 . . . . . . . . . . . 0.2859 
'X-RAY DIFFRACTION' 1.42 1.43  . . 146 2600 78.37 . . . . 0.2377 . . . . . . . . . . . 0.2528 
'X-RAY DIFFRACTION' 1.43 1.45  . . 164 3061 92.54 . . . . 0.1953 . . . . . . . . . . . 0.1918 
'X-RAY DIFFRACTION' 1.45 1.47  . . 192 3069 94.30 . . . . 0.1755 . . . . . . . . . . . 0.2247 
'X-RAY DIFFRACTION' 1.47 1.49  . . 177 3140 95.70 . . . . 0.1643 . . . . . . . . . . . 0.1751 
'X-RAY DIFFRACTION' 1.49 1.51  . . 178 3154 96.22 . . . . 0.1594 . . . . . . . . . . . 0.1951 
'X-RAY DIFFRACTION' 1.51 1.53  . . 182 3177 96.58 . . . . 0.1529 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 1.53 1.55  . . 163 3196 97.08 . . . . 0.1515 . . . . . . . . . . . 0.2024 
'X-RAY DIFFRACTION' 1.55 1.58  . . 138 3287 97.22 . . . . 0.1494 . . . . . . . . . . . 0.1583 
'X-RAY DIFFRACTION' 1.58 1.60  . . 171 3161 96.95 . . . . 0.1480 . . . . . . . . . . . 0.1706 
'X-RAY DIFFRACTION' 1.60 1.63  . . 174 3238 97.12 . . . . 0.1493 . . . . . . . . . . . 0.1534 
'X-RAY DIFFRACTION' 1.63 1.66  . . 167 3208 97.21 . . . . 0.1463 . . . . . . . . . . . 0.1697 
'X-RAY DIFFRACTION' 1.66 1.69  . . 165 3249 97.43 . . . . 0.1336 . . . . . . . . . . . 0.1301 
'X-RAY DIFFRACTION' 1.69 1.73  . . 171 3206 97.52 . . . . 0.1313 . . . . . . . . . . . 0.1630 
'X-RAY DIFFRACTION' 1.73 1.76  . . 173 3240 97.74 . . . . 0.1268 . . . . . . . . . . . 0.1471 
'X-RAY DIFFRACTION' 1.76 1.80  . . 173 3236 97.90 . . . . 0.1251 . . . . . . . . . . . 0.1616 
'X-RAY DIFFRACTION' 1.80 1.85  . . 191 3208 97.98 . . . . 0.1244 . . . . . . . . . . . 0.1409 
'X-RAY DIFFRACTION' 1.85 1.90  . . 154 3295 98.18 . . . . 0.1247 . . . . . . . . . . . 0.1293 
'X-RAY DIFFRACTION' 1.90 1.96  . . 170 3243 98.10 . . . . 0.1274 . . . . . . . . . . . 0.1536 
'X-RAY DIFFRACTION' 1.96 2.02  . . 195 3234 98.42 . . . . 0.1234 . . . . . . . . . . . 0.1408 
'X-RAY DIFFRACTION' 2.02 2.09  . . 171 3283 98.54 . . . . 0.1230 . . . . . . . . . . . 0.1340 
'X-RAY DIFFRACTION' 2.09 2.18  . . 152 3319 98.61 . . . . 0.1184 . . . . . . . . . . . 0.1187 
'X-RAY DIFFRACTION' 2.18 2.27  . . 186 3265 98.74 . . . . 0.1202 . . . . . . . . . . . 0.1403 
'X-RAY DIFFRACTION' 2.27 2.39  . . 175 3306 98.98 . . . . 0.1174 . . . . . . . . . . . 0.1360 
'X-RAY DIFFRACTION' 2.39 2.54  . . 137 3311 99.08 . . . . 0.1143 . . . . . . . . . . . 0.1358 
'X-RAY DIFFRACTION' 2.54 2.74  . . 170 3321 99.20 . . . . 0.1162 . . . . . . . . . . . 0.1473 
'X-RAY DIFFRACTION' 2.74 3.02  . . 173 3328 99.38 . . . . 0.1181 . . . . . . . . . . . 0.1339 
'X-RAY DIFFRACTION' 3.02 3.45  . . 178 3326 99.46 . . . . 0.1221 . . . . . . . . . . . 0.1630 
'X-RAY DIFFRACTION' 3.45 4.35  . . 180 3390 99.69 . . . . 0.1261 . . . . . . . . . . . 0.1314 
'X-RAY DIFFRACTION' 4.35 50.31 . . 173 3465 99.43 . . . . 0.1648 . . . . . . . . . . . 0.1688 
# 
_struct.entry_id                     8OTU 
_struct.title                        'The crystal structure of PET44, a PETase enzyme from Alkalilimnicola ehrlichii' 
_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        8OTU 
_struct_keywords.text            'PETase, PET, enzyme, hydrolase, esterase, plastic, degradation, biotech, enzyme evolution' 
_struct_keywords.pdbx_keywords   HYDROLASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 2 ? 
D  N N 3 ? 
E  N N 3 ? 
F  N N 3 ? 
G  N N 3 ? 
H  N N 3 ? 
I  N N 3 ? 
J  N N 3 ? 
K  N N 3 ? 
L  N N 3 ? 
M  N N 3 ? 
N  N N 3 ? 
O  N N 3 ? 
P  N N 3 ? 
Q  N N 3 ? 
R  N N 3 ? 
S  N N 3 ? 
T  N N 4 ? 
U  N N 4 ? 
V  N N 2 ? 
W  N N 2 ? 
X  N N 3 ? 
Y  N N 3 ? 
Z  N N 3 ? 
AA N N 3 ? 
BA N N 3 ? 
CA N N 3 ? 
DA N N 3 ? 
EA N N 3 ? 
FA N N 3 ? 
GA N N 4 ? 
HA N N 5 ? 
IA N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A3E0WVY1_9GAMM 
_struct_ref.pdbx_db_accession          A0A3E0WVY1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSSIIKRKLASLFAFSAAMLLSTSVWSMNPGDVPDTCEGDCGYARGPDPTESFLEADSGPYTIATSNVSSLVRGFGGGTI
YYPVNAEGTMAAIVVIPGYMSYQSSISFWGPRLASHGFVVMTIDTNRISDQPPSRRDQIEAALEYLVDQSNSSRSPINGM
VDPNRLGAVGWSMGGGGTLRLAADDGIQAAIGLAPWNTSSLGFRSIETPTLIFACERDSIAPVRSHASPFYNAIPSSTDK
AYFEISGGNHYCANGSNRYDALLGKYGVAWMKLHLDQDQRYAPFLCGPNHERDRQISEHRSTCPF
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8OTU A 1 ? 305 ? A0A3E0WVY1 1 ? 305 ? 1 305 
2 1 8OTU B 1 ? 305 ? A0A3E0WVY1 1 ? 305 ? 1 305 
# 
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 8OTU VAL A 306 ? UNP A0A3E0WVY1 ? ? 'expression tag' 306 1  
1 8OTU ASP A 307 ? UNP A0A3E0WVY1 ? ? 'expression tag' 307 2  
1 8OTU LYS A 308 ? UNP A0A3E0WVY1 ? ? 'expression tag' 308 3  
1 8OTU LEU A 309 ? UNP A0A3E0WVY1 ? ? 'expression tag' 309 4  
1 8OTU ALA A 310 ? UNP A0A3E0WVY1 ? ? 'expression tag' 310 5  
1 8OTU ALA A 311 ? UNP A0A3E0WVY1 ? ? 'expression tag' 311 6  
1 8OTU ALA A 312 ? UNP A0A3E0WVY1 ? ? 'expression tag' 312 7  
1 8OTU LEU A 313 ? UNP A0A3E0WVY1 ? ? 'expression tag' 313 8  
1 8OTU GLU A 314 ? UNP A0A3E0WVY1 ? ? 'expression tag' 314 9  
1 8OTU HIS A 315 ? UNP A0A3E0WVY1 ? ? 'expression tag' 315 10 
1 8OTU HIS A 316 ? UNP A0A3E0WVY1 ? ? 'expression tag' 316 11 
1 8OTU HIS A 317 ? UNP A0A3E0WVY1 ? ? 'expression tag' 317 12 
1 8OTU HIS A 318 ? UNP A0A3E0WVY1 ? ? 'expression tag' 318 13 
1 8OTU HIS A 319 ? UNP A0A3E0WVY1 ? ? 'expression tag' 319 14 
1 8OTU HIS A 320 ? UNP A0A3E0WVY1 ? ? 'expression tag' 320 15 
2 8OTU VAL B 306 ? UNP A0A3E0WVY1 ? ? 'expression tag' 306 16 
2 8OTU ASP B 307 ? UNP A0A3E0WVY1 ? ? 'expression tag' 307 17 
2 8OTU LYS B 308 ? UNP A0A3E0WVY1 ? ? 'expression tag' 308 18 
2 8OTU LEU B 309 ? UNP A0A3E0WVY1 ? ? 'expression tag' 309 19 
2 8OTU ALA B 310 ? UNP A0A3E0WVY1 ? ? 'expression tag' 310 20 
2 8OTU ALA B 311 ? UNP A0A3E0WVY1 ? ? 'expression tag' 311 21 
2 8OTU ALA B 312 ? UNP A0A3E0WVY1 ? ? 'expression tag' 312 22 
2 8OTU LEU B 313 ? UNP A0A3E0WVY1 ? ? 'expression tag' 313 23 
2 8OTU GLU B 314 ? UNP A0A3E0WVY1 ? ? 'expression tag' 314 24 
2 8OTU HIS B 315 ? UNP A0A3E0WVY1 ? ? 'expression tag' 315 25 
2 8OTU HIS B 316 ? UNP A0A3E0WVY1 ? ? 'expression tag' 316 26 
2 8OTU HIS B 317 ? UNP A0A3E0WVY1 ? ? 'expression tag' 317 27 
2 8OTU HIS B 318 ? UNP A0A3E0WVY1 ? ? 'expression tag' 318 28 
2 8OTU HIS B 319 ? UNP A0A3E0WVY1 ? ? 'expression tag' 319 29 
2 8OTU HIS B 320 ? UNP A0A3E0WVY1 ? ? 'expression tag' 320 30 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q,R,S,T,U,HA 
2 1 B,V,W,X,Y,Z,AA,BA,CA,DA,EA,FA,GA,IA        
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 50  ? ALA A 56  ? THR A 50  ALA A 56  1 ? 7  
HELX_P HELX_P2  AA2 TYR A 102 ? SER A 107 ? TYR A 102 SER A 107 5 ? 6  
HELX_P HELX_P3  AA3 PHE A 108 ? SER A 115 ? PHE A 108 SER A 115 1 ? 8  
HELX_P HELX_P4  AA4 GLN A 131 ? ASN A 151 ? GLN A 131 ASN A 151 1 ? 21 
HELX_P HELX_P5  AA5 SER A 172 ? ASP A 184 ? SER A 172 ASP A 184 1 ? 13 
HELX_P HELX_P6  AA6 SER A 200 ? ARG A 204 ? SER A 200 ARG A 204 5 ? 5  
HELX_P HELX_P7  AA7 HIS A 226 ? ILE A 234 ? HIS A 226 ILE A 234 1 ? 9  
HELX_P HELX_P8  AA8 TYR A 251 ? GLY A 255 ? TYR A 251 GLY A 255 5 ? 5  
HELX_P HELX_P9  AA9 TYR A 259 ? ASP A 276 ? TYR A 259 ASP A 276 1 ? 18 
HELX_P HELX_P10 AB1 ASP A 278 ? ARG A 280 ? ASP A 278 ARG A 280 5 ? 3  
HELX_P HELX_P11 AB2 TYR A 281 ? CYS A 286 ? TYR A 281 CYS A 286 1 ? 6  
HELX_P HELX_P12 AB3 ASN A 289 ? ASP A 293 ? ASN A 289 ASP A 293 5 ? 5  
HELX_P HELX_P13 AB4 THR B 50  ? ALA B 56  ? THR B 50  ALA B 56  1 ? 7  
HELX_P HELX_P14 AB5 TYR B 102 ? SER B 107 ? TYR B 102 SER B 107 5 ? 6  
HELX_P HELX_P15 AB6 PHE B 108 ? SER B 115 ? PHE B 108 SER B 115 1 ? 8  
HELX_P HELX_P16 AB7 GLN B 131 ? ASN B 151 ? GLN B 131 ASN B 151 1 ? 21 
HELX_P HELX_P17 AB8 SER B 172 ? ASP B 184 ? SER B 172 ASP B 184 1 ? 13 
HELX_P HELX_P18 AB9 SER B 200 ? ARG B 204 ? SER B 200 ARG B 204 5 ? 5  
HELX_P HELX_P19 AC1 HIS B 226 ? ILE B 234 ? HIS B 226 ILE B 234 1 ? 9  
HELX_P HELX_P20 AC2 TYR B 251 ? GLY B 255 ? TYR B 251 GLY B 255 5 ? 5  
HELX_P HELX_P21 AC3 TYR B 259 ? ASP B 276 ? TYR B 259 ASP B 276 1 ? 18 
HELX_P HELX_P22 AC4 ASP B 278 ? LEU B 285 ? ASP B 278 LEU B 285 5 ? 8  
HELX_P HELX_P23 AC5 ASN B 289 ? ASP B 293 ? ASN B 289 ASP B 293 5 ? 5  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 215 SG ? ? ? 1_555 A  CYS 252 SG ? ? A CYS 215 A CYS 252 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
disulf2  disulf ? ? A CYS 286 SG ? ? ? 1_555 A  CYS 303 SG ? ? A CYS 286 A CYS 303 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
disulf3  disulf ? ? B CYS 215 SG ? ? ? 1_555 B  CYS 252 SG ? ? B CYS 215 B CYS 252 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
disulf4  disulf ? ? B CYS 286 SG ? ? ? 1_555 B  CYS 303 SG ? ? B CYS 286 B CYS 303 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc1  metalc ? ? A SER 70  O  ? ? ? 1_555 C  NA  .   NA ? ? A SER 70  A NA  401 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc2  metalc ? ? A VAL 72  O  ? ? ? 1_555 C  NA  .   NA ? ? A VAL 72  A NA  401 1_555 ? ? ? ? ? ? ? 2.245 ? ? 
metalc3  metalc ? ? A PHE 75  O  ? ? ? 1_555 C  NA  .   NA ? ? A PHE 75  A NA  401 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc4  metalc ? ? A SER 153 O  ? ? ? 1_555 W  NA  .   NA ? ? A SER 153 B NA  402 4_446 ? ? ? ? ? ? ? 2.292 ? ? 
metalc5  metalc ? ? C NA  .   NA ? ? ? 1_555 Q  EDO .   O2 ? ? A NA  401 A EDO 415 1_555 ? ? ? ? ? ? ? 2.439 ? ? 
metalc6  metalc ? ? C NA  .   NA ? ? ? 1_555 HA HOH .   O  ? ? A NA  401 A HOH 585 1_555 ? ? ? ? ? ? ? 2.672 ? ? 
metalc7  metalc ? ? C NA  .   NA ? ? ? 1_555 HA HOH .   O  ? ? A NA  401 A HOH 675 1_555 ? ? ? ? ? ? ? 2.368 ? ? 
metalc8  metalc ? ? B SER 70  O  ? ? ? 1_555 V  NA  .   NA ? ? B SER 70  B NA  401 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc9  metalc ? ? B VAL 72  O  ? ? ? 1_555 V  NA  .   NA ? ? B VAL 72  B NA  401 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc10 metalc ? ? B PHE 75  O  ? ? ? 1_555 V  NA  .   NA ? ? B PHE 75  B NA  401 1_555 ? ? ? ? ? ? ? 2.312 ? ? 
metalc11 metalc ? ? B GLU 291 O  ? ? ? 1_555 W  NA  .   NA ? ? B GLU 291 B NA  402 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc12 metalc ? ? B ASP 293 O  ? ? ? 1_555 W  NA  .   NA ? ? B ASP 293 B NA  402 1_555 ? ? ? ? ? ? ? 2.479 ? ? 
metalc13 metalc ? ? B ILE 296 O  ? ? ? 1_555 W  NA  .   NA ? ? B ILE 296 B NA  402 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc14 metalc ? ? V NA  .   NA ? ? ? 1_555 IA HOH .   O  ? ? B NA  401 B HOH 560 1_555 ? ? ? ? ? ? ? 2.649 ? ? 
metalc15 metalc ? ? V NA  .   NA ? ? ? 1_555 IA HOH .   O  ? ? B NA  401 B HOH 652 1_555 ? ? ? ? ? ? ? 2.363 ? ? 
metalc16 metalc ? ? V NA  .   NA ? ? ? 1_555 IA HOH .   O  ? ? B NA  401 B HOH 683 1_555 ? ? ? ? ? ? ? 2.414 ? ? 
metalc17 metalc ? ? W NA  .   NA ? ? ? 1_555 IA HOH .   O  ? ? B NA  402 B HOH 605 1_555 ? ? ? ? ? ? ? 2.503 ? ? 
metalc18 metalc ? ? W NA  .   NA ? ? ? 1_555 IA HOH .   O  ? ? B NA  402 B HOH 665 1_555 ? ? ? ? ? ? ? 2.549 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
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  SER 70  ? A SER 70  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? A  VAL 72  ? A VAL 72  ? 1_555 99.0  ? 
2  O  ? A  SER 70  ? A SER 70  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? A  PHE 75  ? A PHE 75  ? 1_555 108.8 ? 
3  O  ? A  VAL 72  ? A VAL 72  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? A  PHE 75  ? A PHE 75  ? 1_555 87.4  ? 
4  O  ? A  SER 70  ? A SER 70  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O2 ? Q  EDO .   ? A EDO 415 ? 1_555 94.7  ? 
5  O  ? A  VAL 72  ? A VAL 72  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O2 ? Q  EDO .   ? A EDO 415 ? 1_555 162.2 ? 
6  O  ? A  PHE 75  ? A PHE 75  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O2 ? Q  EDO .   ? A EDO 415 ? 1_555 77.4  ? 
7  O  ? A  SER 70  ? A SER 70  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 585 ? 1_555 163.9 ? 
8  O  ? A  VAL 72  ? A VAL 72  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 585 ? 1_555 92.1  ? 
9  O  ? A  PHE 75  ? A PHE 75  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 585 ? 1_555 83.2  ? 
10 O2 ? Q  EDO .   ? A EDO 415 ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 585 ? 1_555 77.2  ? 
11 O  ? A  SER 70  ? A SER 70  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 675 ? 1_555 91.8  ? 
12 O  ? A  VAL 72  ? A VAL 72  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 675 ? 1_555 83.4  ? 
13 O  ? A  PHE 75  ? A PHE 75  ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 675 ? 1_555 158.5 ? 
14 O2 ? Q  EDO .   ? A EDO 415 ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 675 ? 1_555 107.6 ? 
15 O  ? HA HOH .   ? A HOH 585 ? 1_555 NA ? C NA . ? A NA 401 ? 1_555 O  ? HA HOH .   ? A HOH 675 ? 1_555 77.8  ? 
16 O  ? A  SER 153 ? A SER 153 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? B  GLU 291 ? B GLU 291 ? 1_555 61.8  ? 
17 O  ? A  SER 153 ? A SER 153 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? B  ASP 293 ? B ASP 293 ? 1_555 57.7  ? 
18 O  ? B  GLU 291 ? B GLU 291 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? B  ASP 293 ? B ASP 293 ? 1_555 4.5   ? 
19 O  ? A  SER 153 ? A SER 153 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? B  ILE 296 ? B ILE 296 ? 1_555 58.1  ? 
20 O  ? B  GLU 291 ? B GLU 291 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? B  ILE 296 ? B ILE 296 ? 1_555 3.7   ? 
21 O  ? B  ASP 293 ? B ASP 293 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? B  ILE 296 ? B ILE 296 ? 1_555 1.6   ? 
22 O  ? A  SER 153 ? A SER 153 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 605 ? 1_555 58.8  ? 
23 O  ? B  GLU 291 ? B GLU 291 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 605 ? 1_555 5.9   ? 
24 O  ? B  ASP 293 ? B ASP 293 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 605 ? 1_555 3.5   ? 
25 O  ? B  ILE 296 ? B ILE 296 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 605 ? 1_555 4.9   ? 
26 O  ? A  SER 153 ? A SER 153 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 665 ? 1_555 61.7  ? 
27 O  ? B  GLU 291 ? B GLU 291 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 665 ? 1_555 4.2   ? 
28 O  ? B  ASP 293 ? B ASP 293 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 665 ? 1_555 4.7   ? 
29 O  ? B  ILE 296 ? B ILE 296 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 665 ? 1_555 5.4   ? 
30 O  ? IA HOH .   ? B HOH 605 ? 1_555 NA ? W NA . ? B NA 402 ? 4_446 O  ? IA HOH .   ? B HOH 665 ? 1_555 3.1   ? 
31 O  ? B  SER 70  ? B SER 70  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? B  VAL 72  ? B VAL 72  ? 1_555 98.0  ? 
32 O  ? B  SER 70  ? B SER 70  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? B  PHE 75  ? B PHE 75  ? 1_555 110.4 ? 
33 O  ? B  VAL 72  ? B VAL 72  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? B  PHE 75  ? B PHE 75  ? 1_555 87.3  ? 
34 O  ? B  SER 70  ? B SER 70  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 560 ? 1_555 166.6 ? 
35 O  ? B  VAL 72  ? B VAL 72  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 560 ? 1_555 88.0  ? 
36 O  ? B  PHE 75  ? B PHE 75  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 560 ? 1_555 81.7  ? 
37 O  ? B  SER 70  ? B SER 70  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 652 ? 1_555 91.1  ? 
38 O  ? B  VAL 72  ? B VAL 72  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 652 ? 1_555 170.5 ? 
39 O  ? B  PHE 75  ? B PHE 75  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 652 ? 1_555 87.0  ? 
40 O  ? IA HOH .   ? B HOH 560 ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 652 ? 1_555 83.6  ? 
41 O  ? B  SER 70  ? B SER 70  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 683 ? 1_555 91.3  ? 
42 O  ? B  VAL 72  ? B VAL 72  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 683 ? 1_555 87.2  ? 
43 O  ? B  PHE 75  ? B PHE 75  ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 683 ? 1_555 158.1 ? 
44 O  ? IA HOH .   ? B HOH 560 ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 683 ? 1_555 77.0  ? 
45 O  ? IA HOH .   ? B HOH 652 ? 1_555 NA ? V NA . ? B NA 401 ? 1_555 O  ? IA HOH .   ? B HOH 683 ? 1_555 95.3  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 215 ? CYS A 252 ? CYS A 215 ? 1_555 CYS A 252 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 286 ? CYS A 303 ? CYS A 286 ? 1_555 CYS A 303 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS B 215 ? CYS B 252 ? CYS B 215 ? 1_555 CYS B 252 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 286 ? CYS B 303 ? CYS B 286 ? 1_555 CYS B 303 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 CYS 303 A . ? CYS 303 A PRO 304 A ? PRO 304 A 1 -0.70 
2 CYS 303 B . ? CYS 303 B PRO 304 B ? PRO 304 B 1 -4.71 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA2 4 5 ? parallel      
AA2 5 6 ? parallel      
AA2 6 7 ? parallel      
AA2 7 8 ? parallel      
AA2 8 9 ? 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 ILE A 63  ? VAL A 68  ? ILE A 63  VAL A 68  
AA1 2 GLY A 78  ? PRO A 83  ? GLY A 78  PRO A 83  
AA1 3 VAL A 119 ? ILE A 123 ? VAL A 119 ILE A 123 
AA1 4 MET A 90  ? ILE A 96  ? MET A 90  ILE A 96  
AA1 5 VAL A 161 ? TRP A 171 ? VAL A 161 TRP A 171 
AA1 6 ALA A 189 ? LEU A 193 ? ALA A 189 LEU A 193 
AA1 7 THR A 210 ? CYS A 215 ? THR A 210 CYS A 215 
AA1 8 LYS A 240 ? ILE A 245 ? LYS A 240 ILE A 245 
AA1 9 ILE A 296 ? SER A 301 ? ILE A 296 SER A 301 
AA2 1 ILE B 63  ? VAL B 68  ? ILE B 63  VAL B 68  
AA2 2 GLY B 78  ? PRO B 83  ? GLY B 78  PRO B 83  
AA2 3 VAL B 119 ? ILE B 123 ? VAL B 119 ILE B 123 
AA2 4 MET B 90  ? ILE B 96  ? MET B 90  ILE B 96  
AA2 5 VAL B 161 ? TRP B 171 ? VAL B 161 TRP B 171 
AA2 6 ALA B 189 ? LEU B 193 ? ALA B 189 LEU B 193 
AA2 7 THR B 210 ? CYS B 215 ? THR B 210 CYS B 215 
AA2 8 LYS B 240 ? ILE B 245 ? LYS B 240 ILE B 245 
AA2 9 ILE B 296 ? SER B 301 ? ILE B 296 SER B 301 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 68  ? N VAL A 68  O GLY A 78  ? O GLY A 78  
AA1 2 3 N TYR A 81  ? N TYR A 81  O VAL A 120 ? O VAL A 120 
AA1 3 4 O ILE A 123 ? O ILE A 123 N VAL A 95  ? N VAL A 95  
AA1 4 5 N MET A 90  ? N MET A 90  O ASP A 162 ? O ASP A 162 
AA1 5 6 N GLY A 170 ? N GLY A 170 O LEU A 193 ? O LEU A 193 
AA1 6 7 N GLY A 192 ? N GLY A 192 O PHE A 213 ? O PHE A 213 
AA1 7 8 N ALA A 214 ? N ALA A 214 O ILE A 245 ? O ILE A 245 
AA1 8 9 N GLU A 244 ? N GLU A 244 O GLU A 298 ? O GLU A 298 
AA2 1 2 N VAL B 68  ? N VAL B 68  O GLY B 78  ? O GLY B 78  
AA2 2 3 N TYR B 81  ? N TYR B 81  O VAL B 120 ? O VAL B 120 
AA2 3 4 O ILE B 123 ? O ILE B 123 N VAL B 95  ? N VAL B 95  
AA2 4 5 N MET B 90  ? N MET B 90  O ASP B 162 ? O ASP B 162 
AA2 5 6 N GLY B 170 ? N GLY B 170 O LEU B 193 ? O LEU B 193 
AA2 6 7 N GLY B 192 ? N GLY B 192 O PHE B 213 ? O PHE B 213 
AA2 7 8 N ALA B 214 ? N ALA B 214 O ILE B 245 ? O ILE B 245 
AA2 8 9 N GLU B 244 ? N GLU B 244 O GLU B 298 ? O GLU B 298 
# 
_pdbx_entry_details.entry_id                   8OTU 
_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   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 SER A 172 ? ? 59.96   -125.67 
2 1 HIS A 226 ? ? -129.09 -91.12  
3 1 SER B 172 ? ? 63.52   -124.24 
4 1 HIS B 226 ? ? -129.36 -87.09  
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     597 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   HA 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z           
2 -x,y,-z         
3 x+1/2,y+1/2,z   
4 -x+1/2,y+1/2,-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 -10.4215437279 -13.5762082192 37.4457766531  0.215089750386 ? 0.000663802891468 ? 
0.00413983929157  ? 0.15271977814  ? -0.0239056450249  ? 0.185823614465 ? 0.107036763281  ? 0.00492179789705  ? -0.0473455047053 ? 
0.13820687196   ? -0.0566165005631  ? 0.250329184351   ? 0.111677139548    ? -0.199490615686  ? 0.189389296054    ? 0.101586660185 
? -0.0845995226414 ? -0.0652861857668 ? -0.125888476643   ? 0.0588038665224  ? -0.00181098563005  ? 
2  'X-RAY DIFFRACTION' ? refined -16.1080061821 -33.2980792774 35.6079364984  0.252181941263 ? -0.0185934848979  ? 
-0.00156758246123 ? 0.170286964684 ? 0.0117857910908   ? 0.185437087091 ? 0.380365802079  ? 0.0821093765678   ? 0.122573726514   ? 
0.23913736979   ? -0.039611203211   ? 0.270107775197   ? 0.0218030976631   ? -0.153690279343  ? -0.158256137254   ? 0.264144788862 
? -0.0838763423332 ? 0.0028566743386  ? 0.216056304759    ? -0.269472451769  ? 0.00456620647184   ? 
3  'X-RAY DIFFRACTION' ? refined -16.138498935  -29.3907299552 23.2294881858  0.170832145915 ? 0.0207743145374   ? 
-0.00597653962969 ? 0.156655056092 ? -0.0131108974473  ? 0.138019964621 ? 1.10952965687   ? 0.188975086935    ? -0.250184443225  ? 
0.644060684401  ? -0.0568167945382  ? 0.792042696083   ? 0.0201816279053   ? 0.1541267908     ? -0.067427437401   ? 
0.00542932964124   ? -0.0419386946466 ? 0.0012964810226  ? 0.095167457984    ? -0.161983895921  ? -4.81362610219e-08 ? 
4  'X-RAY DIFFRACTION' ? refined -4.5198519187  -20.4750988985 12.2119610851  0.167240136409 ? 0.0544600231326   ? 0.0209893671647 
? 0.253344625471 ? 0.0420155484743   ? 0.17390740904  ? 0.0978016458833 ? 0.0368298950742   ? 0.0974502191613  ? 0.173516755703  ? 
-0.0355395201022  ? 0.0948844833611  ? 0.0333524971389   ? 0.400431368266   ? 0.248347247275    ? -0.0440784144242   ? 
-0.0511526078538 ? -0.114159929277  ? -0.0212895212243  ? -0.0538095055909 ? -0.0029474754042   ? 
5  'X-RAY DIFFRACTION' ? refined -8.1651756418  -16.9611881    19.8567965356  0.170355700798 ? 0.0529884703806   ? 0.0080566324426 
? 0.166098769742 ? 0.0386927770966   ? 0.172425412434 ? 0.444326551286  ? 0.335022131555    ? -0.153081769566  ? 0.295616133512  ? 
0.0553915334291   ? 0.303657521311   ? 0.0731849900469   ? 0.126431535038   ? 0.157046078258    ? 0.0146364744372    ? 
-0.0390992050059 ? -0.0740053599894 ? -0.0783099014961  ? -0.0144539882351 ? 0.0194994436131    ? 
6  'X-RAY DIFFRACTION' ? refined -9.13416590792 -7.7426257482  22.8207782897  0.278369423197 ? 0.0478094728942   ? 0.0497029753866 
? 0.168580933681 ? 0.0618736986949   ? 0.291846492264 ? 0.0733632525407 ? -0.0596244785629  ? -0.0662906251509 ? 0.0555911165099 ? 
0.150792409514    ? 0.208790507088   ? 0.259664290413    ? 0.150657754052   ? 0.405413351485    ? 0.0244602752767    ? 
-0.072126840065  ? -0.0243966145834 ? -0.38985209288    ? -0.0782080117723 ? -0.0862051833711   ? 
7  'X-RAY DIFFRACTION' ? refined -60.6140590473 -4.17374727744 15.1042915239  0.180594986397 ? 0.0321450744949   ? 0.0150287942924 
? 0.22660019905  ? 0.0170684638504   ? 0.19966530231  ? 0.164216356651  ? -0.12052253011    ? 0.121337085206   ? 0.110283730983  ? 
0.0471577393278   ? 0.15649567702    ? 0.0108015946245   ? 0.0803534962488  ? 0.118445004694    ? -0.00365857245305  ? 
0.0434388383834  ? 0.0844121613041  ? -0.0480239624194  ? -0.0966247942301 ? 2.46094867811e-07  ? 
8  'X-RAY DIFFRACTION' ? refined -50.6946647173 -14.08484314   1.78855353667  0.200669281391 ? 0.0428436767737   ? 
-0.0190434004677  ? 0.290756847689 ? -0.0348675001735  ? 0.184394279104 ? 0.176120784689  ? 0.167322470678    ? -0.0116841482431 ? 
0.35247375477   ? -0.118954483169   ? 0.286186987485   ? 0.0240414098838   ? 0.388615883957   ? 0.00335763669625  ? 
-0.0802332243684   ? -0.0250391236016 ? 0.0882085898882  ? 0.0408903635729   ? 0.055065170546   ? 0.0333916820136    ? 
9  'X-RAY DIFFRACTION' ? refined -45.1134818146 -19.3274703885 9.34535167516  0.176564757874 ? 0.0550286543646   ? -0.013774371918 
? 0.209719149517 ? -0.0364725702966  ? 0.199941655263 ? 0.354137227787  ? 0.119132598754    ? 0.283106658989   ? 0.353869702751  ? 
-0.143019185388   ? 0.507029887672   ? 0.0812740887351   ? 0.228702849831   ? -0.119033490958   ? -0.0295302670007   ? 
-0.0409005538234 ? -0.0116291762435 ? 0.104671915198    ? 0.0928974554669  ? -0.000688320146994 ? 
10 'X-RAY DIFFRACTION' ? refined -46.801842811  -6.12724889931 -1.45984748616 0.19351204839  ? 0.00325440988847  ? 0.0134854145654 
? 0.327416673825 ? 0.0180582144468   ? 0.202860759736 ? 0.0157387753498 ? -0.0142870634854  ? 0.0271295788956  ? 0.0140800537258 ? 
-0.0193426589981  ? 0.0287548395199  ? 0.0793772320566   ? 0.253252335555   ? 0.0347994703894   ? -0.0248082836853   ? 
0.0104142204438  ? -0.0752438660338 ? -0.0751808800873  ? 0.174166878263   ? -5.68817863594e-07 ? 
11 'X-RAY DIFFRACTION' ? refined -37.9432052671 -15.5431235077 19.6376815663  0.172194198955 ? 0.0539315897488   ? 
-0.0224585279715  ? 0.227709797035 ? -0.00643114414183 ? 0.223885276158 ? 0.22199723431   ? -0.229188909198   ? 0.0602196639333  ? 
0.135120714073  ? -0.00270841163609 ? 0.143017699277   ? -0.0318158260262  ? 0.0396948897267  ? -0.00403321171536 ? 
-0.000482982096437 ? 0.0143966964836  ? -0.130851456112  ? 0.058379191363    ? 0.238683062011   ? 0.0125056893638    ? 
12 'X-RAY DIFFRACTION' ? refined -45.2245180651 -20.7738608871 28.2791390235  0.219483354041 ? 0.0689373149106   ? 
-0.00122253141627 ? 0.205013094907 ? 0.0388681953221   ? 0.215992195556 ? 0.157337467661  ? -0.00417612939498 ? 0.0423280139476  ? 
0.0803708361773 ? 0.0989537668512   ? 0.139587353239   ? -0.0591272462567  ? -0.166767513893  ? -0.0553343045154  ? 0.096980420574 
? 0.0467083713499  ? -0.106755613565  ? 0.086835144347    ? 0.123698663901   ? 0.0180519489188    ? 
13 'X-RAY DIFFRACTION' ? refined -41.5821813795 -12.0012637555 29.4940337018  0.216401016518 ? 0.0567253011676   ? 
-0.0261047111645  ? 0.259457119659 ? -0.0236709597018  ? 0.225993045243 ? 0.0694879262496 ? -0.0490801176389  ? 0.0148957074839  ? 
0.0343126367898 ? 0.0297351343118   ? 0.0737790996974  ? -0.111774362907   ? -0.426737668981  ? 0.0297102589071   ? 0.24364578139 
? 0.117978898293   ? -0.0674647891947 ? -0.00131109043811 ? 0.0741322422405  ? -1.31343647482e-07 ? 
14 'X-RAY DIFFRACTION' ? refined -54.7657755945 -24.2060401256 24.5214636803  0.254681681805 ? 0.0120212527025   ? 0.0170681175889 
? 0.203163790305 ? 0.0443404215042   ? 0.303708366668 ? 0.0109256287765 ? 0.0199794255364   ? -0.0148530435924 ? 0.0293133438476 ? 
-0.024240483764   ? 0.00495811655879 ? -0.100235228454   ? -0.109650842929  ? -0.460202667303   ? 0.177744974753     ? 
0.0935822145318  ? 0.255305834833   ? 0.279295070418    ? -0.0554072875435 ? -1.5778565417e-06  ? 
15 'X-RAY DIFFRACTION' ? refined -52.8904293716 -8.6176369561  20.5008792882  0.169399878015 ? 0.0320737881004   ? 
0.000659417654045 ? 0.192198049533 ? 0.0100812296842   ? 0.191190862114 ? 0.0803057874404 ? -0.0434712978229  ? 0.0712955275614  ? 
0.0764863505051 ? -0.00654007698355 ? 0.0511722517718  ? -0.00539047937261 ? -0.0164534107394 ? -0.0512651330659  ? 
0.0817648360585    ? 0.0730198083407  ? 0.0135326335959  ? 0.0152929782444   ? -0.0196801730078 ? 7.10284834929e-07  ? 
16 'X-RAY DIFFRACTION' ? refined -52.146197545  -5.17419110366 28.7143730788  0.224168107934 ? 0.0626590718071   ? 
-0.00806523161911 ? 0.239514161711 ? -0.00564756848526 ? 0.189208034536 ? 0.300258122182  ? -0.280484306177   ? 0.0342882369936  ? 
0.202930993974  ? -0.015417208662   ? 0.157606892043   ? -0.115309587751   ? -0.148538661712  ? 0.0796049018232   ? 0.162523603306 
? 0.158088256942   ? -0.05108867747   ? -0.111317137368   ? -0.102482060464  ? 0.000437845833576  ? 
# 
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 42  ? A 21  A 62  ? ? 
;chain 'A' and (resid 42 through 62 )
;
2  'X-RAY DIFFRACTION' 2  A 22  A 63  ? A 50  A 91  ? ? 
;chain 'A' and (resid 63 through 91 )
;
3  'X-RAY DIFFRACTION' 3  A 51  A 92  ? A 167 A 208 ? ? 
;chain 'A' and (resid 92 through 208 )
;
4  'X-RAY DIFFRACTION' 4  A 168 A 209 ? A 185 A 226 ? ? 
;chain 'A' and (resid 209 through 226 )
;
5  'X-RAY DIFFRACTION' 5  A 186 A 227 ? A 234 A 275 ? ? 
;chain 'A' and (resid 227 through 275 )
;
6  'X-RAY DIFFRACTION' 6  A 235 A 276 ? A 264 A 305 ? ? 
;chain 'A' and (resid 276 through 305 )
;
7  'X-RAY DIFFRACTION' 7  B 1   B 42  ? B 21  B 62  ? ? 
;chain 'B' and (resid 42 through 62 )
;
8  'X-RAY DIFFRACTION' 8  B 22  B 63  ? B 50  B 91  ? ? 
;chain 'B' and (resid 63 through 91 )
;
9  'X-RAY DIFFRACTION' 9  B 51  B 92  ? B 109 B 150 ? ? 
;chain 'B' and (resid 92 through 150 )
;
10 'X-RAY DIFFRACTION' 10 B 110 B 151 ? B 124 B 165 ? ? 
;chain 'B' and (resid 151 through 165 )
;
11 'X-RAY DIFFRACTION' 11 B 125 B 166 ? B 167 B 208 ? ? 
;chain 'B' and (resid 166 through 208 )
;
12 'X-RAY DIFFRACTION' 12 B 168 B 209 ? B 185 B 226 ? ? 
;chain 'B' and (resid 209 through 226 )
;
13 'X-RAY DIFFRACTION' 13 B 186 B 227 ? B 204 B 245 ? ? 
;chain 'B' and (resid 227 through 245 )
;
14 'X-RAY DIFFRACTION' 14 B 205 B 246 ? B 218 B 259 ? ? 
;chain 'B' and (resid 246 through 259 )
;
15 'X-RAY DIFFRACTION' 15 B 219 B 260 ? B 234 B 275 ? ? 
;chain 'B' and (resid 260 through 275 )
;
16 'X-RAY DIFFRACTION' 16 B 235 B 276 ? B 266 B 307 ? ? 
;chain 'B' and (resid 276 through 307 )
;
# 
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 SER 2   ? A SER 2   
3   1 Y 1 A SER 3   ? A SER 3   
4   1 Y 1 A ILE 4   ? A ILE 4   
5   1 Y 1 A ILE 5   ? A ILE 5   
6   1 Y 1 A LYS 6   ? A LYS 6   
7   1 Y 1 A ARG 7   ? A ARG 7   
8   1 Y 1 A LYS 8   ? A LYS 8   
9   1 Y 1 A LEU 9   ? A LEU 9   
10  1 Y 1 A ALA 10  ? A ALA 10  
11  1 Y 1 A SER 11  ? A SER 11  
12  1 Y 1 A LEU 12  ? A LEU 12  
13  1 Y 1 A PHE 13  ? A PHE 13  
14  1 Y 1 A ALA 14  ? A ALA 14  
15  1 Y 1 A PHE 15  ? A PHE 15  
16  1 Y 1 A SER 16  ? A SER 16  
17  1 Y 1 A ALA 17  ? A ALA 17  
18  1 Y 1 A ALA 18  ? A ALA 18  
19  1 Y 1 A MET 19  ? A MET 19  
20  1 Y 1 A LEU 20  ? A LEU 20  
21  1 Y 1 A LEU 21  ? A LEU 21  
22  1 Y 1 A SER 22  ? A SER 22  
23  1 Y 1 A THR 23  ? A THR 23  
24  1 Y 1 A SER 24  ? A SER 24  
25  1 Y 1 A VAL 25  ? A VAL 25  
26  1 Y 1 A TRP 26  ? A TRP 26  
27  1 Y 1 A SER 27  ? A SER 27  
28  1 Y 1 A MET 28  ? A MET 28  
29  1 Y 1 A ASN 29  ? A ASN 29  
30  1 Y 1 A PRO 30  ? A PRO 30  
31  1 Y 1 A GLY 31  ? A GLY 31  
32  1 Y 1 A ASP 32  ? A ASP 32  
33  1 Y 1 A VAL 33  ? A VAL 33  
34  1 Y 1 A PRO 34  ? A PRO 34  
35  1 Y 1 A ASP 35  ? A ASP 35  
36  1 Y 1 A THR 36  ? A THR 36  
37  1 Y 1 A CYS 37  ? A CYS 37  
38  1 Y 1 A GLU 38  ? A GLU 38  
39  1 Y 1 A GLY 39  ? A GLY 39  
40  1 Y 1 A ASP 40  ? A ASP 40  
41  1 Y 1 A CYS 41  ? A CYS 41  
42  1 Y 1 A VAL 306 ? A VAL 306 
43  1 Y 1 A ASP 307 ? A ASP 307 
44  1 Y 1 A LYS 308 ? A LYS 308 
45  1 Y 1 A LEU 309 ? A LEU 309 
46  1 Y 1 A ALA 310 ? A ALA 310 
47  1 Y 1 A ALA 311 ? A ALA 311 
48  1 Y 1 A ALA 312 ? A ALA 312 
49  1 Y 1 A LEU 313 ? A LEU 313 
50  1 Y 1 A GLU 314 ? A GLU 314 
51  1 Y 1 A HIS 315 ? A HIS 315 
52  1 Y 1 A HIS 316 ? A HIS 316 
53  1 Y 1 A HIS 317 ? A HIS 317 
54  1 Y 1 A HIS 318 ? A HIS 318 
55  1 Y 1 A HIS 319 ? A HIS 319 
56  1 Y 1 A HIS 320 ? A HIS 320 
57  1 Y 1 B MET 1   ? B MET 1   
58  1 Y 1 B SER 2   ? B SER 2   
59  1 Y 1 B SER 3   ? B SER 3   
60  1 Y 1 B ILE 4   ? B ILE 4   
61  1 Y 1 B ILE 5   ? B ILE 5   
62  1 Y 1 B LYS 6   ? B LYS 6   
63  1 Y 1 B ARG 7   ? B ARG 7   
64  1 Y 1 B LYS 8   ? B LYS 8   
65  1 Y 1 B LEU 9   ? B LEU 9   
66  1 Y 1 B ALA 10  ? B ALA 10  
67  1 Y 1 B SER 11  ? B SER 11  
68  1 Y 1 B LEU 12  ? B LEU 12  
69  1 Y 1 B PHE 13  ? B PHE 13  
70  1 Y 1 B ALA 14  ? B ALA 14  
71  1 Y 1 B PHE 15  ? B PHE 15  
72  1 Y 1 B SER 16  ? B SER 16  
73  1 Y 1 B ALA 17  ? B ALA 17  
74  1 Y 1 B ALA 18  ? B ALA 18  
75  1 Y 1 B MET 19  ? B MET 19  
76  1 Y 1 B LEU 20  ? B LEU 20  
77  1 Y 1 B LEU 21  ? B LEU 21  
78  1 Y 1 B SER 22  ? B SER 22  
79  1 Y 1 B THR 23  ? B THR 23  
80  1 Y 1 B SER 24  ? B SER 24  
81  1 Y 1 B VAL 25  ? B VAL 25  
82  1 Y 1 B TRP 26  ? B TRP 26  
83  1 Y 1 B SER 27  ? B SER 27  
84  1 Y 1 B MET 28  ? B MET 28  
85  1 Y 1 B ASN 29  ? B ASN 29  
86  1 Y 1 B PRO 30  ? B PRO 30  
87  1 Y 1 B GLY 31  ? B GLY 31  
88  1 Y 1 B ASP 32  ? B ASP 32  
89  1 Y 1 B VAL 33  ? B VAL 33  
90  1 Y 1 B PRO 34  ? B PRO 34  
91  1 Y 1 B ASP 35  ? B ASP 35  
92  1 Y 1 B THR 36  ? B THR 36  
93  1 Y 1 B CYS 37  ? B CYS 37  
94  1 Y 1 B GLU 38  ? B GLU 38  
95  1 Y 1 B GLY 39  ? B GLY 39  
96  1 Y 1 B ASP 40  ? B ASP 40  
97  1 Y 1 B CYS 41  ? B CYS 41  
98  1 Y 1 B LYS 308 ? B LYS 308 
99  1 Y 1 B LEU 309 ? B LEU 309 
100 1 Y 1 B ALA 310 ? B ALA 310 
101 1 Y 1 B ALA 311 ? B ALA 311 
102 1 Y 1 B ALA 312 ? B ALA 312 
103 1 Y 1 B LEU 313 ? B LEU 313 
104 1 Y 1 B GLU 314 ? B GLU 314 
105 1 Y 1 B HIS 315 ? B HIS 315 
106 1 Y 1 B HIS 316 ? B HIS 316 
107 1 Y 1 B HIS 317 ? B HIS 317 
108 1 Y 1 B HIS 318 ? B HIS 318 
109 1 Y 1 B HIS 319 ? B HIS 319 
110 1 Y 1 B HIS 320 ? B HIS 320 
# 
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  
EDO C1   C  N N 89  
EDO O1   O  N N 90  
EDO C2   C  N N 91  
EDO O2   O  N N 92  
EDO H11  H  N N 93  
EDO H12  H  N N 94  
EDO HO1  H  N N 95  
EDO H21  H  N N 96  
EDO H22  H  N N 97  
EDO HO2  H  N N 98  
GLN N    N  N N 99  
GLN CA   C  N S 100 
GLN C    C  N N 101 
GLN O    O  N N 102 
GLN CB   C  N N 103 
GLN CG   C  N N 104 
GLN CD   C  N N 105 
GLN OE1  O  N N 106 
GLN NE2  N  N N 107 
GLN OXT  O  N N 108 
GLN H    H  N N 109 
GLN H2   H  N N 110 
GLN HA   H  N N 111 
GLN HB2  H  N N 112 
GLN HB3  H  N N 113 
GLN HG2  H  N N 114 
GLN HG3  H  N N 115 
GLN HE21 H  N N 116 
GLN HE22 H  N N 117 
GLN HXT  H  N N 118 
GLU N    N  N N 119 
GLU CA   C  N S 120 
GLU C    C  N N 121 
GLU O    O  N N 122 
GLU CB   C  N N 123 
GLU CG   C  N N 124 
GLU CD   C  N N 125 
GLU OE1  O  N N 126 
GLU OE2  O  N N 127 
GLU OXT  O  N N 128 
GLU H    H  N N 129 
GLU H2   H  N N 130 
GLU HA   H  N N 131 
GLU HB2  H  N N 132 
GLU HB3  H  N N 133 
GLU HG2  H  N N 134 
GLU HG3  H  N N 135 
GLU HE2  H  N N 136 
GLU HXT  H  N N 137 
GLY N    N  N N 138 
GLY CA   C  N N 139 
GLY C    C  N N 140 
GLY O    O  N N 141 
GLY OXT  O  N N 142 
GLY H    H  N N 143 
GLY H2   H  N N 144 
GLY HA2  H  N N 145 
GLY HA3  H  N N 146 
GLY HXT  H  N N 147 
HIS N    N  N N 148 
HIS CA   C  N S 149 
HIS C    C  N N 150 
HIS O    O  N N 151 
HIS CB   C  N N 152 
HIS CG   C  Y N 153 
HIS ND1  N  Y N 154 
HIS CD2  C  Y N 155 
HIS CE1  C  Y N 156 
HIS NE2  N  Y N 157 
HIS OXT  O  N N 158 
HIS H    H  N N 159 
HIS H2   H  N N 160 
HIS HA   H  N N 161 
HIS HB2  H  N N 162 
HIS HB3  H  N N 163 
HIS HD1  H  N N 164 
HIS HD2  H  N N 165 
HIS HE1  H  N N 166 
HIS HE2  H  N N 167 
HIS HXT  H  N N 168 
HOH O    O  N N 169 
HOH H1   H  N N 170 
HOH H2   H  N N 171 
ILE N    N  N N 172 
ILE CA   C  N S 173 
ILE C    C  N N 174 
ILE O    O  N N 175 
ILE CB   C  N S 176 
ILE CG1  C  N N 177 
ILE CG2  C  N N 178 
ILE CD1  C  N N 179 
ILE OXT  O  N N 180 
ILE H    H  N N 181 
ILE H2   H  N N 182 
ILE HA   H  N N 183 
ILE HB   H  N N 184 
ILE HG12 H  N N 185 
ILE HG13 H  N N 186 
ILE HG21 H  N N 187 
ILE HG22 H  N N 188 
ILE HG23 H  N N 189 
ILE HD11 H  N N 190 
ILE HD12 H  N N 191 
ILE HD13 H  N N 192 
ILE HXT  H  N N 193 
LEU N    N  N N 194 
LEU CA   C  N S 195 
LEU C    C  N N 196 
LEU O    O  N N 197 
LEU CB   C  N N 198 
LEU CG   C  N N 199 
LEU CD1  C  N N 200 
LEU CD2  C  N N 201 
LEU OXT  O  N N 202 
LEU H    H  N N 203 
LEU H2   H  N N 204 
LEU HA   H  N N 205 
LEU HB2  H  N N 206 
LEU HB3  H  N N 207 
LEU HG   H  N N 208 
LEU HD11 H  N N 209 
LEU HD12 H  N N 210 
LEU HD13 H  N N 211 
LEU HD21 H  N N 212 
LEU HD22 H  N N 213 
LEU HD23 H  N N 214 
LEU HXT  H  N N 215 
LYS N    N  N N 216 
LYS CA   C  N S 217 
LYS C    C  N N 218 
LYS O    O  N N 219 
LYS CB   C  N N 220 
LYS CG   C  N N 221 
LYS CD   C  N N 222 
LYS CE   C  N N 223 
LYS NZ   N  N N 224 
LYS OXT  O  N N 225 
LYS H    H  N N 226 
LYS H2   H  N N 227 
LYS HA   H  N N 228 
LYS HB2  H  N N 229 
LYS HB3  H  N N 230 
LYS HG2  H  N N 231 
LYS HG3  H  N N 232 
LYS HD2  H  N N 233 
LYS HD3  H  N N 234 
LYS HE2  H  N N 235 
LYS HE3  H  N N 236 
LYS HZ1  H  N N 237 
LYS HZ2  H  N N 238 
LYS HZ3  H  N N 239 
LYS HXT  H  N N 240 
MET N    N  N N 241 
MET CA   C  N S 242 
MET C    C  N N 243 
MET O    O  N N 244 
MET CB   C  N N 245 
MET CG   C  N N 246 
MET SD   S  N N 247 
MET CE   C  N N 248 
MET OXT  O  N N 249 
MET H    H  N N 250 
MET H2   H  N N 251 
MET HA   H  N N 252 
MET HB2  H  N N 253 
MET HB3  H  N N 254 
MET HG2  H  N N 255 
MET HG3  H  N N 256 
MET HE1  H  N N 257 
MET HE2  H  N N 258 
MET HE3  H  N N 259 
MET HXT  H  N N 260 
NA  NA   NA N N 261 
PHE N    N  N N 262 
PHE CA   C  N S 263 
PHE C    C  N N 264 
PHE O    O  N N 265 
PHE CB   C  N N 266 
PHE CG   C  Y N 267 
PHE CD1  C  Y N 268 
PHE CD2  C  Y N 269 
PHE CE1  C  Y N 270 
PHE CE2  C  Y N 271 
PHE CZ   C  Y N 272 
PHE OXT  O  N N 273 
PHE H    H  N N 274 
PHE H2   H  N N 275 
PHE HA   H  N N 276 
PHE HB2  H  N N 277 
PHE HB3  H  N N 278 
PHE HD1  H  N N 279 
PHE HD2  H  N N 280 
PHE HE1  H  N N 281 
PHE HE2  H  N N 282 
PHE HZ   H  N N 283 
PHE HXT  H  N N 284 
PRO N    N  N N 285 
PRO CA   C  N S 286 
PRO C    C  N N 287 
PRO O    O  N N 288 
PRO CB   C  N N 289 
PRO CG   C  N N 290 
PRO CD   C  N N 291 
PRO OXT  O  N N 292 
PRO H    H  N N 293 
PRO HA   H  N N 294 
PRO HB2  H  N N 295 
PRO HB3  H  N N 296 
PRO HG2  H  N N 297 
PRO HG3  H  N N 298 
PRO HD2  H  N N 299 
PRO HD3  H  N N 300 
PRO HXT  H  N N 301 
SER N    N  N N 302 
SER CA   C  N S 303 
SER C    C  N N 304 
SER O    O  N N 305 
SER CB   C  N N 306 
SER OG   O  N N 307 
SER OXT  O  N N 308 
SER H    H  N N 309 
SER H2   H  N N 310 
SER HA   H  N N 311 
SER HB2  H  N N 312 
SER HB3  H  N N 313 
SER HG   H  N N 314 
SER HXT  H  N N 315 
THR N    N  N N 316 
THR CA   C  N S 317 
THR C    C  N N 318 
THR O    O  N N 319 
THR CB   C  N R 320 
THR OG1  O  N N 321 
THR CG2  C  N N 322 
THR OXT  O  N N 323 
THR H    H  N N 324 
THR H2   H  N N 325 
THR HA   H  N N 326 
THR HB   H  N N 327 
THR HG1  H  N N 328 
THR HG21 H  N N 329 
THR HG22 H  N N 330 
THR HG23 H  N N 331 
THR HXT  H  N N 332 
TRP N    N  N N 333 
TRP CA   C  N S 334 
TRP C    C  N N 335 
TRP O    O  N N 336 
TRP CB   C  N N 337 
TRP CG   C  Y N 338 
TRP CD1  C  Y N 339 
TRP CD2  C  Y N 340 
TRP NE1  N  Y N 341 
TRP CE2  C  Y N 342 
TRP CE3  C  Y N 343 
TRP CZ2  C  Y N 344 
TRP CZ3  C  Y N 345 
TRP CH2  C  Y N 346 
TRP OXT  O  N N 347 
TRP H    H  N N 348 
TRP H2   H  N N 349 
TRP HA   H  N N 350 
TRP HB2  H  N N 351 
TRP HB3  H  N N 352 
TRP HD1  H  N N 353 
TRP HE1  H  N N 354 
TRP HE3  H  N N 355 
TRP HZ2  H  N N 356 
TRP HZ3  H  N N 357 
TRP HH2  H  N N 358 
TRP HXT  H  N N 359 
TYR N    N  N N 360 
TYR CA   C  N S 361 
TYR C    C  N N 362 
TYR O    O  N N 363 
TYR CB   C  N N 364 
TYR CG   C  Y N 365 
TYR CD1  C  Y N 366 
TYR CD2  C  Y N 367 
TYR CE1  C  Y N 368 
TYR CE2  C  Y N 369 
TYR CZ   C  Y N 370 
TYR OH   O  N N 371 
TYR OXT  O  N N 372 
TYR H    H  N N 373 
TYR H2   H  N N 374 
TYR HA   H  N N 375 
TYR HB2  H  N N 376 
TYR HB3  H  N N 377 
TYR HD1  H  N N 378 
TYR HD2  H  N N 379 
TYR HE1  H  N N 380 
TYR HE2  H  N N 381 
TYR HH   H  N N 382 
TYR HXT  H  N N 383 
VAL N    N  N N 384 
VAL CA   C  N S 385 
VAL C    C  N N 386 
VAL O    O  N N 387 
VAL CB   C  N N 388 
VAL CG1  C  N N 389 
VAL CG2  C  N N 390 
VAL OXT  O  N N 391 
VAL H    H  N N 392 
VAL H2   H  N N 393 
VAL HA   H  N N 394 
VAL HB   H  N N 395 
VAL HG11 H  N N 396 
VAL HG12 H  N N 397 
VAL HG13 H  N N 398 
VAL HG21 H  N N 399 
VAL HG22 H  N N 400 
VAL HG23 H  N N 401 
VAL HXT  H  N N 402 
# 
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  
EDO C1  O1   sing N N 83  
EDO C1  C2   sing N N 84  
EDO C1  H11  sing N N 85  
EDO C1  H12  sing N N 86  
EDO O1  HO1  sing N N 87  
EDO C2  O2   sing N N 88  
EDO C2  H21  sing N N 89  
EDO C2  H22  sing N N 90  
EDO O2  HO2  sing N N 91  
GLN N   CA   sing N N 92  
GLN N   H    sing N N 93  
GLN N   H2   sing N N 94  
GLN CA  C    sing N N 95  
GLN CA  CB   sing N N 96  
GLN CA  HA   sing N N 97  
GLN C   O    doub N N 98  
GLN C   OXT  sing N N 99  
GLN CB  CG   sing N N 100 
GLN CB  HB2  sing N N 101 
GLN CB  HB3  sing N N 102 
GLN CG  CD   sing N N 103 
GLN CG  HG2  sing N N 104 
GLN CG  HG3  sing N N 105 
GLN CD  OE1  doub N N 106 
GLN CD  NE2  sing N N 107 
GLN NE2 HE21 sing N N 108 
GLN NE2 HE22 sing N N 109 
GLN OXT HXT  sing N N 110 
GLU N   CA   sing N N 111 
GLU N   H    sing N N 112 
GLU N   H2   sing N N 113 
GLU CA  C    sing N N 114 
GLU CA  CB   sing N N 115 
GLU CA  HA   sing N N 116 
GLU C   O    doub N N 117 
GLU C   OXT  sing N N 118 
GLU CB  CG   sing N N 119 
GLU CB  HB2  sing N N 120 
GLU CB  HB3  sing N N 121 
GLU CG  CD   sing N N 122 
GLU CG  HG2  sing N N 123 
GLU CG  HG3  sing N N 124 
GLU CD  OE1  doub N N 125 
GLU CD  OE2  sing N N 126 
GLU OE2 HE2  sing N N 127 
GLU OXT HXT  sing N N 128 
GLY N   CA   sing N N 129 
GLY N   H    sing N N 130 
GLY N   H2   sing N N 131 
GLY CA  C    sing N N 132 
GLY CA  HA2  sing N N 133 
GLY CA  HA3  sing N N 134 
GLY C   O    doub N N 135 
GLY C   OXT  sing N N 136 
GLY OXT HXT  sing N N 137 
HIS N   CA   sing N N 138 
HIS N   H    sing N N 139 
HIS N   H2   sing N N 140 
HIS CA  C    sing N N 141 
HIS CA  CB   sing N N 142 
HIS CA  HA   sing N N 143 
HIS C   O    doub N N 144 
HIS C   OXT  sing N N 145 
HIS CB  CG   sing N N 146 
HIS CB  HB2  sing N N 147 
HIS CB  HB3  sing N N 148 
HIS CG  ND1  sing Y N 149 
HIS CG  CD2  doub Y N 150 
HIS ND1 CE1  doub Y N 151 
HIS ND1 HD1  sing N N 152 
HIS CD2 NE2  sing Y N 153 
HIS CD2 HD2  sing N N 154 
HIS CE1 NE2  sing Y N 155 
HIS CE1 HE1  sing N N 156 
HIS NE2 HE2  sing N N 157 
HIS OXT HXT  sing N N 158 
HOH O   H1   sing N N 159 
HOH O   H2   sing N N 160 
ILE N   CA   sing N N 161 
ILE N   H    sing N N 162 
ILE N   H2   sing N N 163 
ILE CA  C    sing N N 164 
ILE CA  CB   sing N N 165 
ILE CA  HA   sing N N 166 
ILE C   O    doub N N 167 
ILE C   OXT  sing N N 168 
ILE CB  CG1  sing N N 169 
ILE CB  CG2  sing N N 170 
ILE CB  HB   sing N N 171 
ILE CG1 CD1  sing N N 172 
ILE CG1 HG12 sing N N 173 
ILE CG1 HG13 sing N N 174 
ILE CG2 HG21 sing N N 175 
ILE CG2 HG22 sing N N 176 
ILE CG2 HG23 sing N N 177 
ILE CD1 HD11 sing N N 178 
ILE CD1 HD12 sing N N 179 
ILE CD1 HD13 sing N N 180 
ILE OXT HXT  sing N N 181 
LEU N   CA   sing N N 182 
LEU N   H    sing N N 183 
LEU N   H2   sing N N 184 
LEU CA  C    sing N N 185 
LEU CA  CB   sing N N 186 
LEU CA  HA   sing N N 187 
LEU C   O    doub N N 188 
LEU C   OXT  sing N N 189 
LEU CB  CG   sing N N 190 
LEU CB  HB2  sing N N 191 
LEU CB  HB3  sing N N 192 
LEU CG  CD1  sing N N 193 
LEU CG  CD2  sing N N 194 
LEU CG  HG   sing N N 195 
LEU CD1 HD11 sing N N 196 
LEU CD1 HD12 sing N N 197 
LEU CD1 HD13 sing N N 198 
LEU CD2 HD21 sing N N 199 
LEU CD2 HD22 sing N N 200 
LEU CD2 HD23 sing N N 201 
LEU OXT HXT  sing N N 202 
LYS N   CA   sing N N 203 
LYS N   H    sing N N 204 
LYS N   H2   sing N N 205 
LYS CA  C    sing N N 206 
LYS CA  CB   sing N N 207 
LYS CA  HA   sing N N 208 
LYS C   O    doub N N 209 
LYS C   OXT  sing N N 210 
LYS CB  CG   sing N N 211 
LYS CB  HB2  sing N N 212 
LYS CB  HB3  sing N N 213 
LYS CG  CD   sing N N 214 
LYS CG  HG2  sing N N 215 
LYS CG  HG3  sing N N 216 
LYS CD  CE   sing N N 217 
LYS CD  HD2  sing N N 218 
LYS CD  HD3  sing N N 219 
LYS CE  NZ   sing N N 220 
LYS CE  HE2  sing N N 221 
LYS CE  HE3  sing N N 222 
LYS NZ  HZ1  sing N N 223 
LYS NZ  HZ2  sing N N 224 
LYS NZ  HZ3  sing N N 225 
LYS OXT HXT  sing N N 226 
MET N   CA   sing N N 227 
MET N   H    sing N N 228 
MET N   H2   sing N N 229 
MET CA  C    sing N N 230 
MET CA  CB   sing N N 231 
MET CA  HA   sing N N 232 
MET C   O    doub N N 233 
MET C   OXT  sing N N 234 
MET CB  CG   sing N N 235 
MET CB  HB2  sing N N 236 
MET CB  HB3  sing N N 237 
MET CG  SD   sing N N 238 
MET CG  HG2  sing N N 239 
MET CG  HG3  sing N N 240 
MET SD  CE   sing N N 241 
MET CE  HE1  sing N N 242 
MET CE  HE2  sing N N 243 
MET CE  HE3  sing N N 244 
MET OXT HXT  sing N N 245 
PHE N   CA   sing N N 246 
PHE N   H    sing N N 247 
PHE N   H2   sing N N 248 
PHE CA  C    sing N N 249 
PHE CA  CB   sing N N 250 
PHE CA  HA   sing N N 251 
PHE C   O    doub N N 252 
PHE C   OXT  sing N N 253 
PHE CB  CG   sing N N 254 
PHE CB  HB2  sing N N 255 
PHE CB  HB3  sing N N 256 
PHE CG  CD1  doub Y N 257 
PHE CG  CD2  sing Y N 258 
PHE CD1 CE1  sing Y N 259 
PHE CD1 HD1  sing N N 260 
PHE CD2 CE2  doub Y N 261 
PHE CD2 HD2  sing N N 262 
PHE CE1 CZ   doub Y N 263 
PHE CE1 HE1  sing N N 264 
PHE CE2 CZ   sing Y N 265 
PHE CE2 HE2  sing N N 266 
PHE CZ  HZ   sing N N 267 
PHE OXT HXT  sing N N 268 
PRO N   CA   sing N N 269 
PRO N   CD   sing N N 270 
PRO N   H    sing N N 271 
PRO CA  C    sing N N 272 
PRO CA  CB   sing N N 273 
PRO CA  HA   sing N N 274 
PRO C   O    doub N N 275 
PRO C   OXT  sing N N 276 
PRO CB  CG   sing N N 277 
PRO CB  HB2  sing N N 278 
PRO CB  HB3  sing N N 279 
PRO CG  CD   sing N N 280 
PRO CG  HG2  sing N N 281 
PRO CG  HG3  sing N N 282 
PRO CD  HD2  sing N N 283 
PRO CD  HD3  sing N N 284 
PRO OXT HXT  sing N N 285 
SER N   CA   sing N N 286 
SER N   H    sing N N 287 
SER N   H2   sing N N 288 
SER CA  C    sing N N 289 
SER CA  CB   sing N N 290 
SER CA  HA   sing N N 291 
SER C   O    doub N N 292 
SER C   OXT  sing N N 293 
SER CB  OG   sing N N 294 
SER CB  HB2  sing N N 295 
SER CB  HB3  sing N N 296 
SER OG  HG   sing N N 297 
SER OXT HXT  sing N N 298 
THR N   CA   sing N N 299 
THR N   H    sing N N 300 
THR N   H2   sing N N 301 
THR CA  C    sing N N 302 
THR CA  CB   sing N N 303 
THR CA  HA   sing N N 304 
THR C   O    doub N N 305 
THR C   OXT  sing N N 306 
THR CB  OG1  sing N N 307 
THR CB  CG2  sing N N 308 
THR CB  HB   sing N N 309 
THR OG1 HG1  sing N N 310 
THR CG2 HG21 sing N N 311 
THR CG2 HG22 sing N N 312 
THR CG2 HG23 sing N N 313 
THR OXT HXT  sing N N 314 
TRP N   CA   sing N N 315 
TRP N   H    sing N N 316 
TRP N   H2   sing N N 317 
TRP CA  C    sing N N 318 
TRP CA  CB   sing N N 319 
TRP CA  HA   sing N N 320 
TRP C   O    doub N N 321 
TRP C   OXT  sing N N 322 
TRP CB  CG   sing N N 323 
TRP CB  HB2  sing N N 324 
TRP CB  HB3  sing N N 325 
TRP CG  CD1  doub Y N 326 
TRP CG  CD2  sing Y N 327 
TRP CD1 NE1  sing Y N 328 
TRP CD1 HD1  sing N N 329 
TRP CD2 CE2  doub Y N 330 
TRP CD2 CE3  sing Y N 331 
TRP NE1 CE2  sing Y N 332 
TRP NE1 HE1  sing N N 333 
TRP CE2 CZ2  sing Y N 334 
TRP CE3 CZ3  doub Y N 335 
TRP CE3 HE3  sing N N 336 
TRP CZ2 CH2  doub Y N 337 
TRP CZ2 HZ2  sing N N 338 
TRP CZ3 CH2  sing Y N 339 
TRP CZ3 HZ3  sing N N 340 
TRP CH2 HH2  sing N N 341 
TRP OXT HXT  sing N N 342 
TYR N   CA   sing N N 343 
TYR N   H    sing N N 344 
TYR N   H2   sing N N 345 
TYR CA  C    sing N N 346 
TYR CA  CB   sing N N 347 
TYR CA  HA   sing N N 348 
TYR C   O    doub N N 349 
TYR C   OXT  sing N N 350 
TYR CB  CG   sing N N 351 
TYR CB  HB2  sing N N 352 
TYR CB  HB3  sing N N 353 
TYR CG  CD1  doub Y N 354 
TYR CG  CD2  sing Y N 355 
TYR CD1 CE1  sing Y N 356 
TYR CD1 HD1  sing N N 357 
TYR CD2 CE2  doub Y N 358 
TYR CD2 HD2  sing N N 359 
TYR CE1 CZ   doub Y N 360 
TYR CE1 HE1  sing N N 361 
TYR CE2 CZ   sing Y N 362 
TYR CE2 HE2  sing N N 363 
TYR CZ  OH   sing N N 364 
TYR OH  HH   sing N N 365 
TYR OXT HXT  sing N N 366 
VAL N   CA   sing N N 367 
VAL N   H    sing N N 368 
VAL N   H2   sing N N 369 
VAL CA  C    sing N N 370 
VAL CA  CB   sing N N 371 
VAL CA  HA   sing N N 372 
VAL C   O    doub N N 373 
VAL C   OXT  sing N N 374 
VAL CB  CG1  sing N N 375 
VAL CB  CG2  sing N N 376 
VAL CB  HB   sing N N 377 
VAL CG1 HG11 sing N N 378 
VAL CG1 HG12 sing N N 379 
VAL CG1 HG13 sing N N 380 
VAL CG2 HG21 sing N N 381 
VAL CG2 HG22 sing N N 382 
VAL CG2 HG23 sing N N 383 
VAL OXT HXT  sing N N 384 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'German Research Foundation (DFG)'                   Germany 417919780 1 
'German Federal Ministry for Education and Research' Germany 31B0837A  2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'C 1 2 1' 
_space_group.name_Hall        'C 2y' 
_space_group.IT_number        5 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8OTU 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.007086 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000974 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.021901 
_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]   0.011990 
_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.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N    . GLY A  1 42  ? -26.19700 -11.17200 37.19200  1.000 68.57809  ? 42  GLY A N    1 
ATOM   2    C  CA   . GLY A  1 42  ? -26.96400 -12.43000 37.17200  1.000 56.17263  ? 42  GLY A CA   1 
ATOM   3    C  C    . GLY A  1 42  ? -26.05300 -13.64400 37.21900  1.000 44.30604  ? 42  GLY A C    1 
ATOM   4    O  O    . GLY A  1 42  ? -26.13200 -14.39100 38.18300  1.000 39.90585  ? 42  GLY A O    1 
ATOM   5    H  HA2  . GLY A  1 42  ? -27.57600 -12.44700 37.95000  1.000 67.40972  ? 42  GLY A HA2  1 
ATOM   6    H  HA3  . GLY A  1 42  ? -27.51100 -12.46100 36.34700  1.000 67.40972  ? 42  GLY A HA3  1 
ATOM   7    N  N    . TYR A  1 43  ? -25.17600 -13.79700 36.22800  1.000 31.24130  ? 43  TYR A N    1 
ATOM   8    C  CA   . TYR A  1 43  ? -24.28400 -14.92800 36.15700  1.000 26.45801  ? 43  TYR A CA   1 
ATOM   9    C  C    . TYR A  1 43  ? -22.84200 -14.59100 36.50200  1.000 21.82384  ? 43  TYR A C    1 
ATOM   10   O  O    . TYR A  1 43  ? -22.01400 -15.49600 36.58200  1.000 22.29842  ? 43  TYR A O    1 
ATOM   11   C  CB   . TYR A  1 43  ? -24.31100 -15.53000 34.75700  1.000 20.18897  ? 43  TYR A CB   1 
ATOM   12   C  CG   . TYR A  1 43  ? -25.66000 -15.89200 34.23700  1.000 19.57453  ? 43  TYR A CG   1 
ATOM   13   C  CD1  . TYR A  1 43  ? -26.48000 -16.81700 34.87800  1.000 21.21996  ? 43  TYR A CD1  1 
ATOM   14   C  CD2  . TYR A  1 43  ? -26.14600 -15.32400 33.05300  1.000 21.76808  ? 43  TYR A CD2  1 
ATOM   15   C  CE1  . TYR A  1 43  ? -27.68100 -17.19200 34.35100  1.000 20.51715  ? 43  TYR A CE1  1 
ATOM   16   C  CE2  . TYR A  1 43  ? -27.34500 -15.68100 32.52600  1.000 22.95611  ? 43  TYR A CE2  1 
ATOM   17   C  CZ   . TYR A  1 43  ? -28.14400 -16.60500 33.17100  1.000 22.85317  ? 43  TYR A CZ   1 
ATOM   18   O  OH   . TYR A  1 43  ? -29.34200 -16.96800 32.64300  1.000 24.36334  ? 43  TYR A OH   1 
ATOM   19   H  H    . TYR A  1 43  ? -25.07500 -13.22400 35.59500  1.000 37.49213  ? 43  TYR A H    1 
ATOM   20   H  HA   . TYR A  1 43  ? -24.59900 -15.59000 36.79200  1.000 31.75218  ? 43  TYR A HA   1 
ATOM   21   H  HB2  . TYR A  1 43  ? -23.92800 -14.88700 34.14100  1.000 24.22933  ? 43  TYR A HB2  1 
ATOM   22   H  HB3  . TYR A  1 43  ? -23.77800 -16.34100 34.76400  1.000 24.22933  ? 43  TYR A HB3  1 
ATOM   23   H  HD1  . TYR A  1 43  ? -26.20200 -17.18800 35.68400  1.000 25.46651  ? 43  TYR A HD1  1 
ATOM   24   H  HD2  . TYR A  1 43  ? -25.63300 -14.68400 32.61500  1.000 26.12425  ? 43  TYR A HD2  1 
ATOM   25   H  HE1  . TYR A  1 43  ? -28.19200 -17.84000 34.77900  1.000 24.62314  ? 43  TYR A HE1  1 
ATOM   26   H  HE2  . TYR A  1 43  ? -27.63000 -15.30200 31.72600  1.000 27.54990  ? 43  TYR A HE2  1 
ATOM   27   H  HH   . TYR A  1 43  ? -29.67700 -17.59300 33.09300  1.000 29.23857  ? 43  TYR A HH   1 
ATOM   28   N  N    . ALA A  1 44  ? -22.53800 -13.32300 36.78300  1.000 21.70674  ? 44  ALA A N    1 
ATOM   29   C  CA   . ALA A  1 44  ? -21.16600 -12.94300 37.04100  1.000 21.45130  ? 44  ALA A CA   1 
ATOM   30   C  C    . ALA A  1 44  ? -20.71200 -13.49400 38.38700  1.000 22.98319  ? 44  ALA A C    1 
ATOM   31   O  O    . ALA A  1 44  ? -21.47500 -13.52400 39.37000  1.000 24.80011  ? 44  ALA A O    1 
ATOM   32   C  CB   . ALA A  1 44  ? -21.03000 -11.42200 37.06300  1.000 23.20954  ? 44  ALA A CB   1 
ATOM   33   H  H    . ALA A  1 44  ? -23.10600 -12.67800 36.82700  1.000 26.05065  ? 44  ALA A H    1 
ATOM   34   H  HA   . ALA A  1 44  ? -20.60100 -13.30100 36.33900  1.000 25.74412  ? 44  ALA A HA   1 
ATOM   35   H  HB1  . ALA A  1 44  ? -20.10500 -11.19000 37.24400  1.000 27.85401  ? 44  ALA A HB1  1 
ATOM   36   H  HB2  . ALA A  1 44  ? -21.29700 -11.06900 36.20000  1.000 27.85401  ? 44  ALA A HB2  1 
ATOM   37   H  HB3  . ALA A  1 44  ? -21.60300 -11.06400 37.75900  1.000 27.85401  ? 44  ALA A HB3  1 
ATOM   38   N  N    . ARG A  1 45  ? -19.46300 -13.90000 38.44900  1.000 21.97573  ? 45  ARG A N    1 
ATOM   39   C  CA   . ARG A  1 45  ? -18.88800 -14.37100 39.69200  1.000 24.44226  ? 45  ARG A CA   1 
ATOM   40   C  C    . ARG A  1 45  ? -17.42200 -13.99100 39.75400  1.000 22.20246  ? 45  ARG A C    1 
ATOM   41   O  O    . ARG A  1 45  ? -16.76500 -13.71500 38.74700  1.000 20.90386  ? 45  ARG A O    1 
ATOM   42   C  CB   . ARG A  1 45  ? -19.19500 -15.85700 39.90300  1.000 33.15814  ? 45  ARG A CB   1 
ATOM   43   C  CG   . ARG A  1 45  ? -18.65600 -16.73500 38.84800  1.000 26.77130  ? 45  ARG A CG   1 
ATOM   44   C  CD   . ARG A  1 45  ? -18.98200 -18.24100 39.07000  1.000 26.67071  ? 45  ARG A CD   1 
ATOM   45   N  NE   . ARG A  1 45  ? -20.38000 -18.62800 39.03600  1.000 23.95643  ? 45  ARG A NE   1 
ATOM   46   C  CZ   . ARG A  1 45  ? -21.10500 -19.07000 40.05500  1.000 26.26468  ? 45  ARG A CZ   1 
ATOM   47   N  NH1  . ARG A  1 45  ? -20.63900 -19.07500 41.29900  1.000 28.50054  ? 45  ARG A NH1  1 
ATOM   48   N  NH2  . ARG A  1 45  ? -22.34200 -19.50100 39.84100  1.000 25.97360  ? 45  ARG A NH2  1 
ATOM   49   H  H    . ARG A  1 45  ? -18.92200 -13.91500 37.78000  1.000 26.37344  ? 45  ARG A H    1 
ATOM   50   H  HA   . ARG A  1 45  ? -19.27500 -13.91400 40.45600  1.000 29.33328  ? 45  ARG A HA   1 
ATOM   51   H  HB2  . ARG A  1 45  ? -18.80800 -16.13800 40.74700  1.000 39.79233  ? 45  ARG A HB2  1 
ATOM   52   H  HB3  . ARG A  1 45  ? -20.15700 -15.97700 39.92300  1.000 39.79233  ? 45  ARG A HB3  1 
ATOM   53   H  HG2  . ARG A  1 45  ? -19.03600 -16.47200 37.99500  1.000 32.12813  ? 45  ARG A HG2  1 
ATOM   54   H  HG3  . ARG A  1 45  ? -17.69100 -16.64200 38.82400  1.000 32.12813  ? 45  ARG A HG3  1 
ATOM   55   H  HD2  . ARG A  1 45  ? -18.53300 -18.75100 38.37700  1.000 32.00741  ? 45  ARG A HD2  1 
ATOM   56   H  HD3  . ARG A  1 45  ? -18.64200 -18.49600 39.94200  1.000 32.00741  ? 45  ARG A HD3  1 
ATOM   57   H  HE   . ARG A  1 45  ? -20.77900 -18.56400 38.27700  1.000 28.75028  ? 45  ARG A HE   1 
ATOM   58   H  HH11 . ARG A  1 45  ? -19.84500 -18.78600 41.46200  1.000 34.20321  ? 45  ARG A HH11 1 
ATOM   59   H  HH12 . ARG A  1 45  ? -21.13000 -19.36700 41.94200  1.000 34.20321  ? 45  ARG A HH12 1 
ATOM   60   H  HH21 . ARG A  1 45  ? -22.66900 -19.49300 39.04600  1.000 31.17088  ? 45  ARG A HH21 1 
ATOM   61   H  HH22 . ARG A  1 45  ? -22.81700 -19.78900 40.49800  1.000 31.17088  ? 45  ARG A HH22 1 
ATOM   62   N  N    . GLY A  1 46  ? -16.92100 -13.93600 40.98000  1.000 24.11615  ? 46  GLY A N    1 
ATOM   63   C  CA   . GLY A  1 46  ? -15.52300 -13.66800 41.18800  1.000 24.90875  ? 46  GLY A CA   1 
ATOM   64   C  C    . GLY A  1 46  ? -15.22100 -12.18400 41.23200  1.000 21.92311  ? 46  GLY A C    1 
ATOM   65   O  O    . GLY A  1 46  ? -16.06700 -11.32900 40.95400  1.000 22.66606  ? 46  GLY A O    1 
ATOM   66   H  H    . GLY A  1 46  ? -17.37700 -14.05100 41.70000  1.000 28.94195  ? 46  GLY A H    1 
ATOM   67   H  HA2  . GLY A  1 46  ? -15.24300 -14.06200 42.02900  1.000 29.89307  ? 46  GLY A HA2  1 
ATOM   68   H  HA3  . GLY A  1 46  ? -15.00900 -14.06300 40.46700  1.000 29.89307  ? 46  GLY A HA3  1 
ATOM   69   N  N    . PRO A  1 47  ? -13.97900 -11.86000 41.56400  1.000 22.53129  ? 47  PRO A N    1 
ATOM   70   C  CA   . PRO A  1 47  ? -13.61600 -10.45000 41.74300  1.000 22.14836  ? 47  PRO A CA   1 
ATOM   71   C  C    . PRO A  1 47  ? -13.51400 -9.70200  40.42700  1.000 20.22599  ? 47  PRO A C    1 
ATOM   72   O  O    . PRO A  1 47  ? -13.43100 -10.28300 39.34400  1.000 22.71733  ? 47  PRO A O    1 
ATOM   73   C  CB   . PRO A  1 47  ? -12.25400 -10.51900 42.44400  1.000 27.55466  ? 47  PRO A CB   1 
ATOM   74   C  CG   . PRO A  1 47  ? -11.69300 -11.81500 42.03100  1.000 29.98949  ? 47  PRO A CG   1 
ATOM   75   C  CD   . PRO A  1 47  ? -12.85200 -12.76800 41.84900  1.000 26.98534  ? 47  PRO A CD   1 
ATOM   76   H  HA   . PRO A  1 47  ? -14.26400 -10.00600 42.31200  1.000 26.58060  ? 47  PRO A HA   1 
ATOM   77   H  HB2  . PRO A  1 47  ? -11.69200 -9.78500  42.15000  1.000 33.06815  ? 47  PRO A HB2  1 
ATOM   78   H  HB3  . PRO A  1 47  ? -12.37400 -10.48100 43.40600  1.000 33.06815  ? 47  PRO A HB3  1 
ATOM   79   H  HG2  . PRO A  1 47  ? -11.21100 -11.70600 41.19600  1.000 35.98995  ? 47  PRO A HG2  1 
ATOM   80   H  HG3  . PRO A  1 47  ? -11.09300 -12.14000 42.72000  1.000 35.98995  ? 47  PRO A HG3  1 
ATOM   81   H  HD2  . PRO A  1 47  ? -12.69300 -13.36900 41.10500  1.000 32.38497  ? 47  PRO A HD2  1 
ATOM   82   H  HD3  . PRO A  1 47  ? -13.01200 -13.27700 42.65900  1.000 32.38497  ? 47  PRO A HD3  1 
ATOM   83   N  N    . ASP A  1 48  ? -13.52600 -8.38200  40.53700  1.000 21.76359  ? 48  ASP A N    1 
ATOM   84   C  CA   . ASP A  1 48  ? -13.34500 -7.52200  39.37900  1.000 22.10862  ? 48  ASP A CA   1 
ATOM   85   C  C    . ASP A  1 48  ? -11.99500 -7.81500  38.73200  1.000 22.74873  ? 48  ASP A C    1 
ATOM   86   O  O    . ASP A  1 48  ? -10.96100 -7.81000  39.42200  1.000 25.19770  ? 48  ASP A O    1 
ATOM   87   C  CB   . ASP A  1 48  ? -13.38800 -6.06100  39.81200  1.000 24.73955  ? 48  ASP A CB   1 
ATOM   88   C  CG   . ASP A  1 48  ? -14.75200 -5.63000  40.30100  1.000 28.10032  ? 48  ASP A CG   1 
ATOM   89   O  OD1  . ASP A  1 48  ? -15.75400 -6.36100  40.09400  1.000 25.02215  ? 48  ASP A OD1  1 
ATOM   90   O  OD2  . ASP A  1 48  ? -14.84400 -4.53800  40.92300  1.000 32.73176  ? 48  ASP A OD2  1 
ATOM   91   H  H    . ASP A  1 48  ? -13.63700 -7.95600  41.27600  1.000 26.11887  ? 48  ASP A H    1 
ATOM   92   H  HA   . ASP A  1 48  ? -14.05000 -7.68600  38.73400  1.000 26.53290  ? 48  ASP A HA   1 
ATOM   93   H  HB2  . ASP A  1 48  ? -12.75500 -5.92800  40.53500  1.000 29.69003  ? 48  ASP A HB2  1 
ATOM   94   H  HB3  . ASP A  1 48  ? -13.15100 -5.50200  39.05600  1.000 29.69003  ? 48  ASP A HB3  1 
ATOM   95   N  N    . PRO A  1 49  ? -11.96200 -8.07900  37.43900  1.000 21.48903  ? 49  PRO A N    1 
ATOM   96   C  CA   . PRO A  1 49  ? -10.71400 -8.51000  36.79500  1.000 19.98177  ? 49  PRO A CA   1 
ATOM   97   C  C    . PRO A  1 49  ? -9.75100  -7.35700  36.55700  1.000 23.77591  ? 49  PRO A C    1 
ATOM   98   O  O    . PRO A  1 49  ? -10.14300 -6.19500  36.37800  1.000 25.22310  ? 49  PRO A O    1 
ATOM   99   C  CB   . PRO A  1 49  ? -11.19400 -9.09500  35.46700  1.000 20.73316  ? 49  PRO A CB   1 
ATOM   100  C  CG   . PRO A  1 49  ? -12.48200 -8.36400  35.16600  1.000 21.98015  ? 49  PRO A CG   1 
ATOM   101  C  CD   . PRO A  1 49  ? -13.11600 -8.17500  36.53500  1.000 20.91548  ? 49  PRO A CD   1 
ATOM   102  H  HA   . PRO A  1 49  ? -10.27400 -9.19300  37.32600  1.000 23.98068  ? 49  PRO A HA   1 
ATOM   103  H  HB2  . PRO A  1 49  ? -10.53300 -8.93500  34.77600  1.000 24.88235  ? 49  PRO A HB2  1 
ATOM   104  H  HB3  . PRO A  1 49  ? -11.35000 -10.04800 35.56200  1.000 24.88235  ? 49  PRO A HB3  1 
ATOM   105  H  HG2  . PRO A  1 49  ? -12.29300 -7.51000  34.74500  1.000 26.37875  ? 49  PRO A HG2  1 
ATOM   106  H  HG3  . PRO A  1 49  ? -13.04600 -8.90000  34.58800  1.000 26.37875  ? 49  PRO A HG3  1 
ATOM   107  H  HD2  . PRO A  1 49  ? -13.64300 -7.36100  36.56100  1.000 25.10114  ? 49  PRO A HD2  1 
ATOM   108  H  HD3  . PRO A  1 49  ? -13.67100 -8.93700  36.76500  1.000 25.10114  ? 49  PRO A HD3  1 
ATOM   109  N  N    . THR A  1 50  ? -8.46900  -7.71800  36.55000  1.000 23.31672  ? 50  THR A N    1 
ATOM   110  C  CA   . THR A  1 50  ? -7.39700  -6.85400  36.09600  1.000 22.74065  ? 50  THR A CA   1 
ATOM   111  C  C    . THR A  1 50  ? -6.53100  -7.66700  35.13900  1.000 24.40971  ? 50  THR A C    1 
ATOM   112  O  O    . THR A  1 50  ? -6.68900  -8.89100  34.99600  1.000 21.74390  ? 50  THR A O    1 
ATOM   113  C  CB   . THR A  1 50  ? -6.52900  -6.40600  37.27000  1.000 27.70724  ? 50  THR A CB   1 
ATOM   114  O  OG1  . THR A  1 50  ? -5.87400  -7.54300  37.81400  1.000 25.11863  ? 50  THR A OG1  1 
ATOM   115  C  CG2  . THR A  1 50  ? -7.37000  -5.73600  38.38200  1.000 26.96722  ? 50  THR A CG2  1 
ATOM   116  H  H    . THR A  1 50  ? -8.19200  -8.48800  36.81300  1.000 27.98263  ? 50  THR A H    1 
ATOM   117  H  HA   . THR A  1 50  ? -7.76000  -6.07200  35.65100  1.000 27.29134  ? 50  THR A HA   1 
ATOM   118  H  HB   . THR A  1 50  ? -5.88400  -5.75400  36.95600  1.000 33.25125  ? 50  THR A HB   1 
ATOM   119  H  HG1  . THR A  1 50  ? -5.49400  -7.33800  38.53400  1.000 30.14491  ? 50  THR A HG1  1 
ATOM   120  H  HG21 . THR A  1 50  ? -6.78700  -5.38400  39.07300  1.000 32.36322  ? 50  THR A HG21 1 
ATOM   121  H  HG22 . THR A  1 50  ? -7.89300  -5.00900  38.01000  1.000 32.36322  ? 50  THR A HG22 1 
ATOM   122  H  HG23 . THR A  1 50  ? -7.97200  -6.38500  38.78000  1.000 32.36322  ? 50  THR A HG23 1 
ATOM   123  N  N    A GLU A  1 51  ? -5.60600  -6.97500  34.46700  0.468 25.78744  ? 51  GLU A N    1 
ATOM   124  N  N    B GLU A  1 51  ? -5.59800  -6.97800  34.48300  0.532 25.64523  ? 51  GLU A N    1 
ATOM   125  C  CA   A GLU A  1 51  ? -4.70800  -7.66700  33.54800  0.468 28.48673  ? 51  GLU A CA   1 
ATOM   126  C  CA   B GLU A  1 51  ? -4.71500  -7.66700  33.54900  0.532 28.46193  ? 51  GLU A CA   1 
ATOM   127  C  C    A GLU A  1 51  ? -3.92300  -8.74400  34.27900  0.468 23.17702  ? 51  GLU A C    1 
ATOM   128  C  C    B GLU A  1 51  ? -3.90300  -8.73400  34.26400  0.532 23.51969  ? 51  GLU A C    1 
ATOM   129  O  O    A GLU A  1 51  ? -3.84000  -9.89200  33.83000  0.468 22.34061  ? 51  GLU A O    1 
ATOM   130  O  O    B GLU A  1 51  ? -3.79100  -9.87200  33.79500  0.532 20.66086  ? 51  GLU A O    1 
ATOM   131  C  CB   A GLU A  1 51  ? -3.73300  -6.66900  32.91700  0.468 27.43091  ? 51  GLU A CB   1 
ATOM   132  C  CB   B GLU A  1 51  ? -3.79800  -6.64700  32.87000  0.532 27.28593  ? 51  GLU A CB   1 
ATOM   133  C  CG   A GLU A  1 51  ? -4.37000  -5.56900  32.11300  0.468 33.74347  ? 51  GLU A CG   1 
ATOM   134  C  CG   B GLU A  1 51  ? -3.08300  -7.20100  31.65600  0.532 26.72420  ? 51  GLU A CG   1 
ATOM   135  C  CD   A GLU A  1 51  ? -3.34000  -4.72500  31.38000  0.468 47.79154  ? 51  GLU A CD   1 
ATOM   136  C  CD   B GLU A  1 51  ? -2.39000  -6.10600  30.84900  0.532 44.86565  ? 51  GLU A CD   1 
ATOM   137  O  OE1  A GLU A  1 51  ? -2.68700  -5.25900  30.46000  0.468 56.27539  ? 51  GLU A OE1  1 
ATOM   138  O  OE1  B GLU A  1 51  ? -2.95000  -4.98800  30.75200  0.532 54.72267  ? 51  GLU A OE1  1 
ATOM   139  O  OE2  A GLU A  1 51  ? -3.17400  -3.54000  31.73000  0.468 45.56690  ? 51  GLU A OE2  1 
ATOM   140  O  OE2  B GLU A  1 51  ? -1.29900  -6.37200  30.30200  0.532 49.37759  ? 51  GLU A OE2  1 
ATOM   141  H  H    A GLU A  1 51  ? -5.48300  -6.12600  34.52600  0.468 30.94749  ? 51  GLU A H    1 
ATOM   142  H  H    B GLU A  1 51  ? -5.45900  -6.13300  34.56000  0.532 30.77684  ? 51  GLU A H    1 
ATOM   143  H  HA   A GLU A  1 51  ? -5.23600  -8.07500  32.84500  0.468 34.18664  ? 51  GLU A HA   1 
ATOM   144  H  HA   B GLU A  1 51  ? -5.24500  -8.10300  32.86300  0.532 34.15688  ? 51  GLU A HA   1 
ATOM   145  H  HB2  A GLU A  1 51  ? -3.22200  -6.25000  33.62700  0.468 32.91965  ? 51  GLU A HB2  1 
ATOM   146  H  HB2  B GLU A  1 51  ? -4.33100  -5.88900  32.58200  0.532 32.74568  ? 51  GLU A HB2  1 
ATOM   147  H  HB3  A GLU A  1 51  ? -3.13900  -7.15500  32.32400  0.468 32.91965  ? 51  GLU A HB3  1 
ATOM   148  H  HB3  B GLU A  1 51  ? -3.12600  -6.35800  33.50600  0.532 32.74568  ? 51  GLU A HB3  1 
ATOM   149  H  HG2  A GLU A  1 51  ? -4.96500  -5.95900  31.45500  0.468 40.49472  ? 51  GLU A HG2  1 
ATOM   150  H  HG2  B GLU A  1 51  ? -2.41000  -7.83600  31.94500  0.532 32.07160  ? 51  GLU A HG2  1 
ATOM   151  H  HG3  A GLU A  1 51  ? -4.86900  -4.98700  32.70800  0.468 40.49472  ? 51  GLU A HG3  1 
ATOM   152  H  HG3  B GLU A  1 51  ? -3.72700  -7.64000  31.07900  0.532 32.07160  ? 51  GLU A HG3  1 
ATOM   153  N  N    . SER A  1 52  ? -3.30600  -8.37800  35.39500  1.000 23.14503  ? 52  SER A N    1 
ATOM   154  C  CA   . SER A  1 52  ? -2.52700  -9.33500  36.15700  1.000 20.50319  ? 52  SER A CA   1 
ATOM   155  C  C    . SER A  1 52  ? -3.36000  -10.53500 36.59200  1.000 20.27609  ? 52  SER A C    1 
ATOM   156  O  O    . SER A  1 52  ? -2.93000  -11.69700 36.47500  1.000 21.83552  ? 52  SER A O    1 
ATOM   157  C  CB   . SER A  1 52  ? -1.94900  -8.56900  37.34600  1.000 34.11422  ? 52  SER A CB   1 
ATOM   158  O  OG   . SER A  1 52  ? -1.29100  -9.43800  38.19300  1.000 33.66653  ? 52  SER A OG   1 
ATOM   159  H  H    . SER A  1 52  ? -3.34000  -7.59000  35.73800  1.000 27.77659  ? 52  SER A H    1 
ATOM   160  H  HA   . SER A  1 52  ? -1.80700  -9.70800  35.62500  1.000 24.60640  ? 52  SER A HA   1 
ATOM   161  H  HB2  . SER A  1 52  ? -1.32200  -7.90300  37.02200  1.000 40.93963  ? 52  SER A HB2  1 
ATOM   162  H  HB3  . SER A  1 52  ? -2.67100  -8.13800  37.82900  1.000 40.93963  ? 52  SER A HB3  1 
ATOM   163  H  HG   . SER A  1 52  ? -1.64400  -9.41900  38.95500  1.000 40.40240  ? 52  SER A HG   1 
ATOM   164  N  N    . PHE A  1 53  ? -4.59000  -10.28800 37.04000  1.000 21.36535  ? 53  PHE A N    1 
ATOM   165  C  CA   . PHE A  1 53  ? -5.49400  -11.36700 37.43000  1.000 18.63912  ? 53  PHE A CA   1 
ATOM   166  C  C    . PHE A  1 53  ? -5.78600  -12.31400 36.26800  1.000 18.50339  ? 53  PHE A C    1 
ATOM   167  O  O    . PHE A  1 53  ? -5.83200  -13.53900 36.44900  1.000 18.48306  ? 53  PHE A O    1 
ATOM   168  C  CB   . PHE A  1 53  ? -6.74400  -10.67800 37.96100  1.000 20.80268  ? 53  PHE A CB   1 
ATOM   169  C  CG   . PHE A  1 53  ? -7.91800  -11.55700 38.21300  1.000 18.04417  ? 53  PHE A CG   1 
ATOM   170  C  CD1  . PHE A  1 53  ? -8.09100  -12.18500 39.42300  1.000 19.09853  ? 53  PHE A CD1  1 
ATOM   171  C  CD2  . PHE A  1 53  ? -8.87900  -11.69100 37.24500  1.000 18.21104  ? 53  PHE A CD2  1 
ATOM   172  C  CE1  . PHE A  1 53  ? -9.23300  -12.95100 39.65900  1.000 19.80257  ? 53  PHE A CE1  1 
ATOM   173  C  CE2  . PHE A  1 53  ? -10.01600 -12.44800 37.44700  1.000 18.86571  ? 53  PHE A CE2  1 
ATOM   174  C  CZ   . PHE A  1 53  ? -10.21300 -13.07500 38.66300  1.000 17.68521  ? 53  PHE A CZ   1 
ATOM   175  H  H    . PHE A  1 53  ? -4.92700  -9.50200  37.12800  1.000 25.64098  ? 53  PHE A H    1 
ATOM   176  H  HA   . PHE A  1 53  ? -5.11300  -11.93600 38.11700  1.000 22.36951  ? 53  PHE A HA   1 
ATOM   177  H  HB2  . PHE A  1 53  ? -6.52000  -10.25200 38.80300  1.000 24.96578  ? 53  PHE A HB2  1 
ATOM   178  H  HB3  . PHE A  1 53  ? -7.02000  -10.01000 37.31400  1.000 24.96578  ? 53  PHE A HB3  1 
ATOM   179  H  HD1  . PHE A  1 53  ? -7.44600  -12.09800 40.08700  1.000 22.92079  ? 53  PHE A HD1  1 
ATOM   180  H  HD2  . PHE A  1 53  ? -8.76300  -11.26000 36.43000  1.000 21.85581  ? 53  PHE A HD2  1 
ATOM   181  H  HE1  . PHE A  1 53  ? -9.34400  -13.37900 40.47700  1.000 23.76564  ? 53  PHE A HE1  1 
ATOM   182  H  HE2  . PHE A  1 53  ? -10.64600 -12.53500 36.76900  1.000 22.64142  ? 53  PHE A HE2  1 
ATOM   183  H  HZ   . PHE A  1 53  ? -10.98400 -13.57200 38.81800  1.000 21.22481  ? 53  PHE A HZ   1 
ATOM   184  N  N    . LEU A  1 54  ? -6.00000  -11.77500 35.09700  1.000 18.80908  ? 54  LEU A N    1 
ATOM   185  C  CA   . LEU A  1 54  ? -6.30000  -12.59400 33.92300  1.000 16.96855  ? 54  LEU A CA   1 
ATOM   186  C  C    . LEU A  1 54  ? -5.08600  -13.31900 33.35300  1.000 16.88759  ? 54  LEU A C    1 
ATOM   187  O  O    . LEU A  1 54  ? -5.25100  -14.36400 32.70400  1.000 16.72213  ? 54  LEU A O    1 
ATOM   188  C  CB   . LEU A  1 54  ? -6.96100  -11.73800 32.84100  1.000 17.00021  ? 54  LEU A CB   1 
ATOM   189  C  CG   . LEU A  1 54  ? -8.49400  -11.66500 32.93500  1.000 17.59552  ? 54  LEU A CG   1 
ATOM   190  C  CD1  . LEU A  1 54  ? -8.95700  -10.51200 32.09500  1.000 21.86145  ? 54  LEU A CD1  1 
ATOM   191  C  CD2  . LEU A  1 54  ? -9.12800  -12.99500 32.51200  1.000 16.95482  ? 54  LEU A CD2  1 
ATOM   192  H  H    . LEU A  1 54  ? -5.98000  -10.92900 34.93900  1.000 22.57346  ? 54  LEU A H    1 
ATOM   193  H  HA   . LEU A  1 54  ? -6.93200  -13.28000 34.18800  1.000 20.36482  ? 54  LEU A HA   1 
ATOM   194  H  HB2  . LEU A  1 54  ? -6.61900  -10.83300 32.91300  1.000 20.40282  ? 54  LEU A HB2  1 
ATOM   195  H  HB3  . LEU A  1 54  ? -6.73600  -12.11000 31.97400  1.000 20.40282  ? 54  LEU A HB3  1 
ATOM   196  H  HG   . LEU A  1 54  ? -8.78400  -11.51600 33.84800  1.000 21.11718  ? 54  LEU A HG   1 
ATOM   197  H  HD11 . LEU A  1 54  ? -9.92600  -10.47000 32.12400  1.000 26.23630  ? 54  LEU A HD11 1 
ATOM   198  H  HD12 . LEU A  1 54  ? -8.58000  -9.69200  32.45000  1.000 26.23630  ? 54  LEU A HD12 1 
ATOM   199  H  HD13 . LEU A  1 54  ? -8.65900  -10.64600 31.18200  1.000 26.23630  ? 54  LEU A HD13 1 
ATOM   200  H  HD21 . LEU A  1 54  ? -10.09400 -12.90900 32.54400  1.000 20.34834  ? 54  LEU A HD21 1 
ATOM   201  H  HD22 . LEU A  1 54  ? -8.84500  -13.20800 31.61000  1.000 20.34834  ? 54  LEU A HD22 1 
ATOM   202  H  HD23 . LEU A  1 54  ? -8.83900  -13.69100 33.12300  1.000 20.34834  ? 54  LEU A HD23 1 
ATOM   203  N  N    . GLU A  1 55  ? -3.87700  -12.81000 33.57600  1.000 17.38403  ? 55  GLU A N    1 
ATOM   204  C  CA   . GLU A  1 55  ? -2.65300  -13.41700 33.06700  1.000 17.34811  ? 55  GLU A CA   1 
ATOM   205  C  C    . GLU A  1 55  ? -2.11500  -14.51700 33.98000  1.000 16.36709  ? 55  GLU A C    1 
ATOM   206  O  O    . GLU A  1 55  ? -1.28300  -15.30300 33.54000  1.000 16.52558  ? 55  GLU A O    1 
ATOM   207  C  CB   . GLU A  1 55  ? -1.58800  -12.34300 32.83400  1.000 18.49908  ? 55  GLU A CB   1 
ATOM   208  C  CG   . GLU A  1 55  ? -1.93100  -11.44700 31.65700  1.000 19.47738  ? 55  GLU A CG   1 
ATOM   209  C  CD   . GLU A  1 55  ? -0.95800  -10.36500 31.36800  1.000 33.56550  ? 55  GLU A CD   1 
ATOM   210  O  OE1  . GLU A  1 55  ? 0.05300   -10.26000 32.08900  1.000 32.41260  ? 55  GLU A OE1  1 
ATOM   211  O  OE2  . GLU A  1 55  ? -1.21300  -9.59200  30.39700  1.000 30.27761  ? 55  GLU A OE2  1 
ATOM   212  H  H    . GLU A  1 55  ? -3.73500  -12.09400 34.03100  1.000 20.86340  ? 55  GLU A H    1 
ATOM   213  H  HA   . GLU A  1 55  ? -2.84000  -13.82700 32.20800  1.000 20.82029  ? 55  GLU A HA   1 
ATOM   214  H  HB2  . GLU A  1 55  ? -1.51700  -11.78800 33.62700  1.000 22.20146  ? 55  GLU A HB2  1 
ATOM   215  H  HB3  . GLU A  1 55  ? -0.73700  -12.77100 32.65100  1.000 22.20146  ? 55  GLU A HB3  1 
ATOM   216  H  HG2  . GLU A  1 55  ? -1.99200  -11.99900 30.86200  1.000 23.37542  ? 55  GLU A HG2  1 
ATOM   217  H  HG3  . GLU A  1 55  ? -2.78600  -11.02500 31.83400  1.000 23.37542  ? 55  GLU A HG3  1 
ATOM   218  N  N    . ALA A  1 56  ? -2.53400  -14.53400 35.24500  1.000 17.38560  ? 56  ALA A N    1 
ATOM   219  C  CA   . ALA A  1 56  ? -2.01000  -15.51600 36.18500  1.000 17.10510  ? 56  ALA A CA   1 
ATOM   220  C  C    . ALA A  1 56  ? -2.36700  -16.93400 35.77900  1.000 16.06591  ? 56  ALA A C    1 
ATOM   221  O  O    . ALA A  1 56  ? -3.38500  -17.19600 35.13400  1.000 15.63186  ? 56  ALA A O    1 
ATOM   222  C  CB   . ALA A  1 56  ? -2.62400  -15.25400 37.56000  1.000 19.63750  ? 56  ALA A CB   1 
ATOM   223  H  H    . ALA A  1 56  ? -3.11400  -13.99300 35.57800  1.000 20.86529  ? 56  ALA A H    1 
ATOM   224  H  HA   . ALA A  1 56  ? -1.04300  -15.44100 36.21100  1.000 20.52869  ? 56  ALA A HA   1 
ATOM   225  H  HB1  . ALA A  1 56  ? -2.25200  -15.88500 38.19700  1.000 23.56757  ? 56  ALA A HB1  1 
ATOM   226  H  HB2  . ALA A  1 56  ? -2.41500  -14.34700 37.83200  1.000 23.56757  ? 56  ALA A HB2  1 
ATOM   227  H  HB3  . ALA A  1 56  ? -3.58500  -15.36900 37.50300  1.000 23.56757  ? 56  ALA A HB3  1 
ATOM   228  N  N    . ASP A  1 57  ? -1.54800  -17.88400 36.20700  1.000 16.79520  ? 57  ASP A N    1 
ATOM   229  C  CA   . ASP A  1 57  ? -1.78400  -19.26900 35.81700  1.000 16.40308  ? 57  ASP A CA   1 
ATOM   230  C  C    . ASP A  1 57  ? -3.11100  -19.80100 36.35500  1.000 16.73717  ? 57  ASP A C    1 
ATOM   231  O  O    . ASP A  1 57  ? -3.76400  -20.65500 35.73500  1.000 17.04973  ? 57  ASP A O    1 
ATOM   232  C  CB   . ASP A  1 57  ? -0.65700  -20.17000 36.34500  1.000 17.41987  ? 57  ASP A CB   1 
ATOM   233  C  CG   . ASP A  1 57  ? 0.64100   -20.04200 35.58200  1.000 22.12408  ? 57  ASP A CG   1 
ATOM   234  O  OD1  . ASP A  1 57  ? 0.71000   -19.40600 34.50200  1.000 21.43405  ? 57  ASP A OD1  1 
ATOM   235  O  OD2  . ASP A  1 57  ? 1.65900   -20.56800 36.06700  1.000 23.18608  ? 57  ASP A OD2  1 
ATOM   236  H  H    . ASP A  1 57  ? -0.86400  -17.75900 36.71300  1.000 20.15680  ? 57  ASP A H    1 
ATOM   237  H  HA   . ASP A  1 57  ? -1.79800  -19.30000 34.84700  1.000 19.68626  ? 57  ASP A HA   1 
ATOM   238  H  HB2  . ASP A  1 57  ? -0.48000  -19.93700 37.26900  1.000 20.90640  ? 57  ASP A HB2  1 
ATOM   239  H  HB3  . ASP A  1 57  ? -0.94400  -21.09500 36.28500  1.000 20.90640  ? 57  ASP A HB3  1 
ATOM   240  N  N    . SER A  1 58  ? -3.52100  -19.36000 37.54500  1.000 16.22305  ? 58  SER A N    1 
ATOM   241  C  CA   . SER A  1 58  ? -4.77400  -19.78700 38.14900  1.000 15.99523  ? 58  SER A CA   1 
ATOM   242  C  C    . SER A  1 58  ? -5.69200  -18.61500 38.44300  1.000 16.22414  ? 58  SER A C    1 
ATOM   243  O  O    . SER A  1 58  ? -5.24700  -17.55600 38.91300  1.000 17.96426  ? 58  SER A O    1 
ATOM   244  C  CB   . SER A  1 58  ? -4.51500  -20.54100 39.47000  1.000 15.93713  ? 58  SER A CB   1 
ATOM   245  O  OG   . SER A  1 58  ? -5.74100  -21.03000 40.02000  1.000 17.03964  ? 58  SER A OG   1 
ATOM   246  H  H    . SER A  1 58  ? -3.07800  -18.80200 38.02700  1.000 19.47023  ? 58  SER A H    1 
ATOM   247  H  HA   . SER A  1 58  ? -5.22600  -20.36300 37.51300  1.000 19.19684  ? 58  SER A HA   1 
ATOM   248  H  HB2  . SER A  1 58  ? -3.92400  -21.29100 39.29600  1.000 19.12712  ? 58  SER A HB2  1 
ATOM   249  H  HB3  . SER A  1 58  ? -4.10300  -19.93500 40.10500  1.000 19.12712  ? 58  SER A HB3  1 
ATOM   250  H  HG   . SER A  1 58  ? -6.25800  -20.38900 40.18400  1.000 20.45013  ? 58  SER A HG   1 
ATOM   251  N  N    . GLY A  1 59  ? -6.99000  -18.83700 38.20700  1.000 15.34969  ? 59  GLY A N    1 
ATOM   252  C  CA   . GLY A  1 59  ? -8.02700  -18.00100 38.71800  1.000 15.61798  ? 59  GLY A CA   1 
ATOM   253  C  C    . GLY A  1 59  ? -8.24400  -18.21700 40.19700  1.000 15.32022  ? 59  GLY A C    1 
ATOM   254  O  O    . GLY A  1 59  ? -7.51100  -18.96300 40.85500  1.000 16.07598  ? 59  GLY A O    1 
ATOM   255  H  H    . GLY A  1 59  ? -7.28500  -19.49200 37.73600  1.000 18.42219  ? 59  GLY A H    1 
ATOM   256  H  HA2  . GLY A  1 59  ? -7.79400  -17.07100 38.57400  1.000 18.74413  ? 59  GLY A HA2  1 
ATOM   257  H  HA3  . GLY A  1 59  ? -8.85600  -18.19500 38.25400  1.000 18.74413  ? 59  GLY A HA3  1 
ATOM   258  N  N    . PRO A  1 60  ? -9.25300  -17.53900 40.73800  1.000 14.52916  ? 60  PRO A N    1 
ATOM   259  C  CA   . PRO A  1 60  ? -9.41700  -17.45200 42.19700  1.000 15.18793  ? 60  PRO A CA   1 
ATOM   260  C  C    . PRO A  1 60  ? -10.11700 -18.61900 42.85200  1.000 14.74781  ? 60  PRO A C    1 
ATOM   261  O  O    . PRO A  1 60  ? -10.12400 -18.68200 44.06700  1.000 15.82787  ? 60  PRO A O    1 
ATOM   262  C  CB   . PRO A  1 60  ? -10.22000 -16.15100 42.37800  1.000 16.73974  ? 60  PRO A CB   1 
ATOM   263  C  CG   . PRO A  1 60  ? -11.05200 -16.11900 41.10100  1.000 18.39736  ? 60  PRO A CG   1 
ATOM   264  C  CD   . PRO A  1 60  ? -10.14200 -16.61500 40.00000  1.000 15.97966  ? 60  PRO A CD   1 
ATOM   265  H  HA   . PRO A  1 60  ? -8.54500  -17.35700 42.61100  1.000 18.22807  ? 60  PRO A HA   1 
ATOM   266  H  HB2  . PRO A  1 60  ? -10.77900 -16.19900 43.16900  1.000 20.09025  ? 60  PRO A HB2  1 
ATOM   267  H  HB3  . PRO A  1 60  ? -9.62600  -15.38700 42.43700  1.000 20.09025  ? 60  PRO A HB3  1 
ATOM   268  H  HG2  . PRO A  1 60  ? -11.82200 -16.70200 41.19900  1.000 22.07940  ? 60  PRO A HG2  1 
ATOM   269  H  HG3  . PRO A  1 60  ? -11.34400 -15.21100 40.92300  1.000 22.07940  ? 60  PRO A HG3  1 
ATOM   270  H  HD2  . PRO A  1 60  ? -10.64400 -17.08300 39.31400  1.000 19.17815  ? 60  PRO A HD2  1 
ATOM   271  H  HD3  . PRO A  1 60  ? -9.64000  -15.88500 39.60400  1.000 19.17815  ? 60  PRO A HD3  1 
ATOM   272  N  N    . TYR A  1 61  ? -10.70500 -19.53800 42.08500  1.000 15.60645  ? 61  TYR A N    1 
ATOM   273  C  CA   . TYR A  1 61  ? -11.32900 -20.70100 42.69700  1.000 15.95486  ? 61  TYR A CA   1 
ATOM   274  C  C    . TYR A  1 61  ? -10.34300 -21.84400 42.80700  1.000 16.77634  ? 61  TYR A C    1 
ATOM   275  O  O    . TYR A  1 61  ? -9.65100  -22.14600 41.84500  1.000 17.00808  ? 61  TYR A O    1 
ATOM   276  C  CB   . TYR A  1 61  ? -12.51200 -21.16900 41.85300  1.000 17.20406  ? 61  TYR A CB   1 
ATOM   277  C  CG   . TYR A  1 61  ? -13.70400 -20.23200 41.84700  1.000 19.00334  ? 61  TYR A CG   1 
ATOM   278  C  CD1  . TYR A  1 61  ? -14.66100 -20.34100 42.84000  1.000 21.14633  ? 61  TYR A CD1  1 
ATOM   279  C  CD2  . TYR A  1 61  ? -13.81300 -19.23600 40.88800  1.000 19.41482  ? 61  TYR A CD2  1 
ATOM   280  C  CE1  . TYR A  1 61  ? -15.77900 -19.45700 42.83800  1.000 26.07804  ? 61  TYR A CE1  1 
ATOM   281  C  CE2  . TYR A  1 61  ? -14.92200 -18.34600 40.88400  1.000 23.46571  ? 61  TYR A CE2  1 
ATOM   282  C  CZ   . TYR A  1 61  ? -15.86300 -18.49300 41.84100  1.000 26.39067  ? 61  TYR A CZ   1 
ATOM   283  O  OH   . TYR A  1 61  ? -16.93000 -17.60000 41.84600  1.000 36.34807  ? 61  TYR A OH   1 
ATOM   284  H  H    . TYR A  1 61  ? -10.75200 -19.50700 41.22700  1.000 18.73030  ? 61  TYR A H    1 
ATOM   285  H  HA   . TYR A  1 61  ? -11.63200 -20.46000 43.58600  1.000 19.14840  ? 61  TYR A HA   1 
ATOM   286  H  HB2  . TYR A  1 61  ? -12.21400 -21.26800 40.93500  1.000 20.64743  ? 61  TYR A HB2  1 
ATOM   287  H  HB3  . TYR A  1 61  ? -12.81500 -22.02400 42.19700  1.000 20.64743  ? 61  TYR A HB3  1 
ATOM   288  H  HD1  . TYR A  1 61  ? -14.57600 -20.98600 43.50400  1.000 25.37816  ? 61  TYR A HD1  1 
ATOM   289  H  HD2  . TYR A  1 61  ? -13.15300 -19.14900 40.23900  1.000 23.30035  ? 61  TYR A HD2  1 
ATOM   290  H  HE1  . TYR A  1 61  ? -16.43800 -19.52500 43.49100  1.000 31.29621  ? 61  TYR A HE1  1 
ATOM   291  H  HE2  . TYR A  1 61  ? -14.99700 -17.68000 40.23900  1.000 28.16142  ? 61  TYR A HE2  1 
ATOM   292  H  HH   . TYR A  1 61  ? -16.76300 -16.95000 41.34100  1.000 43.62025  ? 61  TYR A HH   1 
ATOM   293  N  N    . THR A  1 62  ? -10.33100 -22.51300 43.97000  1.000 18.89189  ? 62  THR A N    1 
ATOM   294  C  CA   . THR A  1 62  ? -9.70700  -23.83000 44.03500  1.000 18.05014  ? 62  THR A CA   1 
ATOM   295  C  C    . THR A  1 62  ? -10.60700 -24.80300 43.27000  1.000 18.09305  ? 62  THR A C    1 
ATOM   296  O  O    . THR A  1 62  ? -11.83400 -24.64300 43.21600  1.000 18.80442  ? 62  THR A O    1 
ATOM   297  C  CB   . THR A  1 62  ? -9.47300  -24.32400 45.44500  1.000 22.28494  ? 62  THR A CB   1 
ATOM   298  O  OG1  . THR A  1 62  ? -10.70800 -24.29200 46.14500  1.000 27.24335  ? 62  THR A OG1  1 
ATOM   299  C  CG2  . THR A  1 62  ? -8.49500  -23.45100 46.21100  1.000 23.88115  ? 62  THR A CG2  1 
ATOM   300  H  H    . THR A  1 62  ? -10.66900 -22.23000 44.70800  1.000 22.67283  ? 62  THR A H    1 
ATOM   301  H  HA   . THR A  1 62  ? -8.82000  -23.78800 43.64400  1.000 21.66273  ? 62  THR A HA   1 
ATOM   302  H  HB   . THR A  1 62  ? -9.10400  -25.21900 45.39700  1.000 26.74449  ? 62  THR A HB   1 
ATOM   303  H  HG1  . THR A  1 62  ? -11.23800 -24.85500 45.81800  1.000 32.69459  ? 62  THR A HG1  1 
ATOM   304  H  HG21 . THR A  1 62  ? -8.22500  -23.89500 47.03000  1.000 28.65995  ? 62  THR A HG21 1 
ATOM   305  H  HG22 . THR A  1 62  ? -7.70700  -23.28200 45.67000  1.000 28.65995  ? 62  THR A HG22 1 
ATOM   306  H  HG23 . THR A  1 62  ? -8.91100  -22.60300 46.43500  1.000 28.65995  ? 62  THR A HG23 1 
ATOM   307  N  N    . ILE A  1 63  ? -9.99700  -25.83600 42.71400  1.000 17.66142  ? 63  ILE A N    1 
ATOM   308  C  CA   . ILE A  1 63  ? -10.70900 -26.76400 41.85000  1.000 16.22307  ? 63  ILE A CA   1 
ATOM   309  C  C    . ILE A  1 63  ? -10.48100 -28.19500 42.29500  1.000 16.99301  ? 63  ILE A C    1 
ATOM   310  O  O    . ILE A  1 63  ? -9.52100  -28.52200 42.99200  1.000 18.61402  ? 63  ILE A O    1 
ATOM   311  C  CB   . ILE A  1 63  ? -10.35600 -26.57200 40.37000  1.000 17.77807  ? 63  ILE A CB   1 
ATOM   312  C  CG1  . ILE A  1 63  ? -8.91000  -26.91600 40.10500  1.000 19.40138  ? 63  ILE A CG1  1 
ATOM   313  C  CG2  . ILE A  1 63  ? -10.67900 -25.12900 39.93900  1.000 18.73164  ? 63  ILE A CG2  1 
ATOM   314  C  CD1  . ILE A  1 63  ? -8.56600  -26.90800 38.63100  1.000 21.35135  ? 63  ILE A CD1  1 
ATOM   315  H  H    . ILE A  1 63  ? -9.16500  -26.02400 42.82300  1.000 21.19626  ? 63  ILE A H    1 
ATOM   316  H  HA   . ILE A  1 63  ? -11.66000 -26.60200 41.95400  1.000 19.47024  ? 63  ILE A HA   1 
ATOM   317  H  HB   . ILE A  1 63  ? -10.89600 -27.18100 39.84300  1.000 21.33625  ? 63  ILE A HB   1 
ATOM   318  H  HG12 . ILE A  1 63  ? -8.34500  -26.26400 40.54900  1.000 23.28422  ? 63  ILE A HG12 1 
ATOM   319  H  HG13 . ILE A  1 63  ? -8.72800  -27.80300 40.45200  1.000 23.28422  ? 63  ILE A HG13 1 
ATOM   320  H  HG21 . ILE A  1 63  ? -10.64600 -25.07300 38.97100  1.000 22.48053  ? 63  ILE A HG21 1 
ATOM   321  H  HG22 . ILE A  1 63  ? -11.56700 -24.89600 40.25300  1.000 22.48053  ? 63  ILE A HG22 1 
ATOM   322  H  HG23 . ILE A  1 63  ? -10.02300 -24.52900 40.32700  1.000 22.48053  ? 63  ILE A HG23 1 
ATOM   323  H  HD11 . ILE A  1 63  ? -7.66900  -27.25700 38.51500  1.000 25.62419  ? 63  ILE A HD11 1 
ATOM   324  H  HD12 . ILE A  1 63  ? -9.20200  -27.46500 38.15600  1.000 25.62419  ? 63  ILE A HD12 1 
ATOM   325  H  HD13 . ILE A  1 63  ? -8.61200  -25.99700 38.30100  1.000 25.62419  ? 63  ILE A HD13 1 
ATOM   326  N  N    . ALA A  1 64  ? -11.38500 -29.06000 41.84500  1.000 17.90229  ? 64  ALA A N    1 
ATOM   327  C  CA   . ALA A  1 64  ? -11.31800 -30.49600 42.03400  1.000 17.48161  ? 64  ALA A CA   1 
ATOM   328  C  C    . ALA A  1 64  ? -11.46900 -31.13800 40.66300  1.000 16.22331  ? 64  ALA A C    1 
ATOM   329  O  O    . ALA A  1 64  ? -11.86800 -30.49200 39.69300  1.000 16.14948  ? 64  ALA A O    1 
ATOM   330  C  CB   . ALA A  1 64  ? -12.38400 -30.99000 43.00900  1.000 20.30812  ? 64  ALA A CB   1 
ATOM   331  H  H    . ALA A  1 64  ? -12.08300 -28.82100 41.40300  1.000 21.48532  ? 64  ALA A H    1 
ATOM   332  H  HA   . ALA A  1 64  ? -10.46300 -30.75700 42.41100  1.000 20.98049  ? 64  ALA A HA   1 
ATOM   333  H  HB1  . ALA A  1 64  ? -12.29800 -31.95100 43.11000  1.000 24.37230  ? 64  ALA A HB1  1 
ATOM   334  H  HB2  . ALA A  1 64  ? -12.25400 -30.55400 43.86600  1.000 24.37230  ? 64  ALA A HB2  1 
ATOM   335  H  HB3  . ALA A  1 64  ? -13.26000 -30.77100 42.65600  1.000 24.37230  ? 64  ALA A HB3  1 
ATOM   336  N  N    . THR A  1 65  ? -11.18600 -32.42700 40.60200  1.000 18.19946  ? 65  THR A N    1 
ATOM   337  C  CA   . THR A  1 65  ? -11.29800 -33.18000 39.37100  1.000 17.70971  ? 65  THR A CA   1 
ATOM   338  C  C    . THR A  1 65  ? -12.07100 -34.46800 39.58400  1.000 20.24281  ? 65  THR A C    1 
ATOM   339  O  O    . THR A  1 65  ? -12.07400 -35.04900 40.66800  1.000 22.26373  ? 65  THR A O    1 
ATOM   340  C  CB   . THR A  1 65  ? -9.96900  -33.50400 38.70000  1.000 20.73043  ? 65  THR A CB   1 
ATOM   341  O  OG1  . THR A  1 65  ? -9.20400  -34.34400 39.55700  1.000 24.19366  ? 65  THR A OG1  1 
ATOM   342  C  CG2  . THR A  1 65  ? -9.19300  -32.26000 38.38800  1.000 23.10681  ? 65  THR A CG2  1 
ATOM   343  H  H    . THR A  1 65  ? -10.92200 -32.89500 41.27300  1.000 21.84192  ? 65  THR A H    1 
ATOM   344  H  HA   . THR A  1 65  ? -11.79700 -32.61300 38.76200  1.000 21.25422  ? 65  THR A HA   1 
ATOM   345  H  HB   . THR A  1 65  ? -10.13800 -33.95900 37.86000  1.000 24.87908  ? 65  THR A HB   1 
ATOM   346  H  HG1  . THR A  1 65  ? -8.51800  -34.61500 39.15500  1.000 29.03496  ? 65  THR A HG1  1 
ATOM   347  H  HG21 . THR A  1 65  ? -8.38900  -32.48500 37.89400  1.000 27.73074  ? 65  THR A HG21 1 
ATOM   348  H  HG22 . THR A  1 65  ? -9.73300  -31.65800 37.85300  1.000 27.73074  ? 65  THR A HG22 1 
ATOM   349  H  HG23 . THR A  1 65  ? -8.94200  -31.81100 39.21100  1.000 27.73074  ? 65  THR A HG23 1 
ATOM   350  N  N    A SER A  1 66  ? -12.74900 -34.90300 38.51800  0.563 18.53606  ? 66  SER A N    1 
ATOM   351  N  N    B SER A  1 66  ? -12.68100 -34.93500 38.49700  0.437 20.70253  ? 66  SER A N    1 
ATOM   352  C  CA   A SER A  1 66  ? -13.39800 -36.20600 38.46500  0.563 18.68872  ? 66  SER A CA   1 
ATOM   353  C  CA   B SER A  1 66  ? -13.40400 -36.19500 38.45800  0.437 19.12656  ? 66  SER A CA   1 
ATOM   354  C  C    A SER A  1 66  ? -13.09400 -36.84600 37.12100  0.563 18.74280  ? 66  SER A C    1 
ATOM   355  C  C    B SER A  1 66  ? -13.12900 -36.85700 37.12000  0.437 19.63824  ? 66  SER A C    1 
ATOM   356  O  O    A SER A  1 66  ? -13.21300 -36.19800 36.08200  0.563 20.00551  ? 66  SER A O    1 
ATOM   357  O  O    B SER A  1 66  ? -13.27700 -36.22300 36.07600  0.437 19.34558  ? 66  SER A O    1 
ATOM   358  C  CB   A SER A  1 66  ? -14.91300 -36.06500 38.64800  0.563 22.53401  ? 66  SER A CB   1 
ATOM   359  C  CB   B SER A  1 66  ? -14.90500 -35.94300 38.61300  0.437 20.82525  ? 66  SER A CB   1 
ATOM   360  O  OG   A SER A  1 66  ? -15.55700 -37.33700 38.72900  0.563 23.08644  ? 66  SER A OG   1 
ATOM   361  O  OG   B SER A  1 66  ? -15.24000 -35.65900 39.95900  0.437 27.77034  ? 66  SER A OG   1 
ATOM   362  H  H    A SER A  1 66  ? -12.84700 -34.44500 37.79700  0.563 22.24583  ? 66  SER A H    1 
ATOM   363  H  H    B SER A  1 66  ? -12.68900 -34.52200 37.74300  0.437 24.84560  ? 66  SER A H    1 
ATOM   364  H  HA   A SER A  1 66  ? -13.05100 -36.78000 39.16700  0.563 22.42902  ? 66  SER A HA   1 
ATOM   365  H  HA   B SER A  1 66  ? -13.10500 -36.78600 39.16700  0.437 22.95443  ? 66  SER A HA   1 
ATOM   366  H  HB2  A SER A  1 66  ? -15.08400 -35.57500 39.46800  0.563 27.04338  ? 66  SER A HB2  1 
ATOM   367  H  HB2  B SER A  1 66  ? -15.15500 -35.18600 38.06000  0.437 24.99286  ? 66  SER A HB2  1 
ATOM   368  H  HB3  A SER A  1 66  ? -15.27500 -35.58000 37.89000  0.563 27.04338  ? 66  SER A HB3  1 
ATOM   369  H  HB3  B SER A  1 66  ? -15.38800 -36.73500 38.32900  0.437 24.99286  ? 66  SER A HB3  1 
ATOM   370  H  HG   A SER A  1 66  ? -15.18300 -37.81100 39.31200  0.563 27.70629  ? 66  SER A HG   1 
ATOM   371  H  HG   B SER A  1 66  ? -14.55800 -35.72800 40.44500  0.437 33.32697  ? 66  SER A HG   1 
ATOM   372  N  N    A ASN A  1 67  ? -12.69400 -38.10600 37.13500  0.563 20.04254  ? 67  ASN A N    1 
ATOM   373  N  N    B ASN A  1 67  ? -12.72000 -38.11700 37.14100  0.437 21.23552  ? 67  ASN A N    1 
ATOM   374  C  CA   A ASN A  1 67  ? -12.42800 -38.83100 35.89800  0.563 19.13528  ? 67  ASN A CA   1 
ATOM   375  C  CA   B ASN A  1 67  ? -12.42600 -38.84100 35.91100  0.437 20.74682  ? 67  ASN A CA   1 
ATOM   376  C  C    A ASN A  1 67  ? -13.71800 -39.41300 35.34700  0.563 23.82832  ? 67  ASN A C    1 
ATOM   377  C  C    B ASN A  1 67  ? -13.71000 -39.43100 35.34800  0.437 24.37110  ? 67  ASN A C    1 
ATOM   378  O  O    A ASN A  1 67  ? -14.57500 -39.90500 36.10000  0.563 26.49701  ? 67  ASN A O    1 
ATOM   379  O  O    B ASN A  1 67  ? -14.55700 -39.94500 36.09500  0.437 26.65000  ? 67  ASN A O    1 
ATOM   380  C  CB   A ASN A  1 67  ? -11.44400 -39.96000 36.19400  0.563 25.04304  ? 67  ASN A CB   1 
ATOM   381  C  CB   B ASN A  1 67  ? -11.43800 -39.97400 36.19400  0.437 24.87176  ? 67  ASN A CB   1 
ATOM   382  C  CG   A ASN A  1 67  ? -10.07000 -39.43200 36.50800  0.563 30.43985  ? 67  ASN A CG   1 
ATOM   383  C  CG   B ASN A  1 67  ? -11.15800 -40.81500 34.96500  0.437 26.19986  ? 67  ASN A CG   1 
ATOM   384  O  OD1  A ASN A  1 67  ? -9.72800  -38.31200 36.12600  0.563 30.07943  ? 67  ASN A OD1  1 
ATOM   385  O  OD1  B ASN A  1 67  ? -10.45300 -40.38800 34.04800  0.437 38.48985  ? 67  ASN A OD1  1 
ATOM   386  N  ND2  A ASN A  1 67  ? -9.28000  -40.21800 37.22600  0.563 42.57787  ? 67  ASN A ND2  1 
ATOM   387  N  ND2  B ASN A  1 67  ? -11.73800 -42.01000 34.92400  0.437 30.89363  ? 67  ASN A ND2  1 
ATOM   388  H  H    A ASN A  1 67  ? -12.56800 -38.56900 37.84900  0.563 24.05361  ? 67  ASN A H    1 
ATOM   389  H  H    B ASN A  1 67  ? -12.60400 -38.57800 37.85800  0.437 25.48518  ? 67  ASN A H    1 
ATOM   390  H  HA   A ASN A  1 67  ? -12.05100 -38.23900 35.22800  0.563 22.96490  ? 67  ASN A HA   1 
ATOM   391  H  HA   B ASN A  1 67  ? -12.03800 -38.23900 35.25700  0.437 24.89874  ? 67  ASN A HA   1 
ATOM   392  H  HB2  A ASN A  1 67  ? -11.75800 -40.46600 36.95900  0.563 30.05421  ? 67  ASN A HB2  1 
ATOM   393  H  HB2  B ASN A  1 67  ? -10.59800 -39.59400 36.49800  0.437 29.84868  ? 67  ASN A HB2  1 
ATOM   394  H  HB3  A ASN A  1 67  ? -11.37800 -40.53800 35.41800  0.563 30.05421  ? 67  ASN A HB3  1 
ATOM   395  H  HB3  B ASN A  1 67  ? -11.80700 -40.55300 36.87900  0.437 29.84868  ? 67  ASN A HB3  1 
ATOM   396  H  HD21 A ASN A  1 67  ? -8.48600  -39.95800 37.43000  0.563 51.09601  ? 67  ASN A HD21 1 
ATOM   397  H  HD21 B ASN A  1 67  ? -11.61200 -42.52600 34.24900  0.437 37.07492  ? 67  ASN A HD21 1 
ATOM   398  H  HD22 A ASN A  1 67  ? -9.56200  -40.98700 37.48700  0.563 51.09601  ? 67  ASN A HD22 1 
ATOM   399  H  HD22 B ASN A  1 67  ? -12.24000 -42.26600 35.57400  0.437 37.07492  ? 67  ASN A HD22 1 
ATOM   400  N  N    . VAL A  1 68  ? -13.83600 -39.37800 34.02500  1.000 19.63244  ? 68  VAL A N    1 
ATOM   401  C  CA   . VAL A  1 68  ? -14.95800 -39.95900 33.29600  1.000 20.96993  ? 68  VAL A CA   1 
ATOM   402  C  C    . VAL A  1 68  ? -14.38500 -41.06100 32.41300  1.000 20.33284  ? 68  VAL A C    1 
ATOM   403  O  O    . VAL A  1 68  ? -13.54700 -40.80400 31.53800  1.000 20.38885  ? 68  VAL A O    1 
ATOM   404  C  CB   . VAL A  1 68  ? -15.68700 -38.91000 32.43900  1.000 19.19043  ? 68  VAL A CB   1 
ATOM   405  C  CG1  . VAL A  1 68  ? -16.86300 -39.53900 31.67100  1.000 22.05179  ? 68  VAL A CG1  1 
ATOM   406  C  CG2  . VAL A  1 68  ? -16.19800 -37.76300 33.33300  1.000 21.47545  ? 68  VAL A CG2  1 
ATOM   407  H  H    . VAL A  1 68  ? -13.25800 -39.00900 33.50600  1.000 23.56149  ? 68  VAL A H    1 
ATOM   408  H  HA   . VAL A  1 68  ? -15.59500 -40.34200 33.91800  1.000 25.16648  ? 68  VAL A HA   1 
ATOM   409  H  HB   . VAL A  1 68  ? -15.06000 -38.55400 31.78900  1.000 23.03108  ? 68  VAL A HB   1 
ATOM   410  H  HG11 . VAL A  1 68  ? -17.36400 -38.83600 31.22900  1.000 26.46471  ? 68  VAL A HG11 1 
ATOM   411  H  HG12 . VAL A  1 68  ? -16.51400 -40.16000 31.01300  1.000 26.46471  ? 68  VAL A HG12 1 
ATOM   412  H  HG13 . VAL A  1 68  ? -17.43500 -40.00900 32.29800  1.000 26.46471  ? 68  VAL A HG13 1 
ATOM   413  H  HG21 . VAL A  1 68  ? -16.57600 -37.06900 32.77100  1.000 25.77310  ? 68  VAL A HG21 1 
ATOM   414  H  HG22 . VAL A  1 68  ? -16.87700 -38.10900 33.93400  1.000 25.77310  ? 68  VAL A HG22 1 
ATOM   415  H  HG23 . VAL A  1 68  ? -15.45500 -37.40600 33.84500  1.000 25.77310  ? 68  VAL A HG23 1 
ATOM   416  N  N    . SER A  1 69  ? -14.84000 -42.28000 32.64200  1.000 23.83986  ? 69  SER A N    1 
ATOM   417  C  CA   . SER A  1 69  ? -14.38800 -43.43100 31.88500  1.000 23.32124  ? 69  SER A CA   1 
ATOM   418  C  C    . SER A  1 69  ? -14.79800 -43.33700 30.42600  1.000 24.16088  ? 69  SER A C    1 
ATOM   419  O  O    . SER A  1 69  ? -15.84100 -42.77300 30.08600  1.000 22.94568  ? 69  SER A O    1 
ATOM   420  C  CB   . SER A  1 69  ? -15.02700 -44.67200 32.49600  1.000 27.87710  ? 69  SER A CB   1 
ATOM   421  O  OG   . SER A  1 69  ? -14.90200 -45.78400 31.65200  1.000 27.48081  ? 69  SER A OG   1 
ATOM   422  H  H    . SER A  1 69  ? -15.42400 -42.47200 33.24400  1.000 28.61040  ? 69  SER A H    1 
ATOM   423  H  HA   . SER A  1 69  ? -13.42000 -43.48800 31.91200  1.000 27.98805  ? 69  SER A HA   1 
ATOM   424  H  HB2  . SER A  1 69  ? -14.58700 -44.86800 33.33800  1.000 33.45508  ? 69  SER A HB2  1 
ATOM   425  H  HB3  . SER A  1 69  ? -15.96900 -44.49700 32.64600  1.000 33.45508  ? 69  SER A HB3  1 
ATOM   426  H  HG   . SER A  1 69  ? -15.25300 -46.45700 32.01000  1.000 32.97953  ? 69  SER A HG   1 
ATOM   427  N  N    . SER A  1 70  ? -13.97700 -43.93700 29.55100  1.000 22.38554  ? 70  SER A N    1 
ATOM   428  C  CA   . SER A  1 70  ? -14.33800 -44.05500 28.14000  1.000 21.76342  ? 70  SER A CA   1 
ATOM   429  C  C    . SER A  1 70  ? -15.60900 -44.86400 27.89800  1.000 22.53622  ? 70  SER A C    1 
ATOM   430  O  O    . SER A  1 70  ? -16.15900 -44.79600 26.79800  1.000 24.25797  ? 70  SER A O    1 
ATOM   431  C  CB   . SER A  1 70  ? -13.17900 -44.63800 27.32800  1.000 23.42379  ? 70  SER A CB   1 
ATOM   432  O  OG   . SER A  1 70  ? -12.95400 -45.99300 27.66400  1.000 24.85650  ? 70  SER A OG   1 
ATOM   433  H  H    . SER A  1 70  ? -13.21300 -44.27900 29.75200  1.000 26.86521  ? 70  SER A H    1 
ATOM   434  H  HA   . SER A  1 70  ? -14.50400 -43.15900 27.80800  1.000 26.11867  ? 70  SER A HA   1 
ATOM   435  H  HB2  . SER A  1 70  ? -13.39400 -44.58000 26.38400  1.000 28.11111  ? 70  SER A HB2  1 
ATOM   436  H  HB3  . SER A  1 70  ? -12.37500 -44.13000 27.51700  1.000 28.11111  ? 70  SER A HB3  1 
ATOM   437  H  HG   . SER A  1 70  ? -12.61200 -46.04600 28.42900  1.000 29.83036  ? 70  SER A HG   1 
ATOM   438  N  N    . LEU A  1 71  ? -16.10900 -45.61500 28.89100  1.000 23.09104  ? 71  LEU A N    1 
ATOM   439  C  CA   . LEU A  1 71  ? -17.40400 -46.26400 28.76100  1.000 27.97724  ? 71  LEU A CA   1 
ATOM   440  C  C    . LEU A  1 71  ? -18.54300 -45.27800 28.49600  1.000 23.43598  ? 71  LEU A C    1 
ATOM   441  O  O    . LEU A  1 71  ? -19.58500 -45.69400 27.96700  1.000 29.05074  ? 71  LEU A O    1 
ATOM   442  C  CB   . LEU A  1 71  ? -17.68800 -47.06900 30.03500  1.000 28.13882  ? 71  LEU A CB   1 
ATOM   443  C  CG   . LEU A  1 71  ? -19.06000 -47.71600 30.15300  1.000 43.75493  ? 71  LEU A CG   1 
ATOM   444  C  CD1  . LEU A  1 71  ? -19.26800 -48.69300 29.01100  1.000 40.53646  ? 71  LEU A CD1  1 
ATOM   445  C  CD2  . LEU A  1 71  ? -19.16500 -48.40600 31.50700  1.000 41.42260  ? 71  LEU A CD2  1 
ATOM   446  H  H    . LEU A  1 71  ? -15.71600 -45.75800 29.64200  1.000 27.71180  ? 71  LEU A H    1 
ATOM   447  H  HA   . LEU A  1 71  ? -17.37700 -46.87000 28.00400  1.000 33.57525  ? 71  LEU A HA   1 
ATOM   448  H  HB2  . LEU A  1 71  ? -17.03300 -47.78200 30.08900  1.000 33.76914  ? 71  LEU A HB2  1 
ATOM   449  H  HB3  . LEU A  1 71  ? -17.59100 -46.47100 30.79300  1.000 33.76914  ? 71  LEU A HB3  1 
ATOM   450  H  HG   . LEU A  1 71  ? -19.76400 -47.05000 30.09600  1.000 52.50848  ? 71  LEU A HG   1 
ATOM   451  H  HD11 . LEU A  1 71  ? -20.14600 -49.09700 29.09600  1.000 48.64632  ? 71  LEU A HD11 1 
ATOM   452  H  HD12 . LEU A  1 71  ? -19.20500 -48.21400 28.17000  1.000 48.64632  ? 71  LEU A HD12 1 
ATOM   453  H  HD13 . LEU A  1 71  ? -18.58300 -49.37900 29.05300  1.000 48.64632  ? 71  LEU A HD13 1 
ATOM   454  H  HD21 . LEU A  1 71  ? -20.04700 -48.80200 31.59200  1.000 49.70968  ? 71  LEU A HD21 1 
ATOM   455  H  HD22 . LEU A  1 71  ? -18.48600 -49.09700 31.56200  1.000 49.70968  ? 71  LEU A HD22 1 
ATOM   456  H  HD23 . LEU A  1 71  ? -19.02800 -47.75000 32.20700  1.000 49.70968  ? 71  LEU A HD23 1 
ATOM   457  N  N    . VAL A  1 72  ? -18.36900 -44.00100 28.81900  1.000 23.94499  ? 72  VAL A N    1 
ATOM   458  C  CA   . VAL A  1 72  ? -19.40800 -42.99600 28.61700  1.000 22.68732  ? 72  VAL A CA   1 
ATOM   459  C  C    . VAL A  1 72  ? -19.88300 -42.97800 27.16500  1.000 26.26719  ? 72  VAL A C    1 
ATOM   460  O  O    . VAL A  1 72  ? -19.10400 -43.11400 26.21800  1.000 24.82212  ? 72  VAL A O    1 
ATOM   461  C  CB   . VAL A  1 72  ? -18.85400 -41.62800 29.05100  1.000 26.47059  ? 72  VAL A CB   1 
ATOM   462  C  CG1  . VAL A  1 72  ? -17.78400 -41.11500 28.08200  1.000 23.81115  ? 72  VAL A CG1  1 
ATOM   463  C  CG2  . VAL A  1 72  ? -19.95200 -40.55700 29.19400  1.000 27.11844  ? 72  VAL A CG2  1 
ATOM   464  H  H    . VAL A  1 72  ? -17.64700 -43.68400 29.16300  1.000 28.73655  ? 72  VAL A H    1 
ATOM   465  H  HA   . VAL A  1 72  ? -20.18200 -43.22400 29.15400  1.000 27.22734  ? 72  VAL A HA   1 
ATOM   466  H  HB   . VAL A  1 72  ? -18.45500 -41.77000 29.92400  1.000 31.76727  ? 72  VAL A HB   1 
ATOM   467  H  HG11 . VAL A  1 72  ? -17.28900 -40.39900 28.50900  1.000 28.57595  ? 72  VAL A HG11 1 
ATOM   468  H  HG12 . VAL A  1 72  ? -17.18500 -41.84500 27.85900  1.000 28.57595  ? 72  VAL A HG12 1 
ATOM   469  H  HG13 . VAL A  1 72  ? -18.21700 -40.78600 27.27900  1.000 28.57595  ? 72  VAL A HG13 1 
ATOM   470  H  HG21 . VAL A  1 72  ? -19.56100 -39.75300 29.56900  1.000 32.54469  ? 72  VAL A HG21 1 
ATOM   471  H  HG22 . VAL A  1 72  ? -20.32300 -40.36700 28.31900  1.000 32.54469  ? 72  VAL A HG22 1 
ATOM   472  H  HG23 . VAL A  1 72  ? -20.64600 -40.89300 29.78200  1.000 32.54469  ? 72  VAL A HG23 1 
ATOM   473  N  N    . ARG A  1 73  ? -21.17700 -42.75800 26.98200  1.000 25.84554  ? 73  ARG A N    1 
ATOM   474  C  CA   . ARG A  1 73  ? -21.76000 -42.82100 25.65100  1.000 27.73109  ? 73  ARG A CA   1 
ATOM   475  C  C    . ARG A  1 73  ? -21.44900 -41.55900 24.86100  1.000 25.38585  ? 73  ARG A C    1 
ATOM   476  O  O    . ARG A  1 73  ? -21.66400 -40.43800 25.32100  1.000 29.25723  ? 73  ARG A O    1 
ATOM   477  C  CB   . ARG A  1 73  ? -23.27800 -42.99900 25.75200  1.000 30.36336  ? 73  ARG A CB   1 
ATOM   478  C  CG   . ARG A  1 73  ? -23.72500 -44.33000 26.32300  1.000 56.90521  ? 73  ARG A CG   1 
ATOM   479  C  CD   . ARG A  1 73  ? -25.25800 -44.43900 26.36600  1.000 74.37450  ? 73  ARG A CD   1 
ATOM   480  N  NE   . ARG A  1 73  ? -25.70800 -45.67700 26.99600  1.000 83.21907  ? 73  ARG A NE   1 
ATOM   481  C  CZ   . ARG A  1 73  ? -26.97400 -45.97100 27.26400  1.000 88.40216  ? 73  ARG A CZ   1 
ATOM   482  N  NH1  . ARG A  1 73  ? -27.95700 -45.13900 26.95800  1.000 92.09303  ? 73  ARG A NH1  1 
ATOM   483  N  NH2  . ARG A  1 73  ? -27.26000 -47.12600 27.86000  1.000 82.02692  ? 73  ARG A NH2  1 
ATOM   484  H  H    . ARG A  1 73  ? -21.73600 -42.57200 27.60900  1.000 31.01721  ? 73  ARG A H    1 
ATOM   485  H  HA   . ARG A  1 73  ? -21.37700 -43.57600 25.17800  1.000 33.27987  ? 73  ARG A HA   1 
ATOM   486  H  HB2  . ARG A  1 73  ? -23.63300 -42.30200 26.32500  1.000 36.43860  ? 73  ARG A HB2  1 
ATOM   487  H  HB3  . ARG A  1 73  ? -23.65700 -42.92200 24.86200  1.000 36.43860  ? 73  ARG A HB3  1 
ATOM   488  H  HG2  . ARG A  1 73  ? -23.38400 -45.04900 25.76800  1.000 68.28881  ? 73  ARG A HG2  1 
ATOM   489  H  HG3  . ARG A  1 73  ? -23.38800 -44.42100 27.22800  1.000 68.28881  ? 73  ARG A HG3  1 
ATOM   490  H  HD2  . ARG A  1 73  ? -25.61600 -43.69400 26.87500  1.000 89.25196  ? 73  ARG A HD2  1 
ATOM   491  H  HD3  . ARG A  1 73  ? -25.60500 -44.41800 25.46000  1.000 89.25196  ? 73  ARG A HD3  1 
ATOM   492  H  HE   . ARG A  1 73  ? -25.10900 -46.25700 27.20900  1.000 99.86545  ? 73  ARG A HE   1 
ATOM   493  H  HH11 . ARG A  1 73  ? -27.78200 -44.38900 26.57700  1.000 110.51420 ? 73  ARG A HH11 1 
ATOM   494  H  HH12 . ARG A  1 73  ? -28.77000 -45.34900 27.14100  1.000 110.51420 ? 73  ARG A HH12 1 
ATOM   495  H  HH21 . ARG A  1 73  ? -26.62700 -47.67200 28.06600  1.000 98.43487  ? 73  ARG A HH21 1 
ATOM   496  H  HH22 . ARG A  1 73  ? -28.07600 -47.32800 28.03900  1.000 98.43487  ? 73  ARG A HH22 1 
ATOM   497  N  N    . GLY A  1 74  ? -20.90700 -41.72800 23.67700  1.000 22.06439  ? 74  GLY A N    1 
ATOM   498  C  CA   . GLY A  1 74  ? -20.82300 -40.61900 22.75500  1.000 22.80785  ? 74  GLY A CA   1 
ATOM   499  C  C    . GLY A  1 74  ? -19.47600 -39.94300 22.64000  1.000 19.96804  ? 74  GLY A C    1 
ATOM   500  O  O    . GLY A  1 74  ? -19.32700 -39.07800 21.77500  1.000 22.37943  ? 74  GLY A O    1 
ATOM   501  H  H    . GLY A  1 74  ? -20.58200 -42.47000 23.38600  1.000 26.47983  ? 74  GLY A H    1 
ATOM   502  H  HA2  . GLY A  1 74  ? -21.06300 -40.93800 21.87100  1.000 27.37198  ? 74  GLY A HA2  1 
ATOM   503  H  HA3  . GLY A  1 74  ? -21.46300 -39.94400 23.03200  1.000 27.37198  ? 74  GLY A HA3  1 
ATOM   504  N  N    . PHE A  1 75  ? -18.50600 -40.29700 23.48800  1.000 21.04667  ? 75  PHE A N    1 
ATOM   505  C  CA   . PHE A  1 75  ? -17.15700 -39.74900 23.42200  1.000 19.68067  ? 75  PHE A CA   1 
ATOM   506  C  C    . PHE A  1 75  ? -16.24400 -40.68200 24.21000  1.000 17.94054  ? 75  PHE A C    1 
ATOM   507  O  O    . PHE A  1 75  ? -16.68700 -41.70000 24.74800  1.000 19.28737  ? 75  PHE A O    1 
ATOM   508  C  CB   . PHE A  1 75  ? -17.08700 -38.28500 23.88600  1.000 18.23434  ? 75  PHE A CB   1 
ATOM   509  C  CG   . PHE A  1 75  ? -17.44400 -38.04200 25.34400  1.000 18.97920  ? 75  PHE A CG   1 
ATOM   510  C  CD1  . PHE A  1 75  ? -18.76800 -38.05900 25.75700  1.000 17.53022  ? 75  PHE A CD1  1 
ATOM   511  C  CD2  . PHE A  1 75  ? -16.47000 -37.75100 26.29500  1.000 18.15336  ? 75  PHE A CD2  1 
ATOM   512  C  CE1  . PHE A  1 75  ? -19.09900 -37.82900 27.08200  1.000 20.14417  ? 75  PHE A CE1  1 
ATOM   513  C  CE2  . PHE A  1 75  ? -16.82900 -37.49400 27.62300  1.000 18.06727  ? 75  PHE A CE2  1 
ATOM   514  C  CZ   . PHE A  1 75  ? -18.10500 -37.54000 28.00600  1.000 19.53570  ? 75  PHE A CZ   1 
ATOM   515  H  H    . PHE A  1 75  ? -18.61100 -40.86600 24.12400  1.000 25.25856  ? 75  PHE A H    1 
ATOM   516  H  HA   . PHE A  1 75  ? -16.85900 -39.74400 22.49900  1.000 23.61937  ? 75  PHE A HA   1 
ATOM   517  H  HB2  . PHE A  1 75  ? -16.18000 -37.96700 23.75400  1.000 21.88378  ? 75  PHE A HB2  1 
ATOM   518  H  HB3  . PHE A  1 75  ? -17.70200 -37.76400 23.34700  1.000 21.88378  ? 75  PHE A HB3  1 
ATOM   519  H  HD1  . PHE A  1 75  ? -19.44100 -38.22600 25.13700  1.000 21.03883  ? 75  PHE A HD1  1 
ATOM   520  H  HD2  . PHE A  1 75  ? -15.57400 -37.72700 26.04600  1.000 21.78659  ? 75  PHE A HD2  1 
ATOM   521  H  HE1  . PHE A  1 75  ? -19.98800 -37.86800 27.35300  1.000 24.17557  ? 75  PHE A HE1  1 
ATOM   522  H  HE2  . PHE A  1 75  ? -16.17000 -37.28900 28.24600  1.000 21.68328  ? 75  PHE A HE2  1 
ATOM   523  H  HZ   . PHE A  1 75  ? -18.32900 -37.37700 28.89400  1.000 23.44541  ? 75  PHE A HZ   1 
ATOM   524  N  N    . GLY A  1 76  ? -14.96100 -40.35300 24.24700  1.000 18.17629  ? 76  GLY A N    1 
ATOM   525  C  CA   . GLY A  1 76  ? -13.96200 -41.28600 24.75300  1.000 18.82794  ? 76  GLY A CA   1 
ATOM   526  C  C    . GLY A  1 76  ? -13.55800 -41.08800 26.20100  1.000 20.24632  ? 76  GLY A C    1 
ATOM   527  O  O    . GLY A  1 76  ? -12.47400 -41.51700 26.59000  1.000 21.32452  ? 76  GLY A O    1 
ATOM   528  H  H    . GLY A  1 76  ? -14.64200 -39.59700 23.98700  1.000 21.81411  ? 76  GLY A H    1 
ATOM   529  H  HA2  . GLY A  1 76  ? -14.31000 -42.18800 24.66700  1.000 22.59609  ? 76  GLY A HA2  1 
ATOM   530  H  HA3  . GLY A  1 76  ? -13.16000 -41.20400 24.21300  1.000 22.59609  ? 76  GLY A HA3  1 
ATOM   531  N  N    . GLY A  1 77  ? -14.41900 -40.48900 27.01000  1.000 18.67399  ? 77  GLY A N    1 
ATOM   532  C  CA   . GLY A  1 77  ? -14.09300 -40.18600 28.39200  1.000 19.61140  ? 77  GLY A CA   1 
ATOM   533  C  C    . GLY A  1 77  ? -13.44200 -38.83700 28.52800  1.000 18.31511  ? 77  GLY A C    1 
ATOM   534  O  O    . GLY A  1 77  ? -13.26300 -38.08600 27.55800  1.000 18.32342  ? 77  GLY A O    1 
ATOM   535  H  H    . GLY A  1 77  ? -15.21000 -40.24400 26.77900  1.000 22.41135  ? 77  GLY A H    1 
ATOM   536  H  HA2  . GLY A  1 77  ? -14.90300 -40.19200 28.92500  1.000 23.53624  ? 77  GLY A HA2  1 
ATOM   537  H  HA3  . GLY A  1 77  ? -13.48400 -40.85800 28.73600  1.000 23.53624  ? 77  GLY A HA3  1 
ATOM   538  N  N    . GLY A  1 78  ? -13.06900 -38.50400 29.75500  1.000 17.90153  ? 78  GLY A N    1 
ATOM   539  C  CA   . GLY A  1 78  ? -12.46600 -37.21000 29.97000  1.000 18.67110  ? 78  GLY A CA   1 
ATOM   540  C  C    . GLY A  1 78  ? -12.19300 -36.95700 31.43200  1.000 17.66607  ? 78  GLY A C    1 
ATOM   541  O  O    . GLY A  1 78  ? -12.30300 -37.85000 32.27600  1.000 19.54778  ? 78  GLY A O    1 
ATOM   542  H  H    . GLY A  1 78  ? -13.15300 -38.99700 30.45500  1.000 21.48440  ? 78  GLY A H    1 
ATOM   543  H  HA2  . GLY A  1 78  ? -11.62700 -37.15900 29.48600  1.000 22.40788  ? 78  GLY A HA2  1 
ATOM   544  H  HA3  . GLY A  1 78  ? -13.06200 -36.51700 29.64400  1.000 22.40788  ? 78  GLY A HA3  1 
ATOM   545  N  N    . THR A  1 79  ? -11.79000 -35.72800 31.70200  1.000 15.93570  ? 79  THR A N    1 
ATOM   546  C  CA   . THR A  1 79  ? -11.48900 -35.25400 33.04800  1.000 15.19675  ? 79  THR A CA   1 
ATOM   547  C  C    . THR A  1 79  ? -12.31900 -34.00500 33.27400  1.000 14.65175  ? 79  THR A C    1 
ATOM   548  O  O    . THR A  1 79  ? -12.19000 -33.04200 32.51200  1.000 14.98179  ? 79  THR A O    1 
ATOM   549  C  CB   . THR A  1 79  ? -10.00300 -34.92700 33.24100  1.000 16.93946  ? 79  THR A CB   1 
ATOM   550  O  OG1  . THR A  1 79  ? -9.20200  -36.05600 32.85400  1.000 19.83795  ? 79  THR A OG1  1 
ATOM   551  C  CG2  . THR A  1 79  ? -9.71600  -34.56600 34.69500  1.000 18.47935  ? 79  THR A CG2  1 
ATOM   552  H  H    . THR A  1 79  ? -11.67700 -35.12400 31.10100  1.000 19.12540  ? 79  THR A H    1 
ATOM   553  H  HA   . THR A  1 79  ? -11.72300 -35.94200 33.69000  1.000 18.23867  ? 79  THR A HA   1 
ATOM   554  H  HB   . THR A  1 79  ? -9.76700  -34.16600 32.68800  1.000 20.32991  ? 79  THR A HB   1 
ATOM   555  H  HG1  . THR A  1 79  ? -8.38700  -35.87200 32.93800  1.000 23.80810  ? 79  THR A HG1  1 
ATOM   556  H  HG21 . THR A  1 79  ? -8.76400  -34.42500 34.82000  1.000 22.17778  ? 79  THR A HG21 1 
ATOM   557  H  HG22 . THR A  1 79  ? -10.18900 -33.75400 34.93500  1.000 22.17778  ? 79  THR A HG22 1 
ATOM   558  H  HG23 . THR A  1 79  ? -10.00700 -35.28400 35.27900  1.000 22.17778  ? 79  THR A HG23 1 
ATOM   559  N  N    . ILE A  1 80  ? -13.15700 -33.99700 34.29900  1.000 16.11296  ? 80  ILE A N    1 
ATOM   560  C  CA   . ILE A  1 80  ? -13.92300 -32.81200 34.68400  1.000 15.35673  ? 80  ILE A CA   1 
ATOM   561  C  C    . ILE A  1 80  ? -13.10400 -32.03200 35.71000  1.000 15.69633  ? 80  ILE A C    1 
ATOM   562  O  O    . ILE A  1 80  ? -12.64400 -32.60700 36.70800  1.000 17.25217  ? 80  ILE A O    1 
ATOM   563  C  CB   . ILE A  1 80  ? -15.29000 -33.17500 35.30000  1.000 16.25921  ? 80  ILE A CB   1 
ATOM   564  C  CG1  . ILE A  1 80  ? -16.06600 -34.15300 34.40600  1.000 16.85971  ? 80  ILE A CG1  1 
ATOM   565  C  CG2  . ILE A  1 80  ? -16.08500 -31.86200 35.43600  1.000 20.00257  ? 80  ILE A CG2  1 
ATOM   566  C  CD1  . ILE A  1 80  ? -17.33500 -34.64800 34.98700  1.000 18.84888  ? 80  ILE A CD1  1 
ATOM   567  H  H    . ILE A  1 80  ? -13.30600 -34.68000 34.80100  1.000 19.33811  ? 80  ILE A H    1 
ATOM   568  H  HA   . ILE A  1 80  ? -14.07500 -32.27700 33.88900  1.000 18.43064  ? 80  ILE A HA   1 
ATOM   569  H  HB   . ILE A  1 80  ? -15.15700 -33.60800 36.15800  1.000 19.51362  ? 80  ILE A HB   1 
ATOM   570  H  HG12 . ILE A  1 80  ? -16.28100 -33.70600 33.57300  1.000 20.23421  ? 80  ILE A HG12 1 
ATOM   571  H  HG13 . ILE A  1 80  ? -15.50400 -34.92500 34.23300  1.000 20.23421  ? 80  ILE A HG13 1 
ATOM   572  H  HG21 . ILE A  1 80  ? -16.95400 -32.05700 35.82100  1.000 24.00565  ? 80  ILE A HG21 1 
ATOM   573  H  HG22 . ILE A  1 80  ? -15.59700 -31.25400 36.01300  1.000 24.00565  ? 80  ILE A HG22 1 
ATOM   574  H  HG23 . ILE A  1 80  ? -16.19400 -31.46600 34.55700  1.000 24.00565  ? 80  ILE A HG23 1 
ATOM   575  H  HD11 . ILE A  1 80  ? -17.67400 -35.37100 34.43600  1.000 22.62122  ? 80  ILE A HD11 1 
ATOM   576  H  HD12 . ILE A  1 80  ? -17.16700 -34.96900 35.88700  1.000 22.62122  ? 80  ILE A HD12 1 
ATOM   577  H  HD13 . ILE A  1 80  ? -17.97600 -33.92100 35.01000  1.000 22.62122  ? 80  ILE A HD13 1 
ATOM   578  N  N    . TYR A  1 81  ? -12.97000 -30.73300 35.49400  1.000 14.80452  ? 81  TYR A N    1 
ATOM   579  C  CA   . TYR A  1 81  ? -12.35900 -29.76900 36.40500  1.000 14.68713  ? 81  TYR A CA   1 
ATOM   580  C  C    . TYR A  1 81  ? -13.47100 -28.83900 36.85200  1.000 15.34465  ? 81  TYR A C    1 
ATOM   581  O  O    . TYR A  1 81  ? -14.22600 -28.32500 36.01200  1.000 15.08286  ? 81  TYR A O    1 
ATOM   582  C  CB   . TYR A  1 81  ? -11.28800 -28.95400 35.68000  1.000 15.73774  ? 81  TYR A CB   1 
ATOM   583  C  CG   . TYR A  1 81  ? -10.12000 -29.75400 35.12000  1.000 14.96381  ? 81  TYR A CG   1 
ATOM   584  C  CD1  . TYR A  1 81  ? -10.19500 -30.41400 33.91100  1.000 14.73403  ? 81  TYR A CD1  1 
ATOM   585  C  CD2  . TYR A  1 81  ? -8.94100  -29.85500 35.82800  1.000 15.63047  ? 81  TYR A CD2  1 
ATOM   586  C  CE1  . TYR A  1 81  ? -9.14800  -31.11100 33.43000  1.000 15.46589  ? 81  TYR A CE1  1 
ATOM   587  C  CE2  . TYR A  1 81  ? -7.88500  -30.57500 35.36600  1.000 17.33568  ? 81  TYR A CE2  1 
ATOM   588  C  CZ   . TYR A  1 81  ? -7.98400  -31.21000 34.15400  1.000 17.53333  ? 81  TYR A CZ   1 
ATOM   589  O  OH   . TYR A  1 81  ? -6.89800  -31.91900 33.71000  1.000 19.69322  ? 81  TYR A OH   1 
ATOM   590  H  H    . TYR A  1 81  ? -13.24600 -30.35400 34.77300  1.000 17.76799  ? 81  TYR A H    1 
ATOM   591  H  HA   . TYR A  1 81  ? -11.94800 -30.21200 37.16400  1.000 17.62712  ? 81  TYR A HA   1 
ATOM   592  H  HB2  . TYR A  1 81  ? -11.70700 -28.49500 34.93500  1.000 18.88784  ? 81  TYR A HB2  1 
ATOM   593  H  HB3  . TYR A  1 81  ? -10.92200 -28.30900 36.30400  1.000 18.88784  ? 81  TYR A HB3  1 
ATOM   594  H  HD1  . TYR A  1 81  ? -10.98300 -30.37700 33.41900  1.000 17.68340  ? 81  TYR A HD1  1 
ATOM   595  H  HD2  . TYR A  1 81  ? -8.86600  -29.41800 36.64500  1.000 18.75912  ? 81  TYR A HD2  1 
ATOM   596  H  HE1  . TYR A  1 81  ? -9.21200  -31.52700 32.60100  1.000 18.56163  ? 81  TYR A HE1  1 
ATOM   597  H  HE2  . TYR A  1 81  ? -7.10300  -30.63700 35.86700  1.000 20.80538  ? 81  TYR A HE2  1 
ATOM   598  H  HH   . TYR A  1 81  ? -7.04600  -32.21900 32.93900  1.000 23.63443  ? 81  TYR A HH   1 
ATOM   599  N  N    . TYR A  1 82  ? -13.57600 -28.59600 38.14900  1.000 16.31578  ? 82  TYR A N    1 
ATOM   600  C  CA   . TYR A  1 82  ? -14.68400 -27.77000 38.61700  1.000 16.03246  ? 82  TYR A CA   1 
ATOM   601  C  C    . TYR A  1 82  ? -14.30600 -27.04800 39.89600  1.000 15.96684  ? 82  TYR A C    1 
ATOM   602  O  O    . TYR A  1 82  ? -13.54400 -27.57600 40.72100  1.000 17.12875  ? 82  TYR A O    1 
ATOM   603  C  CB   . TYR A  1 82  ? -15.96400 -28.60600 38.80500  1.000 18.20417  ? 82  TYR A CB   1 
ATOM   604  C  CG   . TYR A  1 82  ? -15.82500 -29.77600 39.72500  1.000 18.17497  ? 82  TYR A CG   1 
ATOM   605  C  CD1  . TYR A  1 82  ? -15.37900 -31.01400 39.23900  1.000 24.48886  ? 82  TYR A CD1  1 
ATOM   606  C  CD2  . TYR A  1 82  ? -16.11700 -29.65700 41.04500  1.000 18.45903  ? 82  TYR A CD2  1 
ATOM   607  C  CE1  . TYR A  1 82  ? -15.25800 -32.08700 40.09400  1.000 29.06733  ? 82  TYR A CE1  1 
ATOM   608  C  CE2  . TYR A  1 82  ? -15.99400 -30.74100 41.93100  1.000 22.95997  ? 82  TYR A CE2  1 
ATOM   609  C  CZ   . TYR A  1 82  ? -15.56800 -31.94800 41.40200  1.000 27.09766  ? 82  TYR A CZ   1 
ATOM   610  O  OH   . TYR A  1 82  ? -15.44600 -32.99500 42.30100  1.000 47.41999  ? 82  TYR A OH   1 
ATOM   611  H  H    . TYR A  1 82  ? -13.03900 -28.88600 38.75600  1.000 19.58150  ? 82  TYR A H    1 
ATOM   612  H  HA   . TYR A  1 82  ? -14.86200 -27.07900 37.96100  1.000 19.24151  ? 82  TYR A HA   1 
ATOM   613  H  HB2  . TYR A  1 82  ? -16.65600 -28.03100 39.16800  1.000 21.84757  ? 82  TYR A HB2  1 
ATOM   614  H  HB3  . TYR A  1 82  ? -16.23700 -28.94700 37.93900  1.000 21.84757  ? 82  TYR A HB3  1 
ATOM   615  H  HD1  . TYR A  1 82  ? -15.16500 -31.11000 38.33900  1.000 29.38919  ? 82  TYR A HD1  1 
ATOM   616  H  HD2  . TYR A  1 82  ? -16.40600 -28.83600 41.37200  1.000 22.15340  ? 82  TYR A HD2  1 
ATOM   617  H  HE1  . TYR A  1 82  ? -14.96300 -32.90800 39.77100  1.000 34.88336  ? 82  TYR A HE1  1 
ATOM   618  H  HE2  . TYR A  1 82  ? -16.19000 -30.65100 42.83600  1.000 27.55453  ? 82  TYR A HE2  1 
ATOM   619  H  HH   . TYR A  1 82  ? -15.08500 -33.65400 41.92600  1.000 56.90654  ? 82  TYR A HH   1 
ATOM   620  N  N    . PRO A  1 83  ? -14.88100 -25.87300 40.13200  1.000 15.60362  ? 83  PRO A N    1 
ATOM   621  C  CA   . PRO A  1 83  ? -14.59600 -25.15400 41.36900  1.000 17.82780  ? 83  PRO A CA   1 
ATOM   622  C  C    . PRO A  1 83  ? -15.18500 -25.85300 42.57500  1.000 21.66150  ? 83  PRO A C    1 
ATOM   623  O  O    . PRO A  1 83  ? -16.25200 -26.46600 42.50100  1.000 23.38708  ? 83  PRO A O    1 
ATOM   624  C  CB   . PRO A  1 83  ? -15.25200 -23.78300 41.17800  1.000 24.20561  ? 83  PRO A CB   1 
ATOM   625  C  CG   . PRO A  1 83  ? -15.71300 -23.73200 39.85500  1.000 22.27756  ? 83  PRO A CG   1 
ATOM   626  C  CD   . PRO A  1 83  ? -15.70500 -25.08600 39.22400  1.000 16.48835  ? 83  PRO A CD   1 
ATOM   627  H  HA   . PRO A  1 83  ? -13.63700 -25.04700 41.47300  1.000 21.39592  ? 83  PRO A HA   1 
ATOM   628  H  HB2  . PRO A  1 83  ? -15.99100 -23.69000 41.79900  1.000 29.04929  ? 83  PRO A HB2  1 
ATOM   629  H  HB3  . PRO A  1 83  ? -14.59600 -23.08600 41.33600  1.000 29.04929  ? 83  PRO A HB3  1 
ATOM   630  H  HG2  . PRO A  1 83  ? -16.61800 -23.38300 39.86200  1.000 26.73564  ? 83  PRO A HG2  1 
ATOM   631  H  HG3  . PRO A  1 83  ? -15.13200 -23.13800 39.35400  1.000 26.73564  ? 83  PRO A HG3  1 
ATOM   632  H  HD2  . PRO A  1 83  ? -16.60400 -25.44700 39.17200  1.000 19.78858  ? 83  PRO A HD2  1 
ATOM   633  H  HD3  . PRO A  1 83  ? -15.30900 -25.05200 38.33900  1.000 19.78858  ? 83  PRO A HD3  1 
ATOM   634  N  N    . VAL A  1 84  ? -14.49400 -25.72400 43.69700  1.000 24.91620  ? 84  VAL A N    1 
ATOM   635  C  CA   . VAL A  1 84  ? -14.93300 -26.37800 44.92200  1.000 27.45157  ? 84  VAL A CA   1 
ATOM   636  C  C    . VAL A  1 84  ? -15.99500 -25.57700 45.65900  1.000 40.48833  ? 84  VAL A C    1 
ATOM   637  O  O    . VAL A  1 84  ? -16.96200 -26.14800 46.17900  1.000 39.95757  ? 84  VAL A O    1 
ATOM   638  C  CB   . VAL A  1 84  ? -13.70900 -26.67100 45.80000  1.000 30.43097  ? 84  VAL A CB   1 
ATOM   639  C  CG1  . VAL A  1 84  ? -14.12600 -26.99900 47.20400  1.000 40.52549  ? 84  VAL A CG1  1 
ATOM   640  C  CG2  . VAL A  1 84  ? -12.93600 -27.81000 45.16600  1.000 32.84072  ? 84  VAL A CG2  1 
ATOM   641  H  H    . VAL A  1 84  ? -13.77100 -25.26500 43.77700  1.000 29.90200  ? 84  VAL A H    1 
ATOM   642  H  HA   . VAL A  1 84  ? -15.35700 -27.21800 44.68500  1.000 32.94445  ? 84  VAL A HA   1 
ATOM   643  H  HB   . VAL A  1 84  ? -13.13500 -25.89100 45.85800  1.000 36.51973  ? 84  VAL A HB   1 
ATOM   644  H  HG11 . VAL A  1 84  ? -13.40600 -27.47700 47.64500  1.000 48.63315  ? 84  VAL A HG11 1 
ATOM   645  H  HG12 . VAL A  1 84  ? -14.31400 -26.17400 47.67900  1.000 48.63315  ? 84  VAL A HG12 1 
ATOM   646  H  HG13 . VAL A  1 84  ? -14.92200 -27.55300 47.17600  1.000 48.63315  ? 84  VAL A HG13 1 
ATOM   647  H  HG21 . VAL A  1 84  ? -12.16800 -28.01800 45.72100  1.000 39.41142  ? 84  VAL A HG21 1 
ATOM   648  H  HG22 . VAL A  1 84  ? -13.51500 -28.58600 45.09900  1.000 39.41142  ? 84  VAL A HG22 1 
ATOM   649  H  HG23 . VAL A  1 84  ? -12.64200 -27.54000 44.28200  1.000 39.41142  ? 84  VAL A HG23 1 
ATOM   650  N  N    . ASN A  1 85  ? -15.83500 -24.26700 45.74800  1.000 33.04845  ? 85  ASN A N    1 
ATOM   651  C  CA   . ASN A  1 85  ? -16.75400 -23.53600 46.62400  1.000 34.79028  ? 85  ASN A CA   1 
ATOM   652  C  C    . ASN A  1 85  ? -17.57800 -22.49700 45.87900  1.000 43.50538  ? 85  ASN A C    1 
ATOM   653  O  O    . ASN A  1 85  ? -17.68000 -21.34400 46.31300  1.000 41.59900  ? 85  ASN A O    1 
ATOM   654  C  CB   . ASN A  1 85  ? -15.99400 -22.79300 47.73600  1.000 38.17569  ? 85  ASN A CB   1 
ATOM   655  C  CG   . ASN A  1 85  ? -15.30400 -23.72500 48.69500  1.000 68.15976  ? 85  ASN A CG   1 
ATOM   656  O  OD1  . ASN A  1 85  ? -15.84900 -24.76500 49.06900  1.000 69.19418  ? 85  ASN A OD1  1 
ATOM   657  N  ND2  . ASN A  1 85  ? -14.09000 -23.35700 49.10700  1.000 70.97686  ? 85  ASN A ND2  1 
ATOM   658  H  H    . ASN A  1 85  ? -15.24000 -23.80100 45.33900  1.000 39.66070  ? 85  ASN A H    1 
ATOM   659  H  HA   . ASN A  1 85  ? -17.34700 -24.20300 47.00300  1.000 41.75090  ? 85  ASN A HA   1 
ATOM   660  H  HB2  . ASN A  1 85  ? -15.31900 -22.22500 47.33300  1.000 45.81340  ? 85  ASN A HB2  1 
ATOM   661  H  HB3  . ASN A  1 85  ? -16.62200 -22.25400 48.24200  1.000 45.81340  ? 85  ASN A HB3  1 
ATOM   662  H  HD21 . ASN A  1 85  ? -13.74400 -22.62200 48.82400  1.000 85.17479  ? 85  ASN A HD21 1 
ATOM   663  H  HD22 . ASN A  1 85  ? -13.65300 -23.85500 49.65600  1.000 85.17479  ? 85  ASN A HD22 1 
ATOM   664  N  N    . ALA A  1 86  ? -18.16700 -22.87300 44.75800  1.000 27.52634  ? 86  ALA A N    1 
ATOM   665  C  CA   . ALA A  1 86  ? -18.89500 -21.93100 43.93400  1.000 29.48129  ? 86  ALA A CA   1 
ATOM   666  C  C    . ALA A  1 86  ? -20.37000 -22.09800 44.28000  1.000 32.47153  ? 86  ALA A C    1 
ATOM   667  O  O    . ALA A  1 86  ? -20.85300 -23.22500 44.42900  1.000 37.09733  ? 86  ALA A O    1 
ATOM   668  C  CB   . ALA A  1 86  ? -18.64500 -22.19000 42.45700  1.000 27.84998  ? 86  ALA A CB   1 
ATOM   669  H  H    . ALA A  1 86  ? -18.15800 -23.67700 44.45200  1.000 33.03417  ? 86  ALA A H    1 
ATOM   670  H  HA   . ALA A  1 86  ? -18.61800 -21.01700 44.10600  1.000 35.38010  ? 86  ALA A HA   1 
ATOM   671  H  HB1  . ALA A  1 86  ? -19.16500 -21.56100 41.93300  1.000 33.42254  ? 86  ALA A HB1  1 
ATOM   672  H  HB2  . ALA A  1 86  ? -17.70000 -22.07500 42.27100  1.000 33.42254  ? 86  ALA A HB2  1 
ATOM   673  H  HB3  . ALA A  1 86  ? -18.91500 -23.09800 42.24600  1.000 33.42254  ? 86  ALA A HB3  1 
ATOM   674  N  N    . GLU A  1 87  ? -21.04700 -20.98500 44.47800  1.000 30.78181  ? 87  GLU A N    1 
ATOM   675  C  CA   . GLU A  1 87  ? -22.46700 -21.00700 44.79200  1.000 33.38083  ? 87  GLU A CA   1 
ATOM   676  C  C    . GLU A  1 87  ? -23.23600 -21.01200 43.48300  1.000 25.81383  ? 87  GLU A C    1 
ATOM   677  O  O    . GLU A  1 87  ? -22.88700 -20.28100 42.55800  1.000 32.18882  ? 87  GLU A O    1 
ATOM   678  C  CB   . GLU A  1 87  ? -22.85000 -19.77500 45.62000  1.000 40.17466  ? 87  GLU A CB   1 
ATOM   679  C  CG   . GLU A  1 87  ? -22.02000 -19.59800 46.89000  1.000 58.12858  ? 87  GLU A CG   1 
ATOM   680  C  CD   . GLU A  1 87  ? -22.73200 -18.76700 47.94700  1.000 68.70071  ? 87  GLU A CD   1 
ATOM   681  O  OE1  . GLU A  1 87  ? -23.98000 -18.69600 47.90900  1.000 67.43950  ? 87  GLU A OE1  1 
ATOM   682  O  OE2  . GLU A  1 87  ? -22.04400 -18.18700 48.81300  1.000 71.55103  ? 87  GLU A OE2  1 
ATOM   683  H  H    . GLU A  1 87  ? -20.70700 -20.19600 44.43600  1.000 36.94073  ? 87  GLU A H    1 
ATOM   684  H  HA   . GLU A  1 87  ? -22.69600 -21.79400 45.31200  1.000 40.05956  ? 87  GLU A HA   1 
ATOM   685  H  HB2  . GLU A  1 87  ? -22.72700 -18.98300 45.07400  1.000 48.21215  ? 87  GLU A HB2  1 
ATOM   686  H  HB3  . GLU A  1 87  ? -23.78000 -19.85500 45.88300  1.000 48.21215  ? 87  GLU A HB3  1 
ATOM   687  H  HG2  . GLU A  1 87  ? -21.83400 -20.47100 47.27000  1.000 69.75686  ? 87  GLU A HG2  1 
ATOM   688  H  HG3  . GLU A  1 87  ? -21.19000 -19.15000 46.66500  1.000 69.75686  ? 87  GLU A HG3  1 
ATOM   689  N  N    . GLY A  1 88  ? -24.26500 -21.84900 43.41700  1.000 26.47036  ? 88  GLY A N    1 
ATOM   690  C  CA   . GLY A  1 88  ? -25.16100 -21.87800 42.26300  1.000 26.57717  ? 88  GLY A CA   1 
ATOM   691  C  C    . GLY A  1 88  ? -24.57300 -22.55000 41.04400  1.000 22.15544  ? 88  GLY A C    1 
ATOM   692  O  O    . GLY A  1 88  ? -23.55900 -23.23300 41.06400  1.000 28.36879  ? 88  GLY A O    1 
ATOM   693  H  H    . GLY A  1 88  ? -24.46900 -22.41500 44.03100  1.000 31.76699  ? 88  GLY A H    1 
ATOM   694  H  HA2  . GLY A  1 88  ? -25.97000 -22.35400 42.50600  1.000 31.89516  ? 88  GLY A HA2  1 
ATOM   695  H  HA3  . GLY A  1 88  ? -25.39100 -20.96700 42.02000  1.000 31.89516  ? 88  GLY A HA3  1 
ATOM   696  N  N    . THR A  1 89  ? -25.25600 -22.32300 39.93200  1.000 22.18051  ? 89  THR A N    1 
ATOM   697  C  CA   . THR A  1 89  ? -24.89300 -22.99100 38.69500  1.000 19.71639  ? 89  THR A CA   1 
ATOM   698  C  C    . THR A  1 89  ? -23.98000 -22.12900 37.84200  1.000 20.22665  ? 89  THR A C    1 
ATOM   699  O  O    . THR A  1 89  ? -23.98100 -20.90100 37.92400  1.000 20.73496  ? 89  THR A O    1 
ATOM   700  C  CB   . THR A  1 89  ? -26.11700 -23.38700 37.88100  1.000 23.66215  ? 89  THR A CB   1 
ATOM   701  O  OG1  . THR A  1 89  ? -26.94600 -22.24700 37.66600  1.000 24.73265  ? 89  THR A OG1  1 
ATOM   702  C  CG2  . THR A  1 89  ? -26.96200 -24.45000 38.63100  1.000 23.24586  ? 89  THR A CG2  1 
ATOM   703  H  H    . THR A  1 89  ? -25.92800 -21.78900 39.87100  1.000 26.61918  ? 89  THR A H    1 
ATOM   704  H  HA   . THR A  1 89  ? -24.41200 -23.80000 38.93100  1.000 23.66223  ? 89  THR A HA   1 
ATOM   705  H  HB   . THR A  1 89  ? -25.81600 -23.75400 37.03400  1.000 28.39714  ? 89  THR A HB   1 
ATOM   706  H  HG1  . THR A  1 89  ? -26.51700 -21.65300 37.25600  1.000 29.68174  ? 89  THR A HG1  1 
ATOM   707  H  HG21 . THR A  1 89  ? -27.71300 -24.72400 38.08100  1.000 27.89759  ? 89  THR A HG21 1 
ATOM   708  H  HG22 . THR A  1 89  ? -26.41800 -25.22700 38.83000  1.000 27.89759  ? 89  THR A HG22 1 
ATOM   709  H  HG23 . THR A  1 89  ? -27.29900 -24.07900 39.46100  1.000 27.89759  ? 89  THR A HG23 1 
ATOM   710  N  N    . MET A  1 90  ? -23.19200 -22.81300 37.04000  1.000 17.20927  ? 90  MET A N    1 
ATOM   711  C  CA   . MET A  1 90  ? -22.16700 -22.21600 36.21200  1.000 17.03562  ? 90  MET A CA   1 
ATOM   712  C  C    . MET A  1 90  ? -22.31300 -22.70500 34.78400  1.000 16.54224  ? 90  MET A C    1 
ATOM   713  O  O    . MET A  1 90  ? -22.96800 -23.70900 34.50100  1.000 17.50112  ? 90  MET A O    1 
ATOM   714  C  CB   . MET A  1 90  ? -20.77100 -22.65900 36.68700  1.000 19.42580  ? 90  MET A CB   1 
ATOM   715  C  CG   . MET A  1 90  ? -20.35900 -21.98700 37.92300  1.000 20.59411  ? 90  MET A CG   1 
ATOM   716  S  SD   . MET A  1 90  ? -18.97600 -22.88100 38.71600  1.000 24.12211  ? 90  MET A SD   1 
ATOM   717  C  CE   . MET A  1 90  ? -19.93200 -24.09500 39.58000  1.000 23.54175  ? 90  MET A CE   1 
ATOM   718  H  H    . MET A  1 90  ? -23.23300 -23.66800 36.95400  1.000 20.65368  ? 90  MET A H    1 
ATOM   719  H  HA   . MET A  1 90  ? -22.26000 -21.25100 36.25200  1.000 20.44531  ? 90  MET A HA   1 
ATOM   720  H  HB2  . MET A  1 90  ? -20.78200 -23.61500 36.85200  1.000 23.31352  ? 90  MET A HB2  1 
ATOM   721  H  HB3  . MET A  1 90  ? -20.12100 -22.44900 35.99800  1.000 23.31352  ? 90  MET A HB3  1 
ATOM   722  H  HG2  . MET A  1 90  ? -20.06700 -21.08500 37.71900  1.000 24.71549  ? 90  MET A HG2  1 
ATOM   723  H  HG3  . MET A  1 90  ? -21.10500 -21.96200 38.54200  1.000 24.71549  ? 90  MET A HG3  1 
ATOM   724  H  HE1  . MET A  1 90  ? -19.34200 -24.61500 40.14900  1.000 28.25266  ? 90  MET A HE1  1 
ATOM   725  H  HE2  . MET A  1 90  ? -20.60000 -23.64400 40.12000  1.000 28.25266  ? 90  MET A HE2  1 
ATOM   726  H  HE3  . MET A  1 90  ? -20.36400 -24.67500 38.93400  1.000 28.25266  ? 90  MET A HE3  1 
ATOM   727  N  N    . ALA A  1 91  ? -21.65600 -22.00600 33.86200  1.000 15.82696  ? 91  ALA A N    1 
ATOM   728  C  CA   . ALA A  1 91  ? -21.57300 -22.51500 32.51100  1.000 15.75016  ? 91  ALA A CA   1 
ATOM   729  C  C    . ALA A  1 91  ? -20.64200 -23.71500 32.46300  1.000 14.51511  ? 91  ALA A C    1 
ATOM   730  O  O    . ALA A  1 91  ? -19.71200 -23.85400 33.27900  1.000 16.10483  ? 91  ALA A O    1 
ATOM   731  C  CB   . ALA A  1 91  ? -21.09300 -21.41600 31.57200  1.000 16.68115  ? 91  ALA A CB   1 
ATOM   732  H  H    . ALA A  1 91  ? -21.26100 -21.25300 33.99600  1.000 18.99492  ? 91  ALA A H    1 
ATOM   733  H  HA   . ALA A  1 91  ? -22.44600 -22.80400 32.20200  1.000 18.90275  ? 91  ALA A HA   1 
ATOM   734  H  HB1  . ALA A  1 91  ? -21.05100 -21.76900 30.66900  1.000 20.01995  ? 91  ALA A HB1  1 
ATOM   735  H  HB2  . ALA A  1 91  ? -21.71600 -20.67400 31.60900  1.000 20.01995  ? 91  ALA A HB2  1 
ATOM   736  H  HB3  . ALA A  1 91  ? -20.21200 -21.12300 31.85400  1.000 20.01995  ? 91  ALA A HB3  1 
ATOM   737  N  N    . ALA A  1 92  ? -20.87600 -24.57600 31.48600  1.000 13.72497  ? 92  ALA A N    1 
ATOM   738  C  CA   . ALA A  1 92  ? -20.08200 -25.76600 31.26500  1.000 14.87192  ? 92  ALA A CA   1 
ATOM   739  C  C    . ALA A  1 92  ? -19.40000 -25.68400 29.91700  1.000 13.66163  ? 92  ALA A C    1 
ATOM   740  O  O    . ALA A  1 92  ? -19.97400 -25.18200 28.94700  1.000 14.19400  ? 92  ALA A O    1 
ATOM   741  C  CB   . ALA A  1 92  ? -20.93000 -27.03000 31.33800  1.000 17.67501  ? 92  ALA A CB   1 
ATOM   742  H  H    . ALA A  1 92  ? -21.51500 -24.48700 30.91800  1.000 16.47252  ? 92  ALA A H    1 
ATOM   743  H  HA   . ALA A  1 92  ? -19.39900 -25.82200 31.95200  1.000 17.84886  ? 92  ALA A HA   1 
ATOM   744  H  HB1  . ALA A  1 92  ? -20.36500 -27.79900 31.16300  1.000 21.21257  ? 92  ALA A HB1  1 
ATOM   745  H  HB2  . ALA A  1 92  ? -21.31800 -27.09900 32.22400  1.000 21.21257  ? 92  ALA A HB2  1 
ATOM   746  H  HB3  . ALA A  1 92  ? -21.63300 -26.97700 30.67200  1.000 21.21257  ? 92  ALA A HB3  1 
ATOM   747  N  N    . ILE A  1 93  ? -18.17400 -26.16400 29.86600  1.000 13.75024  ? 93  ILE A N    1 
ATOM   748  C  CA   . ILE A  1 93  ? -17.29800 -26.09200 28.69200  1.000 13.92836  ? 93  ILE A CA   1 
ATOM   749  C  C    . ILE A  1 93  ? -16.65500 -27.44600 28.44400  1.000 12.73465  ? 93  ILE A C    1 
ATOM   750  O  O    . ILE A  1 93  ? -16.15300 -28.08000 29.37700  1.000 13.90239  ? 93  ILE A O    1 
ATOM   751  C  CB   . ILE A  1 93  ? -16.21900 -25.02200 28.89800  1.000 13.37310  ? 93  ILE A CB   1 
ATOM   752  C  CG1  . ILE A  1 93  ? -16.82800 -23.64700 29.16000  1.000 14.57642  ? 93  ILE A CG1  1 
ATOM   753  C  CG2  . ILE A  1 93  ? -15.28200 -24.98000 27.67900  1.000 14.13395  ? 93  ILE A CG2  1 
ATOM   754  C  CD1  . ILE A  1 93  ? -15.83200 -22.59100 29.63100  1.000 15.12026  ? 93  ILE A CD1  1 
ATOM   755  H  H    . ILE A  1 93  ? -17.79800 -26.55900 30.53000  1.000 16.50285  ? 93  ILE A H    1 
ATOM   756  H  HA   . ILE A  1 93  ? -17.83000 -25.88200 27.90900  1.000 16.71659  ? 93  ILE A HA   1 
ATOM   757  H  HB   . ILE A  1 93  ? -15.70700 -25.26400 29.68600  1.000 16.05028  ? 93  ILE A HB   1 
ATOM   758  H  HG12 . ILE A  1 93  ? -17.22900 -23.32500 28.33700  1.000 17.49426  ? 93  ILE A HG12 1 
ATOM   759  H  HG13 . ILE A  1 93  ? -17.50700 -23.73500 29.84700  1.000 17.49426  ? 93  ILE A HG13 1 
ATOM   760  H  HG21 . ILE A  1 93  ? -14.62800 -24.27600 27.80800  1.000 16.96330  ? 93  ILE A HG21 1 
ATOM   761  H  HG22 . ILE A  1 93  ? -14.83500 -25.83700 27.59500  1.000 16.96330  ? 93  ILE A HG22 1 
ATOM   762  H  HG23 . ILE A  1 93  ? -15.80800 -24.80200 26.88300  1.000 16.96330  ? 93  ILE A HG23 1 
ATOM   763  H  HD11 . ILE A  1 93  ? -16.32000 -21.83800 30.00000  1.000 18.14687  ? 93  ILE A HD11 1 
ATOM   764  H  HD12 . ILE A  1 93  ? -15.25900 -22.97900 30.31100  1.000 18.14687  ? 93  ILE A HD12 1 
ATOM   765  H  HD13 . ILE A  1 93  ? -15.29800 -22.30100 28.87500  1.000 18.14687  ? 93  ILE A HD13 1 
ATOM   766  N  N    . VAL A  1 94  ? -16.65200 -27.89100 27.19900  1.000 13.38161  ? 94  VAL A N    1 
ATOM   767  C  CA   . VAL A  1 94  ? -15.89800 -29.07800 26.77700  1.000 13.55953  ? 94  VAL A CA   1 
ATOM   768  C  C    . VAL A  1 94  ? -14.70200 -28.63100 25.95300  1.000 14.11956  ? 94  VAL A C    1 
ATOM   769  O  O    . VAL A  1 94  ? -14.84500 -27.77600 25.07800  1.000 13.45357  ? 94  VAL A O    1 
ATOM   770  C  CB   . VAL A  1 94  ? -16.80400 -30.04900 25.97400  1.000 14.25584  ? 94  VAL A CB   1 
ATOM   771  C  CG1  . VAL A  1 94  ? -16.01500 -31.07700 25.17200  1.000 14.52682  ? 94  VAL A CG1  1 
ATOM   772  C  CG2  . VAL A  1 94  ? -17.76900 -30.73100 26.94200  1.000 14.94801  ? 94  VAL A CG2  1 
ATOM   773  H  H    . VAL A  1 94  ? -17.08900 -27.51800 26.55900  1.000 16.06050  ? 94  VAL A H    1 
ATOM   774  H  HA   . VAL A  1 94  ? -15.56100 -29.54500 27.55700  1.000 16.27400  ? 94  VAL A HA   1 
ATOM   775  H  HB   . VAL A  1 94  ? -17.30000 -29.53500 25.31700  1.000 17.10957  ? 94  VAL A HB   1 
ATOM   776  H  HG11 . VAL A  1 94  ? -16.63000 -31.73200 24.80700  1.000 17.43474  ? 94  VAL A HG11 1 
ATOM   777  H  HG12 . VAL A  1 94  ? -15.54700 -30.62500 24.45300  1.000 17.43474  ? 94  VAL A HG12 1 
ATOM   778  H  HG13 . VAL A  1 94  ? -15.37700 -31.51300 25.75900  1.000 17.43474  ? 94  VAL A HG13 1 
ATOM   779  H  HG21 . VAL A  1 94  ? -18.33900 -31.33700 26.44400  1.000 17.94017  ? 94  VAL A HG21 1 
ATOM   780  H  HG22 . VAL A  1 94  ? -17.25700 -31.22400 27.60200  1.000 17.94017  ? 94  VAL A HG22 1 
ATOM   781  H  HG23 . VAL A  1 94  ? -18.30800 -30.05400 27.38000  1.000 17.94017  ? 94  VAL A HG23 1 
ATOM   782  N  N    . VAL A  1 95  ? -13.54500 -29.23900 26.20600  1.000 13.50587  ? 95  VAL A N    1 
ATOM   783  C  CA   . VAL A  1 95  ? -12.30200 -28.97300 25.49100  1.000 12.70487  ? 95  VAL A CA   1 
ATOM   784  C  C    . VAL A  1 95  ? -11.86700 -30.25200 24.80000  1.000 14.08433  ? 95  VAL A C    1 
ATOM   785  O  O    . VAL A  1 95  ? -11.77900 -31.30500 25.43500  1.000 14.22122  ? 95  VAL A O    1 
ATOM   786  C  CB   . VAL A  1 95  ? -11.19100 -28.47500 26.43300  1.000 12.97428  ? 95  VAL A CB   1 
ATOM   787  C  CG1  . VAL A  1 95  ? -10.00200 -27.98100 25.63900  1.000 13.98970  ? 95  VAL A CG1  1 
ATOM   788  C  CG2  . VAL A  1 95  ? -11.69900 -27.40400 27.37800  1.000 13.93738  ? 95  VAL A CG2  1 
ATOM   789  H  H    . VAL A  1 95  ? -13.45300 -29.83900 26.81600  1.000 16.20960  ? 95  VAL A H    1 
ATOM   790  H  HA   . VAL A  1 95  ? -12.46700 -28.29100 24.82100  1.000 15.24841  ? 95  VAL A HA   1 
ATOM   791  H  HB   . VAL A  1 95  ? -10.90000 -29.22300 26.97900  1.000 15.57170  ? 95  VAL A HB   1 
ATOM   792  H  HG11 . VAL A  1 95  ? -9.26900  -27.80000 26.24800  1.000 16.79020  ? 95  VAL A HG11 1 
ATOM   793  H  HG12 . VAL A  1 95  ? -9.74200  -28.66400 25.00100  1.000 16.79020  ? 95  VAL A HG12 1 
ATOM   794  H  HG13 . VAL A  1 95  ? -10.25100 -27.16800 25.17100  1.000 16.79020  ? 95  VAL A HG13 1 
ATOM   795  H  HG21 . VAL A  1 95  ? -10.95300 -27.05400 27.89000  1.000 16.72742  ? 95  VAL A HG21 1 
ATOM   796  H  HG22 . VAL A  1 95  ? -12.10700 -26.69300 26.85900  1.000 16.72742  ? 95  VAL A HG22 1 
ATOM   797  H  HG23 . VAL A  1 95  ? -12.35500 -27.79500 27.97600  1.000 16.72742  ? 95  VAL A HG23 1 
ATOM   798  N  N    . ILE A  1 96  ? -11.62500 -30.16900 23.49400  1.000 13.97475  ? 96  ILE A N    1 
ATOM   799  C  CA   . ILE A  1 96  ? -11.36300 -31.35100 22.67100  1.000 14.21106  ? 96  ILE A CA   1 
ATOM   800  C  C    . ILE A  1 96  ? -10.06900 -31.18100 21.88700  1.000 14.09081  ? 96  ILE A C    1 
ATOM   801  O  O    . ILE A  1 96  ? -9.82400  -30.09600 21.32800  1.000 14.81548  ? 96  ILE A O    1 
ATOM   802  C  CB   . ILE A  1 96  ? -12.56300 -31.63300 21.73800  1.000 14.07290  ? 96  ILE A CB   1 
ATOM   803  C  CG1  . ILE A  1 96  ? -12.36300 -32.93000 20.98300  1.000 14.90906  ? 96  ILE A CG1  1 
ATOM   804  C  CG2  . ILE A  1 96  ? -12.87700 -30.42900 20.84100  1.000 14.79781  ? 96  ILE A CG2  1 
ATOM   805  C  CD1  . ILE A  1 96  ? -13.55100 -33.27800 20.05500  1.000 17.93496  ? 96  ILE A CD1  1 
ATOM   806  H  H    . ILE A  1 96  ? -11.60700 -29.43000 23.05400  1.000 16.77226  ? 96  ILE A H    1 
ATOM   807  H  HA   . ILE A  1 96  ? -11.22900 -32.11300 23.25600  1.000 17.05583  ? 96  ILE A HA   1 
ATOM   808  H  HB   . ILE A  1 96  ? -13.35600 -31.75800 22.28300  1.000 16.89005  ? 96  ILE A HB   1 
ATOM   809  H  HG12 . ILE A  1 96  ? -11.56600 -32.85500 20.43500  1.000 17.89343  ? 96  ILE A HG12 1 
ATOM   810  H  HG13 . ILE A  1 96  ? -12.25900 -33.65300 21.62100  1.000 17.89343  ? 96  ILE A HG13 1 
ATOM   811  H  HG21 . ILE A  1 96  ? -13.72000 -30.58500 20.38700  1.000 17.75993  ? 96  ILE A HG21 1 
ATOM   812  H  HG22 . ILE A  1 96  ? -12.94100 -29.63300 21.39200  1.000 17.75993  ? 96  ILE A HG22 1 
ATOM   813  H  HG23 . ILE A  1 96  ? -12.16500 -30.32600 20.19100  1.000 17.75993  ? 96  ILE A HG23 1 
ATOM   814  H  HD11 . ILE A  1 96  ? -13.40900 -34.16100 19.67900  1.000 21.52451  ? 96  ILE A HD11 1 
ATOM   815  H  HD12 . ILE A  1 96  ? -14.37000 -33.26700 20.57400  1.000 21.52451  ? 96  ILE A HD12 1 
ATOM   816  H  HD13 . ILE A  1 96  ? -13.60000 -32.62000 19.34400  1.000 21.52451  ? 96  ILE A HD13 1 
ATOM   817  N  N    . PRO A  1 97  ? -9.24900  -32.23700 21.78800  1.000 14.84054  ? 97  PRO A N    1 
ATOM   818  C  CA   . PRO A  1 97  ? -7.98900  -32.15700 21.03900  1.000 15.60000  ? 97  PRO A CA   1 
ATOM   819  C  C    . PRO A  1 97  ? -8.18800  -32.44100 19.56700  1.000 16.75608  ? 97  PRO A C    1 
ATOM   820  O  O    . PRO A  1 97  ? -9.32600  -32.49500 19.08200  1.000 16.23421  ? 97  PRO A O    1 
ATOM   821  C  CB   . PRO A  1 97  ? -7.15400  -33.24900 21.70600  1.000 17.28759  ? 97  PRO A CB   1 
ATOM   822  C  CG   . PRO A  1 97  ? -8.12700  -34.27400 22.10600  1.000 16.84419  ? 97  PRO A CG   1 
ATOM   823  C  CD   . PRO A  1 97  ? -9.35900  -33.50300 22.54700  1.000 15.62063  ? 97  PRO A CD   1 
ATOM   824  H  HA   . PRO A  1 97  ? -7.56300  -31.29300 21.15000  1.000 18.72257  ? 97  PRO A HA   1 
ATOM   825  H  HB2  . PRO A  1 97  ? -6.51100  -33.60700 21.07400  1.000 20.74767  ? 97  PRO A HB2  1 
ATOM   826  H  HB3  . PRO A  1 97  ? -6.69200  -32.88800 22.47900  1.000 20.74767  ? 97  PRO A HB3  1 
ATOM   827  H  HG2  . PRO A  1 97  ? -8.33000  -34.84800 21.35100  1.000 20.21560  ? 97  PRO A HG2  1 
ATOM   828  H  HG3  . PRO A  1 97  ? -7.76900  -34.80200 22.83700  1.000 20.21560  ? 97  PRO A HG3  1 
ATOM   829  H  HD2  . PRO A  1 97  ? -10.16900 -33.98000 22.31000  1.000 18.74732  ? 97  PRO A HD2  1 
ATOM   830  H  HD3  . PRO A  1 97  ? -9.33900  -33.33700 23.50300  1.000 18.74732  ? 97  PRO A HD3  1 
ATOM   831  N  N    . GLY A  1 98  ? -7.10300  -32.59600 18.82300  1.000 17.28758  ? 98  GLY A N    1 
ATOM   832  C  CA   . GLY A  1 98  ? -7.14700  -32.81800 17.39800  1.000 20.14895  ? 98  GLY A CA   1 
ATOM   833  C  C    . GLY A  1 98  ? -6.72700  -34.21500 16.98100  1.000 18.56367  ? 98  GLY A C    1 
ATOM   834  O  O    . GLY A  1 98  ? -6.61700  -35.14100 17.78700  1.000 17.34806  ? 98  GLY A O    1 
ATOM   835  H  H    . GLY A  1 98  ? -6.30400  -32.57400 19.13800  1.000 20.74766  ? 98  GLY A H    1 
ATOM   836  H  HA2  . GLY A  1 98  ? -8.05200  -32.67100 17.08300  1.000 24.18130  ? 98  GLY A HA2  1 
ATOM   837  H  HA3  . GLY A  1 98  ? -6.55400  -32.18500 16.96200  1.000 24.18130  ? 98  GLY A HA3  1 
ATOM   838  N  N    . TYR A  1 99  ? -6.52200  -34.36000 15.66200  1.000 19.88732  ? 99  TYR A N    1 
ATOM   839  C  CA   . TYR A  1 99  ? -6.18600  -35.63700 15.05600  1.000 20.66404  ? 99  TYR A CA   1 
ATOM   840  C  C    . TYR A  1 99  ? -4.94700  -36.23500 15.69400  1.000 19.53207  ? 99  TYR A C    1 
ATOM   841  O  O    . TYR A  1 99  ? -3.93800  -35.54600 15.90700  1.000 21.43775  ? 99  TYR A O    1 
ATOM   842  C  CB   . TYR A  1 99  ? -5.93700  -35.39300 13.55200  1.000 22.82481  ? 99  TYR A CB   1 
ATOM   843  C  CG   . TYR A  1 99  ? -5.74600  -36.57500 12.63700  1.000 24.79472  ? 99  TYR A CG   1 
ATOM   844  C  CD1  . TYR A  1 99  ? -6.74700  -37.51200 12.45200  1.000 25.77326  ? 99  TYR A CD1  1 
ATOM   845  C  CD2  . TYR A  1 99  ? -4.59000  -36.70900 11.91200  1.000 30.35894  ? 99  TYR A CD2  1 
ATOM   846  C  CE1  . TYR A  1 99  ? -6.57500  -38.57400 11.58700  1.000 26.23313  ? 99  TYR A CE1  1 
ATOM   847  C  CE2  . TYR A  1 99  ? -4.41600  -37.76300 11.05000  1.000 33.70689  ? 99  TYR A CE2  1 
ATOM   848  C  CZ   . TYR A  1 99  ? -5.40900  -38.68700 10.90600  1.000 35.28496  ? 99  TYR A CZ   1 
ATOM   849  O  OH   . TYR A  1 99  ? -5.23400  -39.74500 10.03100  1.000 36.80270  ? 99  TYR A OH   1 
ATOM   850  H  H    . TYR A  1 99  ? -6.57400  -33.71700 15.09300  1.000 23.86734  ? 99  TYR A H    1 
ATOM   851  H  HA   . TYR A  1 99  ? -6.91100  -36.27100 15.17900  1.000 24.79941  ? 99  TYR A HA   1 
ATOM   852  H  HB2  . TYR A  1 99  ? -6.70000  -34.90200 13.20700  1.000 27.39233  ? 99  TYR A HB2  1 
ATOM   853  H  HB3  . TYR A  1 99  ? -5.13400  -34.85500 13.47400  1.000 27.39233  ? 99  TYR A HB3  1 
ATOM   854  H  HD1  . TYR A  1 99  ? -7.54700  -37.42500 12.91700  1.000 30.93047  ? 99  TYR A HD1  1 
ATOM   855  H  HD2  . TYR A  1 99  ? -3.91400  -36.07700 12.00500  1.000 36.43329  ? 99  TYR A HD2  1 
ATOM   856  H  HE1  . TYR A  1 99  ? -7.25000  -39.20400 11.47400  1.000 31.48231  ? 99  TYR A HE1  1 
ATOM   857  H  HE2  . TYR A  1 99  ? -3.62600  -37.84700 10.56800  1.000 40.45083  ? 99  TYR A HE2  1 
ATOM   858  H  HH   . TYR A  1 99  ? -4.47200  -39.70500 9.68100   1.000 44.16580  ? 99  TYR A HH   1 
ATOM   859  N  N    . MET A  1 100 ? -5.03100  -37.52500 16.00600  1.000 20.24951  ? 100 MET A N    1 
ATOM   860  C  CA   . MET A  1 100 ? -3.94100  -38.30600 16.55100  1.000 21.69917  ? 100 MET A CA   1 
ATOM   861  C  C    . MET A  1 100 ? -3.47300  -37.80700 17.90300  1.000 22.11402  ? 100 MET A C    1 
ATOM   862  O  O    . MET A  1 100 ? -2.32500  -38.06400 18.28400  1.000 24.88881  ? 100 MET A O    1 
ATOM   863  C  CB   . MET A  1 100 ? -2.77700  -38.39600 15.55700  1.000 24.58241  ? 100 MET A CB   1 
ATOM   864  C  CG   . MET A  1 100 ? -3.17800  -38.93100 14.19500  1.000 26.94625  ? 100 MET A CG   1 
ATOM   865  S  SD   . MET A  1 100 ? -3.91800  -40.57500 14.27000  1.000 36.83477  ? 100 MET A SD   1 
ATOM   866  C  CE   . MET A  1 100 ? -2.66200  -41.50800 15.07000  1.000 39.40601  ? 100 MET A CE   1 
ATOM   867  H  H    . MET A  1 100 ? -5.74900  -37.98700 15.90300  1.000 24.30198  ? 100 MET A H    1 
ATOM   868  H  HA   . MET A  1 100 ? -4.26700  -39.20800 16.69300  1.000 26.04156  ? 100 MET A HA   1 
ATOM   869  H  HB2  . MET A  1 100 ? -2.40700  -37.50800 15.42900  1.000 29.50146  ? 100 MET A HB2  1 
ATOM   870  H  HB3  . MET A  1 100 ? -2.10100  -38.98800 15.92000  1.000 29.50146  ? 100 MET A HB3  1 
ATOM   871  H  HG2  . MET A  1 100 ? -3.82800  -38.32900 13.79900  1.000 32.33806  ? 100 MET A HG2  1 
ATOM   872  H  HG3  . MET A  1 100 ? -2.38900  -38.98400 13.63300  1.000 32.33806  ? 100 MET A HG3  1 
ATOM   873  H  HE1  . MET A  1 100 ? -2.90700  -42.44600 15.05500  1.000 47.28977  ? 100 MET A HE1  1 
ATOM   874  H  HE2  . MET A  1 100 ? -1.82300  -41.37700 14.60000  1.000 47.28977  ? 100 MET A HE2  1 
ATOM   875  H  HE3  . MET A  1 100 ? -2.57700  -41.20300 15.98700  1.000 47.28977  ? 100 MET A HE3  1 
ATOM   876  N  N    . SER A  1 101 ? -4.33900  -37.12000 18.64900  1.000 18.39927  ? 101 SER A N    1 
ATOM   877  C  CA   . SER A  1 101 ? -3.96900  -36.56100 19.93100  1.000 18.78258  ? 101 SER A CA   1 
ATOM   878  C  C    . SER A  1 101 ? -4.94500  -36.95600 21.01300  1.000 19.87620  ? 101 SER A C    1 
ATOM   879  O  O    . SER A  1 101 ? -6.12200  -37.24900 20.77300  1.000 20.63914  ? 101 SER A O    1 
ATOM   880  C  CB   . SER A  1 101 ? -3.88800  -35.03400 19.86600  1.000 21.20483  ? 101 SER A CB   1 
ATOM   881  O  OG   . SER A  1 101 ? -2.87900  -34.67900 18.93800  1.000 23.03017  ? 101 SER A OG   1 
ATOM   882  H  H    . SER A  1 101 ? -5.15500  -36.96700 18.42300  1.000 22.08168  ? 101 SER A H    1 
ATOM   883  H  HA   . SER A  1 101 ? -3.10400  -36.92600 20.17600  1.000 22.54166  ? 101 SER A HA   1 
ATOM   884  H  HB2  . SER A  1 101 ? -4.74100  -34.67500 19.57300  1.000 25.44836  ? 101 SER A HB2  1 
ATOM   885  H  HB3  . SER A  1 101 ? -3.66400  -34.68200 20.74200  1.000 25.44836  ? 101 SER A HB3  1 
ATOM   886  H  HG   . SER A  1 101 ? -2.92600  -33.85900 18.76100  1.000 27.63877  ? 101 SER A HG   1 
ATOM   887  N  N    . TYR A  1 102 ? -4.44400  -36.90400 22.23600  1.000 18.90697  ? 102 TYR A N    1 
ATOM   888  C  CA   . TYR A  1 102 ? -5.20700  -37.19900 23.42600  1.000 21.32576  ? 102 TYR A CA   1 
ATOM   889  C  C    . TYR A  1 102 ? -5.48900  -35.94600 24.23800  1.000 19.08723  ? 102 TYR A C    1 
ATOM   890  O  O    . TYR A  1 102 ? -4.97300  -34.85400 23.99000  1.000 18.53967  ? 102 TYR A O    1 
ATOM   891  C  CB   . TYR A  1 102 ? -4.42800  -38.21800 24.28300  1.000 20.65696  ? 102 TYR A CB   1 
ATOM   892  C  CG   . TYR A  1 102 ? -4.26800  -39.54300 23.60900  1.000 21.80518  ? 102 TYR A CG   1 
ATOM   893  C  CD1  . TYR A  1 102 ? -5.27200  -40.49200 23.69900  1.000 23.18488  ? 102 TYR A CD1  1 
ATOM   894  C  CD2  . TYR A  1 102 ? -3.14600  -39.85900 22.87100  1.000 23.07012  ? 102 TYR A CD2  1 
ATOM   895  C  CE1  . TYR A  1 102 ? -5.14500  -41.71600 23.08200  1.000 24.26690  ? 102 TYR A CE1  1 
ATOM   896  C  CE2  . TYR A  1 102 ? -3.01200  -41.09500 22.25700  1.000 25.54146  ? 102 TYR A CE2  1 
ATOM   897  C  CZ   . TYR A  1 102 ? -4.02800  -42.02000 22.36600  1.000 22.43863  ? 102 TYR A CZ   1 
ATOM   898  O  OH   . TYR A  1 102 ? -3.90900  -43.24100 21.74500  1.000 27.72740  ? 102 TYR A OH   1 
ATOM   899  H  H    . TYR A  1 102 ? -3.62800  -36.69000 22.40500  1.000 22.69093  ? 102 TYR A H    1 
ATOM   900  H  HA   . TYR A  1 102 ? -6.06800  -37.56500 23.16800  1.000 25.59347  ? 102 TYR A HA   1 
ATOM   901  H  HB2  . TYR A  1 102 ? -3.54300  -37.86500 24.46400  1.000 24.79091  ? 102 TYR A HB2  1 
ATOM   902  H  HB3  . TYR A  1 102 ? -4.90600  -38.36000 25.11500  1.000 24.79091  ? 102 TYR A HB3  1 
ATOM   903  H  HD1  . TYR A  1 102 ? -6.04300  -40.29900 24.18200  1.000 27.82442  ? 102 TYR A HD1  1 
ATOM   904  H  HD2  . TYR A  1 102 ? -2.46600  -39.23000 22.78300  1.000 27.68671  ? 102 TYR A HD2  1 
ATOM   905  H  HE1  . TYR A  1 102 ? -5.82800  -42.34200 23.15600  1.000 29.12284  ? 102 TYR A HE1  1 
ATOM   906  H  HE2  . TYR A  1 102 ? -2.24200  -41.29900 21.77700  1.000 30.65232  ? 102 TYR A HE2  1 
ATOM   907  H  HH   . TYR A  1 102 ? -3.16800  -43.29300 21.35400  1.000 33.27544  ? 102 TYR A HH   1 
ATOM   908  N  N    . GLN A  1 103 ? -6.34400  -36.13900 25.24000  1.000 19.32905  ? 103 GLN A N    1 
ATOM   909  C  CA   . GLN A  1 103 ? -6.76900  -35.07900 26.12200  1.000 21.15692  ? 103 GLN A CA   1 
ATOM   910  C  C    . GLN A  1 103 ? -5.61900  -34.28800 26.69700  1.000 17.63291  ? 103 GLN A C    1 
ATOM   911  O  O    . GLN A  1 103 ? -5.71200  -33.06900 26.86000  1.000 19.59670  ? 103 GLN A O    1 
ATOM   912  C  CB   . GLN A  1 103 ? -7.48500  -35.84700 27.23000  1.000 31.15788  ? 103 GLN A CB   1 
ATOM   913  C  CG   . GLN A  1 103 ? -8.35700  -35.15500 28.06800  1.000 31.33556  ? 103 GLN A CG   1 
ATOM   914  C  CD   . GLN A  1 103 ? -8.77600  -36.04900 29.25600  1.000 21.84777  ? 103 GLN A CD   1 
ATOM   915  O  OE1  . GLN A  1 103 ? -8.97200  -35.54100 30.27900  1.000 20.86966  ? 103 GLN A OE1  1 
ATOM   916  N  NE2  . GLN A  1 103 ? -8.93100  -37.35100 29.06600  1.000 24.72707  ? 103 GLN A NE2  1 
ATOM   917  H  H    . GLN A  1 103 ? -6.69800  -36.89900 25.42900  1.000 23.19743  ? 103 GLN A H    1 
ATOM   918  H  HA   . GLN A  1 103 ? -7.32300  -34.42000 25.67400  1.000 25.39086  ? 103 GLN A HA   1 
ATOM   919  H  HB2  . GLN A  1 103 ? -8.00700  -36.54900 26.80900  1.000 37.39202  ? 103 GLN A HB2  1 
ATOM   920  H  HB3  . GLN A  1 103 ? -6.80500  -36.23700 27.80100  1.000 37.39202  ? 103 GLN A HB3  1 
ATOM   921  H  HG2  . GLN A  1 103 ? -7.91500  -34.36400 28.41500  1.000 37.60524  ? 103 GLN A HG2  1 
ATOM   922  H  HG3  . GLN A  1 103 ? -9.15200  -34.90100 27.57300  1.000 37.60524  ? 103 GLN A HG3  1 
ATOM   923  H  HE21 . GLN A  1 103 ? -8.79900  -37.69100 28.28700  1.000 29.67505  ? 103 GLN A HE21 1 
ATOM   924  H  HE22 . GLN A  1 103 ? -9.16500  -37.85600 29.72200  1.000 29.67505  ? 103 GLN A HE22 1 
ATOM   925  N  N    . SER A  1 104 ? -4.50600  -34.94300 27.00600  1.000 17.92524  ? 104 SER A N    1 
ATOM   926  C  CA   . SER A  1 104 ? -3.39300  -34.24100 27.64300  1.000 18.11290  ? 104 SER A CA   1 
ATOM   927  C  C    . SER A  1 104 ? -2.87100  -33.10000 26.79100  1.000 19.19020  ? 104 SER A C    1 
ATOM   928  O  O    . SER A  1 104 ? -2.35500  -32.12300 27.33400  1.000 20.00563  ? 104 SER A O    1 
ATOM   929  C  CB   . SER A  1 104 ? -2.28300  -35.22400 27.97400  1.000 20.23510  ? 104 SER A CB   1 
ATOM   930  O  OG   . SER A  1 104 ? -1.83800  -35.88300 26.80800  1.000 23.88890  ? 104 SER A OG   1 
ATOM   931  H  H    . SER A  1 104 ? -4.36800  -35.78000 26.86100  1.000 21.51285  ? 104 SER A H    1 
ATOM   932  H  HA   . SER A  1 104 ? -3.70700  -33.85400 28.47600  1.000 21.73804  ? 104 SER A HA   1 
ATOM   933  H  HB2  . SER A  1 104 ? -1.54000  -34.74100 28.36800  1.000 24.28468  ? 104 SER A HB2  1 
ATOM   934  H  HB3  . SER A  1 104 ? -2.62100  -35.88300 28.60000  1.000 24.28468  ? 104 SER A HB3  1 
ATOM   935  H  HG   . SER A  1 104 ? -1.12400  -36.29700 26.96700  1.000 28.66924  ? 104 SER A HG   1 
ATOM   936  N  N    . SER A  1 105 ? -3.06700  -33.15600 25.47100  1.000 16.71596  ? 105 SER A N    1 
ATOM   937  C  CA   . SER A  1 105 ? -2.57400  -32.09300 24.60200  1.000 17.81053  ? 105 SER A CA   1 
ATOM   938  C  C    . SER A  1 105 ? -3.23500  -30.74500 24.84000  1.000 16.32202  ? 105 SER A C    1 
ATOM   939  O  O    . SER A  1 105 ? -2.65700  -29.73200 24.43700  1.000 18.40228  ? 105 SER A O    1 
ATOM   940  C  CB   . SER A  1 105 ? -2.73500  -32.45200 23.12400  1.000 17.74329  ? 105 SER A CB   1 
ATOM   941  O  OG   . SER A  1 105 ? -4.08200  -32.61700 22.74700  1.000 18.49376  ? 105 SER A OG   1 
ATOM   942  H  H    . SER A  1 105 ? -3.47700  -33.79100 25.06100  1.000 20.06172  ? 105 SER A H    1 
ATOM   943  H  HA   . SER A  1 105 ? -1.62800  -32.00800 24.79700  1.000 21.37520  ? 105 SER A HA   1 
ATOM   944  H  HB2  . SER A  1 105 ? -2.35100  -31.73800 22.59000  1.000 21.29451  ? 105 SER A HB2  1 
ATOM   945  H  HB3  . SER A  1 105 ? -2.26400  -33.28300 22.95600  1.000 21.29451  ? 105 SER A HB3  1 
ATOM   946  H  HG   . SER A  1 105 ? -4.43500  -33.22900 23.20200  1.000 22.19508  ? 105 SER A HG   1 
ATOM   947  N  N    . ILE A  1 106 ? -4.44100  -30.70200 25.41400  1.000 14.42395  ? 106 ILE A N    1 
ATOM   948  C  CA   . ILE A  1 106 ? -5.16500  -29.46200 25.64800  1.000 14.47396  ? 106 ILE A CA   1 
ATOM   949  C  C    . ILE A  1 106 ? -5.50700  -29.27400 27.12300  1.000 15.04755  ? 106 ILE A C    1 
ATOM   950  O  O    . ILE A  1 106 ? -6.32400  -28.42100 27.45700  1.000 15.80006  ? 106 ILE A O    1 
ATOM   951  C  CB   . ILE A  1 106 ? -6.40800  -29.32300 24.74900  1.000 15.89760  ? 106 ILE A CB   1 
ATOM   952  C  CG1  . ILE A  1 106 ? -7.28900  -30.57600 24.73600  1.000 15.54467  ? 106 ILE A CG1  1 
ATOM   953  C  CG2  . ILE A  1 106 ? -5.95400  -29.05000 23.28700  1.000 17.56708  ? 106 ILE A CG2  1 
ATOM   954  C  CD1  . ILE A  1 106 ? -8.00100  -30.95500 26.02800  1.000 16.70359  ? 106 ILE A CD1  1 
ATOM   955  H  H    . ILE A  1 106 ? -4.86700  -31.40000 25.68100  1.000 17.31130  ? 106 ILE A H    1 
ATOM   956  H  HA   . ILE A  1 106 ? -4.56600  -28.74100 25.39800  1.000 17.37132  ? 106 ILE A HA   1 
ATOM   957  H  HB   . ILE A  1 106 ? -6.92900  -28.59100 25.11600  1.000 19.07968  ? 106 ILE A HB   1 
ATOM   958  H  HG12 . ILE A  1 106 ? -7.97800  -30.44600 24.06600  1.000 18.65617  ? 106 ILE A HG12 1 
ATOM   959  H  HG13 . ILE A  1 106 ? -6.72900  -31.33000 24.49500  1.000 18.65617  ? 106 ILE A HG13 1 
ATOM   960  H  HG21 . ILE A  1 106 ? -6.73800  -28.98700 22.71900  1.000 21.08306  ? 106 ILE A HG21 1 
ATOM   961  H  HG22 . ILE A  1 106 ? -5.45800  -28.21700 23.26000  1.000 21.08306  ? 106 ILE A HG22 1 
ATOM   962  H  HG23 . ILE A  1 106 ? -5.39000  -29.78100 22.99000  1.000 21.08306  ? 106 ILE A HG23 1 
ATOM   963  H  HD11 . ILE A  1 106 ? -8.66400  -31.63600 25.83500  1.000 20.04687  ? 106 ILE A HD11 1 
ATOM   964  H  HD12 . ILE A  1 106 ? -7.34900  -31.29700 26.65900  1.000 20.04687  ? 106 ILE A HD12 1 
ATOM   965  H  HD13 . ILE A  1 106 ? -8.43400  -30.16700 26.39300  1.000 20.04687  ? 106 ILE A HD13 1 
ATOM   966  N  N    . SER A  1 107 ? -4.78800  -29.98200 28.00400  1.000 14.89413  ? 107 SER A N    1 
ATOM   967  C  CA   . SER A  1 107 ? -5.12300  -29.98800 29.42200  1.000 15.15027  ? 107 SER A CA   1 
ATOM   968  C  C    . SER A  1 107 ? -5.01000  -28.62100 30.08500  1.000 15.11645  ? 107 SER A C    1 
ATOM   969  O  O    . SER A  1 107 ? -5.70900  -28.39100 31.07800  1.000 16.18315  ? 107 SER A O    1 
ATOM   970  C  CB   . SER A  1 107 ? -4.24400  -31.00000 30.17200  1.000 17.19794  ? 107 SER A CB   1 
ATOM   971  O  OG   . SER A  1 107 ? -2.86700  -30.67300 30.08800  1.000 20.06756  ? 107 SER A OG   1 
ATOM   972  H  H    . SER A  1 107 ? -4.10500  -30.46400 27.80200  1.000 17.87552  ? 107 SER A H    1 
ATOM   973  H  HA   . SER A  1 107 ? -6.05200  -30.26000 29.49100  1.000 18.18289  ? 107 SER A HA   1 
ATOM   974  H  HB2  . SER A  1 107 ? -4.50500  -31.00800 31.10600  1.000 20.64009  ? 107 SER A HB2  1 
ATOM   975  H  HB3  . SER A  1 107 ? -4.37900  -31.87800 29.78200  1.000 20.64009  ? 107 SER A HB3  1 
ATOM   976  H  HG   . SER A  1 107 ? -2.60000  -30.75700 29.29600  1.000 24.08364  ? 107 SER A HG   1 
ATOM   977  N  N    . PHE A  1 108 ? -4.14200  -27.72600 29.58300  1.000 13.87387  ? 108 PHE A N    1 
ATOM   978  C  CA   . PHE A  1 108 ? -4.05200  -26.37600 30.14700  1.000 13.84815  ? 108 PHE A CA   1 
ATOM   979  C  C    . PHE A  1 108 ? -5.42900  -25.75800 30.36000  1.000 12.89934  ? 108 PHE A C    1 
ATOM   980  O  O    . PHE A  1 108 ? -5.68200  -25.05500 31.33800  1.000 14.39946  ? 108 PHE A O    1 
ATOM   981  C  CB   . PHE A  1 108 ? -3.28600  -25.51000 29.14700  1.000 14.26154  ? 108 PHE A CB   1 
ATOM   982  C  CG   . PHE A  1 108 ? -3.45900  -24.01100 29.27600  1.000 13.77608  ? 108 PHE A CG   1 
ATOM   983  C  CD1  . PHE A  1 108 ? -2.65700  -23.29800 30.16900  1.000 14.20256  ? 108 PHE A CD1  1 
ATOM   984  C  CD2  . PHE A  1 108 ? -4.31700  -23.31400 28.47600  1.000 13.27511  ? 108 PHE A CD2  1 
ATOM   985  C  CE1  . PHE A  1 108 ? -2.77500  -21.91300 30.25800  1.000 14.09969  ? 108 PHE A CE1  1 
ATOM   986  C  CE2  . PHE A  1 108 ? -4.42900  -21.92900 28.55300  1.000 13.84400  ? 108 PHE A CE2  1 
ATOM   987  C  CZ   . PHE A  1 108 ? -3.62200  -21.23700 29.44300  1.000 14.51445  ? 108 PHE A CZ   1 
ATOM   988  H  H    . PHE A  1 108 ? -3.60500  -27.87600 28.92800  1.000 16.65121  ? 108 PHE A H    1 
ATOM   989  H  HA   . PHE A  1 108 ? -3.59900  -26.41300 31.00400  1.000 16.62034  ? 108 PHE A HA   1 
ATOM   990  H  HB2  . PHE A  1 108 ? -2.33900  -25.69600 29.25000  1.000 17.11641  ? 108 PHE A HB2  1 
ATOM   991  H  HB3  . PHE A  1 108 ? -3.57600  -25.75300 28.25400  1.000 17.11641  ? 108 PHE A HB3  1 
ATOM   992  H  HD1  . PHE A  1 108 ? -2.04500  -23.74800 30.70500  1.000 17.04563  ? 108 PHE A HD1  1 
ATOM   993  H  HD2  . PHE A  1 108 ? -4.84200  -23.77700 27.86400  1.000 15.93269  ? 108 PHE A HD2  1 
ATOM   994  H  HE1  . PHE A  1 108 ? -2.26800  -21.44700 30.88300  1.000 16.92219  ? 108 PHE A HE1  1 
ATOM   995  H  HE2  . PHE A  1 108 ? -5.03600  -21.47500 28.01500  1.000 16.61536  ? 108 PHE A HE2  1 
ATOM   996  H  HZ   . PHE A  1 108 ? -3.66200  -20.30800 29.48000  1.000 17.41990  ? 108 PHE A HZ   1 
ATOM   997  N  N    . TRP A  1 109 ? -6.33200  -25.94600 29.39200  1.000 13.51338  ? 109 TRP A N    1 
ATOM   998  C  CA   . TRP A  1 109 ? -7.61800  -25.26700 29.39300  1.000 12.45864  ? 109 TRP A CA   1 
ATOM   999  C  C    . TRP A  1 109 ? -8.54900  -25.72300 30.51100  1.000 12.98710  ? 109 TRP A C    1 
ATOM   1000 O  O    . TRP A  1 109 ? -9.45700  -24.97000 30.86900  1.000 15.67708  ? 109 TRP A O    1 
ATOM   1001 C  CB   . TRP A  1 109 ? -8.26200  -25.41500 28.01200  1.000 13.22764  ? 109 TRP A CB   1 
ATOM   1002 C  CG   . TRP A  1 109 ? -7.54300  -24.60500 26.96500  1.000 13.20944  ? 109 TRP A CG   1 
ATOM   1003 C  CD1  . TRP A  1 109 ? -6.62400  -25.03800 26.03200  1.000 13.80747  ? 109 TRP A CD1  1 
ATOM   1004 C  CD2  . TRP A  1 109 ? -7.62900  -23.18600 26.80700  1.000 13.53200  ? 109 TRP A CD2  1 
ATOM   1005 N  NE1  . TRP A  1 109 ? -6.16800  -23.95700 25.29900  1.000 14.33466  ? 109 TRP A NE1  1 
ATOM   1006 C  CE2  . TRP A  1 109 ? -6.75900  -22.81900 25.76700  1.000 13.49441  ? 109 TRP A CE2  1 
ATOM   1007 C  CE3  . TRP A  1 109 ? -8.32800  -22.17900 27.48500  1.000 14.72958  ? 109 TRP A CE3  1 
ATOM   1008 C  CZ2  . TRP A  1 109 ? -6.62000  -21.50100 25.33900  1.000 14.13156  ? 109 TRP A CZ2  1 
ATOM   1009 C  CZ3  . TRP A  1 109 ? -8.16300  -20.87400 27.07600  1.000 15.72902  ? 109 TRP A CZ3  1 
ATOM   1010 C  CH2  . TRP A  1 109 ? -7.31100  -20.55000 26.02000  1.000 15.73041  ? 109 TRP A CH2  1 
ATOM   1011 H  H    . TRP A  1 109 ? -6.21700  -26.46800 28.71800  1.000 16.21862  ? 109 TRP A H    1 
ATOM   1012 H  HA   . TRP A  1 109 ? -7.47900  -24.32100 29.55400  1.000 14.95293  ? 109 TRP A HA   1 
ATOM   1013 H  HB2  . TRP A  1 109 ? -8.23600  -26.34700 27.74600  1.000 15.87573  ? 109 TRP A HB2  1 
ATOM   1014 H  HB3  . TRP A  1 109 ? -9.18100  -25.10800 28.05500  1.000 15.87573  ? 109 TRP A HB3  1 
ATOM   1015 H  HD1  . TRP A  1 109 ? -6.35400  -25.92000 25.91400  1.000 16.57153  ? 109 TRP A HD1  1 
ATOM   1016 H  HE1  . TRP A  1 109 ? -5.60200  -23.99600 24.65300  1.000 17.20415  ? 109 TRP A HE1  1 
ATOM   1017 H  HE3  . TRP A  1 109 ? -8.89100  -22.38700 28.19500  1.000 17.67806  ? 109 TRP A HE3  1 
ATOM   1018 H  HZ2  . TRP A  1 109 ? -6.07700  -21.28000 24.61700  1.000 16.96043  ? 109 TRP A HZ2  1 
ATOM   1019 H  HZ3  . TRP A  1 109 ? -8.62800  -20.19600 27.51300  1.000 18.87738  ? 109 TRP A HZ3  1 
ATOM   1020 H  HH2  . TRP A  1 109 ? -7.21400  -19.65800 25.77500  1.000 18.87905  ? 109 TRP A HH2  1 
ATOM   1021 N  N    . GLY A  1 110 ? -8.31500  -26.91400 31.07400  1.000 14.01196  ? 110 GLY A N    1 
ATOM   1022 C  CA   . GLY A  1 110 ? -9.13300  -27.41600 32.15400  1.000 13.91651  ? 110 GLY A CA   1 
ATOM   1023 C  C    . GLY A  1 110 ? -9.01000  -26.58600 33.40200  1.000 13.84130  ? 110 GLY A C    1 
ATOM   1024 O  O    . GLY A  1 110 ? -9.95800  -25.90300 33.82500  1.000 15.58545  ? 110 GLY A O    1 
ATOM   1025 H  H    . GLY A  1 110 ? -7.68100  -27.44600 30.83800  1.000 16.81691  ? 110 GLY A H    1 
ATOM   1026 H  HA2  . GLY A  1 110 ? -10.06300 -27.41600 31.87800  1.000 16.70238  ? 110 GLY A HA2  1 
ATOM   1027 H  HA3  . GLY A  1 110 ? -8.86500  -28.32400 32.36400  1.000 16.70238  ? 110 GLY A HA3  1 
ATOM   1028 N  N    . PRO A  1 111 ? -7.81600  -26.55200 34.00300  1.000 13.42188  ? 111 PRO A N    1 
ATOM   1029 C  CA   . PRO A  1 111 ? -7.66000  -25.71700 35.21100  1.000 14.29074  ? 111 PRO A CA   1 
ATOM   1030 C  C    . PRO A  1 111 ? -7.80600  -24.23800 34.94100  1.000 14.00154  ? 111 PRO A C    1 
ATOM   1031 O  O    . PRO A  1 111 ? -8.31400  -23.49400 35.78500  1.000 14.23219  ? 111 PRO A O    1 
ATOM   1032 C  CB   . PRO A  1 111 ? -6.24300  -26.05700 35.70600  1.000 15.55016  ? 111 PRO A CB   1 
ATOM   1033 C  CG   . PRO A  1 111 ? -5.96700  -27.47900 35.17100  1.000 16.52357  ? 111 PRO A CG   1 
ATOM   1034 C  CD   . PRO A  1 111 ? -6.64200  -27.44100 33.82200  1.000 14.38609  ? 111 PRO A CD   1 
ATOM   1035 H  HA   . PRO A  1 111 ? -8.31000  -25.99300 35.87600  1.000 17.15145  ? 111 PRO A HA   1 
ATOM   1036 H  HB2  . PRO A  1 111 ? -5.60600  -25.42000 35.34600  1.000 18.66275  ? 111 PRO A HB2  1 
ATOM   1037 H  HB3  . PRO A  1 111 ? -6.21800  -26.03900 36.67500  1.000 18.66275  ? 111 PRO A HB3  1 
ATOM   1038 H  HG2  . PRO A  1 111 ? -5.01300  -27.63600 35.08900  1.000 19.83085  ? 111 PRO A HG2  1 
ATOM   1039 H  HG3  . PRO A  1 111 ? -6.36400  -28.14700 35.75100  1.000 19.83085  ? 111 PRO A HG3  1 
ATOM   1040 H  HD2  . PRO A  1 111 ? -6.04200  -27.07600 33.15300  1.000 17.26588  ? 111 PRO A HD2  1 
ATOM   1041 H  HD3  . PRO A  1 111 ? -6.92800  -28.33000 33.56100  1.000 17.26588  ? 111 PRO A HD3  1 
ATOM   1042 N  N    . ARG A  1 112 ? -7.35100  -23.76500 33.77500  1.000 13.68356  ? 112 ARG A N    1 
ATOM   1043 C  CA   . ARG A  1 112 ? -7.33400  -22.33500 33.54200  1.000 13.93664  ? 112 ARG A CA   1 
ATOM   1044 C  C    . ARG A  1 112 ? -8.76100  -21.79500 33.50200  1.000 13.87188  ? 112 ARG A C    1 
ATOM   1045 O  O    . ARG A  1 112 ? -9.04000  -20.73100 34.07600  1.000 14.83842  ? 112 ARG A O    1 
ATOM   1046 C  CB   . ARG A  1 112 ? -6.55600  -21.97500 32.27500  1.000 13.54042  ? 112 ARG A CB   1 
ATOM   1047 C  CG   . ARG A  1 112 ? -6.48100  -20.49700 32.02500  1.000 13.77937  ? 112 ARG A CG   1 
ATOM   1048 C  CD   . ARG A  1 112 ? -5.95400  -19.67900 33.22900  1.000 15.35496  ? 112 ARG A CD   1 
ATOM   1049 N  NE   . ARG A  1 112 ? -5.45400  -18.35800 32.87700  1.000 14.99757  ? 112 ARG A NE   1 
ATOM   1050 C  CZ   . ARG A  1 112 ? -4.24600  -18.11700 32.42100  1.000 14.90437  ? 112 ARG A CZ   1 
ATOM   1051 N  NH1  . ARG A  1 112 ? -3.33900  -19.07300 32.33500  1.000 15.83663  ? 112 ARG A NH1  1 
ATOM   1052 N  NH2  . ARG A  1 112 ? -3.90700  -16.86700 32.08200  1.000 15.59038  ? 112 ARG A NH2  1 
ATOM   1053 H  H    . ARG A  1 112 ? -7.05500  -24.24500 33.12600  1.000 16.42284  ? 112 ARG A H    1 
ATOM   1054 H  HA   . ARG A  1 112 ? -6.85700  -21.90500 34.26900  1.000 16.72652  ? 112 ARG A HA   1 
ATOM   1055 H  HB2  . ARG A  1 112 ? -5.64900  -22.30900 32.35800  1.000 16.25107  ? 112 ARG A HB2  1 
ATOM   1056 H  HB3  . ARG A  1 112 ? -6.99200  -22.38400 31.51200  1.000 16.25107  ? 112 ARG A HB3  1 
ATOM   1057 H  HG2  . ARG A  1 112 ? -5.88300  -20.33700 31.27800  1.000 16.53780  ? 112 ARG A HG2  1 
ATOM   1058 H  HG3  . ARG A  1 112 ? -7.37000  -20.17100 31.81500  1.000 16.53780  ? 112 ARG A HG3  1 
ATOM   1059 H  HD2  . ARG A  1 112 ? -6.67700  -19.56000 33.86500  1.000 18.42851  ? 112 ARG A HD2  1 
ATOM   1060 H  HD3  . ARG A  1 112 ? -5.22600  -20.16800 33.64300  1.000 18.42851  ? 112 ARG A HD3  1 
ATOM   1061 H  HE   . ARG A  1 112 ? -5.98700  -17.68900 32.97300  1.000 17.99965  ? 112 ARG A HE   1 
ATOM   1062 H  HH11 . ARG A  1 112 ? -3.53400  -19.87400 32.58100  1.000 19.00651  ? 112 ARG A HH11 1 
ATOM   1063 H  HH12 . ARG A  1 112 ? -2.55300  -18.89500 32.03400  1.000 19.00651  ? 112 ARG A HH12 1 
ATOM   1064 H  HH21 . ARG A  1 112 ? -4.47900  -16.22900 32.16400  1.000 18.71101  ? 112 ARG A HH21 1 
ATOM   1065 H  HH22 . ARG A  1 112 ? -3.11800  -16.70100 31.78300  1.000 18.71101  ? 112 ARG A HH22 1 
ATOM   1066 N  N    . LEU A  1 113 ? -9.67800  -22.50200 32.82500  1.000 13.88346  ? 113 LEU A N    1 
ATOM   1067 C  CA   . LEU A  1 113 ? -11.07800 -22.07500 32.82300  1.000 13.33714  ? 113 LEU A CA   1 
ATOM   1068 C  C    . LEU A  1 113 ? -11.76800 -22.42800 34.11500  1.000 13.32624  ? 113 LEU A C    1 
ATOM   1069 O  O    . LEU A  1 113 ? -12.52500 -21.61700 34.64400  1.000 13.82085  ? 113 LEU A O    1 
ATOM   1070 C  CB   . LEU A  1 113 ? -11.80300 -22.66400 31.60300  1.000 13.48119  ? 113 LEU A CB   1 
ATOM   1071 C  CG   . LEU A  1 113 ? -11.44600 -21.97600 30.28200  1.000 15.09327  ? 113 LEU A CG   1 
ATOM   1072 C  CD1  . LEU A  1 113 ? -11.76600 -22.91600 29.12200  1.000 15.69915  ? 113 LEU A CD1  1 
ATOM   1073 C  CD2  . LEU A  1 113 ? -12.19000 -20.66100 30.12700  1.000 18.81246  ? 113 LEU A CD2  1 
ATOM   1074 H  H    . LEU A  1 113 ? -9.51700  -23.21500 32.37200  1.000 16.66271  ? 113 LEU A H    1 
ATOM   1075 H  HA   . LEU A  1 113 ? -11.11900 -21.11000 32.73800  1.000 16.00713  ? 113 LEU A HA   1 
ATOM   1076 H  HB2  . LEU A  1 113 ? -11.56700 -23.60100 31.52200  1.000 16.17999  ? 113 LEU A HB2  1 
ATOM   1077 H  HB3  . LEU A  1 113 ? -12.75900 -22.57200 31.73600  1.000 16.17999  ? 113 LEU A HB3  1 
ATOM   1078 H  HG   . LEU A  1 113 ? -10.49900 -21.77000 30.27200  1.000 18.11449  ? 113 LEU A HG   1 
ATOM   1079 H  HD11 . LEU A  1 113 ? -11.53900 -22.47600 28.28800  1.000 18.84154  ? 113 LEU A HD11 1 
ATOM   1080 H  HD12 . LEU A  1 113 ? -11.24400 -23.72700 29.22100  1.000 18.84154  ? 113 LEU A HD12 1 
ATOM   1081 H  HD13 . LEU A  1 113 ? -12.71200 -23.12700 29.13900  1.000 18.84154  ? 113 LEU A HD13 1 
ATOM   1082 H  HD21 . LEU A  1 113 ? -11.87500 -20.21200 29.32600  1.000 22.57751  ? 113 LEU A HD21 1 
ATOM   1083 H  HD22 . LEU A  1 113 ? -13.14000 -20.84200 30.05200  1.000 22.57751  ? 113 LEU A HD22 1 
ATOM   1084 H  HD23 . LEU A  1 113 ? -12.01900 -20.10800 30.90500  1.000 22.57751  ? 113 LEU A HD23 1 
ATOM   1085 N  N    . ALA A  1 114 ? -11.56500 -23.63100 34.63800  1.000 13.49082  ? 114 ALA A N    1 
ATOM   1086 C  CA   . ALA A  1 114 ? -12.36200 -24.01900 35.79000  1.000 13.27574  ? 114 ALA A CA   1 
ATOM   1087 C  C    . ALA A  1 114 ? -12.06800 -23.15100 37.01100  1.000 14.30132  ? 114 ALA A C    1 
ATOM   1088 O  O    . ALA A  1 114 ? -12.97200 -22.85200 37.80100  1.000 14.93796  ? 114 ALA A O    1 
ATOM   1089 C  CB   . ALA A  1 114 ? -12.12200 -25.48400 36.14100  1.000 13.92017  ? 114 ALA A CB   1 
ATOM   1090 H  H    . ALA A  1 114 ? -10.99900 -24.21400 34.35600  1.000 16.19154  ? 114 ALA A H    1 
ATOM   1091 H  HA   . ALA A  1 114 ? -13.29500 -23.90300 35.55000  1.000 15.93344  ? 114 ALA A HA   1 
ATOM   1092 H  HB1  . ALA A  1 114 ? -12.64800 -25.71200 36.92400  1.000 16.70676  ? 114 ALA A HB1  1 
ATOM   1093 H  HB2  . ALA A  1 114 ? -12.39100 -26.03700 35.39100  1.000 16.70676  ? 114 ALA A HB2  1 
ATOM   1094 H  HB3  . ALA A  1 114 ? -11.17900 -25.61500 36.32700  1.000 16.70676  ? 114 ALA A HB3  1 
ATOM   1095 N  N    . SER A  1 115 ? -10.81100 -22.75700 37.19000  1.000 13.82608  ? 115 SER A N    1 
ATOM   1096 C  CA   . SER A  1 115 ? -10.40700 -21.87900 38.29200  1.000 14.15671  ? 115 SER A CA   1 
ATOM   1097 C  C    . SER A  1 115 ? -10.99000 -20.47700 38.20000  1.000 14.31510  ? 115 SER A C    1 
ATOM   1098 O  O    . SER A  1 115 ? -10.87100 -19.71100 39.15300  1.000 14.96908  ? 115 SER A O    1 
ATOM   1099 C  CB   . SER A  1 115 ? -8.87900  -21.82200 38.40400  1.000 14.31273  ? 115 SER A CB   1 
ATOM   1100 O  OG   . SER A  1 115 ? -8.29100  -21.15000 37.32500  1.000 14.74649  ? 115 SER A OG   1 
ATOM   1101 H  H    . SER A  1 115 ? -10.15800 -22.98700 36.67900  1.000 16.59386  ? 115 SER A H    1 
ATOM   1102 H  HA   . SER A  1 115 ? -10.74000 -22.26400 39.11700  1.000 16.99061  ? 115 SER A HA   1 
ATOM   1103 H  HB2  . SER A  1 115 ? -8.64600  -21.35800 39.22300  1.000 17.17784  ? 115 SER A HB2  1 
ATOM   1104 H  HB3  . SER A  1 115 ? -8.53700  -22.72900 38.42800  1.000 17.17784  ? 115 SER A HB3  1 
ATOM   1105 H  HG   . SER A  1 115 ? -8.43600  -21.56900 36.61200  1.000 17.69835  ? 115 SER A HG   1 
ATOM   1106 N  N    . HIS A  1 116 ? -11.65900 -20.14000 37.09200  1.000 14.70096  ? 116 HIS A N    1 
ATOM   1107 C  CA   . HIS A  1 116 ? -12.39700 -18.89700 36.94900  1.000 15.32831  ? 116 HIS A CA   1 
ATOM   1108 C  C    . HIS A  1 116 ? -13.90800 -19.10900 37.01600  1.000 15.75197  ? 116 HIS A C    1 
ATOM   1109 O  O    . HIS A  1 116 ? -14.65800 -18.20600 36.63800  1.000 19.68748  ? 116 HIS A O    1 
ATOM   1110 C  CB   . HIS A  1 116 ? -11.98300 -18.18500 35.66500  1.000 14.91937  ? 116 HIS A CB   1 
ATOM   1111 C  CG   . HIS A  1 116 ? -10.69400 -17.44500 35.76800  1.000 14.15236  ? 116 HIS A CG   1 
ATOM   1112 N  ND1  . HIS A  1 116 ? -10.61200 -16.21200 36.39400  1.000 15.54085  ? 116 HIS A ND1  1 
ATOM   1113 C  CD2  . HIS A  1 116 ? -9.43700  -17.76500 35.36800  1.000 14.32350  ? 116 HIS A CD2  1 
ATOM   1114 C  CE1  . HIS A  1 116 ? -9.35300  -15.79900 36.33500  1.000 15.71521  ? 116 HIS A CE1  1 
ATOM   1115 N  NE2  . HIS A  1 116 ? -8.63000  -16.70900 35.71400  1.000 14.80288  ? 116 HIS A NE2  1 
ATOM   1116 H  H    . HIS A  1 116 ? -11.69700 -20.63600 36.39100  1.000 17.64372  ? 116 HIS A H    1 
ATOM   1117 H  HA   . HIS A  1 116 ? -12.16800 -18.30400 37.68100  1.000 18.39654  ? 116 HIS A HA   1 
ATOM   1118 H  HB2  . HIS A  1 116 ? -11.88800 -18.84500 34.96000  1.000 17.90581  ? 116 HIS A HB2  1 
ATOM   1119 H  HB3  . HIS A  1 116 ? -12.67200 -17.54500 35.42900  1.000 17.90581  ? 116 HIS A HB3  1 
ATOM   1120 H  HD2  . HIS A  1 116 ? -9.17300  -18.54800 34.94100  1.000 17.19077  ? 116 HIS A HD2  1 
ATOM   1121 H  HE1  . HIS A  1 116 ? -9.03200  -14.99600 36.67700  1.000 18.86082  ? 116 HIS A HE1  1 
ATOM   1122 H  HE2  . HIS A  1 116 ? -7.78800  -16.65100 35.55100  1.000 17.76601  ? 116 HIS A HE2  1 
ATOM   1123 N  N    . GLY A  1 117 ? -14.36100 -20.25700 37.49500  1.000 14.27070  ? 117 GLY A N    1 
ATOM   1124 C  CA   . GLY A  1 117 ? -15.77700 -20.42700 37.75900  1.000 13.95178  ? 117 GLY A CA   1 
ATOM   1125 C  C    . GLY A  1 117 ? -16.55600 -21.05700 36.63300  1.000 14.11973  ? 117 GLY A C    1 
ATOM   1126 O  O    . GLY A  1 117 ? -17.62700 -20.55100 36.28500  1.000 15.63847  ? 117 GLY A O    1 
ATOM   1127 H  H    . GLY A  1 117 ? -13.87400 -20.94300 37.67300  1.000 17.12740  ? 117 GLY A H    1 
ATOM   1128 H  HA2  . GLY A  1 117 ? -15.88300 -20.98900 38.54200  1.000 16.74469  ? 117 GLY A HA2  1 
ATOM   1129 H  HA3  . GLY A  1 117 ? -16.16800 -19.55800 37.93800  1.000 16.74469  ? 117 GLY A HA3  1 
ATOM   1130 N  N    . PHE A  1 118 ? -16.05500 -22.13700 36.06600  1.000 13.91841  ? 118 PHE A N    1 
ATOM   1131 C  CA   . PHE A  1 118 ? -16.69700 -22.89400 35.00200  1.000 12.88325  ? 118 PHE A CA   1 
ATOM   1132 C  C    . PHE A  1 118 ? -16.53800 -24.37300 35.31000  1.000 14.39142  ? 118 PHE A C    1 
ATOM   1133 O  O    . PHE A  1 118 ? -15.55400 -24.78600 35.94200  1.000 15.20167  ? 118 PHE A O    1 
ATOM   1134 C  CB   . PHE A  1 118 ? -16.06800 -22.61400 33.62500  1.000 13.52409  ? 118 PHE A CB   1 
ATOM   1135 C  CG   . PHE A  1 118 ? -16.22400 -21.20100 33.16500  1.000 14.77627  ? 118 PHE A CG   1 
ATOM   1136 C  CD1  . PHE A  1 118 ? -17.44300 -20.75300 32.64800  1.000 16.28203  ? 118 PHE A CD1  1 
ATOM   1137 C  CD2  . PHE A  1 118 ? -15.20300 -20.29600 33.22100  1.000 15.12802  ? 118 PHE A CD2  1 
ATOM   1138 C  CE1  . PHE A  1 118 ? -17.61500 -19.44800 32.25700  1.000 16.82353  ? 118 PHE A CE1  1 
ATOM   1139 C  CE2  . PHE A  1 118 ? -15.38000 -18.98300 32.86000  1.000 16.23117  ? 118 PHE A CE2  1 
ATOM   1140 C  CZ   . PHE A  1 118 ? -16.59900 -18.55300 32.37200  1.000 18.32769  ? 118 PHE A CZ   1 
ATOM   1141 H  H    . PHE A  1 118 ? -15.29700 -22.47600 36.29200  1.000 16.70465  ? 118 PHE A H    1 
ATOM   1142 H  HA   . PHE A  1 118 ? -17.63700 -22.65800 34.96300  1.000 15.46246  ? 118 PHE A HA   1 
ATOM   1143 H  HB2  . PHE A  1 118 ? -15.11900 -22.80600 33.67200  1.000 16.23147  ? 118 PHE A HB2  1 
ATOM   1144 H  HB3  . PHE A  1 118 ? -16.49100 -23.18700 32.96700  1.000 16.23147  ? 118 PHE A HB3  1 
ATOM   1145 H  HD1  . PHE A  1 118 ? -18.15100 -21.35000 32.56600  1.000 19.54100  ? 118 PHE A HD1  1 
ATOM   1146 H  HD2  . PHE A  1 118 ? -14.36500 -20.57700 33.51200  1.000 18.15618  ? 118 PHE A HD2  1 
ATOM   1147 H  HE1  . PHE A  1 118 ? -18.43300 -19.17400 31.91100  1.000 20.19080  ? 118 PHE A HE1  1 
ATOM   1148 H  HE2  . PHE A  1 118 ? -14.67600 -18.38000 32.94400  1.000 19.47997  ? 118 PHE A HE2  1 
ATOM   1149 H  HZ   . PHE A  1 118 ? -16.72200 -17.66500 32.12600  1.000 21.99579  ? 118 PHE A HZ   1 
ATOM   1150 N  N    . VAL A  1 119 ? -17.49500 -25.18900 34.87500  1.000 13.65599  ? 119 VAL A N    1 
ATOM   1151 C  CA   . VAL A  1 119 ? -17.33200 -26.64400 34.86300  1.000 13.24541  ? 119 VAL A CA   1 
ATOM   1152 C  C    . VAL A  1 119 ? -16.74500 -27.01800 33.52200  1.000 13.88158  ? 119 VAL A C    1 
ATOM   1153 O  O    . VAL A  1 119 ? -17.33800 -26.71100 32.50300  1.000 14.50173  ? 119 VAL A O    1 
ATOM   1154 C  CB   . VAL A  1 119 ? -18.68700 -27.34100 35.07100  1.000 14.15550  ? 119 VAL A CB   1 
ATOM   1155 C  CG1  . VAL A  1 119 ? -18.55200 -28.84700 34.91700  1.000 16.16734  ? 119 VAL A CG1  1 
ATOM   1156 C  CG2  . VAL A  1 119 ? -19.27000 -26.97600 36.40900  1.000 17.14857  ? 119 VAL A CG2  1 
ATOM   1157 H  H    . VAL A  1 119 ? -18.25700 -24.92300 34.57900  1.000 16.38974  ? 119 VAL A H    1 
ATOM   1158 H  HA   . VAL A  1 119 ? -16.72500 -26.92000 35.56700  1.000 15.89705  ? 119 VAL A HA   1 
ATOM   1159 H  HB   . VAL A  1 119 ? -19.30400 -27.03500 34.38800  1.000 16.98917  ? 119 VAL A HB   1 
ATOM   1160 H  HG11 . VAL A  1 119 ? -19.38700 -29.26800 35.17600  1.000 19.40337  ? 119 VAL A HG11 1 
ATOM   1161 H  HG12 . VAL A  1 119 ? -18.35100 -29.05300 33.99000  1.000 19.40337  ? 119 VAL A HG12 1 
ATOM   1162 H  HG13 . VAL A  1 119 ? -17.83300 -29.16000 35.48800  1.000 19.40337  ? 119 VAL A HG13 1 
ATOM   1163 H  HG21 . VAL A  1 119 ? -20.17000 -27.33400 36.46900  1.000 20.58085  ? 119 VAL A HG21 1 
ATOM   1164 H  HG22 . VAL A  1 119 ? -18.71600 -27.35500 37.10900  1.000 20.58085  ? 119 VAL A HG22 1 
ATOM   1165 H  HG23 . VAL A  1 119 ? -19.29200 -26.01000 36.49000  1.000 20.58085  ? 119 VAL A HG23 1 
ATOM   1166 N  N    . VAL A  1 120 ? -15.57400 -27.62200 33.51000  1.000 13.77064  ? 120 VAL A N    1 
ATOM   1167 C  CA   . VAL A  1 120 ? -14.79300 -27.79800 32.28900  1.000 13.29167  ? 120 VAL A CA   1 
ATOM   1168 C  C    . VAL A  1 120 ? -14.36300 -29.23700 32.16100  1.000 13.83850  ? 120 VAL A C    1 
ATOM   1169 O  O    . VAL A  1 120 ? -13.66600 -29.74800 33.03800  1.000 16.18647  ? 120 VAL A O    1 
ATOM   1170 C  CB   . VAL A  1 120 ? -13.54700 -26.89500 32.27400  1.000 13.94147  ? 120 VAL A CB   1 
ATOM   1171 C  CG1  . VAL A  1 120 ? -12.84200 -26.99100 30.93500  1.000 15.02131  ? 120 VAL A CG1  1 
ATOM   1172 C  CG2  . VAL A  1 120 ? -13.91700 -25.48600 32.59500  1.000 14.68159  ? 120 VAL A CG2  1 
ATOM   1173 H  H    . VAL A  1 120 ? -15.19600 -27.94800 34.21000  1.000 16.52733  ? 120 VAL A H    1 
ATOM   1174 H  HA   . VAL A  1 120 ? -15.36800 -27.58900 31.53600  1.000 15.95257  ? 120 VAL A HA   1 
ATOM   1175 H  HB   . VAL A  1 120 ? -12.92700 -27.19500 32.95600  1.000 16.73232  ? 120 VAL A HB   1 
ATOM   1176 H  HG11 . VAL A  1 120 ? -12.12800 -26.33500 30.90600  1.000 18.02814  ? 120 VAL A HG11 1 
ATOM   1177 H  HG12 . VAL A  1 120 ? -12.47600 -27.88400 30.83400  1.000 18.02814  ? 120 VAL A HG12 1 
ATOM   1178 H  HG13 . VAL A  1 120 ? -13.48200 -26.81400 30.22800  1.000 18.02814  ? 120 VAL A HG13 1 
ATOM   1179 H  HG21 . VAL A  1 120 ? -13.12700 -24.92800 32.52200  1.000 17.62048  ? 120 VAL A HG21 1 
ATOM   1180 H  HG22 . VAL A  1 120 ? -14.59300 -25.18500 31.96800  1.000 17.62048  ? 120 VAL A HG22 1 
ATOM   1181 H  HG23 . VAL A  1 120 ? -14.26500 -25.44900 33.50000  1.000 17.62048  ? 120 VAL A HG23 1 
ATOM   1182 N  N    . MET A  1 121 ? -14.69700 -29.89000 31.06200  1.000 13.01491  ? 121 MET A N    1 
ATOM   1183 C  CA   . MET A  1 121 ? -14.27900 -31.26500 30.82800  1.000 14.52288  ? 121 MET A CA   1 
ATOM   1184 C  C    . MET A  1 121 ? -13.37500 -31.33300 29.60800  1.000 13.55720  ? 121 MET A C    1 
ATOM   1185 O  O    . MET A  1 121 ? -13.80400 -30.98500 28.49800  1.000 14.30211  ? 121 MET A O    1 
ATOM   1186 C  CB   . MET A  1 121 ? -15.45700 -32.21400 30.67700  1.000 15.20797  ? 121 MET A CB   1 
ATOM   1187 C  CG   . MET A  1 121 ? -15.04100 -33.65000 30.59900  1.000 15.15413  ? 121 MET A CG   1 
ATOM   1188 S  SD   . MET A  1 121 ? -16.42800 -34.82400 30.62300  1.000 17.17655  ? 121 MET A SD   1 
ATOM   1189 C  CE   . MET A  1 121 ? -17.44000 -34.26500 29.26800  1.000 20.01145  ? 121 MET A CE   1 
ATOM   1190 H  H    . MET A  1 121 ? -15.17100 -29.55500 30.42700  1.000 15.62045  ? 121 MET A H    1 
ATOM   1191 H  HA   . MET A  1 121 ? -13.77400 -31.55000 31.60600  1.000 17.43002  ? 121 MET A HA   1 
ATOM   1192 H  HB2  . MET A  1 121 ? -16.04400 -32.11300 31.44300  1.000 18.25213  ? 121 MET A HB2  1 
ATOM   1193 H  HB3  . MET A  1 121 ? -15.93500 -31.99600 29.86200  1.000 18.25213  ? 121 MET A HB3  1 
ATOM   1194 H  HG2  . MET A  1 121 ? -14.55300 -33.78800 29.77300  1.000 18.18751  ? 121 MET A HG2  1 
ATOM   1195 H  HG3  . MET A  1 121 ? -14.47200 -33.85100 31.35900  1.000 18.18751  ? 121 MET A HG3  1 
ATOM   1196 H  HE1  . MET A  1 121 ? -18.12900 -34.92500 29.09600  1.000 24.01630  ? 121 MET A HE1  1 
ATOM   1197 H  HE2  . MET A  1 121 ? -17.84600 -33.41700 29.50600  1.000 24.01630  ? 121 MET A HE2  1 
ATOM   1198 H  HE3  . MET A  1 121 ? -16.88200 -34.15600 28.48200  1.000 24.01630  ? 121 MET A HE3  1 
ATOM   1199 N  N    . THR A  1 122 ? -12.13100 -31.77300 29.81800  1.000 14.14964  ? 122 THR A N    1 
ATOM   1200 C  CA   . THR A  1 122 ? -11.24200 -32.09900 28.70800  1.000 13.97263  ? 122 THR A CA   1 
ATOM   1201 C  C    . THR A  1 122 ? -11.54200 -33.53300 28.29100  1.000 15.44437  ? 122 THR A C    1 
ATOM   1202 O  O    . THR A  1 122 ? -11.61500 -34.43900 29.13800  1.000 18.11548  ? 122 THR A O    1 
ATOM   1203 C  CB   . THR A  1 122 ? -9.78400  -31.96000 29.14500  1.000 14.00014  ? 122 THR A CB   1 
ATOM   1204 O  OG1  . THR A  1 122 ? -9.47900  -32.82500 30.24000  1.000 15.60467  ? 122 THR A OG1  1 
ATOM   1205 C  CG2  . THR A  1 122 ? -9.48100  -30.52100 29.51600  1.000 14.18069  ? 122 THR A CG2  1 
ATOM   1206 H  H    . THR A  1 122 ? -11.78200 -31.89000 30.59500  1.000 16.98213  ? 122 THR A H    1 
ATOM   1207 H  HA   . THR A  1 122 ? -11.37900 -31.50000 27.95700  1.000 16.76972  ? 122 THR A HA   1 
ATOM   1208 H  HB   . THR A  1 122 ? -9.21300  -32.21600 28.40300  1.000 16.80273  ? 122 THR A HB   1 
ATOM   1209 H  HG1  . THR A  1 122 ? -8.68300  -32.71200 30.48300  1.000 18.72816  ? 122 THR A HG1  1 
ATOM   1210 H  HG21 . THR A  1 122 ? -8.55400  -30.43600 29.78900  1.000 17.01940  ? 122 THR A HG21 1 
ATOM   1211 H  HG22 . THR A  1 122 ? -9.63800  -29.94100 28.75400  1.000 17.01940  ? 122 THR A HG22 1 
ATOM   1212 H  HG23 . THR A  1 122 ? -10.05100 -30.24000 30.24800  1.000 17.01940  ? 122 THR A HG23 1 
ATOM   1213 N  N    . ILE A  1 123 ? -11.72800 -33.76600 26.99600  1.000 14.29393  ? 123 ILE A N    1 
ATOM   1214 C  CA   . ILE A  1 123 ? -12.17300 -35.08000 26.55800  1.000 15.79660  ? 123 ILE A CA   1 
ATOM   1215 C  C    . ILE A  1 123 ? -11.18200 -35.75300 25.61700  1.000 16.49887  ? 123 ILE A C    1 
ATOM   1216 O  O    . ILE A  1 123 ? -10.37000 -35.11300 24.95000  1.000 16.94568  ? 123 ILE A O    1 
ATOM   1217 C  CB   . ILE A  1 123 ? -13.57300 -35.06700 25.87800  1.000 15.69831  ? 123 ILE A CB   1 
ATOM   1218 C  CG1  . ILE A  1 123 ? -13.56800 -34.26400 24.56500  1.000 15.30216  ? 123 ILE A CG1  1 
ATOM   1219 C  CG2  . ILE A  1 123 ? -14.65100 -34.57900 26.86100  1.000 15.14986  ? 123 ILE A CG2  1 
ATOM   1220 C  CD1  . ILE A  1 123 ? -14.81400 -34.49500 23.68800  1.000 17.35538  ? 123 ILE A CD1  1 
ATOM   1221 H  H    . ILE A  1 123 ? -11.60500 -33.19100 26.36800  1.000 17.15528  ? 123 ILE A H    1 
ATOM   1222 H  HA   . ILE A  1 123 ? -12.20300 -35.61000 27.36900  1.000 18.95848  ? 123 ILE A HA   1 
ATOM   1223 H  HB   . ILE A  1 123 ? -13.79100 -35.98000 25.63300  1.000 18.84054  ? 123 ILE A HB   1 
ATOM   1224 H  HG12 . ILE A  1 123 ? -13.52900 -33.31800 24.77900  1.000 18.36516  ? 123 ILE A HG12 1 
ATOM   1225 H  HG13 . ILE A  1 123 ? -12.79000 -34.52000 24.04600  1.000 18.36516  ? 123 ILE A HG13 1 
ATOM   1226 H  HG21 . ILE A  1 123 ? -15.52400 -34.69400 26.45400  1.000 18.18239  ? 123 ILE A HG21 1 
ATOM   1227 H  HG22 . ILE A  1 123 ? -14.59400 -35.10100 27.67600  1.000 18.18239  ? 123 ILE A HG22 1 
ATOM   1228 H  HG23 . ILE A  1 123 ? -14.49800 -33.64100 27.05700  1.000 18.18239  ? 123 ILE A HG23 1 
ATOM   1229 H  HD11 . ILE A  1 123 ? -14.71600 -33.99400 22.86200  1.000 20.82901  ? 123 ILE A HD11 1 
ATOM   1230 H  HD12 . ILE A  1 123 ? -14.89200 -35.44200 23.49300  1.000 20.82901  ? 123 ILE A HD12 1 
ATOM   1231 H  HD13 . ILE A  1 123 ? -15.59900 -34.19000 24.16800  1.000 20.82901  ? 123 ILE A HD13 1 
ATOM   1232 N  N    . ASP A  1 124 ? -11.28200 -37.07900 25.57200  1.000 16.26137  ? 124 ASP A N    1 
ATOM   1233 C  CA   . ASP A  1 124 ? -10.76900 -37.90100 24.49600  1.000 18.30608  ? 124 ASP A CA   1 
ATOM   1234 C  C    . ASP A  1 124 ? -11.90600 -38.21900 23.52900  1.000 17.58439  ? 124 ASP A C    1 
ATOM   1235 O  O    . ASP A  1 124 ? -13.08400 -38.26600 23.91000  1.000 18.40725  ? 124 ASP A O    1 
ATOM   1236 C  CB   . ASP A  1 124 ? -10.18000 -39.20000 25.02800  1.000 17.21689  ? 124 ASP A CB   1 
ATOM   1237 C  CG   . ASP A  1 124 ? -8.84000  -38.99500 25.67900  1.000 19.37203  ? 124 ASP A CG   1 
ATOM   1238 O  OD1  . ASP A  1 124 ? -7.94900  -38.45900 24.98600  1.000 22.80734  ? 124 ASP A OD1  1 
ATOM   1239 O  OD2  . ASP A  1 124 ? -8.66800  -39.37800 26.85300  1.000 20.86414  ? 124 ASP A OD2  1 
ATOM   1240 H  H    . ASP A  1 124 ? -11.66300 -37.54300 26.18800  1.000 19.51620  ? 124 ASP A H    1 
ATOM   1241 H  HA   . ASP A  1 124 ? -10.06600 -37.42700 24.02600  1.000 21.96986  ? 124 ASP A HA   1 
ATOM   1242 H  HB2  . ASP A  1 124 ? -10.78300 -39.57500 25.68900  1.000 20.66283  ? 124 ASP A HB2  1 
ATOM   1243 H  HB3  . ASP A  1 124 ? -10.06600 -39.82200 24.29200  1.000 20.66283  ? 124 ASP A HB3  1 
ATOM   1244 N  N    . THR A  1 125 ? -11.53100 -38.46500 22.28900  1.000 18.50137  ? 125 THR A N    1 
ATOM   1245 C  CA   . THR A  1 125 ? -12.49800 -38.88600 21.29400  1.000 19.01896  ? 125 THR A CA   1 
ATOM   1246 C  C    . THR A  1 125 ? -12.58800 -40.40300 21.28500  1.000 20.18282  ? 125 THR A C    1 
ATOM   1247 O  O    . THR A  1 125 ? -11.75600 -41.13000 21.84600  1.000 22.10743  ? 125 THR A O    1 
ATOM   1248 C  CB   . THR A  1 125 ? -12.13800 -38.34200 19.91100  1.000 19.41712  ? 125 THR A CB   1 
ATOM   1249 O  OG1  . THR A  1 125 ? -10.78100 -38.65000 19.60600  1.000 21.11461  ? 125 THR A OG1  1 
ATOM   1250 C  CG2  . THR A  1 125 ? -12.29300 -36.84200 19.88600  1.000 21.50618  ? 125 THR A CG2  1 
ATOM   1251 H  H    . THR A  1 125 ? -10.72500 -38.39600 21.99900  1.000 22.20421  ? 125 THR A H    1 
ATOM   1252 H  HA   . THR A  1 125 ? -13.37100 -38.52500 21.51600  1.000 22.82532  ? 125 THR A HA   1 
ATOM   1253 H  HB   . THR A  1 125 ? -12.72600 -38.74100 19.25000  1.000 23.30311  ? 125 THR A HB   1 
ATOM   1254 H  HG1  . THR A  1 125 ? -10.66600 -39.48200 19.61700  1.000 25.34009  ? 125 THR A HG1  1 
ATOM   1255 H  HG21 . THR A  1 125 ? -12.09000 -36.50200 19.00000  1.000 25.80998  ? 125 THR A HG21 1 
ATOM   1256 H  HG22 . THR A  1 125 ? -13.20300 -36.59900 20.11600  1.000 25.80998  ? 125 THR A HG22 1 
ATOM   1257 H  HG23 . THR A  1 125 ? -11.68700 -36.43600 20.52500  1.000 25.80998  ? 125 THR A HG23 1 
ATOM   1258 N  N    . ASN A  1 126 ? -13.59100 -40.90300 20.57000  1.000 20.48325  ? 126 ASN A N    1 
ATOM   1259 C  CA   . ASN A  1 126 ? -13.74500 -42.34200 20.47100  1.000 21.37453  ? 126 ASN A CA   1 
ATOM   1260 C  C    . ASN A  1 126 ? -12.49400 -42.99500 19.88500  1.000 22.66675  ? 126 ASN A C    1 
ATOM   1261 O  O    . ASN A  1 126 ? -12.03500 -44.03200 20.37600  1.000 24.40031  ? 126 ASN A O    1 
ATOM   1262 C  CB   . ASN A  1 126 ? -14.94100 -42.64800 19.58800  1.000 21.79563  ? 126 ASN A CB   1 
ATOM   1263 C  CG   . ASN A  1 126 ? -16.25900 -42.32500 20.25200  1.000 24.35730  ? 126 ASN A CG   1 
ATOM   1264 O  OD1  . ASN A  1 126 ? -16.40700 -42.37100 21.47400  1.000 25.12525  ? 126 ASN A OD1  1 
ATOM   1265 N  ND2  . ASN A  1 126 ? -17.24300 -41.98100 19.43400  1.000 28.10953  ? 126 ASN A ND2  1 
ATOM   1266 H  H    . ASN A  1 126 ? -14.17900 -40.44000 20.14600  1.000 24.58246  ? 126 ASN A H    1 
ATOM   1267 H  HA   . ASN A  1 126 ? -13.89200 -42.70600 21.35800  1.000 25.65200  ? 126 ASN A HA   1 
ATOM   1268 H  HB2  . ASN A  1 126 ? -14.87800 -42.12100 18.77600  1.000 26.15732  ? 126 ASN A HB2  1 
ATOM   1269 H  HB3  . ASN A  1 126 ? -14.94000 -43.59400 19.37000  1.000 26.15732  ? 126 ASN A HB3  1 
ATOM   1270 H  HD21 . ASN A  1 126 ? -18.01800 -41.78500 19.75200  1.000 33.73400  ? 126 ASN A HD21 1 
ATOM   1271 H  HD22 . ASN A  1 126 ? -17.10700 -41.95400 18.58500  1.000 33.73400  ? 126 ASN A HD22 1 
ATOM   1272 N  N    . ARG A  1 127 ? -11.94900 -42.41100 18.81300  1.000 21.75346  ? 127 ARG A N    1 
ATOM   1273 C  CA   . ARG A  1 127 ? -10.68300 -42.82500 18.22200  1.000 22.51919  ? 127 ARG A CA   1 
ATOM   1274 C  C    . ARG A  1 127 ? -9.87300  -41.56500 17.93800  1.000 21.22214  ? 127 ARG A C    1 
ATOM   1275 O  O    . ARG A  1 127 ? -10.42800 -40.52100 17.60700  1.000 21.62129  ? 127 ARG A O    1 
ATOM   1276 C  CB   . ARG A  1 127 ? -10.87400 -43.56000 16.90300  1.000 25.45484  ? 127 ARG A CB   1 
ATOM   1277 C  CG   . ARG A  1 127 ? -11.53000 -44.91100 17.02600  1.000 27.41487  ? 127 ARG A CG   1 
ATOM   1278 C  CD   . ARG A  1 127 ? -11.72300 -45.51400 15.63900  1.000 35.39439  ? 127 ARG A CD   1 
ATOM   1279 N  NE   . ARG A  1 127 ? -12.02800 -46.93900 15.70500  1.000 46.67861  ? 127 ARG A NE   1 
ATOM   1280 C  CZ   . ARG A  1 127 ? -13.24300 -47.42700 15.90700  1.000 45.06574  ? 127 ARG A CZ   1 
ATOM   1281 N  NH1  . ARG A  1 127 ? -14.28100 -46.63000 16.09200  1.000 48.94271  ? 127 ARG A NH1  1 
ATOM   1282 N  NH2  . ARG A  1 127 ? -13.42300 -48.75000 15.90700  1.000 35.34675  ? 127 ARG A NH2  1 
ATOM   1283 H  H    . ARG A  1 127 ? -12.31000 -41.74900 18.39800  1.000 26.10671  ? 127 ARG A H    1 
ATOM   1284 H  HA   . ARG A  1 127 ? -10.21500 -43.41000 18.83900  1.000 27.02559  ? 127 ARG A HA   1 
ATOM   1285 H  HB2  . ARG A  1 127 ? -11.43200 -43.01600 16.32500  1.000 30.54837  ? 127 ARG A HB2  1 
ATOM   1286 H  HB3  . ARG A  1 127 ? -10.00400 -43.69300 16.49500  1.000 30.54837  ? 127 ARG A HB3  1 
ATOM   1287 H  HG2  . ARG A  1 127 ? -10.96700 -45.50300 17.54900  1.000 32.90040  ? 127 ARG A HG2  1 
ATOM   1288 H  HG3  . ARG A  1 127 ? -12.39700 -44.81800 17.45000  1.000 32.90040  ? 127 ARG A HG3  1 
ATOM   1289 H  HD2  . ARG A  1 127 ? -12.45900 -45.06600 15.19500  1.000 42.47583  ? 127 ARG A HD2  1 
ATOM   1290 H  HD3  . ARG A  1 127 ? -10.90800 -45.40200 15.12500  1.000 42.47583  ? 127 ARG A HD3  1 
ATOM   1291 H  HE   . ARG A  1 127 ? -11.38000 -47.49600 15.60700  1.000 56.01690  ? 127 ARG A HE   1 
ATOM   1292 H  HH11 . ARG A  1 127 ? -14.17500 -45.77600 16.08300  1.000 58.73381  ? 127 ARG A HH11 1 
ATOM   1293 H  HH12 . ARG A  1 127 ? -15.06200 -46.96400 16.22200  1.000 58.73381  ? 127 ARG A HH12 1 
ATOM   1294 H  HH21 . ARG A  1 127 ? -12.75400 -49.27500 15.77700  1.000 42.41867  ? 127 ARG A HH21 1 
ATOM   1295 H  HH22 . ARG A  1 127 ? -14.20700 -49.07700 16.03800  1.000 42.41867  ? 127 ARG A HH22 1 
ATOM   1296 N  N    . ILE A  1 128 ? -8.54800  -41.64100 18.08300  1.000 20.25063  ? 128 ILE A N    1 
ATOM   1297 C  CA   . ILE A  1 128 ? -7.76000  -40.43300 17.83600  1.000 21.94726  ? 128 ILE A CA   1 
ATOM   1298 C  C    . ILE A  1 128 ? -7.75000  -40.05500 16.36300  1.000 20.51796  ? 128 ILE A C    1 
ATOM   1299 O  O    . ILE A  1 128 ? -7.47900  -38.90700 16.03100  1.000 21.58214  ? 128 ILE A O    1 
ATOM   1300 C  CB   . ILE A  1 128 ? -6.31800  -40.54600 18.37100  1.000 23.74973  ? 128 ILE A CB   1 
ATOM   1301 C  CG1  . ILE A  1 128 ? -5.56900  -41.70600 17.72300  1.000 22.82589  ? 128 ILE A CG1  1 
ATOM   1302 C  CG2  . ILE A  1 128 ? -6.35100  -40.73200 19.88000  1.000 22.61178  ? 128 ILE A CG2  1 
ATOM   1303 C  CD1  . ILE A  1 128 ? -4.13000  -41.82900 18.21000  1.000 25.83306  ? 128 ILE A CD1  1 
ATOM   1304 H  H    . ILE A  1 128 ? -8.10600  -42.34300 18.31000  1.000 24.30331  ? 128 ILE A H    1 
ATOM   1305 H  HA   . ILE A  1 128 ? -8.17400  -39.71400 18.33800  1.000 26.33927  ? 128 ILE A HA   1 
ATOM   1306 H  HB   . ILE A  1 128 ? -5.84800  -39.72700 18.14600  1.000 28.50224  ? 128 ILE A HB   1 
ATOM   1307 H  HG12 . ILE A  1 128 ? -6.02900  -42.53400 17.93300  1.000 27.39363  ? 128 ILE A HG12 1 
ATOM   1308 H  HG13 . ILE A  1 128 ? -5.55000  -41.57200 16.76200  1.000 27.39363  ? 128 ILE A HG13 1 
ATOM   1309 H  HG21 . ILE A  1 128 ? -5.45800  -40.60000 20.23400  1.000 27.13670  ? 128 ILE A HG21 1 
ATOM   1310 H  HG22 . ILE A  1 128 ? -6.96000  -40.08200 20.26400  1.000 27.13670  ? 128 ILE A HG22 1 
ATOM   1311 H  HG23 . ILE A  1 128 ? -6.65700  -41.63000 20.08000  1.000 27.13670  ? 128 ILE A HG23 1 
ATOM   1312 H  HD11 . ILE A  1 128 ? -3.65200  -42.44200 17.63000  1.000 31.00223  ? 128 ILE A HD11 1 
ATOM   1313 H  HD12 . ILE A  1 128 ? -3.71200  -40.95400 18.18500  1.000 31.00223  ? 128 ILE A HD12 1 
ATOM   1314 H  HD13 . ILE A  1 128 ? -4.13300  -42.16900 19.11900  1.000 31.00223  ? 128 ILE A HD13 1 
ATOM   1315 N  N    . SER A  1 129 ? -8.15700  -40.96300 15.48900  1.000 22.57569  ? 129 SER A N    1 
ATOM   1316 C  CA   . SER A  1 129 ? -8.27000  -40.68200 14.06500  1.000 19.95282  ? 129 SER A CA   1 
ATOM   1317 C  C    . SER A  1 129 ? -9.58200  -40.00800 13.66500  1.000 21.20004  ? 129 SER A C    1 
ATOM   1318 O  O    . SER A  1 129 ? -9.77700  -39.73100 12.47800  1.000 23.47246  ? 129 SER A O    1 
ATOM   1319 C  CB   . SER A  1 129 ? -8.12700  -41.98500 13.27800  1.000 23.90069  ? 129 SER A CB   1 
ATOM   1320 O  OG   . SER A  1 129 ? -9.03600  -42.96700 13.75100  1.000 27.38034  ? 129 SER A OG   1 
ATOM   1321 H  H    . SER A  1 129 ? -8.37900  -41.76700 15.69900  1.000 27.09339  ? 129 SER A H    1 
ATOM   1322 H  HA   . SER A  1 129 ? -7.55000  -40.07900 13.82300  1.000 23.94595  ? 129 SER A HA   1 
ATOM   1323 H  HB2  . SER A  1 129 ? -8.31200  -41.80900 12.34200  1.000 28.68339  ? 129 SER A HB2  1 
ATOM   1324 H  HB3  . SER A  1 129 ? -7.22200  -42.31700 13.38100  1.000 28.68339  ? 129 SER A HB3  1 
ATOM   1325 H  HG   . SER A  1 129 ? -9.82600  -42.71800 13.61200  1.000 32.85897  ? 129 SER A HG   1 
ATOM   1326 N  N    . ASP A  1 130 ? -10.48300 -39.73300 14.60900  1.000 21.41255  ? 130 ASP A N    1 
ATOM   1327 C  CA   . ASP A  1 130 ? -11.78600 -39.17200 14.25700  1.000 21.14836  ? 130 ASP A CA   1 
ATOM   1328 C  C    . ASP A  1 130 ? -11.62600 -37.80400 13.59400  1.000 19.71143  ? 130 ASP A C    1 
ATOM   1329 O  O    . ASP A  1 130 ? -10.74100 -37.01600 13.94700  1.000 20.72659  ? 130 ASP A O    1 
ATOM   1330 C  CB   . ASP A  1 130 ? -12.66400 -39.03700 15.51200  1.000 21.56535  ? 130 ASP A CB   1 
ATOM   1331 C  CG   . ASP A  1 130 ? -13.11900 -40.38200 16.06600  1.000 24.33512  ? 130 ASP A CG   1 
ATOM   1332 O  OD1  . ASP A  1 130 ? -13.08200 -41.40200 15.34000  1.000 25.51518  ? 130 ASP A OD1  1 
ATOM   1333 O  OD2  . ASP A  1 130 ? -13.53700 -40.41700 17.26400  1.000 22.93924  ? 130 ASP A OD2  1 
ATOM   1334 H  H    . ASP A  1 130 ? -10.36500 -39.86100 15.45100  1.000 25.69762  ? 130 ASP A H    1 
ATOM   1335 H  HA   . ASP A  1 130 ? -12.22800 -39.76700 13.63200  1.000 25.38059  ? 130 ASP A HA   1 
ATOM   1336 H  HB2  . ASP A  1 130 ? -12.15700 -38.58400 16.20500  1.000 25.88099  ? 130 ASP A HB2  1 
ATOM   1337 H  HB3  . ASP A  1 130 ? -13.45500 -38.52200 15.29000  1.000 25.88099  ? 130 ASP A HB3  1 
ATOM   1338 N  N    . GLN A  1 131 ? -12.49000 -37.52900 12.60600  1.000 20.89869  ? 131 GLN A N    1 
ATOM   1339 C  CA   . GLN A  1 131 ? -12.46100 -36.30400 11.79800  1.000 20.18906  ? 131 GLN A CA   1 
ATOM   1340 C  C    . GLN A  1 131 ? -13.43300 -35.26800 12.37100  1.000 20.07025  ? 131 GLN A C    1 
ATOM   1341 O  O    . GLN A  1 131 ? -14.20500 -35.56200 13.28200  1.000 19.79743  ? 131 GLN A O    1 
ATOM   1342 C  CB   . GLN A  1 131 ? -12.82100 -36.65000 10.35300  1.000 22.45666  ? 131 GLN A CB   1 
ATOM   1343 C  CG   . GLN A  1 131 ? -11.91100 -37.70000 9.76600   1.000 27.50586  ? 131 GLN A CG   1 
ATOM   1344 C  CD   . GLN A  1 131 ? -10.54000 -37.17700 9.52800   1.000 31.88377  ? 131 GLN A CD   1 
ATOM   1345 O  OE1  . GLN A  1 131 ? -10.32800 -36.33100 8.65400   1.000 33.52950  ? 131 GLN A OE1  1 
ATOM   1346 N  NE2  . GLN A  1 131 ? -9.57500  -37.67600 10.29700  1.000 40.65315  ? 131 GLN A NE2  1 
ATOM   1347 H  H    . GLN A  1 131 ? -13.12600 -38.06100 12.37900  1.000 25.08099  ? 131 GLN A H    1 
ATOM   1348 H  HA   . GLN A  1 131 ? -11.57300 -35.91300 11.80700  1.000 24.22943  ? 131 GLN A HA   1 
ATOM   1349 H  HB2  . GLN A  1 131 ? -13.72900 -36.99000 10.32500  1.000 26.95056  ? 131 GLN A HB2  1 
ATOM   1350 H  HB3  . GLN A  1 131 ? -12.74900 -35.85100 9.80800   1.000 26.95056  ? 131 GLN A HB3  1 
ATOM   1351 H  HG2  . GLN A  1 131 ? -11.84800 -38.44700 10.38200  1.000 33.00959  ? 131 GLN A HG2  1 
ATOM   1352 H  HG3  . GLN A  1 131 ? -12.27300 -37.99900 8.91800   1.000 33.00959  ? 131 GLN A HG3  1 
ATOM   1353 H  HE21 . GLN A  1 131 ? -9.76200  -38.26700 10.89300  1.000 48.78634  ? 131 GLN A HE21 1 
ATOM   1354 H  HE22 . GLN A  1 131 ? -8.76400  -37.40600 10.19900  1.000 48.78634  ? 131 GLN A HE22 1 
ATOM   1355 N  N    . PRO A  1 132 ? -13.43800 -34.03700 11.85200  1.000 18.80413  ? 132 PRO A N    1 
ATOM   1356 C  CA   . PRO A  1 132 ? -14.23700 -32.97000 12.48400  1.000 18.52401  ? 132 PRO A CA   1 
ATOM   1357 C  C    . PRO A  1 132 ? -15.72300 -33.25300 12.58100  1.000 20.74868  ? 132 PRO A C    1 
ATOM   1358 O  O    . PRO A  1 132 ? -16.32400 -32.87200 13.59200  1.000 19.44473  ? 132 PRO A O    1 
ATOM   1359 C  CB   . PRO A  1 132 ? -13.92000 -31.72600 11.65000  1.000 18.48294  ? 132 PRO A CB   1 
ATOM   1360 C  CG   . PRO A  1 132 ? -12.51800 -31.97300 11.23200  1.000 19.83266  ? 132 PRO A CG   1 
ATOM   1361 C  CD   . PRO A  1 132 ? -12.46300 -33.47300 10.88900  1.000 19.35288  ? 132 PRO A CD   1 
ATOM   1362 H  HA   . PRO A  1 132 ? -13.91900 -32.84500 13.39200  1.000 22.23137  ? 132 PRO A HA   1 
ATOM   1363 H  HB2  . PRO A  1 132 ? -14.51500 -31.66700 10.88700  1.000 22.18209  ? 132 PRO A HB2  1 
ATOM   1364 H  HB3  . PRO A  1 132 ? -13.99500 -30.92400 12.19200  1.000 22.18209  ? 132 PRO A HB3  1 
ATOM   1365 H  HG2  . PRO A  1 132 ? -12.30400 -31.43200 10.45600  1.000 23.80175  ? 132 PRO A HG2  1 
ATOM   1366 H  HG3  . PRO A  1 132 ? -11.91400 -31.76200 11.96100  1.000 23.80175  ? 132 PRO A HG3  1 
ATOM   1367 H  HD2  . PRO A  1 132 ? -12.74100 -33.63500 9.97300   1.000 23.22602  ? 132 PRO A HD2  1 
ATOM   1368 H  HD3  . PRO A  1 132 ? -11.57500 -33.83500 11.03500  1.000 23.22602  ? 132 PRO A HD3  1 
ATOM   1369 N  N    . PRO A  1 133 ? -16.37100 -33.85000 11.57800  1.000 19.38994  ? 133 PRO A N    1 
ATOM   1370 C  CA   . PRO A  1 133 ? -17.81500 -34.13400 11.75300  1.000 19.06213  ? 133 PRO A CA   1 
ATOM   1371 C  C    . PRO A  1 133 ? -18.10400 -35.02100 12.96700  1.000 20.30938  ? 133 PRO A C    1 
ATOM   1372 O  O    . PRO A  1 133 ? -18.98000 -34.72100 13.80900  1.000 21.80323  ? 133 PRO A O    1 
ATOM   1373 C  CB   . PRO A  1 133 ? -18.19900 -34.80800 10.43200  1.000 23.98326  ? 133 PRO A CB   1 
ATOM   1374 C  CG   . PRO A  1 133 ? -17.19400 -34.30900 9.42800   1.000 23.27976  ? 133 PRO A CG   1 
ATOM   1375 C  CD   . PRO A  1 133 ? -15.88500 -34.18000 10.23600  1.000 20.23746  ? 133 PRO A CD   1 
ATOM   1376 H  HA   . PRO A  1 133 ? -18.30700 -33.30300 11.83700  1.000 22.87712  ? 133 PRO A HA   1 
ATOM   1377 H  HB2  . PRO A  1 133 ? -18.14500 -35.77200 10.52700  1.000 28.78247  ? 133 PRO A HB2  1 
ATOM   1378 H  HB3  . PRO A  1 133 ? -19.09900 -34.54900 10.18000  1.000 28.78247  ? 133 PRO A HB3  1 
ATOM   1379 H  HG2  . PRO A  1 133 ? -17.09800 -34.94900 8.70600   1.000 27.93828  ? 133 PRO A HG2  1 
ATOM   1380 H  HG3  . PRO A  1 133 ? -17.47300 -33.45000 9.07500   1.000 27.93828  ? 133 PRO A HG3  1 
ATOM   1381 H  HD2  . PRO A  1 133 ? -15.39400 -35.01600 10.23900  1.000 24.28752  ? 133 PRO A HD2  1 
ATOM   1382 H  HD3  . PRO A  1 133 ? -15.32700 -33.46900 9.88300   1.000 24.28752  ? 133 PRO A HD3  1 
ATOM   1383 N  N    . SER A  1 134 ? -17.34100 -36.10300 13.10900  1.000 20.52118  ? 134 SER A N    1 
ATOM   1384 C  CA   . SER A  1 134 ? -17.47100 -36.95200 14.29300  1.000 19.31440  ? 134 SER A CA   1 
ATOM   1385 C  C    . SER A  1 134 ? -17.13600 -36.19400 15.57100  1.000 19.10402  ? 134 SER A C    1 
ATOM   1386 O  O    . SER A  1 134 ? -17.83000 -36.33600 16.58300  1.000 20.10511  ? 134 SER A O    1 
ATOM   1387 C  CB   . SER A  1 134 ? -16.53500 -38.16100 14.12800  1.000 24.68758  ? 134 SER A CB   1 
ATOM   1388 O  OG   . SER A  1 134 ? -16.54600 -38.96500 15.29000  1.000 26.57052  ? 134 SER A OG   1 
ATOM   1389 H  H    . SER A  1 134 ? -16.74900 -36.36600 12.54300  1.000 24.62798  ? 134 SER A H    1 
ATOM   1390 H  HA   . SER A  1 134 ? -18.38800 -37.25800 14.37200  1.000 23.17984  ? 134 SER A HA   1 
ATOM   1391 H  HB2  . SER A  1 134 ? -16.83500 -38.69200 13.37400  1.000 29.62766  ? 134 SER A HB2  1 
ATOM   1392 H  HB3  . SER A  1 134 ? -15.63200 -37.84300 13.97200  1.000 29.62766  ? 134 SER A HB3  1 
ATOM   1393 H  HG   . SER A  1 134 ? -15.91400 -39.51700 15.26300  1.000 31.88719  ? 134 SER A HG   1 
ATOM   1394 N  N    . ARG A  1 135 ? -16.09800 -35.37800 15.55000  1.000 20.00499  ? 135 ARG A N    1 
ATOM   1395 C  CA   . ARG A  1 135 ? -15.68700 -34.58500 16.73900  1.000 17.45903  ? 135 ARG A CA   1 
ATOM   1396 C  C    . ARG A  1 135 ? -16.84500 -33.66500 17.14600  1.000 18.27727  ? 135 ARG A C    1 
ATOM   1397 O  O    . ARG A  1 135 ? -17.09500 -33.53200 18.30900  1.000 18.15537  ? 135 ARG A O    1 
ATOM   1398 C  CB   . ARG A  1 135 ? -14.39300 -33.84000 16.44000  1.000 17.21978  ? 135 ARG A CB   1 
ATOM   1399 C  CG   . ARG A  1 135 ? -13.17000 -34.74400 16.40900  1.000 19.06228  ? 135 ARG A CG   1 
ATOM   1400 C  CD   . ARG A  1 135 ? -11.84600 -34.02100 16.24800  1.000 18.31355  ? 135 ARG A CD   1 
ATOM   1401 N  NE   . ARG A  1 135 ? -10.88600 -35.04700 15.94400  1.000 19.59381  ? 135 ARG A NE   1 
ATOM   1402 C  CZ   . ARG A  1 135 ? -10.04900 -35.58900 16.79300  1.000 19.36069  ? 135 ARG A CZ   1 
ATOM   1403 N  NH1  . ARG A  1 135 ? -9.90700  -35.13300 18.01500  1.000 18.26505  ? 135 ARG A NH1  1 
ATOM   1404 N  NH2  . ARG A  1 135 ? -9.33800  -36.62000 16.41300  1.000 20.50784  ? 135 ARG A NH2  1 
ATOM   1405 H  H    . ARG A  1 135 ? -15.57700 -35.25300 14.81300  1.000 24.00854  ? 135 ARG A H    1 
ATOM   1406 H  HA   . ARG A  1 135 ? -15.51900 -35.21300 17.47800  1.000 20.95340  ? 135 ARG A HA   1 
ATOM   1407 H  HB2  . ARG A  1 135 ? -14.48000 -33.39300 15.57200  1.000 20.66630  ? 135 ARG A HB2  1 
ATOM   1408 H  HB3  . ARG A  1 135 ? -14.26200 -33.15000 17.12400  1.000 20.66630  ? 135 ARG A HB3  1 
ATOM   1409 H  HG2  . ARG A  1 135 ? -13.14100 -35.26200 17.24100  1.000 22.87729  ? 135 ARG A HG2  1 
ATOM   1410 H  HG3  . ARG A  1 135 ? -13.26800 -35.38100 15.66900  1.000 22.87729  ? 135 ARG A HG3  1 
ATOM   1411 H  HD2  . ARG A  1 135 ? -11.89700 -33.37000 15.51500  1.000 21.97883  ? 135 ARG A HD2  1 
ATOM   1412 H  HD3  . ARG A  1 135 ? -11.60400 -33.55700 17.07700  1.000 21.97883  ? 135 ARG A HD3  1 
ATOM   1413 H  HE   . ARG A  1 135 ? -10.96800 -35.44000 15.17700  1.000 23.51513  ? 135 ARG A HE   1 
ATOM   1414 H  HH11 . ARG A  1 135 ? -10.40600 -34.46500 18.29400  1.000 21.92062  ? 135 ARG A HH11 1 
ATOM   1415 H  HH12 . ARG A  1 135 ? -9.32400  -35.50700 18.55700  1.000 21.92062  ? 135 ARG A HH12 1 
ATOM   1416 H  HH21 . ARG A  1 135 ? -9.41400  -36.92500 15.59000  1.000 24.61197  ? 135 ARG A HH21 1 
ATOM   1417 H  HH22 . ARG A  1 135 ? -8.73700  -36.96200 16.95900  1.000 24.61197  ? 135 ARG A HH22 1 
ATOM   1418 N  N    . ARG A  1 136 ? -17.53100 -33.05400 16.19500  1.000 18.29904  ? 136 ARG A N    1 
ATOM   1419 C  CA   . ARG A  1 136 ? -18.70400 -32.23100 16.49300  1.000 18.14867  ? 136 ARG A CA   1 
ATOM   1420 C  C    . ARG A  1 136 ? -19.73900 -33.00000 17.30300  1.000 19.20728  ? 136 ARG A C    1 
ATOM   1421 O  O    . ARG A  1 136 ? -20.21700 -32.51600 18.34400  1.000 18.32531  ? 136 ARG A O    1 
ATOM   1422 C  CB   . ARG A  1 136 ? -19.33400 -31.72600 15.18700  1.000 18.88941  ? 136 ARG A CB   1 
ATOM   1423 C  CG   . ARG A  1 136 ? -20.72500 -31.10400 15.37100  1.000 19.08804  ? 136 ARG A CG   1 
ATOM   1424 C  CD   . ARG A  1 136 ? -21.73800 -31.79100 14.45400  1.000 20.94003  ? 136 ARG A CD   1 
ATOM   1425 N  NE   . ARG A  1 136 ? -23.07500 -31.25000 14.65800  1.000 22.65061  ? 136 ARG A NE   1 
ATOM   1426 C  CZ   . ARG A  1 136 ? -23.87400 -31.61900 15.64300  1.000 25.42295  ? 136 ARG A CZ   1 
ATOM   1427 N  NH1  . ARG A  1 136 ? -23.57500 -32.64600 16.42000  1.000 26.82477  ? 136 ARG A NH1  1 
ATOM   1428 N  NH2  . ARG A  1 136 ? -24.98300 -30.92700 15.86500  1.000 27.43269  ? 136 ARG A NH2  1 
ATOM   1429 H  H    . ARG A  1 136 ? -17.33500 -33.09000 15.35800  1.000 21.96141  ? 136 ARG A H    1 
ATOM   1430 H  HA   . ARG A  1 136 ? -18.41500 -31.46700 17.01700  1.000 21.78097  ? 136 ARG A HA   1 
ATOM   1431 H  HB2  . ARG A  1 136 ? -18.75500 -31.04900 14.80300  1.000 22.66985  ? 136 ARG A HB2  1 
ATOM   1432 H  HB3  . ARG A  1 136 ? -19.42200 -32.47300 14.57400  1.000 22.66985  ? 136 ARG A HB3  1 
ATOM   1433 H  HG2  . ARG A  1 136 ? -21.01300 -31.21600 16.29000  1.000 22.90821  ? 136 ARG A HG2  1 
ATOM   1434 H  HG3  . ARG A  1 136 ? -20.69300 -30.16100 15.14500  1.000 22.90821  ? 136 ARG A HG3  1 
ATOM   1435 H  HD2  . ARG A  1 136 ? -21.48500 -31.64800 13.52900  1.000 25.13060  ? 136 ARG A HD2  1 
ATOM   1436 H  HD3  . ARG A  1 136 ? -21.75800 -32.74100 14.65000  1.000 25.13060  ? 136 ARG A HD3  1 
ATOM   1437 H  HE   . ARG A  1 136 ? -23.36100 -30.65600 14.10500  1.000 27.18329  ? 136 ARG A HE   1 
ATOM   1438 H  HH11 . ARG A  1 136 ? -22.84800 -33.08700 16.28900  1.000 32.19228  ? 136 ARG A HH11 1 
ATOM   1439 H  HH12 . ARG A  1 136 ? -24.10600 -32.87200 17.05700  1.000 32.19228  ? 136 ARG A HH12 1 
ATOM   1440 H  HH21 . ARG A  1 136 ? -25.17300 -30.24900 15.37100  1.000 32.92179  ? 136 ARG A HH21 1 
ATOM   1441 H  HH22 . ARG A  1 136 ? -25.51200 -31.15500 16.50200  1.000 32.92179  ? 136 ARG A HH22 1 
ATOM   1442 N  N    . ASP A  1 137 ? -20.06000 -34.21800 16.85800  1.000 19.36044  ? 137 ASP A N    1 
ATOM   1443 C  CA   . ASP A  1 137 ? -21.03300 -35.04500 17.58600  1.000 20.87993  ? 137 ASP A CA   1 
ATOM   1444 C  C    . ASP A  1 137 ? -20.54600 -35.35100 19.00400  1.000 20.21039  ? 137 ASP A C    1 
ATOM   1445 O  O    . ASP A  1 137 ? -21.34400 -35.42400 19.95500  1.000 20.79690  ? 137 ASP A O    1 
ATOM   1446 C  CB   . ASP A  1 137 ? -21.24800 -36.37200 16.85700  1.000 21.91681  ? 137 ASP A CB   1 
ATOM   1447 C  CG   . ASP A  1 137 ? -22.00400 -36.23000 15.56700  1.000 33.17755  ? 137 ASP A CG   1 
ATOM   1448 O  OD1  . ASP A  1 137 ? -22.62100 -35.18000 15.34100  1.000 25.59494  ? 137 ASP A OD1  1 
ATOM   1449 O  OD2  . ASP A  1 137 ? -21.95700 -37.19700 14.79000  1.000 37.58025  ? 137 ASP A OD2  1 
ATOM   1450 H  H    . ASP A  1 137 ? -19.73600 -34.58500 16.15100  1.000 23.23508  ? 137 ASP A H    1 
ATOM   1451 H  HA   . ASP A  1 137 ? -21.87100 -34.55700 17.62500  1.000 25.05848  ? 137 ASP A HA   1 
ATOM   1452 H  HB2  . ASP A  1 137 ? -20.38300 -36.76100 16.65300  1.000 26.30273  ? 137 ASP A HB2  1 
ATOM   1453 H  HB3  . ASP A  1 137 ? -21.75200 -36.96800 17.43300  1.000 26.30273  ? 137 ASP A HB3  1 
ATOM   1454 N  N    . GLN A  1 138 ? -19.24300 -35.56400 19.16600  1.000 17.84442  ? 138 GLN A N    1 
ATOM   1455 C  CA   . GLN A  1 138 ? -18.70200 -35.94700 20.47300  1.000 16.82164  ? 138 GLN A CA   1 
ATOM   1456 C  C    . GLN A  1 138 ? -18.66600 -34.78100 21.43300  1.000 17.58973  ? 138 GLN A C    1 
ATOM   1457 O  O    . GLN A  1 138 ? -18.88400 -34.96200 22.64000  1.000 17.29065  ? 138 GLN A O    1 
ATOM   1458 C  CB   . GLN A  1 138 ? -17.31900 -36.55400 20.27500  1.000 18.55285  ? 138 GLN A CB   1 
ATOM   1459 C  CG   . GLN A  1 138 ? -17.40500 -37.84200 19.43900  1.000 19.63338  ? 138 GLN A CG   1 
ATOM   1460 C  CD   . GLN A  1 138 ? -16.07600 -38.51500 19.27600  1.000 20.99073  ? 138 GLN A CD   1 
ATOM   1461 O  OE1  . GLN A  1 138 ? -15.44400 -38.90900 20.23300  1.000 21.98845  ? 138 GLN A OE1  1 
ATOM   1462 N  NE2  . GLN A  1 138 ? -15.66300 -38.70200 18.03900  1.000 21.98175  ? 138 GLN A NE2  1 
ATOM   1463 H  H    . GLN A  1 138 ? -18.65300 -35.49500 18.54400  1.000 21.41587  ? 138 GLN A H    1 
ATOM   1464 H  HA   . GLN A  1 138 ? -19.27500 -36.61800 20.87700  1.000 20.18854  ? 138 GLN A HA   1 
ATOM   1465 H  HB2  . GLN A  1 138 ? -16.75200 -35.92000 19.80900  1.000 22.26598  ? 138 GLN A HB2  1 
ATOM   1466 H  HB3  . GLN A  1 138 ? -16.93500 -36.77100 21.13900  1.000 22.26598  ? 138 GLN A HB3  1 
ATOM   1467 H  HG2  . GLN A  1 138 ? -18.00500 -38.46500 19.87800  1.000 23.56262  ? 138 GLN A HG2  1 
ATOM   1468 H  HG3  . GLN A  1 138 ? -17.74200 -37.62400 18.55600  1.000 23.56262  ? 138 GLN A HG3  1 
ATOM   1469 H  HE21 . GLN A  1 138 ? -16.15000 -38.44300 17.37900  1.000 26.38066  ? 138 GLN A HE21 1 
ATOM   1470 H  HE22 . GLN A  1 138 ? -14.90700 -39.08400 17.89100  1.000 26.38066  ? 138 GLN A HE22 1 
ATOM   1471 N  N    . ILE A  1 139 ? -18.41300 -33.57300 20.93700  1.000 17.08026  ? 139 ILE A N    1 
ATOM   1472 C  CA   . ILE A  1 139 ? -18.54500 -32.38500 21.78000  1.000 16.43540  ? 139 ILE A CA   1 
ATOM   1473 C  C    . ILE A  1 139 ? -19.98300 -32.27400 22.28900  1.000 16.80557  ? 139 ILE A C    1 
ATOM   1474 O  O    . ILE A  1 139 ? -20.22900 -32.00700 23.47300  1.000 16.46627  ? 139 ILE A O    1 
ATOM   1475 C  CB   . ILE A  1 139 ? -18.12900 -31.10700 21.02100  1.000 15.76320  ? 139 ILE A CB   1 
ATOM   1476 C  CG1  . ILE A  1 139 ? -16.68000 -31.16200 20.53400  1.000 16.77576  ? 139 ILE A CG1  1 
ATOM   1477 C  CG2  . ILE A  1 139 ? -18.35700 -29.90200 21.87900  1.000 15.56020  ? 139 ILE A CG2  1 
ATOM   1478 C  CD1  . ILE A  1 139 ? -16.40400 -30.16400 19.44800  1.000 17.61684  ? 139 ILE A CD1  1 
ATOM   1479 H  H    . ILE A  1 139 ? -18.16600 -33.41400 20.12900  1.000 20.49887  ? 139 ILE A H    1 
ATOM   1480 H  HA   . ILE A  1 139 ? -17.94600 -32.48400 22.53600  1.000 19.72504  ? 139 ILE A HA   1 
ATOM   1481 H  HB   . ILE A  1 139 ? -18.68700 -31.04700 20.23000  1.000 18.91840  ? 139 ILE A HB   1 
ATOM   1482 H  HG12 . ILE A  1 139 ? -16.08800 -30.97100 21.27800  1.000 20.13347  ? 139 ILE A HG12 1 
ATOM   1483 H  HG13 . ILE A  1 139 ? -16.49700 -32.04800 20.18400  1.000 20.13347  ? 139 ILE A HG13 1 
ATOM   1484 H  HG21 . ILE A  1 139 ? -17.94600 -29.13100 21.45600  1.000 18.67480  ? 139 ILE A HG21 1 
ATOM   1485 H  HG22 . ILE A  1 139 ? -19.31100 -29.75700 21.97300  1.000 18.67480  ? 139 ILE A HG22 1 
ATOM   1486 H  HG23 . ILE A  1 139 ? -17.95800 -30.05400 22.74900  1.000 18.67480  ? 139 ILE A HG23 1 
ATOM   1487 H  HD11 . ILE A  1 139 ? -15.55700 -30.38000 19.02700  1.000 21.14277  ? 139 ILE A HD11 1 
ATOM   1488 H  HD12 . ILE A  1 139 ? -17.11800 -30.20400 18.79300  1.000 21.14277  ? 139 ILE A HD12 1 
ATOM   1489 H  HD13 . ILE A  1 139 ? -16.36200 -29.27600 19.83700  1.000 21.14277  ? 139 ILE A HD13 1 
ATOM   1490 N  N    . GLU A  1 140 ? -20.95200 -32.41400 21.38700  1.000 18.16247  ? 140 GLU A N    1 
ATOM   1491 C  CA   . GLU A  1 140 ? -22.36400 -32.33000 21.76300  1.000 17.71401  ? 140 GLU A CA   1 
ATOM   1492 C  C    . GLU A  1 140 ? -22.70800 -33.38200 22.80800  1.000 17.93377  ? 140 GLU A C    1 
ATOM   1493 O  O    . GLU A  1 140 ? -23.35800 -33.07800 23.81900  1.000 18.87338  ? 140 GLU A O    1 
ATOM   1494 C  CB   . GLU A  1 140 ? -23.21300 -32.49400 20.50900  1.000 19.56182  ? 140 GLU A CB   1 
ATOM   1495 C  CG   . GLU A  1 140 ? -24.72600 -32.47400 20.75400  1.000 19.99317  ? 140 GLU A CG   1 
ATOM   1496 C  CD   . GLU A  1 140 ? -25.50500 -32.59600 19.44800  1.000 27.45297  ? 140 GLU A CD   1 
ATOM   1497 O  OE1  . GLU A  1 140 ? -25.17800 -33.46600 18.63800  1.000 28.37475  ? 140 GLU A OE1  1 
ATOM   1498 O  OE2  . GLU A  1 140 ? -26.47800 -31.84600 19.28000  1.000 45.75692  ? 140 GLU A OE2  1 
ATOM   1499 H  H    . GLU A  1 140 ? -20.82100 -32.55800 20.55000  1.000 21.79753  ? 140 GLU A H    1 
ATOM   1500 H  HA   . GLU A  1 140 ? -22.55500 -31.46200 22.15300  1.000 21.25937  ? 140 GLU A HA   1 
ATOM   1501 H  HB2  . GLU A  1 140 ? -23.00700 -31.76800 19.89900  1.000 23.47675  ? 140 GLU A HB2  1 
ATOM   1502 H  HB3  . GLU A  1 140 ? -22.99500 -33.34500 20.09800  1.000 23.47675  ? 140 GLU A HB3  1 
ATOM   1503 H  HG2  . GLU A  1 140 ? -24.96900 -33.22000 21.32500  1.000 23.99437  ? 140 GLU A HG2  1 
ATOM   1504 H  HG3  . GLU A  1 140 ? -24.97100 -31.63800 21.17900  1.000 23.99437  ? 140 GLU A HG3  1 
ATOM   1505 N  N    . ALA A  1 141 ? -22.25600 -34.61900 22.60300  1.000 17.92338  ? 141 ALA A N    1 
ATOM   1506 C  CA   . ALA A  1 141 ? -22.51800 -35.68100 23.58100  1.000 17.60011  ? 141 ALA A CA   1 
ATOM   1507 C  C    . ALA A  1 141 ? -21.87500 -35.38100 24.93300  1.000 17.96243  ? 141 ALA A C    1 
ATOM   1508 O  O    . ALA A  1 141 ? -22.46000 -35.66800 25.99400  1.000 18.90981  ? 141 ALA A O    1 
ATOM   1509 C  CB   . ALA A  1 141 ? -22.00900 -37.01500 23.02700  1.000 20.91989  ? 141 ALA A CB   1 
ATOM   1510 H  H    . ALA A  1 141 ? -21.80200 -34.87000 21.91700  1.000 21.51062  ? 141 ALA A H    1 
ATOM   1511 H  HA   . ALA A  1 141 ? -23.47500 -35.74500 23.72600  1.000 21.12269  ? 141 ALA A HA   1 
ATOM   1512 H  HB1  . ALA A  1 141 ? -22.16600 -37.71100 23.68500  1.000 25.10643  ? 141 ALA A HB1  1 
ATOM   1513 H  HB2  . ALA A  1 141 ? -22.48800 -37.22000 22.20900  1.000 25.10643  ? 141 ALA A HB2  1 
ATOM   1514 H  HB3  . ALA A  1 141 ? -21.06000 -36.94000 22.84500  1.000 25.10643  ? 141 ALA A HB3  1 
ATOM   1515 N  N    . ALA A  1 142 ? -20.66800 -34.82500 24.92800  1.000 18.06553  ? 142 ALA A N    1 
ATOM   1516 C  CA   . ALA A  1 142 ? -19.97200 -34.51000 26.16900  1.000 16.38298  ? 142 ALA A CA   1 
ATOM   1517 C  C    . ALA A  1 142 ? -20.67500 -33.39500 26.93600  1.000 15.50776  ? 142 ALA A C    1 
ATOM   1518 O  O    . ALA A  1 142 ? -20.77400 -33.45200 28.16800  1.000 16.95091  ? 142 ALA A O    1 
ATOM   1519 C  CB   . ALA A  1 142 ? -18.52700 -34.16400 25.82400  1.000 16.25531  ? 142 ALA A CB   1 
ATOM   1520 H  H    . ALA A  1 142 ? -20.22900 -34.62000 24.21800  1.000 21.68120  ? 142 ALA A H    1 
ATOM   1521 H  HA   . ALA A  1 142 ? -19.96500 -35.27500 26.76500  1.000 19.66214  ? 142 ALA A HA   1 
ATOM   1522 H  HB1  . ALA A  1 142 ? -18.08300 -33.83300 26.62100  1.000 19.50894  ? 142 ALA A HB1  1 
ATOM   1523 H  HB2  . ALA A  1 142 ? -18.07900 -34.96300 25.50400  1.000 19.50894  ? 142 ALA A HB2  1 
ATOM   1524 H  HB3  . ALA A  1 142 ? -18.52100 -33.48200 25.13400  1.000 19.50894  ? 142 ALA A HB3  1 
ATOM   1525 N  N    . LEU A  1 143 ? -21.17500 -32.37800 26.22700  1.000 16.39727  ? 143 LEU A N    1 
ATOM   1526 C  CA   . LEU A  1 143 ? -21.95000 -31.33700 26.90100  1.000 16.28082  ? 143 LEU A CA   1 
ATOM   1527 C  C    . LEU A  1 143 ? -23.24500 -31.90100 27.46800  1.000 16.41121  ? 143 LEU A C    1 
ATOM   1528 O  O    . LEU A  1 143 ? -23.62600 -31.55700 28.60900  1.000 17.71549  ? 143 LEU A O    1 
ATOM   1529 C  CB   . LEU A  1 143 ? -22.22100 -30.18300 25.92700  1.000 17.47793  ? 143 LEU A CB   1 
ATOM   1530 C  CG   . LEU A  1 143 ? -21.02100 -29.30100 25.62300  1.000 16.64694  ? 143 LEU A CG   1 
ATOM   1531 C  CD1  . LEU A  1 143 ? -21.32800 -28.42200 24.43000  1.000 18.80687  ? 143 LEU A CD1  1 
ATOM   1532 C  CD2  . LEU A  1 143 ? -20.61500 -28.46900 26.81000  1.000 15.83663  ? 143 LEU A CD2  1 
ATOM   1533 H  H    . LEU A  1 143 ? -21.08200 -32.27100 25.37900  1.000 19.67929  ? 143 LEU A H    1 
ATOM   1534 H  HA   . LEU A  1 143 ? -21.43800 -30.98100 27.64400  1.000 19.53955  ? 143 LEU A HA   1 
ATOM   1535 H  HB2  . LEU A  1 143 ? -22.52700 -30.55800 25.08600  1.000 20.97608  ? 143 LEU A HB2  1 
ATOM   1536 H  HB3  . LEU A  1 143 ? -22.91000 -29.61700 26.30700  1.000 20.97608  ? 143 LEU A HB3  1 
ATOM   1537 H  HG   . LEU A  1 143 ? -20.26200 -29.86800 25.41400  1.000 19.97888  ? 143 LEU A HG   1 
ATOM   1538 H  HD11 . LEU A  1 143 ? -20.54800 -27.88400 24.22500  1.000 22.57080  ? 143 LEU A HD11 1 
ATOM   1539 H  HD12 . LEU A  1 143 ? -21.55000 -28.98600 23.67200  1.000 22.57080  ? 143 LEU A HD12 1 
ATOM   1540 H  HD13 . LEU A  1 143 ? -22.07900 -27.84800 24.64500  1.000 22.57080  ? 143 LEU A HD13 1 
ATOM   1541 H  HD21 . LEU A  1 143 ? -19.87400 -27.89700 26.55600  1.000 19.00652  ? 143 LEU A HD21 1 
ATOM   1542 H  HD22 . LEU A  1 143 ? -21.37000 -27.92800 27.08900  1.000 19.00652  ? 143 LEU A HD22 1 
ATOM   1543 H  HD23 . LEU A  1 143 ? -20.34600 -29.05900 27.53200  1.000 19.00652  ? 143 LEU A HD23 1 
ATOM   1544 N  N    . GLU A  1 144 ? -23.91000 -32.78900 26.72300  1.000 17.76554  ? 144 GLU A N    1 
ATOM   1545 C  CA   . GLU A  1 144 ? -25.11800 -33.43000 27.24400  1.000 18.52800  ? 144 GLU A CA   1 
ATOM   1546 C  C    . GLU A  1 144 ? -24.79600 -34.21800 28.50400  1.000 18.70184  ? 144 GLU A C    1 
ATOM   1547 O  O    . GLU A  1 144 ? -25.58000 -34.23400 29.46900  1.000 18.88800  ? 144 GLU A O    1 
ATOM   1548 C  CB   . GLU A  1 144 ? -25.73200 -34.32100 26.17500  1.000 21.79794  ? 144 GLU A CB   1 
ATOM   1549 C  CG   . GLU A  1 144 ? -26.35300 -33.53500 25.02100  1.000 27.18158  ? 144 GLU A CG   1 
ATOM   1550 C  CD   . GLU A  1 144 ? -26.81700 -34.39000 23.85700  1.000 56.54470  ? 144 GLU A CD   1 
ATOM   1551 O  OE1  . GLU A  1 144 ? -26.50100 -35.60100 23.83700  1.000 51.15508  ? 144 GLU A OE1  1 
ATOM   1552 O  OE2  . GLU A  1 144 ? -27.48800 -33.84100 22.95400  1.000 60.44868  ? 144 GLU A OE2  1 
ATOM   1553 H  H    . GLU A  1 144 ? -23.68800 -33.03200 25.92800  1.000 21.32121  ? 144 GLU A H    1 
ATOM   1554 H  HA   . GLU A  1 144 ? -25.77700 -32.75600 27.47100  1.000 22.23616  ? 144 GLU A HA   1 
ATOM   1555 H  HB2  . GLU A  1 144 ? -25.04100 -34.89400 25.80800  1.000 26.16009  ? 144 GLU A HB2  1 
ATOM   1556 H  HB3  . GLU A  1 144 ? -26.43000 -34.86000 26.57900  1.000 26.16009  ? 144 GLU A HB3  1 
ATOM   1557 H  HG2  . GLU A  1 144 ? -27.12500 -33.05200 25.35600  1.000 32.62046  ? 144 GLU A HG2  1 
ATOM   1558 H  HG3  . GLU A  1 144 ? -25.69300 -32.91100 24.68100  1.000 32.62046  ? 144 GLU A HG3  1 
ATOM   1559 N  N    . TYR A  1 145 ? -23.64500 -34.88700 28.51300  1.000 18.71316  ? 145 TYR A N    1 
ATOM   1560 C  CA   . TYR A  1 145 ? -23.23400 -35.64200 29.69800  1.000 18.07045  ? 145 TYR A CA   1 
ATOM   1561 C  C    . TYR A  1 145 ? -23.08100 -34.73400 30.91500  1.000 18.63788  ? 145 TYR A C    1 
ATOM   1562 O  O    . TYR A  1 145 ? -23.54100 -35.08300 32.01200  1.000 19.06978  ? 145 TYR A O    1 
ATOM   1563 C  CB   . TYR A  1 145 ? -21.91400 -36.36200 29.38400  1.000 18.29947  ? 145 TYR A CB   1 
ATOM   1564 C  CG   . TYR A  1 145 ? -21.35000 -37.08700 30.56700  1.000 19.46493  ? 145 TYR A CG   1 
ATOM   1565 C  CD1  . TYR A  1 145 ? -21.86400 -38.29900 30.98500  1.000 21.23530  ? 145 TYR A CD1  1 
ATOM   1566 C  CD2  . TYR A  1 145 ? -20.32100 -36.54000 31.28200  1.000 20.93255  ? 145 TYR A CD2  1 
ATOM   1567 C  CE1  . TYR A  1 145 ? -21.35100 -38.94300 32.10800  1.000 24.07217  ? 145 TYR A CE1  1 
ATOM   1568 C  CE2  . TYR A  1 145 ? -19.80600 -37.18700 32.39400  1.000 22.19127  ? 145 TYR A CE2  1 
ATOM   1569 C  CZ   . TYR A  1 145 ? -20.30100 -38.38700 32.76500  1.000 22.31486  ? 145 TYR A CZ   1 
ATOM   1570 O  OH   . TYR A  1 145 ? -19.78600 -39.03100 33.88300  1.000 28.66079  ? 145 TYR A OH   1 
ATOM   1571 H  H    . TYR A  1 145 ? -23.09000 -34.92000 27.85700  1.000 22.45836  ? 145 TYR A H    1 
ATOM   1572 H  HA   . TYR A  1 145 ? -23.91100 -36.30100 29.91700  1.000 21.68710  ? 145 TYR A HA   1 
ATOM   1573 H  HB2  . TYR A  1 145 ? -22.07000 -37.01100 28.68000  1.000 21.96192  ? 145 TYR A HB2  1 
ATOM   1574 H  HB3  . TYR A  1 145 ? -21.26000 -35.70800 29.09200  1.000 21.96192  ? 145 TYR A HB3  1 
ATOM   1575 H  HD1  . TYR A  1 145 ? -22.56200 -38.69000 30.51000  1.000 25.48492  ? 145 TYR A HD1  1 
ATOM   1576 H  HD2  . TYR A  1 145 ? -19.96300 -35.72300 31.01900  1.000 25.12162  ? 145 TYR A HD2  1 
ATOM   1577 H  HE1  . TYR A  1 145 ? -21.72300 -39.74200 32.40400  1.000 28.88916  ? 145 TYR A HE1  1 
ATOM   1578 H  HE2  . TYR A  1 145 ? -19.11900 -36.79500 32.88300  1.000 26.63209  ? 145 TYR A HE2  1 
ATOM   1579 H  HH   . TYR A  1 145 ? -19.17600 -38.56700 34.22700  1.000 34.39551  ? 145 TYR A HH   1 
ATOM   1580 N  N    . LEU A  1 146 ? -22.45400 -33.57000 30.75200  1.000 17.17851  ? 146 LEU A N    1 
ATOM   1581 C  CA   . LEU A  1 146 ? -22.28700 -32.67200 31.88800  1.000 16.81595  ? 146 LEU A CA   1 
ATOM   1582 C  C    . LEU A  1 146 ? -23.63600 -32.18300 32.40100  1.000 17.01940  ? 146 LEU A C    1 
ATOM   1583 O  O    . LEU A  1 146 ? -23.85200 -32.09900 33.60900  1.000 17.70979  ? 146 LEU A O    1 
ATOM   1584 C  CB   . LEU A  1 146 ? -21.39800 -31.49500 31.49300  1.000 17.38164  ? 146 LEU A CB   1 
ATOM   1585 C  CG   . LEU A  1 146 ? -19.95700 -31.84200 31.18500  1.000 15.81887  ? 146 LEU A CG   1 
ATOM   1586 C  CD1  . LEU A  1 146 ? -19.20200 -30.58400 30.69900  1.000 17.86299  ? 146 LEU A CD1  1 
ATOM   1587 C  CD2  . LEU A  1 146 ? -19.24100 -32.48000 32.36900  1.000 17.27794  ? 146 LEU A CD2  1 
ATOM   1588 H  H    . LEU A  1 146 ? -22.12400 -33.28500 30.01100  1.000 20.61677  ? 146 LEU A H    1 
ATOM   1589 H  HA   . LEU A  1 146 ? -21.84700 -33.14800 32.60900  1.000 20.18171  ? 146 LEU A HA   1 
ATOM   1590 H  HB2  . LEU A  1 146 ? -21.77300 -31.08400 30.69800  1.000 20.86053  ? 146 LEU A HB2  1 
ATOM   1591 H  HB3  . LEU A  1 146 ? -21.39300 -30.85900 32.22500  1.000 20.86053  ? 146 LEU A HB3  1 
ATOM   1592 H  HG   . LEU A  1 146 ? -19.95400 -32.50500 30.47700  1.000 18.98520  ? 146 LEU A HG   1 
ATOM   1593 H  HD11 . LEU A  1 146 ? -18.28500 -30.82600 30.49400  1.000 21.43815  ? 146 LEU A HD11 1 
ATOM   1594 H  HD12 . LEU A  1 146 ? -19.63900 -30.24000 29.90500  1.000 21.43815  ? 146 LEU A HD12 1 
ATOM   1595 H  HD13 . LEU A  1 146 ? -19.21800 -29.91500 31.40200  1.000 21.43815  ? 146 LEU A HD13 1 
ATOM   1596 H  HD21 . LEU A  1 146 ? -18.29100 -32.51800 32.18100  1.000 20.73609  ? 146 LEU A HD21 1 
ATOM   1597 H  HD22 . LEU A  1 146 ? -19.40100 -31.94300 33.16100  1.000 20.73609  ? 146 LEU A HD22 1 
ATOM   1598 H  HD23 . LEU A  1 146 ? -19.58800 -33.37700 32.50200  1.000 20.73609  ? 146 LEU A HD23 1 
ATOM   1599 N  N    . VAL A  1 147 ? -24.55200 -31.85500 31.48500  1.000 17.18922  ? 147 VAL A N    1 
ATOM   1600 C  CA   . VAL A  1 147 ? -25.89200 -31.41600 31.89000  1.000 18.19880  ? 147 VAL A CA   1 
ATOM   1601 C  C    . VAL A  1 147 ? -26.57600 -32.51300 32.67200  1.000 20.31055  ? 147 VAL A C    1 
ATOM   1602 O  O    . VAL A  1 147 ? -27.18300 -32.26900 33.74100  1.000 20.77556  ? 147 VAL A O    1 
ATOM   1603 C  CB   . VAL A  1 147 ? -26.70000 -30.98500 30.65800  1.000 19.32037  ? 147 VAL A CB   1 
ATOM   1604 C  CG1  . VAL A  1 147 ? -28.17500 -30.87600 30.99400  1.000 21.36721  ? 147 VAL A CG1  1 
ATOM   1605 C  CG2  . VAL A  1 147 ? -26.17800 -29.67700 30.08700  1.000 19.61810  ? 147 VAL A CG2  1 
ATOM   1606 H  H    . VAL A  1 147 ? -24.42600 -31.87600 30.63400  1.000 20.62963  ? 147 VAL A H    1 
ATOM   1607 H  HA   . VAL A  1 147 ? -25.81500 -30.64500 32.47300  1.000 21.84112  ? 147 VAL A HA   1 
ATOM   1608 H  HB   . VAL A  1 147 ? -26.59800 -31.66500 29.97400  1.000 23.18700  ? 147 VAL A HB   1 
ATOM   1609 H  HG11 . VAL A  1 147 ? -28.62300 -30.37700 30.29200  1.000 25.64321  ? 147 VAL A HG11 1 
ATOM   1610 H  HG12 . VAL A  1 147 ? -28.55100 -31.76700 31.05800  1.000 25.64321  ? 147 VAL A HG12 1 
ATOM   1611 H  HG13 . VAL A  1 147 ? -28.27300 -30.41400 31.84200  1.000 25.64321  ? 147 VAL A HG13 1 
ATOM   1612 H  HG21 . VAL A  1 147 ? -26.71300 -29.43300 29.31600  1.000 23.54428  ? 147 VAL A HG21 1 
ATOM   1613 H  HG22 . VAL A  1 147 ? -26.24200 -28.98800 30.76600  1.000 23.54428  ? 147 VAL A HG22 1 
ATOM   1614 H  HG23 . VAL A  1 147 ? -25.25200 -29.79600 29.82300  1.000 23.54428  ? 147 VAL A HG23 1 
ATOM   1615 N  N    . ASP A  1 148 ? -26.49100 -33.74900 32.16000  1.000 19.64931  ? 148 ASP A N    1 
ATOM   1616 C  CA   . ASP A  1 148 ? -27.14300 -34.86700 32.83200  1.000 20.13816  ? 148 ASP A CA   1 
ATOM   1617 C  C    . ASP A  1 148 ? -26.53200 -35.15100 34.19800  1.000 20.44045  ? 148 ASP A C    1 
ATOM   1618 O  O    . ASP A  1 148 ? -27.25900 -35.45200 35.14200  1.000 22.29475  ? 148 ASP A O    1 
ATOM   1619 C  CB   . ASP A  1 148 ? -27.07900 -36.10600 31.93900  1.000 22.24103  ? 148 ASP A CB   1 
ATOM   1620 C  CG   . ASP A  1 148 ? -27.88200 -37.27500 32.49000  1.000 47.12648  ? 148 ASP A CG   1 
ATOM   1621 O  OD1  . ASP A  1 148 ? -29.12000 -37.15100 32.63600  1.000 51.40353  ? 148 ASP A OD1  1 
ATOM   1622 O  OD2  . ASP A  1 148 ? -27.26500 -38.32200 32.77000  1.000 56.27673  ? 148 ASP A OD2  1 
ATOM   1623 H  H    . ASP A  1 148 ? -26.07000 -33.95800 31.44000  1.000 23.58173  ? 148 ASP A H    1 
ATOM   1624 H  HA   . ASP A  1 148 ? -28.07500 -34.64100 32.97900  1.000 24.16836  ? 148 ASP A HA   1 
ATOM   1625 H  HB2  . ASP A  1 148 ? -27.43700 -35.88300 31.06500  1.000 26.69180  ? 148 ASP A HB2  1 
ATOM   1626 H  HB3  . ASP A  1 148 ? -26.15500 -36.38900 31.85700  1.000 26.69180  ? 148 ASP A HB3  1 
ATOM   1627 N  N    . GLN A  1 149 ? -25.20900 -35.12300 34.30800  1.000 19.76881  ? 149 GLN A N    1 
ATOM   1628 C  CA   . GLN A  1 149 ? -24.58100 -35.39700 35.60100  1.000 18.98843  ? 149 GLN A CA   1 
ATOM   1629 C  C    . GLN A  1 149 ? -24.93900 -34.34400 36.64600  1.000 20.38170  ? 149 GLN A C    1 
ATOM   1630 O  O    . GLN A  1 149 ? -25.09400 -34.67400 37.82700  1.000 20.14746  ? 149 GLN A O    1 
ATOM   1631 C  CB   . GLN A  1 149 ? -23.08800 -35.50600 35.42900  1.000 19.25286  ? 149 GLN A CB   1 
ATOM   1632 C  CG   . GLN A  1 149 ? -22.64300 -36.72100 34.65300  1.000 21.06042  ? 149 GLN A CG   1 
ATOM   1633 C  CD   . GLN A  1 149 ? -23.00800 -38.01700 35.29400  1.000 26.26890  ? 149 GLN A CD   1 
ATOM   1634 O  OE1  . GLN A  1 149 ? -22.55300 -38.33000 36.39400  1.000 26.40281  ? 149 GLN A OE1  1 
ATOM   1635 N  NE2  . GLN A  1 149 ? -23.89300 -38.76300 34.65000  1.000 30.24476  ? 149 GLN A NE2  1 
ATOM   1636 H  H    . GLN A  1 149 ? -24.66200 -34.95300 33.66600  1.000 23.72514  ? 149 GLN A H    1 
ATOM   1637 H  HA   . GLN A  1 149 ? -24.90400 -36.24900 35.93300  1.000 22.78868  ? 149 GLN A HA   1 
ATOM   1638 H  HB2  . GLN A  1 149 ? -22.77100 -34.72100 34.95500  1.000 23.10599  ? 149 GLN A HB2  1 
ATOM   1639 H  HB3  . GLN A  1 149 ? -22.67700 -35.55100 36.30700  1.000 23.10599  ? 149 GLN A HB3  1 
ATOM   1640 H  HG2  . GLN A  1 149 ? -23.05800 -36.69900 33.77600  1.000 25.27506  ? 149 GLN A HG2  1 
ATOM   1641 H  HG3  . GLN A  1 149 ? -21.67800 -36.69700 34.56400  1.000 25.27506  ? 149 GLN A HG3  1 
ATOM   1642 H  HE21 . GLN A  1 149 ? -24.22300 -38.49100 33.90500  1.000 36.29627  ? 149 GLN A HE21 1 
ATOM   1643 H  HE22 . GLN A  1 149 ? -24.13700 -39.52000 34.97800  1.000 36.29627  ? 149 GLN A HE22 1 
ATOM   1644 N  N    . SER A  1 150 ? -25.08500 -33.08300 36.23500  1.000 18.94706  ? 150 SER A N    1 
ATOM   1645 C  CA   . SER A  1 150 ? -25.53600 -32.02600 37.13300  1.000 17.73525  ? 150 SER A CA   1 
ATOM   1646 C  C    . SER A  1 150 ? -26.91200 -32.34000 37.71400  1.000 19.86207  ? 150 SER A C    1 
ATOM   1647 O  O    . SER A  1 150 ? -27.24300 -31.86300 38.82000  1.000 21.26523  ? 150 SER A O    1 
ATOM   1648 C  CB   . SER A  1 150 ? -25.51700 -30.69400 36.41000  1.000 20.13036  ? 150 SER A CB   1 
ATOM   1649 O  OG   . SER A  1 150 ? -25.80800 -29.63200 37.29800  1.000 20.28398  ? 150 SER A OG   1 
ATOM   1650 H  H    . SER A  1 150 ? -24.92700 -32.81200 35.43400  1.000 22.73903  ? 150 SER A H    1 
ATOM   1651 H  HA   . SER A  1 150 ? -24.92500 -31.94000 37.88100  1.000 21.28486  ? 150 SER A HA   1 
ATOM   1652 H  HB2  . SER A  1 150 ? -24.63500 -30.55400 36.03000  1.000 24.15899  ? 150 SER A HB2  1 
ATOM   1653 H  HB3  . SER A  1 150 ? -26.18300 -30.70700 35.70600  1.000 24.15899  ? 150 SER A HB3  1 
ATOM   1654 H  HG   . SER A  1 150 ? -26.61300 -29.66800 37.53500  1.000 24.34334  ? 150 SER A HG   1 
ATOM   1655 N  N    . ASN A  1 151 ? -27.68800 -33.19400 37.04900  1.000 20.59410  ? 151 ASN A N    1 
ATOM   1656 C  CA   . ASN A  1 151 ? -28.99000 -33.61700 37.55000  1.000 21.18291  ? 151 ASN A CA   1 
ATOM   1657 C  C    . ASN A  1 151 ? -28.97600 -34.95800 38.25900  1.000 26.67453  ? 151 ASN A C    1 
ATOM   1658 O  O    . ASN A  1 151 ? -30.04100 -35.44200 38.66900  1.000 31.32774  ? 151 ASN A O    1 
ATOM   1659 C  CB   . ASN A  1 151 ? -29.99100 -33.61900 36.39200  1.000 26.26256  ? 151 ASN A CB   1 
ATOM   1660 C  CG   . ASN A  1 151 ? -30.30500 -32.22700 35.92700  1.000 32.35781  ? 151 ASN A CG   1 
ATOM   1661 O  OD1  . ASN A  1 151 ? -30.46300 -31.31200 36.74200  1.000 34.14860  ? 151 ASN A OD1  1 
ATOM   1662 N  ND2  . ASN A  1 151 ? -30.32800 -32.03700 34.62800  1.000 37.90078  ? 151 ASN A ND2  1 
ATOM   1663 H  H    . ASN A  1 151 ? -27.47700 -33.54700 36.29400  1.000 24.71548  ? 151 ASN A H    1 
ATOM   1664 H  HA   . ASN A  1 151 ? -29.28800 -32.97600 38.21500  1.000 25.42205  ? 151 ASN A HA   1 
ATOM   1665 H  HB2  . ASN A  1 151 ? -29.61600 -34.11200 35.64600  1.000 31.51763  ? 151 ASN A HB2  1 
ATOM   1666 H  HB3  . ASN A  1 151 ? -30.81700 -34.03700 36.68400  1.000 31.51763  ? 151 ASN A HB3  1 
ATOM   1667 H  HD21 . ASN A  1 151 ? -30.50300 -31.25700 34.31000  1.000 45.48350  ? 151 ASN A HD21 1 
ATOM   1668 H  HD22 . ASN A  1 151 ? -30.16700 -32.69200 34.09400  1.000 45.48350  ? 151 ASN A HD22 1 
ATOM   1669 N  N    . SER A  1 152 ? -27.81700 -35.54300 38.48300  1.000 21.64209  ? 152 SER A N    1 
ATOM   1670 C  CA   . SER A  1 152 ? -27.72100 -36.85000 39.11200  1.000 21.29180  ? 152 SER A CA   1 
ATOM   1671 C  C    . SER A  1 152 ? -27.29500 -36.70100 40.56800  1.000 23.66004  ? 152 SER A C    1 
ATOM   1672 O  O    . SER A  1 152 ? -26.28500 -36.04000 40.85700  1.000 23.77246  ? 152 SER A O    1 
ATOM   1673 C  CB   . SER A  1 152 ? -26.64100 -37.67600 38.41100  1.000 25.02236  ? 152 SER A CB   1 
ATOM   1674 O  OG   . SER A  1 152 ? -26.43900 -38.86400 39.17300  1.000 26.96694  ? 152 SER A OG   1 
ATOM   1675 H  H    . SER A  1 152 ? -27.05700 -35.19800 38.27800  1.000 25.97307  ? 152 SER A H    1 
ATOM   1676 H  HA   . SER A  1 152 ? -28.58600 -37.28600 39.06600  1.000 25.55272  ? 152 SER A HA   1 
ATOM   1677 H  HB2  . SER A  1 152 ? -26.93300 -37.90600 37.51500  1.000 30.02939  ? 152 SER A HB2  1 
ATOM   1678 H  HB3  . SER A  1 152 ? -25.81500 -37.16900 38.37000  1.000 30.02939  ? 152 SER A HB3  1 
ATOM   1679 H  HG   . SER A  1 152 ? -25.69500 -39.20500 38.98200  1.000 32.36288  ? 152 SER A HG   1 
ATOM   1680 N  N    . SER A  1 153 ? -28.01600 -37.36800 41.46000  1.000 24.50829  ? 153 SER A N    1 
ATOM   1681 C  CA   . SER A  1 153 ? -27.61200 -37.33600 42.85900  1.000 26.36411  ? 153 SER A CA   1 
ATOM   1682 C  C    . SER A  1 153 ? -26.36400 -38.16600 43.12700  1.000 27.74966  ? 153 SER A C    1 
ATOM   1683 O  O    . SER A  1 153 ? -25.89700 -38.18200 44.27300  1.000 34.36917  ? 153 SER A O    1 
ATOM   1684 C  CB   . SER A  1 153 ? -28.75300 -37.80100 43.76200  1.000 36.65582  ? 153 SER A CB   1 
ATOM   1685 O  OG   . SER A  1 153 ? -29.11200 -39.12700 43.45300  1.000 31.47748  ? 153 SER A OG   1 
ATOM   1686 H  H    . SER A  1 153 ? -28.72000 -37.83100 41.28600  1.000 29.41250  ? 153 SER A H    1 
ATOM   1687 H  HA   . SER A  1 153 ? -27.41700 -36.41600 43.09900  1.000 31.63949  ? 153 SER A HA   1 
ATOM   1688 H  HB2  . SER A  1 153 ? -28.46400 -37.75800 44.68700  1.000 43.98955  ? 153 SER A HB2  1 
ATOM   1689 H  HB3  . SER A  1 153 ? -29.52000 -37.22400 43.62700  1.000 43.98955  ? 153 SER A HB3  1 
ATOM   1690 H  HG   . SER A  1 153 ? -29.75600 -39.37000 43.93500  1.000 37.77554  ? 153 SER A HG   1 
ATOM   1691 N  N    . ARG A  1 154 ? -25.82600 -38.87800 42.14700  1.000 23.46976  ? 154 ARG A N    1 
ATOM   1692 C  CA   . ARG A  1 154 ? -24.59100 -39.62200 42.30900  1.000 26.21992  ? 154 ARG A CA   1 
ATOM   1693 C  C    . ARG A  1 154 ? -23.37300 -38.88100 41.78200  1.000 25.75668  ? 154 ARG A C    1 
ATOM   1694 O  O    . ARG A  1 154 ? -22.26800 -39.44300 41.76000  1.000 33.13337  ? 154 ARG A O    1 
ATOM   1695 C  CB   . ARG A  1 154 ? -24.66900 -40.98200 41.58800  1.000 42.80065  ? 154 ARG A CB   1 
ATOM   1696 C  CG   . ARG A  1 154 ? -25.98600 -41.70700 41.72500  1.000 56.69560  ? 154 ARG A CG   1 
ATOM   1697 C  CD   . ARG A  1 154 ? -26.43900 -41.81300 43.16300  1.000 62.78868  ? 154 ARG A CD   1 
ATOM   1698 N  NE   . ARG A  1 154 ? -27.84700 -42.19300 43.25700  1.000 72.35072  ? 154 ARG A NE   1 
ATOM   1699 C  CZ   . ARG A  1 154 ? -28.32900 -43.16400 44.02100  1.000 56.21608  ? 154 ARG A CZ   1 
ATOM   1700 N  NH1  . ARG A  1 154 ? -27.55000 -43.86000 44.83900  1.000 69.91151  ? 154 ARG A NH1  1 
ATOM   1701 N  NH2  . ARG A  1 154 ? -29.63400 -43.43100 43.98500  1.000 70.24088  ? 154 ARG A NH2  1 
ATOM   1702 H  H    . ARG A  1 154 ? -26.16700 -38.94600 41.36000  1.000 28.16627  ? 154 ARG A H    1 
ATOM   1703 H  HA   . ARG A  1 154 ? -24.47500 -39.78100 43.25900  1.000 31.46647  ? 154 ARG A HA   1 
ATOM   1704 H  HB2  . ARG A  1 154 ? -24.51500 -40.83700 40.64200  1.000 51.36334  ? 154 ARG A HB2  1 
ATOM   1705 H  HB3  . ARG A  1 154 ? -23.98100 -41.56100 41.95100  1.000 51.36334  ? 154 ARG A HB3  1 
ATOM   1706 H  HG2  . ARG A  1 154 ? -26.66700 -41.22600 41.22900  1.000 68.03728  ? 154 ARG A HG2  1 
ATOM   1707 H  HG3  . ARG A  1 154 ? -25.89200 -42.60600 41.37200  1.000 68.03728  ? 154 ARG A HG3  1 
ATOM   1708 H  HD2  . ARG A  1 154 ? -25.91100 -42.48700 43.61700  1.000 75.34898  ? 154 ARG A HD2  1 
ATOM   1709 H  HD3  . ARG A  1 154 ? -26.32600 -40.95300 43.59900  1.000 75.34898  ? 154 ARG A HD3  1 
ATOM   1710 H  HE   . ARG A  1 154 ? -28.40900 -41.75100 42.77900  1.000 86.82342  ? 154 ARG A HE   1 
ATOM   1711 H  HH11 . ARG A  1 154 ? -26.70900 -43.68600 44.88300  1.000 83.89637  ? 154 ARG A HH11 1 
ATOM   1712 H  HH12 . ARG A  1 154 ? -27.88600 -44.48500 45.32400  1.000 83.89637  ? 154 ARG A HH12 1 
ATOM   1713 H  HH21 . ARG A  1 154 ? -30.15200 -42.97600 43.47100  1.000 84.29162  ? 154 ARG A HH21 1 
ATOM   1714 H  HH22 . ARG A  1 154 ? -29.95900 -44.05900 44.47500  1.000 84.29162  ? 154 ARG A HH22 1 
ATOM   1715 N  N    . SER A  1 155 ? -23.53400 -37.62500 41.31800  1.000 24.53494  ? 155 SER A N    1 
ATOM   1716 C  CA   . SER A  1 155 ? -22.42100 -36.93200 40.71200  1.000 22.91147  ? 155 SER A CA   1 
ATOM   1717 C  C    . SER A  1 155 ? -21.80600 -35.88000 41.62900  1.000 20.54246  ? 155 SER A C    1 
ATOM   1718 O  O    . SER A  1 155 ? -22.53100 -35.13600 42.28300  1.000 22.71677  ? 155 SER A O    1 
ATOM   1719 C  CB   . SER A  1 155 ? -22.93600 -36.20400 39.47400  1.000 22.19852  ? 155 SER A CB   1 
ATOM   1720 O  OG   . SER A  1 155 ? -21.92700 -35.39700 38.90600  1.000 22.48274  ? 155 SER A OG   1 
ATOM   1721 H  H    . SER A  1 155 ? -24.26700 -37.17600 41.35000  1.000 29.44449  ? 155 SER A H    1 
ATOM   1722 H  HA   . SER A  1 155 ? -21.72700 -37.57500 40.49700  1.000 27.49633  ? 155 SER A HA   1 
ATOM   1723 H  HB2  . SER A  1 155 ? -23.22100 -36.86000 38.81900  1.000 26.64079  ? 155 SER A HB2  1 
ATOM   1724 H  HB3  . SER A  1 155 ? -23.68400 -35.64200 39.72800  1.000 26.64079  ? 155 SER A HB3  1 
ATOM   1725 H  HG   . SER A  1 155 ? -22.25700 -34.89800 38.31700  1.000 26.98185  ? 155 SER A HG   1 
ATOM   1726 N  N    . PRO A  1 156 ? -20.48000 -35.77100 41.59600  1.000 23.00545  ? 156 PRO A N    1 
ATOM   1727 C  CA   . PRO A  1 156 ? -19.82800 -34.67500 42.31700  1.000 24.50028  ? 156 PRO A CA   1 
ATOM   1728 C  C    . PRO A  1 156 ? -20.12300 -33.31000 41.74500  1.000 20.91798  ? 156 PRO A C    1 
ATOM   1729 O  O    . PRO A  1 156 ? -19.87100 -32.31300 42.43300  1.000 23.96351  ? 156 PRO A O    1 
ATOM   1730 C  CB   . PRO A  1 156 ? -18.33900 -35.00300 42.19200  1.000 28.28444  ? 156 PRO A CB   1 
ATOM   1731 C  CG   . PRO A  1 156 ? -18.24500 -35.83700 40.93800  1.000 30.58317  ? 156 PRO A CG   1 
ATOM   1732 C  CD   . PRO A  1 156 ? -19.50900 -36.64600 40.91300  1.000 26.30807  ? 156 PRO A CD   1 
ATOM   1733 H  HA   . PRO A  1 156 ? -20.08800 -34.69800 43.25100  1.000 29.40290  ? 156 PRO A HA   1 
ATOM   1734 H  HB2  . PRO A  1 156 ? -17.82400 -34.18600 42.10900  1.000 33.94389  ? 156 PRO A HB2  1 
ATOM   1735 H  HB3  . PRO A  1 156 ? -18.04200 -35.50400 42.96800  1.000 33.94389  ? 156 PRO A HB3  1 
ATOM   1736 H  HG2  . PRO A  1 156 ? -18.18700 -35.25900 40.16100  1.000 36.70237  ? 156 PRO A HG2  1 
ATOM   1737 H  HG3  . PRO A  1 156 ? -17.46500 -36.41200 40.98200  1.000 36.70237  ? 156 PRO A HG3  1 
ATOM   1738 H  HD2  . PRO A  1 156 ? -19.78600 -36.82500 40.00100  1.000 31.57225  ? 156 PRO A HD2  1 
ATOM   1739 H  HD3  . PRO A  1 156 ? -19.39500 -37.48000 41.39500  1.000 31.57225  ? 156 PRO A HD3  1 
ATOM   1740 N  N    . ILE A  1 157 ? -20.64700 -33.21600 40.52500  1.000 19.97837  ? 157 ILE A N    1 
ATOM   1741 C  CA   . ILE A  1 157 ? -21.02000 -31.92100 39.94900  1.000 19.23577  ? 157 ILE A CA   1 
ATOM   1742 C  C    . ILE A  1 157 ? -22.53300 -31.69600 40.00400  1.000 19.36640  ? 157 ILE A C    1 
ATOM   1743 O  O    . ILE A  1 157 ? -23.07200 -30.84700 39.28000  1.000 19.19870  ? 157 ILE A O    1 
ATOM   1744 C  CB   . ILE A  1 157 ? -20.44600 -31.68000 38.53700  1.000 18.12028  ? 157 ILE A CB   1 
ATOM   1745 C  CG1  . ILE A  1 157 ? -20.96000 -32.68000 37.50500  1.000 19.04342  ? 157 ILE A CG1  1 
ATOM   1746 C  CG2  . ILE A  1 157 ? -18.91200 -31.70200 38.57700  1.000 21.94476  ? 157 ILE A CG2  1 
ATOM   1747 C  CD1  . ILE A  1 157 ? -20.72700 -32.21000 36.06000  1.000 18.56781  ? 157 ILE A CD1  1 
ATOM   1748 H  H    . ILE A  1 157 ? -20.79700 -33.88700 40.00900  1.000 23.97661  ? 157 ILE A H    1 
ATOM   1749 H  HA   . ILE A  1 157 ? -20.60900 -31.24300 40.50900  1.000 23.08548  ? 157 ILE A HA   1 
ATOM   1750 H  HB   . ILE A  1 157 ? -20.75600 -30.80500 38.25800  1.000 21.74689  ? 157 ILE A HB   1 
ATOM   1751 H  HG12 . ILE A  1 157 ? -20.49800 -33.52500 37.62500  1.000 22.85467  ? 157 ILE A HG12 1 
ATOM   1752 H  HG13 . ILE A  1 157 ? -21.91400 -32.80300 37.63100  1.000 22.85467  ? 157 ILE A HG13 1 
ATOM   1753 H  HG21 . ILE A  1 157 ? -18.56900 -31.42700 37.71200  1.000 26.33627  ? 157 ILE A HG21 1 
ATOM   1754 H  HG22 . ILE A  1 157 ? -18.60500 -31.09000 39.26400  1.000 26.33627  ? 157 ILE A HG22 1 
ATOM   1755 H  HG23 . ILE A  1 157 ? -18.61400 -32.60300 38.78000  1.000 26.33627  ? 157 ILE A HG23 1 
ATOM   1756 H  HD11 . ILE A  1 157 ? -21.15200 -32.83500 35.45200  1.000 22.28394  ? 157 ILE A HD11 1 
ATOM   1757 H  HD12 . ILE A  1 157 ? -21.11100 -31.32700 35.94900  1.000 22.28394  ? 157 ILE A HD12 1 
ATOM   1758 H  HD13 . ILE A  1 157 ? -19.77200 -32.18000 35.88800  1.000 22.28394  ? 157 ILE A HD13 1 
ATOM   1759 N  N    . ASN A  1 158 ? -23.23000 -32.42600 40.87300  1.000 19.89461  ? 158 ASN A N    1 
ATOM   1760 C  CA   . ASN A  1 158 ? -24.63800 -32.17900 41.10500  1.000 20.01466  ? 158 ASN A CA   1 
ATOM   1761 C  C    . ASN A  1 158 ? -24.92000 -30.69700 41.33000  1.000 19.30963  ? 158 ASN A C    1 
ATOM   1762 O  O    . ASN A  1 158 ? -24.30200 -30.04700 42.17900  1.000 21.64171  ? 158 ASN A O    1 
ATOM   1763 C  CB   . ASN A  1 158 ? -25.07400 -32.96400 42.34500  1.000 22.12262  ? 158 ASN A CB   1 
ATOM   1764 C  CG   . ASN A  1 158 ? -26.48400 -32.68400 42.72900  1.000 24.35977  ? 158 ASN A CG   1 
ATOM   1765 O  OD1  . ASN A  1 158 ? -26.76500 -31.75000 43.47400  1.000 25.82057  ? 158 ASN A OD1  1 
ATOM   1766 N  ND2  . ASN A  1 158 ? -27.38900 -33.49900 42.23500  1.000 27.76441  ? 158 ASN A ND2  1 
ATOM   1767 H  H    . ASN A  1 158 ? -22.90400 -33.07100 41.34000  1.000 23.87609  ? 158 ASN A H    1 
ATOM   1768 H  HA   . ASN A  1 158 ? -25.14200 -32.46600 40.32800  1.000 24.02015  ? 158 ASN A HA   1 
ATOM   1769 H  HB2  . ASN A  1 158 ? -24.99300 -33.91400 42.16400  1.000 26.54971  ? 158 ASN A HB2  1 
ATOM   1770 H  HB3  . ASN A  1 158 ? -24.50400 -32.72000 43.09200  1.000 26.54971  ? 158 ASN A HB3  1 
ATOM   1771 H  HD21 . ASN A  1 158 ? -28.22000 -33.38400 42.42400  1.000 33.31985  ? 158 ASN A HD21 1 
ATOM   1772 H  HD22 . ASN A  1 158 ? -27.15000 -34.14700 41.72300  1.000 33.31985  ? 158 ASN A HD22 1 
ATOM   1773 N  N    . GLY A  1 159 ? -25.89700 -30.18700 40.58600  1.000 20.56947  ? 159 GLY A N    1 
ATOM   1774 C  CA   . GLY A  1 159 ? -26.32400 -28.81400 40.75300  1.000 19.86216  ? 159 GLY A CA   1 
ATOM   1775 C  C    . GLY A  1 159 ? -25.35800 -27.76000 40.28800  1.000 20.73649  ? 159 GLY A C    1 
ATOM   1776 O  O    . GLY A  1 159 ? -25.49300 -26.59500 40.70100  1.000 23.11796  ? 159 GLY A O    1 
ATOM   1777 H  H    . GLY A  1 159 ? -26.32500 -30.62000 39.97800  1.000 24.68592  ? 159 GLY A H    1 
ATOM   1778 H  HA2  . GLY A  1 159 ? -27.15000 -28.68900 40.26100  1.000 23.83716  ? 159 GLY A HA2  1 
ATOM   1779 H  HA3  . GLY A  1 159 ? -26.49200 -28.65900 41.69600  1.000 23.83716  ? 159 GLY A HA3  1 
ATOM   1780 N  N    . MET A  1 160 ? -24.33500 -28.11600 39.51800  1.000 17.90690  ? 160 MET A N    1 
ATOM   1781 C  CA   . MET A  1 160 ? -23.32200 -27.13700 39.13800  1.000 17.95547  ? 160 MET A CA   1 
ATOM   1782 C  C    . MET A  1 160 ? -23.48400 -26.55600 37.73900  1.000 19.00416  ? 160 MET A C    1 
ATOM   1783 O  O    . MET A  1 160 ? -22.84200 -25.54800 37.44500  1.000 19.15810  ? 160 MET A O    1 
ATOM   1784 C  CB   . MET A  1 160 ? -21.90200 -27.71700 39.18900  1.000 18.96929  ? 160 MET A CB   1 
ATOM   1785 C  CG   . MET A  1 160 ? -21.42900 -28.05200 40.59300  1.000 19.73966  ? 160 MET A CG   1 
ATOM   1786 S  SD   . MET A  1 160 ? -19.64900 -28.42400 40.64100  1.000 20.83662  ? 160 MET A SD   1 
ATOM   1787 C  CE   . MET A  1 160 ? -19.43600 -28.78100 42.34700  1.000 28.05325  ? 160 MET A CE   1 
ATOM   1788 H  H    . MET A  1 160 ? -24.20700 -28.90700 39.20600  1.000 21.49084  ? 160 MET A H    1 
ATOM   1789 H  HA   . MET A  1 160 ? -23.39900 -26.43400 39.80200  1.000 21.54912  ? 160 MET A HA   1 
ATOM   1790 H  HB2  . MET A  1 160 ? -21.88000 -28.53400 38.66600  1.000 22.76571  ? 160 MET A HB2  1 
ATOM   1791 H  HB3  . MET A  1 160 ? -21.28600 -27.06700 38.81600  1.000 22.76571  ? 160 MET A HB3  1 
ATOM   1792 H  HG2  . MET A  1 160 ? -21.59600 -27.29500 41.17500  1.000 23.69016  ? 160 MET A HG2  1 
ATOM   1793 H  HG3  . MET A  1 160 ? -21.91000 -28.83000 40.91500  1.000 23.69016  ? 160 MET A HG3  1 
ATOM   1794 H  HE1  . MET A  1 160 ? -18.50000 -28.97500 42.51400  1.000 33.66646  ? 160 MET A HE1  1 
ATOM   1795 H  HE2  . MET A  1 160 ? -19.71300 -28.01100 42.86700  1.000 33.66646  ? 160 MET A HE2  1 
ATOM   1796 H  HE3  . MET A  1 160 ? -19.98000 -29.55000 42.57900  1.000 33.66646  ? 160 MET A HE3  1 
ATOM   1797 N  N    . VAL A  1 161 ? -24.25800 -27.17500 36.86200  1.000 16.38945  ? 161 VAL A N    1 
ATOM   1798 C  CA   . VAL A  1 161 ? -24.29300 -26.79600 35.45700  1.000 16.22628  ? 161 VAL A CA   1 
ATOM   1799 C  C    . VAL A  1 161 ? -25.60700 -26.11400 35.11800  1.000 18.14223  ? 161 VAL A C    1 
ATOM   1800 O  O    . VAL A  1 161 ? -26.69200 -26.66400 35.37700  1.000 20.37245  ? 161 VAL A O    1 
ATOM   1801 C  CB   . VAL A  1 161 ? -24.09500 -28.00900 34.53800  1.000 16.61208  ? 161 VAL A CB   1 
ATOM   1802 C  CG1  . VAL A  1 161 ? -24.27600 -27.60700 33.06300  1.000 17.40400  ? 161 VAL A CG1  1 
ATOM   1803 C  CG2  . VAL A  1 161 ? -22.71400 -28.63500 34.76100  1.000 17.78561  ? 161 VAL A CG2  1 
ATOM   1804 H  H    . VAL A  1 161 ? -24.78100 -27.82800 37.05900  1.000 19.66991  ? 161 VAL A H    1 
ATOM   1805 H  HA   . VAL A  1 161 ? -23.57900 -26.15400 35.31800  1.000 19.47410  ? 161 VAL A HA   1 
ATOM   1806 H  HB   . VAL A  1 161 ? -24.76600 -28.67600 34.75300  1.000 19.93706  ? 161 VAL A HB   1 
ATOM   1807 H  HG11 . VAL A  1 161 ? -23.79100 -28.23400 32.50300  1.000 20.88736  ? 161 VAL A HG11 1 
ATOM   1808 H  HG12 . VAL A  1 161 ? -25.22100 -27.63000 32.84300  1.000 20.88736  ? 161 VAL A HG12 1 
ATOM   1809 H  HG13 . VAL A  1 161 ? -23.92800 -26.71100 32.93500  1.000 20.88736  ? 161 VAL A HG13 1 
ATOM   1810 H  HG21 . VAL A  1 161 ? -22.61500 -29.39900 34.17200  1.000 21.34529  ? 161 VAL A HG21 1 
ATOM   1811 H  HG22 . VAL A  1 161 ? -22.03300 -27.97400 34.56400  1.000 21.34529  ? 161 VAL A HG22 1 
ATOM   1812 H  HG23 . VAL A  1 161 ? -22.64200 -28.91900 35.68600  1.000 21.34529  ? 161 VAL A HG23 1 
ATOM   1813 N  N    . ASP A  1 162 ? -25.51400 -24.93600 34.49600  1.000 16.39816  ? 162 ASP A N    1 
ATOM   1814 C  CA   . ASP A  1 162 ? -26.67700 -24.27100 33.92000  1.000 16.94051  ? 162 ASP A CA   1 
ATOM   1815 C  C    . ASP A  1 162 ? -26.79400 -24.74200 32.47600  1.000 17.36537  ? 162 ASP A C    1 
ATOM   1816 O  O    . ASP A  1 162 ? -25.94800 -24.38100 31.65000  1.000 16.33659  ? 162 ASP A O    1 
ATOM   1817 C  CB   . ASP A  1 162 ? -26.48600 -22.76500 33.96700  1.000 17.81515  ? 162 ASP A CB   1 
ATOM   1818 C  CG   . ASP A  1 162 ? -27.68500 -21.99000 33.46200  1.000 17.94546  ? 162 ASP A CG   1 
ATOM   1819 O  OD1  . ASP A  1 162 ? -28.50600 -22.58700 32.73200  1.000 18.49544  ? 162 ASP A OD1  1 
ATOM   1820 O  OD2  . ASP A  1 162 ? -27.78200 -20.78600 33.76900  1.000 18.54876  ? 162 ASP A OD2  1 
ATOM   1821 H  H    . ASP A  1 162 ? -24.78000 -24.50000 34.39600  1.000 19.68036  ? 162 ASP A H    1 
ATOM   1822 H  HA   . ASP A  1 162 ? -27.48500 -24.49700 34.40500  1.000 20.33117  ? 162 ASP A HA   1 
ATOM   1823 H  HB2  . ASP A  1 162 ? -26.32500 -22.49700 34.88500  1.000 21.38074  ? 162 ASP A HB2  1 
ATOM   1824 H  HB3  . ASP A  1 162 ? -25.72500 -22.52700 33.41400  1.000 21.38074  ? 162 ASP A HB3  1 
ATOM   1825 N  N    . PRO A  1 163 ? -27.80300 -25.54100 32.12600  1.000 17.02596  ? 163 PRO A N    1 
ATOM   1826 C  CA   . PRO A  1 163 ? -27.88400 -26.06400 30.76200  1.000 18.06057  ? 163 PRO A CA   1 
ATOM   1827 C  C    . PRO A  1 163 ? -28.05600 -24.99000 29.68900  1.000 18.21287  ? 163 PRO A C    1 
ATOM   1828 O  O    . PRO A  1 163 ? -27.93100 -25.30600 28.50400  1.000 18.57790  ? 163 PRO A O    1 
ATOM   1829 C  CB   . PRO A  1 163 ? -29.09400 -27.00200 30.79600  1.000 22.58771  ? 163 PRO A CB   1 
ATOM   1830 C  CG   . PRO A  1 163 ? -29.95000 -26.46500 31.92600  1.000 25.53369  ? 163 PRO A CG   1 
ATOM   1831 C  CD   . PRO A  1 163 ? -28.96400 -25.92700 32.94000  1.000 18.16777  ? 163 PRO A CD   1 
ATOM   1832 H  HA   . PRO A  1 163 ? -27.08600 -26.58200 30.57200  1.000 21.67525  ? 163 PRO A HA   1 
ATOM   1833 H  HB2  . PRO A  1 163 ? -29.56800 -26.96500 29.95000  1.000 27.10782  ? 163 PRO A HB2  1 
ATOM   1834 H  HB3  . PRO A  1 163 ? -28.80700 -27.91100 30.97600  1.000 27.10782  ? 163 PRO A HB3  1 
ATOM   1835 H  HG2  . PRO A  1 163 ? -30.52800 -25.75900 31.59600  1.000 30.64300  ? 163 PRO A HG2  1 
ATOM   1836 H  HG3  . PRO A  1 163 ? -30.48300 -27.18000 32.30600  1.000 30.64300  ? 163 PRO A HG3  1 
ATOM   1837 H  HD2  . PRO A  1 163 ? -29.33200 -25.15700 33.40200  1.000 21.80389  ? 163 PRO A HD2  1 
ATOM   1838 H  HD3  . PRO A  1 163 ? -28.72200 -26.61300 33.58100  1.000 21.80389  ? 163 PRO A HD3  1 
ATOM   1839 N  N    . ASN A  1 164 ? -28.43500 -23.76700 30.07200  1.000 17.00189  ? 164 ASN A N    1 
ATOM   1840 C  CA   . ASN A  1 164 ? -28.57200 -22.67200 29.11100  1.000 17.99734  ? 164 ASN A CA   1 
ATOM   1841 C  C    . ASN A  1 164 ? -27.23900 -22.11400 28.65700  1.000 16.83786  ? 164 ASN A C    1 
ATOM   1842 O  O    . ASN A  1 164 ? -27.21900 -21.28800 27.75000  1.000 17.27711  ? 164 ASN A O    1 
ATOM   1843 C  CB   . ASN A  1 164 ? -29.35600 -21.52700 29.75500  1.000 17.92383  ? 164 ASN A CB   1 
ATOM   1844 C  CG   . ASN A  1 164 ? -30.76400 -21.88800 30.05500  1.000 18.38305  ? 164 ASN A CG   1 
ATOM   1845 O  OD1  . ASN A  1 164 ? -31.62900 -21.84200 29.19600  1.000 20.84678  ? 164 ASN A OD1  1 
ATOM   1846 N  ND2  . ASN A  1 164 ? -31.03500 -22.21200 31.30200  1.000 19.86901  ? 164 ASN A ND2  1 
ATOM   1847 H  H    . ASN A  1 164 ? -28.61900 -23.54700 30.88200  1.000 20.40483  ? 164 ASN A H    1 
ATOM   1848 H  HA   . ASN A  1 164 ? -29.05200 -23.00500 28.33600  1.000 21.59937  ? 164 ASN A HA   1 
ATOM   1849 H  HB2  . ASN A  1 164 ? -28.92600 -21.28100 30.58900  1.000 21.51116  ? 164 ASN A HB2  1 
ATOM   1850 H  HB3  . ASN A  1 164 ? -29.36400 -20.77000 29.14900  1.000 21.51116  ? 164 ASN A HB3  1 
ATOM   1851 H  HD21 . ASN A  1 164 ? -31.83600 -22.42900 31.52600  1.000 23.84538  ? 164 ASN A HD21 1 
ATOM   1852 H  HD22 . ASN A  1 164 ? -30.41000 -22.20700 31.89300  1.000 23.84538  ? 164 ASN A HD22 1 
ATOM   1853 N  N    . ARG A  1 165 ? -26.12600 -22.49300 29.29500  1.000 15.95557  ? 165 ARG A N    1 
ATOM   1854 C  CA   . ARG A  1 165 ? -24.85600 -21.78600 29.11500  1.000 15.61807  ? 165 ARG A CA   1 
ATOM   1855 C  C    . ARG A  1 165 ? -23.72200 -22.77700 28.87100  1.000 15.16161  ? 165 ARG A C    1 
ATOM   1856 O  O    . ARG A  1 165 ? -23.05900 -23.22900 29.81400  1.000 15.55632  ? 165 ARG A O    1 
ATOM   1857 C  CB   . ARG A  1 165 ? -24.61200 -20.87000 30.33700  1.000 16.07617  ? 165 ARG A CB   1 
ATOM   1858 C  CG   . ARG A  1 165 ? -25.83500 -20.04900 30.68300  1.000 16.55990  ? 165 ARG A CG   1 
ATOM   1859 C  CD   . ARG A  1 165 ? -25.58000 -18.95800 31.67800  1.000 17.37065  ? 165 ARG A CD   1 
ATOM   1860 N  NE   . ARG A  1 165 ? -25.25800 -19.43600 33.02000  1.000 17.52358  ? 165 ARG A NE   1 
ATOM   1861 C  CZ   . ARG A  1 165 ? -24.15600 -19.13500 33.67600  1.000 16.71228  ? 165 ARG A CZ   1 
ATOM   1862 N  NH1  . ARG A  1 165 ? -23.12100 -18.57400 33.07800  1.000 18.09447  ? 165 ARG A NH1  1 
ATOM   1863 N  NH2  . ARG A  1 165 ? -24.10200 -19.40800 34.95600  1.000 17.41113  ? 165 ARG A NH2  1 
ATOM   1864 H  H    . ARG A  1 165 ? -26.08500 -23.15800 29.83900  1.000 19.14925  ? 165 ARG A H    1 
ATOM   1865 H  HA   . ARG A  1 165 ? -24.89800 -21.25400 28.30500  1.000 18.74425  ? 165 ARG A HA   1 
ATOM   1866 H  HB2  . ARG A  1 165 ? -24.38500 -21.41700 31.10500  1.000 19.29396  ? 165 ARG A HB2  1 
ATOM   1867 H  HB3  . ARG A  1 165 ? -23.88400 -20.26000 30.13700  1.000 19.29396  ? 165 ARG A HB3  1 
ATOM   1868 H  HG2  . ARG A  1 165 ? -26.17100 -19.63400 29.87300  1.000 19.87444  ? 165 ARG A HG2  1 
ATOM   1869 H  HG3  . ARG A  1 165 ? -26.50900 -20.63700 31.05800  1.000 19.87444  ? 165 ARG A HG3  1 
ATOM   1870 H  HD2  . ARG A  1 165 ? -24.83100 -18.42400 31.36900  1.000 20.84734  ? 165 ARG A HD2  1 
ATOM   1871 H  HD3  . ARG A  1 165 ? -26.37500 -18.40600 31.74600  1.000 20.84734  ? 165 ARG A HD3  1 
ATOM   1872 H  HE   . ARG A  1 165 ? -25.82800 -19.94900 33.40900  1.000 21.03086  ? 165 ARG A HE   1 
ATOM   1873 H  HH11 . ARG A  1 165 ? -23.15600 -18.39500 32.23700  1.000 21.71592  ? 165 ARG A HH11 1 
ATOM   1874 H  HH12 . ARG A  1 165 ? -22.41300 -18.38700 33.52800  1.000 21.71592  ? 165 ARG A HH12 1 
ATOM   1875 H  HH21 . ARG A  1 165 ? -24.77500 -19.77300 35.34700  1.000 20.89592  ? 165 ARG A HH21 1 
ATOM   1876 H  HH22 . ARG A  1 165 ? -23.39300 -19.22100 35.40600  1.000 20.89592  ? 165 ARG A HH22 1 
ATOM   1877 N  N    . LEU A  1 166 ? -23.51000 -23.11000 27.60000  1.000 14.83876  ? 166 LEU A N    1 
ATOM   1878 C  CA   . LEU A  1 166 ? -22.58300 -24.16100 27.21100  1.000 13.69862  ? 166 LEU A CA   1 
ATOM   1879 C  C    . LEU A  1 166 ? -21.57000 -23.64200 26.21000  1.000 14.76090  ? 166 LEU A C    1 
ATOM   1880 O  O    . LEU A  1 166 ? -21.91500 -22.92400 25.27500  1.000 15.53150  ? 166 LEU A O    1 
ATOM   1881 C  CB   . LEU A  1 166 ? -23.35400 -25.33800 26.60100  1.000 16.69865  ? 166 LEU A CB   1 
ATOM   1882 C  CG   . LEU A  1 166 ? -24.48000 -25.94900 27.44100  1.000 16.17117  ? 166 LEU A CG   1 
ATOM   1883 C  CD1  . LEU A  1 166 ? -25.20100 -27.02400 26.64900  1.000 21.03829  ? 166 LEU A CD1  1 
ATOM   1884 C  CD2  . LEU A  1 166 ? -23.96000 -26.47300 28.73000  1.000 18.59520  ? 166 LEU A CD2  1 
ATOM   1885 H  H    . LEU A  1 166 ? -23.90100 -22.73300 26.93300  1.000 17.80908  ? 166 LEU A H    1 
ATOM   1886 H  HA   . LEU A  1 166 ? -22.08600 -24.46000 27.98900  1.000 16.44091  ? 166 LEU A HA   1 
ATOM   1887 H  HB2  . LEU A  1 166 ? -23.75500 -25.03400 25.77200  1.000 20.04094  ? 166 LEU A HB2  1 
ATOM   1888 H  HB3  . LEU A  1 166 ? -22.71900 -26.04900 26.42200  1.000 20.04094  ? 166 LEU A HB3  1 
ATOM   1889 H  HG   . LEU A  1 166 ? -25.12600 -25.25900 27.65900  1.000 19.40796  ? 166 LEU A HG   1 
ATOM   1890 H  HD11 . LEU A  1 166 ? -25.90500 -27.40300 27.19900  1.000 25.24850  ? 166 LEU A HD11 1 
ATOM   1891 H  HD12 . LEU A  1 166 ? -25.58200 -26.62600 25.85100  1.000 25.24850  ? 166 LEU A HD12 1 
ATOM   1892 H  HD13 . LEU A  1 166 ? -24.56600 -27.71500 26.40300  1.000 25.24850  ? 166 LEU A HD13 1 
ATOM   1893 H  HD21 . LEU A  1 166 ? -24.68400 -26.90800 29.20800  1.000 22.31680  ? 166 LEU A HD21 1 
ATOM   1894 H  HD22 . LEU A  1 166 ? -23.25200 -27.11100 28.54900  1.000 22.31680  ? 166 LEU A HD22 1 
ATOM   1895 H  HD23 . LEU A  1 166 ? -23.61400 -25.73500 29.25500  1.000 22.31680  ? 166 LEU A HD23 1 
ATOM   1896 N  N    . GLY A  1 167 ? -20.31100 -24.03600 26.38700  1.000 14.62287  ? 167 GLY A N    1 
ATOM   1897 C  CA   . GLY A  1 167 ? -19.24700 -23.61000 25.49600  1.000 14.82537  ? 167 GLY A CA   1 
ATOM   1898 C  C    . GLY A  1 167 ? -18.37900 -24.77500 25.05700  1.000 14.06499  ? 167 GLY A C    1 
ATOM   1899 O  O    . GLY A  1 167 ? -18.39500 -25.86600 25.64200  1.000 13.92501  ? 167 GLY A O    1 
ATOM   1900 H  H    . GLY A  1 167 ? -20.05000 -24.55400 27.02200  1.000 17.55000  ? 167 GLY A H    1 
ATOM   1901 H  HA2  . GLY A  1 167 ? -19.63100 -23.19800 24.70700  1.000 17.79301  ? 167 GLY A HA2  1 
ATOM   1902 H  HA3  . GLY A  1 167 ? -18.68500 -22.96200 25.95000  1.000 17.79301  ? 167 GLY A HA3  1 
ATOM   1903 N  N    . ALA A  1 168 ? -17.58100 -24.52600 24.02000  1.000 13.22914  ? 168 ALA A N    1 
ATOM   1904 C  CA   . ALA A  1 168 ? -16.61700 -25.52200 23.57900  1.000 14.12855  ? 168 ALA A CA   1 
ATOM   1905 C  C    . ALA A  1 168 ? -15.35100 -24.84400 23.11200  1.000 13.75167  ? 168 ALA A C    1 
ATOM   1906 O  O    . ALA A  1 168 ? -15.37800 -23.74200 22.55500  1.000 14.48676  ? 168 ALA A O    1 
ATOM   1907 C  CB   . ALA A  1 168 ? -17.18200 -26.39000 22.45400  1.000 17.68476  ? 168 ALA A CB   1 
ATOM   1908 H  H    . ALA A  1 168 ? -17.58100 -23.79600 23.56400  1.000 15.87753  ? 168 ALA A H    1 
ATOM   1909 H  HA   . ALA A  1 168 ? -16.38800 -26.09400 24.32900  1.000 16.95682  ? 168 ALA A HA   1 
ATOM   1910 H  HB1  . ALA A  1 168 ? -16.50000 -27.01600 22.16500  1.000 21.22428  ? 168 ALA A HB1  1 
ATOM   1911 H  HB2  . ALA A  1 168 ? -17.95500 -26.87300 22.78600  1.000 21.22428  ? 168 ALA A HB2  1 
ATOM   1912 H  HB3  . ALA A  1 168 ? -17.44100 -25.81900 21.71400  1.000 21.22428  ? 168 ALA A HB3  1 
ATOM   1913 N  N    . VAL A  1 169 ? -14.24200 -25.54900 23.32200  1.000 13.98861  ? 169 VAL A N    1 
ATOM   1914 C  CA   . VAL A  1 169 ? -12.89100 -25.14300 22.92900  1.000 12.98040  ? 169 VAL A CA   1 
ATOM   1915 C  C    . VAL A  1 169 ? -12.26500 -26.32400 22.20500  1.000 13.04565  ? 169 VAL A C    1 
ATOM   1916 O  O    . VAL A  1 169 ? -12.26300 -27.43400 22.73300  1.000 14.18735  ? 169 VAL A O    1 
ATOM   1917 C  CB   . VAL A  1 169 ? -12.04600 -24.79400 24.16700  1.000 12.89675  ? 169 VAL A CB   1 
ATOM   1918 C  CG1  . VAL A  1 169 ? -10.63500 -24.42300 23.77200  1.000 13.63835  ? 169 VAL A CG1  1 
ATOM   1919 C  CG2  . VAL A  1 169 ? -12.70200 -23.72400 25.06300  1.000 15.09822  ? 169 VAL A CG2  1 
ATOM   1920 H  H    . VAL A  1 169 ? -14.24500 -26.31400 23.71400  1.000 16.78890  ? 169 VAL A H    1 
ATOM   1921 H  HA   . VAL A  1 169 ? -12.92600 -24.37600 22.33600  1.000 15.57904  ? 169 VAL A HA   1 
ATOM   1922 H  HB   . VAL A  1 169 ? -11.99500 -25.59200 24.71600  1.000 15.47866  ? 169 VAL A HB   1 
ATOM   1923 H  HG11 . VAL A  1 169 ? -10.19100 -24.01600 24.53300  1.000 16.36859  ? 169 VAL A HG11 1 
ATOM   1924 H  HG12 . VAL A  1 169 ? -10.16100 -25.22500 23.50300  1.000 16.36859  ? 169 VAL A HG12 1 
ATOM   1925 H  HG13 . VAL A  1 169 ? -10.66800 -23.79500 23.03400  1.000 16.36859  ? 169 VAL A HG13 1 
ATOM   1926 H  HG21 . VAL A  1 169 ? -12.10300 -23.51500 25.79600  1.000 18.12043  ? 169 VAL A HG21 1 
ATOM   1927 H  HG22 . VAL A  1 169 ? -12.86700 -22.92700 24.53400  1.000 18.12043  ? 169 VAL A HG22 1 
ATOM   1928 H  HG23 . VAL A  1 169 ? -13.54000 -24.07100 25.40800  1.000 18.12043  ? 169 VAL A HG23 1 
ATOM   1929 N  N    . GLY A  1 170 ? -11.75800 -26.12300 21.00200  1.000 13.33122  ? 170 GLY A N    1 
ATOM   1930 C  CA   . GLY A  1 170 ? -11.23200 -27.24700 20.24700  1.000 14.48313  ? 170 GLY A CA   1 
ATOM   1931 C  C    . GLY A  1 170 ? -9.97200  -26.91500 19.48200  1.000 14.19332  ? 170 GLY A C    1 
ATOM   1932 O  O    . GLY A  1 170 ? -9.88900  -25.86000 18.84600  1.000 14.04723  ? 170 GLY A O    1 
ATOM   1933 H  H    . GLY A  1 170 ? -11.70700 -25.36100 20.60800  1.000 16.00002  ? 170 GLY A H    1 
ATOM   1934 H  HA2  . GLY A  1 170 ? -11.03200 -27.97400 20.85800  1.000 17.38232  ? 170 GLY A HA2  1 
ATOM   1935 H  HA3  . GLY A  1 170 ? -11.90200 -27.54400 19.61200  1.000 17.38232  ? 170 GLY A HA3  1 
ATOM   1936 N  N    . TRP A  1 171 ? -8.99700  -27.82800 19.50300  1.000 15.03005  ? 171 TRP A N    1 
ATOM   1937 C  CA   . TRP A  1 171 ? -7.74400  -27.69800 18.76600  1.000 13.87665  ? 171 TRP A CA   1 
ATOM   1938 C  C    . TRP A  1 171 ? -7.79500  -28.47200 17.45700  1.000 15.37516  ? 171 TRP A C    1 
ATOM   1939 O  O    . TRP A  1 171 ? -8.17100  -29.65000 17.42600  1.000 15.93306  ? 171 TRP A O    1 
ATOM   1940 C  CB   . TRP A  1 171 ? -6.59600  -28.23500 19.62500  1.000 14.81429  ? 171 TRP A CB   1 
ATOM   1941 C  CG   . TRP A  1 171 ? -5.27700  -28.31400 18.94200  1.000 13.97211  ? 171 TRP A CG   1 
ATOM   1942 C  CD1  . TRP A  1 171 ? -4.70900  -27.39100 18.11700  1.000 14.59971  ? 171 TRP A CD1  1 
ATOM   1943 C  CD2  . TRP A  1 171 ? -4.34000  -29.38400 19.05200  1.000 14.52879  ? 171 TRP A CD2  1 
ATOM   1944 N  NE1  . TRP A  1 171 ? -3.47200  -27.82800 17.69600  1.000 14.69364  ? 171 TRP A NE1  1 
ATOM   1945 C  CE2  . TRP A  1 171 ? -3.23500  -29.06300 18.25600  1.000 13.87877  ? 171 TRP A CE2  1 
ATOM   1946 C  CE3  . TRP A  1 171 ? -4.32000  -30.58100 19.78100  1.000 15.06568  ? 171 TRP A CE3  1 
ATOM   1947 C  CZ2  . TRP A  1 171 ? -2.12700  -29.89300 18.15500  1.000 15.68415  ? 171 TRP A CZ2  1 
ATOM   1948 C  CZ3  . TRP A  1 171 ? -3.22900  -31.40000 19.68900  1.000 17.63076  ? 171 TRP A CZ3  1 
ATOM   1949 C  CH2  . TRP A  1 171 ? -2.14100  -31.06800 18.88900  1.000 16.26618  ? 171 TRP A CH2  1 
ATOM   1950 H  H    . TRP A  1 171 ? -9.04300  -28.55800 19.95600  1.000 18.03862  ? 171 TRP A H    1 
ATOM   1951 H  HA   . TRP A  1 171 ? -7.59800  -26.76500 18.54700  1.000 16.65454  ? 171 TRP A HA   1 
ATOM   1952 H  HB2  . TRP A  1 171 ? -6.49000  -27.65300 20.39300  1.000 17.77971  ? 171 TRP A HB2  1 
ATOM   1953 H  HB3  . TRP A  1 171 ? -6.82500  -29.13100 19.91700  1.000 17.77971  ? 171 TRP A HB3  1 
ATOM   1954 H  HD1  . TRP A  1 171 ? -5.10000  -26.58400 17.87200  1.000 17.52221  ? 171 TRP A HD1  1 
ATOM   1955 H  HE1  . TRP A  1 171 ? -2.93900  -27.40100 17.17300  1.000 17.63493  ? 171 TRP A HE1  1 
ATOM   1956 H  HE3  . TRP A  1 171 ? -5.04000  -30.81500 20.32100  1.000 18.08138  ? 171 TRP A HE3  1 
ATOM   1957 H  HZ2  . TRP A  1 171 ? -1.40400  -29.66900 17.61600  1.000 18.82354  ? 171 TRP A HZ2  1 
ATOM   1958 H  HZ3  . TRP A  1 171 ? -3.21500  -32.19500 20.17100  1.000 21.15947  ? 171 TRP A HZ3  1 
ATOM   1959 H  HH2  . TRP A  1 171 ? -1.41200  -31.64400 18.84600  1.000 19.52198  ? 171 TRP A HH2  1 
ATOM   1960 N  N    . SER A  1 172 ? -7.40000  -27.80800 16.37200  1.000 15.25598  ? 172 SER A N    1 
ATOM   1961 C  CA   . SER A  1 172 ? -7.14600  -28.46400 15.07900  1.000 16.72115  ? 172 SER A CA   1 
ATOM   1962 C  C    . SER A  1 172 ? -8.44700  -29.13500 14.63600  1.000 15.55780  ? 172 SER A C    1 
ATOM   1963 O  O    . SER A  1 172 ? -9.47200  -28.43400 14.55800  1.000 16.72750  ? 172 SER A O    1 
ATOM   1964 C  CB   . SER A  1 172 ? -5.89600  -29.29600 15.21700  1.000 18.67851  ? 172 SER A CB   1 
ATOM   1965 O  OG   . SER A  1 172 ? -5.40100  -29.51600 13.90100  1.000 24.46126  ? 172 SER A OG   1 
ATOM   1966 H  H    . SER A  1 172 ? -7.26800  -26.95800 16.35400  1.000 18.30973  ? 172 SER A H    1 
ATOM   1967 H  HA   . SER A  1 172 ? -6.97300  -27.81300 14.38200  1.000 20.06794  ? 172 SER A HA   1 
ATOM   1968 H  HB2  . SER A  1 172 ? -5.23600  -28.81800 15.74300  1.000 22.41678  ? 172 SER A HB2  1 
ATOM   1969 H  HB3  . SER A  1 172 ? -6.10600  -30.14400 15.63800  1.000 22.41678  ? 172 SER A HB3  1 
ATOM   1970 H  HG   . SER A  1 172 ? -4.78100  -30.08300 13.91800  1.000 29.35607  ? 172 SER A HG   1 
ATOM   1971 N  N    . MET A  1 173 ? -8.48000  -30.42500 14.32900  1.000 16.62311  ? 173 MET A N    1 
ATOM   1972 C  CA   . MET A  1 173 ? -9.74000  -31.02700 13.92400  1.000 17.48982  ? 173 MET A CA   1 
ATOM   1973 C  C    . MET A  1 173 ? -10.79700 -30.88700 15.00000  1.000 15.98027  ? 173 MET A C    1 
ATOM   1974 O  O    . MET A  1 173 ? -11.99400 -30.83300 14.68100  1.000 16.80459  ? 173 MET A O    1 
ATOM   1975 C  CB   . MET A  1 173 ? -9.56000  -32.49000 13.55000  1.000 17.88417  ? 173 MET A CB   1 
ATOM   1976 C  CG   . MET A  1 173 ? -8.86400  -32.67600 12.22800  1.000 19.72144  ? 173 MET A CG   1 
ATOM   1977 S  SD   . MET A  1 173 ? -8.92900  -34.41200 11.76500  1.000 21.23621  ? 173 MET A SD   1 
ATOM   1978 C  CE   . MET A  1 173 ? -7.93100  -34.33700 10.28800  1.000 24.68482  ? 173 MET A CE   1 
ATOM   1979 H  H    . MET A  1 173 ? -7.80600  -30.95900 14.34600  1.000 19.95029  ? 173 MET A H    1 
ATOM   1980 H  HA   . MET A  1 173 ? -10.03900 -30.56700 13.12400  1.000 20.99035  ? 173 MET A HA   1 
ATOM   1981 H  HB2  . MET A  1 173 ? -9.02800  -32.92700 14.23400  1.000 21.46357  ? 173 MET A HB2  1 
ATOM   1982 H  HB3  . MET A  1 173 ? -10.43300 -32.91000 13.49100  1.000 21.46357  ? 173 MET A HB3  1 
ATOM   1983 H  HG2  . MET A  1 173 ? -9.30800  -32.15100 11.54500  1.000 23.66828  ? 173 MET A HG2  1 
ATOM   1984 H  HG3  . MET A  1 173 ? -7.93600  -32.40500 12.30400  1.000 23.66828  ? 173 MET A HG3  1 
ATOM   1985 H  HE1  . MET A  1 173 ? -7.87500  -35.22400 9.89800   1.000 29.62434  ? 173 MET A HE1  1 
ATOM   1986 H  HE2  . MET A  1 173 ? -8.34300  -33.72400 9.65800   1.000 29.62434  ? 173 MET A HE2  1 
ATOM   1987 H  HE3  . MET A  1 173 ? -7.04400  -34.02200 10.52200  1.000 29.62434  ? 173 MET A HE3  1 
ATOM   1988 N  N    . GLY A  1 174 ? -10.40200 -30.81600 16.27500  1.000 15.72704  ? 174 GLY A N    1 
ATOM   1989 C  CA   . GLY A  1 174 ? -11.36300 -30.51200 17.32500  1.000 15.42997  ? 174 GLY A CA   1 
ATOM   1990 C  C    . GLY A  1 174 ? -11.93100 -29.11800 17.23700  1.000 14.74411  ? 174 GLY A C    1 
ATOM   1991 O  O    . GLY A  1 174 ? -13.08000 -28.89300 17.61600  1.000 15.32422  ? 174 GLY A O    1 
ATOM   1992 H  H    . GLY A  1 174 ? -9.59600  -30.93900 16.54900  1.000 18.87501  ? 174 GLY A H    1 
ATOM   1993 H  HA2  . GLY A  1 174 ? -12.09900 -31.14100 17.27100  1.000 18.51852  ? 174 GLY A HA2  1 
ATOM   1994 H  HA3  . GLY A  1 174 ? -10.92900 -30.60700 18.18700  1.000 18.51852  ? 174 GLY A HA3  1 
ATOM   1995 N  N    . GLY A  1 175 ? -11.14300 -28.17500 16.72900  1.000 15.42899  ? 175 GLY A N    1 
ATOM   1996 C  CA   . GLY A  1 175 ? -11.66800 -26.86100 16.39800  1.000 15.45454  ? 175 GLY A CA   1 
ATOM   1997 C  C    . GLY A  1 175 ? -12.62300 -26.86500 15.22900  1.000 16.66504  ? 175 GLY A C    1 
ATOM   1998 O  O    . GLY A  1 175 ? -13.61000 -26.16100 15.25100  1.000 17.48880  ? 175 GLY A O    1 
ATOM   1999 H  H    . GLY A  1 175 ? -10.30400 -28.27100 16.56700  1.000 18.51735  ? 175 GLY A H    1 
ATOM   2000 H  HA2  . GLY A  1 175 ? -12.13900 -26.50700 17.16900  1.000 18.54801  ? 175 GLY A HA2  1 
ATOM   2001 H  HA3  . GLY A  1 175 ? -10.93000 -26.27200 16.18100  1.000 18.54801  ? 175 GLY A HA3  1 
ATOM   2002 N  N    . GLY A  1 176 ? -12.34900 -27.64500 14.19500  1.000 15.99021  ? 176 GLY A N    1 
ATOM   2003 C  CA   . GLY A  1 176 ? -13.35700 -27.82600 13.15900  1.000 16.57223  ? 176 GLY A CA   1 
ATOM   2004 C  C    . GLY A  1 176 ? -14.64600 -28.38700 13.71800  1.000 18.01636  ? 176 GLY A C    1 
ATOM   2005 O  O    . GLY A  1 176 ? -15.73600 -27.93300 13.36400  1.000 17.80626  ? 176 GLY A O    1 
ATOM   2006 H  H    . GLY A  1 176 ? -11.61100 -28.07000 14.07000  1.000 19.19082  ? 176 GLY A H    1 
ATOM   2007 H  HA2  . GLY A  1 176 ? -13.54900 -26.97100 12.74300  1.000 19.88924  ? 176 GLY A HA2  1 
ATOM   2008 H  HA3  . GLY A  1 176 ? -13.02200 -28.43700 12.48500  1.000 19.88924  ? 176 GLY A HA3  1 
ATOM   2009 N  N    . GLY A  1 177 ? -14.54200 -29.35800 14.63100  1.000 16.68700  ? 177 GLY A N    1 
ATOM   2010 C  CA   . GLY A  1 177 ? -15.75000 -29.88300 15.25600  1.000 17.01025  ? 177 GLY A CA   1 
ATOM   2011 C  C    . GLY A  1 177 ? -16.49100 -28.84500 16.07000  1.000 16.70083  ? 177 GLY A C    1 
ATOM   2012 O  O    . GLY A  1 177 ? -17.74100 -28.81900 16.06900  1.000 16.97210  ? 177 GLY A O    1 
ATOM   2013 H  H    . GLY A  1 177 ? -13.80700 -29.71700 14.89600  1.000 20.02697  ? 177 GLY A H    1 
ATOM   2014 H  HA2  . GLY A  1 177 ? -16.34800 -30.21200 14.56700  1.000 20.41486  ? 177 GLY A HA2  1 
ATOM   2015 H  HA3  . GLY A  1 177 ? -15.51200 -30.61700 15.84400  1.000 20.41486  ? 177 GLY A HA3  1 
ATOM   2016 N  N    . THR A  1 178 ? -15.74200 -27.98900 16.76600  1.000 16.36818  ? 178 THR A N    1 
ATOM   2017 C  CA   . THR A  1 178 ? -16.33100 -26.92000 17.57200  1.000 14.92714  ? 178 THR A CA   1 
ATOM   2018 C  C    . THR A  1 178 ? -17.05400 -25.90600 16.71100  1.000 16.16206  ? 178 THR A C    1 
ATOM   2019 O  O    . THR A  1 178 ? -18.19000 -25.51500 17.01400  1.000 17.19711  ? 178 THR A O    1 
ATOM   2020 C  CB   . THR A  1 178 ? -15.21400 -26.24000 18.36600  1.000 15.35120  ? 178 THR A CB   1 
ATOM   2021 O  OG1  . THR A  1 178 ? -14.70100 -27.12300 19.34800  1.000 16.36614  ? 178 THR A OG1  1 
ATOM   2022 C  CG2  . THR A  1 178 ? -15.69500 -25.01500 19.07800  1.000 17.53528  ? 178 THR A CG2  1 
ATOM   2023 H  H    . THR A  1 178 ? -14.88200 -28.00600 16.79100  1.000 19.64438  ? 178 THR A H    1 
ATOM   2024 H  HA   . THR A  1 178 ? -16.98100 -27.29700 18.18500  1.000 17.91513  ? 178 THR A HA   1 
ATOM   2025 H  HB   . THR A  1 178 ? -14.52300 -25.98800 17.73400  1.000 18.42400  ? 178 THR A HB   1 
ATOM   2026 H  HG1  . THR A  1 178 ? -14.39600 -27.81500 18.98100  1.000 19.64193  ? 178 THR A HG1  1 
ATOM   2027 H  HG21 . THR A  1 178 ? -15.02900 -24.72000 19.71800  1.000 21.04490  ? 178 THR A HG21 1 
ATOM   2028 H  HG22 . THR A  1 178 ? -15.85600 -24.30200 18.43900  1.000 21.04490  ? 178 THR A HG22 1 
ATOM   2029 H  HG23 . THR A  1 178 ? -16.52100 -25.20700 19.54900  1.000 21.04490  ? 178 THR A HG23 1 
ATOM   2030 N  N    . LEU A  1 179 ? -16.45900 -25.51500 15.58400  1.000 16.81831  ? 179 LEU A N    1 
ATOM   2031 C  CA   . LEU A  1 179 ? -17.11800 -24.58200 14.67200  1.000 16.71941  ? 179 LEU A CA   1 
ATOM   2032 C  C    . LEU A  1 179 ? -18.33900 -25.20900 14.00600  1.000 19.12512  ? 179 LEU A C    1 
ATOM   2033 O  O    . LEU A  1 179 ? -19.35900 -24.53700 13.77100  1.000 18.62732  ? 179 LEU A O    1 
ATOM   2034 C  CB   . LEU A  1 179 ? -16.09300 -24.10500 13.63700  1.000 19.04704  ? 179 LEU A CB   1 
ATOM   2035 C  CG   . LEU A  1 179 ? -14.99600 -23.24300 14.25600  1.000 20.06622  ? 179 LEU A CG   1 
ATOM   2036 C  CD1  . LEU A  1 179 ? -13.85300 -23.05300 13.21200  1.000 19.63417  ? 179 LEU A CD1  1 
ATOM   2037 C  CD2  . LEU A  1 179 ? -15.44900 -21.90500 14.75400  1.000 24.99735  ? 179 LEU A CD2  1 
ATOM   2038 H  H    . LEU A  1 179 ? -15.68000 -25.77400 15.32500  1.000 20.18453  ? 179 LEU A H    1 
ATOM   2039 H  HA   . LEU A  1 179 ? -17.43900 -23.81100 15.16600  1.000 20.06585  ? 179 LEU A HA   1 
ATOM   2040 H  HB2  . LEU A  1 179 ? -15.67400 -24.87900 13.22700  1.000 22.85902  ? 179 LEU A HB2  1 
ATOM   2041 H  HB3  . LEU A  1 179 ? -16.54700 -23.57800 12.96100  1.000 22.85902  ? 179 LEU A HB3  1 
ATOM   2042 H  HG   . LEU A  1 179 ? -14.68300 -23.71200 15.04500  1.000 24.08202  ? 179 LEU A HG   1 
ATOM   2043 H  HD11 . LEU A  1 179 ? -13.16800 -22.48200 13.59400  1.000 23.56357  ? 179 LEU A HD11 1 
ATOM   2044 H  HD12 . LEU A  1 179 ? -13.47800 -23.92000 12.99400  1.000 23.56357  ? 179 LEU A HD12 1 
ATOM   2045 H  HD13 . LEU A  1 179 ? -14.22000 -22.64100 12.41400  1.000 23.56357  ? 179 LEU A HD13 1 
ATOM   2046 H  HD21 . LEU A  1 179 ? -14.67000 -21.37000 14.97600  1.000 29.99938  ? 179 LEU A HD21 1 
ATOM   2047 H  HD22 . LEU A  1 179 ? -15.96400 -21.46700 14.05900  1.000 29.99938  ? 179 LEU A HD22 1 
ATOM   2048 H  HD23 . LEU A  1 179 ? -15.99900 -22.03200 15.54400  1.000 29.99938  ? 179 LEU A HD23 1 
ATOM   2049 N  N    . ARG A  1 180 ? -18.27500 -26.50600 13.71900  1.000 17.78057  ? 180 ARG A N    1 
ATOM   2050 C  CA   . ARG A  1 180 ? -19.44100 -27.18900 13.17600  1.000 19.23913  ? 180 ARG A CA   1 
ATOM   2051 C  C    . ARG A  1 180 ? -20.60000 -27.17800 14.18300  1.000 18.62913  ? 180 ARG A C    1 
ATOM   2052 O  O    . ARG A  1 180 ? -21.75100 -26.96400 13.80500  1.000 20.36133  ? 180 ARG A O    1 
ATOM   2053 C  CB   . ARG A  1 180 ? -19.09800 -28.61800 12.77300  1.000 18.95423  ? 180 ARG A CB   1 
ATOM   2054 C  CG   . ARG A  1 180 ? -18.26600 -28.72900 11.47700  1.000 19.34593  ? 180 ARG A CG   1 
ATOM   2055 C  CD   . ARG A  1 180 ? -17.65000 -30.10600 11.33300  1.000 19.33993  ? 180 ARG A CD   1 
ATOM   2056 N  NE   . ARG A  1 180 ? -16.95400 -30.26600 10.04800  1.000 18.81815  ? 180 ARG A NE   1 
ATOM   2057 C  CZ   . ARG A  1 180 ? -17.56900 -30.58400 8.91200   1.000 18.30325  ? 180 ARG A CZ   1 
ATOM   2058 N  NH1  . ARG A  1 180 ? -18.88700 -30.78200 8.85900   1.000 20.75906  ? 180 ARG A NH1  1 
ATOM   2059 N  NH2  . ARG A  1 180 ? -16.86000 -30.70500 7.77700   1.000 20.67557  ? 180 ARG A NH2  1 
ATOM   2060 H  H    . ARG A  1 180 ? -17.58100 -27.00300 13.82700  1.000 21.33925  ? 180 ARG A H    1 
ATOM   2061 H  HA   . ARG A  1 180 ? -19.72200 -26.72300 12.37400  1.000 23.08951  ? 180 ARG A HA   1 
ATOM   2062 H  HB2  . ARG A  1 180 ? -18.58600 -29.02700 13.48800  1.000 22.74764  ? 180 ARG A HB2  1 
ATOM   2063 H  HB3  . ARG A  1 180 ? -19.92400 -29.10800 12.63500  1.000 22.74764  ? 180 ARG A HB3  1 
ATOM   2064 H  HG2  . ARG A  1 180 ? -18.84000 -28.56900 10.71200  1.000 23.21768  ? 180 ARG A HG2  1 
ATOM   2065 H  HG3  . ARG A  1 180 ? -17.55100 -28.07400 11.49800  1.000 23.21768  ? 180 ARG A HG3  1 
ATOM   2066 H  HD2  . ARG A  1 180 ? -17.00600 -30.24400 12.04600  1.000 23.21048  ? 180 ARG A HD2  1 
ATOM   2067 H  HD3  . ARG A  1 180 ? -18.35000 -30.77600 11.38400  1.000 23.21048  ? 180 ARG A HD3  1 
ATOM   2068 H  HE   . ARG A  1 180 ? -16.10200 -30.14700 10.02900  1.000 22.58434  ? 180 ARG A HE   1 
ATOM   2069 H  HH11 . ARG A  1 180 ? -19.36200 -30.70600 9.57200   1.000 24.91344  ? 180 ARG A HH11 1 
ATOM   2070 H  HH12 . ARG A  1 180 ? -19.26100 -30.98700 8.11300   1.000 24.91344  ? 180 ARG A HH12 1 
ATOM   2071 H  HH21 . ARG A  1 180 ? -16.01000 -30.57600 7.78600   1.000 24.81324  ? 180 ARG A HH21 1 
ATOM   2072 H  HH22 . ARG A  1 180 ? -17.25700 -30.91000 7.04200   1.000 24.81324  ? 180 ARG A HH22 1 
ATOM   2073 N  N    . LEU A  1 181 ? -20.31600 -27.46400 15.44900  1.000 18.28436  ? 181 LEU A N    1 
ATOM   2074 C  CA   . LEU A  1 181 ? -21.36500 -27.39800 16.46700  1.000 17.90482  ? 181 LEU A CA   1 
ATOM   2075 C  C    . LEU A  1 181 ? -21.89200 -25.97700 16.60000  1.000 16.22428  ? 181 LEU A C    1 
ATOM   2076 O  O    . LEU A  1 181 ? -23.12300 -25.75400 16.71900  1.000 18.39116  ? 181 LEU A O    1 
ATOM   2077 C  CB   . LEU A  1 181 ? -20.82900 -27.91200 17.80500  1.000 17.75694  ? 181 LEU A CB   1 
ATOM   2078 C  CG   . LEU A  1 181 ? -21.90400 -28.08200 18.91500  1.000 17.39307  ? 181 LEU A CG   1 
ATOM   2079 C  CD1  . LEU A  1 181 ? -23.00700 -29.00600 18.47900  1.000 21.26147  ? 181 LEU A CD1  1 
ATOM   2080 C  CD2  . LEU A  1 181 ? -21.19500 -28.58500 20.15200  1.000 19.00746  ? 181 LEU A CD2  1 
ATOM   2081 H  H    . LEU A  1 181 ? -19.54100 -27.69400 15.74200  1.000 21.94380  ? 181 LEU A H    1 
ATOM   2082 H  HA   . LEU A  1 181 ? -22.10300 -27.97100 16.20800  1.000 21.48834  ? 181 LEU A HA   1 
ATOM   2083 H  HB2  . LEU A  1 181 ? -20.42000 -28.78000 17.65800  1.000 21.31089  ? 181 LEU A HB2  1 
ATOM   2084 H  HB3  . LEU A  1 181 ? -20.16700 -27.28400 18.13200  1.000 21.31089  ? 181 LEU A HB3  1 
ATOM   2085 H  HG   . LEU A  1 181 ? -22.34100 -27.23800 19.11000  1.000 20.87424  ? 181 LEU A HG   1 
ATOM   2086 H  HD11 . LEU A  1 181 ? -23.56500 -29.21600 19.24400  1.000 25.51632  ? 181 LEU A HD11 1 
ATOM   2087 H  HD12 . LEU A  1 181 ? -23.53600 -28.56500 17.79500  1.000 25.51632  ? 181 LEU A HD12 1 
ATOM   2088 H  HD13 . LEU A  1 181 ? -22.61600 -29.81800 18.12100  1.000 25.51632  ? 181 LEU A HD13 1 
ATOM   2089 H  HD21 . LEU A  1 181 ? -21.85100 -28.74700 20.84800  1.000 22.81151  ? 181 LEU A HD21 1 
ATOM   2090 H  HD22 . LEU A  1 181 ? -20.73100 -29.41000 19.93700  1.000 22.81151  ? 181 LEU A HD22 1 
ATOM   2091 H  HD23 . LEU A  1 181 ? -20.55900 -27.91500 20.44600  1.000 22.81151  ? 181 LEU A HD23 1 
ATOM   2092 N  N    . ALA A  1 182 ? -20.99800 -24.99600 16.55200  1.000 18.54785  ? 182 ALA A N    1 
ATOM   2093 C  CA   . ALA A  1 182 ? -21.43700 -23.60800 16.57500  1.000 19.37412  ? 182 ALA A CA   1 
ATOM   2094 C  C    . ALA A  1 182 ? -22.36000 -23.27700 15.41000  1.000 19.77622  ? 182 ALA A C    1 
ATOM   2095 O  O    . ALA A  1 182 ? -23.29100 -22.47400 15.55100  1.000 22.03995  ? 182 ALA A O    1 
ATOM   2096 C  CB   . ALA A  1 182 ? -20.27000 -22.66200 16.60200  1.000 19.30639  ? 182 ALA A CB   1 
ATOM   2097 H  H    . ALA A  1 182 ? -20.14600 -25.10600 16.50700  1.000 22.25998  ? 182 ALA A H    1 
ATOM   2098 H  HA   . ALA A  1 182 ? -21.93300 -23.47500 17.39800  1.000 23.25151  ? 182 ALA A HA   1 
ATOM   2099 H  HB1  . ALA A  1 182 ? -20.60200 -21.75000 16.59000  1.000 23.17023  ? 182 ALA A HB1  1 
ATOM   2100 H  HB2  . ALA A  1 182 ? -19.75700 -22.81600 17.41100  1.000 23.17023  ? 182 ALA A HB2  1 
ATOM   2101 H  HB3  . ALA A  1 182 ? -19.71500 -22.82300 15.82300  1.000 23.17023  ? 182 ALA A HB3  1 
ATOM   2102 N  N    . ALA A  1 183 ? -22.15500 -23.88600 14.23600  1.000 19.56786  ? 183 ALA A N    1 
ATOM   2103 C  CA   . ALA A  1 183 ? -23.00100 -23.63700 13.08300  1.000 19.88242  ? 183 ALA A CA   1 
ATOM   2104 C  C    . ALA A  1 183 ? -24.42700 -24.12400 13.29500  1.000 22.10991  ? 183 ALA A C    1 
ATOM   2105 O  O    . ALA A  1 183 ? -25.32500 -23.69500 12.57700  1.000 24.95993  ? 183 ALA A O    1 
ATOM   2106 C  CB   . ALA A  1 183 ? -22.33700 -24.31300 11.88600  1.000 23.37831  ? 183 ALA A CB   1 
ATOM   2107 H  H    . ALA A  1 183 ? -21.52500 -24.45200 14.08700  1.000 23.48400  ? 183 ALA A H    1 
ATOM   2108 H  HA   . ALA A  1 183 ? -23.08000 -22.68800 12.90000  1.000 23.86147  ? 183 ALA A HA   1 
ATOM   2109 H  HB1  . ALA A  1 183 ? -22.87800 -24.16000 11.09600  1.000 28.05653  ? 183 ALA A HB1  1 
ATOM   2110 H  HB2  . ALA A  1 183 ? -21.45300 -23.93400 11.76000  1.000 28.05653  ? 183 ALA A HB2  1 
ATOM   2111 H  HB3  . ALA A  1 183 ? -22.26700 -25.26500 12.06000  1.000 28.05653  ? 183 ALA A HB3  1 
ATOM   2112 N  N    . ASP A  1 184 ? -24.66700 -25.00400 14.26100  1.000 22.00365  ? 184 ASP A N    1 
ATOM   2113 C  CA   . ASP A  1 184 ? -26.02200 -25.39700 14.59500  1.000 22.14337  ? 184 ASP A CA   1 
ATOM   2114 C  C    . ASP A  1 184 ? -26.58200 -24.60500 15.76000  1.000 22.80319  ? 184 ASP A C    1 
ATOM   2115 O  O    . ASP A  1 184 ? -27.70800 -24.89300 16.20700  1.000 25.10547  ? 184 ASP A O    1 
ATOM   2116 C  CB   . ASP A  1 184 ? -26.06900 -26.87800 14.99300  1.000 25.96147  ? 184 ASP A CB   1 
ATOM   2117 C  CG   . ASP A  1 184 ? -25.85900 -27.81200 13.79100  1.000 32.04402  ? 184 ASP A CG   1 
ATOM   2118 O  OD1  . ASP A  1 184 ? -26.19600 -27.43100 12.65200  1.000 33.46990  ? 184 ASP A OD1  1 
ATOM   2119 O  OD2  . ASP A  1 184 ? -25.40800 -28.94900 14.00200  1.000 36.13052  ? 184 ASP A OD2  1 
ATOM   2120 H  H    . ASP A  1 184 ? -24.05900 -25.38600 14.73400  1.000 26.40694  ? 184 ASP A H    1 
ATOM   2121 H  HA   . ASP A  1 184 ? -26.57200 -25.26000 13.80800  1.000 26.57460  ? 184 ASP A HA   1 
ATOM   2122 H  HB2  . ASP A  1 184 ? -25.36900 -27.05600 15.64000  1.000 31.15633  ? 184 ASP A HB2  1 
ATOM   2123 H  HB3  . ASP A  1 184 ? -26.93600 -27.07600 15.38100  1.000 31.15633  ? 184 ASP A HB3  1 
ATOM   2124 N  N    . ASP A  1 185 ? -25.85800 -23.61100 16.25500  1.000 22.50708  ? 185 ASP A N    1 
ATOM   2125 C  CA   . ASP A  1 185 ? -26.15800 -22.98500 17.53900  1.000 25.07401  ? 185 ASP A CA   1 
ATOM   2126 C  C    . ASP A  1 185 ? -26.22400 -24.01200 18.68400  1.000 22.97959  ? 185 ASP A C    1 
ATOM   2127 O  O    . ASP A  1 185 ? -27.01000 -23.88900 19.63100  1.000 23.58362  ? 185 ASP A O    1 
ATOM   2128 C  CB   . ASP A  1 185 ? -27.40800 -22.13200 17.50800  1.000 26.74266  ? 185 ASP A CB   1 
ATOM   2129 C  CG   . ASP A  1 185 ? -27.27200 -20.88900 18.35900  1.000 47.52689  ? 185 ASP A CG   1 
ATOM   2130 O  OD1  . ASP A  1 185 ? -26.21500 -20.20900 18.27700  1.000 35.42608  ? 185 ASP A OD1  1 
ATOM   2131 O  OD2  . ASP A  1 185 ? -28.20500 -20.60100 19.12000  1.000 39.01996  ? 185 ASP A OD2  1 
ATOM   2132 H  H    . ASP A  1 185 ? -25.17300 -23.27300 15.86000  1.000 27.01106  ? 185 ASP A H    1 
ATOM   2133 H  HA   . ASP A  1 185 ? -25.41700 -22.38700 17.72400  1.000 30.09138  ? 185 ASP A HA   1 
ATOM   2134 H  HB2  . ASP A  1 185 ? -27.58200 -21.85600 16.59400  1.000 32.09376  ? 185 ASP A HB2  1 
ATOM   2135 H  HB3  . ASP A  1 185 ? -28.15500 -22.65000 17.84600  1.000 32.09376  ? 185 ASP A HB3  1 
ATOM   2136 N  N    . GLY A  1 186 ? -25.30200 -25.00900 18.63300  1.000 23.01691  ? 186 GLY A N    1 
ATOM   2137 C  CA   . GLY A  1 186 ? -25.26600 -26.00400 19.68300  1.000 24.30000  ? 186 GLY A CA   1 
ATOM   2138 C  C    . GLY A  1 186 ? -24.49000 -25.58600 20.89300  1.000 21.02666  ? 186 GLY A C    1 
ATOM   2139 O  O    . GLY A  1 186 ? -24.37100 -26.38500 21.83200  1.000 22.68555  ? 186 GLY A O    1 
ATOM   2140 H  H    . GLY A  1 186 ? -24.71600 -25.10900 18.01200  1.000 27.62285  ? 186 GLY A H    1 
ATOM   2141 H  HA2  . GLY A  1 186 ? -26.17500 -26.19800 19.96300  1.000 29.16256  ? 186 GLY A HA2  1 
ATOM   2142 H  HA3  . GLY A  1 186 ? -24.86300 -26.81400 19.33400  1.000 29.16256  ? 186 GLY A HA3  1 
ATOM   2143 N  N    . ILE A  1 187 ? -23.99100 -24.34700 20.91300  1.000 21.99933  ? 187 ILE A N    1 
ATOM   2144 C  CA   . ILE A  1 187 ? -23.17000 -23.80600 22.01400  1.000 17.53233  ? 187 ILE A CA   1 
ATOM   2145 C  C    . ILE A  1 187 ? -23.44100 -22.29100 22.05300  1.000 19.41194  ? 187 ILE A C    1 
ATOM   2146 O  O    . ILE A  1 187 ? -23.75100 -21.67200 21.02500  1.000 22.46722  ? 187 ILE A O    1 
ATOM   2147 C  CB   . ILE A  1 187 ? -21.65900 -24.10600 21.93200  1.000 22.43262  ? 187 ILE A CB   1 
ATOM   2148 C  CG1  . ILE A  1 187 ? -21.16800 -24.13000 20.46800  1.000 20.95176  ? 187 ILE A CG1  1 
ATOM   2149 C  CG2  . ILE A  1 187 ? -21.28900 -25.43400 22.62900  1.000 21.01659  ? 187 ILE A CG2  1 
ATOM   2150 C  CD1  . ILE A  1 187 ? -19.69000 -24.43900 20.29800  1.000 21.36644  ? 187 ILE A CD1  1 
ATOM   2151 H  H    . ILE A  1 187 ? -24.11400 -23.77800 20.28100  1.000 26.40176  ? 187 ILE A H    1 
ATOM   2152 H  HA   . ILE A  1 187 ? -23.45800 -24.23200 22.83700  1.000 21.04136  ? 187 ILE A HA   1 
ATOM   2153 H  HB   . ILE A  1 187 ? -21.21400 -23.38300 22.40100  1.000 26.92170  ? 187 ILE A HB   1 
ATOM   2154 H  HG12 . ILE A  1 187 ? -21.66500 -24.81000 19.98700  1.000 25.14468  ? 187 ILE A HG12 1 
ATOM   2155 H  HG13 . ILE A  1 187 ? -21.33100 -23.25900 20.07400  1.000 25.14468  ? 187 ILE A HG13 1 
ATOM   2156 H  HG21 . ILE A  1 187 ? -20.33000 -25.46000 22.77200  1.000 25.22246  ? 187 ILE A HG21 1 
ATOM   2157 H  HG22 . ILE A  1 187 ? -21.75100 -25.48300 23.48100  1.000 25.22246  ? 187 ILE A HG22 1 
ATOM   2158 H  HG23 . ILE A  1 187 ? -21.55900 -26.17400 22.06300  1.000 25.22246  ? 187 ILE A HG23 1 
ATOM   2159 H  HD11 . ILE A  1 187 ? -19.41400 -24.18400 19.40400  1.000 25.64229  ? 187 ILE A HD11 1 
ATOM   2160 H  HD12 . ILE A  1 187 ? -19.18400 -23.93600 20.95600  1.000 25.64229  ? 187 ILE A HD12 1 
ATOM   2161 H  HD13 . ILE A  1 187 ? -19.54900 -25.39000 20.42900  1.000 25.64229  ? 187 ILE A HD13 1 
ATOM   2162 N  N    . GLN A  1 188 ? -23.23000 -21.66800 23.22800  1.000 16.17920  ? 188 GLN A N    1 
ATOM   2163 C  CA   . GLN A  1 188 ? -23.32400 -20.24700 23.48900  1.000 16.35770  ? 188 GLN A CA   1 
ATOM   2164 C  C    . GLN A  1 188 ? -21.98400 -19.50800 23.38300  1.000 15.94470  ? 188 GLN A C    1 
ATOM   2165 O  O    . GLN A  1 188 ? -21.97200 -18.26700 23.39900  1.000 18.04904  ? 188 GLN A O    1 
ATOM   2166 C  CB   . GLN A  1 188 ? -23.94400 -20.02700 24.88500  1.000 16.76431  ? 188 GLN A CB   1 
ATOM   2167 C  CG   . GLN A  1 188 ? -25.43800 -20.27700 24.93600  1.000 17.67114  ? 188 GLN A CG   1 
ATOM   2168 C  CD   . GLN A  1 188 ? -25.81900 -21.69300 24.71700  1.000 19.42330  ? 188 GLN A CD   1 
ATOM   2169 O  OE1  . GLN A  1 188 ? -25.34800 -22.60200 25.40100  1.000 17.36049  ? 188 GLN A OE1  1 
ATOM   2170 N  NE2  . GLN A  1 188 ? -26.73100 -21.91400 23.77300  1.000 21.32999  ? 188 GLN A NE2  1 
ATOM   2171 H  H    . GLN A  1 188 ? -23.01400 -22.09600 23.94200  1.000 19.41760  ? 188 GLN A H    1 
ATOM   2172 H  HA   . GLN A  1 188 ? -23.90900 -19.84300 22.82900  1.000 19.63180  ? 188 GLN A HA   1 
ATOM   2173 H  HB2  . GLN A  1 188 ? -23.52100 -20.63300 25.51300  1.000 20.11974  ? 188 GLN A HB2  1 
ATOM   2174 H  HB3  . GLN A  1 188 ? -23.78900 -19.10800 25.15400  1.000 20.11974  ? 188 GLN A HB3  1 
ATOM   2175 H  HG2  . GLN A  1 188 ? -25.76800 -20.01500 25.81000  1.000 21.20793  ? 188 GLN A HG2  1 
ATOM   2176 H  HG3  . GLN A  1 188 ? -25.86700 -19.74600 24.24700  1.000 21.20793  ? 188 GLN A HG3  1 
ATOM   2177 H  HE21 . GLN A  1 188 ? -27.06200 -21.25400 23.33300  1.000 25.59855  ? 188 GLN A HE21 1 
ATOM   2178 H  HE22 . GLN A  1 188 ? -26.98900 -22.71600 23.60400  1.000 25.59855  ? 188 GLN A HE22 1 
ATOM   2179 N  N    . ALA A  1 189 ? -20.86700 -20.22300 23.23400  1.000 14.68902  ? 189 ALA A N    1 
ATOM   2180 C  CA   . ALA A  1 189 ? -19.56000 -19.62500 22.99000  1.000 15.96198  ? 189 ALA A CA   1 
ATOM   2181 C  C    . ALA A  1 189 ? -18.65400 -20.70400 22.44600  1.000 14.52335  ? 189 ALA A C    1 
ATOM   2182 O  O    . ALA A  1 189 ? -18.75100 -21.86700 22.83100  1.000 15.43368  ? 189 ALA A O    1 
ATOM   2183 C  CB   . ALA A  1 189 ? -18.92400 -19.00300 24.21600  1.000 16.12981  ? 189 ALA A CB   1 
ATOM   2184 H  H    . ALA A  1 189 ? -20.84200 -21.08200 23.27000  1.000 17.62939  ? 189 ALA A H    1 
ATOM   2185 H  HA   . ALA A  1 189 ? -19.67200 -18.91300 22.34100  1.000 19.15694  ? 189 ALA A HA   1 
ATOM   2186 H  HB1  . ALA A  1 189 ? -18.07800 -18.60100 23.96300  1.000 19.35833  ? 189 ALA A HB1  1 
ATOM   2187 H  HB2  . ALA A  1 189 ? -19.52000 -18.32500 24.57100  1.000 19.35833  ? 189 ALA A HB2  1 
ATOM   2188 H  HB3  . ALA A  1 189 ? -18.77700 -19.69500 24.88000  1.000 19.35833  ? 189 ALA A HB3  1 
ATOM   2189 N  N    . ALA A  1 190 ? -17.75600 -20.30000 21.53000  1.000 15.04518  ? 190 ALA A N    1 
ATOM   2190 C  CA   . ALA A  1 190 ? -16.80500 -21.20700 20.90600  1.000 13.83273  ? 190 ALA A CA   1 
ATOM   2191 C  C    . ALA A  1 190 ? -15.42800 -20.57200 20.86900  1.000 14.34393  ? 190 ALA A C    1 
ATOM   2192 O  O    . ALA A  1 190 ? -15.28800 -19.37500 20.56600  1.000 15.71487  ? 190 ALA A O    1 
ATOM   2193 C  CB   . ALA A  1 190 ? -17.25600 -21.51700 19.48300  1.000 16.89797  ? 190 ALA A CB   1 
ATOM   2194 H  H    . ALA A  1 190 ? -17.68400 -19.48800 21.25600  1.000 18.05677  ? 190 ALA A H    1 
ATOM   2195 H  HA   . ALA A  1 190 ? -16.73600 -22.02600 21.42200  1.000 16.60183  ? 190 ALA A HA   1 
ATOM   2196 H  HB1  . ALA A  1 190 ? -16.59800 -22.09100 19.06100  1.000 20.28013  ? 190 ALA A HB1  1 
ATOM   2197 H  HB2  . ALA A  1 190 ? -18.11500 -21.96600 19.51500  1.000 20.28013  ? 190 ALA A HB2  1 
ATOM   2198 H  HB3  . ALA A  1 190 ? -17.33500 -20.68600 18.98900  1.000 20.28013  ? 190 ALA A HB3  1 
ATOM   2199 N  N    . ILE A  1 191 ? -14.40900 -21.40300 21.11500  1.000 13.80371  ? 191 ILE A N    1 
ATOM   2200 C  CA   . ILE A  1 191 ? -13.01700 -21.02700 20.90200  1.000 14.05415  ? 191 ILE A CA   1 
ATOM   2201 C  C    . ILE A  1 191 ? -12.37600 -22.07500 20.02000  1.000 14.36178  ? 191 ILE A C    1 
ATOM   2202 O  O    . ILE A  1 191 ? -12.39900 -23.26900 20.35500  1.000 14.76696  ? 191 ILE A O    1 
ATOM   2203 C  CB   . ILE A  1 191 ? -12.23400 -20.87600 22.21900  1.000 13.05497  ? 191 ILE A CB   1 
ATOM   2204 C  CG1  . ILE A  1 191 ? -12.89600 -19.84700 23.13100  1.000 13.95134  ? 191 ILE A CG1  1 
ATOM   2205 C  CG2  . ILE A  1 191 ? -10.78500 -20.56300 21.91300  1.000 14.63163  ? 191 ILE A CG2  1 
ATOM   2206 C  CD1  . ILE A  1 191 ? -12.21400 -19.68300 24.47200  1.000 15.91029  ? 191 ILE A CD1  1 
ATOM   2207 H  H    . ILE A  1 191 ? -14.50700 -22.20500 21.41100  1.000 16.56701  ? 191 ILE A H    1 
ATOM   2208 H  HA   . ILE A  1 191 ? -12.98900 -20.17300 20.44400  1.000 16.86754  ? 191 ILE A HA   1 
ATOM   2209 H  HB   . ILE A  1 191 ? -12.25200 -21.71400 22.70800  1.000 15.66853  ? 191 ILE A HB   1 
ATOM   2210 H  HG12 . ILE A  1 191 ? -12.88400 -18.98400 22.68700  1.000 16.74417  ? 191 ILE A HG12 1 
ATOM   2211 H  HG13 . ILE A  1 191 ? -13.81100 -20.12200 23.29700  1.000 16.74417  ? 191 ILE A HG13 1 
ATOM   2212 H  HG21 . ILE A  1 191 ? -10.30800 -20.42800 22.74600  1.000 17.56052  ? 191 ILE A HG21 1 
ATOM   2213 H  HG22 . ILE A  1 191 ? -10.39700 -21.30700 21.42600  1.000 17.56052  ? 191 ILE A HG22 1 
ATOM   2214 H  HG23 . ILE A  1 191 ? -10.74300 -19.75700 21.37400  1.000 17.56052  ? 191 ILE A HG23 1 
ATOM   2215 H  HD11 . ILE A  1 191 ? -12.79200 -19.17100 25.06000  1.000 19.09491  ? 191 ILE A HD11 1 
ATOM   2216 H  HD12 . ILE A  1 191 ? -12.04900 -20.56000 24.85200  1.000 19.09491  ? 191 ILE A HD12 1 
ATOM   2217 H  HD13 . ILE A  1 191 ? -11.37400 -19.21400 24.34400  1.000 19.09491  ? 191 ILE A HD13 1 
ATOM   2218 N  N    . GLY A  1 192 ? -11.77000 -21.62400 18.93600  1.000 14.83907  ? 192 GLY A N    1 
ATOM   2219 C  CA   . GLY A  1 192 ? -10.95800 -22.48100 18.06600  1.000 15.10686  ? 192 GLY A CA   1 
ATOM   2220 C  C    . GLY A  1 192 ? -9.47700  -22.23400 18.31200  1.000 15.38962  ? 192 GLY A C    1 
ATOM   2221 O  O    . GLY A  1 192 ? -9.02000  -21.08600 18.30900  1.000 16.66613  ? 192 GLY A O    1 
ATOM   2222 H  H    . GLY A  1 192 ? -11.80900 -20.80700 18.66900  1.000 17.80945  ? 192 GLY A H    1 
ATOM   2223 H  HA2  . GLY A  1 192 ? -11.15500 -23.41300 18.24600  1.000 18.13079  ? 192 GLY A HA2  1 
ATOM   2224 H  HA3  . GLY A  1 192 ? -11.15800 -22.29000 17.13700  1.000 18.13079  ? 192 GLY A HA3  1 
ATOM   2225 N  N    . LEU A  1 193 ? -8.75200  -23.31300 18.56100  1.000 14.69924  ? 193 LEU A N    1 
ATOM   2226 C  CA   . LEU A  1 193 ? -7.29700  -23.27200 18.77800  1.000 13.71515  ? 193 LEU A CA   1 
ATOM   2227 C  C    . LEU A  1 193 ? -6.65200  -23.84500 17.52500  1.000 14.26251  ? 193 LEU A C    1 
ATOM   2228 O  O    . LEU A  1 193 ? -6.75800  -25.04100 17.27800  1.000 14.67683  ? 193 LEU A O    1 
ATOM   2229 C  CB   . LEU A  1 193 ? -6.92600  -24.15500 19.98700  1.000 14.87193  ? 193 LEU A CB   1 
ATOM   2230 C  CG   . LEU A  1 193 ? -7.72800  -23.98900 21.28700  1.000 12.88173  ? 193 LEU A CG   1 
ATOM   2231 C  CD1  . LEU A  1 193 ? -7.32900  -25.08300 22.25000  1.000 14.37506  ? 193 LEU A CD1  1 
ATOM   2232 C  CD2  . LEU A  1 193 ? -7.57000  -22.61000 21.85900  1.000 14.35688  ? 193 LEU A CD2  1 
ATOM   2233 H  H    . LEU A  1 193 ? -9.08100  -24.10600 18.61300  1.000 17.64165  ? 193 LEU A H    1 
ATOM   2234 H  HA   . LEU A  1 193 ? -6.99900  -22.36200 18.93000  1.000 16.46075  ? 193 LEU A HA   1 
ATOM   2235 H  HB2  . LEU A  1 193 ? -7.02700  -25.08100 19.71600  1.000 17.84888  ? 193 LEU A HB2  1 
ATOM   2236 H  HB3  . LEU A  1 193 ? -5.99900  -23.97400 20.20900  1.000 17.84888  ? 193 LEU A HB3  1 
ATOM   2237 H  HG   . LEU A  1 193 ? -8.67800  -24.07900 21.11300  1.000 15.46064  ? 193 LEU A HG   1 
ATOM   2238 H  HD11 . LEU A  1 193 ? -7.74600  -24.91500 23.10900  1.000 17.25264  ? 193 LEU A HD11 1 
ATOM   2239 H  HD12 . LEU A  1 193 ? -7.62600  -25.93700 21.89900  1.000 17.25264  ? 193 LEU A HD12 1 
ATOM   2240 H  HD13 . LEU A  1 193 ? -6.36300  -25.08200 22.34500  1.000 17.25264  ? 193 LEU A HD13 1 
ATOM   2241 H  HD21 . LEU A  1 193 ? -8.01400  -22.57300 22.72100  1.000 17.23082  ? 193 LEU A HD21 1 
ATOM   2242 H  HD22 . LEU A  1 193 ? -6.62500  -22.41800 21.96500  1.000 17.23082  ? 193 LEU A HD22 1 
ATOM   2243 H  HD23 . LEU A  1 193 ? -7.97200  -21.96800 21.25200  1.000 17.23082  ? 193 LEU A HD23 1 
ATOM   2244 N  N    . ALA A  1 194 ? -6.04000  -23.03000 16.69100  1.000 14.89680  ? 194 ALA A N    1 
ATOM   2245 C  CA   . ALA A  1 194 ? -5.43500  -23.49200 15.44700  1.000 16.44693  ? 194 ALA A CA   1 
ATOM   2246 C  C    . ALA A  1 194 ? -6.38900  -24.45500 14.72900  1.000 15.62603  ? 194 ALA A C    1 
ATOM   2247 O  O    . ALA A  1 194 ? -6.03900  -25.59100 14.42600  1.000 16.40856  ? 194 ALA A O    1 
ATOM   2248 C  CB   . ALA A  1 194 ? -4.07300  -24.15000 15.68400  1.000 16.12401  ? 194 ALA A CB   1 
ATOM   2249 H  H    . ALA A  1 194 ? -5.95700  -22.18400 16.82400  1.000 17.87872  ? 194 ALA A H    1 
ATOM   2250 H  HA   . ALA A  1 194 ? -5.27800  -22.72700 14.87300  1.000 19.73888  ? 194 ALA A HA   1 
ATOM   2251 H  HB1  . ALA A  1 194 ? -3.67900  -24.37800 14.82700  1.000 19.35138  ? 194 ALA A HB1  1 
ATOM   2252 H  HB2  . ALA A  1 194 ? -3.49900  -23.52600 16.15600  1.000 19.35138  ? 194 ALA A HB2  1 
ATOM   2253 H  HB3  . ALA A  1 194 ? -4.19700  -24.95200 16.21500  1.000 19.35138  ? 194 ALA A HB3  1 
ATOM   2254 N  N    . PRO A  1 195 ? -7.62900  -24.01000 14.45600  1.000 15.60588  ? 195 PRO A N    1 
ATOM   2255 C  CA   . PRO A  1 195 ? -8.63200  -24.93600 13.91600  1.000 16.10152  ? 195 PRO A CA   1 
ATOM   2256 C  C    . PRO A  1 195 ? -8.29700  -25.44800 12.52100  1.000 16.94464  ? 195 PRO A C    1 
ATOM   2257 O  O    . PRO A  1 195 ? -7.65500  -24.77700 11.71300  1.000 17.58384  ? 195 PRO A O    1 
ATOM   2258 C  CB   . PRO A  1 195 ? -9.91700  -24.07900 13.89900  1.000 18.06000  ? 195 PRO A CB   1 
ATOM   2259 C  CG   . PRO A  1 195 ? -9.39100  -22.66400 13.69700  1.000 17.65866  ? 195 PRO A CG   1 
ATOM   2260 C  CD   . PRO A  1 195 ? -8.14100  -22.64100 14.62300  1.000 15.38238  ? 195 PRO A CD   1 
ATOM   2261 H  HA   . PRO A  1 195 ? -8.73100  -25.69900 14.50700  1.000 19.32439  ? 195 PRO A HA   1 
ATOM   2262 H  HB2  . PRO A  1 195 ? -10.49400 -24.34900 13.16800  1.000 21.67456  ? 195 PRO A HB2  1 
ATOM   2263 H  HB3  . PRO A  1 195 ? -10.38900 -24.16300 14.74300  1.000 21.67456  ? 195 PRO A HB3  1 
ATOM   2264 H  HG2  . PRO A  1 195 ? -9.14900  -22.51900 12.76800  1.000 21.19295  ? 195 PRO A HG2  1 
ATOM   2265 H  HG3  . PRO A  1 195 ? -10.05200 -22.01000 13.97300  1.000 21.19295  ? 195 PRO A HG3  1 
ATOM   2266 H  HD2  . PRO A  1 195 ? -7.49300  -21.98400 14.32500  1.000 18.46142  ? 195 PRO A HD2  1 
ATOM   2267 H  HD3  . PRO A  1 195 ? -8.38900  -22.46700 15.54500  1.000 18.46142  ? 195 PRO A HD3  1 
ATOM   2268 N  N    . TRP A  1 196 ? -8.76300  -26.67400 12.25200  1.000 17.15674  ? 196 TRP A N    1 
ATOM   2269 C  CA   . TRP A  1 196 ? -8.65000  -27.36400 10.96400  1.000 18.06659  ? 196 TRP A CA   1 
ATOM   2270 C  C    . TRP A  1 196 ? -10.04500 -27.86700 10.60800  1.000 16.40841  ? 196 TRP A C    1 
ATOM   2271 O  O    . TRP A  1 196 ? -10.75000 -28.41900 11.44400  1.000 18.08642  ? 196 TRP A O    1 
ATOM   2272 C  CB   . TRP A  1 196 ? -7.68600  -28.55600 11.07500  1.000 17.43178  ? 196 TRP A CB   1 
ATOM   2273 C  CG   . TRP A  1 196 ? -7.34500  -29.22700 9.78000   1.000 18.42632  ? 196 TRP A CG   1 
ATOM   2274 C  CD1  . TRP A  1 196 ? -6.19000  -29.07700 9.07000   1.000 19.90045  ? 196 TRP A CD1  1 
ATOM   2275 C  CD2  . TRP A  1 196 ? -8.15000  -30.14700 9.02600   1.000 19.56141  ? 196 TRP A CD2  1 
ATOM   2276 N  NE1  . TRP A  1 196 ? -6.22100  -29.83700 7.93300   1.000 22.93053  ? 196 TRP A NE1  1 
ATOM   2277 C  CE2  . TRP A  1 196 ? -7.41000  -30.50500 7.87600   1.000 19.72971  ? 196 TRP A CE2  1 
ATOM   2278 C  CE3  . TRP A  1 196 ? -9.42800  -30.69800 9.20600   1.000 19.12663  ? 196 TRP A CE3  1 
ATOM   2279 C  CZ2  . TRP A  1 196 ? -7.89800  -31.37500 6.90800   1.000 22.32054  ? 196 TRP A CZ2  1 
ATOM   2280 C  CZ3  . TRP A  1 196 ? -9.90700  -31.56400 8.24800   1.000 22.30741  ? 196 TRP A CZ3  1 
ATOM   2281 C  CH2  . TRP A  1 196 ? -9.15100  -31.89300 7.11200   1.000 24.04824  ? 196 TRP A CH2  1 
ATOM   2282 H  H    . TRP A  1 196 ? -9.17300  -27.15400 12.83700  1.000 20.59066  ? 196 TRP A H    1 
ATOM   2283 H  HA   . TRP A  1 196 ? -8.32400  -26.76700 10.27300  1.000 21.68247  ? 196 TRP A HA   1 
ATOM   2284 H  HB2  . TRP A  1 196 ? -6.85500  -28.24100 11.46500  1.000 20.92070  ? 196 TRP A HB2  1 
ATOM   2285 H  HB3  . TRP A  1 196 ? -8.09000  -29.22400 11.64900  1.000 20.92070  ? 196 TRP A HB3  1 
ATOM   2286 H  HD1  . TRP A  1 196 ? -5.48000  -28.53400 9.32400   1.000 23.88311  ? 196 TRP A HD1  1 
ATOM   2287 H  HE1  . TRP A  1 196 ? -5.59300  -29.88500 7.34800   1.000 27.51920  ? 196 TRP A HE1  1 
ATOM   2288 H  HE3  . TRP A  1 196 ? -9.93900  -30.48400 9.95400   1.000 22.95452  ? 196 TRP A HE3  1 
ATOM   2289 H  HZ2  . TRP A  1 196 ? -7.39700  -31.59500 6.15500   1.000 26.78721  ? 196 TRP A HZ2  1 
ATOM   2290 H  HZ3  . TRP A  1 196 ? -10.75100 -31.94000 8.35600   1.000 26.77146  ? 196 TRP A HZ3  1 
ATOM   2291 H  HH2  . TRP A  1 196 ? -9.50900  -32.47700 6.48200   1.000 28.86045  ? 196 TRP A HH2  1 
ATOM   2292 N  N    . ASN A  1 197 ? -10.44200 -27.64500 9.36700   1.000 17.74755  ? 197 ASN A N    1 
ATOM   2293 C  CA   . ASN A  1 197 ? -11.68700 -28.18000 8.83600   1.000 18.34773  ? 197 ASN A CA   1 
ATOM   2294 C  C    . ASN A  1 197 ? -11.53700 -28.29500 7.32400   1.000 19.60465  ? 197 ASN A C    1 
ATOM   2295 O  O    . ASN A  1 197 ? -10.75100 -27.57200 6.71200   1.000 21.16778  ? 197 ASN A O    1 
ATOM   2296 C  CB   . ASN A  1 197 ? -12.89700 -27.27100 9.15200   1.000 20.11464  ? 197 ASN A CB   1 
ATOM   2297 C  CG   . ASN A  1 197 ? -14.20700 -28.01800 9.12300   1.000 19.96855  ? 197 ASN A CG   1 
ATOM   2298 O  OD1  . ASN A  1 197 ? -14.42000 -28.92200 9.91300   1.000 18.62386  ? 197 ASN A OD1  1 
ATOM   2299 N  ND2  . ASN A  1 197 ? -15.09900 -27.62500 8.20300   1.000 19.90466  ? 197 ASN A ND2  1 
ATOM   2300 H  H    . ASN A  1 197 ? -10.00000 -27.17600 8.79800   1.000 21.29962  ? 197 ASN A H    1 
ATOM   2301 H  HA   . ASN A  1 197 ? -11.84900 -29.05400 9.22600   1.000 22.01984  ? 197 ASN A HA   1 
ATOM   2302 H  HB2  . ASN A  1 197 ? -12.78700 -26.89300 10.03900  1.000 24.14013  ? 197 ASN A HB2  1 
ATOM   2303 H  HB3  . ASN A  1 197 ? -12.94100 -26.56100 8.49200   1.000 24.14013  ? 197 ASN A HB3  1 
ATOM   2304 H  HD21 . ASN A  1 197 ? -15.86000 -28.02100 8.14700   1.000 23.88815  ? 197 ASN A HD21 1 
ATOM   2305 H  HD22 . ASN A  1 197 ? -14.90900 -26.97800 7.66900   1.000 23.88815  ? 197 ASN A HD22 1 
ATOM   2306 N  N    . THR A  1 198 ? -12.31800 -29.19200 6.69700   1.000 21.18690  ? 198 THR A N    1 
ATOM   2307 C  CA   . THR A  1 198 ? -12.19700 -29.34900 5.24400   1.000 23.74489  ? 198 THR A CA   1 
ATOM   2308 C  C    . THR A  1 198 ? -12.57800 -28.07800 4.48800   1.000 21.13667  ? 198 THR A C    1 
ATOM   2309 O  O    . THR A  1 198 ? -11.99200 -27.78700 3.43800   1.000 25.05887  ? 198 THR A O    1 
ATOM   2310 C  CB   . THR A  1 198 ? -13.04200 -30.51600 4.75900   1.000 26.61698  ? 198 THR A CB   1 
ATOM   2311 O  OG1  . THR A  1 198 ? -12.57600 -31.73300 5.34700   1.000 32.55192  ? 198 THR A OG1  1 
ATOM   2312 C  CG2  . THR A  1 198 ? -12.94100 -30.64200 3.21500   1.000 29.92425  ? 198 THR A CG2  1 
ATOM   2313 H  H    . THR A  1 198 ? -12.90000 -29.69900 7.07600   1.000 25.42684  ? 198 THR A H    1 
ATOM   2314 H  HA   . THR A  1 198 ? -11.26800 -29.54600 5.04500   1.000 28.49643  ? 198 THR A HA   1 
ATOM   2315 H  HB   . THR A  1 198 ? -13.96800 -30.36800 5.00900   1.000 31.94294  ? 198 THR A HB   1 
ATOM   2316 H  HG1  . THR A  1 198 ? -13.07900 -32.36900 5.12800   1.000 39.06486  ? 198 THR A HG1  1 
ATOM   2317 H  HG21 . THR A  1 198 ? -13.47000 -31.39500 2.90800   1.000 35.91166  ? 198 THR A HG21 1 
ATOM   2318 H  HG22 . THR A  1 198 ? -13.27000 -29.83300 2.79400   1.000 35.91166  ? 198 THR A HG22 1 
ATOM   2319 H  HG23 . THR A  1 198 ? -12.01700 -30.78000 2.95300   1.000 35.91166  ? 198 THR A HG23 1 
ATOM   2320 N  N    . SER A  1 199 ? -13.55000 -27.31200 5.00200   1.000 22.41914  ? 199 SER A N    1 
ATOM   2321 C  CA   . SER A  1 199 ? -14.01600 -26.12400 4.30700   1.000 23.27723  ? 199 SER A CA   1 
ATOM   2322 C  C    . SER A  1 199 ? -14.38600 -25.04600 5.30800   1.000 20.70796  ? 199 SER A C    1 
ATOM   2323 O  O    . SER A  1 199 ? -14.61000 -25.32100 6.47800   1.000 22.03143  ? 199 SER A O    1 
ATOM   2324 C  CB   . SER A  1 199 ? -15.24600 -26.49000 3.43000   1.000 29.07687  ? 199 SER A CB   1 
ATOM   2325 O  OG   . SER A  1 199 ? -15.97900 -25.35000 3.11500   1.000 36.59586  ? 199 SER A OG   1 
ATOM   2326 H  H    . SER A  1 199 ? -13.94900 -27.46500 5.74800   1.000 26.90553  ? 199 SER A H    1 
ATOM   2327 H  HA   . SER A  1 199 ? -13.30500 -25.76200 3.75500   1.000 27.93524  ? 199 SER A HA   1 
ATOM   2328 H  HB2  . SER A  1 199 ? -14.93700 -26.90600 2.61000   1.000 34.89480  ? 199 SER A HB2  1 
ATOM   2329 H  HB3  . SER A  1 199 ? -15.81300 -27.10500 3.92100   1.000 34.89480  ? 199 SER A HB3  1 
ATOM   2330 H  HG   . SER A  1 199 ? -16.47900 -25.50300 2.45700   1.000 43.91759  ? 199 SER A HG   1 
ATOM   2331 N  N    . SER A  1 200 ? -14.46800 -23.81500 4.81200   1.000 22.81812  ? 200 SER A N    1 
ATOM   2332 C  CA   . SER A  1 200 ? -15.05800 -22.73500 5.58400   1.000 21.35506  ? 200 SER A CA   1 
ATOM   2333 C  C    . SER A  1 200 ? -16.52900 -22.51600 5.25800   1.000 23.32472  ? 200 SER A C    1 
ATOM   2334 O  O    . SER A  1 200 ? -17.19300 -21.68200 5.89600   1.000 23.67702  ? 200 SER A O    1 
ATOM   2335 C  CB   . SER A  1 200 ? -14.35600 -21.41500 5.31600   1.000 21.48624  ? 200 SER A CB   1 
ATOM   2336 O  OG   . SER A  1 200 ? -14.57900 -20.96700 4.00800   1.000 24.12825  ? 200 SER A OG   1 
ATOM   2337 H  H    . SER A  1 200 ? -14.18900 -23.58400 4.03300   1.000 27.38430  ? 200 SER A H    1 
ATOM   2338 H  HA   . SER A  1 200 ? -14.95100 -22.96400 6.52100   1.000 25.62864  ? 200 SER A HA   1 
ATOM   2339 H  HB2  . SER A  1 200 ? -14.69400 -20.74900 5.93600   1.000 25.78605  ? 200 SER A HB2  1 
ATOM   2340 H  HB3  . SER A  1 200 ? -13.40200 -21.53500 5.44700   1.000 25.78605  ? 200 SER A HB3  1 
ATOM   2341 H  HG   . SER A  1 200 ? -14.18800 -21.47100 3.46200   1.000 28.95646  ? 200 SER A HG   1 
ATOM   2342 N  N    . LEU A  1 201 ? -17.04600 -23.20700 4.23600   1.000 23.01992  ? 201 LEU A N    1 
ATOM   2343 C  CA   . LEU A  1 201 ? -18.32700 -22.86100 3.65200   1.000 23.52063  ? 201 LEU A CA   1 
ATOM   2344 C  C    . LEU A  1 201 ? -19.52400 -23.14700 4.54500   1.000 24.24589  ? 201 LEU A C    1 
ATOM   2345 O  O    . LEU A  1 201 ? -20.58600 -22.54500 4.30900   1.000 28.70283  ? 201 LEU A O    1 
ATOM   2346 C  CB   . LEU A  1 201 ? -18.45700 -23.60600 2.32800   1.000 25.23423  ? 201 LEU A CB   1 
ATOM   2347 C  CG   . LEU A  1 201 ? -17.44600 -23.17600 1.25600   1.000 24.44378  ? 201 LEU A CG   1 
ATOM   2348 C  CD1  . LEU A  1 201 ? -17.53100 -24.12200 0.05400   1.000 26.39094  ? 201 LEU A CD1  1 
ATOM   2349 C  CD2  . LEU A  1 201 ? -17.71600 -21.75000 0.78000   1.000 32.94612  ? 201 LEU A CD2  1 
ATOM   2350 H  H    . LEU A  1 201 ? -16.66700 -23.88500 3.86700   1.000 27.62647  ? 201 LEU A H    1 
ATOM   2351 H  HA   . LEU A  1 201 ? -18.35100 -21.90400 3.49500   1.000 28.22732  ? 201 LEU A HA   1 
ATOM   2352 H  HB2  . LEU A  1 201 ? -18.32500 -24.55300 2.49300   1.000 30.28364  ? 201 LEU A HB2  1 
ATOM   2353 H  HB3  . LEU A  1 201 ? -19.34600 -23.45100 1.97300   1.000 30.28364  ? 201 LEU A HB3  1 
ATOM   2354 H  HG   . LEU A  1 201 ? -16.55700 -23.20700 1.64300   1.000 29.33510  ? 201 LEU A HG   1 
ATOM   2355 H  HD11 . LEU A  1 201 ? -16.87600 -23.85100 -0.60800  1.000 31.67170  ? 201 LEU A HD11 1 
ATOM   2356 H  HD12 . LEU A  1 201 ? -17.34600 -25.02700 0.35100   1.000 31.67170  ? 201 LEU A HD12 1 
ATOM   2357 H  HD13 . LEU A  1 201 ? -18.42300 -24.07400 -0.32300  1.000 31.67170  ? 201 LEU A HD13 1 
ATOM   2358 H  HD21 . LEU A  1 201 ? -17.15900 -21.56400 0.00800   1.000 39.53790  ? 201 LEU A HD21 1 
ATOM   2359 H  HD22 . LEU A  1 201 ? -18.65200 -21.66900 0.54000   1.000 39.53790  ? 201 LEU A HD22 1 
ATOM   2360 H  HD23 . LEU A  1 201 ? -17.50400 -21.13200 1.49700   1.000 39.53790  ? 201 LEU A HD23 1 
ATOM   2361 N  N    . GLY A  1 202 ? -19.40400 -24.04500 5.50700   1.000 23.34447  ? 202 GLY A N    1 
ATOM   2362 C  CA   . GLY A  1 202 ? -20.46400 -24.33400 6.46400   1.000 23.01762  ? 202 GLY A CA   1 
ATOM   2363 C  C    . GLY A  1 202 ? -20.54500 -23.37600 7.61500   1.000 25.32440  ? 202 GLY A C    1 
ATOM   2364 O  O    . GLY A  1 202 ? -21.40200 -23.53400 8.49600   1.000 24.57071  ? 202 GLY A O    1 
ATOM   2365 H  H    . GLY A  1 202 ? -18.69700 -24.51800 5.63400   1.000 28.01593  ? 202 GLY A H    1 
ATOM   2366 H  HA2  . GLY A  1 202 ? -21.31600 -24.31300 6.00000   1.000 27.62371  ? 202 GLY A HA2  1 
ATOM   2367 H  HA3  . GLY A  1 202 ? -20.32400 -25.22200 6.82600   1.000 27.62371  ? 202 GLY A HA3  1 
ATOM   2368 N  N    . PHE A  1 203 ? -19.63500 -22.40800 7.68200   1.000 22.26269  ? 203 PHE A N    1 
ATOM   2369 C  CA   . PHE A  1 203 ? -19.49800 -21.52400 8.83100   1.000 20.29392  ? 203 PHE A CA   1 
ATOM   2370 C  C    . PHE A  1 203 ? -20.09400 -20.13100 8.57200   1.000 24.06618  ? 203 PHE A C    1 
ATOM   2371 O  O    . PHE A  1 203 ? -19.98300 -19.25500 9.43700   1.000 25.57651  ? 203 PHE A O    1 
ATOM   2372 C  CB   . PHE A  1 203 ? -18.00900 -21.38700 9.18500   1.000 20.25065  ? 203 PHE A CB   1 
ATOM   2373 C  CG   . PHE A  1 203 ? -17.35500 -22.67500 9.57700   1.000 18.66030  ? 203 PHE A CG   1 
ATOM   2374 C  CD1  . PHE A  1 203 ? -18.07600 -23.72900 10.10600  1.000 19.68397  ? 203 PHE A CD1  1 
ATOM   2375 C  CD2  . PHE A  1 203 ? -15.98900 -22.82800 9.43800   1.000 19.56593  ? 203 PHE A CD2  1 
ATOM   2376 C  CE1  . PHE A  1 203 ? -17.44300 -24.90200 10.48400  1.000 20.28694  ? 203 PHE A CE1  1 
ATOM   2377 C  CE2  . PHE A  1 203 ? -15.36000 -24.00300 9.81500   1.000 19.06636  ? 203 PHE A CE2  1 
ATOM   2378 C  CZ   . PHE A  1 203 ? -16.08200 -25.04300 10.34000  1.000 20.75182  ? 203 PHE A CZ   1 
ATOM   2379 H  H    . PHE A  1 203 ? -19.07000 -22.24100 7.05600   1.000 26.71779  ? 203 PHE A H    1 
ATOM   2380 H  HA   . PHE A  1 203 ? -19.96500 -21.91200 9.58800   1.000 24.35526  ? 203 PHE A HA   1 
ATOM   2381 H  HB2  . PHE A  1 203 ? -17.53700 -21.03900 8.41200   1.000 24.30334  ? 203 PHE A HB2  1 
ATOM   2382 H  HB3  . PHE A  1 203 ? -17.92200 -20.77300 9.93100   1.000 24.30334  ? 203 PHE A HB3  1 
ATOM   2383 H  HD1  . PHE A  1 203 ? -18.99700 -23.65000 10.20900  1.000 23.62332  ? 203 PHE A HD1  1 
ATOM   2384 H  HD2  . PHE A  1 203 ? -15.48400 -22.13100 9.08700   1.000 23.48168  ? 203 PHE A HD2  1 
ATOM   2385 H  HE1  . PHE A  1 203 ? -17.94300 -25.60100 10.83900  1.000 24.34689  ? 203 PHE A HE1  1 
ATOM   2386 H  HE2  . PHE A  1 203 ? -14.43900 -24.08700 9.71000   1.000 22.88219  ? 203 PHE A HE2  1 
ATOM   2387 H  HZ   . PHE A  1 203 ? -15.65900 -25.83100 10.59500  1.000 24.90475  ? 203 PHE A HZ   1 
ATOM   2388 N  N    . ARG A  1 204 ? -20.78600 -19.92100 7.44900   1.000 23.54716  ? 204 ARG A N    1 
ATOM   2389 C  CA   . ARG A  1 204 ? -21.17300 -18.58500 7.01900   1.000 24.50797  ? 204 ARG A CA   1 
ATOM   2390 C  C    . ARG A  1 204 ? -22.42400 -18.06300 7.70600   1.000 28.30005  ? 204 ARG A C    1 
ATOM   2391 O  O    . ARG A  1 204 ? -22.83100 -16.93000 7.42300   1.000 30.50462  ? 204 ARG A O    1 
ATOM   2392 C  CB   . ARG A  1 204 ? -21.39500 -18.57800 5.49100   1.000 27.91647  ? 204 ARG A CB   1 
ATOM   2393 C  CG   . ARG A  1 204 ? -20.11000 -18.76400 4.72600   1.000 27.67366  ? 204 ARG A CG   1 
ATOM   2394 C  CD   . ARG A  1 204 ? -20.32900 -18.89800 3.20500   1.000 32.12920  ? 204 ARG A CD   1 
ATOM   2395 N  NE   . ARG A  1 204 ? -19.07600 -18.68000 2.50900   1.000 55.73435  ? 204 ARG A NE   1 
ATOM   2396 C  CZ   . ARG A  1 204 ? -18.94000 -18.68200 1.19200   1.000 71.98727  ? 204 ARG A CZ   1 
ATOM   2397 N  NH1  . ARG A  1 204 ? -19.97300 -18.90100 0.39200   1.000 53.78136  ? 204 ARG A NH1  1 
ATOM   2398 N  NH2  . ARG A  1 204 ? -17.73700 -18.46700 0.66700   1.000 69.31272  ? 204 ARG A NH2  1 
ATOM   2399 H  H    . ARG A  1 204 ? -21.04300 -20.54500 6.91600   1.000 28.25916  ? 204 ARG A H    1 
ATOM   2400 H  HA   . ARG A  1 204 ? -20.44900 -17.97600 7.23400   1.000 29.41213  ? 204 ARG A HA   1 
ATOM   2401 H  HB2  . ARG A  1 204 ? -21.99500 -19.30200 5.25400   1.000 33.50233  ? 204 ARG A HB2  1 
ATOM   2402 H  HB3  . ARG A  1 204 ? -21.78200 -17.72700 5.23000   1.000 33.50233  ? 204 ARG A HB3  1 
ATOM   2403 H  HG2  . ARG A  1 204 ? -19.53800 -17.99500 4.87800   1.000 33.21096  ? 204 ARG A HG2  1 
ATOM   2404 H  HG3  . ARG A  1 204 ? -19.67100 -19.57100 5.03700   1.000 33.21096  ? 204 ARG A HG3  1 
ATOM   2405 H  HD2  . ARG A  1 204 ? -20.65100 -19.79000 2.99800   1.000 38.55760  ? 204 ARG A HD2  1 
ATOM   2406 H  HD3  . ARG A  1 204 ? -20.97200 -18.23600 2.90600   1.000 38.55760  ? 204 ARG A HD3  1 
ATOM   2407 H  HE   . ARG A  1 204 ? -18.37300 -18.53900 2.98400   1.000 66.88378  ? 204 ARG A HE   1 
ATOM   2408 H  HH11 . ARG A  1 204 ? -20.75200 -19.04600 0.72500   1.000 64.54020  ? 204 ARG A HH11 1 
ATOM   2409 H  HH12 . ARG A  1 204 ? -19.86400 -18.89800 -0.46100  1.000 64.54020  ? 204 ARG A HH12 1 
ATOM   2410 H  HH21 . ARG A  1 204 ? -17.06200 -18.33000 1.18100   1.000 83.17782  ? 204 ARG A HH21 1 
ATOM   2411 H  HH22 . ARG A  1 204 ? -17.63400 -18.46600 -0.18700  1.000 83.17782  ? 204 ARG A HH22 1 
ATOM   2412 N  N    . SER A  1 205 ? -23.03400 -18.84500 8.59400   1.000 23.83217  ? 205 SER A N    1 
ATOM   2413 C  CA   . SER A  1 205 ? -24.18200 -18.40600 9.37600   1.000 27.71334  ? 205 SER A CA   1 
ATOM   2414 C  C    . SER A  1 205 ? -24.01500 -18.56600 10.88300  1.000 24.94229  ? 205 SER A C    1 
ATOM   2415 O  O    . SER A  1 205 ? -25.00400 -18.42300 11.62200  1.000 27.50612  ? 205 SER A O    1 
ATOM   2416 C  CB   . SER A  1 205 ? -25.44000 -19.17200 8.92200   1.000 30.97179  ? 205 SER A CB   1 
ATOM   2417 O  OG   . SER A  1 205 ? -25.70800 -18.85700 7.56000   1.000 39.89388  ? 205 SER A OG   1 
ATOM   2418 H  H    . SER A  1 205 ? -22.79400 -19.65300 8.76600   1.000 28.60117  ? 205 SER A H    1 
ATOM   2419 H  HA   . SER A  1 205 ? -24.30300 -17.45700 9.21300   1.000 33.25857  ? 205 SER A HA   1 
ATOM   2420 H  HB2  . SER A  1 205 ? -25.28600 -20.12600 9.00900   1.000 37.16871  ? 205 SER A HB2  1 
ATOM   2421 H  HB3  . SER A  1 205 ? -26.19500 -18.90600 9.47000   1.000 37.16871  ? 205 SER A HB3  1 
ATOM   2422 H  HG   . SER A  1 205 ? -26.52500 -18.96700 7.39500   1.000 47.87522  ? 205 SER A HG   1 
ATOM   2423 N  N    . ILE A  1 206 ? -22.79700 -18.81800 11.38000  1.000 22.85998  ? 206 ILE A N    1 
ATOM   2424 C  CA   . ILE A  1 206 ? -22.59000 -18.96000 12.81500  1.000 21.73505  ? 206 ILE A CA   1 
ATOM   2425 C  C    . ILE A  1 206 ? -22.96700 -17.67400 13.53500  1.000 20.78167  ? 206 ILE A C    1 
ATOM   2426 O  O    . ILE A  1 206 ? -22.51700 -16.58500 13.16800  1.000 22.49704  ? 206 ILE A O    1 
ATOM   2427 C  CB   . ILE A  1 206 ? -21.11400 -19.27700 13.08400  1.000 19.75187  ? 206 ILE A CB   1 
ATOM   2428 C  CG1  . ILE A  1 206 ? -20.78600 -20.70600 12.68000  1.000 21.54334  ? 206 ILE A CG1  1 
ATOM   2429 C  CG2  . ILE A  1 206 ? -20.79300 -19.05700 14.57700  1.000 19.82240  ? 206 ILE A CG2  1 
ATOM   2430 C  CD1  . ILE A  1 206 ? -19.31200 -21.06000 12.72900  1.000 21.13166  ? 206 ILE A CD1  1 
ATOM   2431 H  H    . ILE A  1 206 ? -22.08400 -18.90900 10.90700  1.000 27.43454  ? 206 ILE A H    1 
ATOM   2432 H  HA   . ILE A  1 206 ? -23.15900 -19.67700 13.13500  1.000 26.08463  ? 206 ILE A HA   1 
ATOM   2433 H  HB   . ILE A  1 206 ? -20.57000 -18.67800 12.54800  1.000 23.70481  ? 206 ILE A HB   1 
ATOM   2434 H  HG12 . ILE A  1 206 ? -21.25100 -21.30900 13.28100  1.000 25.85456  ? 206 ILE A HG12 1 
ATOM   2435 H  HG13 . ILE A  1 206 ? -21.09000 -20.84500 11.76900  1.000 25.85456  ? 206 ILE A HG13 1 
ATOM   2436 H  HG21 . ILE A  1 206 ? -19.91100 -19.41400 14.76600  1.000 23.78944  ? 206 ILE A HG21 1 
ATOM   2437 H  HG22 . ILE A  1 206 ? -20.81200 -18.10600 14.76800  1.000 23.78944  ? 206 ILE A HG22 1 
ATOM   2438 H  HG23 . ILE A  1 206 ? -21.45800 -19.51500 15.11400  1.000 23.78944  ? 206 ILE A HG23 1 
ATOM   2439 H  HD11 . ILE A  1 206 ? -19.16000 -21.85300 12.19100  1.000 25.36056  ? 206 ILE A HD11 1 
ATOM   2440 H  HD12 . ILE A  1 206 ? -18.79700 -20.31800 12.37700  1.000 25.36056  ? 206 ILE A HD12 1 
ATOM   2441 H  HD13 . ILE A  1 206 ? -19.05800 -21.23100 13.65000  1.000 25.36056  ? 206 ILE A HD13 1 
ATOM   2442 N  N    . GLU A  1 207 ? -23.80500 -17.79800 14.57800  1.000 19.80987  ? 207 GLU A N    1 
ATOM   2443 C  CA   . GLU A  1 207 ? -24.12400 -16.70700 15.48900  1.000 21.09353  ? 207 GLU A CA   1 
ATOM   2444 C  C    . GLU A  1 207 ? -23.50200 -16.88600 16.87100  1.000 19.65270  ? 207 GLU A C    1 
ATOM   2445 O  O    . GLU A  1 207 ? -23.43900 -15.91400 17.63700  1.000 21.92210  ? 207 GLU A O    1 
ATOM   2446 C  CB   . GLU A  1 207 ? -25.65300 -16.57100 15.66300  1.000 23.67314  ? 207 GLU A CB   1 
ATOM   2447 C  CG   . GLU A  1 207 ? -26.34400 -16.19400 14.37300  1.000 27.08912  ? 207 GLU A CG   1 
ATOM   2448 C  CD   . GLU A  1 207 ? -27.79000 -15.69600 14.54700  1.000 32.34465  ? 207 GLU A CD   1 
ATOM   2449 O  OE1  . GLU A  1 207 ? -28.29600 -15.76800 15.66800  1.000 32.45095  ? 207 GLU A OE1  1 
ATOM   2450 O  OE2  . GLU A  1 207 ? -28.35000 -15.28200 13.54600  1.000 35.36108  ? 207 GLU A OE2  1 
ATOM   2451 H  H    . GLU A  1 207 ? -24.21000 -18.53100 14.77800  1.000 23.77441  ? 207 GLU A H    1 
ATOM   2452 H  HA   . GLU A  1 207 ? -23.79800 -15.87800 15.10600  1.000 25.31480  ? 207 GLU A HA   1 
ATOM   2453 H  HB2  . GLU A  1 207 ? -26.01600 -17.41900 15.96300  1.000 28.41033  ? 207 GLU A HB2  1 
ATOM   2454 H  HB3  . GLU A  1 207 ? -25.83900 -15.88000 16.31800  1.000 28.41033  ? 207 GLU A HB3  1 
ATOM   2455 H  HG2  . GLU A  1 207 ? -25.83900 -15.48400 13.94700  1.000 32.50950  ? 207 GLU A HG2  1 
ATOM   2456 H  HG3  . GLU A  1 207 ? -26.37100 -16.97400 13.79700  1.000 32.50950  ? 207 GLU A HG3  1 
ATOM   2457 N  N    . THR A  1 208 ? -23.07100 -18.08700 17.21500  1.000 17.81115  ? 208 THR A N    1 
ATOM   2458 C  CA   . THR A  1 208 ? -22.33900 -18.31700 18.44500  1.000 17.89577  ? 208 THR A CA   1 
ATOM   2459 C  C    . THR A  1 208 ? -21.13600 -17.38300 18.53500  1.000 17.51682  ? 208 THR A C    1 
ATOM   2460 O  O    . THR A  1 208 ? -20.31100 -17.34400 17.59200  1.000 18.05354  ? 208 THR A O    1 
ATOM   2461 C  CB   . THR A  1 208 ? -21.80500 -19.74800 18.46200  1.000 18.45266  ? 208 THR A CB   1 
ATOM   2462 O  OG1  . THR A  1 208 ? -22.86100 -20.68500 18.24900  1.000 20.54133  ? 208 THR A OG1  1 
ATOM   2463 C  CG2  . THR A  1 208 ? -21.05000 -20.08900 19.69800  1.000 18.43951  ? 208 THR A CG2  1 
ATOM   2464 H  H    . THR A  1 208 ? -23.19200 -18.79800 16.74500  1.000 21.37594  ? 208 THR A H    1 
ATOM   2465 H  HA   . THR A  1 208 ? -22.93300 -18.16100 19.19600  1.000 21.47749  ? 208 THR A HA   1 
ATOM   2466 H  HB   . THR A  1 208 ? -21.16700 -19.82000 17.73600  1.000 22.14576  ? 208 THR A HB   1 
ATOM   2467 H  HG1  . THR A  1 208 ? -23.46100 -20.57900 18.82800  1.000 24.65216  ? 208 THR A HG1  1 
ATOM   2468 H  HG21 . THR A  1 208 ? -20.88700 -21.04500 19.73400  1.000 22.12998  ? 208 THR A HG21 1 
ATOM   2469 H  HG22 . THR A  1 208 ? -20.19800 -19.62400 19.70500  1.000 22.12998  ? 208 THR A HG22 1 
ATOM   2470 H  HG23 . THR A  1 208 ? -21.55900 -19.82700 20.48100  1.000 22.12998  ? 208 THR A HG23 1 
ATOM   2471 N  N    . PRO A  1 209 ? -20.95300 -16.66100 19.63400  1.000 16.48898  ? 209 PRO A N    1 
ATOM   2472 C  CA   . PRO A  1 209 ? -19.74500 -15.82800 19.77100  1.000 17.48869  ? 209 PRO A CA   1 
ATOM   2473 C  C    . PRO A  1 209 ? -18.50700 -16.69500 19.67400  1.000 17.21353  ? 209 PRO A C    1 
ATOM   2474 O  O    . PRO A  1 209 ? -18.32200 -17.63200 20.46800  1.000 16.79729  ? 209 PRO A O    1 
ATOM   2475 C  CB   . PRO A  1 209 ? -19.90000 -15.23100 21.16500  1.000 17.47273  ? 209 PRO A CB   1 
ATOM   2476 C  CG   . PRO A  1 209 ? -21.37200 -15.14000 21.35000  1.000 19.10660  ? 209 PRO A CG   1 
ATOM   2477 C  CD   . PRO A  1 209 ? -21.94900 -16.35000 20.65900  1.000 16.50075  ? 209 PRO A CD   1 
ATOM   2478 H  HA   . PRO A  1 209 ? -19.72000 -15.12000 19.10900  1.000 20.98899  ? 209 PRO A HA   1 
ATOM   2479 H  HB2  . PRO A  1 209 ? -19.49800 -15.81500 21.82700  1.000 20.96984  ? 209 PRO A HB2  1 
ATOM   2480 H  HB3  . PRO A  1 209 ? -19.48600 -14.35400 21.20200  1.000 20.96984  ? 209 PRO A HB3  1 
ATOM   2481 H  HG2  . PRO A  1 209 ? -21.58500 -15.15100 22.29700  1.000 22.93048  ? 209 PRO A HG2  1 
ATOM   2482 H  HG3  . PRO A  1 209 ? -21.70300 -14.32300 20.94600  1.000 22.93048  ? 209 PRO A HG3  1 
ATOM   2483 H  HD2  . PRO A  1 209 ? -22.04700 -17.08800 21.28000  1.000 19.80346  ? 209 PRO A HD2  1 
ATOM   2484 H  HD3  . PRO A  1 209 ? -22.80600 -16.14100 20.25500  1.000 19.80346  ? 209 PRO A HD3  1 
ATOM   2485 N  N    . THR A  1 210 ? -17.62700 -16.37300 18.71900  1.000 15.50872  ? 210 THR A N    1 
ATOM   2486 C  CA   . THR A  1 210 ? -16.51500 -17.23700 18.36600  1.000 15.18434  ? 210 THR A CA   1 
ATOM   2487 C  C    . THR A  1 210 ? -15.18800 -16.51100 18.37800  1.000 15.45805  ? 210 THR A C    1 
ATOM   2488 O  O    . THR A  1 210 ? -15.03200 -15.46600 17.71800  1.000 17.29345  ? 210 THR A O    1 
ATOM   2489 C  CB   . THR A  1 210 ? -16.74800 -17.85100 16.97500  1.000 17.09757  ? 210 THR A CB   1 
ATOM   2490 O  OG1  . THR A  1 210 ? -17.91400 -18.67700 16.97200  1.000 18.11001  ? 210 THR A OG1  1 
ATOM   2491 C  CG2  . THR A  1 210 ? -15.55500 -18.64500 16.53300  1.000 17.54722  ? 210 THR A CG2  1 
ATOM   2492 H  H    . THR A  1 210 ? -17.66000 -15.64700 18.26000  1.000 18.61302  ? 210 THR A H    1 
ATOM   2493 H  HA   . THR A  1 210 ? -16.44900 -17.92500 19.04700  1.000 18.22377  ? 210 THR A HA   1 
ATOM   2494 H  HB   . THR A  1 210 ? -16.88300 -17.13200 16.33800  1.000 20.51965  ? 210 THR A HB   1 
ATOM   2495 H  HG1  . THR A  1 210 ? -18.58700 -18.22500 17.19300  1.000 21.73458  ? 210 THR A HG1  1 
ATOM   2496 H  HG21 . THR A  1 210 ? -15.79300 -19.21100 15.78200  1.000 21.05923  ? 210 THR A HG21 1 
ATOM   2497 H  HG22 . THR A  1 210 ? -14.84000 -18.04800 16.26300  1.000 21.05923  ? 210 THR A HG22 1 
ATOM   2498 H  HG23 . THR A  1 210 ? -15.24100 -19.20400 17.26100  1.000 21.05923  ? 210 THR A HG23 1 
ATOM   2499 N  N    A LEU A  1 211 ? -14.25300 -17.02600 19.17600  0.518 15.54543  ? 211 LEU A N    1 
ATOM   2500 N  N    B LEU A  1 211 ? -14.22700 -17.10400 19.08900  0.482 13.71988  ? 211 LEU A N    1 
ATOM   2501 C  CA   A LEU A  1 211 ? -12.87800 -16.55500 19.21200  0.518 16.24803  ? 211 LEU A CA   1 
ATOM   2502 C  CA   B LEU A  1 211 ? -12.87100 -16.59500 19.24100  0.482 14.24566  ? 211 LEU A CA   1 
ATOM   2503 C  C    A LEU A  1 211 ? -12.01100 -17.59400 18.53000  0.518 14.87025  ? 211 LEU A C    1 
ATOM   2504 C  C    B LEU A  1 211 ? -11.95200 -17.60000 18.58100  0.482 16.38916  ? 211 LEU A C    1 
ATOM   2505 O  O    A LEU A  1 211 ? -12.13300 -18.78500 18.82000  0.518 15.74638  ? 211 LEU A O    1 
ATOM   2506 O  O    B LEU A  1 211 ? -11.97200 -18.77800 18.94200  0.482 14.99252  ? 211 LEU A O    1 
ATOM   2507 C  CB   A LEU A  1 211 ? -12.39800 -16.32200 20.63900  0.518 13.72375  ? 211 LEU A CB   1 
ATOM   2508 C  CB   B LEU A  1 211 ? -12.52200 -16.46800 20.71800  0.482 20.39457  ? 211 LEU A CB   1 
ATOM   2509 C  CG   A LEU A  1 211 ? -11.00400 -15.68700 20.74900  0.518 17.50855  ? 211 LEU A CG   1 
ATOM   2510 C  CG   B LEU A  1 211 ? -11.05200 -16.30100 21.10400  0.482 15.70795  ? 211 LEU A CG   1 
ATOM   2511 C  CD1  A LEU A  1 211 ? -10.96800 -14.78000 21.98800  0.518 16.63845  ? 211 LEU A CD1  1 
ATOM   2512 C  CD1  B LEU A  1 211 ? -10.60300 -14.92200 20.67100  0.482 22.00341  ? 211 LEU A CD1  1 
ATOM   2513 C  CD2  A LEU A  1 211 ? -9.94700  -16.72400 20.84000  0.518 15.13315  ? 211 LEU A CD2  1 
ATOM   2514 C  CD2  B LEU A  1 211 ? -10.88500 -16.45700 22.59100  0.482 16.99669  ? 211 LEU A CD2  1 
ATOM   2515 H  H    A LEU A  1 211 ? -14.40200 -17.67300 19.72300  0.518 18.65708  ? 211 LEU A H    1 
ATOM   2516 H  H    B LEU A  1 211 ? -14.34800 -17.84200 19.51400  0.482 16.46642  ? 211 LEU A H    1 
ATOM   2517 H  HA   A LEU A  1 211 ? -12.80500 -15.70900 18.74300  0.518 19.50020  ? 211 LEU A HA   1 
ATOM   2518 H  HA   B LEU A  1 211 ? -12.77400 -15.72700 18.81900  0.482 17.09735  ? 211 LEU A HA   1 
ATOM   2519 H  HB2  A LEU A  1 211 ? -13.02500 -15.73000 21.08300  0.518 16.47107  ? 211 LEU A HB2  1 
ATOM   2520 H  HB2  B LEU A  1 211 ? -12.98900 -15.69100 21.06400  0.482 24.47605  ? 211 LEU A HB2  1 
ATOM   2521 H  HB3  A LEU A  1 211 ? -12.36700 -17.17700 21.09700  0.518 16.47107  ? 211 LEU A HB3  1 
ATOM   2522 H  HB3  B LEU A  1 211 ? -12.83600 -17.27000 21.16400  0.482 24.47605  ? 211 LEU A HB3  1 
ATOM   2523 H  HG   A LEU A  1 211 ? -10.82400 -15.16000 19.95500  0.518 21.01282  ? 211 LEU A HG   1 
ATOM   2524 H  HG   B LEU A  1 211 ? -10.50700 -16.97700 20.67000  0.482 18.85210  ? 211 LEU A HG   1 
ATOM   2525 H  HD11 A LEU A  1 211 ? -10.07000 -14.43100 22.09800  0.518 19.96870  ? 211 LEU A HD11 1 
ATOM   2526 H  HD11 B LEU A  1 211 ? -9.78500  -14.69500 21.14100  0.482 26.40666  ? 211 LEU A HD11 1 
ATOM   2527 H  HD12 A LEU A  1 211 ? -11.59300 -14.04900 21.86300  0.518 19.96870  ? 211 LEU A HD12 1 
ATOM   2528 H  HD12 B LEU A  1 211 ? -10.44400 -14.92700 19.71400  0.482 26.40666  ? 211 LEU A HD12 1 
ATOM   2529 H  HD13 A LEU A  1 211 ? -11.21900 -15.30000 22.76800  0.518 19.96870  ? 211 LEU A HD13 1 
ATOM   2530 H  HD13 B LEU A  1 211 ? -11.29700 -14.28100 20.88800  0.482 26.40666  ? 211 LEU A HD13 1 
ATOM   2531 H  HD21 A LEU A  1 211 ? -9.08100  -16.30400 20.71800  0.518 18.16234  ? 211 LEU A HD21 1 
ATOM   2532 H  HD21 B LEU A  1 211 ? -9.94000  -16.41600 22.80800  0.482 20.39859  ? 211 LEU A HD21 1 
ATOM   2533 H  HD22 A LEU A  1 211 ? -9.99100  -17.14500 21.71300  0.518 18.16234  ? 211 LEU A HD22 1 
ATOM   2534 H  HD22 B LEU A  1 211 ? -11.35800 -15.73800 23.03900  0.482 20.39859  ? 211 LEU A HD22 1 
ATOM   2535 H  HD23 A LEU A  1 211 ? -10.09300 -17.38600 20.14600  0.518 18.16234  ? 211 LEU A HD23 1 
ATOM   2536 H  HD23 B LEU A  1 211 ? -11.25000 -17.31300 22.86200  0.482 20.39859  ? 211 LEU A HD23 1 
ATOM   2537 N  N    . ILE A  1 212 ? -11.13400 -17.14700 17.63400  1.000 15.30419  ? 212 ILE A N    1 
ATOM   2538 C  CA   . ILE A  1 212 ? -10.16800 -18.02000 16.95700  1.000 15.47773  ? 212 ILE A CA   1 
ATOM   2539 C  C    . ILE A  1 212 ? -8.76300  -17.55500 17.30300  1.000 16.68766  ? 212 ILE A C    1 
ATOM   2540 O  O    . ILE A  1 212 ? -8.40600  -16.39000 17.07900  1.000 17.07973  ? 212 ILE A O    1 
ATOM   2541 C  CB   . ILE A  1 212 ? -10.42500 -18.07000 15.43700  1.000 16.66256  ? 212 ILE A CB   1 
ATOM   2542 C  CG1  . ILE A  1 212 ? -11.72700 -18.83200 15.16000  1.000 18.44031  ? 212 ILE A CG1  1 
ATOM   2543 C  CG2  . ILE A  1 212 ? -9.19800  -18.70600 14.75700  1.000 18.54754  ? 212 ILE A CG2  1 
ATOM   2544 C  CD1  . ILE A  1 212 ? -12.23700 -18.70300 13.75200  1.000 22.60461  ? 212 ILE A CD1  1 
ATOM   2545 H  H    . ILE A  1 212 ? -11.07300 -16.32400 17.39300  1.000 18.36759  ? 212 ILE A H    1 
ATOM   2546 H  HA   . ILE A  1 212 ? -10.24900 -18.92400 17.30000  1.000 18.57583  ? 212 ILE A HA   1 
ATOM   2547 H  HB   . ILE A  1 212 ? -10.54100 -17.17900 15.07100  1.000 19.99763  ? 212 ILE A HB   1 
ATOM   2548 H  HG12 . ILE A  1 212 ? -11.57500 -19.77500 15.33100  1.000 22.13094  ? 212 ILE A HG12 1 
ATOM   2549 H  HG13 . ILE A  1 212 ? -12.41600 -18.49400 15.75400  1.000 22.13094  ? 212 ILE A HG13 1 
ATOM   2550 H  HG21 . ILE A  1 212 ? -9.41700  -18.90700 13.83400  1.000 22.25961  ? 212 ILE A HG21 1 
ATOM   2551 H  HG22 . ILE A  1 212 ? -8.45800  -18.08000 14.79300  1.000 22.25961  ? 212 ILE A HG22 1 
ATOM   2552 H  HG23 . ILE A  1 212 ? -8.96500  -19.52200 15.22700  1.000 22.25961  ? 212 ILE A HG23 1 
ATOM   2553 H  HD11 . ILE A  1 212 ? -13.08200 -19.17300 13.67800  1.000 27.12809  ? 212 ILE A HD11 1 
ATOM   2554 H  HD12 . ILE A  1 212 ? -12.36100 -17.76300 13.54700  1.000 27.12809  ? 212 ILE A HD12 1 
ATOM   2555 H  HD13 . ILE A  1 212 ? -11.58800 -19.09200 13.14500  1.000 27.12809  ? 212 ILE A HD13 1 
ATOM   2556 N  N    . PHE A  1 213 ? -7.98300  -18.47100 17.87400  1.000 15.50123  ? 213 PHE A N    1 
ATOM   2557 C  CA   . PHE A  1 213 ? -6.53800  -18.31600 17.99500  1.000 14.84330  ? 213 PHE A CA   1 
ATOM   2558 C  C    . PHE A  1 213 ? -5.90500  -18.96900 16.77400  1.000 17.89203  ? 213 PHE A C    1 
ATOM   2559 O  O    . PHE A  1 213 ? -6.05000  -20.17500 16.55200  1.000 18.43090  ? 213 PHE A O    1 
ATOM   2560 C  CB   . PHE A  1 213 ? -6.01200  -18.98600 19.25100  1.000 16.57096  ? 213 PHE A CB   1 
ATOM   2561 C  CG   . PHE A  1 213 ? -6.36300  -18.27300 20.53800  1.000 15.25770  ? 213 PHE A CG   1 
ATOM   2562 C  CD1  . PHE A  1 213 ? -5.80400  -17.05100 20.85700  1.000 17.56244  ? 213 PHE A CD1  1 
ATOM   2563 C  CD2  . PHE A  1 213 ? -7.22900  -18.86600 21.47400  1.000 16.32620  ? 213 PHE A CD2  1 
ATOM   2564 C  CE1  . PHE A  1 213 ? -6.10900  -16.41200 22.05100  1.000 16.38584  ? 213 PHE A CE1  1 
ATOM   2565 C  CE2  . PHE A  1 213 ? -7.51200  -18.24700 22.66200  1.000 17.21537  ? 213 PHE A CE2  1 
ATOM   2566 C  CZ   . PHE A  1 213 ? -6.96500  -17.03200 22.96600  1.000 16.62331  ? 213 PHE A CZ   1 
ATOM   2567 H  H    . PHE A  1 213 ? -8.27500  -19.20800 18.20600  1.000 18.60404  ? 213 PHE A H    1 
ATOM   2568 H  HA   . PHE A  1 213 ? -6.31300  -17.37300 18.03900  1.000 17.81452  ? 213 PHE A HA   1 
ATOM   2569 H  HB2  . PHE A  1 213 ? -6.38300  -19.88100 19.30200  1.000 19.88772  ? 213 PHE A HB2  1 
ATOM   2570 H  HB3  . PHE A  1 213 ? -5.04500  -19.03100 19.19600  1.000 19.88772  ? 213 PHE A HB3  1 
ATOM   2571 H  HD1  . PHE A  1 213 ? -5.21400  -16.64900 20.26100  1.000 21.07749  ? 213 PHE A HD1  1 
ATOM   2572 H  HD2  . PHE A  1 213 ? -7.61500  -19.69000 21.28300  1.000 19.59401  ? 213 PHE A HD2  1 
ATOM   2573 H  HE1  . PHE A  1 213 ? -5.74600  -15.57700 22.24100  1.000 19.66557  ? 213 PHE A HE1  1 
ATOM   2574 H  HE2  . PHE A  1 213 ? -8.08400  -18.65800 23.27000  1.000 20.66101  ? 213 PHE A HE2  1 
ATOM   2575 H  HZ   . PHE A  1 213 ? -7.16100  -16.62100 23.77600  1.000 19.95054  ? 213 PHE A HZ   1 
ATOM   2576 N  N    . ALA A  1 214 ? -5.18500  -18.17200 16.00600  1.000 17.58452  ? 214 ALA A N    1 
ATOM   2577 C  CA   . ALA A  1 214 ? -4.45100  -18.58900 14.82400  1.000 15.82392  ? 214 ALA A CA   1 
ATOM   2578 C  C    . ALA A  1 214 ? -2.97100  -18.59900 15.15200  1.000 19.73627  ? 214 ALA A C    1 
ATOM   2579 O  O    . ALA A  1 214 ? -2.48800  -17.73000 15.86600  1.000 20.63602  ? 214 ALA A O    1 
ATOM   2580 C  CB   . ALA A  1 214 ? -4.70800  -17.61400 13.69300  1.000 19.04329  ? 214 ALA A CB   1 
ATOM   2581 H  H    . ALA A  1 214 ? -5.09900  -17.33000 16.15800  1.000 21.10399  ? 214 ALA A H    1 
ATOM   2582 H  HA   . ALA A  1 214 ? -4.72000  -19.47800 14.54300  1.000 18.99126  ? 214 ALA A HA   1 
ATOM   2583 H  HB1  . ALA A  1 214 ? -4.16000  -17.86200 12.93200  1.000 22.85451  ? 214 ALA A HB1  1 
ATOM   2584 H  HB2  . ALA A  1 214 ? -5.64700  -17.65200 13.45000  1.000 22.85451  ? 214 ALA A HB2  1 
ATOM   2585 H  HB3  . ALA A  1 214 ? -4.47900  -16.71900 13.98800  1.000 22.85451  ? 214 ALA A HB3  1 
ATOM   2586 N  N    . CYS A  1 215 ? -2.26900  -19.63200 14.71000  1.000 17.06201  ? 215 CYS A N    1 
ATOM   2587 C  CA   . CYS A  1 215 ? -0.83800  -19.74200 14.94900  1.000 16.34976  ? 215 CYS A CA   1 
ATOM   2588 C  C    . CYS A  1 215 ? -0.11700  -19.36400 13.66200  1.000 17.87649  ? 215 CYS A C    1 
ATOM   2589 O  O    . CYS A  1 215 ? -0.20500  -20.08100 12.66300  1.000 18.29676  ? 215 CYS A O    1 
ATOM   2590 C  CB   . CYS A  1 215 ? -0.50700  -21.15300 15.40200  1.000 17.68082  ? 215 CYS A CB   1 
ATOM   2591 S  SG   . CYS A  1 215 ? -1.29300  -21.55700 17.04000  1.000 17.12312  ? 215 CYS A SG   1 
ATOM   2592 H  H    . CYS A  1 215 ? -2.60300  -20.28900 14.26600  1.000 20.47697  ? 215 CYS A H    1 
ATOM   2593 H  HA   . CYS A  1 215 ? -0.54900  -19.12500 15.63900  1.000 19.62227  ? 215 CYS A HA   1 
ATOM   2594 H  HB2  . CYS A  1 215 ? -0.83500  -21.78500 14.74400  1.000 21.21955  ? 215 CYS A HB2  1 
ATOM   2595 H  HB3  . CYS A  1 215 ? 0.45400   -21.24100 15.49700  1.000 21.21955  ? 215 CYS A HB3  1 
ATOM   2596 N  N    . GLU A  1 216 ? 0.52600   -18.19100 13.66900  1.000 17.85705  ? 216 GLU A N    1 
ATOM   2597 C  CA   . GLU A  1 216 ? 0.93000   -17.55000 12.42100  1.000 18.35428  ? 216 GLU A CA   1 
ATOM   2598 C  C    . GLU A  1 216 ? 1.66000   -18.49600 11.47000  1.000 20.17768  ? 216 GLU A C    1 
ATOM   2599 O  O    . GLU A  1 216 ? 1.40300   -18.48500 10.24500  1.000 21.38861  ? 216 GLU A O    1 
ATOM   2600 C  CB   . GLU A  1 216 ? 1.82000   -16.33200 12.67700  1.000 19.80766  ? 216 GLU A CB   1 
ATOM   2601 C  CG   . GLU A  1 216 ? 2.20900   -15.59200 11.39500  1.000 20.90414  ? 216 GLU A CG   1 
ATOM   2602 C  CD   . GLU A  1 216 ? 3.20400   -14.50200 11.63900  1.000 27.12966  ? 216 GLU A CD   1 
ATOM   2603 O  OE1  . GLU A  1 216 ? 3.99600   -14.53500 12.61100  1.000 25.39564  ? 216 GLU A OE1  1 
ATOM   2604 O  OE2  . GLU A  1 216 ? 3.30200   -13.59000 10.78500  1.000 32.66287  ? 216 GLU A OE2  1 
ATOM   2605 H  H    . GLU A  1 216 ? 0.73700   -17.75200 14.37800  1.000 21.43103  ? 216 GLU A H    1 
ATOM   2606 H  HA   . GLU A  1 216 ? 0.10800   -17.25700 11.99600  1.000 22.02770  ? 216 GLU A HA   1 
ATOM   2607 H  HB2  . GLU A  1 216 ? 1.34500   -15.71000 13.24900  1.000 23.77175  ? 216 GLU A HB2  1 
ATOM   2608 H  HB3  . GLU A  1 216 ? 2.63600   -16.62600 13.11200  1.000 23.77175  ? 216 GLU A HB3  1 
ATOM   2609 H  HG2  . GLU A  1 216 ? 2.60100   -16.22400 10.77200  1.000 25.08753  ? 216 GLU A HG2  1 
ATOM   2610 H  HG3  . GLU A  1 216 ? 1.41500   -15.19300 11.00700  1.000 25.08753  ? 216 GLU A HG3  1 
ATOM   2611 N  N    . ARG A  1 217 ? 2.60600   -19.28400 11.98300  1.000 19.50995  ? 217 ARG A N    1 
ATOM   2612 C  CA   . ARG A  1 217 ? 3.50100   -20.08900 11.15800  1.000 18.68009  ? 217 ARG A CA   1 
ATOM   2613 C  C    . ARG A  1 217 ? 3.10400   -21.56000 11.15000  1.000 19.98608  ? 217 ARG A C    1 
ATOM   2614 O  O    . ARG A  1 217 ? 3.93800   -22.44000 10.87300  1.000 22.37457  ? 217 ARG A O    1 
ATOM   2615 C  CB   . ARG A  1 217 ? 4.92500   -19.88700 11.63200  1.000 21.46699  ? 217 ARG A CB   1 
ATOM   2616 C  CG   . ARG A  1 217 ? 5.38100   -18.47100 11.36900  1.000 25.80867  ? 217 ARG A CG   1 
ATOM   2617 C  CD   . ARG A  1 217 ? 6.80600   -18.27300 11.65800  1.000 40.80065  ? 217 ARG A CD   1 
ATOM   2618 N  NE   . ARG A  1 217 ? 7.61700   -18.95000 10.66100  1.000 40.51289  ? 217 ARG A NE   1 
ATOM   2619 C  CZ   . ARG A  1 217 ? 8.90600   -18.73600 10.52700  1.000 38.09122  ? 217 ARG A CZ   1 
ATOM   2620 N  NH1  . ARG A  1 217 ? 9.54000   -17.86900 11.30000  1.000 43.67607  ? 217 ARG A NH1  1 
ATOM   2621 N  NH2  . ARG A  1 217 ? 9.58000   -19.41900 9.61400   1.000 34.11619  ? 217 ARG A NH2  1 
ATOM   2622 H  H    . ARG A  1 217 ? 2.75000   -19.36900 12.82700  1.000 23.41451  ? 217 ARG A H    1 
ATOM   2623 H  HA   . ARG A  1 217 ? 3.45600   -19.79300 10.23600  1.000 22.41868  ? 217 ARG A HA   1 
ATOM   2624 H  HB2  . ARG A  1 217 ? 4.97600   -20.05600 12.58600  1.000 25.76295  ? 217 ARG A HB2  1 
ATOM   2625 H  HB3  . ARG A  1 217 ? 5.51300   -20.49500 11.15600  1.000 25.76295  ? 217 ARG A HB3  1 
ATOM   2626 H  HG2  . ARG A  1 217 ? 5.23200   -18.25800 10.43500  1.000 30.97296  ? 217 ARG A HG2  1 
ATOM   2627 H  HG3  . ARG A  1 217 ? 4.87400   -17.86500 11.93200  1.000 30.97296  ? 217 ARG A HG3  1 
ATOM   2628 H  HD2  . ARG A  1 217 ? 7.01500   -17.32600 11.63700  1.000 48.96334  ? 217 ARG A HD2  1 
ATOM   2629 H  HD3  . ARG A  1 217 ? 7.01600   -18.64000 12.53100  1.000 48.96334  ? 217 ARG A HD3  1 
ATOM   2630 H  HE   . ARG A  1 217 ? 7.23600   -19.51600 10.13700  1.000 48.61802  ? 217 ARG A HE   1 
ATOM   2631 H  HH11 . ARG A  1 217 ? 9.10800   -17.43300 11.90300  1.000 52.41384  ? 217 ARG A HH11 1 
ATOM   2632 H  HH12 . ARG A  1 217 ? 10.38500  -17.74000 11.19900  1.000 52.41384  ? 217 ARG A HH12 1 
ATOM   2633 H  HH21 . ARG A  1 217 ? 9.17400   -19.99300 9.11900   1.000 40.94199  ? 217 ARG A HH21 1 
ATOM   2634 H  HH22 . ARG A  1 217 ? 10.42500  -19.28900 9.51600   1.000 40.94199  ? 217 ARG A HH22 1 
ATOM   2635 N  N    . ASP A  1 218 ? 1.81500   -21.82900 11.36700  1.000 19.98641  ? 218 ASP A N    1 
ATOM   2636 C  CA   . ASP A  1 218 ? 1.25700   -23.18400 11.38400  1.000 19.71589  ? 218 ASP A CA   1 
ATOM   2637 C  C    . ASP A  1 218 ? 1.37100   -23.83000 10.00900  1.000 22.34429  ? 218 ASP A C    1 
ATOM   2638 O  O    . ASP A  1 218 ? 0.89700   -23.27300 9.02300   1.000 22.49296  ? 218 ASP A O    1 
ATOM   2639 C  CB   . ASP A  1 218 ? -0.21200  -23.05500 11.79400  1.000 18.53382  ? 218 ASP A CB   1 
ATOM   2640 C  CG   . ASP A  1 218 ? -0.87300  -24.36300 12.14700  1.000 17.83551  ? 218 ASP A CG   1 
ATOM   2641 O  OD1  . ASP A  1 218 ? -0.45500  -25.42600 11.65900  1.000 19.33622  ? 218 ASP A OD1  1 
ATOM   2642 O  OD2  . ASP A  1 218 ? -1.85900  -24.30600 12.90500  1.000 17.73986  ? 218 ASP A OD2  1 
ATOM   2643 H  H    . ASP A  1 218 ? 1.22100   -21.22400 11.51200  1.000 23.98625  ? 218 ASP A H    1 
ATOM   2644 H  HA   . ASP A  1 218 ? 1.73700   -23.75000 12.00900  1.000 23.66163  ? 218 ASP A HA   1 
ATOM   2645 H  HB2  . ASP A  1 218 ? -0.26800  -22.47900 12.57200  1.000 22.24314  ? 218 ASP A HB2  1 
ATOM   2646 H  HB3  . ASP A  1 218 ? -0.70700  -22.66500 11.05600  1.000 22.24314  ? 218 ASP A HB3  1 
ATOM   2647 N  N    A SER A  1 219 ? 2.01000   -24.99700 9.93000   0.700 20.29822  ? 219 SER A N    1 
ATOM   2648 N  N    B SER A  1 219 ? 2.02500   -24.99300 9.94700   0.300 20.69978  ? 219 SER A N    1 
ATOM   2649 C  CA   A SER A  1 219 ? 2.10800   -25.71700 8.67200   0.700 20.57541  ? 219 SER A CA   1 
ATOM   2650 C  CA   B SER A  1 219 ? 2.16400   -25.75000 8.71100   0.300 22.06020  ? 219 SER A CA   1 
ATOM   2651 C  C    A SER A  1 219 ? 1.15100   -26.90200 8.59000   0.700 22.67132  ? 219 SER A C    1 
ATOM   2652 C  C    B SER A  1 219 ? 1.20500   -26.93700 8.61900   0.300 22.06429  ? 219 SER A C    1 
ATOM   2653 O  O    A SER A  1 219 ? 1.06200   -27.54200 7.52700   0.700 23.22403  ? 219 SER A O    1 
ATOM   2654 O  O    B SER A  1 219 ? 1.17700   -27.61800 7.58600   0.300 26.49052  ? 219 SER A O    1 
ATOM   2655 C  CB   A SER A  1 219 ? 3.53600   -26.19300 8.43600   0.700 29.55842  ? 219 SER A CB   1 
ATOM   2656 C  CB   B SER A  1 219 ? 3.61300   -26.23500 8.53100   0.300 28.87113  ? 219 SER A CB   1 
ATOM   2657 O  OG   A SER A  1 219 ? 3.83500   -27.13900 9.41600   0.700 26.07267  ? 219 SER A OG   1 
ATOM   2658 O  OG   B SER A  1 219 ? 4.52200   -25.14900 8.43300   0.300 28.02487  ? 219 SER A OG   1 
ATOM   2659 H  H    A SER A  1 219 ? 2.39300   -25.38800 10.59400  0.700 24.36042  ? 219 SER A H    1 
ATOM   2660 H  H    B SER A  1 219 ? 2.40300   -25.36700 10.62300  0.300 24.84230  ? 219 SER A H    1 
ATOM   2661 H  HA   A SER A  1 219 ? 1.88300   -25.10400 7.95500   0.700 24.69306  ? 219 SER A HA   1 
ATOM   2662 H  HA   B SER A  1 219 ? 1.96300   -25.15400 7.97300   0.300 26.47481  ? 219 SER A HA   1 
ATOM   2663 H  HB2  A SER A  1 219 ? 3.60600   -26.59800 7.55700   0.700 35.47267  ? 219 SER A HB2  1 
ATOM   2664 H  HB2  B SER A  1 219 ? 3.85800   -26.77900 9.29500   0.300 34.64792  ? 219 SER A HB2  1 
ATOM   2665 H  HB3  A SER A  1 219 ? 4.14800   -25.44300 8.50500   0.700 35.47267  ? 219 SER A HB3  1 
ATOM   2666 H  HB3  B SER A  1 219 ? 3.66700   -26.76100 7.71800   0.300 34.64792  ? 219 SER A HB3  1 
ATOM   2667 H  HG   A SER A  1 219 ? 3.65300   -26.83100 10.17700  0.700 31.28977  ? 219 SER A HG   1 
ATOM   2668 H  HG   B SER A  1 219 ? 4.25400   -24.60100 7.85600   0.300 33.63241  ? 219 SER A HG   1 
ATOM   2669 N  N    . ILE A  1 220 ? 0.43700   -27.20600 9.67400   1.000 21.71888  ? 220 ILE A N    1 
ATOM   2670 C  CA   . ILE A  1 220 ? -0.49100  -28.32600 9.71800   1.000 23.50730  ? 220 ILE A CA   1 
ATOM   2671 C  C    . ILE A  1 220 ? -1.91800  -27.89200 9.39600   1.000 22.34116  ? 220 ILE A C    1 
ATOM   2672 O  O    . ILE A  1 220 ? -2.61700  -28.55500 8.62400   1.000 24.24488  ? 220 ILE A O    1 
ATOM   2673 C  CB   . ILE A  1 220 ? -0.41200  -28.97800 11.12200  1.000 22.83375  ? 220 ILE A CB   1 
ATOM   2674 C  CG1  . ILE A  1 220 ? 1.05200   -29.36100 11.46800  1.000 27.89240  ? 220 ILE A CG1  1 
ATOM   2675 C  CG2  . ILE A  1 220 ? -1.34400  -30.13800 11.21000  1.000 26.22904  ? 220 ILE A CG2  1 
ATOM   2676 C  CD1  . ILE A  1 220 ? 1.79600   -30.13300 10.43100  1.000 34.61524  ? 220 ILE A CD1  1 
ATOM   2677 H  H    . ILE A  1 220 ? 0.47500   -26.76600 10.41200  1.000 26.06522  ? 220 ILE A H    1 
ATOM   2678 H  HA   . ILE A  1 220 ? -0.23900  -28.98000 9.04800   1.000 28.21132  ? 220 ILE A HA   1 
ATOM   2679 H  HB   . ILE A  1 220 ? -0.69600  -28.33000 11.78600  1.000 27.40306  ? 220 ILE A HB   1 
ATOM   2680 H  HG12 . ILE A  1 220 ? 1.54900   -28.54300 11.62600  1.000 33.47344  ? 220 ILE A HG12 1 
ATOM   2681 H  HG13 . ILE A  1 220 ? 1.04000   -29.90200 12.27300  1.000 33.47344  ? 220 ILE A HG13 1 
ATOM   2682 H  HG21 . ILE A  1 220 ? -1.23100  -30.57000 12.07100  1.000 31.47741  ? 220 ILE A HG21 1 
ATOM   2683 H  HG22 . ILE A  1 220 ? -2.25500  -29.81900 11.11700  1.000 31.47741  ? 220 ILE A HG22 1 
ATOM   2684 H  HG23 . ILE A  1 220 ? -1.13800  -30.76300 10.49700  1.000 31.47741  ? 220 ILE A HG23 1 
ATOM   2685 H  HD11 . ILE A  1 220 ? 2.68100   -30.34400 10.76900  1.000 41.54085  ? 220 ILE A HD11 1 
ATOM   2686 H  HD12 . ILE A  1 220 ? 1.31200   -30.95100 10.23800  1.000 41.54085  ? 220 ILE A HD12 1 
ATOM   2687 H  HD13 . ILE A  1 220 ? 1.86800   -29.59500 9.62800   1.000 41.54085  ? 220 ILE A HD13 1 
ATOM   2688 N  N    . ALA A  1 221 ? -2.33800  -26.77000 9.98300   1.000 21.22979  ? 221 ALA A N    1 
ATOM   2689 C  CA   . ALA A  1 221 ? -3.59000  -26.08300 9.65300   1.000 19.95778  ? 221 ALA A CA   1 
ATOM   2690 C  C    . ALA A  1 221 ? -3.24000  -24.65300 9.25200   1.000 18.84405  ? 221 ALA A C    1 
ATOM   2691 O  O    . ALA A  1 221 ? -3.48300  -23.70800 10.01500  1.000 19.80632  ? 221 ALA A O    1 
ATOM   2692 C  CB   . ALA A  1 221 ? -4.53300  -26.10900 10.85400  1.000 20.41623  ? 221 ALA A CB   1 
ATOM   2693 H  H    . ALA A  1 221 ? -1.89600  -26.37000 10.60300  1.000 25.47831  ? 221 ALA A H    1 
ATOM   2694 H  HA   . ALA A  1 221 ? -4.03700  -26.51100 8.90500   1.000 23.95190  ? 221 ALA A HA   1 
ATOM   2695 H  HB1  . ALA A  1 221 ? -5.36700  -25.67600 10.61100  1.000 24.50204  ? 221 ALA A HB1  1 
ATOM   2696 H  HB2  . ALA A  1 221 ? -4.70000  -27.03100 11.10500  1.000 24.50204  ? 221 ALA A HB2  1 
ATOM   2697 H  HB3  . ALA A  1 221 ? -4.11800  -25.63500 11.59200  1.000 24.50204  ? 221 ALA A HB3  1 
ATOM   2698 N  N    . PRO A  1 222 ? -2.58600  -24.47600 8.10400   1.000 20.33303  ? 222 PRO A N    1 
ATOM   2699 C  CA   . PRO A  1 222 ? -2.12000  -23.14600 7.71900   1.000 20.63243  ? 222 PRO A CA   1 
ATOM   2700 C  C    . PRO A  1 222 ? -3.21300  -22.09700 7.83800   1.000 21.24822  ? 222 PRO A C    1 
ATOM   2701 O  O    . PRO A  1 222 ? -4.34300  -22.28800 7.38500   1.000 22.02568  ? 222 PRO A O    1 
ATOM   2702 C  CB   . PRO A  1 222 ? -1.67400  -23.33400 6.26800   1.000 23.37880  ? 222 PRO A CB   1 
ATOM   2703 C  CG   . PRO A  1 222 ? -1.41800  -24.79800 6.11500   1.000 32.37174  ? 222 PRO A CG   1 
ATOM   2704 C  CD   . PRO A  1 222 ? -2.30000  -25.52000 7.11700   1.000 23.33846  ? 222 PRO A CD   1 
ATOM   2705 H  HA   . PRO A  1 222 ? -1.36500  -22.88300 8.26800   1.000 24.76147  ? 222 PRO A HA   1 
ATOM   2706 H  HB2  . PRO A  1 222 ? -2.37800  -23.04200 5.66800   1.000 28.05712  ? 222 PRO A HB2  1 
ATOM   2707 H  HB3  . PRO A  1 222 ? -0.86500  -22.82400 6.10500   1.000 28.05712  ? 222 PRO A HB3  1 
ATOM   2708 H  HG2  . PRO A  1 222 ? -1.64100  -25.07000 5.21100   1.000 38.84865  ? 222 PRO A HG2  1 
ATOM   2709 H  HG3  . PRO A  1 222 ? -0.48300  -24.98100 6.29500   1.000 38.84865  ? 222 PRO A HG3  1 
ATOM   2710 H  HD2  . PRO A  1 222 ? -3.11700  -25.83500 6.69800   1.000 28.00872  ? 222 PRO A HD2  1 
ATOM   2711 H  HD3  . PRO A  1 222 ? -1.82800  -26.26300 7.52400   1.000 28.00872  ? 222 PRO A HD3  1 
ATOM   2712 N  N    A VAL A  1 223 ? -2.87500  -20.96400 8.46100   0.602 18.11587  ? 223 VAL A N    1 
ATOM   2713 N  N    B VAL A  1 223 ? -2.82700  -20.96100 8.40800   0.398 21.70902  ? 223 VAL A N    1 
ATOM   2714 C  CA   A VAL A  1 223 ? -3.87900  -19.92800 8.70500   0.602 20.73128  ? 223 VAL A CA   1 
ATOM   2715 C  CA   B VAL A  1 223 ? -3.75000  -19.86700 8.69900   0.398 19.41962  ? 223 VAL A CA   1 
ATOM   2716 C  C    A VAL A  1 223 ? -4.56800  -19.49200 7.41100   0.602 20.59347  ? 223 VAL A C    1 
ATOM   2717 C  C    B VAL A  1 223 ? -4.50300  -19.41800 7.44900   0.398 20.09686  ? 223 VAL A C    1 
ATOM   2718 O  O    A VAL A  1 223 ? -5.78100  -19.24000 7.40700   0.602 20.97701  ? 223 VAL A O    1 
ATOM   2719 O  O    B VAL A  1 223 ? -5.69300  -19.08000 7.51500   0.398 21.63622  ? 223 VAL A O    1 
ATOM   2720 C  CB   A VAL A  1 223 ? -3.29000  -18.73100 9.47500   0.602 22.02588  ? 223 VAL A CB   1 
ATOM   2721 C  CB   B VAL A  1 223 ? -2.96100  -18.72300 9.35600   0.398 23.50351  ? 223 VAL A CB   1 
ATOM   2722 C  CG1  A VAL A  1 223 ? -2.64900  -19.20200 10.79400  0.602 22.39322  ? 223 VAL A CG1  1 
ATOM   2723 C  CG1  B VAL A  1 223 ? -3.64500  -17.40700 9.21500   0.398 29.17308  ? 223 VAL A CG1  1 
ATOM   2724 C  CG2  A VAL A  1 223 ? -2.26900  -18.00400 8.63300   0.602 23.11156  ? 223 VAL A CG2  1 
ATOM   2725 C  CG2  B VAL A  1 223 ? -2.70600  -19.06300 10.83900  0.398 23.42727  ? 223 VAL A CG2  1 
ATOM   2726 H  H    A VAL A  1 223 ? -2.08600  -20.77400 8.74600   0.602 21.74161  ? 223 VAL A H    1 
ATOM   2727 H  H    B VAL A  1 223 ? -2.01800  -20.79200 8.64400   0.398 26.05339  ? 223 VAL A H    1 
ATOM   2728 H  HA   A VAL A  1 223 ? -4.55700  -20.32600 9.27300   0.602 24.88010  ? 223 VAL A HA   1 
ATOM   2729 H  HA   B VAL A  1 223 ? -4.43000  -20.17800 9.31700   0.398 23.30611  ? 223 VAL A HA   1 
ATOM   2730 H  HB   A VAL A  1 223 ? -4.00900  -18.11400 9.68200   0.602 26.43362  ? 223 VAL A HB   1 
ATOM   2731 H  HB   B VAL A  1 223 ? -2.11000  -18.63300 8.89900   0.398 28.20677  ? 223 VAL A HB   1 
ATOM   2732 H  HG11 A VAL A  1 223 ? -2.30100  -18.43100 11.26900  0.602 26.87442  ? 223 VAL A HG11 1 
ATOM   2733 H  HG11 B VAL A  1 223 ? -3.23800  -16.77200 9.82500   0.398 35.01026  ? 223 VAL A HG11 1 
ATOM   2734 H  HG12 A VAL A  1 223 ? -3.32300  -19.64500 11.33200  0.602 26.87442  ? 223 VAL A HG12 1 
ATOM   2735 H  HG12 B VAL A  1 223 ? -3.54700  -17.09600 8.30100   0.398 35.01026  ? 223 VAL A HG12 1 
ATOM   2736 H  HG13 A VAL A  1 223 ? -1.92800  -19.81900 10.59200  0.602 26.87442  ? 223 VAL A HG13 1 
ATOM   2737 H  HG13 B VAL A  1 223 ? -4.58500  -17.51400 9.42800   0.398 35.01026  ? 223 VAL A HG13 1 
ATOM   2738 H  HG21 A VAL A  1 223 ? -1.86100  -17.30300 9.16600   0.602 27.73643  ? 223 VAL A HG21 1 
ATOM   2739 H  HG21 B VAL A  1 223 ? -2.47300  -18.25000 11.31300  0.398 28.11529  ? 223 VAL A HG21 1 
ATOM   2740 H  HG22 A VAL A  1 223 ? -1.59200  -18.63500 8.34200   0.602 27.73643  ? 223 VAL A HG22 1 
ATOM   2741 H  HG22 B VAL A  1 223 ? -3.51200  -19.44800 11.21700  0.398 28.11529  ? 223 VAL A HG22 1 
ATOM   2742 H  HG23 A VAL A  1 223 ? -2.71300  -17.61700 7.86200   0.602 27.73643  ? 223 VAL A HG23 1 
ATOM   2743 H  HG23 B VAL A  1 223 ? -1.97700  -19.70100 10.89600  0.398 28.11529  ? 223 VAL A HG23 1 
ATOM   2744 N  N    . ARG A  1 224 ? -3.83900  -19.38800 6.31100   1.000 23.07046  ? 224 ARG A N    1 
ATOM   2745 C  CA   . ARG A  1 224 ? -4.47100  -18.92200 5.08600   1.000 22.81806  ? 224 ARG A CA   1 
ATOM   2746 C  C    . ARG A  1 224 ? -5.56700  -19.85100 4.57200   1.000 22.62078  ? 224 ARG A C    1 
ATOM   2747 O  O    . ARG A  1 224 ? -6.41100  -19.40000 3.78300   1.000 24.72849  ? 224 ARG A O    1 
ATOM   2748 C  CB   . ARG A  1 224 ? -3.39600  -18.67500 4.02200   1.000 26.04589  ? 224 ARG A CB   1 
ATOM   2749 C  CG   . ARG A  1 224 ? -2.50800  -17.49800 4.35600   1.000 55.31505  ? 224 ARG A CG   1 
ATOM   2750 C  CD   . ARG A  1 224 ? -1.47600  -17.25000 3.26300   1.000 76.68926  ? 224 ARG A CD   1 
ATOM   2751 N  NE   . ARG A  1 224 ? -0.54400  -16.19100 3.63300   1.000 85.05343  ? 224 ARG A NE   1 
ATOM   2752 C  CZ   . ARG A  1 224 ? 0.53400   -15.86000 2.93600   1.000 93.48331  ? 224 ARG A CZ   1 
ATOM   2753 N  NH1  . ARG A  1 224 ? 0.84900   -16.48300 1.81100   1.000 97.33129  ? 224 ARG A NH1  1 
ATOM   2754 N  NH2  . ARG A  1 224 ? 1.31900   -14.88200 3.38200   1.000 94.28659  ? 224 ARG A NH2  1 
ATOM   2755 H  H    . ARG A  1 224 ? -3.00100  -19.57500 6.25100   1.000 27.68711  ? 224 ARG A H    1 
ATOM   2756 H  HA   . ARG A  1 224 ? -4.91200  -18.07600 5.26100   1.000 27.38423  ? 224 ARG A HA   1 
ATOM   2757 H  HB2  . ARG A  1 224 ? -2.83600  -19.46400 3.95000   1.000 31.25763  ? 224 ARG A HB2  1 
ATOM   2758 H  HB3  . ARG A  1 224 ? -3.82800  -18.49500 3.17300   1.000 31.25763  ? 224 ARG A HB3  1 
ATOM   2759 H  HG2  . ARG A  1 224 ? -3.05300  -16.70000 4.44800   1.000 66.38063  ? 224 ARG A HG2  1 
ATOM   2760 H  HG3  . ARG A  1 224 ? -2.03700  -17.67600 5.18600   1.000 66.38063  ? 224 ARG A HG3  1 
ATOM   2761 H  HD2  . ARG A  1 224 ? -0.96900  -18.06300 3.11100   1.000 92.02968  ? 224 ARG A HD2  1 
ATOM   2762 H  HD3  . ARG A  1 224 ? -1.93000  -16.98500 2.44800   1.000 92.02968  ? 224 ARG A HD3  1 
ATOM   2763 H  HE   . ARG A  1 224 ? -0.70500  -15.75100 4.35400   1.000 102.06668 ? 224 ARG A HE   1 
ATOM   2764 H  HH11 . ARG A  1 224 ? 0.34900   -17.11800 1.51700   1.000 116.80011 ? 224 ARG A HH11 1 
ATOM   2765 H  HH12 . ARG A  1 224 ? 1.55300   -16.25200 1.37400   1.000 116.80011 ? 224 ARG A HH12 1 
ATOM   2766 H  HH21 . ARG A  1 224 ? 1.12500   -14.47400 4.11300   1.000 113.14647 ? 224 ARG A HH21 1 
ATOM   2767 H  HH22 . ARG A  1 224 ? 2.02100   -14.65900 2.93800   1.000 113.14647 ? 224 ARG A HH22 1 
ATOM   2768 N  N    . SER A  1 225 ? -5.55100  -21.13400 4.92500   1.000 23.26355  ? 225 SER A N    1 
ATOM   2769 C  CA   . SER A  1 225 ? -6.54100  -22.09400 4.46400   1.000 24.20087  ? 225 SER A CA   1 
ATOM   2770 C  C    . SER A  1 225 ? -7.52500  -22.52400 5.54500   1.000 21.96595  ? 225 SER A C    1 
ATOM   2771 O  O    . SER A  1 225 ? -8.53300  -23.16500 5.22400   1.000 23.16016  ? 225 SER A O    1 
ATOM   2772 C  CB   . SER A  1 225 ? -5.85000  -23.36300 3.93800   1.000 27.29812  ? 225 SER A CB   1 
ATOM   2773 O  OG   . SER A  1 225 ? -5.03400  -23.05000 2.82200   1.000 30.87739  ? 225 SER A OG   1 
ATOM   2774 H  H    . SER A  1 225 ? -4.96000  -21.47800 5.44500   1.000 27.91882  ? 225 SER A H    1 
ATOM   2775 H  HA   . SER A  1 225 ? -7.03700  -21.68200 3.73900   1.000 29.04361  ? 225 SER A HA   1 
ATOM   2776 H  HB2  . SER A  1 225 ? -5.29800  -23.73900 4.64200   1.000 32.76031  ? 225 SER A HB2  1 
ATOM   2777 H  HB3  . SER A  1 225 ? -6.52600  -24.00400 3.66900   1.000 32.76031  ? 225 SER A HB3  1 
ATOM   2778 H  HG   . SER A  1 225 ? -4.55900  -23.71300 2.61900   1.000 37.05543  ? 225 SER A HG   1 
ATOM   2779 N  N    . HIS A  1 226 ? -7.26800  -22.20000 6.80300   1.000 20.38235  ? 226 HIS A N    1 
ATOM   2780 C  CA   . HIS A  1 226 ? -8.09100  -22.64300 7.91800   1.000 19.46377  ? 226 HIS A CA   1 
ATOM   2781 C  C    . HIS A  1 226 ? -8.46600  -21.43900 8.77200   1.000 19.75836  ? 226 HIS A C    1 
ATOM   2782 O  O    . HIS A  1 226 ? -9.49000  -20.81400 8.49100   1.000 20.50969  ? 226 HIS A O    1 
ATOM   2783 C  CB   . HIS A  1 226 ? -7.36000  -23.75400 8.67600   1.000 19.61066  ? 226 HIS A CB   1 
ATOM   2784 C  CG   . HIS A  1 226 ? -7.14300  -24.98200 7.85900   1.000 19.69481  ? 226 HIS A CG   1 
ATOM   2785 N  ND1  . HIS A  1 226 ? -8.08300  -25.98000 7.76900   1.000 22.23284  ? 226 HIS A ND1  1 
ATOM   2786 C  CD2  . HIS A  1 226 ? -6.10600  -25.36600 7.08800   1.000 21.30650  ? 226 HIS A CD2  1 
ATOM   2787 C  CE1  . HIS A  1 226 ? -7.63700  -26.93000 6.97400   1.000 22.10552  ? 226 HIS A CE1  1 
ATOM   2788 N  NE2  . HIS A  1 226 ? -6.44200  -26.57500 6.52600   1.000 23.94207  ? 226 HIS A NE2  1 
ATOM   2789 H  H    . HIS A  1 226 ? -6.60400  -21.71100 7.04600   1.000 24.46139  ? 226 HIS A H    1 
ATOM   2790 H  HA   . HIS A  1 226 ? -8.92900  -23.03500 7.62700   1.000 23.35908  ? 226 HIS A HA   1 
ATOM   2791 H  HB2  . HIS A  1 226 ? -6.49200  -23.42400 8.95500   1.000 23.53536  ? 226 HIS A HB2  1 
ATOM   2792 H  HB3  . HIS A  1 226 ? -7.88600  -24.00200 9.45300   1.000 23.53536  ? 226 HIS A HB3  1 
ATOM   2793 H  HD2  . HIS A  1 226 ? -5.31100  -24.89900 6.96000   1.000 25.57036  ? 226 HIS A HD2  1 
ATOM   2794 H  HE1  . HIS A  1 226 ? -8.08400  -27.71700 6.76300   1.000 26.52918  ? 226 HIS A HE1  1 
ATOM   2795 H  HE2  . HIS A  1 226 ? -5.95700  -27.02500 5.97600   1.000 28.73304  ? 226 HIS A HE2  1 
ATOM   2796 N  N    . ALA A  1 227 ? -7.70000  -21.07800 9.79600   1.000 18.48903  ? 227 ALA A N    1 
ATOM   2797 C  CA   . ALA A  1 227 ? -8.17200  -20.08700 10.76500  1.000 18.96607  ? 227 ALA A CA   1 
ATOM   2798 C  C    . ALA A  1 227 ? -8.69600  -18.80200 10.13400  1.000 18.70271  ? 227 ALA A C    1 
ATOM   2799 O  O    . ALA A  1 227 ? -9.74100  -18.28600 10.55900  1.000 18.83059  ? 227 ALA A O    1 
ATOM   2800 C  CB   . ALA A  1 227 ? -7.05000  -19.77500 11.77000  1.000 18.49727  ? 227 ALA A CB   1 
ATOM   2801 H  H    . ALA A  1 227 ? -6.91200  -21.38500 9.95300   1.000 22.18939  ? 227 ALA A H    1 
ATOM   2802 H  HA   . ALA A  1 227 ? -8.92500  -20.48200 11.23100  1.000 22.76185  ? 227 ALA A HA   1 
ATOM   2803 H  HB1  . ALA A  1 227 ? -7.37300  -19.12000 12.41000  1.000 22.19929  ? 227 ALA A HB1  1 
ATOM   2804 H  HB2  . ALA A  1 227 ? -6.80200  -20.59200 12.23000  1.000 22.19929  ? 227 ALA A HB2  1 
ATOM   2805 H  HB3  . ALA A  1 227 ? -6.28600  -19.41900 11.29100  1.000 22.19929  ? 227 ALA A HB3  1 
ATOM   2806 N  N    . SER A  1 228 ? -7.97900  -18.25200 9.15500   1.000 19.20901  ? 228 SER A N    1 
ATOM   2807 C  CA   . SER A  1 228 ? -8.37700  -16.95500 8.60800   1.000 19.37855  ? 228 SER A CA   1 
ATOM   2808 C  C    . SER A  1 228 ? -9.66000  -17.04800 7.81900   1.000 19.16211  ? 228 SER A C    1 
ATOM   2809 O  O    . SER A  1 228 ? -10.60100 -16.29200 8.11600   1.000 19.89349  ? 228 SER A O    1 
ATOM   2810 C  CB   . SER A  1 228 ? -7.22500  -16.32300 7.82900   1.000 22.29313  ? 228 SER A CB   1 
ATOM   2811 O  OG   . SER A  1 228 ? -7.61900  -15.09600 7.25400   1.000 22.41149  ? 228 SER A OG   1 
ATOM   2812 H  H    . SER A  1 228 ? -7.27700  -18.59800 8.79800   1.000 23.05337  ? 228 SER A H    1 
ATOM   2813 H  HA   . SER A  1 228 ? -8.55200  -16.35800 9.35300   1.000 23.25682  ? 228 SER A HA   1 
ATOM   2814 H  HB2  . SER A  1 228 ? -6.48400  -16.16400 8.43400   1.000 26.75432  ? 228 SER A HB2  1 
ATOM   2815 H  HB3  . SER A  1 228 ? -6.95200  -16.93000 7.12200   1.000 26.75432  ? 228 SER A HB3  1 
ATOM   2816 H  HG   . SER A  1 228 ? -8.24700  -15.22200 6.71000   1.000 26.89635  ? 228 SER A HG   1 
ATOM   2817 N  N    . PRO A  1 229 ? -9.80000  -17.94500 6.86000   1.000 19.86980  ? 229 PRO A N    1 
ATOM   2818 C  CA   . PRO A  1 229 ? -11.09100 -18.04500 6.18800   1.000 20.68361  ? 229 PRO A CA   1 
ATOM   2819 C  C    . PRO A  1 229 ? -12.20600 -18.47300 7.12300   1.000 19.91334  ? 229 PRO A C    1 
ATOM   2820 O  O    . PRO A  1 229 ? -13.36000 -18.10300 6.85900   1.000 20.91345  ? 229 PRO A O    1 
ATOM   2821 C  CB   . PRO A  1 229 ? -10.88700 -19.06400 5.07000   1.000 22.99850  ? 229 PRO A CB   1 
ATOM   2822 C  CG   . PRO A  1 229 ? -9.59400  -19.72000 5.35400   1.000 26.76648  ? 229 PRO A CG   1 
ATOM   2823 C  CD   . PRO A  1 229 ? -8.76600  -18.76400 6.20000   1.000 23.51325  ? 229 PRO A CD   1 
ATOM   2824 H  HA   . PRO A  1 229 ? -11.29800 -17.19000 5.77800   1.000 24.82289  ? 229 PRO A HA   1 
ATOM   2825 H  HB2  . PRO A  1 229 ? -11.61100 -19.71000 5.08100   1.000 27.60076  ? 229 PRO A HB2  1 
ATOM   2826 H  HB3  . PRO A  1 229 ? -10.86200 -18.60900 4.21400   1.000 27.60076  ? 229 PRO A HB3  1 
ATOM   2827 H  HG2  . PRO A  1 229 ? -9.75400  -20.54500 5.83800   1.000 32.12234  ? 229 PRO A HG2  1 
ATOM   2828 H  HG3  . PRO A  1 229 ? -9.14000  -19.90800 4.51800   1.000 32.12234  ? 229 PRO A HG3  1 
ATOM   2829 H  HD2  . PRO A  1 229 ? -8.23500  -19.24700 6.85300   1.000 28.21846  ? 229 PRO A HD2  1 
ATOM   2830 H  HD3  . PRO A  1 229 ? -8.19000  -18.21700 5.64400   1.000 28.21846  ? 229 PRO A HD3  1 
ATOM   2831 N  N    . PHE A  1 230 ? -11.94200 -19.24600 8.16900   1.000 19.31198  ? 230 PHE A N    1 
ATOM   2832 C  CA   . PHE A  1 230 ? -13.01700 -19.56800 9.10100   1.000 19.86561  ? 230 PHE A CA   1 
ATOM   2833 C  C    . PHE A  1 230 ? -13.52500 -18.29700 9.76300   1.000 21.30401  ? 230 PHE A C    1 
ATOM   2834 O  O    . PHE A  1 230 ? -14.73500 -18.07500 9.87300   1.000 19.85502  ? 230 PHE A O    1 
ATOM   2835 C  CB   . PHE A  1 230 ? -12.60000 -20.60400 10.15800  1.000 20.14430  ? 230 PHE A CB   1 
ATOM   2836 C  CG   . PHE A  1 230 ? -12.11900 -21.92100 9.60000   1.000 18.91710  ? 230 PHE A CG   1 
ATOM   2837 C  CD1  . PHE A  1 230 ? -12.39000 -22.29800 8.29300   1.000 19.29846  ? 230 PHE A CD1  1 
ATOM   2838 C  CD2  . PHE A  1 230 ? -11.36000 -22.77100 10.39900  1.000 19.30697  ? 230 PHE A CD2  1 
ATOM   2839 C  CE1  . PHE A  1 230 ? -11.87400 -23.49200 7.76600   1.000 18.58504  ? 230 PHE A CE1  1 
ATOM   2840 C  CE2  . PHE A  1 230 ? -10.89700 -23.97000 9.91500   1.000 19.97255  ? 230 PHE A CE2  1 
ATOM   2841 C  CZ   . PHE A  1 230 ? -11.14300 -24.32900 8.57000   1.000 20.77850  ? 230 PHE A CZ   1 
ATOM   2842 H  H    . PHE A  1 230 ? -11.17500 -19.58600 8.35700   1.000 23.17694  ? 230 PHE A H    1 
ATOM   2843 H  HA   . PHE A  1 230 ? -13.73200 -19.98500 8.59500   1.000 23.84129  ? 230 PHE A HA   1 
ATOM   2844 H  HB2  . PHE A  1 230 ? -11.87700 -20.23000 10.68700  1.000 24.17572  ? 230 PHE A HB2  1 
ATOM   2845 H  HB3  . PHE A  1 230 ? -13.36400 -20.79000 10.72600  1.000 24.17572  ? 230 PHE A HB3  1 
ATOM   2846 H  HD1  . PHE A  1 230 ? -12.92100 -21.75300 7.75900   1.000 23.16071  ? 230 PHE A HD1  1 
ATOM   2847 H  HD2  . PHE A  1 230 ? -11.16300 -22.52400 11.27400  1.000 23.17092  ? 230 PHE A HD2  1 
ATOM   2848 H  HE1  . PHE A  1 230 ? -12.02700 -23.71400 6.87600   1.000 22.30461  ? 230 PHE A HE1  1 
ATOM   2849 H  HE2  . PHE A  1 230 ? -10.42300 -24.54500 10.47100  1.000 23.96962  ? 230 PHE A HE2  1 
ATOM   2850 H  HZ   . PHE A  1 230 ? -10.81000 -25.12900 8.23100   1.000 24.93676  ? 230 PHE A HZ   1 
ATOM   2851 N  N    . TYR A  1 231 ? -12.61500 -17.45900 10.25300  1.000 18.54850  ? 231 TYR A N    1 
ATOM   2852 C  CA   . TYR A  1 231 ? -13.03600 -16.21800 10.88700  1.000 19.10126  ? 231 TYR A CA   1 
ATOM   2853 C  C    . TYR A  1 231 ? -13.76700 -15.32800 9.89800   1.000 20.20534  ? 231 TYR A C    1 
ATOM   2854 O  O    . TYR A  1 231 ? -14.80000 -14.72500 10.22400  1.000 21.07049  ? 231 TYR A O    1 
ATOM   2855 C  CB   . TYR A  1 231 ? -11.81500 -15.47700 11.46500  1.000 20.34542  ? 231 TYR A CB   1 
ATOM   2856 C  CG   . TYR A  1 231 ? -12.19000 -14.11200 11.96500  1.000 20.39021  ? 231 TYR A CG   1 
ATOM   2857 C  CD1  . TYR A  1 231 ? -12.21200 -13.01100 11.12500  1.000 23.09420  ? 231 TYR A CD1  1 
ATOM   2858 C  CD2  . TYR A  1 231 ? -12.58400 -13.93900 13.31200  1.000 20.14301  ? 231 TYR A CD2  1 
ATOM   2859 C  CE1  . TYR A  1 231 ? -12.61300 -11.74900 11.56700  1.000 21.21181  ? 231 TYR A CE1  1 
ATOM   2860 C  CE2  . TYR A  1 231 ? -12.95200 -12.69100 13.75700  1.000 20.51069  ? 231 TYR A CE2  1 
ATOM   2861 C  CZ   . TYR A  1 231 ? -12.96200 -11.61300 12.92300  1.000 22.31330  ? 231 TYR A CZ   1 
ATOM   2862 O  OH   . TYR A  1 231 ? -13.36000 -10.36500 13.38600  1.000 24.51501  ? 231 TYR A OH   1 
ATOM   2863 H  H    . TYR A  1 231 ? -11.76500 -17.58400 10.23100  1.000 22.26076  ? 231 TYR A H    1 
ATOM   2864 H  HA   . TYR A  1 231 ? -13.63700 -16.42700 11.62000  1.000 22.92408  ? 231 TYR A HA   1 
ATOM   2865 H  HB2  . TYR A  1 231 ? -11.45200 -15.98600 12.20600  1.000 24.41706  ? 231 TYR A HB2  1 
ATOM   2866 H  HB3  . TYR A  1 231 ? -11.14400 -15.37500 10.77200  1.000 24.41706  ? 231 TYR A HB3  1 
ATOM   2867 H  HD1  . TYR A  1 231 ? -11.95100 -13.11600 10.23800  1.000 27.71560  ? 231 TYR A HD1  1 
ATOM   2868 H  HD2  . TYR A  1 231 ? -12.59400 -14.66500 13.89300  1.000 24.17417  ? 231 TYR A HD2  1 
ATOM   2869 H  HE1  . TYR A  1 231 ? -12.64900 -11.02400 10.98600  1.000 25.45674  ? 231 TYR A HE1  1 
ATOM   2870 H  HE2  . TYR A  1 231 ? -13.19900 -12.58000 14.64700  1.000 24.61539  ? 231 TYR A HE2  1 
ATOM   2871 H  HH   . TYR A  1 231 ? -13.29900 -9.79700  12.77000  1.000 29.42057  ? 231 TYR A HH   1 
ATOM   2872 N  N    . ASN A  1 232 ? -13.25900 -15.23000 8.67100   1.000 20.35006  ? 232 ASN A N    1 
ATOM   2873 C  CA   . ASN A  1 232 ? -13.89000 -14.35200 7.69700   1.000 20.47817  ? 232 ASN A CA   1 
ATOM   2874 C  C    . ASN A  1 232 ? -15.24600 -14.85400 7.22100   1.000 23.07490  ? 232 ASN A C    1 
ATOM   2875 O  O    . ASN A  1 232 ? -16.07500 -14.02700 6.79900   1.000 26.97085  ? 232 ASN A O    1 
ATOM   2876 C  CB   . ASN A  1 232 ? -12.97300 -14.17400 6.49900   1.000 22.76380  ? 232 ASN A CB   1 
ATOM   2877 C  CG   . ASN A  1 232 ? -11.72500 -13.38500 6.82500   1.000 23.97161  ? 232 ASN A CG   1 
ATOM   2878 O  OD1  . ASN A  1 232 ? -11.66400 -12.66200 7.81600   1.000 25.13914  ? 232 ASN A OD1  1 
ATOM   2879 N  ND2  . ASN A  1 232 ? -10.72400 -13.49200 5.95300   1.000 25.98938  ? 232 ASN A ND2  1 
ATOM   2880 H  H    . ASN A  1 232 ? -12.56600 -15.65300 8.38600   1.000 24.42263  ? 232 ASN A H    1 
ATOM   2881 H  HA   . ASN A  1 232 ? -14.03100 -13.49000 8.11900   1.000 24.57637  ? 232 ASN A HA   1 
ATOM   2882 H  HB2  . ASN A  1 232 ? -12.70000 -15.04800 6.17800   1.000 27.31913  ? 232 ASN A HB2  1 
ATOM   2883 H  HB3  . ASN A  1 232 ? -13.45300 -13.70000 5.80200   1.000 27.31913  ? 232 ASN A HB3  1 
ATOM   2884 H  HD21 . ASN A  1 232 ? -9.99000  -13.06500 6.08800   1.000 31.18981  ? 232 ASN A HD21 1 
ATOM   2885 H  HD22 . ASN A  1 232 ? -10.81200 -13.98700 5.25600   1.000 31.18981  ? 232 ASN A HD22 1 
ATOM   2886 N  N    . ALA A  1 233 ? -15.50800 -16.15400 7.32300   1.000 21.53116  ? 233 ALA A N    1 
ATOM   2887 C  CA   . ALA A  1 233 ? -16.79300 -16.68900 6.89900   1.000 22.11740  ? 233 ALA A CA   1 
ATOM   2888 C  C    . ALA A  1 233 ? -17.89700 -16.33300 7.87200   1.000 21.38819  ? 233 ALA A C    1 
ATOM   2889 O  O    . ALA A  1 233 ? -19.06100 -16.20300 7.48100   1.000 24.45558  ? 233 ALA A O    1 
ATOM   2890 C  CB   . ALA A  1 233 ? -16.69800 -18.21300 6.85400   1.000 21.94213  ? 233 ALA A CB   1 
ATOM   2891 H  H    . ALA A  1 233 ? -14.96200 -16.74200 7.63200   1.000 25.83996  ? 233 ALA A H    1 
ATOM   2892 H  HA   . ALA A  1 233 ? -17.00500 -16.32800 6.02400   1.000 26.54344  ? 233 ALA A HA   1 
ATOM   2893 H  HB1  . ALA A  1 233 ? -17.56200 -18.57600 6.60200   1.000 26.33312  ? 233 ALA A HB1  1 
ATOM   2894 H  HB2  . ALA A  1 233 ? -16.02900 -18.46900 6.20000   1.000 26.33312  ? 233 ALA A HB2  1 
ATOM   2895 H  HB3  . ALA A  1 233 ? -16.44500 -18.54000 7.73100   1.000 26.33312  ? 233 ALA A HB3  1 
ATOM   2896 N  N    . ILE A  1 234 ? -17.56500 -16.19200 9.13900   1.000 20.72590  ? 234 ILE A N    1 
ATOM   2897 C  CA   . ILE A  1 234 ? -18.59200 -15.92100 10.15200  1.000 21.26768  ? 234 ILE A CA   1 
ATOM   2898 C  C    . ILE A  1 234 ? -19.20200 -14.54800 9.91000   1.000 21.52905  ? 234 ILE A C    1 
ATOM   2899 O  O    . ILE A  1 234 ? -18.47300 -13.58800 9.62800   1.000 22.75776  ? 234 ILE A O    1 
ATOM   2900 C  CB   . ILE A  1 234 ? -17.96200 -16.03900 11.53900  1.000 20.72576  ? 234 ILE A CB   1 
ATOM   2901 C  CG1  . ILE A  1 234 ? -17.51000 -17.48300 11.73700  1.000 20.09592  ? 234 ILE A CG1  1 
ATOM   2902 C  CG2  . ILE A  1 234 ? -18.97600 -15.62700 12.63600  1.000 20.24790  ? 234 ILE A CG2  1 
ATOM   2903 C  CD1  . ILE A  1 234 ? -16.71400 -17.69400 13.03300  1.000 20.64710  ? 234 ILE A CD1  1 
ATOM   2904 H  H    . ILE A  1 234 ? -16.76400 -16.24600 9.44600   1.000 24.87365  ? 234 ILE A H    1 
ATOM   2905 H  HA   . ILE A  1 234 ? -19.31400 -16.56600 10.08200  1.000 25.52378  ? 234 ILE A HA   1 
ATOM   2906 H  HB   . ILE A  1 234 ? -17.20000 -15.44300 11.60700  1.000 24.87347  ? 234 ILE A HB   1 
ATOM   2907 H  HG12 . ILE A  1 234 ? -18.29300 -18.05500 11.77000  1.000 24.11767  ? 234 ILE A HG12 1 
ATOM   2908 H  HG13 . ILE A  1 234 ? -16.94300 -17.73900 10.99300  1.000 24.11767  ? 234 ILE A HG13 1 
ATOM   2909 H  HG21 . ILE A  1 234 ? -18.55600 -15.71700 13.50500  1.000 24.30004  ? 234 ILE A HG21 1 
ATOM   2910 H  HG22 . ILE A  1 234 ? -19.24100 -14.70500 12.49000  1.000 24.30004  ? 234 ILE A HG22 1 
ATOM   2911 H  HG23 . ILE A  1 234 ? -19.75200 -16.20600 12.58200  1.000 24.30004  ? 234 ILE A HG23 1 
ATOM   2912 H  HD11 . ILE A  1 234 ? -16.24400 -18.54100 12.98100  1.000 24.77909  ? 234 ILE A HD11 1 
ATOM   2913 H  HD12 . ILE A  1 234 ? -16.07800 -16.96800 13.13500  1.000 24.77909  ? 234 ILE A HD12 1 
ATOM   2914 H  HD13 . ILE A  1 234 ? -17.32900 -17.70300 13.78400  1.000 24.77909  ? 234 ILE A HD13 1 
ATOM   2915 N  N    . PRO A  1 235 ? -20.52000 -14.40200 10.02500  1.000 22.20981  ? 235 PRO A N    1 
ATOM   2916 C  CA   . PRO A  1 235 ? -21.13700 -13.09900 9.77700   1.000 23.55950  ? 235 PRO A CA   1 
ATOM   2917 C  C    . PRO A  1 235 ? -20.53300 -11.95800 10.57500  1.000 23.75974  ? 235 PRO A C    1 
ATOM   2918 O  O    . PRO A  1 235 ? -20.15100 -12.11200 11.73400  1.000 23.22579  ? 235 PRO A O    1 
ATOM   2919 C  CB   . PRO A  1 235 ? -22.60000 -13.32300 10.18600  1.000 26.70816  ? 235 PRO A CB   1 
ATOM   2920 C  CG   . PRO A  1 235 ? -22.84700 -14.76200 9.95500   1.000 24.16524  ? 235 PRO A CG   1 
ATOM   2921 C  CD   . PRO A  1 235 ? -21.52900 -15.47000 10.19000  1.000 22.38454  ? 235 PRO A CD   1 
ATOM   2922 H  HA   . PRO A  1 235 ? -21.05300 -12.89200 8.83400   1.000 28.27397  ? 235 PRO A HA   1 
ATOM   2923 H  HB2  . PRO A  1 235 ? -22.72000 -13.09700 11.12100  1.000 32.05236  ? 235 PRO A HB2  1 
ATOM   2924 H  HB3  . PRO A  1 235 ? -23.18300 -12.77800 9.63500   1.000 32.05236  ? 235 PRO A HB3  1 
ATOM   2925 H  HG2  . PRO A  1 235 ? -23.52100 -15.08000 10.57700  1.000 29.00085  ? 235 PRO A HG2  1 
ATOM   2926 H  HG3  . PRO A  1 235 ? -23.14900 -14.89700 9.04200   1.000 29.00085  ? 235 PRO A HG3  1 
ATOM   2927 H  HD2  . PRO A  1 235 ? -21.49400 -15.84100 11.08600  1.000 26.86401  ? 235 PRO A HD2  1 
ATOM   2928 H  HD3  . PRO A  1 235 ? -21.39500 -16.17300 9.53500   1.000 26.86401  ? 235 PRO A HD3  1 
ATOM   2929 N  N    . SER A  1 236 ? -20.50200 -10.77800 9.95000   1.000 26.47989  ? 236 SER A N    1 
ATOM   2930 C  CA   . SER A  1 236 ? -20.01300 -9.58700  10.63800  1.000 26.52138  ? 236 SER A CA   1 
ATOM   2931 C  C    . SER A  1 236 ? -20.92900 -9.13900  11.76800  1.000 25.61167  ? 236 SER A C    1 
ATOM   2932 O  O    . SER A  1 236 ? -20.49900 -8.36400  12.62600  1.000 26.89148  ? 236 SER A O    1 
ATOM   2933 C  CB   . SER A  1 236 ? -19.84500 -8.46400  9.61200   1.000 34.68032  ? 236 SER A CB   1 
ATOM   2934 O  OG   . SER A  1 236 ? -21.11100 -7.92200  9.29200   1.000 39.32039  ? 236 SER A OG   1 
ATOM   2935 H  H    . SER A  1 236 ? -20.75500 -10.64400 9.13900   1.000 31.77843  ? 236 SER A H    1 
ATOM   2936 H  HA   . SER A  1 236 ? -19.15000 -9.77700  11.03800  1.000 31.82822  ? 236 SER A HA   1 
ATOM   2937 H  HB2  . SER A  1 236 ? -19.28400 -7.76800  9.98800   1.000 41.61895  ? 236 SER A HB2  1 
ATOM   2938 H  HB3  . SER A  1 236 ? -19.43700 -8.82300  8.80800   1.000 41.61895  ? 236 SER A HB3  1 
ATOM   2939 H  HG   . SER A  1 236 ? -21.01800 -7.25000  8.79700   1.000 47.18703  ? 236 SER A HG   1 
ATOM   2940 N  N    . SER A  1 237 ? -22.16000 -9.64000  11.81400  1.000 24.42285  ? 237 SER A N    1 
ATOM   2941 C  CA   . SER A  1 237 ? -23.06900 -9.31500  12.90600  1.000 24.05472  ? 237 SER A CA   1 
ATOM   2942 C  C    . SER A  1 237 ? -22.87800 -10.20500 14.12400  1.000 24.86936  ? 237 SER A C    1 
ATOM   2943 O  O    . SER A  1 237 ? -23.52000 -9.96900  15.15400  1.000 25.20445  ? 237 SER A O    1 
ATOM   2944 C  CB   . SER A  1 237 ? -24.51600 -9.45600  12.43600  1.000 25.97376  ? 237 SER A CB   1 
ATOM   2945 O  OG   . SER A  1 237 ? -24.70000 -10.65500 11.70500  1.000 27.44103  ? 237 SER A OG   1 
ATOM   2946 H  H    . SER A  1 237 ? -22.49200 -10.17000 11.22400  1.000 29.30998  ? 237 SER A H    1 
ATOM   2947 H  HA   . SER A  1 237 ? -22.91000 -8.39500  13.16900  1.000 28.86823  ? 237 SER A HA   1 
ATOM   2948 H  HB2  . SER A  1 237 ? -25.09900 -9.46700  13.21100  1.000 31.17107  ? 237 SER A HB2  1 
ATOM   2949 H  HB3  . SER A  1 237 ? -24.73600 -8.70300  11.86600  1.000 31.17107  ? 237 SER A HB3  1 
ATOM   2950 H  HG   . SER A  1 237 ? -24.54600 -11.31800 12.19700  1.000 32.93180  ? 237 SER A HG   1 
ATOM   2951 N  N    . THR A  1 238 ? -22.03500 -11.22900 14.02600  1.000 21.95100  ? 238 THR A N    1 
ATOM   2952 C  CA   . THR A  1 238 ? -21.73400 -12.12100 15.13300  1.000 22.83207  ? 238 THR A CA   1 
ATOM   2953 C  C    . THR A  1 238 ? -20.56800 -11.56400 15.92100  1.000 20.36198  ? 238 THR A C    1 
ATOM   2954 O  O    . THR A  1 238 ? -19.67500 -10.95300 15.34600  1.000 21.48389  ? 238 THR A O    1 
ATOM   2955 C  CB   . THR A  1 238 ? -21.39700 -13.48600 14.53300  1.000 22.95950  ? 238 THR A CB   1 
ATOM   2956 O  OG1  . THR A  1 238 ? -22.56500 -14.02600 13.90500  1.000 24.47894  ? 238 THR A OG1  1 
ATOM   2957 C  CG2  . THR A  1 238 ? -20.87100 -14.44900 15.60300  1.000 20.71505  ? 238 THR A CG2  1 
ATOM   2958 H  H    . THR A  1 238 ? -21.61200 -11.43200 13.30500  1.000 26.34376  ? 238 THR A H    1 
ATOM   2959 H  HA   . THR A  1 238 ? -22.47600 -12.21500 15.75100  1.000 27.40104  ? 238 THR A HA   1 
ATOM   2960 H  HB   . THR A  1 238 ? -20.69400 -13.38700 13.87100  1.000 27.55396  ? 238 THR A HB   1 
ATOM   2961 H  HG1  . THR A  1 238 ? -22.40300 -14.79600 13.61100  1.000 29.37728  ? 238 THR A HG1  1 
ATOM   2962 H  HG21 . THR A  1 238 ? -20.87100 -15.35700 15.26200  1.000 24.86062  ? 238 THR A HG21 1 
ATOM   2963 H  HG22 . THR A  1 238 ? -19.96500 -14.20700 15.85100  1.000 24.86062  ? 238 THR A HG22 1 
ATOM   2964 H  HG23 . THR A  1 238 ? -21.43400 -14.40900 16.39100  1.000 24.86062  ? 238 THR A HG23 1 
ATOM   2965 N  N    . ASP A  1 239 ? -20.62500 -11.71100 17.24600  1.000 20.05482  ? 239 ASP A N    1 
ATOM   2966 C  CA   . ASP A  1 239 ? -19.49000 -11.35800 18.08800  1.000 21.85018  ? 239 ASP A CA   1 
ATOM   2967 C  C    . ASP A  1 239 ? -18.36300 -12.33200 17.77900  1.000 20.77186  ? 239 ASP A C    1 
ATOM   2968 O  O    . ASP A  1 239 ? -18.50200 -13.53600 18.01100  1.000 19.99630  ? 239 ASP A O    1 
ATOM   2969 C  CB   . ASP A  1 239 ? -19.84600 -11.52900 19.56300  1.000 20.67134  ? 239 ASP A CB   1 
ATOM   2970 C  CG   . ASP A  1 239 ? -20.82900 -10.49400 20.05500  1.000 31.39476  ? 239 ASP A CG   1 
ATOM   2971 O  OD1  . ASP A  1 239 ? -21.28700 -9.64400  19.27700  1.000 28.02997  ? 239 ASP A OD1  1 
ATOM   2972 O  OD2  . ASP A  1 239 ? -21.15100 -10.54600 21.25700  1.000 34.30423  ? 239 ASP A OD2  1 
ATOM   2973 H  H    . ASP A  1 239 ? -21.30700 -12.01100 17.67500  1.000 24.06834  ? 239 ASP A H    1 
ATOM   2974 H  HA   . ASP A  1 239 ? -19.23600 -10.43700 17.91900  1.000 26.22277  ? 239 ASP A HA   1 
ATOM   2975 H  HB2  . ASP A  1 239 ? -20.24200 -12.40400 19.69300  1.000 24.80817  ? 239 ASP A HB2  1 
ATOM   2976 H  HB3  . ASP A  1 239 ? -19.03700 -11.44900 20.09400  1.000 24.80817  ? 239 ASP A HB3  1 
ATOM   2977 N  N    . LYS A  1 240 ? -17.24800 -11.83500 17.26400  1.000 18.83007  ? 240 LYS A N    1 
ATOM   2978 C  CA   . LYS A  1 240 ? -16.14200 -12.70900 16.90100  1.000 18.71200  ? 240 LYS A CA   1 
ATOM   2979 C  C    . LYS A  1 240 ? -14.83700 -11.97000 17.09000  1.000 18.33888  ? 240 LYS A C    1 
ATOM   2980 O  O    . LYS A  1 240 ? -14.79000 -10.74000 17.06100  1.000 19.32650  ? 240 LYS A O    1 
ATOM   2981 C  CB   . LYS A  1 240 ? -16.26100 -13.24800 15.47000  1.000 18.45440  ? 240 LYS A CB   1 
ATOM   2982 C  CG   . LYS A  1 240 ? -16.36100 -12.18100 14.38600  1.000 19.85317  ? 240 LYS A CG   1 
ATOM   2983 C  CD   . LYS A  1 240 ? -16.39100 -12.82000 12.99100  1.000 19.86970  ? 240 LYS A CD   1 
ATOM   2984 C  CE   . LYS A  1 240 ? -16.37100 -11.76900 11.89200  1.000 20.70558  ? 240 LYS A CE   1 
ATOM   2985 N  NZ   . LYS A  1 240 ? -16.23200 -12.36400 10.50900  1.000 22.12809  ? 240 LYS A NZ   1 
ATOM   2986 H  H    . LYS A  1 240 ? -17.10800 -10.99900 17.11400  1.000 22.59865  ? 240 LYS A H    1 
ATOM   2987 H  HA   . LYS A  1 240 ? -16.14400 -13.47200 17.50000  1.000 22.45696  ? 240 LYS A HA   1 
ATOM   2988 H  HB2  . LYS A  1 240 ? -15.47700 -13.78600 15.27800  1.000 22.14784  ? 240 LYS A HB2  1 
ATOM   2989 H  HB3  . LYS A  1 240 ? -17.06100 -13.79500 15.41400  1.000 22.14784  ? 240 LYS A HB3  1 
ATOM   2990 H  HG2  . LYS A  1 240 ? -17.17700 -11.67100 14.50800  1.000 23.82637  ? 240 LYS A HG2  1 
ATOM   2991 H  HG3  . LYS A  1 240 ? -15.59100 -11.59300 14.43800  1.000 23.82637  ? 240 LYS A HG3  1 
ATOM   2992 H  HD2  . LYS A  1 240 ? -15.61300 -13.38900 12.88200  1.000 23.84620  ? 240 LYS A HD2  1 
ATOM   2993 H  HD3  . LYS A  1 240 ? -17.20200 -13.34400 12.89600  1.000 23.84620  ? 240 LYS A HD3  1 
ATOM   2994 H  HE2  . LYS A  1 240 ? -17.20100 -11.26800 11.92000  1.000 24.84925  ? 240 LYS A HE2  1 
ATOM   2995 H  HE3  . LYS A  1 240 ? -15.61900 -11.17400 12.03900  1.000 24.84925  ? 240 LYS A HE3  1 
ATOM   2996 H  HZ1  . LYS A  1 240 ? -16.30800 -11.72500 9.89400   1.000 26.55627  ? 240 LYS A HZ1  1 
ATOM   2997 H  HZ2  . LYS A  1 240 ? -15.43600 -12.75400 10.42400  1.000 26.55627  ? 240 LYS A HZ2  1 
ATOM   2998 H  HZ3  . LYS A  1 240 ? -16.86700 -12.97200 10.37400  1.000 26.55627  ? 240 LYS A HZ3  1 
ATOM   2999 N  N    . ALA A  1 241 ? -13.76900 -12.75000 17.28300  1.000 18.27249  ? 241 ALA A N    1 
ATOM   3000 C  CA   . ALA A  1 241 ? -12.43200 -12.19900 17.44300  1.000 18.00206  ? 241 ALA A CA   1 
ATOM   3001 C  C    . ALA A  1 241 ? -11.41800 -13.18500 16.88800  1.000 19.23104  ? 241 ALA A C    1 
ATOM   3002 O  O    . ALA A  1 241 ? -11.63600 -14.39900 16.89200  1.000 18.45457  ? 241 ALA A O    1 
ATOM   3003 C  CB   . ALA A  1 241 ? -12.14200 -11.88300 18.89900  1.000 20.13084  ? 241 ALA A CB   1 
ATOM   3004 H  H    . ALA A  1 241 ? -13.79800 -13.60900 17.32400  1.000 21.92955  ? 241 ALA A H    1 
ATOM   3005 H  HA   . ALA A  1 241 ? -12.34900 -11.37700 16.93500  1.000 21.60504  ? 241 ALA A HA   1 
ATOM   3006 H  HB1  . ALA A  1 241 ? -11.24000 -11.53200 18.97300  1.000 24.15957  ? 241 ALA A HB1  1 
ATOM   3007 H  HB2  . ALA A  1 241 ? -12.78000 -11.22300 19.21300  1.000 24.15957  ? 241 ALA A HB2  1 
ATOM   3008 H  HB3  . ALA A  1 241 ? -12.22300 -12.69600 19.42100  1.000 24.15957  ? 241 ALA A HB3  1 
ATOM   3009 N  N    . TYR A  1 242 ? -10.32200 -12.63700 16.39000  1.000 18.91290  ? 242 TYR A N    1 
ATOM   3010 C  CA   . TYR A  1 242 ? -9.22000  -13.37400 15.76200  1.000 18.07030  ? 242 TYR A CA   1 
ATOM   3011 C  C    . TYR A  1 242 ? -7.93800  -12.86700 16.39500  1.000 18.22121  ? 242 TYR A C    1 
ATOM   3012 O  O    . TYR A  1 242 ? -7.63800  -11.67300 16.30800  1.000 19.82041  ? 242 TYR A O    1 
ATOM   3013 C  CB   . TYR A  1 242 ? -9.23600  -13.10300 14.26200  1.000 19.89985  ? 242 TYR A CB   1 
ATOM   3014 C  CG   . TYR A  1 242 ? -8.20300  -13.81000 13.42900  1.000 18.60878  ? 242 TYR A CG   1 
ATOM   3015 C  CD1  . TYR A  1 242 ? -8.42100  -15.09100 12.97200  1.000 19.41898  ? 242 TYR A CD1  1 
ATOM   3016 C  CD2  . TYR A  1 242 ? -7.05100  -13.16100 13.02400  1.000 19.43725  ? 242 TYR A CD2  1 
ATOM   3017 C  CE1  . TYR A  1 242 ? -7.51800  -15.71800 12.16600  1.000 19.54061  ? 242 TYR A CE1  1 
ATOM   3018 C  CE2  . TYR A  1 242 ? -6.12200  -13.77400 12.21500  1.000 19.28981  ? 242 TYR A CE2  1 
ATOM   3019 C  CZ   . TYR A  1 242 ? -6.37500  -15.06900 11.77500  1.000 19.46186  ? 242 TYR A CZ   1 
ATOM   3020 O  OH   . TYR A  1 242 ? -5.46300  -15.69900 10.96400  1.000 25.43700  ? 242 TYR A OH   1 
ATOM   3021 H  H    . TYR A  1 242 ? -10.17900 -11.78900 16.40000  1.000 22.69805  ? 242 TYR A H    1 
ATOM   3022 H  HA   . TYR A  1 242 ? -9.28200  -14.33000 15.91000  1.000 21.68693  ? 242 TYR A HA   1 
ATOM   3023 H  HB2  . TYR A  1 242 ? -10.10400 -13.36800 13.91900  1.000 23.88239  ? 242 TYR A HB2  1 
ATOM   3024 H  HB3  . TYR A  1 242 ? -9.10200  -12.15200 14.12800  1.000 23.88239  ? 242 TYR A HB3  1 
ATOM   3025 H  HD1  . TYR A  1 242 ? -9.19900  -15.53700 13.21800  1.000 23.30534  ? 242 TYR A HD1  1 
ATOM   3026 H  HD2  . TYR A  1 242 ? -6.90100  -12.28700 13.30500  1.000 23.32727  ? 242 TYR A HD2  1 
ATOM   3027 H  HE1  . TYR A  1 242 ? -7.67700  -16.58900 11.88000  1.000 23.45130  ? 242 TYR A HE1  1 
ATOM   3028 H  HE2  . TYR A  1 242 ? -5.34200  -13.33200 11.96800  1.000 23.15034  ? 242 TYR A HE2  1 
ATOM   3029 H  HH   . TYR A  1 242 ? -4.78900  -15.20900 10.85500  1.000 30.52697  ? 242 TYR A HH   1 
ATOM   3030 N  N    . PHE A  1 243 ? -7.19300  -13.75000 17.04600  1.000 16.88461  ? 243 PHE A N    1 
ATOM   3031 C  CA   . PHE A  1 243 ? -5.88200  -13.42700 17.59700  1.000 18.59302  ? 243 PHE A CA   1 
ATOM   3032 C  C    . PHE A  1 243 ? -4.87200  -14.35300 16.93700  1.000 17.58708  ? 243 PHE A C    1 
ATOM   3033 O  O    . PHE A  1 243 ? -4.86700  -15.56100 17.20000  1.000 17.99037  ? 243 PHE A O    1 
ATOM   3034 C  CB   . PHE A  1 243 ? -5.88700  -13.65300 19.11500  1.000 19.13127  ? 243 PHE A CB   1 
ATOM   3035 C  CG   . PHE A  1 243 ? -6.65800  -12.61000 19.89000  1.000 17.86342  ? 243 PHE A CG   1 
ATOM   3036 C  CD1  . PHE A  1 243 ? -8.00300  -12.74400 20.13100  1.000 19.42651  ? 243 PHE A CD1  1 
ATOM   3037 C  CD2  . PHE A  1 243 ? -6.01100  -11.49400 20.38400  1.000 20.92968  ? 243 PHE A CD2  1 
ATOM   3038 C  CE1  . PHE A  1 243 ? -8.70900  -11.76700 20.82200  1.000 21.55383  ? 243 PHE A CE1  1 
ATOM   3039 C  CE2  . PHE A  1 243 ? -6.71500  -10.54300 21.10000  1.000 20.93047  ? 243 PHE A CE2  1 
ATOM   3040 C  CZ   . PHE A  1 243 ? -8.04400  -10.67900 21.30800  1.000 21.00838  ? 243 PHE A CZ   1 
ATOM   3041 H  H    . PHE A  1 243 ? -7.43000  -14.56500 17.18500  1.000 20.26409  ? 243 PHE A H    1 
ATOM   3042 H  HA   . PHE A  1 243 ? -5.64900  -12.50500 17.40600  1.000 22.31419  ? 243 PHE A HA   1 
ATOM   3043 H  HB2  . PHE A  1 243 ? -6.29100  -14.51500 19.30000  1.000 22.96009  ? 243 PHE A HB2  1 
ATOM   3044 H  HB3  . PHE A  1 243 ? -4.97200  -13.64000 19.43500  1.000 22.96009  ? 243 PHE A HB3  1 
ATOM   3045 H  HD1  . PHE A  1 243 ? -8.44800  -13.50200 19.82800  1.000 23.31437  ? 243 PHE A HD1  1 
ATOM   3046 H  HD2  . PHE A  1 243 ? -5.10000  -11.38200 20.23500  1.000 25.11818  ? 243 PHE A HD2  1 
ATOM   3047 H  HE1  . PHE A  1 243 ? -9.62600  -11.85300 20.95100  1.000 25.86716  ? 243 PHE A HE1  1 
ATOM   3048 H  HE2  . PHE A  1 243 ? -6.26900  -9.80100  21.44200  1.000 25.11912  ? 243 PHE A HE2  1 
ATOM   3049 H  HZ   . PHE A  1 243 ? -8.50700  -10.02800 21.78400  1.000 25.21261  ? 243 PHE A HZ   1 
ATOM   3050 N  N    . GLU A  1 244 ? -4.00700  -13.79000 16.11600  1.000 18.07245  ? 244 GLU A N    1 
ATOM   3051 C  CA   . GLU A  1 244 ? -2.94000  -14.54800 15.46500  1.000 18.71531  ? 244 GLU A CA   1 
ATOM   3052 C  C    . GLU A  1 244 ? -1.68300  -14.38100 16.30700  1.000 19.06744  ? 244 GLU A C    1 
ATOM   3053 O  O    . GLU A  1 244 ? -1.24600  -13.25200 16.55300  1.000 19.59909  ? 244 GLU A O    1 
ATOM   3054 C  CB   . GLU A  1 244 ? -2.66800  -14.07600 14.04300  1.000 20.15551  ? 244 GLU A CB   1 
ATOM   3055 C  CG   . GLU A  1 244 ? -1.68900  -14.98000 13.32200  1.000 20.48906  ? 244 GLU A CG   1 
ATOM   3056 C  CD   . GLU A  1 244 ? -1.30700  -14.46700 11.93600  1.000 28.25757  ? 244 GLU A CD   1 
ATOM   3057 O  OE1  . GLU A  1 244 ? -0.66700  -13.41200 11.88500  1.000 24.51875  ? 244 GLU A OE1  1 
ATOM   3058 O  OE2  . GLU A  1 244 ? -1.61700  -15.12800 10.93300  1.000 39.14189  ? 244 GLU A OE2  1 
ATOM   3059 H  H    . GLU A  1 244 ? -4.01200  -12.95500 15.91300  1.000 21.68951  ? 244 GLU A H    1 
ATOM   3060 H  HA   . GLU A  1 244 ? -3.20200  -15.48100 15.41500  1.000 22.46094  ? 244 GLU A HA   1 
ATOM   3061 H  HB2  . GLU A  1 244 ? -3.50000  -14.07200 13.54400  1.000 24.18918  ? 244 GLU A HB2  1 
ATOM   3062 H  HB3  . GLU A  1 244 ? -2.29300  -13.18200 14.07000  1.000 24.18918  ? 244 GLU A HB3  1 
ATOM   3063 H  HG2  . GLU A  1 244 ? -0.87700  -15.04800 13.84900  1.000 24.58944  ? 244 GLU A HG2  1 
ATOM   3064 H  HG3  . GLU A  1 244 ? -2.09000  -15.85600 13.21500  1.000 24.58944  ? 244 GLU A HG3  1 
ATOM   3065 N  N    . ILE A  1 245 ? -1.13000  -15.50100 16.75600  1.000 17.87319  ? 245 ILE A N    1 
ATOM   3066 C  CA   . ILE A  1 245 ? 0.05700   -15.52300 17.61000  1.000 17.52805  ? 245 ILE A CA   1 
ATOM   3067 C  C    . ILE A  1 245 ? 1.30800   -15.54500 16.73300  1.000 17.76516  ? 245 ILE A C    1 
ATOM   3068 O  O    . ILE A  1 245 ? 1.49400   -16.43900 15.89300  1.000 18.49559  ? 245 ILE A O    1 
ATOM   3069 C  CB   . ILE A  1 245 ? -0.00500  -16.71900 18.56300  1.000 17.35675  ? 245 ILE A CB   1 
ATOM   3070 C  CG1  . ILE A  1 245 ? -1.17700  -16.51800 19.51400  1.000 20.99015  ? 245 ILE A CG1  1 
ATOM   3071 C  CG2  . ILE A  1 245 ? 1.31200   -16.86700 19.29400  1.000 19.48071  ? 245 ILE A CG2  1 
ATOM   3072 C  CD1  . ILE A  1 245 ? -1.50100  -17.72000 20.38900  1.000 28.96644  ? 245 ILE A CD1  1 
ATOM   3073 H  H    . ILE A  1 245 ? -1.43100  -16.28600 16.57600  1.000 21.45039  ? 245 ILE A H    1 
ATOM   3074 H  HA   . ILE A  1 245 ? 0.10200   -14.71000 18.13700  1.000 21.03622  ? 245 ILE A HA   1 
ATOM   3075 H  HB   . ILE A  1 245 ? -0.14800  -17.54200 18.07100  1.000 20.83066  ? 245 ILE A HB   1 
ATOM   3076 H  HG12 . ILE A  1 245 ? -0.97200  -15.77500 20.10300  1.000 25.19074  ? 245 ILE A HG12 1 
ATOM   3077 H  HG13 . ILE A  1 245 ? -1.96800  -16.31700 18.99000  1.000 25.19074  ? 245 ILE A HG13 1 
ATOM   3078 H  HG21 . ILE A  1 245 ? 1.21600   -17.54200 19.98400  1.000 23.37941  ? 245 ILE A HG21 1 
ATOM   3079 H  HG22 . ILE A  1 245 ? 1.99600   -17.13500 18.66200  1.000 23.37941  ? 245 ILE A HG22 1 
ATOM   3080 H  HG23 . ILE A  1 245 ? 1.54800   -16.01500 19.69500  1.000 23.37941  ? 245 ILE A HG23 1 
ATOM   3081 H  HD11 . ILE A  1 245 ? -2.27900  -17.51600 20.93000  1.000 34.76229  ? 245 ILE A HD11 1 
ATOM   3082 H  HD12 . ILE A  1 245 ? -1.68500  -18.48400 19.82000  1.000 34.76229  ? 245 ILE A HD12 1 
ATOM   3083 H  HD13 . ILE A  1 245 ? -0.74000  -17.90900 20.96000  1.000 34.76229  ? 245 ILE A HD13 1 
ATOM   3084 N  N    . SER A  1 246 ? 2.10200   -14.47600 16.85800  1.000 19.81197  ? 246 SER A N    1 
ATOM   3085 C  CA   . SER A  1 246 ? 3.31100   -14.25500 16.08200  1.000 19.17199  ? 246 SER A CA   1 
ATOM   3086 C  C    . SER A  1 246 ? 4.25800   -15.43100 16.18300  1.000 19.11814  ? 246 SER A C    1 
ATOM   3087 O  O    . SER A  1 246 ? 4.52600   -15.93000 17.28200  1.000 20.69740  ? 246 SER A O    1 
ATOM   3088 C  CB   . SER A  1 246 ? 3.96200   -12.98900 16.61700  1.000 21.70392  ? 246 SER A CB   1 
ATOM   3089 O  OG   . SER A  1 246 ? 5.16400   -12.73400 15.92400  1.000 26.42419  ? 246 SER A OG   1 
ATOM   3090 H  H    . SER A  1 246 ? 1.95100   -13.83800 17.41500  1.000 23.77692  ? 246 SER A H    1 
ATOM   3091 H  HA   . SER A  1 246 ? 3.10200   -14.15000 15.14000  1.000 23.00895  ? 246 SER A HA   1 
ATOM   3092 H  HB2  . SER A  1 246 ? 3.35600   -12.24200 16.49300  1.000 26.04726  ? 246 SER A HB2  1 
ATOM   3093 H  HB3  . SER A  1 246 ? 4.15600   -13.10500 17.56100  1.000 26.04726  ? 246 SER A HB3  1 
ATOM   3094 H  HG   . SER A  1 246 ? 5.02300   -12.73500 15.09600  1.000 31.71159  ? 246 SER A HG   1 
ATOM   3095 N  N    . GLY A  1 247 ? 4.70900   -15.90200 15.02500  1.000 19.56434  ? 247 GLY A N    1 
ATOM   3096 C  CA   . GLY A  1 247 ? 5.64800   -17.03000 14.96200  1.000 18.41423  ? 247 GLY A CA   1 
ATOM   3097 C  C    . GLY A  1 247 ? 5.05400   -18.36400 15.34700  1.000 19.86116  ? 247 GLY A C    1 
ATOM   3098 O  O    . GLY A  1 247 ? 5.78400   -19.34500 15.46200  1.000 20.03860  ? 247 GLY A O    1 
ATOM   3099 H  H    . GLY A  1 247 ? 4.48800   -15.58900 14.25500  1.000 23.47977  ? 247 GLY A H    1 
ATOM   3100 H  HA2  . GLY A  1 247 ? 5.98500   -17.10500 14.05600  1.000 22.09964  ? 247 GLY A HA2  1 
ATOM   3101 H  HA3  . GLY A  1 247 ? 6.39100   -16.85100 15.56100  1.000 22.09964  ? 247 GLY A HA3  1 
ATOM   3102 N  N    . GLY A  1 248 ? 3.74900   -18.46300 15.53400  1.000 18.19587  ? 248 GLY A N    1 
ATOM   3103 C  CA   . GLY A  1 248 ? 3.20200   -19.59600 16.25500  1.000 18.59081  ? 248 GLY A CA   1 
ATOM   3104 C  C    . GLY A  1 248 ? 3.27600   -20.89100 15.47400  1.000 16.32488  ? 248 GLY A C    1 
ATOM   3105 O  O    . GLY A  1 248 ? 2.95700   -20.95500 14.29500  1.000 17.13074  ? 248 GLY A O    1 
ATOM   3106 H  H    . GLY A  1 248 ? 3.16500   -17.89600 15.25700  1.000 21.83760  ? 248 GLY A H    1 
ATOM   3107 H  HA2  . GLY A  1 248 ? 3.69400   -19.71400 17.08200  1.000 22.31153  ? 248 GLY A HA2  1 
ATOM   3108 H  HA3  . GLY A  1 248 ? 2.27100   -19.42100 16.46300  1.000 22.31153  ? 248 GLY A HA3  1 
ATOM   3109 N  N    . ASN A  1 249 ? 3.65900   -21.96000 16.17200  1.000 16.80645  ? 249 ASN A N    1 
ATOM   3110 C  CA   . ASN A  1 249 ? 3.57800   -23.30600 15.61200  1.000 15.54770  ? 249 ASN A CA   1 
ATOM   3111 C  C    . ASN A  1 249 ? 2.15300   -23.85000 15.82500  1.000 16.12750  ? 249 ASN A C    1 
ATOM   3112 O  O    . ASN A  1 249 ? 1.32900   -23.24800 16.50200  1.000 16.01593  ? 249 ASN A O    1 
ATOM   3113 C  CB   . ASN A  1 249 ? 4.68300   -24.21600 16.17900  1.000 16.92124  ? 249 ASN A CB   1 
ATOM   3114 C  CG   . ASN A  1 249 ? 4.45200   -24.63400 17.62500  1.000 16.49235  ? 249 ASN A CG   1 
ATOM   3115 O  OD1  . ASN A  1 249 ? 3.46900   -25.25600 17.93300  1.000 16.99639  ? 249 ASN A OD1  1 
ATOM   3116 N  ND2  . ASN A  1 249 ? 5.40500   -24.31300 18.50000  1.000 16.59853  ? 249 ASN A ND2  1 
ATOM   3117 H  H    . ASN A  1 249 ? 3.96900   -21.93100 16.97400  1.000 20.17030  ? 249 ASN A H    1 
ATOM   3118 H  HA   . ASN A  1 249 ? 3.74100   -23.29500 14.65600  1.000 18.65980  ? 249 ASN A HA   1 
ATOM   3119 H  HB2  . ASN A  1 249 ? 4.73000   -25.02300 15.64200  1.000 20.30805  ? 249 ASN A HB2  1 
ATOM   3120 H  HB3  . ASN A  1 249 ? 5.52900   -23.74200 16.14000  1.000 20.30805  ? 249 ASN A HB3  1 
ATOM   3121 H  HD21 . ASN A  1 249 ? 5.31800   -24.52800 19.32900  1.000 19.92080  ? 249 ASN A HD21 1 
ATOM   3122 H  HD22 . ASN A  1 249 ? 6.10600   -23.89000 18.23700  1.000 19.92080  ? 249 ASN A HD22 1 
ATOM   3123 N  N    . HIS A  1 250 ? 1.84500   -24.99900 15.23200  1.000 16.22776  ? 250 HIS A N    1 
ATOM   3124 C  CA   . HIS A  1 250 ? 0.48800   -25.54500 15.25900  1.000 15.32323  ? 250 HIS A CA   1 
ATOM   3125 C  C    . HIS A  1 250 ? -0.02900  -25.83900 16.66800  1.000 15.03729  ? 250 HIS A C    1 
ATOM   3126 O  O    . HIS A  1 250 ? -1.24500  -25.95200 16.85800  1.000 16.48136  ? 250 HIS A O    1 
ATOM   3127 C  CB   . HIS A  1 250 ? 0.44000   -26.83500 14.43700  1.000 16.48409  ? 250 HIS A CB   1 
ATOM   3128 C  CG   . HIS A  1 250 ? -0.89900  -27.49200 14.38100  1.000 17.91663  ? 250 HIS A CG   1 
ATOM   3129 N  ND1  . HIS A  1 250 ? -2.01800  -26.86200 13.89300  1.000 17.83381  ? 250 HIS A ND1  1 
ATOM   3130 C  CD2  . HIS A  1 250 ? -1.29200  -28.74800 14.70500  1.000 18.26736  ? 250 HIS A CD2  1 
ATOM   3131 C  CE1  . HIS A  1 250 ? -3.05000  -27.68800 13.95200  1.000 18.45560  ? 250 HIS A CE1  1 
ATOM   3132 N  NE2  . HIS A  1 250 ? -2.62500  -28.85000 14.41500  1.000 19.59699  ? 250 HIS A NE2  1 
ATOM   3133 H  H    . HIS A  1 250 ? 2.40700   -25.48900 14.80300  1.000 19.47587  ? 250 HIS A H    1 
ATOM   3134 H  HA   . HIS A  1 250 ? -0.10100  -24.88300 14.86500  1.000 18.39044  ? 250 HIS A HA   1 
ATOM   3135 H  HB2  . HIS A  1 250 ? 0.70100   -26.62900 13.52600  1.000 19.78348  ? 250 HIS A HB2  1 
ATOM   3136 H  HB3  . HIS A  1 250 ? 1.06100   -27.47100 14.82500  1.000 19.78348  ? 250 HIS A HB3  1 
ATOM   3137 H  HD1  . HIS A  1 250 ? -2.04400  -26.05500 13.59500  1.000 21.40314  ? 250 HIS A HD1  1 
ATOM   3138 H  HD2  . HIS A  1 250 ? -0.75300  -29.41800 15.06000  1.000 21.92339  ? 250 HIS A HD2  1 
ATOM   3139 H  HE1  . HIS A  1 250 ? -3.92500  -27.48500 13.70900  1.000 22.14928  ? 250 HIS A HE1  1 
ATOM   3140 N  N    . TYR A  1 251 ? 0.85700   -26.00600 17.63100  1.000 15.96788  ? 251 TYR A N    1 
ATOM   3141 C  CA   . TYR A  1 251 ? 0.50800   -26.30400 19.01700  1.000 15.39532  ? 251 TYR A CA   1 
ATOM   3142 C  C    . TYR A  1 251 ? 0.44200   -25.04400 19.84200  1.000 14.37768  ? 251 TYR A C    1 
ATOM   3143 O  O    . TYR A  1 251 ? 0.27200   -25.13900 21.05800  1.000 16.09027  ? 251 TYR A O    1 
ATOM   3144 C  CB   . TYR A  1 251 ? 1.60400   -27.25100 19.63400  1.000 16.51043  ? 251 TYR A CB   1 
ATOM   3145 C  CG   . TYR A  1 251 ? 1.76900   -28.54900 18.84500  1.000 16.83551  ? 251 TYR A CG   1 
ATOM   3146 C  CD1  . TYR A  1 251 ? 2.47400   -28.57400 17.66600  1.000 17.73258  ? 251 TYR A CD1  1 
ATOM   3147 C  CD2  . TYR A  1 251 ? 1.23400   -29.73900 19.31000  1.000 18.22064  ? 251 TYR A CD2  1 
ATOM   3148 C  CE1  . TYR A  1 251 ? 2.57200   -29.73000 16.91300  1.000 19.12201  ? 251 TYR A CE1  1 
ATOM   3149 C  CE2  . TYR A  1 251 ? 1.35500   -30.91100 18.56200  1.000 20.36180  ? 251 TYR A CE2  1 
ATOM   3150 C  CZ   . TYR A  1 251 ? 2.00300   -30.87700 17.37100  1.000 20.12359  ? 251 TYR A CZ   1 
ATOM   3151 O  OH   . TYR A  1 251 ? 2.11400   -32.01400 16.59600  1.000 24.05834  ? 251 TYR A OH   1 
ATOM   3152 H  H    . TYR A  1 251 ? 1.70600   -25.94900 17.50800  1.000 19.16402  ? 251 TYR A H    1 
ATOM   3153 H  HA   . TYR A  1 251 ? -0.35000  -26.75600 19.04900  1.000 18.47695  ? 251 TYR A HA   1 
ATOM   3154 H  HB2  . TYR A  1 251 ? 2.45700   -26.78800 19.63500  1.000 19.81508  ? 251 TYR A HB2  1 
ATOM   3155 H  HB3  . TYR A  1 251 ? 1.35000   -27.48000 20.54200  1.000 19.81508  ? 251 TYR A HB3  1 
ATOM   3156 H  HD1  . TYR A  1 251 ? 2.89300   -27.79900 17.36900  1.000 21.28166  ? 251 TYR A HD1  1 
ATOM   3157 H  HD2  . TYR A  1 251 ? 0.79000   -29.75800 20.12700  1.000 21.86732  ? 251 TYR A HD2  1 
ATOM   3158 H  HE1  . TYR A  1 251 ? 3.02400   -29.72200 16.10000  1.000 22.94898  ? 251 TYR A HE1  1 
ATOM   3159 H  HE2  . TYR A  1 251 ? 0.99500   -31.70800 18.87700  1.000 24.43673  ? 251 TYR A HE2  1 
ATOM   3160 H  HH   . TYR A  1 251 ? 1.76500   -32.66700 16.99300  1.000 28.87258  ? 251 TYR A HH   1 
ATOM   3161 N  N    . CYS A  1 252 ? 0.55300   -23.86200 19.23200  1.000 15.15374  ? 252 CYS A N    1 
ATOM   3162 C  CA   . CYS A  1 252 ? 0.78300   -22.65200 20.01800  1.000 15.46794  ? 252 CYS A CA   1 
ATOM   3163 C  C    . CYS A  1 252 ? -0.38500  -22.29600 20.93300  1.000 15.51840  ? 252 CYS A C    1 
ATOM   3164 O  O    . CYS A  1 252 ? -0.16000  -21.66400 21.98200  1.000 16.94470  ? 252 CYS A O    1 
ATOM   3165 C  CB   . CYS A  1 252 ? 1.11000   -21.44600 19.10800  1.000 17.31860  ? 252 CYS A CB   1 
ATOM   3166 S  SG   . CYS A  1 252 ? -0.24800  -20.45200 18.38600  1.000 18.71700  ? 252 CYS A SG   1 
ATOM   3167 H  H    . CYS A  1 252 ? 0.50000   -23.73700 18.38300  1.000 18.18705  ? 252 CYS A H    1 
ATOM   3168 H  HA   . CYS A  1 252 ? 1.55500   -22.83200 20.57800  1.000 18.56409  ? 252 CYS A HA   1 
ATOM   3169 H  HB2  . CYS A  1 252 ? 1.64700   -20.82900 19.62900  1.000 20.78488  ? 252 CYS A HB2  1 
ATOM   3170 H  HB3  . CYS A  1 252 ? 1.62500   -21.78200 18.35800  1.000 20.78488  ? 252 CYS A HB3  1 
ATOM   3171 N  N    . ALA A  1 253 ? -1.61800  -22.62400 20.55100  1.000 14.25810  ? 253 ALA A N    1 
ATOM   3172 C  CA   . ALA A  1 253 ? -2.79600  -22.25600 21.33100  1.000 14.07917  ? 253 ALA A CA   1 
ATOM   3173 C  C    . ALA A  1 253 ? -3.21900  -23.33800 22.30500  1.000 15.01844  ? 253 ALA A C    1 
ATOM   3174 O  O    . ALA A  1 253 ? -4.25900  -23.20200 22.96200  1.000 15.79328  ? 253 ALA A O    1 
ATOM   3175 C  CB   . ALA A  1 253 ? -3.92400  -21.83600 20.39900  1.000 15.80046  ? 253 ALA A CB   1 
ATOM   3176 H  H    . ALA A  1 253 ? -1.79900  -23.06400 19.83400  1.000 17.11228  ? 253 ALA A H    1 
ATOM   3177 H  HA   . ALA A  1 253 ? -2.59500  -21.47900 21.87500  1.000 16.89756  ? 253 ALA A HA   1 
ATOM   3178 H  HB1  . ALA A  1 253 ? -4.71900  -21.65800 20.92600  1.000 18.96312  ? 253 ALA A HB1  1 
ATOM   3179 H  HB2  . ALA A  1 253 ? -3.65800  -21.03500 19.92100  1.000 18.96312  ? 253 ALA A HB2  1 
ATOM   3180 H  HB3  . ALA A  1 253 ? -4.09900  -22.55400 19.77000  1.000 18.96312  ? 253 ALA A HB3  1 
ATOM   3181 N  N    . ASN A  1 254 ? -2.41700  -24.37500 22.47000  1.000 14.80194  ? 254 ASN A N    1 
ATOM   3182 C  CA   . ASN A  1 254 ? -2.78200  -25.45800 23.37000  1.000 14.64973  ? 254 ASN A CA   1 
ATOM   3183 C  C    . ASN A  1 254 ? -2.43900  -25.12000 24.82200  1.000 15.76706  ? 254 ASN A C    1 
ATOM   3184 O  O    . ASN A  1 254 ? -2.92300  -25.79700 25.73600  1.000 17.58631  ? 254 ASN A O    1 
ATOM   3185 C  CB   . ASN A  1 254 ? -2.07800  -26.75200 22.98600  1.000 15.19743  ? 254 ASN A CB   1 
ATOM   3186 C  CG   . ASN A  1 254 ? -2.44300  -27.24600 21.63100  1.000 17.61054  ? 254 ASN A CG   1 
ATOM   3187 O  OD1  . ASN A  1 254 ? -3.30200  -26.66600 20.97000  1.000 20.94463  ? 254 ASN A OD1  1 
ATOM   3188 N  ND2  . ASN A  1 254 ? -1.88600  -28.37900 21.29000  1.000 20.65663  ? 254 ASN A ND2  1 
ATOM   3189 H  H    . ASN A  1 254 ? -1.66000  -24.47700 22.07600  1.000 17.76490  ? 254 ASN A H    1 
ATOM   3190 H  HA   . ASN A  1 254 ? -3.73500  -25.61600 23.29100  1.000 17.58224  ? 254 ASN A HA   1 
ATOM   3191 H  HB2  . ASN A  1 254 ? -1.12000  -26.60400 22.99900  1.000 18.23948  ? 254 ASN A HB2  1 
ATOM   3192 H  HB3  . ASN A  1 254 ? -2.31700  -27.44100 23.62600  1.000 18.23948  ? 254 ASN A HB3  1 
ATOM   3193 H  HD21 . ASN A  1 254 ? -2.05200  -28.72400 20.52000  1.000 24.79052  ? 254 ASN A HD21 1 
ATOM   3194 H  HD22 . ASN A  1 254 ? -1.35400  -28.77800 21.83500  1.000 24.79052  ? 254 ASN A HD22 1 
ATOM   3195 N  N    . GLY A  1 255 ? -1.63700  -24.11200 25.04100  1.000 15.02829  ? 255 GLY A N    1 
ATOM   3196 C  CA   . GLY A  1 255 ? -1.24600  -23.72500 26.36200  1.000 15.70473  ? 255 GLY A CA   1 
ATOM   3197 C  C    . GLY A  1 255 ? -0.20200  -24.65100 26.96100  1.000 17.60496  ? 255 GLY A C    1 
ATOM   3198 O  O    . GLY A  1 255 ? 0.41000   -25.48300 26.28100  1.000 18.36989  ? 255 GLY A O    1 
ATOM   3199 H  H    . GLY A  1 255 ? -1.29700  -23.62200 24.42200  1.000 18.03651  ? 255 GLY A H    1 
ATOM   3200 H  HA2  . GLY A  1 255 ? -0.87700  -22.82800 26.33600  1.000 18.84823  ? 255 GLY A HA2  1 
ATOM   3201 H  HA3  . GLY A  1 255 ? -2.02500  -23.73000 26.94100  1.000 18.84823  ? 255 GLY A HA3  1 
ATOM   3202 N  N    . SER A  1 256 ? 0.00000   -24.50800 28.27000  1.000 17.41081  ? 256 SER A N    1 
ATOM   3203 C  CA   . SER A  1 256 ? 1.17500   -25.08600 28.95200  1.000 17.61228  ? 256 SER A CA   1 
ATOM   3204 C  C    . SER A  1 256 ? 2.43600   -24.69900 28.20000  1.000 19.44614  ? 256 SER A C    1 
ATOM   3205 O  O    . SER A  1 256 ? 3.34600   -25.52100 27.98600  1.000 22.43459  ? 256 SER A O    1 
ATOM   3206 C  CB   . SER A  1 256 ? 1.07100   -26.60700 29.06800  1.000 22.36064  ? 256 SER A CB   1 
ATOM   3207 O  OG   . SER A  1 256 ? -0.14300  -26.98600 29.72100  1.000 28.55582  ? 256 SER A OG   1 
ATOM   3208 H  H    . SER A  1 256 ? -0.52800  -24.07900 28.79500  1.000 20.89554  ? 256 SER A H    1 
ATOM   3209 H  HA   . SER A  1 256 ? 1.21700   -24.73200 29.85400  1.000 21.13730  ? 256 SER A HA   1 
ATOM   3210 H  HB2  . SER A  1 256 ? 1.08400   -26.99300 28.17800  1.000 26.83533  ? 256 SER A HB2  1 
ATOM   3211 H  HB3  . SER A  1 256 ? 1.82300   -26.93600 29.58400  1.000 26.83533  ? 256 SER A HB3  1 
ATOM   3212 H  HG   . SER A  1 256 ? -0.73800  -27.14600 29.15000  1.000 34.26955  ? 256 SER A HG   1 
ATOM   3213 N  N    . ASN A  1 257 ? 2.50800   -23.42700 27.81100  1.000 17.69513  ? 257 ASN A N    1 
ATOM   3214 C  CA   . ASN A  1 257 ? 3.62400   -22.94400 27.00700  1.000 16.21497  ? 257 ASN A CA   1 
ATOM   3215 C  C    . ASN A  1 257 ? 3.84400   -21.46600 27.24700  1.000 17.86594  ? 257 ASN A C    1 
ATOM   3216 O  O    . ASN A  1 257 ? 3.24100   -20.85800 28.13900  1.000 18.31551  ? 257 ASN A O    1 
ATOM   3217 C  CB   . ASN A  1 257 ? 3.36400   -23.26300 25.52700  1.000 15.89275  ? 257 ASN A CB   1 
ATOM   3218 C  CG   . ASN A  1 257 ? 2.18100   -22.53500 24.94100  1.000 15.56319  ? 257 ASN A CG   1 
ATOM   3219 O  OD1  . ASN A  1 257 ? 1.74400   -21.50200 25.45000  1.000 16.81189  ? 257 ASN A OD1  1 
ATOM   3220 N  ND2  . ASN A  1 257 ? 1.66200   -23.05900 23.81200  1.000 16.26662  ? 257 ASN A ND2  1 
ATOM   3221 H  H    . ASN A  1 257 ? 1.92300   -22.82700 28.00100  1.000 21.23671  ? 257 ASN A H    1 
ATOM   3222 H  HA   . ASN A  1 257 ? 4.43000   -23.39500 27.30500  1.000 19.46053  ? 257 ASN A HA   1 
ATOM   3223 H  HB2  . ASN A  1 257 ? 4.14800   -23.01500 25.01300  1.000 19.07386  ? 257 ASN A HB2  1 
ATOM   3224 H  HB3  . ASN A  1 257 ? 3.19800   -24.21500 25.43900  1.000 19.07386  ? 257 ASN A HB3  1 
ATOM   3225 H  HD21 . ASN A  1 257 ? 0.98600   -22.68300 23.43500  1.000 19.52250  ? 257 ASN A HD21 1 
ATOM   3226 H  HD22 . ASN A  1 257 ? 2.00700   -23.76800 23.46900  1.000 19.52250  ? 257 ASN A HD22 1 
ATOM   3227 N  N    . ARG A  1 258 ? 4.72000   -20.87800 26.43400  1.000 17.18144  ? 258 ARG A N    1 
ATOM   3228 C  CA   . ARG A  1 258 ? 5.10700   -19.47700 26.58600  1.000 18.32479  ? 258 ARG A CA   1 
ATOM   3229 C  C    . ARG A  1 258 ? 3.97200   -18.49500 26.40400  1.000 17.40206  ? 258 ARG A C    1 
ATOM   3230 O  O    . ARG A  1 258 ? 4.13800   -17.30700 26.73400  1.000 20.25635  ? 258 ARG A O    1 
ATOM   3231 C  CB   . ARG A  1 258 ? 6.22300   -19.15100 25.57900  1.000 18.00204  ? 258 ARG A CB   1 
ATOM   3232 C  CG   . ARG A  1 258 ? 5.85000   -19.38100 24.12200  1.000 18.53548  ? 258 ARG A CG   1 
ATOM   3233 C  CD   . ARG A  1 258 ? 6.97200   -18.99700 23.16400  1.000 19.28863  ? 258 ARG A CD   1 
ATOM   3234 N  NE   . ARG A  1 258 ? 7.06600   -17.54300 23.10600  1.000 21.69070  ? 258 ARG A NE   1 
ATOM   3235 C  CZ   . ARG A  1 258 ? 7.87100   -16.85900 22.31500  1.000 24.41696  ? 258 ARG A CZ   1 
ATOM   3236 N  NH1  . ARG A  1 258 ? 8.73100   -17.45900 21.50800  1.000 25.67117  ? 258 ARG A NH1  1 
ATOM   3237 N  NH2  . ARG A  1 258 ? 7.80200   -15.53400 22.32200  1.000 28.48379  ? 258 ARG A NH2  1 
ATOM   3238 H  H    . ARG A  1 258 ? 5.11100   -21.27300 25.77700  1.000 20.62029  ? 258 ARG A H    1 
ATOM   3239 H  HA   . ARG A  1 258 ? 5.43700   -19.35700 27.49000  1.000 21.99231  ? 258 ARG A HA   1 
ATOM   3240 H  HB2  . ARG A  1 258 ? 6.46200   -18.21600 25.67600  1.000 21.60500  ? 258 ARG A HB2  1 
ATOM   3241 H  HB3  . ARG A  1 258 ? 6.99000   -19.71100 25.77600  1.000 21.60500  ? 258 ARG A HB3  1 
ATOM   3242 H  HG2  . ARG A  1 258 ? 5.65100   -20.32100 23.99000  1.000 22.24514  ? 258 ARG A HG2  1 
ATOM   3243 H  HG3  . ARG A  1 258 ? 5.07300   -18.84200 23.90500  1.000 22.24514  ? 258 ARG A HG3  1 
ATOM   3244 H  HD2  . ARG A  1 258 ? 7.81600   -19.35600 23.48100  1.000 23.14892  ? 258 ARG A HD2  1 
ATOM   3245 H  HD3  . ARG A  1 258 ? 6.78000   -19.33800 22.27600  1.000 23.14892  ? 258 ARG A HD3  1 
ATOM   3246 H  HE   . ARG A  1 258 ? 6.55400   -17.09300 23.63100  1.000 26.03140  ? 258 ARG A HE   1 
ATOM   3247 H  HH11 . ARG A  1 258 ? 8.77600   -18.31800 21.49000  1.000 30.80796  ? 258 ARG A HH11 1 
ATOM   3248 H  HH12 . ARG A  1 258 ? 9.24500   -16.99100 21.00200  1.000 30.80796  ? 258 ARG A HH12 1 
ATOM   3249 H  HH21 . ARG A  1 258 ? 7.24000   -15.13500 22.83600  1.000 34.18311  ? 258 ARG A HH21 1 
ATOM   3250 H  HH22 . ARG A  1 258 ? 8.32000   -15.07400 21.81200  1.000 34.18311  ? 258 ARG A HH22 1 
ATOM   3251 N  N    . TYR A  1 259 ? 2.83800   -18.93000 25.86100  1.000 16.12866  ? 259 TYR A N    1 
ATOM   3252 C  CA   . TYR A  1 259 ? 1.71500   -18.04400 25.57500  1.000 16.46189  ? 259 TYR A CA   1 
ATOM   3253 C  C    . TYR A  1 259 ? 0.60700   -18.13900 26.61300  1.000 16.07824  ? 259 TYR A C    1 
ATOM   3254 O  O    . TYR A  1 259 ? -0.45800  -17.55300 26.41000  1.000 16.95981  ? 259 TYR A O    1 
ATOM   3255 C  CB   . TYR A  1 259 ? 1.13500   -18.32400 24.18100  1.000 16.97814  ? 259 TYR A CB   1 
ATOM   3256 C  CG   . TYR A  1 259 ? 2.18600   -18.38700 23.08000  1.000 16.26997  ? 259 TYR A CG   1 
ATOM   3257 C  CD1  . TYR A  1 259 ? 2.85900   -17.24700 22.68400  1.000 17.94215  ? 259 TYR A CD1  1 
ATOM   3258 C  CD2  . TYR A  1 259 ? 2.50200   -19.60800 22.48700  1.000 16.25988  ? 259 TYR A CD2  1 
ATOM   3259 C  CE1  . TYR A  1 259 ? 3.86700   -17.32400 21.70700  1.000 18.45656  ? 259 TYR A CE1  1 
ATOM   3260 C  CE2  . TYR A  1 259 ? 3.49200   -19.69600 21.51800  1.000 17.38551  ? 259 TYR A CE2  1 
ATOM   3261 C  CZ   . TYR A  1 259 ? 4.12600   -18.55800 21.11900  1.000 16.14492  ? 259 TYR A CZ   1 
ATOM   3262 O  OH   . TYR A  1 259 ? 5.11900   -18.67700 20.15700  1.000 17.43705  ? 259 TYR A OH   1 
ATOM   3263 H  H    . TYR A  1 259 ? 2.69300   -19.74900 25.64400  1.000 19.35696  ? 259 TYR A H    1 
ATOM   3264 H  HA   . TYR A  1 259 ? 2.05400   -17.13500 25.57800  1.000 19.75683  ? 259 TYR A HA   1 
ATOM   3265 H  HB2  . TYR A  1 259 ? 0.67400   -19.17700 24.20100  1.000 20.37634  ? 259 TYR A HB2  1 
ATOM   3266 H  HB3  . TYR A  1 259 ? 0.51100   -17.61600 23.95500  1.000 20.37634  ? 259 TYR A HB3  1 
ATOM   3267 H  HD1  . TYR A  1 259 ? 2.64500   -16.42600 23.06500  1.000 21.53314  ? 259 TYR A HD1  1 
ATOM   3268 H  HD2  . TYR A  1 259 ? 2.04400   -20.37500 22.74500  1.000 19.51442  ? 259 TYR A HD2  1 
ATOM   3269 H  HE1  . TYR A  1 259 ? 4.35000   -16.56800 21.46000  1.000 22.15043  ? 259 TYR A HE1  1 
ATOM   3270 H  HE2  . TYR A  1 259 ? 3.71900   -20.51800 21.14700  1.000 20.86518  ? 259 TYR A HE2  1 
ATOM   3271 H  HH   . TYR A  1 259 ? 5.46600   -17.92600 20.00900  1.000 20.92703  ? 259 TYR A HH   1 
ATOM   3272 N  N    . ASP A  1 260 ? 0.84300   -18.84400 27.72700  1.000 16.12758  ? 260 ASP A N    1 
ATOM   3273 C  CA   . ASP A  1 260 ? -0.21300  -19.04000 28.71900  1.000 15.78328  ? 260 ASP A CA   1 
ATOM   3274 C  C    . ASP A  1 260 ? -0.88400  -17.75100 29.16100  1.000 16.05751  ? 260 ASP A C    1 
ATOM   3275 O  O    . ASP A  1 260 ? -2.11500  -17.72700 29.34500  1.000 15.77338  ? 260 ASP A O    1 
ATOM   3276 C  CB   . ASP A  1 260 ? 0.33700   -19.75700 29.93400  1.000 16.65237  ? 260 ASP A CB   1 
ATOM   3277 C  CG   . ASP A  1 260 ? 0.55700   -21.23000 29.71300  1.000 18.17899  ? 260 ASP A CG   1 
ATOM   3278 O  OD1  . ASP A  1 260 ? 0.26500   -21.74800 28.63300  1.000 20.63923  ? 260 ASP A OD1  1 
ATOM   3279 O  OD2  . ASP A  1 260 ? 1.04200   -21.86500 30.67600  1.000 26.21567  ? 260 ASP A OD2  1 
ATOM   3280 H  H    . ASP A  1 260 ? 1.59400   -19.21300 27.92600  1.000 19.35566  ? 260 ASP A H    1 
ATOM   3281 H  HA   . ASP A  1 260 ? -0.89200  -19.58700 28.29400  1.000 18.94250  ? 260 ASP A HA   1 
ATOM   3282 H  HB2  . ASP A  1 260 ? 1.19000   -19.36200 30.17100  1.000 19.98541  ? 260 ASP A HB2  1 
ATOM   3283 H  HB3  . ASP A  1 260 ? -0.29000  -19.65800 30.66700  1.000 19.98541  ? 260 ASP A HB3  1 
ATOM   3284 N  N    . ALA A  1 261 ? -0.12000  -16.67700 29.41700  1.000 16.13570  ? 261 ALA A N    1 
ATOM   3285 C  CA   . ALA A  1 261 ? -0.73600  -15.43400 29.90300  1.000 15.82772  ? 261 ALA A CA   1 
ATOM   3286 C  C    . ALA A  1 261 ? -1.72700  -14.87500 28.89100  1.000 16.86079  ? 261 ALA A C    1 
ATOM   3287 O  O    . ALA A  1 261 ? -2.85000  -14.50000 29.24200  1.000 16.90740  ? 261 ALA A O    1 
ATOM   3288 C  CB   . ALA A  1 261 ? 0.33100   -14.41500 30.28500  1.000 18.61760  ? 261 ALA A CB   1 
ATOM   3289 H  H    . ALA A  1 261 ? 0.73300   -16.64300 29.31900  1.000 19.36540  ? 261 ALA A H    1 
ATOM   3290 H  HA   . ALA A  1 261 ? -1.23300  -15.63000 30.71200  1.000 18.99583  ? 261 ALA A HA   1 
ATOM   3291 H  HB1  . ALA A  1 261 ? -0.10300  -13.59200 30.55900  1.000 22.34369  ? 261 ALA A HB1  1 
ATOM   3292 H  HB2  . ALA A  1 261 ? 0.85900   -14.77100 31.01700  1.000 22.34369  ? 261 ALA A HB2  1 
ATOM   3293 H  HB3  . ALA A  1 261 ? 0.89900   -14.25000 29.51700  1.000 22.34369  ? 261 ALA A HB3  1 
ATOM   3294 N  N    . LEU A  1 262 ? -1.33300  -14.83900 27.62100  1.000 16.57861  ? 262 LEU A N    1 
ATOM   3295 C  CA   . LEU A  1 262 ? -2.19500  -14.32300 26.57000  1.000 18.13077  ? 262 LEU A CA   1 
ATOM   3296 C  C    . LEU A  1 262 ? -3.38400  -15.23900 26.32000  1.000 15.15380  ? 262 LEU A C    1 
ATOM   3297 O  O    . LEU A  1 262 ? -4.52700  -14.78500 26.20300  1.000 15.88248  ? 262 LEU A O    1 
ATOM   3298 C  CB   . LEU A  1 262 ? -1.33000  -14.15700 25.30800  1.000 23.73221  ? 262 LEU A CB   1 
ATOM   3299 C  CG   . LEU A  1 262 ? -1.87800  -13.84400 23.94600  1.000 27.39608  ? 262 LEU A CG   1 
ATOM   3300 C  CD1  . LEU A  1 262 ? -0.63100  -13.39100 23.15300  1.000 29.64725  ? 262 LEU A CD1  1 
ATOM   3301 C  CD2  . LEU A  1 262 ? -2.51000  -15.03300 23.28400  1.000 19.92869  ? 262 LEU A CD2  1 
ATOM   3302 H  H    . LEU A  1 262 ? -0.56600  -15.11000 27.34200  1.000 19.89689  ? 262 LEU A H    1 
ATOM   3303 H  HA   . LEU A  1 262 ? -2.56500  -13.46300 26.82400  1.000 21.75949  ? 262 LEU A HA   1 
ATOM   3304 H  HB2  . LEU A  1 262 ? -0.70800  -13.43700 25.50000  1.000 28.48121  ? 262 LEU A HB2  1 
ATOM   3305 H  HB3  . LEU A  1 262 ? -0.84800  -14.99100 25.19900  1.000 28.48121  ? 262 LEU A HB3  1 
ATOM   3306 H  HG   . LEU A  1 262 ? -2.58400  -13.17900 23.98100  1.000 32.87786  ? 262 LEU A HG   1 
ATOM   3307 H  HD11 . LEU A  1 262 ? -0.79700  -13.51500 22.20500  1.000 35.57926  ? 262 LEU A HD11 1 
ATOM   3308 H  HD12 . LEU A  1 262 ? -0.46100  -12.45500 23.33900  1.000 35.57926  ? 262 LEU A HD12 1 
ATOM   3309 H  HD13 . LEU A  1 262 ? 0.13000   -13.92700 23.42800  1.000 35.57926  ? 262 LEU A HD13 1 
ATOM   3310 H  HD21 . LEU A  1 262 ? -2.62300  -14.84500 22.33900  1.000 23.91699  ? 262 LEU A HD21 1 
ATOM   3311 H  HD22 . LEU A  1 262 ? -1.93300  -15.80400 23.40100  1.000 23.91699  ? 262 LEU A HD22 1 
ATOM   3312 H  HD23 . LEU A  1 262 ? -3.37300  -15.20000 23.69300  1.000 23.91699  ? 262 LEU A HD23 1 
ATOM   3313 N  N    . LEU A  1 263 ? -3.13600  -16.54600 26.22600  1.000 15.48635  ? 263 LEU A N    1 
ATOM   3314 C  CA   . LEU A  1 263 ? -4.20000  -17.48600 25.90600  1.000 14.65415  ? 263 LEU A CA   1 
ATOM   3315 C  C    . LEU A  1 263 ? -5.26700  -17.47100 26.97400  1.000 13.97035  ? 263 LEU A C    1 
ATOM   3316 O  O    . LEU A  1 263 ? -6.47200  -17.39200 26.69700  1.000 14.17404  ? 263 LEU A O    1 
ATOM   3317 C  CB   . LEU A  1 263 ? -3.66700  -18.90400 25.75500  1.000 14.17435  ? 263 LEU A CB   1 
ATOM   3318 C  CG   . LEU A  1 263 ? -2.76200  -19.20000 24.56100  1.000 15.20985  ? 263 LEU A CG   1 
ATOM   3319 C  CD1  . LEU A  1 263 ? -2.07600  -20.53600 24.76100  1.000 16.41363  ? 263 LEU A CD1  1 
ATOM   3320 C  CD2  . LEU A  1 263 ? -3.55500  -19.18200 23.25700  1.000 17.09196  ? 263 LEU A CD2  1 
ATOM   3321 H  H    . LEU A  1 263 ? -2.36500  -16.90900 26.34200  1.000 18.58618  ? 263 LEU A H    1 
ATOM   3322 H  HA   . LEU A  1 263 ? -4.58100  -17.21600 25.05600  1.000 17.58754  ? 263 LEU A HA   1 
ATOM   3323 H  HB2  . LEU A  1 263 ? -3.15500  -19.11400 26.55200  1.000 17.01178  ? 263 LEU A HB2  1 
ATOM   3324 H  HB3  . LEU A  1 263 ? -4.42900  -19.50000 25.68300  1.000 17.01178  ? 263 LEU A HB3  1 
ATOM   3325 H  HG   . LEU A  1 263 ? -2.08300  -18.51100 24.49200  1.000 18.25438  ? 263 LEU A HG   1 
ATOM   3326 H  HD11 . LEU A  1 263 ? -1.46300  -20.68900 24.02500  1.000 19.69891  ? 263 LEU A HD11 1 
ATOM   3327 H  HD12 . LEU A  1 263 ? -1.58800  -20.51800 25.59900  1.000 19.69891  ? 263 LEU A HD12 1 
ATOM   3328 H  HD13 . LEU A  1 263 ? -2.74700  -21.23600 24.78300  1.000 19.69891  ? 263 LEU A HD13 1 
ATOM   3329 H  HD21 . LEU A  1 263 ? -2.95000  -19.35100 22.51700  1.000 20.51291  ? 263 LEU A HD21 1 
ATOM   3330 H  HD22 . LEU A  1 263 ? -4.23600  -19.87200 23.29100  1.000 20.51291  ? 263 LEU A HD22 1 
ATOM   3331 H  HD23 . LEU A  1 263 ? -3.97000  -18.31200 23.15200  1.000 20.51291  ? 263 LEU A HD23 1 
ATOM   3332 N  N    . GLY A  1 264 ? -4.84300  -17.58600 28.22700  1.000 14.47101  ? 264 GLY A N    1 
ATOM   3333 C  CA   . GLY A  1 264 ? -5.81600  -17.59200 29.27700  1.000 14.32460  ? 264 GLY A CA   1 
ATOM   3334 C  C    . GLY A  1 264 ? -6.51000  -16.26600 29.46900  1.000 15.32399  ? 264 GLY A C    1 
ATOM   3335 O  O    . GLY A  1 264 ? -7.71200  -16.24000 29.78300  1.000 15.48735  ? 264 GLY A O    1 
ATOM   3336 H  H    . GLY A  1 264 ? -4.02300  -17.65900 28.47500  1.000 17.36777  ? 264 GLY A H    1 
ATOM   3337 H  HA2  . GLY A  1 264 ? -6.49200  -18.25900 29.07800  1.000 17.19208  ? 264 GLY A HA2  1 
ATOM   3338 H  HA3  . GLY A  1 264 ? -5.37900  -17.82500 30.11100  1.000 17.19208  ? 264 GLY A HA3  1 
ATOM   3339 N  N    . LYS A  1 265 ? -5.79100  -15.15800 29.29200  1.000 15.25265  ? 265 LYS A N    1 
ATOM   3340 C  CA   . LYS A  1 265 ? -6.43700  -13.86200 29.44200  1.000 16.41993  ? 265 LYS A CA   1 
ATOM   3341 C  C    . LYS A  1 265 ? -7.57200  -13.71700 28.44000  1.000 14.67654  ? 265 LYS A C    1 
ATOM   3342 O  O    . LYS A  1 265 ? -8.71500  -13.42600 28.80700  1.000 15.36453  ? 265 LYS A O    1 
ATOM   3343 C  CB   . LYS A  1 265 ? -5.42600  -12.73600 29.27200  1.000 16.98622  ? 265 LYS A CB   1 
ATOM   3344 C  CG   . LYS A  1 265 ? -6.04900  -11.35900 29.06200  1.000 18.31970  ? 265 LYS A CG   1 
ATOM   3345 C  CD   . LYS A  1 265 ? -5.00900  -10.23900 29.18700  1.000 20.77546  ? 265 LYS A CD   1 
ATOM   3346 C  CE   . LYS A  1 265 ? -3.97500  -10.35000 28.15300  1.000 23.39320  ? 265 LYS A CE   1 
ATOM   3347 N  NZ   . LYS A  1 265 ? -2.97400  -9.21700  28.26300  1.000 28.61523  ? 265 LYS A NZ   1 
ATOM   3348 H  H    . LYS A  1 265 ? -4.95500  -15.13200 29.09100  1.000 18.30574  ? 265 LYS A H    1 
ATOM   3349 H  HA   . LYS A  1 265 ? -6.80100  -13.79400 30.33900  1.000 19.70648  ? 265 LYS A HA   1 
ATOM   3350 H  HB2  . LYS A  1 265 ? -4.87500  -12.69100 30.06900  1.000 20.38602  ? 265 LYS A HB2  1 
ATOM   3351 H  HB3  . LYS A  1 265 ? -4.87400  -12.93000 28.49800  1.000 20.38602  ? 265 LYS A HB3  1 
ATOM   3352 H  HG2  . LYS A  1 265 ? -6.43800  -11.31500 28.17400  1.000 21.98620  ? 265 LYS A HG2  1 
ATOM   3353 H  HG3  . LYS A  1 265 ? -6.73500  -11.21300 29.73200  1.000 21.98620  ? 265 LYS A HG3  1 
ATOM   3354 H  HD2  . LYS A  1 265 ? -5.44800  -9.38000  29.08900  1.000 24.93312  ? 265 LYS A HD2  1 
ATOM   3355 H  HD3  . LYS A  1 265 ? -4.58000  -10.29500 30.05600  1.000 24.93312  ? 265 LYS A HD3  1 
ATOM   3356 H  HE2  . LYS A  1 265 ? -3.50100  -11.19000 28.25900  1.000 28.07440  ? 265 LYS A HE2  1 
ATOM   3357 H  HE3  . LYS A  1 265 ? -4.38800  -10.31100 27.27700  1.000 28.07440  ? 265 LYS A HE3  1 
ATOM   3358 H  HZ1  . LYS A  1 265 ? -3.38100  -8.43700  28.12600  1.000 34.34083  ? 265 LYS A HZ1  1 
ATOM   3359 H  HZ2  . LYS A  1 265 ? -2.60600  -9.21200  29.07300  1.000 34.34083  ? 265 LYS A HZ2  1 
ATOM   3360 H  HZ3  . LYS A  1 265 ? -2.33200  -9.31800  27.65500  1.000 34.34083  ? 265 LYS A HZ3  1 
ATOM   3361 N  N    . TYR A  1 266 ? -7.27800  -13.92600 27.16100  1.000 14.63481  ? 266 TYR A N    1 
ATOM   3362 C  CA   . TYR A  1 266 ? -8.31500  -13.70700 26.16000  1.000 15.93858  ? 266 TYR A CA   1 
ATOM   3363 C  C    . TYR A  1 266 ? -9.36400  -14.81300 26.18500  1.000 15.11527  ? 266 TYR A C    1 
ATOM   3364 O  O    . TYR A  1 266 ? -10.54200 -14.54500 25.95400  1.000 15.69644  ? 266 TYR A O    1 
ATOM   3365 C  CB   . TYR A  1 266 ? -7.67200  -13.57800 24.79300  1.000 17.77187  ? 266 TYR A CB   1 
ATOM   3366 C  CG   . TYR A  1 266 ? -6.81900  -12.33600 24.62300  1.000 17.02411  ? 266 TYR A CG   1 
ATOM   3367 C  CD1  . TYR A  1 266 ? -7.30700  -11.08400 24.91200  1.000 18.74568  ? 266 TYR A CD1  1 
ATOM   3368 C  CD2  . TYR A  1 266 ? -5.54200  -12.43200 24.12900  1.000 17.61465  ? 266 TYR A CD2  1 
ATOM   3369 C  CE1  . TYR A  1 266 ? -6.53600  -9.94500  24.69400  1.000 20.53268  ? 266 TYR A CE1  1 
ATOM   3370 C  CE2  . TYR A  1 266 ? -4.76300  -11.31100 23.90000  1.000 20.74788  ? 266 TYR A CE2  1 
ATOM   3371 C  CZ   . TYR A  1 266 ? -5.26500  -10.07800 24.22000  1.000 20.24381  ? 266 TYR A CZ   1 
ATOM   3372 O  OH   . TYR A  1 266 ? -4.49100  -8.94700  23.96400  1.000 24.40042  ? 266 TYR A OH   1 
ATOM   3373 H  H    . TYR A  1 266 ? -6.51600  -14.18500 26.85800  1.000 17.56433  ? 266 TYR A H    1 
ATOM   3374 H  HA   . TYR A  1 266 ? -8.77800  -12.87700 26.35200  1.000 19.12886  ? 266 TYR A HA   1 
ATOM   3375 H  HB2  . TYR A  1 266 ? -7.10200  -14.34900 24.64400  1.000 21.32880  ? 266 TYR A HB2  1 
ATOM   3376 H  HB3  . TYR A  1 266 ? -8.37200  -13.54800 24.12200  1.000 21.32880  ? 266 TYR A HB3  1 
ATOM   3377 H  HD1  . TYR A  1 266 ? -8.16600  -10.99600 25.25900  1.000 22.49738  ? 266 TYR A HD1  1 
ATOM   3378 H  HD2  . TYR A  1 266 ? -5.19100  -13.27300 23.94300  1.000 21.14014  ? 266 TYR A HD2  1 
ATOM   3379 H  HE1  . TYR A  1 266 ? -6.88500  -9.10100  24.87000  1.000 24.64178  ? 266 TYR A HE1  1 
ATOM   3380 H  HE2  . TYR A  1 266 ? -3.91200  -11.39400 23.53400  1.000 24.90002  ? 266 TYR A HE2  1 
ATOM   3381 H  HH   . TYR A  1 266 ? -4.88900  -8.26000  24.23800  1.000 29.28306  ? 266 TYR A HH   1 
ATOM   3382 N  N    . GLY A  1 267 ? -8.96300  -16.06100 26.43800  1.000 14.08088  ? 267 GLY A N    1 
ATOM   3383 C  CA   . GLY A  1 267 ? -9.92000  -17.16300 26.43800  1.000 15.70424  ? 267 GLY A CA   1 
ATOM   3384 C  C    . GLY A  1 267 ? -10.88600 -17.08200 27.60200  1.000 13.88670  ? 267 GLY A C    1 
ATOM   3385 O  O    . GLY A  1 267 ? -12.09600 -17.24500 27.45400  1.000 13.85830  ? 267 GLY A O    1 
ATOM   3386 H  H    . GLY A  1 267 ? -8.15300  -16.29300 26.61100  1.000 16.89962  ? 267 GLY A H    1 
ATOM   3387 H  HA2  . GLY A  1 267 ? -10.43100 -17.14500 25.61400  1.000 18.84765  ? 267 GLY A HA2  1 
ATOM   3388 H  HA3  . GLY A  1 267 ? -9.44100  -18.00500 26.49500  1.000 18.84765  ? 267 GLY A HA3  1 
ATOM   3389 N  N    . VAL A  1 268 ? -10.36500 -16.82700 28.79900  1.000 13.14388  ? 268 VAL A N    1 
ATOM   3390 C  CA   . VAL A  1 268 ? -11.24900 -16.64700 29.94600  1.000 14.24591  ? 268 VAL A CA   1 
ATOM   3391 C  C    . VAL A  1 268 ? -12.14900 -15.44000 29.72300  1.000 14.75827  ? 268 VAL A C    1 
ATOM   3392 O  O    . VAL A  1 268 ? -13.34300 -15.47900 30.02100  1.000 14.95752  ? 268 VAL A O    1 
ATOM   3393 C  CB   . VAL A  1 268 ? -10.45400 -16.54700 31.26500  1.000 13.11267  ? 268 VAL A CB   1 
ATOM   3394 C  CG1  . VAL A  1 268 ? -11.34900 -16.10800 32.41900  1.000 16.23606  ? 268 VAL A CG1  1 
ATOM   3395 C  CG2  . VAL A  1 268 ? -9.80700  -17.90100 31.56100  1.000 15.11495  ? 268 VAL A CG2  1 
ATOM   3396 H  H    . VAL A  1 268 ? -9.52500  -16.75600 28.97000  1.000 15.77521  ? 268 VAL A H    1 
ATOM   3397 H  HA   . VAL A  1 268 ? -11.81000 -17.43400 30.02200  1.000 17.09765  ? 268 VAL A HA   1 
ATOM   3398 H  HB   . VAL A  1 268 ? -9.76200  -15.87400 31.17400  1.000 15.73777  ? 268 VAL A HB   1 
ATOM   3399 H  HG11 . VAL A  1 268 ? -10.87400 -16.24100 33.25400  1.000 19.48583  ? 268 VAL A HG11 1 
ATOM   3400 H  HG12 . VAL A  1 268 ? -11.56900 -15.17000 32.30900  1.000 19.48583  ? 268 VAL A HG12 1 
ATOM   3401 H  HG13 . VAL A  1 268 ? -12.15900 -16.64100 32.41000  1.000 19.48583  ? 268 VAL A HG13 1 
ATOM   3402 H  HG21 . VAL A  1 268 ? -9.24600  -17.81800 32.34800  1.000 18.14051  ? 268 VAL A HG21 1 
ATOM   3403 H  HG22 . VAL A  1 268 ? -10.50400 -18.55700 31.71900  1.000 18.14051  ? 268 VAL A HG22 1 
ATOM   3404 H  HG23 . VAL A  1 268 ? -9.26900  -18.16700 30.79900  1.000 18.14051  ? 268 VAL A HG23 1 
ATOM   3405 N  N    . ALA A  1 269 ? -11.59500 -14.32100 29.25300  1.000 14.55796  ? 269 ALA A N    1 
ATOM   3406 C  CA   . ALA A  1 269 ? -12.42200 -13.15200 29.02800  1.000 15.86082  ? 269 ALA A CA   1 
ATOM   3407 C  C    . ALA A  1 269 ? -13.54700 -13.46800 28.05800  1.000 16.01868  ? 269 ALA A C    1 
ATOM   3408 O  O    . ALA A  1 269 ? -14.67400 -13.01900 28.24100  1.000 15.38870  ? 269 ALA A O    1 
ATOM   3409 C  CB   . ALA A  1 269 ? -11.56700 -11.97400 28.55300  1.000 16.17306  ? 269 ALA A CB   1 
ATOM   3410 H  H    . ALA A  1 269 ? -10.76200 -14.22200 29.06300  1.000 17.47211  ? 269 ALA A H    1 
ATOM   3411 H  HA   . ALA A  1 269 ? -12.82700 -12.87900 29.86600  1.000 19.03555  ? 269 ALA A HA   1 
ATOM   3412 H  HB1  . ALA A  1 269 ? -12.14100 -11.20400 28.41300  1.000 19.41024  ? 269 ALA A HB1  1 
ATOM   3413 H  HB2  . ALA A  1 269 ? -10.90300 -11.77200 29.23000  1.000 19.41024  ? 269 ALA A HB2  1 
ATOM   3414 H  HB3  . ALA A  1 269 ? -11.12900 -12.21600 27.72200  1.000 19.41024  ? 269 ALA A HB3  1 
ATOM   3415 N  N    . TRP A  1 270 ? -13.25000 -14.24200 27.01800  1.000 14.71824  ? 270 TRP A N    1 
ATOM   3416 C  CA   . TRP A  1 270 ? -14.27600 -14.59500 26.04200  1.000 14.01892  ? 270 TRP A CA   1 
ATOM   3417 C  C    . TRP A  1 270 ? -15.40800 -15.36900 26.70100  1.000 14.76468  ? 270 TRP A C    1 
ATOM   3418 O  O    . TRP A  1 270 ? -16.59300 -15.09700 26.46000  1.000 15.75339  ? 270 TRP A O    1 
ATOM   3419 C  CB   . TRP A  1 270 ? -13.66800 -15.43500 24.91200  1.000 14.40605  ? 270 TRP A CB   1 
ATOM   3420 C  CG   . TRP A  1 270 ? -14.56200 -15.50300 23.70100  1.000 14.42165  ? 270 TRP A CG   1 
ATOM   3421 C  CD1  . TRP A  1 270 ? -15.31300 -16.55100 23.27200  1.000 14.93775  ? 270 TRP A CD1  1 
ATOM   3422 C  CD2  . TRP A  1 270 ? -14.77600 -14.44600 22.77200  1.000 16.40344  ? 270 TRP A CD2  1 
ATOM   3423 N  NE1  . TRP A  1 270 ? -16.01100 -16.20100 22.13100  1.000 15.35524  ? 270 TRP A NE1  1 
ATOM   3424 C  CE2  . TRP A  1 270 ? -15.70200 -14.89900 21.81300  1.000 16.11894  ? 270 TRP A CE2  1 
ATOM   3425 C  CE3  . TRP A  1 270 ? -14.29400 -13.14900 22.67800  1.000 17.85771  ? 270 TRP A CE3  1 
ATOM   3426 C  CZ2  . TRP A  1 270 ? -16.10700 -14.10800 20.76400  1.000 17.17423  ? 270 TRP A CZ2  1 
ATOM   3427 C  CZ3  . TRP A  1 270 ? -14.70600 -12.36400 21.63100  1.000 18.10446  ? 270 TRP A CZ3  1 
ATOM   3428 C  CH2  . TRP A  1 270 ? -15.63900 -12.83700 20.70600  1.000 18.44544  ? 270 TRP A CH2  1 
ATOM   3429 H  H    . TRP A  1 270 ? -12.47300 -14.57200 26.85600  1.000 17.66445  ? 270 TRP A H    1 
ATOM   3430 H  HA   . TRP A  1 270 ? -14.63100 -13.77700 25.66200  1.000 16.82527  ? 270 TRP A HA   1 
ATOM   3431 H  HB2  . TRP A  1 270 ? -12.82400 -15.04100 24.64300  1.000 17.28982  ? 270 TRP A HB2  1 
ATOM   3432 H  HB3  . TRP A  1 270 ? -13.52400 -16.34000 25.23200  1.000 17.28982  ? 270 TRP A HB3  1 
ATOM   3433 H  HD1  . TRP A  1 270 ? -15.35100 -17.38300 23.68600  1.000 17.92786  ? 270 TRP A HD1  1 
ATOM   3434 H  HE1  . TRP A  1 270 ? -16.54800 -16.71100 21.69400  1.000 18.42885  ? 270 TRP A HE1  1 
ATOM   3435 H  HE3  . TRP A  1 270 ? -13.70300 -12.81700 23.31400  1.000 21.43181  ? 270 TRP A HE3  1 
ATOM   3436 H  HZ2  . TRP A  1 270 ? -16.68400 -14.43600 20.11200  1.000 20.61164  ? 270 TRP A HZ2  1 
ATOM   3437 H  HZ3  . TRP A  1 270 ? -14.35800 -11.50600 21.53500  1.000 21.72791  ? 270 TRP A HZ3  1 
ATOM   3438 H  HH2  . TRP A  1 270 ? -15.94600 -12.26800 20.03800  1.000 22.13710  ? 270 TRP A HH2  1 
ATOM   3439 N  N    . MET A  1 271 ? -15.06500 -16.38700 27.49100  1.000 13.91283  ? 271 MET A N    1 
ATOM   3440 C  CA   . MET A  1 271 ? -16.08500 -17.20600 28.12400  1.000 14.61771  ? 271 MET A CA   1 
ATOM   3441 C  C    . MET A  1 271 ? -16.83500 -16.42800 29.18400  1.000 14.89004  ? 271 MET A C    1 
ATOM   3442 O  O    . MET A  1 271 ? -18.05200 -16.58000 29.32600  1.000 14.91358  ? 271 MET A O    1 
ATOM   3443 C  CB   . MET A  1 271 ? -15.46900 -18.50100 28.68700  1.000 14.08034  ? 271 MET A CB   1 
ATOM   3444 C  CG   . MET A  1 271 ? -14.83600 -19.37800 27.60400  1.000 14.51254  ? 271 MET A CG   1 
ATOM   3445 S  SD   . MET A  1 271 ? -15.97400 -19.63800 26.21000  1.000 15.80275  ? 271 MET A SD   1 
ATOM   3446 C  CE   . MET A  1 271 ? -15.53200 -21.28700 25.63900  1.000 16.56660  ? 271 MET A CE   1 
ATOM   3447 H  H    . MET A  1 271 ? -14.25600 -16.61900 27.67200  1.000 16.69796  ? 271 MET A H    1 
ATOM   3448 H  HA   . MET A  1 271 ? -16.72500 -17.48000 27.44800  1.000 17.54381  ? 271 MET A HA   1 
ATOM   3449 H  HB2  . MET A  1 271 ? -14.77900 -18.26900 29.32700  1.000 16.89897  ? 271 MET A HB2  1 
ATOM   3450 H  HB3  . MET A  1 271 ? -16.16500 -19.01800 29.12200  1.000 16.89897  ? 271 MET A HB3  1 
ATOM   3451 H  HG2  . MET A  1 271 ? -14.03500 -18.94500 27.26800  1.000 17.41761  ? 271 MET A HG2  1 
ATOM   3452 H  HG3  . MET A  1 271 ? -14.61200 -20.24300 27.98100  1.000 17.41761  ? 271 MET A HG3  1 
ATOM   3453 H  HE1  . MET A  1 271 ? -16.11600 -21.53400 24.90500  1.000 19.88248  ? 271 MET A HE1  1 
ATOM   3454 H  HE2  . MET A  1 271 ? -14.60900 -21.28100 25.33900  1.000 19.88248  ? 271 MET A HE2  1 
ATOM   3455 H  HE3  . MET A  1 271 ? -15.63700 -21.91400 26.37100  1.000 19.88248  ? 271 MET A HE3  1 
ATOM   3456 N  N    . LYS A  1 272 ? -16.14400 -15.59100 29.94300  1.000 14.61863  ? 272 LYS A N    1 
ATOM   3457 C  CA   . LYS A  1 272 ? -16.83700 -14.73700 30.90400  1.000 15.63367  ? 272 LYS A CA   1 
ATOM   3458 C  C    . LYS A  1 272 ? -17.84200 -13.81100 30.21000  1.000 16.47516  ? 272 LYS A C    1 
ATOM   3459 O  O    . LYS A  1 272 ? -18.98900 -13.66600 30.64600  1.000 15.87292  ? 272 LYS A O    1 
ATOM   3460 C  CB   . LYS A  1 272 ? -15.82700 -13.88700 31.66200  1.000 15.26608  ? 272 LYS A CB   1 
ATOM   3461 C  CG   . LYS A  1 272 ? -15.01900 -14.60800 32.70100  1.000 15.63878  ? 272 LYS A CG   1 
ATOM   3462 C  CD   . LYS A  1 272 ? -15.81000 -14.88100 33.95900  1.000 16.09484  ? 272 LYS A CD   1 
ATOM   3463 C  CE   . LYS A  1 272 ? -14.88200 -15.35900 35.08300  1.000 17.36311  ? 272 LYS A CE   1 
ATOM   3464 N  NZ   . LYS A  1 272 ? -15.60200 -15.57000 36.34400  1.000 17.14793  ? 272 LYS A NZ   1 
ATOM   3465 H  H    . LYS A  1 272 ? -15.28900 -15.49800 29.92600  1.000 17.54492  ? 272 LYS A H    1 
ATOM   3466 H  HA   . LYS A  1 272 ? -17.31400 -15.31000 31.52500  1.000 18.76296  ? 272 LYS A HA   1 
ATOM   3467 H  HB2  . LYS A  1 272 ? -15.20300 -13.51200 31.02100  1.000 18.32186  ? 272 LYS A HB2  1 
ATOM   3468 H  HB3  . LYS A  1 272 ? -16.30700 -13.17500 32.11400  1.000 18.32186  ? 272 LYS A HB3  1 
ATOM   3469 H  HG2  . LYS A  1 272 ? -14.72500 -15.45900 32.34000  1.000 18.76910  ? 272 LYS A HG2  1 
ATOM   3470 H  HG3  . LYS A  1 272 ? -14.25100 -14.06600 32.93900  1.000 18.76910  ? 272 LYS A HG3  1 
ATOM   3471 H  HD2  . LYS A  1 272 ? -16.25200 -14.06700 34.24700  1.000 19.31637  ? 272 LYS A HD2  1 
ATOM   3472 H  HD3  . LYS A  1 272 ? -16.46800 -15.57200 33.78600  1.000 19.31637  ? 272 LYS A HD3  1 
ATOM   3473 H  HE2  . LYS A  1 272 ? -14.47400 -16.20000 34.82300  1.000 20.83830  ? 272 LYS A HE2  1 
ATOM   3474 H  HE3  . LYS A  1 272 ? -14.19600 -14.69000 35.23500  1.000 20.83830  ? 272 LYS A HE3  1 
ATOM   3475 H  HZ1  . LYS A  1 272 ? -15.03300 -15.81500 36.98200  1.000 20.58008  ? 272 LYS A HZ1  1 
ATOM   3476 H  HZ2  . LYS A  1 272 ? -16.00900 -14.81900 36.59200  1.000 20.58008  ? 272 LYS A HZ2  1 
ATOM   3477 H  HZ3  . LYS A  1 272 ? -16.21400 -16.20900 36.24100  1.000 20.58008  ? 272 LYS A HZ3  1 
ATOM   3478 N  N    . LEU A  1 273 ? -17.39900 -13.12800 29.15600  1.000 16.68737  ? 273 LEU A N    1 
ATOM   3479 C  CA   . LEU A  1 273 ? -18.25400 -12.16800 28.47200  1.000 15.76312  ? 273 LEU A CA   1 
ATOM   3480 C  C    . LEU A  1 273 ? -19.46700 -12.84300 27.85700  1.000 17.50822  ? 273 LEU A C    1 
ATOM   3481 O  O    . LEU A  1 273 ? -20.57900 -12.31500 27.92600  1.000 19.01271  ? 273 LEU A O    1 
ATOM   3482 C  CB   . LEU A  1 273 ? -17.44500 -11.41100 27.41100  1.000 17.54809  ? 273 LEU A CB   1 
ATOM   3483 C  CG   . LEU A  1 273 ? -18.24600 -10.31700 26.70900  1.000 18.20810  ? 273 LEU A CG   1 
ATOM   3484 C  CD1  . LEU A  1 273 ? -18.75900 -9.26800  27.62700  1.000 20.93991  ? 273 LEU A CD1  1 
ATOM   3485 C  CD2  . LEU A  1 273 ? -17.32400 -9.69200  25.64400  1.000 21.72696  ? 273 LEU A CD2  1 
ATOM   3486 H  H    . LEU A  1 273 ? -16.61000 -13.20200 28.82000  1.000 20.02741  ? 273 LEU A H    1 
ATOM   3487 H  HA   . LEU A  1 273 ? -18.57800 -11.51900 29.11600  1.000 18.91831  ? 273 LEU A HA   1 
ATOM   3488 H  HB2  . LEU A  1 273 ? -16.68100 -10.99400 27.83900  1.000 21.06027  ? 273 LEU A HB2  1 
ATOM   3489 H  HB3  . LEU A  1 273 ? -17.14600 -12.04100 26.73700  1.000 21.06027  ? 273 LEU A HB3  1 
ATOM   3490 H  HG   . LEU A  1 273 ? -19.03900 -10.71100 26.31200  1.000 21.85228  ? 273 LEU A HG   1 
ATOM   3491 H  HD11 . LEU A  1 273 ? -19.10000 -8.52800  27.10200  1.000 25.13046  ? 273 LEU A HD11 1 
ATOM   3492 H  HD12 . LEU A  1 273 ? -19.46900 -9.64300  28.17100  1.000 25.13046  ? 273 LEU A HD12 1 
ATOM   3493 H  HD13 . LEU A  1 273 ? -18.03400 -8.96300  28.19500  1.000 25.13046  ? 273 LEU A HD13 1 
ATOM   3494 H  HD21 . LEU A  1 273 ? -17.81700 -9.00900  25.16200  1.000 26.07492  ? 273 LEU A HD21 1 
ATOM   3495 H  HD22 . LEU A  1 273 ? -16.55600 -9.29700  26.08400  1.000 26.07492  ? 273 LEU A HD22 1 
ATOM   3496 H  HD23 . LEU A  1 273 ? -17.03400 -10.38500 25.03100  1.000 26.07492  ? 273 LEU A HD23 1 
ATOM   3497 N  N    . HIS A  1 274 ? -19.28800 -14.02000 27.26200  1.000 16.01434  ? 274 HIS A N    1 
ATOM   3498 C  CA   . HIS A  1 274 ? -20.38200 -14.60100 26.50500  1.000 17.22985  ? 274 HIS A CA   1 
ATOM   3499 C  C    . HIS A  1 274 ? -21.15200 -15.66600 27.24200  1.000 18.55792  ? 274 HIS A C    1 
ATOM   3500 O  O    . HIS A  1 274 ? -22.37100 -15.69700 27.15000  1.000 22.89040  ? 274 HIS A O    1 
ATOM   3501 C  CB   . HIS A  1 274 ? -19.84700 -15.13200 25.20000  1.000 17.49973  ? 274 HIS A CB   1 
ATOM   3502 C  CG   . HIS A  1 274 ? -19.27400 -14.04600 24.35900  1.000 15.61621  ? 274 HIS A CG   1 
ATOM   3503 N  ND1  . HIS A  1 274 ? -20.02500 -13.01700 23.82600  1.000 20.25583  ? 274 HIS A ND1  1 
ATOM   3504 C  CD2  . HIS A  1 274 ? -17.99300 -13.79200 24.03100  1.000 16.06266  ? 274 HIS A CD2  1 
ATOM   3505 C  CE1  . HIS A  1 274 ? -19.21400 -12.19300 23.17200  1.000 18.10514  ? 274 HIS A CE1  1 
ATOM   3506 N  NE2  . HIS A  1 274 ? -17.98500 -12.64600 23.27600  1.000 20.90814  ? 274 HIS A NE2  1 
ATOM   3507 H  H    . HIS A  1 274 ? -18.56300 -14.48200 27.28400  1.000 19.21977  ? 274 HIS A H    1 
ATOM   3508 H  HA   . HIS A  1 274 ? -21.03300 -13.91000 26.30600  1.000 20.67838  ? 274 HIS A HA   1 
ATOM   3509 H  HB2  . HIS A  1 274 ? -19.14700 -15.77900 25.38100  1.000 21.00224  ? 274 HIS A HB2  1 
ATOM   3510 H  HB3  . HIS A  1 274 ? -20.56700 -15.55300 24.70600  1.000 21.00224  ? 274 HIS A HB3  1 
ATOM   3511 H  HD2  . HIS A  1 274 ? -17.25100 -14.29900 24.27100  1.000 19.27775  ? 274 HIS A HD2  1 
ATOM   3512 H  HE1  . HIS A  1 274 ? -19.47300 -11.42500 22.71700  1.000 21.72873  ? 274 HIS A HE1  1 
ATOM   3513 H  HE2  . HIS A  1 274 ? -17.28700 -12.28300 22.92700  1.000 25.09233  ? 274 HIS A HE2  1 
ATOM   3514 N  N    . LEU A  1 275 ? -20.51400 -16.51200 28.02500  1.000 16.07645  ? 275 LEU A N    1 
ATOM   3515 C  CA   . LEU A  1 275 ? -21.26500 -17.50700 28.78700  1.000 15.30182  ? 275 LEU A CA   1 
ATOM   3516 C  C    . LEU A  1 275 ? -21.81600 -16.95400 30.07600  1.000 16.63516  ? 275 LEU A C    1 
ATOM   3517 O  O    . LEU A  1 275 ? -22.90300 -17.36600 30.48000  1.000 17.23716  ? 275 LEU A O    1 
ATOM   3518 C  CB   . LEU A  1 275 ? -20.37800 -18.72400 29.09500  1.000 14.89205  ? 275 LEU A CB   1 
ATOM   3519 C  CG   . LEU A  1 275 ? -19.84900 -19.52400 27.91900  1.000 15.34024  ? 275 LEU A CG   1 
ATOM   3520 C  CD1  . LEU A  1 275 ? -19.01400 -20.68100 28.42200  1.000 16.45390  ? 275 LEU A CD1  1 
ATOM   3521 C  CD2  . LEU A  1 275 ? -20.98400 -19.99500 27.00500  1.000 16.50978  ? 275 LEU A CD2  1 
ATOM   3522 H  H    . LEU A  1 275 ? -19.66200 -16.53700 28.13700  1.000 19.29430  ? 275 LEU A H    1 
ATOM   3523 H  HA   . LEU A  1 275 ? -22.01100 -17.80000 28.24100  1.000 18.36474  ? 275 LEU A HA   1 
ATOM   3524 H  HB2  . LEU A  1 275 ? -19.60500 -18.41000 29.59000  1.000 17.87302  ? 275 LEU A HB2  1 
ATOM   3525 H  HB3  . LEU A  1 275 ? -20.89500 -19.33700 29.64000  1.000 17.87302  ? 275 LEU A HB3  1 
ATOM   3526 H  HG   . LEU A  1 275 ? -19.28100 -18.95700 27.37400  1.000 18.41086  ? 275 LEU A HG   1 
ATOM   3527 H  HD11 . LEU A  1 275 ? -18.60600 -21.13000 27.66500  1.000 19.74725  ? 275 LEU A HD11 1 
ATOM   3528 H  HD12 . LEU A  1 275 ? -18.32500 -20.34000 29.01400  1.000 19.74725  ? 275 LEU A HD12 1 
ATOM   3529 H  HD13 . LEU A  1 275 ? -19.58700 -21.29900 28.90300  1.000 19.74725  ? 275 LEU A HD13 1 
ATOM   3530 H  HD21 . LEU A  1 275 ? -20.62200 -20.59900 26.33800  1.000 19.81429  ? 275 LEU A HD21 1 
ATOM   3531 H  HD22 . LEU A  1 275 ? -21.65000 -20.45500 27.54000  1.000 19.81429  ? 275 LEU A HD22 1 
ATOM   3532 H  HD23 . LEU A  1 275 ? -21.38200 -19.22400 26.57200  1.000 19.81429  ? 275 LEU A HD23 1 
ATOM   3533 N  N    . ASP A  1 276 ? -21.14500 -15.99800 30.69300  1.000 15.58383  ? 276 ASP A N    1 
ATOM   3534 C  CA   . ASP A  1 276 ? -21.65500 -15.38700 31.94500  1.000 16.63970  ? 276 ASP A CA   1 
ATOM   3535 C  C    . ASP A  1 276 ? -22.28700 -14.01600 31.66200  1.000 17.70000  ? 276 ASP A C    1 
ATOM   3536 O  O    . ASP A  1 276 ? -22.81500 -13.46500 32.58300  1.000 18.77356  ? 276 ASP A O    1 
ATOM   3537 C  CB   . ASP A  1 276 ? -20.54900 -15.20300 32.98500  1.000 15.93526  ? 276 ASP A CB   1 
ATOM   3538 C  CG   . ASP A  1 276 ? -19.96100 -16.46800 33.58500  1.000 17.47298  ? 276 ASP A CG   1 
ATOM   3539 O  OD1  . ASP A  1 276 ? -20.51200 -17.51900 33.39700  1.000 18.03323  ? 276 ASP A OD1  1 
ATOM   3540 O  OD2  . ASP A  1 276 ? -18.97900 -16.33100 34.25300  1.000 18.14122  ? 276 ASP A OD2  1 
ATOM   3541 H  H    . ASP A  1 276 ? -20.34600 -15.67100 30.40100  1.000 18.70315  ? 276 ASP A H    1 
ATOM   3542 H  HA   . ASP A  1 276 ? -22.34500 -15.98200 32.32300  1.000 19.97021  ? 276 ASP A HA   1 
ATOM   3543 H  HB2  . ASP A  1 276 ? -19.81600 -14.70400 32.56900  1.000 19.12487  ? 276 ASP A HB2  1 
ATOM   3544 H  HB3  . ASP A  1 276 ? -20.90200 -14.66100 33.71900  1.000 19.12487  ? 276 ASP A HB3  1 
ATOM   3545 N  N    . GLN A  1 277 ? -22.20300 -13.48700 30.45400  1.000 17.64458  ? 277 GLN A N    1 
ATOM   3546 C  CA   . GLN A  1 277 ? -22.71500 -12.11800 30.16100  1.000 19.22791  ? 277 GLN A CA   1 
ATOM   3547 C  C    . GLN A  1 277 ? -22.06200 -11.14800 31.14800  1.000 19.10296  ? 277 GLN A C    1 
ATOM   3548 O  O    . GLN A  1 277 ? -22.71700 -10.22100 31.55500  1.000 21.68073  ? 277 GLN A O    1 
ATOM   3549 C  CB   . GLN A  1 277 ? -24.23900 -12.08500 30.10200  1.000 21.33372  ? 277 GLN A CB   1 
ATOM   3550 C  CG   . GLN A  1 277 ? -24.79700 -13.24200 29.33200  1.000 30.59578  ? 277 GLN A CG   1 
ATOM   3551 C  CD   . GLN A  1 277 ? -25.03300 -12.84100 27.91400  1.000 45.54059  ? 277 GLN A CD   1 
ATOM   3552 O  OE1  . GLN A  1 277 ? -26.05500 -12.25700 27.61700  1.000 41.35997  ? 277 GLN A OE1  1 
ATOM   3553 N  NE2  . GLN A  1 277 ? -24.11300 -13.18700 27.03000  1.000 36.22611  ? 277 GLN A NE2  1 
ATOM   3554 H  H    . GLN A  1 277 ? -21.83900 -13.91400 29.73900  1.000 21.17606  ? 277 GLN A H    1 
ATOM   3555 H  HA   . GLN A  1 277 ? -22.38700 -11.87900 29.26300  1.000 23.07606  ? 277 GLN A HA   1 
ATOM   3556 H  HB2  . GLN A  1 277 ? -24.59200 -12.10200 31.01700  1.000 25.60302  ? 277 GLN A HB2  1 
ATOM   3557 H  HB3  . GLN A  1 277 ? -24.52200 -11.24600 29.68200  1.000 25.60302  ? 277 GLN A HB3  1 
ATOM   3558 H  HG2  . GLN A  1 277 ? -24.17000 -13.99500 29.36000  1.000 36.71750  ? 277 GLN A HG2  1 
ATOM   3559 H  HG3  . GLN A  1 277 ? -25.64300 -13.53000 29.73600  1.000 36.71750  ? 277 GLN A HG3  1 
ATOM   3560 H  HE21 . GLN A  1 277 ? -23.48900 -13.77400 27.24700  1.000 43.47389  ? 277 GLN A HE21 1 
ATOM   3561 H  HE22 . GLN A  1 277 ? -24.12100 -12.83200 26.22100  1.000 43.47389  ? 277 GLN A HE22 1 
ATOM   3562 N  N    . ASP A  1 278 ? -20.78900 -11.36100 31.48200  1.000 18.43027  ? 278 ASP A N    1 
ATOM   3563 C  CA   . ASP A  1 278 ? -20.09300 -10.57200 32.50200  1.000 19.41580  ? 278 ASP A CA   1 
ATOM   3564 C  C    . ASP A  1 278 ? -19.33900 -9.45200  31.80300  1.000 18.64487  ? 278 ASP A C    1 
ATOM   3565 O  O    . ASP A  1 278 ? -18.21700 -9.65000  31.31100  1.000 19.70456  ? 278 ASP A O    1 
ATOM   3566 C  CB   . ASP A  1 278 ? -19.15700 -11.47200 33.28700  1.000 18.60878  ? 278 ASP A CB   1 
ATOM   3567 C  CG   . ASP A  1 278 ? -18.50900 -10.76400 34.46400  1.000 18.77972  ? 278 ASP A CG   1 
ATOM   3568 O  OD1  . ASP A  1 278 ? -18.56000 -9.52700  34.56100  1.000 20.40060  ? 278 ASP A OD1  1 
ATOM   3569 O  OD2  . ASP A  1 278 ? -17.93100 -11.49900 35.30300  1.000 19.18746  ? 278 ASP A OD2  1 
ATOM   3570 H  H    . ASP A  1 278 ? -20.30200 -11.98400 31.14400  1.000 22.11889  ? 278 ASP A H    1 
ATOM   3571 H  HA   . ASP A  1 278 ? -20.73100 -10.17000 33.11100  1.000 23.30153  ? 278 ASP A HA   1 
ATOM   3572 H  HB2  . ASP A  1 278 ? -19.66000 -12.22700 33.63000  1.000 22.33309  ? 278 ASP A HB2  1 
ATOM   3573 H  HB3  . ASP A  1 278 ? -18.45100 -11.78300 32.69800  1.000 22.33309  ? 278 ASP A HB3  1 
ATOM   3574 N  N    . GLN A  1 279 ? -19.95200 -8.27500  31.75600  1.000 20.13343  ? 279 GLN A N    1 
ATOM   3575 C  CA   . GLN A  1 279 ? -19.42100 -7.16100  30.98100  1.000 23.72632  ? 279 GLN A CA   1 
ATOM   3576 C  C    . GLN A  1 279 ? -18.11700 -6.61200  31.54200  1.000 21.35639  ? 279 GLN A C    1 
ATOM   3577 O  O    . GLN A  1 279 ? -17.40000 -5.91200  30.81900  1.000 22.91163  ? 279 GLN A O    1 
ATOM   3578 C  CB   . GLN A  1 279 ? -20.48300 -6.06600  30.85400  1.000 26.50011  ? 279 GLN A CB   1 
ATOM   3579 C  CG   . GLN A  1 279 ? -21.67500 -6.48600  30.00000  1.000 33.79974  ? 279 GLN A CG   1 
ATOM   3580 C  CD   . GLN A  1 279 ? -21.38800 -6.39400  28.50400  1.000 59.04850  ? 279 GLN A CD   1 
ATOM   3581 O  OE1  . GLN A  1 279 ? -20.34200 -5.89300  28.08400  1.000 62.01899  ? 279 GLN A OE1  1 
ATOM   3582 N  NE2  . GLN A  1 279 ? -22.32400 -6.87400  27.69500  1.000 75.89194  ? 279 GLN A NE2  1 
ATOM   3583 H  H    . GLN A  1 279 ? -20.68400 -8.09300  32.16700  1.000 24.16268  ? 279 GLN A H    1 
ATOM   3584 H  HA   . GLN A  1 279 ? -19.21600 -7.47000  30.08400  1.000 28.47414  ? 279 GLN A HA   1 
ATOM   3585 H  HB2  . GLN A  1 279 ? -20.81300 -5.84400  31.73900  1.000 31.80269  ? 279 GLN A HB2  1 
ATOM   3586 H  HB3  . GLN A  1 279 ? -20.08200 -5.28400  30.44400  1.000 31.80269  ? 279 GLN A HB3  1 
ATOM   3587 H  HG2  . GLN A  1 279 ? -21.90300 -7.40600  30.20600  1.000 40.56225  ? 279 GLN A HG2  1 
ATOM   3588 H  HG3  . GLN A  1 279 ? -22.42600 -5.90500  30.19800  1.000 40.56225  ? 279 GLN A HG3  1 
ATOM   3589 H  HE21 . GLN A  1 279 ? -23.04300 -7.21400  28.02200  1.000 91.07289  ? 279 GLN A HE21 1 
ATOM   3590 H  HE22 . GLN A  1 279 ? -22.21100 -6.84700  26.84300  1.000 91.07289  ? 279 GLN A HE22 1 
ATOM   3591 N  N    . ARG A  1 280 ? -17.77200 -6.96500  32.78000  1.000 20.29897  ? 280 ARG A N    1 
ATOM   3592 C  CA   . ARG A  1 280 ? -16.49400 -6.54700  33.32900  1.000 21.15879  ? 280 ARG A CA   1 
ATOM   3593 C  C    . ARG A  1 280 ? -15.33000 -7.03600  32.48100  1.000 20.76540  ? 280 ARG A C    1 
ATOM   3594 O  O    . ARG A  1 280 ? -14.22500 -6.48400  32.57700  1.000 21.87700  ? 280 ARG A O    1 
ATOM   3595 C  CB   . ARG A  1 280 ? -16.31300 -7.08200  34.74400  1.000 19.98409  ? 280 ARG A CB   1 
ATOM   3596 C  CG   . ARG A  1 280 ? -17.35500 -6.60500  35.72500  1.000 21.19259  ? 280 ARG A CG   1 
ATOM   3597 C  CD   . ARG A  1 280 ? -17.17000 -7.22700  37.08600  1.000 22.01267  ? 280 ARG A CD   1 
ATOM   3598 N  NE   . ARG A  1 280 ? -17.34500 -8.67200  37.06000  1.000 20.79407  ? 280 ARG A NE   1 
ATOM   3599 C  CZ   . ARG A  1 280 ? -17.05600 -9.48300  38.07200  1.000 19.33138  ? 280 ARG A CZ   1 
ATOM   3600 N  NH1  . ARG A  1 280 ? -16.58500 -9.01000  39.23000  1.000 22.17040  ? 280 ARG A NH1  1 
ATOM   3601 N  NH2  . ARG A  1 280 ? -17.27400 -10.77900 37.94700  1.000 19.71170  ? 280 ARG A NH2  1 
ATOM   3602 H  H    . ARG A  1 280 ? -18.25500 -7.44000  33.31000  1.000 24.36133  ? 280 ARG A H    1 
ATOM   3603 H  HA   . ARG A  1 280 ? -16.48500 -5.57700  33.36400  1.000 25.39312  ? 280 ARG A HA   1 
ATOM   3604 H  HB2  . ARG A  1 280 ? -16.35700 -8.05100  34.71700  1.000 23.98347  ? 280 ARG A HB2  1 
ATOM   3605 H  HB3  . ARG A  1 280 ? -15.44700 -6.79800  35.07500  1.000 23.98347  ? 280 ARG A HB3  1 
ATOM   3606 H  HG2  . ARG A  1 280 ? -17.28900 -5.64200  35.82000  1.000 25.43367  ? 280 ARG A HG2  1 
ATOM   3607 H  HG3  . ARG A  1 280 ? -18.23600 -6.84700  35.39900  1.000 25.43367  ? 280 ARG A HG3  1 
ATOM   3608 H  HD2  . ARG A  1 280 ? -16.27300 -7.03800  37.40300  1.000 26.41776  ? 280 ARG A HD2  1 
ATOM   3609 H  HD3  . ARG A  1 280 ? -17.82300 -6.85500  37.69800  1.000 26.41776  ? 280 ARG A HD3  1 
ATOM   3610 H  HE   . ARG A  1 280 ? -17.65600 -9.02500  36.34000  1.000 24.95545  ? 280 ARG A HE   1 
ATOM   3611 H  HH11 . ARG A  1 280 ? -16.46400 -8.16500  39.33200  1.000 26.60704  ? 280 ARG A HH11 1 
ATOM   3612 H  HH12 . ARG A  1 280 ? -16.40400 -9.55100  39.87400  1.000 26.60704  ? 280 ARG A HH12 1 
ATOM   3613 H  HH21 . ARG A  1 280 ? -17.60100 -11.09100 37.21500  1.000 23.65661  ? 280 ARG A HH21 1 
ATOM   3614 H  HH22 . ARG A  1 280 ? -17.09100 -11.31100 38.59700  1.000 23.65661  ? 280 ARG A HH22 1 
ATOM   3615 N  N    . TYR A  1 281 ? -15.53000 -8.10400  31.70500  1.000 18.58475  ? 281 TYR A N    1 
ATOM   3616 C  CA   . TYR A  1 281 ? -14.45000 -8.66700  30.90000  1.000 19.00413  ? 281 TYR A CA   1 
ATOM   3617 C  C    . TYR A  1 281 ? -14.36600 -8.05900  29.50800  1.000 18.94488  ? 281 TYR A C    1 
ATOM   3618 O  O    . TYR A  1 281 ? -13.35800 -8.27800  28.81700  1.000 19.93126  ? 281 TYR A O    1 
ATOM   3619 C  CB   . TYR A  1 281 ? -14.59500 -10.19300 30.85700  1.000 17.14973  ? 281 TYR A CB   1 
ATOM   3620 C  CG   . TYR A  1 281 ? -14.20900 -10.81300 32.17600  1.000 16.56771  ? 281 TYR A CG   1 
ATOM   3621 C  CD1  . TYR A  1 281 ? -15.09800 -10.84300 33.23200  1.000 17.38143  ? 281 TYR A CD1  1 
ATOM   3622 C  CD2  . TYR A  1 281 ? -12.91800 -11.25500 32.39900  1.000 16.62608  ? 281 TYR A CD2  1 
ATOM   3623 C  CE1  . TYR A  1 281 ? -14.71300 -11.35100 34.48500  1.000 17.36726  ? 281 TYR A CE1  1 
ATOM   3624 C  CE2  . TYR A  1 281 ? -12.50900 -11.75300 33.61600  1.000 17.65136  ? 281 TYR A CE2  1 
ATOM   3625 C  CZ   . TYR A  1 281 ? -13.40800 -11.79900 34.64600  1.000 18.30144  ? 281 TYR A CZ   1 
ATOM   3626 O  OH   . TYR A  1 281 ? -12.94000 -12.32100 35.84000  1.000 19.52131  ? 281 TYR A OH   1 
ATOM   3627 H  H    . TYR A  1 281 ? -16.28100 -8.51700  31.63000  1.000 22.29438  ? 281 TYR A H    1 
ATOM   3628 H  HA   . TYR A  1 281 ? -13.59200 -8.48400  31.31400  1.000 22.80752  ? 281 TYR A HA   1 
ATOM   3629 H  HB2  . TYR A  1 281 ? -15.51800 -10.42300 30.66800  1.000 20.56687  ? 281 TYR A HB2  1 
ATOM   3630 H  HB3  . TYR A  1 281 ? -14.01600 -10.55200 30.16700  1.000 20.56687  ? 281 TYR A HB3  1 
ATOM   3631 H  HD1  . TYR A  1 281 ? -15.96300 -10.52400 33.11300  1.000 20.86028  ? 281 TYR A HD1  1 
ATOM   3632 H  HD2  . TYR A  1 281 ? -12.30400 -11.21400 31.70200  1.000 19.95386  ? 281 TYR A HD2  1 
ATOM   3633 H  HE1  . TYR A  1 281 ? -15.31800 -11.38600 35.19000  1.000 20.84327  ? 281 TYR A HE1  1 
ATOM   3634 H  HE2  . TYR A  1 281 ? -11.63600 -12.05200 33.73600  1.000 21.18419  ? 281 TYR A HE2  1 
ATOM   3635 H  HH   . TYR A  1 281 ? -13.58000 -12.44800 36.36900  1.000 23.42814  ? 281 TYR A HH   1 
ATOM   3636 N  N    . ALA A  1 282 ? -15.36900 -7.28500  29.08200  1.000 20.00780  ? 282 ALA A N    1 
ATOM   3637 C  CA   . ALA A  1 282 ? -15.31900 -6.69700  27.75100  1.000 22.05662  ? 282 ALA A CA   1 
ATOM   3638 C  C    . ALA A  1 282 ? -14.11000 -5.81400  27.51600  1.000 20.89190  ? 282 ALA A C    1 
ATOM   3639 O  O    . ALA A  1 282 ? -13.54200 -5.88500  26.41500  1.000 22.43066  ? 282 ALA A O    1 
ATOM   3640 C  CB   . ALA A  1 282 ? -16.60000 -5.91200  27.45600  1.000 24.21268  ? 282 ALA A CB   1 
ATOM   3641 H  H    . ALA A  1 282 ? -16.07300 -7.09200  29.53700  1.000 24.01193  ? 282 ALA A H    1 
ATOM   3642 H  HA   . ALA A  1 282 ? -15.26700 -7.44200  27.13200  1.000 26.47051  ? 282 ALA A HA   1 
ATOM   3643 H  HB1  . ALA A  1 282 ? -16.54000 -5.53100  26.56600  1.000 29.05778  ? 282 ALA A HB1  1 
ATOM   3644 H  HB2  . ALA A  1 282 ? -17.35900 -6.51500  27.50700  1.000 29.05778  ? 282 ALA A HB2  1 
ATOM   3645 H  HB3  . ALA A  1 282 ? -16.69600 -5.20400  28.11200  1.000 29.05778  ? 282 ALA A HB3  1 
ATOM   3646 N  N    . PRO A  1 283 ? -13.64500 -5.00300  28.46600  1.000 21.76620  ? 283 PRO A N    1 
ATOM   3647 C  CA   . PRO A  1 283 ? -12.49800 -4.11400  28.16700  1.000 22.04489  ? 283 PRO A CA   1 
ATOM   3648 C  C    . PRO A  1 283 ? -11.18700 -4.82900  27.85400  1.000 22.56856  ? 283 PRO A C    1 
ATOM   3649 O  O    . PRO A  1 283 ? -10.26500 -4.19900  27.29600  1.000 24.54683  ? 283 PRO A O    1 
ATOM   3650 C  CB   . PRO A  1 283 ? -12.38600 -3.25800  29.43400  1.000 24.13048  ? 283 PRO A CB   1 
ATOM   3651 C  CG   . PRO A  1 283 ? -13.80300 -3.23200  30.01500  1.000 24.47166  ? 283 PRO A CG   1 
ATOM   3652 C  CD   . PRO A  1 283 ? -14.30600 -4.65300  29.74600  1.000 21.59295  ? 283 PRO A CD   1 
ATOM   3653 H  HA   . PRO A  1 283 ? -12.72100 -3.55300  27.40800  1.000 26.45643  ? 283 PRO A HA   1 
ATOM   3654 H  HB2  . PRO A  1 283 ? -11.76200 -3.66600  30.05500  1.000 28.95914  ? 283 PRO A HB2  1 
ATOM   3655 H  HB3  . PRO A  1 283 ? -12.08700 -2.36400  29.20400  1.000 28.95914  ? 283 PRO A HB3  1 
ATOM   3656 H  HG2  . PRO A  1 283 ? -13.77700 -3.03900  30.96500  1.000 29.36855  ? 283 PRO A HG2  1 
ATOM   3657 H  HG3  . PRO A  1 283 ? -14.34500 -2.57100  29.55700  1.000 29.36855  ? 283 PRO A HG3  1 
ATOM   3658 H  HD2  . PRO A  1 283 ? -14.03300 -5.25800  30.45300  1.000 25.91410  ? 283 PRO A HD2  1 
ATOM   3659 H  HD3  . PRO A  1 283 ? -15.27200 -4.66700  29.65200  1.000 25.91410  ? 283 PRO A HD3  1 
ATOM   3660 N  N    . PHE A  1 284 ? -11.05100 -6.11300  28.20100  1.000 20.71902  ? 284 PHE A N    1 
ATOM   3661 C  CA   . PHE A  1 284 ? -9.85500  -6.86900  27.85500  1.000 22.04029  ? 284 PHE A CA   1 
ATOM   3662 C  C    . PHE A  1 284 ? -9.87100  -7.35000  26.42100  1.000 21.74697  ? 284 PHE A C    1 
ATOM   3663 O  O    . PHE A  1 284 ? -8.81100  -7.69600  25.89400  1.000 23.72288  ? 284 PHE A O    1 
ATOM   3664 C  CB   . PHE A  1 284 ? -9.67100  -8.04100  28.84400  1.000 19.90432  ? 284 PHE A CB   1 
ATOM   3665 C  CG   . PHE A  1 284 ? -9.53700  -7.56500  30.22300  1.000 21.85537  ? 284 PHE A CG   1 
ATOM   3666 C  CD1  . PHE A  1 284 ? -8.31200  -7.15200  30.71100  1.000 24.01264  ? 284 PHE A CD1  1 
ATOM   3667 C  CD2  . PHE A  1 284 ? -10.65300 -7.46700  31.04400  1.000 22.13776  ? 284 PHE A CD2  1 
ATOM   3668 C  CE1  . PHE A  1 284 ? -8.19800  -6.63400  31.99300  1.000 27.65590  ? 284 PHE A CE1  1 
ATOM   3669 C  CE2  . PHE A  1 284 ? -10.54400 -6.95600  32.29600  1.000 26.90838  ? 284 PHE A CE2  1 
ATOM   3670 C  CZ   . PHE A  1 284 ? -9.32000  -6.53500  32.78300  1.000 27.90463  ? 284 PHE A CZ   1 
ATOM   3671 H  H    . PHE A  1 284 ? -11.63800 -6.56500  28.63700  1.000 24.86539  ? 284 PHE A H    1 
ATOM   3672 H  HA   . PHE A  1 284 ? -9.07300  -6.30300  27.94800  1.000 26.45091  ? 284 PHE A HA   1 
ATOM   3673 H  HB2  . PHE A  1 284 ? -10.44400 -8.62500  28.79600  1.000 23.88774  ? 284 PHE A HB2  1 
ATOM   3674 H  HB3  . PHE A  1 284 ? -8.86800  -8.53400  28.61100  1.000 23.88774  ? 284 PHE A HB3  1 
ATOM   3675 H  HD1  . PHE A  1 284 ? -7.55600  -7.22200  30.17500  1.000 28.81773  ? 284 PHE A HD1  1 
ATOM   3676 H  HD2  . PHE A  1 284 ? -11.48100 -7.75500  30.73300  1.000 26.56787  ? 284 PHE A HD2  1 
ATOM   3677 H  HE1  . PHE A  1 284 ? -7.37100  -6.35700  32.31600  1.000 33.18964  ? 284 PHE A HE1  1 
ATOM   3678 H  HE2  . PHE A  1 284 ? -11.30000 -6.88800  32.83200  1.000 32.29262  ? 284 PHE A HE2  1 
ATOM   3679 H  HZ   . PHE A  1 284 ? -9.25600  -6.18500  33.64200  1.000 33.48812  ? 284 PHE A HZ   1 
ATOM   3680 N  N    . LEU A  1 285 ? -11.03100 -7.36000  25.78700  1.000 20.63355  ? 285 LEU A N    1 
ATOM   3681 C  CA   . LEU A  1 285 ? -11.21600 -7.82700  24.42000  1.000 21.71904  ? 285 LEU A CA   1 
ATOM   3682 C  C    . LEU A  1 285 ? -11.43100 -6.69400  23.44400  1.000 23.35196  ? 285 LEU A C    1 
ATOM   3683 O  O    . LEU A  1 285 ? -10.91200 -6.75100  22.33000  1.000 24.70673  ? 285 LEU A O    1 
ATOM   3684 C  CB   . LEU A  1 285 ? -12.43900 -8.75000  24.34500  1.000 20.32379  ? 285 LEU A CB   1 
ATOM   3685 C  CG   . LEU A  1 285 ? -12.21400 -10.08000 25.05900  1.000 19.92042  ? 285 LEU A CG   1 
ATOM   3686 C  CD1  . LEU A  1 285 ? -13.54900 -10.73400 25.40800  1.000 21.07022  ? 285 LEU A CD1  1 
ATOM   3687 C  CD2  . LEU A  1 285 ? -11.36500 -10.99300 24.20100  1.000 21.06322  ? 285 LEU A CD2  1 
ATOM   3688 H  H    . LEU A  1 285 ? -11.76500 -7.08800  26.14500  1.000 24.76282  ? 285 LEU A H    1 
ATOM   3689 H  HA   . LEU A  1 285 ? -10.43100 -8.33000  24.15200  1.000 26.06540  ? 285 LEU A HA   1 
ATOM   3690 H  HB2  . LEU A  1 285 ? -13.19500 -8.30800  24.76300  1.000 24.39111  ? 285 LEU A HB2  1 
ATOM   3691 H  HB3  . LEU A  1 285 ? -12.63700 -8.93700  23.41400  1.000 24.39111  ? 285 LEU A HB3  1 
ATOM   3692 H  HG   . LEU A  1 285 ? -11.74000 -9.92400  25.89100  1.000 23.90706  ? 285 LEU A HG   1 
ATOM   3693 H  HD11 . LEU A  1 285 ? -13.37900 -11.57000 25.87000  1.000 25.28683  ? 285 LEU A HD11 1 
ATOM   3694 H  HD12 . LEU A  1 285 ? -14.05300 -10.13500 25.98200  1.000 25.28683  ? 285 LEU A HD12 1 
ATOM   3695 H  HD13 . LEU A  1 285 ? -14.04200 -10.90100 24.59000  1.000 25.28683  ? 285 LEU A HD13 1 
ATOM   3696 H  HD21 . LEU A  1 285 ? -11.26300 -11.84600 24.65200  1.000 25.27842  ? 285 LEU A HD21 1 
ATOM   3697 H  HD22 . LEU A  1 285 ? -11.80400 -11.12200 23.34600  1.000 25.27842  ? 285 LEU A HD22 1 
ATOM   3698 H  HD23 . LEU A  1 285 ? -10.49600 -10.58400 24.06800  1.000 25.27842  ? 285 LEU A HD23 1 
ATOM   3699 N  N    . CYS A  1 286 ? -12.21500 -5.68000  23.81800  1.000 22.91413  ? 286 CYS A N    1 
ATOM   3700 C  CA   . CYS A  1 286 ? -12.56500 -4.56300  22.95600  1.000 24.07874  ? 286 CYS A CA   1 
ATOM   3701 C  C    . CYS A  1 286 ? -12.01100 -3.30000  23.57900  1.000 27.82883  ? 286 CYS A C    1 
ATOM   3702 O  O    . CYS A  1 286 ? -12.41400 -2.92300  24.68500  1.000 28.85460  ? 286 CYS A O    1 
ATOM   3703 C  CB   . CYS A  1 286 ? -14.07400 -4.47400  22.80600  1.000 30.31634  ? 286 CYS A CB   1 
ATOM   3704 S  SG   . CYS A  1 286 ? -14.80600 -5.89300  21.97000  1.000 32.74492  ? 286 CYS A SG   1 
ATOM   3705 H  H    . CYS A  1 286 ? -12.56800 -5.62000  24.60000  1.000 27.49951  ? 286 CYS A H    1 
ATOM   3706 H  HA   . CYS A  1 286 ? -12.17100 -4.67100  22.07600  1.000 28.89705  ? 286 CYS A HA   1 
ATOM   3707 H  HB2  . CYS A  1 286 ? -14.47200 -4.41300  23.68800  1.000 36.38216  ? 286 CYS A HB2  1 
ATOM   3708 H  HB3  . CYS A  1 286 ? -14.29000 -3.68300  22.28900  1.000 36.38216  ? 286 CYS A HB3  1 
ATOM   3709 N  N    . GLY A  1 287 ? -11.07400 -2.67600  22.88000  1.000 29.17677  ? 287 GLY A N    1 
ATOM   3710 C  CA   . GLY A  1 287 ? -10.46400 -1.44600  23.32800  1.000 30.02206  ? 287 GLY A CA   1 
ATOM   3711 C  C    . GLY A  1 287 ? -8.95700  -1.47100  23.16400  1.000 32.57115  ? 287 GLY A C    1 
ATOM   3712 O  O    . GLY A  1 287 ? -8.36700  -0.57300  22.56700  1.000 31.90633  ? 287 GLY A O    1 
ATOM   3713 H  H    . GLY A  1 287 ? -10.77000 -2.95500  22.12500  1.000 35.01469  ? 287 GLY A H    1 
ATOM   3714 H  HA2  . GLY A  1 287 ? -10.81800 -0.70400  22.81400  1.000 36.02904  ? 287 GLY A HA2  1 
ATOM   3715 H  HA3  . GLY A  1 287 ? -10.66900 -1.30700  24.26600  1.000 36.02904  ? 287 GLY A HA3  1 
ATOM   3716 N  N    . PRO A  1 288 ? -8.30100  -2.50400  23.69200  1.000 28.72737  ? 288 PRO A N    1 
ATOM   3717 C  CA   . PRO A  1 288 ? -6.83100  -2.56000  23.61700  1.000 26.09408  ? 288 PRO A CA   1 
ATOM   3718 C  C    . PRO A  1 288 ? -6.30600  -2.68400  22.19300  1.000 29.94083  ? 288 PRO A C    1 
ATOM   3719 O  O    . PRO A  1 288 ? -6.93200  -3.27900  21.31200  1.000 27.38675  ? 288 PRO A O    1 
ATOM   3720 C  CB   . PRO A  1 288 ? -6.47700  -3.82300  24.42500  1.000 27.28410  ? 288 PRO A CB   1 
ATOM   3721 C  CG   . PRO A  1 288 ? -7.65000  -3.98800  25.36900  1.000 31.27640  ? 288 PRO A CG   1 
ATOM   3722 C  CD   . PRO A  1 288 ? -8.84400  -3.55900  24.56000  1.000 29.24066  ? 288 PRO A CD   1 
ATOM   3723 H  HA   . PRO A  1 288 ? -6.45700  -1.76500  24.02900  1.000 31.31545  ? 288 PRO A HA   1 
ATOM   3724 H  HB2  . PRO A  1 288 ? -6.39200  -4.58700  23.83300  1.000 32.74348  ? 288 PRO A HB2  1 
ATOM   3725 H  HB3  . PRO A  1 288 ? -5.65000  -3.68800  24.91300  1.000 32.74348  ? 288 PRO A HB3  1 
ATOM   3726 H  HG2  . PRO A  1 288 ? -7.73000  -4.91600  25.64300  1.000 37.53424  ? 288 PRO A HG2  1 
ATOM   3727 H  HG3  . PRO A  1 288 ? -7.53400  -3.42100  26.14800  1.000 37.53424  ? 288 PRO A HG3  1 
ATOM   3728 H  HD2  . PRO A  1 288 ? -9.18700  -4.29700  24.03300  1.000 35.09136  ? 288 PRO A HD2  1 
ATOM   3729 H  HD3  . PRO A  1 288 ? -9.54200  -3.20800  25.13400  1.000 35.09136  ? 288 PRO A HD3  1 
ATOM   3730 N  N    . ASN A  1 289 ? -5.10700  -2.15000  21.97800  1.000 29.95645  ? 289 ASN A N    1 
ATOM   3731 C  CA   . ASN A  1 289 ? -4.41900  -2.28100  20.69100  1.000 28.36489  ? 289 ASN A CA   1 
ATOM   3732 C  C    . ASN A  1 289 ? -3.59800  -3.56800  20.75700  1.000 29.66174  ? 289 ASN A C    1 
ATOM   3733 O  O    . ASN A  1 289 ? -2.38200  -3.56700  20.93200  1.000 29.54375  ? 289 ASN A O    1 
ATOM   3734 C  CB   . ASN A  1 289 ? -3.56900  -1.04900  20.40600  1.000 31.91764  ? 289 ASN A CB   1 
ATOM   3735 C  CG   . ASN A  1 289 ? -3.00600  -1.04600  18.99600  1.000 48.37059  ? 289 ASN A CG   1 
ATOM   3736 O  OD1  . ASN A  1 289 ? -3.40100  -1.85100  18.15500  1.000 41.89540  ? 289 ASN A OD1  1 
ATOM   3737 N  ND2  . ASN A  1 289 ? -2.09200  -0.11900  18.72500  1.000 53.48234  ? 289 ASN A ND2  1 
ATOM   3738 H  H    . ASN A  1 289 ? -4.66600  -1.70300  22.56600  1.000 35.95030  ? 289 ASN A H    1 
ATOM   3739 H  HA   . ASN A  1 289 ? -5.06100  -2.35600  19.96800  1.000 34.04043  ? 289 ASN A HA   1 
ATOM   3740 H  HB2  . ASN A  1 289 ? -4.11600  -0.25500  20.51400  1.000 38.30373  ? 289 ASN A HB2  1 
ATOM   3741 H  HB3  . ASN A  1 289 ? -2.82500  -1.02600  21.02800  1.000 38.30373  ? 289 ASN A HB3  1 
ATOM   3742 H  HD21 . ASN A  1 289 ? -1.74200  -0.07600  17.94100  1.000 64.18137  ? 289 ASN A HD21 1 
ATOM   3743 H  HD22 . ASN A  1 289 ? -1.84900  0.43700   19.33500  1.000 64.18137  ? 289 ASN A HD22 1 
ATOM   3744 N  N    . HIS A  1 290 ? -4.30100  -4.69000  20.58800  1.000 27.94247  ? 290 HIS A N    1 
ATOM   3745 C  CA   . HIS A  1 290 ? -3.70500  -6.00000  20.82900  1.000 28.19290  ? 290 HIS A CA   1 
ATOM   3746 C  C    . HIS A  1 290 ? -2.44000  -6.21200  19.99800  1.000 23.74352  ? 290 HIS A C    1 
ATOM   3747 O  O    . HIS A  1 290 ? -1.48600  -6.85300  20.46300  1.000 25.00682  ? 290 HIS A O    1 
ATOM   3748 C  CB   . HIS A  1 290 ? -4.73000  -7.09200  20.52300  1.000 23.38038  ? 290 HIS A CB   1 
ATOM   3749 C  CG   . HIS A  1 290 ? -6.02300  -6.94500  21.23700  1.000 23.40554  ? 290 HIS A CG   1 
ATOM   3750 N  ND1  . HIS A  1 290 ? -6.17100  -7.22900  22.57600  1.000 23.21278  ? 290 HIS A ND1  1 
ATOM   3751 C  CD2  . HIS A  1 290 ? -7.24900  -6.56700  20.79700  1.000 25.40200  ? 290 HIS A CD2  1 
ATOM   3752 C  CE1  . HIS A  1 290 ? -7.42500  -7.01400  22.93700  1.000 24.15031  ? 290 HIS A CE1  1 
ATOM   3753 N  NE2  . HIS A  1 290 ? -8.09600  -6.59300  21.87800  1.000 24.73769  ? 290 HIS A NE2  1 
ATOM   3754 H  H    . HIS A  1 290 ? -5.12200  -4.71900  20.33600  1.000 33.53353  ? 290 HIS A H    1 
ATOM   3755 H  HA   . HIS A  1 290 ? -3.45500  -6.05800  21.76400  1.000 33.83405  ? 290 HIS A HA   1 
ATOM   3756 H  HB2  . HIS A  1 290 ? -4.91800  -7.08100  19.57200  1.000 28.05902  ? 290 HIS A HB2  1 
ATOM   3757 H  HB3  . HIS A  1 290 ? -4.35200  -7.94900  20.77700  1.000 28.05902  ? 290 HIS A HB3  1 
ATOM   3758 H  HD2  . HIS A  1 290 ? -7.47400  -6.33300  19.92500  1.000 30.48496  ? 290 HIS A HD2  1 
ATOM   3759 H  HE1  . HIS A  1 290 ? -7.77400  -7.13700  23.79000  1.000 28.98293  ? 290 HIS A HE1  1 
ATOM   3760 H  HE2  . HIS A  1 290 ? -8.92700  -6.37200  21.86800  1.000 29.68779  ? 290 HIS A HE2  1 
ATOM   3761 N  N    . GLU A  1 291 ? -2.39800  -5.69400  18.77600  1.000 26.67180  ? 291 GLU A N    1 
ATOM   3762 C  CA   . GLU A  1 291 ? -1.25400  -5.94700  17.90600  1.000 27.56811  ? 291 GLU A CA   1 
ATOM   3763 C  C    . GLU A  1 291 ? 0.02900   -5.28400  18.38600  1.000 28.66001  ? 291 GLU A C    1 
ATOM   3764 O  O    . GLU A  1 291 ? 1.10800   -5.58200  17.83900  1.000 28.63555  ? 291 GLU A O    1 
ATOM   3765 C  CB   . GLU A  1 291 ? -1.56000  -5.51800  16.46900  1.000 27.87204  ? 291 GLU A CB   1 
ATOM   3766 C  CG   . GLU A  1 291 ? -2.48500  -6.47000  15.71500  1.000 33.22216  ? 291 GLU A CG   1 
ATOM   3767 C  CD   . GLU A  1 291 ? -2.81400  -5.96300  14.32400  1.000 36.71316  ? 291 GLU A CD   1 
ATOM   3768 O  OE1  . GLU A  1 291 ? -2.17200  -4.98000  13.87000  1.000 42.88847  ? 291 GLU A OE1  1 
ATOM   3769 O  OE2  . GLU A  1 291 ? -3.69700  -6.53500  13.66700  1.000 27.99057  ? 291 GLU A OE2  1 
ATOM   3770 H  H    . GLU A  1 291 ? -3.01000  -5.19800  18.43100  1.000 32.00872  ? 291 GLU A H    1 
ATOM   3771 H  HA   . GLU A  1 291 ? -1.09900  -6.90500  17.89600  1.000 33.08429  ? 291 GLU A HA   1 
ATOM   3772 H  HB2  . GLU A  1 291 ? -1.98700  -4.64700  16.48900  1.000 33.44901  ? 291 GLU A HB2  1 
ATOM   3773 H  HB3  . GLU A  1 291 ? -0.72600  -5.46700  15.97600  1.000 33.44901  ? 291 GLU A HB3  1 
ATOM   3774 H  HG2  . GLU A  1 291 ? -2.05200  -7.33400  15.62800  1.000 39.86916  ? 291 GLU A HG2  1 
ATOM   3775 H  HG3  . GLU A  1 291 ? -3.31600  -6.56300  16.20800  1.000 39.86916  ? 291 GLU A HG3  1 
ATOM   3776 N  N    . ARG A  1 292 ? -0.04300  -4.36100  19.34800  1.000 29.10049  ? 292 ARG A N    1 
ATOM   3777 C  CA   . ARG A  1 292 ? 1.19400   -3.79100  19.89500  1.000 30.82068  ? 292 ARG A CA   1 
ATOM   3778 C  C    . ARG A  1 292 ? 2.00000   -4.85400  20.62900  1.000 38.72690  ? 292 ARG A C    1 
ATOM   3779 O  O    . ARG A  1 292 ? 3.22900   -4.76700  20.69000  1.000 39.21767  ? 292 ARG A O    1 
ATOM   3780 C  CB   . ARG A  1 292 ? 0.88100   -2.64600  20.86000  1.000 36.11905  ? 292 ARG A CB   1 
ATOM   3781 C  CG   . ARG A  1 292 ? 0.57200   -1.31800  20.21000  1.000 62.53296  ? 292 ARG A CG   1 
ATOM   3782 C  CD   . ARG A  1 292 ? 1.81500   -0.67400  19.60200  1.000 75.34311  ? 292 ARG A CD   1 
ATOM   3783 N  NE   . ARG A  1 292 ? 2.07700   -1.19400  18.26600  1.000 88.09027  ? 292 ARG A NE   1 
ATOM   3784 C  CZ   . ARG A  1 292 ? 1.45700   -0.78100  17.16900  1.000 84.88201  ? 292 ARG A CZ   1 
ATOM   3785 N  NH1  . ARG A  1 292 ? 0.56000   0.19200   17.20700  1.000 79.11632  ? 292 ARG A NH1  1 
ATOM   3786 N  NH2  . ARG A  1 292 ? 1.74300   -1.35900  16.00600  1.000 81.18651  ? 292 ARG A NH2  1 
ATOM   3787 H  H    . ARG A  1 292 ? -0.77000  -4.05600  19.69300  1.000 34.92315  ? 292 ARG A H    1 
ATOM   3788 H  HA   . ARG A  1 292 ? 1.71800   -3.43400  19.16000  1.000 36.98737  ? 292 ARG A HA   1 
ATOM   3789 H  HB2  . ARG A  1 292 ? 0.10700   -2.89600  21.39000  1.000 43.34542  ? 292 ARG A HB2  1 
ATOM   3790 H  HB3  . ARG A  1 292 ? 1.64900   -2.51400  21.43700  1.000 43.34542  ? 292 ARG A HB3  1 
ATOM   3791 H  HG2  . ARG A  1 292 ? -0.07600  -1.45300  19.50100  1.000 75.04211  ? 292 ARG A HG2  1 
ATOM   3792 H  HG3  . ARG A  1 292 ? 0.21200   -0.71200  20.87600  1.000 75.04211  ? 292 ARG A HG3  1 
ATOM   3793 H  HD2  . ARG A  1 292 ? 1.68200   0.28400   19.53800  1.000 90.41430  ? 292 ARG A HD2  1 
ATOM   3794 H  HD3  . ARG A  1 292 ? 2.58300   -0.86600  20.16200  1.000 90.41430  ? 292 ARG A HD3  1 
ATOM   3795 H  HE   . ARG A  1 292 ? 2.67200   -1.80900  18.18400  1.000 105.71089 ? 292 ARG A HE   1 
ATOM   3796 H  HH11 . ARG A  1 292 ? 0.36700   0.57100   17.95500  1.000 94.94215  ? 292 ARG A HH11 1 
ATOM   3797 H  HH12 . ARG A  1 292 ? 0.16900   0.44500   16.48400  1.000 94.94215  ? 292 ARG A HH12 1 
ATOM   3798 H  HH21 . ARG A  1 292 ? 2.32400   -1.99300  15.97200  1.000 97.42638  ? 292 ARG A HH21 1 
ATOM   3799 H  HH22 . ARG A  1 292 ? 1.34800   -1.10000  15.28700  1.000 97.42638  ? 292 ARG A HH22 1 
ATOM   3800 N  N    A ASP A  1 293 ? 1.33500   -5.86500  21.16600  0.448 32.34879  ? 293 ASP A N    1 
ATOM   3801 N  N    B ASP A  1 293 ? 1.32500   -5.85000  21.20300  0.552 31.99661  ? 293 ASP A N    1 
ATOM   3802 C  CA   A ASP A  1 293 ? 2.06500   -6.92500  21.84000  0.448 37.80526  ? 293 ASP A CA   1 
ATOM   3803 C  CA   B ASP A  1 293 ? 1.97800   -7.00800  21.81900  0.552 36.47834  ? 293 ASP A CA   1 
ATOM   3804 C  C    A ASP A  1 293 ? 2.84700   -7.72300  20.81100  0.448 34.65159  ? 293 ASP A C    1 
ATOM   3805 C  C    B ASP A  1 293 ? 2.83200   -7.74000  20.78900  0.552 34.32085  ? 293 ASP A C    1 
ATOM   3806 O  O    A ASP A  1 293 ? 2.31300   -8.11900  19.77200  0.448 26.80619  ? 293 ASP A O    1 
ATOM   3807 O  O    B ASP A  1 293 ? 2.34100   -8.11800  19.72300  0.552 26.14578  ? 293 ASP A O    1 
ATOM   3808 C  CB   A ASP A  1 293 ? 1.14000   -7.85200  22.60400  0.448 31.61606  ? 293 ASP A CB   1 
ATOM   3809 C  CB   B ASP A  1 293 ? 0.86400   -7.93900  22.32400  0.552 30.95903  ? 293 ASP A CB   1 
ATOM   3810 C  CG   A ASP A  1 293 ? 1.89200   -8.68800  23.62100  0.448 41.08214  ? 293 ASP A CG   1 
ATOM   3811 C  CG   B ASP A  1 293 ? 1.36000   -9.04500  23.24900  0.552 40.16066  ? 293 ASP A CG   1 
ATOM   3812 O  OD1  A ASP A  1 293 ? 2.23300   -8.13600  24.69500  0.448 26.24490  ? 293 ASP A OD1  1 
ATOM   3813 O  OD1  B ASP A  1 293 ? 2.54800   -9.44800  23.14900  0.552 26.65051  ? 293 ASP A OD1  1 
ATOM   3814 O  OD2  A ASP A  1 293 ? 2.16900   -9.87400  23.33000  0.448 29.75486  ? 293 ASP A OD2  1 
ATOM   3815 O  OD2  B ASP A  1 293 ? 0.54100   -9.50400  24.06900  0.552 34.20333  ? 293 ASP A OD2  1 
ATOM   3816 H  H    A ASP A  1 293 ? 0.48000   -5.95900  21.15400  0.448 38.82111  ? 293 ASP A H    1 
ATOM   3817 H  H    B ASP A  1 293 ? 0.46600   -5.88100  21.25100  0.552 38.39849  ? 293 ASP A H    1 
ATOM   3818 H  HA   A ASP A  1 293 ? 2.66900   -6.52600  22.48500  0.448 45.36888  ? 293 ASP A HA   1 
ATOM   3819 H  HA   B ASP A  1 293 ? 2.55500   -6.73900  22.55000  0.552 43.77657  ? 293 ASP A HA   1 
ATOM   3820 H  HB2  A ASP A  1 293 ? 0.47700   -7.32400  23.07600  0.448 37.94184  ? 293 ASP A HB2  1 
ATOM   3821 H  HB2  B ASP A  1 293 ? 0.21500   -7.41200  22.81600  0.552 37.15339  ? 293 ASP A HB2  1 
ATOM   3822 H  HB3  A ASP A  1 293 ? 0.70300   -8.45300  21.98100  0.448 37.94184  ? 293 ASP A HB3  1 
ATOM   3823 H  HB3  B ASP A  1 293 ? 0.43900   -8.36100  21.56100  0.552 37.15339  ? 293 ASP A HB3  1 
ATOM   3824 N  N    . ARG A  1 294 ? 4.12200   -7.94600  21.10200  1.000 29.80720  ? 294 ARG A N    1 
ATOM   3825 C  CA   . ARG A  1 294 ? 4.98000   -8.69000  20.19700  1.000 32.18511  ? 294 ARG A CA   1 
ATOM   3826 C  C    . ARG A  1 294 ? 4.46800   -10.09600 19.92200  1.000 22.93680  ? 294 ARG A C    1 
ATOM   3827 O  O    . ARG A  1 294 ? 4.75800   -10.64200 18.84300  1.000 26.58213  ? 294 ARG A O    1 
ATOM   3828 C  CB   . ARG A  1 294 ? 6.41400   -8.77000  20.73600  1.000 36.74605  ? 294 ARG A CB   1 
ATOM   3829 C  CG   . ARG A  1 294 ? 7.17600   -7.44700  20.69300  1.000 61.24706  ? 294 ARG A CG   1 
ATOM   3830 C  CD   . ARG A  1 294 ? 8.67900   -7.64500  20.89600  1.000 68.62850  ? 294 ARG A CD   1 
ATOM   3831 N  NE   . ARG A  1 294 ? 8.99700   -8.25100  22.18500  1.000 86.01779  ? 294 ARG A NE   1 
ATOM   3832 C  CZ   . ARG A  1 294 ? 9.09500   -7.57900  23.32500  1.000 93.80824  ? 294 ARG A CZ   1 
ATOM   3833 N  NH1  . ARG A  1 294 ? 8.87100   -6.27500  23.38000  1.000 96.61681  ? 294 ARG A NH1  1 
ATOM   3834 N  NH2  . ARG A  1 294 ? 9.42400   -8.23200  24.43800  1.000 86.58866  ? 294 ARG A NH2  1 
ATOM   3835 H  H    . ARG A  1 294 ? 4.50400   -7.66700  21.82000  1.000 35.77120  ? 294 ARG A H    1 
ATOM   3836 H  HA   . ARG A  1 294 ? 5.00300   -8.20400  19.35800  1.000 38.62469  ? 294 ARG A HA   1 
ATOM   3837 H  HB2  . ARG A  1 294 ? 6.38200   -9.06100  21.66100  1.000 44.09782  ? 294 ARG A HB2  1 
ATOM   3838 H  HB3  . ARG A  1 294 ? 6.91000   -9.41200  20.20400  1.000 44.09782  ? 294 ARG A HB3  1 
ATOM   3839 H  HG2  . ARG A  1 294 ? 7.03900   -7.02800  19.82900  1.000 73.49904  ? 294 ARG A HG2  1 
ATOM   3840 H  HG3  . ARG A  1 294 ? 6.84900   -6.86700  21.39800  1.000 73.49904  ? 294 ARG A HG3  1 
ATOM   3841 H  HD2  . ARG A  1 294 ? 9.01900   -8.22800  20.19900  1.000 82.35677  ? 294 ARG A HD2  1 
ATOM   3842 H  HD3  . ARG A  1 294 ? 9.12100   -6.78300  20.85200  1.000 82.35677  ? 294 ARG A HD3  1 
ATOM   3843 H  HE   . ARG A  1 294 ? 9.13100   -9.10000  22.20700  1.000 103.22391 ? 294 ARG A HE   1 
ATOM   3844 H  HH11 . ARG A  1 294 ? 8.65800   -5.84500  22.66600  1.000 115.94273 ? 294 ARG A HH11 1 
ATOM   3845 H  HH12 . ARG A  1 294 ? 8.94000   -5.85800  24.12900  1.000 115.94273 ? 294 ARG A HH12 1 
ATOM   3846 H  HH21 . ARG A  1 294 ? 9.57000   -9.07900  24.41200  1.000 103.90896 ? 294 ARG A HH21 1 
ATOM   3847 H  HH22 . ARG A  1 294 ? 9.49000   -7.80600  25.18200  1.000 103.90896 ? 294 ARG A HH22 1 
ATOM   3848 N  N    . GLN A  1 295 ? 3.65300   -10.65500 20.81300  1.000 23.45595  ? 295 GLN A N    1 
ATOM   3849 C  CA   . GLN A  1 295 ? 3.13200   -11.98900 20.59600  1.000 19.41321  ? 295 GLN A CA   1 
ATOM   3850 C  C    . GLN A  1 295 ? 1.95200   -12.04000 19.65200  1.000 20.44410  ? 295 GLN A C    1 
ATOM   3851 O  O    . GLN A  1 295 ? 1.52700   -13.13400 19.27400  1.000 21.50553  ? 295 GLN A O    1 
ATOM   3852 C  CB   . GLN A  1 295 ? 2.70500   -12.64100 21.90500  1.000 20.61842  ? 295 GLN A CB   1 
ATOM   3853 C  CG   . GLN A  1 295 ? 3.82400   -12.79500 22.89800  1.000 25.62847  ? 295 GLN A CG   1 
ATOM   3854 C  CD   . GLN A  1 295 ? 3.24700   -13.02400 24.25000  1.000 26.35469  ? 295 GLN A CD   1 
ATOM   3855 O  OE1  . GLN A  1 295 ? 3.22000   -14.14500 24.73000  1.000 25.49874  ? 295 GLN A OE1  1 
ATOM   3856 N  NE2  . GLN A  1 295 ? 2.72100   -11.95400 24.86500  1.000 28.47053  ? 295 GLN A NE2  1 
ATOM   3857 H  H    . GLN A  1 295 ? 3.39200   -10.28100 21.54300  1.000 28.14971  ? 295 GLN A H    1 
ATOM   3858 H  HA   . GLN A  1 295 ? 3.86000   -12.50600 20.21600  1.000 23.29842  ? 295 GLN A HA   1 
ATOM   3859 H  HB2  . GLN A  1 295 ? 2.01700   -12.09400 22.31600  1.000 24.74467  ? 295 GLN A HB2  1 
ATOM   3860 H  HB3  . GLN A  1 295 ? 2.35500   -13.52500 21.71400  1.000 24.74467  ? 295 GLN A HB3  1 
ATOM   3861 H  HG2  . GLN A  1 295 ? 4.37600   -13.55500 22.65800  1.000 30.75673  ? 295 GLN A HG2  1 
ATOM   3862 H  HG3  . GLN A  1 295 ? 4.36200   -11.98800 22.91700  1.000 30.75673  ? 295 GLN A HG3  1 
ATOM   3863 H  HE21 . GLN A  1 295 ? 2.72900   -11.18700 24.47600  1.000 34.16720  ? 295 GLN A HE21 1 
ATOM   3864 H  HE22 . GLN A  1 295 ? 2.37500   -12.03500 25.64800  1.000 34.16720  ? 295 GLN A HE22 1 
ATOM   3865 N  N    . ILE A  1 296 ? 1.37600   -10.90200 19.28000  1.000 21.13086  ? 296 ILE A N    1 
ATOM   3866 C  CA   . ILE A  1 296 ? 0.17000   -10.86500 18.45000  1.000 21.92589  ? 296 ILE A CA   1 
ATOM   3867 C  C    . ILE A  1 296 ? 0.53000   -10.24000 17.11600  1.000 22.31192  ? 296 ILE A C    1 
ATOM   3868 O  O    . ILE A  1 296 ? 0.75900   -9.02600  17.03600  1.000 24.70951  ? 296 ILE A O    1 
ATOM   3869 C  CB   . ILE A  1 296 ? -0.95300  -10.07800 19.13700  1.000 21.65080  ? 296 ILE A CB   1 
ATOM   3870 C  CG1  . ILE A  1 296 ? -1.34700  -10.76000 20.43800  1.000 23.36188  ? 296 ILE A CG1  1 
ATOM   3871 C  CG2  . ILE A  1 296 ? -2.16000  -9.93400  18.20400  1.000 22.76485  ? 296 ILE A CG2  1 
ATOM   3872 C  CD1  . ILE A  1 296 ? -1.97300  -12.12000 20.25500  1.000 29.75315  ? 296 ILE A CD1  1 
ATOM   3873 H  H    . ILE A  1 296 ? 1.66900   -10.12400 19.49800  1.000 25.35960  ? 296 ILE A H    1 
ATOM   3874 H  HA   . ILE A  1 296 ? -0.12900  -11.77200 18.28000  1.000 26.31363  ? 296 ILE A HA   1 
ATOM   3875 H  HB   . ILE A  1 296 ? -0.62800  -9.18800  19.34300  1.000 25.98352  ? 296 ILE A HB   1 
ATOM   3876 H  HG12 . ILE A  1 296 ? -0.55200  -10.87200 20.98200  1.000 28.03682  ? 296 ILE A HG12 1 
ATOM   3877 H  HG13 . ILE A  1 296 ? -1.98900  -10.19900 20.90000  1.000 28.03682  ? 296 ILE A HG13 1 
ATOM   3878 H  HG21 . ILE A  1 296 ? -2.94300  -9.71600  18.73300  1.000 27.32038  ? 296 ILE A HG21 1 
ATOM   3879 H  HG22 . ILE A  1 296 ? -1.98300  -9.22500  17.56600  1.000 27.32038  ? 296 ILE A HG22 1 
ATOM   3880 H  HG23 . ILE A  1 296 ? -2.29900  -10.77300 17.73600  1.000 27.32038  ? 296 ILE A HG23 1 
ATOM   3881 H  HD11 . ILE A  1 296 ? -2.31300  -12.42900 21.11000  1.000 35.70634  ? 296 ILE A HD11 1 
ATOM   3882 H  HD12 . ILE A  1 296 ? -2.70000  -12.05100 19.61600  1.000 35.70634  ? 296 ILE A HD12 1 
ATOM   3883 H  HD13 . ILE A  1 296 ? -1.30000  -12.73600 19.92500  1.000 35.70634  ? 296 ILE A HD13 1 
ATOM   3884 N  N    . SER A  1 297 ? 0.55000   -11.04900 16.04600  1.000 20.93115  ? 297 SER A N    1 
ATOM   3885 C  CA   . SER A  1 297 ? 0.86300   -10.55100 14.71900  1.000 21.46288  ? 297 SER A CA   1 
ATOM   3886 C  C    . SER A  1 297 ? -0.33700  -9.98600  13.98300  1.000 21.61630  ? 297 SER A C    1 
ATOM   3887 O  O    . SER A  1 297 ? -0.16300  -9.16500  13.07700  1.000 24.77080  ? 297 SER A O    1 
ATOM   3888 C  CB   . SER A  1 297 ? 1.51600   -11.65300 13.86600  1.000 22.34432  ? 297 SER A CB   1 
ATOM   3889 O  OG   . SER A  1 297 ? 0.85600   -12.88600 14.02300  1.000 23.18831  ? 297 SER A OG   1 
ATOM   3890 H  H    . SER A  1 297 ? 0.38300   -11.89200 16.07300  1.000 25.11994  ? 297 SER A H    1 
ATOM   3891 H  HA   . SER A  1 297 ? 1.50900   -9.83300  14.81400  1.000 25.75801  ? 297 SER A HA   1 
ATOM   3892 H  HB2  . SER A  1 297 ? 1.47400   -11.39200 12.93200  1.000 26.81574  ? 297 SER A HB2  1 
ATOM   3893 H  HB3  . SER A  1 297 ? 2.44000   -11.75500 14.14100  1.000 26.81574  ? 297 SER A HB3  1 
ATOM   3894 H  HG   . SER A  1 297 ? 0.14400   -12.89000 13.57600  1.000 27.82853  ? 297 SER A HG   1 
ATOM   3895 N  N    . GLU A  1 298 ? -1.54600  -10.38400 14.38000  1.000 22.33793  ? 298 GLU A N    1 
ATOM   3896 C  CA   . GLU A  1 298 ? -2.74700  -9.82400  13.77600  1.000 23.01242  ? 298 GLU A CA   1 
ATOM   3897 C  C    . GLU A  1 298 ? -3.90500  -9.96500  14.75300  1.000 20.31390  ? 298 GLU A C    1 
ATOM   3898 O  O    . GLU A  1 298 ? -4.00500  -10.97000 15.46600  1.000 20.36127  ? 298 GLU A O    1 
ATOM   3899 C  CB   . GLU A  1 298 ? -3.13200  -10.52400 12.46000  1.000 22.53326  ? 298 GLU A CB   1 
ATOM   3900 C  CG   . GLU A  1 298 ? -4.21400  -9.75600  11.74400  1.000 25.62924  ? 298 GLU A CG   1 
ATOM   3901 C  CD   . GLU A  1 298 ? -4.68700  -10.35700 10.44200  1.000 26.88426  ? 298 GLU A CD   1 
ATOM   3902 O  OE1  . GLU A  1 298 ? -4.28100  -11.46500 10.07300  1.000 28.83140  ? 298 GLU A OE1  1 
ATOM   3903 O  OE2  . GLU A  1 298 ? -5.54500  -9.71900  9.80900   1.000 28.30299  ? 298 GLU A OE2  1 
ATOM   3904 H  H    . GLU A  1 298 ? -1.69200  -10.97200 14.99000  1.000 26.80808  ? 298 GLU A H    1 
ATOM   3905 H  HA   . GLU A  1 298 ? -2.57900  -8.88600  13.59400  1.000 27.61747  ? 298 GLU A HA   1 
ATOM   3906 H  HB2  . GLU A  1 298 ? -2.35500  -10.57500 11.88200  1.000 27.04247  ? 298 GLU A HB2  1 
ATOM   3907 H  HB3  . GLU A  1 298 ? -3.46200  -11.41600 12.65200  1.000 27.04247  ? 298 GLU A HB3  1 
ATOM   3908 H  HG2  . GLU A  1 298 ? -4.98400  -9.69500  12.33000  1.000 30.75765  ? 298 GLU A HG2  1 
ATOM   3909 H  HG3  . GLU A  1 298 ? -3.87700  -8.86800  11.54600  1.000 30.75765  ? 298 GLU A HG3  1 
ATOM   3910 N  N    . HIS A  1 299 ? -4.76300  -8.95700  14.78800  1.000 21.77827  ? 299 HIS A N    1 
ATOM   3911 C  CA   . HIS A  1 299 ? -6.01700  -9.05200  15.51800  1.000 21.43142  ? 299 HIS A CA   1 
ATOM   3912 C  C    . HIS A  1 299 ? -7.13700  -8.53500  14.63800  1.000 22.71858  ? 299 HIS A C    1 
ATOM   3913 O  O    . HIS A  1 299 ? -6.97000  -7.52400  13.95300  1.000 24.65976  ? 299 HIS A O    1 
ATOM   3914 C  CB   . HIS A  1 299 ? -5.97700  -8.22700  16.79500  1.000 23.80027  ? 299 HIS A CB   1 
ATOM   3915 C  CG   . HIS A  1 299 ? -7.29400  -8.15500  17.50000  1.000 22.13285  ? 299 HIS A CG   1 
ATOM   3916 N  ND1  . HIS A  1 299 ? -8.11300  -7.04500  17.45400  1.000 29.02696  ? 299 HIS A ND1  1 
ATOM   3917 C  CD2  . HIS A  1 299 ? -7.96400  -9.09300  18.19300  1.000 19.83079  ? 299 HIS A CD2  1 
ATOM   3918 C  CE1  . HIS A  1 299 ? -9.21400  -7.29000  18.14800  1.000 24.41804  ? 299 HIS A CE1  1 
ATOM   3919 N  NE2  . HIS A  1 299 ? -9.14300  -8.52200  18.61700  1.000 23.61383  ? 299 HIS A NE2  1 
ATOM   3920 H  H    . HIS A  1 299 ? -4.64100  -8.20300  14.39300  1.000 26.13649  ? 299 HIS A H    1 
ATOM   3921 H  HA   . HIS A  1 299 ? -6.18900  -9.97800  15.74900  1.000 25.72026  ? 299 HIS A HA   1 
ATOM   3922 H  HB2  . HIS A  1 299 ? -5.33500  -8.62500  17.40500  1.000 28.56289  ? 299 HIS A HB2  1 
ATOM   3923 H  HB3  . HIS A  1 299 ? -5.70800  -7.32200  16.57500  1.000 28.56289  ? 299 HIS A HB3  1 
ATOM   3924 H  HD1  . HIS A  1 299 ? -7.93700  -6.31200  17.04000  1.000 34.83492  ? 299 HIS A HD1  1 
ATOM   3925 H  HD2  . HIS A  1 299 ? -7.68300  -9.96400  18.35600  1.000 23.79951  ? 299 HIS A HD2  1 
ATOM   3926 H  HE1  . HIS A  1 299 ? -9.91600  -6.69600  18.28300  1.000 29.30421  ? 299 HIS A HE1  1 
ATOM   3927 N  N    . ARG A  1 300 ? -8.28300  -9.22400  14.66700  1.000 21.66685  ? 300 ARG A N    1 
ATOM   3928 C  CA   . ARG A  1 300 ? -9.51300  -8.78200  14.03000  1.000 22.93225  ? 300 ARG A CA   1 
ATOM   3929 C  C    . ARG A  1 300 ? -10.63700 -8.99700  15.03900  1.000 21.81788  ? 300 ARG A C    1 
ATOM   3930 O  O    . ARG A  1 300 ? -10.59300 -9.92800  15.84000  1.000 21.15545  ? 300 ARG A O    1 
ATOM   3931 C  CB   . ARG A  1 300 ? -9.88500  -9.63200  12.81100  1.000 21.22986  ? 300 ARG A CB   1 
ATOM   3932 C  CG   . ARG A  1 300 ? -8.76400  -9.79400  11.77600  1.000 23.56862  ? 300 ARG A CG   1 
ATOM   3933 C  CD   . ARG A  1 300 ? -9.10500  -10.86200 10.75400  1.000 24.93401  ? 300 ARG A CD   1 
ATOM   3934 N  NE   . ARG A  1 300 ? -7.93600  -11.24300 9.95200   1.000 23.55061  ? 300 ARG A NE   1 
ATOM   3935 C  CZ   . ARG A  1 300 ? -7.86400  -12.34800 9.22600   1.000 26.38554  ? 300 ARG A CZ   1 
ATOM   3936 N  NH1  . ARG A  1 300 ? -8.92500  -13.10500 9.01100   1.000 24.46255  ? 300 ARG A NH1  1 
ATOM   3937 N  NH2  . ARG A  1 300 ? -6.69400  -12.70900 8.70400   1.000 26.41014  ? 300 ARG A NH2  1 
ATOM   3938 H  H    . ARG A  1 300 ? -8.36900  -9.98100  15.06700  1.000 26.00278  ? 300 ARG A H    1 
ATOM   3939 H  HA   . ARG A  1 300 ? -9.41500  -7.85600  13.75800  1.000 27.52126  ? 300 ARG A HA   1 
ATOM   3940 H  HB2  . ARG A  1 300 ? -10.13000 -10.51900 13.11700  1.000 25.47839  ? 300 ARG A HB2  1 
ATOM   3941 H  HB3  . ARG A  1 300 ? -10.63800 -9.21500  12.36400  1.000 25.47839  ? 300 ARG A HB3  1 
ATOM   3942 H  HG2  . ARG A  1 300 ? -8.63400  -8.95500  11.30800  1.000 28.28491  ? 300 ARG A HG2  1 
ATOM   3943 H  HG3  . ARG A  1 300 ? -7.94500  -10.05300 12.22600  1.000 28.28491  ? 300 ARG A HG3  1 
ATOM   3944 H  HD2  . ARG A  1 300 ? -9.42800  -11.65300 11.21400  1.000 29.92338  ? 300 ARG A HD2  1 
ATOM   3945 H  HD3  . ARG A  1 300 ? -9.78800  -10.52500 10.15400  1.000 29.92338  ? 300 ARG A HD3  1 
ATOM   3946 H  HE   . ARG A  1 300 ? -7.25700  -10.71500 9.95400   1.000 28.26330  ? 300 ARG A HE   1 
ATOM   3947 H  HH11 . ARG A  1 300 ? -9.68500  -12.88400 9.34600   1.000 29.35763  ? 300 ARG A HH11 1 
ATOM   3948 H  HH12 . ARG A  1 300 ? -8.85400  -13.81900 8.53700   1.000 29.35763  ? 300 ARG A HH12 1 
ATOM   3949 H  HH21 . ARG A  1 300 ? -5.99500  -12.22600 8.83900   1.000 31.69473  ? 300 ARG A HH21 1 
ATOM   3950 H  HH22 . ARG A  1 300 ? -6.63600  -13.42500 8.23100   1.000 31.69473  ? 300 ARG A HH22 1 
ATOM   3951 N  N    . SER A  1 301 ? -11.67900 -8.17700  14.94600  1.000 22.85425  ? 301 SER A N    1 
ATOM   3952 C  CA   . SER A  1 301 ? -12.85300 -8.44700  15.76900  1.000 21.91345  ? 301 SER A CA   1 
ATOM   3953 C  C    . SER A  1 301 ? -14.03100 -7.62900  15.26300  1.000 23.97132  ? 301 SER A C    1 
ATOM   3954 O  O    . SER A  1 301 ? -13.87300 -6.65400  14.53000  1.000 25.04988  ? 301 SER A O    1 
ATOM   3955 C  CB   . SER A  1 301 ? -12.62000 -8.08200  17.23800  1.000 23.04139  ? 301 SER A CB   1 
ATOM   3956 O  OG   . SER A  1 301 ? -12.69400 -6.66900  17.33600  1.000 27.55019  ? 301 SER A OG   1 
ATOM   3957 H  H    . SER A  1 301 ? -11.72900 -7.48600  14.43500  1.000 27.42766  ? 301 SER A H    1 
ATOM   3958 H  HA   . SER A  1 301 ? -13.05000 -9.39300  15.68000  1.000 26.29870  ? 301 SER A HA   1 
ATOM   3959 H  HB2  . SER A  1 301 ? -13.30600 -8.48800  17.79100  1.000 27.65223  ? 301 SER A HB2  1 
ATOM   3960 H  HB3  . SER A  1 301 ? -11.74300 -8.38700  17.51900  1.000 27.65223  ? 301 SER A HB3  1 
ATOM   3961 H  HG   . SER A  1 301 ? -12.55800 -6.42900  18.12900  1.000 33.06279  ? 301 SER A HG   1 
ATOM   3962 N  N    . THR A  1 302 ? -15.22000 -7.99300  15.73800  1.000 22.88932  ? 302 THR A N    1 
ATOM   3963 C  CA   . THR A  1 302 ? -16.41600 -7.19800  15.50900  1.000 24.12640  ? 302 THR A CA   1 
ATOM   3964 C  C    . THR A  1 302 ? -16.77200 -6.36400  16.73100  1.000 27.29767  ? 302 THR A C    1 
ATOM   3965 O  O    . THR A  1 302 ? -17.94400 -6.03300  16.93300  1.000 30.39604  ? 302 THR A O    1 
ATOM   3966 C  CB   . THR A  1 302 ? -17.58700 -8.07200  15.06400  1.000 25.00380  ? 302 THR A CB   1 
ATOM   3967 O  OG1  . THR A  1 302 ? -17.77600 -9.11900  16.00300  1.000 23.37241  ? 302 THR A OG1  1 
ATOM   3968 C  CG2  . THR A  1 302 ? -17.31100 -8.71600  13.73500  1.000 25.19534  ? 302 THR A CG2  1 
ATOM   3969 H  H    . THR A  1 302 ? -15.35700 -8.70500  16.20000  1.000 27.46975  ? 302 THR A H    1 
ATOM   3970 H  HA   . THR A  1 302 ? -16.24700 -6.58700  14.77500  1.000 28.95424  ? 302 THR A HA   1 
ATOM   3971 H  HB   . THR A  1 302 ? -18.37700 -7.51400  14.99300  1.000 30.00712  ? 302 THR A HB   1 
ATOM   3972 H  HG1  . THR A  1 302 ? -18.37500 -9.64300  15.73400  1.000 28.04946  ? 302 THR A HG1  1 
ATOM   3973 H  HG21 . THR A  1 302 ? -18.06800 -9.26100  13.46700  1.000 30.23697  ? 302 THR A HG21 1 
ATOM   3974 H  HG22 . THR A  1 302 ? -17.15900 -8.03500  13.06200  1.000 30.23697  ? 302 THR A HG22 1 
ATOM   3975 H  HG23 . THR A  1 302 ? -16.52400 -9.28000  13.79700  1.000 30.23697  ? 302 THR A HG23 1 
ATOM   3976 N  N    . CYS A  1 303 ? -15.78500 -5.99800  17.53300  1.000 26.39494  ? 303 CYS A N    1 
ATOM   3977 C  CA   . CYS A  1 303 ? -15.99000 -5.05500  18.62500  1.000 26.99553  ? 303 CYS A CA   1 
ATOM   3978 C  C    . CYS A  1 303 ? -16.52900 -3.73500  18.08000  1.000 33.43961  ? 303 CYS A C    1 
ATOM   3979 O  O    . CYS A  1 303 ? -16.19400 -3.33400  16.95900  1.000 33.83957  ? 303 CYS A O    1 
ATOM   3980 C  CB   . CYS A  1 303 ? -14.62900 -4.75400  19.27200  1.000 28.63524  ? 303 CYS A CB   1 
ATOM   3981 S  SG   . CYS A  1 303 ? -13.81500 -6.06300  20.18800  1.000 30.46553  ? 303 CYS A SG   1 
ATOM   3982 H  H    . CYS A  1 303 ? -14.97600 -6.28200  17.46800  1.000 31.67649  ? 303 CYS A H    1 
ATOM   3983 H  HA   . CYS A  1 303 ? -16.61400 -5.42500  19.26900  1.000 32.39720  ? 303 CYS A HA   1 
ATOM   3984 H  HB2  . CYS A  1 303 ? -14.01900 -4.49200  18.56500  1.000 34.36485  ? 303 CYS A HB2  1 
ATOM   3985 H  HB3  . CYS A  1 303 ? -14.75400 -4.01900  19.89200  1.000 34.36485  ? 303 CYS A HB3  1 
ATOM   3986 N  N    . PRO A  1 304 ? -17.33800 -3.01200  18.87100  1.000 32.53122  ? 304 PRO A N    1 
ATOM   3987 C  CA   . PRO A  1 304 ? -17.79400 -3.34200  20.22200  1.000 33.89987  ? 304 PRO A CA   1 
ATOM   3988 C  C    . PRO A  1 304 ? -18.93400 -4.35000  20.16500  1.000 40.12979  ? 304 PRO A C    1 
ATOM   3989 O  O    . PRO A  1 304 ? -19.73700 -4.31700  19.23400  1.000 52.91425  ? 304 PRO A O    1 
ATOM   3990 C  CB   . PRO A  1 304 ? -18.32200 -1.99800  20.75900  1.000 46.82460  ? 304 PRO A CB   1 
ATOM   3991 C  CG   . PRO A  1 304 ? -17.85600 -0.93700  19.78000  1.000 57.46163  ? 304 PRO A CG   1 
ATOM   3992 C  CD   . PRO A  1 304 ? -17.72600 -1.65100  18.45800  1.000 38.76174  ? 304 PRO A CD   1 
ATOM   3993 H  HA   . PRO A  1 304 ? -17.06700 -3.65500  20.78300  1.000 40.68241  ? 304 PRO A HA   1 
ATOM   3994 H  HB2  . PRO A  1 304 ? -19.29100 -2.02400  20.80100  1.000 56.19208  ? 304 PRO A HB2  1 
ATOM   3995 H  HB3  . PRO A  1 304 ? -17.95500 -1.83400  21.64200  1.000 56.19208  ? 304 PRO A HB3  1 
ATOM   3996 H  HG2  . PRO A  1 304 ? -18.51300 -0.22600  19.72600  1.000 68.95651  ? 304 PRO A HG2  1 
ATOM   3997 H  HG3  . PRO A  1 304 ? -17.00100 -0.57700  20.06500  1.000 68.95651  ? 304 PRO A HG3  1 
ATOM   3998 H  HD2  . PRO A  1 304 ? -18.57000 -1.65800  17.98100  1.000 46.51665  ? 304 PRO A HD2  1 
ATOM   3999 H  HD3  . PRO A  1 304 ? -17.03800 -1.24400  17.90800  1.000 46.51665  ? 304 PRO A HD3  1 
ATOM   4000 N  N    . PHE A  1 305 ? -19.01800 -5.21300  21.16200  1.000 38.34914  ? 305 PHE A N    1 
ATOM   4001 C  CA   . PHE A  1 305 ? -20.03400 -6.26400  21.20100  1.000 52.29286  ? 305 PHE A CA   1 
ATOM   4002 C  C    . PHE A  1 305 ? -21.30100 -5.69600  21.83200  1.000 65.74985  ? 305 PHE A C    1 
ATOM   4003 O  O    . PHE A  1 305 ? -21.60400 -5.92500  23.00500  1.000 60.42428  ? 305 PHE A O    1 
ATOM   4004 C  CB   . PHE A  1 305 ? -19.50000 -7.46100  21.97000  1.000 44.63233  ? 305 PHE A CB   1 
ATOM   4005 C  CG   . PHE A  1 305 ? -18.26400 -8.06200  21.36300  1.000 33.36056  ? 305 PHE A CG   1 
ATOM   4006 C  CD1  . PHE A  1 305 ? -18.15200 -8.21000  19.98500  1.000 32.81370  ? 305 PHE A CD1  1 
ATOM   4007 C  CD2  . PHE A  1 305 ? -17.20500 -8.46100  22.15000  1.000 32.02009  ? 305 PHE A CD2  1 
ATOM   4008 C  CE1  . PHE A  1 305 ? -17.01900 -8.76800  19.44400  1.000 27.00935  ? 305 PHE A CE1  1 
ATOM   4009 C  CE2  . PHE A  1 305 ? -16.08400 -9.00100  21.60900  1.000 34.81416  ? 305 PHE A CE2  1 
ATOM   4010 C  CZ   . PHE A  1 305 ? -15.97600 -9.15900  20.25400  1.000 31.95759  ? 305 PHE A CZ   1 
ATOM   4011 H  H    . PHE A  1 305 ? -18.49200 -5.21600  21.84200  1.000 46.02153  ? 305 PHE A H    1 
ATOM   4012 H  HA   . PHE A  1 305 ? -20.25300 -6.54300  20.29800  1.000 62.75400  ? 305 PHE A HA   1 
ATOM   4013 H  HB2  . PHE A  1 305 ? -19.28100 -7.18100  22.87200  1.000 53.56136  ? 305 PHE A HB2  1 
ATOM   4014 H  HB3  . PHE A  1 305 ? -20.18300 -8.14900  21.99200  1.000 53.56136  ? 305 PHE A HB3  1 
ATOM   4015 H  HD1  . PHE A  1 305 ? -18.84300 -7.93100  19.43000  1.000 39.37900  ? 305 PHE A HD1  1 
ATOM   4016 H  HD2  . PHE A  1 305 ? -17.26100 -8.35800  23.07300  1.000 38.42668  ? 305 PHE A HD2  1 
ATOM   4017 H  HE1  . PHE A  1 305 ? -16.95500 -8.88300  18.52300  1.000 32.41378  ? 305 PHE A HE1  1 
ATOM   4018 H  HE2  . PHE A  1 305 ? -15.38500 -9.26600  22.16300  1.000 41.77955  ? 305 PHE A HE2  1 
ATOM   4019 H  HZ   . PHE A  1 305 ? -15.20700 -9.52700  19.88400  1.000 38.35166  ? 305 PHE A HZ   1 
ATOM   4020 N  N    . GLY B  1 42  ? -50.61100 7.94200   8.77900   1.000 63.45245  ? 42  GLY B N    1 
ATOM   4021 C  CA   . GLY B  1 42  ? -50.39600 7.01300   9.86900   1.000 50.73934  ? 42  GLY B CA   1 
ATOM   4022 C  C    . GLY B  1 42  ? -50.61000 5.56400   9.47500   1.000 36.56872  ? 42  GLY B C    1 
ATOM   4023 O  O    . GLY B  1 42  ? -51.17800 5.26900   8.42400   1.000 34.94919  ? 42  GLY B O    1 
ATOM   4024 H  H    . GLY B  1 42  ? -50.46500 7.60300   8.00300   1.000 76.14550  ? 42  GLY B H    1 
ATOM   4025 H  HA2  . GLY B  1 42  ? -49.48500 7.10700   10.19100  1.000 60.88977  ? 42  GLY B HA2  1 
ATOM   4026 H  HA3  . GLY B  1 42  ? -51.00900 7.22300   10.59100  1.000 60.88977  ? 42  GLY B HA3  1 
ATOM   4027 N  N    . TYR B  1 43  ? -50.16700 4.65200   10.33900  1.000 26.25942  ? 43  TYR B N    1 
ATOM   4028 C  CA   . TYR B  1 43  ? -50.33200 3.22700   10.11000  1.000 23.59012  ? 43  TYR B CA   1 
ATOM   4029 C  C    . TYR B  1 43  ? -51.61800 2.64500   10.69900  1.000 22.75919  ? 43  TYR B C    1 
ATOM   4030 O  O    . TYR B  1 43  ? -51.91300 1.46100   10.47200  1.000 21.74720  ? 43  TYR B O    1 
ATOM   4031 C  CB   . TYR B  1 43  ? -49.13400 2.46900   10.70900  1.000 22.39451  ? 43  TYR B CB   1 
ATOM   4032 C  CG   . TYR B  1 43  ? -47.78500 2.94500   10.26400  1.000 23.37596  ? 43  TYR B CG   1 
ATOM   4033 C  CD1  . TYR B  1 43  ? -47.45900 3.03200   8.93700   1.000 23.52333  ? 43  TYR B CD1  1 
ATOM   4034 C  CD2  . TYR B  1 43  ? -46.82600 3.31700   11.20300  1.000 26.68619  ? 43  TYR B CD2  1 
ATOM   4035 C  CE1  . TYR B  1 43  ? -46.22600 3.46600   8.53400   1.000 24.81962  ? 43  TYR B CE1  1 
ATOM   4036 C  CE2  . TYR B  1 43  ? -45.58100 3.76000   10.80100  1.000 29.19855  ? 43  TYR B CE2  1 
ATOM   4037 C  CZ   . TYR B  1 43  ? -45.29800 3.82100   9.46700   1.000 27.88363  ? 43  TYR B CZ   1 
ATOM   4038 O  OH   . TYR B  1 43  ? -44.04900 4.24600   9.05200   1.000 33.43871  ? 43  TYR B OH   1 
ATOM   4039 H  H    . TYR B  1 43  ? -49.76200 4.84100   11.07400  1.000 31.51387  ? 43  TYR B H    1 
ATOM   4040 H  HA   . TYR B  1 43  ? -50.36000 3.07900   9.15200   1.000 28.31071  ? 43  TYR B HA   1 
ATOM   4041 H  HB2  . TYR B  1 43  ? -49.16900 2.55800   11.67500  1.000 26.87597  ? 43  TYR B HB2  1 
ATOM   4042 H  HB3  . TYR B  1 43  ? -49.20800 1.53400   10.45900  1.000 26.87597  ? 43  TYR B HB3  1 
ATOM   4043 H  HD1  . TYR B  1 43  ? -48.08900 2.79200   8.29600   1.000 28.23056  ? 43  TYR B HD1  1 
ATOM   4044 H  HD2  . TYR B  1 43  ? -47.02600 3.26800   12.11000  1.000 32.02599  ? 43  TYR B HD2  1 
ATOM   4045 H  HE1  . TYR B  1 43  ? -46.02200 3.51900   7.62800   1.000 29.78611  ? 43  TYR B HE1  1 
ATOM   4046 H  HE2  . TYR B  1 43  ? -44.94500 4.01300   11.43000  1.000 35.04082  ? 43  TYR B HE2  1 
ATOM   4047 H  HH   . TYR B  1 43  ? -43.53200 4.30400   9.71200   1.000 40.12902  ? 43  TYR B HH   1 
ATOM   4048 N  N    . ALA B  1 44  ? -52.37100 3.40000   11.49000  1.000 20.94218  ? 44  ALA B N    1 
ATOM   4049 C  CA   . ALA B  1 44  ? -53.55500 2.84000   12.11400  1.000 18.54072  ? 44  ALA B CA   1 
ATOM   4050 C  C    . ALA B  1 44  ? -54.62800 2.48300   11.07900  1.000 19.08990  ? 44  ALA B C    1 
ATOM   4051 O  O    . ALA B  1 44  ? -54.83900 3.21500   10.10500  1.000 22.14500  ? 44  ALA B O    1 
ATOM   4052 C  CB   . ALA B  1 44  ? -54.14700 3.84300   13.10500  1.000 22.03676  ? 44  ALA B CB   1 
ATOM   4053 H  H    . ALA B  1 44  ? -52.21900 4.22600   11.67700  1.000 25.13318  ? 44  ALA B H    1 
ATOM   4054 H  HA   . ALA B  1 44  ? -53.29900 2.02800   12.57900  1.000 22.25143  ? 44  ALA B HA   1 
ATOM   4055 H  HB1  . ALA B  1 44  ? -54.91800 3.44300   13.53700  1.000 26.44668  ? 44  ALA B HB1  1 
ATOM   4056 H  HB2  . ALA B  1 44  ? -53.47500 4.06500   13.76800  1.000 26.44668  ? 44  ALA B HB2  1 
ATOM   4057 H  HB3  . ALA B  1 44  ? -54.41400 4.64200   12.62400  1.000 26.44668  ? 44  ALA B HB3  1 
ATOM   4058 N  N    . ARG B  1 45  ? -55.24200 1.32700   11.27600  1.000 18.61089  ? 45  ARG B N    1 
ATOM   4059 C  CA   . ARG B  1 45  ? -56.28900 0.81000   10.40800  1.000 18.68906  ? 45  ARG B CA   1 
ATOM   4060 C  C    . ARG B  1 45  ? -57.49400 0.39700   11.22200  1.000 19.33265  ? 45  ARG B C    1 
ATOM   4061 O  O    . ARG B  1 45  ? -57.39100 -0.07500  12.35800  1.000 19.49572  ? 45  ARG B O    1 
ATOM   4062 C  CB   . ARG B  1 45  ? -55.79600 -0.43900  9.60100   1.000 18.43831  ? 45  ARG B CB   1 
ATOM   4063 C  CG   . ARG B  1 45  ? -54.47700 -0.26000  8.88900   1.000 18.25186  ? 45  ARG B CG   1 
ATOM   4064 C  CD   . ARG B  1 45  ? -54.60200 0.59500   7.65700   1.000 19.81638  ? 45  ARG B CD   1 
ATOM   4065 N  NE   . ARG B  1 45  ? -53.32700 0.86800   6.99900   1.000 19.71543  ? 45  ARG B NE   1 
ATOM   4066 C  CZ   . ARG B  1 45  ? -52.69300 2.03400   7.06600   1.000 25.52914  ? 45  ARG B CZ   1 
ATOM   4067 N  NH1  . ARG B  1 45  ? -53.19000 3.05300   7.75500   1.000 26.03591  ? 45  ARG B NH1  1 
ATOM   4068 N  NH2  . ARG B  1 45  ? -51.50900 2.17600   6.47300   1.000 23.29941  ? 45  ARG B NH2  1 
ATOM   4069 H  H    . ARG B  1 45  ? -55.06300 0.80200   11.93300  1.000 22.33563  ? 45  ARG B H    1 
ATOM   4070 H  HA   . ARG B  1 45  ? -56.55300 1.51300   9.79400   1.000 22.42943  ? 45  ARG B HA   1 
ATOM   4071 H  HB2  . ARG B  1 45  ? -55.69600 -1.18200  10.21700  1.000 22.12853  ? 45  ARG B HB2  1 
ATOM   4072 H  HB3  . ARG B  1 45  ? -56.46300 -0.65300  8.92900   1.000 22.12853  ? 45  ARG B HB3  1 
ATOM   4073 H  HG2  . ARG B  1 45  ? -53.84700 0.16800   9.49000   1.000 21.90479  ? 45  ARG B HG2  1 
ATOM   4074 H  HG3  . ARG B  1 45  ? -54.14000 -1.12900  8.62000   1.000 21.90479  ? 45  ARG B HG3  1 
ATOM   4075 H  HD2  . ARG B  1 45  ? -55.17300 0.14000   7.01800   1.000 23.78221  ? 45  ARG B HD2  1 
ATOM   4076 H  HD3  . ARG B  1 45  ? -54.99500 1.44600   7.90600   1.000 23.78221  ? 45  ARG B HD3  1 
ATOM   4077 H  HE   . ARG B  1 45  ? -52.96400 0.23600   6.54200   1.000 23.66108  ? 45  ARG B HE   1 
ATOM   4078 H  HH11 . ARG B  1 45  ? -53.93800 2.96800   8.17100   1.000 31.24566  ? 45  ARG B HH11 1 
ATOM   4079 H  HH12 . ARG B  1 45  ? -52.76400 3.80000   7.78600   1.000 31.24566  ? 45  ARG B HH12 1 
ATOM   4080 H  HH21 . ARG B  1 45  ? -51.15800 1.51500   6.04900   1.000 27.96185  ? 45  ARG B HH21 1 
ATOM   4081 H  HH22 . ARG B  1 45  ? -51.09500 2.92900   6.51400   1.000 27.96185  ? 45  ARG B HH22 1 
ATOM   4082 N  N    . GLY B  1 46  ? -58.66200 0.57900   10.62900  1.000 19.06407  ? 46  GLY B N    1 
ATOM   4083 C  CA   . GLY B  1 46  ? -59.86300 0.03400   11.23600  1.000 17.59790  ? 46  GLY B CA   1 
ATOM   4084 C  C    . GLY B  1 46  ? -60.52800 0.92700   12.25500  1.000 18.23465  ? 46  GLY B C    1 
ATOM   4085 O  O    . GLY B  1 46  ? -60.04500 2.01200   12.62300  1.000 20.74520  ? 46  GLY B O    1 
ATOM   4086 H  H    . GLY B  1 46  ? -58.78300 1.00400   9.89200   1.000 22.87945  ? 46  GLY B H    1 
ATOM   4087 H  HA2  . GLY B  1 46  ? -60.51000 -0.14600  10.53600  1.000 21.12004  ? 46  GLY B HA2  1 
ATOM   4088 H  HA3  . GLY B  1 46  ? -59.63600 -0.79900  11.67800  1.000 21.12004  ? 46  GLY B HA3  1 
ATOM   4089 N  N    . PRO B  1 47  ? -61.67500 0.46800   12.73800  1.000 18.33796  ? 47  PRO B N    1 
ATOM   4090 C  CA   . PRO B  1 47  ? -62.42600 1.26600   13.70600  1.000 17.85988  ? 47  PRO B CA   1 
ATOM   4091 C  C    . PRO B  1 47  ? -61.78100 1.30700   15.08200  1.000 18.51989  ? 47  PRO B C    1 
ATOM   4092 O  O    . PRO B  1 47  ? -60.89100 0.52800   15.40900  1.000 18.48158  ? 47  PRO B O    1 
ATOM   4093 C  CB   . PRO B  1 47  ? -63.75300 0.53000   13.77200  1.000 19.11975  ? 47  PRO B CB   1 
ATOM   4094 C  CG   . PRO B  1 47  ? -63.40400 -0.92100  13.54200  1.000 19.02366  ? 47  PRO B CG   1 
ATOM   4095 C  CD   . PRO B  1 47  ? -62.24400 -0.87600  12.53300  1.000 19.99082  ? 47  PRO B CD   1 
ATOM   4096 H  HA   . PRO B  1 47  ? -62.53200 2.17400   13.38100  1.000 21.43442  ? 47  PRO B HA   1 
ATOM   4097 H  HB2  . PRO B  1 47  ? -64.15800 0.65500   14.64500  1.000 22.94626  ? 47  PRO B HB2  1 
ATOM   4098 H  HB3  . PRO B  1 47  ? -64.34900 0.85800   13.08100  1.000 22.94626  ? 47  PRO B HB3  1 
ATOM   4099 H  HG2  . PRO B  1 47  ? -63.12700 -1.33400  14.37400  1.000 22.83096  ? 47  PRO B HG2  1 
ATOM   4100 H  HG3  . PRO B  1 47  ? -64.16800 -1.39300  13.17500  1.000 22.83096  ? 47  PRO B HG3  1 
ATOM   4101 H  HD2  . PRO B  1 47  ? -61.58800 -1.56200  12.72900  1.000 23.99155  ? 47  PRO B HD2  1 
ATOM   4102 H  HD3  . PRO B  1 47  ? -62.57000 -0.97800  11.62500  1.000 23.99155  ? 47  PRO B HD3  1 
ATOM   4103 N  N    . ASP B  1 48  ? -62.22300 2.26300   15.87900  1.000 18.03647  ? 48  ASP B N    1 
ATOM   4104 C  CA   . ASP B  1 48  ? -61.72400 2.33400   17.24500  1.000 17.10088  ? 48  ASP B CA   1 
ATOM   4105 C  C    . ASP B  1 48  ? -62.08600 1.04300   17.98600  1.000 17.98880  ? 48  ASP B C    1 
ATOM   4106 O  O    . ASP B  1 48  ? -63.24300 0.61000   17.93600  1.000 17.46026  ? 48  ASP B O    1 
ATOM   4107 C  CB   . ASP B  1 48  ? -62.27700 3.55500   17.98300  1.000 18.52409  ? 48  ASP B CB   1 
ATOM   4108 C  CG   . ASP B  1 48  ? -61.80800 4.87500   17.41700  1.000 19.86642  ? 48  ASP B CG   1 
ATOM   4109 O  OD1  . ASP B  1 48  ? -60.85600 4.85700   16.57600  1.000 20.48376  ? 48  ASP B OD1  1 
ATOM   4110 O  OD2  . ASP B  1 48  ? -62.35600 5.91300   17.76500  1.000 22.35958  ? 48  ASP B OD2  1 
ATOM   4111 H  H    . ASP B  1 48  ? -62.79600 2.86700   15.66300  1.000 21.64633  ? 48  ASP B H    1 
ATOM   4112 H  HA   . ASP B  1 48  ? -60.75900 2.42800   17.22800  1.000 20.52362  ? 48  ASP B HA   1 
ATOM   4113 H  HB2  . ASP B  1 48  ? -63.24600 3.53900   17.93000  1.000 22.23147  ? 48  ASP B HB2  1 
ATOM   4114 H  HB3  . ASP B  1 48  ? -61.99500 3.51300   18.91000  1.000 22.23147  ? 48  ASP B HB3  1 
ATOM   4115 N  N    . PRO B  1 49  ? -61.15600 0.42800   18.69700  1.000 16.55857  ? 49  PRO B N    1 
ATOM   4116 C  CA   . PRO B  1 49  ? -61.42800 -0.87600  19.31500  1.000 16.34611  ? 49  PRO B CA   1 
ATOM   4117 C  C    . PRO B  1 49  ? -62.19600 -0.76000  20.63400  1.000 16.88657  ? 49  PRO B C    1 
ATOM   4118 O  O    . PRO B  1 49  ? -62.15200 0.24800   21.34200  1.000 17.73916  ? 49  PRO B O    1 
ATOM   4119 C  CB   . PRO B  1 49  ? -60.01800 -1.43500  19.55900  1.000 17.12140  ? 49  PRO B CB   1 
ATOM   4120 C  CG   . PRO B  1 49  ? -59.18400 -0.19200  19.75500  1.000 18.34543  ? 49  PRO B CG   1 
ATOM   4121 C  CD   . PRO B  1 49  ? -59.72500 0.81000   18.75600  1.000 17.25641  ? 49  PRO B CD   1 
ATOM   4122 H  HA   . PRO B  1 49  ? -61.92400 -1.44400  18.70600  1.000 19.60252  ? 49  PRO B HA   1 
ATOM   4123 H  HB2  . PRO B  1 49  ? -60.01000 -1.99600  20.35100  1.000 20.54825  ? 49  PRO B HB2  1 
ATOM   4124 H  HB3  . PRO B  1 49  ? -59.71900 -1.94400  18.78900  1.000 20.54825  ? 49  PRO B HB3  1 
ATOM   4125 H  HG2  . PRO B  1 49  ? -59.28700 0.13400   20.66300  1.000 22.01708  ? 49  PRO B HG2  1 
ATOM   4126 H  HG3  . PRO B  1 49  ? -58.25100 -0.38900  19.57700  1.000 22.01708  ? 49  PRO B HG3  1 
ATOM   4127 H  HD2  . PRO B  1 49  ? -59.61700 1.71900   19.07600  1.000 20.71026  ? 49  PRO B HD2  1 
ATOM   4128 H  HD3  . PRO B  1 49  ? -59.29800 0.70900   17.89100  1.000 20.71026  ? 49  PRO B HD3  1 
ATOM   4129 N  N    . THR B  1 50  ? -62.88200 -1.85500  20.95400  1.000 16.35786  ? 50  THR B N    1 
ATOM   4130 C  CA   . THR B  1 50  ? -63.42000 -2.12100  22.28100  1.000 16.35664  ? 50  THR B CA   1 
ATOM   4131 C  C    . THR B  1 50  ? -63.10900 -3.57100  22.61200  1.000 16.25643  ? 50  THR B C    1 
ATOM   4132 O  O    . THR B  1 50  ? -62.74300 -4.35800  21.75600  1.000 15.92091  ? 50  THR B O    1 
ATOM   4133 C  CB   . THR B  1 50  ? -64.93300 -1.88500  22.34900  1.000 18.22778  ? 50  THR B CB   1 
ATOM   4134 O  OG1  . THR B  1 50  ? -65.56000 -2.77100  21.40400  1.000 17.27215  ? 50  THR B OG1  1 
ATOM   4135 C  CG2  . THR B  1 50  ? -65.29100 -0.42300  22.01700  1.000 18.10313  ? 50  THR B CG2  1 
ATOM   4136 H  H    . THR B  1 50  ? -63.05400 -2.48500  20.39500  1.000 19.61662  ? 50  THR B H    1 
ATOM   4137 H  HA   . THR B  1 50  ? -63.00000 -1.53300  22.92700  1.000 19.61516  ? 50  THR B HA   1 
ATOM   4138 H  HB   . THR B  1 50  ? -65.25900 -2.05600  23.24600  1.000 21.87590  ? 50  THR B HB   1 
ATOM   4139 H  HG1  . THR B  1 50  ? -66.39200 -2.77100  21.51900  1.000 20.72914  ? 50  THR B HG1  1 
ATOM   4140 H  HG21 . THR B  1 50  ? -66.25200 -0.29700  22.06700  1.000 21.72632  ? 50  THR B HG21 1 
ATOM   4141 H  HG22 . THR B  1 50  ? -64.86200 0.17600   22.64900  1.000 21.72632  ? 50  THR B HG22 1 
ATOM   4142 H  HG23 . THR B  1 50  ? -64.99100 -0.20300  21.12200  1.000 21.72632  ? 50  THR B HG23 1 
ATOM   4143 N  N    . GLU B  1 51  ? -63.31300 -3.94000  23.86700  1.000 17.62174  ? 51  GLU B N    1 
ATOM   4144 C  CA   . GLU B  1 51  ? -63.00100 -5.29700  24.30700  1.000 16.81809  ? 51  GLU B CA   1 
ATOM   4145 C  C    . GLU B  1 51  ? -63.82400 -6.34600  23.55900  1.000 16.94904  ? 51  GLU B C    1 
ATOM   4146 O  O    . GLU B  1 51  ? -63.27000 -7.32300  23.04400  1.000 17.09947  ? 51  GLU B O    1 
ATOM   4147 C  CB   . GLU B  1 51  ? -63.17600 -5.38200  25.82200  1.000 20.17564  ? 51  GLU B CB   1 
ATOM   4148 C  CG   . GLU B  1 51  ? -62.45000 -4.26100  26.61900  1.000 31.94614  ? 51  GLU B CG   1 
ATOM   4149 C  CD   . GLU B  1 51  ? -63.21400 -2.89800  26.84900  1.000 47.57626  ? 51  GLU B CD   1 
ATOM   4150 O  OE1  . GLU B  1 51  ? -64.12200 -2.41600  26.07800  1.000 23.20928  ? 51  GLU B OE1  1 
ATOM   4151 O  OE2  . GLU B  1 51  ? -62.85300 -2.26400  27.87100  1.000 57.90945  ? 51  GLU B OE2  1 
ATOM   4152 H  H    . GLU B  1 51  ? -63.63000 -3.43100  24.48400  1.000 21.14865  ? 51  GLU B H    1 
ATOM   4153 H  HA   . GLU B  1 51  ? -62.07400 -5.50000  24.10500  1.000 20.18427  ? 51  GLU B HA   1 
ATOM   4154 H  HB2  . GLU B  1 51  ? -64.12200 -5.32200  26.02800  1.000 24.21333  ? 51  GLU B HB2  1 
ATOM   4155 H  HB3  . GLU B  1 51  ? -62.82300 -6.23300  26.12700  1.000 24.21333  ? 51  GLU B HB3  1 
ATOM   4156 H  HG2  . GLU B  1 51  ? -62.23900 -4.61200  27.49800  1.000 38.33793  ? 51  GLU B HG2  1 
ATOM   4157 H  HG3  . GLU B  1 51  ? -61.63300 -4.04300  26.14400  1.000 38.33793  ? 51  GLU B HG3  1 
ATOM   4158 N  N    . SER B  1 52  ? -65.13900 -6.14800  23.44200  1.000 17.53087  ? 52  SER B N    1 
ATOM   4159 C  CA   . SER B  1 52  ? -65.95700 -7.16400  22.79000  1.000 17.55558  ? 52  SER B CA   1 
ATOM   4160 C  C    . SER B  1 52  ? -65.59500 -7.29400  21.32800  1.000 17.32128  ? 52  SER B C    1 
ATOM   4161 O  O    . SER B  1 52  ? -65.58700 -8.39800  20.77300  1.000 17.04034  ? 52  SER B O    1 
ATOM   4162 C  CB   . SER B  1 52  ? -67.44200 -6.81200  22.89600  1.000 19.86478  ? 52  SER B CB   1 
ATOM   4163 O  OG   . SER B  1 52  ? -67.88600 -6.95700  24.22200  1.000 28.33636  ? 52  SER B OG   1 
ATOM   4164 H  H    . SER B  1 52  ? -65.56600 -5.45600  23.72400  1.000 21.03961  ? 52  SER B H    1 
ATOM   4165 H  HA   . SER B  1 52  ? -65.80000 -8.00700  23.24300  1.000 21.06926  ? 52  SER B HA   1 
ATOM   4166 H  HB2  . SER B  1 52  ? -67.57100 -5.89200  22.61700  1.000 23.84030  ? 52  SER B HB2  1 
ATOM   4167 H  HB3  . SER B  1 52  ? -67.95100 -7.40700  22.32400  1.000 23.84030  ? 52  SER B HB3  1 
ATOM   4168 H  HG   . SER B  1 52  ? -67.45900 -6.43900  24.72700  1.000 34.00619  ? 52  SER B HG   1 
ATOM   4169 N  N    . PHE B  1 53  ? -65.24800 -6.17600  20.69600  1.000 16.61290  ? 53  PHE B N    1 
ATOM   4170 C  CA   . PHE B  1 53  ? -64.77000 -6.20000  19.31200  1.000 16.61877  ? 53  PHE B CA   1 
ATOM   4171 C  C    . PHE B  1 53  ? -63.52000 -7.04900  19.16100  1.000 16.41712  ? 53  PHE B C    1 
ATOM   4172 O  O    . PHE B  1 53  ? -63.37300 -7.77700  18.17700  1.000 16.74881  ? 53  PHE B O    1 
ATOM   4173 C  CB   . PHE B  1 53  ? -64.56800 -4.72700  18.89600  1.000 16.67198  ? 53  PHE B CB   1 
ATOM   4174 C  CG   . PHE B  1 53  ? -63.74300 -4.48400  17.67300  1.000 16.30053  ? 53  PHE B CG   1 
ATOM   4175 C  CD1  . PHE B  1 53  ? -64.30700 -4.45000  16.40900  1.000 16.48800  ? 53  PHE B CD1  1 
ATOM   4176 C  CD2  . PHE B  1 53  ? -62.38700 -4.21000  17.79300  1.000 16.67011  ? 53  PHE B CD2  1 
ATOM   4177 C  CE1  . PHE B  1 53  ? -63.50800 -4.19200  15.28400  1.000 16.77038  ? 53  PHE B CE1  1 
ATOM   4178 C  CE2  . PHE B  1 53  ? -61.61200 -3.92500  16.69400  1.000 16.84994  ? 53  PHE B CE2  1 
ATOM   4179 C  CZ   . PHE B  1 53  ? -62.18000 -3.92700  15.44400  1.000 16.49904  ? 53  PHE B CZ   1 
ATOM   4180 H  H    . PHE B  1 53  ? -65.27800 -5.39000  21.04400  1.000 19.93805  ? 53  PHE B H    1 
ATOM   4181 H  HA   . PHE B  1 53  ? -65.41400 -6.60800  18.71300  1.000 19.94509  ? 53  PHE B HA   1 
ATOM   4182 H  HB2  . PHE B  1 53  ? -65.44100 -4.33800  18.73100  1.000 20.00893  ? 53  PHE B HB2  1 
ATOM   4183 H  HB3  . PHE B  1 53  ? -64.13200 -4.26400  19.62900  1.000 20.00893  ? 53  PHE B HB3  1 
ATOM   4184 H  HD1  . PHE B  1 53  ? -65.21900 -4.60000  16.30500  1.000 19.77278  ? 53  PHE B HD1  1 
ATOM   4185 H  HD2  . PHE B  1 53  ? -61.99400 -4.21900  18.63600  1.000 20.00670  ? 53  PHE B HD2  1 
ATOM   4186 H  HE1  . PHE B  1 53  ? -63.88300 -4.20100  14.43300  1.000 20.12702  ? 53  PHE B HE1  1 
ATOM   4187 H  HE2  . PHE B  1 53  ? -60.70800 -3.73200  16.79600  1.000 20.22250  ? 53  PHE B HE2  1 
ATOM   4188 H  HZ   . PHE B  1 53  ? -61.65400 -3.74500  14.69900  1.000 19.80141  ? 53  PHE B HZ   1 
ATOM   4189 N  N    . LEU B  1 54  ? -62.59600 -6.92200  20.08700  1.000 15.61931  ? 54  LEU B N    1 
ATOM   4190 C  CA   . LEU B  1 54  ? -61.36200 -7.68500  20.03700  1.000 15.57381  ? 54  LEU B CA   1 
ATOM   4191 C  C    . LEU B  1 54  ? -61.54600 -9.14300  20.42000  1.000 16.18639  ? 54  LEU B C    1 
ATOM   4192 O  O    . LEU B  1 54  ? -60.72300 -9.96800  20.03700  1.000 17.27567  ? 54  LEU B O    1 
ATOM   4193 C  CB   . LEU B  1 54  ? -60.33500 -7.06400  21.01100  1.000 16.83509  ? 54  LEU B CB   1 
ATOM   4194 C  CG   . LEU B  1 54  ? -59.49300 -5.94700  20.38700  1.000 17.77103  ? 54  LEU B CG   1 
ATOM   4195 C  CD1  . LEU B  1 54  ? -58.76400 -5.12000  21.39700  1.000 19.41188  ? 54  LEU B CD1  1 
ATOM   4196 C  CD2  . LEU B  1 54  ? -58.46700 -6.59600  19.39400  1.000 21.22232  ? 54  LEU B CD2  1 
ATOM   4197 H  H    . LEU B  1 54  ? -62.65600 -6.39600  20.76500  1.000 18.73036  ? 54  LEU B H    1 
ATOM   4198 H  HA   . LEU B  1 54  ? -61.02000 -7.64600  19.13000  1.000 18.69113  ? 54  LEU B HA   1 
ATOM   4199 H  HB2  . LEU B  1 54  ? -60.81000 -6.69000  21.76900  1.000 20.20467  ? 54  LEU B HB2  1 
ATOM   4200 H  HB3  . LEU B  1 54  ? -59.72900 -7.76100  21.31100  1.000 20.20467  ? 54  LEU B HB3  1 
ATOM   4201 H  HG   . LEU B  1 54  ? -60.09200 -5.33900  19.92500  1.000 21.32780  ? 54  LEU B HG   1 
ATOM   4202 H  HD11 . LEU B  1 54  ? -58.24700 -4.44100  20.93500  1.000 23.29681  ? 54  LEU B HD11 1 
ATOM   4203 H  HD12 . LEU B  1 54  ? -59.40900 -4.70000  21.98600  1.000 23.29681  ? 54  LEU B HD12 1 
ATOM   4204 H  HD13 . LEU B  1 54  ? -58.17300 -5.69400  21.90800  1.000 23.29681  ? 54  LEU B HD13 1 
ATOM   4205 H  HD21 . LEU B  1 54  ? -57.80500 -5.93200  19.14500  1.000 25.46934  ? 54  LEU B HD21 1 
ATOM   4206 H  HD22 . LEU B  1 54  ? -58.03400 -7.34600  19.83100  1.000 25.46934  ? 54  LEU B HD22 1 
ATOM   4207 H  HD23 . LEU B  1 54  ? -58.94100 -6.90200  18.60500  1.000 25.46934  ? 54  LEU B HD23 1 
ATOM   4208 N  N    . GLU B  1 55  ? -62.57400 -9.47800  21.18000  1.000 16.15710  ? 55  GLU B N    1 
ATOM   4209 C  CA   . GLU B  1 55  ? -62.85300 -10.85800 21.56600  1.000 16.87832  ? 55  GLU B CA   1 
ATOM   4210 C  C    . GLU B  1 55  ? -63.59800 -11.62700 20.48300  1.000 17.79473  ? 55  GLU B C    1 
ATOM   4211 O  O    . GLU B  1 55  ? -63.65100 -12.85900 20.55500  1.000 18.79057  ? 55  GLU B O    1 
ATOM   4212 C  CB   . GLU B  1 55  ? -63.66800 -10.87400 22.86600  1.000 18.91021  ? 55  GLU B CB   1 
ATOM   4213 C  CG   . GLU B  1 55  ? -62.83700 -10.42100 24.06800  1.000 18.60708  ? 55  GLU B CG   1 
ATOM   4214 C  CD   . GLU B  1 55  ? -63.59300 -10.17000 25.32200  1.000 27.37060  ? 55  GLU B CD   1 
ATOM   4215 O  OE1  . GLU B  1 55  ? -64.83800 -10.24600 25.30300  1.000 29.74499  ? 55  GLU B OE1  1 
ATOM   4216 O  OE2  . GLU B  1 55  ? -62.94300 -9.85700  26.33000  1.000 29.00761  ? 55  GLU B OE2  1 
ATOM   4217 H  H    . GLU B  1 55  ? -63.14300 -8.91500  21.49500  1.000 19.39108  ? 55  GLU B H    1 
ATOM   4218 H  HA   . GLU B  1 55  ? -62.01400 -11.31700 21.72900  1.000 20.25654  ? 55  GLU B HA   1 
ATOM   4219 H  HB2  . GLU B  1 55  ? -64.42400 -10.27300 22.77600  1.000 22.69482  ? 55  GLU B HB2  1 
ATOM   4220 H  HB3  . GLU B  1 55  ? -63.98000 -11.77700 23.03500  1.000 22.69482  ? 55  GLU B HB3  1 
ATOM   4221 H  HG2  . GLU B  1 55  ? -62.18200 -11.10900 24.26100  1.000 22.33106  ? 55  GLU B HG2  1 
ATOM   4222 H  HG3  . GLU B  1 55  ? -62.38900 -9.59300  23.83300  1.000 22.33106  ? 55  GLU B HG3  1 
ATOM   4223 N  N    . ALA B  1 56  ? -64.21600 -10.94100 19.51900  1.000 17.04447  ? 56  ALA B N    1 
ATOM   4224 C  CA   . ALA B  1 56  ? -65.03300 -11.59900 18.51400  1.000 17.90294  ? 56  ALA B CA   1 
ATOM   4225 C  C    . ALA B  1 56  ? -64.20000 -12.54300 17.66800  1.000 17.24142  ? 56  ALA B C    1 
ATOM   4226 O  O    . ALA B  1 56  ? -63.01000 -12.34200 17.45100  1.000 17.73569  ? 56  ALA B O    1 
ATOM   4227 C  CB   . ALA B  1 56  ? -65.70300 -10.54300 17.62700  1.000 18.71688  ? 56  ALA B CB   1 
ATOM   4228 H  H    . ALA B  1 56  ? -64.17500 -10.08700 19.42800  1.000 20.45593  ? 56  ALA B H    1 
ATOM   4229 H  HA   . ALA B  1 56  ? -65.72300 -12.12600 18.94700  1.000 21.48609  ? 56  ALA B HA   1 
ATOM   4230 H  HB1  . ALA B  1 56  ? -66.24300 -10.99000 16.95700  1.000 22.46281  ? 56  ALA B HB1  1 
ATOM   4231 H  HB2  . ALA B  1 56  ? -66.26300 -9.97600  18.18000  1.000 22.46281  ? 56  ALA B HB2  1 
ATOM   4232 H  HB3  . ALA B  1 56  ? -65.01600 -10.01100 17.19700  1.000 22.46281  ? 56  ALA B HB3  1 
ATOM   4233 N  N    . ASP B  1 57  ? -64.87300 -13.55500 17.11600  1.000 18.89946  ? 57  ASP B N    1 
ATOM   4234 C  CA   . ASP B  1 57  ? -64.17800 -14.54600 16.30600  1.000 18.73002  ? 57  ASP B CA   1 
ATOM   4235 C  C    . ASP B  1 57  ? -63.57400 -13.95400 15.03800  1.000 21.44163  ? 57  ASP B C    1 
ATOM   4236 O  O    . ASP B  1 57  ? -62.59100 -14.48500 14.52600  1.000 21.55209  ? 57  ASP B O    1 
ATOM   4237 C  CB   . ASP B  1 57  ? -65.13500 -15.67300 15.92000  1.000 22.96806  ? 57  ASP B CB   1 
ATOM   4238 C  CG   . ASP B  1 57  ? -65.44400 -16.63600 17.05900  1.000 27.93627  ? 57  ASP B CG   1 
ATOM   4239 O  OD1  . ASP B  1 57  ? -64.66700 -16.76100 18.03200  1.000 27.56606  ? 57  ASP B OD1  1 
ATOM   4240 O  OD2  . ASP B  1 57  ? -66.50200 -17.29600 16.95300  1.000 34.04427  ? 57  ASP B OD2  1 
ATOM   4241 H  H    . ASP B  1 57  ? -65.71900 -13.68700 17.19600  1.000 22.68191  ? 57  ASP B H    1 
ATOM   4242 H  HA   . ASP B  1 57  ? -63.45600 -14.90600 16.84500  1.000 22.47858  ? 57  ASP B HA   1 
ATOM   4243 H  HB2  . ASP B  1 57  ? -65.97300 -15.28300 15.62700  1.000 27.56423  ? 57  ASP B HB2  1 
ATOM   4244 H  HB3  . ASP B  1 57  ? -64.73700 -16.18600 15.19900  1.000 27.56423  ? 57  ASP B HB3  1 
ATOM   4245 N  N    . SER B  1 58  ? -64.16500 -12.88800 14.49000  1.000 20.45289  ? 58  SER B N    1 
ATOM   4246 C  CA   . SER B  1 58  ? -63.61000 -12.23200 13.31800  1.000 23.15008  ? 58  SER B CA   1 
ATOM   4247 C  C    . SER B  1 58  ? -63.46600 -10.73400 13.53500  1.000 18.51630  ? 58  SER B C    1 
ATOM   4248 O  O    . SER B  1 58  ? -64.30300 -10.10600 14.21100  1.000 19.34546  ? 58  SER B O    1 
ATOM   4249 C  CB   . SER B  1 58  ? -64.53500 -12.41400 12.10700  1.000 27.61262  ? 58  SER B CB   1 
ATOM   4250 O  OG   . SER B  1 58  ? -63.91900 -11.78600 10.99600  1.000 36.54225  ? 58  SER B OG   1 
ATOM   4251 H  H    . SER B  1 58  ? -64.88900 -12.53000 14.78600  1.000 24.54603  ? 58  SER B H    1 
ATOM   4252 H  HA   . SER B  1 58  ? -62.73300 -12.61400 13.15600  1.000 27.78266  ? 58  SER B HA   1 
ATOM   4253 H  HB2  . SER B  1 58  ? -64.65600 -13.35900 11.92500  1.000 33.13771  ? 58  SER B HB2  1 
ATOM   4254 H  HB3  . SER B  1 58  ? -65.39300 -11.99700 12.28500  1.000 33.13771  ? 58  SER B HB3  1 
ATOM   4255 H  HG   . SER B  1 58  ? -64.43800 -11.79500 10.33600  1.000 43.85326  ? 58  SER B HG   1 
ATOM   4256 N  N    . GLY B  1 59  ? -62.39100 -10.17300 12.98200  1.000 18.92190  ? 59  GLY B N    1 
ATOM   4257 C  CA   . GLY B  1 59  ? -62.25200 -8.76000  12.87600  1.000 19.24054  ? 59  GLY B CA   1 
ATOM   4258 C  C    . GLY B  1 59  ? -63.13300 -8.19600  11.76500  1.000 17.11648  ? 59  GLY B C    1 
ATOM   4259 O  O    . GLY B  1 59  ? -63.91400 -8.92400  11.11500  1.000 19.92836  ? 59  GLY B O    1 
ATOM   4260 H  H    . GLY B  1 59  ? -61.72600 -10.61300 12.66000  1.000 22.70884  ? 59  GLY B H    1 
ATOM   4261 H  HA2  . GLY B  1 59  ? -62.50700 -8.34400  13.71500  1.000 23.09121  ? 59  GLY B HA2  1 
ATOM   4262 H  HA3  . GLY B  1 59  ? -61.32800 -8.53800  12.68200  1.000 23.09121  ? 59  GLY B HA3  1 
ATOM   4263 N  N    . PRO B  1 60  ? -63.02200 -6.88800  11.54300  1.000 16.40580  ? 60  PRO B N    1 
ATOM   4264 C  CA   . PRO B  1 60  ? -63.95400 -6.20700  10.63800  1.000 18.07562  ? 60  PRO B CA   1 
ATOM   4265 C  C    . PRO B  1 60  ? -63.70600 -6.37700  9.17400   1.000 18.76269  ? 60  PRO B C    1 
ATOM   4266 O  O    . PRO B  1 60  ? -64.62300 -6.09100  8.39300   1.000 19.61077  ? 60  PRO B O    1 
ATOM   4267 C  CB   . PRO B  1 60  ? -63.81000 -4.73300  11.06900  1.000 20.38843  ? 60  PRO B CB   1 
ATOM   4268 C  CG   . PRO B  1 60  ? -62.38000 -4.67100  11.54500  1.000 19.68964  ? 60  PRO B CG   1 
ATOM   4269 C  CD   . PRO B  1 60  ? -62.17400 -5.93700  12.28700  1.000 17.20619  ? 60  PRO B CD   1 
ATOM   4270 H  HA   . PRO B  1 60  ? -64.85500 -6.52300  10.81000  1.000 21.69331  ? 60  PRO B HA   1 
ATOM   4271 H  HB2  . PRO B  1 60  ? -63.96100 -4.14100  10.31600  1.000 24.46867  ? 60  PRO B HB2  1 
ATOM   4272 H  HB3  . PRO B  1 60  ? -64.43300 -4.52500  11.78400  1.000 24.46867  ? 60  PRO B HB3  1 
ATOM   4273 H  HG2  . PRO B  1 60  ? -61.78000 -4.61100  10.78600  1.000 23.63012  ? 60  PRO B HG2  1 
ATOM   4274 H  HG3  . PRO B  1 60  ? -62.25700 -3.90400  12.12600  1.000 23.63012  ? 60  PRO B HG3  1 
ATOM   4275 H  HD2  . PRO B  1 60  ? -61.24200 -6.20700  12.26100  1.000 20.64999  ? 60  PRO B HD2  1 
ATOM   4276 H  HD3  . PRO B  1 60  ? -62.46900 -5.85300  13.20700  1.000 20.64999  ? 60  PRO B HD3  1 
ATOM   4277 N  N    . TYR B  1 61  ? -62.50500 -6.79900  8.76000   1.000 16.88029  ? 61  TYR B N    1 
ATOM   4278 C  CA   . TYR B  1 61  ? -62.19900 -6.87300  7.34600   1.000 17.75546  ? 61  TYR B CA   1 
ATOM   4279 C  C    . TYR B  1 61  ? -62.59200 -8.22000  6.77000   1.000 17.27579  ? 61  TYR B C    1 
ATOM   4280 O  O    . TYR B  1 61  ? -62.45400 -9.25600  7.42500   1.000 21.05924  ? 61  TYR B O    1 
ATOM   4281 C  CB   . TYR B  1 61  ? -60.69500 -6.65800  7.12100   1.000 17.90562  ? 61  TYR B CB   1 
ATOM   4282 C  CG   . TYR B  1 61  ? -60.23700 -5.26900  7.47900   1.000 18.33634  ? 61  TYR B CG   1 
ATOM   4283 C  CD1  . TYR B  1 61  ? -60.44500 -4.22200  6.63400   1.000 25.72490  ? 61  TYR B CD1  1 
ATOM   4284 C  CD2  . TYR B  1 61  ? -59.63400 -5.00700  8.68500   1.000 19.46487  ? 61  TYR B CD2  1 
ATOM   4285 C  CE1  . TYR B  1 61  ? -60.06700 -2.94000  6.97900   1.000 27.09194  ? 61  TYR B CE1  1 
ATOM   4286 C  CE2  . TYR B  1 61  ? -59.24400 -3.76600  9.01200   1.000 20.44884  ? 61  TYR B CE2  1 
ATOM   4287 C  CZ   . TYR B  1 61  ? -59.45700 -2.73100  8.19900   1.000 22.99132  ? 61  TYR B CZ   1 
ATOM   4288 O  OH   . TYR B  1 61  ? -59.07300 -1.45700  8.54700   1.000 24.72538  ? 61  TYR B OH   1 
ATOM   4289 H  H    . TYR B  1 61  ? -61.86500 -7.04200  9.28000   1.000 20.25891  ? 61  TYR B H    1 
ATOM   4290 H  HA   . TYR B  1 61  ? -62.70100 -6.18500  6.88200   1.000 21.30911  ? 61  TYR B HA   1 
ATOM   4291 H  HB2  . TYR B  1 61  ? -60.20200 -7.28700  7.67100   1.000 21.48931  ? 61  TYR B HB2  1 
ATOM   4292 H  HB3  . TYR B  1 61  ? -60.49300 -6.80800  6.18400   1.000 21.48931  ? 61  TYR B HB3  1 
ATOM   4293 H  HD1  . TYR B  1 61  ? -60.84900 -4.37300  5.81000   1.000 30.87244  ? 61  TYR B HD1  1 
ATOM   4294 H  HD2  . TYR B  1 61  ? -59.49400 -5.70300  9.28600   1.000 23.36040  ? 61  TYR B HD2  1 
ATOM   4295 H  HE1  . TYR B  1 61  ? -60.22000 -2.22900  6.40000   1.000 32.51289  ? 61  TYR B HE1  1 
ATOM   4296 H  HE2  . TYR B  1 61  ? -58.81500 -3.62400  9.82500   1.000 24.54117  ? 61  TYR B HE2  1 
ATOM   4297 H  HH   . TYR B  1 61  ? -59.40900 -0.90000  8.01500   1.000 29.67302  ? 61  TYR B HH   1 
ATOM   4298 N  N    . THR B  1 62  ? -63.07200 -8.19500  5.55000   1.000 20.58795  ? 62  THR B N    1 
ATOM   4299 C  CA   . THR B  1 62  ? -63.31700 -9.39500  4.78100   1.000 19.97169  ? 62  THR B CA   1 
ATOM   4300 C  C    . THR B  1 62  ? -61.97300 -9.82900  4.21500   1.000 18.16837  ? 62  THR B C    1 
ATOM   4301 O  O    . THR B  1 62  ? -61.21300 -9.00600  3.68900   1.000 18.98288  ? 62  THR B O    1 
ATOM   4302 C  CB   . THR B  1 62  ? -64.28400 -9.07100  3.65500   1.000 22.07372  ? 62  THR B CB   1 
ATOM   4303 O  OG1  . THR B  1 62  ? -65.56700 -8.70500  4.19200   1.000 24.17126  ? 62  THR B OG1  1 
ATOM   4304 C  CG2  . THR B  1 62  ? -64.50700 -10.25900 2.72000   1.000 23.99764  ? 62  THR B CG2  1 
ATOM   4305 H  H    . THR B  1 62  ? -63.27200 -7.47300  5.12700   1.000 24.70810  ? 62  THR B H    1 
ATOM   4306 H  HA   . THR B  1 62  ? -63.70600 -10.11000 5.30900   1.000 23.96859  ? 62  THR B HA   1 
ATOM   4307 H  HB   . THR B  1 62  ? -63.89600 -8.34200  3.14700   1.000 26.49103  ? 62  THR B HB   1 
ATOM   4308 H  HG1  . THR B  1 62  ? -65.50400 -7.98900  4.62500   1.000 29.00807  ? 62  THR B HG1  1 
ATOM   4309 H  HG21 . THR B  1 62  ? -65.21300 -10.05400 2.08700   1.000 28.79973  ? 62  THR B HG21 1 
ATOM   4310 H  HG22 . THR B  1 62  ? -63.69200 -10.45400 2.23200   1.000 28.79973  ? 62  THR B HG22 1 
ATOM   4311 H  HG23 . THR B  1 62  ? -64.76300 -11.04100 3.23300   1.000 28.79973  ? 62  THR B HG23 1 
ATOM   4312 N  N    . ILE B  1 63  ? -61.70700 -11.12600 4.27100   1.000 17.88393  ? 63  ILE B N    1 
ATOM   4313 C  CA   . ILE B  1 63  ? -60.41500 -11.63900 3.86000   1.000 17.70587  ? 63  ILE B CA   1 
ATOM   4314 C  C    . ILE B  1 63  ? -60.54300 -12.66200 2.75600   1.000 19.42662  ? 63  ILE B C    1 
ATOM   4315 O  O    . ILE B  1 63  ? -61.58500 -13.29300 2.55400   1.000 21.38040  ? 63  ILE B O    1 
ATOM   4316 C  CB   . ILE B  1 63  ? -59.60900 -12.23000 5.06600   1.000 18.14255  ? 63  ILE B CB   1 
ATOM   4317 C  CG1  . ILE B  1 63  ? -60.31300 -13.46900 5.58900   1.000 18.67366  ? 63  ILE B CG1  1 
ATOM   4318 C  CG2  . ILE B  1 63  ? -59.40300 -11.14700 6.09900   1.000 18.56934  ? 63  ILE B CG2  1 
ATOM   4319 C  CD1  . ILE B  1 63  ? -59.47700 -14.18800 6.69700   1.000 22.72916  ? 63  ILE B CD1  1 
ATOM   4320 H  H    . ILE B  1 63  ? -62.26000 -11.72600 4.54300   1.000 21.46328  ? 63  ILE B H    1 
ATOM   4321 H  HA   . ILE B  1 63  ? -59.92400 -10.89600 3.47600   1.000 21.24961  ? 63  ILE B HA   1 
ATOM   4322 H  HB   . ILE B  1 63  ? -58.72600 -12.52300 4.79100   1.000 21.77362  ? 63  ILE B HB   1 
ATOM   4323 H  HG12 . ILE B  1 63  ? -61.16700 -13.21300 5.97100   1.000 22.41096  ? 63  ILE B HG12 1 
ATOM   4324 H  HG13 . ILE B  1 63  ? -60.45000 -14.09200 4.85900   1.000 22.41096  ? 63  ILE B HG13 1 
ATOM   4325 H  HG21 . ILE B  1 63  ? -58.89300 -11.51000 6.84000   1.000 22.28577  ? 63  ILE B HG21 1 
ATOM   4326 H  HG22 . ILE B  1 63  ? -58.91900 -10.41200 5.69300   1.000 22.28577  ? 63  ILE B HG22 1 
ATOM   4327 H  HG23 . ILE B  1 63  ? -60.26800 -10.84100 6.41200   1.000 22.28577  ? 63  ILE B HG23 1 
ATOM   4328 H  HD11 . ILE B  1 63  ? -59.90300 -15.03100 6.91600   1.000 27.27755  ? 63  ILE B HD11 1 
ATOM   4329 H  HD12 . ILE B  1 63  ? -58.58100 -14.34700 6.36200   1.000 27.27755  ? 63  ILE B HD12 1 
ATOM   4330 H  HD13 . ILE B  1 63  ? -59.44100 -13.62100 7.48300   1.000 27.27755  ? 63  ILE B HD13 1 
ATOM   4331 N  N    . ALA B  1 64  ? -59.41700 -12.81800 2.04200   1.000 19.42746  ? 64  ALA B N    1 
ATOM   4332 C  CA   . ALA B  1 64  ? -59.24200 -13.86000 1.04300   1.000 19.60274  ? 64  ALA B CA   1 
ATOM   4333 C  C    . ALA B  1 64  ? -57.97600 -14.62000 1.37900   1.000 18.73949  ? 64  ALA B C    1 
ATOM   4334 O  O    . ALA B  1 64  ? -57.19600 -14.20200 2.23800   1.000 19.21038  ? 64  ALA B O    1 
ATOM   4335 C  CB   . ALA B  1 64  ? -59.13100 -13.23700 -0.36100  1.000 21.64102  ? 64  ALA B CB   1 
ATOM   4336 H  H    . ALA B  1 64  ? -58.72600 -12.31300 2.12800   1.000 23.31551  ? 64  ALA B H    1 
ATOM   4337 H  HA   . ALA B  1 64  ? -59.99100 -14.47700 1.05000   1.000 23.52585  ? 64  ALA B HA   1 
ATOM   4338 H  HB1  . ALA B  1 64  ? -58.98900 -13.94400 -1.01000  1.000 25.97179  ? 64  ALA B HB1  1 
ATOM   4339 H  HB2  . ALA B  1 64  ? -59.95300 -12.76300 -0.56200  1.000 25.97179  ? 64  ALA B HB2  1 
ATOM   4340 H  HB3  . ALA B  1 64  ? -58.38200 -12.62100 -0.37500  1.000 25.97179  ? 64  ALA B HB3  1 
ATOM   4341 N  N    . THR B  1 65  ? -57.76200 -15.73000 0.67100   1.000 21.88909  ? 65  THR B N    1 
ATOM   4342 C  CA   . THR B  1 65  ? -56.56700 -16.51200 0.85100   1.000 20.51321  ? 65  THR B CA   1 
ATOM   4343 C  C    . THR B  1 65  ? -55.88700 -16.77300 -0.47500  1.000 21.79945  ? 65  THR B C    1 
ATOM   4344 O  O    . THR B  1 65  ? -56.52000 -16.78800 -1.53900  1.000 22.57920  ? 65  THR B O    1 
ATOM   4345 C  CB   . THR B  1 65  ? -56.85500 -17.85800 1.50100   1.000 23.72409  ? 65  THR B CB   1 
ATOM   4346 O  OG1  . THR B  1 65  ? -57.72500 -18.61400 0.66500   1.000 27.32498  ? 65  THR B OG1  1 
ATOM   4347 C  CG2  . THR B  1 65  ? -57.49600 -17.69600 2.85700   1.000 24.67215  ? 65  THR B CG2  1 
ATOM   4348 H  H    . THR B  1 65  ? -58.30500 -16.04100 0.08000   1.000 26.26947  ? 65  THR B H    1 
ATOM   4349 H  HA   . THR B  1 65  ? -55.96800 -15.99800 1.41500   1.000 24.61841  ? 65  THR B HA   1 
ATOM   4350 H  HB   . THR B  1 65  ? -56.01600 -18.32900 1.62400   1.000 28.47147  ? 65  THR B HB   1 
ATOM   4351 H  HG1  . THR B  1 65  ? -57.92600 -19.33900 1.03900   1.000 32.79254  ? 65  THR B HG1  1 
ATOM   4352 H  HG21 . THR B  1 65  ? -57.59700 -18.56200 3.28100   1.000 29.60915  ? 65  THR B HG21 1 
ATOM   4353 H  HG22 . THR B  1 65  ? -56.94300 -17.13200 3.42000   1.000 29.60915  ? 65  THR B HG22 1 
ATOM   4354 H  HG23 . THR B  1 65  ? -58.37100 -17.28700 2.76300   1.000 29.60915  ? 65  THR B HG23 1 
ATOM   4355 N  N    . SER B  1 66  ? -54.58600 -17.03900 -0.36900  1.000 21.23073  ? 66  SER B N    1 
ATOM   4356 C  CA   . SER B  1 66  ? -53.80000 -17.46400 -1.52100  1.000 21.98699  ? 66  SER B CA   1 
ATOM   4357 C  C    . SER B  1 66  ? -52.81600 -18.52400 -1.06400  1.000 22.76020  ? 66  SER B C    1 
ATOM   4358 O  O    . SER B  1 66  ? -52.10900 -18.33100 -0.07300  1.000 23.59460  ? 66  SER B O    1 
ATOM   4359 C  CB   . SER B  1 66  ? -53.03000 -16.27200 -2.08800  1.000 26.49656  ? 66  SER B CB   1 
ATOM   4360 O  OG   . SER B  1 66  ? -52.39600 -16.66100 -3.31100  1.000 35.12872  ? 66  SER B OG   1 
ATOM   4361 H  H    . SER B  1 66  ? -54.13700 -16.98000 0.36300   1.000 25.47944  ? 66  SER B H    1 
ATOM   4362 H  HA   . SER B  1 66  ? -54.37400 -17.83900 -2.20700  1.000 26.38696  ? 66  SER B HA   1 
ATOM   4363 H  HB2  . SER B  1 66  ? -53.64600 -15.54300 -2.26200  1.000 31.79844  ? 66  SER B HB2  1 
ATOM   4364 H  HB3  . SER B  1 66  ? -52.35500 -15.99100 -1.45100  1.000 31.79844  ? 66  SER B HB3  1 
ATOM   4365 H  HG   . SER B  1 66  ? -51.84500 -16.07300 -3.54900  1.000 42.15703  ? 66  SER B HG   1 
ATOM   4366 N  N    . ASN B  1 67  ? -52.73600 -19.61800 -1.80300  1.000 24.85592  ? 67  ASN B N    1 
ATOM   4367 C  CA   . ASN B  1 67  ? -51.85200 -20.71000 -1.44600  1.000 25.09033  ? 67  ASN B CA   1 
ATOM   4368 C  C    . ASN B  1 67  ? -50.46000 -20.50100 -2.00500  1.000 24.63044  ? 67  ASN B C    1 
ATOM   4369 O  O    . ASN B  1 67  ? -50.29200 -20.04800 -3.14400  1.000 29.11035  ? 67  ASN B O    1 
ATOM   4370 C  CB   . ASN B  1 67  ? -52.40000 -22.03000 -1.98400  1.000 27.24434  ? 67  ASN B CB   1 
ATOM   4371 C  CG   . ASN B  1 67  ? -53.71200 -22.42100 -1.33200  1.000 41.25333  ? 67  ASN B CG   1 
ATOM   4372 O  OD1  . ASN B  1 67  ? -54.00900 -21.99100 -0.21700  1.000 54.51771  ? 67  ASN B OD1  1 
ATOM   4373 N  ND2  . ASN B  1 67  ? -54.50300 -23.24000 -2.02300  1.000 53.27086  ? 67  ASN B ND2  1 
ATOM   4374 H  H    . ASN B  1 67  ? -53.18800 -19.75200 -2.52200  1.000 29.82966  ? 67  ASN B H    1 
ATOM   4375 H  HA   . ASN B  1 67  ? -51.78800 -20.74900 -0.47800  1.000 30.11096  ? 67  ASN B HA   1 
ATOM   4376 H  HB2  . ASN B  1 67  ? -52.55100 -21.94500 -2.93800  1.000 32.69577  ? 67  ASN B HB2  1 
ATOM   4377 H  HB3  . ASN B  1 67  ? -51.75600 -22.73400 -1.81100  1.000 32.69577  ? 67  ASN B HB3  1 
ATOM   4378 H  HD21 . ASN B  1 67  ? -54.25900 -23.52000 -2.79900  1.000 63.92760  ? 67  ASN B HD21 1 
ATOM   4379 H  HD22 . ASN B  1 67  ? -55.25700 -23.48900 -1.69400  1.000 63.92760  ? 67  ASN B HD22 1 
ATOM   4380 N  N    . VAL B  1 68  ? -49.46200 -20.86000 -1.19600  1.000 24.78945  ? 68  VAL B N    1 
ATOM   4381 C  CA   . VAL B  1 68  ? -48.05500 -20.78000 -1.56900  1.000 26.15968  ? 68  VAL B CA   1 
ATOM   4382 C  C    . VAL B  1 68  ? -47.50700 -22.20200 -1.58100  1.000 25.33913  ? 68  VAL B C    1 
ATOM   4383 O  O    . VAL B  1 68  ? -47.51200 -22.89100 -0.55300  1.000 25.81151  ? 68  VAL B O    1 
ATOM   4384 C  CB   . VAL B  1 68  ? -47.26400 -19.89600 -0.59500  1.000 27.22971  ? 68  VAL B CB   1 
ATOM   4385 C  CG1  . VAL B  1 68  ? -45.80100 -19.86400 -0.99600  1.000 27.61137  ? 68  VAL B CG1  1 
ATOM   4386 C  CG2  . VAL B  1 68  ? -47.86300 -18.48200 -0.53400  1.000 27.10348  ? 68  VAL B CG2  1 
ATOM   4387 H  H    . VAL B  1 68  ? -49.58300 -21.16300 -0.40000  1.000 29.74990  ? 68  VAL B H    1 
ATOM   4388 H  HA   . VAL B  1 68  ? -47.97000 -20.40800 -2.46000  1.000 31.39418  ? 68  VAL B HA   1 
ATOM   4389 H  HB   . VAL B  1 68  ? -47.32100 -20.27000 0.29800   1.000 32.67821  ? 68  VAL B HB   1 
ATOM   4390 H  HG11 . VAL B  1 68  ? -45.34700 -19.18000 -0.48000  1.000 33.13620  ? 68  VAL B HG11 1 
ATOM   4391 H  HG12 . VAL B  1 68  ? -45.40500 -20.73100 -0.81600  1.000 33.13620  ? 68  VAL B HG12 1 
ATOM   4392 H  HG13 . VAL B  1 68  ? -45.73700 -19.66100 -1.94200  1.000 33.13620  ? 68  VAL B HG13 1 
ATOM   4393 H  HG21 . VAL B  1 68  ? -47.32000 -17.93500 0.05500   1.000 32.52674  ? 68  VAL B HG21 1 
ATOM   4394 H  HG22 . VAL B  1 68  ? -47.86800 -18.10300 -1.42700  1.000 32.52674  ? 68  VAL B HG22 1 
ATOM   4395 H  HG23 . VAL B  1 68  ? -48.76900 -18.53800 -0.19200  1.000 32.52674  ? 68  VAL B HG23 1 
ATOM   4396 N  N    . SER B  1 69  ? -47.04700 -22.64600 -2.73300  1.000 27.67989  ? 69  SER B N    1 
ATOM   4397 C  CA   . SER B  1 69  ? -46.57800 -24.01100 -2.85400  1.000 32.58950  ? 69  SER B CA   1 
ATOM   4398 C  C    . SER B  1 69  ? -45.31300 -24.24700 -2.03500  1.000 33.16040  ? 69  SER B C    1 
ATOM   4399 O  O    . SER B  1 69  ? -44.51200 -23.33900 -1.80100  1.000 28.10436  ? 69  SER B O    1 
ATOM   4400 C  CB   . SER B  1 69  ? -46.29600 -24.27600 -4.33600  1.000 36.36641  ? 69  SER B CB   1 
ATOM   4401 O  OG   . SER B  1 69  ? -45.36300 -25.31500 -4.53400  1.000 33.40851  ? 69  SER B OG   1 
ATOM   4402 H  H    . SER B  1 69  ? -46.99700 -22.18200 -3.45500  1.000 33.21843  ? 69  SER B H    1 
ATOM   4403 H  HA   . SER B  1 69  ? -47.24600 -24.63000 -2.52100  1.000 39.10997  ? 69  SER B HA   1 
ATOM   4404 H  HB2  . SER B  1 69  ? -47.12800 -24.52200 -4.76900  1.000 43.64225  ? 69  SER B HB2  1 
ATOM   4405 H  HB3  . SER B  1 69  ? -45.94200 -23.46400 -4.73300  1.000 43.64225  ? 69  SER B HB3  1 
ATOM   4406 H  HG   . SER B  1 69  ? -45.31400 -25.50500 -5.35000  1.000 40.09277  ? 69  SER B HG   1 
ATOM   4407 N  N    . SER B  1 70  ? -45.14000 -25.49700 -1.59800  1.000 29.25020  ? 70  SER B N    1 
ATOM   4408 C  CA   . SER B  1 70  ? -43.92400 -25.88300 -0.89200  1.000 30.50013  ? 70  SER B CA   1 
ATOM   4409 C  C    . SER B  1 70  ? -42.68100 -25.78400 -1.76500  1.000 31.73411  ? 70  SER B C    1 
ATOM   4410 O  O    . SER B  1 70  ? -41.55800 -25.86200 -1.24400  1.000 32.79938  ? 70  SER B O    1 
ATOM   4411 C  CB   . SER B  1 70  ? -44.05300 -27.31100 -0.36000  1.000 34.26618  ? 70  SER B CB   1 
ATOM   4412 O  OG   . SER B  1 70  ? -44.13400 -28.25100 -1.41900  1.000 38.86792  ? 70  SER B OG   1 
ATOM   4413 H  H    . SER B  1 70  ? -45.70900 -26.13400 -1.69800  1.000 35.10281  ? 70  SER B H    1 
ATOM   4414 H  HA   . SER B  1 70  ? -43.81000 -25.28700 -0.13500  1.000 36.60272  ? 70  SER B HA   1 
ATOM   4415 H  HB2  . SER B  1 70  ? -43.27600 -27.51600 0.18200   1.000 41.12197  ? 70  SER B HB2  1 
ATOM   4416 H  HB3  . SER B  1 70  ? -44.85900 -27.37400 0.17700   1.000 41.12197  ? 70  SER B HB3  1 
ATOM   4417 H  HG   . SER B  1 70  ? -44.84100 -28.12900 -1.85700  1.000 46.64406  ? 70  SER B HG   1 
ATOM   4418 N  N    . LEU B  1 71  ? -42.84400 -25.65700 -3.08400  1.000 31.88281  ? 71  LEU B N    1 
ATOM   4419 C  CA   . LEU B  1 71  ? -41.70600 -25.43400 -3.95500  1.000 38.00972  ? 71  LEU B CA   1 
ATOM   4420 C  C    . LEU B  1 71  ? -41.06200 -24.07400 -3.74300  1.000 37.81788  ? 71  LEU B C    1 
ATOM   4421 O  O    . LEU B  1 71  ? -39.96800 -23.84300 -4.28300  1.000 35.13365  ? 71  LEU B O    1 
ATOM   4422 C  CB   . LEU B  1 71  ? -42.13100 -25.58100 -5.41900  1.000 41.00602  ? 71  LEU B CB   1 
ATOM   4423 C  CG   . LEU B  1 71  ? -42.46400 -27.01100 -5.81300  1.000 51.72391  ? 71  LEU B CG   1 
ATOM   4424 C  CD1  . LEU B  1 71  ? -43.06500 -27.04100 -7.20500  1.000 50.54213  ? 71  LEU B CD1  1 
ATOM   4425 C  CD2  . LEU B  1 71  ? -41.23300 -27.87700 -5.78300  1.000 53.84997  ? 71  LEU B CD2  1 
ATOM   4426 H  H    . LEU B  1 71  ? -43.60100 -25.69800 -3.49100  1.000 38.26194  ? 71  LEU B H    1 
ATOM   4427 H  HA   . LEU B  1 71  ? -41.03600 -26.11000 -3.76900  1.000 45.61422  ? 71  LEU B HA   1 
ATOM   4428 H  HB2  . LEU B  1 71  ? -42.92000 -25.03800 -5.57100  1.000 49.20978  ? 71  LEU B HB2  1 
ATOM   4429 H  HB3  . LEU B  1 71  ? -41.40500 -25.27700 -5.98700  1.000 49.20978  ? 71  LEU B HB3  1 
ATOM   4430 H  HG   . LEU B  1 71  ? -43.10600 -27.36500 -5.17800  1.000 62.07125  ? 71  LEU B HG   1 
ATOM   4431 H  HD11 . LEU B  1 71  ? -43.22700 -27.96300 -7.46000  1.000 60.65311  ? 71  LEU B HD11 1 
ATOM   4432 H  HD12 . LEU B  1 71  ? -43.90000 -26.54800 -7.20000  1.000 60.65311  ? 71  LEU B HD12 1 
ATOM   4433 H  HD13 . LEU B  1 71  ? -42.44300 -26.63100 -7.82600  1.000 60.65311  ? 71  LEU B HD13 1 
ATOM   4434 H  HD21 . LEU B  1 71  ? -41.43000 -28.72200 -6.21800  1.000 64.62253  ? 71  LEU B HD21 1 
ATOM   4435 H  HD22 . LEU B  1 71  ? -40.51500 -27.42300 -6.25200  1.000 64.62253  ? 71  LEU B HD22 1 
ATOM   4436 H  HD23 . LEU B  1 71  ? -40.97800 -28.03300 -4.86000  1.000 64.62253  ? 71  LEU B HD23 1 
ATOM   4437 N  N    . VAL B  1 72  ? -41.70100 -23.17500 -2.98300  1.000 29.13240  ? 72  VAL B N    1 
ATOM   4438 C  CA   . VAL B  1 72  ? -41.10300 -21.87800 -2.68900  1.000 28.99778  ? 72  VAL B CA   1 
ATOM   4439 C  C    . VAL B  1 72  ? -39.76800 -22.07800 -1.98300  1.000 30.75160  ? 72  VAL B C    1 
ATOM   4440 O  O    . VAL B  1 72  ? -39.58000 -23.02900 -1.20500  1.000 32.50380  ? 72  VAL B O    1 
ATOM   4441 C  CB   . VAL B  1 72  ? -42.07600 -21.04500 -1.83100  1.000 30.25346  ? 72  VAL B CB   1 
ATOM   4442 C  CG1  . VAL B  1 72  ? -42.16700 -21.62300 -0.41900  1.000 28.87907  ? 72  VAL B CG1  1 
ATOM   4443 C  CG2  . VAL B  1 72  ? -41.66300 -19.59300 -1.79300  1.000 34.91329  ? 72  VAL B CG2  1 
ATOM   4444 H  H    . VAL B  1 72  ? -42.47600 -23.29500 -2.63000  1.000 34.96145  ? 72  VAL B H    1 
ATOM   4445 H  HA   . VAL B  1 72  ? -40.93400 -21.40100 -3.51600  1.000 34.79989  ? 72  VAL B HA   1 
ATOM   4446 H  HB   . VAL B  1 72  ? -42.95700 -21.08600 -2.23500  1.000 36.30671  ? 72  VAL B HB   1 
ATOM   4447 H  HG11 . VAL B  1 72  ? -42.93900 -21.24300 0.02900   1.000 34.65744  ? 72  VAL B HG11 1 
ATOM   4448 H  HG12 . VAL B  1 72  ? -42.26100 -22.58700 -0.47800  1.000 34.65744  ? 72  VAL B HG12 1 
ATOM   4449 H  HG13 . VAL B  1 72  ? -41.35800 -21.39900 0.06700   1.000 34.65744  ? 72  VAL B HG13 1 
ATOM   4450 H  HG21 . VAL B  1 72  ? -42.35800 -19.07900 -1.35400  1.000 41.89851  ? 72  VAL B HG21 1 
ATOM   4451 H  HG22 . VAL B  1 72  ? -40.83100 -19.51500 -1.29900  1.000 41.89851  ? 72  VAL B HG22 1 
ATOM   4452 H  HG23 . VAL B  1 72  ? -41.54000 -19.27600 -2.70100  1.000 41.89851  ? 72  VAL B HG23 1 
ATOM   4453 N  N    . ARG B  1 73  ? -38.82500 -21.18300 -2.27000  1.000 34.65219  ? 73  ARG B N    1 
ATOM   4454 C  CA   . ARG B  1 73  ? -37.48900 -21.26300 -1.69200  1.000 31.21322  ? 73  ARG B CA   1 
ATOM   4455 C  C    . ARG B  1 73  ? -37.48300 -20.70400 -0.27400  1.000 30.45420  ? 73  ARG B C    1 
ATOM   4456 O  O    . ARG B  1 73  ? -37.99500 -19.60900 -0.01900  1.000 36.32535  ? 73  ARG B O    1 
ATOM   4457 C  CB   . ARG B  1 73  ? -36.51000 -20.47400 -2.55800  1.000 40.19143  ? 73  ARG B CB   1 
ATOM   4458 C  CG   . ARG B  1 73  ? -36.19500 -21.13200 -3.90000  1.000 45.57859  ? 73  ARG B CG   1 
ATOM   4459 C  CD   . ARG B  1 73  ? -34.71300 -21.52500 -3.99400  1.000 75.68977  ? 73  ARG B CD   1 
ATOM   4460 N  NE   . ARG B  1 73  ? -34.42700 -22.76300 -3.27500  1.000 93.40090  ? 73  ARG B NE   1 
ATOM   4461 C  CZ   . ARG B  1 73  ? -33.33900 -22.99000 -2.54800  1.000 77.46433  ? 73  ARG B CZ   1 
ATOM   4462 N  NH1  . ARG B  1 73  ? -32.40600 -22.06500 -2.38500  1.000 75.54407  ? 73  ARG B NH1  1 
ATOM   4463 N  NH2  . ARG B  1 73  ? -33.19200 -24.17100 -1.95400  1.000 65.38201  ? 73  ARG B NH2  1 
ATOM   4464 H  H    . ARG B  1 73  ? -38.93600 -20.51600 -2.80100  1.000 41.58518  ? 73  ARG B H    1 
ATOM   4465 H  HA   . ARG B  1 73  ? -37.21000 -22.19200 -1.65200  1.000 37.45842  ? 73  ARG B HA   1 
ATOM   4466 H  HB2  . ARG B  1 73  ? -36.89100 -19.60100 -2.74000  1.000 48.23227  ? 73  ARG B HB2  1 
ATOM   4467 H  HB3  . ARG B  1 73  ? -35.67500 -20.37700 -2.07400  1.000 48.23227  ? 73  ARG B HB3  1 
ATOM   4468 H  HG2  . ARG B  1 73  ? -36.73100 -21.93400 -3.99900  1.000 54.69687  ? 73  ARG B HG2  1 
ATOM   4469 H  HG3  . ARG B  1 73  ? -36.39200 -20.51000 -4.61800  1.000 54.69687  ? 73  ARG B HG3  1 
ATOM   4470 H  HD2  . ARG B  1 73  ? -34.47600 -21.65400 -4.92500  1.000 90.83029  ? 73  ARG B HD2  1 
ATOM   4471 H  HD3  . ARG B  1 73  ? -34.17100 -20.81900 -3.60800  1.000 90.83029  ? 73  ARG B HD3  1 
ATOM   4472 H  HE   . ARG B  1 73  ? -35.00800 -23.39500 -3.32700  1.000 112.08364 ? 73  ARG B HE   1 
ATOM   4473 H  HH11 . ARG B  1 73  ? -32.49600 -21.29300 -2.75400  1.000 90.65545  ? 73  ARG B HH11 1 
ATOM   4474 H  HH12 . ARG B  1 73  ? -31.71000 -22.23500 -1.90900  1.000 90.65545  ? 73  ARG B HH12 1 
ATOM   4475 H  HH21 . ARG B  1 73  ? -33.79700 -24.77600 -2.04300  1.000 78.46098  ? 73  ARG B HH21 1 
ATOM   4476 H  HH22 . ARG B  1 73  ? -32.49200 -24.33000 -1.48000  1.000 78.46098  ? 73  ARG B HH22 1 
ATOM   4477 N  N    . GLY B  1 74  ? -36.89900 -21.46200 0.64700   1.000 28.19218  ? 74  GLY B N    1 
ATOM   4478 C  CA   . GLY B  1 74  ? -36.61900 -20.94900 1.97300   1.000 27.94171  ? 74  GLY B CA   1 
ATOM   4479 C  C    . GLY B  1 74  ? -37.57000 -21.39400 3.05900   1.000 24.20451  ? 74  GLY B C    1 
ATOM   4480 O  O    . GLY B  1 74  ? -37.25200 -21.19400 4.24100   1.000 25.47399  ? 74  GLY B O    1 
ATOM   4481 H  H    . GLY B  1 74  ? -36.65600 -22.27800 0.52300   1.000 33.83318  ? 74  GLY B H    1 
ATOM   4482 H  HA2  . GLY B  1 74  ? -35.72800 -21.23100 2.23100   1.000 33.53261  ? 74  GLY B HA2  1 
ATOM   4483 H  HA3  . GLY B  1 74  ? -36.64700 -19.98000 1.93900   1.000 33.53261  ? 74  GLY B HA3  1 
ATOM   4484 N  N    . PHE B  1 75  ? -38.70200 -21.99100 2.70300   1.000 25.35824  ? 75  PHE B N    1 
ATOM   4485 C  CA   . PHE B  1 75  ? -39.65600 -22.53900 3.66300   1.000 23.76104  ? 75  PHE B CA   1 
ATOM   4486 C  C    . PHE B  1 75  ? -40.53800 -23.55300 2.93000   1.000 25.90490  ? 75  PHE B C    1 
ATOM   4487 O  O    . PHE B  1 75  ? -40.34500 -23.83700 1.74400   1.000 26.57017  ? 75  PHE B O    1 
ATOM   4488 C  CB   . PHE B  1 75  ? -40.43600 -21.43900 4.40700   1.000 23.96863  ? 75  PHE B CB   1 
ATOM   4489 C  CG   . PHE B  1 75  ? -41.28900 -20.56300 3.52500   1.000 23.14694  ? 75  PHE B CG   1 
ATOM   4490 C  CD1  . PHE B  1 75  ? -40.72000 -19.59100 2.72700   1.000 23.26744  ? 75  PHE B CD1  1 
ATOM   4491 C  CD2  . PHE B  1 75  ? -42.66900 -20.69800 3.53800   1.000 22.94851  ? 75  PHE B CD2  1 
ATOM   4492 C  CE1  . PHE B  1 75  ? -41.50800 -18.79200 1.93500   1.000 24.12967  ? 75  PHE B CE1  1 
ATOM   4493 C  CE2  . PHE B  1 75  ? -43.46100 -19.90500 2.76800   1.000 22.07988  ? 75  PHE B CE2  1 
ATOM   4494 C  CZ   . PHE B  1 75  ? -42.89700 -18.94500 1.95100   1.000 22.75050  ? 75  PHE B CZ   1 
ATOM   4495 H  H    . PHE B  1 75  ? -38.94900 -22.09500 1.88600   1.000 30.43245  ? 75  PHE B H    1 
ATOM   4496 H  HA   . PHE B  1 75  ? -39.17600 -23.02700 4.35000   1.000 28.51581  ? 75  PHE B HA   1 
ATOM   4497 H  HB2  . PHE B  1 75  ? -41.02200 -21.86200 5.05300   1.000 28.76492  ? 75  PHE B HB2  1 
ATOM   4498 H  HB3  . PHE B  1 75  ? -39.80000 -20.86500 4.86100   1.000 28.76492  ? 75  PHE B HB3  1 
ATOM   4499 H  HD1  . PHE B  1 75  ? -39.79700 -19.47700 2.72500   1.000 27.92349  ? 75  PHE B HD1  1 
ATOM   4500 H  HD2  . PHE B  1 75  ? -43.06000 -21.34200 4.08300   1.000 27.54077  ? 75  PHE B HD2  1 
ATOM   4501 H  HE1  . PHE B  1 75  ? -41.11700 -18.14900 1.38800   1.000 28.95817  ? 75  PHE B HE1  1 
ATOM   4502 H  HE2  . PHE B  1 75  ? -44.38400 -20.01000 2.79200   1.000 26.49841  ? 75  PHE B HE2  1 
ATOM   4503 H  HZ   . PHE B  1 75  ? -43.43600 -18.40600 1.41800   1.000 27.30317  ? 75  PHE B HZ   1 
ATOM   4504 N  N    . GLY B  1 76  ? -41.51300 -24.10400 3.65600   1.000 24.13975  ? 76  GLY B N    1 
ATOM   4505 C  CA   . GLY B  1 76  ? -42.27100 -25.22600 3.14000   1.000 25.52694  ? 76  GLY B CA   1 
ATOM   4506 C  C    . GLY B  1 76  ? -43.63000 -24.88100 2.56800   1.000 26.74341  ? 76  GLY B C    1 
ATOM   4507 O  O    . GLY B  1 76  ? -44.51200 -25.74800 2.47600   1.000 28.83947  ? 76  GLY B O    1 
ATOM   4508 H  H    . GLY B  1 76  ? -41.74800 -23.84400 4.44100   1.000 28.97026  ? 76  GLY B H    1 
ATOM   4509 H  HA2  . GLY B  1 76  ? -41.75600 -25.65100 2.43700   1.000 30.63490  ? 76  GLY B HA2  1 
ATOM   4510 H  HA3  . GLY B  1 76  ? -42.40900 -25.86300 3.85900   1.000 30.63490  ? 76  GLY B HA3  1 
ATOM   4511 N  N    . GLY B  1 77  ? -43.81000 -23.63600 2.13200   1.000 24.37484  ? 77  GLY B N    1 
ATOM   4512 C  CA   . GLY B  1 77  ? -45.09300 -23.21500 1.61100   1.000 24.54110  ? 77  GLY B CA   1 
ATOM   4513 C  C    . GLY B  1 77  ? -45.96400 -22.67300 2.71400   1.000 23.08805  ? 77  GLY B C    1 
ATOM   4514 O  O    . GLY B  1 77  ? -45.56800 -22.59100 3.88000   1.000 23.30478  ? 77  GLY B O    1 
ATOM   4515 H  H    . GLY B  1 77  ? -43.20500 -23.02400 2.13100   1.000 29.25238  ? 77  GLY B H    1 
ATOM   4516 H  HA2  . GLY B  1 77  ? -44.96500 -22.52300 0.94500   1.000 29.45188  ? 77  GLY B HA2  1 
ATOM   4517 H  HA3  . GLY B  1 77  ? -45.54300 -23.97000 1.20000   1.000 29.45188  ? 77  GLY B HA3  1 
ATOM   4518 N  N    . GLY B  1 78  ? -47.17800 -22.29000 2.35200   1.000 23.68037  ? 78  GLY B N    1 
ATOM   4519 C  CA   . GLY B  1 78  ? -48.05000 -21.67600 3.33200   1.000 23.27981  ? 78  GLY B CA   1 
ATOM   4520 C  C    . GLY B  1 78  ? -49.35000 -21.17900 2.72500   1.000 21.93445  ? 78  GLY B C    1 
ATOM   4521 O  O    . GLY B  1 78  ? -49.62800 -21.36400 1.54000   1.000 22.87669  ? 78  GLY B O    1 
ATOM   4522 H  H    . GLY B  1 78  ? -47.51200 -22.37300 1.56300   1.000 28.41901  ? 78  GLY B H    1 
ATOM   4523 H  HA2  . GLY B  1 78  ? -48.26400 -22.32400 4.02100   1.000 27.93833  ? 78  GLY B HA2  1 
ATOM   4524 H  HA3  . GLY B  1 78  ? -47.59500 -20.92100 3.73800   1.000 27.93833  ? 78  GLY B HA3  1 
ATOM   4525 N  N    . THR B  1 79  ? -50.13400 -20.52100 3.57100   1.000 21.52473  ? 79  THR B N    1 
ATOM   4526 C  CA   . THR B  1 79  ? -51.40300 -19.92300 3.17900   1.000 20.17834  ? 79  THR B CA   1 
ATOM   4527 C  C    . THR B  1 79  ? -51.36600 -18.46200 3.58100   1.000 19.21948  ? 79  THR B C    1 
ATOM   4528 O  O    . THR B  1 79  ? -51.15100 -18.15200 4.75500   1.000 19.74029  ? 79  THR B O    1 
ATOM   4529 C  CB   . THR B  1 79  ? -52.57700 -20.61600 3.88600   1.000 20.97602  ? 79  THR B CB   1 
ATOM   4530 O  OG1  . THR B  1 79  ? -52.52000 -22.03000 3.63100   1.000 25.24368  ? 79  THR B OG1  1 
ATOM   4531 C  CG2  . THR B  1 79  ? -53.90800 -20.08400 3.37400   1.000 22.75106  ? 79  THR B CG2  1 
ATOM   4532 H  H    . THR B  1 79  ? -49.94600 -20.40400 4.40200   1.000 25.83224  ? 79  THR B H    1 
ATOM   4533 H  HA   . THR B  1 79  ? -51.52300 -19.99900 2.21900   1.000 24.21657  ? 79  THR B HA   1 
ATOM   4534 H  HB   . THR B  1 79  ? -52.52000 -20.44500 4.83900   1.000 25.17378  ? 79  THR B HB   1 
ATOM   4535 H  HG1  . THR B  1 79  ? -51.77700 -22.33700 3.87700   1.000 30.29497  ? 79  THR B HG1  1 
ATOM   4536 H  HG21 . THR B  1 79  ? -54.63800 -20.60100 3.74800   1.000 27.30383  ? 79  THR B HG21 1 
ATOM   4537 H  HG22 . THR B  1 79  ? -54.01600 -19.15500 3.63200   1.000 27.30383  ? 79  THR B HG22 1 
ATOM   4538 H  HG23 . THR B  1 79  ? -53.94100 -20.14800 2.40700   1.000 27.30383  ? 79  THR B HG23 1 
ATOM   4539 N  N    . ILE B  1 80  ? -51.57000 -17.56400 2.59900   1.000 19.96856  ? 80  ILE B N    1 
ATOM   4540 C  CA   . ILE B  1 80  ? -51.64600 -16.14200 2.88900   1.000 18.67567  ? 80  ILE B CA   1 
ATOM   4541 C  C    . ILE B  1 80  ? -53.10800 -15.78900 3.11800   1.000 18.81717  ? 80  ILE B C    1 
ATOM   4542 O  O    . ILE B  1 80  ? -53.97100 -16.13800 2.30000   1.000 20.10248  ? 80  ILE B O    1 
ATOM   4543 C  CB   . ILE B  1 80  ? -51.08500 -15.30100 1.74400   1.000 19.59543  ? 80  ILE B CB   1 
ATOM   4544 C  CG1  . ILE B  1 80  ? -49.68000 -15.74300 1.34600   1.000 20.01028  ? 80  ILE B CG1  1 
ATOM   4545 C  CG2  . ILE B  1 80  ? -51.05500 -13.83000 2.12600   1.000 22.07187  ? 80  ILE B CG2  1 
ATOM   4546 C  CD1  . ILE B  1 80  ? -49.18000 -15.03200 0.09100   1.000 22.02048  ? 80  ILE B CD1  1 
ATOM   4547 H  H    . ILE B  1 80  ? -51.66500 -17.76400 1.76800   1.000 23.96483  ? 80  ILE B H    1 
ATOM   4548 H  HA   . ILE B  1 80  ? -51.12900 -15.95600 3.68800   1.000 22.41337  ? 80  ILE B HA   1 
ATOM   4549 H  HB   . ILE B  1 80  ? -51.67500 -15.43400 0.98500   1.000 23.51707  ? 80  ILE B HB   1 
ATOM   4550 H  HG12 . ILE B  1 80  ? -49.06800 -15.54300 2.07100   1.000 24.01489  ? 80  ILE B HG12 1 
ATOM   4551 H  HG13 . ILE B  1 80  ? -49.68600 -16.69700 1.17000   1.000 24.01489  ? 80  ILE B HG13 1 
ATOM   4552 H  HG21 . ILE B  1 80  ? -50.74500 -13.31300 1.36600   1.000 26.48880  ? 80  ILE B HG21 1 
ATOM   4553 H  HG22 . ILE B  1 80  ? -51.95000 -13.55000 2.37300   1.000 26.48880  ? 80  ILE B HG22 1 
ATOM   4554 H  HG23 . ILE B  1 80  ? -50.45200 -13.71100 2.87600   1.000 26.48880  ? 80  ILE B HG23 1 
ATOM   4555 H  HD11 . ILE B  1 80  ? -48.36800 -15.46500 -0.21500  1.000 26.42713  ? 80  ILE B HD11 1 
ATOM   4556 H  HD12 . ILE B  1 80  ? -49.86200 -15.08600 -0.59600  1.000 26.42713  ? 80  ILE B HD12 1 
ATOM   4557 H  HD13 . ILE B  1 80  ? -48.99900 -14.10300 0.30500   1.000 26.42713  ? 80  ILE B HD13 1 
ATOM   4558 N  N    . TYR B  1 81  ? -53.38100 -15.10400 4.21900   1.000 18.24217  ? 81  TYR B N    1 
ATOM   4559 C  CA   . TYR B  1 81  ? -54.68400 -14.53100 4.54300   1.000 16.96023  ? 81  TYR B CA   1 
ATOM   4560 C  C    . TYR B  1 81  ? -54.52800 -13.02500 4.47400   1.000 17.26831  ? 81  TYR B C    1 
ATOM   4561 O  O    . TYR B  1 81  ? -53.58200 -12.48100 5.05500   1.000 17.10930  ? 81  TYR B O    1 
ATOM   4562 C  CB   . TYR B  1 81  ? -55.07800 -14.91800 5.97900   1.000 17.47673  ? 81  TYR B CB   1 
ATOM   4563 C  CG   . TYR B  1 81  ? -55.26100 -16.39700 6.22300   1.000 17.22774  ? 81  TYR B CG   1 
ATOM   4564 C  CD1  . TYR B  1 81  ? -54.16500 -17.18100 6.49900   1.000 18.97815  ? 81  TYR B CD1  1 
ATOM   4565 C  CD2  . TYR B  1 81  ? -56.49300 -17.00000 6.16900   1.000 20.18103  ? 81  TYR B CD2  1 
ATOM   4566 C  CE1  . TYR B  1 81  ? -54.29500 -18.53700 6.72700   1.000 19.62987  ? 81  TYR B CE1  1 
ATOM   4567 C  CE2  . TYR B  1 81  ? -56.64000 -18.34400 6.37200   1.000 20.71174  ? 81  TYR B CE2  1 
ATOM   4568 C  CZ   . TYR B  1 81  ? -55.52800 -19.11400 6.66100   1.000 23.82978  ? 81  TYR B CZ   1 
ATOM   4569 O  OH   . TYR B  1 81  ? -55.67200 -20.45900 6.87300   1.000 23.59493  ? 81  TYR B OH   1 
ATOM   4570 H  H    . TYR B  1 81  ? -52.79600 -14.94900 4.83000   1.000 21.89317  ? 81  TYR B H    1 
ATOM   4571 H  HA   . TYR B  1 81  ? -55.36900 -14.83500 3.92800   1.000 20.35484  ? 81  TYR B HA   1 
ATOM   4572 H  HB2  . TYR B  1 81  ? -54.38300 -14.60900 6.58100   1.000 20.97464  ? 81  TYR B HB2  1 
ATOM   4573 H  HB3  . TYR B  1 81  ? -55.91900 -14.48300 6.19300   1.000 20.97464  ? 81  TYR B HB3  1 
ATOM   4574 H  HD1  . TYR B  1 81  ? -53.32100 -16.79100 6.53200   1.000 22.77634  ? 81  TYR B HD1  1 
ATOM   4575 H  HD2  . TYR B  1 81  ? -57.24500 -16.48300 5.99000   1.000 24.21980  ? 81  TYR B HD2  1 
ATOM   4576 H  HE1  . TYR B  1 81  ? -53.54600 -19.05300 6.92300   1.000 23.55840  ? 81  TYR B HE1  1 
ATOM   4577 H  HE2  . TYR B  1 81  ? -57.48100 -18.73800 6.31600   1.000 24.85665  ? 81  TYR B HE2  1 
ATOM   4578 H  HH   . TYR B  1 81  ? -56.46400 -20.69100 6.71600   1.000 28.31647  ? 81  TYR B HH   1 
ATOM   4579 N  N    . TYR B  1 82  ? -55.42000 -12.33800 3.75700   1.000 17.41028  ? 82  TYR B N    1 
ATOM   4580 C  CA   . TYR B  1 82  ? -55.27000 -10.89400 3.60100   1.000 17.88065  ? 82  TYR B CA   1 
ATOM   4581 C  C    . TYR B  1 82  ? -56.62200 -10.22100 3.43900   1.000 17.72436  ? 82  TYR B C    1 
ATOM   4582 O  O    . TYR B  1 82  ? -57.55700 -10.80300 2.86500   1.000 18.47808  ? 82  TYR B O    1 
ATOM   4583 C  CB   . TYR B  1 82  ? -54.34800 -10.55000 2.39300   1.000 19.30742  ? 82  TYR B CB   1 
ATOM   4584 C  CG   . TYR B  1 82  ? -54.81700 -11.09400 1.08300   1.000 18.37627  ? 82  TYR B CG   1 
ATOM   4585 C  CD1  . TYR B  1 82  ? -54.52500 -12.39700 0.68400   1.000 20.27589  ? 82  TYR B CD1  1 
ATOM   4586 C  CD2  . TYR B  1 82  ? -55.57800 -10.32300 0.20900   1.000 19.44360  ? 82  TYR B CD2  1 
ATOM   4587 C  CE1  . TYR B  1 82  ? -54.99900 -12.89700 -0.49600  1.000 22.82766  ? 82  TYR B CE1  1 
ATOM   4588 C  CE2  . TYR B  1 82  ? -56.06200 -10.82700 -0.97000  1.000 22.12956  ? 82  TYR B CE2  1 
ATOM   4589 C  CZ   . TYR B  1 82  ? -55.74600 -12.11400 -1.34200  1.000 22.18739  ? 82  TYR B CZ   1 
ATOM   4590 O  OH   . TYR B  1 82  ? -56.25100 -12.56300 -2.55900  1.000 27.03152  ? 82  TYR B OH   1 
ATOM   4591 H  H    . TYR B  1 82  ? -56.10300 -12.67900 3.36200   1.000 20.89490  ? 82  TYR B H    1 
ATOM   4592 H  HA   . TYR B  1 82  ? -54.88200 -10.53800 4.41600   1.000 21.45934  ? 82  TYR B HA   1 
ATOM   4593 H  HB2  . TYR B  1 82  ? -54.29600 -9.58500  2.30900   1.000 23.17147  ? 82  TYR B HB2  1 
ATOM   4594 H  HB3  . TYR B  1 82  ? -53.46600 -10.91600 2.56400   1.000 23.17147  ? 82  TYR B HB3  1 
ATOM   4595 H  HD1  . TYR B  1 82  ? -53.99900 -12.93500 1.23000   1.000 24.33363  ? 82  TYR B HD1  1 
ATOM   4596 H  HD2  . TYR B  1 82  ? -55.76300 -9.43900  0.43200   1.000 23.33488  ? 82  TYR B HD2  1 
ATOM   4597 H  HE1  . TYR B  1 82  ? -54.81300 -13.77800 -0.72900  1.000 27.39575  ? 82  TYR B HE1  1 
ATOM   4598 H  HE2  . TYR B  1 82  ? -56.60200 -10.30200 -1.51600  1.000 26.55804  ? 82  TYR B HE2  1 
ATOM   4599 H  HH   . TYR B  1 82  ? -56.81300 -12.01500 -2.85700  1.000 32.44039  ? 82  TYR B HH   1 
ATOM   4600 N  N    . PRO B  1 83  ? -56.75600 -8.99200  3.91100   1.000 17.28607  ? 83  PRO B N    1 
ATOM   4601 C  CA   . PRO B  1 83  ? -57.99500 -8.24900  3.65300   1.000 18.49565  ? 83  PRO B CA   1 
ATOM   4602 C  C    . PRO B  1 83  ? -58.17100 -7.88000  2.19300   1.000 20.23169  ? 83  PRO B C    1 
ATOM   4603 O  O    . PRO B  1 83  ? -57.20100 -7.54700  1.50300   1.000 22.22452  ? 83  PRO B O    1 
ATOM   4604 C  CB   . PRO B  1 83  ? -57.84500 -6.97400  4.49600   1.000 22.54690  ? 83  PRO B CB   1 
ATOM   4605 C  CG   . PRO B  1 83  ? -56.68500 -7.19800  5.37300   1.000 21.60735  ? 83  PRO B CG   1 
ATOM   4606 C  CD   . PRO B  1 83  ? -55.82700 -8.24000  4.77000   1.000 19.28354  ? 83  PRO B CD   1 
ATOM   4607 H  HA   . PRO B  1 83  ? -58.74900 -8.78000  3.95300   1.000 22.19735  ? 83  PRO B HA   1 
ATOM   4608 H  HB2  . PRO B  1 83  ? -57.69200 -6.21400  3.91200   1.000 27.05884  ? 83  PRO B HB2  1 
ATOM   4609 H  HB3  . PRO B  1 83  ? -58.64900 -6.83300  5.01900   1.000 27.05884  ? 83  PRO B HB3  1 
ATOM   4610 H  HG2  . PRO B  1 83  ? -56.19000 -6.36900  5.46000   1.000 25.93138  ? 83  PRO B HG2  1 
ATOM   4611 H  HG3  . PRO B  1 83  ? -57.00000 -7.49000  6.24400   1.000 25.93138  ? 83  PRO B HG3  1 
ATOM   4612 H  HD2  . PRO B  1 83  ? -55.11800 -7.84000  4.24300   1.000 23.14281  ? 83  PRO B HD2  1 
ATOM   4613 H  HD3  . PRO B  1 83  ? -55.44800 -8.81400  5.45400   1.000 23.14281  ? 83  PRO B HD3  1 
ATOM   4614 N  N    . VAL B  1 84  ? -59.42100 -7.90300  1.74200   1.000 20.14689  ? 84  VAL B N    1 
ATOM   4615 C  CA   . VAL B  1 84  ? -59.73000 -7.42500  0.39700   1.000 20.62120  ? 84  VAL B CA   1 
ATOM   4616 C  C    . VAL B  1 84  ? -60.16100 -5.97400  0.39100   1.000 27.64945  ? 84  VAL B C    1 
ATOM   4617 O  O    . VAL B  1 84  ? -60.24200 -5.37500  -0.70600  1.000 27.14755  ? 84  VAL B O    1 
ATOM   4618 C  CB   . VAL B  1 84  ? -60.77800 -8.30700  -0.29600  1.000 23.59988  ? 84  VAL B CB   1 
ATOM   4619 C  CG1  . VAL B  1 84  ? -60.26700 -9.75200  -0.34900  1.000 28.04423  ? 84  VAL B CG1  1 
ATOM   4620 C  CG2  . VAL B  1 84  ? -62.11900 -8.20200  0.36700   1.000 24.85385  ? 84  VAL B CG2  1 
ATOM   4621 H  H    . VAL B  1 84  ? -60.09900 -8.18600  2.18900   1.000 24.17884  ? 84  VAL B H    1 
ATOM   4622 H  HA   . VAL B  1 84  ? -58.92200 -7.48900  -0.13600  1.000 24.74800  ? 84  VAL B HA   1 
ATOM   4623 H  HB   . VAL B  1 84  ? -60.91200 -7.99600  -1.20500  1.000 28.32242  ? 84  VAL B HB   1 
ATOM   4624 H  HG11 . VAL B  1 84  ? -60.92100 -10.30100 -0.81000  1.000 33.65564  ? 84  VAL B HG11 1 
ATOM   4625 H  HG12 . VAL B  1 84  ? -59.42300 -9.77100  -0.82800  1.000 33.65564  ? 84  VAL B HG12 1 
ATOM   4626 H  HG13 . VAL B  1 84  ? -60.14100 -10.07600 0.55600   1.000 33.65564  ? 84  VAL B HG13 1 
ATOM   4627 H  HG21 . VAL B  1 84  ? -62.72400 -8.84100  -0.04200  1.000 29.82718  ? 84  VAL B HG21 1 
ATOM   4628 H  HG22 . VAL B  1 84  ? -62.02100 -8.39800  1.31200   1.000 29.82718  ? 84  VAL B HG22 1 
ATOM   4629 H  HG23 . VAL B  1 84  ? -62.46100 -7.30200  0.24900   1.000 29.82718  ? 84  VAL B HG23 1 
ATOM   4630 N  N    . ASN B  1 85  ? -60.41000 -5.38700  1.55900   1.000 21.38243  ? 85  ASN B N    1 
ATOM   4631 C  CA   . ASN B  1 85  ? -61.01000 -4.07300  1.73700   1.000 27.15366  ? 85  ASN B CA   1 
ATOM   4632 C  C    . ASN B  1 85  ? -60.31000 -3.25300  2.83400   1.000 27.50806  ? 85  ASN B C    1 
ATOM   4633 O  O    . ASN B  1 85  ? -60.94600 -2.45600  3.52800   1.000 28.82286  ? 85  ASN B O    1 
ATOM   4634 C  CB   . ASN B  1 85  ? -62.52100 -4.16500  2.00700   1.000 26.45699  ? 85  ASN B CB   1 
ATOM   4635 C  CG   . ASN B  1 85  ? -62.89700 -4.94600  3.31300   1.000 24.96265  ? 85  ASN B CG   1 
ATOM   4636 O  OD1  . ASN B  1 85  ? -62.09100 -5.68900  3.87700   1.000 24.27054  ? 85  ASN B OD1  1 
ATOM   4637 N  ND2  . ASN B  1 85  ? -64.14400 -4.78100  3.75600   1.000 32.02951  ? 85  ASN B ND2  1 
ATOM   4638 H  H    . ASN B  1 85  ? -60.22700 -5.75800  2.31300   1.000 25.66148  ? 85  ASN B H    1 
ATOM   4639 H  HA   . ASN B  1 85  ? -60.87700 -3.59300  0.90500   1.000 32.58695  ? 85  ASN B HA   1 
ATOM   4640 H  HB2  . ASN B  1 85  ? -62.87600 -3.26600  2.09000   1.000 31.75095  ? 85  ASN B HB2  1 
ATOM   4641 H  HB3  . ASN B  1 85  ? -62.94200 -4.62000  1.26100   1.000 31.75095  ? 85  ASN B HB3  1 
ATOM   4642 H  HD21 . ASN B  1 85  ? -64.40400 -5.18600  4.46900   1.000 38.43797  ? 85  ASN B HD21 1 
ATOM   4643 H  HD22 . ASN B  1 85  ? -64.68800 -4.27000  3.32900   1.000 38.43797  ? 85  ASN B HD22 1 
ATOM   4644 N  N    . ALA B  1 86  ? -58.99200 -3.36300  2.96100   1.000 32.38713  ? 86  ALA B N    1 
ATOM   4645 C  CA   . ALA B  1 86  ? -58.26600 -2.48700  3.87400   1.000 24.86094  ? 86  ALA B CA   1 
ATOM   4646 C  C    . ALA B  1 86  ? -57.91200 -1.16600  3.19600   1.000 29.85585  ? 86  ALA B C    1 
ATOM   4647 O  O    . ALA B  1 86  ? -57.73400 -1.08300  1.98000   1.000 31.04616  ? 86  ALA B O    1 
ATOM   4648 C  CB   . ALA B  1 86  ? -57.00000 -3.17700  4.39600   1.000 41.85067  ? 86  ALA B CB   1 
ATOM   4649 H  H    . ALA B  1 86  ? -58.50300 -3.92800  2.53500   1.000 38.86712  ? 86  ALA B H    1 
ATOM   4650 H  HA   . ALA B  1 86  ? -58.82900 -2.28200  4.63700   1.000 29.83569  ? 86  ALA B HA   1 
ATOM   4651 H  HB1  . ALA B  1 86  ? -56.53000 -2.57000  4.98900   1.000 50.22337  ? 86  ALA B HB1  1 
ATOM   4652 H  HB2  . ALA B  1 86  ? -57.25400 -3.98000  4.87800   1.000 50.22337  ? 86  ALA B HB2  1 
ATOM   4653 H  HB3  . ALA B  1 86  ? -56.43400 -3.40900  3.64300   1.000 50.22337  ? 86  ALA B HB3  1 
ATOM   4654 N  N    . GLU B  1 87  ? -57.79700 -0.11900  4.00100   1.000 27.26994  ? 87  GLU B N    1 
ATOM   4655 C  CA   . GLU B  1 87  ? -57.70000 1.22500   3.45700   1.000 26.21126  ? 87  GLU B CA   1 
ATOM   4656 C  C    . GLU B  1 87  ? -56.26700 1.68600   3.18000   1.000 30.78574  ? 87  GLU B C    1 
ATOM   4657 O  O    . GLU B  1 87  ? -56.09100 2.82500   2.73000   1.000 34.32938  ? 87  GLU B O    1 
ATOM   4658 C  CB   . GLU B  1 87  ? -58.41900 2.22000   4.37900   1.000 29.82007  ? 87  GLU B CB   1 
ATOM   4659 C  CG   . GLU B  1 87  ? -57.81200 2.42800   5.77900   1.000 28.90974  ? 87  GLU B CG   1 
ATOM   4660 C  CD   . GLU B  1 87  ? -58.30300 1.46000   6.84800   1.000 38.41867  ? 87  GLU B CD   1 
ATOM   4661 O  OE1  . GLU B  1 87  ? -58.59100 0.28900   6.54100   1.000 29.75819  ? 87  GLU B OE1  1 
ATOM   4662 O  OE2  . GLU B  1 87  ? -58.37600 1.88800   8.02000   1.000 25.50275  ? 87  GLU B OE2  1 
ATOM   4663 H  H    . GLU B  1 87  ? -57.77300 -0.16200  4.86000   1.000 32.72649  ? 87  GLU B H    1 
ATOM   4664 H  HA   . GLU B  1 87  ? -58.15600 1.23700   2.60100   1.000 31.45608  ? 87  GLU B HA   1 
ATOM   4665 H  HB2  . GLU B  1 87  ? -58.42500 3.08500   3.94100   1.000 35.78665  ? 87  GLU B HB2  1 
ATOM   4666 H  HB3  . GLU B  1 87  ? -59.32800 1.90700   4.50700   1.000 35.78665  ? 87  GLU B HB3  1 
ATOM   4667 H  HG2  . GLU B  1 87  ? -56.84900 2.32400   5.71500   1.000 34.69425  ? 87  GLU B HG2  1 
ATOM   4668 H  HG3  . GLU B  1 87  ? -58.03000 3.32500   6.07800   1.000 34.69425  ? 87  GLU B HG3  1 
ATOM   4669 N  N    . GLY B  1 88  ? -55.25500 0.84700   3.39200   1.000 24.66244  ? 88  GLY B N    1 
ATOM   4670 C  CA   . GLY B  1 88  ? -53.86900 1.23600   3.13000   1.000 23.12284  ? 88  GLY B CA   1 
ATOM   4671 C  C    . GLY B  1 88  ? -52.90700 0.07500   3.31500   1.000 21.33383  ? 88  GLY B C    1 
ATOM   4672 O  O    . GLY B  1 88  ? -53.31600 -1.03900  3.62900   1.000 22.40470  ? 88  GLY B O    1 
ATOM   4673 H  H    . GLY B  1 88  ? -55.34300 0.04500   3.68800   1.000 29.59749  ? 88  GLY B H    1 
ATOM   4674 H  HA2  . GLY B  1 88  ? -53.79000 1.55700   2.21900   1.000 27.74997  ? 88  GLY B HA2  1 
ATOM   4675 H  HA3  . GLY B  1 88  ? -53.61200 1.94600   3.73900   1.000 27.74997  ? 88  GLY B HA3  1 
ATOM   4676 N  N    A THR B  1 89  ? -51.61200 0.35200   3.11900   0.561 20.49554  ? 89  THR B N    1 
ATOM   4677 N  N    B THR B  1 89  ? -51.60900 0.37200   3.13400   0.439 20.68008  ? 89  THR B N    1 
ATOM   4678 C  CA   A THR B  1 89  ? -50.59000 -0.68000  3.27600   0.561 21.09492  ? 89  THR B CA   1 
ATOM   4679 C  CA   B THR B  1 89  ? -50.56600 -0.63400  3.29900   0.439 20.73601  ? 89  THR B CA   1 
ATOM   4680 C  C    A THR B  1 89  ? -50.54100 -1.14800  4.72700   0.561 20.67614  ? 89  THR B C    1 
ATOM   4681 C  C    B THR B  1 89  ? -50.53300 -1.13800  4.74000   0.439 20.81046  ? 89  THR B C    1 
ATOM   4682 O  O    A THR B  1 89  ? -50.86500 -0.39900  5.65500   0.561 20.17949  ? 89  THR B O    1 
ATOM   4683 O  O    B THR B  1 89  ? -50.84000 -0.40000  5.67900   0.439 20.39927  ? 89  THR B O    1 
ATOM   4684 C  CB   A THR B  1 89  ? -49.25500 -0.12400  2.81500   0.561 22.16369  ? 89  THR B CB   1 
ATOM   4685 C  CB   B THR B  1 89  ? -49.20000 -0.08200  2.89100   0.439 21.63425  ? 89  THR B CB   1 
ATOM   4686 O  OG1  A THR B  1 89  ? -49.36500 0.27700   1.43700   0.561 25.99827  ? 89  THR B OG1  1 
ATOM   4687 O  OG1  B THR B  1 89  ? -48.80600 1.03600   3.69500   0.439 20.02039  ? 89  THR B OG1  1 
ATOM   4688 C  CG2  A THR B  1 89  ? -48.14700 -1.14000  2.85800   0.561 26.60863  ? 89  THR B CG2  1 
ATOM   4689 C  CG2  B THR B  1 89  ? -49.21900 0.39600   1.45400   0.439 28.54675  ? 89  THR B CG2  1 
ATOM   4690 H  H    A THR B  1 89  ? -51.30400 1.12400   2.89600   0.561 24.59721  ? 89  THR B H    1 
ATOM   4691 H  H    B THR B  1 89  ? -51.31300 1.15000   2.91500   0.439 24.81866  ? 89  THR B H    1 
ATOM   4692 H  HA   A THR B  1 89  ? -50.78800 -1.46100  2.73500   0.561 25.31646  ? 89  THR B HA   1 
ATOM   4693 H  HA   B THR B  1 89  ? -50.75600 -1.38700  2.71900   0.439 24.88577  ? 89  THR B HA   1 
ATOM   4694 H  HB   A THR B  1 89  ? -49.03300 0.61100   3.40800   0.561 26.59899  ? 89  THR B HB   1 
ATOM   4695 H  HB   B THR B  1 89  ? -48.56200 -0.80400  3.00600   0.439 25.96366  ? 89  THR B HB   1 
ATOM   4696 H  HG1  A THR B  1 89  ? -49.91200 0.91000   1.36400   0.561 31.20049  ? 89  THR B HG1  1 
ATOM   4697 H  HG1  B THR B  1 89  ? -48.62500 0.78000   4.47400   0.439 24.02703  ? 89  THR B HG1  1 
ATOM   4698 H  HG21 A THR B  1 89  ? -47.28700 -0.69500  2.80300   0.561 31.93292  ? 89  THR B HG21 1 
ATOM   4699 H  HG21 B THR B  1 89  ? -48.31200 0.53000   1.13700   0.439 34.25866  ? 89  THR B HG21 1 
ATOM   4700 H  HG22 A THR B  1 89  ? -48.18900 -1.64100  3.68800   0.561 31.93292  ? 89  THR B HG22 1 
ATOM   4701 H  HG22 B THR B  1 89  ? -49.65500 -0.26300  0.89100   0.439 34.25866  ? 89  THR B HG22 1 
ATOM   4702 H  HG23 A THR B  1 89  ? -48.23200 -1.75600  2.11400   0.561 31.93292  ? 89  THR B HG23 1 
ATOM   4703 H  HG23 B THR B  1 89  ? -49.70200 1.23400   1.38900   0.439 34.25866  ? 89  THR B HG23 1 
ATOM   4704 N  N    . MET B  1 90  ? -50.17700 -2.41300  4.90900   1.000 18.39460  ? 90  MET B N    1 
ATOM   4705 C  CA   . MET B  1 90  ? -50.25600 -3.08100  6.20200   1.000 18.66172  ? 90  MET B CA   1 
ATOM   4706 C  C    . MET B  1 90  ? -48.94400 -3.75700  6.57500   1.000 17.14469  ? 90  MET B C    1 
ATOM   4707 O  O    . MET B  1 90  ? -48.08800 -4.02300  5.72300   1.000 17.34755  ? 90  MET B O    1 
ATOM   4708 C  CB   . MET B  1 90  ? -51.30700 -4.16500  6.17400   1.000 19.14728  ? 90  MET B CB   1 
ATOM   4709 C  CG   . MET B  1 90  ? -52.70200 -3.61000  6.09100   1.000 18.80427  ? 90  MET B CG   1 
ATOM   4710 S  SD   . MET B  1 90  ? -53.92900 -4.84200  5.52100   1.000 20.60528  ? 90  MET B SD   1 
ATOM   4711 C  CE   . MET B  1 90  ? -53.56400 -4.94800  3.77600   1.000 21.77469  ? 90  MET B CE   1 
ATOM   4712 H  H    . MET B  1 90  ? -49.87300 -2.91900  4.28300   1.000 22.07608  ? 90  MET B H    1 
ATOM   4713 H  HA   . MET B  1 90  ? -50.46100 -2.39900  6.86100   1.000 22.39663  ? 90  MET B HA   1 
ATOM   4714 H  HB2  . MET B  1 90  ? -51.16000 -4.72800  5.39800   1.000 22.97929  ? 90  MET B HB2  1 
ATOM   4715 H  HB3  . MET B  1 90  ? -51.23900 -4.69200  6.98500   1.000 22.97929  ? 90  MET B HB3  1 
ATOM   4716 H  HG2  . MET B  1 90  ? -52.97200 -3.30500  6.97100   1.000 22.56768  ? 90  MET B HG2  1 
ATOM   4717 H  HG3  . MET B  1 90  ? -52.71000 -2.86900  5.46600   1.000 22.56768  ? 90  MET B HG3  1 
ATOM   4718 H  HE1  . MET B  1 90  ? -54.16400 -5.59000  3.36600   1.000 26.13219  ? 90  MET B HE1  1 
ATOM   4719 H  HE2  . MET B  1 90  ? -53.68900 -4.07400  3.37400   1.000 26.13219  ? 90  MET B HE2  1 
ATOM   4720 H  HE3  . MET B  1 90  ? -52.64400 -5.23500  3.66300   1.000 26.13219  ? 90  MET B HE3  1 
ATOM   4721 N  N    . ALA B  1 91  ? -48.80100 -4.04100  7.85800   1.000 16.81681  ? 91  ALA B N    1 
ATOM   4722 C  CA   . ALA B  1 91  ? -47.74300 -4.91600  8.31400   1.000 15.70095  ? 91  ALA B CA   1 
ATOM   4723 C  C    . ALA B  1 91  ? -48.00800 -6.35800  7.88900   1.000 16.89140  ? 91  ALA B C    1 
ATOM   4724 O  O    . ALA B  1 91  ? -49.16100 -6.77700  7.68700   1.000 16.98418  ? 91  ALA B O    1 
ATOM   4725 C  CB   . ALA B  1 91  ? -47.63400 -4.81700  9.81500   1.000 16.26423  ? 91  ALA B CB   1 
ATOM   4726 H  H    . ALA B  1 91  ? -49.30600 -3.73900  8.48500   1.000 20.18273  ? 91  ALA B H    1 
ATOM   4727 H  HA   . ALA B  1 91  ? -46.89500 -4.65300  7.92300   1.000 18.84371  ? 91  ALA B HA   1 
ATOM   4728 H  HB1  . ALA B  1 91  ? -46.94600 -5.42800  10.12300  1.000 19.51964  ? 91  ALA B HB1  1 
ATOM   4729 H  HB2  . ALA B  1 91  ? -47.39900 -3.90700  10.05500  1.000 19.51964  ? 91  ALA B HB2  1 
ATOM   4730 H  HB3  . ALA B  1 91  ? -48.48700 -5.05400  10.21000  1.000 19.51964  ? 91  ALA B HB3  1 
ATOM   4731 N  N    . ALA B  1 92  ? -46.92000 -7.11400  7.73300   1.000 17.22476  ? 92  ALA B N    1 
ATOM   4732 C  CA   . ALA B  1 92  ? -46.97700 -8.52500  7.38900   1.000 16.08411  ? 92  ALA B CA   1 
ATOM   4733 C  C    . ALA B  1 92  ? -46.52200 -9.35700  8.56900   1.000 17.04656  ? 92  ALA B C    1 
ATOM   4734 O  O    . ALA B  1 92  ? -45.63000 -8.93800  9.31600   1.000 17.26475  ? 92  ALA B O    1 
ATOM   4735 C  CB   . ALA B  1 92  ? -46.12600 -8.83700  6.18700   1.000 19.03686  ? 92  ALA B CB   1 
ATOM   4736 H  H    . ALA B  1 92  ? -46.11700 -6.81900  7.82600   1.000 20.67228  ? 92  ALA B H    1 
ATOM   4737 H  HA   . ALA B  1 92  ? -47.89300 -8.76300  7.17600   1.000 19.30350  ? 92  ALA B HA   1 
ATOM   4738 H  HB1  . ALA B  1 92  ? -46.18100 -9.78800  5.99900   1.000 22.84679  ? 92  ALA B HB1  1 
ATOM   4739 H  HB2  . ALA B  1 92  ? -46.45500 -8.33100  5.42700   1.000 22.84679  ? 92  ALA B HB2  1 
ATOM   4740 H  HB3  . ALA B  1 92  ? -45.20800 -8.59000  6.37700   1.000 22.84679  ? 92  ALA B HB3  1 
ATOM   4741 N  N    . ILE B  1 93  ? -47.16000 -10.51500 8.74800   1.000 16.68398  ? 93  ILE B N    1 
ATOM   4742 C  CA   . ILE B  1 93  ? -46.89900 -11.41700 9.86400   1.000 16.73075  ? 93  ILE B CA   1 
ATOM   4743 C  C    . ILE B  1 93  ? -46.81300 -12.84500 9.35000   1.000 15.72826  ? 93  ILE B C    1 
ATOM   4744 O  O    . ILE B  1 93  ? -47.64400 -13.26800 8.53400   1.000 17.25795  ? 93  ILE B O    1 
ATOM   4745 C  CB   . ILE B  1 93  ? -48.04700 -11.35200 10.88900  1.000 14.95204  ? 93  ILE B CB   1 
ATOM   4746 C  CG1  . ILE B  1 93  ? -48.21900 -9.93200  11.40400  1.000 15.91556  ? 93  ILE B CG1  1 
ATOM   4747 C  CG2  . ILE B  1 93  ? -47.78300 -12.34700 11.99400  1.000 16.60339  ? 93  ILE B CG2  1 
ATOM   4748 C  CD1  . ILE B  1 93  ? -49.46200 -9.73300  12.30400  1.000 16.63516  ? 93  ILE B CD1  1 
ATOM   4749 H  H    . ILE B  1 93  ? -47.76900 -10.80800 8.21600   1.000 20.02334  ? 93  ILE B H    1 
ATOM   4750 H  HA   . ILE B  1 93  ? -46.05200 -11.16900 10.26800  1.000 20.07946  ? 93  ILE B HA   1 
ATOM   4751 H  HB   . ILE B  1 93  ? -48.88500 -11.59300 10.46500  1.000 17.94501  ? 93  ILE B HB   1 
ATOM   4752 H  HG12 . ILE B  1 93  ? -47.43700 -9.69300  11.92500  1.000 19.10124  ? 93  ILE B HG12 1 
ATOM   4753 H  HG13 . ILE B  1 93  ? -48.30700 -9.33400  10.64500  1.000 19.10124  ? 93  ILE B HG13 1 
ATOM   4754 H  HG21 . ILE B  1 93  ? -48.46300 -12.24700 12.67800  1.000 19.92662  ? 93  ILE B HG21 1 
ATOM   4755 H  HG22 . ILE B  1 93  ? -47.81300 -13.24400 11.62500  1.000 19.92662  ? 93  ILE B HG22 1 
ATOM   4756 H  HG23 . ILE B  1 93  ? -46.90600 -12.17500 12.37100  1.000 19.92662  ? 93  ILE B HG23 1 
ATOM   4757 H  HD11 . ILE B  1 93  ? -49.58000 -8.78600  12.47600  1.000 19.96476  ? 93  ILE B HD11 1 
ATOM   4758 H  HD12 . ILE B  1 93  ? -50.24200 -10.08700 11.84900  1.000 19.96476  ? 93  ILE B HD12 1 
ATOM   4759 H  HD13 . ILE B  1 93  ? -49.32500 -10.20600 13.14000  1.000 19.96476  ? 93  ILE B HD13 1 
ATOM   4760 N  N    . VAL B  1 94  ? -45.79400 -13.59200 9.81900   1.000 15.55377  ? 94  VAL B N    1 
ATOM   4761 C  CA   . VAL B  1 94  ? -45.66300 -15.02600 9.55700   1.000 16.13297  ? 94  VAL B CA   1 
ATOM   4762 C  C    . VAL B  1 94  ? -45.98900 -15.78400 10.83700  1.000 16.41892  ? 94  VAL B C    1 
ATOM   4763 O  O    . VAL B  1 94  ? -45.50700 -15.41600 11.92500  1.000 17.66419  ? 94  VAL B O    1 
ATOM   4764 C  CB   . VAL B  1 94  ? -44.25700 -15.35800 9.02700   1.000 17.44368  ? 94  VAL B CB   1 
ATOM   4765 C  CG1  . VAL B  1 94  ? -43.96100 -16.84500 9.09300   1.000 18.36038  ? 94  VAL B CG1  1 
ATOM   4766 C  CG2  . VAL B  1 94  ? -44.14300 -14.84700 7.59800   1.000 18.53195  ? 94  VAL B CG2  1 
ATOM   4767 H  H    . VAL B  1 94  ? -45.15700 -13.27600 10.30200  1.000 18.66709  ? 94  VAL B H    1 
ATOM   4768 H  HA   . VAL B  1 94  ? -46.30500 -15.30400 8.88600   1.000 19.36213  ? 94  VAL B HA   1 
ATOM   4769 H  HB   . VAL B  1 94  ? -43.59500 -14.92200 9.58600   1.000 20.93497  ? 94  VAL B HB   1 
ATOM   4770 H  HG11 . VAL B  1 94  ? -43.18000 -17.03600 8.55000   1.000 22.03502  ? 94  VAL B HG11 1 
ATOM   4771 H  HG12 . VAL B  1 94  ? -43.79200 -17.09300 10.01500  1.000 22.03502  ? 94  VAL B HG12 1 
ATOM   4772 H  HG13 . VAL B  1 94  ? -44.72700 -17.33400 8.75400   1.000 22.03502  ? 94  VAL B HG13 1 
ATOM   4773 H  HG21 . VAL B  1 94  ? -43.23700 -14.99000 7.28300   1.000 22.24090  ? 94  VAL B HG21 1 
ATOM   4774 H  HG22 . VAL B  1 94  ? -44.76800 -15.33300 7.03800   1.000 22.24090  ? 94  VAL B HG22 1 
ATOM   4775 H  HG23 . VAL B  1 94  ? -44.35200 -13.90000 7.58400   1.000 22.24090  ? 94  VAL B HG23 1 
ATOM   4776 N  N    . VAL B  1 95  ? -46.78500 -16.84000 10.70600  1.000 16.18380  ? 95  VAL B N    1 
ATOM   4777 C  CA   . VAL B  1 95  ? -47.13100 -17.73100 11.81800  1.000 16.31234  ? 95  VAL B CA   1 
ATOM   4778 C  C    . VAL B  1 95  ? -46.56200 -19.10500 11.52700  1.000 17.58211  ? 95  VAL B C    1 
ATOM   4779 O  O    . VAL B  1 95  ? -46.82000 -19.67000 10.45800  1.000 18.37711  ? 95  VAL B O    1 
ATOM   4780 C  CB   . VAL B  1 95  ? -48.65600 -17.80400 12.01000  1.000 16.88177  ? 95  VAL B CB   1 
ATOM   4781 C  CG1  . VAL B  1 95  ? -48.97800 -18.51700 13.32500  1.000 17.87210  ? 95  VAL B CG1  1 
ATOM   4782 C  CG2  . VAL B  1 95  ? -49.29900 -16.41400 11.98500  1.000 17.30420  ? 95  VAL B CG2  1 
ATOM   4783 H  H    . VAL B  1 95  ? -47.14900 -17.07000 9.96200   1.000 19.42313  ? 95  VAL B H    1 
ATOM   4784 H  HA   . VAL B  1 95  ? -46.72500 -17.40300 12.63600  1.000 19.57738  ? 95  VAL B HA   1 
ATOM   4785 H  HB   . VAL B  1 95  ? -49.03300 -18.30800 11.27200  1.000 20.26068  ? 95  VAL B HB   1 
ATOM   4786 H  HG11 . VAL B  1 95  ? -49.94100 -18.56500 13.43000  1.000 21.44909  ? 95  VAL B HG11 1 
ATOM   4787 H  HG12 . VAL B  1 95  ? -48.60300 -19.41100 13.30000  1.000 21.44909  ? 95  VAL B HG12 1 
ATOM   4788 H  HG13 . VAL B  1 95  ? -48.59000 -18.01500 14.05900  1.000 21.44909  ? 95  VAL B HG13 1 
ATOM   4789 H  HG21 . VAL B  1 95  ? -50.23100 -16.49300 12.24200  1.000 20.76760  ? 95  VAL B HG21 1 
ATOM   4790 H  HG22 . VAL B  1 95  ? -48.83100 -15.83800 12.60900  1.000 20.76760  ? 95  VAL B HG22 1 
ATOM   4791 H  HG23 . VAL B  1 95  ? -49.23300 -16.05200 11.08700  1.000 20.76760  ? 95  VAL B HG23 1 
ATOM   4792 N  N    . ILE B  1 96  ? -45.80700 -19.64900 12.47000  1.000 17.47788  ? 96  ILE B N    1 
ATOM   4793 C  CA   . ILE B  1 96  ? -45.05600 -20.89000 12.27500  1.000 19.48483  ? 96  ILE B CA   1 
ATOM   4794 C  C    . ILE B  1 96  ? -45.35600 -21.88900 13.38400  1.000 18.89234  ? 96  ILE B C    1 
ATOM   4795 O  O    . ILE B  1 96  ? -45.42100 -21.50600 14.56600  1.000 18.62346  ? 96  ILE B O    1 
ATOM   4796 C  CB   . ILE B  1 96  ? -43.55000 -20.59500 12.15500  1.000 18.17030  ? 96  ILE B CB   1 
ATOM   4797 C  CG1  . ILE B  1 96  ? -42.75600 -21.86800 11.86200  1.000 19.64809  ? 96  ILE B CG1  1 
ATOM   4798 C  CG2  . ILE B  1 96  ? -43.02400 -19.94700 13.43200  1.000 18.59639  ? 96  ILE B CG2  1 
ATOM   4799 C  CD1  . ILE B  1 96  ? -41.24800 -21.63100 11.64200  1.000 20.87933  ? 96  ILE B CD1  1 
ATOM   4800 H  H    . ILE B  1 96  ? -45.70800 -19.31200 13.25500  1.000 20.97602  ? 96  ILE B H    1 
ATOM   4801 H  HA   . ILE B  1 96  ? -45.36200 -21.30700 11.45400  1.000 23.38436  ? 96  ILE B HA   1 
ATOM   4802 H  HB   . ILE B  1 96  ? -43.43700 -19.98100 11.41300  1.000 21.80692  ? 96  ILE B HB   1 
ATOM   4803 H  HG12 . ILE B  1 96  ? -42.85300 -22.47400 12.61200  1.000 23.58027  ? 96  ILE B HG12 1 
ATOM   4804 H  HG13 . ILE B  1 96  ? -43.11100 -22.27700 11.05700  1.000 23.58027  ? 96  ILE B HG13 1 
ATOM   4805 H  HG21 . ILE B  1 96  ? -42.10400 -19.67300 13.29100  1.000 22.31823  ? 96  ILE B HG21 1 
ATOM   4806 H  HG22 . ILE B  1 96  ? -43.57100 -19.17500 13.64300  1.000 22.31823  ? 96  ILE B HG22 1 
ATOM   4807 H  HG23 . ILE B  1 96  ? -43.06900 -20.59200 14.15500  1.000 22.31823  ? 96  ILE B HG23 1 
ATOM   4808 H  HD11 . ILE B  1 96  ? -40.83900 -22.45700 11.33900  1.000 25.05776  ? 96  ILE B HD11 1 
ATOM   4809 H  HD12 . ILE B  1 96  ? -41.13100 -20.93900 10.97200  1.000 25.05776  ? 96  ILE B HD12 1 
ATOM   4810 H  HD13 . ILE B  1 96  ? -40.84700 -21.35200 12.48000  1.000 25.05776  ? 96  ILE B HD13 1 
ATOM   4811 N  N    . PRO B  1 97  ? -45.56900 -23.17700 13.03100  1.000 18.91075  ? 97  PRO B N    1 
ATOM   4812 C  CA   . PRO B  1 97  ? -45.83000 -24.21100 14.03000  1.000 19.33959  ? 97  PRO B CA   1 
ATOM   4813 C  C    . PRO B  1 97  ? -44.56500 -24.76100 14.67100  1.000 19.88243  ? 97  PRO B C    1 
ATOM   4814 O  O    . PRO B  1 97  ? -43.46600 -24.20800 14.51000  1.000 20.36854  ? 97  PRO B O    1 
ATOM   4815 C  CB   . PRO B  1 97  ? -46.59500 -25.26900 13.22200  1.000 22.39692  ? 97  PRO B CB   1 
ATOM   4816 C  CG   . PRO B  1 97  ? -45.94900 -25.20200 11.86900  1.000 21.93568  ? 97  PRO B CG   1 
ATOM   4817 C  CD   . PRO B  1 97  ? -45.69600 -23.70400 11.65000  1.000 20.87201  ? 97  PRO B CD   1 
ATOM   4818 H  HA   . PRO B  1 97  ? -46.40100 -23.87200 14.73700  1.000 23.21007  ? 97  PRO B HA   1 
ATOM   4819 H  HB2  . PRO B  1 97  ? -46.48400 -26.14600 13.62300  1.000 26.87886  ? 97  PRO B HB2  1 
ATOM   4820 H  HB3  . PRO B  1 97  ? -47.53700 -25.04300 13.17500  1.000 26.87886  ? 97  PRO B HB3  1 
ATOM   4821 H  HG2  . PRO B  1 97  ? -45.11700 -25.70100 11.87000  1.000 26.32538  ? 97  PRO B HG2  1 
ATOM   4822 H  HG3  . PRO B  1 97  ? -46.54800 -25.55800 11.19400  1.000 26.32538  ? 97  PRO B HG3  1 
ATOM   4823 H  HD2  . PRO B  1 97  ? -44.87800 -23.56100 11.14900  1.000 25.04897  ? 97  PRO B HD2  1 
ATOM   4824 H  HD3  . PRO B  1 97  ? -46.44400 -23.29100 11.19000  1.000 25.04897  ? 97  PRO B HD3  1 
ATOM   4825 N  N    . GLY B  1 98  ? -44.70800 -25.86600 15.41000  1.000 22.50221  ? 98  GLY B N    1 
ATOM   4826 C  CA   . GLY B  1 98  ? -43.62900 -26.45800 16.16100  1.000 23.03175  ? 98  GLY B CA   1 
ATOM   4827 C  C    . GLY B  1 98  ? -43.15400 -27.77400 15.57000  1.000 22.85406  ? 98  GLY B C    1 
ATOM   4828 O  O    . GLY B  1 98  ? -43.53500 -28.18400 14.46700  1.000 24.35804  ? 98  GLY B O    1 
ATOM   4829 H  H    . GLY B  1 98  ? -45.45000 -26.29400 15.48600  1.000 27.00521  ? 98  GLY B H    1 
ATOM   4830 H  HA2  . GLY B  1 98  ? -42.87700 -25.84400 16.17900  1.000 27.64066  ? 98  GLY B HA2  1 
ATOM   4831 H  HA3  . GLY B  1 98  ? -43.92400 -26.62100 17.07000  1.000 27.64066  ? 98  GLY B HA3  1 
ATOM   4832 N  N    . TYR B  1 99  ? -42.30500 -28.44300 16.34300  1.000 23.62611  ? 99  TYR B N    1 
ATOM   4833 C  CA   . TYR B  1 99  ? -41.73700 -29.73500 15.97400  1.000 23.38172  ? 99  TYR B CA   1 
ATOM   4834 C  C    . TYR B  1 99  ? -42.82000 -30.75000 15.65400  1.000 25.51262  ? 99  TYR B C    1 
ATOM   4835 O  O    . TYR B  1 99  ? -43.78500 -30.91700 16.40400  1.000 29.24558  ? 99  TYR B O    1 
ATOM   4836 C  CB   . TYR B  1 99  ? -40.88300 -30.20400 17.14500  1.000 25.67651  ? 99  TYR B CB   1 
ATOM   4837 C  CG   . TYR B  1 99  ? -40.01300 -31.40700 16.92000  1.000 30.90908  ? 99  TYR B CG   1 
ATOM   4838 C  CD1  . TYR B  1 99  ? -38.97000 -31.38400 16.00900  1.000 29.24501  ? 99  TYR B CD1  1 
ATOM   4839 C  CD2  . TYR B  1 99  ? -40.19500 -32.55500 17.67200  1.000 38.85927  ? 99  TYR B CD2  1 
ATOM   4840 C  CE1  . TYR B  1 99  ? -38.15300 -32.49100 15.83100  1.000 33.72304  ? 99  TYR B CE1  1 
ATOM   4841 C  CE2  . TYR B  1 99  ? -39.39000 -33.65700 17.50000  1.000 38.39900  ? 99  TYR B CE2  1 
ATOM   4842 C  CZ   . TYR B  1 99  ? -38.37100 -33.61400 16.58600  1.000 40.12511  ? 99  TYR B CZ   1 
ATOM   4843 O  OH   . TYR B  1 99  ? -37.58300 -34.72700 16.43800  1.000 45.65288  ? 99  TYR B OH   1 
ATOM   4844 H  H    . TYR B  1 99  ? -42.03300 -28.16200 17.11000  1.000 28.35389  ? 99  TYR B H    1 
ATOM   4845 H  HA   . TYR B  1 99  ? -41.19500 -29.65500 15.17300  1.000 28.06063  ? 99  TYR B HA   1 
ATOM   4846 H  HB2  . TYR B  1 99  ? -40.29500 -29.47500 17.39700  1.000 30.81438  ? 99  TYR B HB2  1 
ATOM   4847 H  HB3  . TYR B  1 99  ? -41.47700 -30.42100 17.88000  1.000 30.81438  ? 99  TYR B HB3  1 
ATOM   4848 H  HD1  . TYR B  1 99  ? -38.81500 -30.61500 15.51000  1.000 35.09658  ? 99  TYR B HD1  1 
ATOM   4849 H  HD2  . TYR B  1 99  ? -40.87600 -32.58100 18.30500  1.000 46.63369  ? 99  TYR B HD2  1 
ATOM   4850 H  HE1  . TYR B  1 99  ? -37.46500 -32.47200 15.20500  1.000 40.47020  ? 99  TYR B HE1  1 
ATOM   4851 H  HE2  . TYR B  1 99  ? -39.53700 -34.42600 18.00200  1.000 46.08137  ? 99  TYR B HE2  1 
ATOM   4852 H  HH   . TYR B  1 99  ? -37.83500 -35.33000 16.96600  1.000 54.78602  ? 99  TYR B HH   1 
ATOM   4853 N  N    . MET B  1 100 ? -42.63400 -31.44800 14.54200  1.000 27.65657  ? 100 MET B N    1 
ATOM   4854 C  CA   . MET B  1 100 ? -43.51600 -32.53200 14.12200  1.000 30.21596  ? 100 MET B CA   1 
ATOM   4855 C  C    . MET B  1 100 ? -44.93700 -32.07400 13.88600  1.000 32.01656  ? 100 MET B C    1 
ATOM   4856 O  O    . MET B  1 100 ? -45.85800 -32.89500 13.93500  1.000 37.26445  ? 100 MET B O    1 
ATOM   4857 C  CB   . MET B  1 100 ? -43.48300 -33.68800 15.12900  1.000 37.40048  ? 100 MET B CB   1 
ATOM   4858 C  CG   . MET B  1 100 ? -42.08300 -34.24700 15.33300  1.000 39.58613  ? 100 MET B CG   1 
ATOM   4859 S  SD   . MET B  1 100 ? -41.36200 -34.88600 13.79800  1.000 46.12986  ? 100 MET B SD   1 
ATOM   4860 C  CE   . MET B  1 100 ? -42.40100 -36.31900 13.56200  1.000 47.79504  ? 100 MET B CE   1 
ATOM   4861 H  H    . MET B  1 100 ? -41.98400 -31.30800 13.99600  1.000 33.19044  ? 100 MET B H    1 
ATOM   4862 H  HA   . MET B  1 100 ? -43.18400 -32.87000 13.27600  1.000 36.26171  ? 100 MET B HA   1 
ATOM   4863 H  HB2  . MET B  1 100 ? -43.80700 -33.37000 15.98600  1.000 44.88313  ? 100 MET B HB2  1 
ATOM   4864 H  HB3  . MET B  1 100 ? -44.04900 -34.40600 14.80500  1.000 44.88313  ? 100 MET B HB3  1 
ATOM   4865 H  HG2  . MET B  1 100 ? -41.50500 -33.54200 15.66600  1.000 47.50591  ? 100 MET B HG2  1 
ATOM   4866 H  HG3  . MET B  1 100 ? -42.12200 -34.97400 15.97300  1.000 47.50591  ? 100 MET B HG3  1 
ATOM   4867 H  HE1  . MET B  1 100 ? -42.10600 -36.79600 12.77100  1.000 57.35661  ? 100 MET B HE1  1 
ATOM   4868 H  HE2  . MET B  1 100 ? -42.32700 -36.89300 14.34100  1.000 57.35661  ? 100 MET B HE2  1 
ATOM   4869 H  HE3  . MET B  1 100 ? -43.31900 -36.02800 13.45100  1.000 57.35661  ? 100 MET B HE3  1 
ATOM   4870 N  N    . SER B  1 101 ? -45.13500 -30.79300 13.57600  1.000 27.54459  ? 101 SER B N    1 
ATOM   4871 C  CA   A SER B  1 101 ? -46.46200 -30.24700 13.36000  0.571 28.38028  ? 101 SER B CA   1 
ATOM   4872 C  CA   B SER B  1 101 ? -46.46700 -30.26300 13.35300  0.429 28.66077  ? 101 SER B CA   1 
ATOM   4873 C  C    . SER B  1 101 ? -46.53200 -29.50500 12.03300  1.000 28.41663  ? 101 SER B C    1 
ATOM   4874 O  O    . SER B  1 101 ? -45.52500 -29.03700 11.48300  1.000 26.92384  ? 101 SER B O    1 
ATOM   4875 C  CB   A SER B  1 101 ? -46.86900 -29.30000 14.48700  0.571 27.14043  ? 101 SER B CB   1 
ATOM   4876 C  CB   B SER B  1 101 ? -46.91100 -29.33800 14.48800  0.429 27.03743  ? 101 SER B CB   1 
ATOM   4877 O  OG   A SER B  1 101 ? -46.94900 -30.00400 15.70800  0.571 29.30001  ? 101 SER B OG   1 
ATOM   4878 O  OG   B SER B  1 101 ? -46.13400 -28.15400 14.49600  0.429 29.11266  ? 101 SER B OG   1 
ATOM   4879 H  H    A SER B  1 101 ? -44.50300 -30.21700 13.48500  0.571 33.05607  ? 101 SER B H    1 
ATOM   4880 H  H    B SER B  1 101 ? -44.50600 -30.21300 13.49000  0.429 33.05607  ? 101 SER B H    1 
ATOM   4881 H  HA   A SER B  1 101 ? -47.09000 -30.98500 13.32100  0.571 34.05890  ? 101 SER B HA   1 
ATOM   4882 H  HA   B SER B  1 101 ? -47.08200 -31.01100 13.29900  0.429 34.39548  ? 101 SER B HA   1 
ATOM   4883 H  HB2  A SER B  1 101 ? -46.20600 -28.59700 14.56700  0.571 32.57108  ? 101 SER B HB2  1 
ATOM   4884 H  HB2  B SER B  1 101 ? -47.84400 -29.10400 14.36000  0.429 32.44747  ? 101 SER B HB2  1 
ATOM   4885 H  HB3  A SER B  1 101 ? -47.73600 -28.91600 14.28300  0.571 32.57108  ? 101 SER B HB3  1 
ATOM   4886 H  HB3  B SER B  1 101 ? -46.79800 -29.79700 15.33500  0.429 32.44747  ? 101 SER B HB3  1 
ATOM   4887 H  HG   A SER B  1 101 ? -46.99000 -29.46300 16.34900  0.571 35.16257  ? 101 SER B HG   1 
ATOM   4888 H  HG   B SER B  1 101 ? -45.32400 -28.34200 14.38300  0.429 34.93775  ? 101 SER B HG   1 
ATOM   4889 N  N    . TYR B  1 102 ? -47.73800 -29.39100 11.53300  1.000 26.59666  ? 102 TYR B N    1 
ATOM   4890 C  CA   . TYR B  1 102 ? -47.98600 -28.72100 10.28200  1.000 27.90367  ? 102 TYR B CA   1 
ATOM   4891 C  C    . TYR B  1 102 ? -48.72200 -27.41300 10.50900  1.000 26.68832  ? 102 TYR B C    1 
ATOM   4892 O  O    . TYR B  1 102 ? -49.20400 -27.09300 11.59900  1.000 26.29140  ? 102 TYR B O    1 
ATOM   4893 C  CB   . TYR B  1 102 ? -48.79500 -29.63800 9.34800   1.000 30.15041  ? 102 TYR B CB   1 
ATOM   4894 C  CG   . TYR B  1 102 ? -48.06400 -30.88800 8.93400   1.000 26.81689  ? 102 TYR B CG   1 
ATOM   4895 C  CD1  . TYR B  1 102 ? -47.29900 -30.90300 7.79300   1.000 30.41165  ? 102 TYR B CD1  1 
ATOM   4896 C  CD2  . TYR B  1 102 ? -48.17800 -32.06000 9.66400   1.000 33.72641  ? 102 TYR B CD2  1 
ATOM   4897 C  CE1  . TYR B  1 102 ? -46.63400 -32.06000 7.39400   1.000 35.53601  ? 102 TYR B CE1  1 
ATOM   4898 C  CE2  . TYR B  1 102 ? -47.52000 -33.21300 9.27500   1.000 39.23039  ? 102 TYR B CE2  1 
ATOM   4899 C  CZ   . TYR B  1 102 ? -46.75300 -33.19800 8.14600   1.000 37.89469  ? 102 TYR B CZ   1 
ATOM   4900 O  OH   . TYR B  1 102 ? -46.09900 -34.35100 7.75600   1.000 44.34289  ? 102 TYR B OH   1 
ATOM   4901 H  H    . TYR B  1 102 ? -48.44600 -29.70100 11.90900  1.000 31.91855  ? 102 TYR B H    1 
ATOM   4902 H  HA   . TYR B  1 102 ? -47.14000 -28.50800 9.85900   1.000 33.48697  ? 102 TYR B HA   1 
ATOM   4903 H  HB2  . TYR B  1 102 ? -49.60700 -29.90800 9.80300   1.000 36.18306  ? 102 TYR B HB2  1 
ATOM   4904 H  HB3  . TYR B  1 102 ? -49.01500 -29.14500 8.54200   1.000 36.18306  ? 102 TYR B HB3  1 
ATOM   4905 H  HD1  . TYR B  1 102 ? -47.22400 -30.13100 7.28100   1.000 36.49655  ? 102 TYR B HD1  1 
ATOM   4906 H  HD2  . TYR B  1 102 ? -48.70600 -32.07200 10.43000  1.000 40.47426  ? 102 TYR B HD2  1 
ATOM   4907 H  HE1  . TYR B  1 102 ? -46.11400 -32.06000 6.62300   1.000 42.64578  ? 102 TYR B HE1  1 
ATOM   4908 H  HE2  . TYR B  1 102 ? -47.59900 -33.99100 9.77800   1.000 47.07904  ? 102 TYR B HE2  1 
ATOM   4909 H  HH   . TYR B  1 102 ? -45.64300 -34.20300 7.06600   1.000 53.21404  ? 102 TYR B HH   1 
ATOM   4910 N  N    . GLN B  1 103 ? -48.78900 -26.66200 9.42200   1.000 25.08350  ? 103 GLN B N    1 
ATOM   4911 C  CA   . GLN B  1 103 ? -49.42200 -25.35700 9.40400   1.000 25.33243  ? 103 GLN B CA   1 
ATOM   4912 C  C    . GLN B  1 103 ? -50.80000 -25.35500 10.04600  1.000 25.78326  ? 103 GLN B C    1 
ATOM   4913 O  O    . GLN B  1 103 ? -51.16700 -24.39600 10.73300  1.000 25.42387  ? 103 GLN B O    1 
ATOM   4914 C  CB   . GLN B  1 103 ? -49.45100 -24.99800 7.91700   1.000 35.97504  ? 103 GLN B CB   1 
ATOM   4915 C  CG   . GLN B  1 103 ? -50.13900 -23.81000 7.58500   1.000 31.56932  ? 103 GLN B CG   1 
ATOM   4916 C  CD   . GLN B  1 103 ? -50.30900 -23.59400 6.08400   1.000 25.07181  ? 103 GLN B CD   1 
ATOM   4917 O  OE1  . GLN B  1 103 ? -50.98100 -22.67400 5.72200   1.000 25.97106  ? 103 GLN B OE1  1 
ATOM   4918 N  NE2  . GLN B  1 103 ? -49.68400 -24.41500 5.24400   1.000 32.16884  ? 103 GLN B NE2  1 
ATOM   4919 H  H    . GLN B  1 103 ? -48.46700 -26.89100 8.65900   1.000 30.10276  ? 103 GLN B H    1 
ATOM   4920 H  HA   . GLN B  1 103 ? -48.93800 -24.69400 9.92100   1.000 30.40148  ? 103 GLN B HA   1 
ATOM   4921 H  HB2  . GLN B  1 103 ? -48.53600 -24.89500 7.61200   1.000 43.17262  ? 103 GLN B HB2  1 
ATOM   4922 H  HB3  . GLN B  1 103 ? -49.88100 -25.72300 7.43800   1.000 43.17262  ? 103 GLN B HB3  1 
ATOM   4923 H  HG2  . GLN B  1 103 ? -51.02400 -23.84100 7.98100   1.000 37.88574  ? 103 GLN B HG2  1 
ATOM   4924 H  HG3  . GLN B  1 103 ? -49.64400 -23.05400 7.93800   1.000 37.88574  ? 103 GLN B HG3  1 
ATOM   4925 H  HE21 . GLN B  1 103 ? -49.19500 -25.05300 5.55000   1.000 38.60517  ? 103 GLN B HE21 1 
ATOM   4926 H  HE22 . GLN B  1 103 ? -49.76900 -24.30800 4.39500   1.000 38.60517  ? 103 GLN B HE22 1 
ATOM   4927 N  N    . SER B  1 104 ? -51.57500 -26.41500 9.85100   1.000 24.68769  ? 104 SER B N    1 
ATOM   4928 C  CA   . SER B  1 104 ? -52.93000 -26.44600 10.38100  1.000 22.77343  ? 104 SER B CA   1 
ATOM   4929 C  C    . SER B  1 104 ? -52.96600 -26.30100 11.89200  1.000 23.31796  ? 104 SER B C    1 
ATOM   4930 O  O    . SER B  1 104 ? -53.98100 -25.83500 12.44500  1.000 25.11052  ? 104 SER B O    1 
ATOM   4931 C  CB   . SER B  1 104 ? -53.64100 -27.72400 9.92600   1.000 28.57671  ? 104 SER B CB   1 
ATOM   4932 O  OG   . SER B  1 104 ? -52.96900 -28.87200 10.38900  1.000 33.30513  ? 104 SER B OG   1 
ATOM   4933 H  H    . SER B  1 104 ? -51.34300 -27.12200 9.41900   1.000 29.62779  ? 104 SER B H    1 
ATOM   4934 H  HA   . SER B  1 104 ? -53.42100 -25.69200 10.01900  1.000 27.33068  ? 104 SER B HA   1 
ATOM   4935 H  HB2  . SER B  1 104 ? -54.54400 -27.72400 10.28000  1.000 34.29461  ? 104 SER B HB2  1 
ATOM   4936 H  HB3  . SER B  1 104 ? -53.66500 -27.74300 8.95700   1.000 34.29461  ? 104 SER B HB3  1 
ATOM   4937 H  HG   . SER B  1 104 ? -52.18000 -28.88000 10.09900  1.000 39.96872  ? 104 SER B HG   1 
ATOM   4938 N  N    . SER B  1 105 ? -51.89800 -26.66300 12.58700  1.000 23.20748  ? 105 SER B N    1 
ATOM   4939 C  CA   . SER B  1 105 ? -51.91400 -26.56300 14.04400  1.000 23.59289  ? 105 SER B CA   1 
ATOM   4940 C  C    . SER B  1 105 ? -51.99700 -25.13500 14.55900  1.000 22.98240  ? 105 SER B C    1 
ATOM   4941 O  O    . SER B  1 105 ? -52.37800 -24.94200 15.72100  1.000 24.08995  ? 105 SER B O    1 
ATOM   4942 C  CB   . SER B  1 105 ? -50.69000 -27.23600 14.64600  1.000 25.55944  ? 105 SER B CB   1 
ATOM   4943 O  OG   . SER B  1 105 ? -49.50000 -26.55600 14.27600  1.000 26.51610  ? 105 SER B OG   1 
ATOM   4944 H  H    . SER B  1 105 ? -51.16600 -26.96400 12.25000  1.000 27.85154  ? 105 SER B H    1 
ATOM   4945 H  HA   . SER B  1 105 ? -52.70700 -27.03300 14.34800  1.000 28.31403  ? 105 SER B HA   1 
ATOM   4946 H  HB2  . SER B  1 105 ? -50.77000 -27.22700 15.61300  1.000 30.67388  ? 105 SER B HB2  1 
ATOM   4947 H  HB3  . SER B  1 105 ? -50.64300 -28.15000 14.32600  1.000 30.67388  ? 105 SER B HB3  1 
ATOM   4948 H  HG   . SER B  1 105 ? -49.33300 -26.69200 13.46400  1.000 31.82188  ? 105 SER B HG   1 
ATOM   4949 N  N    . ILE B  1 106 ? -51.65500 -24.13500 13.74500  1.000 20.10157  ? 106 ILE B N    1 
ATOM   4950 C  CA   . ILE B  1 106 ? -51.69700 -22.73900 14.17300  1.000 20.41792  ? 106 ILE B CA   1 
ATOM   4951 C  C    . ILE B  1 106 ? -52.62100 -21.89000 13.29300  1.000 18.51481  ? 106 ILE B C    1 
ATOM   4952 O  O    . ILE B  1 106 ? -52.57200 -20.65500 13.34700  1.000 19.03298  ? 106 ILE B O    1 
ATOM   4953 C  CB   . ILE B  1 106 ? -50.29900 -22.10300 14.33400  1.000 19.76268  ? 106 ILE B CB   1 
ATOM   4954 C  CG1  . ILE B  1 106 ? -49.37300 -22.32400 13.13500  1.000 20.65491  ? 106 ILE B CG1  1 
ATOM   4955 C  CG2  . ILE B  1 106 ? -49.62000 -22.69200 15.58400  1.000 22.80054  ? 106 ILE B CG2  1 
ATOM   4956 C  CD1  . ILE B  1 106 ? -49.83000 -21.68400 11.80200  1.000 19.34770  ? 106 ILE B CD1  1 
ATOM   4957 H  H    . ILE B  1 106 ? -51.39300 -24.24300 12.93300  1.000 24.12445  ? 106 ILE B H    1 
ATOM   4958 H  HA   . ILE B  1 106 ? -52.08300 -22.74600 15.06200  1.000 24.50407  ? 106 ILE B HA   1 
ATOM   4959 H  HB   . ILE B  1 106 ? -50.44400 -21.14700 14.41100  1.000 23.71778  ? 106 ILE B HB   1 
ATOM   4960 H  HG12 . ILE B  1 106 ? -48.50400 -21.95100 13.34900  1.000 24.78845  ? 106 ILE B HG12 1 
ATOM   4961 H  HG13 . ILE B  1 106 ? -49.29600 -23.27900 12.98200  1.000 24.78845  ? 106 ILE B HG13 1 
ATOM   4962 H  HG21 . ILE B  1 106 ? -48.72400 -22.32800 15.65800  1.000 27.36321  ? 106 ILE B HG21 1 
ATOM   4963 H  HG22 . ILE B  1 106 ? -50.14000 -22.45200 16.36800  1.000 27.36321  ? 106 ILE B HG22 1 
ATOM   4964 H  HG23 . ILE B  1 106 ? -49.58000 -23.65700 15.49700  1.000 27.36321  ? 106 ILE B HG23 1 
ATOM   4965 H  HD11 . ILE B  1 106 ? -49.12600 -21.78800 11.14400  1.000 23.21980  ? 106 ILE B HD11 1 
ATOM   4966 H  HD12 . ILE B  1 106 ? -50.63600 -22.12900 11.49800  1.000 23.21980  ? 106 ILE B HD12 1 
ATOM   4967 H  HD13 . ILE B  1 106 ? -50.00900 -20.74200 11.95000  1.000 23.21980  ? 106 ILE B HD13 1 
ATOM   4968 N  N    . SER B  1 107 ? -53.52200 -22.54100 12.56000  1.000 20.62913  ? 107 SER B N    1 
ATOM   4969 C  CA   . SER B  1 107 ? -54.33900 -21.86500 11.55900  1.000 19.82275  ? 107 SER B CA   1 
ATOM   4970 C  C    . SER B  1 107 ? -55.25300 -20.79600 12.14400  1.000 19.26664  ? 107 SER B C    1 
ATOM   4971 O  O    . SER B  1 107 ? -55.56300 -19.82000 11.43700  1.000 19.95262  ? 107 SER B O    1 
ATOM   4972 C  CB   . SER B  1 107 ? -55.10400 -22.91300 10.74300  1.000 23.31473  ? 107 SER B CB   1 
ATOM   4973 O  OG   . SER B  1 107 ? -56.03700 -23.60500 11.56000  1.000 26.53229  ? 107 SER B OG   1 
ATOM   4974 H  H    . SER B  1 107 ? -53.68100 -23.38300 12.62300  1.000 24.75752  ? 107 SER B H    1 
ATOM   4975 H  HA   . SER B  1 107 ? -53.75800 -21.38400 10.94900  1.000 23.78986  ? 107 SER B HA   1 
ATOM   4976 H  HB2  . SER B  1 107 ? -55.58200 -22.46700 10.02600  1.000 27.98024  ? 107 SER B HB2  1 
ATOM   4977 H  HB3  . SER B  1 107 ? -54.47200 -23.55000 10.37500  1.000 27.98024  ? 107 SER B HB3  1 
ATOM   4978 H  HG   . SER B  1 107 ? -55.65600 -23.89000 12.25200  1.000 31.84131  ? 107 SER B HG   1 
ATOM   4979 N  N    . PHE B  1 108 ? -55.71200 -20.95300 13.38500  1.000 18.76055  ? 108 PHE B N    1 
ATOM   4980 C  CA   . PHE B  1 108 ? -56.50700 -19.89900 14.04000  1.000 18.78066  ? 108 PHE B CA   1 
ATOM   4981 C  C    . PHE B  1 108 ? -55.94600 -18.50600 13.81100  1.000 18.23294  ? 108 PHE B C    1 
ATOM   4982 O  O    . PHE B  1 108 ? -56.68800 -17.55100 13.56200  1.000 17.76851  ? 108 PHE B O    1 
ATOM   4983 C  CB   . PHE B  1 108 ? -56.52000 -20.18100 15.53300  1.000 17.89208  ? 108 PHE B CB   1 
ATOM   4984 C  CG   . PHE B  1 108 ? -56.92600 -19.01600 16.41000  1.000 16.98480  ? 108 PHE B CG   1 
ATOM   4985 C  CD1  . PHE B  1 108 ? -58.28400 -18.75700 16.67400  1.000 18.46007  ? 108 PHE B CD1  1 
ATOM   4986 C  CD2  . PHE B  1 108 ? -55.99800 -18.21900 17.00700  1.000 17.48132  ? 108 PHE B CD2  1 
ATOM   4987 C  CE1  . PHE B  1 108 ? -58.62700 -17.71400 17.51400  1.000 17.82079  ? 108 PHE B CE1  1 
ATOM   4988 C  CE2  . PHE B  1 108 ? -56.34800 -17.16000 17.84700  1.000 17.43252  ? 108 PHE B CE2  1 
ATOM   4989 C  CZ   . PHE B  1 108 ? -57.68100 -16.94300 18.12600  1.000 18.44224  ? 108 PHE B CZ   1 
ATOM   4990 H  H    . PHE B  1 108 ? -55.58100 -21.65200 13.86900  1.000 22.51522  ? 108 PHE B H    1 
ATOM   4991 H  HA   . PHE B  1 108 ? -57.40200 -19.90700 13.66600  1.000 22.53935  ? 108 PHE B HA   1 
ATOM   4992 H  HB2  . PHE B  1 108 ? -57.14500 -20.90300 15.70200  1.000 21.47306  ? 108 PHE B HB2  1 
ATOM   4993 H  HB3  . PHE B  1 108 ? -55.62600 -20.44700 15.80100  1.000 21.47306  ? 108 PHE B HB3  1 
ATOM   4994 H  HD1  . PHE B  1 108 ? -58.94600 -19.28300 16.28700  1.000 22.15464  ? 108 PHE B HD1  1 
ATOM   4995 H  HD2  . PHE B  1 108 ? -55.09600 -18.38700 16.85000  1.000 20.98015  ? 108 PHE B HD2  1 
ATOM   4996 H  HE1  . PHE B  1 108 ? -59.52700 -17.53300 17.66600  1.000 21.38751  ? 108 PHE B HE1  1 
ATOM   4997 H  HE2  . PHE B  1 108 ? -55.69400 -16.60900 18.21100  1.000 20.92158  ? 108 PHE B HE2  1 
ATOM   4998 H  HZ   . PHE B  1 108 ? -57.93300 -16.27800 18.72600  1.000 22.13325  ? 108 PHE B HZ   1 
ATOM   4999 N  N    . TRP B  1 109 ? -54.63400 -18.36200 13.89400  1.000 16.81878  ? 109 TRP B N    1 
ATOM   5000 C  CA   . TRP B  1 109 ? -54.00000 -17.05700 13.84700  1.000 16.71360  ? 109 TRP B CA   1 
ATOM   5001 C  C    . TRP B  1 109 ? -54.05600 -16.40000 12.47400  1.000 16.53716  ? 109 TRP B C    1 
ATOM   5002 O  O    . TRP B  1 109 ? -53.95000 -15.16700 12.42200  1.000 16.98205  ? 109 TRP B O    1 
ATOM   5003 C  CB   . TRP B  1 109 ? -52.54500 -17.23600 14.32400  1.000 15.46943  ? 109 TRP B CB   1 
ATOM   5004 C  CG   . TRP B  1 109 ? -52.48000 -17.48200 15.78800  1.000 15.98010  ? 109 TRP B CG   1 
ATOM   5005 C  CD1  . TRP B  1 109 ? -52.30000 -18.67000 16.41900  1.000 16.68819  ? 109 TRP B CD1  1 
ATOM   5006 C  CD2  . TRP B  1 109 ? -52.67600 -16.50200 16.82000  1.000 15.79288  ? 109 TRP B CD2  1 
ATOM   5007 N  NE1  . TRP B  1 109 ? -52.35600 -18.48600 17.77200  1.000 16.94993  ? 109 TRP B NE1  1 
ATOM   5008 C  CE2  . TRP B  1 109 ? -52.58000 -17.16300 18.04800  1.000 15.44097  ? 109 TRP B CE2  1 
ATOM   5009 C  CE3  . TRP B  1 109 ? -52.93100 -15.12200 16.80600  1.000 17.58653  ? 109 TRP B CE3  1 
ATOM   5010 C  CZ2  . TRP B  1 109 ? -52.70500 -16.50000 19.27100  1.000 17.94380  ? 109 TRP B CZ2  1 
ATOM   5011 C  CZ3  . TRP B  1 109 ? -53.07400 -14.45900 18.02000  1.000 19.08147  ? 109 TRP B CZ3  1 
ATOM   5012 C  CH2  . TRP B  1 109 ? -52.94600 -15.15200 19.23900  1.000 17.48934  ? 109 TRP B CH2  1 
ATOM   5013 H  H    . TRP B  1 109 ? -54.08000 -19.01400 13.98000  1.000 20.18510  ? 109 TRP B H    1 
ATOM   5014 H  HA   . TRP B  1 109 ? -54.45900 -16.44100 14.43900  1.000 20.05889  ? 109 TRP B HA   1 
ATOM   5015 H  HB2  . TRP B  1 109 ? -52.14900 -17.99600 13.86900  1.000 18.56588  ? 109 TRP B HB2  1 
ATOM   5016 H  HB3  . TRP B  1 109 ? -52.04100 -16.43100 14.12700  1.000 18.56588  ? 109 TRP B HB3  1 
ATOM   5017 H  HD1  . TRP B  1 109 ? -52.16000 -19.48600 15.99500  1.000 20.02838  ? 109 TRP B HD1  1 
ATOM   5018 H  HE1  . TRP B  1 109 ? -52.26400 -19.10700 18.36000  1.000 20.34248  ? 109 TRP B HE1  1 
ATOM   5019 H  HE3  . TRP B  1 109 ? -53.00400 -14.66100 16.00200  1.000 21.10640  ? 109 TRP B HE3  1 
ATOM   5020 H  HZ2  . TRP B  1 109 ? -52.62800 -16.95700 20.07700  1.000 21.53512  ? 109 TRP B HZ2  1 
ATOM   5021 H  HZ3  . TRP B  1 109 ? -53.25700 -13.54800 18.02600  1.000 22.90033  ? 109 TRP B HZ3  1 
ATOM   5022 H  HH2  . TRP B  1 109 ? -53.02600 -14.68400 20.03900  1.000 20.98977  ? 109 TRP B HH2  1 
ATOM   5023 N  N    . GLY B  1 110 ? -54.22400 -17.16300 11.39200  1.000 17.00569  ? 110 GLY B N    1 
ATOM   5024 C  CA   . GLY B  1 110 ? -54.28000 -16.58200 10.07400  1.000 17.47744  ? 110 GLY B CA   1 
ATOM   5025 C  C    . GLY B  1 110 ? -55.46700 -15.64700 9.89000   1.000 17.42909  ? 110 GLY B C    1 
ATOM   5026 O  O    . GLY B  1 110 ? -55.29600 -14.43300 9.69700   1.000 17.98793  ? 110 GLY B O    1 
ATOM   5027 H  H    . GLY B  1 110 ? -54.30700 -18.01900 11.40700  1.000 20.40938  ? 110 GLY B H    1 
ATOM   5028 H  HA2  . GLY B  1 110 ? -53.46800 -16.07600 9.91400   1.000 20.97548  ? 110 GLY B HA2  1 
ATOM   5029 H  HA3  . GLY B  1 110 ? -54.34600 -17.29000 9.41500   1.000 20.97548  ? 110 GLY B HA3  1 
ATOM   5030 N  N    . PRO B  1 111 ? -56.68800 -16.19000 9.97200   1.000 16.77643  ? 111 PRO B N    1 
ATOM   5031 C  CA   . PRO B  1 111 ? -57.86600 -15.32900 9.82500   1.000 17.80878  ? 111 PRO B CA   1 
ATOM   5032 C  C    . PRO B  1 111 ? -57.99900 -14.32600 10.94800  1.000 16.32235  ? 111 PRO B C    1 
ATOM   5033 O  O    . PRO B  1 111 ? -58.45400 -13.19800 10.72800  1.000 17.03705  ? 111 PRO B O    1 
ATOM   5034 C  CB   . PRO B  1 111 ? -59.03200 -16.31700 9.83900   1.000 18.49311  ? 111 PRO B CB   1 
ATOM   5035 C  CG   . PRO B  1 111 ? -58.45200 -17.62900 9.44200   1.000 21.27146  ? 111 PRO B CG   1 
ATOM   5036 C  CD   . PRO B  1 111 ? -57.05800 -17.61100 9.99900   1.000 17.35376  ? 111 PRO B CD   1 
ATOM   5037 H  HA   . PRO B  1 111 ? -57.83300 -14.87300 8.96900   1.000 21.37310  ? 111 PRO B HA   1 
ATOM   5038 H  HB2  . PRO B  1 111 ? -59.41100 -16.36300 10.73100  1.000 22.19429  ? 111 PRO B HB2  1 
ATOM   5039 H  HB3  . PRO B  1 111 ? -59.71000 -16.03400 9.20600   1.000 22.19429  ? 111 PRO B HB3  1 
ATOM   5040 H  HG2  . PRO B  1 111 ? -58.97100 -18.35200 9.82700   1.000 25.52831  ? 111 PRO B HG2  1 
ATOM   5041 H  HG3  . PRO B  1 111 ? -58.43900 -17.70800 8.47500   1.000 25.52831  ? 111 PRO B HG3  1 
ATOM   5042 H  HD2  . PRO B  1 111 ? -57.04800 -17.95100 10.90800  1.000 20.82708  ? 111 PRO B HD2  1 
ATOM   5043 H  HD3  . PRO B  1 111 ? -56.45900 -18.13300 9.44200   1.000 20.82708  ? 111 PRO B HD3  1 
ATOM   5044 N  N    . ARG B  1 112 ? -57.66300 -14.70400 12.17700  1.000 16.44632  ? 112 ARG B N    1 
ATOM   5045 C  CA   . ARG B  1 112 ? -57.88000 -13.80500 13.30400  1.000 16.05420  ? 112 ARG B CA   1 
ATOM   5046 C  C    . ARG B  1 112 ? -57.05800 -12.54600 13.18100  1.000 15.81468  ? 112 ARG B C    1 
ATOM   5047 O  O    . ARG B  1 112 ? -57.55100 -11.44500 13.43400  1.000 16.73452  ? 112 ARG B O    1 
ATOM   5048 C  CB   . ARG B  1 112 ? -57.58700 -14.51600 14.60800  1.000 17.05437  ? 112 ARG B CB   1 
ATOM   5049 C  CG   . ARG B  1 112 ? -57.90200 -13.68800 15.86600  1.000 15.83753  ? 112 ARG B CG   1 
ATOM   5050 C  CD   . ARG B  1 112 ? -59.33600 -13.12400 15.85400  1.000 16.06767  ? 112 ARG B CD   1 
ATOM   5051 N  NE   . ARG B  1 112 ? -59.74500 -12.64500 17.18600  1.000 16.66648  ? 112 ARG B NE   1 
ATOM   5052 C  CZ   . ARG B  1 112 ? -60.30600 -13.38600 18.11800  1.000 16.80470  ? 112 ARG B CZ   1 
ATOM   5053 N  NH1  . ARG B  1 112 ? -60.59600 -14.65700 17.90500  1.000 18.25647  ? 112 ARG B NH1  1 
ATOM   5054 N  NH2  . ARG B  1 112 ? -60.56900 -12.84000 19.30800  1.000 16.61841  ? 112 ARG B NH2  1 
ATOM   5055 H  H    . ARG B  1 112 ? -57.31300 -15.46200 12.38300  1.000 19.73815  ? 112 ARG B H    1 
ATOM   5056 H  HA   . ARG B  1 112 ? -58.81500 -13.54400 13.31200  1.000 19.26760  ? 112 ARG B HA   1 
ATOM   5057 H  HB2  . ARG B  1 112 ? -58.12100 -15.32500 14.64700  1.000 20.46780  ? 112 ARG B HB2  1 
ATOM   5058 H  HB3  . ARG B  1 112 ? -56.64300 -14.74100 14.63300  1.000 20.46780  ? 112 ARG B HB3  1 
ATOM   5059 H  HG2  . ARG B  1 112 ? -57.80800 -14.25200 16.65000  1.000 19.00760  ? 112 ARG B HG2  1 
ATOM   5060 H  HG3  . ARG B  1 112 ? -57.28500 -12.94200 15.91800  1.000 19.00760  ? 112 ARG B HG3  1 
ATOM   5061 H  HD2  . ARG B  1 112 ? -59.38100 -12.37800 15.23600  1.000 19.28376  ? 112 ARG B HD2  1 
ATOM   5062 H  HD3  . ARG B  1 112 ? -59.95200 -13.82000 15.57900  1.000 19.28376  ? 112 ARG B HD3  1 
ATOM   5063 H  HE   . ARG B  1 112 ? -59.60700 -11.81600 17.36800  1.000 20.00234  ? 112 ARG B HE   1 
ATOM   5064 H  HH11 . ARG B  1 112 ? -60.41900 -15.01800 17.14500  1.000 21.91032  ? 112 ARG B HH11 1 
ATOM   5065 H  HH12 . ARG B  1 112 ? -60.96300 -15.12500 18.52700  1.000 21.91032  ? 112 ARG B HH12 1 
ATOM   5066 H  HH21 . ARG B  1 112 ? -60.37200 -12.01600 19.45600  1.000 19.94466  ? 112 ARG B HH21 1 
ATOM   5067 H  HH22 . ARG B  1 112 ? -60.93500 -13.31200 19.92700  1.000 19.94466  ? 112 ARG B HH22 1 
ATOM   5068 N  N    . LEU B  1 113 ? -55.77700 -12.68000 12.79600  1.000 15.56868  ? 113 LEU B N    1 
ATOM   5069 C  CA   . LEU B  1 113 ? -54.96900 -11.48700 12.58400  1.000 15.45540  ? 113 LEU B CA   1 
ATOM   5070 C  C    . LEU B  1 113 ? -55.33700 -10.79000 11.26700  1.000 15.01901  ? 113 LEU B C    1 
ATOM   5071 O  O    . LEU B  1 113 ? -55.47000 -9.55400  11.22800  1.000 16.18103  ? 113 LEU B O    1 
ATOM   5072 C  CB   . LEU B  1 113 ? -53.48400 -11.85000 12.63500  1.000 15.94592  ? 113 LEU B CB   1 
ATOM   5073 C  CG   . LEU B  1 113 ? -52.92100 -12.14700 13.99600  1.000 17.60511  ? 113 LEU B CG   1 
ATOM   5074 C  CD1  . LEU B  1 113 ? -51.61200 -12.89900 13.86200  1.000 17.89908  ? 113 LEU B CD1  1 
ATOM   5075 C  CD2  . LEU B  1 113 ? -52.70500 -10.83000 14.73300  1.000 19.36549  ? 113 LEU B CD2  1 
ATOM   5076 H  H    . LEU B  1 113 ? -55.37400 -13.42700 12.65900  1.000 18.68498  ? 113 LEU B H    1 
ATOM   5077 H  HA   . LEU B  1 113 ? -55.13300 -10.85200 13.30000  1.000 18.54904  ? 113 LEU B HA   1 
ATOM   5078 H  HB2  . LEU B  1 113 ? -53.34800 -12.64100 12.09000  1.000 19.13767  ? 113 LEU B HB2  1 
ATOM   5079 H  HB3  . LEU B  1 113 ? -52.97900 -11.10600 12.27200  1.000 19.13767  ? 113 LEU B HB3  1 
ATOM   5080 H  HG   . LEU B  1 113 ? -53.53300 -12.70100 14.50400  1.000 21.12870  ? 113 LEU B HG   1 
ATOM   5081 H  HD11 . LEU B  1 113 ? -51.25800 -13.07800 14.74700  1.000 21.48146  ? 113 LEU B HD11 1 
ATOM   5082 H  HD12 . LEU B  1 113 ? -51.77400 -13.73400 13.39500  1.000 21.48146  ? 113 LEU B HD12 1 
ATOM   5083 H  HD13 . LEU B  1 113 ? -50.98500 -12.35500 13.35900  1.000 21.48146  ? 113 LEU B HD13 1 
ATOM   5084 H  HD21 . LEU B  1 113 ? -52.40600 -11.01900 15.63600  1.000 23.24115  ? 113 LEU B HD21 1 
ATOM   5085 H  HD22 . LEU B  1 113 ? -52.03200 -10.31200 14.26400  1.000 23.24115  ? 113 LEU B HD22 1 
ATOM   5086 H  HD23 . LEU B  1 113 ? -53.54200 -10.34100 14.75700  1.000 23.24115  ? 113 LEU B HD23 1 
ATOM   5087 N  N    . ALA B  1 114 ? -55.51700 -11.54500 10.16900  1.000 15.69873  ? 114 ALA B N    1 
ATOM   5088 C  CA   . ALA B  1 114 ? -55.73800 -10.88400 8.88400   1.000 16.39591  ? 114 ALA B CA   1 
ATOM   5089 C  C    . ALA B  1 114 ? -56.99700 -10.03500 8.88700   1.000 16.10907  ? 114 ALA B C    1 
ATOM   5090 O  O    . ALA B  1 114 ? -57.05200 -8.98100  8.23900   1.000 16.37377  ? 114 ALA B O    1 
ATOM   5091 C  CB   . ALA B  1 114 ? -55.77300 -11.91200 7.76300   1.000 17.09422  ? 114 ALA B CB   1 
ATOM   5092 H  H    . ALA B  1 114 ? -55.51400 -12.40500 10.14800  1.000 18.84104  ? 114 ALA B H    1 
ATOM   5093 H  HA   . ALA B  1 114 ? -54.99300 -10.28600 8.71600   1.000 19.67765  ? 114 ALA B HA   1 
ATOM   5094 H  HB1  . ALA B  1 114 ? -55.86700 -11.45100 6.91500   1.000 20.51562  ? 114 ALA B HB1  1 
ATOM   5095 H  HB2  . ALA B  1 114 ? -54.94600 -12.41900 7.77400   1.000 20.51562  ? 114 ALA B HB2  1 
ATOM   5096 H  HB3  . ALA B  1 114 ? -56.52700 -12.50600 7.90200   1.000 20.51562  ? 114 ALA B HB3  1 
ATOM   5097 N  N    . SER B  1 115 ? -58.05000 -10.52000 9.53700   1.000 15.62220  ? 115 SER B N    1 
ATOM   5098 C  CA   . SER B  1 115 ? -59.32500 -9.82700  9.57300   1.000 15.69416  ? 115 SER B CA   1 
ATOM   5099 C  C    . SER B  1 115 ? -59.27700 -8.54400  10.38200  1.000 14.87942  ? 115 SER B C    1 
ATOM   5100 O  O    . SER B  1 115 ? -60.25600 -7.78100  10.37100  1.000 15.80997  ? 115 SER B O    1 
ATOM   5101 C  CB   . SER B  1 115 ? -60.41100 -10.77200 10.04200  1.000 17.99086  ? 115 SER B CB   1 
ATOM   5102 O  OG   . SER B  1 115 ? -60.26500 -11.10300 11.41400  1.000 16.90124  ? 115 SER B OG   1 
ATOM   5103 H  H    . SER B  1 115 ? -58.04900 -11.26200 9.97200   1.000 18.74920  ? 115 SER B H    1 
ATOM   5104 H  HA   . SER B  1 115 ? -59.57700 -9.55800  8.67600   1.000 18.83556  ? 115 SER B HA   1 
ATOM   5105 H  HB2  . SER B  1 115 ? -61.27300 -10.34600 9.91400   1.000 21.59159  ? 115 SER B HB2  1 
ATOM   5106 H  HB3  . SER B  1 115 ? -60.36300 -11.58700 9.51700   1.000 21.59159  ? 115 SER B HB3  1 
ATOM   5107 H  HG   . SER B  1 115 ? -59.57500 -11.56900 11.52500  1.000 20.28405  ? 115 SER B HG   1 
ATOM   5108 N  N    . HIS B  1 116 ? -58.15800 -8.27500  11.06300  1.000 15.29256  ? 116 HIS B N    1 
ATOM   5109 C  CA   . HIS B  1 116 ? -57.91400 -7.00000  11.72800  1.000 14.91112  ? 116 HIS B CA   1 
ATOM   5110 C  C    . HIS B  1 116 ? -56.92000 -6.13000  10.96700  1.000 17.40854  ? 116 HIS B C    1 
ATOM   5111 O  O    . HIS B  1 116 ? -56.45200 -5.13600  11.50800  1.000 18.82475  ? 116 HIS B O    1 
ATOM   5112 C  CB   . HIS B  1 116 ? -57.45900 -7.24000  13.16900  1.000 15.04907  ? 116 HIS B CB   1 
ATOM   5113 C  CG   . HIS B  1 116 ? -58.58600 -7.52900  14.06300  1.000 13.85430  ? 116 HIS B CG   1 
ATOM   5114 N  ND1  . HIS B  1 116 ? -59.38000 -6.53200  14.59200  1.000 15.89631  ? 116 HIS B ND1  1 
ATOM   5115 C  CD2  . HIS B  1 116 ? -59.02300 -8.69200  14.59400  1.000 14.50579  ? 116 HIS B CD2  1 
ATOM   5116 C  CE1  . HIS B  1 116 ? -60.29300 -7.08100  15.35400  1.000 14.82017  ? 116 HIS B CE1  1 
ATOM   5117 N  NE2  . HIS B  1 116 ? -60.09900 -8.38700  15.38300  1.000 15.37680  ? 116 HIS B NE2  1 
ATOM   5118 H  H    . HIS B  1 116 ? -57.51100 -8.83400  11.15400  1.000 18.35363  ? 116 HIS B H    1 
ATOM   5119 H  HA   . HIS B  1 116 ? -58.74600 -6.50200  11.77000  1.000 17.89591  ? 116 HIS B HA   1 
ATOM   5120 H  HB2  . HIS B  1 116 ? -56.85500 -7.99800  13.18900  1.000 18.06144  ? 116 HIS B HB2  1 
ATOM   5121 H  HB3  . HIS B  1 116 ? -57.00800 -6.44700  13.49600  1.000 18.06144  ? 116 HIS B HB3  1 
ATOM   5122 H  HD2  . HIS B  1 116 ? -58.66200 -9.53700  14.45200  1.000 17.40951  ? 116 HIS B HD2  1 
ATOM   5123 H  HE1  . HIS B  1 116 ? -60.96800 -6.62500  15.80200  1.000 17.78676  ? 116 HIS B HE1  1 
ATOM   5124 H  HE2  . HIS B  1 116 ? -60.57200 -8.95400  15.82600  1.000 18.45472  ? 116 HIS B HE2  1 
ATOM   5125 N  N    . GLY B  1 117 ? -56.64200 -6.42700  9.69800   1.000 16.15878  ? 117 GLY B N    1 
ATOM   5126 C  CA   . GLY B  1 117 ? -55.84800 -5.50400  8.90100   1.000 16.01843  ? 117 GLY B CA   1 
ATOM   5127 C  C    . GLY B  1 117 ? -54.35900 -5.81500  8.89600   1.000 16.77695  ? 117 GLY B C    1 
ATOM   5128 O  O    . GLY B  1 117 ? -53.53500 -4.91900  9.07100   1.000 16.97652  ? 117 GLY B O    1 
ATOM   5129 H  H    . GLY B  1 117 ? -56.89600 -7.13900  9.28900   1.000 19.39310  ? 117 GLY B H    1 
ATOM   5130 H  HA2  . GLY B  1 117 ? -56.16200 -5.53100  7.98300   1.000 19.22468  ? 117 GLY B HA2  1 
ATOM   5131 H  HA3  . GLY B  1 117 ? -55.96600 -4.60600  9.24900   1.000 19.22468  ? 117 GLY B HA3  1 
ATOM   5132 N  N    . PHE B  1 118 ? -54.01100 -7.07700  8.63700   1.000 15.97409  ? 118 PHE B N    1 
ATOM   5133 C  CA   . PHE B  1 118 ? -52.64900 -7.52500  8.46100   1.000 14.73461  ? 118 PHE B CA   1 
ATOM   5134 C  C    . PHE B  1 118 ? -52.59000 -8.51200  7.30700   1.000 15.66471  ? 118 PHE B C    1 
ATOM   5135 O  O    . PHE B  1 118 ? -53.56600 -9.20800  7.01500   1.000 17.08926  ? 118 PHE B O    1 
ATOM   5136 C  CB   . PHE B  1 118 ? -52.12400 -8.23200  9.73700   1.000 15.19751  ? 118 PHE B CB   1 
ATOM   5137 C  CG   . PHE B  1 118 ? -52.05300 -7.33200  10.93800  1.000 15.41565  ? 118 PHE B CG   1 
ATOM   5138 C  CD1  . PHE B  1 118 ? -51.00800 -6.43900  11.11200  1.000 16.19131  ? 118 PHE B CD1  1 
ATOM   5139 C  CD2  . PHE B  1 118 ? -53.03700 -7.37200  11.92000  1.000 15.54651  ? 118 PHE B CD2  1 
ATOM   5140 C  CE1  . PHE B  1 118 ? -50.95700 -5.58000  12.20900  1.000 15.53285  ? 118 PHE B CE1  1 
ATOM   5141 C  CE2  . PHE B  1 118 ? -52.98600 -6.53700  13.02300  1.000 16.94331  ? 118 PHE B CE2  1 
ATOM   5142 C  CZ   . PHE B  1 118 ? -51.93900 -5.64800  13.15900  1.000 16.82979  ? 118 PHE B CZ   1 
ATOM   5143 H  H    . PHE B  1 118 ? -54.58100 -7.71600  8.55500   1.000 19.17147  ? 118 PHE B H    1 
ATOM   5144 H  HA   . PHE B  1 118 ? -52.08500 -6.76400  8.25700   1.000 17.68410  ? 118 PHE B HA   1 
ATOM   5145 H  HB2  . PHE B  1 118 ? -52.71800 -8.96800  9.95300   1.000 18.23957  ? 118 PHE B HB2  1 
ATOM   5146 H  HB3  . PHE B  1 118 ? -51.23100 -8.56600  9.56300   1.000 18.23957  ? 118 PHE B HB3  1 
ATOM   5147 H  HD1  . PHE B  1 118 ? -50.32400 -6.41300  10.48300  1.000 19.43213  ? 118 PHE B HD1  1 
ATOM   5148 H  HD2  . PHE B  1 118 ? -53.74300 -7.97100  11.83300  1.000 18.65838  ? 118 PHE B HD2  1 
ATOM   5149 H  HE1  . PHE B  1 118 ? -50.26300 -4.96700  12.29500  1.000 18.64198  ? 118 PHE B HE1  1 
ATOM   5150 H  HE2  . PHE B  1 118 ? -53.65400 -6.57500  13.66900  1.000 20.33454  ? 118 PHE B HE2  1 
ATOM   5151 H  HZ   . PHE B  1 118 ? -51.90100 -5.09100  13.90200  1.000 20.19831  ? 118 PHE B HZ   1 
ATOM   5152 N  N    . VAL B  1 119 ? -51.42300 -8.59300  6.67700   1.000 15.88726  ? 119 VAL B N    1 
ATOM   5153 C  CA   . VAL B  1 119 ? -51.17000 -9.63900  5.68300   1.000 16.27032  ? 119 VAL B CA   1 
ATOM   5154 C  C    . VAL B  1 119 ? -50.47800 -10.76700 6.42700   1.000 16.80032  ? 119 VAL B C    1 
ATOM   5155 O  O    . VAL B  1 119 ? -49.40500 -10.54900 7.00400   1.000 17.92358  ? 119 VAL B O    1 
ATOM   5156 C  CB   . VAL B  1 119 ? -50.30200 -9.12000  4.53800   1.000 16.85953  ? 119 VAL B CB   1 
ATOM   5157 C  CG1  . VAL B  1 119 ? -49.93300 -10.28400 3.62600   1.000 19.50795  ? 119 VAL B CG1  1 
ATOM   5158 C  CG2  . VAL B  1 119 ? -51.04500 -8.02900  3.77600   1.000 18.74150  ? 119 VAL B CG2  1 
ATOM   5159 H  H    . VAL B  1 119 ? -50.76200 -8.05700  6.80500   1.000 19.06728  ? 119 VAL B H    1 
ATOM   5160 H  HA   . VAL B  1 119 ? -52.00100 -9.95700  5.29800   1.000 19.52695  ? 119 VAL B HA   1 
ATOM   5161 H  HB   . VAL B  1 119 ? -49.48300 -8.73000  4.88200   1.000 20.23399  ? 119 VAL B HB   1 
ATOM   5162 H  HG11 . VAL B  1 119 ? -49.58100 -9.93300  2.79300   1.000 23.41211  ? 119 VAL B HG11 1 
ATOM   5163 H  HG12 . VAL B  1 119 ? -49.26100 -10.82800 4.06500   1.000 23.41211  ? 119 VAL B HG12 1 
ATOM   5164 H  HG13 . VAL B  1 119 ? -50.72700 -10.81300 3.45200   1.000 23.41211  ? 119 VAL B HG13 1 
ATOM   5165 H  HG21 . VAL B  1 119 ? -50.48800 -7.71900  3.04500   1.000 22.49236  ? 119 VAL B HG21 1 
ATOM   5166 H  HG22 . VAL B  1 119 ? -51.87400 -8.39500  3.42800   1.000 22.49236  ? 119 VAL B HG22 1 
ATOM   5167 H  HG23 . VAL B  1 119 ? -51.23600 -7.29600  4.38100   1.000 22.49236  ? 119 VAL B HG23 1 
ATOM   5168 N  N    . VAL B  1 120 ? -51.08900 -11.94500 6.49200   1.000 16.28010  ? 120 VAL B N    1 
ATOM   5169 C  CA   . VAL B  1 120 ? -50.66200 -12.97300 7.44400   1.000 15.19122  ? 120 VAL B CA   1 
ATOM   5170 C  C    . VAL B  1 120 ? -50.46200 -14.28900 6.72200   1.000 17.30028  ? 120 VAL B C    1 
ATOM   5171 O  O    . VAL B  1 120 ? -51.37400 -14.76400 6.04800   1.000 19.51952  ? 120 VAL B O    1 
ATOM   5172 C  CB   . VAL B  1 120 ? -51.71500 -13.17700 8.55400   1.000 16.11413  ? 120 VAL B CB   1 
ATOM   5173 C  CG1  . VAL B  1 120 ? -51.19000 -14.22300 9.58700   1.000 18.54017  ? 120 VAL B CG1  1 
ATOM   5174 C  CG2  . VAL B  1 120 ? -52.08700 -11.87400 9.21700   1.000 15.98418  ? 120 VAL B CG2  1 
ATOM   5175 H  H    . VAL B  1 120 ? -51.75300 -12.17500 5.99600   1.000 19.53868  ? 120 VAL B H    1 
ATOM   5176 H  HA   . VAL B  1 120 ? -49.81400 -12.69700 7.82600   1.000 18.23203  ? 120 VAL B HA   1 
ATOM   5177 H  HB   . VAL B  1 120 ? -52.53200 -13.52100 8.15900   1.000 19.33952  ? 120 VAL B HB   1 
ATOM   5178 H  HG11 . VAL B  1 120 ? -51.74400 -14.18700 10.38200  1.000 22.25077  ? 120 VAL B HG11 1 
ATOM   5179 H  HG12 . VAL B  1 120 ? -51.23500 -15.10800 9.19100   1.000 22.25077  ? 120 VAL B HG12 1 
ATOM   5180 H  HG13 . VAL B  1 120 ? -50.27100 -14.00900 9.81300   1.000 22.25077  ? 120 VAL B HG13 1 
ATOM   5181 H  HG21 . VAL B  1 120 ? -52.70900 -12.05300 9.94000   1.000 19.18358  ? 120 VAL B HG21 1 
ATOM   5182 H  HG22 . VAL B  1 120 ? -51.28400 -11.45700 9.56700   1.000 19.18358  ? 120 VAL B HG22 1 
ATOM   5183 H  HG23 . VAL B  1 120 ? -52.50200 -11.29300 8.56100   1.000 19.18358  ? 120 VAL B HG23 1 
ATOM   5184 N  N    . MET B  1 121 ? -49.28600 -14.89100 6.82400   1.000 16.87519  ? 121 MET B N    1 
ATOM   5185 C  CA   . MET B  1 121 ? -49.06200 -16.18100 6.19300   1.000 17.38635  ? 121 MET B CA   1 
ATOM   5186 C  C    . MET B  1 121 ? -48.75200 -17.22400 7.25600   1.000 18.04630  ? 121 MET B C    1 
ATOM   5187 O  O    . MET B  1 121 ? -47.76300 -17.09900 7.99000   1.000 17.42628  ? 121 MET B O    1 
ATOM   5188 C  CB   . MET B  1 121 ? -47.94700 -16.09900 5.14300   1.000 18.91066  ? 121 MET B CB   1 
ATOM   5189 C  CG   . MET B  1 121 ? -47.78300 -17.38200 4.37600   1.000 19.36201  ? 121 MET B CG   1 
ATOM   5190 S  SD   . MET B  1 121 ? -46.60200 -17.28100 2.98900   1.000 20.87223  ? 121 MET B SD   1 
ATOM   5191 C  CE   . MET B  1 121 ? -45.12400 -16.73700 3.82400   1.000 21.00091  ? 121 MET B CE   1 
ATOM   5192 H  H    . MET B  1 121 ? -48.60900 -14.57300 7.25000   1.000 20.25279  ? 121 MET B H    1 
ATOM   5193 H  HA   . MET B  1 121 ? -49.87500 -16.45200 5.73800   1.000 20.86618  ? 121 MET B HA   1 
ATOM   5194 H  HB2  . MET B  1 121 ? -48.15900 -15.39400 4.51100   1.000 22.69535  ? 121 MET B HB2  1 
ATOM   5195 H  HB3  . MET B  1 121 ? -47.10700 -15.90400 5.58800   1.000 22.69535  ? 121 MET B HB3  1 
ATOM   5196 H  HG2  . MET B  1 121 ? -47.46500 -18.06800 4.98300   1.000 23.23697  ? 121 MET B HG2  1 
ATOM   5197 H  HG3  . MET B  1 121 ? -48.64500 -17.63700 4.01000   1.000 23.23697  ? 121 MET B HG3  1 
ATOM   5198 H  HE1  . MET B  1 121 ? -44.37600 -16.78900 3.20800   1.000 25.20366  ? 121 MET B HE1  1 
ATOM   5199 H  HE2  . MET B  1 121 ? -45.24700 -15.82100 4.11800   1.000 25.20366  ? 121 MET B HE2  1 
ATOM   5200 H  HE3  . MET B  1 121 ? -44.96300 -17.31200 4.58800   1.000 25.20366  ? 121 MET B HE3  1 
ATOM   5201 N  N    . THR B  1 122 ? -49.56600 -18.28300 7.29900   1.000 17.83344  ? 122 THR B N    1 
ATOM   5202 C  CA   . THR B  1 122 ? -49.26100 -19.45800 8.11700   1.000 17.54390  ? 122 THR B CA   1 
ATOM   5203 C  C    . THR B  1 122 ? -48.37100 -20.36300 7.27500   1.000 19.37070  ? 122 THR B C    1 
ATOM   5204 O  O    . THR B  1 122 ? -48.69500 -20.63000 6.11500   1.000 21.15847  ? 122 THR B O    1 
ATOM   5205 C  CB   . THR B  1 122 ? -50.54600 -20.17000 8.51200   1.000 18.22431  ? 122 THR B CB   1 
ATOM   5206 O  OG1  . THR B  1 122 ? -51.31800 -20.51000 7.34700   1.000 21.34477  ? 122 THR B OG1  1 
ATOM   5207 C  CG2  . THR B  1 122 ? -51.42100 -19.27700 9.38700   1.000 19.34375  ? 122 THR B CG2  1 
ATOM   5208 H  H    . THR B  1 122 ? -50.30300 -18.34300 6.86200   1.000 21.40269  ? 122 THR B H    1 
ATOM   5209 H  HA   . THR B  1 122 ? -48.80300 -19.21900 8.93800   1.000 21.05524  ? 122 THR B HA   1 
ATOM   5210 H  HB   . THR B  1 122 ? -50.30100 -20.97100 9.00100   1.000 21.87173  ? 122 THR B HB   1 
ATOM   5211 H  HG1  . THR B  1 122 ? -50.88000 -21.03100 6.85500   1.000 25.61629  ? 122 THR B HG1  1 
ATOM   5212 H  HG21 . THR B  1 122 ? -52.22600 -19.75200 9.64400   1.000 23.21506  ? 122 THR B HG21 1 
ATOM   5213 H  HG22 . THR B  1 122 ? -50.93700 -19.02100 10.18800  1.000 23.21506  ? 122 THR B HG22 1 
ATOM   5214 H  HG23 . THR B  1 122 ? -51.66900 -18.47600 8.90000   1.000 23.21506  ? 122 THR B HG23 1 
ATOM   5215 N  N    . ILE B  1 123 ? -47.26100 -20.82200 7.83200   1.000 19.18870  ? 123 ILE B N    1 
ATOM   5216 C  CA   . ILE B  1 123 ? -46.30700 -21.56700 7.02300   1.000 20.05445  ? 123 ILE B CA   1 
ATOM   5217 C  C    . ILE B  1 123 ? -46.12500 -22.99500 7.49900   1.000 20.78455  ? 123 ILE B C    1 
ATOM   5218 O  O    . ILE B  1 123 ? -46.35300 -23.34400 8.65300   1.000 22.92151  ? 123 ILE B O    1 
ATOM   5219 C  CB   . ILE B  1 123 ? -44.91800 -20.89700 6.91000   1.000 19.61535  ? 123 ILE B CB   1 
ATOM   5220 C  CG1  . ILE B  1 123 ? -44.23700 -20.76900 8.27600   1.000 20.55401  ? 123 ILE B CG1  1 
ATOM   5221 C  CG2  . ILE B  1 123 ? -45.06500 -19.52900 6.23700   1.000 20.25120  ? 123 ILE B CG2  1 
ATOM   5222 C  CD1  . ILE B  1 123 ? -42.73200 -20.47900 8.11400   1.000 21.75899  ? 123 ILE B CD1  1 
ATOM   5223 H  H    . ILE B  1 123 ? -47.04200 -20.71800 8.65700   1.000 23.02901  ? 123 ILE B H    1 
ATOM   5224 H  HA   . ILE B  1 123 ? -46.71900 -21.60800 6.14600   1.000 24.06790  ? 123 ILE B HA   1 
ATOM   5225 H  HB   . ILE B  1 123 ? -44.34900 -21.46300 6.36600   1.000 23.54099  ? 123 ILE B HB   1 
ATOM   5226 H  HG12 . ILE B  1 123 ? -44.64000 -20.03900 8.77100   1.000 24.66737  ? 123 ILE B HG12 1 
ATOM   5227 H  HG13 . ILE B  1 123 ? -44.34000 -21.60000 8.76700   1.000 24.66737  ? 123 ILE B HG13 1 
ATOM   5228 H  HG21 . ILE B  1 123 ? -44.18300 -19.15800 6.08000   1.000 24.30400  ? 123 ILE B HG21 1 
ATOM   5229 H  HG22 . ILE B  1 123 ? -45.53200 -19.64000 5.39500   1.000 24.30400  ? 123 ILE B HG22 1 
ATOM   5230 H  HG23 . ILE B  1 123 ? -45.57100 -18.94300 6.82100   1.000 24.30400  ? 123 ILE B HG23 1 
ATOM   5231 H  HD11 . ILE B  1 123 ? -42.31100 -20.49600 8.98800   1.000 26.11335  ? 123 ILE B HD11 1 
ATOM   5232 H  HD12 . ILE B  1 123 ? -42.33900 -21.15900 7.54500   1.000 26.11335  ? 123 ILE B HD12 1 
ATOM   5233 H  HD13 . ILE B  1 123 ? -42.62100 -19.60400 7.71000   1.000 26.11335  ? 123 ILE B HD13 1 
ATOM   5234 N  N    . ASP B  1 124 ? -45.69500 -23.83300 6.56400   1.000 21.51505  ? 124 ASP B N    1 
ATOM   5235 C  CA   . ASP B  1 124 ? -45.01200 -25.07400 6.87900   1.000 22.28205  ? 124 ASP B CA   1 
ATOM   5236 C  C    . ASP B  1 124 ? -43.50700 -24.86600 6.77400   1.000 22.99923  ? 124 ASP B C    1 
ATOM   5237 O  O    . ASP B  1 124 ? -43.02500 -23.99900 6.03800   1.000 22.89022  ? 124 ASP B O    1 
ATOM   5238 C  CB   . ASP B  1 124 ? -45.42600 -26.15900 5.88900   1.000 23.28296  ? 124 ASP B CB   1 
ATOM   5239 C  CG   . ASP B  1 124 ? -46.78900 -26.72700 6.18900   1.000 27.56568  ? 124 ASP B CG   1 
ATOM   5240 O  OD1  . ASP B  1 124 ? -46.97400 -27.20800 7.31900   1.000 30.09321  ? 124 ASP B OD1  1 
ATOM   5241 O  OD2  . ASP B  1 124 ? -47.64500 -26.72900 5.28000   1.000 26.99930  ? 124 ASP B OD2  1 
ATOM   5242 H  H    . ASP B  1 124 ? -45.79000 -23.69900 5.72000   1.000 25.82062  ? 124 ASP B H    1 
ATOM   5243 H  HA   . ASP B  1 124 ? -45.23500 -25.35800 7.78000   1.000 26.74102  ? 124 ASP B HA   1 
ATOM   5244 H  HB2  . ASP B  1 124 ? -45.44800 -25.78100 4.99600   1.000 27.94211  ? 124 ASP B HB2  1 
ATOM   5245 H  HB3  . ASP B  1 124 ? -44.78300 -26.88400 5.92700   1.000 27.94211  ? 124 ASP B HB3  1 
ATOM   5246 N  N    . THR B  1 125 ? -42.76900 -25.66000 7.53200   1.000 22.91898  ? 125 THR B N    1 
ATOM   5247 C  CA   . THR B  1 125 ? -41.31900 -25.64800 7.43500   1.000 23.31519  ? 125 THR B CA   1 
ATOM   5248 C  C    . THR B  1 125 ? -40.87100 -26.62900 6.35800   1.000 23.90078  ? 125 THR B C    1 
ATOM   5249 O  O    . THR B  1 125 ? -41.65200 -27.44200 5.83900   1.000 25.91115  ? 125 THR B O    1 
ATOM   5250 C  CB   . THR B  1 125 ? -40.69300 -25.98200 8.78700   1.000 27.05966  ? 125 THR B CB   1 
ATOM   5251 O  OG1  . THR B  1 125 ? -41.25300 -27.18900 9.29700   1.000 24.84422  ? 125 THR B OG1  1 
ATOM   5252 C  CG2  . THR B  1 125 ? -40.92700 -24.83500 9.75500   1.000 23.92206  ? 125 THR B CG2  1 
ATOM   5253 H  H    . THR B  1 125 ? -43.08400 -26.21300 8.11000   1.000 27.50534  ? 125 THR B H    1 
ATOM   5254 H  HA   . THR B  1 125 ? -41.00800 -24.76300 7.18600   1.000 27.98079  ? 125 THR B HA   1 
ATOM   5255 H  HB   . THR B  1 125 ? -39.73600 -26.11100 8.69200   1.000 32.47415  ? 125 THR B HB   1 
ATOM   5256 H  HG1  . THR B  1 125 ? -41.09600 -27.82400 8.77000   1.000 29.81562  ? 125 THR B HG1  1 
ATOM   5257 H  HG21 . THR B  1 125 ? -40.53100 -25.04100 10.61600  1.000 28.70904  ? 125 THR B HG21 1 
ATOM   5258 H  HG22 . THR B  1 125 ? -40.52400 -24.02200 9.41000   1.000 28.70904  ? 125 THR B HG22 1 
ATOM   5259 H  HG23 . THR B  1 125 ? -41.87900 -24.68900 9.87200   1.000 28.70904  ? 125 THR B HG23 1 
ATOM   5260 N  N    . ASN B  1 126 ? -39.59300 -26.54700 6.01100   1.000 24.63931  ? 126 ASN B N    1 
ATOM   5261 C  CA   . ASN B  1 126 ? -39.04200 -27.47600 5.03100   1.000 27.68614  ? 126 ASN B CA   1 
ATOM   5262 C  C    . ASN B  1 126 ? -39.27500 -28.92600 5.44200   1.000 31.37412  ? 126 ASN B C    1 
ATOM   5263 O  O    . ASN B  1 126 ? -39.64300 -29.76600 4.61200   1.000 30.89060  ? 126 ASN B O    1 
ATOM   5264 C  CB   . ASN B  1 126 ? -37.55500 -27.21500 4.86000   1.000 28.71459  ? 126 ASN B CB   1 
ATOM   5265 C  CG   . ASN B  1 126 ? -37.26000 -25.89400 4.20100   1.000 28.32395  ? 126 ASN B CG   1 
ATOM   5266 O  OD1  . ASN B  1 126 ? -38.00500 -25.44100 3.33600   1.000 32.16851  ? 126 ASN B OD1  1 
ATOM   5267 N  ND2  . ASN B  1 126 ? -36.15600 -25.27100 4.58700   1.000 31.13960  ? 126 ASN B ND2  1 
ATOM   5268 H  H    . ASN B  1 126 ? -39.03200 -25.97500 6.32200   1.000 29.56974  ? 126 ASN B H    1 
ATOM   5269 H  HA   . ASN B  1 126 ? -39.48600 -27.32800 4.18100   1.000 33.22593  ? 126 ASN B HA   1 
ATOM   5270 H  HB2  . ASN B  1 126 ? -37.13300 -27.21400 5.73300   1.000 34.46007  ? 126 ASN B HB2  1 
ATOM   5271 H  HB3  . ASN B  1 126 ? -37.17400 -27.91500 4.30800   1.000 34.46007  ? 126 ASN B HB3  1 
ATOM   5272 H  HD21 . ASN B  1 126 ? -35.94600 -24.51300 4.23800   1.000 37.37009  ? 126 ASN B HD21 1 
ATOM   5273 H  HD22 . ASN B  1 126 ? -35.65000 -25.62400 5.18500   1.000 37.37009  ? 126 ASN B HD22 1 
ATOM   5274 N  N    . ARG B  1 127 ? -38.99100 -29.25600 6.70500   1.000 29.12541  ? 127 ARG B N    1 
ATOM   5275 C  CA   . ARG B  1 127 ? -39.33600 -30.54700 7.28600   1.000 32.05924  ? 127 ARG B CA   1 
ATOM   5276 C  C    . ARG B  1 127 ? -39.94200 -30.31700 8.66400   1.000 30.42452  ? 127 ARG B C    1 
ATOM   5277 O  O    . ARG B  1 127 ? -39.58100 -29.36600 9.36600   1.000 28.04358  ? 127 ARG B O    1 
ATOM   5278 C  CB   . ARG B  1 127 ? -38.12200 -31.45800 7.45300   1.000 31.42742  ? 127 ARG B CB   1 
ATOM   5279 C  CG   . ARG B  1 127 ? -37.37500 -31.71500 6.16700   1.000 37.83594  ? 127 ARG B CG   1 
ATOM   5280 C  CD   . ARG B  1 127 ? -36.46700 -32.90000 6.28600   1.000 56.54470  ? 127 ARG B CD   1 
ATOM   5281 N  NE   . ARG B  1 127 ? -35.87500 -33.18800 4.98800   1.000 63.42192  ? 127 ARG B NE   1 
ATOM   5282 C  CZ   . ARG B  1 127 ? -34.68700 -33.74500 4.80900   1.000 72.03886  ? 127 ARG B CZ   1 
ATOM   5283 N  NH1  . ARG B  1 127 ? -33.91900 -34.08200 5.83400   1.000 68.52831  ? 127 ARG B NH1  1 
ATOM   5284 N  NH2  . ARG B  1 127 ? -34.26000 -33.97100 3.57100   1.000 76.33807  ? 127 ARG B NH2  1 
ATOM   5285 H  H    . ARG B  1 127 ? -38.58900 -28.73200 7.25600   1.000 34.95305  ? 127 ARG B H    1 
ATOM   5286 H  HA   . ARG B  1 127 ? -39.97700 -30.98600 6.70500   1.000 38.47365  ? 127 ARG B HA   1 
ATOM   5287 H  HB2  . ARG B  1 127 ? -37.50400 -31.04500 8.07600   1.000 37.71546  ? 127 ARG B HB2  1 
ATOM   5288 H  HB3  . ARG B  1 127 ? -38.41900 -32.31400 7.79900   1.000 37.71546  ? 127 ARG B HB3  1 
ATOM   5289 H  HG2  . ARG B  1 127 ? -38.01200 -31.89000 5.45500   1.000 45.40569  ? 127 ARG B HG2  1 
ATOM   5290 H  HG3  . ARG B  1 127 ? -36.83700 -30.93900 5.94700   1.000 45.40569  ? 127 ARG B HG3  1 
ATOM   5291 H  HD2  . ARG B  1 127 ? -35.75800 -32.70800 6.91900   1.000 67.85621  ? 127 ARG B HD2  1 
ATOM   5292 H  HD3  . ARG B  1 127 ? -36.97300 -33.67400 6.57900   1.000 67.85621  ? 127 ARG B HD3  1 
ATOM   5293 H  HE   . ARG B  1 127 ? -36.32900 -32.98100 4.28700   1.000 76.10886  ? 127 ARG B HE   1 
ATOM   5294 H  HH11 . ARG B  1 127 ? -34.18900 -33.94000 6.63800   1.000 82.23653  ? 127 ARG B HH11 1 
ATOM   5295 H  HH12 . ARG B  1 127 ? -33.15100 -34.44200 5.69500   1.000 82.23653  ? 127 ARG B HH12 1 
ATOM   5296 H  HH21 . ARG B  1 127 ? -34.75300 -33.75700 2.90000   1.000 91.60825  ? 127 ARG B HH21 1 
ATOM   5297 H  HH22 . ARG B  1 127 ? -33.49000 -34.33300 3.44100   1.000 91.60825  ? 127 ARG B HH22 1 
ATOM   5298 N  N    . ILE B  1 128 ? -40.86900 -31.19200 9.05800   1.000 31.38606  ? 128 ILE B N    1 
ATOM   5299 C  CA   . ILE B  1 128 ? -41.52000 -30.99500 10.35000  1.000 28.93516  ? 128 ILE B CA   1 
ATOM   5300 C  C    . ILE B  1 128 ? -40.52400 -31.18700 11.48400  1.000 28.15889  ? 128 ILE B C    1 
ATOM   5301 O  O    . ILE B  1 128 ? -40.75900 -30.72800 12.60300  1.000 29.34030  ? 128 ILE B O    1 
ATOM   5302 C  CB   . ILE B  1 128 ? -42.77200 -31.87000 10.51800  1.000 28.53538  ? 128 ILE B CB   1 
ATOM   5303 C  CG1  . ILE B  1 128 ? -42.41800 -33.34900 10.42700  1.000 37.82466  ? 128 ILE B CG1  1 
ATOM   5304 C  CG2  . ILE B  1 128 ? -43.80400 -31.48900 9.46800   1.000 35.10393  ? 128 ILE B CG2  1 
ATOM   5305 C  CD1  . ILE B  1 128 ? -43.60300 -34.26700 10.61800  1.000 39.98720  ? 128 ILE B CD1  1 
ATOM   5306 H  H    . ILE B  1 128 ? -41.12800 -31.88000 8.61300   1.000 37.66584  ? 128 ILE B H    1 
ATOM   5307 H  HA   . ILE B  1 128 ? -41.84900 -30.08300 10.38600  1.000 34.72475  ? 128 ILE B HA   1 
ATOM   5308 H  HB   . ILE B  1 128 ? -43.14600 -31.71500 11.40000  1.000 34.24502  ? 128 ILE B HB   1 
ATOM   5309 H  HG12 . ILE B  1 128 ? -42.04200 -33.52700 9.55100   1.000 45.39215  ? 128 ILE B HG12 1 
ATOM   5310 H  HG13 . ILE B  1 128 ? -41.76700 -33.55800 11.11500  1.000 45.39215  ? 128 ILE B HG13 1 
ATOM   5311 H  HG21 . ILE B  1 128 ? -44.62900 -31.96800 9.64700   1.000 42.12727  ? 128 ILE B HG21 1 
ATOM   5312 H  HG22 . ILE B  1 128 ? -43.96100 -30.53300 9.51100   1.000 42.12727  ? 128 ILE B HG22 1 
ATOM   5313 H  HG23 . ILE B  1 128 ? -43.46600 -31.72900 8.59100   1.000 42.12727  ? 128 ILE B HG23 1 
ATOM   5314 H  HD11 . ILE B  1 128 ? -43.29000 -35.18500 10.65200  1.000 47.98721  ? 128 ILE B HD11 1 
ATOM   5315 H  HD12 . ILE B  1 128 ? -44.04900 -34.03900 11.44900  1.000 47.98721  ? 128 ILE B HD12 1 
ATOM   5316 H  HD13 . ILE B  1 128 ? -44.21400 -34.15300 9.87300   1.000 47.98721  ? 128 ILE B HD13 1 
ATOM   5317 N  N    . SER B  1 129 ? -39.39500 -31.82600 11.21500  1.000 29.27655  ? 129 SER B N    1 
ATOM   5318 C  CA   . SER B  1 129 ? -38.37600 -32.06100 12.22100  1.000 28.27111  ? 129 SER B CA   1 
ATOM   5319 C  C    . SER B  1 129 ? -37.41200 -30.88900 12.40300  1.000 27.80708  ? 129 SER B C    1 
ATOM   5320 O  O    . SER B  1 129 ? -36.52000 -30.98400 13.23700  1.000 29.87728  ? 129 SER B O    1 
ATOM   5321 C  CB   . SER B  1 129 ? -37.59200 -33.32800 11.89400  1.000 30.32354  ? 129 SER B CB   1 
ATOM   5322 O  OG   . SER B  1 129 ? -37.04000 -33.26800 10.58800  1.000 33.43868  ? 129 SER B OG   1 
ATOM   5323 H  H    . SER B  1 129 ? -39.19400 -32.13900 10.44000  1.000 35.13443  ? 129 SER B H    1 
ATOM   5324 H  HA   . SER B  1 129 ? -38.82100 -32.19900 13.07200  1.000 33.92789  ? 129 SER B HA   1 
ATOM   5325 H  HB2  . SER B  1 129 ? -36.87100 -33.42600 12.53600  1.000 36.39081  ? 129 SER B HB2  1 
ATOM   5326 H  HB3  . SER B  1 129 ? -38.19000 -34.09000 11.94800  1.000 36.39081  ? 129 SER B HB3  1 
ATOM   5327 H  HG   . SER B  1 129 ? -36.49000 -32.63500 10.53700  1.000 40.12898  ? 129 SER B HG   1 
ATOM   5328 N  N    . ASP B  1 130 ? -37.58400 -29.77900 11.68000  1.000 24.75460  ? 130 ASP B N    1 
ATOM   5329 C  CA   . ASP B  1 130 ? -36.62700 -28.67800 11.78500  1.000 25.50946  ? 130 ASP B CA   1 
ATOM   5330 C  C    . ASP B  1 130 ? -36.60100 -28.09500 13.20500  1.000 23.58859  ? 130 ASP B C    1 
ATOM   5331 O  O    . ASP B  1 130 ? -37.62000 -28.04400 13.90100  1.000 25.75948  ? 130 ASP B O    1 
ATOM   5332 C  CB   . ASP B  1 130 ? -36.95200 -27.57800 10.77500  1.000 26.95406  ? 130 ASP B CB   1 
ATOM   5333 C  CG   . ASP B  1 130 ? -36.75400 -28.01600 9.33300   1.000 28.15900  ? 130 ASP B CG   1 
ATOM   5334 O  OD1  . ASP B  1 130 ? -36.00200 -28.99700 9.09700   1.000 29.78975  ? 130 ASP B OD1  1 
ATOM   5335 O  OD2  . ASP B  1 130 ? -37.36600 -27.38400 8.43300   1.000 27.31270  ? 130 ASP B OD2  1 
ATOM   5336 H  H    . ASP B  1 130 ? -38.23400 -29.64200 11.13400  1.000 29.70809  ? 130 ASP B H    1 
ATOM   5337 H  HA   . ASP B  1 130 ? -35.74100 -29.01900 11.58500  1.000 30.61392  ? 130 ASP B HA   1 
ATOM   5338 H  HB2  . ASP B  1 130 ? -37.88000 -27.31500 10.88300  1.000 32.34744  ? 130 ASP B HB2  1 
ATOM   5339 H  HB3  . ASP B  1 130 ? -36.37100 -26.81800 10.93900  1.000 32.34744  ? 130 ASP B HB3  1 
ATOM   5340 N  N    . GLN B  1 131 ? -35.41600 -27.67300 13.62900  1.000 25.06309  ? 131 GLN B N    1 
ATOM   5341 C  CA   . GLN B  1 131 ? -35.13000 -27.14900 14.96200  1.000 24.22696  ? 131 GLN B CA   1 
ATOM   5342 C  C    . GLN B  1 131 ? -35.18400 -25.62900 14.97700  1.000 23.13361  ? 131 GLN B C    1 
ATOM   5343 O  O    . GLN B  1 131 ? -35.32400 -24.99100 13.92700  1.000 23.54887  ? 131 GLN B O    1 
ATOM   5344 C  CB   . GLN B  1 131 ? -33.76000 -27.63700 15.40500  1.000 25.10740  ? 131 GLN B CB   1 
ATOM   5345 C  CG   . GLN B  1 131 ? -33.64800 -29.15600 15.45600  1.000 32.22637  ? 131 GLN B CG   1 
ATOM   5346 C  CD   . GLN B  1 131 ? -34.54400 -29.77300 16.50400  1.000 43.01307  ? 131 GLN B CD   1 
ATOM   5347 O  OE1  . GLN B  1 131 ? -34.38500 -29.53000 17.70300  1.000 38.98440  ? 131 GLN B OE1  1 
ATOM   5348 N  NE2  . GLN B  1 131 ? -35.52400 -30.55400 16.05600  1.000 46.61578  ? 131 GLN B NE2  1 
ATOM   5349 H  H    . GLN B  1 131 ? -34.71600 -27.68100 13.13000  1.000 30.07827  ? 131 GLN B H    1 
ATOM   5350 H  HA   . GLN B  1 131 ? -35.79700 -27.47000 15.58900  1.000 29.07491  ? 131 GLN B HA   1 
ATOM   5351 H  HB2  . GLN B  1 131 ? -33.09400 -27.31000 14.78000  1.000 30.13144  ? 131 GLN B HB2  1 
ATOM   5352 H  HB3  . GLN B  1 131 ? -33.57800 -27.29400 16.29400  1.000 30.13144  ? 131 GLN B HB3  1 
ATOM   5353 H  HG2  . GLN B  1 131 ? -33.90000 -29.52100 14.59400  1.000 38.67421  ? 131 GLN B HG2  1 
ATOM   5354 H  HG3  . GLN B  1 131 ? -32.73200 -29.39900 15.66400  1.000 38.67421  ? 131 GLN B HG3  1 
ATOM   5355 H  HE21 . GLN B  1 131 ? -35.61900 -30.68200 15.21100  1.000 55.94150  ? 131 GLN B HE21 1 
ATOM   5356 H  HE22 . GLN B  1 131 ? -36.06300 -30.92900 16.61100  1.000 55.94150  ? 131 GLN B HE22 1 
ATOM   5357 N  N    . PRO B  1 132 ? -35.15000 -25.00100 16.16000  1.000 22.42606  ? 132 PRO B N    1 
ATOM   5358 C  CA   . PRO B  1 132 ? -35.42900 -23.55300 16.22800  1.000 22.03992  ? 132 PRO B CA   1 
ATOM   5359 C  C    . PRO B  1 132 ? -34.50500 -22.68400 15.37900  1.000 19.94936  ? 132 PRO B C    1 
ATOM   5360 O  O    . PRO B  1 132 ? -34.98600 -21.69700 14.80500  1.000 21.38841  ? 132 PRO B O    1 
ATOM   5361 C  CB   . PRO B  1 132 ? -35.33100 -23.22900 17.73400  1.000 21.07128  ? 132 PRO B CB   1 
ATOM   5362 C  CG   . PRO B  1 132 ? -35.75400 -24.50700 18.39900  1.000 21.75303  ? 132 PRO B CG   1 
ATOM   5363 C  CD   . PRO B  1 132 ? -35.17800 -25.62200 17.51300  1.000 21.93920  ? 132 PRO B CD   1 
ATOM   5364 H  HA   . PRO B  1 132 ? -36.33300 -23.39600 15.91300  1.000 26.45047  ? 132 PRO B HA   1 
ATOM   5365 H  HB2  . PRO B  1 132 ? -34.42000 -22.99400 17.96800  1.000 25.28810  ? 132 PRO B HB2  1 
ATOM   5366 H  HB3  . PRO B  1 132 ? -35.93000 -22.50000 17.96000  1.000 25.28810  ? 132 PRO B HB3  1 
ATOM   5367 H  HG2  . PRO B  1 132 ? -35.38600 -24.55100 19.29500  1.000 26.10620  ? 132 PRO B HG2  1 
ATOM   5368 H  HG3  . PRO B  1 132 ? -36.72200 -24.55700 18.43500  1.000 26.10620  ? 132 PRO B HG3  1 
ATOM   5369 H  HD2  . PRO B  1 132 ? -34.28400 -25.86600 17.80100  1.000 26.32961  ? 132 PRO B HD2  1 
ATOM   5370 H  HD3  . PRO B  1 132 ? -35.75400 -26.40300 17.52300  1.000 26.32961  ? 132 PRO B HD3  1 
ATOM   5371 N  N    . PRO B  1 133 ? -33.19700 -22.96400 15.26900  1.000 22.35362  ? 133 PRO B N    1 
ATOM   5372 C  CA   . PRO B  1 133 ? -32.35900 -22.10500 14.38800  1.000 19.89685  ? 133 PRO B CA   1 
ATOM   5373 C  C    . PRO B  1 133 ? -32.81100 -22.11500 12.93200  1.000 20.72273  ? 133 PRO B C    1 
ATOM   5374 O  O    . PRO B  1 133 ? -32.96300 -21.05600 12.30300  1.000 23.72883  ? 133 PRO B O    1 
ATOM   5375 C  CB   . PRO B  1 133 ? -30.93000 -22.63000 14.59700  1.000 23.70599  ? 133 PRO B CB   1 
ATOM   5376 C  CG   . PRO B  1 133 ? -30.96100 -23.30600 15.92200  1.000 22.59742  ? 133 PRO B CG   1 
ATOM   5377 C  CD   . PRO B  1 133 ? -32.38000 -23.92400 16.00200  1.000 23.42469  ? 133 PRO B CD   1 
ATOM   5378 H  HA   . PRO B  1 133 ? -32.38200 -21.19100 14.71300  1.000 23.87878  ? 133 PRO B HA   1 
ATOM   5379 H  HB2  . PRO B  1 133 ? -30.70100 -23.25700 13.89200  1.000 28.44975  ? 133 PRO B HB2  1 
ATOM   5380 H  HB3  . PRO B  1 133 ? -30.30300 -21.89000 14.59900  1.000 28.44975  ? 133 PRO B HB3  1 
ATOM   5381 H  HG2  . PRO B  1 133 ? -30.27800 -23.99400 15.96200  1.000 27.11946  ? 133 PRO B HG2  1 
ATOM   5382 H  HG3  . PRO B  1 133 ? -30.82200 -22.65900 16.63000  1.000 27.11946  ? 133 PRO B HG3  1 
ATOM   5383 H  HD2  . PRO B  1 133 ? -32.40300 -24.79500 15.57600  1.000 28.11219  ? 133 PRO B HD2  1 
ATOM   5384 H  HD3  . PRO B  1 133 ? -32.67400 -23.99700 16.92300  1.000 28.11219  ? 133 PRO B HD3  1 
ATOM   5385 N  N    . SER B  1 134 ? -33.07000 -23.30600 12.38700  1.000 22.70525  ? 134 SER B N    1 
ATOM   5386 C  CA   . SER B  1 134 ? -33.61900 -23.39700 11.03300  1.000 23.68865  ? 134 SER B CA   1 
ATOM   5387 C  C    . SER B  1 134 ? -34.97700 -22.70600 10.92700  1.000 20.97380  ? 134 SER B C    1 
ATOM   5388 O  O    . SER B  1 134 ? -35.27900 -22.02700 9.93200   1.000 22.64385  ? 134 SER B O    1 
ATOM   5389 C  CB   . SER B  1 134 ? -33.76600 -24.86600 10.66400  1.000 24.40023  ? 134 SER B CB   1 
ATOM   5390 O  OG   . SER B  1 134 ? -34.34000 -25.01100 9.38100   1.000 27.81206  ? 134 SER B OG   1 
ATOM   5391 H  H    . SER B  1 134 ? -32.93900 -24.06300 12.77300  1.000 27.24886  ? 134 SER B H    1 
ATOM   5392 H  HA   . SER B  1 134 ? -33.01200 -22.96000 10.41500  1.000 28.42894  ? 134 SER B HA   1 
ATOM   5393 H  HB2  . SER B  1 134 ? -32.88900 -25.28000 10.66500  1.000 29.28283  ? 134 SER B HB2  1 
ATOM   5394 H  HB3  . SER B  1 134 ? -34.33800 -25.29900 11.31600  1.000 29.28283  ? 134 SER B HB3  1 
ATOM   5395 H  HG   . SER B  1 134 ? -34.50800 -25.82100 9.23200   1.000 33.37703  ? 134 SER B HG   1 
ATOM   5396 N  N    . ARG B  1 135 ? -35.81200 -22.84500 11.94400  1.000 20.73932  ? 135 ARG B N    1 
ATOM   5397 C  CA   . ARG B  1 135 ? -37.14700 -22.19100 11.97300  1.000 20.26957  ? 135 ARG B CA   1 
ATOM   5398 C  C    . ARG B  1 135 ? -36.94700 -20.67600 11.90200  1.000 19.90191  ? 135 ARG B C    1 
ATOM   5399 O  O    . ARG B  1 135 ? -37.66100 -20.03800 11.17800  1.000 20.41504  ? 135 ARG B O    1 
ATOM   5400 C  CB   . ARG B  1 135 ? -37.93000 -22.65500 13.19600  1.000 20.04991  ? 135 ARG B CB   1 
ATOM   5401 C  CG   . ARG B  1 135 ? -38.46900 -24.06700 13.06300  1.000 19.56233  ? 135 ARG B CG   1 
ATOM   5402 C  CD   . ARG B  1 135 ? -39.32200 -24.55900 14.21600  1.000 20.55531  ? 135 ARG B CD   1 
ATOM   5403 N  NE   . ARG B  1 135 ? -39.45600 -25.97900 14.04000  1.000 23.55472  ? 135 ARG B NE   1 
ATOM   5404 C  CZ   . ARG B  1 135 ? -40.48300 -26.59400 13.49400  1.000 22.87302  ? 135 ARG B CZ   1 
ATOM   5405 N  NH1  . ARG B  1 135 ? -41.58000 -25.94600 13.16700  1.000 21.89015  ? 135 ARG B NH1  1 
ATOM   5406 N  NH2  . ARG B  1 135 ? -40.42500 -27.88900 13.27700  1.000 24.87481  ? 135 ARG B NH2  1 
ATOM   5407 H  H    . ARG B  1 135 ? -35.62100 -23.34500 12.68200  1.000 24.88974  ? 135 ARG B H    1 
ATOM   5408 H  HA   . ARG B  1 135 ? -37.63800 -22.47400 11.16700  1.000 24.32604  ? 135 ARG B HA   1 
ATOM   5409 H  HB2  . ARG B  1 135 ? -37.34400 -22.61100 13.98000  1.000 24.06246  ? 135 ARG B HB2  1 
ATOM   5410 H  HB3  . ARG B  1 135 ? -38.67900 -22.04000 13.34200  1.000 24.06246  ? 135 ARG B HB3  1 
ATOM   5411 H  HG2  . ARG B  1 135 ? -39.00300 -24.12100 12.24100  1.000 23.47736  ? 135 ARG B HG2  1 
ATOM   5412 H  HG3  . ARG B  1 135 ? -37.71200 -24.68100 12.95800  1.000 23.47736  ? 135 ARG B HG3  1 
ATOM   5413 H  HD2  . ARG B  1 135 ? -38.88600 -24.36100 15.07200  1.000 24.66894  ? 135 ARG B HD2  1 
ATOM   5414 H  HD3  . ARG B  1 135 ? -40.20300 -24.12900 14.19700  1.000 24.66894  ? 135 ARG B HD3  1 
ATOM   5415 H  HE   . ARG B  1 135 ? -38.76700 -26.44200 14.19200  1.000 28.26822  ? 135 ARG B HE   1 
ATOM   5416 H  HH11 . ARG B  1 135 ? -41.62200 -25.07500 13.27500  1.000 26.27074  ? 135 ARG B HH11 1 
ATOM   5417 H  HH12 . ARG B  1 135 ? -42.25700 -26.38200 12.81600  1.000 26.27074  ? 135 ARG B HH12 1 
ATOM   5418 H  HH21 . ARG B  1 135 ? -39.70600 -28.34100 13.51000  1.000 29.85233  ? 135 ARG B HH21 1 
ATOM   5419 H  HH22 . ARG B  1 135 ? -41.12800 -28.31000 12.95400  1.000 29.85233  ? 135 ARG B HH22 1 
ATOM   5420 N  N    . ARG B  1 136 ? -35.97700 -20.12500 12.61000  1.000 21.19531  ? 136 ARG B N    1 
ATOM   5421 C  CA   . ARG B  1 136 ? -35.70100 -18.69000 12.51500  1.000 18.89668  ? 136 ARG B CA   1 
ATOM   5422 C  C    . ARG B  1 136 ? -35.39500 -18.28500 11.07800  1.000 19.95189  ? 136 ARG B C    1 
ATOM   5423 O  O    . ARG B  1 136 ? -35.95300 -17.30400 10.56900  1.000 19.91646  ? 136 ARG B O    1 
ATOM   5424 C  CB   . ARG B  1 136 ? -34.52800 -18.35200 13.43500  1.000 21.21648  ? 136 ARG B CB   1 
ATOM   5425 C  CG   . ARG B  1 136 ? -33.96000 -16.94800 13.25200  1.000 20.10535  ? 136 ARG B CG   1 
ATOM   5426 C  CD   . ARG B  1 136 ? -32.47400 -17.03100 12.83400  1.000 27.11891  ? 136 ARG B CD   1 
ATOM   5427 N  NE   . ARG B  1 136 ? -31.91600 -15.71200 12.55100  1.000 25.96000  ? 136 ARG B NE   1 
ATOM   5428 C  CZ   . ARG B  1 136 ? -31.95700 -15.12600 11.36100  1.000 28.11609  ? 136 ARG B CZ   1 
ATOM   5429 N  NH1  . ARG B  1 136 ? -32.38500 -15.77300 10.28700  1.000 30.27379  ? 136 ARG B NH1  1 
ATOM   5430 N  NH2  . ARG B  1 136 ? -31.56200 -13.86200 11.24700  1.000 33.03822  ? 136 ARG B NH2  1 
ATOM   5431 H  H    . ARG B  1 136 ? -35.46900 -20.55500 13.15400  1.000 25.43694  ? 136 ARG B H    1 
ATOM   5432 H  HA   . ARG B  1 136 ? -36.47800 -18.18600 12.80300  1.000 22.67858  ? 136 ARG B HA   1 
ATOM   5433 H  HB2  . ARG B  1 136 ? -34.82500 -18.43000 14.35500  1.000 25.46234  ? 136 ARG B HB2  1 
ATOM   5434 H  HB3  . ARG B  1 136 ? -33.81000 -18.98200 13.26400  1.000 25.46234  ? 136 ARG B HB3  1 
ATOM   5435 H  HG2  . ARG B  1 136 ? -34.45400 -16.48300 12.55800  1.000 24.12898  ? 136 ARG B HG2  1 
ATOM   5436 H  HG3  . ARG B  1 136 ? -34.02200 -16.45800 14.08800  1.000 24.12898  ? 136 ARG B HG3  1 
ATOM   5437 H  HD2  . ARG B  1 136 ? -31.96100 -17.43000 13.55400  1.000 32.54525  ? 136 ARG B HD2  1 
ATOM   5438 H  HD3  . ARG B  1 136 ? -32.39700 -17.57200 12.03200  1.000 32.54525  ? 136 ARG B HD3  1 
ATOM   5439 H  HE   . ARG B  1 136 ? -31.53700 -15.28800 13.19600  1.000 31.15457  ? 136 ARG B HE   1 
ATOM   5440 H  HH11 . ARG B  1 136 ? -32.64300 -16.59100 10.35200  1.000 36.33112  ? 136 ARG B HH11 1 
ATOM   5441 H  HH12 . ARG B  1 136 ? -32.40400 -15.37600 9.52500   1.000 36.33112  ? 136 ARG B HH12 1 
ATOM   5442 H  HH21 . ARG B  1 136 ? -31.28400 -13.43400 11.93900  1.000 39.64842  ? 136 ARG B HH21 1 
ATOM   5443 H  HH22 . ARG B  1 136 ? -31.58400 -13.47200 10.48100  1.000 39.64842  ? 136 ARG B HH22 1 
ATOM   5444 N  N    . ASP B  1 137 ? -34.56300 -19.06700 10.39300  1.000 22.07653  ? 137 ASP B N    1 
ATOM   5445 C  CA   . ASP B  1 137 ? -34.22400 -18.75400 9.00100   1.000 21.16837  ? 137 ASP B CA   1 
ATOM   5446 C  C    . ASP B  1 137 ? -35.44600 -18.81800 8.11200   1.000 20.95930  ? 137 ASP B C    1 
ATOM   5447 O  O    . ASP B  1 137 ? -35.60500 -17.99500 7.20200   1.000 21.50620  ? 137 ASP B O    1 
ATOM   5448 C  CB   . ASP B  1 137 ? -33.19900 -19.74700 8.47000   1.000 22.56425  ? 137 ASP B CB   1 
ATOM   5449 C  CG   . ASP B  1 137 ? -31.85500 -19.64500 9.16300   1.000 30.90858  ? 137 ASP B CG   1 
ATOM   5450 O  OD1  . ASP B  1 137 ? -31.59000 -18.61700 9.80200   1.000 26.67837  ? 137 ASP B OD1  1 
ATOM   5451 O  OD2  . ASP B  1 137 ? -31.06300 -20.60200 9.03200   1.000 32.86015  ? 137 ASP B OD2  1 
ATOM   5452 H  H    . ASP B  1 137 ? -34.18500 -19.77400 10.70300  1.000 26.49440  ? 137 ASP B H    1 
ATOM   5453 H  HA   . ASP B  1 137 ? -33.85000 -17.86000 8.98100   1.000 25.40461  ? 137 ASP B HA   1 
ATOM   5454 H  HB2  . ASP B  1 137 ? -33.53500 -20.64800 8.60400   1.000 27.07966  ? 137 ASP B HB2  1 
ATOM   5455 H  HB3  . ASP B  1 137 ? -33.06000 -19.58100 7.52500   1.000 27.07966  ? 137 ASP B HB3  1 
ATOM   5456 N  N    . GLN B  1 138 ? -36.33100 -19.77000 8.38100   1.000 20.94623  ? 138 GLN B N    1 
ATOM   5457 C  CA   . GLN B  1 138 ? -37.51700 -19.94000 7.55000   1.000 20.68437  ? 138 GLN B CA   1 
ATOM   5458 C  C    . GLN B  1 138 ? -38.53500 -18.83300 7.78100   1.000 19.92868  ? 138 GLN B C    1 
ATOM   5459 O  O    . GLN B  1 138 ? -39.22000 -18.40900 6.84100   1.000 21.77601  ? 138 GLN B O    1 
ATOM   5460 C  CB   . GLN B  1 138 ? -38.09600 -21.32600 7.75700   1.000 21.30529  ? 138 GLN B CB   1 
ATOM   5461 C  CG   . GLN B  1 138 ? -37.12400 -22.41300 7.27900   1.000 22.48500  ? 138 GLN B CG   1 
ATOM   5462 C  CD   . GLN B  1 138 ? -37.67400 -23.80500 7.44500   1.000 27.32940  ? 138 GLN B CD   1 
ATOM   5463 O  OE1  . GLN B  1 138 ? -38.69800 -24.15400 6.86300   1.000 24.88922  ? 138 GLN B OE1  1 
ATOM   5464 N  NE2  . GLN B  1 138 ? -37.00000 -24.61400 8.25300   1.000 26.26523  ? 138 GLN B NE2  1 
ATOM   5465 H  H    . GLN B  1 138 ? -36.27100 -20.32800 9.03300   1.000 25.13804  ? 138 GLN B H    1 
ATOM   5466 H  HA   . GLN B  1 138 ? -37.26700 -19.87800 6.61500   1.000 24.82381  ? 138 GLN B HA   1 
ATOM   5467 H  HB2  . GLN B  1 138 ? -38.27000 -21.46400 8.70100   1.000 25.56891  ? 138 GLN B HB2  1 
ATOM   5468 H  HB3  . GLN B  1 138 ? -38.92100 -21.40900 7.25200   1.000 25.56891  ? 138 GLN B HB3  1 
ATOM   5469 H  HG2  . GLN B  1 138 ? -36.93500 -22.27500 6.33800   1.000 26.98456  ? 138 GLN B HG2  1 
ATOM   5470 H  HG3  . GLN B  1 138 ? -36.30400 -22.35100 7.79400   1.000 26.98456  ? 138 GLN B HG3  1 
ATOM   5471 H  HE21 . GLN B  1 138 ? -36.29000 -24.33300 8.64800   1.000 31.52083  ? 138 GLN B HE21 1 
ATOM   5472 H  HE22 . GLN B  1 138 ? -37.27400 -25.41900 8.38100   1.000 31.52083  ? 138 GLN B HE22 1 
ATOM   5473 N  N    . ILE B  1 139 ? -38.67600 -18.34400 9.01200   1.000 19.39176  ? 139 ILE B N    1 
ATOM   5474 C  CA   . ILE B  1 139 ? -39.51800 -17.18500 9.24600   1.000 18.96109  ? 139 ILE B CA   1 
ATOM   5475 C  C    . ILE B  1 139 ? -39.00900 -15.99800 8.44500   1.000 19.10668  ? 139 ILE B C    1 
ATOM   5476 O  O    . ILE B  1 139 ? -39.78800 -15.26300 7.80800   1.000 19.47830  ? 139 ILE B O    1 
ATOM   5477 C  CB   . ILE B  1 139 ? -39.59900 -16.84400 10.74900  1.000 18.53999  ? 139 ILE B CB   1 
ATOM   5478 C  CG1  . ILE B  1 139 ? -40.18000 -17.98000 11.58100  1.000 18.55433  ? 139 ILE B CG1  1 
ATOM   5479 C  CG2  . ILE B  1 139 ? -40.42800 -15.58100 10.95400  1.000 18.99076  ? 139 ILE B CG2  1 
ATOM   5480 C  CD1  . ILE B  1 139 ? -39.85600 -17.88700 13.07800  1.000 18.66411  ? 139 ILE B CD1  1 
ATOM   5481 H  H    . ILE B  1 139 ? -38.29900 -18.66300 9.71600   1.000 23.27268  ? 139 ILE B H    1 
ATOM   5482 H  HA   . ILE B  1 139 ? -40.41400 -17.40400 8.94500   1.000 22.75587  ? 139 ILE B HA   1 
ATOM   5483 H  HB   . ILE B  1 139 ? -38.68900 -16.70200 11.05200  1.000 22.25055  ? 139 ILE B HB   1 
ATOM   5484 H  HG12 . ILE B  1 139 ? -41.14600 -17.97100 11.48700  1.000 22.26776  ? 139 ILE B HG12 1 
ATOM   5485 H  HG13 . ILE B  1 139 ? -39.82300 -18.82000 11.25300  1.000 22.26776  ? 139 ILE B HG13 1 
ATOM   5486 H  HG21 . ILE B  1 139 ? -40.57000 -15.44700 11.90500  1.000 22.79148  ? 139 ILE B HG21 1 
ATOM   5487 H  HG22 . ILE B  1 139 ? -39.94700 -14.82400 10.58300  1.000 22.79148  ? 139 ILE B HG22 1 
ATOM   5488 H  HG23 . ILE B  1 139 ? -41.28000 -15.68500 10.50300  1.000 22.79148  ? 139 ILE B HG23 1 
ATOM   5489 H  HD11 . ILE B  1 139 ? -40.09200 -18.72600 13.50500  1.000 22.39949  ? 139 ILE B HD11 1 
ATOM   5490 H  HD12 . ILE B  1 139 ? -38.90700 -17.71800 13.18600  1.000 22.39949  ? 139 ILE B HD12 1 
ATOM   5491 H  HD13 . ILE B  1 139 ? -40.36800 -17.16200 13.46800  1.000 22.39949  ? 139 ILE B HD13 1 
ATOM   5492 N  N    . GLU B  1 140 ? -37.69700 -15.77300 8.50200   1.000 20.12712  ? 140 GLU B N    1 
ATOM   5493 C  CA   . GLU B  1 140 ? -37.08700 -14.65900 7.79200   1.000 19.20335  ? 140 GLU B CA   1 
ATOM   5494 C  C    . GLU B  1 140 ? -37.34600 -14.78300 6.29800   1.000 20.61396  ? 140 GLU B C    1 
ATOM   5495 O  O    . GLU B  1 140 ? -37.72800 -13.81400 5.64100   1.000 21.17562  ? 140 GLU B O    1 
ATOM   5496 C  CB   . GLU B  1 140 ? -35.60200 -14.62800 8.09100   1.000 23.60608  ? 140 GLU B CB   1 
ATOM   5497 C  CG   . GLU B  1 140 ? -34.82800 -13.53400 7.40400   1.000 24.76088  ? 140 GLU B CG   1 
ATOM   5498 C  CD   . GLU B  1 140 ? -33.34400 -13.55200 7.79500   1.000 31.51359  ? 140 GLU B CD   1 
ATOM   5499 O  OE1  . GLU B  1 140 ? -32.72800 -14.62400 7.68500   1.000 34.91194  ? 140 GLU B OE1  1 
ATOM   5500 O  OE2  . GLU B  1 140 ? -32.83700 -12.50600 8.22900   1.000 45.21654  ? 140 GLU B OE2  1 
ATOM   5501 H  H    . GLU B  1 140 ? -37.13900 -16.25300 8.94500   1.000 24.15511  ? 140 GLU B H    1 
ATOM   5502 H  HA   . GLU B  1 140 ? -37.46900 -13.82100 8.09600   1.000 23.04658  ? 140 GLU B HA   1 
ATOM   5503 H  HB2  . GLU B  1 140 ? -35.48600 -14.50800 9.04700   1.000 28.32985  ? 140 GLU B HB2  1 
ATOM   5504 H  HB3  . GLU B  1 140 ? -35.21700 -15.47300 7.81300   1.000 28.32985  ? 140 GLU B HB3  1 
ATOM   5505 H  HG2  . GLU B  1 140 ? -34.89100 -13.65300 6.44300   1.000 29.71562  ? 140 GLU B HG2  1 
ATOM   5506 H  HG3  . GLU B  1 140 ? -35.19800 -12.67300 7.65600   1.000 29.71562  ? 140 GLU B HG3  1 
ATOM   5507 N  N    . ALA B  1 141 ? -37.13600 -15.98200 5.74700   1.000 21.23099  ? 141 ALA B N    1 
ATOM   5508 C  CA   . ALA B  1 141 ? -37.36900 -16.19800 4.31800   1.000 21.18622  ? 141 ALA B CA   1 
ATOM   5509 C  C    . ALA B  1 141 ? -38.83500 -15.97800 3.95400   1.000 20.02382  ? 141 ALA B C    1 
ATOM   5510 O  O    . ALA B  1 141 ? -39.14600 -15.43100 2.88300   1.000 21.85120  ? 141 ALA B O    1 
ATOM   5511 C  CB   . ALA B  1 141 ? -36.94400 -17.60700 3.93700   1.000 23.07123  ? 141 ALA B CB   1 
ATOM   5512 H  H    . ALA B  1 141 ? -36.86300 -16.67800 6.17300   1.000 25.47975  ? 141 ALA B H    1 
ATOM   5513 H  HA   . ALA B  1 141 ? -36.83400 -15.56400 3.81600   1.000 25.42603  ? 141 ALA B HA   1 
ATOM   5514 H  HB1  . ALA B  1 141 ? -37.12200 -17.74600 2.99300   1.000 27.68803  ? 141 ALA B HB1  1 
ATOM   5515 H  HB2  . ALA B  1 141 ? -35.99600 -17.71000 4.11400   1.000 27.68803  ? 141 ALA B HB2  1 
ATOM   5516 H  HB3  . ALA B  1 141 ? -37.45000 -18.24400 4.46500   1.000 27.68803  ? 141 ALA B HB3  1 
ATOM   5517 N  N    . ALA B  1 142 ? -39.76100 -16.42200 4.80900   1.000 19.38336  ? 142 ALA B N    1 
ATOM   5518 C  CA   . ALA B  1 142 ? -41.18200 -16.23400 4.53700   1.000 20.38128  ? 142 ALA B CA   1 
ATOM   5519 C  C    . ALA B  1 142 ? -41.57700 -14.76200 4.57500   1.000 19.13371  ? 142 ALA B C    1 
ATOM   5520 O  O    . ALA B  1 142 ? -42.39700 -14.30900 3.75800   1.000 20.07612  ? 142 ALA B O    1 
ATOM   5521 C  CB   . ALA B  1 142 ? -41.99500 -17.07500 5.51300   1.000 20.60953  ? 142 ALA B CB   1 
ATOM   5522 H  H    . ALA B  1 142 ? -39.59200 -16.83100 5.54700   1.000 23.26259  ? 142 ALA B H    1 
ATOM   5523 H  HA   . ALA B  1 142 ? -41.38500 -16.54400 3.64000   1.000 24.46010  ? 142 ALA B HA   1 
ATOM   5524 H  HB1  . ALA B  1 142 ? -42.93900 -16.90400 5.36700   1.000 24.73400  ? 142 ALA B HB1  1 
ATOM   5525 H  HB2  . ALA B  1 142 ? -41.80200 -18.01300 5.35900   1.000 24.73400  ? 142 ALA B HB2  1 
ATOM   5526 H  HB3  . ALA B  1 142 ? -41.75100 -16.83200 6.41900   1.000 24.73400  ? 142 ALA B HB3  1 
ATOM   5527 N  N    . LEU B  1 143 ? -41.01900 -13.98900 5.49500   1.000 19.12224  ? 143 LEU B N    1 
ATOM   5528 C  CA   . LEU B  1 143 ? -41.30100 -12.55800 5.50100   1.000 19.70115  ? 143 LEU B CA   1 
ATOM   5529 C  C    . LEU B  1 143 ? -40.72700 -11.88800 4.25700   1.000 19.06197  ? 143 LEU B C    1 
ATOM   5530 O  O    . LEU B  1 143 ? -41.39500 -11.02800 3.65800   1.000 21.18777  ? 143 LEU B O    1 
ATOM   5531 C  CB   . LEU B  1 143 ? -40.74500 -11.91600 6.78100   1.000 21.15261  ? 143 LEU B CB   1 
ATOM   5532 C  CG   . LEU B  1 143 ? -41.54400 -12.24400 8.02900   1.000 18.51415  ? 143 LEU B CG   1 
ATOM   5533 C  CD1  . LEU B  1 143 ? -40.69600 -11.92900 9.28800   1.000 20.08079  ? 143 LEU B CD1  1 
ATOM   5534 C  CD2  . LEU B  1 143 ? -42.83500 -11.47900 8.07200   1.000 19.28169  ? 143 LEU B CD2  1 
ATOM   5535 H  H    . LEU B  1 143 ? -40.48400 -14.25800 6.11300   1.000 22.94924  ? 143 LEU B H    1 
ATOM   5536 H  HA   . LEU B  1 143 ? -42.26200 -12.42000 5.50000   1.000 23.64394  ? 143 LEU B HA   1 
ATOM   5537 H  HB2  . LEU B  1 143 ? -39.83800 -12.23200 6.91800   1.000 25.38570  ? 143 LEU B HB2  1 
ATOM   5538 H  HB3  . LEU B  1 143 ? -40.74700 -10.95200 6.67300   1.000 25.38570  ? 143 LEU B HB3  1 
ATOM   5539 H  HG   . LEU B  1 143 ? -41.76600 -13.18900 8.01900   1.000 22.21954  ? 143 LEU B HG   1 
ATOM   5540 H  HD11 . LEU B  1 143 ? -41.25000 -12.03800 10.07700  1.000 24.09951  ? 143 LEU B HD11 1 
ATOM   5541 H  HD12 . LEU B  1 143 ? -39.94500 -12.54100 9.32500   1.000 24.09951  ? 143 LEU B HD12 1 
ATOM   5542 H  HD13 . LEU B  1 143 ? -40.37500 -11.01500 9.23200   1.000 24.09951  ? 143 LEU B HD13 1 
ATOM   5543 H  HD21 . LEU B  1 143 ? -43.31200 -11.71000 8.88400   1.000 23.14059  ? 143 LEU B HD21 1 
ATOM   5544 H  HD22 . LEU B  1 143 ? -42.63900 -10.52900 8.06300   1.000 23.14059  ? 143 LEU B HD22 1 
ATOM   5545 H  HD23 . LEU B  1 143 ? -43.36800 -11.71400 7.29700   1.000 23.14059  ? 143 LEU B HD23 1 
ATOM   5546 N  N    . GLU B  1 144 ? -39.52500 -12.27500 3.83100   1.000 20.56095  ? 144 GLU B N    1 
ATOM   5547 C  CA   . GLU B  1 144 ? -38.96100 -11.72900 2.60200   1.000 21.62694  ? 144 GLU B CA   1 
ATOM   5548 C  C    . GLU B  1 144 ? -39.83900 -12.09100 1.42400   1.000 21.53696  ? 144 GLU B C    1 
ATOM   5549 O  O    . GLU B  1 144 ? -40.00300 -11.29200 0.49400   1.000 22.48017  ? 144 GLU B O    1 
ATOM   5550 C  CB   . GLU B  1 144 ? -37.53600 -12.25700 2.41000   1.000 25.89627  ? 144 GLU B CB   1 
ATOM   5551 C  CG   . GLU B  1 144 ? -36.56300 -11.60000 3.39000   1.000 30.54383  ? 144 GLU B CG   1 
ATOM   5552 C  CD   . GLU B  1 144 ? -35.18900 -12.23200 3.46400   1.000 56.00676  ? 144 GLU B CD   1 
ATOM   5553 O  OE1  . GLU B  1 144 ? -34.88100 -13.15200 2.67600   1.000 49.15331  ? 144 GLU B OE1  1 
ATOM   5554 O  OE2  . GLU B  1 144 ? -34.41800 -11.78800 4.34100   1.000 48.71272  ? 144 GLU B OE2  1 
ATOM   5555 H  H    . GLU B  1 144 ? -39.02200 -12.84600 4.23100   1.000 24.67570  ? 144 GLU B H    1 
ATOM   5556 H  HA   . GLU B  1 144 ? -38.90900 -10.76200 2.66100   1.000 25.95488  ? 144 GLU B HA   1 
ATOM   5557 H  HB2  . GLU B  1 144 ? -37.52500 -13.21500 2.56300   1.000 31.07808  ? 144 GLU B HB2  1 
ATOM   5558 H  HB3  . GLU B  1 144 ? -37.24000 -12.06200 1.50700   1.000 31.07808  ? 144 GLU B HB3  1 
ATOM   5559 H  HG2  . GLU B  1 144 ? -36.44100 -10.67400 3.12600   1.000 36.65516  ? 144 GLU B HG2  1 
ATOM   5560 H  HG3  . GLU B  1 144 ? -36.94800 -11.64200 4.27900   1.000 36.65516  ? 144 GLU B HG3  1 
ATOM   5561 N  N    . TYR B  1 145 ? -40.40400 -13.30000 1.43700   1.000 22.32426  ? 145 TYR B N    1 
ATOM   5562 C  CA   . TYR B  1 145 ? -41.30400 -13.70400 0.36300   1.000 21.42405  ? 145 TYR B CA   1 
ATOM   5563 C  C    . TYR B  1 145 ? -42.52800 -12.79800 0.30600   1.000 21.96117  ? 145 TYR B C    1 
ATOM   5564 O  O    . TYR B  1 145 ? -42.92800 -12.36700 -0.78500  1.000 22.10996  ? 145 TYR B O    1 
ATOM   5565 C  CB   . TYR B  1 145 ? -41.70700 -15.17000 0.54900   1.000 23.49366  ? 145 TYR B CB   1 
ATOM   5566 C  CG   . TYR B  1 145 ? -42.74200 -15.62800 -0.45400  1.000 24.26964  ? 145 TYR B CG   1 
ATOM   5567 C  CD1  . TYR B  1 145 ? -42.38200 -16.01900 -1.72000  1.000 26.46204  ? 145 TYR B CD1  1 
ATOM   5568 C  CD2  . TYR B  1 145 ? -44.08100 -15.67000 -0.10900  1.000 24.65303  ? 145 TYR B CD2  1 
ATOM   5569 C  CE1  . TYR B  1 145 ? -43.36800 -16.40900 -2.64200  1.000 26.04662  ? 145 TYR B CE1  1 
ATOM   5570 C  CE2  . TYR B  1 145 ? -45.03700 -16.06900 -1.01100  1.000 24.43440  ? 145 TYR B CE2  1 
ATOM   5571 C  CZ   . TYR B  1 145 ? -44.66900 -16.45100 -2.25100  1.000 27.11903  ? 145 TYR B CZ   1 
ATOM   5572 O  OH   . TYR B  1 145 ? -45.62700 -16.84700 -3.18300  1.000 34.70551  ? 145 TYR B OH   1 
ATOM   5573 H  H    . TYR B  1 145 ? -40.28300 -13.89400 2.04600   1.000 26.79167  ? 145 TYR B H    1 
ATOM   5574 H  HA   . TYR B  1 145 ? -40.84500 -13.63000 -0.48800  1.000 25.71143  ? 145 TYR B HA   1 
ATOM   5575 H  HB2  . TYR B  1 145 ? -40.92100 -15.72900 0.44400   1.000 28.19495  ? 145 TYR B HB2  1 
ATOM   5576 H  HB3  . TYR B  1 145 ? -42.07900 -15.28500 1.43700   1.000 28.19495  ? 145 TYR B HB3  1 
ATOM   5577 H  HD1  . TYR B  1 145 ? -41.48600 -16.02500 -1.96700  1.000 31.75701  ? 145 TYR B HD1  1 
ATOM   5578 H  HD2  . TYR B  1 145 ? -44.33800 -15.42300 0.75000   1.000 29.58619  ? 145 TYR B HD2  1 
ATOM   5579 H  HE1  . TYR B  1 145 ? -43.13200 -16.63700 -3.51300  1.000 31.25850  ? 145 TYR B HE1  1 
ATOM   5580 H  HE2  . TYR B  1 145 ? -45.93500 -16.07600 -0.76800  1.000 29.32385  ? 145 TYR B HE2  1 
ATOM   5581 H  HH   . TYR B  1 145 ? -46.39200 -16.82100 -2.83800  1.000 41.64918  ? 145 TYR B HH   1 
ATOM   5582 N  N    . LEU B  1 146 ? -43.10900 -12.46100 1.45400   1.000 20.15992  ? 146 LEU B N    1 
ATOM   5583 C  CA   . LEU B  1 146 ? -44.27100 -11.58500 1.44100   1.000 19.48714  ? 146 LEU B CA   1 
ATOM   5584 C  C    . LEU B  1 146 ? -43.91600 -10.19800 0.93100   1.000 19.06059  ? 146 LEU B C    1 
ATOM   5585 O  O    . LEU B  1 146 ? -44.68600 -9.59400  0.16600   1.000 20.72084  ? 146 LEU B O    1 
ATOM   5586 C  CB   . LEU B  1 146 ? -44.90300 -11.49100 2.82300   1.000 19.37086  ? 146 LEU B CB   1 
ATOM   5587 C  CG   . LEU B  1 146 ? -45.51100 -12.78100 3.36100   1.000 18.71965  ? 146 LEU B CG   1 
ATOM   5588 C  CD1  . LEU B  1 146 ? -45.98600 -12.56800 4.77900   1.000 20.04705  ? 146 LEU B CD1  1 
ATOM   5589 C  CD2  . LEU B  1 146 ? -46.65300 -13.26300 2.46800   1.000 20.70726  ? 146 LEU B CD2  1 
ATOM   5590 H  H    . LEU B  1 146 ? -42.85600 -12.72100 2.23400   1.000 24.19447  ? 146 LEU B H    1 
ATOM   5591 H  HA   . LEU B  1 146 ? -44.92800 -11.97300 0.84300   1.000 23.38713  ? 146 LEU B HA   1 
ATOM   5592 H  HB2  . LEU B  1 146 ? -44.22000 -11.21000 3.45100   1.000 23.24760  ? 146 LEU B HB2  1 
ATOM   5593 H  HB3  . LEU B  1 146 ? -45.61300 -10.83000 2.78800   1.000 23.24760  ? 146 LEU B HB3  1 
ATOM   5594 H  HG   . LEU B  1 146 ? -44.83600 -13.47700 3.36300   1.000 22.46615  ? 146 LEU B HG   1 
ATOM   5595 H  HD11 . LEU B  1 146 ? -46.33900 -13.40300 5.12300   1.000 24.05902  ? 146 LEU B HD11 1 
ATOM   5596 H  HD12 . LEU B  1 146 ? -45.23800 -12.27600 5.32300   1.000 24.05902  ? 146 LEU B HD12 1 
ATOM   5597 H  HD13 . LEU B  1 146 ? -46.68100 -11.89000 4.78100   1.000 24.05902  ? 146 LEU B HD13 1 
ATOM   5598 H  HD21 . LEU B  1 146 ? -47.03800 -14.06500 2.85300   1.000 24.85127  ? 146 LEU B HD21 1 
ATOM   5599 H  HD22 . LEU B  1 146 ? -47.32700 -12.56600 2.41300   1.000 24.85127  ? 146 LEU B HD22 1 
ATOM   5600 H  HD23 . LEU B  1 146 ? -46.30400 -13.45500 1.58400   1.000 24.85127  ? 146 LEU B HD23 1 
ATOM   5601 N  N    . VAL B  1 147 ? -42.73600 -9.69000  1.28600   1.000 20.45001  ? 147 VAL B N    1 
ATOM   5602 C  CA   . VAL B  1 147 ? -42.30500 -8.38900  0.79100   1.000 22.41387  ? 147 VAL B CA   1 
ATOM   5603 C  C    . VAL B  1 147 ? -42.12700 -8.45000  -0.71800  1.000 23.31426  ? 147 VAL B C    1 
ATOM   5604 O  O    . VAL B  1 147 ? -42.58600 -7.56900  -1.45800  1.000 23.29293  ? 147 VAL B O    1 
ATOM   5605 C  CB   . VAL B  1 147 ? -41.01100 -7.95300  1.50800   1.000 22.75524  ? 147 VAL B CB   1 
ATOM   5606 C  CG1  . VAL B  1 147 ? -40.39400 -6.77200  0.73900   1.000 26.79693  ? 147 VAL B CG1  1 
ATOM   5607 C  CG2  . VAL B  1 147 ? -41.27500 -7.59400  2.94500   1.000 22.94885  ? 147 VAL B CG2  1 
ATOM   5608 H  H    . VAL B  1 147 ? -42.17300 -10.07600 1.80900   1.000 24.54258  ? 147 VAL B H    1 
ATOM   5609 H  HA   . VAL B  1 147 ? -42.98700 -7.72700  0.98700   1.000 26.89921  ? 147 VAL B HA   1 
ATOM   5610 H  HB   . VAL B  1 147 ? -40.38000 -8.69000  1.52100   1.000 27.30885  ? 147 VAL B HB   1 
ATOM   5611 H  HG11 . VAL B  1 147 ? -39.76600 -6.31200  1.31800   1.000 32.15887  ? 147 VAL B HG11 1 
ATOM   5612 H  HG12 . VAL B  1 147 ? -39.93300 -7.11200  -0.04400  1.000 32.15887  ? 147 VAL B HG12 1 
ATOM   5613 H  HG13 . VAL B  1 147 ? -41.10100 -6.16600  0.47000   1.000 32.15887  ? 147 VAL B HG13 1 
ATOM   5614 H  HG21 . VAL B  1 147 ? -40.43100 -7.39800  3.38200   1.000 27.54118  ? 147 VAL B HG21 1 
ATOM   5615 H  HG22 . VAL B  1 147 ? -41.85100 -6.81400  2.97500   1.000 27.54118  ? 147 VAL B HG22 1 
ATOM   5616 H  HG23 . VAL B  1 147 ? -41.70800 -8.34300  3.38400   1.000 27.54118  ? 147 VAL B HG23 1 
ATOM   5617 N  N    . ASP B  1 148 ? -41.49100 -9.51300  -1.21400  1.000 22.37920  ? 148 ASP B N    1 
ATOM   5618 C  CA   . ASP B  1 148 ? -41.26900 -9.64200  -2.64900  1.000 23.60473  ? 148 ASP B CA   1 
ATOM   5619 C  C    . ASP B  1 148 ? -42.58300 -9.75500  -3.40500  1.000 23.03767  ? 148 ASP B C    1 
ATOM   5620 O  O    . ASP B  1 148 ? -42.72300 -9.23600  -4.51900  1.000 25.46970  ? 148 ASP B O    1 
ATOM   5621 C  CB   . ASP B  1 148 ? -40.40900 -10.87600 -2.91300  1.000 26.25124  ? 148 ASP B CB   1 
ATOM   5622 C  CG   . ASP B  1 148 ? -38.98600 -10.68900 -2.47000  1.000 44.98207  ? 148 ASP B CG   1 
ATOM   5623 O  OD1  . ASP B  1 148 ? -38.55100 -9.52500  -2.34900  1.000 40.39343  ? 148 ASP B OD1  1 
ATOM   5624 O  OD2  . ASP B  1 148 ? -38.30100 -11.71100 -2.25500  1.000 43.33164  ? 148 ASP B OD2  1 
ATOM   5625 H  H    . ASP B  1 148 ? -41.18200 -10.16500 -0.74400  1.000 26.85760  ? 148 ASP B H    1 
ATOM   5626 H  HA   . ASP B  1 148 ? -40.80400 -8.85300  -2.97100  1.000 28.32824  ? 148 ASP B HA   1 
ATOM   5627 H  HB2  . ASP B  1 148 ? -40.77800 -11.63000 -2.42800  1.000 31.50405  ? 148 ASP B HB2  1 
ATOM   5628 H  HB3  . ASP B  1 148 ? -40.40600 -11.06300 -3.86500  1.000 31.50405  ? 148 ASP B HB3  1 
ATOM   5629 N  N    . GLN B  1 149 ? -43.52300 -10.50600 -2.86100  1.000 22.67544  ? 149 GLN B N    1 
ATOM   5630 C  CA   . GLN B  1 149 ? -44.81000 -10.64100 -3.53400  1.000 21.15090  ? 149 GLN B CA   1 
ATOM   5631 C  C    . GLN B  1 149 ? -45.55500 -9.31200  -3.56200  1.000 21.67731  ? 149 GLN B C    1 
ATOM   5632 O  O    . GLN B  1 149 ? -46.17600 -8.96500  -4.57100  1.000 22.02167  ? 149 GLN B O    1 
ATOM   5633 C  CB   . GLN B  1 149 ? -45.65100 -11.73400 -2.87400  1.000 22.92010  ? 149 GLN B CB   1 
ATOM   5634 C  CG   . GLN B  1 149 ? -45.07900 -13.13800 -3.08600  1.000 27.64652  ? 149 GLN B CG   1 
ATOM   5635 C  CD   . GLN B  1 149 ? -44.82900 -13.49100 -4.55300  1.000 32.16495  ? 149 GLN B CD   1 
ATOM   5636 O  OE1  . GLN B  1 149 ? -43.68100 -13.63800 -4.99200  1.000 41.73631  ? 149 GLN B OE1  1 
ATOM   5637 N  NE2  . GLN B  1 149 ? -45.87800 -13.62400 -5.30000  1.000 30.26021  ? 149 GLN B NE2  1 
ATOM   5638 H  H    . GLN B  1 149 ? -43.44900 -10.93900 -2.12100  1.000 27.21309  ? 149 GLN B H    1 
ATOM   5639 H  HA   . GLN B  1 149 ? -44.65600 -10.91600 -4.45200  1.000 25.38364  ? 149 GLN B HA   1 
ATOM   5640 H  HB2  . GLN B  1 149 ? -45.69000 -11.56700 -1.91900  1.000 27.50668  ? 149 GLN B HB2  1 
ATOM   5641 H  HB3  . GLN B  1 149 ? -46.54500 -11.71500 -3.25000  1.000 27.50668  ? 149 GLN B HB3  1 
ATOM   5642 H  HG2  . GLN B  1 149 ? -44.23100 -13.20300 -2.61800  1.000 33.17839  ? 149 GLN B HG2  1 
ATOM   5643 H  HG3  . GLN B  1 149 ? -45.70500 -13.78700 -2.72900  1.000 33.17839  ? 149 GLN B HG3  1 
ATOM   5644 H  HE21 . GLN B  1 149 ? -46.66200 -13.51500 -4.96400  1.000 36.31482  ? 149 GLN B HE21 1 
ATOM   5645 H  HE22 . GLN B  1 149 ? -45.79100 -13.82200 -6.13300  1.000 36.31482  ? 149 GLN B HE22 1 
ATOM   5646 N  N    . SER B  1 150 ? -45.52800 -8.56000  -2.46300  1.000 21.20755  ? 150 SER B N    1 
ATOM   5647 C  CA   . SER B  1 150 ? -46.14100 -7.23800  -2.46300  1.000 20.78118  ? 150 SER B CA   1 
ATOM   5648 C  C    . SER B  1 150 ? -45.52900 -6.34000  -3.51500  1.000 20.87695  ? 150 SER B C    1 
ATOM   5649 O  O    . SER B  1 150 ? -46.23900 -5.53100  -4.12100  1.000 21.72069  ? 150 SER B O    1 
ATOM   5650 C  CB   . SER B  1 150 ? -45.96700 -6.59000  -1.08400  1.000 22.01416  ? 150 SER B CB   1 
ATOM   5651 O  OG   . SER B  1 150 ? -46.61900 -5.31100  -0.99200  1.000 21.53648  ? 150 SER B OG   1 
ATOM   5652 H  H    . SER B  1 150 ? -45.16700 -8.78900  -1.71700  1.000 25.45162  ? 150 SER B H    1 
ATOM   5653 H  HA   . SER B  1 150 ? -47.08800 -7.33500  -2.65200  1.000 24.93997  ? 150 SER B HA   1 
ATOM   5654 H  HB2  . SER B  1 150 ? -46.34800 -7.18000  -0.41500  1.000 26.41955  ? 150 SER B HB2  1 
ATOM   5655 H  HB3  . SER B  1 150 ? -45.02000 -6.46700  -0.91700  1.000 26.41955  ? 150 SER B HB3  1 
ATOM   5656 H  HG   . SER B  1 150 ? -46.23500 -4.75600  -1.49300  1.000 25.84634  ? 150 SER B HG   1 
ATOM   5657 N  N    . ASN B  1 151 ? -44.24800 -6.51100  -3.82600  1.000 21.81290  ? 151 ASN B N    1 
ATOM   5658 C  CA   . ASN B  1 151 ? -43.59800 -5.71700  -4.84800  1.000 21.28183  ? 151 ASN B CA   1 
ATOM   5659 C  C    . ASN B  1 151 ? -43.87800 -6.21300  -6.25300  1.000 24.56337  ? 151 ASN B C    1 
ATOM   5660 O  O    . ASN B  1 151 ? -43.29900 -5.63800  -7.17400  1.000 30.49365  ? 151 ASN B O    1 
ATOM   5661 C  CB   . ASN B  1 151 ? -42.08700 -5.66200  -4.62500  1.000 26.52829  ? 151 ASN B CB   1 
ATOM   5662 C  CG   . ASN B  1 151 ? -41.73100 -4.89600  -3.39300  1.000 34.67935  ? 151 ASN B CG   1 
ATOM   5663 O  OD1  . ASN B  1 151 ? -42.45900 -3.98200  -2.99600  1.000 41.98149  ? 151 ASN B OD1  1 
ATOM   5664 N  ND2  . ASN B  1 151 ? -40.61200 -5.25100  -2.77400  1.000 35.18348  ? 151 ASN B ND2  1 
ATOM   5665 H  H    . ASN B  1 151 ? -43.73300 -7.08900  -3.45100  1.000 26.17804  ? 151 ASN B H    1 
ATOM   5666 H  HA   . ASN B  1 151 ? -43.93800 -4.81200  -4.77000  1.000 25.54076  ? 151 ASN B HA   1 
ATOM   5667 H  HB2  . ASN B  1 151 ? -41.74600 -6.56500  -4.53000  1.000 31.83651  ? 151 ASN B HB2  1 
ATOM   5668 H  HB3  . ASN B  1 151 ? -41.66900 -5.22700  -5.38400  1.000 31.83651  ? 151 ASN B HB3  1 
ATOM   5669 H  HD21 . ASN B  1 151 ? -40.36600 -4.83900  -2.06100  1.000 42.22274  ? 151 ASN B HD21 1 
ATOM   5670 H  HD22 . ASN B  1 151 ? -40.13300 -5.89300  -3.08700  1.000 42.22274  ? 151 ASN B HD22 1 
ATOM   5671 N  N    . SER B  1 152 ? -44.73600 -7.22300  -6.43600  1.000 22.01691  ? 152 SER B N    1 
ATOM   5672 C  CA   . SER B  1 152 ? -44.95100 -7.83000  -7.74100  1.000 21.31578  ? 152 SER B CA   1 
ATOM   5673 C  C    . SER B  1 152 ? -46.37600 -7.58500  -8.20800  1.000 20.97815  ? 152 SER B C    1 
ATOM   5674 O  O    . SER B  1 152 ? -47.32500 -7.95800  -7.53000  1.000 20.84015  ? 152 SER B O    1 
ATOM   5675 C  CB   . SER B  1 152 ? -44.70300 -9.33800  -7.69200  1.000 24.19969  ? 152 SER B CB   1 
ATOM   5676 O  OG   . SER B  1 152 ? -45.07300 -9.92700  -8.94000  1.000 27.41695  ? 152 SER B OG   1 
ATOM   5677 H  H    . SER B  1 152 ? -45.20800 -7.57200  -5.80800  1.000 26.42285  ? 152 SER B H    1 
ATOM   5678 H  HA   . SER B  1 152 ? -44.34000 -7.41200  -8.36700  1.000 25.58150  ? 152 SER B HA   1 
ATOM   5679 H  HB2  . SER B  1 152 ? -43.76100 -9.50300  -7.52700  1.000 29.04219  ? 152 SER B HB2  1 
ATOM   5680 H  HB3  . SER B  1 152 ? -45.23800 -9.72800  -6.98300  1.000 29.04219  ? 152 SER B HB3  1 
ATOM   5681 H  HG   . SER B  1 152 ? -45.14300 -10.75900 -8.85500  1.000 32.90290  ? 152 SER B HG   1 
ATOM   5682 N  N    . SER B  1 153 ? -46.50300 -7.02700  -9.41100  1.000 22.88412  ? 153 SER B N    1 
ATOM   5683 C  CA   . SER B  1 153 ? -47.79300 -6.89100  -10.06100 1.000 21.99248  ? 153 SER B CA   1 
ATOM   5684 C  C    . SER B  1 153 ? -48.43700 -8.23500  -10.40300 1.000 20.76829  ? 153 SER B C    1 
ATOM   5685 O  O    . SER B  1 153 ? -49.60200 -8.26800  -10.81400 1.000 22.82466  ? 153 SER B O    1 
ATOM   5686 C  CB   . SER B  1 153 ? -47.59500 -6.09000  -11.36200 1.000 25.38451  ? 153 SER B CB   1 
ATOM   5687 O  OG   . SER B  1 153 ? -46.86000 -6.87200  -12.27800 1.000 29.08077  ? 153 SER B OG   1 
ATOM   5688 H  H    . SER B  1 153 ? -45.84700 -6.71600  -9.87300  1.000 27.46351  ? 153 SER B H    1 
ATOM   5689 H  HA   . SER B  1 153 ? -48.39900 -6.41800  -9.46900  1.000 26.39354  ? 153 SER B HA   1 
ATOM   5690 H  HB2  . SER B  1 153 ? -48.46100 -5.87500  -11.74400 1.000 30.46398  ? 153 SER B HB2  1 
ATOM   5691 H  HB3  . SER B  1 153 ? -47.10600 -5.27500  -11.16800 1.000 30.46398  ? 153 SER B HB3  1 
ATOM   5692 H  HG   . SER B  1 153 ? -46.69600 -6.42500  -12.97000 1.000 34.89949  ? 153 SER B HG   1 
ATOM   5693 N  N    . ARG B  1 154 ? -47.72100 -9.33400  -10.28800 1.000 21.86641  ? 154 ARG B N    1 
ATOM   5694 C  CA   . ARG B  1 154 ? -48.26000 -10.66900 -10.52200 1.000 24.46704  ? 154 ARG B CA   1 
ATOM   5695 C  C    . ARG B  1 154 ? -48.84200 -11.31300 -9.26100  1.000 22.86039  ? 154 ARG B C    1 
ATOM   5696 O  O    . ARG B  1 154 ? -49.29500 -12.46000 -9.33100  1.000 25.30652  ? 154 ARG B O    1 
ATOM   5697 C  CB   . ARG B  1 154 ? -47.16100 -11.56100 -11.09300 1.000 23.74904  ? 154 ARG B CB   1 
ATOM   5698 C  CG   . ARG B  1 154 ? -46.50300 -10.93100 -12.32200 1.000 24.72916  ? 154 ARG B CG   1 
ATOM   5699 C  CD   . ARG B  1 154 ? -45.42500 -11.79200 -12.87300 1.000 26.72584  ? 154 ARG B CD   1 
ATOM   5700 N  NE   . ARG B  1 154 ? -45.91600 -13.06600 -13.36000 1.000 29.80113  ? 154 ARG B NE   1 
ATOM   5701 C  CZ   . ARG B  1 154 ? -45.50100 -14.26000 -12.97600 1.000 56.94736  ? 154 ARG B CZ   1 
ATOM   5702 N  NH1  . ARG B  1 154 ? -44.52300 -14.40700 -12.09500 1.000 48.11271  ? 154 ARG B NH1  1 
ATOM   5703 N  NH2  . ARG B  1 154 ? -46.07100 -15.33800 -13.50500 1.000 50.66724  ? 154 ARG B NH2  1 
ATOM   5704 H  H    . ARG B  1 154 ? -46.89000 -9.33900  -10.06800 1.000 26.24225  ? 154 ARG B H    1 
ATOM   5705 H  HA   . ARG B  1 154 ? -48.97900 -10.61000 -11.17000 1.000 29.36301  ? 154 ARG B HA   1 
ATOM   5706 H  HB2  . ARG B  1 154 ? -46.47700 -11.69800 -10.41900 1.000 28.50141  ? 154 ARG B HB2  1 
ATOM   5707 H  HB3  . ARG B  1 154 ? -47.54400 -12.41300 -11.35500 1.000 28.50141  ? 154 ARG B HB3  1 
ATOM   5708 H  HG2  . ARG B  1 154 ? -47.17200 -10.80300 -13.01300 1.000 29.67755  ? 154 ARG B HG2  1 
ATOM   5709 H  HG3  . ARG B  1 154 ? -46.11400 -10.07800 -12.07600 1.000 29.67755  ? 154 ARG B HG3  1 
ATOM   5710 H  HD2  . ARG B  1 154 ? -45.00100 -11.33200 -13.61300 1.000 32.07357  ? 154 ARG B HD2  1 
ATOM   5711 H  HD3  . ARG B  1 154 ? -44.77500 -11.96900 -12.17500 1.000 32.07357  ? 154 ARG B HD3  1 
ATOM   5712 H  HE   . ARG B  1 154 ? -46.53600 -13.04200 -13.95600 1.000 35.76392  ? 154 ARG B HE   1 
ATOM   5713 H  HH11 . ARG B  1 154 ? -44.14100 -13.71400 -11.75800 1.000 57.73781  ? 154 ARG B HH11 1 
ATOM   5714 H  HH12 . ARG B  1 154 ? -44.27000 -15.19500 -11.86000 1.000 57.73781  ? 154 ARG B HH12 1 
ATOM   5715 H  HH21 . ARG B  1 154 ? -46.69800 -15.25100 -14.08700 1.000 60.80325  ? 154 ARG B HH21 1 
ATOM   5716 H  HH22 . ARG B  1 154 ? -45.81200 -16.12300 -13.26600 1.000 60.80325  ? 154 ARG B HH22 1 
ATOM   5717 N  N    . SER B  1 155 ? -48.85700 -10.60700 -8.12500  1.000 21.03985  ? 155 SER B N    1 
ATOM   5718 C  CA   . SER B  1 155 ? -49.30800 -11.19800 -6.87800  1.000 22.97485  ? 155 SER B CA   1 
ATOM   5719 C  C    . SER B  1 155 ? -50.65800 -10.63100 -6.45600  1.000 19.96755  ? 155 SER B C    1 
ATOM   5720 O  O    . SER B  1 155 ? -50.89500 -9.42500  -6.54300  1.000 21.52592  ? 155 SER B O    1 
ATOM   5721 C  CB   . SER B  1 155 ? -48.30200 -10.89200 -5.76400  1.000 21.53436  ? 155 SER B CB   1 
ATOM   5722 O  OG   . SER B  1 155 ? -48.84000 -11.21900 -4.49300  1.000 22.29253  ? 155 SER B OG   1 
ATOM   5723 H  H    . SER B  1 155 ? -48.61100 -9.78600  -8.05900  1.000 25.25038  ? 155 SER B H    1 
ATOM   5724 H  HA   . SER B  1 155 ? -49.39700 -12.15700 -6.99100  1.000 27.57239  ? 155 SER B HA   1 
ATOM   5725 H  HB2  . SER B  1 155 ? -47.49900 -11.41500 -5.91200  1.000 25.84380  ? 155 SER B HB2  1 
ATOM   5726 H  HB3  . SER B  1 155 ? -48.08900 -9.94500  -5.78300  1.000 25.84380  ? 155 SER B HB3  1 
ATOM   5727 H  HG   . SER B  1 155 ? -48.98300 -12.04500 -4.44600  1.000 26.75360  ? 155 SER B HG   1 
ATOM   5728 N  N    . PRO B  1 156 ? -51.53200 -11.46500 -5.89400  1.000 21.18504  ? 156 PRO B N    1 
ATOM   5729 C  CA   . PRO B  1 156 ? -52.76100 -10.91800 -5.30100  1.000 23.11665  ? 156 PRO B CA   1 
ATOM   5730 C  C    . PRO B  1 156 ? -52.51100 -9.89400  -4.21800  1.000 23.06952  ? 156 PRO B C    1 
ATOM   5731 O  O    . PRO B  1 156 ? -53.36600 -9.01600  -4.00100  1.000 24.39054  ? 156 PRO B O    1 
ATOM   5732 C  CB   . PRO B  1 156 ? -53.50300 -12.14800 -4.77000  1.000 27.30889  ? 156 PRO B CB   1 
ATOM   5733 C  CG   . PRO B  1 156 ? -52.68000 -13.31300 -5.05600  1.000 34.15921  ? 156 PRO B CG   1 
ATOM   5734 C  CD   . PRO B  1 156 ? -51.39600 -12.92100 -5.73100  1.000 26.68166  ? 156 PRO B CD   1 
ATOM   5735 H  HA   . PRO B  1 156 ? -53.29800 -10.51500 -6.00100  1.000 27.74254  ? 156 PRO B HA   1 
ATOM   5736 H  HB2  . PRO B  1 156 ? -53.63500 -12.05400 -3.81400  1.000 32.77323  ? 156 PRO B HB2  1 
ATOM   5737 H  HB3  . PRO B  1 156 ? -54.36100 -12.22300 -5.21700  1.000 32.77323  ? 156 PRO B HB3  1 
ATOM   5738 H  HG2  . PRO B  1 156 ? -52.48100 -13.75900 -4.21800  1.000 40.99361  ? 156 PRO B HG2  1 
ATOM   5739 H  HG3  . PRO B  1 156 ? -53.18200 -13.90600 -5.63700  1.000 40.99361  ? 156 PRO B HG3  1 
ATOM   5740 H  HD2  . PRO B  1 156 ? -50.63300 -13.13700 -5.17300  1.000 32.02055  ? 156 PRO B HD2  1 
ATOM   5741 H  HD3  . PRO B  1 156 ? -51.31100 -13.35800 -6.59300  1.000 32.02055  ? 156 PRO B HD3  1 
ATOM   5742 N  N    . ILE B  1 157 ? -51.39800 -9.97200  -3.50700  1.000 20.52160  ? 157 ILE B N    1 
ATOM   5743 C  CA   . ILE B  1 157 ? -51.10900 -9.04300  -2.40800  1.000 19.34287  ? 157 ILE B CA   1 
ATOM   5744 C  C    . ILE B  1 157 ? -50.24200 -7.86200  -2.85100  1.000 19.95635  ? 157 ILE B C    1 
ATOM   5745 O  O    . ILE B  1 157 ? -49.66000 -7.16100  -2.00200  1.000 20.61758  ? 157 ILE B O    1 
ATOM   5746 C  CB   . ILE B  1 157 ? -50.52600 -9.75200  -1.16800  1.000 19.56285  ? 157 ILE B CB   1 
ATOM   5747 C  CG1  . ILE B  1 157 ? -49.18300 -10.42100 -1.44500  1.000 18.74958  ? 157 ILE B CG1  1 
ATOM   5748 C  CG2  . ILE B  1 157 ? -51.57900 -10.71800 -0.61200  1.000 22.10511  ? 157 ILE B CG2  1 
ATOM   5749 C  CD1  . ILE B  1 157 ? -48.44600 -10.71500 -0.13400  1.000 21.94809  ? 157 ILE B CD1  1 
ATOM   5750 H  H    . ILE B  1 157 ? -50.78200 -10.55800 -3.63800  1.000 24.62849  ? 157 ILE B H    1 
ATOM   5751 H  HA   . ILE B  1 157 ? -51.96100 -8.66600  -2.13700  1.000 23.21401  ? 157 ILE B HA   1 
ATOM   5752 H  HB   . ILE B  1 157 ? -50.32600 -9.08600  -0.49200  1.000 23.47798  ? 157 ILE B HB   1 
ATOM   5753 H  HG12 . ILE B  1 157 ? -49.32800 -11.25800 -1.91300  1.000 22.50206  ? 157 ILE B HG12 1 
ATOM   5754 H  HG13 . ILE B  1 157 ? -48.63200 -9.83200  -1.98400  1.000 22.50206  ? 157 ILE B HG13 1 
ATOM   5755 H  HG21 . ILE B  1 157 ? -51.22000 -11.15600 0.17600   1.000 26.52870  ? 157 ILE B HG21 1 
ATOM   5756 H  HG22 . ILE B  1 157 ? -52.37500 -10.21700 -0.37800  1.000 26.52870  ? 157 ILE B HG22 1 
ATOM   5757 H  HG23 . ILE B  1 157 ? -51.79100 -11.37900 -1.29000  1.000 26.52870  ? 157 ILE B HG23 1 
ATOM   5758 H  HD11 . ILE B  1 157 ? -47.58100 -11.10600 -0.33900  1.000 26.34027  ? 157 ILE B HD11 1 
ATOM   5759 H  HD12 . ILE B  1 157 ? -48.32700 -9.88600  0.35400   1.000 26.34027  ? 157 ILE B HD12 1 
ATOM   5760 H  HD13 . ILE B  1 157 ? -48.97300 -11.33700 0.39200   1.000 26.34027  ? 157 ILE B HD13 1 
ATOM   5761 N  N    . ASN B  1 158 ? -50.11500 -7.64100  -4.16200  1.000 18.83248  ? 158 ASN B N    1 
ATOM   5762 C  CA   . ASN B  1 158 ? -49.38700 -6.50100  -4.68400  1.000 20.24449  ? 158 ASN B CA   1 
ATOM   5763 C  C    . ASN B  1 158 ? -49.77600 -5.21500  -3.96600  1.000 20.37481  ? 158 ASN B C    1 
ATOM   5764 O  O    . ASN B  1 158 ? -50.95900 -4.86500  -3.86600  1.000 19.99658  ? 158 ASN B O    1 
ATOM   5765 C  CB   . ASN B  1 158 ? -49.71900 -6.41700  -6.18700  1.000 20.03304  ? 158 ASN B CB   1 
ATOM   5766 C  CG   . ASN B  1 158 ? -49.08900 -5.26000  -6.87900  1.000 22.27679  ? 158 ASN B CG   1 
ATOM   5767 O  OD1  . ASN B  1 158 ? -47.89900 -4.90800  -6.67800  1.000 25.10013  ? 158 ASN B OD1  1 
ATOM   5768 N  ND2  . ASN B  1 158 ? -49.85000 -4.68600  -7.79900  1.000 21.19011  ? 158 ASN B ND2  1 
ATOM   5769 H  H    . ASN B  1 158 ? -50.44800 -8.14800  -4.77300  1.000 22.58617  ? 158 ASN B H    1 
ATOM   5770 H  HA   . ASN B  1 158 ? -48.43100 -6.60500  -4.55400  1.000 24.29595  ? 158 ASN B HA   1 
ATOM   5771 H  HB2  . ASN B  1 158 ? -49.40800 -7.22600  -6.62100  1.000 24.04222  ? 158 ASN B HB2  1 
ATOM   5772 H  HB3  . ASN B  1 158 ? -50.68000 -6.33400  -6.29000  1.000 24.04222  ? 158 ASN B HB3  1 
ATOM   5773 H  HD21 . ASN B  1 158 ? -49.55400 -4.01000  -8.24100  1.000 25.43069  ? 158 ASN B HD21 1 
ATOM   5774 H  HD22 . ASN B  1 158 ? -50.64000 -4.98800  -7.95300  1.000 25.43069  ? 158 ASN B HD22 1 
ATOM   5775 N  N    . GLY B  1 159 ? -48.75600 -4.52100  -3.46700  1.000 21.59947  ? 159 GLY B N    1 
ATOM   5776 C  CA   . GLY B  1 159 ? -48.90400 -3.22800  -2.83100  1.000 21.46191  ? 159 GLY B CA   1 
ATOM   5777 C  C    . GLY B  1 159 ? -49.31400 -3.24000  -1.38400  1.000 22.04833  ? 159 GLY B C    1 
ATOM   5778 O  O    . GLY B  1 159 ? -49.36000 -2.16400  -0.76600  1.000 23.19106  ? 159 GLY B O    1 
ATOM   5779 H  H    . GLY B  1 159 ? -47.94100 -4.79300  -3.48900  1.000 25.92192  ? 159 GLY B H    1 
ATOM   5780 H  HA2  . GLY B  1 159 ? -48.05600 -2.76200  -2.88800  1.000 25.75686  ? 159 GLY B HA2  1 
ATOM   5781 H  HA3  . GLY B  1 159 ? -49.57500 -2.72400  -3.31700  1.000 25.75686  ? 159 GLY B HA3  1 
ATOM   5782 N  N    . MET B  1 160 ? -49.62200 -4.40000  -0.82600  1.000 19.28292  ? 160 MET B N    1 
ATOM   5783 C  CA   . MET B  1 160 ? -50.27700 -4.45000  0.47200   1.000 19.29671  ? 160 MET B CA   1 
ATOM   5784 C  C    . MET B  1 160 ? -49.33700 -4.43500  1.66600   1.000 20.42139  ? 160 MET B C    1 
ATOM   5785 O  O    . MET B  1 160 ? -49.82400 -4.21000  2.78800   1.000 22.29560  ? 160 MET B O    1 
ATOM   5786 C  CB   . MET B  1 160 ? -51.15200 -5.68500  0.59400   1.000 20.27523  ? 160 MET B CB   1 
ATOM   5787 C  CG   . MET B  1 160 ? -52.34700 -5.68300  -0.29600  1.000 22.81520  ? 160 MET B CG   1 
ATOM   5788 S  SD   . MET B  1 160 ? -53.38900 -7.15500  0.03100   1.000 24.41291  ? 160 MET B SD   1 
ATOM   5789 C  CE   . MET B  1 160 ? -54.57700 -6.94200  -1.25500  1.000 28.73335  ? 160 MET B CE   1 
ATOM   5790 H  H    . MET B  1 160 ? -49.46200 -5.16900  -1.17600  1.000 23.14207  ? 160 MET B H    1 
ATOM   5791 H  HA   . MET B  1 160 ? -50.84000 -3.66200  0.51300   1.000 23.15861  ? 160 MET B HA   1 
ATOM   5792 H  HB2  . MET B  1 160 ? -50.62100 -6.46500  0.36900   1.000 24.33283  ? 160 MET B HB2  1 
ATOM   5793 H  HB3  . MET B  1 160 ? -51.46800 -5.75200  1.50900   1.000 24.33283  ? 160 MET B HB3  1 
ATOM   5794 H  HG2  . MET B  1 160 ? -52.87500 -4.88700  -0.12900  1.000 27.38080  ? 160 MET B HG2  1 
ATOM   5795 H  HG3  . MET B  1 160 ? -52.06200 -5.70500  -1.22300  1.000 27.38080  ? 160 MET B HG3  1 
ATOM   5796 H  HE1  . MET B  1 160 ? -55.15600 -7.71900  -1.28200  1.000 34.48258  ? 160 MET B HE1  1 
ATOM   5797 H  HE2  . MET B  1 160 ? -55.10100 -6.14600  -1.07300  1.000 34.48258  ? 160 MET B HE2  1 
ATOM   5798 H  HE3  . MET B  1 160 ? -54.11300 -6.84500  -2.10100  1.000 34.48258  ? 160 MET B HE3  1 
ATOM   5799 N  N    . VAL B  1 161 ? -48.05000 -4.69300  1.48500   1.000 19.71357  ? 161 VAL B N    1 
ATOM   5800 C  CA   . VAL B  1 161 ? -47.12100 -4.89400  2.59700   1.000 19.03430  ? 161 VAL B CA   1 
ATOM   5801 C  C    . VAL B  1 161 ? -46.18300 -3.71700  2.71900   1.000 22.61742  ? 161 VAL B C    1 
ATOM   5802 O  O    . VAL B  1 161 ? -45.52400 -3.32300  1.74900   1.000 22.67350  ? 161 VAL B O    1 
ATOM   5803 C  CB   . VAL B  1 161 ? -46.34200 -6.20600  2.43800   1.000 19.83443  ? 161 VAL B CB   1 
ATOM   5804 C  CG1  . VAL B  1 161 ? -45.27200 -6.33800  3.53400   1.000 20.67951  ? 161 VAL B CG1  1 
ATOM   5805 C  CG2  . VAL B  1 161 ? -47.26400 -7.37700  2.47000   1.000 20.06204  ? 161 VAL B CG2  1 
ATOM   5806 H  H    . VAL B  1 161 ? -47.68000 -4.75900  0.71100   1.000 23.65885  ? 161 VAL B H    1 
ATOM   5807 H  HA   . VAL B  1 161 ? -47.63700 -4.92600  3.41800   1.000 22.84372  ? 161 VAL B HA   1 
ATOM   5808 H  HB   . VAL B  1 161 ? -45.89600 -6.19500  1.57700   1.000 23.80388  ? 161 VAL B HB   1 
ATOM   5809 H  HG11 . VAL B  1 161 ? -44.93500 -7.24700  3.53800   1.000 24.81797  ? 161 VAL B HG11 1 
ATOM   5810 H  HG12 . VAL B  1 161 ? -44.54900 -5.71800  3.34600   1.000 24.81797  ? 161 VAL B HG12 1 
ATOM   5811 H  HG13 . VAL B  1 161 ? -45.67100 -6.12900  4.39300   1.000 24.81797  ? 161 VAL B HG13 1 
ATOM   5812 H  HG21 . VAL B  1 161 ? -46.74100 -8.19200  2.42900   1.000 24.07702  ? 161 VAL B HG21 1 
ATOM   5813 H  HG22 . VAL B  1 161 ? -47.77700 -7.35300  3.29300   1.000 24.07702  ? 161 VAL B HG22 1 
ATOM   5814 H  HG23 . VAL B  1 161 ? -47.86200 -7.32900  1.70700   1.000 24.07702  ? 161 VAL B HG23 1 
ATOM   5815 N  N    . ASP B  1 162 ? -46.05600 -3.20300  3.95000   1.000 20.59350  ? 162 ASP B N    1 
ATOM   5816 C  CA   . ASP B  1 162 ? -45.01700 -2.24200  4.28500   1.000 20.69986  ? 162 ASP B CA   1 
ATOM   5817 C  C    . ASP B  1 162 ? -43.79300 -3.02300  4.76000   1.000 21.96996  ? 162 ASP B C    1 
ATOM   5818 O  O    . ASP B  1 162 ? -43.85000 -3.65500  5.83200   1.000 21.79052  ? 162 ASP B O    1 
ATOM   5819 C  CB   . ASP B  1 162 ? -45.53600 -1.30500  5.37400   1.000 20.42134  ? 162 ASP B CB   1 
ATOM   5820 C  CG   . ASP B  1 162 ? -44.54600 -0.23700  5.76300   1.000 22.79109  ? 162 ASP B CG   1 
ATOM   5821 O  OD1  . ASP B  1 162 ? -43.32800 -0.39100  5.47700   1.000 23.78139  ? 162 ASP B OD1  1 
ATOM   5822 O  OD2  . ASP B  1 162 ? -44.96300 0.80300   6.35100   1.000 22.57620  ? 162 ASP B OD2  1 
ATOM   5823 H  H    . ASP B  1 162 ? -46.56900 -3.40200  4.61000   1.000 24.71476  ? 162 ASP B H    1 
ATOM   5824 H  HA   . ASP B  1 162 ? -44.75900 -1.71200  3.51500   1.000 24.84239  ? 162 ASP B HA   1 
ATOM   5825 H  HB2  . ASP B  1 162 ? -46.33900 -0.86500  5.05400   1.000 24.50817  ? 162 ASP B HB2  1 
ATOM   5826 H  HB3  . ASP B  1 162 ? -45.73800 -1.82700  6.16700   1.000 24.50817  ? 162 ASP B HB3  1 
ATOM   5827 N  N    . PRO B  1 163 ? -42.69500 -3.04900  4.00100   1.000 21.32684  ? 163 PRO B N    1 
ATOM   5828 C  CA   . PRO B  1 163 ? -41.55700 -3.88700  4.39100   1.000 21.19999  ? 163 PRO B CA   1 
ATOM   5829 C  C    . PRO B  1 163 ? -40.91400 -3.47700  5.69600   1.000 20.98207  ? 163 PRO B C    1 
ATOM   5830 O  O    . PRO B  1 163 ? -40.08100 -4.23400  6.23600   1.000 23.00404  ? 163 PRO B O    1 
ATOM   5831 C  CB   . PRO B  1 163 ? -40.56100 -3.70400  3.23900   1.000 24.99765  ? 163 PRO B CB   1 
ATOM   5832 C  CG   . PRO B  1 163 ? -40.91100 -2.36400  2.66400   1.000 28.84413  ? 163 PRO B CG   1 
ATOM   5833 C  CD   . PRO B  1 163 ? -42.40300 -2.26200  2.78600   1.000 24.81886  ? 163 PRO B CD   1 
ATOM   5834 H  HA   . PRO B  1 163 ? -41.84300 -4.81300  4.43800   1.000 25.44255  ? 163 PRO B HA   1 
ATOM   5835 H  HB2  . PRO B  1 163 ? -39.65200 -3.71400  3.57800   1.000 29.99974  ? 163 PRO B HB2  1 
ATOM   5836 H  HB3  . PRO B  1 163 ? -40.67700 -4.40800  2.58200   1.000 29.99974  ? 163 PRO B HB3  1 
ATOM   5837 H  HG2  . PRO B  1 163 ? -40.47300 -1.66300  3.17100   1.000 34.61552  ? 163 PRO B HG2  1 
ATOM   5838 H  HG3  . PRO B  1 163 ? -40.63600 -2.32200  1.73500   1.000 34.61552  ? 163 PRO B HG3  1 
ATOM   5839 H  HD2  . PRO B  1 163 ? -42.67800 -1.33800  2.89800   1.000 29.78519  ? 163 PRO B HD2  1 
ATOM   5840 H  HD3  . PRO B  1 163 ? -42.84000 -2.64700  2.01100   1.000 29.78519  ? 163 PRO B HD3  1 
ATOM   5841 N  N    . ASN B  1 164 ? -41.23800 -2.29500  6.21500   1.000 21.43736  ? 164 ASN B N    1 
ATOM   5842 C  CA   . ASN B  1 164 ? -40.62600 -1.82800  7.44500   1.000 22.88287  ? 164 ASN B CA   1 
ATOM   5843 C  C    . ASN B  1 164 ? -41.35700 -2.33300  8.68500   1.000 20.12321  ? 164 ASN B C    1 
ATOM   5844 O  O    . ASN B  1 164 ? -40.96200 -2.00900  9.80500   1.000 21.39134  ? 164 ASN B O    1 
ATOM   5845 C  CB   . ASN B  1 164 ? -40.64800 -0.29400  7.47700   1.000 25.98370  ? 164 ASN B CB   1 
ATOM   5846 C  CG   . ASN B  1 164 ? -39.90100 0.32000   6.33000   1.000 33.43388  ? 164 ASN B CG   1 
ATOM   5847 O  OD1  . ASN B  1 164 ? -38.74100 0.01700   6.11700   1.000 31.10021  ? 164 ASN B OD1  1 
ATOM   5848 N  ND2  . ASN B  1 164 ? -40.57700 1.16300   5.55200   1.000 41.72940  ? 164 ASN B ND2  1 
ATOM   5849 H  H    . ASN B  1 164 ? -41.80900 -1.75100  5.87100   1.000 25.72740  ? 164 ASN B H    1 
ATOM   5850 H  HA   . ASN B  1 164 ? -39.70600 -2.13600  7.47200   1.000 27.46201  ? 164 ASN B HA   1 
ATOM   5851 H  HB2  . ASN B  1 164 ? -41.56900 0.00900   7.43400   1.000 31.18300  ? 164 ASN B HB2  1 
ATOM   5852 H  HB3  . ASN B  1 164 ? -40.23700 0.01100   8.30100   1.000 31.18300  ? 164 ASN B HB3  1 
ATOM   5853 H  HD21 . ASN B  1 164 ? -41.40300 1.33200   5.71900   1.000 50.07784  ? 164 ASN B HD21 1 
ATOM   5854 H  HD22 . ASN B  1 164 ? -40.18700 1.53700   4.88400   1.000 50.07784  ? 164 ASN B HD22 1 
ATOM   5855 N  N    . ARG B  1 165 ? -42.45800 -3.07200  8.52900   1.000 18.75332  ? 165 ARG B N    1 
ATOM   5856 C  CA   . ARG B  1 165 ? -43.33500 -3.42200  9.64400   1.000 17.31156  ? 165 ARG B CA   1 
ATOM   5857 C  C    . ARG B  1 165 ? -43.68500 -4.88900  9.53600   1.000 17.25027  ? 165 ARG B C    1 
ATOM   5858 O  O    . ARG B  1 165 ? -44.63300 -5.27300  8.84800   1.000 18.71629  ? 165 ARG B O    1 
ATOM   5859 C  CB   . ARG B  1 165 ? -44.58300 -2.51000  9.63100   1.000 17.87002  ? 165 ARG B CB   1 
ATOM   5860 C  CG   . ARG B  1 165 ? -44.19500 -1.04500  9.57900   1.000 19.57867  ? 165 ARG B CG   1 
ATOM   5861 C  CD   . ARG B  1 165 ? -45.37300 -0.08000  9.80200   1.000 18.86601  ? 165 ARG B CD   1 
ATOM   5862 N  NE   . ARG B  1 165 ? -46.34500 -0.13500  8.71600   1.000 18.45923  ? 165 ARG B NE   1 
ATOM   5863 C  CZ   . ARG B  1 165 ? -47.62300 -0.48700  8.85000   1.000 18.40173  ? 165 ARG B CZ   1 
ATOM   5864 N  NH1  . ARG B  1 165 ? -48.08900 -1.00300  9.99400   1.000 18.31356  ? 165 ARG B NH1  1 
ATOM   5865 N  NH2  . ARG B  1 165 ? -48.45300 -0.31300  7.80700   1.000 19.58445  ? 165 ARG B NH2  1 
ATOM   5866 H  H    . ARG B  1 165 ? -42.72000 -3.38500  7.77200   1.000 22.50655  ? 165 ARG B H    1 
ATOM   5867 H  HA   . ARG B  1 165 ? -42.86500 -3.30600  10.48500  1.000 20.76106  ? 165 ARG B HA   1 
ATOM   5868 H  HB2  . ARG B  1 165 ? -45.12100 -2.71200  8.85000   1.000 21.44658  ? 165 ARG B HB2  1 
ATOM   5869 H  HB3  . ARG B  1 165 ? -45.10000 -2.66100  10.43800  1.000 21.44658  ? 165 ARG B HB3  1 
ATOM   5870 H  HG2  . ARG B  1 165 ? -43.53700 -0.87200  10.26900  1.000 23.49697  ? 165 ARG B HG2  1 
ATOM   5871 H  HG3  . ARG B  1 165 ? -43.81900 -0.85300  8.70600   1.000 23.49697  ? 165 ARG B HG3  1 
ATOM   5872 H  HD2  . ARG B  1 165 ? -45.82700 -0.31600  10.62600  1.000 22.64178  ? 165 ARG B HD2  1 
ATOM   5873 H  HD3  . ARG B  1 165 ? -45.03500 0.82800   9.85900   1.000 22.64178  ? 165 ARG B HD3  1 
ATOM   5874 H  HE   . ARG B  1 165 ? -46.07100 0.07500   7.92800   1.000 22.15364  ? 165 ARG B HE   1 
ATOM   5875 H  HH11 . ARG B  1 165 ? -47.56000 -1.11400  10.66200  1.000 21.97883  ? 165 ARG B HH11 1 
ATOM   5876 H  HH12 . ARG B  1 165 ? -48.91800 -1.22300  10.06000  1.000 21.97883  ? 165 ARG B HH12 1 
ATOM   5877 H  HH21 . ARG B  1 165 ? -48.15600 0.01900   7.07200   1.000 23.50390  ? 165 ARG B HH21 1 
ATOM   5878 H  HH22 . ARG B  1 165 ? -49.28200 -0.53400  7.87500   1.000 23.50390  ? 165 ARG B HH22 1 
ATOM   5879 N  N    . LEU B  1 166 ? -42.87800 -5.72300  10.18700  1.000 18.26276  ? 166 LEU B N    1 
ATOM   5880 C  CA   . LEU B  1 166 ? -42.92100 -7.16600  10.02800  1.000 15.91836  ? 166 LEU B CA   1 
ATOM   5881 C  C    . LEU B  1 166 ? -43.01900 -7.81600  11.38800  1.000 16.49538  ? 166 LEU B C    1 
ATOM   5882 O  O    . LEU B  1 166 ? -42.30300 -7.42500  12.32700  1.000 16.47084  ? 166 LEU B O    1 
ATOM   5883 C  CB   . LEU B  1 166 ? -41.69200 -7.70600  9.31700   1.000 18.57146  ? 166 LEU B CB   1 
ATOM   5884 C  CG   . LEU B  1 166 ? -41.44800 -7.11100  7.93800   1.000 18.94949  ? 166 LEU B CG   1 
ATOM   5885 C  CD1  . LEU B  1 166 ? -40.12500 -7.63600  7.39900   1.000 22.90491  ? 166 LEU B CD1  1 
ATOM   5886 C  CD2  . LEU B  1 166 ? -42.54600 -7.40000  6.98400   1.000 21.26601  ? 166 LEU B CD2  1 
ATOM   5887 H  H    . LEU B  1 166 ? -42.27700 -5.46300  10.74500  1.000 21.91787  ? 166 LEU B H    1 
ATOM   5888 H  HA   . LEU B  1 166 ? -43.70300 -7.39400  9.50100   1.000 19.10459  ? 166 LEU B HA   1 
ATOM   5889 H  HB2  . LEU B  1 166 ? -40.91200 -7.51600  9.86100   1.000 22.28831  ? 166 LEU B HB2  1 
ATOM   5890 H  HB3  . LEU B  1 166 ? -41.79600 -8.66500  9.20900   1.000 22.28831  ? 166 LEU B HB3  1 
ATOM   5891 H  HG   . LEU B  1 166 ? -41.41400 -6.14600  8.02300   1.000 22.74195  ? 166 LEU B HG   1 
ATOM   5892 H  HD11 . LEU B  1 166 ? -39.98100 -7.27600  6.51000   1.000 27.48846  ? 166 LEU B HD11 1 
ATOM   5893 H  HD12 . LEU B  1 166 ? -39.40900 -7.35400  7.99000   1.000 27.48846  ? 166 LEU B HD12 1 
ATOM   5894 H  HD13 . LEU B  1 166 ? -40.16100 -8.60500  7.36200   1.000 27.48846  ? 166 LEU B HD13 1 
ATOM   5895 H  HD21 . LEU B  1 166 ? -42.28500 -7.09600  6.10000   1.000 25.52177  ? 166 LEU B HD21 1 
ATOM   5896 H  HD22 . LEU B  1 166 ? -42.70900 -8.35600  6.96900   1.000 25.52177  ? 166 LEU B HD22 1 
ATOM   5897 H  HD23 . LEU B  1 166 ? -43.34600 -6.93300  7.27100   1.000 25.52177  ? 166 LEU B HD23 1 
ATOM   5898 N  N    . GLY B  1 167 ? -43.88200 -8.83100  11.51300  1.000 16.24822  ? 167 GLY B N    1 
ATOM   5899 C  CA   . GLY B  1 167 ? -44.03400 -9.54800  12.76300  1.000 16.31873  ? 167 GLY B CA   1 
ATOM   5900 C  C    . GLY B  1 167 ? -44.00400 -11.05000 12.56800  1.000 15.81553  ? 167 GLY B C    1 
ATOM   5901 O  O    . GLY B  1 167 ? -44.12500 -11.55700 11.45900  1.000 16.23684  ? 167 GLY B O    1 
ATOM   5902 H  H    . GLY B  1 167 ? -44.38900 -9.11800  10.88000  1.000 19.50042  ? 167 GLY B H    1 
ATOM   5903 H  HA2  . GLY B  1 167 ? -43.31400 -9.30200  13.36500  1.000 19.58504  ? 167 GLY B HA2  1 
ATOM   5904 H  HA3  . GLY B  1 167 ? -44.88200 -9.30900  13.17000  1.000 19.58504  ? 167 GLY B HA3  1 
ATOM   5905 N  N    . ALA B  1 168 ? -43.85700 -11.76800 13.70000  1.000 15.18048  ? 168 ALA B N    1 
ATOM   5906 C  CA   . ALA B  1 168 ? -43.89200 -13.22000 13.67800  1.000 15.34251  ? 168 ALA B CA   1 
ATOM   5907 C  C    . ALA B  1 168 ? -44.58400 -13.73900 14.93100  1.000 16.03254  ? 168 ALA B C    1 
ATOM   5908 O  O    . ALA B  1 168 ? -44.47200 -13.16100 16.02200  1.000 16.45407  ? 168 ALA B O    1 
ATOM   5909 C  CB   . ALA B  1 168 ? -42.50200 -13.85700 13.48100  1.000 17.50029  ? 168 ALA B CB   1 
ATOM   5910 H  H    . ALA B  1 168 ? -43.73600 -11.42600 14.48100  1.000 18.21914  ? 168 ALA B H    1 
ATOM   5911 H  HA   . ALA B  1 168 ? -44.42700 -13.50800 12.92200  1.000 18.41357  ? 168 ALA B HA   1 
ATOM   5912 H  HB1  . ALA B  1 168 ? -42.59700 -14.82200 13.46400  1.000 21.00290  ? 168 ALA B HB1  1 
ATOM   5913 H  HB2  . ALA B  1 168 ? -42.12900 -13.54700 12.64100  1.000 21.00290  ? 168 ALA B HB2  1 
ATOM   5914 H  HB3  . ALA B  1 168 ? -41.92700 -13.59300 14.21600  1.000 21.00290  ? 168 ALA B HB3  1 
ATOM   5915 N  N    . VAL B  1 169 ? -45.26100 -14.86900 14.75200  1.000 16.25512  ? 169 VAL B N    1 
ATOM   5916 C  CA   . VAL B  1 169 ? -45.96300 -15.60900 15.79500  1.000 15.77402  ? 169 VAL B CA   1 
ATOM   5917 C  C    . VAL B  1 169 ? -45.52200 -17.05500 15.66200  1.000 15.74913  ? 169 VAL B C    1 
ATOM   5918 O  O    . VAL B  1 169 ? -45.60800 -17.63000 14.57500  1.000 17.06768  ? 169 VAL B O    1 
ATOM   5919 C  CB   . VAL B  1 169 ? -47.48100 -15.53800 15.58100  1.000 15.19018  ? 169 VAL B CB   1 
ATOM   5920 C  CG1  . VAL B  1 169 ? -48.21000 -16.30900 16.68400  1.000 17.88084  ? 169 VAL B CG1  1 
ATOM   5921 C  CG2  . VAL B  1 169 ? -47.92500 -14.07800 15.53300  1.000 15.60499  ? 169 VAL B CG2  1 
ATOM   5922 H  H    . VAL B  1 169 ? -45.33200 -15.25100 13.98500  1.000 19.50870  ? 169 VAL B H    1 
ATOM   5923 H  HA   . VAL B  1 169 ? -45.74000 -15.26200 16.67300  1.000 18.93138  ? 169 VAL B HA   1 
ATOM   5924 H  HB   . VAL B  1 169 ? -47.71500 -15.95200 14.73500  1.000 18.23077  ? 169 VAL B HB   1 
ATOM   5925 H  HG11 . VAL B  1 169 ? -49.16500 -16.16200 16.59400  1.000 21.45957  ? 169 VAL B HG11 1 
ATOM   5926 H  HG12 . VAL B  1 169 ? -48.01200 -17.25400 16.59200  1.000 21.45957  ? 169 VAL B HG12 1 
ATOM   5927 H  HG13 . VAL B  1 169 ? -47.90600 -15.98900 17.54700  1.000 21.45957  ? 169 VAL B HG13 1 
ATOM   5928 H  HG21 . VAL B  1 169 ? -48.89400 -14.04300 15.49900  1.000 18.72855  ? 169 VAL B HG21 1 
ATOM   5929 H  HG22 . VAL B  1 169 ? -47.60600 -13.62500 16.33000  1.000 18.72855  ? 169 VAL B HG22 1 
ATOM   5930 H  HG23 . VAL B  1 169 ? -47.55100 -13.65900 14.74200  1.000 18.72855  ? 169 VAL B HG23 1 
ATOM   5931 N  N    . GLY B  1 170 ? -45.06900 -17.66200 16.74900  1.000 15.75422  ? 170 GLY B N    1 
ATOM   5932 C  CA   . GLY B  1 170 ? -44.55100 -19.00400 16.65100  1.000 17.06740  ? 170 GLY B CA   1 
ATOM   5933 C  C    . GLY B  1 170 ? -44.88800 -19.88500 17.82800  1.000 17.51534  ? 170 GLY B C    1 
ATOM   5934 O  O    . GLY B  1 170 ? -44.79300 -19.46000 18.98600  1.000 17.55332  ? 170 GLY B O    1 
ATOM   5935 H  H    . GLY B  1 170 ? -45.05300 -17.31900 17.53700  1.000 18.90763  ? 170 GLY B H    1 
ATOM   5936 H  HA2  . GLY B  1 170 ? -44.91200 -19.42200 15.85400  1.000 20.48345  ? 170 GLY B HA2  1 
ATOM   5937 H  HA3  . GLY B  1 170 ? -43.58500 -18.96300 16.57700  1.000 20.48345  ? 170 GLY B HA3  1 
ATOM   5938 N  N    . TRP B  1 171 ? -45.27000 -21.13000 17.53500  1.000 17.58304  ? 171 TRP B N    1 
ATOM   5939 C  CA   . TRP B  1 171 ? -45.62600 -22.12300 18.55200  1.000 17.57766  ? 171 TRP B CA   1 
ATOM   5940 C  C    . TRP B  1 171 ? -44.46000 -23.05000 18.82900  1.000 19.89819  ? 171 TRP B C    1 
ATOM   5941 O  O    . TRP B  1 171 ? -43.89100 -23.64900 17.90600  1.000 18.69393  ? 171 TRP B O    1 
ATOM   5942 C  CB   . TRP B  1 171 ? -46.85500 -22.92500 18.11900  1.000 21.00547  ? 171 TRP B CB   1 
ATOM   5943 C  CG   . TRP B  1 171 ? -47.19600 -24.10200 19.01200  1.000 19.40030  ? 171 TRP B CG   1 
ATOM   5944 C  CD1  . TRP B  1 171 ? -47.22500 -24.12600 20.37200  1.000 20.46292  ? 171 TRP B CD1  1 
ATOM   5945 C  CD2  . TRP B  1 171 ? -47.56300 -25.40700 18.58300  1.000 21.98853  ? 171 TRP B CD2  1 
ATOM   5946 N  NE1  . TRP B  1 171 ? -47.59100 -25.37600 20.81800  1.000 21.09235  ? 171 TRP B NE1  1 
ATOM   5947 C  CE2  . TRP B  1 171 ? -47.79600 -26.18400 19.73500  1.000 22.64297  ? 171 TRP B CE2  1 
ATOM   5948 C  CE3  . TRP B  1 171 ? -47.73200 -25.99800 17.32900  1.000 22.81962  ? 171 TRP B CE3  1 
ATOM   5949 C  CZ2  . TRP B  1 171 ? -48.20400 -27.51800 19.67000  1.000 26.41607  ? 171 TRP B CZ2  1 
ATOM   5950 C  CZ3  . TRP B  1 171 ? -48.12900 -27.31800 17.27000  1.000 25.62351  ? 171 TRP B CZ3  1 
ATOM   5951 C  CH2  . TRP B  1 171 ? -48.37200 -28.06200 18.42700  1.000 26.62924  ? 171 TRP B CH2  1 
ATOM   5952 H  H    . TRP B  1 171 ? -45.33200 -21.43200 16.73200  1.000 21.10221  ? 171 TRP B H    1 
ATOM   5953 H  HA   . TRP B  1 171 ? -45.83100 -21.66200 19.38100  1.000 21.09575  ? 171 TRP B HA   1 
ATOM   5954 H  HB2  . TRP B  1 171 ? -47.62300 -22.33200 18.11400  1.000 25.20913  ? 171 TRP B HB2  1 
ATOM   5955 H  HB3  . TRP B  1 171 ? -46.69700 -23.27200 17.22800  1.000 25.20913  ? 171 TRP B HB3  1 
ATOM   5956 H  HD1  . TRP B  1 171 ? -47.02600 -23.40200 20.92100  1.000 24.55807  ? 171 TRP B HD1  1 
ATOM   5957 H  HE1  . TRP B  1 171 ? -47.67600 -25.60900 21.64200  1.000 25.31338  ? 171 TRP B HE1  1 
ATOM   5958 H  HE3  . TRP B  1 171 ? -47.58200 -25.51200 16.55100  1.000 27.38611  ? 171 TRP B HE3  1 
ATOM   5959 H  HZ2  . TRP B  1 171 ? -48.35600 -28.01600 20.44100  1.000 31.70185  ? 171 TRP B HZ2  1 
ATOM   5960 H  HZ3  . TRP B  1 171 ? -48.23600 -27.72300 16.44000  1.000 30.75077  ? 171 TRP B HZ3  1 
ATOM   5961 H  HH2  . TRP B  1 171 ? -48.65400 -28.94400 18.35000  1.000 31.95765  ? 171 TRP B HH2  1 
ATOM   5962 N  N    . SER B  1 172 ? -44.09400 -23.14900 20.10400  1.000 18.12847  ? 172 SER B N    1 
ATOM   5963 C  CA   . SER B  1 172 ? -43.17700 -24.18600 20.56400  1.000 19.72750  ? 172 SER B CA   1 
ATOM   5964 C  C    . SER B  1 172 ? -41.82100 -23.98000 19.89200  1.000 19.80228  ? 172 SER B C    1 
ATOM   5965 O  O    . SER B  1 172 ? -41.27300 -22.87200 20.00200  1.000 19.88553  ? 172 SER B O    1 
ATOM   5966 C  CB   . SER B  1 172 ? -43.82800 -25.56600 20.43400  1.000 22.49190  ? 172 SER B CB   1 
ATOM   5967 O  OG   . SER B  1 172 ? -43.10300 -26.47400 21.27600  1.000 25.48402  ? 172 SER B OG   1 
ATOM   5968 H  H    . SER B  1 172 ? -44.36600 -22.62100 20.72600  1.000 21.75672  ? 172 SER B H    1 
ATOM   5969 H  HA   . SER B  1 172 ? -43.02600 -24.04200 21.51100  1.000 23.67556  ? 172 SER B HA   1 
ATOM   5970 H  HB2  . SER B  1 172 ? -44.75300 -25.52000 20.72200  1.000 26.99285  ? 172 SER B HB2  1 
ATOM   5971 H  HB3  . SER B  1 172 ? -43.78100 -25.86500 19.51300  1.000 26.99285  ? 172 SER B HB3  1 
ATOM   5972 H  HG   . SER B  1 172 ? -42.28300 -26.43900 21.09800  1.000 30.58338  ? 172 SER B HG   1 
ATOM   5973 N  N    . MET B  1 173 ? -41.24800 -24.96200 19.18300  1.000 19.35044  ? 173 MET B N    1 
ATOM   5974 C  CA   . MET B  1 173 ? -39.96500 -24.69600 18.53300  1.000 21.88466  ? 173 MET B CA   1 
ATOM   5975 C  C    . MET B  1 173 ? -40.08800 -23.51700 17.56500  1.000 21.44922  ? 173 MET B C    1 
ATOM   5976 O  O    . MET B  1 173 ? -39.11300 -22.80700 17.31100  1.000 20.24366  ? 173 MET B O    1 
ATOM   5977 C  CB   . MET B  1 173 ? -39.45800 -25.92600 17.80300  1.000 21.86719  ? 173 MET B CB   1 
ATOM   5978 C  CG   . MET B  1 173 ? -38.89600 -26.98200 18.69700  1.000 23.68834  ? 173 MET B CG   1 
ATOM   5979 S  SD   . MET B  1 173 ? -37.96200 -28.14200 17.72100  1.000 26.80164  ? 173 MET B SD   1 
ATOM   5980 C  CE   . MET B  1 173 ? -37.58400 -29.37400 18.96300  1.000 32.84391  ? 173 MET B CE   1 
ATOM   5981 H  H    . MET B  1 173 ? -41.56900 -25.75200 19.07000  1.000 23.22309  ? 173 MET B H    1 
ATOM   5982 H  HA   . MET B  1 173 ? -39.31000 -24.49000 19.21900  1.000 26.26416  ? 173 MET B HA   1 
ATOM   5983 H  HB2  . MET B  1 173 ? -40.19500 -26.32000 17.31000  1.000 26.24319  ? 173 MET B HB2  1 
ATOM   5984 H  HB3  . MET B  1 173 ? -38.75600 -25.65500 17.19000  1.000 26.24319  ? 173 MET B HB3  1 
ATOM   5985 H  HG2  . MET B  1 173 ? -38.30700 -26.57900 19.35400  1.000 28.42856  ? 173 MET B HG2  1 
ATOM   5986 H  HG3  . MET B  1 173 ? -39.61600 -27.45400 19.14300  1.000 28.42856  ? 173 MET B HG3  1 
ATOM   5987 H  HE1  . MET B  1 173 ? -37.01100 -30.05200 18.57200  1.000 39.41525  ? 173 MET B HE1  1 
ATOM   5988 H  HE2  . MET B  1 173 ? -37.12900 -28.94400 19.70500  1.000 39.41525  ? 173 MET B HE2  1 
ATOM   5989 H  HE3  . MET B  1 173 ? -38.41100 -29.77700 19.27100  1.000 39.41525  ? 173 MET B HE3  1 
ATOM   5990 N  N    . GLY B  1 174 ? -41.26900 -23.31900 16.97000  1.000 19.91087  ? 174 GLY B N    1 
ATOM   5991 C  CA   . GLY B  1 174 ? -41.46000 -22.13500 16.15000  1.000 18.36502  ? 174 GLY B CA   1 
ATOM   5992 C  C    . GLY B  1 174 ? -41.42800 -20.85700 16.95100  1.000 18.69894  ? 174 GLY B C    1 
ATOM   5993 O  O    . GLY B  1 174 ? -41.07400 -19.79300 16.42900  1.000 18.49192  ? 174 GLY B O    1 
ATOM   5994 H  H    . GLY B  1 174 ? -41.95000 -23.84100 17.02700  1.000 23.89560  ? 174 GLY B H    1 
ATOM   5995 H  HA2  . GLY B  1 174 ? -40.75900 -22.09200 15.48200  1.000 22.04058  ? 174 GLY B HA2  1 
ATOM   5996 H  HA3  . GLY B  1 174 ? -42.31900 -22.19200 15.70300  1.000 22.04058  ? 174 GLY B HA3  1 
ATOM   5997 N  N    . GLY B  1 175 ? -41.86200 -20.92600 18.20900  1.000 17.97731  ? 175 GLY B N    1 
ATOM   5998 C  CA   . GLY B  1 175 ? -41.68000 -19.81000 19.12000  1.000 16.39739  ? 175 GLY B CA   1 
ATOM   5999 C  C    . GLY B  1 175 ? -40.21600 -19.56500 19.46600  1.000 17.80840  ? 175 GLY B C    1 
ATOM   6000 O  O    . GLY B  1 175 ? -39.79300 -18.41400 19.54500  1.000 19.09217  ? 175 GLY B O    1 
ATOM   6001 H  H    . GLY B  1 175 ? -42.26100 -21.60400 18.55400  1.000 21.57533  ? 175 GLY B H    1 
ATOM   6002 H  HA2  . GLY B  1 175 ? -42.03500 -19.00400 18.71300  1.000 19.67944  ? 175 GLY B HA2  1 
ATOM   6003 H  HA3  . GLY B  1 175 ? -42.16200 -19.98700 19.94300  1.000 19.67944  ? 175 GLY B HA3  1 
ATOM   6004 N  N    . GLY B  1 176 ? -39.43700 -20.62600 19.64900  1.000 18.19044  ? 176 GLY B N    1 
ATOM   6005 C  CA   . GLY B  1 176 ? -37.98800 -20.44900 19.74600  1.000 19.65079  ? 176 GLY B CA   1 
ATOM   6006 C  C    . GLY B  1 176 ? -37.43700 -19.75000 18.51600  1.000 18.87738  ? 176 GLY B C    1 
ATOM   6007 O  O    . GLY B  1 176 ? -36.63600 -18.82500 18.62300  1.000 18.99438  ? 176 GLY B O    1 
ATOM   6008 H  H    . GLY B  1 176 ? -39.71100 -21.43800 19.71800  1.000 21.83110  ? 176 GLY B H    1 
ATOM   6009 H  HA2  . GLY B  1 176 ? -37.77700 -19.91500 20.52800  1.000 23.58351  ? 176 GLY B HA2  1 
ATOM   6010 H  HA3  . GLY B  1 176 ? -37.55900 -21.31500 19.83000  1.000 23.58351  ? 176 GLY B HA3  1 
ATOM   6011 N  N    . GLY B  1 177 ? -37.88300 -20.16000 17.32300  1.000 18.46737  ? 177 GLY B N    1 
ATOM   6012 C  CA   . GLY B  1 177 ? -37.40200 -19.50300 16.12600  1.000 18.95847  ? 177 GLY B CA   1 
ATOM   6013 C  C    . GLY B  1 177 ? -37.79800 -18.04400 16.04200  1.000 17.05594  ? 177 GLY B C    1 
ATOM   6014 O  O    . GLY B  1 177 ? -37.01600 -17.20100 15.55900  1.000 18.70212  ? 177 GLY B O    1 
ATOM   6015 H  H    . GLY B  1 177 ? -38.44700 -20.79600 17.19300  1.000 22.16341  ? 177 GLY B H    1 
ATOM   6016 H  HA2  . GLY B  1 177 ? -36.43400 -19.55400 16.10300  1.000 22.75272  ? 177 GLY B HA2  1 
ATOM   6017 H  HA3  . GLY B  1 177 ? -37.76100 -19.95800 15.34800  1.000 22.75272  ? 177 GLY B HA3  1 
ATOM   6018 N  N    . THR B  1 178 ? -39.02200 -17.74200 16.47200  1.000 17.77168  ? 178 THR B N    1 
ATOM   6019 C  CA   . THR B  1 178 ? -39.51800 -16.37300 16.51500  1.000 17.58234  ? 178 THR B CA   1 
ATOM   6020 C  C    . THR B  1 178 ? -38.67400 -15.51100 17.45500  1.000 17.51495  ? 178 THR B C    1 
ATOM   6021 O  O    . THR B  1 178 ? -38.30300 -14.37700 17.11600  1.000 17.73129  ? 178 THR B O    1 
ATOM   6022 C  CB   . THR B  1 178 ? -40.99900 -16.37600 16.92300  1.000 17.44549  ? 178 THR B CB   1 
ATOM   6023 O  OG1  . THR B  1 178 ? -41.78700 -16.96500 15.88200  1.000 17.71730  ? 178 THR B OG1  1 
ATOM   6024 C  CG2  . THR B  1 178 ? -41.51700 -14.97100 17.12600  1.000 17.85755  ? 178 THR B CG2  1 
ATOM   6025 H  H    . THR B  1 178 ? -39.59400 -18.32200 16.74800  1.000 21.32857  ? 178 THR B H    1 
ATOM   6026 H  HA   . THR B  1 178 ? -39.45600 -15.97900 15.63100  1.000 21.10137  ? 178 THR B HA   1 
ATOM   6027 H  HB   . THR B  1 178 ? -41.08200 -16.87400 17.75100  1.000 20.93715  ? 178 THR B HB   1 
ATOM   6028 H  HG1  . THR B  1 178 ? -41.65400 -17.79400 15.85600  1.000 21.26332  ? 178 THR B HG1  1 
ATOM   6029 H  HG21 . THR B  1 178 ? -42.47800 -14.98700 17.25800  1.000 21.43162  ? 178 THR B HG21 1 
ATOM   6030 H  HG22 . THR B  1 178 ? -41.09900 -14.57300 17.90600  1.000 21.43162  ? 178 THR B HG22 1 
ATOM   6031 H  HG23 . THR B  1 178 ? -41.31500 -14.42700 16.34900  1.000 21.43162  ? 178 THR B HG23 1 
ATOM   6032 N  N    . LEU B  1 179 ? -38.42400 -16.00100 18.67500  1.000 18.17933  ? 179 LEU B N    1 
ATOM   6033 C  CA   . LEU B  1 179 ? -37.59900 -15.24300 19.60400  1.000 18.47134  ? 179 LEU B CA   1 
ATOM   6034 C  C    . LEU B  1 179 ? -36.16400 -15.09900 19.10200  1.000 18.49035  ? 179 LEU B C    1 
ATOM   6035 O  O    . LEU B  1 179 ? -35.55400 -14.04500 19.30600  1.000 19.65848  ? 179 LEU B O    1 
ATOM   6036 C  CB   . LEU B  1 179 ? -37.60400 -15.95200 20.96400  1.000 18.51494  ? 179 LEU B CB   1 
ATOM   6037 C  CG   . LEU B  1 179 ? -38.96900 -15.97300 21.65100  1.000 19.33110  ? 179 LEU B CG   1 
ATOM   6038 C  CD1  . LEU B  1 179 ? -38.95700 -16.85200 22.90200  1.000 21.27435  ? 179 LEU B CD1  1 
ATOM   6039 C  CD2  . LEU B  1 179 ? -39.41400 -14.55400 22.03200  1.000 24.08443  ? 179 LEU B CD2  1 
ATOM   6040 H  H    . LEU B  1 179 ? -38.71500 -16.75200 18.97600  1.000 21.81776  ? 179 LEU B H    1 
ATOM   6041 H  HA   . LEU B  1 179 ? -37.96800 -14.35200 19.70600  1.000 22.16816  ? 179 LEU B HA   1 
ATOM   6042 H  HB2  . LEU B  1 179 ? -37.32400 -16.87200 20.83500  1.000 22.22049  ? 179 LEU B HB2  1 
ATOM   6043 H  HB3  . LEU B  1 179 ? -36.98300 -15.49600 21.55300  1.000 22.22049  ? 179 LEU B HB3  1 
ATOM   6044 H  HG   . LEU B  1 179 ? -39.60500 -16.34600 21.02100  1.000 23.19988  ? 179 LEU B HG   1 
ATOM   6045 H  HD11 . LEU B  1 179 ? -39.84700 -16.86200 23.28900  1.000 25.53178  ? 179 LEU B HD11 1 
ATOM   6046 H  HD12 . LEU B  1 179 ? -38.69400 -17.75200 22.65400  1.000 25.53178  ? 179 LEU B HD12 1 
ATOM   6047 H  HD13 . LEU B  1 179 ? -38.32400 -16.48600 23.53900  1.000 25.53178  ? 179 LEU B HD13 1 
ATOM   6048 H  HD21 . LEU B  1 179 ? -40.22900 -14.60900 22.55400  1.000 28.90388  ? 179 LEU B HD21 1 
ATOM   6049 H  HD22 . LEU B  1 179 ? -38.71300 -14.13400 22.55500  1.000 28.90388  ? 179 LEU B HD22 1 
ATOM   6050 H  HD23 . LEU B  1 179 ? -39.57300 -14.04500 21.22200  1.000 28.90388  ? 179 LEU B HD23 1 
ATOM   6051 N  N    . ARG B  1 180 ? -35.64300 -16.11200 18.41400  1.000 18.61627  ? 180 ARG B N    1 
ATOM   6052 C  CA   . ARG B  1 180 ? -34.33700 -15.99400 17.77800  1.000 20.16648  ? 180 ARG B CA   1 
ATOM   6053 C  C    . ARG B  1 180 ? -34.32100 -14.89000 16.73400  1.000 20.34638  ? 180 ARG B C    1 
ATOM   6054 O  O    . ARG B  1 180 ? -33.35100 -14.13800 16.62000  1.000 22.06859  ? 180 ARG B O    1 
ATOM   6055 C  CB   . ARG B  1 180 ? -33.94400 -17.32800 17.16100  1.000 19.11849  ? 180 ARG B CB   1 
ATOM   6056 C  CG   . ARG B  1 180 ? -33.58600 -18.35900 18.21500  1.000 19.34267  ? 180 ARG B CG   1 
ATOM   6057 C  CD   . ARG B  1 180 ? -33.42800 -19.73800 17.59700  1.000 20.83580  ? 180 ARG B CD   1 
ATOM   6058 N  NE   . ARG B  1 180 ? -32.90600 -20.73200 18.52900  1.000 21.72570  ? 180 ARG B NE   1 
ATOM   6059 C  CZ   . ARG B  1 180 ? -31.62300 -20.93800 18.75500  1.000 23.12796  ? 180 ARG B CZ   1 
ATOM   6060 N  NH1  . ARG B  1 180 ? -30.69300 -20.28200 18.07700  1.000 24.12205  ? 180 ARG B NH1  1 
ATOM   6061 N  NH2  . ARG B  1 180 ? -31.26400 -21.85100 19.66000  1.000 24.50145  ? 180 ARG B NH2  1 
ATOM   6062 H  H    . ARG B  1 180 ? -36.02400 -16.87400 18.30100  1.000 22.34209  ? 180 ARG B H    1 
ATOM   6063 H  HA   . ARG B  1 180 ? -33.68000 -15.76600 18.45400  1.000 24.20234  ? 180 ARG B HA   1 
ATOM   6064 H  HB2  . ARG B  1 180 ? -34.68900 -17.67000 16.64200  1.000 22.94475  ? 180 ARG B HB2  1 
ATOM   6065 H  HB3  . ARG B  1 180 ? -33.17300 -17.19800 16.58800  1.000 22.94475  ? 180 ARG B HB3  1 
ATOM   6066 H  HG2  . ARG B  1 180 ? -32.74700 -18.11400 18.63500  1.000 23.21377  ? 180 ARG B HG2  1 
ATOM   6067 H  HG3  . ARG B  1 180 ? -34.29000 -18.40000 18.88000  1.000 23.21377  ? 180 ARG B HG3  1 
ATOM   6068 H  HD2  . ARG B  1 180 ? -34.29600 -20.04500 17.28900  1.000 25.00553  ? 180 ARG B HD2  1 
ATOM   6069 H  HD3  . ARG B  1 180 ? -32.81300 -19.67900 16.85000  1.000 25.00553  ? 180 ARG B HD3  1 
ATOM   6070 H  HE   . ARG B  1 180 ? -33.47200 -21.21500 18.96000  1.000 26.07340  ? 180 ARG B HE   1 
ATOM   6071 H  HH11 . ARG B  1 180 ? -30.92200 -19.70900 17.47800  1.000 28.94902  ? 180 ARG B HH11 1 
ATOM   6072 H  HH12 . ARG B  1 180 ? -29.86100 -20.42800 18.23700  1.000 28.94902  ? 180 ARG B HH12 1 
ATOM   6073 H  HH21 . ARG B  1 180 ? -31.86500 -22.29500 20.08600  1.000 29.40431  ? 180 ARG B HH21 1 
ATOM   6074 H  HH22 . ARG B  1 180 ? -30.43100 -21.99600 19.81800  1.000 29.40431  ? 180 ARG B HH22 1 
ATOM   6075 N  N    . LEU B  1 181 ? -35.37900 -14.78800 15.92900  1.000 19.61127  ? 181 LEU B N    1 
ATOM   6076 C  CA   . LEU B  1 181 ? -35.38500 -13.74400 14.90600  1.000 18.81365  ? 181 LEU B CA   1 
ATOM   6077 C  C    . LEU B  1 181 ? -35.54700 -12.37200 15.54800  1.000 19.26610  ? 181 LEU B C    1 
ATOM   6078 O  O    . LEU B  1 181 ? -34.92100 -11.40400 15.10300  1.000 21.55123  ? 181 LEU B O    1 
ATOM   6079 C  CB   . LEU B  1 181 ? -36.51900 -14.03300 13.90900  1.000 19.16394  ? 181 LEU B CB   1 
ATOM   6080 C  CG   . LEU B  1 181 ? -36.53600 -13.10900 12.68900  1.000 19.37592  ? 181 LEU B CG   1 
ATOM   6081 C  CD1  . LEU B  1 181 ? -35.28500 -13.16800 11.87700  1.000 20.93672  ? 181 LEU B CD1  1 
ATOM   6082 C  CD2  . LEU B  1 181 ? -37.76800 -13.43600 11.78100  1.000 20.25723  ? 181 LEU B CD2  1 
ATOM   6083 H  H    . LEU B  1 181 ? -36.07800 -15.28900 15.95300  1.000 23.53608  ? 181 LEU B H    1 
ATOM   6084 H  HA   . LEU B  1 181 ? -34.54700 -13.74400 14.41800  1.000 22.57895  ? 181 LEU B HA   1 
ATOM   6085 H  HB2  . LEU B  1 181 ? -36.42300 -14.94300 13.58900  1.000 22.99929  ? 181 LEU B HB2  1 
ATOM   6086 H  HB3  . LEU B  1 181 ? -37.36700 -13.93000 14.36800  1.000 22.99929  ? 181 LEU B HB3  1 
ATOM   6087 H  HG   . LEU B  1 181 ? -36.60200 -12.20200 13.02600  1.000 23.25366  ? 181 LEU B HG   1 
ATOM   6088 H  HD11 . LEU B  1 181 ? -35.41600 -12.66200 11.05900  1.000 25.12663  ? 181 LEU B HD11 1 
ATOM   6089 H  HD12 . LEU B  1 181 ? -34.55700 -12.78400 12.39000  1.000 25.12663  ? 181 LEU B HD12 1 
ATOM   6090 H  HD13 . LEU B  1 181 ? -35.08900 -14.09400 11.66500  1.000 25.12663  ? 181 LEU B HD13 1 
ATOM   6091 H  HD21 . LEU B  1 181 ? -37.78900 -12.81100 11.04000  1.000 24.31124  ? 181 LEU B HD21 1 
ATOM   6092 H  HD22 . LEU B  1 181 ? -37.68100 -14.34300 11.44600  1.000 24.31124  ? 181 LEU B HD22 1 
ATOM   6093 H  HD23 . LEU B  1 181 ? -38.57800 -13.35400 12.30700  1.000 24.31124  ? 181 LEU B HD23 1 
ATOM   6094 N  N    . ALA B  1 182 ? -36.33300 -12.29000 16.62000  1.000 18.89228  ? 182 ALA B N    1 
ATOM   6095 C  CA   . ALA B  1 182 ? -36.41500 -11.05100 17.41000  1.000 19.65856  ? 182 ALA B CA   1 
ATOM   6096 C  C    . ALA B  1 182 ? -35.04200 -10.64100 17.95500  1.000 21.57541  ? 182 ALA B C    1 
ATOM   6097 O  O    . ALA B  1 182 ? -34.64800 -9.47100  17.87300  1.000 24.12284  ? 182 ALA B O    1 
ATOM   6098 C  CB   . ALA B  1 182 ? -37.41900 -11.21800 18.55100  1.000 20.48024  ? 182 ALA B CB   1 
ATOM   6099 H  H    . ALA B  1 182 ? -36.82900 -12.92900 16.91300  1.000 22.67330  ? 182 ALA B H    1 
ATOM   6100 H  HA   . ALA B  1 182 ? -36.73100 -10.33800 16.83400  1.000 23.59283  ? 182 ALA B HA   1 
ATOM   6101 H  HB1  . ALA B  1 182 ? -37.41600 -10.41500 19.09400  1.000 24.57885  ? 182 ALA B HB1  1 
ATOM   6102 H  HB2  . ALA B  1 182 ? -38.30200 -11.36100 18.17500  1.000 24.57885  ? 182 ALA B HB2  1 
ATOM   6103 H  HB3  . ALA B  1 182 ? -37.16100 -11.98300 19.08900  1.000 24.57885  ? 182 ALA B HB3  1 
ATOM   6104 N  N    . ALA B  1 183 ? -34.26300 -11.60200 18.43900  1.000 19.76991  ? 183 ALA B N    1 
ATOM   6105 C  CA   . ALA B  1 183 ? -32.95100 -11.26700 18.98600  1.000 21.97018  ? 183 ALA B CA   1 
ATOM   6106 C  C    . ALA B  1 183 ? -32.00800 -10.73900 17.90500  1.000 25.64857  ? 183 ALA B C    1 
ATOM   6107 O  O    . ALA B  1 183 ? -31.07600 -9.97800  18.20200  1.000 27.99839  ? 183 ALA B O    1 
ATOM   6108 C  CB   . ALA B  1 183 ? -32.38600 -12.52900 19.62400  1.000 22.91608  ? 183 ALA B CB   1 
ATOM   6109 H  H    . ALA B  1 183 ? -34.46300 -12.43800 18.46300  1.000 23.72645  ? 183 ALA B H    1 
ATOM   6110 H  HA   . ALA B  1 183 ? -33.02900 -10.57000 19.65600  1.000 26.36678  ? 183 ALA B HA   1 
ATOM   6111 H  HB1  . ALA B  1 183 ? -31.52500 -12.32300 20.02100  1.000 27.50185  ? 183 ALA B HB1  1 
ATOM   6112 H  HB2  . ALA B  1 183 ? -33.00000 -12.83900 20.30800  1.000 27.50185  ? 183 ALA B HB2  1 
ATOM   6113 H  HB3  . ALA B  1 183 ? -32.28100 -13.20900 18.94000  1.000 27.50185  ? 183 ALA B HB3  1 
ATOM   6114 N  N    . ASP B  1 184 ? -32.22800 -11.13000 16.65300  1.000 22.88093  ? 184 ASP B N    1 
ATOM   6115 C  CA   . ASP B  1 184 ? -31.45100 -10.65000 15.50900  1.000 24.15234  ? 184 ASP B CA   1 
ATOM   6116 C  C    . ASP B  1 184 ? -32.03100 -9.38100  14.86600  1.000 27.10210  ? 184 ASP B C    1 
ATOM   6117 O  O    . ASP B  1 184 ? -31.58500 -8.97900  13.77500  1.000 28.72424  ? 184 ASP B O    1 
ATOM   6118 C  CB   . ASP B  1 184 ? -31.39300 -11.75300 14.43600  1.000 25.09362  ? 184 ASP B CB   1 
ATOM   6119 C  CG   . ASP B  1 184 ? -30.37300 -12.81800 14.75000  1.000 32.43922  ? 184 ASP B CG   1 
ATOM   6120 O  OD1  . ASP B  1 184 ? -29.52100 -12.56900 15.61500  1.000 36.91699  ? 184 ASP B OD1  1 
ATOM   6121 O  OD2  . ASP B  1 184 ? -30.43500 -13.89700 14.12800  1.000 29.47294  ? 184 ASP B OD2  1 
ATOM   6122 H  H    . ASP B  1 184 ? -32.84100 -11.69100 16.43100  1.000 27.45968  ? 184 ASP B H    1 
ATOM   6123 H  HA   . ASP B  1 184 ? -30.55500 -10.44600 15.82000  1.000 28.98538  ? 184 ASP B HA   1 
ATOM   6124 H  HB2  . ASP B  1 184 ? -32.26300 -12.17900 14.37400  1.000 30.11491  ? 184 ASP B HB2  1 
ATOM   6125 H  HB3  . ASP B  1 184 ? -31.15800 -11.35300 13.58400  1.000 30.11491  ? 184 ASP B HB3  1 
ATOM   6126 N  N    . ASP B  1 185 ? -33.02000 -8.74900  15.49100  1.000 26.54989  ? 185 ASP B N    1 
ATOM   6127 C  CA   . ASP B  1 185 ? -33.64000 -7.52500  14.96500  1.000 29.67652  ? 185 ASP B CA   1 
ATOM   6128 C  C    . ASP B  1 185 ? -34.32800 -7.75300  13.62900  1.000 26.48339  ? 185 ASP B C    1 
ATOM   6129 O  O    . ASP B  1 185 ? -34.41300 -6.85600  12.80400  1.000 27.97415  ? 185 ASP B O    1 
ATOM   6130 C  CB   . ASP B  1 185 ? -32.62800 -6.38900  14.87300  1.000 29.30425  ? 185 ASP B CB   1 
ATOM   6131 C  CG   . ASP B  1 185 ? -31.81200 -6.23600  16.14200  1.000 60.44903  ? 185 ASP B CG   1 
ATOM   6132 O  OD1  . ASP B  1 185 ? -32.36700 -6.49300  17.23000  1.000 62.63491  ? 185 ASP B OD1  1 
ATOM   6133 O  OD2  . ASP B  1 185 ? -30.61800 -5.87600  16.05400  1.000 76.97721  ? 185 ASP B OD2  1 
ATOM   6134 H  H    . ASP B  1 185 ? -33.35900 -9.01100  16.23700  1.000 31.86243  ? 185 ASP B H    1 
ATOM   6135 H  HA   . ASP B  1 185 ? -34.33300 -7.25300  15.58700  1.000 35.61438  ? 185 ASP B HA   1 
ATOM   6136 H  HB2  . ASP B  1 185 ? -32.01600 -6.56700  14.14200  1.000 35.16767  ? 185 ASP B HB2  1 
ATOM   6137 H  HB3  . ASP B  1 185 ? -33.09900 -5.55600  14.71600  1.000 35.16767  ? 185 ASP B HB3  1 
ATOM   6138 N  N    . GLY B  1 186 ? -34.86500 -8.93600  13.41700  1.000 22.05533  ? 186 GLY B N    1 
ATOM   6139 C  CA   . GLY B  1 186 ? -35.45300 -9.26500  12.14000  1.000 23.41281  ? 186 GLY B CA   1 
ATOM   6140 C  C    . GLY B  1 186 ? -36.92300 -9.02400  12.03700  1.000 21.35903  ? 186 GLY B C    1 
ATOM   6141 O  O    . GLY B  1 186 ? -37.50100 -9.28800  10.98400  1.000 24.74750  ? 186 GLY B O    1 
ATOM   6142 H  H    . GLY B  1 186 ? -34.90000 -9.56700  14.00100  1.000 26.46895  ? 186 GLY B H    1 
ATOM   6143 H  HA2  . GLY B  1 186 ? -35.01800 -8.73500  11.45300  1.000 28.09793  ? 186 GLY B HA2  1 
ATOM   6144 H  HA3  . GLY B  1 186 ? -35.29500 -10.20500 11.95900  1.000 28.09793  ? 186 GLY B HA3  1 
ATOM   6145 N  N    . ILE B  1 187 ? -37.55800 -8.53500  13.10800  1.000 20.18021  ? 187 ILE B N    1 
ATOM   6146 C  CA   . ILE B  1 187 ? -38.99000 -8.29400  13.18500  1.000 18.12122  ? 187 ILE B CA   1 
ATOM   6147 C  C    . ILE B  1 187 ? -39.22700 -7.13800  14.15500  1.000 19.09281  ? 187 ILE B C    1 
ATOM   6148 O  O    . ILE B  1 187 ? -38.40100 -6.84600  15.04100  1.000 20.08614  ? 187 ILE B O    1 
ATOM   6149 C  CB   . ILE B  1 187 ? -39.79800 -9.54100  13.61400  1.000 19.24911  ? 187 ILE B CB   1 
ATOM   6150 C  CG1  . ILE B  1 187 ? -39.09600 -10.32500 14.71600  1.000 19.18172  ? 187 ILE B CG1  1 
ATOM   6151 C  CG2  . ILE B  1 187 ? -40.12700 -10.44900 12.40300  1.000 21.61908  ? 187 ILE B CG2  1 
ATOM   6152 C  CD1  . ILE B  1 187 ? -39.88100 -11.50100 15.21100  1.000 19.42980  ? 187 ILE B CD1  1 
ATOM   6153 H  H    . ILE B  1 187 ? -37.15400 -8.32600  13.83800  1.000 24.21882  ? 187 ILE B H    1 
ATOM   6154 H  HA   . ILE B  1 187 ? -39.30800 -8.03600  12.30600  1.000 21.74803  ? 187 ILE B HA   1 
ATOM   6155 H  HB   . ILE B  1 187 ? -40.63600 -9.21600  13.97900  1.000 23.10149  ? 187 ILE B HB   1 
ATOM   6156 H  HG12 . ILE B  1 187 ? -38.25100 -10.65600 14.37300  1.000 23.02062  ? 187 ILE B HG12 1 
ATOM   6157 H  HG13 . ILE B  1 187 ? -38.94000 -9.73400  15.46900  1.000 23.02062  ? 187 ILE B HG13 1 
ATOM   6158 H  HG21 . ILE B  1 187 ? -40.71200 -11.16500 12.69500  1.000 25.94546  ? 187 ILE B HG21 1 
ATOM   6159 H  HG22 . ILE B  1 187 ? -40.56800 -9.91900  11.72100  1.000 25.94546  ? 187 ILE B HG22 1 
ATOM   6160 H  HG23 . ILE B  1 187 ? -39.30200 -10.81800 12.05200  1.000 25.94546  ? 187 ILE B HG23 1 
ATOM   6161 H  HD11 . ILE B  1 187 ? -39.46400 -11.84300 16.01700  1.000 23.31832  ? 187 ILE B HD11 1 
ATOM   6162 H  HD12 . ILE B  1 187 ? -40.78800 -11.21700 15.40300  1.000 23.31832  ? 187 ILE B HD12 1 
ATOM   6163 H  HD13 . ILE B  1 187 ? -39.88800 -12.18800 14.52600  1.000 23.31832  ? 187 ILE B HD13 1 
ATOM   6164 N  N    . GLN B  1 188 ? -40.38000 -6.49400  13.99700  1.000 17.18831  ? 188 GLN B N    1 
ATOM   6165 C  CA   . GLN B  1 188 ? -40.80200 -5.35200  14.77500  1.000 18.34195  ? 188 GLN B CA   1 
ATOM   6166 C  C    . GLN B  1 188 ? -41.79600 -5.72200  15.87300  1.000 18.43469  ? 188 GLN B C    1 
ATOM   6167 O  O    . GLN B  1 188 ? -42.10600 -4.87400  16.72500  1.000 19.39272  ? 188 GLN B O    1 
ATOM   6168 C  CB   . GLN B  1 188 ? -41.41700 -4.29000  13.84700  1.000 21.20405  ? 188 GLN B CB   1 
ATOM   6169 C  CG   . GLN B  1 188 ? -40.35200 -3.54000  13.00700  1.000 21.65782  ? 188 GLN B CG   1 
ATOM   6170 C  CD   . GLN B  1 188 ? -39.63200 -4.41600  12.01200  1.000 22.40680  ? 188 GLN B CD   1 
ATOM   6171 O  OE1  . GLN B  1 188 ? -40.24000 -4.97000  11.10300  1.000 20.46243  ? 188 GLN B OE1  1 
ATOM   6172 N  NE2  . GLN B  1 188 ? -38.32000 -4.51200  12.13800  1.000 24.63188  ? 188 GLN B NE2  1 
ATOM   6173 H  H    . GLN B  1 188 ? -40.96500 -6.72000  13.40800  1.000 20.62853  ? 188 GLN B H    1 
ATOM   6174 H  HA   . GLN B  1 188 ? -40.03100 -4.95200  15.20500  1.000 22.01290  ? 188 GLN B HA   1 
ATOM   6175 H  HB2  . GLN B  1 188 ? -42.03200 -4.72400  13.23500  1.000 25.44742  ? 188 GLN B HB2  1 
ATOM   6176 H  HB3  . GLN B  1 188 ? -41.89100 -3.63700  14.38500  1.000 25.44742  ? 188 GLN B HB3  1 
ATOM   6177 H  HG2  . GLN B  1 188 ? -40.78900 -2.82900  12.51200  1.000 25.99195  ? 188 GLN B HG2  1 
ATOM   6178 H  HG3  . GLN B  1 188 ? -39.68800 -3.16700  13.60700  1.000 25.99195  ? 188 GLN B HG3  1 
ATOM   6179 H  HE21 . GLN B  1 188 ? -37.91600 -4.08500  12.76600  1.000 29.56082  ? 188 GLN B HE21 1 
ATOM   6180 H  HE22 . GLN B  1 188 ? -37.87000 -5.00100  11.59200  1.000 29.56082  ? 188 GLN B HE22 1 
ATOM   6181 N  N    . ALA B  1 189 ? -42.27700 -6.96800  15.88800  1.000 16.57986  ? 189 ALA B N    1 
ATOM   6182 C  CA   . ALA B  1 189 ? -43.08200 -7.47600  16.98800  1.000 15.71889  ? 189 ALA B CA   1 
ATOM   6183 C  C    . ALA B  1 189 ? -43.03300 -8.99300  16.93400  1.000 15.45808  ? 189 ALA B C    1 
ATOM   6184 O  O    . ALA B  1 189 ? -42.96100 -9.58600  15.85400  1.000 16.82094  ? 189 ALA B O    1 
ATOM   6185 C  CB   . ALA B  1 189 ? -44.53500 -7.01500  16.92700  1.000 16.48182  ? 189 ALA B CB   1 
ATOM   6186 H  H    . ALA B  1 189 ? -42.14700 -7.54300  15.26200  1.000 19.89839  ? 189 ALA B H    1 
ATOM   6187 H  HA   . ALA B  1 189 ? -42.70700 -7.15600  17.82400  1.000 18.86523  ? 189 ALA B HA   1 
ATOM   6188 H  HB1  . ALA B  1 189 ? -45.00200 -7.33700  17.71400  1.000 19.78075  ? 189 ALA B HB1  1 
ATOM   6189 H  HB2  . ALA B  1 189 ? -44.55800 -6.04500  16.90300  1.000 19.78075  ? 189 ALA B HB2  1 
ATOM   6190 H  HB3  . ALA B  1 189 ? -44.94700 -7.37600  16.12600  1.000 19.78075  ? 189 ALA B HB3  1 
ATOM   6191 N  N    . ALA B  1 190 ? -43.07600 -9.60900  18.11800  1.000 15.86158  ? 190 ALA B N    1 
ATOM   6192 C  CA   . ALA B  1 190 ? -42.97600 -11.05500 18.22800  1.000 14.58815  ? 190 ALA B CA   1 
ATOM   6193 C  C    . ALA B  1 190 ? -43.99500 -11.56800 19.21500  1.000 15.67705  ? 190 ALA B C    1 
ATOM   6194 O  O    . ALA B  1 190 ? -44.21100 -10.94600 20.27200  1.000 17.41723  ? 190 ALA B O    1 
ATOM   6195 C  CB   . ALA B  1 190 ? -41.59700 -11.47700 18.71400  1.000 17.96682  ? 190 ALA B CB   1 
ATOM   6196 H  H    . ALA B  1 190 ? -43.16300 -9.20500  18.87200  1.000 19.03645  ? 190 ALA B H    1 
ATOM   6197 H  HA   . ALA B  1 190 ? -43.15300 -11.44400 17.35700  1.000 17.50834  ? 190 ALA B HA   1 
ATOM   6198 H  HB1  . ALA B  1 190 ? -41.59300 -12.43600 18.85900  1.000 21.56274  ? 190 ALA B HB1  1 
ATOM   6199 H  HB2  . ALA B  1 190 ? -40.93900 -11.24200 18.04100  1.000 21.56274  ? 190 ALA B HB2  1 
ATOM   6200 H  HB3  . ALA B  1 190 ? -41.40000 -11.01600 19.54400  1.000 21.56274  ? 190 ALA B HB3  1 
ATOM   6201 N  N    . ILE B  1 191 ? -44.61100 -12.70500 18.89000  1.000 15.53370  ? 191 ILE B N    1 
ATOM   6202 C  CA   . ILE B  1 191 ? -45.47800 -13.42500 19.82300  1.000 15.90387  ? 191 ILE B CA   1 
ATOM   6203 C  C    . ILE B  1 191 ? -44.99900 -14.86500 19.91300  1.000 16.23826  ? 191 ILE B C    1 
ATOM   6204 O  O    . ILE B  1 191 ? -44.87900 -15.55100 18.88900  1.000 16.82224  ? 191 ILE B O    1 
ATOM   6205 C  CB   . ILE B  1 191 ? -46.95900 -13.38500 19.41400  1.000 15.50958  ? 191 ILE B CB   1 
ATOM   6206 C  CG1  . ILE B  1 191 ? -47.46800 -11.93900 19.37100  1.000 15.96537  ? 191 ILE B CG1  1 
ATOM   6207 C  CG2  . ILE B  1 191 ? -47.77600 -14.25900 20.36900  1.000 17.02088  ? 191 ILE B CG2  1 
ATOM   6208 C  CD1  . ILE B  1 191 ? -48.94800 -11.80600 18.92100  1.000 16.96173  ? 191 ILE B CD1  1 
ATOM   6209 H  H    . ILE B  1 191 ? -44.54000 -13.08400 18.12100  1.000 18.64300  ? 191 ILE B H    1 
ATOM   6210 H  HA   . ILE B  1 191 ? -45.39700 -13.01100 20.69600  1.000 19.08720  ? 191 ILE B HA   1 
ATOM   6211 H  HB   . ILE B  1 191 ? -47.05700 -13.74300 18.51800  1.000 18.61406  ? 191 ILE B HB   1 
ATOM   6212 H  HG12 . ILE B  1 191 ? -47.39400 -11.55700 20.26000  1.000 19.16101  ? 191 ILE B HG12 1 
ATOM   6213 H  HG13 . ILE B  1 191 ? -46.92300 -11.43500 18.74700  1.000 19.16101  ? 191 ILE B HG13 1 
ATOM   6214 H  HG21 . ILE B  1 191 ? -48.71800 -14.16200 20.15800  1.000 20.42761  ? 191 ILE B HG21 1 
ATOM   6215 H  HG22 . ILE B  1 191 ? -47.50700 -15.18400 20.25900  1.000 20.42761  ? 191 ILE B HG22 1 
ATOM   6216 H  HG23 . ILE B  1 191 ? -47.61000 -13.97200 21.28000  1.000 20.42761  ? 191 ILE B HG23 1 
ATOM   6217 H  HD11 . ILE B  1 191 ? -49.13500 -10.87600 18.72000  1.000 20.35663  ? 191 ILE B HD11 1 
ATOM   6218 H  HD12 . ILE B  1 191 ? -49.08800 -12.35000 18.13000  1.000 20.35663  ? 191 ILE B HD12 1 
ATOM   6219 H  HD13 . ILE B  1 191 ? -49.52500 -12.11100 19.63900  1.000 20.35663  ? 191 ILE B HD13 1 
ATOM   6220 N  N    . GLY B  1 192 ? -44.72700 -15.34100 21.12700  1.000 16.36318  ? 192 GLY B N    1 
ATOM   6221 C  CA   . GLY B  1 192 ? -44.39300 -16.73300 21.34400  1.000 16.34277  ? 192 GLY B CA   1 
ATOM   6222 C  C    . GLY B  1 192 ? -45.57900 -17.46200 21.95200  1.000 17.09247  ? 192 GLY B C    1 
ATOM   6223 O  O    . GLY B  1 192 ? -46.16200 -17.00100 22.93200  1.000 18.65098  ? 192 GLY B O    1 
ATOM   6224 H  H    . GLY B  1 192 ? -44.73100 -14.86600 21.84400  1.000 19.63837  ? 192 GLY B H    1 
ATOM   6225 H  HA2  . GLY B  1 192 ? -44.16200 -17.15400 20.50100  1.000 19.61389  ? 192 GLY B HA2  1 
ATOM   6226 H  HA3  . GLY B  1 192 ? -43.63700 -16.80200 21.94900  1.000 19.61389  ? 192 GLY B HA3  1 
ATOM   6227 N  N    . LEU B  1 193 ? -45.96700 -18.56700 21.31100  1.000 16.98359  ? 193 LEU B N    1 
ATOM   6228 C  CA   . LEU B  1 193 ? -47.08500 -19.41100 21.76300  1.000 17.51565  ? 193 LEU B CA   1 
ATOM   6229 C  C    . LEU B  1 193 ? -46.44900 -20.64100 22.41100  1.000 17.64990  ? 193 LEU B C    1 
ATOM   6230 O  O    . LEU B  1 193 ? -45.88300 -21.48900 21.72400  1.000 17.83886  ? 193 LEU B O    1 
ATOM   6231 C  CB   . LEU B  1 193 ? -47.95300 -19.84200 20.58300  1.000 16.81831  ? 193 LEU B CB   1 
ATOM   6232 C  CG   . LEU B  1 193 ? -48.38500 -18.76600 19.59800  1.000 16.52468  ? 193 LEU B CG   1 
ATOM   6233 C  CD1  . LEU B  1 193 ? -49.08800 -19.43700 18.41600  1.000 18.19923  ? 193 LEU B CD1  1 
ATOM   6234 C  CD2  . LEU B  1 193 ? -49.31700 -17.73200 20.22700  1.000 17.12269  ? 193 LEU B CD2  1 
ATOM   6235 H  H    . LEU B  1 193 ? -45.59200 -18.85900 20.59500  1.000 20.38287  ? 193 LEU B H    1 
ATOM   6236 H  HA   . LEU B  1 193 ? -47.64200 -18.93000 22.39500  1.000 21.02135  ? 193 LEU B HA   1 
ATOM   6237 H  HB2  . LEU B  1 193 ? -47.45600 -20.50300 20.07500  1.000 20.18454  ? 193 LEU B HB2  1 
ATOM   6238 H  HB3  . LEU B  1 193 ? -48.76300 -20.23800 20.93900  1.000 20.18454  ? 193 LEU B HB3  1 
ATOM   6239 H  HG   . LEU B  1 193 ? -47.59600 -18.28500 19.30200  1.000 19.83218  ? 193 LEU B HG   1 
ATOM   6240 H  HD11 . LEU B  1 193 ? -49.46900 -18.75100 17.84500  1.000 21.84163  ? 193 LEU B HD11 1 
ATOM   6241 H  HD12 . LEU B  1 193 ? -48.43900 -19.95800 17.91800  1.000 21.84163  ? 193 LEU B HD12 1 
ATOM   6242 H  HD13 . LEU B  1 193 ? -49.79000 -20.01500 18.75200  1.000 21.84163  ? 193 LEU B HD13 1 
ATOM   6243 H  HD21 . LEU B  1 193 ? -49.53600 -17.06000 19.56300  1.000 20.54979  ? 193 LEU B HD21 1 
ATOM   6244 H  HD22 . LEU B  1 193 ? -50.12500 -18.17700 20.52700  1.000 20.54979  ? 193 LEU B HD22 1 
ATOM   6245 H  HD23 . LEU B  1 193 ? -48.86700 -17.31900 20.98100  1.000 20.54979  ? 193 LEU B HD23 1 
ATOM   6246 N  N    . ALA B  1 194 ? -46.50100 -20.76000 23.72900  1.000 17.80279  ? 194 ALA B N    1 
ATOM   6247 C  CA   . ALA B  1 194 ? -45.89200 -21.88800 24.43100  1.000 18.38896  ? 194 ALA B CA   1 
ATOM   6248 C  C    . ALA B  1 194 ? -44.48200 -22.15700 23.87000  1.000 19.13813  ? 194 ALA B C    1 
ATOM   6249 O  O    . ALA B  1 194 ? -44.19000 -23.27500 23.43600  1.000 20.03809  ? 194 ALA B O    1 
ATOM   6250 C  CB   . ALA B  1 194 ? -46.76800 -23.12900 24.33100  1.000 20.77398  ? 194 ALA B CB   1 
ATOM   6251 H  H    . ALA B  1 194 ? -46.88900 -20.19300 24.24700  1.000 21.36590  ? 194 ALA B H    1 
ATOM   6252 H  HA   . ALA B  1 194 ? -45.80500 -21.67500 25.37300  1.000 22.06932  ? 194 ALA B HA   1 
ATOM   6253 H  HB1  . ALA B  1 194 ? -46.36500 -23.84200 24.85000  1.000 24.93134  ? 194 ALA B HB1  1 
ATOM   6254 H  HB2  . ALA B  1 194 ? -47.64900 -22.92200 24.68000  1.000 24.93134  ? 194 ALA B HB2  1 
ATOM   6255 H  HB3  . ALA B  1 194 ? -46.83500 -23.39300 23.40000  1.000 24.93134  ? 194 ALA B HB3  1 
ATOM   6256 N  N    . PRO B  1 195 ? -43.62300 -21.15100 23.85000  1.000 18.34809  ? 195 PRO B N    1 
ATOM   6257 C  CA   . PRO B  1 195 ? -42.33700 -21.28700 23.14900  1.000 19.19675  ? 195 PRO B CA   1 
ATOM   6258 C  C    . PRO B  1 195 ? -41.42500 -22.33100 23.77900  1.000 19.62161  ? 195 PRO B C    1 
ATOM   6259 O  O    . PRO B  1 195 ? -41.46200 -22.58300 24.98500  1.000 20.53678  ? 195 PRO B O    1 
ATOM   6260 C  CB   . PRO B  1 195 ? -41.71800 -19.88400 23.31700  1.000 18.82379  ? 195 PRO B CB   1 
ATOM   6261 C  CG   . PRO B  1 195 ? -42.33600 -19.35300 24.57000  1.000 18.74850  ? 195 PRO B CG   1 
ATOM   6262 C  CD   . PRO B  1 195 ? -43.75700 -19.83100 24.50600  1.000 19.13928  ? 195 PRO B CD   1 
ATOM   6263 H  HA   . PRO B  1 195 ? -42.48600 -21.50900 22.21600  1.000 23.03866  ? 195 PRO B HA   1 
ATOM   6264 H  HB2  . PRO B  1 195 ? -40.75500 -19.95300 23.40500  1.000 22.59111  ? 195 PRO B HB2  1 
ATOM   6265 H  HB3  . PRO B  1 195 ? -41.94300 -19.32800 22.55500  1.000 22.59111  ? 195 PRO B HB3  1 
ATOM   6266 H  HG2  . PRO B  1 195 ? -41.88000 -19.71400 25.34700  1.000 22.50076  ? 195 PRO B HG2  1 
ATOM   6267 H  HG3  . PRO B  1 195 ? -42.29300 -18.38400 24.58100  1.000 22.50076  ? 195 PRO B HG3  1 
ATOM   6268 H  HD2  . PRO B  1 195 ? -44.13500 -19.92100 25.39500  1.000 22.96970  ? 195 PRO B HD2  1 
ATOM   6269 H  HD3  . PRO B  1 195 ? -44.30200 -19.23100 23.97300  1.000 22.96970  ? 195 PRO B HD3  1 
ATOM   6270 N  N    . TRP B  1 196 ? -40.56100 -22.89300 22.93300  1.000 19.17444  ? 196 TRP B N    1 
ATOM   6271 C  CA   . TRP B  1 196 ? -39.54400 -23.86600 23.31600  1.000 19.72422  ? 196 TRP B CA   1 
ATOM   6272 C  C    . TRP B  1 196 ? -38.23100 -23.47500 22.65200  1.000 20.55816  ? 196 TRP B C    1 
ATOM   6273 O  O    . TRP B  1 196 ? -38.20400 -23.09300 21.47900  1.000 20.70048  ? 196 TRP B O    1 
ATOM   6274 C  CB   . TRP B  1 196 ? -39.95400 -25.26600 22.82400  1.000 21.26836  ? 196 TRP B CB   1 
ATOM   6275 C  CG   . TRP B  1 196 ? -39.08800 -26.42600 23.27100  1.000 24.19102  ? 196 TRP B CG   1 
ATOM   6276 C  CD1  . TRP B  1 196 ? -39.36900 -27.31300 24.26400  1.000 27.10752  ? 196 TRP B CD1  1 
ATOM   6277 C  CD2  . TRP B  1 196 ? -37.84100 -26.83600 22.70600  1.000 25.12337  ? 196 TRP B CD2  1 
ATOM   6278 N  NE1  . TRP B  1 196 ? -38.36600 -28.26600 24.36400  1.000 25.78897  ? 196 TRP B NE1  1 
ATOM   6279 C  CE2  . TRP B  1 196 ? -37.41700 -27.98600 23.41400  1.000 24.14462  ? 196 TRP B CE2  1 
ATOM   6280 C  CE3  . TRP B  1 196 ? -37.03400 -26.34800 21.68100  1.000 24.00823  ? 196 TRP B CE3  1 
ATOM   6281 C  CZ2  . TRP B  1 196 ? -36.22400 -28.64400 23.12300  1.000 26.37775  ? 196 TRP B CZ2  1 
ATOM   6282 C  CZ3  . TRP B  1 196 ? -35.84000 -27.01300 21.40200  1.000 25.04199  ? 196 TRP B CZ3  1 
ATOM   6283 C  CH2  . TRP B  1 196 ? -35.45400 -28.13900 22.11400  1.000 25.67145  ? 196 TRP B CH2  1 
ATOM   6284 H  H    . TRP B  1 196 ? -40.54500 -22.71600 22.09200  1.000 23.01189  ? 196 TRP B H    1 
ATOM   6285 H  HA   . TRP B  1 196 ? -39.42200 -23.88200 24.27800  1.000 23.67162  ? 196 TRP B HA   1 
ATOM   6286 H  HB2  . TRP B  1 196 ? -40.85300 -25.44400 23.14200  1.000 25.52460  ? 196 TRP B HB2  1 
ATOM   6287 H  HB3  . TRP B  1 196 ? -39.94000 -25.25900 21.85400  1.000 25.52460  ? 196 TRP B HB3  1 
ATOM   6288 H  HD1  . TRP B  1 196 ? -40.12800 -27.28400 24.80100  1.000 32.53158  ? 196 TRP B HD1  1 
ATOM   6289 H  HE1  . TRP B  1 196 ? -38.34300 -28.91800 24.92400  1.000 30.94932  ? 196 TRP B HE1  1 
ATOM   6290 H  HE3  . TRP B  1 196 ? -37.28600 -25.59600 21.19400  1.000 28.81244  ? 196 TRP B HE3  1 
ATOM   6291 H  HZ2  . TRP B  1 196 ? -35.96100 -29.39900 23.59800  1.000 31.65587  ? 196 TRP B HZ2  1 
ATOM   6292 H  HZ3  . TRP B  1 196 ? -35.29100 -26.69400 20.72200  1.000 30.05295  ? 196 TRP B HZ3  1 
ATOM   6293 H  HH2  . TRP B  1 196 ? -34.65300 -28.56000 21.90000  1.000 30.80830  ? 196 TRP B HH2  1 
ATOM   6294 N  N    . ASN B  1 197 ? -37.14000 -23.54900 23.41700  1.000 20.55987  ? 197 ASN B N    1 
ATOM   6295 C  CA   . ASN B  1 197 ? -35.79800 -23.31400 22.90100  1.000 18.98545  ? 197 ASN B CA   1 
ATOM   6296 C  C    . ASN B  1 197 ? -34.82700 -24.00600 23.84700  1.000 21.52736  ? 197 ASN B C    1 
ATOM   6297 O  O    . ASN B  1 197 ? -35.13900 -24.22500 25.01600  1.000 22.66584  ? 197 ASN B O    1 
ATOM   6298 C  CB   . ASN B  1 197 ? -35.50200 -21.80900 22.79000  1.000 20.61836  ? 197 ASN B CB   1 
ATOM   6299 C  CG   . ASN B  1 197 ? -34.42700 -21.49600 21.78200  1.000 21.50483  ? 197 ASN B CG   1 
ATOM   6300 O  OD1  . ASN B  1 197 ? -34.58300 -21.75800 20.59000  1.000 22.83812  ? 197 ASN B OD1  1 
ATOM   6301 N  ND2  . ASN B  1 197 ? -33.32500 -20.91300 22.23600  1.000 21.78237  ? 197 ASN B ND2  1 
ATOM   6302 H  H    . ASN B  1 197 ? -37.15400 -23.73900 24.25600  1.000 24.67441  ? 197 ASN B H    1 
ATOM   6303 H  HA   . ASN B  1 197 ? -35.69400 -23.69700 22.01500  1.000 22.78510  ? 197 ASN B HA   1 
ATOM   6304 H  HB2  . ASN B  1 197 ? -36.31100 -21.34800 22.51700  1.000 24.74459  ? 197 ASN B HB2  1 
ATOM   6305 H  HB3  . ASN B  1 197 ? -35.20800 -21.48100 23.65300  1.000 24.74459  ? 197 ASN B HB3  1 
ATOM   6306 H  HD21 . ASN B  1 197 ? -32.68700 -20.71800 21.69400  1.000 26.14140  ? 197 ASN B HD21 1 
ATOM   6307 H  HD22 . ASN B  1 197 ? -33.24900 -20.73100 23.07400  1.000 26.14140  ? 197 ASN B HD22 1 
ATOM   6308 N  N    . THR B  1 198 ? -33.62400 -24.31900 23.35600  1.000 21.16465  ? 198 THR B N    1 
ATOM   6309 C  CA   . THR B  1 198 ? -32.68400 -25.01300 24.23700  1.000 22.16009  ? 198 THR B CA   1 
ATOM   6310 C  C    . THR B  1 198 ? -31.98800 -24.08700 25.22700  1.000 22.55509  ? 198 THR B C    1 
ATOM   6311 O  O    . THR B  1 198 ? -31.40400 -24.58500 26.19600  1.000 26.47333  ? 198 THR B O    1 
ATOM   6312 C  CB   . THR B  1 198 ? -31.59800 -25.74700 23.45300  1.000 25.85869  ? 198 THR B CB   1 
ATOM   6313 O  OG1  . THR B  1 198 ? -30.89500 -24.80000 22.65400  1.000 26.73391  ? 198 THR B OG1  1 
ATOM   6314 C  CG2  . THR B  1 198 ? -32.18800 -26.84700 22.56100  1.000 29.91252  ? 198 THR B CG2  1 
ATOM   6315 H  H    . THR B  1 198 ? -33.34500 -24.15000 22.56100  1.000 25.40014  ? 198 THR B H    1 
ATOM   6316 H  HA   . THR B  1 198 ? -33.20600 -25.67100 24.72200  1.000 26.59466  ? 198 THR B HA   1 
ATOM   6317 H  HB   . THR B  1 198 ? -30.98900 -26.18100 24.07100  1.000 31.03299  ? 198 THR B HB   1 
ATOM   6318 H  HG1  . THR B  1 198 ? -31.40900 -24.47400 22.07500  1.000 32.08325  ? 198 THR B HG1  1 
ATOM   6319 H  HG21 . THR B  1 198 ? -31.47600 -27.31900 22.10200  1.000 35.89759  ? 198 THR B HG21 1 
ATOM   6320 H  HG22 . THR B  1 198 ? -32.68700 -27.47900 23.10100  1.000 35.89759  ? 198 THR B HG22 1 
ATOM   6321 H  HG23 . THR B  1 198 ? -32.78300 -26.45600 21.90200  1.000 35.89759  ? 198 THR B HG23 1 
ATOM   6322 N  N    . SER B  1 199 ? -32.04800 -22.77800 25.03300  1.000 21.06695  ? 199 SER B N    1 
ATOM   6323 C  CA   . SER B  1 199 ? -31.37200 -21.84400 25.91400  1.000 20.30149  ? 199 SER B CA   1 
ATOM   6324 C  C    . SER B  1 199 ? -32.12000 -20.53700 25.91800  1.000 20.22009  ? 199 SER B C    1 
ATOM   6325 O  O    . SER B  1 199 ? -32.69400 -20.13100 24.90200  1.000 21.20456  ? 199 SER B O    1 
ATOM   6326 C  CB   . SER B  1 199 ? -29.93300 -21.57000 25.44100  1.000 23.66247  ? 199 SER B CB   1 
ATOM   6327 O  OG   . SER B  1 199 ? -29.31100 -20.56700 26.24700  1.000 22.44125  ? 199 SER B OG   1 
ATOM   6328 H  H    . SER B  1 199 ? -32.47900 -22.40300 24.39100  1.000 25.28290  ? 199 SER B H    1 
ATOM   6329 H  HA   . SER B  1 199 ? -31.36000 -22.21300 26.81100  1.000 24.36435  ? 199 SER B HA   1 
ATOM   6330 H  HB2  . SER B  1 199 ? -29.41900 -22.39000 25.50600  1.000 28.39752  ? 199 SER B HB2  1 
ATOM   6331 H  HB3  . SER B  1 199 ? -29.95600 -21.26400 24.52100  1.000 28.39752  ? 199 SER B HB3  1 
ATOM   6332 H  HG   . SER B  1 199 ? -28.50300 -20.48500 26.03000  1.000 26.93206  ? 199 SER B HG   1 
ATOM   6333 N  N    . SER B  1 200 ? -32.09800 -19.87000 27.06200  1.000 20.13796  ? 200 SER B N    1 
ATOM   6334 C  CA   . SER B  1 200 ? -32.59000 -18.52100 27.19600  1.000 18.60795  ? 200 SER B CA   1 
ATOM   6335 C  C    . SER B  1 200 ? -31.53200 -17.44600 26.98400  1.000 19.91555  ? 200 SER B C    1 
ATOM   6336 O  O    . SER B  1 200 ? -31.90000 -16.26500 26.86600  1.000 20.37552  ? 200 SER B O    1 
ATOM   6337 C  CB   . SER B  1 200 ? -33.12600 -18.31100 28.61300  1.000 20.75763  ? 200 SER B CB   1 
ATOM   6338 O  OG   . SER B  1 200 ? -32.04200 -18.42200 29.51800  1.000 21.80908  ? 200 SER B OG   1 
ATOM   6339 H  H    . SER B  1 200 ? -31.79200 -20.19300 27.79800  1.000 24.16812  ? 200 SER B H    1 
ATOM   6340 H  HA   . SER B  1 200 ? -33.29300 -18.40700 26.53700  1.000 22.33210  ? 200 SER B HA   1 
ATOM   6341 H  HB2  . SER B  1 200 ? -33.52100 -17.42900 28.68500  1.000 24.91171  ? 200 SER B HB2  1 
ATOM   6342 H  HB3  . SER B  1 200 ? -33.78900 -18.99000 28.81400  1.000 24.91171  ? 200 SER B HB3  1 
ATOM   6343 H  HG   . SER B  1 200 ? -32.33000 -18.46400 30.30600  1.000 26.17346  ? 200 SER B HG   1 
ATOM   6344 N  N    . LEU B  1 201 ? -30.25900 -17.82300 26.85000  1.000 19.93267  ? 201 LEU B N    1 
ATOM   6345 C  CA   . LEU B  1 201 ? -29.17500 -16.85700 26.95000  1.000 20.06803  ? 201 LEU B CA   1 
ATOM   6346 C  C    . LEU B  1 201 ? -29.21500 -15.86300 25.79700  1.000 20.74162  ? 201 LEU B C    1 
ATOM   6347 O  O    . LEU B  1 201 ? -28.91900 -14.68800 25.99300  1.000 25.78958  ? 201 LEU B O    1 
ATOM   6348 C  CB   . LEU B  1 201 ? -27.83600 -17.58500 27.02100  1.000 21.45150  ? 201 LEU B CB   1 
ATOM   6349 C  CG   . LEU B  1 201 ? -26.71600 -16.73400 27.55000  1.000 23.36535  ? 201 LEU B CG   1 
ATOM   6350 C  CD1  . LEU B  1 201 ? -26.96100 -16.33800 29.01000  1.000 23.98334  ? 201 LEU B CD1  1 
ATOM   6351 C  CD2  . LEU B  1 201 ? -25.37400 -17.46600 27.43900  1.000 24.69036  ? 201 LEU B CD2  1 
ATOM   6352 H  H    . LEU B  1 201 ? -30.00100 -18.63000 26.70100  1.000 23.92177  ? 201 LEU B H    1 
ATOM   6353 H  HA   . LEU B  1 201 ? -29.27200 -16.34900 27.77100  1.000 24.08420  ? 201 LEU B HA   1 
ATOM   6354 H  HB2  . LEU B  1 201 ? -27.92900 -18.35200 27.60600  1.000 25.74436  ? 201 LEU B HB2  1 
ATOM   6355 H  HB3  . LEU B  1 201 ? -27.59200 -17.87600 26.12800  1.000 25.74436  ? 201 LEU B HB3  1 
ATOM   6356 H  HG   . LEU B  1 201 ? -26.67900 -15.92700 27.01400  1.000 28.04098  ? 201 LEU B HG   1 
ATOM   6357 H  HD11 . LEU B  1 201 ? -26.14200 -15.97200 29.37900  1.000 28.78257  ? 201 LEU B HD11 1 
ATOM   6358 H  HD12 . LEU B  1 201 ? -27.66500 -15.67200 29.04300  1.000 28.78257  ? 201 LEU B HD12 1 
ATOM   6359 H  HD13 . LEU B  1 201 ? -27.22600 -17.12500 29.51100  1.000 28.78257  ? 201 LEU B HD13 1 
ATOM   6360 H  HD21 . LEU B  1 201 ? -24.68000 -16.91500 27.83400  1.000 29.63099  ? 201 LEU B HD21 1 
ATOM   6361 H  HD22 . LEU B  1 201 ? -25.43500 -18.31100 27.91200  1.000 29.63099  ? 201 LEU B HD22 1 
ATOM   6362 H  HD23 . LEU B  1 201 ? -25.17700 -17.62500 26.50200  1.000 29.63099  ? 201 LEU B HD23 1 
ATOM   6363 N  N    . GLY B  1 202 ? -29.56800 -16.31300 24.60100  1.000 20.85583  ? 202 GLY B N    1 
ATOM   6364 C  CA   . GLY B  1 202 ? -29.58900 -15.44200 23.45100  1.000 22.96285  ? 202 GLY B CA   1 
ATOM   6365 C  C    . GLY B  1 202 ? -30.72900 -14.47300 23.41900  1.000 25.15997  ? 202 GLY B C    1 
ATOM   6366 O  O    . GLY B  1 202 ? -30.80900 -13.65000 22.50400  1.000 28.38131  ? 202 GLY B O    1 
ATOM   6367 H  H    . GLY B  1 202 ? -29.80100 -17.12400 24.43400  1.000 25.02956  ? 202 GLY B H    1 
ATOM   6368 H  HA2  . GLY B  1 202 ? -28.76500 -14.93100 23.43300  1.000 27.55798  ? 202 GLY B HA2  1 
ATOM   6369 H  HA3  . GLY B  1 202 ? -29.64000 -15.98600 22.64900  1.000 27.55798  ? 202 GLY B HA3  1 
ATOM   6370 N  N    . PHE B  1 203 ? -31.65900 -14.56700 24.35000  1.000 20.97549  ? 203 PHE B N    1 
ATOM   6371 C  CA   . PHE B  1 203 ? -32.80900 -13.68500 24.39500  1.000 19.87037  ? 203 PHE B CA   1 
ATOM   6372 C  C    . PHE B  1 203 ? -32.55900 -12.46100 25.25200  1.000 21.27061  ? 203 PHE B C    1 
ATOM   6373 O  O    . PHE B  1 203 ? -33.44100 -11.59200 25.36100  1.000 20.99037  ? 203 PHE B O    1 
ATOM   6374 C  CB   . PHE B  1 203 ? -34.07000 -14.42800 24.85800  1.000 20.54981  ? 203 PHE B CB   1 
ATOM   6375 C  CG   . PHE B  1 203 ? -34.40200 -15.63500 24.01200  1.000 19.07699  ? 203 PHE B CG   1 
ATOM   6376 C  CD1  . PHE B  1 203 ? -34.07600 -15.69400 22.66900  1.000 19.65376  ? 203 PHE B CD1  1 
ATOM   6377 C  CD2  . PHE B  1 203 ? -35.08200 -16.72900 24.56700  1.000 20.03138  ? 203 PHE B CD2  1 
ATOM   6378 C  CE1  . PHE B  1 203 ? -34.37800 -16.83000 21.89200  1.000 20.56299  ? 203 PHE B CE1  1 
ATOM   6379 C  CE2  . PHE B  1 203 ? -35.36900 -17.85100 23.80700  1.000 21.38721  ? 203 PHE B CE2  1 
ATOM   6380 C  CZ   . PHE B  1 203 ? -35.02900 -17.88900 22.45400  1.000 21.53641  ? 203 PHE B CZ   1 
ATOM   6381 H  H    . PHE B  1 203 ? -31.64600 -15.14900 24.98300  1.000 25.17315  ? 203 PHE B H    1 
ATOM   6382 H  HA   . PHE B  1 203 ? -33.00100 -13.38200 23.49400  1.000 23.84701  ? 203 PHE B HA   1 
ATOM   6383 H  HB2  . PHE B  1 203 ? -33.93800 -14.73200 25.77000  1.000 24.66234  ? 203 PHE B HB2  1 
ATOM   6384 H  HB3  . PHE B  1 203 ? -34.82500 -13.82000 24.81800  1.000 24.66234  ? 203 PHE B HB3  1 
ATOM   6385 H  HD1  . PHE B  1 203 ? -33.64900 -14.97000 22.27000  1.000 23.58707  ? 203 PHE B HD1  1 
ATOM   6386 H  HD2  . PHE B  1 203 ? -35.34400 -16.70000 25.45900  1.000 24.04022  ? 203 PHE B HD2  1 
ATOM   6387 H  HE1  . PHE B  1 203 ? -34.13400 -16.85900 20.99600  1.000 24.67815  ? 203 PHE B HE1  1 
ATOM   6388 H  HE2  . PHE B  1 203 ? -35.79000 -18.58100 24.20000  1.000 25.66721  ? 203 PHE B HE2  1 
ATOM   6389 H  HZ   . PHE B  1 203 ? -35.24500 -18.63200 21.93900  1.000 25.84626  ? 203 PHE B HZ   1 
ATOM   6390 N  N    . ARG B  1 204 ? -31.38100 -12.37100 25.86700  1.000 23.92441  ? 204 ARG B N    1 
ATOM   6391 C  CA   . ARG B  1 204 ? -31.05900 -11.31100 26.80600  1.000 22.62441  ? 204 ARG B CA   1 
ATOM   6392 C  C    . ARG B  1 204 ? -30.83600 -9.96900  26.13300  1.000 23.21123  ? 204 ARG B C    1 
ATOM   6393 O  O    . ARG B  1 204 ? -30.65800 -8.98200  26.86100  1.000 30.54671  ? 204 ARG B O    1 
ATOM   6394 C  CB   . ARG B  1 204 ? -29.86400 -11.71200 27.65700  1.000 22.99895  ? 204 ARG B CB   1 
ATOM   6395 C  CG   . ARG B  1 204 ? -30.13200 -13.04300 28.33200  1.000 30.11616  ? 204 ARG B CG   1 
ATOM   6396 C  CD   . ARG B  1 204 ? -30.22300 -12.92500 29.82300  1.000 50.59277  ? 204 ARG B CD   1 
ATOM   6397 N  NE   . ARG B  1 204 ? -29.01800 -12.33800 30.41100  1.000 33.31627  ? 204 ARG B NE   1 
ATOM   6398 C  CZ   . ARG B  1 204 ? -28.85500 -12.16900 31.70700  1.000 54.81559  ? 204 ARG B CZ   1 
ATOM   6399 N  NH1  . ARG B  1 204 ? -29.73000 -12.64800 32.57600  1.000 60.68997  ? 204 ARG B NH1  1 
ATOM   6400 N  NH2  . ARG B  1 204 ? -27.77600 -11.53100 32.14000  1.000 54.27973  ? 204 ARG B NH2  1 
ATOM   6401 H  H    . ARG B  1 204 ? -30.73600 -12.92900 25.75100  1.000 28.71186  ? 204 ARG B H    1 
ATOM   6402 H  HA   . ARG B  1 204 ? -31.80600 -11.19000 27.41300  1.000 27.15186  ? 204 ARG B HA   1 
ATOM   6403 H  HB2  . ARG B  1 204 ? -29.07800 -11.80000 27.09500  1.000 27.60130  ? 204 ARG B HB2  1 
ATOM   6404 H  HB3  . ARG B  1 204 ? -29.70900 -11.04100 28.34000  1.000 27.60130  ? 204 ARG B HB3  1 
ATOM   6405 H  HG2  . ARG B  1 204 ? -30.97300 -13.40000 28.00800  1.000 36.14195  ? 204 ARG B HG2  1 
ATOM   6406 H  HG3  . ARG B  1 204 ? -29.40900 -13.65600 28.12400  1.000 36.14195  ? 204 ARG B HG3  1 
ATOM   6407 H  HD2  . ARG B  1 204 ? -30.97700 -12.35800 30.05100  1.000 60.71389  ? 204 ARG B HD2  1 
ATOM   6408 H  HD3  . ARG B  1 204 ? -30.34500 -13.80800 30.20400  1.000 60.71389  ? 204 ARG B HD3  1 
ATOM   6409 H  HE   . ARG B  1 204 ? -28.38500 -12.09100 29.88400  1.000 39.98208  ? 204 ARG B HE   1 
ATOM   6410 H  HH11 . ARG B  1 204 ? -30.42000 -13.07900 32.29800  1.000 72.83053  ? 204 ARG B HH11 1 
ATOM   6411 H  HH12 . ARG B  1 204 ? -29.60800 -12.52800 33.41900  1.000 72.83053  ? 204 ARG B HH12 1 
ATOM   6412 H  HH21 . ARG B  1 204 ? -27.19700 -11.23500 31.57800  1.000 65.13824  ? 204 ARG B HH21 1 
ATOM   6413 H  HH22 . ARG B  1 204 ? -27.65600 -11.41300 32.98300  1.000 65.13824  ? 204 ARG B HH22 1 
ATOM   6414 N  N    . SER B  1 205 ? -30.86300 -9.82800  24.84000  1.000 24.82197  ? 205 SER B N    1 
ATOM   6415 C  CA   . SER B  1 205 ? -30.78100 -8.45000  24.28300  1.000 36.04091  ? 205 SER B CA   1 
ATOM   6416 C  C    . SER B  1 205 ? -31.95400 -8.21200  23.31800  1.000 30.41539  ? 205 SER B C    1 
ATOM   6417 O  O    . SER B  1 205 ? -31.81500 -7.32000  22.51900  1.000 33.23845  ? 205 SER B O    1 
ATOM   6418 C  CB   . SER B  1 205 ? -29.46900 -8.19600  23.62200  1.000 48.50497  ? 205 SER B CB   1 
ATOM   6419 O  OG   . SER B  1 205 ? -29.30500 -9.10100  22.54900  1.000 65.04638  ? 205 SER B OG   1 
ATOM   6420 H  H    . SER B  1 205 ? -30.88100 -10.48500 24.26100  1.000 29.78893  ? 205 SER B H    1 
ATOM   6421 H  HA   . SER B  1 205 ? -30.87400 -7.81200  25.04100  1.000 43.25165  ? 205 SER B HA   1 
ATOM   6422 H  HB2  . SER B  1 205 ? -29.44000 -7.27200  23.28700  1.000 58.20853  ? 205 SER B HB2  1 
ATOM   6423 H  HB3  . SER B  1 205 ? -28.74100 -8.31400  24.27300  1.000 58.20853  ? 205 SER B HB3  1 
ATOM   6424 H  HG   . SER B  1 205 ? -29.77300 -8.83200  21.89800  1.000 78.05822  ? 205 SER B HG   1 
ATOM   6425 N  N    . ILE B  1 206 ? -33.00600 -9.03400  23.32100  1.000 24.29167  ? 206 ILE B N    1 
ATOM   6426 C  CA   . ILE B  1 206 ? -34.15700 -8.72400  22.47900  1.000 22.31753  ? 206 ILE B CA   1 
ATOM   6427 C  C    . ILE B  1 206 ? -34.68100 -7.32700  22.77600  1.000 21.91744  ? 206 ILE B C    1 
ATOM   6428 O  O    . ILE B  1 206 ? -35.01200 -7.00700  23.92100  1.000 22.47127  ? 206 ILE B O    1 
ATOM   6429 C  CB   . ILE B  1 206 ? -35.27000 -9.75400  22.70700  1.000 19.77778  ? 206 ILE B CB   1 
ATOM   6430 C  CG1  . ILE B  1 206 ? -34.89800 -11.09300 22.05900  1.000 21.55463  ? 206 ILE B CG1  1 
ATOM   6431 C  CG2  . ILE B  1 206 ? -36.60600 -9.25400  22.15600  1.000 19.61200  ? 206 ILE B CG2  1 
ATOM   6432 C  CD1  . ILE B  1 206 ? -35.82100 -12.22000 22.38600  1.000 21.76633  ? 206 ILE B CD1  1 
ATOM   6433 H  H    . ILE B  1 206 ? -33.11000 -9.70800  23.84500  1.000 29.15257  ? 206 ILE B H    1 
ATOM   6434 H  HA   . ILE B  1 206 ? -33.86200 -8.75300  21.55500  1.000 26.78360  ? 206 ILE B HA   1 
ATOM   6435 H  HB   . ILE B  1 206 ? -35.36500 -9.88100  23.66400  1.000 23.73590  ? 206 ILE B HB   1 
ATOM   6436 H  HG12 . ILE B  1 206 ? -34.90200 -10.98100 21.09500  1.000 25.86812  ? 206 ILE B HG12 1 
ATOM   6437 H  HG13 . ILE B  1 206 ? -34.01000 -11.34500 22.36000  1.000 25.86812  ? 206 ILE B HG13 1 
ATOM   6438 H  HG21 . ILE B  1 206 ? -37.22100 -10.00200 22.09200  1.000 23.53697  ? 206 ILE B HG21 1 
ATOM   6439 H  HG22 . ILE B  1 206 ? -36.96400 -8.58200  22.75600  1.000 23.53697  ? 206 ILE B HG22 1 
ATOM   6440 H  HG23 . ILE B  1 206 ? -36.46200 -8.87000  21.27700  1.000 23.53697  ? 206 ILE B HG23 1 
ATOM   6441 H  HD11 . ILE B  1 206 ? -35.40700 -13.05500 22.11800  1.000 26.12216  ? 206 ILE B HD11 1 
ATOM   6442 H  HD12 . ILE B  1 206 ? -35.98700 -12.22400 23.34200  1.000 26.12216  ? 206 ILE B HD12 1 
ATOM   6443 H  HD13 . ILE B  1 206 ? -36.65400 -12.09400 21.90600  1.000 26.12216  ? 206 ILE B HD13 1 
ATOM   6444 N  N    . GLU B  1 207 ? -34.80600 -6.50900  21.72900  1.000 19.62958  ? 207 GLU B N    1 
ATOM   6445 C  CA   . GLU B  1 207 ? -35.45000 -5.20000  21.81200  1.000 22.02057  ? 207 GLU B CA   1 
ATOM   6446 C  C    . GLU B  1 207 ? -36.79700 -5.19400  21.11500  1.000 21.63505  ? 207 GLU B C    1 
ATOM   6447 O  O    . GLU B  1 207 ? -37.61700 -4.30000  21.38200  1.000 22.96790  ? 207 GLU B O    1 
ATOM   6448 C  CB   . GLU B  1 207 ? -34.55000 -4.11700  21.21400  1.000 26.12492  ? 207 GLU B CB   1 
ATOM   6449 C  CG   . GLU B  1 207 ? -33.27000 -3.93100  22.00200  1.000 32.19869  ? 207 GLU B CG   1 
ATOM   6450 C  CD   . GLU B  1 207 ? -32.34900 -2.89300  21.39000  1.000 56.22466  ? 207 GLU B CD   1 
ATOM   6451 O  OE1  . GLU B  1 207 ? -32.83400 -1.80900  21.00400  1.000 63.86976  ? 207 GLU B OE1  1 
ATOM   6452 O  OE2  . GLU B  1 207 ? -31.14000 -3.17100  21.28300  1.000 67.14054  ? 207 GLU B OE2  1 
ATOM   6453 H  H    . GLU B  1 207 ? -34.51800 -6.69600  20.94000  1.000 23.55805  ? 207 GLU B H    1 
ATOM   6454 H  HA   . GLU B  1 207 ? -35.58200 -4.96000  22.74300  1.000 26.42725  ? 207 GLU B HA   1 
ATOM   6455 H  HB2  . GLU B  1 207 ? -34.31300 -4.36700  20.30700  1.000 31.35247  ? 207 GLU B HB2  1 
ATOM   6456 H  HB3  . GLU B  1 207 ? -35.02900 -3.27400  21.21100  1.000 31.35247  ? 207 GLU B HB3  1 
ATOM   6457 H  HG2  . GLU B  1 207 ? -33.49200 -3.64300  22.90100  1.000 38.64099  ? 207 GLU B HG2  1 
ATOM   6458 H  HG3  . GLU B  1 207 ? -32.79300 -4.77500  22.03200  1.000 38.64099  ? 207 GLU B HG3  1 
ATOM   6459 N  N    . THR B  1 208 ? -37.07700 -6.18200  20.27400  1.000 21.28236  ? 208 THR B N    1 
ATOM   6460 C  CA   . THR B  1 208 ? -38.37100 -6.30000  19.63200  1.000 18.74500  ? 208 THR B CA   1 
ATOM   6461 C  C    . THR B  1 208 ? -39.46600 -6.43900  20.68100  1.000 18.62158  ? 208 THR B C    1 
ATOM   6462 O  O    . THR B  1 208 ? -39.35700 -7.29600  21.56200  1.000 18.59095  ? 208 THR B O    1 
ATOM   6463 C  CB   . THR B  1 208 ? -38.39900 -7.58300  18.80000  1.000 21.39919  ? 208 THR B CB   1 
ATOM   6464 O  OG1  . THR B  1 208 ? -37.32100 -7.56900  17.84200  1.000 25.37115  ? 208 THR B OG1  1 
ATOM   6465 C  CG2  . THR B  1 208 ? -39.69500 -7.76100  18.06000  1.000 21.12124  ? 208 THR B CG2  1 
ATOM   6466 H  H    . THR B  1 208 ? -36.52500 -6.80500  20.05600  1.000 25.54139  ? 208 THR B H    1 
ATOM   6467 H  HA   . THR B  1 208 ? -38.52700 -5.51400  19.08400  1.000 22.49657  ? 208 THR B HA   1 
ATOM   6468 H  HB   . THR B  1 208 ? -38.30200 -8.33100  19.40900  1.000 25.68159  ? 208 THR B HB   1 
ATOM   6469 H  HG1  . THR B  1 208 ? -37.39300 -6.90000  17.33800  1.000 30.44794  ? 208 THR B HG1  1 
ATOM   6470 H  HG21 . THR B  1 208 ? -39.63100 -8.51600  17.45500  1.000 25.34805  ? 208 THR B HG21 1 
ATOM   6471 H  HG22 . THR B  1 208 ? -40.41700 -7.92100  18.68800  1.000 25.34805  ? 208 THR B HG22 1 
ATOM   6472 H  HG23 . THR B  1 208 ? -39.89600 -6.96300  17.54600  1.000 25.34805  ? 208 THR B HG23 1 
ATOM   6473 N  N    . PRO B  1 209 ? -40.55700 -5.67600  20.59600  1.000 17.11358  ? 209 PRO B N    1 
ATOM   6474 C  CA   . PRO B  1 209 ? -41.67700 -5.89700  21.51700  1.000 18.67554  ? 209 PRO B CA   1 
ATOM   6475 C  C    . PRO B  1 209 ? -42.17700 -7.33100  21.42600  1.000 17.18023  ? 209 PRO B C    1 
ATOM   6476 O  O    . PRO B  1 209 ? -42.61800 -7.79100  20.36600  1.000 17.32118  ? 209 PRO B O    1 
ATOM   6477 C  CB   . PRO B  1 209 ? -42.73100 -4.91000  21.01000  1.000 18.29780  ? 209 PRO B CB   1 
ATOM   6478 C  CG   . PRO B  1 209 ? -41.90700 -3.77500  20.46000  1.000 20.02704  ? 209 PRO B CG   1 
ATOM   6479 C  CD   . PRO B  1 209 ? -40.72800 -4.45300  19.79000  1.000 18.44218  ? 209 PRO B CD   1 
ATOM   6480 H  HA   . PRO B  1 209 ? -41.42600 -5.68800  22.43100  1.000 22.41321  ? 209 PRO B HA   1 
ATOM   6481 H  HB2  . PRO B  1 209 ? -43.27200 -5.32100  20.31700  1.000 21.95992  ? 209 PRO B HB2  1 
ATOM   6482 H  HB3  . PRO B  1 209 ? -43.29600 -4.61500  21.74100  1.000 21.95992  ? 209 PRO B HB3  1 
ATOM   6483 H  HG2  . PRO B  1 209 ? -42.42700 -3.26600  19.81900  1.000 24.03501  ? 209 PRO B HG2  1 
ATOM   6484 H  HG3  . PRO B  1 209 ? -41.61300 -3.19800  21.18200  1.000 24.03501  ? 209 PRO B HG3  1 
ATOM   6485 H  HD2  . PRO B  1 209 ? -40.93100 -4.67000  18.86600  1.000 22.13318  ? 209 PRO B HD2  1 
ATOM   6486 H  HD3  . PRO B  1 209 ? -39.93600 -3.89500  19.83200  1.000 22.13318  ? 209 PRO B HD3  1 
ATOM   6487 N  N    . THR B  1 210 ? -42.18600 -8.01300  22.57100  1.000 16.20010  ? 210 THR B N    1 
ATOM   6488 C  CA   . THR B  1 210 ? -42.40200 -9.45400  22.61200  1.000 15.39071  ? 210 THR B CA   1 
ATOM   6489 C  C    . THR B  1 210 ? -43.46500 -9.82100  23.62500  1.000 17.29989  ? 210 THR B C    1 
ATOM   6490 O  O    . THR B  1 210 ? -43.37300 -9.43000  24.79200  1.000 17.41135  ? 210 THR B O    1 
ATOM   6491 C  CB   . THR B  1 210 ? -41.08600 -10.18400 22.98800  1.000 17.63845  ? 210 THR B CB   1 
ATOM   6492 O  OG1  . THR B  1 210 ? -40.12400 -9.98700  21.97300  1.000 18.84663  ? 210 THR B OG1  1 
ATOM   6493 C  CG2  . THR B  1 210 ? -41.28100 -11.69000 23.13600  1.000 17.12862  ? 210 THR B CG2  1 
ATOM   6494 H  H    . THR B  1 210 ? -42.06700 -7.65600  23.34400  1.000 19.44268  ? 210 THR B H    1 
ATOM   6495 H  HA   . THR B  1 210 ? -42.71700 -9.73800  21.74000  1.000 18.47142  ? 210 THR B HA   1 
ATOM   6496 H  HB   . THR B  1 210 ? -40.78400 -9.82300  23.83600  1.000 21.16871  ? 210 THR B HB   1 
ATOM   6497 H  HG1  . THR B  1 210 ? -39.99100 -9.16600  21.85800  1.000 22.61852  ? 210 THR B HG1  1 
ATOM   6498 H  HG21 . THR B  1 210 ? -40.42000 -12.13500 23.16700  1.000 20.55691  ? 210 THR B HG21 1 
ATOM   6499 H  HG22 . THR B  1 210 ? -41.76500 -11.88300 23.95400  1.000 20.55691  ? 210 THR B HG22 1 
ATOM   6500 H  HG23 . THR B  1 210 ? -41.78600 -12.03500 22.38300  1.000 20.55691  ? 210 THR B HG23 1 
ATOM   6501 N  N    A LEU B  1 211 ? -44.48600 -10.54400 23.16800  0.295 15.35571  ? 211 LEU B N    1 
ATOM   6502 N  N    B LEU B  1 211 ? -44.47100 -10.55500 23.16700  0.240 15.61491  ? 211 LEU B N    1 
ATOM   6503 N  N    C LEU B  1 211 ? -44.48700 -10.54600 23.16100  0.464 15.85548  ? 211 LEU B N    1 
ATOM   6504 C  CA   A LEU B  1 211 ? -45.53300 -11.09100 24.02100  0.295 16.00643  ? 211 LEU B CA   1 
ATOM   6505 C  CA   B LEU B  1 211 ? -45.51300 -11.09900 24.02200  0.240 15.94111  ? 211 LEU B CA   1 
ATOM   6506 C  CA   C LEU B  1 211 ? -45.56300 -11.10300 23.97800  0.464 16.31973  ? 211 LEU B CA   1 
ATOM   6507 C  C    A LEU B  1 211 ? -45.38800 -12.60600 24.04500  0.295 16.14565  ? 211 LEU B C    1 
ATOM   6508 C  C    B LEU B  1 211 ? -45.36100 -12.61000 24.04800  0.240 16.25182  ? 211 LEU B C    1 
ATOM   6509 C  C    C LEU B  1 211 ? -45.39900 -12.61900 24.03400  0.464 16.85774  ? 211 LEU B C    1 
ATOM   6510 O  O    A LEU B  1 211 ? -45.26300 -13.24200 22.99400  0.295 16.89740  ? 211 LEU B O    1 
ATOM   6511 O  O    B LEU B  1 211 ? -45.19900 -13.24300 22.99800  0.240 17.14097  ? 211 LEU B O    1 
ATOM   6512 O  O    C LEU B  1 211 ? -45.28700 -13.27300 22.99200  0.464 16.62185  ? 211 LEU B O    1 
ATOM   6513 C  CB   A LEU B  1 211 ? -46.91700 -10.70700 23.49400  0.295 17.27528  ? 211 LEU B CB   1 
ATOM   6514 C  CB   B LEU B  1 211 ? -46.89000 -10.71200 23.49100  0.240 16.84278  ? 211 LEU B CB   1 
ATOM   6515 C  CB   C LEU B  1 211 ? -46.90500 -10.76600 23.32500  0.464 18.15647  ? 211 LEU B CB   1 
ATOM   6516 C  CG   A LEU B  1 211 ? -48.12900 -11.11000 24.34700  0.295 15.56688  ? 211 LEU B CG   1 
ATOM   6517 C  CG   B LEU B  1 211 ? -48.08600 -11.11900 24.35600  0.240 16.36172  ? 211 LEU B CG   1 
ATOM   6518 C  CG   C LEU B  1 211 ? -48.18700 -11.47800 23.75900  0.464 16.31745  ? 211 LEU B CG   1 
ATOM   6519 C  CD1  A LEU B  1 211 ? -49.26900 -10.10900 24.16500  0.295 20.24127  ? 211 LEU B CD1  1 
ATOM   6520 C  CD1  B LEU B  1 211 ? -49.21300 -10.11300 24.17200  0.240 20.21690  ? 211 LEU B CD1  1 
ATOM   6521 C  CD1  C LEU B  1 211 ? -48.44900 -11.08300 25.18300  0.464 16.59481  ? 211 LEU B CD1  1 
ATOM   6522 C  CD2  A LEU B  1 211 ? -48.59500 -12.51400 23.98900  0.295 16.74070  ? 211 LEU B CD2  1 
ATOM   6523 C  CD2  B LEU B  1 211 ? -48.54200 -12.51900 23.99400  0.240 16.35781  ? 211 LEU B CD2  1 
ATOM   6524 C  CD2  C LEU B  1 211 ? -49.34200 -11.10200 22.86100  0.464 16.68835  ? 211 LEU B CD2  1 
ATOM   6525 H  H    A LEU B  1 211 ? -44.59500 -10.73600 22.33700  0.295 18.42941  ? 211 LEU B H    1 
ATOM   6526 H  H    B LEU B  1 211 ? -44.57400 -10.75600 22.33700  0.240 18.74046  ? 211 LEU B H    1 
ATOM   6527 H  H    C LEU B  1 211 ? -44.58200 -10.73800 22.32800  0.464 19.02914  ? 211 LEU B H    1 
ATOM   6528 H  HA   A LEU B  1 211 ? -45.44400 -10.74700 24.92400  0.295 19.21028  ? 211 LEU B HA   1 
ATOM   6529 H  HA   B LEU B  1 211 ? -45.43000 -10.75800 24.92600  0.240 19.13189  ? 211 LEU B HA   1 
ATOM   6530 H  HA   C LEU B  1 211 ? -45.53100 -10.75000 24.88100  0.464 19.58624  ? 211 LEU B HA   1 
ATOM   6531 H  HB2  A LEU B  1 211 ? -46.94400 -9.74200  23.40400  0.295 20.73290  ? 211 LEU B HB2  1 
ATOM   6532 H  HB2  B LEU B  1 211 ? -46.91800 -9.74700  23.39900  0.240 20.21390  ? 211 LEU B HB2  1 
ATOM   6533 H  HB2  C LEU B  1 211 ? -47.06200 -9.82000  23.47200  0.464 21.79033  ? 211 LEU B HB2  1 
ATOM   6534 H  HB3  A LEU B  1 211 ? -47.03100 -11.12500 22.62600  0.295 20.73290  ? 211 LEU B HB3  1 
ATOM   6535 H  HB3  B LEU B  1 211 ? -47.00700 -11.13200 22.62400  0.240 20.21390  ? 211 LEU B HB3  1 
ATOM   6536 H  HB3  C LEU B  1 211 ? -46.81000 -10.94300 22.37600  0.464 21.79033  ? 211 LEU B HB3  1 
ATOM   6537 H  HG   A LEU B  1 211 ? -47.86800 -11.10800 25.28100  0.295 18.68282  ? 211 LEU B HG   1 
ATOM   6538 H  HG   B LEU B  1 211 ? -47.83200 -11.12400 25.29200  0.240 19.63662  ? 211 LEU B HG   1 
ATOM   6539 H  HG   C LEU B  1 211 ? -48.09600 -12.44200 23.69300  0.464 19.58350  ? 211 LEU B HG   1 
ATOM   6540 H  HD11 A LEU B  1 211 ? -50.01500 -10.37600 24.72500  0.295 24.29209  ? 211 LEU B HD11 1 
ATOM   6541 H  HD11 B LEU B  1 211 ? -49.96400 -10.37600 24.72700  0.240 24.26284  ? 211 LEU B HD11 1 
ATOM   6542 H  HD11 C LEU B  1 211 ? -49.36600 -11.30700 25.40900  0.464 19.91633  ? 211 LEU B HD11 1 
ATOM   6543 H  HD12 A LEU B  1 211 ? -48.96000 -9.22700  24.42400  0.295 24.29209  ? 211 LEU B HD12 1 
ATOM   6544 H  HD12 B LEU B  1 211 ? -48.89900 -9.23400  24.43600  0.240 24.26284  ? 211 LEU B HD12 1 
ATOM   6545 H  HD12 C LEU B  1 211 ? -47.83800 -11.56500 25.76200  0.464 19.91633  ? 211 LEU B HD12 1 
ATOM   6546 H  HD13 A LEU B  1 211 ? -49.54000 -10.10500 23.23300  0.295 24.29209  ? 211 LEU B HD13 1 
ATOM   6547 H  HD13 B LEU B  1 211 ? -49.47800 -10.10300 23.23900  0.240 24.26284  ? 211 LEU B HD13 1 
ATOM   6548 H  HD13 C LEU B  1 211 ? -48.31000 -10.12800 25.27700  0.464 19.91633  ? 211 LEU B HD13 1 
ATOM   6549 H  HD21 A LEU B  1 211 ? -49.44100 -12.68800 24.43100  0.295 20.09140  ? 211 LEU B HD21 1 
ATOM   6550 H  HD21 B LEU B  1 211 ? -49.39000 -12.69800 24.43000  0.240 19.63194  ? 211 LEU B HD21 1 
ATOM   6551 H  HD21 C LEU B  1 211 ? -50.17400 -11.33400 23.30200  0.464 20.02858  ? 211 LEU B HD21 1 
ATOM   6552 H  HD22 A LEU B  1 211 ? -48.70700 -12.57400 23.02700  0.295 20.09140  ? 211 LEU B HD22 1 
ATOM   6553 H  HD22 B LEU B  1 211 ? -48.64600 -12.57900 23.03100  0.240 19.63194  ? 211 LEU B HD22 1 
ATOM   6554 H  HD22 C LEU B  1 211 ? -49.31300 -10.14700 22.69200  0.464 20.02858  ? 211 LEU B HD22 1 
ATOM   6555 H  HD23 A LEU B  1 211 ? -47.92900 -13.15300 24.28500  0.295 20.09140  ? 211 LEU B HD23 1 
ATOM   6556 H  HD23 B LEU B  1 211 ? -47.87500 -13.15600 24.29400  0.240 19.63194  ? 211 LEU B HD23 1 
ATOM   6557 H  HD23 C LEU B  1 211 ? -49.26400 -11.58800 22.02500  0.464 20.02858  ? 211 LEU B HD23 1 
ATOM   6558 N  N    . ILE B  1 212 ? -45.41500 -13.18200 25.24300  1.000 16.38106  ? 212 ILE B N    1 
ATOM   6559 C  CA   . ILE B  1 212 ? -45.32900 -14.62000 25.43300  1.000 16.15849  ? 212 ILE B CA   1 
ATOM   6560 C  C    . ILE B  1 212 ? -46.59700 -15.11400 26.09600  1.000 18.69996  ? 212 ILE B C    1 
ATOM   6561 O  O    . ILE B  1 212 ? -46.99600 -14.62000 27.16400  1.000 18.25432  ? 212 ILE B O    1 
ATOM   6562 C  CB   . ILE B  1 212 ? -44.08500 -15.00400 26.24700  1.000 17.78157  ? 212 ILE B CB   1 
ATOM   6563 C  CG1  . ILE B  1 212 ? -42.83900 -14.78800 25.37200  1.000 19.83491  ? 212 ILE B CG1  1 
ATOM   6564 C  CG2  . ILE B  1 212 ? -44.19100 -16.47000 26.74600  1.000 19.31158  ? 212 ILE B CG2  1 
ATOM   6565 C  CD1  . ILE B  1 212 ? -41.51200 -14.81600 26.12000  1.000 22.66035  ? 212 ILE B CD1  1 
ATOM   6566 H  H    . ILE B  1 212 ? -45.47500 -12.74300 25.98000  1.000 19.65983  ? 212 ILE B H    1 
ATOM   6567 H  HA   . ILE B  1 212 ? -45.28100 -15.04900 24.56500  1.000 19.39275  ? 212 ILE B HA   1 
ATOM   6568 H  HB   . ILE B  1 212 ? -44.01700 -14.44000 27.03400  1.000 21.34045  ? 212 ILE B HB   1 
ATOM   6569 H  HG12 . ILE B  1 212 ? -42.81000 -15.48900 24.70200  1.000 23.80445  ? 212 ILE B HG12 1 
ATOM   6570 H  HG13 . ILE B  1 212 ? -42.91200 -13.92200 24.94300  1.000 23.80445  ? 212 ILE B HG13 1 
ATOM   6571 H  HG21 . ILE B  1 212 ? -43.32800 -16.75100 27.08800  1.000 23.17646  ? 212 ILE B HG21 1 
ATOM   6572 H  HG22 . ILE B  1 212 ? -44.85700 -16.51700 27.45000  1.000 23.17646  ? 212 ILE B HG22 1 
ATOM   6573 H  HG23 . ILE B  1 212 ? -44.45300 -17.03800 26.00400  1.000 23.17646  ? 212 ILE B HG23 1 
ATOM   6574 H  HD11 . ILE B  1 212 ? -40.79600 -14.60400 25.50100  1.000 27.19498  ? 212 ILE B HD11 1 
ATOM   6575 H  HD12 . ILE B  1 212 ? -41.53700 -14.16000 26.83400  1.000 27.19498  ? 212 ILE B HD12 1 
ATOM   6576 H  HD13 . ILE B  1 212 ? -41.37700 -15.70300 26.49000  1.000 27.19498  ? 212 ILE B HD13 1 
ATOM   6577 N  N    . PHE B  1 213 ? -47.25700 -16.06100 25.44200  1.000 16.72742  ? 213 PHE B N    1 
ATOM   6578 C  CA   . PHE B  1 213 ? -48.35500 -16.81600 26.03800  1.000 16.84269  ? 213 PHE B CA   1 
ATOM   6579 C  C    . PHE B  1 213 ? -47.73200 -18.09500 26.59700  1.000 19.73817  ? 213 PHE B C    1 
ATOM   6580 O  O    . PHE B  1 213 ? -47.12900 -18.89200 25.85600  1.000 20.29712  ? 213 PHE B O    1 
ATOM   6581 C  CB   . PHE B  1 213 ? -49.41800 -17.17200 25.00600  1.000 17.65500  ? 213 PHE B CB   1 
ATOM   6582 C  CG   . PHE B  1 213 ? -50.25000 -16.01700 24.52900  1.000 16.20023  ? 213 PHE B CG   1 
ATOM   6583 C  CD1  . PHE B  1 213 ? -51.16600 -15.41300 25.39200  1.000 18.50395  ? 213 PHE B CD1  1 
ATOM   6584 C  CD2  . PHE B  1 213 ? -50.20100 -15.57700 23.22200  1.000 17.72372  ? 213 PHE B CD2  1 
ATOM   6585 C  CE1  . PHE B  1 213 ? -51.94500 -14.36300 24.96800  1.000 20.04792  ? 213 PHE B CE1  1 
ATOM   6586 C  CE2  . PHE B  1 213 ? -50.98400 -14.54600 22.77000  1.000 18.87093  ? 213 PHE B CE2  1 
ATOM   6587 C  CZ   . PHE B  1 213 ? -51.90400 -13.93200 23.65500  1.000 18.63421  ? 213 PHE B CZ   1 
ATOM   6588 H  H    . PHE B  1 213 ? -47.08400 -16.29000 24.63100  1.000 20.07546  ? 213 PHE B H    1 
ATOM   6589 H  HA   . PHE B  1 213 ? -48.78600 -16.29800 26.73500  1.000 20.21379  ? 213 PHE B HA   1 
ATOM   6590 H  HB2  . PHE B  1 213 ? -48.97700 -17.55400 24.23100  1.000 21.18856  ? 213 PHE B HB2  1 
ATOM   6591 H  HB3  . PHE B  1 213 ? -50.02100 -17.82300 25.39900  1.000 21.18856  ? 213 PHE B HB3  1 
ATOM   6592 H  HD1  . PHE B  1 213 ? -51.25000 -15.72400 26.26400  1.000 22.20730  ? 213 PHE B HD1  1 
ATOM   6593 H  HD2  . PHE B  1 213 ? -49.61800 -15.99300 22.62800  1.000 21.27102  ? 213 PHE B HD2  1 
ATOM   6594 H  HE1  . PHE B  1 213 ? -52.50700 -13.93600 25.57300  1.000 24.06006  ? 213 PHE B HE1  1 
ATOM   6595 H  HE2  . PHE B  1 213 ? -50.91200 -14.25200 21.89100  1.000 22.64768  ? 213 PHE B HE2  1 
ATOM   6596 H  HZ   . PHE B  1 213 ? -52.46800 -13.25400 23.36000  1.000 22.36361  ? 213 PHE B HZ   1 
ATOM   6597 N  N    . ALA B  1 214 ? -47.85700 -18.28300 27.89600  1.000 19.54697  ? 214 ALA B N    1 
ATOM   6598 C  CA   . ALA B  1 214 ? -47.40800 -19.47000 28.59900  1.000 18.97394  ? 214 ALA B CA   1 
ATOM   6599 C  C    . ALA B  1 214 ? -48.61300 -20.31800 28.93900  1.000 20.11675  ? 214 ALA B C    1 
ATOM   6600 O  O    . ALA B  1 214 ? -49.63900 -19.80500 29.38100  1.000 23.19708  ? 214 ALA B O    1 
ATOM   6601 C  CB   . ALA B  1 214 ? -46.70800 -19.06000 29.88700  1.000 20.67436  ? 214 ALA B CB   1 
ATOM   6602 H  H    . ALA B  1 214 ? -48.21700 -17.70500 28.42200  1.000 23.45892  ? 214 ALA B H    1 
ATOM   6603 H  HA   . ALA B  1 214 ? -46.80000 -19.98900 28.05000  1.000 22.77129  ? 214 ALA B HA   1 
ATOM   6604 H  HB1  . ALA B  1 214 ? -46.41200 -19.85700 30.35300  1.000 24.81179  ? 214 ALA B HB1  1 
ATOM   6605 H  HB2  . ALA B  1 214 ? -45.94500 -18.50200 29.66800  1.000 24.81179  ? 214 ALA B HB2  1 
ATOM   6606 H  HB3  . ALA B  1 214 ? -47.33100 -18.56500 30.44100  1.000 24.81179  ? 214 ALA B HB3  1 
ATOM   6607 N  N    . CYS B  1 215 ? -48.51100 -21.61100 28.72500  1.000 20.13224  ? 215 CYS B N    1 
ATOM   6608 C  CA   . CYS B  1 215 ? -49.62300 -22.52000 29.01200  1.000 22.74909  ? 215 CYS B CA   1 
ATOM   6609 C  C    . CYS B  1 215 ? -49.35000 -23.20500 30.35100  1.000 23.86379  ? 215 CYS B C    1 
ATOM   6610 O  O    . CYS B  1 215 ? -48.42300 -24.01000 30.47100  1.000 24.75926  ? 215 CYS B O    1 
ATOM   6611 C  CB   . CYS B  1 215 ? -49.79500 -23.52800 27.88200  1.000 21.61587  ? 215 CYS B CB   1 
ATOM   6612 S  SG   . CYS B  1 215 ? -50.31200 -22.75600 26.32200  1.000 21.83821  ? 215 CYS B SG   1 
ATOM   6613 H  H    . CYS B  1 215 ? -47.80900 -21.99700 28.41200  1.000 24.16125  ? 215 CYS B H    1 
ATOM   6614 H  HA   . CYS B  1 215 ? -50.44900 -22.01800 29.09500  1.000 27.30147  ? 215 CYS B HA   1 
ATOM   6615 H  HB2  . CYS B  1 215 ? -48.94900 -23.97700 27.72900  1.000 25.94160  ? 215 CYS B HB2  1 
ATOM   6616 H  HB3  . CYS B  1 215 ? -50.47200 -24.17400 28.13600  1.000 25.94160  ? 215 CYS B HB3  1 
ATOM   6617 N  N    . GLU B  1 216 ? -50.14000 -22.86000 31.36700  1.000 22.93523  ? 216 GLU B N    1 
ATOM   6618 C  CA   . GLU B  1 216 ? -49.81100 -23.18200 32.75900  1.000 24.49094  ? 216 GLU B CA   1 
ATOM   6619 C  C    . GLU B  1 216 ? -49.38200 -24.63200 32.94900  1.000 24.90936  ? 216 GLU B C    1 
ATOM   6620 O  O    . GLU B  1 216 ? -48.41400 -24.90900 33.66500  1.000 26.48067  ? 216 GLU B O    1 
ATOM   6621 C  CB   . GLU B  1 216 ? -51.00600 -22.86700 33.66000  1.000 24.48853  ? 216 GLU B CB   1 
ATOM   6622 C  CG   . GLU B  1 216 ? -50.66600 -23.07300 35.13700  1.000 26.43706  ? 216 GLU B CG   1 
ATOM   6623 C  CD   . GLU B  1 216 ? -51.87500 -23.06300 36.03600  1.000 33.32671  ? 216 GLU B CD   1 
ATOM   6624 O  OE1  . GLU B  1 216 ? -53.01300 -23.25500 35.55500  1.000 32.05878  ? 216 GLU B OE1  1 
ATOM   6625 O  OE2  . GLU B  1 216 ? -51.67900 -22.88400 37.25700  1.000 37.90077  ? 216 GLU B OE2  1 
ATOM   6626 H  H    . GLU B  1 216 ? -50.88200 -22.43400 31.27900  1.000 27.52484  ? 216 GLU B H    1 
ATOM   6627 H  HA   . GLU B  1 216 ? -49.06000 -22.62400 33.01600  1.000 29.39169  ? 216 GLU B HA   1 
ATOM   6628 H  HB2  . GLU B  1 216 ? -51.26700 -21.94100 33.53400  1.000 29.38880  ? 216 GLU B HB2  1 
ATOM   6629 H  HB3  . GLU B  1 216 ? -51.74300 -23.45400 33.43200  1.000 29.38880  ? 216 GLU B HB3  1 
ATOM   6630 H  HG2  . GLU B  1 216 ? -50.22600 -23.93100 35.24100  1.000 31.72704  ? 216 GLU B HG2  1 
ATOM   6631 H  HG3  . GLU B  1 216 ? -50.07500 -22.35900 35.42500  1.000 31.72704  ? 216 GLU B HG3  1 
ATOM   6632 N  N    . ARG B  1 217 ? -50.13500 -25.57600 32.37900  1.000 26.10815  ? 217 ARG B N    1 
ATOM   6633 C  CA   . ARG B  1 217 ? -49.95100 -26.99700 32.63600  1.000 29.68298  ? 217 ARG B CA   1 
ATOM   6634 C  C    . ARG B  1 217 ? -49.13300 -27.68000 31.54100  1.000 28.56474  ? 217 ARG B C    1 
ATOM   6635 O  O    . ARG B  1 217 ? -49.12200 -28.91600 31.46300  1.000 33.45716  ? 217 ARG B O    1 
ATOM   6636 C  CB   . ARG B  1 217 ? -51.29900 -27.69300 32.79900  1.000 28.25478  ? 217 ARG B CB   1 
ATOM   6637 C  CG   . ARG B  1 217 ? -52.08100 -27.26000 34.02400  1.000 40.15940  ? 217 ARG B CG   1 
ATOM   6638 C  CD   . ARG B  1 217 ? -53.35200 -28.10200 34.18900  1.000 55.89660  ? 217 ARG B CD   1 
ATOM   6639 N  NE   . ARG B  1 217 ? -53.26800 -29.03100 35.31200  1.000 78.37429  ? 217 ARG B NE   1 
ATOM   6640 C  CZ   . ARG B  1 217 ? -53.91500 -28.88100 36.46100  1.000 80.88664  ? 217 ARG B CZ   1 
ATOM   6641 N  NH1  . ARG B  1 217 ? -54.74100 -27.86600 36.66400  1.000 76.40433  ? 217 ARG B NH1  1 
ATOM   6642 N  NH2  . ARG B  1 217 ? -53.73000 -29.77400 37.43100  1.000 84.33777  ? 217 ARG B NH2  1 
ATOM   6643 H  H    . ARG B  1 217 ? -50.77300 -25.40900 31.82700  1.000 31.33234  ? 217 ARG B H    1 
ATOM   6644 H  HA   . ARG B  1 217 ? -49.46900 -27.09300 33.47300  1.000 35.62214  ? 217 ARG B HA   1 
ATOM   6645 H  HB2  . ARG B  1 217 ? -51.84400 -27.50000 32.02000  1.000 33.90830  ? 217 ARG B HB2  1 
ATOM   6646 H  HB3  . ARG B  1 217 ? -51.14800 -28.64900 32.87000  1.000 33.90830  ? 217 ARG B HB3  1 
ATOM   6647 H  HG2  . ARG B  1 217 ? -51.53200 -27.37400 34.81500  1.000 48.19384  ? 217 ARG B HG2  1 
ATOM   6648 H  HG3  . ARG B  1 217 ? -52.33900 -26.33000 33.93100  1.000 48.19384  ? 217 ARG B HG3  1 
ATOM   6649 H  HD2  . ARG B  1 217 ? -54.10600 -27.51200 34.34200  1.000 67.07848  ? 217 ARG B HD2  1 
ATOM   6650 H  HD3  . ARG B  1 217 ? -53.49500 -28.62000 33.38100  1.000 67.07848  ? 217 ARG B HD3  1 
ATOM   6651 H  HE   . ARG B  1 217 ? -52.76500 -29.72300 35.22300  1.000 94.05171  ? 217 ARG B HE   1 
ATOM   6652 H  HH11 . ARG B  1 217 ? -54.86800 -27.28400 36.04400  1.000 91.68776  ? 217 ARG B HH11 1 
ATOM   6653 H  HH12 . ARG B  1 217 ? -55.15000 -27.78800 37.41700  1.000 91.68776  ? 217 ARG B HH12 1 
ATOM   6654 H  HH21 . ARG B  1 217 ? -53.19700 -30.43700 37.30900  1.000 101.20788 ? 217 ARG B HH21 1 
ATOM   6655 H  HH22 . ARG B  1 217 ? -54.14400 -29.68700 38.18000  1.000 101.20788 ? 217 ARG B HH22 1 
ATOM   6656 N  N    . ASP B  1 218 ? -48.41700 -26.90200 30.73100  1.000 25.88865  ? 218 ASP B N    1 
ATOM   6657 C  CA   . ASP B  1 218 ? -47.62900 -27.43300 29.63100  1.000 25.08577  ? 218 ASP B CA   1 
ATOM   6658 C  C    . ASP B  1 218 ? -46.58800 -28.41200 30.14700  1.000 28.13349  ? 218 ASP B C    1 
ATOM   6659 O  O    . ASP B  1 218 ? -45.78800 -28.07700 31.02600  1.000 26.62302  ? 218 ASP B O    1 
ATOM   6660 C  CB   . ASP B  1 218 ? -46.93500 -26.24800 28.96100  1.000 23.84792  ? 218 ASP B CB   1 
ATOM   6661 C  CG   . ASP B  1 218 ? -46.38200 -26.58000 27.60700  1.000 24.67477  ? 218 ASP B CG   1 
ATOM   6662 O  OD1  . ASP B  1 218 ? -46.02800 -27.74000 27.38000  1.000 25.84212  ? 218 ASP B OD1  1 
ATOM   6663 O  OD2  . ASP B  1 218 ? -46.29800 -25.65100 26.77300  1.000 23.42793  ? 218 ASP B OD2  1 
ATOM   6664 H  H    . ASP B  1 218 ? -48.37100 -26.04700 30.80200  1.000 31.06895  ? 218 ASP B H    1 
ATOM   6665 H  HA   . ASP B  1 218 ? -48.19400 -27.90200 28.99800  1.000 30.10548  ? 218 ASP B HA   1 
ATOM   6666 H  HB2  . ASP B  1 218 ? -47.57500 -25.52800 28.85400  1.000 28.62007  ? 218 ASP B HB2  1 
ATOM   6667 H  HB3  . ASP B  1 218 ? -46.19900 -25.95700 29.52100  1.000 28.62007  ? 218 ASP B HB3  1 
ATOM   6668 N  N    . SER B  1 219 ? -46.61900 -29.64200 29.63700  1.000 25.58558  ? 219 SER B N    1 
ATOM   6669 C  CA   . SER B  1 219 ? -45.65800 -30.66600 30.02200  1.000 29.65233  ? 219 SER B CA   1 
ATOM   6670 C  C    . SER B  1 219 ? -44.63600 -30.92900 28.93200  1.000 29.52153  ? 219 SER B C    1 
ATOM   6671 O  O    . SER B  1 219 ? -43.73800 -31.75600 29.11500  1.000 34.14268  ? 219 SER B O    1 
ATOM   6672 C  CB   . SER B  1 219 ? -46.39700 -31.96200 30.37100  1.000 36.68604  ? 219 SER B CB   1 
ATOM   6673 O  OG   . SER B  1 219 ? -47.01500 -32.50100 29.21700  1.000 41.28716  ? 219 SER B OG   1 
ATOM   6674 H  H    . SER B  1 219 ? -47.19600 -29.90900 29.05800  1.000 30.70526  ? 219 SER B H    1 
ATOM   6675 H  HA   . SER B  1 219 ? -45.18000 -30.37900 30.81600  1.000 35.58536  ? 219 SER B HA   1 
ATOM   6676 H  HB2  . SER B  1 219 ? -45.76200 -32.60600 30.72100  1.000 44.02581  ? 219 SER B HB2  1 
ATOM   6677 H  HB3  . SER B  1 219 ? -47.07700 -31.77100 31.03500  1.000 44.02581  ? 219 SER B HB3  1 
ATOM   6678 H  HG   . SER B  1 219 ? -47.48000 -31.91200 28.83800  1.000 49.54716  ? 219 SER B HG   1 
ATOM   6679 N  N    . ILE B  1 220 ? -44.75600 -30.25400 27.79700  1.000 27.31353  ? 220 ILE B N    1 
ATOM   6680 C  CA   . ILE B  1 220 ? -43.85300 -30.44200 26.66800  1.000 27.33189  ? 220 ILE B CA   1 
ATOM   6681 C  C    . ILE B  1 220 ? -42.80800 -29.33800 26.60800  1.000 28.09837  ? 220 ILE B C    1 
ATOM   6682 O  O    . ILE B  1 220 ? -41.62200 -29.60000 26.37500  1.000 27.86442  ? 220 ILE B O    1 
ATOM   6683 C  CB   . ILE B  1 220 ? -44.69800 -30.50400 25.37500  1.000 30.19445  ? 220 ILE B CB   1 
ATOM   6684 C  CG1  . ILE B  1 220 ? -45.56700 -31.76300 25.39200  1.000 35.66655  ? 220 ILE B CG1  1 
ATOM   6685 C  CG2  . ILE B  1 220 ? -43.81400 -30.49300 24.17300  1.000 28.28838  ? 220 ILE B CG2  1 
ATOM   6686 C  CD1  . ILE B  1 220 ? -46.55200 -31.86800 24.26400  1.000 36.32408  ? 220 ILE B CD1  1 
ATOM   6687 H  H    . ILE B  1 220 ? -45.36700 -29.66700 27.65100  1.000 32.77880  ? 220 ILE B H    1 
ATOM   6688 H  HA   . ILE B  1 220 ? -43.36800 -31.27700 26.76100  1.000 32.80083  ? 220 ILE B HA   1 
ATOM   6689 H  HB   . ILE B  1 220 ? -45.27200 -29.72300 25.33500  1.000 36.23590  ? 220 ILE B HB   1 
ATOM   6690 H  HG12 . ILE B  1 220 ? -44.98600 -32.53800 25.34400  1.000 42.80242  ? 220 ILE B HG12 1 
ATOM   6691 H  HG13 . ILE B  1 220 ? -46.07100 -31.77700 26.22100  1.000 42.80242  ? 220 ILE B HG13 1 
ATOM   6692 H  HG21 . ILE B  1 220 ? -44.33800 -30.73600 23.39400  1.000 33.94862  ? 220 ILE B HG21 1 
ATOM   6693 H  HG22 . ILE B  1 220 ? -43.44700 -29.60200 24.05900  1.000 33.94862  ? 220 ILE B HG22 1 
ATOM   6694 H  HG23 . ILE B  1 220 ? -43.09600 -31.13200 24.30300  1.000 33.94862  ? 220 ILE B HG23 1 
ATOM   6695 H  HD11 . ILE B  1 220 ? -47.20200 -32.55600 24.47600  1.000 43.59146  ? 220 ILE B HD11 1 
ATOM   6696 H  HD12 . ILE B  1 220 ? -46.99800 -31.01400 24.15400  1.000 43.59146  ? 220 ILE B HD12 1 
ATOM   6697 H  HD13 . ILE B  1 220 ? -46.07700 -32.10000 23.45100  1.000 43.59146  ? 220 ILE B HD13 1 
ATOM   6698 N  N    . ALA B  1 221 ? -43.25000 -28.10000 26.79800  1.000 27.12688  ? 221 ALA B N    1 
ATOM   6699 C  CA   . ALA B  1 221 ? -42.39400 -26.93400 26.97600  1.000 26.72674  ? 221 ALA B CA   1 
ATOM   6700 C  C    . ALA B  1 221 ? -42.75000 -26.32500 28.33000  1.000 24.52834  ? 221 ALA B C    1 
ATOM   6701 O  O    . ALA B  1 221 ? -43.38300 -25.26500 28.40200  1.000 24.42592  ? 221 ALA B O    1 
ATOM   6702 C  CB   . ALA B  1 221 ? -42.59400 -25.91800 25.85800  1.000 24.57948  ? 221 ALA B CB   1 
ATOM   6703 H  H    . ALA B  1 221 ? -44.08600 -27.90100 26.82900  1.000 32.55481  ? 221 ALA B H    1 
ATOM   6704 H  HA   . ALA B  1 221 ? -41.46000 -27.19700 26.96700  1.000 32.07465  ? 221 ALA B HA   1 
ATOM   6705 H  HB1  . ALA B  1 221 ? -41.98900 -25.17200 25.99700  1.000 29.49794  ? 221 ALA B HB1  1 
ATOM   6706 H  HB2  . ALA B  1 221 ? -42.40500 -26.34300 25.00700  1.000 29.49794  ? 221 ALA B HB2  1 
ATOM   6707 H  HB3  . ALA B  1 221 ? -43.51300 -25.60600 25.87600  1.000 29.49794  ? 221 ALA B HB3  1 
ATOM   6708 N  N    . PRO B  1 222 ? -42.36700 -26.97700 29.42100  1.000 24.71699  ? 222 PRO B N    1 
ATOM   6709 C  CA   . PRO B  1 222 ? -42.82600 -26.50900 30.73100  1.000 26.00559  ? 222 PRO B CA   1 
ATOM   6710 C  C    . PRO B  1 222 ? -42.49300 -25.03900 30.92100  1.000 23.56584  ? 222 PRO B C    1 
ATOM   6711 O  O    . PRO B  1 222 ? -41.38800 -24.59200 30.61600  1.000 25.22269  ? 222 PRO B O    1 
ATOM   6712 C  CB   . PRO B  1 222 ? -42.03900 -27.38100 31.71500  1.000 31.77821  ? 222 PRO B CB   1 
ATOM   6713 C  CG   . PRO B  1 222 ? -41.69100 -28.59000 30.95400  1.000 33.21716  ? 222 PRO B CG   1 
ATOM   6714 C  CD   . PRO B  1 222 ? -41.54800 -28.19400 29.51300  1.000 29.28082  ? 222 PRO B CD   1 
ATOM   6715 H  HA   . PRO B  1 222 ? -43.77700 -26.66100 30.84100  1.000 31.20927  ? 222 PRO B HA   1 
ATOM   6716 H  HB2  . PRO B  1 222 ? -41.24200 -26.91300 32.00800  1.000 38.13641  ? 222 PRO B HB2  1 
ATOM   6717 H  HB3  . PRO B  1 222 ? -42.59400 -27.60000 32.48000  1.000 38.13641  ? 222 PRO B HB3  1 
ATOM   6718 H  HG2  . PRO B  1 222 ? -40.85400 -28.94900 31.29000  1.000 39.86316  ? 222 PRO B HG2  1 
ATOM   6719 H  HG3  . PRO B  1 222 ? -42.39800 -29.24600 31.05500  1.000 39.86316  ? 222 PRO B HG3  1 
ATOM   6720 H  HD2  . PRO B  1 222 ? -40.62100 -28.00500 29.29600  1.000 35.13955  ? 222 PRO B HD2  1 
ATOM   6721 H  HD3  . PRO B  1 222 ? -41.89100 -28.88700 28.92800  1.000 35.13955  ? 222 PRO B HD3  1 
ATOM   6722 N  N    . VAL B  1 223 ? -43.43300 -24.31500 31.51200  1.000 24.07768  ? 223 VAL B N    1 
ATOM   6723 C  CA   . VAL B  1 223 ? -43.29000 -22.87500 31.69600  1.000 24.16139  ? 223 VAL B CA   1 
ATOM   6724 C  C    . VAL B  1 223 ? -42.03900 -22.54300 32.49400  1.000 25.95503  ? 223 VAL B C    1 
ATOM   6725 O  O    . VAL B  1 223 ? -41.34400 -21.56000 32.21400  1.000 24.91546  ? 223 VAL B O    1 
ATOM   6726 C  CB   . VAL B  1 223 ? -44.56900 -22.32500 32.35700  1.000 26.96995  ? 223 VAL B CB   1 
ATOM   6727 C  CG1  . VAL B  1 223 ? -44.35600 -20.92700 32.87300  1.000 40.20908  ? 223 VAL B CG1  1 
ATOM   6728 C  CG2  . VAL B  1 223 ? -45.70700 -22.39700 31.39200  1.000 26.21456  ? 223 VAL B CG2  1 
ATOM   6729 H  H    . VAL B  1 223 ? -44.17000 -24.63300 31.81900  1.000 28.89578  ? 223 VAL B H    1 
ATOM   6730 H  HA   . VAL B  1 223 ? -43.18200 -22.45100 30.83000  1.000 28.99623  ? 223 VAL B HA   1 
ATOM   6731 H  HB   . VAL B  1 223 ? -44.79400 -22.87200 33.12600  1.000 32.36650  ? 223 VAL B HB   1 
ATOM   6732 H  HG11 . VAL B  1 223 ? -45.22000 -20.50900 33.01800  1.000 48.25346  ? 223 VAL B HG11 1 
ATOM   6733 H  HG12 . VAL B  1 223 ? -43.86600 -20.97000 33.70900  1.000 48.25346  ? 223 VAL B HG12 1 
ATOM   6734 H  HG13 . VAL B  1 223 ? -43.85000 -20.42200 32.21800  1.000 48.25346  ? 223 VAL B HG13 1 
ATOM   6735 H  HG21 . VAL B  1 223 ? -46.48000 -21.96000 31.78200  1.000 31.46003  ? 223 VAL B HG21 1 
ATOM   6736 H  HG22 . VAL B  1 223 ? -45.45400 -21.94900 30.57000  1.000 31.46003  ? 223 VAL B HG22 1 
ATOM   6737 H  HG23 . VAL B  1 223 ? -45.91000 -23.32800 31.21100  1.000 31.46003  ? 223 VAL B HG23 1 
ATOM   6738 N  N    . ARG B  1 224 ? -41.73300 -23.34500 33.49700  1.000 25.50926  ? 224 ARG B N    1 
ATOM   6739 C  CA   . ARG B  1 224 ? -40.58900 -23.01800 34.34900  1.000 27.31740  ? 224 ARG B CA   1 
ATOM   6740 C  C    . ARG B  1 224 ? -39.25500 -23.17000 33.62100  1.000 25.08190  ? 224 ARG B C    1 
ATOM   6741 O  O    . ARG B  1 224 ? -38.25700 -22.60000 34.06500  1.000 26.71712  ? 224 ARG B O    1 
ATOM   6742 C  CB   . ARG B  1 224 ? -40.61300 -23.90700 35.58000  1.000 32.26454  ? 224 ARG B CB   1 
ATOM   6743 C  CG   . ARG B  1 224 ? -40.34300 -25.35800 35.27300  1.000 48.05306  ? 224 ARG B CG   1 
ATOM   6744 C  CD   . ARG B  1 224 ? -41.13500 -26.28600 36.19500  1.000 76.53202  ? 224 ARG B CD   1 
ATOM   6745 N  NE   . ARG B  1 224 ? -40.79800 -27.68500 35.96100  1.000 81.86613  ? 224 ARG B NE   1 
ATOM   6746 C  CZ   . ARG B  1 224 ? -41.67500 -28.68000 35.94300  1.000 84.72967  ? 224 ARG B CZ   1 
ATOM   6747 N  NH1  . ARG B  1 224 ? -42.97400 -28.46200 36.08700  1.000 68.14458  ? 224 ARG B NH1  1 
ATOM   6748 N  NH2  . ARG B  1 224 ? -41.23900 -29.92500 35.76900  1.000 81.16528  ? 224 ARG B NH2  1 
ATOM   6749 H  H    . ARG B  1 224 ? -42.15400 -24.06600 33.70600  1.000 30.61367  ? 224 ARG B H    1 
ATOM   6750 H  HA   . ARG B  1 224 ? -40.65800 -22.09300 34.63400  1.000 32.78344  ? 224 ARG B HA   1 
ATOM   6751 H  HB2  . ARG B  1 224 ? -39.93300 -23.60200 36.20100  1.000 38.72001  ? 224 ARG B HB2  1 
ATOM   6752 H  HB3  . ARG B  1 224 ? -41.48900 -23.84700 35.99300  1.000 38.72001  ? 224 ARG B HB3  1 
ATOM   6753 H  HG2  . ARG B  1 224 ? -40.60300 -25.54600 34.35700  1.000 57.66623  ? 224 ARG B HG2  1 
ATOM   6754 H  HG3  . ARG B  1 224 ? -39.39900 -25.54200 35.39400  1.000 57.66623  ? 224 ARG B HG3  1 
ATOM   6755 H  HD2  . ARG B  1 224 ? -40.92800 -26.07300 37.11900  1.000 91.84098  ? 224 ARG B HD2  1 
ATOM   6756 H  HD3  . ARG B  1 224 ? -42.08300 -26.16800 36.03200  1.000 91.84098  ? 224 ARG B HD3  1 
ATOM   6757 H  HE   . ARG B  1 224 ? -39.97100 -27.88000 35.82500  1.000 98.24192  ? 224 ARG B HE   1 
ATOM   6758 H  HH11 . ARG B  1 224 ? -43.26500 -27.66100 36.19600  1.000 81.77606  ? 224 ARG B HH11 1 
ATOM   6759 H  HH12 . ARG B  1 224 ? -43.52500 -29.12200 36.07200  1.000 81.77606  ? 224 ARG B HH12 1 
ATOM   6760 H  HH21 . ARG B  1 224 ? -40.39800 -30.07600 35.67000  1.000 97.40089  ? 224 ARG B HH21 1 
ATOM   6761 H  HH22 . ARG B  1 224 ? -41.79700 -30.57900 35.75500  1.000 97.40089  ? 224 ARG B HH22 1 
ATOM   6762 N  N    . SER B  1 225 ? -39.21500 -23.94600 32.54200  1.000 24.85082  ? 225 SER B N    1 
ATOM   6763 C  CA   . SER B  1 225 ? -38.00000 -24.18900 31.79000  1.000 26.75778  ? 225 SER B CA   1 
ATOM   6764 C  C    . SER B  1 225 ? -37.94400 -23.41000 30.47700  1.000 23.86816  ? 225 SER B C    1 
ATOM   6765 O  O    . SER B  1 225 ? -36.84800 -23.29100 29.89900  1.000 25.98196  ? 225 SER B O    1 
ATOM   6766 C  CB   . SER B  1 225 ? -37.90900 -25.67400 31.45000  1.000 29.29496  ? 225 SER B CB   1 
ATOM   6767 O  OG   . SER B  1 225 ? -37.71700 -26.42400 32.64700  1.000 38.79685  ? 225 SER B OG   1 
ATOM   6768 H  H    . SER B  1 225 ? -39.90100 -24.35300 32.22100  1.000 29.82355  ? 225 SER B H    1 
ATOM   6769 H  HA   . SER B  1 225 ? -37.23600 -23.93400 32.33100  1.000 32.11190  ? 225 SER B HA   1 
ATOM   6770 H  HB2  . SER B  1 225 ? -38.73300 -25.95600 31.02300  1.000 35.15651  ? 225 SER B HB2  1 
ATOM   6771 H  HB3  . SER B  1 225 ? -37.15800 -25.82200 30.85400  1.000 35.15651  ? 225 SER B HB3  1 
ATOM   6772 H  HG   . SER B  1 225 ? -37.95500 -27.22100 32.52700  1.000 46.55878  ? 225 SER B HG   1 
ATOM   6773 N  N    . HIS B  1 226 ? -39.07000 -22.87500 30.01400  1.000 21.92836  ? 226 HIS B N    1 
ATOM   6774 C  CA   . HIS B  1 226 ? -39.14200 -22.20100 28.72300  1.000 21.29472  ? 226 HIS B CA   1 
ATOM   6775 C  C    . HIS B  1 226 ? -39.78200 -20.83400 28.82000  1.000 20.15936  ? 226 HIS B C    1 
ATOM   6776 O  O    . HIS B  1 226 ? -39.08000 -19.84200 28.99800  1.000 21.38161  ? 226 HIS B O    1 
ATOM   6777 C  CB   . HIS B  1 226 ? -39.81400 -23.12500 27.69800  1.000 21.09093  ? 226 HIS B CB   1 
ATOM   6778 C  CG   . HIS B  1 226 ? -39.06100 -24.39100 27.45500  1.000 20.06898  ? 226 HIS B CG   1 
ATOM   6779 N  ND1  . HIS B  1 226 ? -38.09000 -24.48700 26.48600  1.000 23.53557  ? 226 HIS B ND1  1 
ATOM   6780 C  CD2  . HIS B  1 226 ? -39.09600 -25.59200 28.07600  1.000 23.32517  ? 226 HIS B CD2  1 
ATOM   6781 C  CE1  . HIS B  1 226 ? -37.57200 -25.69800 26.50700  1.000 26.66031  ? 226 HIS B CE1  1 
ATOM   6782 N  NE2  . HIS B  1 226 ? -38.16400 -26.39000 27.46600  1.000 25.49599  ? 226 HIS B NE2  1 
ATOM   6783 H  H    . HIS B  1 226 ? -39.81800 -22.88900 30.43700  1.000 26.31660  ? 226 HIS B H    1 
ATOM   6784 H  HA   . HIS B  1 226 ? -38.24700 -22.02100 28.39600  1.000 25.55622  ? 226 HIS B HA   1 
ATOM   6785 H  HB2  . HIS B  1 226 ? -40.69700 -23.36200 28.02200  1.000 25.31168  ? 226 HIS B HB2  1 
ATOM   6786 H  HB3  . HIS B  1 226 ? -39.88600 -22.65500 26.85300  1.000 25.31168  ? 226 HIS B HB3  1 
ATOM   6787 H  HD2  . HIS B  1 226 ? -39.64800 -25.83100 28.78500  1.000 27.99276  ? 226 HIS B HD2  1 
ATOM   6788 H  HE1  . HIS B  1 226 ? -36.90300 -26.01300 25.94300  1.000 31.99493  ? 226 HIS B HE1  1 
ATOM   6789 H  HE2  . HIS B  1 226 ? -37.99300 -27.20700 27.67300  1.000 30.59775  ? 226 HIS B HE2  1 
ATOM   6790 N  N    . ALA B  1 227 ? -41.11300 -20.76300 28.72600  1.000 20.38396  ? 227 ALA B N    1 
ATOM   6791 C  CA   . ALA B  1 227 ? -41.76700 -19.46600 28.60800  1.000 18.87892  ? 227 ALA B CA   1 
ATOM   6792 C  C    . ALA B  1 227 ? -41.32400 -18.49200 29.69600  1.000 20.11794  ? 227 ALA B C    1 
ATOM   6793 O  O    . ALA B  1 227 ? -41.06100 -17.31800 29.41000  1.000 20.26943  ? 227 ALA B O    1 
ATOM   6794 C  CB   . ALA B  1 227 ? -43.29300 -19.62600 28.61900  1.000 19.84793  ? 227 ALA B CB   1 
ATOM   6795 H  H    . ALA B  1 227 ? -41.64600 -21.43800 28.72700  1.000 24.46332  ? 227 ALA B H    1 
ATOM   6796 H  HA   . ALA B  1 227 ? -41.51000 -19.08600 27.75300  1.000 22.65726  ? 227 ALA B HA   1 
ATOM   6797 H  HB1  . ALA B  1 227 ? -43.70300 -18.75300 28.52100  1.000 23.82008  ? 227 ALA B HB1  1 
ATOM   6798 H  HB2  . ALA B  1 227 ? -43.55500 -20.20000 27.88200  1.000 23.82008  ? 227 ALA B HB2  1 
ATOM   6799 H  HB3  . ALA B  1 227 ? -43.56200 -20.02600 29.46100  1.000 23.82008  ? 227 ALA B HB3  1 
ATOM   6800 N  N    . SER B  1 228 ? -41.32400 -18.92700 30.96300  1.000 20.52809  ? 228 SER B N    1 
ATOM   6801 C  CA   . SER B  1 228 ? -40.98900 -18.00600 32.04800  1.000 21.44639  ? 228 SER B CA   1 
ATOM   6802 C  C    . SER B  1 228 ? -39.54800 -17.50800 31.96900  1.000 21.98334  ? 228 SER B C    1 
ATOM   6803 O  O    . SER B  1 228 ? -39.34000 -16.28500 31.99000  1.000 21.48042  ? 228 SER B O    1 
ATOM   6804 C  CB   . SER B  1 228 ? -41.35000 -18.61000 33.40800  1.000 20.83914  ? 228 SER B CB   1 
ATOM   6805 O  OG   . SER B  1 228 ? -40.98900 -17.70700 34.43500  1.000 24.85533  ? 228 SER B OG   1 
ATOM   6806 H  H    . SER B  1 228 ? -41.50900 -19.72900 31.21300  1.000 24.63627  ? 228 SER B H    1 
ATOM   6807 H  HA   . SER B  1 228 ? -41.55400 -17.22400 31.94400  1.000 25.73823  ? 228 SER B HA   1 
ATOM   6808 H  HB2  . SER B  1 228 ? -42.30600 -18.77300 33.44400  1.000 25.00953  ? 228 SER B HB2  1 
ATOM   6809 H  HB3  . SER B  1 228 ? -40.86700 -19.44300 33.52900  1.000 25.00953  ? 228 SER B HB3  1 
ATOM   6810 H  HG   . SER B  1 228 ? -40.15500 -17.61800 34.46000  1.000 29.82895  ? 228 SER B HG   1 
ATOM   6811 N  N    . PRO B  1 229 ? -38.52400 -18.36000 31.89600  1.000 21.89818  ? 229 PRO B N    1 
ATOM   6812 C  CA   . PRO B  1 229 ? -37.16200 -17.80700 31.78600  1.000 21.23712  ? 229 PRO B CA   1 
ATOM   6813 C  C    . PRO B  1 229 ? -36.93800 -17.03600 30.50000  1.000 20.87284  ? 229 PRO B C    1 
ATOM   6814 O  O    . PRO B  1 229 ? -36.14600 -16.09000 30.48600  1.000 22.06978  ? 229 PRO B O    1 
ATOM   6815 C  CB   . PRO B  1 229 ? -36.24500 -19.03600 31.88300  1.000 22.08590  ? 229 PRO B CB   1 
ATOM   6816 C  CG   . PRO B  1 229 ? -37.10800 -20.22000 31.65000  1.000 22.95533  ? 229 PRO B CG   1 
ATOM   6817 C  CD   . PRO B  1 229 ? -38.49400 -19.82000 32.14100  1.000 22.73773  ? 229 PRO B CD   1 
ATOM   6818 H  HA   . PRO B  1 229 ? -36.98300 -17.23300 32.54700  1.000 25.48711  ? 229 PRO B HA   1 
ATOM   6819 H  HB2  . PRO B  1 229 ? -35.55300 -18.97900 31.20600  1.000 26.50564  ? 229 PRO B HB2  1 
ATOM   6820 H  HB3  . PRO B  1 229 ? -35.84500 -19.07300 32.76500  1.000 26.50564  ? 229 PRO B HB3  1 
ATOM   6821 H  HG2  . PRO B  1 229 ? -37.12500 -20.43200 30.70300  1.000 27.54896  ? 229 PRO B HG2  1 
ATOM   6822 H  HG3  . PRO B  1 229 ? -36.76900 -20.97700 32.15300  1.000 27.54896  ? 229 PRO B HG3  1 
ATOM   6823 H  HD2  . PRO B  1 229 ? -39.18500 -20.27100 31.63200  1.000 27.28784  ? 229 PRO B HD2  1 
ATOM   6824 H  HD3  . PRO B  1 229 ? -38.59600 -20.01500 33.08600  1.000 27.28784  ? 229 PRO B HD3  1 
ATOM   6825 N  N    . PHE B  1 230 ? -37.61200 -17.40500 29.40700  1.000 19.74339  ? 230 PHE B N    1 
ATOM   6826 C  CA   . PHE B  1 230 ? -37.46200 -16.61900 28.18900  1.000 20.13928  ? 230 PHE B CA   1 
ATOM   6827 C  C    . PHE B  1 230 ? -37.96200 -15.19700 28.39800  1.000 20.45653  ? 230 PHE B C    1 
ATOM   6828 O  O    . PHE B  1 230 ? -37.30800 -14.23300 27.99900  1.000 21.10926  ? 230 PHE B O    1 
ATOM   6829 C  CB   . PHE B  1 230 ? -38.17700 -17.24100 26.98800  1.000 19.18765  ? 230 PHE B CB   1 
ATOM   6830 C  CG   . PHE B  1 230 ? -37.69500 -18.61000 26.61400  1.000 19.32981  ? 230 PHE B CG   1 
ATOM   6831 C  CD1  . PHE B  1 230 ? -36.48200 -19.12000 27.08700  1.000 21.22587  ? 230 PHE B CD1  1 
ATOM   6832 C  CD2  . PHE B  1 230 ? -38.46400 -19.41700 25.80300  1.000 20.38979  ? 230 PHE B CD2  1 
ATOM   6833 C  CE1  . PHE B  1 230 ? -36.07300 -20.40600 26.78300  1.000 19.77722  ? 230 PHE B CE1  1 
ATOM   6834 C  CE2  . PHE B  1 230 ? -38.07200 -20.70100 25.50100  1.000 20.66112  ? 230 PHE B CE2  1 
ATOM   6835 C  CZ   . PHE B  1 230 ? -36.87000 -21.19400 25.96200  1.000 19.37939  ? 230 PHE B CZ   1 
ATOM   6836 H  H    . PHE B  1 230 ? -38.14100 -18.08100 29.35000  1.000 23.69463  ? 230 PHE B H    1 
ATOM   6837 H  HA   . PHE B  1 230 ? -36.51500 -16.61200 27.97900  1.000 24.16970  ? 230 PHE B HA   1 
ATOM   6838 H  HB2  . PHE B  1 230 ? -39.12200 -17.30900 27.19300  1.000 23.02774  ? 230 PHE B HB2  1 
ATOM   6839 H  HB3  . PHE B  1 230 ? -38.04600 -16.66400 26.21800  1.000 23.02774  ? 230 PHE B HB3  1 
ATOM   6840 H  HD1  . PHE B  1 230 ? -35.93800 -18.58300 27.61800  1.000 25.47360  ? 230 PHE B HD1  1 
ATOM   6841 H  HD2  . PHE B  1 230 ? -39.26100 -19.08900 25.45500  1.000 24.47031  ? 230 PHE B HD2  1 
ATOM   6842 H  HE1  . PHE B  1 230 ? -35.27400 -20.74000 27.12400  1.000 23.73523  ? 230 PHE B HE1  1 
ATOM   6843 H  HE2  . PHE B  1 230 ? -38.62200 -21.24100 24.98100  1.000 24.79591  ? 230 PHE B HE2  1 
ATOM   6844 H  HZ   . PHE B  1 230 ? -36.59500 -22.05000 25.72400  1.000 23.25783  ? 230 PHE B HZ   1 
ATOM   6845 N  N    . TYR B  1 231 ? -39.16400 -15.05100 28.96400  1.000 19.62939  ? 231 TYR B N    1 
ATOM   6846 C  CA   . TYR B  1 231 ? -39.68700 -13.71700 29.26200  1.000 19.91777  ? 231 TYR B CA   1 
ATOM   6847 C  C    . TYR B  1 231 ? -38.73300 -12.97000 30.19300  1.000 20.75425  ? 231 TYR B C    1 
ATOM   6848 O  O    . TYR B  1 231 ? -38.41900 -11.79300 29.98200  1.000 21.32736  ? 231 TYR B O    1 
ATOM   6849 C  CB   . TYR B  1 231 ? -41.08300 -13.80600 29.90900  1.000 21.41995  ? 231 TYR B CB   1 
ATOM   6850 C  CG   . TYR B  1 231 ? -41.55800 -12.46900 30.38300  1.000 19.83083  ? 231 TYR B CG   1 
ATOM   6851 C  CD1  . TYR B  1 231 ? -42.24400 -11.64400 29.52400  1.000 22.20074  ? 231 TYR B CD1  1 
ATOM   6852 C  CD2  . TYR B  1 231 ? -41.28000 -12.00600 31.65200  1.000 22.20589  ? 231 TYR B CD2  1 
ATOM   6853 C  CE1  . TYR B  1 231 ? -42.67200 -10.40300 29.93300  1.000 21.24239  ? 231 TYR B CE1  1 
ATOM   6854 C  CE2  . TYR B  1 231 ? -41.68500 -10.76300 32.07500  1.000 22.64875  ? 231 TYR B CE2  1 
ATOM   6855 C  CZ   . TYR B  1 231 ? -42.39700 -9.97200  31.19700  1.000 20.53646  ? 231 TYR B CZ   1 
ATOM   6856 O  OH   . TYR B  1 231 ? -42.79900 -8.70900  31.62000  1.000 24.65116  ? 231 TYR B OH   1 
ATOM   6857 H  H    . TYR B  1 231 ? -39.68800 -15.69800 29.18200  1.000 23.55783  ? 231 TYR B H    1 
ATOM   6858 H  HA   . TYR B  1 231 ? -39.77500 -13.22900 28.42800  1.000 23.90388  ? 231 TYR B HA   1 
ATOM   6859 H  HB2  . TYR B  1 231 ? -41.71700 -14.14200 29.25700  1.000 25.70650  ? 231 TYR B HB2  1 
ATOM   6860 H  HB3  . TYR B  1 231 ? -41.04400 -14.40400 30.67200  1.000 25.70650  ? 231 TYR B HB3  1 
ATOM   6861 H  HD1  . TYR B  1 231 ? -42.42100 -11.92800 28.65600  1.000 26.64345  ? 231 TYR B HD1  1 
ATOM   6862 H  HD2  . TYR B  1 231 ? -40.80500 -12.55000 32.23700  1.000 26.64964  ? 231 TYR B HD2  1 
ATOM   6863 H  HE1  . TYR B  1 231 ? -43.14800 -9.85800  29.34900  1.000 25.49343  ? 231 TYR B HE1  1 
ATOM   6864 H  HE2  . TYR B  1 231 ? -41.48500 -10.46200 32.93200  1.000 27.18106  ? 231 TYR B HE2  1 
ATOM   6865 H  HH   . TYR B  1 231 ? -42.59900 -8.60000  32.42800  1.000 29.58395  ? 231 TYR B HH   1 
ATOM   6866 N  N    . ASN B  1 232 ? -38.27700 -13.62900 31.26400  1.000 21.22479  ? 232 ASN B N    1 
ATOM   6867 C  CA   . ASN B  1 232 ? -37.44600 -12.94900 32.25000  1.000 21.95338  ? 232 ASN B CA   1 
ATOM   6868 C  C    . ASN B  1 232 ? -36.09700 -12.54300 31.66300  1.000 22.48551  ? 232 ASN B C    1 
ATOM   6869 O  O    . ASN B  1 232 ? -35.49200 -11.57000 32.12500  1.000 26.59328  ? 232 ASN B O    1 
ATOM   6870 C  CB   . ASN B  1 232 ? -37.23300 -13.84700 33.46000  1.000 23.25413  ? 232 ASN B CB   1 
ATOM   6871 C  CG   . ASN B  1 232 ? -38.48600 -14.01200 34.30400  1.000 25.32651  ? 232 ASN B CG   1 
ATOM   6872 O  OD1  . ASN B  1 232 ? -39.45200 -13.25900 34.19200  1.000 25.04681  ? 232 ASN B OD1  1 
ATOM   6873 N  ND2  . ASN B  1 232 ? -38.46200 -15.04700 35.16400  1.000 28.14694  ? 232 ASN B ND2  1 
ATOM   6874 H  H    . ASN B  1 232 ? -38.43500 -14.45600 31.43700  1.000 25.47231  ? 232 ASN B H    1 
ATOM   6875 H  HA   . ASN B  1 232 ? -37.90500 -12.14700 32.54300  1.000 26.34661  ? 232 ASN B HA   1 
ATOM   6876 H  HB2  . ASN B  1 232 ? -36.95900 -14.72600 33.15600  1.000 27.90751  ? 232 ASN B HB2  1 
ATOM   6877 H  HB3  . ASN B  1 232 ? -36.54200 -13.46100 34.02200  1.000 27.90751  ? 232 ASN B HB3  1 
ATOM   6878 H  HD21 . ASN B  1 232 ? -39.13900 -15.19900 35.67300  1.000 33.77889  ? 232 ASN B HD21 1 
ATOM   6879 H  HD22 . ASN B  1 232 ? -37.77100 -15.55700 35.20500  1.000 33.77889  ? 232 ASN B HD22 1 
ATOM   6880 N  N    . ALA B  1 233 ? -35.61900 -13.25600 30.63300  1.000 20.81688  ? 233 ALA B N    1 
ATOM   6881 C  CA   . ALA B  1 233 ? -34.33400 -12.93200 30.02700  1.000 23.34735  ? 233 ALA B CA   1 
ATOM   6882 C  C    . ALA B  1 233 ? -34.38100 -11.63600 29.22600  1.000 21.90341  ? 233 ALA B C    1 
ATOM   6883 O  O    . ALA B  1 233 ? -33.36000 -10.94500 29.09300  1.000 23.51824  ? 233 ALA B O    1 
ATOM   6884 C  CB   . ALA B  1 233 ? -33.91100 -14.07700 29.10500  1.000 22.12504  ? 233 ALA B CB   1 
ATOM   6885 H  H    . ALA B  1 233 ? -36.02000 -13.92700 30.27400  1.000 24.98282  ? 233 ALA B H    1 
ATOM   6886 H  HA   . ALA B  1 233 ? -33.68000 -12.82300 30.73400  1.000 28.01939  ? 233 ALA B HA   1 
ATOM   6887 H  HB1  . ALA B  1 233 ? -33.06700 -13.84900 28.68600  1.000 26.55261  ? 233 ALA B HB1  1 
ATOM   6888 H  HB2  . ALA B  1 233 ? -33.81300 -14.88600 29.63100  1.000 26.55261  ? 233 ALA B HB2  1 
ATOM   6889 H  HB3  . ALA B  1 233 ? -34.59300 -14.20400 28.42600  1.000 26.55261  ? 233 ALA B HB3  1 
ATOM   6890 N  N    . ILE B  1 234 ? -35.53900 -11.29700 28.67800  1.000 20.97951  ? 234 ILE B N    1 
ATOM   6891 C  CA   . ILE B  1 234 ? -35.64000 -10.10400 27.82700  1.000 21.04638  ? 234 ILE B CA   1 
ATOM   6892 C  C    . ILE B  1 234 ? -35.41400 -8.86100  28.67500  1.000 22.23122  ? 234 ILE B C    1 
ATOM   6893 O  O    . ILE B  1 234 ? -35.94100 -8.77400  29.79400  1.000 22.47591  ? 234 ILE B O    1 
ATOM   6894 C  CB   . ILE B  1 234 ? -37.01500 -10.08000 27.14500  1.000 20.87425  ? 234 ILE B CB   1 
ATOM   6895 C  CG1  . ILE B  1 234 ? -37.14100 -11.32300 26.26000  1.000 21.12902  ? 234 ILE B CG1  1 
ATOM   6896 C  CG2  . ILE B  1 234 ? -37.22600 -8.79800  26.35900  1.000 21.02556  ? 234 ILE B CG2  1 
ATOM   6897 C  CD1  . ILE B  1 234 ? -38.48800 -11.45800 25.52600  1.000 20.09007  ? 234 ILE B CD1  1 
ATOM   6898 H  H    . ILE B  1 234 ? -36.27500 -11.72900 28.77700  1.000 25.17797  ? 234 ILE B H    1 
ATOM   6899 H  HA   . ILE B  1 234 ? -34.95300 -10.12500 27.14200  1.000 25.25822  ? 234 ILE B HA   1 
ATOM   6900 H  HB   . ILE B  1 234 ? -37.71100 -10.09900 27.82100  1.000 25.05166  ? 234 ILE B HB   1 
ATOM   6901 H  HG12 . ILE B  1 234 ? -36.44400 -11.29300 25.58600  1.000 25.35739  ? 234 ILE B HG12 1 
ATOM   6902 H  HG13 . ILE B  1 234 ? -37.03200 -12.11000 26.81600  1.000 25.35739  ? 234 ILE B HG13 1 
ATOM   6903 H  HG21 . ILE B  1 234 ? -38.09400 -8.83100  25.92800  1.000 25.23324  ? 234 ILE B HG21 1 
ATOM   6904 H  HG22 . ILE B  1 234 ? -37.18700 -8.04400  26.96800  1.000 25.23324  ? 234 ILE B HG22 1 
ATOM   6905 H  HG23 . ILE B  1 234 ? -36.52800 -8.72000  25.69000  1.000 25.23324  ? 234 ILE B HG23 1 
ATOM   6906 H  HD11 . ILE B  1 234 ? -38.54700 -12.34300 25.13300  1.000 24.11065  ? 234 ILE B HD11 1 
ATOM   6907 H  HD12 . ILE B  1 234 ? -39.20900 -11.33000 26.16200  1.000 24.11065  ? 234 ILE B HD12 1 
ATOM   6908 H  HD13 . ILE B  1 234 ? -38.53800 -10.78300 24.83000  1.000 24.11065  ? 234 ILE B HD13 1 
ATOM   6909 N  N    . PRO B  1 235 ? -34.65800 -7.88600  28.19300  1.000 21.89061  ? 235 PRO B N    1 
ATOM   6910 C  CA   . PRO B  1 235 ? -34.41200 -6.66900  28.96600  1.000 24.43760  ? 235 PRO B CA   1 
ATOM   6911 C  C    . PRO B  1 235 ? -35.68000 -6.01900  29.50500  1.000 23.38939  ? 235 PRO B C    1 
ATOM   6912 O  O    . PRO B  1 235 ? -36.70400 -5.94300  28.82600  1.000 24.08498  ? 235 PRO B O    1 
ATOM   6913 C  CB   . PRO B  1 235 ? -33.71100 -5.75700  27.94800  1.000 29.97163  ? 235 PRO B CB   1 
ATOM   6914 C  CG   . PRO B  1 235 ? -33.05500 -6.68400  27.00300  1.000 27.15289  ? 235 PRO B CG   1 
ATOM   6915 C  CD   . PRO B  1 235 ? -33.90700 -7.90100  26.91300  1.000 22.85171  ? 235 PRO B CD   1 
ATOM   6916 H  HA   . PRO B  1 235 ? -33.83000 -6.87400  29.71400  1.000 29.32768  ? 235 PRO B HA   1 
ATOM   6917 H  HB2  . PRO B  1 235 ? -34.36600 -5.20300  27.49400  1.000 35.96851  ? 235 PRO B HB2  1 
ATOM   6918 H  HB3  . PRO B  1 235 ? -33.05800 -5.19900  28.39700  1.000 35.96851  ? 235 PRO B HB3  1 
ATOM   6919 H  HG2  . PRO B  1 235 ? -32.98100 -6.25800  26.13400  1.000 32.58602  ? 235 PRO B HG2  1 
ATOM   6920 H  HG3  . PRO B  1 235 ? -32.17400 -6.91200  27.33700  1.000 32.58602  ? 235 PRO B HG3  1 
ATOM   6921 H  HD2  . PRO B  1 235 ? -34.51200 -7.84400  26.15700  1.000 27.42462  ? 235 PRO B HD2  1 
ATOM   6922 H  HD3  . PRO B  1 235 ? -33.36200 -8.70000  26.84200  1.000 27.42462  ? 235 PRO B HD3  1 
ATOM   6923 N  N    . SER B  1 236 ? -35.57600 -5.49700  30.73400  1.000 25.63541  ? 236 SER B N    1 
ATOM   6924 C  CA   . SER B  1 236 ? -36.67800 -4.74100  31.30100  1.000 27.96996  ? 236 SER B CA   1 
ATOM   6925 C  C    . SER B  1 236 ? -36.95800 -3.44700  30.52700  1.000 24.38810  ? 236 SER B C    1 
ATOM   6926 O  O    . SER B  1 236 ? -37.99600 -2.82400  30.75100  1.000 29.49956  ? 236 SER B O    1 
ATOM   6927 C  CB   . SER B  1 236 ? -36.37700 -4.39500  32.75200  1.000 31.18028  ? 236 SER B CB   1 
ATOM   6928 O  OG   . SER B  1 236 ? -35.26900 -3.52000  32.80000  1.000 37.33902  ? 236 SER B OG   1 
ATOM   6929 H  H    . SER B  1 236 ? -34.88700 -5.57000  31.24400  1.000 30.76505  ? 236 SER B H    1 
ATOM   6930 H  HA   . SER B  1 236 ? -37.47500 -5.29400  31.27000  1.000 33.56652  ? 236 SER B HA   1 
ATOM   6931 H  HB2  . SER B  1 236 ? -37.14900 -3.96000  33.14700  1.000 37.41890  ? 236 SER B HB2  1 
ATOM   6932 H  HB3  . SER B  1 236 ? -36.16800 -5.20700  33.24100  1.000 37.41890  ? 236 SER B HB3  1 
ATOM   6933 H  HG   . SER B  1 236 ? -35.19400 -3.19300  33.57000  1.000 44.80939  ? 236 SER B HG   1 
ATOM   6934 N  N    . SER B  1 237 ? -36.01900 -2.99900  29.68700  1.000 26.99728  ? 237 SER B N    1 
ATOM   6935 C  CA   . SER B  1 237 ? -36.22400 -1.81200  28.86200  1.000 26.76604  ? 237 SER B CA   1 
ATOM   6936 C  C    . SER B  1 237 ? -36.97900 -2.10300  27.57200  1.000 29.13982  ? 237 SER B C    1 
ATOM   6937 O  O    . SER B  1 237 ? -37.28300 -1.16100  26.82800  1.000 31.37971  ? 237 SER B O    1 
ATOM   6938 C  CB   . SER B  1 237 ? -34.86700 -1.20700  28.49100  1.000 31.73731  ? 237 SER B CB   1 
ATOM   6939 O  OG   . SER B  1 237 ? -33.97200 -2.21900  28.06200  1.000 30.54907  ? 237 SER B OG   1 
ATOM   6940 H  H    . SER B  1 237 ? -35.25100 -3.36900  29.57800  1.000 32.39930  ? 237 SER B H    1 
ATOM   6941 H  HA   . SER B  1 237 ? -36.73400 -1.16700  29.37800  1.000 32.12181  ? 237 SER B HA   1 
ATOM   6942 H  HB2  . SER B  1 237 ? -34.99100 -0.56800  27.77200  1.000 38.08734  ? 237 SER B HB2  1 
ATOM   6943 H  HB3  . SER B  1 237 ? -34.49500 -0.76300  29.26900  1.000 38.08734  ? 237 SER B HB3  1 
ATOM   6944 H  HG   . SER B  1 237 ? -34.28300 -2.61100  27.38700  1.000 36.66145  ? 237 SER B HG   1 
ATOM   6945 N  N    . THR B  1 238 ? -37.26100 -3.37100  27.27000  1.000 24.36367  ? 238 THR B N    1 
ATOM   6946 C  CA   . THR B  1 238 ? -38.04000 -3.76100  26.10700  1.000 23.06346  ? 238 THR B CA   1 
ATOM   6947 C  C    . THR B  1 238 ? -39.51400 -3.84700  26.47300  1.000 22.53213  ? 238 THR B C    1 
ATOM   6948 O  O    . THR B  1 238 ? -39.86100 -4.20500  27.59800  1.000 22.32255  ? 238 THR B O    1 
ATOM   6949 C  CB   . THR B  1 238 ? -37.51800 -5.12200  25.63900  1.000 20.39679  ? 238 THR B CB   1 
ATOM   6950 O  OG1  . THR B  1 238 ? -36.15100 -4.95800  25.24200  1.000 23.60187  ? 238 THR B OG1  1 
ATOM   6951 C  CG2  . THR B  1 238 ? -38.31000 -5.68800  24.50300  1.000 23.00865  ? 238 THR B CG2  1 
ATOM   6952 H  H    . THR B  1 238 ? -37.00200 -4.04200  27.74200  1.000 29.23897  ? 238 THR B H    1 
ATOM   6953 H  HA   . THR B  1 238 ? -37.96400 -3.11400  25.38800  1.000 27.67871  ? 238 THR B HA   1 
ATOM   6954 H  HB   . THR B  1 238 ? -37.59600 -5.76200  26.36500  1.000 24.47871  ? 238 THR B HB   1 
ATOM   6955 H  HG1  . THR B  1 238 ? -35.81000 -5.70500  25.06600  1.000 28.32481  ? 238 THR B HG1  1 
ATOM   6956 H  HG21 . THR B  1 238 ? -37.86000 -6.46600  24.13900  1.000 27.61295  ? 238 THR B HG21 1 
ATOM   6957 H  HG22 . THR B  1 238 ? -39.19200 -5.95000  24.81200  1.000 27.61295  ? 238 THR B HG22 1 
ATOM   6958 H  HG23 . THR B  1 238 ? -38.40700 -5.02300  23.80300  1.000 27.61295  ? 238 THR B HG23 1 
ATOM   6959 N  N    . ASP B  1 239 ? -40.39000 -3.43900  25.54000  1.000 22.50405  ? 239 ASP B N    1 
ATOM   6960 C  CA   . ASP B  1 239 ? -41.82400 -3.66200  25.71100  1.000 20.74253  ? 239 ASP B CA   1 
ATOM   6961 C  C    . ASP B  1 239 ? -42.08100 -5.16100  25.66200  1.000 18.74069  ? 239 ASP B C    1 
ATOM   6962 O  O    . ASP B  1 239 ? -41.81600 -5.81400  24.64400  1.000 19.71172  ? 239 ASP B O    1 
ATOM   6963 C  CB   . ASP B  1 239 ? -42.64200 -3.00700  24.58800  1.000 21.99807  ? 239 ASP B CB   1 
ATOM   6964 C  CG   . ASP B  1 239 ? -42.54300 -1.50600  24.56900  1.000 25.72643  ? 239 ASP B CG   1 
ATOM   6965 O  OD1  . ASP B  1 239 ? -41.96200 -0.89700  25.46300  1.000 30.75469  ? 239 ASP B OD1  1 
ATOM   6966 O  OD2  . ASP B  1 239 ? -43.10300 -0.91800  23.62800  1.000 33.26234  ? 239 ASP B OD2  1 
ATOM   6967 H  H    . ASP B  1 239 ? -40.17600 -3.03700  24.81000  1.000 27.00742  ? 239 ASP B H    1 
ATOM   6968 H  HA   . ASP B  1 239 ? -42.09700 -3.27300  26.55600  1.000 24.89360  ? 239 ASP B HA   1 
ATOM   6969 H  HB2  . ASP B  1 239 ? -42.32200 -3.33600  23.73400  1.000 26.40024  ? 239 ASP B HB2  1 
ATOM   6970 H  HB3  . ASP B  1 239 ? -43.57700 -3.24000  24.70400  1.000 26.40024  ? 239 ASP B HB3  1 
ATOM   6971 N  N    . LYS B  1 240 ? -42.57600 -5.73600  26.74900  1.000 18.29614  ? 240 LYS B N    1 
ATOM   6972 C  CA   . LYS B  1 240 ? -42.78600 -7.16800  26.79500  1.000 18.54694  ? 240 LYS B CA   1 
ATOM   6973 C  C    . LYS B  1 240 ? -43.97300 -7.43900  27.70800  1.000 17.99050  ? 240 LYS B C    1 
ATOM   6974 O  O    . LYS B  1 240 ? -44.28800 -6.65800  28.60800  1.000 19.69335  ? 240 LYS B O    1 
ATOM   6975 C  CB   . LYS B  1 240 ? -41.52400 -7.92600  27.23300  1.000 18.84372  ? 240 LYS B CB   1 
ATOM   6976 C  CG   . LYS B  1 240 ? -41.02600 -7.55400  28.62900  1.000 19.89251  ? 240 LYS B CG   1 
ATOM   6977 C  CD   . LYS B  1 240 ? -39.83700 -8.41400  29.01100  1.000 20.01196  ? 240 LYS B CD   1 
ATOM   6978 C  CE   . LYS B  1 240 ? -39.39200 -8.11300  30.42000  1.000 19.64137  ? 240 LYS B CE   1 
ATOM   6979 N  NZ   . LYS B  1 240 ? -38.38100 -9.13400  30.90500  1.000 22.54624  ? 240 LYS B NZ   1 
ATOM   6980 H  H    . LYS B  1 240 ? -42.79700 -5.31800  27.46700  1.000 21.95793  ? 240 LYS B H    1 
ATOM   6981 H  HA   . LYS B  1 240 ? -43.00800 -7.50400  25.91300  1.000 22.25889  ? 240 LYS B HA   1 
ATOM   6982 H  HB2  . LYS B  1 240 ? -41.71700 -8.87700  27.23200  1.000 22.61502  ? 240 LYS B HB2  1 
ATOM   6983 H  HB3  . LYS B  1 240 ? -40.81100 -7.73200  26.60400  1.000 22.61502  ? 240 LYS B HB3  1 
ATOM   6984 H  HG2  . LYS B  1 240 ? -40.75100 -6.62400  28.63900  1.000 23.87357  ? 240 LYS B HG2  1 
ATOM   6985 H  HG3  . LYS B  1 240 ? -41.73400 -7.69900  29.27600  1.000 23.87357  ? 240 LYS B HG3  1 
ATOM   6986 H  HD2  . LYS B  1 240 ? -40.08500 -9.35100  28.95900  1.000 24.01691  ? 240 LYS B HD2  1 
ATOM   6987 H  HD3  . LYS B  1 240 ? -39.09900 -8.23200  28.40900  1.000 24.01691  ? 240 LYS B HD3  1 
ATOM   6988 H  HE2  . LYS B  1 240 ? -38.97900 -7.23600  30.44700  1.000 23.57221  ? 240 LYS B HE2  1 
ATOM   6989 H  HE3  . LYS B  1 240 ? -40.16000 -8.13700  31.01300  1.000 23.57221  ? 240 LYS B HE3  1 
ATOM   6990 H  HZ1  . LYS B  1 240 ? -38.76000 -9.93700  30.95900  1.000 27.05805  ? 240 LYS B HZ1  1 
ATOM   6991 H  HZ2  . LYS B  1 240 ? -37.69500 -9.17600  30.33900  1.000 27.05805  ? 240 LYS B HZ2  1 
ATOM   6992 H  HZ3  . LYS B  1 240 ? -38.07700 -8.90300  31.70900  1.000 27.05805  ? 240 LYS B HZ3  1 
ATOM   6993 N  N    . ALA B  1 241 ? -44.60400 -8.58200  27.48000  1.000 17.85121  ? 241 ALA B N    1 
ATOM   6994 C  CA   . ALA B  1 241 ? -45.72600 -9.02000  28.28400  1.000 17.28984  ? 241 ALA B CA   1 
ATOM   6995 C  C    . ALA B  1 241 ? -45.75400 -10.53600 28.34100  1.000 17.35706  ? 241 ALA B C    1 
ATOM   6996 O  O    . ALA B  1 241 ? -45.36800 -11.22000 27.37600  1.000 18.65353  ? 241 ALA B O    1 
ATOM   6997 C  CB   . ALA B  1 241 ? -47.06500 -8.48200  27.78200  1.000 19.58110  ? 241 ALA B CB   1 
ATOM   6998 H  H    . ALA B  1 241 ? -44.39500 -9.13000  26.85200  1.000 21.42401  ? 241 ALA B H    1 
ATOM   6999 H  HA   . ALA B  1 241 ? -45.59800 -8.68700  29.18600  1.000 20.73500  ? 241 ALA B HA   1 
ATOM   7000 H  HB1  . ALA B  1 241 ? -47.77000 -8.78500  28.37600  1.000 23.49989  ? 241 ALA B HB1  1 
ATOM   7001 H  HB2  . ALA B  1 241 ? -47.03300 -7.51300  27.77400  1.000 23.49989  ? 241 ALA B HB2  1 
ATOM   7002 H  HB3  . ALA B  1 241 ? -47.22300 -8.81500  26.88500  1.000 23.49989  ? 241 ALA B HB3  1 
ATOM   7003 N  N    . TYR B  1 242 ? -46.30000 -11.04700 29.43900  1.000 19.31178  ? 242 TYR B N    1 
ATOM   7004 C  CA   . TYR B  1 242 ? -46.35200 -12.47100 29.72700  1.000 18.53444  ? 242 TYR B CA   1 
ATOM   7005 C  C    . TYR B  1 242 ? -47.76000 -12.76600 30.20500  1.000 18.29277  ? 242 TYR B C    1 
ATOM   7006 O  O    . TYR B  1 242 ? -48.23700 -12.14100 31.16400  1.000 20.29010  ? 242 TYR B O    1 
ATOM   7007 C  CB   . TYR B  1 242 ? -45.37000 -12.79300 30.83300  1.000 19.40998  ? 242 TYR B CB   1 
ATOM   7008 C  CG   . TYR B  1 242 ? -45.27800 -14.21600 31.26800  1.000 19.05070  ? 242 TYR B CG   1 
ATOM   7009 C  CD1  . TYR B  1 242 ? -44.45500 -15.11400 30.60400  1.000 19.78984  ? 242 TYR B CD1  1 
ATOM   7010 C  CD2  . TYR B  1 242 ? -45.94800 -14.66400 32.40500  1.000 21.38106  ? 242 TYR B CD2  1 
ATOM   7011 C  CE1  . TYR B  1 242 ? -44.31800 -16.41200 31.03000  1.000 21.55799  ? 242 TYR B CE1  1 
ATOM   7012 C  CE2  . TYR B  1 242 ? -45.79300 -15.98000 32.84900  1.000 20.54390  ? 242 TYR B CE2  1 
ATOM   7013 C  CZ   . TYR B  1 242 ? -44.96500 -16.83300 32.14000  1.000 22.13930  ? 242 TYR B CZ   1 
ATOM   7014 O  OH   . TYR B  1 242 ? -44.79000 -18.14400 32.56300  1.000 25.12330  ? 242 TYR B OH   1 
ATOM   7015 H  H    . TYR B  1 242 ? -46.66100 -10.56700 30.05500  1.000 23.17670  ? 242 TYR B H    1 
ATOM   7016 H  HA   . TYR B  1 242 ? -46.14800 -13.00300 28.94200  1.000 22.24389  ? 242 TYR B HA   1 
ATOM   7017 H  HB2  . TYR B  1 242 ? -44.48500 -12.53300 30.53300  1.000 23.29453  ? 242 TYR B HB2  1 
ATOM   7018 H  HB3  . TYR B  1 242 ? -45.62000 -12.27500 31.61500  1.000 23.29453  ? 242 TYR B HB3  1 
ATOM   7019 H  HD1  . TYR B  1 242 ? -43.98600 -14.83100 29.85300  1.000 23.75037  ? 242 TYR B HD1  1 
ATOM   7020 H  HD2  . TYR B  1 242 ? -46.50200 -14.08200 32.87300  1.000 25.65983  ? 242 TYR B HD2  1 
ATOM   7021 H  HE1  . TYR B  1 242 ? -43.77900 -17.00200 30.55400  1.000 25.87215  ? 242 TYR B HE1  1 
ATOM   7022 H  HE2  . TYR B  1 242 ? -46.24000 -16.27800 33.60900  1.000 24.65525  ? 242 TYR B HE2  1 
ATOM   7023 H  HH   . TYR B  1 242 ? -45.21200 -18.27400 33.27700  1.000 30.15052  ? 242 TYR B HH   1 
ATOM   7024 N  N    . PHE B  1 243 ? -48.44500 -13.69300 29.53700  1.000 18.98009  ? 243 PHE B N    1 
ATOM   7025 C  CA   . PHE B  1 243 ? -49.77000 -14.12000 29.95400  1.000 18.62899  ? 243 PHE B CA   1 
ATOM   7026 C  C    . PHE B  1 243 ? -49.72700 -15.61700 30.13300  1.000 19.02293  ? 243 PHE B C    1 
ATOM   7027 O  O    . PHE B  1 243 ? -49.60300 -16.34800 29.14400  1.000 20.79298  ? 243 PHE B O    1 
ATOM   7028 C  CB   . PHE B  1 243 ? -50.84000 -13.76800 28.90400  1.000 19.27302  ? 243 PHE B CB   1 
ATOM   7029 C  CG   . PHE B  1 243 ? -51.15200 -12.28900 28.79600  1.000 19.61417  ? 243 PHE B CG   1 
ATOM   7030 C  CD1  . PHE B  1 243 ? -50.40000 -11.44700 28.01800  1.000 20.42448  ? 243 PHE B CD1  1 
ATOM   7031 C  CD2  . PHE B  1 243 ? -52.24900 -11.75900 29.44300  1.000 20.02499  ? 243 PHE B CD2  1 
ATOM   7032 C  CE1  . PHE B  1 243 ? -50.70300 -10.08400 27.93100  1.000 22.91162  ? 243 PHE B CE1  1 
ATOM   7033 C  CE2  . PHE B  1 243 ? -52.56000 -10.40200 29.34100  1.000 20.66588  ? 243 PHE B CE2  1 
ATOM   7034 C  CZ   . PHE B  1 243 ? -51.79300 -9.58100  28.60200  1.000 20.87469  ? 243 PHE B CZ   1 
ATOM   7035 H  H    . PHE B  1 243 ? -48.15600 -14.09100 28.83200  1.000 22.77867  ? 243 PHE B H    1 
ATOM   7036 H  HA   . PHE B  1 243 ? -49.99200 -13.68200 30.79000  1.000 22.35735  ? 243 PHE B HA   1 
ATOM   7037 H  HB2  . PHE B  1 243 ? -50.53000 -14.06600 28.03500  1.000 23.13019  ? 243 PHE B HB2  1 
ATOM   7038 H  HB3  . PHE B  1 243 ? -51.66400 -14.22500 29.13700  1.000 23.13019  ? 243 PHE B HB3  1 
ATOM   7039 H  HD1  . PHE B  1 243 ? -49.67800 -11.78700 27.54100  1.000 24.51193  ? 243 PHE B HD1  1 
ATOM   7040 H  HD2  . PHE B  1 243 ? -52.79000 -12.31500 29.95600  1.000 24.03255  ? 243 PHE B HD2  1 
ATOM   7041 H  HE1  . PHE B  1 243 ? -50.16900 -9.51900  27.42000  1.000 27.49651  ? 243 PHE B HE1  1 
ATOM   7042 H  HE2  . PHE B  1 243 ? -53.30300 -10.06300 29.78600  1.000 24.80162  ? 243 PHE B HE2  1 
ATOM   7043 H  HZ   . PHE B  1 243 ? -51.99800 -8.67500  28.54500  1.000 25.05219  ? 243 PHE B HZ   1 
ATOM   7044 N  N    . GLU B  1 244 ? -49.85600 -16.07700 31.36500  1.000 19.64952  ? 244 GLU B N    1 
ATOM   7045 C  CA   . GLU B  1 244 ? -49.95500 -17.49600 31.65600  1.000 21.30217  ? 244 GLU B CA   1 
ATOM   7046 C  C    . GLU B  1 244 ? -51.43300 -17.85300 31.64100  1.000 20.73787  ? 244 GLU B C    1 
ATOM   7047 O  O    . GLU B  1 244 ? -52.24500 -17.24000 32.35800  1.000 22.60852  ? 244 GLU B O    1 
ATOM   7048 C  CB   . GLU B  1 244 ? -49.32800 -17.88100 32.99000  1.000 22.41854  ? 244 GLU B CB   1 
ATOM   7049 C  CG   . GLU B  1 244 ? -49.24200 -19.37600 33.14400  1.000 23.51055  ? 244 GLU B CG   1 
ATOM   7050 C  CD   . GLU B  1 244 ? -48.79400 -19.82700 34.51400  1.000 29.29159  ? 244 GLU B CD   1 
ATOM   7051 O  OE1  . GLU B  1 244 ? -49.50600 -19.56300 35.48500  1.000 28.22529  ? 244 GLU B OE1  1 
ATOM   7052 O  OE2  . GLU B  1 244 ? -47.73000 -20.46000 34.62100  1.000 30.87402  ? 244 GLU B OE2  1 
ATOM   7053 H  H    . GLU B  1 244 ? -49.89000 -15.57700 32.06400  1.000 23.58199  ? 244 GLU B H    1 
ATOM   7054 H  HA   . GLU B  1 244 ? -49.47000 -17.99400 30.97900  1.000 25.56517  ? 244 GLU B HA   1 
ATOM   7055 H  HB2  . GLU B  1 244 ? -48.43100 -17.51500 33.04000  1.000 26.90481  ? 244 GLU B HB2  1 
ATOM   7056 H  HB3  . GLU B  1 244 ? -49.87000 -17.52900 33.71300  1.000 26.90481  ? 244 GLU B HB3  1 
ATOM   7057 H  HG2  . GLU B  1 244 ? -50.11800 -19.75600 32.98000  1.000 28.21522  ? 244 GLU B HG2  1 
ATOM   7058 H  HG3  . GLU B  1 244 ? -48.60400 -19.71900 32.49800  1.000 28.21522  ? 244 GLU B HG3  1 
ATOM   7059 N  N    . ILE B  1 245 ? -51.77500 -18.82900 30.81200  1.000 22.19302  ? 245 ILE B N    1 
ATOM   7060 C  CA   . ILE B  1 245 ? -53.15600 -19.21800 30.56600  1.000 21.13482  ? 245 ILE B CA   1 
ATOM   7061 C  C    . ILE B  1 245 ? -53.52400 -20.36600 31.48500  1.000 23.36786  ? 245 ILE B C    1 
ATOM   7062 O  O    . ILE B  1 245 ? -52.89800 -21.43900 31.46400  1.000 24.85198  ? 245 ILE B O    1 
ATOM   7063 C  CB   . ILE B  1 245 ? -53.35700 -19.59000 29.09100  1.000 20.29748  ? 245 ILE B CB   1 
ATOM   7064 C  CG1  . ILE B  1 245 ? -53.09800 -18.35000 28.22000  1.000 24.94183  ? 245 ILE B CG1  1 
ATOM   7065 C  CG2  . ILE B  1 245 ? -54.73700 -20.12500 28.87700  1.000 25.87793  ? 245 ILE B CG2  1 
ATOM   7066 C  CD1  . ILE B  1 245 ? -53.07300 -18.61300 26.73500  1.000 25.28110  ? 245 ILE B CD1  1 
ATOM   7067 H  H    . ILE B  1 245 ? -51.20700 -19.29500 30.36400  1.000 26.63418  ? 245 ILE B H    1 
ATOM   7068 H  HA   . ILE B  1 245 ? -53.74200 -18.47700 30.78400  1.000 25.36434  ? 245 ILE B HA   1 
ATOM   7069 H  HB   . ILE B  1 245 ? -52.72800 -20.28400 28.84000  1.000 24.35954  ? 245 ILE B HB   1 
ATOM   7070 H  HG12 . ILE B  1 245 ? -53.80000 -17.70300 28.39000  1.000 29.93276  ? 245 ILE B HG12 1 
ATOM   7071 H  HG13 . ILE B  1 245 ? -52.23600 -17.97700 28.46500  1.000 29.93276  ? 245 ILE B HG13 1 
ATOM   7072 H  HG21 . ILE B  1 245 ? -54.94800 -20.08300 27.93100  1.000 31.05608  ? 245 ILE B HG21 1 
ATOM   7073 H  HG22 . ILE B  1 245 ? -54.77000 -21.04500 29.18300  1.000 31.05608  ? 245 ILE B HG22 1 
ATOM   7074 H  HG23 . ILE B  1 245 ? -55.36600 -19.58600 29.38000  1.000 31.05608  ? 245 ILE B HG23 1 
ATOM   7075 H  HD11 . ILE B  1 245 ? -52.75100 -17.81900 26.28000  1.000 30.33988  ? 245 ILE B HD11 1 
ATOM   7076 H  HD12 . ILE B  1 245 ? -52.48100 -19.36000 26.55700  1.000 30.33988  ? 245 ILE B HD12 1 
ATOM   7077 H  HD13 . ILE B  1 245 ? -53.97200 -18.82400 26.43700  1.000 30.33988  ? 245 ILE B HD13 1 
ATOM   7078 N  N    . SER B  1 246 ? -54.52900 -20.12300 32.31900  1.000 23.49245  ? 246 SER B N    1 
ATOM   7079 C  CA   . SER B  1 246 ? -54.86800 -21.04200 33.38200  1.000 25.21359  ? 246 SER B CA   1 
ATOM   7080 C  C    . SER B  1 246 ? -55.36300 -22.37200 32.82600  1.000 23.95389  ? 246 SER B C    1 
ATOM   7081 O  O    . SER B  1 246 ? -56.24300 -22.40100 31.95900  1.000 26.99613  ? 246 SER B O    1 
ATOM   7082 C  CB   . SER B  1 246 ? -55.96500 -20.40500 34.24100  1.000 28.38808  ? 246 SER B CB   1 
ATOM   7083 O  OG   . SER B  1 246 ? -56.27800 -21.20900 35.36900  1.000 29.83704  ? 246 SER B OG   1 
ATOM   7084 H  H    . SER B  1 246 ? -55.03000 -19.42500 32.28600  1.000 28.19350  ? 246 SER B H    1 
ATOM   7085 H  HA   . SER B  1 246 ? -54.08100 -21.22500 33.91900  1.000 30.25887  ? 246 SER B HA   1 
ATOM   7086 H  HB2  . SER B  1 246 ? -55.65700 -19.53900 34.55000  1.000 34.06826  ? 246 SER B HB2  1 
ATOM   7087 H  HB3  . SER B  1 246 ? -56.76400 -20.30000 33.70100  1.000 34.06826  ? 246 SER B HB3  1 
ATOM   7088 H  HG   . SER B  1 246 ? -56.80000 -20.79500 35.88100  1.000 35.80701  ? 246 SER B HG   1 
ATOM   7089 N  N    . GLY B  1 247 ? -54.80000 -23.46300 33.33600  1.000 25.28943  ? 247 GLY B N    1 
ATOM   7090 C  CA   . GLY B  1 247 ? -55.17800 -24.80400 32.93500  1.000 29.40407  ? 247 GLY B CA   1 
ATOM   7091 C  C    . GLY B  1 247 ? -54.71800 -25.23300 31.56100  1.000 27.47466  ? 247 GLY B C    1 
ATOM   7092 O  O    . GLY B  1 247 ? -55.09500 -26.30800 31.10700  1.000 31.53938  ? 247 GLY B O    1 
ATOM   7093 H  H    . GLY B  1 247 ? -54.18000 -23.45000 33.93200  1.000 30.34988  ? 247 GLY B H    1 
ATOM   7094 H  HA2  . GLY B  1 247 ? -54.80800 -25.43200 33.57600  1.000 35.28745  ? 247 GLY B HA2  1 
ATOM   7095 H  HA3  . GLY B  1 247 ? -56.14600 -24.86800 32.95200  1.000 35.28745  ? 247 GLY B HA3  1 
ATOM   7096 N  N    . GLY B  1 248 ? -53.89700 -24.43800 30.87700  1.000 26.20652  ? 248 GLY B N    1 
ATOM   7097 C  CA   . GLY B  1 248 ? -53.61200 -24.71900 29.49200  1.000 25.34316  ? 248 GLY B CA   1 
ATOM   7098 C  C    . GLY B  1 248 ? -52.56000 -25.81300 29.32400  1.000 26.16956  ? 248 GLY B C    1 
ATOM   7099 O  O    . GLY B  1 248 ? -51.56800 -25.87900 30.05700  1.000 26.71108  ? 248 GLY B O    1 
ATOM   7100 H  H    . GLY B  1 248 ? -53.50200 -23.74300 31.19500  1.000 31.45039  ? 248 GLY B H    1 
ATOM   7101 H  HA2  . GLY B  1 248 ? -54.42500 -25.00800 29.04900  1.000 30.41435  ? 248 GLY B HA2  1 
ATOM   7102 H  HA3  . GLY B  1 248 ? -53.28600 -23.91400 29.06100  1.000 30.41435  ? 248 GLY B HA3  1 
ATOM   7103 N  N    . ASN B  1 249 ? -52.81100 -26.70700 28.36400  1.000 25.08640  ? 249 ASN B N    1 
ATOM   7104 C  CA   . ASN B  1 249 ? -51.80700 -27.68200 27.96500  1.000 26.17286  ? 249 ASN B CA   1 
ATOM   7105 C  C    . ASN B  1 249 ? -50.94300 -27.04600 26.88000  1.000 23.58946  ? 249 ASN B C    1 
ATOM   7106 O  O    . ASN B  1 249 ? -51.08800 -25.87000 26.55000  1.000 22.60051  ? 249 ASN B O    1 
ATOM   7107 C  CB   . ASN B  1 249 ? -52.43300 -29.02100 27.54700  1.000 28.43524  ? 249 ASN B CB   1 
ATOM   7108 C  CG   . ASN B  1 249 ? -53.30900 -28.92100 26.31900  1.000 30.29646  ? 249 ASN B CG   1 
ATOM   7109 O  OD1  . ASN B  1 249 ? -53.12400 -28.06300 25.46900  1.000 27.24172  ? 249 ASN B OD1  1 
ATOM   7110 N  ND2  . ASN B  1 249 ? -54.28900 -29.82200 26.22300  1.000 34.19992  ? 249 ASN B ND2  1 
ATOM   7111 H  H    . ASN B  1 249 ? -53.55400 -26.76500 27.93400  1.000 30.10624  ? 249 ASN B H    1 
ATOM   7112 H  HA   . ASN B  1 249 ? -51.24400 -27.90700 28.72300  1.000 31.40999  ? 249 ASN B HA   1 
ATOM   7113 H  HB2  . ASN B  1 249 ? -51.72300 -29.65200 27.35400  1.000 34.12485  ? 249 ASN B HB2  1 
ATOM   7114 H  HB3  . ASN B  1 249 ? -52.98100 -29.35100 28.27600  1.000 34.12485  ? 249 ASN B HB3  1 
ATOM   7115 H  HD21 . ASN B  1 249 ? -54.81800 -29.81200 25.54500  1.000 41.04246  ? 249 ASN B HD21 1 
ATOM   7116 H  HD22 . ASN B  1 249 ? -54.39100 -30.41300 26.84000  1.000 41.04246  ? 249 ASN B HD22 1 
ATOM   7117 N  N    . HIS B  1 250 ? -50.04000 -27.83300 26.31100  1.000 24.26688  ? 250 HIS B N    1 
ATOM   7118 C  CA   . HIS B  1 250 ? -49.06300 -27.28600 25.36800  1.000 22.09850  ? 250 HIS B CA   1 
ATOM   7119 C  C    . HIS B  1 250 ? -49.70500 -26.65100 24.13900  1.000 21.42593  ? 250 HIS B C    1 
ATOM   7120 O  O    . HIS B  1 250 ? -49.04400 -25.86800 23.44400  1.000 22.15719  ? 250 HIS B O    1 
ATOM   7121 C  CB   . HIS B  1 250 ? -48.13000 -28.41100 24.95000  1.000 25.05421  ? 250 HIS B CB   1 
ATOM   7122 C  CG   . HIS B  1 250 ? -47.01300 -27.96700 24.06600  1.000 23.68643  ? 250 HIS B CG   1 
ATOM   7123 N  ND1  . HIS B  1 250 ? -46.16300 -26.93700 24.41200  1.000 22.07678  ? 250 HIS B ND1  1 
ATOM   7124 C  CD2  . HIS B  1 250 ? -46.57900 -28.43600 22.87100  1.000 23.66045  ? 250 HIS B CD2  1 
ATOM   7125 C  CE1  . HIS B  1 250 ? -45.25200 -26.79200 23.45600  1.000 22.34176  ? 250 HIS B CE1  1 
ATOM   7126 N  NE2  . HIS B  1 250 ? -45.47700 -27.69200 22.51800  1.000 24.42037  ? 250 HIS B NE2  1 
ATOM   7127 H  H    . HIS B  1 250 ? -49.96800 -28.67900 26.44900  1.000 29.12282  ? 250 HIS B H    1 
ATOM   7128 H  HA   . HIS B  1 250 ? -48.55300 -26.58500 25.80300  1.000 26.52077  ? 250 HIS B HA   1 
ATOM   7129 H  HB2  . HIS B  1 250 ? -47.74000 -28.80500 25.74600  1.000 30.06762  ? 250 HIS B HB2  1 
ATOM   7130 H  HB3  . HIS B  1 250 ? -48.64200 -29.07800 24.46700  1.000 30.06762  ? 250 HIS B HB3  1 
ATOM   7131 H  HD1  . HIS B  1 250 ? -46.21400 -26.46500 25.12900  1.000 26.49470  ? 250 HIS B HD1  1 
ATOM   7132 H  HD2  . HIS B  1 250 ? -46.95500 -29.13000 22.38100  1.000 28.39510  ? 250 HIS B HD2  1 
ATOM   7133 H  HE1  . HIS B  1 250 ? -44.56900 -26.16100 23.45000  1.000 26.81267  ? 250 HIS B HE1  1 
ATOM   7134 N  N    . TYR B  1 251 ? -50.93400 -27.01500 23.81000  1.000 22.29684  ? 251 TYR B N    1 
ATOM   7135 C  CA   . TYR B  1 251 ? -51.64100 -26.48400 22.64800  1.000 22.00862  ? 251 TYR B CA   1 
ATOM   7136 C  C    . TYR B  1 251 ? -52.50700 -25.27900 22.97500  1.000 20.63468  ? 251 TYR B C    1 
ATOM   7137 O  O    . TYR B  1 251 ? -53.23000 -24.80500 22.08800  1.000 22.92741  ? 251 TYR B O    1 
ATOM   7138 C  CB   . TYR B  1 251 ? -52.50500 -27.59700 22.04100  1.000 25.44899  ? 251 TYR B CB   1 
ATOM   7139 C  CG   . TYR B  1 251 ? -51.70200 -28.80800 21.64600  1.000 29.01507  ? 251 TYR B CG   1 
ATOM   7140 C  CD1  . TYR B  1 251 ? -51.31400 -29.73900 22.59400  1.000 34.96438  ? 251 TYR B CD1  1 
ATOM   7141 C  CD2  . TYR B  1 251 ? -51.32000 -29.00900 20.33100  1.000 35.49174  ? 251 TYR B CD2  1 
ATOM   7142 C  CE1  . TYR B  1 251 ? -50.55000 -30.85000 22.24400  1.000 45.97431  ? 251 TYR B CE1  1 
ATOM   7143 C  CE2  . TYR B  1 251 ? -50.55700 -30.12500 19.96500  1.000 44.42520  ? 251 TYR B CE2  1 
ATOM   7144 C  CZ   . TYR B  1 251 ? -50.18100 -31.03000 20.92900  1.000 40.49403  ? 251 TYR B CZ   1 
ATOM   7145 O  OH   . TYR B  1 251 ? -49.43400 -32.14300 20.58200  1.000 55.91675  ? 251 TYR B OH   1 
ATOM   7146 H  H    . TYR B  1 251 ? -51.39800 -27.58600 24.25600  1.000 26.75877  ? 251 TYR B H    1 
ATOM   7147 H  HA   . TYR B  1 251 ? -50.99500 -26.19700 21.98400  1.000 26.41291  ? 251 TYR B HA   1 
ATOM   7148 H  HB2  . TYR B  1 251 ? -53.16700 -27.87400 22.69400  1.000 30.54135  ? 251 TYR B HB2  1 
ATOM   7149 H  HB3  . TYR B  1 251 ? -52.94600 -27.25600 21.24700  1.000 30.54135  ? 251 TYR B HB3  1 
ATOM   7150 H  HD1  . TYR B  1 251 ? -51.56700 -29.62000 23.48100  1.000 41.95981  ? 251 TYR B HD1  1 
ATOM   7151 H  HD2  . TYR B  1 251 ? -51.57300 -28.39300 19.68100  1.000 42.59265  ? 251 TYR B HD2  1 
ATOM   7152 H  HE1  . TYR B  1 251 ? -50.29200 -31.46500 22.89200  1.000 55.17173  ? 251 TYR B HE1  1 
ATOM   7153 H  HE2  . TYR B  1 251 ? -50.30700 -30.25300 19.07900  1.000 53.31280  ? 251 TYR B HE2  1 
ATOM   7154 H  HH   . TYR B  1 251 ? -49.26500 -32.13000 19.75900  1.000 67.10267  ? 251 TYR B HH   1 
ATOM   7155 N  N    . CYS B  1 252 ? -52.46700 -24.77000 24.21000  1.000 21.45399  ? 252 CYS B N    1 
ATOM   7156 C  CA   . CYS B  1 252 ? -53.48000 -23.81100 24.65200  1.000 20.51839  ? 252 CYS B CA   1 
ATOM   7157 C  C    . CYS B  1 252 ? -53.44200 -22.50700 23.86500  1.000 21.56239  ? 252 CYS B C    1 
ATOM   7158 O  O    . CYS B  1 252 ? -54.48900 -21.85800 23.70300  1.000 21.75296  ? 252 CYS B O    1 
ATOM   7159 C  CB   . CYS B  1 252 ? -53.34400 -23.56300 26.16300  1.000 22.61193  ? 252 CYS B CB   1 
ATOM   7160 S  SG   . CYS B  1 252 ? -52.25000 -22.20900 26.70600  1.000 22.57392  ? 252 CYS B SG   1 
ATOM   7161 H  H    . CYS B  1 252 ? -51.87300 -24.96100 24.80200  1.000 25.74735  ? 252 CYS B H    1 
ATOM   7162 H  HA   . CYS B  1 252 ? -54.35600 -24.19700 24.49500  1.000 24.62463  ? 252 CYS B HA   1 
ATOM   7163 H  HB2  . CYS B  1 252 ? -54.22700 -23.36500 26.51100  1.000 27.13687  ? 252 CYS B HB2  1 
ATOM   7164 H  HB3  . CYS B  1 252 ? -53.00300 -24.37600 26.56700  1.000 27.13687  ? 252 CYS B HB3  1 
ATOM   7165 N  N    . ALA B  1 253 ? -52.27300 -22.10700 23.35600  1.000 18.37698  ? 253 ALA B N    1 
ATOM   7166 C  CA   . ALA B  1 253 ? -52.11500 -20.82200 22.68600  1.000 17.75149  ? 253 ALA B CA   1 
ATOM   7167 C  C    . ALA B  1 253 ? -52.24200 -20.93800 21.18000  1.000 17.30557  ? 253 ALA B C    1 
ATOM   7168 O  O    . ALA B  1 253 ? -52.07800 -19.93800 20.46500  1.000 18.74947  ? 253 ALA B O    1 
ATOM   7169 C  CB   . ALA B  1 253 ? -50.82700 -20.13300 23.10800  1.000 20.13857  ? 253 ALA B CB   1 
ATOM   7170 H  H    . ALA B  1 253 ? -51.55000 -22.57100 23.38800  1.000 22.05494  ? 253 ALA B H    1 
ATOM   7171 H  HA   . ALA B  1 253 ? -52.82000 -20.22300 22.97900  1.000 21.30435  ? 253 ALA B HA   1 
ATOM   7172 H  HB1  . ALA B  1 253 ? -50.75800 -19.28200 22.64700  1.000 24.16885  ? 253 ALA B HB1  1 
ATOM   7173 H  HB2  . ALA B  1 253 ? -50.84500 -19.98800 24.06700  1.000 24.16885  ? 253 ALA B HB2  1 
ATOM   7174 H  HB3  . ALA B  1 253 ? -50.07500 -20.69800 22.87300  1.000 24.16885  ? 253 ALA B HB3  1 
ATOM   7175 N  N    . ASN B  1 254 ? -52.56000 -22.13300 20.68000  1.000 19.31097  ? 254 ASN B N    1 
ATOM   7176 C  CA   . ASN B  1 254 ? -52.75100 -22.32500 19.24200  1.000 19.86395  ? 254 ASN B CA   1 
ATOM   7177 C  C    . ASN B  1 254 ? -54.11000 -21.85100 18.77100  1.000 21.21708  ? 254 ASN B C    1 
ATOM   7178 O  O    . ASN B  1 254 ? -54.31000 -21.69500 17.56300  1.000 21.66355  ? 254 ASN B O    1 
ATOM   7179 C  CB   . ASN B  1 254 ? -52.60500 -23.80400 18.92100  1.000 19.88635  ? 254 ASN B CB   1 
ATOM   7180 C  CG   . ASN B  1 254 ? -51.20300 -24.30800 19.13500  1.000 24.23333  ? 254 ASN B CG   1 
ATOM   7181 O  OD1  . ASN B  1 254 ? -50.31900 -23.55700 19.55300  1.000 27.18361  ? 254 ASN B OD1  1 
ATOM   7182 N  ND2  . ASN B  1 254 ? -50.98400 -25.56400 18.83200  1.000 25.21214  ? 254 ASN B ND2  1 
ATOM   7183 H  H    . ASN B  1 254 ? -52.67100 -22.84500 21.15000  1.000 23.17572  ? 254 ASN B H    1 
ATOM   7184 H  HA   . ASN B  1 254 ? -52.07500 -21.82600 18.75800  1.000 23.83930  ? 254 ASN B HA   1 
ATOM   7185 H  HB2  . ASN B  1 254 ? -53.19800 -24.31300 19.49500  1.000 23.86618  ? 254 ASN B HB2  1 
ATOM   7186 H  HB3  . ASN B  1 254 ? -52.83800 -23.95000 17.99100  1.000 23.86618  ? 254 ASN B HB3  1 
ATOM   7187 H  HD21 . ASN B  1 254 ? -50.20000 -25.90100 18.93600  1.000 30.25714  ? 254 ASN B HD21 1 
ATOM   7188 H  HD22 . ASN B  1 254 ? -51.62500 -26.05100 18.53000  1.000 30.25714  ? 254 ASN B HD22 1 
ATOM   7189 N  N    . GLY B  1 255 ? -55.05000 -21.63300 19.69000  1.000 18.81051  ? 255 GLY B N    1 
ATOM   7190 C  CA   . GLY B  1 255 ? -56.38300 -21.22500 19.30000  1.000 19.56554  ? 255 GLY B CA   1 
ATOM   7191 C  C    . GLY B  1 255 ? -57.20900 -22.36600 18.76700  1.000 21.43267  ? 255 GLY B C    1 
ATOM   7192 O  O    . GLY B  1 255 ? -56.87900 -23.56000 18.88900  1.000 23.22025  ? 255 GLY B O    1 
ATOM   7193 H  H    . GLY B  1 255 ? -54.93500 -21.71500 20.53900  1.000 22.57518  ? 255 GLY B H    1 
ATOM   7194 H  HA2  . GLY B  1 255 ? -56.84100 -20.85200 20.07000  1.000 23.48121  ? 255 GLY B HA2  1 
ATOM   7195 H  HA3  . GLY B  1 255 ? -56.32100 -20.54600 18.61000  1.000 23.48121  ? 255 GLY B HA3  1 
ATOM   7196 N  N    . SER B  1 256 ? -58.35700 -21.98600 18.17500  1.000 20.77729  ? 256 SER B N    1 
ATOM   7197 C  CA   . SER B  1 256 ? -59.42700 -22.93000 17.88100  1.000 24.83891  ? 256 SER B CA   1 
ATOM   7198 C  C    . SER B  1 256 ? -59.78700 -23.75400 19.12300  1.000 23.56364  ? 256 SER B C    1 
ATOM   7199 O  O    . SER B  1 256 ? -59.94900 -24.98400 19.06400  1.000 27.89512  ? 256 SER B O    1 
ATOM   7200 C  CB   . SER B  1 256 ? -59.05900 -23.84900 16.72000  1.000 31.20807  ? 256 SER B CB   1 
ATOM   7201 O  OG   . SER B  1 256 ? -58.73400 -23.08600 15.56900  1.000 34.58264  ? 256 SER B OG   1 
ATOM   7202 H  H    . SER B  1 256 ? -58.53100 -21.17800 17.93600  1.000 24.93531  ? 256 SER B H    1 
ATOM   7203 H  HA   . SER B  1 256 ? -60.20800 -22.41800 17.61900  1.000 29.80925  ? 256 SER B HA   1 
ATOM   7204 H  HB2  . SER B  1 256 ? -58.29100 -24.38600 16.97200  1.000 37.45225  ? 256 SER B HB2  1 
ATOM   7205 H  HB3  . SER B  1 256 ? -59.81400 -24.42300 16.51800  1.000 37.45225  ? 256 SER B HB3  1 
ATOM   7206 H  HG   . SER B  1 256 ? -58.40800 -23.58500 14.97600  1.000 41.50173  ? 256 SER B HG   1 
ATOM   7207 N  N    . ASN B  1 257 ? -59.92400 -23.06200 20.25500  1.000 23.44682  ? 257 ASN B N    1 
ATOM   7208 C  CA   . ASN B  1 257 ? -60.14800 -23.71200 21.54600  1.000 22.80011  ? 257 ASN B CA   1 
ATOM   7209 C  C    . ASN B  1 257 ? -60.87300 -22.73800 22.46400  1.000 23.70018  ? 257 ASN B C    1 
ATOM   7210 O  O    . ASN B  1 257 ? -61.31600 -21.66700 22.04400  1.000 24.26034  ? 257 ASN B O    1 
ATOM   7211 C  CB   . ASN B  1 257 ? -58.82400 -24.22900 22.13200  1.000 24.30832  ? 257 ASN B CB   1 
ATOM   7212 C  CG   . ASN B  1 257 ? -57.83600 -23.12800 22.45500  1.000 22.90496  ? 257 ASN B CG   1 
ATOM   7213 O  OD1  . ASN B  1 257 ? -58.18800 -21.94700 22.61900  1.000 22.34414  ? 257 ASN B OD1  1 
ATOM   7214 N  ND2  . ASN B  1 257 ? -56.55400 -23.50500 22.53500  1.000 24.12154  ? 257 ASN B ND2  1 
ATOM   7215 H  H    . ASN B  1 257 ? -59.89000 -22.20400 20.30200  1.000 28.13874  ? 257 ASN B H    1 
ATOM   7216 H  HA   . ASN B  1 257 ? -60.73100 -24.47500 21.41200  1.000 27.36269  ? 257 ASN B HA   1 
ATOM   7217 H  HB2  . ASN B  1 257 ? -59.01200 -24.70900 22.95400  1.000 29.17255  ? 257 ASN B HB2  1 
ATOM   7218 H  HB3  . ASN B  1 257 ? -58.40700 -24.82300 21.48800  1.000 29.17255  ? 257 ASN B HB3  1 
ATOM   7219 H  HD21 . ASN B  1 257 ? -55.94600 -22.92500 22.71600  1.000 28.94841  ? 257 ASN B HD21 1 
ATOM   7220 H  HD22 . ASN B  1 257 ? -56.33900 -24.32800 22.40600  1.000 28.94841  ? 257 ASN B HD22 1 
ATOM   7221 N  N    . ARG B  1 258 ? -60.96900 -23.09800 23.74600  1.000 24.04413  ? 258 ARG B N    1 
ATOM   7222 C  CA   . ARG B  1 258 ? -61.72000 -22.28700 24.68900  1.000 23.67095  ? 258 ARG B CA   1 
ATOM   7223 C  C    . ARG B  1 258 ? -61.04900 -20.96500 25.02800  1.000 21.97217  ? 258 ARG B C    1 
ATOM   7224 O  O    . ARG B  1 258 ? -61.65200 -20.17200 25.76700  1.000 24.20838  ? 258 ARG B O    1 
ATOM   7225 C  CB   . ARG B  1 258 ? -61.93000 -23.05600 25.99300  1.000 25.36468  ? 258 ARG B CB   1 
ATOM   7226 C  CG   . ARG B  1 258 ? -60.63500 -23.28300 26.75400  1.000 24.88423  ? 258 ARG B CG   1 
ATOM   7227 C  CD   . ARG B  1 258 ? -60.84100 -24.25500 27.93500  1.000 32.05325  ? 258 ARG B CD   1 
ATOM   7228 N  NE   . ARG B  1 258 ? -60.92300 -25.62600 27.44900  1.000 65.77160  ? 258 ARG B NE   1 
ATOM   7229 C  CZ   . ARG B  1 258 ? -60.88200 -26.70200 28.22300  1.000 81.70745  ? 258 ARG B CZ   1 
ATOM   7230 N  NH1  . ARG B  1 258 ? -60.73900 -26.60400 29.53500  1.000 72.66918  ? 258 ARG B NH1  1 
ATOM   7231 N  NH2  . ARG B  1 258 ? -60.98400 -27.90500 27.66600  1.000 81.01879  ? 258 ARG B NH2  1 
ATOM   7232 H  H    . ARG B  1 258 ? -60.61000 -23.80100 24.08600  1.000 28.85552  ? 258 ARG B H    1 
ATOM   7233 H  HA   . ARG B  1 258 ? -62.58100 -22.09800 24.28300  1.000 28.40770  ? 258 ARG B HA   1 
ATOM   7234 H  HB2  . ARG B  1 258 ? -62.53000 -22.55200 26.56400  1.000 30.44018  ? 258 ARG B HB2  1 
ATOM   7235 H  HB3  . ARG B  1 258 ? -62.31500 -23.92300 25.79000  1.000 30.44018  ? 258 ARG B HB3  1 
ATOM   7236 H  HG2  . ARG B  1 258 ? -59.97300 -23.66400 26.15600  1.000 29.86363  ? 258 ARG B HG2  1 
ATOM   7237 H  HG3  . ARG B  1 258 ? -60.31700 -22.43700 27.10600  1.000 29.86363  ? 258 ARG B HG3  1 
ATOM   7238 H  HD2  . ARG B  1 258 ? -60.09200 -24.18700 28.54700  1.000 38.46646  ? 258 ARG B HD2  1 
ATOM   7239 H  HD3  . ARG B  1 258 ? -61.66700 -24.03800 28.39500  1.000 38.46646  ? 258 ARG B HD3  1 
ATOM   7240 H  HE   . ARG B  1 258 ? -61.00400 -25.74600 26.60100  1.000 78.92848  ? 258 ARG B HE   1 
ATOM   7241 H  HH11 . ARG B  1 258 ? -60.67000 -25.83000 29.90300  1.000 87.20558  ? 258 ARG B HH11 1 
ATOM   7242 H  HH12 . ARG B  1 258 ? -60.71500 -27.31500 30.01800  1.000 87.20558  ? 258 ARG B HH12 1 
ATOM   7243 H  HH21 . ARG B  1 258 ? -61.07600 -27.97900 26.81400  1.000 97.22511  ? 258 ARG B HH21 1 
ATOM   7244 H  HH22 . ARG B  1 258 ? -60.95900 -28.61000 28.15800  1.000 97.22511  ? 258 ARG B HH22 1 
ATOM   7245 N  N    . TYR B  1 259 ? -59.84700 -20.72500 24.53300  1.000 19.68907  ? 259 TYR B N    1 
ATOM   7246 C  CA   . TYR B  1 259 ? -59.07400 -19.51800 24.81400  1.000 20.55251  ? 259 TYR B CA   1 
ATOM   7247 C  C    . TYR B  1 259 ? -59.09300 -18.50400 23.66300  1.000 19.96963  ? 259 TYR B C    1 
ATOM   7248 O  O    . TYR B  1 259 ? -58.37400 -17.50700 23.72100  1.000 19.60737  ? 259 TYR B O    1 
ATOM   7249 C  CB   . TYR B  1 259 ? -57.62600 -19.87400 25.17800  1.000 21.68069  ? 259 TYR B CB   1 
ATOM   7250 C  CG   . TYR B  1 259 ? -57.51300 -20.82000 26.34800  1.000 20.93520  ? 259 TYR B CG   1 
ATOM   7251 C  CD1  . TYR B  1 259 ? -57.86400 -20.42100 27.61200  1.000 22.02410  ? 259 TYR B CD1  1 
ATOM   7252 C  CD2  . TYR B  1 259 ? -57.03500 -22.11300 26.17100  1.000 21.50566  ? 259 TYR B CD2  1 
ATOM   7253 C  CE1  . TYR B  1 259 ? -57.76800 -21.30000 28.69100  1.000 22.76834  ? 259 TYR B CE1  1 
ATOM   7254 C  CE2  . TYR B  1 259 ? -56.93400 -22.99100 27.23700  1.000 21.80266  ? 259 TYR B CE2  1 
ATOM   7255 C  CZ   . TYR B  1 259 ? -57.28700 -22.57700 28.48800  1.000 21.50907  ? 259 TYR B CZ   1 
ATOM   7256 O  OH   . TYR B  1 259 ? -57.16800 -23.49800 29.54200  1.000 25.94698  ? 259 TYR B OH   1 
ATOM   7257 H  H    . TYR B  1 259 ? -59.43500 -21.26800 24.00900  1.000 23.62945  ? 259 TYR B H    1 
ATOM   7258 H  HA   . TYR B  1 259 ? -59.47400 -19.08700 25.58600  1.000 24.66557  ? 259 TYR B HA   1 
ATOM   7259 H  HB2  . TYR B  1 259 ? -57.20600 -20.29700 24.41300  1.000 26.01939  ? 259 TYR B HB2  1 
ATOM   7260 H  HB3  . TYR B  1 259 ? -57.15200 -19.05900 25.40900  1.000 26.01939  ? 259 TYR B HB3  1 
ATOM   7261 H  HD1  . TYR B  1 259 ? -58.16900 -19.55400 27.75100  1.000 26.43148  ? 259 TYR B HD1  1 
ATOM   7262 H  HD2  . TYR B  1 259 ? -56.77900 -22.39300 25.32200  1.000 25.80935  ? 259 TYR B HD2  1 
ATOM   7263 H  HE1  . TYR B  1 259 ? -58.02700 -21.02700 29.54200  1.000 27.32457  ? 259 TYR B HE1  1 
ATOM   7264 H  HE2  . TYR B  1 259 ? -56.62700 -23.85800 27.10100  1.000 26.16576  ? 259 TYR B HE2  1 
ATOM   7265 H  HH   . TYR B  1 259 ? -57.30600 -23.11400 30.27600  1.000 31.13894  ? 259 TYR B HH   1 
ATOM   7266 N  N    . ASP B  1 260 ? -59.91300 -18.73700 22.63000  1.000 19.05457  ? 260 ASP B N    1 
ATOM   7267 C  CA   . ASP B  1 260 ? -59.85800 -17.89800 21.43100  1.000 18.53034  ? 260 ASP B CA   1 
ATOM   7268 C  C    . ASP B  1 260 ? -60.06800 -16.40700 21.72000  1.000 19.10066  ? 260 ASP B C    1 
ATOM   7269 O  O    . ASP B  1 260 ? -59.39400 -15.55300 21.13000  1.000 18.88854  ? 260 ASP B O    1 
ATOM   7270 C  CB   . ASP B  1 260 ? -60.92300 -18.32700 20.42700  1.000 19.19547  ? 260 ASP B CB   1 
ATOM   7271 C  CG   . ASP B  1 260 ? -60.57600 -19.59500 19.65200  1.000 22.28736  ? 260 ASP B CG   1 
ATOM   7272 O  OD1  . ASP B  1 260 ? -59.52700 -20.18400 19.87700  1.000 24.25179  ? 260 ASP B OD1  1 
ATOM   7273 O  OD2  . ASP B  1 260 ? -61.44400 -19.98900 18.83000  1.000 29.08947  ? 260 ASP B OD2  1 
ATOM   7274 H  H    . ASP B  1 260 ? -60.49900 -19.36600 22.60000  1.000 22.86804  ? 260 ASP B H    1 
ATOM   7275 H  HA   . ASP B  1 260 ? -58.97000 -18.02200 21.06000  1.000 22.23897  ? 260 ASP B HA   1 
ATOM   7276 H  HB2  . ASP B  1 260 ? -61.75100 -18.49200 20.90400  1.000 23.03712  ? 260 ASP B HB2  1 
ATOM   7277 H  HB3  . ASP B  1 260 ? -61.04800 -17.61300 19.78200  1.000 23.03712  ? 260 ASP B HB3  1 
ATOM   7278 N  N    . ALA B  1 261 ? -61.04900 -16.06300 22.55300  1.000 19.28832  ? 261 ALA B N    1 
ATOM   7279 C  CA   . ALA B  1 261 ? -61.32100 -14.64800 22.82000  1.000 18.43676  ? 261 ALA B CA   1 
ATOM   7280 C  C    . ALA B  1 261 ? -60.11200 -13.96400 23.44300  1.000 18.71513  ? 261 ALA B C    1 
ATOM   7281 O  O    . ALA B  1 261 ? -59.72900 -12.85400 23.03600  1.000 18.35772  ? 261 ALA B O    1 
ATOM   7282 C  CB   . ALA B  1 261 ? -62.53100 -14.50400 23.74400  1.000 20.05522  ? 261 ALA B CB   1 
ATOM   7283 H  H    . ALA B  1 261 ? -61.56200 -16.61400 22.96800  1.000 23.14854  ? 261 ALA B H    1 
ATOM   7284 H  HA   . ALA B  1 261 ? -61.52500 -14.21200 21.97800  1.000 22.12667  ? 261 ALA B HA   1 
ATOM   7285 H  HB1  . ALA B  1 261 ? -62.68100 -13.56200 23.92300  1.000 24.06883  ? 261 ALA B HB1  1 
ATOM   7286 H  HB2  . ALA B  1 261 ? -63.30800 -14.88500 23.30700  1.000 24.06883  ? 261 ALA B HB2  1 
ATOM   7287 H  HB3  . ALA B  1 261 ? -62.35300 -14.97400 24.57300  1.000 24.06883  ? 261 ALA B HB3  1 
ATOM   7288 N  N    . LEU B  1 262 ? -59.50300 -14.61900 24.42600  1.000 17.98313  ? 262 LEU B N    1 
ATOM   7289 C  CA   . LEU B  1 262 ? -58.32500 -14.07700 25.10500  1.000 17.58832  ? 262 LEU B CA   1 
ATOM   7290 C  C    . LEU B  1 262 ? -57.13800 -13.97900 24.15600  1.000 18.91898  ? 262 LEU B C    1 
ATOM   7291 O  O    . LEU B  1 262 ? -56.44900 -12.95600 24.09600  1.000 17.30982  ? 262 LEU B O    1 
ATOM   7292 C  CB   . LEU B  1 262 ? -58.01700 -14.96500 26.30200  1.000 21.47719  ? 262 LEU B CB   1 
ATOM   7293 C  CG   . LEU B  1 262 ? -56.79900 -14.72400 27.15700  1.000 23.36258  ? 262 LEU B CG   1 
ATOM   7294 C  CD1  . LEU B  1 262 ? -56.99300 -15.44100 28.50800  1.000 27.02734  ? 262 LEU B CD1  1 
ATOM   7295 C  CD2  . LEU B  1 262 ? -55.51800 -15.20100 26.51400  1.000 22.46364  ? 262 LEU B CD2  1 
ATOM   7296 H  H    . LEU B  1 262 ? -59.75100 -15.38600 24.72500  1.000 21.58231  ? 262 LEU B H    1 
ATOM   7297 H  HA   . LEU B  1 262 ? -58.50300 -13.17800 25.42200  1.000 21.10854  ? 262 LEU B HA   1 
ATOM   7298 H  HB2  . LEU B  1 262 ? -58.77700 -14.90600 26.90100  1.000 25.77519  ? 262 LEU B HB2  1 
ATOM   7299 H  HB3  . LEU B  1 262 ? -57.92900 -15.87100 25.96700  1.000 25.77519  ? 262 LEU B HB3  1 
ATOM   7300 H  HG   . LEU B  1 262 ? -56.70300 -13.76600 27.28100  1.000 28.03766  ? 262 LEU B HG   1 
ATOM   7301 H  HD11 . LEU B  1 262 ? -56.17300 -15.37400 29.02200  1.000 32.43537  ? 262 LEU B HD11 1 
ATOM   7302 H  HD12 . LEU B  1 262 ? -57.72100 -15.01600 28.99000  1.000 32.43537  ? 262 LEU B HD12 1 
ATOM   7303 H  HD13 . LEU B  1 262 ? -57.20500 -16.37300 28.34400  1.000 32.43537  ? 262 LEU B HD13 1 
ATOM   7304 H  HD21 . LEU B  1 262 ? -54.83700 -15.29700 27.19800  1.000 26.95893  ? 262 LEU B HD21 1 
ATOM   7305 H  HD22 . LEU B  1 262 ? -55.67900 -16.05600 26.08500  1.000 26.95893  ? 262 LEU B HD22 1 
ATOM   7306 H  HD23 . LEU B  1 262 ? -55.23400 -14.54900 25.85400  1.000 26.95893  ? 262 LEU B HD23 1 
ATOM   7307 N  N    . LEU B  1 263 ? -56.86600 -15.05000 23.43000  1.000 17.14696  ? 263 LEU B N    1 
ATOM   7308 C  CA   . LEU B  1 263 ? -55.71700 -15.07300 22.54300  1.000 16.63811  ? 263 LEU B CA   1 
ATOM   7309 C  C    . LEU B  1 263 ? -55.83100 -14.00500 21.48100  1.000 16.39324  ? 263 LEU B C    1 
ATOM   7310 O  O    . LEU B  1 263 ? -54.86300 -13.27600 21.20900  1.000 16.09141  ? 263 LEU B O    1 
ATOM   7311 C  CB   . LEU B  1 263 ? -55.60300 -16.44100 21.89400  1.000 17.79090  ? 263 LEU B CB   1 
ATOM   7312 C  CG   . LEU B  1 263 ? -55.20800 -17.58200 22.82800  1.000 16.98933  ? 263 LEU B CG   1 
ATOM   7313 C  CD1  . LEU B  1 263 ? -55.45800 -18.89200 22.08400  1.000 18.62262  ? 263 LEU B CD1  1 
ATOM   7314 C  CD2  . LEU B  1 263 ? -53.76000 -17.48200 23.26200  1.000 18.65783  ? 263 LEU B CD2  1 
ATOM   7315 H  H    . LEU B  1 263 ? -57.32900 -15.77500 23.43200  1.000 20.57891  ? 263 LEU B H    1 
ATOM   7316 H  HA   . LEU B  1 263 ? -54.91500 -14.90600 23.06300  1.000 19.96829  ? 263 LEU B HA   1 
ATOM   7317 H  HB2  . LEU B  1 263 ? -56.46400 -16.66700 21.50900  1.000 21.35164  ? 263 LEU B HB2  1 
ATOM   7318 H  HB3  . LEU B  1 263 ? -54.93100 -16.39200 21.19600  1.000 21.35164  ? 263 LEU B HB3  1 
ATOM   7319 H  HG   . LEU B  1 263 ? -55.73500 -17.54600 23.64100  1.000 20.38976  ? 263 LEU B HG   1 
ATOM   7320 H  HD11 . LEU B  1 263 ? -55.19900 -19.63300 22.65300  1.000 22.34971  ? 263 LEU B HD11 1 
ATOM   7321 H  HD12 . LEU B  1 263 ? -56.40000 -18.95600 21.86500  1.000 22.34971  ? 263 LEU B HD12 1 
ATOM   7322 H  HD13 . LEU B  1 263 ? -54.92900 -18.89900 21.27100  1.000 22.34971  ? 263 LEU B HD13 1 
ATOM   7323 H  HD21 . LEU B  1 263 ? -53.57700 -18.17600 23.91500  1.000 22.39196  ? 263 LEU B HD21 1 
ATOM   7324 H  HD22 . LEU B  1 263 ? -53.18900 -17.59800 22.48700  1.000 22.39196  ? 263 LEU B HD22 1 
ATOM   7325 H  HD23 . LEU B  1 263 ? -53.60900 -16.60900 23.65700  1.000 22.39196  ? 263 LEU B HD23 1 
ATOM   7326 N  N    . GLY B  1 264 ? -56.98100 -13.94900 20.80600  1.000 16.62322  ? 264 GLY B N    1 
ATOM   7327 C  CA   . GLY B  1 264 ? -57.12900 -12.98700 19.73300  1.000 16.91925  ? 264 GLY B CA   1 
ATOM   7328 C  C    . GLY B  1 264 ? -57.12700 -11.56800 20.24400  1.000 16.60797  ? 264 GLY B C    1 
ATOM   7329 O  O    . GLY B  1 264 ? -56.56200 -10.68800 19.60700  1.000 15.53051  ? 264 GLY B O    1 
ATOM   7330 H  H    . GLY B  1 264 ? -57.66800 -14.44600 20.95000  1.000 19.95042  ? 264 GLY B H    1 
ATOM   7331 H  HA2  . GLY B  1 264 ? -56.39800 -13.08900 19.10500  1.000 20.30567  ? 264 GLY B HA2  1 
ATOM   7332 H  HA3  . GLY B  1 264 ? -57.96700 -13.14600 19.27100  1.000 20.30567  ? 264 GLY B HA3  1 
ATOM   7333 N  N    . LYS B  1 265 ? -57.75100 -11.32000 21.40000  1.000 15.82533  ? 265 LYS B N    1 
ATOM   7334 C  CA   . LYS B  1 265 ? -57.75100 -9.96000  21.94900  1.000 15.61330  ? 265 LYS B CA   1 
ATOM   7335 C  C    . LYS B  1 265 ? -56.31900 -9.47300  22.19500  1.000 15.11686  ? 265 LYS B C    1 
ATOM   7336 O  O    . LYS B  1 265 ? -55.89800 -8.42100  21.70000  1.000 16.34366  ? 265 LYS B O    1 
ATOM   7337 C  CB   . LYS B  1 265 ? -58.55300 -9.92400  23.24900  1.000 17.24180  ? 265 LYS B CB   1 
ATOM   7338 C  CG   . LYS B  1 265 ? -58.42200 -8.62000  24.02700  1.000 18.42777  ? 265 LYS B CG   1 
ATOM   7339 C  CD   . LYS B  1 265 ? -59.41400 -8.52200  25.20200  1.000 18.23885  ? 265 LYS B CD   1 
ATOM   7340 C  CE   . LYS B  1 265 ? -59.25700 -9.68400  26.12900  1.000 20.02367  ? 265 LYS B CE   1 
ATOM   7341 N  NZ   . LYS B  1 265 ? -60.29500 -9.59900  27.27100  1.000 23.87978  ? 265 LYS B NZ   1 
ATOM   7342 H  H    . LYS B  1 265 ? -58.17000 -11.90400 21.87200  1.000 18.99295  ? 265 LYS B H    1 
ATOM   7343 H  HA   . LYS B  1 265 ? -58.17400 -9.36500  21.31100  1.000 18.73852  ? 265 LYS B HA   1 
ATOM   7344 H  HB2  . LYS B  1 265 ? -59.49200 -10.04700 23.03700  1.000 20.69273  ? 265 LYS B HB2  1 
ATOM   7345 H  HB3  . LYS B  1 265 ? -58.24600 -10.64200 23.82400  1.000 20.69273  ? 265 LYS B HB3  1 
ATOM   7346 H  HG2  . LYS B  1 265 ? -57.52400 -8.55700  24.38800  1.000 22.11589  ? 265 LYS B HG2  1 
ATOM   7347 H  HG3  . LYS B  1 265 ? -58.59300 -7.87600  23.42900  1.000 22.11589  ? 265 LYS B HG3  1 
ATOM   7348 H  HD2  . LYS B  1 265 ? -59.24700 -7.70600  25.69900  1.000 21.88918  ? 265 LYS B HD2  1 
ATOM   7349 H  HD3  . LYS B  1 265 ? -60.32200 -8.52200  24.86000  1.000 21.88918  ? 265 LYS B HD3  1 
ATOM   7350 H  HE2  . LYS B  1 265 ? -59.39800 -10.51100 25.64300  1.000 24.03097  ? 265 LYS B HE2  1 
ATOM   7351 H  HE3  . LYS B  1 265 ? -58.36800 -9.67400  26.51700  1.000 24.03097  ? 265 LYS B HE3  1 
ATOM   7352 H  HZ1  . LYS B  1 265 ? -60.20000 -10.29300 27.82100  1.000 28.65829  ? 265 LYS B HZ1  1 
ATOM   7353 H  HZ2  . LYS B  1 265 ? -60.17900 -8.84700  27.73300  1.000 28.65829  ? 265 LYS B HZ2  1 
ATOM   7354 H  HZ3  . LYS B  1 265 ? -61.11900 -9.60800  26.93500  1.000 28.65829  ? 265 LYS B HZ3  1 
ATOM   7355 N  N    . TYR B  1 266 ? -55.55800 -10.22800 22.97200  1.000 15.19885  ? 266 TYR B N    1 
ATOM   7356 C  CA   . TYR B  1 266 ? -54.22900 -9.76900  23.34700  1.000 15.55805  ? 266 TYR B CA   1 
ATOM   7357 C  C    . TYR B  1 266 ? -53.24900 -9.86100  22.19200  1.000 15.92356  ? 266 TYR B C    1 
ATOM   7358 O  O    . TYR B  1 266 ? -52.39800 -8.98700  22.03400  1.000 15.60586  ? 266 TYR B O    1 
ATOM   7359 C  CB   . TYR B  1 266 ? -53.74300 -10.55300 24.55500  1.000 15.94739  ? 266 TYR B CB   1 
ATOM   7360 C  CG   . TYR B  1 266 ? -54.46400 -10.23100 25.85600  1.000 17.52168  ? 266 TYR B CG   1 
ATOM   7361 C  CD1  . TYR B  1 266 ? -54.53900 -8.94400  26.34000  1.000 17.99476  ? 266 TYR B CD1  1 
ATOM   7362 C  CD2  . TYR B  1 266 ? -55.06500 -11.23000 26.58100  1.000 19.79188  ? 266 TYR B CD2  1 
ATOM   7363 C  CE1  . TYR B  1 266 ? -55.19400 -8.65200  27.49700  1.000 21.04361  ? 266 TYR B CE1  1 
ATOM   7364 C  CE2  . TYR B  1 266 ? -55.71100 -10.95500 27.78700  1.000 21.74229  ? 266 TYR B CE2  1 
ATOM   7365 C  CZ   . TYR B  1 266 ? -55.75900 -9.65900  28.22000  1.000 21.25690  ? 266 TYR B CZ   1 
ATOM   7366 O  OH   . TYR B  1 266 ? -56.36400 -9.40300  29.44600  1.000 24.81134  ? 266 TYR B OH   1 
ATOM   7367 H  H    . TYR B  1 266 ? -55.78100 -10.99500 23.29100  1.000 18.24119  ? 266 TYR B H    1 
ATOM   7368 H  HA   . TYR B  1 266 ? -54.27600 -8.83300  23.59700  1.000 18.67222  ? 266 TYR B HA   1 
ATOM   7369 H  HB2  . TYR B  1 266 ? -53.86800 -11.49900 24.37900  1.000 19.13943  ? 266 TYR B HB2  1 
ATOM   7370 H  HB3  . TYR B  1 266 ? -52.80100 -10.36200 24.68800  1.000 19.13943  ? 266 TYR B HB3  1 
ATOM   7371 H  HD1  . TYR B  1 266 ? -54.13100 -8.25700  25.86400  1.000 21.59627  ? 266 TYR B HD1  1 
ATOM   7372 H  HD2  . TYR B  1 266 ? -55.04200 -12.10300 26.26400  1.000 23.75282  ? 266 TYR B HD2  1 
ATOM   7373 H  HE1  . TYR B  1 266 ? -55.25500 -7.77200  27.79200  1.000 25.25489  ? 266 TYR B HE1  1 
ATOM   7374 H  HE2  . TYR B  1 266 ? -56.09900 -11.63800 28.28500  1.000 26.09331  ? 266 TYR B HE2  1 
ATOM   7375 H  HH   . TYR B  1 266 ? -56.49200 -10.12300 29.85900  1.000 29.77617  ? 266 TYR B HH   1 
ATOM   7376 N  N    . GLY B  1 267 ? -53.39000 -10.86700 21.33600  1.000 14.83270  ? 267 GLY B N    1 
ATOM   7377 C  CA   . GLY B  1 267 ? -52.48400 -10.98300 20.20800  1.000 15.38453  ? 267 GLY B CA   1 
ATOM   7378 C  C    . GLY B  1 267 ? -52.67600 -9.87400  19.19400  1.000 14.56835  ? 267 GLY B C    1 
ATOM   7379 O  O    . GLY B  1 267 ? -51.71900 -9.29100  18.69100  1.000 15.39629  ? 267 GLY B O    1 
ATOM   7380 H  H    . GLY B  1 267 ? -53.98900 -11.48200 21.38600  1.000 17.80180  ? 267 GLY B H    1 
ATOM   7381 H  HA2  . GLY B  1 267 ? -51.56800 -10.95000 20.52800  1.000 18.46400  ? 267 GLY B HA2  1 
ATOM   7382 H  HA3  . GLY B  1 267 ? -52.63200 -11.83200 19.76400  1.000 18.46400  ? 267 GLY B HA3  1 
ATOM   7383 N  N    . VAL B  1 268 ? -53.92400 -9.60900  18.81900  1.000 14.49388  ? 268 VAL B N    1 
ATOM   7384 C  CA   . VAL B  1 268 ? -54.21100 -8.50700  17.90300  1.000 14.75491  ? 268 VAL B CA   1 
ATOM   7385 C  C    . VAL B  1 268 ? -53.78400 -7.19200  18.52800  1.000 15.81853  ? 268 VAL B C    1 
ATOM   7386 O  O    . VAL B  1 268 ? -53.16600 -6.35500  17.85300  1.000 14.82224  ? 268 VAL B O    1 
ATOM   7387 C  CB   . VAL B  1 268 ? -55.68200 -8.50400  17.44500  1.000 14.71514  ? 268 VAL B CB   1 
ATOM   7388 C  CG1  . VAL B  1 268 ? -56.02600 -7.19800  16.72600  1.000 16.50812  ? 268 VAL B CG1  1 
ATOM   7389 C  CG2  . VAL B  1 268 ? -55.93800 -9.68900  16.54400  1.000 15.87162  ? 268 VAL B CG2  1 
ATOM   7390 H  H    . VAL B  1 268 ? -54.61800 -10.04700 19.07800  1.000 17.37984  ? 268 VAL B H    1 
ATOM   7391 H  HA   . VAL B  1 268 ? -53.68600 -8.63800  17.09800  1.000 17.70846  ? 268 VAL B HA   1 
ATOM   7392 H  HB   . VAL B  1 268 ? -56.25600 -8.57300  18.22300  1.000 17.66073  ? 268 VAL B HB   1 
ATOM   7393 H  HG11 . VAL B  1 268 ? -56.88400 -7.29800  16.28400  1.000 19.81230  ? 268 VAL B HG11 1 
ATOM   7394 H  HG12 . VAL B  1 268 ? -56.07200 -6.48100  17.37800  1.000 19.81230  ? 268 VAL B HG12 1 
ATOM   7395 H  HG13 . VAL B  1 268 ? -55.33600 -7.00600  16.07200  1.000 19.81230  ? 268 VAL B HG13 1 
ATOM   7396 H  HG21 . VAL B  1 268 ? -56.87600 -9.70100  16.29600  1.000 19.04850  ? 268 VAL B HG21 1 
ATOM   7397 H  HG22 . VAL B  1 268 ? -55.38800 -9.60700  15.74900  1.000 19.04850  ? 268 VAL B HG22 1 
ATOM   7398 H  HG23 . VAL B  1 268 ? -55.71200 -10.50300 17.02000  1.000 19.04850  ? 268 VAL B HG23 1 
ATOM   7399 N  N    . ALA B  1 269 ? -54.13700 -6.96300  19.81100  1.000 15.79945  ? 269 ALA B N    1 
ATOM   7400 C  CA   . ALA B  1 269 ? -53.73900 -5.69500  20.41500  1.000 15.77558  ? 269 ALA B CA   1 
ATOM   7401 C  C    . ALA B  1 269 ? -52.22200 -5.52500  20.35900  1.000 14.81113  ? 269 ALA B C    1 
ATOM   7402 O  O    . ALA B  1 269 ? -51.73700 -4.42200  20.10500  1.000 15.39820  ? 269 ALA B O    1 
ATOM   7403 C  CB   . ALA B  1 269 ? -54.22400 -5.60300  21.86000  1.000 16.07522  ? 269 ALA B CB   1 
ATOM   7404 H  H    . ALA B  1 269 ? -54.58000 -7.49900  20.31600  1.000 18.96191  ? 269 ALA B H    1 
ATOM   7405 H  HA   . ALA B  1 269 ? -54.15700 -4.97500  19.91800  1.000 18.93326  ? 269 ALA B HA   1 
ATOM   7406 H  HB1  . ALA B  1 269 ? -53.95900 -4.74500  22.22800  1.000 19.29283  ? 269 ALA B HB1  1 
ATOM   7407 H  HB2  . ALA B  1 269 ? -55.19000 -5.68500  21.87500  1.000 19.29283  ? 269 ALA B HB2  1 
ATOM   7408 H  HB3  . ALA B  1 269 ? -53.82300 -6.32100  22.37400  1.000 19.29283  ? 269 ALA B HB3  1 
ATOM   7409 N  N    . TRP B  1 270 ? -51.45300 -6.59900  20.63600  1.000 14.40206  ? 270 TRP B N    1 
ATOM   7410 C  CA   . TRP B  1 270 ? -49.99200 -6.50700  20.58600  1.000 14.35638  ? 270 TRP B CA   1 
ATOM   7411 C  C    . TRP B  1 270 ? -49.51700 -6.07800  19.20600  1.000 15.90890  ? 270 TRP B C    1 
ATOM   7412 O  O    . TRP B  1 270 ? -48.64600 -5.20800  19.07900  1.000 15.67069  ? 270 TRP B O    1 
ATOM   7413 C  CB   . TRP B  1 270 ? -49.38200 -7.85300  20.93900  1.000 15.23365  ? 270 TRP B CB   1 
ATOM   7414 C  CG   . TRP B  1 270 ? -47.91000 -7.72600  21.28900  1.000 14.96864  ? 270 TRP B CG   1 
ATOM   7415 C  CD1  . TRP B  1 270 ? -46.82500 -8.08400  20.54300  1.000 16.39336  ? 270 TRP B CD1  1 
ATOM   7416 C  CD2  . TRP B  1 270 ? -47.40000 -7.19200  22.51100  1.000 15.55161  ? 270 TRP B CD2  1 
ATOM   7417 N  NE1  . TRP B  1 270 ? -45.66700 -7.79800  21.22900  1.000 16.06290  ? 270 TRP B NE1  1 
ATOM   7418 C  CE2  . TRP B  1 270 ? -45.99200 -7.25100  22.44100  1.000 15.44605  ? 270 TRP B CE2  1 
ATOM   7419 C  CE3  . TRP B  1 270 ? -48.00000 -6.67100  23.66500  1.000 18.09913  ? 270 TRP B CE3  1 
ATOM   7420 C  CZ2  . TRP B  1 270 ? -45.18300 -6.80600  23.47800  1.000 17.54595  ? 270 TRP B CZ2  1 
ATOM   7421 C  CZ3  . TRP B  1 270 ? -47.18400 -6.22400  24.68800  1.000 16.55671  ? 270 TRP B CZ3  1 
ATOM   7422 C  CH2  . TRP B  1 270 ? -45.79300 -6.29800  24.58300  1.000 17.04931  ? 270 TRP B CH2  1 
ATOM   7423 H  H    . TRP B  1 270 ? -51.75400 -7.37600  20.85000  1.000 17.26966  ? 270 TRP B H    1 
ATOM   7424 H  HA   . TRP B  1 270 ? -49.70000 -5.84700  21.23400  1.000 17.21485  ? 270 TRP B HA   1 
ATOM   7425 H  HB2  . TRP B  1 270 ? -49.84700 -8.22400  21.70500  1.000 18.28295  ? 270 TRP B HB2  1 
ATOM   7426 H  HB3  . TRP B  1 270 ? -49.46400 -8.45100  20.18000  1.000 18.28295  ? 270 TRP B HB3  1 
ATOM   7427 H  HD1  . TRP B  1 270 ? -46.86300 -8.46600  19.69500  1.000 19.67460  ? 270 TRP B HD1  1 
ATOM   7428 H  HE1  . TRP B  1 270 ? -44.86900 -7.94100  20.94300  1.000 19.27804  ? 270 TRP B HE1  1 
ATOM   7429 H  HE3  . TRP B  1 270 ? -48.92500 -6.62700  23.74100  1.000 21.72152  ? 270 TRP B HE3  1 
ATOM   7430 H  HZ2  . TRP B  1 270 ? -44.25600 -6.85300  23.41900  1.000 21.05770  ? 270 TRP B HZ2  1 
ATOM   7431 H  HZ3  . TRP B  1 270 ? -47.56700 -5.86900  25.45700  1.000 19.87062  ? 270 TRP B HZ3  1 
ATOM   7432 H  HH2  . TRP B  1 270 ? -45.27000 -5.99200  25.28800  1.000 20.46173  ? 270 TRP B HH2  1 
ATOM   7433 N  N    . MET B  1 271 ? -50.02700 -6.73400  18.15800  1.000 14.27804  ? 271 MET B N    1 
ATOM   7434 C  CA   . MET B  1 271 ? -49.57900 -6.41500  16.81300  1.000 14.03203  ? 271 MET B CA   1 
ATOM   7435 C  C    . MET B  1 271 ? -50.03200 -5.02600  16.38200  1.000 15.99554  ? 271 MET B C    1 
ATOM   7436 O  O    . MET B  1 271 ? -49.28200 -4.29800  15.73200  1.000 16.15495  ? 271 MET B O    1 
ATOM   7437 C  CB   . MET B  1 271 ? -50.03300 -7.49800  15.83500  1.000 14.85081  ? 271 MET B CB   1 
ATOM   7438 C  CG   . MET B  1 271 ? -49.43600 -8.86400  16.14000  1.000 15.04353  ? 271 MET B CG   1 
ATOM   7439 S  SD   . MET B  1 271 ? -47.64800 -8.81200  16.36000  1.000 16.56925  ? 271 MET B SD   1 
ATOM   7440 C  CE   . MET B  1 271 ? -47.16700 -10.42100 15.74700  1.000 18.94239  ? 271 MET B CE   1 
ATOM   7441 H  H    . MET B  1 271 ? -50.62100 -7.35400  18.20300  1.000 17.13621  ? 271 MET B H    1 
ATOM   7442 H  HA   . MET B  1 271 ? -48.60900 -6.42000  16.80100  1.000 16.82562  ? 271 MET B HA   1 
ATOM   7443 H  HB2  . MET B  1 271 ? -50.99900 -7.57600  15.87800  1.000 17.82353  ? 271 MET B HB2  1 
ATOM   7444 H  HB3  . MET B  1 271 ? -49.76100 -7.24600  14.93800  1.000 17.82353  ? 271 MET B HB3  1 
ATOM   7445 H  HG2  . MET B  1 271 ? -49.82900 -9.20500  16.95900  1.000 18.05480  ? 271 MET B HG2  1 
ATOM   7446 H  HG3  . MET B  1 271 ? -49.63000 -9.46600  15.40400  1.000 18.05480  ? 271 MET B HG3  1 
ATOM   7447 H  HE1  . MET B  1 271 ? -46.20300 -10.50900 15.81500  1.000 22.73343  ? 271 MET B HE1  1 
ATOM   7448 H  HE2  . MET B  1 271 ? -47.60000 -11.10500 16.28200  1.000 22.73343  ? 271 MET B HE2  1 
ATOM   7449 H  HE3  . MET B  1 271 ? -47.44300 -10.50100 14.82100  1.000 22.73343  ? 271 MET B HE3  1 
ATOM   7450 N  N    . LYS B  1 272 ? -51.24200 -4.62900  16.74900  1.000 15.32951  ? 272 LYS B N    1 
ATOM   7451 C  CA   . LYS B  1 272 ? -51.68300 -3.26700  16.46700  1.000 14.68790  ? 272 LYS B CA   1 
ATOM   7452 C  C    . LYS B  1 272 ? -50.79500 -2.22900  17.14000  1.000 16.52500  ? 272 LYS B C    1 
ATOM   7453 O  O    . LYS B  1 272 ? -50.34000 -1.27700  16.50100  1.000 15.88369  ? 272 LYS B O    1 
ATOM   7454 C  CB   . LYS B  1 272 ? -53.11000 -3.09100  16.95100  1.000 15.60666  ? 272 LYS B CB   1 
ATOM   7455 C  CG   . LYS B  1 272 ? -54.17400 -3.79100  16.15500  1.000 15.70774  ? 272 LYS B CG   1 
ATOM   7456 C  CD   . LYS B  1 272 ? -54.49600 -3.04500  14.89100  1.000 17.09721  ? 272 LYS B CD   1 
ATOM   7457 C  CE   . LYS B  1 272 ? -55.78800 -3.54500  14.27600  1.000 17.23460  ? 272 LYS B CE   1 
ATOM   7458 N  NZ   . LYS B  1 272 ? -56.10800 -2.83300  13.03500  1.000 17.69206  ? 272 LYS B NZ   1 
ATOM   7459 H  H    . LYS B  1 272 ? -51.82100 -5.11800  17.15600  1.000 18.39797  ? 272 LYS B H    1 
ATOM   7460 H  HA   . LYS B  1 272 ? -51.63900 -3.12700  15.50800  1.000 17.62804  ? 272 LYS B HA   1 
ATOM   7461 H  HB2  . LYS B  1 272 ? -53.16400 -3.42900  17.85800  1.000 18.73056  ? 272 LYS B HB2  1 
ATOM   7462 H  HB3  . LYS B  1 272 ? -53.31900 -2.14400  16.93600  1.000 18.73056  ? 272 LYS B HB3  1 
ATOM   7463 H  HG2  . LYS B  1 272 ? -53.86500 -4.67800  15.91500  1.000 18.85185  ? 272 LYS B HG2  1 
ATOM   7464 H  HG3  . LYS B  1 272 ? -54.98300 -3.85400  16.68700  1.000 18.85185  ? 272 LYS B HG3  1 
ATOM   7465 H  HD2  . LYS B  1 272 ? -54.59600 -2.10100  15.09000  1.000 20.51921  ? 272 LYS B HD2  1 
ATOM   7466 H  HD3  . LYS B  1 272 ? -53.78100 -3.17400  14.24800  1.000 20.51921  ? 272 LYS B HD3  1 
ATOM   7467 H  HE2  . LYS B  1 272 ? -55.70100 -4.48900  14.07100  1.000 20.68409  ? 272 LYS B HE2  1 
ATOM   7468 H  HE3  . LYS B  1 272 ? -56.51600 -3.40600  14.90200  1.000 20.68409  ? 272 LYS B HE3  1 
ATOM   7469 H  HZ1  . LYS B  1 272 ? -56.86300 -3.15200  12.68800  1.000 21.23304  ? 272 LYS B HZ1  1 
ATOM   7470 H  HZ2  . LYS B  1 272 ? -56.21000 -1.96500  13.20000  1.000 21.23304  ? 272 LYS B HZ2  1 
ATOM   7471 H  HZ3  . LYS B  1 272 ? -55.45000 -2.94000  12.44500  1.000 21.23304  ? 272 LYS B HZ3  1 
ATOM   7472 N  N    . LEU B  1 273 ? -50.50500 -2.41700  18.42100  1.000 16.31090  ? 273 LEU B N    1 
ATOM   7473 C  CA   . LEU B  1 273 ? -49.72800 -1.42300  19.14400  1.000 17.02009  ? 273 LEU B CA   1 
ATOM   7474 C  C    . LEU B  1 273 ? -48.32200 -1.31500  18.57900  1.000 18.65168  ? 273 LEU B C    1 
ATOM   7475 O  O    . LEU B  1 273 ? -47.80700 -0.21100  18.38000  1.000 20.43410  ? 273 LEU B O    1 
ATOM   7476 C  CB   . LEU B  1 273 ? -49.68100 -1.81000  20.61800  1.000 17.69977  ? 273 LEU B CB   1 
ATOM   7477 C  CG   . LEU B  1 273 ? -48.90300 -0.84900  21.52700  1.000 18.76465  ? 273 LEU B CG   1 
ATOM   7478 C  CD1  . LEU B  1 273 ? -49.50100 0.56900   21.43200  1.000 21.37141  ? 273 LEU B CD1  1 
ATOM   7479 C  CD2  . LEU B  1 273 ? -48.92900 -1.33800  22.97800  1.000 21.74964  ? 273 LEU B CD2  1 
ATOM   7480 H  H    . LEU B  1 273 ? -50.74200 -3.10000  18.88800  1.000 19.57564  ? 273 LEU B H    1 
ATOM   7481 H  HA   . LEU B  1 273 ? -50.14900 -0.55300  19.06000  1.000 20.42667  ? 273 LEU B HA   1 
ATOM   7482 H  HB2  . LEU B  1 273 ? -50.59100 -1.85100  20.95100  1.000 21.24229  ? 273 LEU B HB2  1 
ATOM   7483 H  HB3  . LEU B  1 273 ? -49.26100 -2.68200  20.69100  1.000 21.24229  ? 273 LEU B HB3  1 
ATOM   7484 H  HG   . LEU B  1 273 ? -47.97800 -0.81700  21.23700  1.000 22.52014  ? 273 LEU B HG   1 
ATOM   7485 H  HD11 . LEU B  1 273 ? -49.13500 1.11500   22.14500  1.000 25.64825  ? 273 LEU B HD11 1 
ATOM   7486 H  HD12 . LEU B  1 273 ? -49.27100 0.95200   20.57100  1.000 25.64825  ? 273 LEU B HD12 1 
ATOM   7487 H  HD13 . LEU B  1 273 ? -50.46600 0.51200   21.52200  1.000 25.64825  ? 273 LEU B HD13 1 
ATOM   7488 H  HD21 . LEU B  1 273 ? -48.38200 -0.74800  23.52000  1.000 26.10213  ? 273 LEU B HD21 1 
ATOM   7489 H  HD22 . LEU B  1 273 ? -49.84500 -1.32700  23.29800  1.000 26.10213  ? 273 LEU B HD22 1 
ATOM   7490 H  HD23 . LEU B  1 273 ? -48.57700 -2.24100  23.01300  1.000 26.10213  ? 273 LEU B HD23 1 
ATOM   7491 N  N    . HIS B  1 274 ? -47.70400 -2.43600  18.23600  1.000 15.97745  ? 274 HIS B N    1 
ATOM   7492 C  CA   . HIS B  1 274 ? -46.29000 -2.43000  17.91000  1.000 16.83077  ? 274 HIS B CA   1 
ATOM   7493 C  C    . HIS B  1 274 ? -46.02400 -2.40300  16.42800  1.000 18.10942  ? 274 HIS B C    1 
ATOM   7494 O  O    . HIS B  1 274 ? -45.08100 -1.73800  16.00400  1.000 24.06915  ? 274 HIS B O    1 
ATOM   7495 C  CB   . HIS B  1 274 ? -45.58900 -3.58200  18.58700  1.000 17.39519  ? 274 HIS B CB   1 
ATOM   7496 C  CG   . HIS B  1 274 ? -45.65000 -3.47700  20.07300  1.000 15.54821  ? 274 HIS B CG   1 
ATOM   7497 N  ND1  . HIS B  1 274 ? -45.04800 -2.45400  20.78800  1.000 20.22233  ? 274 HIS B ND1  1 
ATOM   7498 C  CD2  . HIS B  1 274 ? -46.32400 -4.22300  20.98000  1.000 16.96767  ? 274 HIS B CD2  1 
ATOM   7499 C  CE1  . HIS B  1 274 ? -45.30400 -2.61900  22.07500  1.000 18.76306  ? 274 HIS B CE1  1 
ATOM   7500 N  NE2  . HIS B  1 274 ? -46.08000 -3.67800  22.21500  1.000 19.52189  ? 274 HIS B NE2  1 
ATOM   7501 H  H    . HIS B  1 274 ? -48.08200 -3.20700  18.18700  1.000 19.17550  ? 274 HIS B H    1 
ATOM   7502 H  HA   . HIS B  1 274 ? -45.88100 -1.62700  18.26800  1.000 20.19949  ? 274 HIS B HA   1 
ATOM   7503 H  HB2  . HIS B  1 274 ? -46.01400 -4.41300  18.32300  1.000 20.87679  ? 274 HIS B HB2  1 
ATOM   7504 H  HB3  . HIS B  1 274 ? -44.65600 -3.58800  18.32100  1.000 20.87679  ? 274 HIS B HB3  1 
ATOM   7505 H  HD2  . HIS B  1 274 ? -46.85400 -4.96600  20.80000  1.000 20.36377  ? 274 HIS B HD2  1 
ATOM   7506 H  HE1  . HIS B  1 274 ? -44.99100 -2.07900  22.76500  1.000 22.51823  ? 274 HIS B HE1  1 
ATOM   7507 H  HE2  . HIS B  1 274 ? -46.38300 -3.97900  22.96200  1.000 23.42883  ? 274 HIS B HE2  1 
ATOM   7508 N  N    . LEU B  1 275 ? -46.78200 -3.13200  15.61700  1.000 16.27158  ? 275 LEU B N    1 
ATOM   7509 C  CA   . LEU B  1 275 ? -46.57300 -3.05300  14.18000  1.000 16.36969  ? 275 LEU B CA   1 
ATOM   7510 C  C    . LEU B  1 275 ? -47.21800 -1.82800  13.55700  1.000 18.50942  ? 275 LEU B C    1 
ATOM   7511 O  O    . LEU B  1 275 ? -46.66500 -1.29600  12.58600  1.000 18.70272  ? 275 LEU B O    1 
ATOM   7512 C  CB   . LEU B  1 275 ? -47.07900 -4.31200  13.46600  1.000 16.45577  ? 275 LEU B CB   1 
ATOM   7513 C  CG   . LEU B  1 275 ? -46.39600 -5.63000  13.86900  1.000 16.57204  ? 275 LEU B CG   1 
ATOM   7514 C  CD1  . LEU B  1 275 ? -46.99400 -6.77900  13.08400  1.000 18.02921  ? 275 LEU B CD1  1 
ATOM   7515 C  CD2  . LEU B  1 275 ? -44.91500 -5.55300  13.68200  1.000 18.28342  ? 275 LEU B CD2  1 
ATOM   7516 H  H    . LEU B  1 275 ? -47.40700 -3.66600  15.86800  1.000 19.52846  ? 275 LEU B H    1 
ATOM   7517 H  HA   . LEU B  1 275 ? -45.61500 -3.00000  14.03900  1.000 19.64620  ? 275 LEU B HA   1 
ATOM   7518 H  HB2  . LEU B  1 275 ? -48.02500 -4.40900  13.65500  1.000 19.74949  ? 275 LEU B HB2  1 
ATOM   7519 H  HB3  . LEU B  1 275 ? -46.94100 -4.19600  12.51300  1.000 19.74949  ? 275 LEU B HB3  1 
ATOM   7520 H  HG   . LEU B  1 275 ? -46.54800 -5.79500  14.81300  1.000 19.88901  ? 275 LEU B HG   1 
ATOM   7521 H  HD11 . LEU B  1 275 ? -46.62200 -7.61300  13.41100  1.000 21.63762  ? 275 LEU B HD11 1 
ATOM   7522 H  HD12 . LEU B  1 275 ? -47.95700 -6.77700  13.20500  1.000 21.63762  ? 275 LEU B HD12 1 
ATOM   7523 H  HD13 . LEU B  1 275 ? -46.77900 -6.66600  12.14500  1.000 21.63762  ? 275 LEU B HD13 1 
ATOM   7524 H  HD21 . LEU B  1 275 ? -44.53800 -6.44100  13.77900  1.000 21.94267  ? 275 LEU B HD21 1 
ATOM   7525 H  HD22 . LEU B  1 275 ? -44.72700 -5.20900  12.79400  1.000 21.94267  ? 275 LEU B HD22 1 
ATOM   7526 H  HD23 . LEU B  1 275 ? -44.54300 -4.95900  14.35200  1.000 21.94267  ? 275 LEU B HD23 1 
ATOM   7527 N  N    . ASP B  1 276 ? -48.34600 -1.38900  14.08400  1.000 16.34467  ? 276 ASP B N    1 
ATOM   7528 C  CA   . ASP B  1 276 ? -49.04100 -0.21800  13.51000  1.000 15.57930  ? 276 ASP B CA   1 
ATOM   7529 C  C    . ASP B  1 276 ? -48.82800 1.01300   14.38400  1.000 16.62367  ? 276 ASP B C    1 
ATOM   7530 O  O    . ASP B  1 276 ? -49.35000 2.03100   13.99900  1.000 20.31925  ? 276 ASP B O    1 
ATOM   7531 C  CB   . ASP B  1 276 ? -50.54300 -0.45500  13.36700  1.000 16.23286  ? 276 ASP B CB   1 
ATOM   7532 C  CG   . ASP B  1 276 ? -50.95300 -1.58900  12.44700  1.000 16.78275  ? 276 ASP B CG   1 
ATOM   7533 O  OD1  . ASP B  1 276 ? -50.12800 -2.08600  11.72800  1.000 17.30048  ? 276 ASP B OD1  1 
ATOM   7534 O  OD2  . ASP B  1 276 ? -52.10200 -1.94300  12.50300  1.000 18.38361  ? 276 ASP B OD2  1 
ATOM   7535 H  H    . ASP B  1 276 ? -48.75100 -1.76700  14.80700  1.000 19.61616  ? 276 ASP B H    1 
ATOM   7536 H  HA   . ASP B  1 276 ? -48.66500 -0.04000  12.61500  1.000 18.69773  ? 276 ASP B HA   1 
ATOM   7537 H  HB2  . ASP B  1 276 ? -50.91400 -0.64000  14.25500  1.000 19.48199  ? 276 ASP B HB2  1 
ATOM   7538 H  HB3  . ASP B  1 276 ? -50.95700 0.36600   13.03300  1.000 19.48199  ? 276 ASP B HB3  1 
ATOM   7539 N  N    . GLN B  1 277 ? -48.05300 0.93300   15.47200  1.000 17.31000  ? 277 GLN B N    1 
ATOM   7540 C  CA   . GLN B  1 277 ? -47.85200 2.07700   16.37100  1.000 18.35150  ? 277 GLN B CA   1 
ATOM   7541 C  C    . GLN B  1 277 ? -49.20000 2.68600   16.75500  1.000 19.09782  ? 277 GLN B C    1 
ATOM   7542 O  O    . GLN B  1 277 ? -49.33300 3.90100   16.91200  1.000 21.55800  ? 277 GLN B O    1 
ATOM   7543 C  CB   . GLN B  1 277 ? -46.91200 3.09100   15.72800  1.000 22.92360  ? 277 GLN B CB   1 
ATOM   7544 C  CG   . GLN B  1 277 ? -45.51200 2.48500   15.53600  1.000 23.84734  ? 277 GLN B CG   1 
ATOM   7545 C  CD   . GLN B  1 277 ? -44.88700 2.11000   16.88500  1.000 45.51898  ? 277 GLN B CD   1 
ATOM   7546 O  OE1  . GLN B  1 277 ? -44.93900 2.89700   17.83500  1.000 46.32296  ? 277 GLN B OE1  1 
ATOM   7547 N  NE2  . GLN B  1 277 ? -44.33400 0.90200   16.98400  1.000 40.09302  ? 277 GLN B NE2  1 
ATOM   7548 H  H    . GLN B  1 277 ? -47.64400 0.21700   15.71600  1.000 20.77456  ? 277 GLN B H    1 
ATOM   7549 H  HA   . GLN B  1 277 ? -47.43300 1.78600   17.19600  1.000 22.02436  ? 277 GLN B HA   1 
ATOM   7550 H  HB2  . GLN B  1 277 ? -47.25900 3.34900   14.86000  1.000 27.51088  ? 277 GLN B HB2  1 
ATOM   7551 H  HB3  . GLN B  1 277 ? -46.83600 3.87000   16.30100  1.000 27.51088  ? 277 GLN B HB3  1 
ATOM   7552 H  HG2  . GLN B  1 277 ? -45.57900 1.68300   14.99500  1.000 28.61936  ? 277 GLN B HG2  1 
ATOM   7553 H  HG3  . GLN B  1 277 ? -44.93700 3.13300   15.10000  1.000 28.61936  ? 277 GLN B HG3  1 
ATOM   7554 H  HE21 . GLN B  1 277 ? -44.33900 0.37100   16.30800  1.000 48.11419  ? 277 GLN B HE21 1 
ATOM   7555 H  HE22 . GLN B  1 277 ? -43.97300 0.65400   17.72400  1.000 48.11419  ? 277 GLN B HE22 1 
ATOM   7556 N  N    . ASP B  1 278 ? -50.18700 1.83000   16.94400  1.000 17.41060  ? 278 ASP B N    1 
ATOM   7557 C  CA   . ASP B  1 278 ? -51.58500 2.25800   17.12000  1.000 17.94587  ? 278 ASP B CA   1 
ATOM   7558 C  C    . ASP B  1 278 ? -51.91200 2.30500   18.60700  1.000 17.71044  ? 278 ASP B C    1 
ATOM   7559 O  O    . ASP B  1 278 ? -52.25900 1.28900   19.22500  1.000 18.22302  ? 278 ASP B O    1 
ATOM   7560 C  CB   . ASP B  1 278 ? -52.49700 1.31500   16.35100  1.000 17.88269  ? 278 ASP B CB   1 
ATOM   7561 C  CG   . ASP B  1 278 ? -53.94200 1.74800   16.32600  1.000 18.30232  ? 278 ASP B CG   1 
ATOM   7562 O  OD1  . ASP B  1 278 ? -54.33700 2.68100   17.06700  1.000 18.63196  ? 278 ASP B OD1  1 
ATOM   7563 O  OD2  . ASP B  1 278 ? -54.68500 1.13700   15.53000  1.000 18.01010  ? 278 ASP B OD2  1 
ATOM   7564 H  H    . ASP B  1 278 ? -50.08200 0.97700   16.97500  1.000 20.89528  ? 278 ASP B H    1 
ATOM   7565 H  HA   . ASP B  1 278 ? -51.70000 3.16100   16.78500  1.000 21.53760  ? 278 ASP B HA   1 
ATOM   7566 H  HB2  . ASP B  1 278 ? -52.18900 1.26200   15.43300  1.000 21.46179  ? 278 ASP B HB2  1 
ATOM   7567 H  HB3  . ASP B  1 278 ? -52.45900 0.43800   16.76400  1.000 21.46179  ? 278 ASP B HB3  1 
ATOM   7568 N  N    . GLN B  1 279 ? -51.82500 3.51100   19.16800  1.000 19.60850  ? 279 GLN B N    1 
ATOM   7569 C  CA   . GLN B  1 279 ? -51.99100 3.69200   20.59400  1.000 21.96877  ? 279 GLN B CA   1 
ATOM   7570 C  C    . GLN B  1 279 ? -53.41600 3.42000   21.05800  1.000 18.67730  ? 279 GLN B C    1 
ATOM   7571 O  O    . GLN B  1 279 ? -53.63300 3.28800   22.27400  1.000 21.05305  ? 279 GLN B O    1 
ATOM   7572 C  CB   . GLN B  1 279 ? -51.56000 5.11600   20.98100  1.000 24.69052  ? 279 GLN B CB   1 
ATOM   7573 C  CG   . GLN B  1 279 ? -50.05100 5.31400   20.84700  1.000 27.23389  ? 279 GLN B CG   1 
ATOM   7574 C  CD   . GLN B  1 279 ? -49.24800 4.40500   21.75600  1.000 32.15922  ? 279 GLN B CD   1 
ATOM   7575 O  OE1  . GLN B  1 279 ? -49.65600 4.09800   22.89100  1.000 33.32514  ? 279 GLN B OE1  1 
ATOM   7576 N  NE2  . GLN B  1 279 ? -48.09500 3.95200   21.26400  1.000 46.14519  ? 279 GLN B NE2  1 
ATOM   7577 H  H    . GLN B  1 279 ? -51.67000 4.23900   18.73700  1.000 23.53276  ? 279 GLN B H    1 
ATOM   7578 H  HA   . GLN B  1 279 ? -51.41500 3.07000   21.06600  1.000 26.36509  ? 279 GLN B HA   1 
ATOM   7579 H  HB2  . GLN B  1 279 ? -52.00200 5.75200   20.39700  1.000 29.63118  ? 279 GLN B HB2  1 
ATOM   7580 H  HB3  . GLN B  1 279 ? -51.80700 5.28400   21.90300  1.000 29.63118  ? 279 GLN B HB3  1 
ATOM   7581 H  HG2  . GLN B  1 279 ? -49.78900 5.12700   19.93200  1.000 32.68323  ? 279 GLN B HG2  1 
ATOM   7582 H  HG3  . GLN B  1 279 ? -49.83300 6.23100   21.07400  1.000 32.68323  ? 279 GLN B HG3  1 
ATOM   7583 H  HE21 . GLN B  1 279 ? -47.84700 4.17900   20.47300  1.000 55.37679  ? 279 GLN B HE21 1 
ATOM   7584 H  HE22 . GLN B  1 279 ? -47.60000 3.43300   21.73800  1.000 55.37679  ? 279 GLN B HE22 1 
ATOM   7585 N  N    . ARG B  1 280 ? -54.38600 3.33800   20.13900  1.000 18.14977  ? 280 ARG B N    1 
ATOM   7586 C  CA   . ARG B  1 280 ? -55.73400 2.96800   20.57000  1.000 18.88394  ? 280 ARG B CA   1 
ATOM   7587 C  C    . ARG B  1 280 ? -55.74900 1.59700   21.22300  1.000 18.39333  ? 280 ARG B C    1 
ATOM   7588 O  O    . ARG B  1 280 ? -56.67700 1.29800   21.98700  1.000 19.98809  ? 280 ARG B O    1 
ATOM   7589 C  CB   . ARG B  1 280 ? -56.66400 2.92400   19.36300  1.000 19.00167  ? 280 ARG B CB   1 
ATOM   7590 C  CG   . ARG B  1 280 ? -56.79100 4.26300   18.64200  1.000 18.75981  ? 280 ARG B CG   1 
ATOM   7591 C  CD   . ARG B  1 280 ? -57.69600 4.18700   17.43000  1.000 19.93181  ? 280 ARG B CD   1 
ATOM   7592 N  NE   . ARG B  1 280 ? -57.15900 3.26100   16.45900  1.000 18.08480  ? 280 ARG B NE   1 
ATOM   7593 C  CZ   . ARG B  1 280 ? -57.76700 2.83500   15.36800  1.000 17.09531  ? 280 ARG B CZ   1 
ATOM   7594 N  NH1  . ARG B  1 280 ? -58.99600 3.22100   15.07900  1.000 18.30815  ? 280 ARG B NH1  1 
ATOM   7595 N  NH2  . ARG B  1 280 ? -57.15000 1.99400   14.56800  1.000 18.69560  ? 280 ARG B NH2  1 
ATOM   7596 H  H    . ARG B  1 280 ? -54.29200 3.48500   19.29700  1.000 21.78229  ? 280 ARG B H    1 
ATOM   7597 H  HA   . ARG B  1 280 ? -56.05400 3.63200   21.19900  1.000 22.66329  ? 280 ARG B HA   1 
ATOM   7598 H  HB2  . ARG B  1 280 ? -56.32200 2.27600   18.72800  1.000 22.80456  ? 280 ARG B HB2  1 
ATOM   7599 H  HB3  . ARG B  1 280 ? -57.55000 2.66200   19.66000  1.000 22.80456  ? 280 ARG B HB3  1 
ATOM   7600 H  HG2  . ARG B  1 280 ? -57.16200 4.91800   19.25300  1.000 22.51433  ? 280 ARG B HG2  1 
ATOM   7601 H  HG3  . ARG B  1 280 ? -55.91300 4.54700   18.34400  1.000 22.51433  ? 280 ARG B HG3  1 
ATOM   7602 H  HD2  . ARG B  1 280 ? -58.57600 3.87900   17.69900  1.000 23.92074  ? 280 ARG B HD2  1 
ATOM   7603 H  HD3  . ARG B  1 280 ? -57.76300 5.06300   17.01900  1.000 23.92074  ? 280 ARG B HD3  1 
ATOM   7604 H  HE   . ARG B  1 280 ? -56.36800 2.95800   16.60600  1.000 21.70432  ? 280 ARG B HE   1 
ATOM   7605 H  HH11 . ARG B  1 280 ? -59.41400 3.75800   15.60500  1.000 21.97234  ? 280 ARG B HH11 1 
ATOM   7606 H  HH12 . ARG B  1 280 ? -59.38000 2.93500   14.36400  1.000 21.97234  ? 280 ARG B HH12 1 
ATOM   7607 H  HH21 . ARG B  1 280 ? -56.35500 1.72500   14.75700  1.000 22.43728  ? 280 ARG B HH21 1 
ATOM   7608 H  HH22 . ARG B  1 280 ? -57.54100 1.71200   13.85600  1.000 22.43728  ? 280 ARG B HH22 1 
ATOM   7609 N  N    . TYR B  1 281 ? -54.73900 0.76900   20.96100  1.000 17.10684  ? 281 TYR B N    1 
ATOM   7610 C  CA   . TYR B  1 281 ? -54.70500 -0.58500  21.50500  1.000 18.67194  ? 281 TYR B CA   1 
ATOM   7611 C  C    . TYR B  1 281 ? -53.91600 -0.68600  22.80000  1.000 19.08009  ? 281 TYR B C    1 
ATOM   7612 O  O    . TYR B  1 281 ? -53.98400 -1.72600  23.45700  1.000 19.01860  ? 281 TYR B O    1 
ATOM   7613 C  CB   . TYR B  1 281 ? -54.20000 -1.53900  20.41700  1.000 16.73990  ? 281 TYR B CB   1 
ATOM   7614 C  CG   . TYR B  1 281 ? -55.25800 -1.78200  19.37900  1.000 16.76654  ? 281 TYR B CG   1 
ATOM   7615 C  CD1  . TYR B  1 281 ? -55.42600 -0.91200  18.27800  1.000 15.84835  ? 281 TYR B CD1  1 
ATOM   7616 C  CD2  . TYR B  1 281 ? -56.15500 -2.83300  19.50300  1.000 15.65229  ? 281 TYR B CD2  1 
ATOM   7617 C  CE1  . TYR B  1 281 ? -56.42700 -1.10300  17.34800  1.000 16.75448  ? 281 TYR B CE1  1 
ATOM   7618 C  CE2  . TYR B  1 281 ? -57.15000 -3.04400  18.57000  1.000 16.81922  ? 281 TYR B CE2  1 
ATOM   7619 C  CZ   . TYR B  1 281 ? -57.29500 -2.18600  17.49100  1.000 16.10432  ? 281 TYR B CZ   1 
ATOM   7620 O  OH   . TYR B  1 281 ? -58.32800 -2.40800  16.59200  1.000 18.27976  ? 281 TYR B OH   1 
ATOM   7621 H  H    . TYR B  1 281 ? -54.06200 0.96900   20.47000  1.000 20.53077  ? 281 TYR B H    1 
ATOM   7622 H  HA   . TYR B  1 281 ? -55.59700 -0.88800  21.73800  1.000 22.40889  ? 281 TYR B HA   1 
ATOM   7623 H  HB2  . TYR B  1 281 ? -53.42600 -1.14900  19.98100  1.000 20.09044  ? 281 TYR B HB2  1 
ATOM   7624 H  HB3  . TYR B  1 281 ? -53.96200 -2.38900  20.81800  1.000 20.09044  ? 281 TYR B HB3  1 
ATOM   7625 H  HD1  . TYR B  1 281 ? -54.84600 -0.19200  18.17700  1.000 19.02058  ? 281 TYR B HD1  1 
ATOM   7626 H  HD2  . TYR B  1 281 ? -56.08400 -3.40800  20.23000  1.000 18.78531  ? 281 TYR B HD2  1 
ATOM   7627 H  HE1  . TYR B  1 281 ? -56.52300 -0.51600  16.63300  1.000 20.10793  ? 281 TYR B HE1  1 
ATOM   7628 H  HE2  . TYR B  1 281 ? -57.72700 -3.76700  18.66500  1.000 20.18563  ? 281 TYR B HE2  1 
ATOM   7629 H  HH   . TYR B  1 281 ? -58.35800 -1.78500  16.03000  1.000 21.93827  ? 281 TYR B HH   1 
ATOM   7630 N  N    . ALA B  1 282 ? -53.21900 0.36600   23.20800  1.000 18.86801  ? 282 ALA B N    1 
ATOM   7631 C  CA   . ALA B  1 282 ? -52.44800 0.28700   24.43900  1.000 19.18477  ? 282 ALA B CA   1 
ATOM   7632 C  C    . ALA B  1 282 ? -53.31000 0.01300   25.66900  1.000 19.34490  ? 282 ALA B C    1 
ATOM   7633 O  O    . ALA B  1 282 ? -52.86500 -0.76300  26.53900  1.000 19.74439  ? 282 ALA B O    1 
ATOM   7634 C  CB   . ALA B  1 282 ? -51.63800 1.57200   24.62400  1.000 22.05379  ? 282 ALA B CB   1 
ATOM   7635 H  H    . ALA B  1 282 ? -53.17600 1.12100   22.79900  1.000 22.64417  ? 282 ALA B H    1 
ATOM   7636 H  HA   . ALA B  1 282 ? -51.82700 -0.45300  24.34800  1.000 23.02429  ? 282 ALA B HA   1 
ATOM   7637 H  HB1  . ALA B  1 282 ? -51.09500 1.49100   25.42400  1.000 26.46711  ? 282 ALA B HB1  1 
ATOM   7638 H  HB2  . ALA B  1 282 ? -51.06900 1.70200   23.84900  1.000 26.46711  ? 282 ALA B HB2  1 
ATOM   7639 H  HB3  . ALA B  1 282 ? -52.24900 2.32000   24.71400  1.000 26.46711  ? 282 ALA B HB3  1 
ATOM   7640 N  N    . PRO B  1 283 ? -54.52300 0.55300   25.80100  1.000 20.55798  ? 283 PRO B N    1 
ATOM   7641 C  CA   . PRO B  1 283 ? -55.28100 0.32800   27.04600  1.000 20.27983  ? 283 PRO B CA   1 
ATOM   7642 C  C    . PRO B  1 283 ? -55.70700 -1.10200  27.27500  1.000 21.74966  ? 283 PRO B C    1 
ATOM   7643 O  O    . PRO B  1 283 ? -56.06400 -1.45400  28.40400  1.000 22.80793  ? 283 PRO B O    1 
ATOM   7644 C  CB   . PRO B  1 283 ? -56.49900 1.24500   26.88800  1.000 23.87426  ? 283 PRO B CB   1 
ATOM   7645 C  CG   . PRO B  1 283 ? -56.09600 2.30000   25.92500  1.000 26.59236  ? 283 PRO B CG   1 
ATOM   7646 C  CD   . PRO B  1 283 ? -55.12000 1.61700   24.97000  1.000 21.45920  ? 283 PRO B CD   1 
ATOM   7647 H  HA   . PRO B  1 283 ? -54.74600 0.61800   27.80100  1.000 24.33836  ? 283 PRO B HA   1 
ATOM   7648 H  HB2  . PRO B  1 283 ? -57.24900 0.73500   26.54300  1.000 28.65167  ? 283 PRO B HB2  1 
ATOM   7649 H  HB3  . PRO B  1 283 ? -56.72800 1.63400   27.74600  1.000 28.65167  ? 283 PRO B HB3  1 
ATOM   7650 H  HG2  . PRO B  1 283 ? -56.87500 2.62700   25.44900  1.000 31.91339  ? 283 PRO B HG2  1 
ATOM   7651 H  HG3  . PRO B  1 283 ? -55.66500 3.03000   26.39700  1.000 31.91339  ? 283 PRO B HG3  1 
ATOM   7652 H  HD2  . PRO B  1 283 ? -55.58900 1.23900   24.21000  1.000 25.75360  ? 283 PRO B HD2  1 
ATOM   7653 H  HD3  . PRO B  1 283 ? -54.44200 2.24000   24.66600  1.000 25.75360  ? 283 PRO B HD3  1 
ATOM   7654 N  N    . PHE B  1 284 ? -55.69400 -1.95700  26.26400  1.000 19.17347  ? 284 PHE B N    1 
ATOM   7655 C  CA   . PHE B  1 284 ? -56.02500 -3.35900  26.45300  1.000 20.43952  ? 284 PHE B CA   1 
ATOM   7656 C  C    . PHE B  1 284 ? -54.86700 -4.11700  27.04800  1.000 19.89585  ? 284 PHE B C    1 
ATOM   7657 O  O    . PHE B  1 284 ? -55.07100 -5.22300  27.53900  1.000 22.10388  ? 284 PHE B O    1 
ATOM   7658 C  CB   . PHE B  1 284 ? -56.48500 -3.97900  25.11300  1.000 21.00115  ? 284 PHE B CB   1 
ATOM   7659 C  CG   . PHE B  1 284 ? -57.64600 -3.25900  24.52200  1.000 20.24907  ? 284 PHE B CG   1 
ATOM   7660 C  CD1  . PHE B  1 284 ? -58.92200 -3.44400  24.98400  1.000 22.95228  ? 284 PHE B CD1  1 
ATOM   7661 C  CD2  . PHE B  1 284 ? -57.42800 -2.33800  23.51900  1.000 23.01579  ? 284 PHE B CD2  1 
ATOM   7662 C  CE1  . PHE B  1 284 ? -59.95600 -2.72900  24.47400  1.000 23.99503  ? 284 PHE B CE1  1 
ATOM   7663 C  CE2  . PHE B  1 284 ? -58.46800 -1.63300  22.98700  1.000 23.14920  ? 284 PHE B CE2  1 
ATOM   7664 C  CZ   . PHE B  1 284 ? -59.73000 -1.81200  23.48100  1.000 24.41157  ? 284 PHE B CZ   1 
ATOM   7665 H  H    . PHE B  1 284 ? -55.49500 -1.75000  25.45400  1.000 23.01072  ? 284 PHE B H    1 
ATOM   7666 H  HA   . PHE B  1 284 ? -56.77500 -3.45000  27.06100  1.000 24.52998  ? 284 PHE B HA   1 
ATOM   7667 H  HB2  . PHE B  1 284 ? -55.75200 -3.94200  24.47800  1.000 25.20394  ? 284 PHE B HB2  1 
ATOM   7668 H  HB3  . PHE B  1 284 ? -56.74700 -4.90100  25.26300  1.000 25.20394  ? 284 PHE B HB3  1 
ATOM   7669 H  HD1  . PHE B  1 284 ? -59.08200 -4.06800  25.65500  1.000 27.54530  ? 284 PHE B HD1  1 
ATOM   7670 H  HD2  . PHE B  1 284 ? -56.56500 -2.19700  23.20200  1.000 27.62151  ? 284 PHE B HD2  1 
ATOM   7671 H  HE1  . PHE B  1 284 ? -60.81700 -2.86100  24.79900  1.000 28.79659  ? 284 PHE B HE1  1 
ATOM   7672 H  HE2  . PHE B  1 284 ? -58.31900 -1.03300  22.29300  1.000 27.78160  ? 284 PHE B HE2  1 
ATOM   7673 H  HZ   . PHE B  1 284 ? -60.43600 -1.31100  23.14200  1.000 29.29645  ? 284 PHE B HZ   1 
ATOM   7674 N  N    . LEU B  1 285 ? -53.68400 -3.55000  26.97900  1.000 19.17747  ? 285 LEU B N    1 
ATOM   7675 C  CA   . LEU B  1 285 ? -52.46900 -4.20800  27.42000  1.000 19.52693  ? 285 LEU B CA   1 
ATOM   7676 C  C    . LEU B  1 285 ? -51.90600 -3.61600  28.69500  1.000 19.49335  ? 285 LEU B C    1 
ATOM   7677 O  O    . LEU B  1 285 ? -51.44600 -4.36800  29.55600  1.000 21.93764  ? 285 LEU B O    1 
ATOM   7678 C  CB   . LEU B  1 285 ? -51.43400 -4.11600  26.30000  1.000 19.80982  ? 285 LEU B CB   1 
ATOM   7679 C  CG   . LEU B  1 285 ? -51.79100 -4.94900  25.04800  1.000 20.00258  ? 285 LEU B CG   1 
ATOM   7680 C  CD1  . LEU B  1 285 ? -51.02000 -4.39700  23.87500  1.000 21.11051  ? 285 LEU B CD1  1 
ATOM   7681 C  CD2  . LEU B  1 285 ? -51.54500 -6.41000  25.32600  1.000 22.33313  ? 285 LEU B CD2  1 
ATOM   7682 H  H    . LEU B  1 285 ? -53.55200 -2.75800  26.67100  1.000 23.01552  ? 285 LEU B H    1 
ATOM   7683 H  HA   . LEU B  1 285 ? -52.64000 -5.14600  27.59900  1.000 23.43488  ? 285 LEU B HA   1 
ATOM   7684 H  HB2  . LEU B  1 285 ? -51.35400 -3.18900  26.02600  1.000 23.77434  ? 285 LEU B HB2  1 
ATOM   7685 H  HB3  . LEU B  1 285 ? -50.58300 -4.43700  26.63700  1.000 23.77434  ? 285 LEU B HB3  1 
ATOM   7686 H  HG   . LEU B  1 285 ? -52.73100 -4.88800  24.81600  1.000 24.00566  ? 285 LEU B HG   1 
ATOM   7687 H  HD11 . LEU B  1 285 ? -51.16300 -4.97000  23.10500  1.000 25.33517  ? 285 LEU B HD11 1 
ATOM   7688 H  HD12 . LEU B  1 285 ? -51.33500 -3.50000  23.68300  1.000 25.33517  ? 285 LEU B HD12 1 
ATOM   7689 H  HD13 . LEU B  1 285 ? -50.07600 -4.37500  24.09900  1.000 25.33517  ? 285 LEU B HD13 1 
ATOM   7690 H  HD21 . LEU B  1 285 ? -51.70800 -6.91700  24.51500  1.000 26.80232  ? 285 LEU B HD21 1 
ATOM   7691 H  HD22 . LEU B  1 285 ? -50.62500 -6.52700  25.61000  1.000 26.80232  ? 285 LEU B HD22 1 
ATOM   7692 H  HD23 . LEU B  1 285 ? -52.14800 -6.70400  26.02600  1.000 26.80232  ? 285 LEU B HD23 1 
ATOM   7693 N  N    . CYS B  1 286 ? -51.91400 -2.29200  28.82700  1.000 20.75100  ? 286 CYS B N    1 
ATOM   7694 C  CA   . CYS B  1 286 ? -51.35600 -1.60100  29.97700  1.000 21.89771  ? 286 CYS B CA   1 
ATOM   7695 C  C    . CYS B  1 286 ? -52.47000 -0.85600  30.68600  1.000 23.26750  ? 286 CYS B C    1 
ATOM   7696 O  O    . CYS B  1 286 ? -53.10400 0.04100   30.09700  1.000 24.26747  ? 286 CYS B O    1 
ATOM   7697 C  CB   . CYS B  1 286 ? -50.25700 -0.64100  29.54600  1.000 24.57939  ? 286 CYS B CB   1 
ATOM   7698 S  SG   . CYS B  1 286 ? -48.78100 -1.48700  28.86200  1.000 27.73299  ? 286 CYS B SG   1 
ATOM   7699 H  H    . CYS B  1 286 ? -52.25000 -1.75800  28.24200  1.000 24.90377  ? 286 CYS B H    1 
ATOM   7700 H  HA   . CYS B  1 286 ? -50.97900 -2.24500  30.59700  1.000 26.27981  ? 286 CYS B HA   1 
ATOM   7701 H  HB2  . CYS B  1 286 ? -50.60800 -0.05200  28.85900  1.000 29.49783  ? 286 CYS B HB2  1 
ATOM   7702 H  HB3  . CYS B  1 286 ? -49.97400 -0.12300  30.31500  1.000 29.49783  ? 286 CYS B HB3  1 
ATOM   7703 N  N    . GLY B  1 287 ? -52.71500 -1.23600  31.93800  1.000 22.59886  ? 287 GLY B N    1 
ATOM   7704 C  CA   . GLY B  1 287 ? -53.80300 -0.66500  32.69700  1.000 24.00483  ? 287 GLY B CA   1 
ATOM   7705 C  C    . GLY B  1 287 ? -54.64400 -1.70600  33.40100  1.000 28.67241  ? 287 GLY B C    1 
ATOM   7706 O  O    . GLY B  1 287 ? -54.89300 -1.62300  34.60200  1.000 28.62378  ? 287 GLY B O    1 
ATOM   7707 H  H    . GLY B  1 287 ? -52.25800 -1.82600  32.36500  1.000 27.12119  ? 287 GLY B H    1 
ATOM   7708 H  HA2  . GLY B  1 287 ? -53.44300 -0.06300  33.36600  1.000 28.80835  ? 287 GLY B HA2  1 
ATOM   7709 H  HA3  . GLY B  1 287 ? -54.37900 -0.16300  32.09900  1.000 28.80835  ? 287 GLY B HA3  1 
ATOM   7710 N  N    . PRO B  1 288 ? -55.13000 -2.69800  32.66700  1.000 24.80831  ? 288 PRO B N    1 
ATOM   7711 C  CA   . PRO B  1 288 ? -56.04000 -3.67400  33.27900  1.000 26.04863  ? 288 PRO B CA   1 
ATOM   7712 C  C    . PRO B  1 288 ? -55.35000 -4.57400  34.28500  1.000 24.74597  ? 288 PRO B C    1 
ATOM   7713 O  O    . PRO B  1 288 ? -54.15600 -4.84500  34.21200  1.000 24.93473  ? 288 PRO B O    1 
ATOM   7714 C  CB   . PRO B  1 288 ? -56.56000 -4.48600  32.08300  1.000 25.72247  ? 288 PRO B CB   1 
ATOM   7715 C  CG   . PRO B  1 288 ? -56.35000 -3.58100  30.90100  1.000 22.77792  ? 288 PRO B CG   1 
ATOM   7716 C  CD   . PRO B  1 288 ? -55.04900 -2.86200  31.20300  1.000 23.25803  ? 288 PRO B CD   1 
ATOM   7717 H  HA   . PRO B  1 288 ? -56.77200 -3.21100  33.71500  1.000 31.26092  ? 288 PRO B HA   1 
ATOM   7718 H  HB2  . PRO B  1 288 ? -56.05000 -5.30700  31.99000  1.000 30.86953  ? 288 PRO B HB2  1 
ATOM   7719 H  HB3  . PRO B  1 288 ? -57.50000 -4.69200  32.20300  1.000 30.86953  ? 288 PRO B HB3  1 
ATOM   7720 H  HG2  . PRO B  1 288 ? -56.27800 -4.10500  30.08900  1.000 27.33607  ? 288 PRO B HG2  1 
ATOM   7721 H  HG3  . PRO B  1 288 ? -57.08600 -2.95400  30.82800  1.000 27.33607  ? 288 PRO B HG3  1 
ATOM   7722 H  HD2  . PRO B  1 288 ? -54.28300 -3.40200  30.95200  1.000 27.91219  ? 288 PRO B HD2  1 
ATOM   7723 H  HD3  . PRO B  1 288 ? -55.01000 -2.00300  30.75500  1.000 27.91219  ? 288 PRO B HD3  1 
ATOM   7724 N  N    . ASN B  1 289 ? -56.14100 -5.07400  35.23500  1.000 24.72935  ? 289 ASN B N    1 
ATOM   7725 C  CA   . ASN B  1 289 ? -55.68700 -6.14000  36.12100  1.000 23.69991  ? 289 ASN B CA   1 
ATOM   7726 C  C    . ASN B  1 289 ? -56.04500 -7.47200  35.45500  1.000 25.43757  ? 289 ASN B C    1 
ATOM   7727 O  O    . ASN B  1 289 ? -57.06400 -8.11400  35.74700  1.000 25.24315  ? 289 ASN B O    1 
ATOM   7728 C  CB   . ASN B  1 289 ? -56.34600 -6.01000  37.49200  1.000 25.84305  ? 289 ASN B CB   1 
ATOM   7729 C  CG   . ASN B  1 289 ? -55.65700 -4.96800  38.40400  1.000 33.18726  ? 289 ASN B CG   1 
ATOM   7730 O  OD1  . ASN B  1 289 ? -56.00600 -3.79400  38.38800  1.000 55.18702  ? 289 ASN B OD1  1 
ATOM   7731 N  ND2  . ASN B  1 289 ? -54.70400 -5.41500  39.19600  1.000 42.96613  ? 289 ASN B ND2  1 
ATOM   7732 H  H    . ASN B  1 289 ? -56.94600 -4.81100  35.38500  1.000 29.67778  ? 289 ASN B H    1 
ATOM   7733 H  HA   . ASN B  1 289 ? -54.72600 -6.08500  36.23600  1.000 28.44245  ? 289 ASN B HA   1 
ATOM   7734 H  HB2  . ASN B  1 289 ? -57.26900 -5.73700  37.37300  1.000 31.01422  ? 289 ASN B HB2  1 
ATOM   7735 H  HB3  . ASN B  1 289 ? -56.30900 -6.86900  37.94100  1.000 31.01422  ? 289 ASN B HB3  1 
ATOM   7736 H  HD21 . ASN B  1 289 ? -54.49400 -6.24900  39.18700  1.000 51.56192  ? 289 ASN B HD21 1 
ATOM   7737 H  HD22 . ASN B  1 289 ? -54.29200 -4.87300  39.72100  1.000 51.56192  ? 289 ASN B HD22 1 
ATOM   7738 N  N    . HIS B  1 290 ? -55.14000 -7.90400  34.57400  1.000 22.69090  ? 290 HIS B N    1 
ATOM   7739 C  CA   . HIS B  1 290 ? -55.40500 -9.05900  33.71500  1.000 22.07767  ? 290 HIS B CA   1 
ATOM   7740 C  C    . HIS B  1 290 ? -55.66800 -10.34300 34.49100  1.000 22.97872  ? 290 HIS B C    1 
ATOM   7741 O  O    . HIS B  1 290 ? -56.44000 -11.18400 34.02200  1.000 23.16486  ? 290 HIS B O    1 
ATOM   7742 C  CB   . HIS B  1 290 ? -54.25100 -9.29700  32.75300  1.000 21.52075  ? 290 HIS B CB   1 
ATOM   7743 C  CG   . HIS B  1 290 ? -53.92100 -8.10900  31.91300  1.000 20.73747  ? 290 HIS B CG   1 
ATOM   7744 N  ND1  . HIS B  1 290 ? -54.65000 -7.75700  30.79000  1.000 21.44905  ? 290 HIS B ND1  1 
ATOM   7745 C  CD2  . HIS B  1 290 ? -52.93700 -7.18700  32.03700  1.000 21.13361  ? 290 HIS B CD2  1 
ATOM   7746 C  CE1  . HIS B  1 290 ? -54.12600 -6.66100  30.26900  1.000 20.49490  ? 290 HIS B CE1  1 
ATOM   7747 N  NE2  . HIS B  1 290 ? -53.08700 -6.29900  31.00200  1.000 19.98461  ? 290 HIS B NE2  1 
ATOM   7748 H  H    . HIS B  1 290 ? -54.36700 -7.54700  34.45300  1.000 27.23164  ? 290 HIS B H    1 
ATOM   7749 H  HA   . HIS B  1 290 ? -56.20400 -8.84400  33.20800  1.000 26.49577  ? 290 HIS B HA   1 
ATOM   7750 H  HB2  . HIS B  1 290 ? -53.46000 -9.52800  33.26400  1.000 25.82746  ? 290 HIS B HB2  1 
ATOM   7751 H  HB3  . HIS B  1 290 ? -54.48600 -10.02500 32.15700  1.000 25.82746  ? 290 HIS B HB3  1 
ATOM   7752 H  HD2  . HIS B  1 290 ? -52.28400 -7.16100  32.69900  1.000 25.36290  ? 290 HIS B HD2  1 
ATOM   7753 H  HE1  . HIS B  1 290 ? -54.43800 -6.21800  29.51300  1.000 24.59644  ? 290 HIS B HE1  1 
ATOM   7754 H  HE2  . HIS B  1 290 ? -52.58500 -5.61700  30.85300  1.000 23.98410  ? 290 HIS B HE2  1 
ATOM   7755 N  N    . GLU B  1 291 ? -55.09900 -10.49500 35.69700  1.000 24.59674  ? 291 GLU B N    1 
ATOM   7756 C  CA   . GLU B  1 291 ? -55.29300 -11.72800 36.44400  1.000 23.60810  ? 291 GLU B CA   1 
ATOM   7757 C  C    . GLU B  1 291 ? -56.71600 -11.88100 36.97000  1.000 25.71129  ? 291 GLU B C    1 
ATOM   7758 O  O    . GLU B  1 291 ? -57.07700 -12.96900 37.42700  1.000 29.39831  ? 291 GLU B O    1 
ATOM   7759 C  CB   . GLU B  1 291 ? -54.27200 -11.83600 37.58600  1.000 25.54087  ? 291 GLU B CB   1 
ATOM   7760 C  CG   . GLU B  1 291 ? -52.82800 -12.02500 37.06600  1.000 22.93383  ? 291 GLU B CG   1 
ATOM   7761 C  CD   . GLU B  1 291 ? -51.77600 -11.94000 38.15400  1.000 28.93090  ? 291 GLU B CD   1 
ATOM   7762 O  OE1  . GLU B  1 291 ? -52.14700 -11.64400 39.31500  1.000 28.86027  ? 291 GLU B OE1  1 
ATOM   7763 O  OE2  . GLU B  1 291 ? -50.58100 -12.14200 37.84500  1.000 26.89419  ? 291 GLU B OE2  1 
ATOM   7764 H  H    . GLU B  1 291 ? -54.60800 -9.90700  36.08800  1.000 29.51865  ? 291 GLU B H    1 
ATOM   7765 H  HA   . GLU B  1 291 ? -55.12500 -12.47800 35.85100  1.000 28.33228  ? 291 GLU B HA   1 
ATOM   7766 H  HB2  . GLU B  1 291 ? -54.29900 -11.02200 38.11400  1.000 30.65160  ? 291 GLU B HB2  1 
ATOM   7767 H  HB3  . GLU B  1 291 ? -54.49600 -12.59900 38.14200  1.000 30.65160  ? 291 GLU B HB3  1 
ATOM   7768 H  HG2  . GLU B  1 291 ? -52.75700 -12.89900 36.65200  1.000 27.52316  ? 291 GLU B HG2  1 
ATOM   7769 H  HG3  . GLU B  1 291 ? -52.63700 -11.33300 36.41400  1.000 27.52316  ? 291 GLU B HG3  1 
ATOM   7770 N  N    . ARG B  1 292 ? -57.54100 -10.83200 36.90900  1.000 24.36692  ? 292 ARG B N    1 
ATOM   7771 C  CA   . ARG B  1 292 ? -58.95200 -11.00300 37.23300  1.000 26.31747  ? 292 ARG B CA   1 
ATOM   7772 C  C    . ARG B  1 292 ? -59.65000 -11.93100 36.25500  1.000 29.28948  ? 292 ARG B C    1 
ATOM   7773 O  O    . ARG B  1 292 ? -60.67000 -12.54200 36.61500  1.000 35.30912  ? 292 ARG B O    1 
ATOM   7774 C  CB   . ARG B  1 292 ? -59.67600 -9.66300  37.23300  1.000 29.62148  ? 292 ARG B CB   1 
ATOM   7775 C  CG   . ARG B  1 292 ? -59.33700 -8.80000  38.38700  1.000 27.92827  ? 292 ARG B CG   1 
ATOM   7776 C  CD   . ARG B  1 292 ? -60.14000 -7.52000  38.39300  1.000 34.15295  ? 292 ARG B CD   1 
ATOM   7777 N  NE   . ARG B  1 292 ? -59.47600 -6.56700  39.25900  1.000 29.39708  ? 292 ARG B NE   1 
ATOM   7778 C  CZ   . ARG B  1 292 ? -59.60200 -5.25900  39.19200  1.000 27.21223  ? 292 ARG B CZ   1 
ATOM   7779 N  NH1  . ARG B  1 292 ? -60.42700 -4.69000  38.32200  1.000 33.13432  ? 292 ARG B NH1  1 
ATOM   7780 N  NH2  . ARG B  1 292 ? -58.90300 -4.50000  40.03300  1.000 33.03233  ? 292 ARG B NH2  1 
ATOM   7781 H  H    . ARG B  1 292 ? -57.31100 -10.03300 36.68800  1.000 29.24286  ? 292 ARG B H    1 
ATOM   7782 H  HA   . ARG B  1 292 ? -59.00900 -11.37800 38.12600  1.000 31.58352  ? 292 ARG B HA   1 
ATOM   7783 H  HB2  . ARG B  1 292 ? -59.44000 -9.18200  36.42500  1.000 35.54834  ? 292 ARG B HB2  1 
ATOM   7784 H  HB3  . ARG B  1 292 ? -60.63200 -9.82500  37.25600  1.000 35.54834  ? 292 ARG B HB3  1 
ATOM   7785 H  HG2  . ARG B  1 292 ? -59.52400 -9.27900  39.21000  1.000 33.51648  ? 292 ARG B HG2  1 
ATOM   7786 H  HG3  . ARG B  1 292 ? -58.39600 -8.56700  38.34600  1.000 33.51648  ? 292 ARG B HG3  1 
ATOM   7787 H  HD2  . ARG B  1 292 ? -60.18900 -7.15300  37.49600  1.000 40.98611  ? 292 ARG B HD2  1 
ATOM   7788 H  HD3  . ARG B  1 292 ? -61.03300 -7.68900  38.73100  1.000 40.98611  ? 292 ARG B HD3  1 
ATOM   7789 H  HE   . ARG B  1 292 ? -58.95700 -6.88300  39.86700  1.000 35.27906  ? 292 ARG B HE   1 
ATOM   7790 H  HH11 . ARG B  1 292 ? -60.89200 -5.17800  37.78800  1.000 39.76375  ? 292 ARG B HH11 1 
ATOM   7791 H  HH12 . ARG B  1 292 ? -60.49700 -3.83300  38.29300  1.000 39.76375  ? 292 ARG B HH12 1 
ATOM   7792 H  HH21 . ARG B  1 292 ? -58.37900 -4.86600  40.60900  1.000 39.64136  ? 292 ARG B HH21 1 
ATOM   7793 H  HH22 . ARG B  1 292 ? -58.97500 -3.64300  40.00100  1.000 39.64136  ? 292 ARG B HH22 1 
ATOM   7794 N  N    . ASP B  1 293 ? -59.12100 -12.06300 35.04800  1.000 26.38326  ? 293 ASP B N    1 
ATOM   7795 C  CA   . ASP B  1 293 ? -59.67500 -12.97200 34.05500  1.000 27.65650  ? 293 ASP B CA   1 
ATOM   7796 C  C    . ASP B  1 293 ? -59.51100 -14.38800 34.58400  1.000 27.99590  ? 293 ASP B C    1 
ATOM   7797 O  O    . ASP B  1 293 ? -58.40700 -14.78900 34.98600  1.000 25.03966  ? 293 ASP B O    1 
ATOM   7798 C  CB   . ASP B  1 293 ? -58.90000 -12.77100 32.75100  1.000 26.45368  ? 293 ASP B CB   1 
ATOM   7799 C  CG   . ASP B  1 293 ? -59.49400 -13.51500 31.55700  1.000 26.24587  ? 293 ASP B CG   1 
ATOM   7800 O  OD1  . ASP B  1 293 ? -60.01500 -14.63900 31.70500  1.000 29.52002  ? 293 ASP B OD1  1 
ATOM   7801 O  OD2  . ASP B  1 293 ? -59.43300 -12.91200 30.45100  1.000 31.23536  ? 293 ASP B OD2  1 
ATOM   7802 H  H    . ASP B  1 293 ? -58.43000 -11.63200 34.77300  1.000 31.66247  ? 293 ASP B H    1 
ATOM   7803 H  HA   . ASP B  1 293 ? -60.61500 -12.81100 33.87800  1.000 33.19037  ? 293 ASP B HA   1 
ATOM   7804 H  HB2  . ASP B  1 293 ? -58.89300 -11.82500 32.53500  1.000 31.74698  ? 293 ASP B HB2  1 
ATOM   7805 H  HB3  . ASP B  1 293 ? -57.99200 -13.08900 32.87600  1.000 31.74698  ? 293 ASP B HB3  1 
ATOM   7806 N  N    . ARG B  1 294 ? -60.60000 -15.15100 34.57200  1.000 29.28073  ? 294 ARG B N    1 
ATOM   7807 C  CA   . ARG B  1 294 ? -60.53300 -16.50500 35.08900  1.000 28.35330  ? 294 ARG B CA   1 
ATOM   7808 C  C    . ARG B  1 294 ? -59.56500 -17.36500 34.29300  1.000 26.00770  ? 294 ARG B C    1 
ATOM   7809 O  O    . ARG B  1 294 ? -59.09400 -18.37200 34.81600  1.000 27.86202  ? 294 ARG B O    1 
ATOM   7810 C  CB   . ARG B  1 294 ? -61.92700 -17.14300 35.16500  1.000 38.17583  ? 294 ARG B CB   1 
ATOM   7811 C  CG   . ARG B  1 294 ? -62.77500 -16.50900 36.27700  1.000 67.59812  ? 294 ARG B CG   1 
ATOM   7812 C  CD   . ARG B  1 294 ? -64.02100 -17.30700 36.62600  1.000 79.14680  ? 294 ARG B CD   1 
ATOM   7813 N  NE   . ARG B  1 294 ? -64.94000 -17.40000 35.49800  1.000 92.14912  ? 294 ARG B NE   1 
ATOM   7814 C  CZ   . ARG B  1 294 ? -65.83900 -16.47900 35.17600  1.000 92.61867  ? 294 ARG B CZ   1 
ATOM   7815 N  NH1  . ARG B  1 294 ? -65.97100 -15.36400 35.87600  1.000 86.64924  ? 294 ARG B NH1  1 
ATOM   7816 N  NH2  . ARG B  1 294 ? -66.62600 -16.68300 34.12200  1.000 93.99097  ? 294 ARG B NH2  1 
ATOM   7817 H  H    . ARG B  1 294 ? -61.37100 -14.91100 34.27600  1.000 35.13944  ? 294 ARG B H    1 
ATOM   7818 H  HA   . ARG B  1 294 ? -60.21000 -16.47300 36.00300  1.000 34.02652  ? 294 ARG B HA   1 
ATOM   7819 H  HB2  . ARG B  1 294 ? -62.38500 -17.01500 34.32000  1.000 45.81356  ? 294 ARG B HB2  1 
ATOM   7820 H  HB3  . ARG B  1 294 ? -61.83600 -18.09100 35.35300  1.000 45.81356  ? 294 ARG B HB3  1 
ATOM   7821 H  HG2  . ARG B  1 294 ? -62.23600 -16.43800 37.08000  1.000 81.12031  ? 294 ARG B HG2  1 
ATOM   7822 H  HG3  . ARG B  1 294 ? -63.05900 -15.62800 35.99000  1.000 81.12031  ? 294 ARG B HG3  1 
ATOM   7823 H  HD2  . ARG B  1 294 ? -63.76400 -18.20600 36.88300  1.000 94.97872  ? 294 ARG B HD2  1 
ATOM   7824 H  HD3  . ARG B  1 294 ? -64.48400 -16.87200 37.35900  1.000 94.97872  ? 294 ARG B HD3  1 
ATOM   7825 H  HE   . ARG B  1 294 ? -64.89700 -18.10400 35.00600  1.000 110.58150 ? 294 ARG B HE   1 
ATOM   7826 H  HH11 . ARG B  1 294 ? -65.46600 -15.22200 36.55800  1.000 103.98166 ? 294 ARG B HH11 1 
ATOM   7827 H  HH12 . ARG B  1 294 ? -66.56000 -14.78000 35.64900  1.000 103.98166 ? 294 ARG B HH12 1 
ATOM   7828 H  HH21 . ARG B  1 294 ? -66.54800 -17.40400 33.66000  1.000 112.79172 ? 294 ARG B HH21 1 
ATOM   7829 H  HH22 . ARG B  1 294 ? -67.21200 -16.09400 33.90300  1.000 112.79172 ? 294 ARG B HH22 1 
ATOM   7830 N  N    . GLN B  1 295 ? -59.28100 -17.00000 33.05200  1.000 25.79053  ? 295 GLN B N    1 
ATOM   7831 C  CA   . GLN B  1 295 ? -58.38400 -17.78200 32.21000  1.000 24.19773  ? 295 GLN B CA   1 
ATOM   7832 C  C    . GLN B  1 295 ? -56.93600 -17.35800 32.32700  1.000 23.80678  ? 295 GLN B C    1 
ATOM   7833 O  O    . GLN B  1 295 ? -56.09500 -17.92800 31.62500  1.000 24.09769  ? 295 GLN B O    1 
ATOM   7834 C  CB   . GLN B  1 295 ? -58.85100 -17.73600 30.76400  1.000 23.87511  ? 295 GLN B CB   1 
ATOM   7835 C  CG   . GLN B  1 295 ? -60.16400 -18.45600 30.53200  1.000 25.80641  ? 295 GLN B CG   1 
ATOM   7836 C  CD   . GLN B  1 295 ? -60.57500 -18.51300 29.08200  1.000 29.88250  ? 295 GLN B CD   1 
ATOM   7837 O  OE1  . GLN B  1 295 ? -60.33600 -17.57500 28.34500  1.000 34.25903  ? 295 GLN B OE1  1 
ATOM   7838 N  NE2  . GLN B  1 295 ? -61.16100 -19.63100 28.66800  1.000 29.96853  ? 295 GLN B NE2  1 
ATOM   7839 H  H    . GLN B  1 295 ? -59.59700 -16.29700 32.67000  1.000 30.95120  ? 295 GLN B H    1 
ATOM   7840 H  HA   . GLN B  1 295 ? -58.42200 -18.71100 32.48800  1.000 29.03983  ? 295 GLN B HA   1 
ATOM   7841 H  HB2  . GLN B  1 295 ? -58.97000 -16.81000 30.50300  1.000 28.65270  ? 295 GLN B HB2  1 
ATOM   7842 H  HB3  . GLN B  1 295 ? -58.17900 -18.15500 30.20400  1.000 28.65270  ? 295 GLN B HB3  1 
ATOM   7843 H  HG2  . GLN B  1 295 ? -60.08100 -19.36800 30.85200  1.000 30.97026  ? 295 GLN B HG2  1 
ATOM   7844 H  HG3  . GLN B  1 295 ? -60.86400 -17.99500 31.02000  1.000 30.97026  ? 295 GLN B HG3  1 
ATOM   7845 H  HE21 . GLN B  1 295 ? -61.29000 -20.27800 29.21900  1.000 35.96480  ? 295 GLN B HE21 1 
ATOM   7846 H  HE22 . GLN B  1 295 ? -61.41200 -19.70700 27.84900  1.000 35.96480  ? 295 GLN B HE22 1 
ATOM   7847 N  N    . ILE B  1 296 ? -56.61700 -16.34300 33.13700  1.000 23.08585  ? 296 ILE B N    1 
ATOM   7848 C  CA   . ILE B  1 296 ? -55.24800 -15.86400 33.30700  1.000 22.97485  ? 296 ILE B CA   1 
ATOM   7849 C  C    . ILE B  1 296 ? -54.76600 -16.19400 34.70800  1.000 23.70192  ? 296 ILE B C    1 
ATOM   7850 O  O    . ILE B  1 296 ? -55.27300 -15.65600 35.69700  1.000 24.05278  ? 296 ILE B O    1 
ATOM   7851 C  CB   . ILE B  1 296 ? -55.10200 -14.36300 33.00500  1.000 22.10568  ? 296 ILE B CB   1 
ATOM   7852 C  CG1  . ILE B  1 296 ? -55.54900 -14.09300 31.58400  1.000 24.51291  ? 296 ILE B CG1  1 
ATOM   7853 C  CG2  . ILE B  1 296 ? -53.71700 -13.87900 33.35800  1.000 23.82173  ? 296 ILE B CG2  1 
ATOM   7854 C  CD1  . ILE B  1 296 ? -55.60700 -12.63900 31.19000  1.000 29.32902  ? 296 ILE B CD1  1 
ATOM   7855 H  H    . ILE B  1 296 ? -57.19200 -15.90800 33.60700  1.000 27.70558  ? 296 ILE B H    1 
ATOM   7856 H  HA   . ILE B  1 296 ? -54.69000 -16.35900 32.68700  1.000 27.57238  ? 296 ILE B HA   1 
ATOM   7857 H  HB   . ILE B  1 296 ? -55.69000 -13.83700 33.57000  1.000 26.52937  ? 296 ILE B HB   1 
ATOM   7858 H  HG12 . ILE B  1 296 ? -54.92900 -14.53200 30.98000  1.000 29.41806  ? 296 ILE B HG12 1 
ATOM   7859 H  HG13 . ILE B  1 296 ? -56.44000 -14.46000 31.46900  1.000 29.41806  ? 296 ILE B HG13 1 
ATOM   7860 H  HG21 . ILE B  1 296 ? -53.57800 -13.00400 32.96300  1.000 28.58864  ? 296 ILE B HG21 1 
ATOM   7861 H  HG22 . ILE B  1 296 ? -53.63800 -13.82200 34.32300  1.000 28.58864  ? 296 ILE B HG22 1 
ATOM   7862 H  HG23 . ILE B  1 296 ? -53.06400 -14.50600 33.01000  1.000 28.58864  ? 296 ILE B HG23 1 
ATOM   7863 H  HD11 . ILE B  1 296 ? -56.12600 -12.55300 30.37500  1.000 35.19739  ? 296 ILE B HD11 1 
ATOM   7864 H  HD12 . ILE B  1 296 ? -56.02700 -12.13400 31.90400  1.000 35.19739  ? 296 ILE B HD12 1 
ATOM   7865 H  HD13 . ILE B  1 296 ? -54.70500 -12.31500 31.04300  1.000 35.19739  ? 296 ILE B HD13 1 
ATOM   7866 N  N    . SER B  1 297 ? -53.75800 -17.06000 34.80200  1.000 22.02386  ? 297 SER B N    1 
ATOM   7867 C  CA   . SER B  1 297 ? -53.17500 -17.44700 36.08300  1.000 22.88838  ? 297 SER B CA   1 
ATOM   7868 C  C    . SER B  1 297 ? -51.94000 -16.63300 36.46000  1.000 20.76854  ? 297 SER B C    1 
ATOM   7869 O  O    . SER B  1 297 ? -51.53500 -16.66900 37.62800  1.000 23.75971  ? 297 SER B O    1 
ATOM   7870 C  CB   . SER B  1 297 ? -52.85300 -18.95900 36.12700  1.000 26.75520  ? 297 SER B CB   1 
ATOM   7871 O  OG   . SER B  1 297 ? -52.17900 -19.36000 34.93900  1.000 27.42711  ? 297 SER B OG   1 
ATOM   7872 H  H    . SER B  1 297 ? -53.38900 -17.44300 34.12700  1.000 26.43120  ? 297 SER B H    1 
ATOM   7873 H  HA   . SER B  1 297 ? -53.84300 -17.29200 36.76900  1.000 27.46862  ? 297 SER B HA   1 
ATOM   7874 H  HB2  . SER B  1 297 ? -52.28300 -19.14000 36.89100  1.000 32.10880  ? 297 SER B HB2  1 
ATOM   7875 H  HB3  . SER B  1 297 ? -53.68100 -19.45800 36.20600  1.000 32.10880  ? 297 SER B HB3  1 
ATOM   7876 H  HG   . SER B  1 297 ? -51.44700 -18.95400 34.87300  1.000 32.91510  ? 297 SER B HG   1 
ATOM   7877 N  N    . GLU B  1 298 ? -51.34500 -15.88500 35.52600  1.000 22.37264  ? 298 GLU B N    1 
ATOM   7878 C  CA   . GLU B  1 298 ? -50.26200 -14.97100 35.85800  1.000 21.73905  ? 298 GLU B CA   1 
ATOM   7879 C  C    . GLU B  1 298 ? -50.11100 -13.95400 34.73400  1.000 22.66463  ? 298 GLU B C    1 
ATOM   7880 O  O    . GLU B  1 298 ? -50.27400 -14.29600 33.56000  1.000 21.29988  ? 298 GLU B O    1 
ATOM   7881 C  CB   . GLU B  1 298 ? -48.91000 -15.68300 36.03700  1.000 21.43220  ? 298 GLU B CB   1 
ATOM   7882 C  CG   . GLU B  1 298 ? -47.86600 -14.73600 36.63600  1.000 22.12870  ? 298 GLU B CG   1 
ATOM   7883 C  CD   . GLU B  1 298 ? -46.47500 -15.31400 36.82000  1.000 27.21836  ? 298 GLU B CD   1 
ATOM   7884 O  OE1  . GLU B  1 298 ? -46.21700 -16.45900 36.42900  1.000 27.50006  ? 298 GLU B OE1  1 
ATOM   7885 O  OE2  . GLU B  1 298 ? -45.63000 -14.56600 37.35100  1.000 28.77840  ? 298 GLU B OE2  1 
ATOM   7886 H  H    . GLU B  1 298 ? -51.55400 -15.89300 34.69200  1.000 26.84973  ? 298 GLU B H    1 
ATOM   7887 H  HA   . GLU B  1 298 ? -50.49600 -14.52800 36.68800  1.000 26.08943  ? 298 GLU B HA   1 
ATOM   7888 H  HB2  . GLU B  1 298 ? -49.02100 -16.43800 36.63500  1.000 25.72120  ? 298 GLU B HB2  1 
ATOM   7889 H  HB3  . GLU B  1 298 ? -48.59000 -15.98800 35.17300  1.000 25.72120  ? 298 GLU B HB3  1 
ATOM   7890 H  HG2  . GLU B  1 298 ? -47.78100 -13.96700 36.05100  1.000 26.55701  ? 298 GLU B HG2  1 
ATOM   7891 H  HG3  . GLU B  1 298 ? -48.17700 -14.45500 37.51100  1.000 26.55701  ? 298 GLU B HG3  1 
ATOM   7892 N  N    . HIS B  1 299 ? -49.81600 -12.72000 35.09200  1.000 21.75897  ? 299 HIS B N    1 
ATOM   7893 C  CA   . HIS B  1 299 ? -49.45600 -11.69500 34.12500  1.000 21.16579  ? 299 HIS B CA   1 
ATOM   7894 C  C    . HIS B  1 299 ? -48.19100 -10.97500 34.57500  1.000 21.14659  ? 299 HIS B C    1 
ATOM   7895 O  O    . HIS B  1 299 ? -48.01600 -10.67400 35.75200  1.000 24.24688  ? 299 HIS B O    1 
ATOM   7896 C  CB   . HIS B  1 299 ? -50.56000 -10.67100 33.94200  1.000 21.26309  ? 299 HIS B CB   1 
ATOM   7897 C  CG   . HIS B  1 299 ? -50.18300 -9.53300  33.03600  1.000 20.49152  ? 299 HIS B CG   1 
ATOM   7898 N  ND1  . HIS B  1 299 ? -49.83300 -8.28400  33.50900  1.000 24.12269  ? 299 HIS B ND1  1 
ATOM   7899 C  CD2  . HIS B  1 299 ? -50.06800 -9.47100  31.68600  1.000 20.99061  ? 299 HIS B CD2  1 
ATOM   7900 C  CE1  . HIS B  1 299 ? -49.55600 -7.49100  32.48300  1.000 21.29957  ? 299 HIS B CE1  1 
ATOM   7901 N  NE2  . HIS B  1 299 ? -49.67600 -8.18900  31.37600  1.000 22.64303  ? 299 HIS B NE2  1 
ATOM   7902 H  H    . HIS B  1 299 ? -49.81700 -12.44400 35.90600  1.000 26.11332  ? 299 HIS B H    1 
ATOM   7903 H  HA   . HIS B  1 299 ? -49.28800 -12.12500 33.27200  1.000 25.40151  ? 299 HIS B HA   1 
ATOM   7904 H  HB2  . HIS B  1 299 ? -51.33400 -11.11200 33.55900  1.000 25.51827  ? 299 HIS B HB2  1 
ATOM   7905 H  HB3  . HIS B  1 299 ? -50.78500 -10.29800 34.80900  1.000 25.51827  ? 299 HIS B HB3  1 
ATOM   7906 H  HD1  . HIS B  1 299 ? -49.80000 -8.05600  34.33800  1.000 28.94979  ? 299 HIS B HD1  1 
ATOM   7907 H  HD2  . HIS B  1 299 ? -50.22500 -10.16300 31.08400  1.000 25.19130  ? 299 HIS B HD2  1 
ATOM   7908 H  HE1  . HIS B  1 299 ? -49.31800 -6.59400  32.53800  1.000 25.56205  ? 299 HIS B HE1  1 
ATOM   7909 N  N    . ARG B  1 300 ? -47.29400 -10.72100 33.62800  1.000 20.31706  ? 300 ARG B N    1 
ATOM   7910 C  CA   . ARG B  1 300 ? -46.17400 -9.82900  33.87200  1.000 20.08587  ? 300 ARG B CA   1 
ATOM   7911 C  C    . ARG B  1 300 ? -46.08300 -8.87500  32.68900  1.000 19.41752  ? 300 ARG B C    1 
ATOM   7912 O  O    . ARG B  1 300 ? -46.45200 -9.23900  31.57100  1.000 19.63180  ? 300 ARG B O    1 
ATOM   7913 C  CB   . ARG B  1 300 ? -44.85100 -10.59000 33.92400  1.000 21.47698  ? 300 ARG B CB   1 
ATOM   7914 C  CG   . ARG B  1 300 ? -44.84000 -11.80200 34.82800  1.000 22.42619  ? 300 ARG B CG   1 
ATOM   7915 C  CD   . ARG B  1 300 ? -43.56000 -12.62100 34.66900  1.000 22.91095  ? 300 ARG B CD   1 
ATOM   7916 N  NE   . ARG B  1 300 ? -43.70700 -13.90900 35.34500  1.000 23.52392  ? 300 ARG B NE   1 
ATOM   7917 C  CZ   . ARG B  1 300 ? -42.98100 -14.98400 35.06600  1.000 21.89064  ? 300 ARG B CZ   1 
ATOM   7918 N  NH1  . ARG B  1 300 ? -41.91800 -14.92700 34.26700  1.000 23.55586  ? 300 ARG B NH1  1 
ATOM   7919 N  NH2  . ARG B  1 300 ? -43.31800 -16.15000 35.60600  1.000 26.96237  ? 300 ARG B NH2  1 
ATOM   7920 H  H    . ARG B  1 300 ? -47.31600 -11.05500 32.83600  1.000 24.38303  ? 300 ARG B H    1 
ATOM   7921 H  HA   . ARG B  1 300 ? -46.30800 -9.35600  34.70800  1.000 24.10561  ? 300 ARG B HA   1 
ATOM   7922 H  HB2  . ARG B  1 300 ? -44.63800 -10.89400 33.02800  1.000 25.77494  ? 300 ARG B HB2  1 
ATOM   7923 H  HB3  . ARG B  1 300 ? -44.16300 -9.98500  34.24200  1.000 25.77494  ? 300 ARG B HB3  1 
ATOM   7924 H  HG2  . ARG B  1 300 ? -44.90200 -11.51200 35.75100  1.000 26.91399  ? 300 ARG B HG2  1 
ATOM   7925 H  HG3  . ARG B  1 300 ? -45.59300 -12.37200 34.60700  1.000 26.91399  ? 300 ARG B HG3  1 
ATOM   7926 H  HD2  . ARG B  1 300 ? -43.38900 -12.78100 33.72800  1.000 27.49570  ? 300 ARG B HD2  1 
ATOM   7927 H  HD3  . ARG B  1 300 ? -42.81500 -12.14400 35.06600  1.000 27.49570  ? 300 ARG B HD3  1 
ATOM   7928 H  HE   . ARG B  1 300 ? -44.30200 -13.97400 35.96300  1.000 28.23127  ? 300 ARG B HE   1 
ATOM   7929 H  HH11 . ARG B  1 300 ? -41.68400 -14.17800 33.91400  1.000 28.26959  ? 300 ARG B HH11 1 
ATOM   7930 H  HH12 . ARG B  1 300 ? -41.46500 -15.63900 34.10200  1.000 28.26959  ? 300 ARG B HH12 1 
ATOM   7931 H  HH21 . ARG B  1 300 ? -43.99900 -16.20100 36.12900  1.000 32.35741  ? 300 ARG B HH21 1 
ATOM   7932 H  HH22 . ARG B  1 300 ? -42.85500 -16.85400 35.43300  1.000 32.35741  ? 300 ARG B HH22 1 
ATOM   7933 N  N    . SER B  1 301 ? -45.53300 -7.68200  32.91900  1.000 20.39000  ? 301 SER B N    1 
ATOM   7934 C  CA   . SER B  1 301 ? -45.24900 -6.80200  31.79400  1.000 19.03952  ? 301 SER B CA   1 
ATOM   7935 C  C    . SER B  1 301 ? -44.31000 -5.69100  32.21200  1.000 22.44634  ? 301 SER B C    1 
ATOM   7936 O  O    . SER B  1 301 ? -44.06200 -5.46900  33.39800  1.000 24.22470  ? 301 SER B O    1 
ATOM   7937 C  CB   . SER B  1 301 ? -46.50400 -6.18400  31.20300  1.000 21.52791  ? 301 SER B CB   1 
ATOM   7938 O  OG   . SER B  1 301 ? -46.92400 -5.08600  32.01000  1.000 24.73389  ? 301 SER B OG   1 
ATOM   7939 H  H    . SER B  1 301 ? -45.32300 -7.37300  33.69300  1.000 24.47057  ? 301 SER B H    1 
ATOM   7940 H  HA   . SER B  1 301 ? -44.80800 -7.35100  31.12700  1.000 22.84999  ? 301 SER B HA   1 
ATOM   7941 H  HB2  . SER B  1 301 ? -46.31400 -5.86800  30.30500  1.000 25.83605  ? 301 SER B HB2  1 
ATOM   7942 H  HB3  . SER B  1 301 ? -47.20800 -6.85100  31.17700  1.000 25.83605  ? 301 SER B HB3  1 
ATOM   7943 H  HG   . SER B  1 301 ? -47.55400 -4.67700  31.63300  1.000 29.68323  ? 301 SER B HG   1 
ATOM   7944 N  N    . THR B  1 302 ? -43.75800 -5.00100  31.20800  1.000 20.36206  ? 302 THR B N    1 
ATOM   7945 C  CA   . THR B  1 302 ? -43.00100 -3.77500  31.43400  1.000 21.39392  ? 302 THR B CA   1 
ATOM   7946 C  C    . THR B  1 302 ? -43.87500 -2.54300  31.14400  1.000 23.77254  ? 302 THR B C    1 
ATOM   7947 O  O    . THR B  1 302 ? -43.35500 -1.47300  30.81500  1.000 26.81788  ? 302 THR B O    1 
ATOM   7948 C  CB   . THR B  1 302 ? -41.71200 -3.75400  30.60400  1.000 21.88688  ? 302 THR B CB   1 
ATOM   7949 O  OG1  . THR B  1 302 ? -42.07200 -3.97600  29.23400  1.000 21.13410  ? 302 THR B OG1  1 
ATOM   7950 C  CG2  . THR B  1 302 ? -40.77700 -4.81800  31.09300  1.000 21.19540  ? 302 THR B CG2  1 
ATOM   7951 H  H    . THR B  1 302 ? -43.81100 -5.23000  30.38100  1.000 24.43704  ? 302 THR B H    1 
ATOM   7952 H  HA   . THR B  1 302 ? -42.71700 -3.74000  32.36100  1.000 25.67527  ? 302 THR B HA   1 
ATOM   7953 H  HB   . THR B  1 302 ? -41.24700 -2.90600  30.68100  1.000 26.26682  ? 302 THR B HB   1 
ATOM   7954 H  HG1  . THR B  1 302 ? -41.39300 -3.91000  28.74400  1.000 25.36349  ? 302 THR B HG1  1 
ATOM   7955 H  HG21 . THR B  1 302 ? -39.99000 -4.85400  30.52700  1.000 25.43704  ? 302 THR B HG21 1 
ATOM   7956 H  HG22 . THR B  1 302 ? -40.50300 -4.62600  32.00300  1.000 25.43704  ? 302 THR B HG22 1 
ATOM   7957 H  HG23 . THR B  1 302 ? -41.21800 -5.68200  31.07300  1.000 25.43704  ? 302 THR B HG23 1 
ATOM   7958 N  N    . CYS B  1 303 ? -45.17900 -2.67400  31.32200  1.000 23.44843  ? 303 CYS B N    1 
ATOM   7959 C  CA   . CYS B  1 303 ? -46.05400 -1.51700  31.23800  1.000 25.99509  ? 303 CYS B CA   1 
ATOM   7960 C  C    . CYS B  1 303 ? -45.65800 -0.48000  32.29000  1.000 26.91353  ? 303 CYS B C    1 
ATOM   7961 O  O    . CYS B  1 303 ? -45.21500 -0.82700  33.38400  1.000 29.65333  ? 303 CYS B O    1 
ATOM   7962 C  CB   . CYS B  1 303 ? -47.48700 -1.93600  31.53300  1.000 23.24732  ? 303 CYS B CB   1 
ATOM   7963 S  SG   . CYS B  1 303 ? -48.26100 -2.89600  30.26000  1.000 25.63065  ? 303 CYS B SG   1 
ATOM   7964 H  H    . CYS B  1 303 ? -45.58100 -3.41500  31.49100  1.000 28.14068  ? 303 CYS B H    1 
ATOM   7965 H  HA   . CYS B  1 303 ? -45.98700 -1.13000  30.35100  1.000 31.19667  ? 303 CYS B HA   1 
ATOM   7966 H  HB2  . CYS B  1 303 ? -47.49100 -2.46900  32.34300  1.000 27.89934  ? 303 CYS B HB2  1 
ATOM   7967 H  HB3  . CYS B  1 303 ? -48.02100 -1.13600  31.66000  1.000 27.89934  ? 303 CYS B HB3  1 
ATOM   7968 N  N    . PRO B  1 304 ? -45.87100 0.80900   32.00500  1.000 30.39166  ? 304 PRO B N    1 
ATOM   7969 C  CA   . PRO B  1 304 ? -46.36000 1.37100   30.75100  1.000 32.54524  ? 304 PRO B CA   1 
ATOM   7970 C  C    . PRO B  1 304 ? -45.26900 1.38800   29.70200  1.000 37.35578  ? 304 PRO B C    1 
ATOM   7971 O  O    . PRO B  1 304 ? -44.10300 1.57700   30.05900  1.000 40.82919  ? 304 PRO B O    1 
ATOM   7972 C  CB   . PRO B  1 304 ? -46.78200 2.79400   31.14500  1.000 45.21754  ? 304 PRO B CB   1 
ATOM   7973 C  CG   . PRO B  1 304 ? -45.95500 3.12200   32.31600  1.000 40.67738  ? 304 PRO B CG   1 
ATOM   7974 C  CD   . PRO B  1 304 ? -45.75200 1.83600   33.07300  1.000 38.46646  ? 304 PRO B CD   1 
ATOM   7975 H  HA   . PRO B  1 304 ? -47.13700 0.89900   30.41400  1.000 39.05685  ? 304 PRO B HA   1 
ATOM   7976 H  HB2  . PRO B  1 304 ? -46.60700 3.40600   30.41300  1.000 54.26361  ? 304 PRO B HB2  1 
ATOM   7977 H  HB3  . PRO B  1 304 ? -47.72500 2.80800   31.37100  1.000 54.26361  ? 304 PRO B HB3  1 
ATOM   7978 H  HG2  . PRO B  1 304 ? -45.10400 3.48200   32.02100  1.000 48.81542  ? 304 PRO B HG2  1 
ATOM   7979 H  HG3  . PRO B  1 304 ? -46.41700 3.77300   32.86700  1.000 48.81542  ? 304 PRO B HG3  1 
ATOM   7980 H  HD2  . PRO B  1 304 ? -44.87400 1.81000   33.48500  1.000 46.16232  ? 304 PRO B HD2  1 
ATOM   7981 H  HD3  . PRO B  1 304 ? -46.43900 1.71800   33.74800  1.000 46.16232  ? 304 PRO B HD3  1 
ATOM   7982 N  N    . PHE B  1 305 ? -45.63200 1.17100   28.45100  1.000 35.68290  ? 305 PHE B N    1 
ATOM   7983 C  CA   . PHE B  1 305 ? -44.65500 1.12500   27.37000  1.000 45.30041  ? 305 PHE B CA   1 
ATOM   7984 C  C    . PHE B  1 305 ? -44.35500 2.53900   26.88200  1.000 61.88466  ? 305 PHE B C    1 
ATOM   7985 O  O    . PHE B  1 305 ? -45.27000 3.29100   26.53200  1.000 69.87515  ? 305 PHE B O    1 
ATOM   7986 C  CB   . PHE B  1 305 ? -45.19900 0.30500   26.19500  1.000 38.58582  ? 305 PHE B CB   1 
ATOM   7987 C  CG   . PHE B  1 305 ? -45.53800 -1.11800  26.54300  1.000 30.42961  ? 305 PHE B CG   1 
ATOM   7988 C  CD1  . PHE B  1 305 ? -44.75300 -1.84500  27.42000  1.000 28.15405  ? 305 PHE B CD1  1 
ATOM   7989 C  CD2  . PHE B  1 305 ? -46.61100 -1.73500  25.97900  1.000 24.42725  ? 305 PHE B CD2  1 
ATOM   7990 C  CE1  . PHE B  1 305 ? -45.08400 -3.16600  27.71800  1.000 23.56589  ? 305 PHE B CE1  1 
ATOM   7991 C  CE2  . PHE B  1 305 ? -46.94200 -3.03900  26.29700  1.000 26.66093  ? 305 PHE B CE2  1 
ATOM   7992 C  CZ   . PHE B  1 305 ? -46.15000 -3.74900  27.17600  1.000 23.93361  ? 305 PHE B CZ   1 
ATOM   7993 H  H    . PHE B  1 305 ? -46.44300 1.04500   28.19600  1.000 42.82204  ? 305 PHE B H    1 
ATOM   7994 H  HA   . PHE B  1 305 ? -43.84000 0.71400   27.69800  1.000 54.36306  ? 305 PHE B HA   1 
ATOM   7995 H  HB2  . PHE B  1 305 ? -46.00800 0.73000   25.86900  1.000 46.30554  ? 305 PHE B HB2  1 
ATOM   7996 H  HB3  . PHE B  1 305 ? -44.52900 0.28600   25.49400  1.000 46.30554  ? 305 PHE B HB3  1 
ATOM   7997 H  HD1  . PHE B  1 305 ? -44.00600 -1.45300  27.81000  1.000 33.78742  ? 305 PHE B HD1  1 
ATOM   7998 H  HD2  . PHE B  1 305 ? -47.13300 -1.27000  25.36600  1.000 29.31526  ? 305 PHE B HD2  1 
ATOM   7999 H  HE1  . PHE B  1 305 ? -44.54900 -3.64800  28.30700  1.000 28.28163  ? 305 PHE B HE1  1 
ATOM   8000 H  HE2  . PHE B  1 305 ? -47.69400 -3.43500  25.92100  1.000 31.99568  ? 305 PHE B HE2  1 
ATOM   8001 H  HZ   . PHE B  1 305 ? -46.36000 -4.63000  27.38800  1.000 28.72289  ? 305 PHE B HZ   1 
ATOM   8002 N  N    . VAL B  1 306 ? -43.06800 2.88600   26.82700  1.000 64.51980  ? 306 VAL B N    1 
ATOM   8003 C  CA   . VAL B  1 306 ? -42.67300 4.20800   26.35500  1.000 66.35636  ? 306 VAL B CA   1 
ATOM   8004 C  C    . VAL B  1 306 ? -43.22100 4.45100   24.95300  1.000 74.14285  ? 306 VAL B C    1 
ATOM   8005 O  O    . VAL B  1 306 ? -43.23200 3.55400   24.09900  1.000 65.85210  ? 306 VAL B O    1 
ATOM   8006 C  CB   . VAL B  1 306 ? -41.14000 4.32900   26.40000  1.000 66.25697  ? 306 VAL B CB   1 
ATOM   8007 C  CG1  . VAL B  1 306 ? -40.68500 5.62700   25.76000  1.000 67.65581  ? 306 VAL B CG1  1 
ATOM   8008 C  CG2  . VAL B  1 306 ? -40.63900 4.24400   27.83900  1.000 59.12652  ? 306 VAL B CG2  1 
ATOM   8009 H  H    . VAL B  1 306 ? -42.41200 2.37800   27.05600  1.000 77.42633  ? 306 VAL B H    1 
ATOM   8010 H  HA   . VAL B  1 306 ? -43.05300 4.88600   26.93400  1.000 79.63019  ? 306 VAL B HA   1 
ATOM   8011 H  HB   . VAL B  1 306 ? -40.75700 3.59400   25.89700  1.000 79.51093  ? 306 VAL B HB   1 
ATOM   8012 H  HG11 . VAL B  1 306 ? -39.76900 5.80500   26.02400  1.000 81.18953  ? 306 VAL B HG11 1 
ATOM   8013 H  HG12 . VAL B  1 306 ? -40.74100 5.54000   24.79600  1.000 81.18953  ? 306 VAL B HG12 1 
ATOM   8014 H  HG13 . VAL B  1 306 ? -41.26200 6.34700   26.06100  1.000 81.18953  ? 306 VAL B HG13 1 
ATOM   8015 H  HG21 . VAL B  1 306 ? -39.67800 4.37100   27.84700  1.000 70.95439  ? 306 VAL B HG21 1 
ATOM   8016 H  HG22 . VAL B  1 306 ? -41.06800 4.93800   28.36400  1.000 70.95439  ? 306 VAL B HG22 1 
ATOM   8017 H  HG23 . VAL B  1 306 ? -40.86100 3.37200   28.20000  1.000 70.95439  ? 306 VAL B HG23 1 
ATOM   8018 N  N    . ASP B  1 307 ? -43.69000 5.67600   24.71600  1.000 81.61767  ? 307 ASP B N    1 
ATOM   8019 C  CA   . ASP B  1 307 ? -44.21100 6.07700   23.41100  1.000 67.35497  ? 307 ASP B CA   1 
ATOM   8020 C  C    . ASP B  1 307 ? -43.09700 6.09500   22.36200  1.000 67.60639  ? 307 ASP B C    1 
ATOM   8021 O  O    . ASP B  1 307 ? -41.98100 6.53200   22.63800  1.000 72.36852  ? 307 ASP B O    1 
ATOM   8022 C  CB   . ASP B  1 307 ? -44.84800 7.47000   23.49900  1.000 69.02818  ? 307 ASP B CB   1 
ATOM   8023 C  CG   . ASP B  1 307 ? -45.85600 7.72300   22.39000  1.000 79.36167  ? 307 ASP B CG   1 
ATOM   8024 O  OD1  . ASP B  1 307 ? -46.97200 7.16700   22.46900  1.000 79.36438  ? 307 ASP B OD1  1 
ATOM   8025 O  OD2  . ASP B  1 307 ? -45.53500 8.47300   21.44300  1.000 84.51960  ? 307 ASP B OD2  1 
ATOM   8026 H  H    . ASP B  1 307 ? -43.71800 6.30300   25.30400  1.000 97.94377  ? 307 ASP B H    1 
ATOM   8027 H  HA   . ASP B  1 307 ? -44.88800 5.44100   23.13200  1.000 80.82853  ? 307 ASP B HA   1 
ATOM   8028 H  HB2  . ASP B  1 307 ? -45.30900 7.55500   24.34800  1.000 82.83638  ? 307 ASP B HB2  1 
ATOM   8029 H  HB3  . ASP B  1 307 ? -44.15200 8.14200   23.43100  1.000 82.83638  ? 307 ASP B HB3  1 
HETATM 8030 NA NA   . NA  C  2 .   ? -17.35000 -43.91200 25.06600  1.000 23.36084  ? 401 NA  A NA   1 
HETATM 8031 C  C1   . EDO D  3 .   ? 2.40800   -16.46000 39.28100  1.000 34.79923  ? 402 EDO A C1   1 
HETATM 8032 O  O1   . EDO D  3 .   ? 3.27500   -15.72700 38.41700  1.000 39.73154  ? 402 EDO A O1   1 
HETATM 8033 C  C2   . EDO D  3 .   ? 1.78700   -17.54000 38.41800  1.000 29.93943  ? 402 EDO A C2   1 
HETATM 8034 O  O2   . EDO D  3 .   ? 0.92600   -16.90100 37.44800  1.000 30.00205  ? 402 EDO A O2   1 
HETATM 8035 H  H11  . EDO D  3 .   ? 1.63900   -15.80900 39.70300  1.000 41.76163  ? 402 EDO A H11  1 
HETATM 8036 H  H12  . EDO D  3 .   ? 2.96800   -16.89900 40.11000  1.000 41.76163  ? 402 EDO A H12  1 
HETATM 8037 H  HO1  . EDO D  3 .   ? 4.19500   -15.89100 38.66800  1.000 47.68041  ? 402 EDO A HO1  1 
HETATM 8038 H  H21  . EDO D  3 .   ? 1.21100   -18.23200 39.03600  1.000 35.92988  ? 402 EDO A H21  1 
HETATM 8039 H  H22  . EDO D  3 .   ? 2.56700   -18.11200 37.91100  1.000 35.92988  ? 402 EDO A H22  1 
HETATM 8040 H  HO2  . EDO D  3 .   ? 0.93600   -17.40900 36.62500  1.000 36.00502  ? 402 EDO A HO2  1 
HETATM 8041 C  C1   . EDO E  3 .   ? -5.12300  -6.00500  27.72000  0.960 50.70611  ? 403 EDO A C1   1 
HETATM 8042 O  O1   . EDO E  3 .   ? -4.50800  -6.86100  28.69000  0.960 50.17383  ? 403 EDO A O1   1 
HETATM 8043 C  C2   . EDO E  3 .   ? -5.66900  -6.92500  26.64800  0.960 50.34524  ? 403 EDO A C2   1 
HETATM 8044 O  O2   . EDO E  3 .   ? -6.47300  -7.89500  27.33000  0.960 50.33420  ? 403 EDO A O2   1 
HETATM 8045 H  H11  . EDO E  3 .   ? -5.92600  -5.41900  28.17400  0.960 60.84990  ? 403 EDO A H11  1 
HETATM 8046 H  H12  . EDO E  3 .   ? -4.39500  -5.30800  27.30000  0.960 60.84990  ? 403 EDO A H12  1 
HETATM 8047 H  HO1  . EDO E  3 .   ? -4.15500  -6.32700  29.41400  0.960 60.21116  ? 403 EDO A HO1  1 
HETATM 8048 H  H21  . EDO E  3 .   ? -4.85500  -7.41100  26.10500  0.960 60.41686  ? 403 EDO A H21  1 
HETATM 8049 H  H22  . EDO E  3 .   ? -6.26700  -6.36600  25.92600  0.960 60.41686  ? 403 EDO A H22  1 
HETATM 8050 H  HO2  . EDO E  3 .   ? -6.39400  -7.76500  28.28500  0.960 60.40360  ? 403 EDO A HO2  1 
HETATM 8051 C  C1   . EDO F  3 .   ? 1.88200   -12.10200 8.96100   0.989 55.04262  ? 404 EDO A C1   1 
HETATM 8052 O  O1   . EDO F  3 .   ? 1.90500   -13.42400 8.42200   0.989 54.86832  ? 404 EDO A O1   1 
HETATM 8053 C  C2   . EDO F  3 .   ? 0.76700   -12.01900 9.99900   0.989 54.47188  ? 404 EDO A C2   1 
HETATM 8054 O  O2   . EDO F  3 .   ? -0.51700  -12.11700 9.37000   0.989 54.39239  ? 404 EDO A O2   1 
HETATM 8055 H  H11  . EDO F  3 .   ? 2.84300   -11.87000 9.42400   0.989 66.05371  ? 404 EDO A H11  1 
HETATM 8056 H  H12  . EDO F  3 .   ? 1.70800   -11.37600 8.16500   0.989 66.05371  ? 404 EDO A H12  1 
HETATM 8057 H  HO1  . EDO F  3 .   ? 1.96600   -14.06500 9.14300   0.989 65.84455  ? 404 EDO A HO1  1 
HETATM 8058 H  H21  . EDO F  3 .   ? 0.83900   -11.07100 10.53700  0.989 65.36882  ? 404 EDO A H21  1 
HETATM 8059 H  H22  . EDO F  3 .   ? 0.88200   -12.82600 10.72500  0.989 65.36882  ? 404 EDO A H22  1 
HETATM 8060 H  HO2  . EDO F  3 .   ? -0.61800  -11.40100 8.72800   0.989 65.27343  ? 404 EDO A HO2  1 
HETATM 8061 C  C1   . EDO G  3 .   ? -12.13500 -7.10900  44.19500  0.906 53.08745  ? 405 EDO A C1   1 
HETATM 8062 O  O1   . EDO G  3 .   ? -10.92100 -6.43900  43.84300  0.906 53.52788  ? 405 EDO A O1   1 
HETATM 8063 C  C2   . EDO G  3 .   ? -13.11300 -6.86500  43.05200  0.906 51.78548  ? 405 EDO A C2   1 
HETATM 8064 O  O2   . EDO G  3 .   ? -14.36600 -7.47000  43.31700  0.906 52.33359  ? 405 EDO A O2   1 
HETATM 8065 H  H11  . EDO G  3 .   ? -12.53300 -6.71500  45.13200  0.906 63.70750  ? 405 EDO A H11  1 
HETATM 8066 H  H12  . EDO G  3 .   ? -11.95800 -8.17800  44.32800  0.906 63.70750  ? 405 EDO A H12  1 
HETATM 8067 H  HO1  . EDO G  3 .   ? -10.93100 -6.22700  42.90000  0.906 64.23602  ? 405 EDO A HO1  1 
HETATM 8068 H  H21  . EDO G  3 .   ? -12.70000 -7.27200  42.12700  0.906 62.14514  ? 405 EDO A H21  1 
HETATM 8069 H  H22  . EDO G  3 .   ? -13.25000 -5.79000  42.91400  0.906 62.14514  ? 405 EDO A H22  1 
HETATM 8070 H  HO2  . EDO G  3 .   ? -14.25600 -8.42900  43.36300  0.906 62.80287  ? 405 EDO A HO2  1 
HETATM 8071 C  C1   . EDO H  3 .   ? -6.27100  -25.97800 43.71200  1.000 34.10561  ? 406 EDO A C1   1 
HETATM 8072 O  O1   . EDO H  3 .   ? -7.21100  -25.49200 42.77200  1.000 31.96931  ? 406 EDO A O1   1 
HETATM 8073 C  C2   . EDO H  3 .   ? -6.66700  -27.36300 44.20100  1.000 37.24051  ? 406 EDO A C2   1 
HETATM 8074 O  O2   . EDO H  3 .   ? -7.84000  -27.27300 45.01700  1.000 40.15283  ? 406 EDO A O2   1 
HETATM 8075 H  H11  . EDO H  3 .   ? -6.21500  -25.29300 44.56100  1.000 40.92929  ? 406 EDO A H11  1 
HETATM 8076 H  H12  . EDO H  3 .   ? -5.28200  -26.02200 43.25100  1.000 40.92929  ? 406 EDO A H12  1 
HETATM 8077 H  HO1  . EDO H  3 .   ? -6.74600  -25.18600 41.98000  1.000 38.36573  ? 406 EDO A HO1  1 
HETATM 8078 H  H21  . EDO H  3 .   ? -5.84900  -27.80000 44.77700  1.000 44.69117  ? 406 EDO A H21  1 
HETATM 8079 H  H22  . EDO H  3 .   ? -6.86100  -28.01500 43.34600  1.000 44.69117  ? 406 EDO A H22  1 
HETATM 8080 H  HO2  . EDO H  3 .   ? -8.60100  -27.61300 44.52600  1.000 48.18596  ? 406 EDO A HO2  1 
HETATM 8081 C  C1   . EDO I  3 .   ? -4.78400  -32.20900 10.23300  1.000 47.55618  ? 407 EDO A C1   1 
HETATM 8082 O  O1   . EDO I  3 .   ? -4.52700  -33.01200 11.38500  1.000 48.01275  ? 407 EDO A O1   1 
HETATM 8083 C  C2   . EDO I  3 .   ? -4.53400  -33.02600 8.97100   1.000 46.09828  ? 407 EDO A C2   1 
HETATM 8084 O  O2   . EDO I  3 .   ? -3.12000  -33.10700 8.82400   1.000 47.51870  ? 407 EDO A O2   1 
HETATM 8085 H  H11  . EDO I  3 .   ? -5.81800  -31.86000 10.24800  1.000 57.06998  ? 407 EDO A H11  1 
HETATM 8086 H  H12  . EDO I  3 .   ? -4.13300  -31.33100 10.24000  1.000 57.06998  ? 407 EDO A H12  1 
HETATM 8087 H  HO1  . EDO I  3 .   ? -4.55500  -33.94600 11.14000  1.000 57.61787  ? 407 EDO A HO1  1 
HETATM 8088 H  H21  . EDO I  3 .   ? -4.98500  -32.54300 8.10200   1.000 55.32050  ? 407 EDO A H21  1 
HETATM 8089 H  H22  . EDO I  3 .   ? -4.96900  -34.02300 9.06500   1.000 55.32050  ? 407 EDO A H22  1 
HETATM 8090 H  HO2  . EDO I  3 .   ? -2.85000  -32.62100 8.03200   1.000 57.02501  ? 407 EDO A HO2  1 
HETATM 8091 C  C1   . EDO J  3 .   ? -24.74400 -29.09700 23.30300  1.000 41.72607  ? 408 EDO A C1   1 
HETATM 8092 O  O1   . EDO J  3 .   ? -25.00600 -29.03900 21.89100  1.000 37.57846  ? 408 EDO A O1   1 
HETATM 8093 C  C2   . EDO J  3 .   ? -25.43600 -30.30100 23.94400  1.000 42.26995  ? 408 EDO A C2   1 
HETATM 8094 O  O2   . EDO J  3 .   ? -26.83300 -29.99500 24.09000  1.000 45.87664  ? 408 EDO A O2   1 
HETATM 8095 H  H11  . EDO J  3 .   ? -25.09900 -28.17900 23.77600  1.000 50.07384  ? 408 EDO A H11  1 
HETATM 8096 H  H12  . EDO J  3 .   ? -23.66700 -29.16500 23.46900  1.000 50.07384  ? 408 EDO A H12  1 
HETATM 8097 H  HO1  . EDO J  3 .   ? -24.16900 -28.99900 21.40800  1.000 45.09671  ? 408 EDO A HO1  1 
HETATM 8098 H  H21  . EDO J  3 .   ? -24.99300 -30.51400 24.91900  1.000 50.72650  ? 408 EDO A H21  1 
HETATM 8099 H  H22  . EDO J  3 .   ? -25.30800 -31.18600 23.31700  1.000 50.72650  ? 408 EDO A H22  1 
HETATM 8100 H  HO2  . EDO J  3 .   ? -27.21400 -29.80800 23.22100  1.000 55.05454  ? 408 EDO A HO2  1 
HETATM 8101 C  C1   . EDO K  3 .   ? -26.12600 -15.95700 23.08200  1.000 63.54238  ? 409 EDO A C1   1 
HETATM 8102 O  O1   . EDO K  3 .   ? -25.70600 -14.68200 22.56900  1.000 65.04674  ? 409 EDO A O1   1 
HETATM 8103 C  C2   . EDO K  3 .   ? -24.88900 -16.85500 23.16000  1.000 61.49768  ? 409 EDO A C2   1 
HETATM 8104 O  O2   . EDO K  3 .   ? -23.92600 -16.17000 23.94100  1.000 58.91415  ? 409 EDO A O2   1 
HETATM 8105 H  H11  . EDO K  3 .   ? -26.87700 -16.40100 22.42500  1.000 76.25342  ? 409 EDO A H11  1 
HETATM 8106 H  H12  . EDO K  3 .   ? -26.57300 -15.83900 24.07100  1.000 76.25342  ? 409 EDO A H12  1 
HETATM 8107 H  HO1  . EDO K  3 .   ? -25.80500 -14.01000 23.25700  1.000 78.05865  ? 409 EDO A HO1  1 
HETATM 8108 H  H21  . EDO K  3 .   ? -25.14200 -17.81300 23.62000  1.000 73.79978  ? 409 EDO A H21  1 
HETATM 8109 H  H22  . EDO K  3 .   ? -24.49800 -17.05500 22.16100  1.000 73.79978  ? 409 EDO A H22  1 
HETATM 8110 H  HO2  . EDO K  3 .   ? -23.06500 -16.59900 23.84000  1.000 70.69954  ? 409 EDO A HO2  1 
HETATM 8111 C  C1   . EDO L  3 .   ? -16.15100 -8.63900  10.41200  0.958 55.53142  ? 410 EDO A C1   1 
HETATM 8112 O  O1   . EDO L  3 .   ? -15.73300 -7.28400  10.21000  0.958 55.83538  ? 410 EDO A O1   1 
HETATM 8113 C  C2   . EDO L  3 .   ? -16.51200 -9.33800  9.10300   0.958 55.27992  ? 410 EDO A C2   1 
HETATM 8114 O  O2   . EDO L  3 .   ? -15.42700 -10.17900 8.68300   0.958 55.87497  ? 410 EDO A O2   1 
HETATM 8115 H  H11  . EDO L  3 .   ? -17.01800 -8.65100  11.07500  0.958 66.64026  ? 410 EDO A H11  1 
HETATM 8116 H  H12  . EDO L  3 .   ? -15.34600 -9.19200  10.90200  0.958 66.64026  ? 410 EDO A H12  1 
HETATM 8117 H  HO1  . EDO L  3 .   ? -15.84400 -6.78700  11.03200  0.958 67.00502  ? 410 EDO A HO1  1 
HETATM 8118 H  H21  . EDO L  3 .   ? -16.72300 -8.59400  8.33300   0.958 66.33847  ? 410 EDO A H21  1 
HETATM 8119 H  H22  . EDO L  3 .   ? -17.41300 -9.94000  9.24300   0.958 66.33847  ? 410 EDO A H22  1 
HETATM 8120 H  HO2  . EDO L  3 .   ? -15.07100 -10.65200 9.44700   0.958 67.05253  ? 410 EDO A HO2  1 
HETATM 8121 C  C1   . EDO M  3 .   ? -10.98800 -3.29400  19.03900  1.000 53.97706  ? 411 EDO A C1   1 
HETATM 8122 O  O1   . EDO M  3 .   ? -11.23800 -2.09600  19.78400  1.000 55.41003  ? 411 EDO A O1   1 
HETATM 8123 C  C2   . EDO M  3 .   ? -9.61500  -3.83600  19.41100  1.000 51.67620  ? 411 EDO A C2   1 
HETATM 8124 O  O2   . EDO M  3 .   ? -9.46800  -3.82800  20.83600  1.000 47.15477  ? 411 EDO A O2   1 
HETATM 8125 H  H11  . EDO M  3 .   ? -11.02800 -3.08200  17.96900  1.000 64.77503  ? 411 EDO A H11  1 
HETATM 8126 H  H12  . EDO M  3 .   ? -11.75500 -4.03800  19.26300  1.000 64.77503  ? 411 EDO A H12  1 
HETATM 8127 H  HO1  . EDO M  3 .   ? -11.81000 -1.51000  19.27000  1.000 66.49460  ? 411 EDO A HO1  1 
HETATM 8128 H  H21  . EDO M  3 .   ? -8.83700  -3.22000  18.95500  1.000 62.01400  ? 411 EDO A H21  1 
HETATM 8129 H  H22  . EDO M  3 .   ? -9.50300  -4.85400  19.03200  1.000 62.01400  ? 411 EDO A H22  1 
HETATM 8130 H  HO2  . EDO M  3 .   ? -10.13400 -4.40700  21.23200  1.000 56.58828  ? 411 EDO A HO2  1 
HETATM 8131 C  C1   . EDO N  3 .   ? -1.43200  -5.26800  24.40700  1.000 69.15921  ? 412 EDO A C1   1 
HETATM 8132 O  O1   . EDO N  3 .   ? -0.53300  -4.16300  24.26200  1.000 69.05486  ? 412 EDO A O1   1 
HETATM 8133 C  C2   . EDO N  3 .   ? -2.81700  -4.66300  24.56200  1.000 69.83552  ? 412 EDO A C2   1 
HETATM 8134 O  O2   . EDO N  3 .   ? -2.70700  -3.53600  25.43900  1.000 70.38868  ? 412 EDO A O2   1 
HETATM 8135 H  H11  . EDO N  3 .   ? -1.17200  -5.86700  25.28200  1.000 82.99362  ? 412 EDO A H11  1 
HETATM 8136 H  H12  . EDO N  3 .   ? -1.39000  -5.91900  23.53100  1.000 82.99362  ? 412 EDO A H12  1 
HETATM 8137 H  HO1  . EDO N  3 .   ? -0.19700  -4.13700  23.35500  1.000 82.86839  ? 412 EDO A HO1  1 
HETATM 8138 H  H21  . EDO N  3 .   ? -3.50800  -5.39900  24.97700  1.000 83.80519  ? 412 EDO A H21  1 
HETATM 8139 H  H22  . EDO N  3 .   ? -3.20400  -4.34900  23.59000  1.000 83.80519  ? 412 EDO A H22  1 
HETATM 8140 H  HO2  . EDO N  3 .   ? -3.48500  -2.97100  25.33800  1.000 84.46897  ? 412 EDO A HO2  1 
HETATM 8141 C  C1   . EDO O  3 .   ? 7.67300   -25.11800 8.20000   1.000 41.06346  ? 413 EDO A C1   1 
HETATM 8142 O  O1   . EDO O  3 .   ? 6.66100   -24.59200 9.07500   1.000 43.26774  ? 413 EDO A O1   1 
HETATM 8143 C  C2   . EDO O  3 .   ? 7.00600   -25.68300 6.95500   1.000 41.33780  ? 413 EDO A C2   1 
HETATM 8144 O  O2   . EDO O  3 .   ? 6.18700   -24.68000 6.34000   1.000 41.59843  ? 413 EDO A O2   1 
HETATM 8145 H  H11  . EDO O  3 .   ? 8.23800   -25.90100 8.71000   1.000 49.27871  ? 413 EDO A H11  1 
HETATM 8146 H  H12  . EDO O  3 .   ? 8.37300   -24.32700 7.92200   1.000 49.27871  ? 413 EDO A H12  1 
HETATM 8147 H  HO1  . EDO O  3 .   ? 5.96100   -25.25000 9.18900   1.000 51.92386  ? 413 EDO A HO1  1 
HETATM 8148 H  H21  . EDO O  3 .   ? 7.76800   -26.02200 6.25000   1.000 49.60792  ? 413 EDO A H21  1 
HETATM 8149 H  H22  . EDO O  3 .   ? 6.39200   -26.54500 7.22500   1.000 49.60792  ? 413 EDO A H22  1 
HETATM 8150 H  HO2  . EDO O  3 .   ? 5.90500   -24.98600 5.46700   1.000 49.92068  ? 413 EDO A HO2  1 
HETATM 8151 C  C1   . EDO P  3 .   ? -6.15400  0.67400   26.41200  0.971 63.44591  ? 414 EDO A C1   1 
HETATM 8152 O  O1   . EDO P  3 .   ? -5.61200  0.54400   25.09400  0.971 64.13944  ? 414 EDO A O1   1 
HETATM 8153 C  C2   . EDO P  3 .   ? -7.23800  -0.37800  26.60300  0.971 63.04356  ? 414 EDO A C2   1 
HETATM 8154 O  O2   . EDO P  3 .   ? -8.44000  0.12000   26.00200  0.971 63.03738  ? 414 EDO A O2   1 
HETATM 8155 H  H11  . EDO P  3 .   ? -6.57400  1.67300   26.54700  0.971 76.13766  ? 414 EDO A H11  1 
HETATM 8156 H  H12  . EDO P  3 .   ? -5.36600  0.53900   27.15600  0.971 76.13766  ? 414 EDO A H12  1 
HETATM 8157 H  HO1  . EDO P  3 .   ? -5.40300  1.42000   24.74300  0.971 76.96989  ? 414 EDO A HO1  1 
HETATM 8158 H  H21  . EDO P  3 .   ? -7.39700  -0.56900  27.66700  0.971 75.65483  ? 414 EDO A H21  1 
HETATM 8159 H  H22  . EDO P  3 .   ? -6.94000  -1.31800  26.13400  0.971 75.65483  ? 414 EDO A H22  1 
HETATM 8160 H  HO2  . EDO P  3 .   ? -8.91500  -0.60900  25.57900  0.971 75.64741  ? 414 EDO A HO2  1 
HETATM 8161 C  C1   . EDO Q  3 .   ? -13.60500 -45.51200 22.85400  1.000 43.80201  ? 415 EDO A C1   1 
HETATM 8162 O  O1   . EDO Q  3 .   ? -12.68000 -44.50100 23.29500  1.000 44.15248  ? 415 EDO A O1   1 
HETATM 8163 C  C2   . EDO Q  3 .   ? -14.93100 -45.41600 23.59100  1.000 41.99086  ? 415 EDO A C2   1 
HETATM 8164 O  O2   . EDO Q  3 .   ? -15.53600 -44.12600 23.44900  1.000 36.33908  ? 415 EDO A O2   1 
HETATM 8165 H  H11  . EDO Q  3 .   ? -13.16900 -46.49900 23.02300  1.000 52.56497  ? 415 EDO A H11  1 
HETATM 8166 H  H12  . EDO Q  3 .   ? -13.77800 -45.40100 21.78200  1.000 52.56497  ? 415 EDO A H12  1 
HETATM 8167 H  HO1  . EDO Q  3 .   ? -11.87100 -44.55300 22.76800  1.000 52.98554  ? 415 EDO A HO1  1 
HETATM 8168 H  H21  . EDO Q  3 .   ? -14.76800 -45.62100 24.65100  1.000 50.39159  ? 415 EDO A H21  1 
HETATM 8169 H  H22  . EDO Q  3 .   ? -15.61200 -46.17600 23.20300  1.000 50.39159  ? 415 EDO A H22  1 
HETATM 8170 H  HO2  . EDO Q  3 .   ? -16.43700 -44.22700 23.11100  1.000 43.60946  ? 415 EDO A HO2  1 
HETATM 8171 C  C1   . EDO R  3 .   ? -29.49900 -26.33700 18.57200  1.000 54.02447  ? 416 EDO A C1   1 
HETATM 8172 O  O1   . EDO R  3 .   ? -29.69800 -25.79200 19.87300  1.000 54.92119  ? 416 EDO A O1   1 
HETATM 8173 C  C2   . EDO R  3 .   ? -30.83600 -26.29500 17.84600  1.000 51.52512  ? 416 EDO A C2   1 
HETATM 8174 O  O2   . EDO R  3 .   ? -31.89600 -26.16700 18.80100  1.000 47.92994  ? 416 EDO A O2   1 
HETATM 8175 H  H11  . EDO R  3 .   ? -29.13800 -27.36500 18.64200  1.000 64.83192  ? 416 EDO A H11  1 
HETATM 8176 H  H12  . EDO R  3 .   ? -28.75300 -25.75600 18.02600  1.000 64.83192  ? 416 EDO A H12  1 
HETATM 8177 H  HO1  . EDO R  3 .   ? -28.99300 -26.09500 20.46100  1.000 65.90799  ? 416 EDO A HO1  1 
HETATM 8178 H  H21  . EDO R  3 .   ? -30.85700 -25.45000 17.15500  1.000 61.83270  ? 416 EDO A H21  1 
HETATM 8179 H  H22  . EDO R  3 .   ? -30.97100 -27.20900 17.26300  1.000 61.83270  ? 416 EDO A H22  1 
HETATM 8180 H  HO2  . EDO R  3 .   ? -32.45900 -26.95300 18.76600  1.000 57.51849  ? 416 EDO A HO2  1 
HETATM 8181 C  C1   . EDO S  3 .   ? -18.41500 -38.01300 36.84400  1.000 34.96315  ? 417 EDO A C1   1 
HETATM 8182 O  O1   . EDO S  3 .   ? -18.10700 -38.33500 38.20400  1.000 36.89653  ? 417 EDO A O1   1 
HETATM 8183 C  C2   . EDO S  3 .   ? -19.44000 -36.89000 36.82400  1.000 32.18696  ? 417 EDO A C2   1 
HETATM 8184 O  O2   . EDO S  3 .   ? -20.59900 -37.19200 37.60400  1.000 27.81098  ? 417 EDO A O2   1 
HETATM 8185 H  H11  . EDO S  3 .   ? -17.50900 -37.70200 36.32000  1.000 41.95834  ? 417 EDO A H11  1 
HETATM 8186 H  H12  . EDO S  3 .   ? -18.81300 -38.89200 36.33300  1.000 41.95834  ? 417 EDO A H12  1 
HETATM 8187 H  HO1  . EDO S  3 .   ? -17.32000 -38.89600 38.23300  1.000 44.27839  ? 417 EDO A HO1  1 
HETATM 8188 H  H21  . EDO S  3 .   ? -19.74400 -36.70300 35.79200  1.000 38.62691  ? 417 EDO A H21  1 
HETATM 8189 H  H22  . EDO S  3 .   ? -18.97900 -35.97800 37.20900  1.000 38.62691  ? 417 EDO A H22  1 
HETATM 8190 H  HO2  . EDO S  3 .   ? -21.38700 -37.13300 37.04700  1.000 33.37573  ? 417 EDO A HO2  1 
HETATM 8191 CL CL   . CL  T  4 .   ? -13.86900 -31.79600 7.97600   1.000 24.29864  ? 418 CL  A CL   1 
HETATM 8192 CL CL   . CL  U  4 .   ? 3.72500   -26.25100 13.12400  0.799 26.06006  ? 419 CL  A CL   1 
HETATM 8193 NA NA   . NA  V  2 .   ? -39.69800 -25.01200 -0.13900  1.000 27.65627  ? 401 NA  B NA   1 
HETATM 8194 NA NA   . NA  W  2 .   ? -57.09900 -15.18200 37.05500  1.000 24.09317  ? 402 NA  B NA   1 
HETATM 8195 C  C1   . EDO X  3 .   ? -50.01300 5.05700   13.82800  1.000 43.78951  ? 403 EDO B C1   1 
HETATM 8196 O  O1   . EDO X  3 .   ? -49.02500 5.75300   13.05800  1.000 45.34354  ? 403 EDO B O1   1 
HETATM 8197 C  C2   . EDO X  3 .   ? -51.23200 5.96100   13.95800  1.000 43.60007  ? 403 EDO B C2   1 
HETATM 8198 O  O2   . EDO X  3 .   ? -51.75500 6.18500   12.63600  1.000 42.73622  ? 403 EDO B O2   1 
HETATM 8199 H  H11  . EDO X  3 .   ? -49.61800 4.81300   14.81600  1.000 52.54997  ? 403 EDO B H11  1 
HETATM 8200 H  H12  . EDO X  3 .   ? -50.28700 4.12200   13.33500  1.000 52.54997  ? 403 EDO B H12  1 
HETATM 8201 H  HO1  . EDO X  3 .   ? -48.50900 5.11600   12.54500  1.000 54.41481  ? 403 EDO B HO1  1 
HETATM 8202 H  H21  . EDO X  3 .   ? -50.95300 6.91000   14.42000  1.000 52.32264  ? 403 EDO B H21  1 
HETATM 8203 H  H22  . EDO X  3 .   ? -51.98800 5.48900   14.58900  1.000 52.32264  ? 403 EDO B H22  1 
HETATM 8204 H  HO2  . EDO X  3 .   ? -51.36600 5.54600   12.02300  1.000 51.28603  ? 403 EDO B HO2  1 
HETATM 8205 C  C1   . EDO Y  3 .   ? -27.35700 -25.46200 22.90000  1.000 49.61692  ? 404 EDO B C1   1 
HETATM 8206 O  O1   . EDO Y  3 .   ? -28.40400 -24.74800 23.56500  1.000 43.85324  ? 404 EDO B O1   1 
HETATM 8207 C  C2   . EDO Y  3 .   ? -27.54900 -26.93100 23.23900  1.000 51.68073  ? 404 EDO B C2   1 
HETATM 8208 O  O2   . EDO Y  3 .   ? -28.77600 -27.39200 22.65500  1.000 52.86564  ? 404 EDO B O2   1 
HETATM 8209 H  H11  . EDO Y  3 .   ? -26.38000 -25.11400 23.24000  1.000 59.54287  ? 404 EDO B H11  1 
HETATM 8210 H  H12  . EDO Y  3 .   ? -27.41200 -25.30700 21.82100  1.000 59.54287  ? 404 EDO B H12  1 
HETATM 8211 H  HO1  . EDO Y  3 .   ? -28.23600 -23.79800 23.50200  1.000 52.62645  ? 404 EDO B HO1  1 
HETATM 8212 H  H21  . EDO Y  3 .   ? -26.71100 -27.51500 22.85400  1.000 62.01944  ? 404 EDO B H21  1 
HETATM 8213 H  H22  . EDO Y  3 .   ? -27.58000 -27.06300 24.32300  1.000 62.01944  ? 404 EDO B H22  1 
HETATM 8214 H  HO2  . EDO Y  3 .   ? -28.83900 -28.35200 22.75300  1.000 63.44133  ? 404 EDO B HO2  1 
HETATM 8215 C  C1   . EDO Z  3 .   ? -36.48900 -9.34600  7.01700   1.000 53.40259  ? 405 EDO B C1   1 
HETATM 8216 O  O1   . EDO Z  3 .   ? -37.27000 -10.44900 6.54700   1.000 53.25118  ? 405 EDO B O1   1 
HETATM 8217 C  C2   . EDO Z  3 .   ? -36.43700 -9.48900  8.53300   1.000 52.21564  ? 405 EDO B C2   1 
HETATM 8218 O  O2   . EDO Z  3 .   ? -36.68700 -10.85800 8.88200   1.000 49.56535  ? 405 EDO B O2   1 
HETATM 8219 H  H11  . EDO Z  3 .   ? -35.48500 -9.37400  6.59000   1.000 64.08567  ? 405 EDO B H11  1 
HETATM 8220 H  H12  . EDO Z  3 .   ? -36.94900 -8.39700  6.73300   1.000 64.08567  ? 405 EDO B H12  1 
HETATM 8221 H  HO1  . EDO Z  3 .   ? -36.91300 -10.76200 5.70500   1.000 63.90397  ? 405 EDO B HO1  1 
HETATM 8222 H  H21  . EDO Z  3 .   ? -35.45700 -9.18200  8.90300   1.000 62.66133  ? 405 EDO B H21  1 
HETATM 8223 H  H22  . EDO Z  3 .   ? -37.18700 -8.84300  8.99400   1.000 62.66133  ? 405 EDO B H22  1 
HETATM 8224 H  HO2  . EDO Z  3 .   ? -35.87200 -11.36900 8.78600   1.000 59.48099  ? 405 EDO B HO2  1 
HETATM 8225 C  C1   . EDO AA 3 .   ? -58.17600 -6.24800  28.16700  0.950 49.62478  ? 406 EDO B C1   1 
HETATM 8226 O  O1   . EDO AA 3 .   ? -58.03700 -6.76600  29.43200  0.950 51.94047  ? 406 EDO B O1   1 
HETATM 8227 C  C2   . EDO AA 3 .   ? -59.56500 -5.95700  27.98100  0.950 48.64020  ? 406 EDO B C2   1 
HETATM 8228 O  O2   . EDO AA 3 .   ? -60.42500 -6.97600  28.38200  0.950 50.17222  ? 406 EDO B O2   1 
HETATM 8229 H  H11  . EDO AA 3 .   ? -57.87700 -6.90000  27.49900  0.950 59.55230  ? 406 EDO B H11  1 
HETATM 8230 H  H12  . EDO AA 3 .   ? -57.64800 -5.43100  28.08000  0.950 59.55230  ? 406 EDO B H12  1 
HETATM 8231 H  HO1  . EDO AA 3 .   ? -57.57700 -6.23400  29.90300  0.950 62.33113  ? 406 EDO B HO1  1 
HETATM 8232 H  H21  . EDO AA 3 .   ? -59.74400 -5.81500  27.05400  0.950 58.37081  ? 406 EDO B H21  1 
HETATM 8233 H  H22  . EDO AA 3 .   ? -59.78800 -5.13600  28.46700  0.950 58.37081  ? 406 EDO B H22  1 
HETATM 8234 H  HO2  . EDO AA 3 .   ? -60.60900 -6.88200  29.20200  0.950 60.20922  ? 406 EDO B HO2  1 
HETATM 8235 C  C1   . EDO BA 3 .   ? -41.82700 -0.56800  13.76200  1.000 60.26303  ? 407 EDO B C1   1 
HETATM 8236 O  O1   . EDO BA 3 .   ? -41.73800 -0.14400  15.13100  1.000 60.87521  ? 407 EDO B O1   1 
HETATM 8237 C  C2   . EDO BA 3 .   ? -43.24800 -1.00500  13.44900  1.000 58.28050  ? 407 EDO B C2   1 
HETATM 8238 O  O2   . EDO BA 3 .   ? -43.99200 0.17300   13.15700  1.000 56.47054  ? 407 EDO B O2   1 
HETATM 8239 H  H11  . EDO BA 3 .   ? -41.13800 -1.39700  13.58700  1.000 72.31820  ? 407 EDO B H11  1 
HETATM 8240 H  H12  . EDO BA 3 .   ? -41.53900 0.25300   13.10200  1.000 72.31820  ? 407 EDO B H12  1 
HETATM 8241 H  HO1  . EDO BA 3 .   ? -42.62800 -0.00100  15.48200  1.000 73.05282  ? 407 EDO B HO1  1 
HETATM 8242 H  H21  . EDO BA 3 .   ? -43.68300 -1.53000  14.30200  1.000 69.93917  ? 407 EDO B H21  1 
HETATM 8243 H  H22  . EDO BA 3 .   ? -43.25900 -1.68600  12.59500  1.000 69.93917  ? 407 EDO B H22  1 
HETATM 8244 H  HO2  . EDO BA 3 .   ? -44.93300 -0.04500  13.10000  1.000 67.76721  ? 407 EDO B HO2  1 
HETATM 8245 C  C1   . EDO CA 3 .   ? -52.52000 -8.80000  36.98500  1.000 37.63294  ? 408 EDO B C1   1 
HETATM 8246 O  O1   . EDO CA 3 .   ? -53.85300 -8.48500  37.40200  1.000 34.39394  ? 408 EDO B O1   1 
HETATM 8247 C  C2   . EDO CA 3 .   ? -51.75100 -7.60400  36.44200  1.000 39.52123  ? 408 EDO B C2   1 
HETATM 8248 O  O2   . EDO CA 3 .   ? -52.43200 -7.09100  35.30700  1.000 39.89505  ? 408 EDO B O2   1 
HETATM 8249 H  H11  . EDO CA 3 .   ? -52.56700 -9.56900  36.21200  1.000 45.16209  ? 408 EDO B H11  1 
HETATM 8250 H  H12  . EDO CA 3 .   ? -51.97500 -9.21300  37.83700  1.000 45.16209  ? 408 EDO B H12  1 
HETATM 8251 H  HO1  . EDO CA 3 .   ? -53.99000 -7.52900  37.34600  1.000 41.27529  ? 408 EDO B HO1  1 
HETATM 8252 H  H21  . EDO CA 3 .   ? -51.67200 -6.83100  37.21000  1.000 47.42803  ? 408 EDO B H21  1 
HETATM 8253 H  H22  . EDO CA 3 .   ? -50.73900 -7.90600  36.16500  1.000 47.42803  ? 408 EDO B H22  1 
HETATM 8254 H  HO2  . EDO CA 3 .   ? -51.97100 -6.30700  34.98100  1.000 47.87662  ? 408 EDO B HO2  1 
HETATM 8255 C  C1   . EDO DA 3 .   ? -37.43900 -9.81100  34.38500  1.000 59.93937  ? 409 EDO B C1   1 
HETATM 8256 O  O1   . EDO DA 3 .   ? -36.28000 -9.40300  33.64700  1.000 60.29282  ? 409 EDO B O1   1 
HETATM 8257 C  C2   . EDO DA 3 .   ? -38.62700 -8.96100  33.93400  1.000 58.60174  ? 409 EDO B C2   1 
HETATM 8258 O  O2   . EDO DA 3 .   ? -38.13100 -7.64800  33.62200  1.000 58.09544  ? 409 EDO B O2   1 
HETATM 8259 H  H11  . EDO DA 3 .   ? -37.26800 -9.67900  35.45600  1.000 71.92980  ? 409 EDO B H11  1 
HETATM 8260 H  H12  . EDO DA 3 .   ? -37.64500 -10.86800 34.20600  1.000 71.92980  ? 409 EDO B H12  1 
HETATM 8261 H  HO1  . EDO DA 3 .   ? -35.98800 -8.53500  33.95900  1.000 72.35394  ? 409 EDO B HO1  1 
HETATM 8262 H  H21  . EDO DA 3 .   ? -39.10000 -9.40600  33.05600  1.000 70.32466  ? 409 EDO B H21  1 
HETATM 8263 H  H22  . EDO DA 3 .   ? -39.37600 -8.90400  34.72700  1.000 70.32466  ? 409 EDO B H22  1 
HETATM 8264 H  HO2  . EDO DA 3 .   ? -37.67700 -7.67000  32.76900  1.000 69.71709  ? 409 EDO B HO2  1 
HETATM 8265 C  C1   . EDO EA 3 .   ? -57.77900 4.96600   11.05800  1.000 48.87866  ? 410 EDO B C1   1 
HETATM 8266 O  O1   . EDO EA 3 .   ? -57.93600 3.61800   11.52900  1.000 48.23778  ? 410 EDO B O1   1 
HETATM 8267 C  C2   . EDO EA 3 .   ? -57.83300 5.08200   9.53800   1.000 48.07385  ? 410 EDO B C2   1 
HETATM 8268 O  O2   . EDO EA 3 .   ? -58.49100 3.96100   8.94500   1.000 46.71660  ? 410 EDO B O2   1 
HETATM 8269 H  H11  . EDO EA 3 .   ? -58.56800 5.58500   11.48800  1.000 58.65695  ? 410 EDO B H11  1 
HETATM 8270 H  H12  . EDO EA 3 .   ? -56.82000 5.35300   11.40800  1.000 58.65695  ? 410 EDO B H12  1 
HETATM 8271 H  HO1  . EDO EA 3 .   ? -57.83300 3.59900   12.49000  1.000 57.88790  ? 410 EDO B HO1  1 
HETATM 8272 H  H21  . EDO EA 3 .   ? -56.81700 5.15300   9.14500   1.000 57.69118  ? 410 EDO B H21  1 
HETATM 8273 H  H22  . EDO EA 3 .   ? -58.36300 5.99600   9.26500   1.000 57.69118  ? 410 EDO B H22  1 
HETATM 8274 H  HO2  . EDO EA 3 .   ? -59.07600 4.26700   8.23900   1.000 56.06248  ? 410 EDO B HO2  1 
HETATM 8275 C  C1   . EDO FA 3 .   ? -39.31500 -31.14200 22.06200  0.544 35.67150  ? 411 EDO B C1   1 
HETATM 8276 O  O1   . EDO FA 3 .   ? -39.82600 -32.20300 22.78900  0.544 37.82061  ? 411 EDO B O1   1 
HETATM 8277 C  C2   . EDO FA 3 .   ? -40.29700 -30.07600 21.96700  0.544 34.25911  ? 411 EDO B C2   1 
HETATM 8278 O  O2   . EDO FA 3 .   ? -41.10700 -30.27700 20.86800  0.544 35.53676  ? 411 EDO B O2   1 
HETATM 8279 H  H11  . EDO FA 3 .   ? -39.07700 -31.44600 21.16100  0.544 42.80836  ? 411 EDO B H11  1 
HETATM 8280 H  H12  . EDO FA 3 .   ? -38.50800 -30.80300 22.50100  0.544 42.80836  ? 411 EDO B H12  1 
HETATM 8281 H  HO1  . EDO FA 3 .   ? -39.75600 -32.03700 23.61500  0.544 45.38729  ? 411 EDO B HO1  1 
HETATM 8282 H  H21  . EDO FA 3 .   ? -40.84400 -30.06200 22.78100  0.544 41.11349  ? 411 EDO B H21  1 
HETATM 8283 H  H22  . EDO FA 3 .   ? -39.83700 -29.21400 21.88400  0.544 41.11349  ? 411 EDO B H22  1 
HETATM 8284 H  HO2  . EDO FA 3 .   ? -40.81700 -30.93400 20.42200  0.544 42.64667  ? 411 EDO B HO2  1 
HETATM 8285 CL CL   . CL  GA 4 .   ? -49.03600 -30.53900 27.76600  1.000 40.41792  ? 412 CL  B CL   1 
HETATM 8286 O  O    . HOH HA 5 .   ? -8.21000  -37.83900 34.59600  1.000 47.81743  ? 501 HOH A O    1 
HETATM 8287 O  O    . HOH HA 5 .   ? -24.26300 -10.58500 36.17900  1.000 49.33935  ? 502 HOH A O    1 
HETATM 8288 O  O    . HOH HA 5 .   ? -25.22500 -39.12000 32.06700  1.000 46.37554  ? 503 HOH A O    1 
HETATM 8289 O  O    . HOH HA 5 .   ? 2.40400   -7.43900  17.33200  1.000 22.11874  ? 504 HOH A O    1 
HETATM 8290 O  O    . HOH HA 5 .   ? -26.55200 -29.11700 10.87800  1.000 33.25271  ? 505 HOH A O    1 
HETATM 8291 O  O    . HOH HA 5 .   ? -0.25000  -14.66200 8.67200   1.000 46.38377  ? 506 HOH A O    1 
HETATM 8292 O  O    . HOH HA 5 .   ? -14.31500 -35.24900 42.42800  1.000 45.73677  ? 507 HOH A O    1 
HETATM 8293 O  O    . HOH HA 5 .   ? -3.75300  -0.84700  24.08100  1.000 48.58667  ? 508 HOH A O    1 
HETATM 8294 O  O    . HOH HA 5 .   ? -3.74400  -14.17600 9.88700   1.000 32.06296  ? 509 HOH A O    1 
HETATM 8295 O  O    . HOH HA 5 .   ? -11.63900 -24.07200 49.21000  1.000 46.67740  ? 510 HOH A O    1 
HETATM 8296 O  O    . HOH HA 5 .   ? 4.94600   -24.76200 11.28300  1.000 32.25100  ? 511 HOH A O    1 
HETATM 8297 O  O    . HOH HA 5 .   ? -5.96600  -44.77400 21.88500  1.000 46.17282  ? 512 HOH A O    1 
HETATM 8298 O  O    . HOH HA 5 .   ? -22.20800 -24.81600 42.59700  1.000 35.02698  ? 513 HOH A O    1 
HETATM 8299 O  O    . HOH HA 5 .   ? -2.11300  -30.85600 7.54600   1.000 39.83322  ? 514 HOH A O    1 
HETATM 8300 O  O    . HOH HA 5 .   ? 7.13400   -22.03700 9.12600   1.000 44.25933  ? 515 HOH A O    1 
HETATM 8301 O  O    . HOH HA 5 .   ? -25.38600 -18.76700 20.28000  1.000 39.30214  ? 516 HOH A O    1 
HETATM 8302 O  O    . HOH HA 5 .   ? -17.54600 -17.56900 36.04100  1.000 18.67855  ? 517 HOH A O    1 
HETATM 8303 O  O    . HOH HA 5 .   ? -9.77500  0.01300   20.26300  1.000 38.16060  ? 518 HOH A O    1 
HETATM 8304 O  O    . HOH HA 5 .   ? -3.92400  -33.14200 16.93500  1.000 31.66912  ? 519 HOH A O    1 
HETATM 8305 O  O    . HOH HA 5 .   ? -26.90900 -25.32500 42.49700  1.000 36.93140  ? 520 HOH A O    1 
HETATM 8306 O  O    . HOH HA 5 .   ? 1.38600   -22.48500 37.82800  1.000 31.78707  ? 521 HOH A O    1 
HETATM 8307 O  O    . HOH HA 5 .   ? -10.760   -25.966   2.006     1.000 49.35539  ? 522 HOH A O    1 
HETATM 8308 O  O    . HOH HA 5 .   ? -32.68800 -24.33700 20.51000  1.000 26.51906  ? 523 HOH A O    1 
HETATM 8309 O  O    . HOH HA 5 .   ? 3.79400   -13.10000 6.60700   1.000 62.50539  ? 524 HOH A O    1 
HETATM 8310 O  O    . HOH HA 5 .   ? -6.19700  -39.77600 27.69600  1.000 28.80911  ? 525 HOH A O    1 
HETATM 8311 O  O    . HOH HA 5 .   ? 5.14700   -12.23000 13.19400  1.000 35.19006  ? 526 HOH A O    1 
HETATM 8312 O  O    . HOH HA 5 .   ? -26.71900 -20.04100 36.22000  1.000 20.70767  ? 527 HOH A O    1 
HETATM 8313 O  O    . HOH HA 5 .   ? -6.86200  -32.70100 31.17800  1.000 21.73441  ? 528 HOH A O    1 
HETATM 8314 O  O    . HOH HA 5 .   ? -20.02800 -19.70200 34.82200  1.000 16.43962  ? 529 HOH A O    1 
HETATM 8315 O  O    . HOH HA 5 .   ? -4.81600  -5.74800  11.39300  1.000 50.58189  ? 530 HOH A O    1 
HETATM 8316 O  O    . HOH HA 5 .   ? -14.19100 -12.61300 38.17000  1.000 22.25224  ? 531 HOH A O    1 
HETATM 8317 O  O    . HOH HA 5 .   ? -20.68000 -41.50400 34.30500  1.000 50.42675  ? 532 HOH A O    1 
HETATM 8318 O  O    . HOH HA 5 .   ? 1.24500   -27.35200 24.57500  1.000 21.92258  ? 533 HOH A O    1 
HETATM 8319 O  O    . HOH HA 5 .   ? -0.31800  -22.02900 32.96300  1.000 27.09749  ? 534 HOH A O    1 
HETATM 8320 O  O    . HOH HA 5 .   ? -2.96000  -21.83000 33.48100  1.000 17.80210  ? 535 HOH A O    1 
HETATM 8321 O  O    . HOH HA 5 .   ? -18.51100 -32.13200 44.72800  1.000 34.29448  ? 536 HOH A O    1 
HETATM 8322 O  O    . HOH HA 5 .   ? -2.13500  -33.80700 12.29700  1.000 58.24641  ? 537 HOH A O    1 
HETATM 8323 O  O    . HOH HA 5 .   ? -25.14500 -22.04900 10.46600  1.000 40.38329  ? 538 HOH A O    1 
HETATM 8324 O  O    . HOH HA 5 .   ? -12.68100 -3.06500  41.52600  1.000 47.89846  ? 539 HOH A O    1 
HETATM 8325 O  O    . HOH HA 5 .   ? 3.97800   -9.15800  16.74400  1.000 35.97091  ? 540 HOH A O    1 
HETATM 8326 O  O    . HOH HA 5 .   ? -24.75700 -20.21900 15.73100  1.000 25.57916  ? 541 HOH A O    1 
HETATM 8327 O  O    . HOH HA 5 .   ? -8.14500  -15.51600 4.64300   1.000 33.63341  ? 542 HOH A O    1 
HETATM 8328 O  O    . HOH HA 5 .   ? -25.58900 -36.69100 21.54500  1.000 49.28620  ? 543 HOH A O    1 
HETATM 8329 O  O    . HOH HA 5 .   ? -13.48900 -8.36400  11.58200  1.000 32.77689  ? 544 HOH A O    1 
HETATM 8330 O  O    . HOH HA 5 .   ? -18.20900 -14.13100 35.86300  1.000 18.58993  ? 545 HOH A O    1 
HETATM 8331 O  O    . HOH HA 5 .   ? -18.53300 -40.79800 15.18500  1.000 45.96217  ? 546 HOH A O    1 
HETATM 8332 O  O    . HOH HA 5 .   ? -10.44400 -40.90900 28.27800  1.000 26.05706  ? 547 HOH A O    1 
HETATM 8333 O  O    . HOH HA 5 .   ? -17.35100 -25.02400 6.97900   1.000 23.81334  ? 548 HOH A O    1 
HETATM 8334 O  O    . HOH HA 5 .   ? 5.75300   -12.46400 10.52800  1.000 58.21647  ? 549 HOH A O    1 
HETATM 8335 O  O    . HOH HA 5 .   ? -30.13100 -19.45900 33.36600  1.000 28.12193  ? 550 HOH A O    1 
HETATM 8336 O  O    . HOH HA 5 .   ? -10.45200 -1.38700  27.02100  1.000 35.73637  ? 551 HOH A O    1 
HETATM 8337 O  O    . HOH HA 5 .   ? -30.58200 -16.17400 30.36400  1.000 25.66013  ? 552 HOH A O    1 
HETATM 8338 O  O    . HOH HA 5 .   ? -14.55200 -43.60000 15.95400  1.000 34.98864  ? 553 HOH A O    1 
HETATM 8339 O  O    . HOH HA 5 .   ? -6.06200  -14.90300 38.78500  1.000 27.58804  ? 554 HOH A O    1 
HETATM 8340 O  O    . HOH HA 5 .   ? -14.85800 -37.93000 41.39800  1.000 43.74961  ? 555 HOH A O    1 
HETATM 8341 O  O    . HOH HA 5 .   ? -12.43900 -4.74300  36.45400  1.000 42.08450  ? 556 HOH A O    1 
HETATM 8342 O  O    . HOH HA 5 .   ? -14.50400 -2.16200  26.25800  1.000 32.40782  ? 557 HOH A O    1 
HETATM 8343 O  O    . HOH HA 5 .   ? -5.88700  -16.16300 35.44700  1.000 18.32215  ? 558 HOH A O    1 
HETATM 8344 O  O    . HOH HA 5 .   ? 6.14300   -15.80300 27.80900  1.000 43.19373  ? 559 HOH A O    1 
HETATM 8345 O  O    . HOH HA 5 .   ? -9.49800  -27.49700 47.17200  1.000 48.64428  ? 560 HOH A O    1 
HETATM 8346 O  O    . HOH HA 5 .   ? -23.95800 -39.86300 38.16100  1.000 41.50444  ? 561 HOH A O    1 
HETATM 8347 O  O    . HOH HA 5 .   ? -13.50100 -4.26000  33.98900  1.000 36.57419  ? 562 HOH A O    1 
HETATM 8348 O  O    . HOH HA 5 .   ? -7.20800  -23.26900 41.18100  1.000 21.11897  ? 563 HOH A O    1 
HETATM 8349 O  O    . HOH HA 5 .   ? 5.61800   -15.43200 24.46500  1.000 29.21046  ? 564 HOH A O    1 
HETATM 8350 O  O    . HOH HA 5 .   ? -1.40700  -43.87700 20.83600  1.000 40.68904  ? 565 HOH A O    1 
HETATM 8351 O  O    . HOH HA 5 .   ? -23.17300 -39.12700 27.19100  1.000 41.55589  ? 566 HOH A O    1 
HETATM 8352 O  O    . HOH HA 5 .   ? -3.19500  -31.50400 14.77300  1.000 34.48608  ? 567 HOH A O    1 
HETATM 8353 O  O    . HOH HA 5 .   ? -5.94500  -32.19300 13.67100  1.000 18.42300  ? 568 HOH A O    1 
HETATM 8354 O  O    . HOH HA 5 .   ? -11.69800 -42.59300 13.19400  1.000 30.18670  ? 569 HOH A O    1 
HETATM 8355 O  O    . HOH HA 5 .   ? -24.99200 -12.91900 13.25000  1.000 28.62311  ? 570 HOH A O    1 
HETATM 8356 O  O    . HOH HA 5 .   ? -18.61200 -25.40300 43.42500  1.000 36.75374  ? 571 HOH A O    1 
HETATM 8357 O  O    . HOH HA 5 .   ? -6.66800  -16.74100 3.13400   1.000 44.14906  ? 572 HOH A O    1 
HETATM 8358 O  O    . HOH HA 5 .   ? -7.28200  -16.21800 32.66300  1.000 16.94221  ? 573 HOH A O    1 
HETATM 8359 O  O    . HOH HA 5 .   ? -8.44600  -37.22200 19.27000  1.000 19.96085  ? 574 HOH A O    1 
HETATM 8360 O  O    . HOH HA 5 .   ? -22.81600 -21.43900 9.59900   1.000 26.65464  ? 575 HOH A O    1 
HETATM 8361 O  O    . HOH HA 5 .   ? 4.13500   -19.35100 36.19400  1.000 45.37209  ? 576 HOH A O    1 
HETATM 8362 O  O    . HOH HA 5 .   ? -4.46100  -6.77200  40.06200  1.000 53.26611  ? 577 HOH A O    1 
HETATM 8363 O  O    . HOH HA 5 .   ? -21.00200 -38.91600 19.57900  1.000 30.27132  ? 578 HOH A O    1 
HETATM 8364 O  O    . HOH HA 5 .   ? -22.70000 -21.75800 5.91300   1.000 36.47501  ? 579 HOH A O    1 
HETATM 8365 O  O    . HOH HA 5 .   ? -9.00400  -41.37200 22.05400  1.000 33.66833  ? 580 HOH A O    1 
HETATM 8366 O  O    . HOH HA 5 .   ? -0.56300  -32.17100 29.71400  1.000 50.52659  ? 581 HOH A O    1 
HETATM 8367 O  O    . HOH HA 5 .   ? -3.90700  -24.47900 33.39000  1.000 17.45951  ? 582 HOH A O    1 
HETATM 8368 O  O    . HOH HA 5 .   ? -5.64300  -22.74200 11.46500  1.000 18.36645  ? 583 HOH A O    1 
HETATM 8369 O  O    . HOH HA 5 .   ? -20.44100 -39.51000 15.02400  1.000 50.67543  ? 584 HOH A O    1 
HETATM 8370 O  O    . HOH HA 5 .   ? -18.59100 -43.54200 22.72900  1.000 31.64926  ? 585 HOH A O    1 
HETATM 8371 O  O    . HOH HA 5 .   ? -0.15600  -29.67300 23.22900  1.000 24.43213  ? 586 HOH A O    1 
HETATM 8372 O  O    . HOH HA 5 .   ? -0.68800  -17.88200 32.64400  1.000 17.55497  ? 587 HOH A O    1 
HETATM 8373 O  O    . HOH HA 5 .   ? -4.96700  -9.66100  7.08400   1.000 55.60468  ? 588 HOH A O    1 
HETATM 8374 O  O    . HOH HA 5 .   ? -34.35500 -21.59400 29.74600  1.000 26.46185  ? 589 HOH A O    1 
HETATM 8375 O  O    . HOH HA 5 .   ? -10.28500 -25.46000 4.94300   1.000 32.47831  ? 590 HOH A O    1 
HETATM 8376 O  O    . HOH HA 5 .   ? -8.46100  -38.56200 22.24100  1.000 21.25042  ? 591 HOH A O    1 
HETATM 8377 O  O    . HOH HA 5 .   ? -21.80800 -18.28200 36.45400  1.000 19.08843  ? 592 HOH A O    1 
HETATM 8378 O  O    . HOH HA 5 .   ? -2.23700  -28.00000 27.31900  1.000 21.22693  ? 593 HOH A O    1 
HETATM 8379 O  O    . HOH HA 5 .   ? -16.07100 -18.71500 3.27700   1.000 38.91025  ? 594 HOH A O    1 
HETATM 8380 O  O    . HOH HA 5 .   ? -2.32400  -23.57900 2.34800   1.000 52.83596  ? 595 HOH A O    1 
HETATM 8381 O  O    . HOH HA 5 .   ? -22.80900 -13.27600 18.34100  1.000 26.78095  ? 596 HOH A O    1 
HETATM 8382 O  O    . HOH HA 5 .   ? -5.73458  -16.96700 41.70105  0.50  27.09825  ? 597 HOH A O    1 
HETATM 8383 O  O    . HOH HA 5 .   ? -2.04100  -8.60300  25.28400  1.000 39.71956  ? 598 HOH A O    1 
HETATM 8384 O  O    . HOH HA 5 .   ? -24.03700 -36.18800 19.77200  1.000 35.56150  ? 599 HOH A O    1 
HETATM 8385 O  O    . HOH HA 5 .   ? -2.75300  -24.76800 18.97800  1.000 16.15989  ? 600 HOH A O    1 
HETATM 8386 O  O    . HOH HA 5 .   ? -10.56900 -43.37200 24.76100  1.000 43.19688  ? 601 HOH A O    1 
HETATM 8387 O  O    . HOH HA 5 .   ? -0.53800  -34.35100 20.45300  1.000 29.23893  ? 602 HOH A O    1 
HETATM 8388 O  O    . HOH HA 5 .   ? -7.37000  -41.35200 9.17000   1.000 46.39494  ? 603 HOH A O    1 
HETATM 8389 O  O    . HOH HA 5 .   ? -6.32300  -7.06100  10.27800  1.000 44.59208  ? 604 HOH A O    1 
HETATM 8390 O  O    . HOH HA 5 .   ? -28.88300 -22.40000 21.18000  1.000 30.28222  ? 605 HOH A O    1 
HETATM 8391 O  O    . HOH HA 5 .   ? -13.17700 -23.17800 2.38600   1.000 33.88738  ? 606 HOH A O    1 
HETATM 8392 O  O    . HOH HA 5 .   ? -13.96600 -17.12500 4.28000   1.000 34.90872  ? 607 HOH A O    1 
HETATM 8393 O  O    . HOH HA 5 .   ? 1.69900   -14.83600 27.00700  1.000 23.39364  ? 608 HOH A O    1 
HETATM 8394 O  O    . HOH HA 5 .   ? 0.08400   -20.57700 8.78500   1.000 20.01778  ? 609 HOH A O    1 
HETATM 8395 O  O    . HOH HA 5 .   ? 2.59200   -20.22600 32.55700  1.000 33.52364  ? 610 HOH A O    1 
HETATM 8396 O  O    . HOH HA 5 .   ? -4.71100  -4.28300  17.54500  1.000 38.08469  ? 611 HOH A O    1 
HETATM 8397 O  O    . HOH HA 5 .   ? -12.28800 -39.24300 39.70600  1.000 36.83994  ? 612 HOH A O    1 
HETATM 8398 O  O    . HOH HA 5 .   ? -28.60400 -29.16500 37.36800  1.000 39.18799  ? 613 HOH A O    1 
HETATM 8399 O  O    . HOH HA 5 .   ? -22.81800 -12.55100 24.01200  1.000 33.40969  ? 614 HOH A O    1 
HETATM 8400 O  O    . HOH HA 5 .   ? -21.23300 -14.78100 6.32000   1.000 45.10901  ? 615 HOH A O    1 
HETATM 8401 O  O    . HOH HA 5 .   ? -22.37700 -20.16200 1.25100   1.000 47.75552  ? 616 HOH A O    1 
HETATM 8402 O  O    . HOH HA 5 .   ? -4.56700  -27.68800 4.69000   1.000 35.27746  ? 617 HOH A O    1 
HETATM 8403 O  O    . HOH HA 5 .   ? -11.25400 -4.93900  15.58500  1.000 39.85889  ? 618 HOH A O    1 
HETATM 8404 O  O    . HOH HA 5 .   ? -23.57700 -25.36400 8.21100   1.000 32.04322  ? 619 HOH A O    1 
HETATM 8405 O  O    . HOH HA 5 .   ? -16.78400 -42.80800 34.67200  1.000 34.96821  ? 620 HOH A O    1 
HETATM 8406 O  O    . HOH HA 5 .   ? -11.49900 -8.85000  20.46200  1.000 29.52921  ? 621 HOH A O    1 
HETATM 8407 O  O    . HOH HA 5 .   ? 5.24400   -7.00200  23.57300  1.000 43.88028  ? 622 HOH A O    1 
HETATM 8408 O  O    . HOH HA 5 .   ? 7.36700   -12.55900 17.76100  1.000 41.56381  ? 623 HOH A O    1 
HETATM 8409 O  O    . HOH HA 5 .   ? -29.29600 -26.52600 36.60100  1.000 47.04733  ? 624 HOH A O    1 
HETATM 8410 O  O    . HOH HA 5 .   ? -3.41700  -21.90600 13.25600  1.000 17.15651  ? 625 HOH A O    1 
HETATM 8411 O  O    . HOH HA 5 .   ? -16.765   -18.228   -2.042    1.000 46.64537  ? 626 HOH A O    1 
HETATM 8412 O  O    . HOH HA 5 .   ? -22.30000 -22.49600 1.98400   1.000 39.37656  ? 627 HOH A O    1 
HETATM 8413 O  O    . HOH HA 5 .   ? -5.76500  -4.10400  34.75900  1.000 41.64385  ? 628 HOH A O    1 
HETATM 8414 O  O    . HOH HA 5 .   ? -19.392   -5.453    25.387    1.000 52.20442  ? 629 HOH A O    1 
HETATM 8415 O  O    . HOH HA 5 .   ? -9.90200  -37.07900 38.91000  1.000 47.22897  ? 630 HOH A O    1 
HETATM 8416 O  O    . HOH HA 5 .   ? -4.29200  -30.80800 34.32200  1.000 32.57211  ? 631 HOH A O    1 
HETATM 8417 O  O    . HOH HA 5 .   ? -17.07500 -42.33000 16.56100  1.000 37.90226  ? 632 HOH A O    1 
HETATM 8418 O  O    . HOH HA 5 .   ? -26.88200 -34.63900 16.59900  1.000 50.64031  ? 633 HOH A O    1 
HETATM 8419 O  O    . HOH HA 5 .   ? -11.889   -34.103   3.778     1.000 39.13716  ? 634 HOH A O    1 
HETATM 8420 O  O    . HOH HA 5 .   ? -18.68700 -14.47500 43.25900  1.000 42.53055  ? 635 HOH A O    1 
HETATM 8421 O  O    . HOH HA 5 .   ? -22.25400 -7.56800  33.45000  1.000 31.16809  ? 636 HOH A O    1 
HETATM 8422 O  O    . HOH HA 5 .   ? -4.49100  -30.70500 5.71400   1.000 35.24854  ? 637 HOH A O    1 
HETATM 8423 O  O    . HOH HA 5 .   ? 4.00400   -18.88600 30.19000  1.000 39.06039  ? 638 HOH A O    1 
HETATM 8424 O  O    . HOH HA 5 .   ? -25.08900 -8.53400  31.09200  1.000 44.53965  ? 639 HOH A O    1 
HETATM 8425 O  O    . HOH HA 5 .   ? -1.57100  -36.28000 22.44900  1.000 25.81019  ? 640 HOH A O    1 
HETATM 8426 O  O    . HOH HA 5 .   ? 2.81600   -16.44100 29.22400  1.000 23.50901  ? 641 HOH A O    1 
HETATM 8427 O  O    . HOH HA 5 .   ? -14.75100 -40.67300 38.95000  1.000 57.25699  ? 642 HOH A O    1 
HETATM 8428 O  O    . HOH HA 5 .   ? -1.75500  -38.82600 27.07400  1.000 42.19979  ? 643 HOH A O    1 
HETATM 8429 O  O    . HOH HA 5 .   ? -21.58600 -10.74300 7.19700   1.000 47.53119  ? 644 HOH A O    1 
HETATM 8430 O  O    . HOH HA 5 .   ? -18.43300 -5.11600  40.27000  1.000 50.64819  ? 645 HOH A O    1 
HETATM 8431 O  O    . HOH HA 5 .   ? -14.40700 -39.59900 11.69300  1.000 26.53166  ? 646 HOH A O    1 
HETATM 8432 O  O    . HOH HA 5 .   ? -0.39100  -29.95000 26.82600  1.000 40.75185  ? 647 HOH A O    1 
HETATM 8433 O  O    . HOH HA 5 .   ? -24.92200 -11.72000 33.74900  1.000 37.24670  ? 648 HOH A O    1 
HETATM 8434 O  O    . HOH HA 5 .   ? -20.20800 -42.03100 19.69000  1.000 35.74548  ? 649 HOH A O    1 
HETATM 8435 O  O    . HOH HA 5 .   ? -3.18800  -5.55400  36.33100  1.000 34.95413  ? 650 HOH A O    1 
HETATM 8436 O  O    . HOH HA 5 .   ? -23.06900 -42.67000 29.28200  1.000 40.24031  ? 651 HOH A O    1 
HETATM 8437 O  O    . HOH HA 5 .   ? -11.30000 -44.84300 30.49800  1.000 38.56495  ? 652 HOH A O    1 
HETATM 8438 O  O    . HOH HA 5 .   ? -13.02300 -15.36900 37.93200  1.000 18.58938  ? 653 HOH A O    1 
HETATM 8439 O  O    . HOH HA 5 .   ? 9.64400   -14.18900 20.40100  1.000 53.23224  ? 654 HOH A O    1 
HETATM 8440 O  O    . HOH HA 5 .   ? -30.51700 -38.52800 40.31600  1.000 38.28894  ? 655 HOH A O    1 
HETATM 8441 O  O    . HOH HA 5 .   ? 3.81900   -22.92000 30.99600  1.000 52.46640  ? 656 HOH A O    1 
HETATM 8442 O  O    . HOH HA 5 .   ? -30.71400 -29.21200 33.71200  1.000 36.40713  ? 657 HOH A O    1 
HETATM 8443 O  O    . HOH HA 5 .   ? -0.86800  -19.76500 6.23000   1.000 22.08581  ? 658 HOH A O    1 
HETATM 8444 O  O    . HOH HA 5 .   ? -9.94200  -33.47500 43.11900  1.000 32.78935  ? 659 HOH A O    1 
HETATM 8445 O  O    . HOH HA 5 .   ? 9.10500   -16.49400 13.92900  1.000 47.62722  ? 660 HOH A O    1 
HETATM 8446 O  O    . HOH HA 5 .   ? -9.50100  -29.92800 45.64600  1.000 45.23366  ? 661 HOH A O    1 
HETATM 8447 O  O    . HOH HA 5 .   ? -8.432    2.768     24.582    1.000 45.54282  ? 662 HOH A O    1 
HETATM 8448 O  O    . HOH HA 5 .   ? -33.88900 -21.90500 32.23400  1.000 28.17734  ? 663 HOH A O    1 
HETATM 8449 O  O    . HOH HA 5 .   ? -27.69000 -20.62700 40.51500  1.000 46.58852  ? 664 HOH A O    1 
HETATM 8450 O  O    . HOH HA 5 .   ? -29.80900 -26.71900 15.02100  1.000 38.81804  ? 665 HOH A O    1 
HETATM 8451 O  O    . HOH HA 5 .   ? -4.29300  -37.88800 27.71600  1.000 23.75847  ? 666 HOH A O    1 
HETATM 8452 O  O    . HOH HA 5 .   ? -21.02600 -8.05800  35.56000  1.000 40.37744  ? 667 HOH A O    1 
HETATM 8453 O  O    . HOH HA 5 .   ? -29.61400 -23.03700 36.43100  1.000 48.86268  ? 668 HOH A O    1 
HETATM 8454 O  O    . HOH HA 5 .   ? 1.24000   -12.15100 27.52000  1.000 33.80361  ? 669 HOH A O    1 
HETATM 8455 O  O    . HOH HA 5 .   ? -1.00700  -10.75400 26.50100  1.000 36.01248  ? 670 HOH A O    1 
HETATM 8456 O  O    . HOH HA 5 .   ? -20.84700 -37.09700 11.94100  1.000 37.26843  ? 671 HOH A O    1 
HETATM 8457 O  O    . HOH HA 5 .   ? -9.90800  -39.50400 31.01000  1.000 34.99834  ? 672 HOH A O    1 
HETATM 8458 O  O    . HOH HA 5 .   ? -16.22000 -37.68800 10.73800  1.000 24.70326  ? 673 HOH A O    1 
HETATM 8459 O  O    . HOH HA 5 .   ? -7.85600  -44.32400 19.39600  1.000 37.70292  ? 674 HOH A O    1 
HETATM 8460 O  O    . HOH HA 5 .   ? -18.69100 -45.85600 24.89900  1.000 32.92832  ? 675 HOH A O    1 
HETATM 8461 O  O    . HOH HA 5 .   ? -27.70700 -19.57800 22.02400  1.000 39.80964  ? 676 HOH A O    1 
HETATM 8462 O  O    . HOH HA 5 .   ? -20.79100 -7.21300  17.06100  1.000 43.98590  ? 677 HOH A O    1 
HETATM 8463 O  O    . HOH HA 5 .   ? -17.705   -4.827    23.928    1.000 32.33644  ? 678 HOH A O    1 
HETATM 8464 O  O    . HOH HA 5 .   ? -27.95200 -29.15900 34.04300  1.000 32.67168  ? 679 HOH A O    1 
HETATM 8465 O  O    . HOH HA 5 .   ? 11.11600  -16.01700 20.14200  1.000 47.39443  ? 680 HOH A O    1 
HETATM 8466 O  O    . HOH HA 5 .   ? -11.06300 -5.84900  12.97300  1.000 34.85896  ? 681 HOH A O    1 
HETATM 8467 O  O    . HOH HA 5 .   ? -25.73200 -18.63800 39.15700  1.000 45.70064  ? 682 HOH A O    1 
HETATM 8468 O  O    . HOH HA 5 .   ? -22.21900 -14.73800 42.14900  1.000 55.31257  ? 683 HOH A O    1 
HETATM 8469 O  O    . HOH HA 5 .   ? -19.16100 -17.98400 44.02000  1.000 42.49977  ? 684 HOH A O    1 
HETATM 8470 O  O    . HOH HA 5 .   ? 7.55200   -12.39900 22.40100  1.000 54.42827  ? 685 HOH A O    1 
HETATM 8471 O  O    . HOH HA 5 .   ? -2.80800  -29.13200 32.83900  1.000 39.95338  ? 686 HOH A O    1 
HETATM 8472 O  O    . HOH HA 5 .   ? -8.24300  -11.51500 5.95400   1.000 36.68375  ? 687 HOH A O    1 
HETATM 8473 O  O    . HOH HA 5 .   ? 0.15300   -12.47700 36.60100  1.000 41.11898  ? 688 HOH A O    1 
HETATM 8474 O  O    . HOH HA 5 .   ? 4.25900   -6.05100  17.78600  1.000 42.13606  ? 689 HOH A O    1 
HETATM 8475 O  O    . HOH HA 5 .   ? -7.32200  -44.28900 16.12200  1.000 38.47751  ? 690 HOH A O    1 
HETATM 8476 O  O    . HOH HA 5 .   ? -11.29400 -15.50600 3.50600   1.000 37.06155  ? 691 HOH A O    1 
HETATM 8477 O  O    . HOH HA 5 .   ? -29.96300 -40.17900 31.89800  1.000 64.42673  ? 692 HOH A O    1 
HETATM 8478 O  O    . HOH HA 5 .   ? -8.77200  -8.68700  41.64200  1.000 48.75260  ? 693 HOH A O    1 
HETATM 8479 O  O    . HOH HA 5 .   ? -19.12500 -5.43800  12.93800  1.000 50.87826  ? 694 HOH A O    1 
HETATM 8480 O  O    . HOH HA 5 .   ? -10.93100 -22.91000 3.03300   1.000 52.12478  ? 695 HOH A O    1 
HETATM 8481 O  O    . HOH HA 5 .   ? 6.34200   -13.59400 20.13600  1.000 34.97788  ? 696 HOH A O    1 
HETATM 8482 O  O    . HOH HA 5 .   ? -10.22400 -37.73100 41.04800  1.000 54.33707  ? 697 HOH A O    1 
HETATM 8483 O  O    . HOH HA 5 .   ? -27.12900 -30.93600 12.02800  1.000 54.57015  ? 698 HOH A O    1 
HETATM 8484 O  O    . HOH HA 5 .   ? 2.54800   -6.56500  15.02600  1.000 38.04962  ? 699 HOH A O    1 
HETATM 8485 O  O    . HOH HA 5 .   ? -6.95700  -30.28100 46.08600  1.000 41.87742  ? 700 HOH A O    1 
HETATM 8486 O  O    . HOH HA 5 .   ? -15.13600 -41.49400 12.73300  1.000 48.75558  ? 701 HOH A O    1 
HETATM 8487 O  O    . HOH HA 5 .   ? -3.467    -10.361   40.529    1.000 46.49705  ? 702 HOH A O    1 
HETATM 8488 O  O    . HOH HA 5 .   ? -29.33400 -27.84200 26.87600  1.000 48.82425  ? 703 HOH A O    1 
HETATM 8489 O  O    . HOH HA 5 .   ? -32.706   -37.460   38.745    1.000 49.66851  ? 704 HOH A O    1 
HETATM 8490 O  O    . HOH HA 5 .   ? -20.51100 -44.81300 22.42300  1.000 42.83963  ? 705 HOH A O    1 
HETATM 8491 O  O    . HOH HA 5 .   ? -1.47200  -33.45800 14.86900  1.000 53.56986  ? 706 HOH A O    1 
HETATM 8492 O  O    . HOH HA 5 .   ? -20.632   -38.177   44.463    1.000 48.81258  ? 707 HOH A O    1 
HETATM 8493 O  O    . HOH HA 5 .   ? -4.16500  -14.33600 7.00700   1.000 39.54200  ? 708 HOH A O    1 
HETATM 8494 O  O    . HOH HA 5 .   ? -29.85100 -38.30800 35.83700  1.000 56.47603  ? 709 HOH A O    1 
HETATM 8495 O  O    . HOH HA 5 .   ? -18.79700 -38.57100 11.08700  1.000 38.36127  ? 710 HOH A O    1 
HETATM 8496 O  O    . HOH HA 5 .   ? -7.01500  -14.94100 41.56800  1.000 37.55729  ? 711 HOH A O    1 
HETATM 8497 O  O    . HOH HA 5 .   ? 3.55400   -21.86600 7.10900   1.000 53.38506  ? 712 HOH A O    1 
HETATM 8498 O  O    . HOH HA 5 .   ? -22.21200 -10.24500 25.45600  1.000 51.63579  ? 713 HOH A O    1 
HETATM 8499 O  O    . HOH HA 5 .   ? -25.47000 -39.07100 23.80200  1.000 57.16818  ? 714 HOH A O    1 
HETATM 8500 O  O    . HOH HA 5 .   ? -26.93700 -20.42100 13.97800  1.000 41.34011  ? 715 HOH A O    1 
HETATM 8501 O  O    . HOH HA 5 .   ? 2.26800   -16.04200 34.13600  1.000 54.03289  ? 716 HOH A O    1 
HETATM 8502 O  O    . HOH HA 5 .   ? 7.69200   -21.44700 28.53300  1.000 48.24044  ? 717 HOH A O    1 
HETATM 8503 O  O    . HOH HA 5 .   ? -16.94000 -47.89400 24.96500  1.000 42.99162  ? 718 HOH A O    1 
HETATM 8504 O  O    . HOH HA 5 .   ? -5.86600  -34.57100 36.06200  1.000 57.77012  ? 719 HOH A O    1 
HETATM 8505 O  O    . HOH HA 5 .   ? -2.43400  -34.04500 31.52900  1.000 46.24855  ? 720 HOH A O    1 
HETATM 8506 O  O    . HOH HA 5 .   ? -29.08900 -19.07600 13.99700  1.000 44.89784  ? 721 HOH A O    1 
HETATM 8507 O  O    . HOH HA 5 .   ? -27.87500 -18.55800 37.99400  1.000 37.32193  ? 722 HOH A O    1 
HETATM 8508 O  O    . HOH HA 5 .   ? 1.934     -34.654   19.374    1.000 44.49827  ? 723 HOH A O    1 
HETATM 8509 O  O    . HOH HA 5 .   ? -4.98500  -34.60800 30.79800  1.000 25.88241  ? 724 HOH A O    1 
HETATM 8510 O  O    . HOH HA 5 .   ? -1.87500  -6.69700  10.29100  1.000 57.95357  ? 725 HOH A O    1 
HETATM 8511 O  O    . HOH HA 5 .   ? -17.22800 -4.42100  13.40400  1.000 55.98036  ? 726 HOH A O    1 
HETATM 8512 O  O    . HOH HA 5 .   ? -33.37000 -25.30900 29.52000  1.000 57.10230  ? 727 HOH A O    1 
HETATM 8513 O  O    . HOH HA 5 .   ? -16.62000 -3.54900  37.45100  1.000 55.25458  ? 728 HOH A O    1 
HETATM 8514 O  O    . HOH HA 5 .   ? -14.26600 -34.78800 7.23900   1.000 31.53117  ? 729 HOH A O    1 
HETATM 8515 O  O    . HOH HA 5 .   ? -6.874    0.082     17.866    1.000 56.79531  ? 730 HOH A O    1 
HETATM 8516 O  O    . HOH HA 5 .   ? 12.68100  -17.15100 22.11800  1.000 44.14097  ? 731 HOH A O    1 
HETATM 8517 O  O    . HOH HA 5 .   ? -20.53800 -16.02000 43.95100  1.000 52.68596  ? 732 HOH A O    1 
HETATM 8518 O  O    . HOH HA 5 .   ? -7.60700  -3.15600  30.16900  1.000 55.77957  ? 733 HOH A O    1 
HETATM 8519 O  O    . HOH HA 5 .   ? -23.55700 -38.84600 19.70100  1.000 45.08877  ? 734 HOH A O    1 
HETATM 8520 O  O    . HOH HA 5 .   ? -0.293    3.842     18.920    1.000 55.01592  ? 735 HOH A O    1 
HETATM 8521 O  O    . HOH HA 5 .   ? -4.35900  -37.21000 30.47000  1.000 40.97421  ? 736 HOH A O    1 
HETATM 8522 O  O    . HOH HA 5 .   ? -5.19000  -44.24000 14.62800  1.000 51.56576  ? 737 HOH A O    1 
HETATM 8523 O  O    . HOH HA 5 .   ? -13.07100 -44.75900 12.23400  1.000 56.43920  ? 738 HOH A O    1 
HETATM 8524 O  O    . HOH HA 5 .   ? -19.03000 -43.91600 33.04300  1.000 48.19528  ? 739 HOH A O    1 
HETATM 8525 O  O    . HOH HA 5 .   ? -3.790    -13.232   40.476    1.000 45.26177  ? 740 HOH A O    1 
HETATM 8526 O  O    . HOH HA 5 .   ? -31.70900 -27.41100 35.08900  1.000 49.11723  ? 741 HOH A O    1 
HETATM 8527 O  O    . HOH HA 5 .   ? -19.145   -44.706   16.481    1.000 61.06582  ? 742 HOH A O    1 
HETATM 8528 O  O    . HOH HA 5 .   ? -2.27600  -26.65400 33.74000  1.000 30.75518  ? 743 HOH A O    1 
HETATM 8529 O  O    . HOH HA 5 .   ? -20.15700 -3.91000  35.09300  1.000 55.42374  ? 744 HOH A O    1 
HETATM 8530 O  O    . HOH HA 5 .   ? 4.00700   -14.70200 30.65300  1.000 45.23597  ? 745 HOH A O    1 
HETATM 8531 O  O    . HOH HA 5 .   ? -31.73500 -29.68900 30.79400  1.000 43.48570  ? 746 HOH A O    1 
HETATM 8532 O  O    . HOH HA 5 .   ? -15.57200 -36.98300 8.06900   1.000 32.05634  ? 747 HOH A O    1 
HETATM 8533 O  O    . HOH HA 5 .   ? -29.36600 -12.12300 40.96000  1.000 59.90647  ? 748 HOH A O    1 
HETATM 8534 O  O    . HOH IA 5 .   ? -30.53200 -10.91600 22.36700  1.000 44.55847  ? 501 HOH B O    1 
HETATM 8535 O  O    . HOH IA 5 .   ? -53.84900 -23.27000 1.65000   1.000 48.01176  ? 502 HOH B O    1 
HETATM 8536 O  O    . HOH IA 5 .   ? -32.88100 -28.47100 19.21400  1.000 41.23946  ? 503 HOH B O    1 
HETATM 8537 O  O    . HOH IA 5 .   ? -53.53800 -17.63300 -5.18200  1.000 52.01256  ? 504 HOH B O    1 
HETATM 8538 O  O    . HOH IA 5 .   ? -62.80300 -6.61000  28.41700  1.000 53.52406  ? 505 HOH B O    1 
HETATM 8539 O  O    . HOH IA 5 .   ? -47.59200 1.55000   5.74000   1.000 24.91469  ? 506 HOH B O    1 
HETATM 8540 O  O    . HOH IA 5 .   ? -38.74400 -7.34100  -3.55700  1.000 43.22358  ? 507 HOH B O    1 
HETATM 8541 O  O    . HOH IA 5 .   ? -44.04500 -15.44600 39.11600  1.000 45.19079  ? 508 HOH B O    1 
HETATM 8542 O  O    . HOH IA 5 .   ? -49.71400 -28.21100 5.48100   1.000 34.25113  ? 509 HOH B O    1 
HETATM 8543 O  O    . HOH IA 5 .   ? -27.55400 -24.29500 25.95100  1.000 19.43019  ? 510 HOH B O    1 
HETATM 8544 O  O    . HOH IA 5 .   ? -37.41800 -9.26200  -0.04500  1.000 44.72359  ? 511 HOH B O    1 
HETATM 8545 O  O    . HOH IA 5 .   ? -34.10600 -7.14600  19.04900  1.000 28.16389  ? 512 HOH B O    1 
HETATM 8546 O  O    . HOH IA 5 .   ? -33.51800 -10.15600 9.11100   1.000 49.69671  ? 513 HOH B O    1 
HETATM 8547 O  O    . HOH IA 5 .   ? -64.418   6.395     19.279    1.000 21.36334  ? 514 HOH B O    1 
HETATM 8548 O  O    . HOH IA 5 .   ? -34.84600 -23.54400 -0.04000  1.000 53.07211  ? 515 HOH B O    1 
HETATM 8549 O  O    . HOH IA 5 .   ? -58.99500 -1.12100  14.41800  1.000 19.11986  ? 516 HOH B O    1 
HETATM 8550 O  O    . HOH IA 5 .   ? -45.82100 -18.72400 35.03400  1.000 30.52792  ? 517 HOH B O    1 
HETATM 8551 O  O    . HOH IA 5 .   ? -61.57300 -15.41600 29.75600  1.000 36.16300  ? 518 HOH B O    1 
HETATM 8552 O  O    . HOH IA 5 .   ? -48.29000 -13.90800 -4.32800  1.000 33.06564  ? 519 HOH B O    1 
HETATM 8553 O  O    . HOH IA 5 .   ? -58.82600 -10.42000 29.86300  1.000 28.70067  ? 520 HOH B O    1 
HETATM 8554 O  O    . HOH IA 5 .   ? -38.86500 -14.22500 -2.79100  1.000 55.67765  ? 521 HOH B O    1 
HETATM 8555 O  O    . HOH IA 5 .   ? -41.93800 -7.97900  34.00200  1.000 35.64661  ? 522 HOH B O    1 
HETATM 8556 O  O    . HOH IA 5 .   ? -53.23000 -29.60000 12.91000  1.000 55.74791  ? 523 HOH B O    1 
HETATM 8557 O  O    . HOH IA 5 .   ? -43.14200 2.64300   6.88800   1.000 31.32115  ? 524 HOH B O    1 
HETATM 8558 O  O    . HOH IA 5 .   ? -61.06100 -16.80300 25.90500  1.000 23.18574  ? 525 HOH B O    1 
HETATM 8559 O  O    . HOH IA 5 .   ? -56.32200 -15.03500 -3.54900  1.000 40.45846  ? 526 HOH B O    1 
HETATM 8560 O  O    . HOH IA 5 .   ? -63.14700 -12.08500 37.48500  1.000 40.87019  ? 527 HOH B O    1 
HETATM 8561 O  O    . HOH IA 5 .   ? -64.23600 -20.00500 26.39800  1.000 37.05454  ? 528 HOH B O    1 
HETATM 8562 O  O    . HOH IA 5 .   ? -41.59700 -2.27000  16.98700  1.000 35.18402  ? 529 HOH B O    1 
HETATM 8563 O  O    . HOH IA 5 .   ? -62.23900 -18.29200 16.93000  1.000 35.89429  ? 530 HOH B O    1 
HETATM 8564 O  O    . HOH IA 5 .   ? -61.02000 -16.39500 15.54200  1.000 21.64028  ? 531 HOH B O    1 
HETATM 8565 O  O    . HOH IA 5 .   ? -54.10300 -3.02900  11.09800  1.000 18.49545  ? 532 HOH B O    1 
HETATM 8566 O  O    . HOH IA 5 .   ? -53.70500 -21.96900 7.88200   1.000 25.43641  ? 533 HOH B O    1 
HETATM 8567 O  O    . HOH IA 5 .   ? -43.24400 -29.40500 6.73100   1.000 36.05645  ? 534 HOH B O    1 
HETATM 8568 O  O    . HOH IA 5 .   ? -34.41200 -2.79300  25.48100  1.000 30.99512  ? 535 HOH B O    1 
HETATM 8569 O  O    . HOH IA 5 .   ? -32.57900 -19.31200 31.99300  1.000 25.93194  ? 536 HOH B O    1 
HETATM 8570 O  O    . HOH IA 5 .   ? -56.37400 -20.34000 -0.89300  1.000 48.83823  ? 537 HOH B O    1 
HETATM 8571 O  O    . HOH IA 5 .   ? -41.02200 -9.32500  -6.61200  1.000 43.80372  ? 538 HOH B O    1 
HETATM 8572 O  O    . HOH IA 5 .   ? -58.77400 2.77600   22.82500  1.000 25.26096  ? 539 HOH B O    1 
HETATM 8573 O  O    . HOH IA 5 .   ? -60.90200 -14.97100 12.47400  1.000 31.38864  ? 540 HOH B O    1 
HETATM 8574 O  O    . HOH IA 5 .   ? -56.98800 -4.85300  1.45100   1.000 33.22977  ? 541 HOH B O    1 
HETATM 8575 O  O    . HOH IA 5 .   ? -51.07000 -3.41100  9.56100   1.000 16.94823  ? 542 HOH B O    1 
HETATM 8576 O  O    . HOH IA 5 .   ? -52.00900 -3.75400  32.95900  1.000 27.08917  ? 543 HOH B O    1 
HETATM 8577 O  O    . HOH IA 5 .   ? -45.32600 -1.19400  0.07400   1.000 41.80860  ? 544 HOH B O    1 
HETATM 8578 O  O    . HOH IA 5 .   ? -63.73800 0.16200   25.30600  1.000 23.25712  ? 545 HOH B O    1 
HETATM 8579 O  O    . HOH IA 5 .   ? -60.27800 -12.48200 27.90100  1.000 34.63780  ? 546 HOH B O    1 
HETATM 8580 O  O    . HOH IA 5 .   ? -47.43200 -5.30900  34.67600  1.000 36.25196  ? 547 HOH B O    1 
HETATM 8581 O  O    . HOH IA 5 .   ? -47.21000 -26.08000 2.63700   1.000 33.66316  ? 548 HOH B O    1 
HETATM 8582 O  O    . HOH IA 5 .   ? -44.82500 -3.39400  -1.77600  1.000 34.30061  ? 549 HOH B O    1 
HETATM 8583 O  O    . HOH IA 5 .   ? -45.19300 -29.06100 17.82000  1.000 48.07158  ? 550 HOH B O    1 
HETATM 8584 O  O    . HOH IA 5 .   ? -54.22900 -0.32000  13.26600  1.000 17.41232  ? 551 HOH B O    1 
HETATM 8585 O  O    . HOH IA 5 .   ? -35.09400 -31.39800 10.03700  1.000 35.99247  ? 552 HOH B O    1 
HETATM 8586 O  O    . HOH IA 5 .   ? -61.88700 -9.88600  17.00000  1.000 16.97473  ? 553 HOH B O    1 
HETATM 8587 O  O    . HOH IA 5 .   ? -66.85700 -11.51200 23.95100  1.000 42.17285  ? 554 HOH B O    1 
HETATM 8588 O  O    . HOH IA 5 .   ? -63.38700 -11.75800 8.04300   1.000 34.55337  ? 555 HOH B O    1 
HETATM 8589 O  O    . HOH IA 5 .   ? -45.79200 -25.85800 32.63500  1.000 27.45184  ? 556 HOH B O    1 
HETATM 8590 O  O    . HOH IA 5 .   ? -56.78700 0.22300   30.44800  1.000 33.38070  ? 557 HOH B O    1 
HETATM 8591 O  O    . HOH IA 5 .   ? -51.07700 -0.63200  8.91100   1.000 18.58805  ? 558 HOH B O    1 
HETATM 8592 O  O    . HOH IA 5 .   ? -62.322   8.280     16.378    1.000 44.44146  ? 559 HOH B O    1 
HETATM 8593 O  O    . HOH IA 5 .   ? -37.29100 -24.51900 0.85200   1.000 37.67585  ? 560 HOH B O    1 
HETATM 8594 O  O    . HOH IA 5 .   ? -58.09100 -26.57100 28.81000  1.000 52.53028  ? 561 HOH B O    1 
HETATM 8595 O  O    . HOH IA 5 .   ? -58.89300 -10.08100 17.99100  1.000 16.73295  ? 562 HOH B O    1 
HETATM 8596 O  O    . HOH IA 5 .   ? -60.96000 2.71400   21.10400  1.000 21.31966  ? 563 HOH B O    1 
HETATM 8597 O  O    . HOH IA 5 .   ? -44.77200 -17.60700 -5.68900  1.000 45.05406  ? 564 HOH B O    1 
HETATM 8598 O  O    . HOH IA 5 .   ? -48.26900 2.68800   24.81000  1.000 42.09312  ? 565 HOH B O    1 
HETATM 8599 O  O    . HOH IA 5 .   ? -49.034   -19.482   38.203    1.000 44.50641  ? 566 HOH B O    1 
HETATM 8600 O  O    . HOH IA 5 .   ? -63.54800 -20.08100 22.42700  1.000 33.98519  ? 567 HOH B O    1 
HETATM 8601 O  O    . HOH IA 5 .   ? -34.64000 -20.70500 5.01100   1.000 30.98073  ? 568 HOH B O    1 
HETATM 8602 O  O    . HOH IA 5 .   ? -41.98800 -28.01300 19.26400  1.000 24.24405  ? 569 HOH B O    1 
HETATM 8603 O  O    . HOH IA 5 .   ? -55.14400 -23.09700 15.32300  1.000 27.76473  ? 570 HOH B O    1 
HETATM 8604 O  O    . HOH IA 5 .   ? -65.66500 1.70000   18.74800  1.000 18.23563  ? 571 HOH B O    1 
HETATM 8605 O  O    . HOH IA 5 .   ? -68.055   -2.830    22.622    1.000 16.70647  ? 572 HOH B O    1 
HETATM 8606 O  O    . HOH IA 5 .   ? -38.62800 -18.60500 35.59200  1.000 39.69782  ? 573 HOH B O    1 
HETATM 8607 O  O    . HOH IA 5 .   ? -53.31400 -26.88500 17.47600  1.000 33.73050  ? 574 HOH B O    1 
HETATM 8608 O  O    . HOH IA 5 .   ? -59.46600 -17.54100 13.42100  1.000 19.67571  ? 575 HOH B O    1 
HETATM 8609 O  O    . HOH IA 5 .   ? -29.09700 -18.58800 11.04100  1.000 48.36175  ? 576 HOH B O    1 
HETATM 8610 O  O    . HOH IA 5 .   ? -52.62800 -4.83400  -7.61100  1.000 23.08597  ? 577 HOH B O    1 
HETATM 8611 O  O    . HOH IA 5 .   ? -43.20400 -22.71500 27.28500  1.000 22.12398  ? 578 HOH B O    1 
HETATM 8612 O  O    . HOH IA 5 .   ? -65.61700 -6.31400  5.79500   1.000 25.72181  ? 579 HOH B O    1 
HETATM 8613 O  O    . HOH IA 5 .   ? -41.31100 -28.92200 2.53500   1.000 42.12359  ? 580 HOH B O    1 
HETATM 8614 O  O    . HOH IA 5 .   ? -64.22300 -7.58500  15.41700  1.000 18.92884  ? 581 HOH B O    1 
HETATM 8615 O  O    . HOH IA 5 .   ? -62.81800 -15.36800 19.63000  1.000 20.21403  ? 582 HOH B O    1 
HETATM 8616 O  O    . HOH IA 5 .   ? -34.90900 -23.84200 27.78100  1.000 32.96200  ? 583 HOH B O    1 
HETATM 8617 O  O    . HOH IA 5 .   ? -53.13900 -6.25200  -4.95400  1.000 23.97700  ? 584 HOH B O    1 
HETATM 8618 O  O    . HOH IA 5 .   ? -54.42100 5.97800   9.83200   1.000 47.15895  ? 585 HOH B O    1 
HETATM 8619 O  O    . HOH IA 5 .   ? -44.60300 -27.71500 8.74400   1.000 27.45747  ? 586 HOH B O    1 
HETATM 8620 O  O    . HOH IA 5 .   ? -38.71000 -17.04900 -0.95000  1.000 43.86169  ? 587 HOH B O    1 
HETATM 8621 O  O    . HOH IA 5 .   ? -52.64600 -30.52300 8.12900   1.000 45.00780  ? 588 HOH B O    1 
HETATM 8622 O  O    . HOH IA 5 .   ? -38.75500 -4.59900  8.69600   1.000 24.31807  ? 589 HOH B O    1 
HETATM 8623 O  O    . HOH IA 5 .   ? -44.47400 -28.83400 20.14400  1.000 42.21730  ? 590 HOH B O    1 
HETATM 8624 O  O    . HOH IA 5 .   ? -58.31300 -23.04000 34.67300  1.000 48.40421  ? 591 HOH B O    1 
HETATM 8625 O  O    . HOH IA 5 .   ? -54.49800 -19.98400 -3.98200  1.000 36.01693  ? 592 HOH B O    1 
HETATM 8626 O  O    . HOH IA 5 .   ? -49.36400 -6.26000  29.23500  1.000 29.94673  ? 593 HOH B O    1 
HETATM 8627 O  O    . HOH IA 5 .   ? -38.55800 -0.85800  10.76800  1.000 40.26075  ? 594 HOH B O    1 
HETATM 8628 O  O    . HOH IA 5 .   ? -33.46800 -16.85300 5.72000   1.000 35.98259  ? 595 HOH B O    1 
HETATM 8629 O  O    . HOH IA 5 .   ? -30.74500 -18.74900 23.35800  1.000 34.65502  ? 596 HOH B O    1 
HETATM 8630 O  O    . HOH IA 5 .   ? -30.83300 -15.32900 17.20900  1.000 29.48190  ? 597 HOH B O    1 
HETATM 8631 O  O    . HOH IA 5 .   ? -42.91700 -27.85600 11.51000  1.000 24.56695  ? 598 HOH B O    1 
HETATM 8632 O  O    . HOH IA 5 .   ? -39.35500 -2.62600  22.89700  1.000 26.54601  ? 599 HOH B O    1 
HETATM 8633 O  O    . HOH IA 5 .   ? -46.12700 -22.94000 27.63400  1.000 21.57005  ? 600 HOH B O    1 
HETATM 8634 O  O    . HOH IA 5 .   ? -49.81100 -30.73000 12.95900  1.000 35.67356  ? 601 HOH B O    1 
HETATM 8635 O  O    . HOH IA 5 .   ? -36.85800 -3.33600  14.28600  1.000 40.21326  ? 602 HOH B O    1 
HETATM 8636 O  O    . HOH IA 5 .   ? -49.84200 -23.31200 22.45200  1.000 22.46986  ? 603 HOH B O    1 
HETATM 8637 O  O    . HOH IA 5 .   ? -51.12100 3.13500   2.59700   1.000 30.54550  ? 604 HOH B O    1 
HETATM 8638 O  O    . HOH IA 5 .   ? -57.64800 -17.62200 37.16300  1.000 34.75207  ? 605 HOH B O    1 
HETATM 8639 O  O    . HOH IA 5 .   ? -55.40500 -26.68700 24.43500  1.000 35.97657  ? 606 HOH B O    1 
HETATM 8640 O  O    . HOH IA 5 .   ? -67.44600 -10.47500 21.40700  1.000 27.69663  ? 607 HOH B O    1 
HETATM 8641 O  O    . HOH IA 5 .   ? -38.04500 -29.13100 28.27900  1.000 49.28988  ? 608 HOH B O    1 
HETATM 8642 O  O    . HOH IA 5 .   ? -62.97400 -22.41600 18.94200  1.000 47.21054  ? 609 HOH B O    1 
HETATM 8643 O  O    . HOH IA 5 .   ? -34.75500 -28.70200 6.52500   1.000 41.07972  ? 610 HOH B O    1 
HETATM 8644 O  O    . HOH IA 5 .   ? -47.35900 -27.30600 -1.85500  1.000 42.32001  ? 611 HOH B O    1 
HETATM 8645 O  O    . HOH IA 5 .   ? -33.15000 -5.97400  32.20100  1.000 42.98404  ? 612 HOH B O    1 
HETATM 8646 O  O    . HOH IA 5 .   ? -26.65000 -12.59700 15.41200  1.000 38.92703  ? 613 HOH B O    1 
HETATM 8647 O  O    . HOH IA 5 .   ? -60.76600 -21.19200 14.81500  1.000 47.40171  ? 614 HOH B O    1 
HETATM 8648 O  O    . HOH IA 5 .   ? -43.37600 -0.50200  19.49000  1.000 38.23072  ? 615 HOH B O    1 
HETATM 8649 O  O    . HOH IA 5 .   ? -58.93300 -4.39300  35.02300  1.000 34.68387  ? 616 HOH B O    1 
HETATM 8650 O  O    . HOH IA 5 .   ? -37.83200 -15.48400 0.31800   1.000 38.28782  ? 617 HOH B O    1 
HETATM 8651 O  O    . HOH IA 5 .   ? -33.08400 -28.12200 11.99400  1.000 29.54256  ? 618 HOH B O    1 
HETATM 8652 O  O    . HOH IA 5 .   ? -55.41600 -26.40500 27.12000  1.000 32.82967  ? 619 HOH B O    1 
HETATM 8653 O  O    . HOH IA 5 .   ? -46.48100 -14.67800 -7.93800  1.000 51.07348  ? 620 HOH B O    1 
HETATM 8654 O  O    . HOH IA 5 .   ? -30.79800 -18.26000 15.98900  1.000 30.43422  ? 621 HOH B O    1 
HETATM 8655 O  O    . HOH IA 5 .   ? -37.87100 -5.62100  4.93800   1.000 43.96317  ? 622 HOH B O    1 
HETATM 8656 O  O    . HOH IA 5 .   ? -66.40900 -4.09900  25.08000  1.000 22.67901  ? 623 HOH B O    1 
HETATM 8657 O  O    . HOH IA 5 .   ? -67.72400 -13.82700 17.68200  1.000 31.68107  ? 624 HOH B O    1 
HETATM 8658 O  O    . HOH IA 5 .   ? -38.01400 -30.77000 25.83800  1.000 42.83212  ? 625 HOH B O    1 
HETATM 8659 O  O    . HOH IA 5 .   ? -39.14300 -19.17700 -4.37800  1.000 48.34099  ? 626 HOH B O    1 
HETATM 8660 O  O    . HOH IA 5 .   ? -64.33400 -19.22800 19.57300  1.000 41.27334  ? 627 HOH B O    1 
HETATM 8661 O  O    . HOH IA 5 .   ? -63.16500 -14.04600 33.67900  1.000 38.79006  ? 628 HOH B O    1 
HETATM 8662 O  O    . HOH IA 5 .   ? -51.61600 6.07600   17.76100  1.000 32.45637  ? 629 HOH B O    1 
HETATM 8663 O  O    . HOH IA 5 .   ? -55.75800 -26.03200 21.23900  1.000 43.13553  ? 630 HOH B O    1 
HETATM 8664 O  O    . HOH IA 5 .   ? -59.03300 -3.90700  13.29800  1.000 18.92398  ? 631 HOH B O    1 
HETATM 8665 O  O    . HOH IA 5 .   ? -55.72000 -26.27500 19.01900  1.000 45.74769  ? 632 HOH B O    1 
HETATM 8666 O  O    . HOH IA 5 .   ? -39.50100 -1.96400  33.14600  1.000 47.02034  ? 633 HOH B O    1 
HETATM 8667 O  O    . HOH IA 5 .   ? -63.86400 -12.75400 5.47100   1.000 25.27279  ? 634 HOH B O    1 
HETATM 8668 O  O    . HOH IA 5 .   ? -40.38900 -15.62400 37.33600  1.000 38.13719  ? 635 HOH B O    1 
HETATM 8669 O  O    . HOH IA 5 .   ? -51.55900 -28.28300 7.54700   1.000 27.56227  ? 636 HOH B O    1 
HETATM 8670 O  O    . HOH IA 5 .   ? -58.14000 -21.48900 8.15800   1.000 48.05974  ? 637 HOH B O    1 
HETATM 8671 O  O    . HOH IA 5 .   ? -54.50400 -31.99400 28.23500  1.000 54.79629  ? 638 HOH B O    1 
HETATM 8672 O  O    . HOH IA 5 .   ? -59.14400 -21.83200 32.26900  1.000 48.50441  ? 639 HOH B O    1 
HETATM 8673 O  O    . HOH IA 5 .   ? -41.58700 -33.17100 6.95200   1.000 43.31232  ? 640 HOH B O    1 
HETATM 8674 O  O    . HOH IA 5 .   ? -29.77500 -14.50300 7.27600   1.000 53.82786  ? 641 HOH B O    1 
HETATM 8675 O  O    . HOH IA 5 .   ? -62.97300 -17.87300 23.94300  1.000 24.70362  ? 642 HOH B O    1 
HETATM 8676 O  O    . HOH IA 5 .   ? -32.47100 -26.59900 -0.37000  1.000 45.15002  ? 643 HOH B O    1 
HETATM 8677 O  O    . HOH IA 5 .   ? -50.84100 -31.05300 30.27100  1.000 56.05591  ? 644 HOH B O    1 
HETATM 8678 O  O    . HOH IA 5 .   ? -67.03900 -8.91600  13.93300  1.000 35.57641  ? 645 HOH B O    1 
HETATM 8679 O  O    . HOH IA 5 .   ? -60.11400 -16.51300 -1.01500  1.000 29.47598  ? 646 HOH B O    1 
HETATM 8680 O  O    . HOH IA 5 .   ? -35.93700 -16.66300 35.09600  1.000 35.22176  ? 647 HOH B O    1 
HETATM 8681 O  O    . HOH IA 5 .   ? -60.47600 -26.11000 24.52200  1.000 33.01842  ? 648 HOH B O    1 
HETATM 8682 O  O    . HOH IA 5 .   ? -41.19200 -0.61400  28.35000  1.000 45.04821  ? 649 HOH B O    1 
HETATM 8683 O  O    . HOH IA 5 .   ? -31.53600 -25.80900 13.04100  1.000 31.12554  ? 650 HOH B O    1 
HETATM 8684 O  O    . HOH IA 5 .   ? -53.84400 5.55600   16.32100  1.000 35.94858  ? 651 HOH B O    1 
HETATM 8685 O  O    . HOH IA 5 .   ? -39.58700 -26.92500 1.24400   1.000 32.58505  ? 652 HOH B O    1 
HETATM 8686 O  O    . HOH IA 5 .   ? -44.78600 -7.30100  35.81500  1.000 36.36817  ? 653 HOH B O    1 
HETATM 8687 O  O    . HOH IA 5 .   ? -43.56400 -25.53900 34.46900  1.000 28.93164  ? 654 HOH B O    1 
HETATM 8688 O  O    . HOH IA 5 .   ? -43.35500 10.48400  20.85100  1.000 57.03677  ? 655 HOH B O    1 
HETATM 8689 O  O    . HOH IA 5 .   ? -55.58900 -25.53400 15.01100  1.000 46.31097  ? 656 HOH B O    1 
HETATM 8690 O  O    . HOH IA 5 .   ? -59.87800 -2.24300  28.54900  1.000 49.80374  ? 657 HOH B O    1 
HETATM 8691 O  O    . HOH IA 5 .   ? -67.19100 -12.62100 14.78800  1.000 28.85498  ? 658 HOH B O    1 
HETATM 8692 O  O    . HOH IA 5 .   ? -38.19700 -20.66700 36.42700  1.000 48.32224  ? 659 HOH B O    1 
HETATM 8693 O  O    . HOH IA 5 .   ? -33.51100 -15.75800 3.55100   1.000 50.14898  ? 660 HOH B O    1 
HETATM 8694 O  O    . HOH IA 5 .   ? -50.05900 -24.36800 2.02800   1.000 46.88722  ? 661 HOH B O    1 
HETATM 8695 O  O    . HOH IA 5 .   ? -31.81900 -23.36600 7.91600   1.000 48.19544  ? 662 HOH B O    1 
HETATM 8696 O  O    . HOH IA 5 .   ? -64.725   -0.628    29.681    1.000 49.30096  ? 663 HOH B O    1 
HETATM 8697 O  O    . HOH IA 5 .   ? -31.46600 -8.74300  30.11600  1.000 48.33020  ? 664 HOH B O    1 
HETATM 8698 O  O    . HOH IA 5 .   ? -59.30600 -14.92500 38.30400  1.000 38.64296  ? 665 HOH B O    1 
HETATM 8699 O  O    . HOH IA 5 .   ? -47.07200 -20.66400 -5.10800  1.000 41.48740  ? 666 HOH B O    1 
HETATM 8700 O  O    . HOH IA 5 .   ? -63.23100 -13.02800 -0.06900  1.000 41.18647  ? 667 HOH B O    1 
HETATM 8701 O  O    . HOH IA 5 .   ? -34.24800 -23.20800 3.25800   1.000 40.69060  ? 668 HOH B O    1 
HETATM 8702 O  O    . HOH IA 5 .   ? -44.09100 -28.73700 3.22400   1.000 48.86539  ? 669 HOH B O    1 
HETATM 8703 O  O    . HOH IA 5 .   ? -58.00600 4.69500   1.13500   1.000 57.24709  ? 670 HOH B O    1 
HETATM 8704 O  O    . HOH IA 5 .   ? -66.09400 -9.61500  8.99600   1.000 44.33985  ? 671 HOH B O    1 
HETATM 8705 O  O    . HOH IA 5 .   ? -40.68100 -14.09400 -4.25300  1.000 45.38831  ? 672 HOH B O    1 
HETATM 8706 O  O    . HOH IA 5 .   ? -46.41100 -11.66400 38.26100  1.000 45.30608  ? 673 HOH B O    1 
HETATM 8707 O  O    . HOH IA 5 .   ? -62.16500 -14.09100 9.74500   1.000 39.03670  ? 674 HOH B O    1 
HETATM 8708 O  O    . HOH IA 5 .   ? -36.56700 -6.45900  9.93900   1.000 54.65557  ? 675 HOH B O    1 
HETATM 8709 O  O    . HOH IA 5 .   ? -52.56200 2.60400   28.33100  1.000 45.64528  ? 676 HOH B O    1 
HETATM 8710 O  O    . HOH IA 5 .   ? -48.57200 1.78600   27.43100  1.000 39.67252  ? 677 HOH B O    1 
HETATM 8711 O  O    . HOH IA 5 .   ? -33.73900 -16.43200 32.54000  1.000 43.63778  ? 678 HOH B O    1 
HETATM 8712 O  O    . HOH IA 5 .   ? -32.50000 -3.11300  30.74200  1.000 50.54054  ? 679 HOH B O    1 
HETATM 8713 O  O    . HOH IA 5 .   ? -49.01500 4.11000   5.90400   1.000 43.67347  ? 680 HOH B O    1 
HETATM 8714 O  O    . HOH IA 5 .   ? -60.73400 -22.14000 30.62200  1.000 55.16738  ? 681 HOH B O    1 
HETATM 8715 O  O    . HOH IA 5 .   ? -57.56400 -3.43900  -0.21000  1.000 51.45030  ? 682 HOH B O    1 
HETATM 8716 O  O    . HOH IA 5 .   ? -38.22100 -25.88000 -1.84000  1.000 41.87209  ? 683 HOH B O    1 
HETATM 8717 O  O    . HOH IA 5 .   ? -49.27700 -16.04000 -3.85300  1.000 41.73047  ? 684 HOH B O    1 
HETATM 8718 O  O    . HOH IA 5 .   ? -57.706   6.181     13.498    1.000 64.53078  ? 685 HOH B O    1 
HETATM 8719 O  O    . HOH IA 5 .   ? -50.73400 -23.88600 -0.19900  1.000 49.29446  ? 686 HOH B O    1 
HETATM 8720 O  O    . HOH IA 5 .   ? -50.14600 -30.72600 15.93000  1.000 51.44940  ? 687 HOH B O    1 
HETATM 8721 O  O    . HOH IA 5 .   ? -32.30500 -14.74400 32.49100  1.000 46.17110  ? 688 HOH B O    1 
HETATM 8722 O  O    . HOH IA 5 .   ? -62.287   -4.568    -3.198    1.000 50.80053  ? 689 HOH B O    1 
HETATM 8723 O  O    . HOH IA 5 .   ? -58.58200 -21.52000 10.88100  1.000 48.09297  ? 690 HOH B O    1 
HETATM 8724 O  O    . HOH IA 5 .   ? -27.58200 -12.05200 24.38300  1.000 45.54090  ? 691 HOH B O    1 
HETATM 8725 O  O    . HOH IA 5 .   ? -41.78500 2.40200   10.82300  1.000 51.38184  ? 692 HOH B O    1 
HETATM 8726 O  O    . HOH IA 5 .   ? -57.91800 -0.68100  32.81100  1.000 42.47309  ? 693 HOH B O    1 
HETATM 8727 O  O    . HOH IA 5 .   ? -31.24800 -15.87300 19.88000  1.000 39.16450  ? 694 HOH B O    1 
HETATM 8728 O  O    . HOH IA 5 .   ? -31.07400 -18.50700 21.05000  1.000 33.03132  ? 695 HOH B O    1 
HETATM 8729 O  O    . HOH IA 5 .   ? -28.39900 -12.91600 20.09100  1.000 50.64373  ? 696 HOH B O    1 
HETATM 8730 O  O    . HOH IA 5 .   ? -66.261   -15.121   21.228    1.000 50.33447  ? 697 HOH B O    1 
HETATM 8731 O  O    . HOH IA 5 .   ? -59.27400 -8.34900  32.97500  1.000 46.52012  ? 698 HOH B O    1 
HETATM 8732 O  O    . HOH IA 5 .   ? -49.71000 0.28800   33.12900  1.000 41.36614  ? 699 HOH B O    1 
HETATM 8733 O  O    . HOH IA 5 .   ? -55.08900 -15.97000 -5.56500  1.000 55.93510  ? 700 HOH B O    1 
HETATM 8734 O  O    . HOH IA 5 .   ? -57.51000 -22.45900 4.48200   1.000 57.62305  ? 701 HOH B O    1 
HETATM 8735 O  O    . HOH IA 5 .   ? -29.82600 -24.09700 10.98600  1.000 49.82885  ? 702 HOH B O    1 
HETATM 8736 O  O    . HOH IA 5 .   ? -45.52100 1.34000   21.05200  1.000 53.71055  ? 703 HOH B O    1 
HETATM 8737 O  O    . HOH IA 5 .   ? -65.97200 -6.39000  13.66300  1.000 23.15469  ? 704 HOH B O    1 
HETATM 8738 O  O    . HOH IA 5 .   ? -35.07500 -0.91000  23.76600  1.000 56.53641  ? 705 HOH B O    1 
HETATM 8739 O  O    . HOH IA 5 .   ? -56.41800 -25.43900 8.38100   1.000 48.76498  ? 706 HOH B O    1 
HETATM 8740 O  O    . HOH IA 5 .   ? -43.43100 -19.77000 36.35700  1.000 41.72240  ? 707 HOH B O    1 
HETATM 8741 O  O    . HOH IA 5 .   ? -69.296   -10.300   24.954    1.000 52.60331  ? 708 HOH B O    1 
HETATM 8742 O  O    . HOH IA 5 .   ? -36.41300 -25.07800 36.14200  1.000 56.18703  ? 709 HOH B O    1 
HETATM 8743 O  O    . HOH IA 5 .   ? -61.78500 -14.11800 27.32800  1.000 47.84572  ? 710 HOH B O    1 
HETATM 8744 O  O    . HOH IA 5 .   ? -37.20500 -2.27900  9.17500   1.000 49.30946  ? 711 HOH B O    1 
HETATM 8745 O  O    . HOH IA 5 .   ? -54.08000 -24.56800 7.58900   1.000 36.11703  ? 712 HOH B O    1 
HETATM 8746 O  O    . HOH IA 5 .   ? -43.46500 4.47700   5.25600   1.000 56.90362  ? 713 HOH B O    1 
HETATM 8747 O  O    . HOH IA 5 .   ? -28.58400 -11.42600 11.67500  1.000 51.19338  ? 714 HOH B O    1 
HETATM 8748 O  O    . HOH IA 5 .   ? -31.40500 -3.43600  25.15700  1.000 53.57618  ? 715 HOH B O    1 
HETATM 8749 O  O    . HOH IA 5 .   ? -54.43700 5.58900   4.95300   1.000 60.16173  ? 716 HOH B O    1 
HETATM 8750 O  O    . HOH IA 5 .   ? -53.10300 -26.35500 6.09900   1.000 48.67193  ? 717 HOH B O    1 
HETATM 8751 O  O    . HOH IA 5 .   ? -70.097   -9.453    21.935    1.000 30.46571  ? 718 HOH B O    1 
HETATM 8752 O  O    . HOH IA 5 .   ? -32.11200 -30.25900 20.97300  1.000 55.56712  ? 719 HOH B O    1 
HETATM 8753 O  O    . HOH IA 5 .   ? -51.83500 -32.89800 27.24400  1.000 59.06609  ? 720 HOH B O    1 
HETATM 8754 O  O    . HOH IA 5 .   ? -67.32100 -14.72900 12.67700  1.000 50.92787  ? 721 HOH B O    1 
HETATM 8755 O  O    . HOH IA 5 .   ? -30.10200 -13.91700 36.44400  1.000 61.17601  ? 722 HOH B O    1 
HETATM 8756 O  O    . HOH IA 5 .   ? -41.38900 -2.29600  34.31400  1.000 55.78042  ? 723 HOH B O    1 
HETATM 8757 O  O    . HOH IA 5 .   ? -60.492   1.742     25.058    1.000 42.08710  ? 724 HOH B O    1 
HETATM 8758 O  O    . HOH IA 5 .   ? -34.80500 -12.85100 36.21000  1.000 54.83388  ? 725 HOH B O    1 
HETATM 8759 O  O    . HOH IA 5 .   ? -60.25000 -19.84800 12.36800  1.000 43.59204  ? 726 HOH B O    1 
HETATM 8760 O  O    . HOH IA 5 .   ? -34.33000 -28.40300 26.26900  1.000 50.76681  ? 727 HOH B O    1 
HETATM 8761 O  O    . HOH IA 5 .   ? -52.67300 -29.34500 16.49200  1.000 51.41802  ? 728 HOH B O    1 
HETATM 8762 O  O    . HOH IA 5 .   ? -60.46200 -18.00700 5.70700   1.000 51.56993  ? 729 HOH B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . GLY A  42  ? 0.91393 0.82642 0.86530 0.03656  0.03879  -0.04241 42  GLY A N   
2    C  CA  . GLY A  42  ? 0.75587 0.67448 0.70395 0.03814  0.03671  -0.03859 42  GLY A CA  
3    C  C   . GLY A  42  ? 0.60453 0.52833 0.55057 0.03571  0.03178  -0.03441 42  GLY A C   
4    O  O   . GLY A  42  ? 0.54849 0.47843 0.48932 0.03272  0.02946  -0.03520 42  GLY A O   
7    N  N   . TYR A  43  ? 0.43859 0.35983 0.38861 0.03692  0.03034  -0.03020 43  TYR A N   
8    C  CA  . TYR A  43  ? 0.37703 0.30269 0.32557 0.03516  0.02587  -0.02584 43  TYR A CA  
9    C  C   . TYR A  43  ? 0.31800 0.24335 0.26786 0.03105  0.02408  -0.02726 43  TYR A C   
10   O  O   . TYR A  43  ? 0.32309 0.25260 0.27155 0.02917  0.02028  -0.02405 43  TYR A O   
11   C  CB  . TYR A  43  ? 0.29722 0.22098 0.24889 0.03960  0.02512  -0.01934 43  TYR A CB  
12   C  CG  . TYR A  43  ? 0.28961 0.21353 0.24061 0.04386  0.02663  -0.01721 43  TYR A CG  
13   C  CD1 . TYR A  43  ? 0.31023 0.24007 0.25597 0.04326  0.02522  -0.01677 43  TYR A CD1 
14   C  CD2 . TYR A  43  ? 0.31773 0.23591 0.27345 0.04863  0.02947  -0.01537 43  TYR A CD2 
15   C  CE1 . TYR A  43  ? 0.30130 0.23160 0.24666 0.04704  0.02639  -0.01446 43  TYR A CE1 
16   C  CE2 . TYR A  43  ? 0.33275 0.25140 0.28808 0.05252  0.03061  -0.01309 43  TYR A CE2 
17   C  CZ  . TYR A  43  ? 0.33110 0.25587 0.28134 0.05174  0.02913  -0.01269 43  TYR A CZ  
18   O  OH  . TYR A  43  ? 0.35006 0.27560 0.30003 0.05544  0.03020  -0.01036 43  TYR A OH  
28   N  N   . ALA A  44  ? 0.31725 0.23805 0.26946 0.02939  0.02671  -0.03217 44  ALA A N   
29   C  CA  . ALA A  44  ? 0.31359 0.23391 0.26755 0.02546  0.02512  -0.03346 44  ALA A CA  
30   C  C   . ALA A  44  ? 0.33252 0.25967 0.28107 0.02019  0.02193  -0.03581 44  ALA A C   
31   O  O   . ALA A  44  ? 0.35617 0.28612 0.29999 0.01871  0.02258  -0.03946 44  ALA A O   
32   C  CB  . ALA A  44  ? 0.33703 0.25048 0.29435 0.02476  0.02889  -0.03849 44  ALA A CB  
38   N  N   . ARG A  45  ? 0.31861 0.24850 0.26786 0.01736  0.01858  -0.03381 45  ARG A N   
39   C  CA  . ARG A  45  ? 0.34929 0.28559 0.29382 0.01222  0.01536  -0.03589 45  ARG A CA  
40   C  C   . ARG A  45  ? 0.31995 0.25616 0.26748 0.00863  0.01355  -0.03631 45  ARG A C   
41   O  O   . ARG A  45  ? 0.30293 0.23541 0.25591 0.01036  0.01390  -0.03342 45  ARG A O   
42   C  CB  . ARG A  45  ? 0.45899 0.40202 0.39885 0.01278  0.01200  -0.03171 45  ARG A CB  
43   C  CG  . ARG A  45  ? 0.37706 0.32067 0.31946 0.01547  0.00967  -0.02489 45  ARG A CG  
44   C  CD  . ARG A  45  ? 0.37540 0.32527 0.31269 0.01600  0.00637  -0.02071 45  ARG A CD  
45   N  NE  . ARG A  45  ? 0.34191 0.29214 0.27619 0.01883  0.00791  -0.02035 45  ARG A NE  
46   C  CZ  . ARG A  45  ? 0.37156 0.32635 0.30003 0.01704  0.00738  -0.02258 45  ARG A CZ  
47   N  NH1 . ARG A  45  ? 0.39973 0.35883 0.32434 0.01223  0.00564  -0.02613 45  ARG A NH1 
48   N  NH2 . ARG A  45  ? 0.36843 0.32359 0.29486 0.02003  0.00867  -0.02131 45  ARG A NH2 
62   N  N   . GLY A  46  ? 0.34400 0.28442 0.28788 0.00342  0.01169  -0.04016 46  GLY A N   
63   C  CA  . GLY A  46  ? 0.35287 0.29453 0.29902 -0.00058 0.00949  -0.04065 46  GLY A CA  
64   C  C   . GLY A  46  ? 0.31601 0.25138 0.26559 -0.00246 0.01262  -0.04579 46  GLY A C   
65   O  O   . GLY A  46  ? 0.32706 0.25630 0.27784 -0.00008 0.01673  -0.04855 46  GLY A O   
69   N  N   . PRO A  47  ? 0.32267 0.25945 0.27397 -0.00680 0.01069  -0.04701 47  PRO A N   
70   C  CA  . PRO A  47  ? 0.31886 0.24988 0.27280 -0.00947 0.01339  -0.05234 47  PRO A CA  
71   C  C   . PRO A  47  ? 0.29483 0.21812 0.25555 -0.00584 0.01644  -0.05041 47  PRO A C   
72   O  O   . PRO A  47  ? 0.32541 0.24833 0.28942 -0.00185 0.01587  -0.04458 47  PRO A O   
73   C  CB  . PRO A  47  ? 0.38571 0.32174 0.33949 -0.01524 0.00974  -0.05328 47  PRO A CB  
74   C  CG  . PRO A  47  ? 0.41434 0.35653 0.36860 -0.01393 0.00578  -0.04668 47  PRO A CG  
75   C  CD  . PRO A  47  ? 0.37691 0.32084 0.32757 -0.00966 0.00589  -0.04372 47  PRO A CD  
83   N  N   . ASP A  48  ? 0.31588 0.23263 0.27841 -0.00729 0.01980  -0.05546 48  ASP A N   
84   C  CA  . ASP A  48  ? 0.32075 0.22964 0.28964 -0.00448 0.02287  -0.05430 48  ASP A CA  
85   C  C   . ASP A  48  ? 0.32661 0.23742 0.30032 -0.00558 0.02015  -0.04987 48  ASP A C   
86   O  O   . ASP A  48  ? 0.35638 0.27134 0.32967 -0.01075 0.01740  -0.05138 48  ASP A O   
87   C  CB  . ASP A  48  ? 0.35618 0.25827 0.32554 -0.00708 0.02642  -0.06099 48  ASP A CB  
88   C  CG  . ASP A  48  ? 0.40111 0.30009 0.36648 -0.00526 0.02987  -0.06530 48  ASP A CG  
89   O  OD1 . ASP A  48  ? 0.36212 0.26322 0.32539 -0.00121 0.03009  -0.06273 48  ASP A OD1 
90   O  OD2 . ASP A  48  ? 0.46173 0.35606 0.42587 -0.00797 0.03247  -0.07144 48  ASP A OD2 
95   N  N   . PRO A  49  ? 0.31003 0.21819 0.28827 -0.00092 0.02077  -0.04441 49  PRO A N   
96   C  CA  . PRO A  49  ? 0.28864 0.19935 0.27123 -0.00151 0.01805  -0.03956 49  PRO A CA  
97   C  C   . PRO A  49  ? 0.33660 0.24249 0.32428 -0.00438 0.01953  -0.04182 49  PRO A C   
98   O  O   . PRO A  49  ? 0.35693 0.25515 0.34629 -0.00391 0.02349  -0.04557 49  PRO A O   
99   C  CB  . PRO A  49  ? 0.29804 0.20646 0.28327 0.00490  0.01889  -0.03339 49  PRO A CB  
100  C  CG  . PRO A  49  ? 0.31627 0.21772 0.30116 0.00855  0.02337  -0.03596 49  PRO A CG  
101  C  CD  . PRO A  49  ? 0.30396 0.20777 0.28296 0.00530  0.02360  -0.04191 49  PRO A CD  
109  N  N   . THR A  50  ? 0.32839 0.23902 0.31851 -0.00734 0.01625  -0.03931 50  THR A N   
110  C  CA  . THR A  50  ? 0.32034 0.22746 0.31624 -0.00961 0.01705  -0.03966 50  THR A CA  
111  C  C   . THR A  50  ? 0.33896 0.24937 0.33913 -0.00746 0.01465  -0.03259 50  THR A C   
112  O  O   . THR A  50  ? 0.30411 0.21991 0.30215 -0.00497 0.01204  -0.02802 50  THR A O   
113  C  CB  . THR A  50  ? 0.38250 0.29327 0.37698 -0.01674 0.01509  -0.04448 50  THR A CB  
114  O  OG1 . THR A  50  ? 0.34721 0.26769 0.33949 -0.01893 0.01025  -0.04167 50  THR A OG1 
115  C  CG2 . THR A  50  ? 0.37568 0.28417 0.36478 -0.01928 0.01701  -0.05165 50  THR A CG2 
123  N  N   A GLU A  51  ? 0.35556 0.26251 0.36174 -0.00839 0.01564  -0.03165 51  GLU A N   
124  N  N   B GLU A  51  ? 0.35374 0.26078 0.35988 -0.00847 0.01559  -0.03168 51  GLU A N   
125  C  CA  A GLU A  51  ? 0.38729 0.29720 0.39787 -0.00648 0.01359  -0.02507 51  GLU A CA  
126  C  CA  B GLU A  51  ? 0.38699 0.29688 0.39755 -0.00647 0.01360  -0.02508 51  GLU A CA  
127  C  C   A GLU A  51  ? 0.31739 0.23758 0.32565 -0.00956 0.00857  -0.02299 51  GLU A C   
128  C  C   B GLU A  51  ? 0.32170 0.24185 0.33009 -0.00957 0.00858  -0.02295 51  GLU A C   
129  O  O   A GLU A  51  ? 0.30551 0.23002 0.31330 -0.00646 0.00627  -0.01738 51  GLU A O   
130  O  O   B GLU A  51  ? 0.28417 0.20860 0.29225 -0.00648 0.00629  -0.01727 51  GLU A O   
131  C  CB  A GLU A  51  ? 0.37324 0.27855 0.39046 -0.00819 0.01529  -0.02519 51  GLU A CB  
132  C  CB  B GLU A  51  ? 0.37155 0.27640 0.38879 -0.00788 0.01552  -0.02517 51  GLU A CB  
133  C  CG  A GLU A  51  ? 0.45574 0.35056 0.47580 -0.00515 0.02026  -0.02681 51  GLU A CG  
134  C  CG  B GLU A  51  ? 0.36248 0.26811 0.38481 -0.00452 0.01468  -0.01820 51  GLU A CG  
135  C  CD  A GLU A  51  ? 0.63280 0.52345 0.65961 -0.00652 0.02171  -0.02592 51  GLU A CD  
136  C  CD  B GLU A  51  ? 0.59219 0.49136 0.62114 -0.00507 0.01743  -0.01827 51  GLU A CD  
137  O  OE1 A GLU A  51  ? 0.73834 0.63070 0.76917 -0.00414 0.02060  -0.02009 51  GLU A OE1 
138  O  OE1 B GLU A  51  ? 0.71951 0.61061 0.74908 -0.00490 0.02129  -0.02234 51  GLU A OE1 
139  O  OE2 A GLU A  51  ? 0.60590 0.49157 0.63387 -0.01003 0.02396  -0.03101 51  GLU A OE2 
140  O  OE2 B GLU A  51  ? 0.64685 0.54893 0.68034 -0.00552 0.01583  -0.01415 51  GLU A OE2 
153  N  N   . SER A  52  ? 0.31618 0.24027 0.32296 -0.01570 0.00680  -0.02742 52  SER A N   
154  C  CA  . SER A  52  ? 0.28014 0.21419 0.28469 -0.01892 0.00198  -0.02573 52  SER A CA  
155  C  C   . SER A  52  ? 0.27775 0.21660 0.27604 -0.01655 -0.00003 -0.02396 52  SER A C   
156  O  O   . SER A  52  ? 0.29559 0.24087 0.29319 -0.01532 -0.00337 -0.01891 52  SER A O   
157  C  CB  . SER A  52  ? 0.45221 0.38845 0.45553 -0.02596 0.00102  -0.03186 52  SER A CB  
158  O  OG  . SER A  52  ? 0.44424 0.39011 0.44482 -0.02925 -0.00357 -0.03082 52  SER A OG  
164  N  N   . PHE A  53  ? 0.29419 0.22970 0.28789 -0.01554 0.00215  -0.02781 53  PHE A N   
165  C  CA  . PHE A  53  ? 0.26035 0.19981 0.24804 -0.01320 0.00066  -0.02634 53  PHE A CA  
166  C  C   . PHE A  53  ? 0.25833 0.19730 0.24741 -0.00711 0.00047  -0.01943 53  PHE A C   
167  O  O   . PHE A  53  ? 0.25722 0.20217 0.24288 -0.00598 -0.00258 -0.01578 53  PHE A O   
168  C  CB  . PHE A  53  ? 0.29066 0.22526 0.27448 -0.01302 0.00391  -0.03197 53  PHE A CB  
169  C  CG  . PHE A  53  ? 0.25691 0.19359 0.23510 -0.00998 0.00361  -0.03097 53  PHE A CG  
170  C  CD1 . PHE A  53  ? 0.27011 0.21344 0.24211 -0.01303 0.00091  -0.03298 53  PHE A CD1 
171  C  CD2 . PHE A  53  ? 0.26037 0.19211 0.23946 -0.00418 0.00621  -0.02825 53  PHE A CD2 
172  C  CE1 . PHE A  53  ? 0.28023 0.22518 0.24700 -0.01030 0.00091  -0.03223 53  PHE A CE1 
173  C  CE2 . PHE A  53  ? 0.26976 0.20319 0.24387 -0.00142 0.00616  -0.02743 53  PHE A CE2 
174  C  CZ  . PHE A  53  ? 0.25469 0.19466 0.22260 -0.00450 0.00359  -0.02949 53  PHE A CZ  
184  N  N   . LEU A  54  ? 0.26305 0.19485 0.25675 -0.00323 0.00368  -0.01763 54  LEU A N   
185  C  CA  . LEU A  54  ? 0.23971 0.17025 0.23477 0.00264  0.00378  -0.01122 54  LEU A CA  
186  C  C   . LEU A  54  ? 0.23609 0.17097 0.23459 0.00296  0.00086  -0.00544 54  LEU A C   
187  O  O   . LEU A  54  ? 0.23377 0.17021 0.23139 0.00700  -0.00042 0.00006  54  LEU A O   
188  C  CB  . LEU A  54  ? 0.24199 0.16319 0.24075 0.00683  0.00830  -0.01124 54  LEU A CB  
189  C  CG  . LEU A  54  ? 0.25204 0.16968 0.24683 0.00988  0.01083  -0.01344 54  LEU A CG  
190  C  CD1 . LEU A  54  ? 0.30779 0.21619 0.30666 0.01262  0.01542  -0.01492 54  LEU A CD1 
191  C  CD2 . LEU A  54  ? 0.24399 0.16464 0.23558 0.01418  0.00913  -0.00822 54  LEU A CD2 
203  N  N   . GLU A  55  ? 0.24043 0.17735 0.24273 -0.00117 -0.00022 -0.00649 55  GLU A N   
204  C  CA  . GLU A  55  ? 0.23724 0.17861 0.24331 -0.00109 -0.00285 -0.00119 55  GLU A CA  
205  C  C   . GLU A  55  ? 0.22288 0.17398 0.22502 -0.00372 -0.00755 0.00032  55  GLU A C   
206  O  O   . GLU A  55  ? 0.22280 0.17816 0.22694 -0.00256 -0.00997 0.00559  55  GLU A O   
207  C  CB  . GLU A  55  ? 0.25040 0.18964 0.26284 -0.00429 -0.00174 -0.00277 55  GLU A CB  
208  C  CG  . GLU A  55  ? 0.26439 0.19415 0.28152 -0.00075 0.00264  -0.00235 55  GLU A CG  
209  C  CD  . GLU A  55  ? 0.44171 0.36859 0.46503 -0.00370 0.00408  -0.00384 55  GLU A CD  
210  O  OE1 . GLU A  55  ? 0.42488 0.35738 0.44927 -0.00887 0.00160  -0.00534 55  GLU A OE1 
211  O  OE2 . GLU A  55  ? 0.40147 0.32028 0.42866 -0.00086 0.00778  -0.00348 55  GLU A OE2 
218  N  N   . ALA A  56  ? 0.23643 0.19099 0.23315 -0.00731 -0.00878 -0.00429 56  ALA A N   
219  C  CA  . ALA A  56  ? 0.23111 0.19492 0.22389 -0.01012 -0.01325 -0.00318 56  ALA A CA  
220  C  C   . ALA A  56  ? 0.21805 0.18476 0.20762 -0.00567 -0.01517 0.00269  56  ALA A C   
221  O  O   . ALA A  56  ? 0.21462 0.17667 0.20264 -0.00107 -0.01314 0.00433  56  ALA A O   
222  C  CB  . ALA A  56  ? 0.26447 0.23033 0.25134 -0.01415 -0.01365 -0.00937 56  ALA A CB  
228  N  N   . ASP A  57  ? 0.22512 0.19973 0.21329 -0.00714 -0.01922 0.00582  57  ASP A N   
229  C  CA  . ASP A  57  ? 0.22032 0.19759 0.20533 -0.00304 -0.02118 0.01164  57  ASP A CA  
230  C  C   . ASP A  57  ? 0.22705 0.20396 0.20493 -0.00177 -0.02096 0.01006  57  ASP A C   
231  O  O   . ASP A  57  ? 0.23230 0.20764 0.20786 0.00277  -0.02082 0.01411  57  ASP A O   
232  C  CB  . ASP A  57  ? 0.23044 0.21671 0.21472 -0.00526 -0.02569 0.01481  57  ASP A CB  
233  C  CG  . ASP A  57  ? 0.28731 0.27479 0.27851 -0.00499 -0.02629 0.01859  57  ASP A CG  
234  O  OD1 . ASP A  57  ? 0.27884 0.26012 0.27543 -0.00247 -0.02335 0.01976  57  ASP A OD1 
235  O  OD2 . ASP A  57  ? 0.29815 0.29316 0.28966 -0.00739 -0.02976 0.02052  57  ASP A OD2 
240  N  N   . SER A  58  ? 0.22125 0.19992 0.19523 -0.00586 -0.02107 0.00425  58  SER A N   
241  C  CA  . SER A  58  ? 0.22061 0.19928 0.18785 -0.00511 -0.02073 0.00227  58  SER A CA  
242  C  C   . SER A  58  ? 0.22555 0.19851 0.19239 -0.00617 -0.01701 -0.00401 58  SER A C   
243  O  O   . SER A  58  ? 0.24715 0.21914 0.21626 -0.01013 -0.01609 -0.00874 58  SER A O   
244  C  CB  . SER A  58  ? 0.21905 0.20608 0.18041 -0.00897 -0.02462 0.00126  58  SER A CB  
245  O  OG  . SER A  58  ? 0.23517 0.22234 0.18991 -0.00807 -0.02428 -0.00024 58  SER A OG  
251  N  N   . GLY A  59  ? 0.21673 0.18612 0.18038 -0.00270 -0.01496 -0.00406 59  GLY A N   
252  C  CA  . GLY A  59  ? 0.22215 0.18770 0.18357 -0.00358 -0.01194 -0.00986 59  GLY A CA  
253  C  C   . GLY A  59  ? 0.21863 0.18978 0.17369 -0.00794 -0.01388 -0.01400 59  GLY A C   
254  O  O   . GLY A  59  ? 0.22668 0.20484 0.17929 -0.01061 -0.01771 -0.01251 59  GLY A O   
258  N  N   . PRO A  60  ? 0.21056 0.17861 0.16287 -0.00866 -0.01116 -0.01930 60  PRO A N   
259  C  CA  . PRO A  60  ? 0.21932 0.19177 0.16599 -0.01340 -0.01239 -0.02443 60  PRO A CA  
260  C  C   . PRO A  60  ? 0.21433 0.19200 0.15402 -0.01291 -0.01449 -0.02300 60  PRO A C   
261  O  O   . PRO A  60  ? 0.22815 0.21028 0.16296 -0.01693 -0.01603 -0.02659 60  PRO A O   
262  C  CB  . PRO A  60  ? 0.24099 0.20693 0.18811 -0.01386 -0.00803 -0.03062 60  PRO A CB  
263  C  CG  . PRO A  60  ? 0.26305 0.22272 0.21324 -0.00783 -0.00492 -0.02748 60  PRO A CG  
264  C  CD  . PRO A  60  ? 0.23072 0.19054 0.18590 -0.00543 -0.00652 -0.02122 60  PRO A CD  
272  N  N   . TYR A  61  ? 0.22565 0.20276 0.16457 -0.00823 -0.01458 -0.01789 61  TYR A N   
273  C  CA  . TYR A  61  ? 0.23064 0.21275 0.16282 -0.00793 -0.01672 -0.01623 61  TYR A CA  
274  C  C   . TYR A  61  ? 0.23934 0.22784 0.17025 -0.00875 -0.02122 -0.01131 61  TYR A C   
275  O  O   . TYR A  61  ? 0.24115 0.22871 0.17637 -0.00634 -0.02202 -0.00650 61  TYR A O   
276  C  CB  . TYR A  61  ? 0.24793 0.22634 0.17940 -0.00265 -0.01467 -0.01321 61  TYR A CB  
277  C  CG  . TYR A  61  ? 0.27249 0.24552 0.20403 -0.00139 -0.01035 -0.01777 61  TYR A CG  
278  C  CD1 . TYR A  61  ? 0.30084 0.27613 0.22649 -0.00287 -0.00980 -0.02139 61  TYR A CD1 
279  C  CD2 . TYR A  61  ? 0.27809 0.24405 0.21554 0.00113  -0.00688 -0.01844 61  TYR A CD2 
280  C  CE1 . TYR A  61  ? 0.36486 0.33529 0.29070 -0.00149 -0.00562 -0.02560 61  TYR A CE1 
281  C  CE2 . TYR A  61  ? 0.33103 0.29195 0.26861 0.00252  -0.00276 -0.02263 61  TYR A CE2 
282  C  CZ  . TYR A  61  ? 0.36915 0.33253 0.30105 0.00126  -0.00227 -0.02598 61  TYR A CZ  
283  O  OH  . TYR A  61  ? 0.49677 0.45535 0.42894 0.00274  0.00188  -0.03009 61  TYR A OH  
293  N  N   . THR A  62  ? 0.26605 0.26097 0.19078 -0.01188 -0.02404 -0.01235 62  THR A N   
294  C  CA  . THR A  62  ? 0.25428 0.25503 0.17651 -0.01157 -0.02812 -0.00694 62  THR A CA  
295  C  C   . THR A  62  ? 0.25619 0.25497 0.17629 -0.00661 -0.02763 -0.00215 62  THR A C   
296  O  O   . THR A  62  ? 0.26697 0.26252 0.18499 -0.00482 -0.02499 -0.00399 62  THR A O   
297  C  CB  . THR A  62  ? 0.30758 0.31556 0.22358 -0.01600 -0.03129 -0.00900 62  THR A CB  
298  O  OG1 . THR A  62  ? 0.37237 0.37990 0.28286 -0.01647 -0.02965 -0.01265 62  THR A OG1 
299  C  CG2 . THR A  62  ? 0.32633 0.33685 0.24419 -0.02117 -0.03228 -0.01338 62  THR A CG2 
307  N  N   . ILE A  63  ? 0.30196 0.18760 0.18149 0.02288  -0.03910 0.02406  63  ILE A N   
308  C  CA  . ILE A  63  ? 0.28016 0.16976 0.16648 0.01822  -0.03419 0.02304  63  ILE A CA  
309  C  C   . ILE A  63  ? 0.29668 0.17331 0.17567 0.01163  -0.03397 0.02934  63  ILE A C   
310  O  O   . ILE A  63  ? 0.32411 0.18736 0.19579 0.01187  -0.03882 0.03498  63  ILE A O   
311  C  CB  . ILE A  63  ? 0.29335 0.18687 0.19526 0.02306  -0.03593 0.02037  63  ILE A CB  
312  C  CG1 . ILE A  63  ? 0.31756 0.19742 0.22219 0.02667  -0.04273 0.02525  63  ILE A CG1 
313  C  CG2 . ILE A  63  ? 0.29848 0.20556 0.20769 0.02923  -0.03598 0.01417  63  ILE A CG2 
314  C  CD1 . ILE A  63  ? 0.33617 0.21942 0.25567 0.03058  -0.04396 0.02302  63  ILE A CD1 
326  N  N   . ALA A  64  ? 0.30595 0.18673 0.18753 0.00566  -0.02841 0.02837  64  ALA A N   
327  C  CA  . ALA A  64  ? 0.30584 0.17553 0.18284 -0.00104 -0.02755 0.03368  64  ALA A CA  
328  C  C   . ALA A  64  ? 0.28501 0.15675 0.17465 -0.00160 -0.02595 0.03173  64  ALA A C   
329  O  O   . ALA A  64  ? 0.27656 0.16017 0.17687 0.00188  -0.02430 0.02611  64  ALA A O   
330  C  CB  . ALA A  64  ? 0.34447 0.21701 0.21013 -0.00912 -0.02187 0.03472  64  ALA A CB  
336  N  N   . THR A  65  ? 0.31439 0.17458 0.20252 -0.00626 -0.02638 0.03634  65  THR A N   
337  C  CA  . THR A  65  ? 0.30452 0.16491 0.20345 -0.00744 -0.02495 0.03482  65  THR A CA  
338  C  C   . THR A  65  ? 0.33936 0.19616 0.23362 -0.01658 -0.02044 0.03715  65  THR A C   
339  O  O   . THR A  65  ? 0.37165 0.21997 0.25430 -0.02159 -0.02042 0.04220  65  THR A O   
340  C  CB  . THR A  65  ? 0.34427 0.19327 0.25012 -0.00250 -0.03096 0.03747  65  THR A CB  
341  O  OG1 . THR A  65  ? 0.39658 0.22920 0.29346 -0.00504 -0.03451 0.04455  65  THR A OG1 
342  C  CG2 . THR A  65  ? 0.37119 0.22403 0.28274 0.00633  -0.03549 0.03529  65  THR A CG2 
350  N  N   A SER A  66  ? 0.31237 0.17602 0.21590 -0.01890 -0.01664 0.03341  66  SER A N   
351  N  N   B SER A  66  ? 0.34001 0.20288 0.24372 -0.01874 -0.01694 0.03361  66  SER A N   
352  C  CA  A SER A  66  ? 0.31631 0.17586 0.21791 -0.02728 -0.01287 0.03533  66  SER A CA  
353  C  CA  B SER A  66  ? 0.32178 0.18149 0.22345 -0.02724 -0.01284 0.03526  66  SER A CA  
354  C  C   A SER A  66  ? 0.31398 0.17075 0.22741 -0.02614 -0.01370 0.03361  66  SER A C   
355  C  C   B SER A  66  ? 0.32526 0.18225 0.23866 -0.02633 -0.01353 0.03354  66  SER A C   
356  O  O   A SER A  66  ? 0.32298 0.19009 0.24705 -0.02157 -0.01320 0.02823  66  SER A O   
357  O  O   B SER A  66  ? 0.31449 0.18200 0.23855 -0.02193 -0.01289 0.02812  66  SER A O   
358  C  CB  A SER A  66  ? 0.36084 0.23493 0.26042 -0.03302 -0.00570 0.03161  66  SER A CB  
359  C  CB  B SER A  66  ? 0.33868 0.21379 0.23880 -0.03234 -0.00579 0.03116  66  SER A CB  
360  O  OG  A SER A  66  ? 0.37031 0.24001 0.26686 -0.04182 -0.00214 0.03407  66  SER A OG  
361  O  OG  B SER A  66  ? 0.43063 0.30638 0.31813 -0.03518 -0.00441 0.03357  66  SER A OG  
372  N  N   A ASN A  67  ? 0.33572 0.17850 0.24730 -0.03019 -0.01508 0.03811  67  ASN A N   
373  N  N   B ASN A  67  ? 0.35082 0.19372 0.26231 -0.03036 -0.01496 0.03809  67  ASN A N   
374  C  CA  A ASN A  67  ? 0.32191 0.16111 0.24403 -0.02967 -0.01565 0.03642  67  ASN A CA  
375  C  CA  B ASN A  67  ? 0.34242 0.18146 0.26440 -0.02974 -0.01566 0.03649  67  ASN A CA  
376  C  C   A ASN A  67  ? 0.37734 0.22525 0.30278 -0.03659 -0.00944 0.03288  67  ASN A C   
377  C  C   B ASN A  67  ? 0.38430 0.23198 0.30971 -0.03664 -0.00947 0.03295  67  ASN A C   
378  O  O   A ASN A  67  ? 0.41358 0.26217 0.33102 -0.04410 -0.00561 0.03482  67  ASN A O   
379  O  O   B ASN A  67  ? 0.41568 0.26378 0.33311 -0.04419 -0.00568 0.03495  67  ASN A O   
380  C  CB  A ASN A  67  ? 0.40437 0.22414 0.32301 -0.03105 -0.01994 0.04278  67  ASN A CB  
381  C  CB  B ASN A  67  ? 0.40226 0.22186 0.32089 -0.03108 -0.01996 0.04283  67  ASN A CB  
382  C  CG  A ASN A  67  ? 0.47584 0.28708 0.39366 -0.02358 -0.02654 0.04594  67  ASN A CG  
383  C  CG  B ASN A  67  ? 0.41724 0.23208 0.34616 -0.03083 -0.02044 0.04105  67  ASN A CG  
384  O  OD1 A ASN A  67  ? 0.46677 0.28616 0.38995 -0.01658 -0.02829 0.04260  67  ASN A OD1 
385  O  OD1 B ASN A  67  ? 0.56921 0.38566 0.50756 -0.02398 -0.02321 0.03829  67  ASN A OD1 
386  N  ND2 A ASN A  67  ? 0.63724 0.43214 0.54838 -0.02511 -0.03040 0.05258  67  ASN A ND2 
387  N  ND2 B ASN A  67  ? 0.47908 0.28844 0.40630 -0.03845 -0.01763 0.04244  67  ASN A ND2 
400  N  N   . VAL A  68  ? 0.31806 0.17257 0.25531 -0.03422 -0.00856 0.02785  68  VAL A N   
401  C  CA  . VAL A  68  ? 0.33068 0.19317 0.27291 -0.04022 -0.00329 0.02408  68  VAL A CA  
402  C  C   . VAL A  68  ? 0.32430 0.17551 0.27275 -0.04088 -0.00528 0.02470  68  VAL A C   
403  O  O   . VAL A  68  ? 0.32272 0.17248 0.27949 -0.03430 -0.00865 0.02276  68  VAL A O   
404  C  CB  . VAL A  68  ? 0.29882 0.18038 0.24995 -0.03693 -0.00033 0.01698  68  VAL A CB  
405  C  CG1 . VAL A  68  ? 0.33047 0.22049 0.28691 -0.04342 0.00499  0.01314  68  VAL A CG1 
406  C  CG2 . VAL A  68  ? 0.32611 0.21848 0.27137 -0.03552 0.00136  0.01609  68  VAL A CG2 
416  N  N   . SER A  69  ? 0.37265 0.21604 0.31712 -0.04883 -0.00318 0.02733  69  SER A N   
417  C  CA  . SER A  69  ? 0.36823 0.20005 0.31782 -0.05032 -0.00477 0.02792  69  SER A CA  
418  C  C   . SER A  69  ? 0.37136 0.21367 0.33297 -0.04888 -0.00262 0.02107  69  SER A C   
419  O  O   . SER A  69  ? 0.34965 0.20785 0.31434 -0.05055 0.00168  0.01644  69  SER A O   
420  C  CB  . SER A  69  ? 0.43113 0.25456 0.37351 -0.06014 -0.00226 0.03182  69  SER A CB  
421  O  OG  . SER A  69  ? 0.42700 0.24197 0.37518 -0.06272 -0.00261 0.03104  69  SER A OG  
427  N  N   . SER A  70  ? 0.34962 0.18284 0.31808 -0.04591 -0.00562 0.02044  70  SER A N   
428  C  CA  . SER A  70  ? 0.33543 0.17674 0.31473 -0.04541 -0.00366 0.01421  70  SER A CA  
429  C  C   . SER A  70  ? 0.34379 0.18941 0.32307 -0.05452 0.00146  0.01215  70  SER A C   
430  O  O   . SER A  70  ? 0.35942 0.21524 0.34703 -0.05483 0.00387  0.00646  70  SER A O   
431  C  CB  . SER A  70  ? 0.35822 0.18779 0.34399 -0.04079 -0.00780 0.01417  70  SER A CB  
432  O  OG  . SER A  70  ? 0.38324 0.19627 0.36492 -0.04597 -0.00877 0.01824  70  SER A OG  
438  N  N   . LEU A  71  ? 0.35621 0.19479 0.32636 -0.06218 0.00316  0.01668  71  LEU A N   
439  C  CA  . LEU A  71  ? 0.41629 0.26071 0.38601 -0.07118 0.00827  0.01494  71  LEU A CA  
440  C  C   . LEU A  71  ? 0.35064 0.21623 0.32359 -0.07169 0.01288  0.00980  71  LEU A C   
441  O  O   . LEU A  71  ? 0.41801 0.29139 0.39440 -0.07770 0.01697  0.00652  71  LEU A O   
442  C  CB  . LEU A  71  ? 0.42559 0.25961 0.38395 -0.07885 0.00905  0.02148  71  LEU A CB  
443  C  CG  . LEU A  71  ? 0.62212 0.46208 0.57829 -0.08898 0.01442  0.02086  71  LEU A CG  
444  C  CD1 . LEU A  71  ? 0.57996 0.41631 0.54393 -0.09230 0.01508  0.01750  71  LEU A CD1 
445  C  CD2 . LEU A  71  ? 0.60022 0.42923 0.54442 -0.09567 0.01450  0.02817  71  LEU A CD2 
457  N  N   . VAL A  72  ? 0.35417 0.22908 0.32655 -0.06555 0.01217  0.00891  72  VAL A N   
458  C  CA  . VAL A  72  ? 0.33051 0.22537 0.30614 -0.06536 0.01623  0.00413  72  VAL A CA  
459  C  C   . VAL A  72  ? 0.36852 0.27386 0.35566 -0.06491 0.01800  -0.00232 72  VAL A C   
460  O  O   . VAL A  72  ? 0.34943 0.25017 0.34353 -0.06026 0.01498  -0.00422 72  VAL A O   
461  C  CB  . VAL A  72  ? 0.37693 0.27743 0.35140 -0.05717 0.01381  0.00409  72  VAL A CB  
462  C  CG1 . VAL A  72  ? 0.34080 0.24001 0.32390 -0.04825 0.00939  0.00172  72  VAL A CG1 
463  C  CG2 . VAL A  72  ? 0.37833 0.29826 0.35379 -0.05728 0.01800  0.00019  72  VAL A CG2 
473  N  N   . ARG A  73  ? 0.35743 0.27785 0.34673 -0.06958 0.02296  -0.00584 73  ARG A N   
474  C  CA  . ARG A  73  ? 0.37443 0.30521 0.37401 -0.07038 0.02492  -0.01175 73  ARG A CA  
475  C  C   . ARG A  73  ? 0.33799 0.28074 0.34581 -0.06166 0.02328  -0.01620 73  ARG A C   
476  O  O   . ARG A  73  ? 0.38395 0.33699 0.39070 -0.05801 0.02384  -0.01686 73  ARG A O   
477  C  CB  . ARG A  73  ? 0.40363 0.34710 0.40294 -0.07851 0.03070  -0.01377 73  ARG A CB  
478  C  CG  . ARG A  73  ? 0.74545 0.67852 0.73817 -0.08817 0.03269  -0.00993 73  ARG A CG  
479  C  CD  . ARG A  73  ? 0.96173 0.90907 0.95510 -0.09615 0.03854  -0.01216 73  ARG A CD  
480  N  NE  . ARG A  73  ? 1.07923 1.01690 1.06581 -0.10578 0.04045  -0.00799 73  ARG A NE  
481  C  CZ  . ARG A  73  ? 1.14220 1.08929 1.12739 -0.11400 0.04540  -0.00836 73  ARG A CZ  
482  N  NH1 . ARG A  73  ? 1.18070 1.14742 1.17100 -0.11384 0.04912  -0.01290 73  ARG A NH1 
483  N  NH2 . ARG A  73  ? 1.06710 1.00373 1.04582 -0.12262 0.04656  -0.00392 73  ARG A NH2 
497  N  N   . GLY A  74  ? 0.29374 0.23488 0.30972 -0.05816 0.02109  -0.01921 74  GLY A N   
498  C  CA  . GLY A  74  ? 0.29574 0.25027 0.32059 -0.05129 0.02020  -0.02392 74  GLY A CA  
499  C  C   . GLY A  74  ? 0.26107 0.20994 0.28769 -0.04198 0.01504  -0.02271 74  GLY A C   
500  O  O   . GLY A  74  ? 0.28552 0.24473 0.32006 -0.03627 0.01393  -0.02645 74  GLY A O   
504  N  N   . PHE A  75  ? 0.28231 0.21546 0.30191 -0.04044 0.01178  -0.01743 75  PHE A N   
505  C  CA  . PHE A  75  ? 0.26671 0.19322 0.28784 -0.03190 0.00659  -0.01576 75  PHE A CA  
506  C  C   . PHE A  75  ? 0.25377 0.16037 0.26752 -0.03302 0.00363  -0.00991 75  PHE A C   
507  O  O   . PHE A  75  ? 0.27543 0.17411 0.28329 -0.04028 0.00560  -0.00738 75  PHE A O   
508  C  CB  . PHE A  75  ? 0.24521 0.18179 0.26582 -0.02591 0.00551  -0.01600 75  PHE A CB  
509  C  CG  . PHE A  75  ? 0.25862 0.19371 0.26879 -0.02852 0.00672  -0.01228 75  PHE A CG  
510  C  CD1 . PHE A  75  ? 0.23796 0.18296 0.24515 -0.03488 0.01182  -0.01365 75  PHE A CD1 
511  C  CD2 . PHE A  75  ? 0.25387 0.17856 0.25732 -0.02452 0.00280  -0.00757 75  PHE A CD2 
512  C  CE1 . PHE A  75  ? 0.27455 0.21883 0.27201 -0.03725 0.01316  -0.01045 75  PHE A CE1 
513  C  CE2 . PHE A  75  ? 0.25628 0.18041 0.24979 -0.02698 0.00403  -0.00447 75  PHE A CE2 
514  C  CZ  . PHE A  75  ? 0.27272 0.20635 0.26319 -0.03317 0.00917  -0.00591 75  PHE A CZ  
524  N  N   . GLY A  76  ? 0.25920 0.15772 0.27370 -0.02591 -0.00127 -0.00765 76  GLY A N   
525  C  CA  . GLY A  76  ? 0.27544 0.15482 0.28512 -0.02607 -0.00470 -0.00252 76  GLY A CA  
526  C  C   . GLY A  76  ? 0.29965 0.17066 0.29896 -0.02582 -0.00676 0.00344  76  GLY A C   
527  O  O   . GLY A  76  ? 0.31912 0.17552 0.31560 -0.02333 -0.01091 0.00782  76  GLY A O   
531  N  N   . GLY A  77  ? 0.27870 0.15859 0.27223 -0.02855 -0.00391 0.00368  77  GLY A N   
532  C  CA  . GLY A  77  ? 0.29609 0.16968 0.27938 -0.02821 -0.00568 0.00887  77  GLY A CA  
533  C  C   . GLY A  77  ? 0.27729 0.15652 0.26207 -0.01988 -0.00893 0.00840  77  GLY A C   
534  O  O   . GLY A  77  ? 0.27122 0.15984 0.26515 -0.01432 -0.00978 0.00419  77  GLY A O   
538  N  N   . GLY A  78  ? 0.27707 0.15049 0.25262 -0.01903 -0.01097 0.01287  78  GLY A N   
539  C  CA  . GLY A  78  ? 0.28494 0.16322 0.26126 -0.01141 -0.01424 0.01254  78  GLY A CA  
540  C  C   . GLY A  78  ? 0.27835 0.14990 0.24298 -0.01183 -0.01601 0.01751  78  GLY A C   
541  O  O   . GLY A  78  ? 0.30850 0.16987 0.26435 -0.01764 -0.01534 0.02194  78  GLY A O   
545  N  N   . THR A  79  ? 0.25462 0.13157 0.21929 -0.00550 -0.01859 0.01683  79  THR A N   
546  C  CA  . THR A  79  ? 0.25039 0.12265 0.20437 -0.00474 -0.02066 0.02077  79  THR A CA  
547  C  C   . THR A  79  ? 0.23828 0.12641 0.19201 -0.00307 -0.01796 0.01655  79  THR A C   
548  O  O   . THR A  79  ? 0.23640 0.13412 0.19872 0.00289  -0.01912 0.01254  79  THR A O   
549  C  CB  . THR A  79  ? 0.27601 0.13761 0.23000 0.00213  -0.02752 0.02444  79  THR A CB  
550  O  OG1 . THR A  79  ? 0.31653 0.16435 0.27287 0.00145  -0.03008 0.02768  79  THR A OG1 
551  C  CG2 . THR A  79  ? 0.30157 0.15718 0.24339 0.00199  -0.02970 0.02886  79  THR A CG2 
559  N  N   . ILE A  80  ? 0.25895 0.15009 0.20318 -0.00813 -0.01444 0.01739  80  ILE A N   
560  C  CA  . ILE A  80  ? 0.24512 0.15047 0.18790 -0.00646 -0.01191 0.01359  80  ILE A CA  
561  C  C   . ILE A  80  ? 0.25390 0.15349 0.18899 -0.00181 -0.01643 0.01657  80  ILE A C   
562  O  O   . ILE A  80  ? 0.28116 0.16835 0.20599 -0.00455 -0.01827 0.02204  80  ILE A O   
563  C  CB  . ILE A  80  ? 0.25629 0.16889 0.19259 -0.01437 -0.00542 0.01270  80  ILE A CB  
564  C  CG1 . ILE A  80  ? 0.26074 0.17661 0.20324 -0.02023 -0.00122 0.01074  80  ILE A CG1 
565  C  CG2 . ILE A  80  ? 0.29766 0.22688 0.23547 -0.01145 -0.00277 0.00755  80  ILE A CG2 
566  C  CD1 . ILE A  80  ? 0.28599 0.20777 0.22241 -0.02855 0.00488  0.01057  80  ILE A CD1 
578  N  N   . TYR A  81  ? 0.23804 0.14672 0.17775 0.00484  -0.01817 0.01303  81  TYR A N   
579  C  CA  . TYR A  81  ? 0.23949 0.14574 0.17281 0.00964  -0.02206 0.01448  81  TYR A CA  
580  C  C   . TYR A  81  ? 0.24380 0.16456 0.17466 0.00919  -0.01778 0.00994  81  TYR A C   
581  O  O   . TYR A  81  ? 0.23288 0.16739 0.17281 0.01044  -0.01476 0.00453  81  TYR A O   
582  C  CB  . TYR A  81  ? 0.25008 0.15566 0.19223 0.01816  -0.02781 0.01364  81  TYR A CB  
583  C  CG  . TYR A  81  ? 0.24323 0.13580 0.18953 0.01977  -0.03224 0.01754  81  TYR A CG  
584  C  CD1 . TYR A  81  ? 0.23662 0.13058 0.19263 0.01886  -0.03085 0.01580  81  TYR A CD1 
585  C  CD2 . TYR A  81  ? 0.25821 0.13713 0.19855 0.02220  -0.03785 0.02291  81  TYR A CD2 
586  C  CE1 . TYR A  81  ? 0.24844 0.13101 0.20819 0.02059  -0.03468 0.01896  81  TYR A CE1 
587  C  CE2 . TYR A  81  ? 0.28237 0.14971 0.22659 0.02382  -0.04182 0.02644  81  TYR A CE2 
588  C  CZ  . TYR A  81  ? 0.28098 0.15014 0.23507 0.02312  -0.04014 0.02435  81  TYR A CZ  
589  O  OH  . TYR A  81  ? 0.31090 0.16843 0.26892 0.02510  -0.04411 0.02767  81  TYR A OH  
599  N  N   . TYR A  82  ? 0.26095 0.17912 0.17986 0.00761  -0.01756 0.01194  82  TYR A N   
600  C  CA  . TYR A  82  ? 0.25360 0.18572 0.16984 0.00692  -0.01300 0.00739  82  TYR A CA  
601  C  C   . TYR A  82  ? 0.25771 0.18609 0.16286 0.00921  -0.01554 0.00900  82  TYR A C   
602  O  O   . TYR A  82  ? 0.28016 0.19487 0.17579 0.00763  -0.01878 0.01466  82  TYR A O   
603  C  CB  . TYR A  82  ? 0.28027 0.21831 0.19310 -0.00164 -0.00586 0.00670  82  TYR A CB  
604  C  CG  . TYR A  82  ? 0.28800 0.21341 0.18916 -0.00853 -0.00534 0.01282  82  TYR A CG  
605  C  CD1 . TYR A  82  ? 0.37098 0.28523 0.27426 -0.01199 -0.00655 0.01672  82  TYR A CD1 
606  C  CD2 . TYR A  82  ? 0.29623 0.22062 0.18451 -0.01153 -0.00381 0.01472  82  TYR A CD2 
607  C  CE1 . TYR A  82  ? 0.43646 0.33880 0.32917 -0.01840 -0.00632 0.02261  82  TYR A CE1 
608  C  CE2 . TYR A  82  ? 0.36090 0.27357 0.23790 -0.01823 -0.00347 0.02084  82  TYR A CE2 
609  C  CZ  . TYR A  82  ? 0.41597 0.31773 0.29588 -0.02154 -0.00483 0.02475  82  TYR A CZ  
610  O  OH  . TYR A  82  ? 0.68100 0.57094 0.54980 -0.02813 -0.00478 0.03103  82  TYR A OH  
620  N  N   . PRO A  83  ? 0.24897 0.18933 0.15457 0.01254  -0.01395 0.00410  83  PRO A N   
621  C  CA  . PRO A  83  ? 0.28175 0.21922 0.17640 0.01459  -0.01606 0.00497  83  PRO A CA  
622  C  C   . PRO A  83  ? 0.33591 0.27048 0.21665 0.00713  -0.01203 0.00783  83  PRO A C   
623  O  O   . PRO A  83  ? 0.35551 0.29706 0.23603 0.00094  -0.00584 0.00661  83  PRO A O   
624  C  CB  . PRO A  83  ? 0.35563 0.30828 0.25579 0.01959  -0.01442 -0.00188 83  PRO A CB  
625  C  CG  . PRO A  83  ? 0.32339 0.28570 0.23735 0.02079  -0.01247 -0.00566 83  PRO A CG  
626  C  CD  . PRO A  83  ? 0.25103 0.20754 0.16791 0.01537  -0.01094 -0.00251 83  PRO A CD  
634  N  N   . VAL A  84  ? 0.38431 0.30903 0.25336 0.00768  -0.01564 0.01164  84  VAL A N   
635  C  CA  . VAL A  84  ? 0.42251 0.34337 0.27716 0.00064  -0.01246 0.01507  84  VAL A CA  
636  C  C   . VAL A  84  ? 0.58516 0.51917 0.43404 -0.00011 -0.00739 0.01019  84  VAL A C   
637  O  O   . VAL A  84  ? 0.57899 0.51781 0.42140 -0.00705 -0.00142 0.01043  84  VAL A O   
638  C  CB  . VAL A  84  ? 0.46928 0.37337 0.31359 0.00114  -0.01870 0.02172  84  VAL A CB  
639  C  CG1 . VAL A  84  ? 0.60329 0.50492 0.43158 -0.00482 -0.01603 0.02459  84  VAL A CG1 
640  C  CG2 . VAL A  84  ? 0.50247 0.39402 0.35130 -0.00057 -0.02180 0.02700  84  VAL A CG2 
650  N  N   . ASN A  85  ? 0.48832 0.42817 0.33920 0.00682  -0.00965 0.00582  85  ASN A N   
651  C  CA  . ASN A  85  ? 0.50921 0.45989 0.35277 0.00615  -0.00518 0.00151  85  ASN A CA  
652  C  C   . ASN A  85  ? 0.61022 0.57757 0.46522 0.01071  -0.00216 -0.00636 85  ASN A C   
653  O  O   . ASN A  85  ? 0.58465 0.55797 0.43796 0.01562  -0.00287 -0.01064 85  ASN A O   
654  C  CB  . ASN A  85  ? 0.55815 0.50172 0.39063 0.00984  -0.00992 0.00271  85  ASN A CB  
655  C  CG  . ASN A  85  ? 0.94745 0.87580 0.76651 0.00496  -0.01250 0.01034  85  ASN A CG  
656  O  OD1 . ASN A  85  ? 0.96316 0.89006 0.77585 -0.00278 -0.00821 0.01360  85  ASN A OD1 
657  N  ND2 . ASN A  85  ? 0.98841 0.90523 0.80316 0.00935  -0.01974 0.01348  85  ASN A ND2 
664  N  N   . ALA A  86  ? 0.40140 0.37633 0.26815 0.00926  0.00101  -0.00842 86  ALA A N   
665  C  CA  . ALA A  86  ? 0.41697 0.40736 0.29583 0.01369  0.00332  -0.01544 86  ALA A CA  
666  C  C   . ALA A  86  ? 0.45110 0.45515 0.32752 0.00813  0.01166  -0.01890 86  ALA A C   
667  O  O   . ALA A  86  ? 0.51155 0.51408 0.38390 0.00043  0.01573  -0.01581 86  ALA A O   
668  C  CB  . ALA A  86  ? 0.39115 0.38234 0.28469 0.01565  0.00156  -0.01578 86  ALA A CB  
674  N  N   . GLU A  87  ? 0.42481 0.44159 0.30316 0.01197  0.01399  -0.02505 87  GLU A N   
675  C  CA  . GLU A  87  ? 0.45329 0.48466 0.33036 0.00754  0.02195  -0.02899 87  GLU A CA  
676  C  C   . GLU A  87  ? 0.34821 0.39195 0.24065 0.00773  0.02498  -0.03285 87  GLU A C   
677  O  O   . GLU A  87  ? 0.42422 0.47072 0.32809 0.01425  0.02132  -0.03560 87  GLU A O   
678  C  CB  . GLU A  87  ? 0.53814 0.57783 0.41048 0.01198  0.02308  -0.03424 87  GLU A CB  
679  C  CG  . GLU A  87  ? 0.77452 0.80222 0.63188 0.01279  0.01932  -0.03104 87  GLU A CG  
680  C  CD  . GLU A  87  ? 0.90806 0.94505 0.75721 0.01380  0.02309  -0.03587 87  GLU A CD  
681  O  OE1 . GLU A  87  ? 0.88614 0.93796 0.73829 0.01126  0.03005  -0.04024 87  GLU A OE1 
682  O  OE2 . GLU A  87  ? 0.94973 0.97937 0.78951 0.01715  0.01909  -0.03540 87  GLU A OE2 
689  N  N   . GLY A  88  ? 0.35409 0.40508 0.24658 0.00036  0.03149  -0.03277 88  GLY A N   
690  C  CA  . GLY A  88  ? 0.34640 0.41071 0.25270 -0.00033 0.03514  -0.03671 88  GLY A CA  
691  C  C   . GLY A  88  ? 0.28951 0.34703 0.20526 -0.00051 0.03177  -0.03405 88  GLY A C   
692  O  O   . GLY A  88  ? 0.37463 0.41692 0.28633 -0.00145 0.02744  -0.02863 88  GLY A O   
696  N  N   . THR A  89  ? 0.28127 0.35111 0.21037 0.00060  0.03389  -0.03824 89  THR A N   
697  C  CA  . THR A  89  ? 0.24819 0.31404 0.18691 -0.00021 0.03174  -0.03653 89  THR A CA  
698  C  C   . THR A  89  ? 0.25229 0.31582 0.20040 0.00838  0.02529  -0.03792 89  THR A C   
699  O  O   . THR A  89  ? 0.25553 0.32561 0.20670 0.01494  0.02362  -0.04181 89  THR A O   
700  C  CB  . THR A  89  ? 0.29045 0.37022 0.23838 -0.00477 0.03747  -0.03969 89  THR A CB  
701  O  OG1 . THR A  89  ? 0.29597 0.39234 0.25142 -0.00042 0.03981  -0.04603 89  THR A OG1 
702  C  CG2 . THR A  89  ? 0.28783 0.36856 0.22685 -0.01442 0.04370  -0.03733 89  THR A CG2 
710  N  N   . MET A  90  ? 0.21585 0.26971 0.16831 0.00811  0.02170  -0.03459 90  MET A N   
711  C  CA  . MET A  90  ? 0.21242 0.26181 0.17304 0.01538  0.01527  -0.03464 90  MET A CA  
712  C  C   . MET A  90  ? 0.20078 0.25411 0.17364 0.01435  0.01556  -0.03556 90  MET A C   
713  O  O   . MET A  90  ? 0.21208 0.26734 0.18554 0.00757  0.01981  -0.03494 90  MET A O   
714  C  CB  . MET A  90  ? 0.25156 0.28223 0.20430 0.01641  0.00953  -0.02870 90  MET A CB  
715  C  CG  . MET A  90  ? 0.27152 0.29729 0.21367 0.01922  0.00737  -0.02785 90  MET A CG  
716  S  SD  . MET A  90  ? 0.32756 0.33127 0.25771 0.01739  0.00226  -0.01987 90  MET A SD  
717  C  CE  . MET A  90  ? 0.32398 0.32731 0.24320 0.00699  0.00907  -0.01742 90  MET A CE  
727  N  N   . ALA A  91  ? 0.18821 0.24232 0.17082 0.02104  0.01078  -0.03690 91  ALA A N   
728  C  CA  . ALA A  91  ? 0.18319 0.23881 0.17644 0.02038  0.01020  -0.03716 91  ALA A CA  
729  C  C   . ALA A  91  ? 0.17444 0.21382 0.16325 0.01721  0.00775  -0.03168 91  ALA A C   
730  O  O   . ALA A  91  ? 0.20197 0.22805 0.18189 0.01827  0.00421  -0.02752 91  ALA A O   
731  C  CB  . ALA A  91  ? 0.18948 0.25043 0.19390 0.02837  0.00564  -0.03978 91  ALA A CB  
737  N  N   . ALA A  92  ? 0.19057 0.17533 0.15559 0.01679  0.00665  -0.00927 92  ALA A N   
738  C  CA  . ALA A  92  ? 0.20804 0.18734 0.16968 0.01382  0.00362  -0.00860 92  ALA A CA  
739  C  C   . ALA A  92  ? 0.19117 0.17191 0.15600 0.01742  0.00134  -0.00742 92  ALA A C   
740  O  O   . ALA A  92  ? 0.19345 0.18284 0.16302 0.02066  0.00172  -0.00724 92  ALA A O   
741  C  CB  . ALA A  92  ? 0.24270 0.22523 0.20364 0.00886  0.00394  -0.00999 92  ALA A CB  
747  N  N   . ILE A  93  ? 0.19569 0.16872 0.15804 0.01697  -0.00093 -0.00633 93  ILE A N   
748  C  CA  . ILE A  93  ? 0.19709 0.17035 0.16177 0.02019  -0.00266 -0.00524 93  ILE A CA  
749  C  C   . ILE A  93  ? 0.18417 0.15257 0.14712 0.01771  -0.00445 -0.00582 93  ILE A C   
750  O  O   . ILE A  93  ? 0.20260 0.16327 0.16236 0.01501  -0.00526 -0.00509 93  ILE A O   
751  C  CB  . ILE A  93  ? 0.19160 0.15984 0.15667 0.02320  -0.00299 -0.00315 93  ILE A CB  
752  C  CG1 . ILE A  93  ? 0.20514 0.17625 0.17245 0.02584  -0.00059 -0.00289 93  ILE A CG1 
753  C  CG2 . ILE A  93  ? 0.20013 0.16917 0.16773 0.02623  -0.00428 -0.00175 93  ILE A CG2 
754  C  CD1 . ILE A  93  ? 0.21425 0.17875 0.18150 0.02735  -0.00044 -0.00170 93  ILE A CD1 
766  N  N   . VAL A  94  ? 0.19021 0.16305 0.15518 0.01872  -0.00495 -0.00704 94  VAL A N   
767  C  CA  . VAL A  94  ? 0.19443 0.16204 0.15874 0.01737  -0.00603 -0.00816 94  VAL A CA  
768  C  C   . VAL A  94  ? 0.20111 0.16810 0.16726 0.02144  -0.00670 -0.00679 94  VAL A C   
769  O  O   . VAL A  94  ? 0.18972 0.16382 0.15763 0.02451  -0.00624 -0.00616 94  VAL A O   
770  C  CB  . VAL A  94  ? 0.20132 0.17429 0.16605 0.01446  -0.00555 -0.01191 94  VAL A CB  
771  C  CG1 . VAL A  94  ? 0.20613 0.17484 0.17099 0.01418  -0.00591 -0.01409 94  VAL A CG1 
772  C  CG2 . VAL A  94  ? 0.21115 0.18248 0.17433 0.00942  -0.00470 -0.01295 94  VAL A CG2 
782  N  N   . VAL A  95  ? 0.19596 0.15507 0.16213 0.02151  -0.00765 -0.00594 95  VAL A N   
783  C  CA  . VAL A  95  ? 0.18520 0.14365 0.15388 0.02497  -0.00796 -0.00475 95  VAL A CA  
784  C  C   . VAL A  95  ? 0.20331 0.15902 0.17281 0.02446  -0.00760 -0.00739 95  VAL A C   
785  O  O   . VAL A  95  ? 0.20762 0.15615 0.17657 0.02210  -0.00799 -0.00787 95  VAL A O   
786  C  CB  . VAL A  95  ? 0.19032 0.14284 0.15981 0.02593  -0.00935 -0.00138 95  VAL A CB  
787  C  CG1 . VAL A  95  ? 0.20148 0.15544 0.17463 0.02940  -0.00925 0.00003  95  VAL A CG1 
788  C  CG2 . VAL A  95  ? 0.20296 0.15594 0.17066 0.02520  -0.00935 -0.00001 95  VAL A CG2 
798  N  N   . ILE A  96  ? 0.19971 0.16092 0.17034 0.02662  -0.00652 -0.00912 96  ILE A N   
799  C  CA  . ILE A  96  ? 0.20312 0.16271 0.17412 0.02597  -0.00535 -0.01315 96  ILE A CA  
800  C  C   . ILE A  96  ? 0.20051 0.16059 0.17429 0.02973  -0.00436 -0.01257 96  ILE A C   
801  O  O   . ILE A  96  ? 0.20740 0.17391 0.18161 0.03230  -0.00405 -0.01034 96  ILE A O   
802  C  CB  . ILE A  96  ? 0.19949 0.16722 0.16800 0.02363  -0.00453 -0.01753 96  ILE A CB  
803  C  CG1 . ILE A  96  ? 0.21113 0.17592 0.17943 0.02195  -0.00298 -0.02299 96  ILE A CG1 
804  C  CG2 . ILE A  96  ? 0.20510 0.18418 0.17297 0.02628  -0.00450 -0.01593 96  ILE A CG2 
805  C  CD1 . ILE A  96  ? 0.24744 0.22112 0.21288 0.01857  -0.00254 -0.02819 96  ILE A CD1 
817  N  N   . PRO A  97  ? 0.21137 0.16494 0.18756 0.03020  -0.00344 -0.01445 97  PRO A N   
818  C  CA  . PRO A  97  ? 0.21943 0.17411 0.19920 0.03387  -0.00190 -0.01428 97  PRO A CA  
819  C  C   . PRO A  97  ? 0.23260 0.19382 0.21024 0.03406  0.00076  -0.01930 97  PRO A C   
820  O  O   . PRO A  97  ? 0.22562 0.19227 0.19893 0.03143  0.00075  -0.02233 97  PRO A O   
821  C  CB  . PRO A  97  ? 0.24276 0.18738 0.22671 0.03446  -0.00200 -0.01403 97  PRO A CB  
822  C  CG  . PRO A  97  ? 0.23994 0.17885 0.22121 0.03060  -0.00205 -0.01694 97  PRO A CG  
823  C  CD  . PRO A  97  ? 0.22430 0.16821 0.20100 0.02771  -0.00368 -0.01573 97  PRO A CD  
831  N  N   . GLY A  98  ? 0.23808 0.20013 0.21864 0.03698  0.00306  -0.02032 98  GLY A N   
832  C  CA  . GLY A  98  ? 0.27298 0.24186 0.25073 0.03720  0.00600  -0.02522 98  GLY A CA  
833  C  C   . GLY A  98  ? 0.25441 0.21708 0.23384 0.03697  0.00896  -0.03156 98  GLY A C   
834  O  O   . GLY A  98  ? 0.24141 0.19372 0.22402 0.03625  0.00859  -0.03222 98  GLY A O   
838  N  N   . TYR A  99  ? 0.26986 0.23903 0.24673 0.03753  0.01223  -0.03635 99  TYR A N   
839  C  CA  . TYR A  99  ? 0.28110 0.24521 0.25883 0.03718  0.01602  -0.04395 99  TYR A CA  
840  C  C   . TYR A  99  ? 0.26718 0.22129 0.25366 0.04092  0.01739  -0.04223 99  TYR A C   
841  O  O   . TYR A  99  ? 0.28889 0.24526 0.28039 0.04472  0.01718  -0.03680 99  TYR A O   
842  C  CB  . TYR A  99  ? 0.30640 0.28113 0.27971 0.03791  0.01952  -0.04815 99  TYR A CB  
843  C  CG  . TYR A  99  ? 0.33263 0.30492 0.30453 0.03687  0.02420  -0.05785 99  TYR A CG  
844  C  CD1 . TYR A  99  ? 0.34751 0.31666 0.31510 0.03190  0.02436  -0.06527 99  TYR A CD1 
845  C  CD2 . TYR A  99  ? 0.40161 0.37548 0.37641 0.04050  0.02883  -0.06005 99  TYR A CD2 
846  C  CE1 . TYR A  99  ? 0.35480 0.32115 0.32079 0.03048  0.02905  -0.07515 99  TYR A CE1 
847  C  CE2 . TYR A  99  ? 0.44530 0.41685 0.41856 0.03962  0.03379  -0.06976 99  TYR A CE2 
848  C  CZ  . TYR A  99  ? 0.46824 0.43549 0.43694 0.03456  0.03383  -0.07743 99  TYR A CZ  
849  O  OH  . TYR A  99  ? 0.48908 0.45321 0.45604 0.03321  0.03920  -0.08818 99  TYR A OH  
859  N  N   . MET A  100 ? 0.27910 0.22227 0.26802 0.03976  0.01876  -0.04660 100 MET A N   
860  C  CA  . MET A  100 ? 0.29787 0.23087 0.29573 0.04361  0.02031  -0.04534 100 MET A CA  
861  C  C   . MET A  100 ? 0.30252 0.23224 0.30547 0.04563  0.01599  -0.03607 100 MET A C   
862  O  O   . MET A  100 ? 0.33614 0.26205 0.34747 0.04997  0.01652  -0.03290 100 MET A O   
863  C  CB  . MET A  100 ? 0.33166 0.26859 0.33376 0.04798  0.02518  -0.04850 100 MET A CB  
864  C  CG  . MET A  100 ? 0.36243 0.30290 0.35850 0.04572  0.02986  -0.05854 100 MET A CG  
865  S  SD  . MET A  100 ? 0.49253 0.41908 0.48795 0.04178  0.03212  -0.06732 100 MET A SD  
866  C  CE  . MET A  100 ? 0.52542 0.43788 0.53395 0.04768  0.03418  -0.06449 100 MET A CE  
876  N  N   . SER A  101 ? 0.25639 0.18802 0.25468 0.04252  0.01179  -0.03189 101 SER A N   
877  C  CA  . SER A  101 ? 0.26091 0.19040 0.26234 0.04361  0.00766  -0.02384 101 SER A CA  
878  C  C   . SER A  101 ? 0.27820 0.20070 0.27630 0.03968  0.00478  -0.02210 101 SER A C   
879  O  O   . SER A  101 ? 0.28974 0.21225 0.28220 0.03546  0.00524  -0.02621 101 SER A O   
880  C  CB  . SER A  101 ? 0.28885 0.22858 0.28826 0.04411  0.00574  -0.01955 101 SER A CB  
881  O  OG  . SER A  101 ? 0.30863 0.25463 0.31178 0.04761  0.00863  -0.02021 101 SER A OG  
887  N  N   . TYR A  102 ? 0.26636 0.18412 0.26789 0.04081  0.00163  -0.01562 102 TYR A N   
888  C  CA  . TYR A  102 ? 0.30016 0.21165 0.29847 0.03731  -0.00118 -0.01252 102 TYR A CA  
889  C  C   . TYR A  102 ? 0.27112 0.18834 0.26576 0.03594  -0.00479 -0.00758 102 TYR A C   
890  O  O   . TYR A  102 ? 0.26136 0.18606 0.25700 0.03790  -0.00544 -0.00580 102 TYR A O   
891  C  CB  . TYR A  102 ? 0.29315 0.19421 0.29751 0.03950  -0.00205 -0.00849 102 TYR A CB  
892  C  CG  . TYR A  102 ? 0.30911 0.20194 0.31745 0.04066  0.00202  -0.01359 102 TYR A CG  
893  C  CD1 . TYR A  102 ? 0.33044 0.21507 0.33541 0.03633  0.00349  -0.01705 102 TYR A CD1 
894  C  CD2 . TYR A  102 ? 0.32259 0.21563 0.33834 0.04575  0.00491  -0.01550 102 TYR A CD2 
895  C  CE1 . TYR A  102 ? 0.34586 0.22160 0.35458 0.03693  0.00766  -0.02251 102 TYR A CE1 
896  C  CE2 . TYR A  102 ? 0.35547 0.23992 0.37507 0.04691  0.00934  -0.02104 102 TYR A CE2 
897  C  CZ  . TYR A  102 ? 0.32049 0.19573 0.33635 0.04233  0.01069  -0.02473 102 TYR A CZ  
898  O  OH  . TYR A  102 ? 0.38940 0.25496 0.40915 0.04303  0.01551  -0.03102 102 TYR A OH  
908  N  N   . GLN A  103 ? 0.27702 0.19004 0.26736 0.03219  -0.00670 -0.00559 103 GLN A N   
909  C  CA  . GLN A  103 ? 0.30021 0.21731 0.28634 0.03028  -0.00952 -0.00189 103 GLN A CA  
910  C  C   . GLN A  103 ? 0.25365 0.17317 0.24315 0.03304  -0.01217 0.00317  103 GLN A C   
911  O  O   . GLN A  103 ? 0.27723 0.20273 0.26463 0.03261  -0.01328 0.00435  103 GLN A O   
912  C  CB  . GLN A  103 ? 0.43052 0.34013 0.41321 0.02648  -0.01066 0.00013  103 GLN A CB  
913  C  CG  . GLN A  103 ? 0.43377 0.34611 0.41073 0.02311  -0.01213 0.00179  103 GLN A CG  
914  C  CD  . GLN A  103 ? 0.31728 0.22147 0.29137 0.01967  -0.01314 0.00505  103 GLN A CD  
915  O  OE1 . GLN A  103 ? 0.30590 0.21102 0.27603 0.01785  -0.01509 0.00842  103 GLN A OE1 
916  N  NE2 . GLN A  103 ? 0.35580 0.25202 0.33170 0.01861  -0.01141 0.00375  103 GLN A NE2 
925  N  N   . SER A  104 ? 0.25680 0.17202 0.25226 0.03590  -0.01320 0.00621  104 SER A N   
926  C  CA  . SER A  104 ? 0.25676 0.17542 0.25602 0.03790  -0.01636 0.01120  104 SER A CA  
927  C  C   . SER A  104 ? 0.26669 0.19394 0.26851 0.03980  -0.01518 0.00983  104 SER A C   
928  O  O   . SER A  104 ? 0.27539 0.20678 0.27795 0.03949  -0.01764 0.01290  104 SER A O   
929  C  CB  . SER A  104 ? 0.28269 0.19665 0.28951 0.04133  -0.01752 0.01480  104 SER A CB  
930  O  OG  . SER A  104 ? 0.32729 0.24034 0.34004 0.04484  -0.01363 0.01095  104 SER A OG  
936  N  N   . SER A  105 ? 0.23418 0.16438 0.23657 0.04113  -0.01136 0.00518  105 SER A N   
937  C  CA  . SER A  105 ? 0.24462 0.18299 0.24910 0.04287  -0.00983 0.00462  105 SER A CA  
938  C  C   . SER A  105 ? 0.22601 0.16874 0.22542 0.04051  -0.01089 0.00563  105 SER A C   
939  O  O   . SER A  105 ? 0.24967 0.19793 0.25161 0.04167  -0.01035 0.00695  105 SER A O   
940  C  CB  . SER A  105 ? 0.24278 0.18410 0.24728 0.04440  -0.00544 -0.00052 105 SER A CB  
941  O  OG  . SER A  105 ? 0.25463 0.19590 0.25214 0.04156  -0.00434 -0.00434 105 SER A OG  
947  N  N   . ILE A  106 ? 0.20490 0.14533 0.19782 0.03733  -0.01178 0.00491  106 ILE A N   
948  C  CA  . ILE A  106 ? 0.20574 0.14974 0.19447 0.03558  -0.01216 0.00547  106 ILE A CA  
949  C  C   . ILE A  106 ? 0.21550 0.15562 0.20062 0.03262  -0.01501 0.00770  106 ILE A C   
950  O  O   . ILE A  106 ? 0.22582 0.16756 0.20695 0.03088  -0.01483 0.00733  106 ILE A O   
951  C  CB  . ILE A  106 ? 0.22383 0.17181 0.20840 0.03492  -0.00977 0.00208  106 ILE A CB  
952  C  CG1 . ILE A  106 ? 0.22151 0.16594 0.20319 0.03279  -0.00918 -0.00116 106 ILE A CG1 
953  C  CG2 . ILE A  106 ? 0.24211 0.19624 0.22912 0.03774  -0.00711 0.00075  106 ILE A CG2 
954  C  CD1 . ILE A  106 ? 0.23914 0.17829 0.21723 0.02939  -0.01095 -0.00007 106 ILE A CD1 
966  N  N   . SER A  107 ? 0.21444 0.15012 0.20135 0.03236  -0.01758 0.01035  107 SER A N   
967  C  CA  . SER A  107 ? 0.22043 0.15264 0.20257 0.02915  -0.02032 0.01259  107 SER A CA  
968  C  C   . SER A  107 ? 0.21971 0.15483 0.19981 0.02751  -0.02166 0.01350  107 SER A C   
969  O  O   . SER A  107 ? 0.23580 0.16920 0.20988 0.02434  -0.02253 0.01356  107 SER A O   
970  C  CB  . SER A  107 ? 0.24688 0.17476 0.23180 0.02972  -0.02322 0.01639  107 SER A CB  
971  O  OG  . SER A  107 ? 0.27980 0.21107 0.27160 0.03225  -0.02499 0.01882  107 SER A OG  
977  N  N   . PHE A  108 ? 0.20100 0.14017 0.18597 0.02925  -0.02149 0.01396  108 PHE A N   
978  C  CA  . PHE A  108 ? 0.20062 0.14145 0.18410 0.02729  -0.02219 0.01409  108 PHE A CA  
979  C  C   . PHE A  108 ? 0.19092 0.13098 0.16822 0.02549  -0.02009 0.01162  108 PHE A C   
980  O  O   . PHE A  108 ? 0.21166 0.15048 0.18497 0.02274  -0.02087 0.01115  108 PHE A O   
981  C  CB  . PHE A  108 ? 0.20237 0.14744 0.19207 0.02956  -0.02048 0.01425  108 PHE A CB  
982  C  CG  . PHE A  108 ? 0.19623 0.14210 0.18510 0.02812  -0.01933 0.01358  108 PHE A CG  
983  C  CD1 . PHE A  108 ? 0.20130 0.14700 0.19134 0.02544  -0.02178 0.01441  108 PHE A CD1 
984  C  CD2 . PHE A  108 ? 0.18988 0.13688 0.17763 0.02948  -0.01591 0.01229  108 PHE A CD2 
985  C  CE1 . PHE A  108 ? 0.20025 0.14530 0.19017 0.02391  -0.02016 0.01325  108 PHE A CE1 
986  C  CE2 . PHE A  108 ? 0.19710 0.14364 0.18526 0.02873  -0.01438 0.01212  108 PHE A CE2 
987  C  CZ  . PHE A  108 ? 0.20573 0.15059 0.19516 0.02583  -0.01629 0.01234  108 PHE A CZ  
997  N  N   . TRP A  109 ? 0.19830 0.14000 0.17515 0.02712  -0.01718 0.00970  109 TRP A N   
998  C  CA  . TRP A  109 ? 0.18576 0.12871 0.15890 0.02639  -0.01491 0.00772  109 TRP A CA  
999  C  C   . TRP A  109 ? 0.19539 0.13559 0.16247 0.02309  -0.01539 0.00679  109 TRP A C   
1000 O  O   . TRP A  109 ? 0.23006 0.17119 0.19441 0.02214  -0.01365 0.00524  109 TRP A O   
1001 C  CB  . TRP A  109 ? 0.19351 0.14085 0.16823 0.02894  -0.01236 0.00640  109 TRP A CB  
1002 C  CG  . TRP A  109 ? 0.19056 0.14143 0.16991 0.03189  -0.01107 0.00766  109 TRP A CG  
1003 C  CD1 . TRP A  109 ? 0.19614 0.14904 0.17944 0.03401  -0.01074 0.00830  109 TRP A CD1 
1004 C  CD2 . TRP A  109 ? 0.19373 0.14599 0.17443 0.03288  -0.00955 0.00873  109 TRP A CD2 
1005 N  NE1 . TRP A  109 ? 0.20065 0.15685 0.18715 0.03592  -0.00911 0.01000  109 TRP A NE1 
1006 C  CE2 . TRP A  109 ? 0.19077 0.14603 0.17592 0.03526  -0.00847 0.01054  109 TRP A CE2 
1007 C  CE3 . TRP A  109 ? 0.21003 0.16069 0.18894 0.03198  -0.00858 0.00828  109 TRP A CE3 
1008 C  CZ2 . TRP A  109 ? 0.19761 0.15403 0.18530 0.03661  -0.00658 0.01255  109 TRP A CZ2 
1009 C  CZ3 . TRP A  109 ? 0.22152 0.17260 0.20350 0.03366  -0.00666 0.00981  109 TRP A CZ3 
1010 C  CH2 . TRP A  109 ? 0.21923 0.17292 0.20553 0.03582  -0.00580 0.01225  109 TRP A CH2 
1021 N  N   . GLY A  110 ? 0.21007 0.14689 0.17544 0.02151  -0.01740 0.00803  110 GLY A N   
1022 C  CA  . GLY A  110 ? 0.21177 0.14595 0.17104 0.01797  -0.01769 0.00793  110 GLY A CA  
1023 C  C   . GLY A  110 ? 0.21261 0.14589 0.16740 0.01530  -0.01883 0.00822  110 GLY A C   
1024 O  O   . GLY A  110 ? 0.23555 0.16991 0.18672 0.01380  -0.01658 0.00591  110 GLY A O   
1028 N  N   . PRO A  111 ? 0.20754 0.13956 0.16287 0.01468  -0.02222 0.01068  111 PRO A N   
1029 C  CA  . PRO A  111 ? 0.22033 0.15209 0.17056 0.01136  -0.02352 0.01014  111 PRO A CA  
1030 C  C   . PRO A  111 ? 0.21566 0.14884 0.16749 0.01194  -0.02103 0.00695  111 PRO A C   
1031 O  O   . PRO A  111 ? 0.22055 0.15293 0.16728 0.00928  -0.01976 0.00440  111 PRO A O   
1032 C  CB  . PRO A  111 ? 0.23562 0.16747 0.18774 0.01088  -0.02828 0.01377  111 PRO A CB  
1033 C  CG  . PRO A  111 ? 0.24723 0.17740 0.20319 0.01338  -0.02930 0.01698  111 PRO A CG  
1034 C  CD  . PRO A  111 ? 0.21860 0.14957 0.17844 0.01633  -0.02527 0.01412  111 PRO A CD  
1042 N  N   . ARG A  112 ? 0.20870 0.14363 0.16759 0.01539  -0.01993 0.00705  112 ARG A N   
1043 C  CA  . ARG A  112 ? 0.21108 0.14621 0.17223 0.01594  -0.01768 0.00503  112 ARG A CA  
1044 C  C   . ARG A  112 ? 0.21108 0.14624 0.16975 0.01651  -0.01360 0.00227  112 ARG A C   
1045 O  O   . ARG A  112 ? 0.22453 0.15780 0.18146 0.01519  -0.01169 -0.00029 112 ARG A O   
1046 C  CB  . ARG A  112 ? 0.20273 0.14001 0.17173 0.01938  -0.01707 0.00663  112 ARG A CB  
1047 C  CG  . ARG A  112 ? 0.20509 0.14150 0.17696 0.01982  -0.01456 0.00542  112 ARG A CG  
1048 C  CD  . ARG A  112 ? 0.22689 0.16030 0.19623 0.01552  -0.01590 0.00340  112 ARG A CD  
1049 N  NE  . ARG A  112 ? 0.22130 0.15303 0.19551 0.01556  -0.01393 0.00275  112 ARG A NE  
1050 C  CZ  . ARG A  112 ? 0.21756 0.15091 0.19783 0.01543  -0.01532 0.00475  112 ARG A CZ  
1051 N  NH1 . ARG A  112 ? 0.22734 0.16446 0.20992 0.01552  -0.01890 0.00732  112 ARG A NH1 
1052 N  NH2 . ARG A  112 ? 0.22554 0.15653 0.21029 0.01511  -0.01284 0.00427  112 ARG A NH2 
1066 N  N   . LEU A  113 ? 0.21030 0.14787 0.16935 0.01843  -0.01207 0.00245  113 LEU A N   
1067 C  CA  . LEU A  113 ? 0.20324 0.14260 0.16091 0.01904  -0.00849 0.00018  113 LEU A CA  
1068 C  C   . LEU A  113 ? 0.20588 0.14384 0.15661 0.01515  -0.00814 -0.00158 113 LEU A C   
1069 O  O   . LEU A  113 ? 0.21277 0.15067 0.16169 0.01462  -0.00514 -0.00428 113 LEU A O   
1070 C  CB  . LEU A  113 ? 0.20238 0.14654 0.16330 0.02192  -0.00732 0.00081  113 LEU A CB  
1071 C  CG  . LEU A  113 ? 0.21987 0.16685 0.18675 0.02607  -0.00636 0.00231  113 LEU A CG  
1072 C  CD1 . LEU A  113 ? 0.22537 0.17719 0.19393 0.02777  -0.00659 0.00286  113 LEU A CD1 
1073 C  CD2 . LEU A  113 ? 0.26577 0.21404 0.23497 0.02842  -0.00310 0.00174  113 LEU A CD2 
1085 N  N   . ALA A  114 ? 0.20966 0.14640 0.15653 0.01253  -0.01069 0.00004  114 ALA A N   
1086 C  CA  . ALA A  114 ? 0.20950 0.14561 0.14931 0.00868  -0.00977 -0.00105 114 ALA A CA  
1087 C  C   . ALA A  114 ? 0.22507 0.15896 0.15936 0.00565  -0.00975 -0.00307 114 ALA A C   
1088 O  O   . ALA A  114 ? 0.23459 0.16902 0.16397 0.00344  -0.00679 -0.00580 114 ALA A O   
1089 C  CB  . ALA A  114 ? 0.21933 0.15352 0.15606 0.00637  -0.01255 0.00208  114 ALA A CB  
1095 N  N   . SER A  115 ? 0.21944 0.15142 0.15447 0.00515  -0.01287 -0.00214 115 SER A N   
1096 C  CA  . SER A  115 ? 0.22594 0.15614 0.15581 0.00164  -0.01325 -0.00479 115 SER A CA  
1097 C  C   . SER A  115 ? 0.22769 0.15677 0.15945 0.00282  -0.00855 -0.00949 115 SER A C   
1098 O  O   . SER A  115 ? 0.23830 0.16530 0.16516 -0.00047 -0.00771 -0.01315 115 SER A O   
1099 C  CB  . SER A  115 ? 0.22745 0.15721 0.15916 0.00061  -0.01812 -0.00257 115 SER A CB  
1100 O  OG  . SER A  115 ? 0.23005 0.15985 0.17039 0.00402  -0.01759 -0.00239 115 SER A OG  
1106 N  N   . HIS A  116 ? 0.22982 0.16031 0.16844 0.00743  -0.00534 -0.00951 116 HIS A N   
1107 C  CA  . HIS A  116 ? 0.23714 0.16659 0.17868 0.00961  -0.00038 -0.01303 116 HIS A CA  
1108 C  C   . HIS A  116 ? 0.24157 0.17457 0.18236 0.01079  0.00363  -0.01455 116 HIS A C   
1109 O  O   . HIS A  116 ? 0.28962 0.22322 0.23519 0.01420  0.00786  -0.01637 116 HIS A O   
1110 C  CB  . HIS A  116 ? 0.22908 0.15822 0.17958 0.01422  0.00025  -0.01109 116 HIS A CB  
1111 C  CG  . HIS A  116 ? 0.22012 0.14525 0.17236 0.01266  -0.00156 -0.01131 116 HIS A CG  
1112 N  ND1 . HIS A  116 ? 0.23958 0.15973 0.19118 0.01091  0.00112  -0.01549 116 HIS A ND1 
1113 C  CD2 . HIS A  116 ? 0.22123 0.14681 0.17619 0.01217  -0.00554 -0.00828 116 HIS A CD2 
1114 C  CE1 . HIS A  116 ? 0.24175 0.15964 0.19572 0.00901  -0.00141 -0.01490 116 HIS A CE1 
1115 N  NE2 . HIS A  116 ? 0.22814 0.14981 0.18449 0.00993  -0.00542 -0.01035 116 HIS A NE2 
1123 N  N   . GLY A  117 ? 0.22370 0.15920 0.15933 0.00808  0.00253  -0.01354 117 GLY A N   
1124 C  CA  . GLY A  117 ? 0.21867 0.15817 0.15326 0.00801  0.00661  -0.01546 117 GLY A CA  
1125 C  C   . GLY A  117 ? 0.21682 0.16207 0.15759 0.01119  0.00702  -0.01319 117 GLY A C   
1126 O  O   . GLY A  117 ? 0.23300 0.18278 0.17841 0.01404  0.01086  -0.01471 117 GLY A O   
1130 N  N   . PHE A  118 ? 0.21401 0.15957 0.15525 0.01076  0.00326  -0.00985 118 PHE A N   
1131 C  CA  . PHE A  118 ? 0.19754 0.14843 0.14354 0.01263  0.00314  -0.00835 118 PHE A CA  
1132 C  C   . PHE A  118 ? 0.21859 0.16788 0.16033 0.00875  0.00059  -0.00645 118 PHE A C   
1133 O  O   . PHE A  118 ? 0.23210 0.17610 0.16939 0.00644  -0.00239 -0.00467 118 PHE A O   
1134 C  CB  . PHE A  118 ? 0.20313 0.15508 0.15565 0.01706  0.00147  -0.00637 118 PHE A CB  
1135 C  CG  . PHE A  118 ? 0.21692 0.16997 0.17454 0.02131  0.00401  -0.00698 118 PHE A CG  
1136 C  CD1 . PHE A  118 ? 0.23215 0.19189 0.19460 0.02444  0.00710  -0.00756 118 PHE A CD1 
1137 C  CD2 . PHE A  118 ? 0.22283 0.17062 0.18135 0.02232  0.00346  -0.00666 118 PHE A CD2 
1138 C  CE1 . PHE A  118 ? 0.23715 0.19716 0.20490 0.02888  0.00966  -0.00733 118 PHE A CE1 
1139 C  CE2 . PHE A  118 ? 0.23534 0.18261 0.19876 0.02601  0.00634  -0.00698 118 PHE A CE2 
1140 C  CZ  . PHE A  118 ? 0.25842 0.21142 0.22653 0.02965  0.00954  -0.00706 118 PHE A CZ  
1150 N  N   . VAL A  119 ? 0.20714 0.16105 0.15068 0.00789  0.00166  -0.00659 119 VAL A N   
1151 C  CA  . VAL A  119 ? 0.20348 0.15488 0.14491 0.00475  -0.00048 -0.00468 119 VAL A CA  
1152 C  C   . VAL A  119 ? 0.20965 0.16142 0.15637 0.00781  -0.00267 -0.00379 119 VAL A C   
1153 O  O   . VAL A  119 ? 0.21373 0.17184 0.16543 0.01043  -0.00151 -0.00509 119 VAL A O   
1154 C  CB  . VAL A  119 ? 0.21359 0.16968 0.15457 0.00136  0.00221  -0.00592 119 VAL A CB  
1155 C  CG1 . VAL A  119 ? 0.24067 0.19303 0.18058 -0.00191 0.00045  -0.00415 119 VAL A CG1 
1156 C  CG2 . VAL A  119 ? 0.25329 0.20963 0.18864 -0.00178 0.00506  -0.00697 119 VAL A CG2 
1166 N  N   . VAL A  120 ? 0.21053 0.15634 0.15634 0.00776  -0.00572 -0.00151 120 VAL A N   
1167 C  CA  . VAL A  120 ? 0.20282 0.14869 0.15352 0.01114  -0.00735 -0.00098 120 VAL A CA  
1168 C  C   . VAL A  120 ? 0.21145 0.15244 0.16191 0.00944  -0.00898 0.00027  120 VAL A C   
1169 O  O   . VAL A  120 ? 0.24422 0.17915 0.19165 0.00776  -0.01091 0.00297  120 VAL A O   
1170 C  CB  . VAL A  120 ? 0.21133 0.15493 0.16345 0.01393  -0.00902 0.00047  120 VAL A CB  
1171 C  CG1 . VAL A  120 ? 0.22274 0.16786 0.18013 0.01750  -0.00980 0.00087  120 VAL A CG1 
1172 C  CG2 . VAL A  120 ? 0.21995 0.16587 0.17201 0.01506  -0.00705 -0.00085 120 VAL A CG2 
1182 N  N   . MET A  121 ? 0.19912 0.14250 0.15289 0.01001  -0.00833 -0.00157 121 MET A N   
1183 C  CA  . MET A  121 ? 0.21993 0.15751 0.17436 0.00868  -0.00919 -0.00119 121 MET A CA  
1184 C  C   . MET A  121 ? 0.20606 0.14409 0.16496 0.01255  -0.00983 -0.00201 121 MET A C   
1185 O  O   . MET A  121 ? 0.21250 0.15729 0.17363 0.01416  -0.00867 -0.00468 121 MET A O   
1186 C  CB  . MET A  121 ? 0.22841 0.16707 0.18235 0.00464  -0.00736 -0.00363 121 MET A CB  
1187 C  CG  . MET A  121 ? 0.23028 0.16064 0.18486 0.00282  -0.00773 -0.00322 121 MET A CG  
1188 S  SD  . MET A  121 ? 0.25626 0.18621 0.21016 -0.00351 -0.00530 -0.00601 121 MET A SD  
1189 C  CE  . MET A  121 ? 0.28672 0.22975 0.24387 -0.00297 -0.00403 -0.01152 121 MET A CE  
1199 N  N   . THR A  122 ? 0.21519 0.14697 0.17546 0.01410  -0.01163 0.00052  122 THR A N   
1200 C  CA  . THR A  122 ? 0.21151 0.14301 0.17638 0.01745  -0.01157 -0.00052 122 THR A CA  
1201 C  C   . THR A  122 ? 0.23146 0.15820 0.19716 0.01552  -0.01032 -0.00295 122 THR A C   
1202 O  O   . THR A  122 ? 0.26821 0.18762 0.23248 0.01292  -0.01076 -0.00099 122 THR A O   
1203 C  CB  . THR A  122 ? 0.21226 0.14003 0.17965 0.02008  -0.01384 0.00325  122 THR A CB  
1204 O  OG1 . THR A  122 ? 0.23551 0.15599 0.20141 0.01824  -0.01561 0.00664  122 THR A OG1 
1205 C  CG2 . THR A  122 ? 0.21333 0.14536 0.18011 0.02118  -0.01483 0.00480  122 THR A CG2 
1213 N  N   . ILE A  123 ? 0.21494 0.14550 0.18266 0.01645  -0.00860 -0.00721 123 ILE A N   
1214 C  CA  . ILE A  123 ? 0.23528 0.16147 0.20345 0.01369  -0.00694 -0.01094 123 ILE A CA  
1215 C  C   . ILE A  123 ? 0.24403 0.16670 0.21615 0.01666  -0.00578 -0.01326 123 ILE A C   
1216 O  O   . ILE A  123 ? 0.24751 0.17452 0.22182 0.02068  -0.00577 -0.01308 123 ILE A O   
1217 C  CB  . ILE A  123 ? 0.23203 0.16610 0.19833 0.01025  -0.00549 -0.01572 123 ILE A CB  
1218 C  CG1 . ILE A  123 ? 0.22329 0.16782 0.19030 0.01317  -0.00508 -0.01832 123 ILE A CG1 
1219 C  CG2 . ILE A  123 ? 0.22496 0.16230 0.18836 0.00708  -0.00585 -0.01383 123 ILE A CG2 
1220 C  CD1 . ILE A  123 ? 0.24683 0.19999 0.21261 0.00983  -0.00410 -0.02346 123 ILE A CD1 
1232 N  N   . ASP A  124 ? 0.24342 0.15776 0.21669 0.01443  -0.00429 -0.01564 124 ASP A N   
1233 C  CA  . ASP A  124 ? 0.26928 0.18054 0.24573 0.01590  -0.00187 -0.02053 124 ASP A CA  
1234 C  C   . ASP A  124 ? 0.25920 0.17591 0.23302 0.01171  0.00006  -0.02768 124 ASP A C   
1235 O  O   . ASP A  124 ? 0.26975 0.18887 0.24077 0.00696  -0.00029 -0.02840 124 ASP A O   
1236 C  CB  . ASP A  124 ? 0.25884 0.15642 0.23890 0.01606  -0.00100 -0.01911 124 ASP A CB  
1237 C  CG  . ASP A  124 ? 0.28596 0.17995 0.27013 0.02114  -0.00297 -0.01271 124 ASP A CG  
1238 O  OD1 . ASP A  124 ? 0.32671 0.22584 0.31402 0.02554  -0.00265 -0.01330 124 ASP A OD1 
1239 O  OD2 . ASP A  124 ? 0.30717 0.19404 0.29153 0.02055  -0.00483 -0.00697 124 ASP A OD2 
1244 N  N   . THR A  125 ? 0.26961 0.18890 0.24446 0.01325  0.00216  -0.03309 125 THR A N   
1245 C  CA  . THR A  125 ? 0.27526 0.20000 0.24738 0.00892  0.00381  -0.04064 125 THR A CA  
1246 C  C   . THR A  125 ? 0.29346 0.20598 0.26741 0.00535  0.00645  -0.04551 125 THR A C   
1247 O  O   . THR A  125 ? 0.32070 0.22062 0.29866 0.00753  0.00742  -0.04303 125 THR A O   
1248 C  CB  . THR A  125 ? 0.27733 0.21232 0.24812 0.01168  0.00486  -0.04445 125 THR A CB  
1249 O  OG1 . THR A  125 ? 0.29959 0.22852 0.27415 0.01642  0.00682  -0.04451 125 THR A OG1 
1250 C  CG2 . THR A  125 ? 0.30044 0.24732 0.26938 0.01431  0.00247  -0.03954 125 THR A CG2 
1258 N  N   . ASN A  126 ? 0.29678 0.21327 0.26823 -0.00021 0.00774  -0.05277 126 ASN A N   
1259 C  CA  . ASN A  126 ? 0.31150 0.21588 0.28475 -0.00444 0.01076  -0.05853 126 ASN A CA  
1260 C  C   . ASN A  126 ? 0.32965 0.22500 0.30658 0.00005  0.01395  -0.06166 126 ASN A C   
1261 O  O   . ASN A  126 ? 0.35523 0.23537 0.33650 0.00034  0.01605  -0.06122 126 ASN A O   
1262 C  CB  . ASN A  126 ? 0.31518 0.22796 0.28500 -0.01131 0.01150  -0.06706 126 ASN A CB  
1263 C  CG  . ASN A  126 ? 0.34585 0.26559 0.31402 -0.01659 0.00919  -0.06466 126 ASN A CG  
1264 O  OD1 . ASN A  126 ? 0.35736 0.27045 0.32684 -0.01723 0.00837  -0.05833 126 ASN A OD1 
1265 N  ND2 . ASN A  126 ? 0.38944 0.32390 0.35469 -0.02044 0.00816  -0.06962 126 ASN A ND2 
1272 N  N   . ARG A  127 ? 0.31541 0.22018 0.29094 0.00369  0.01469  -0.06472 127 ARG A N   
1273 C  CA  . ARG A  127 ? 0.32578 0.22471 0.30514 0.00887  0.01802  -0.06729 127 ARG A CA  
1274 C  C   . ARG A  127 ? 0.30577 0.21559 0.28498 0.01496  0.01647  -0.06231 127 ARG A C   
1275 O  O   . ARG A  127 ? 0.30790 0.23117 0.28244 0.01419  0.01410  -0.06091 127 ARG A O   
1276 C  CB  . ARG A  127 ? 0.36343 0.26339 0.34034 0.00576  0.02206  -0.07887 127 ARG A CB  
1277 C  CG  . ARG A  127 ? 0.39206 0.27959 0.37000 -0.00052 0.02462  -0.08541 127 ARG A CG  
1278 C  CD  . ARG A  127 ? 0.49334 0.38372 0.46777 -0.00413 0.02854  -0.09804 127 ARG A CD  
1279 N  NE  . ARG A  127 ? 0.64057 0.51528 0.61772 -0.00924 0.03233  -0.10522 127 ARG A NE  
1280 C  CZ  . ARG A  127 ? 0.62121 0.49486 0.59622 -0.01765 0.03154  -0.10876 127 ARG A CZ  
1281 N  NH1 . ARG A  127 ? 0.66704 0.55491 0.63765 -0.02149 0.02705  -0.10567 127 ARG A NH1 
1282 N  NH2 . ARG A  127 ? 0.50234 0.36030 0.48037 -0.02237 0.03567  -0.11571 127 ARG A NH2 
1296 N  N   . ILE A  128 ? 0.29338 0.19757 0.27848 0.02111  0.01786  -0.05916 128 ILE A N   
1297 C  CA  . ILE A  128 ? 0.31127 0.22577 0.29686 0.02621  0.01660  -0.05431 128 ILE A CA  
1298 C  C   . ILE A  128 ? 0.29079 0.21691 0.27189 0.02629  0.01910  -0.06058 128 ILE A C   
1299 O  O   . ILE A  128 ? 0.30120 0.23826 0.28057 0.02882  0.01780  -0.05672 128 ILE A O   
1300 C  CB  . ILE A  128 ? 0.33357 0.24131 0.32750 0.03258  0.01715  -0.04897 128 ILE A CB  
1301 C  CG1 . ILE A  128 ? 0.32297 0.22223 0.32208 0.03498  0.02237  -0.05539 128 ILE A CG1 
1302 C  CG2 . ILE A  128 ? 0.32114 0.21996 0.31804 0.03241  0.01367  -0.04129 128 ILE A CG2 
1303 C  CD1 . ILE A  128 ? 0.35946 0.25371 0.36836 0.04187  0.02291  -0.04982 128 ILE A CD1 
1315 N  N   . SER A  129 ? 0.31835 0.24275 0.29667 0.02279  0.02249  -0.07017 129 SER A N   
1316 C  CA  . SER A  129 ? 0.28315 0.21953 0.25543 0.02182  0.02474  -0.07680 129 SER A CA  
1317 C  C   . SER A  129 ? 0.29712 0.24695 0.26143 0.01689  0.02142  -0.07752 129 SER A C   
1318 O  O   . SER A  129 ? 0.32404 0.28551 0.28229 0.01569  0.02257  -0.08231 129 SER A O   
1319 C  CB  . SER A  129 ? 0.33565 0.26453 0.30794 0.01974  0.03008  -0.08794 129 SER A CB  
1320 O  OG  . SER A  129 ? 0.38300 0.30208 0.35526 0.01392  0.02984  -0.09204 129 SER A OG  
1326 N  N   . ASP A  130 ? 0.29997 0.24940 0.26421 0.01416  0.01744  -0.07272 130 ASP A N   
1327 C  CA  . ASP A  130 ? 0.29423 0.25683 0.25248 0.00970  0.01442  -0.07348 130 ASP A CA  
1328 C  C   . ASP A  130 ? 0.27217 0.24976 0.22702 0.01332  0.01286  -0.06872 130 ASP A C   
1329 O  O   . ASP A  130 ? 0.28422 0.26103 0.24227 0.01869  0.01256  -0.06171 130 ASP A O   
1330 C  CB  . ASP A  130 ? 0.29997 0.25933 0.26009 0.00709  0.01100  -0.06822 130 ASP A CB  
1331 C  CG  . ASP A  130 ? 0.33864 0.28508 0.30090 0.00191  0.01243  -0.07292 130 ASP A CG  
1332 O  OD1 . ASP A  130 ? 0.35538 0.29727 0.31681 -0.00108 0.01570  -0.08176 130 ASP A OD1 
1333 O  OD2 . ASP A  130 ? 0.32217 0.26259 0.28683 0.00052  0.01054  -0.06772 130 ASP A OD2 
1338 N  N   . GLN A  131 ? 0.28465 0.27631 0.23310 0.01009  0.01180  -0.07241 131 GLN A N   
1339 C  CA  . GLN A  131 ? 0.27197 0.27882 0.21630 0.01305  0.01049  -0.06803 131 GLN A CA  
1340 C  C   . GLN A  131 ? 0.26765 0.28259 0.21234 0.01312  0.00603  -0.06061 131 GLN A C   
1341 O  O   . GLN A  131 ? 0.26482 0.27530 0.21209 0.01016  0.00420  -0.06015 131 GLN A O   
1342 C  CB  . GLN A  131 ? 0.29939 0.31776 0.23610 0.00960  0.01181  -0.07613 131 GLN A CB  
1343 C  CG  . GLN A  131 ? 0.36623 0.37634 0.30253 0.00940  0.01702  -0.08471 131 GLN A CG  
1344 C  CD  . GLN A  131 ? 0.42139 0.43017 0.35988 0.01582  0.01996  -0.08056 131 GLN A CD  
1345 O  OE1 . GLN A  131 ? 0.43964 0.46097 0.37335 0.01786  0.02014  -0.07788 131 GLN A OE1 
1346 N  NE2 . GLN A  131 ? 0.53479 0.52891 0.48094 0.01907  0.02233  -0.07953 131 GLN A NE2 
1355 N  N   . PRO A  132 ? 0.24838 0.27526 0.19084 0.01654  0.00457  -0.05455 132 PRO A N   
1356 C  CA  . PRO A  132 ? 0.24222 0.27496 0.18664 0.01788  0.00102  -0.04686 132 PRO A CA  
1357 C  C   . PRO A  132 ? 0.26818 0.30855 0.21162 0.01289  -0.00175 -0.04960 132 PRO A C   
1358 O  O   . PRO A  132 ? 0.25103 0.28938 0.19840 0.01298  -0.00359 -0.04531 132 PRO A O   
1359 C  CB  . PRO A  132 ? 0.23878 0.28283 0.18065 0.02233  0.00072  -0.04069 132 PRO A CB  
1360 C  CG  . PRO A  132 ? 0.25797 0.29583 0.19975 0.02486  0.00446  -0.04218 132 PRO A CG  
1361 C  CD  . PRO A  132 ? 0.25439 0.28677 0.19416 0.02052  0.00684  -0.05279 132 PRO A CD  
1369 N  N   . PRO A  133 ? 0.24932 0.29962 0.18779 0.00834  -0.00214 -0.05656 133 PRO A N   
1370 C  CA  . PRO A  133 ? 0.24230 0.30074 0.18123 0.00304  -0.00501 -0.05909 133 PRO A CA  
1371 C  C   . PRO A  133 ? 0.26111 0.30579 0.20477 -0.00077 -0.00427 -0.06166 133 PRO A C   
1372 O  O   . PRO A  133 ? 0.27813 0.32479 0.22550 -0.00185 -0.00623 -0.05814 133 PRO A O   
1373 C  CB  . PRO A  133 ? 0.30313 0.37267 0.23545 -0.00195 -0.00506 -0.06773 133 PRO A CB  
1374 C  CG  . PRO A  133 ? 0.29452 0.36815 0.22185 0.00244  -0.00325 -0.06624 133 PRO A CG  
1375 C  CD  . PRO A  133 ? 0.26007 0.31669 0.19217 0.00763  -0.00017 -0.06213 133 PRO A CD  
1383 N  N   . SER A  134 ? 0.26853 0.29873 0.21246 -0.00246 -0.00109 -0.06726 134 SER A N   
1384 C  CA  . SER A  134 ? 0.25669 0.27214 0.20503 -0.00551 -0.00011 -0.06834 134 SER A CA  
1385 C  C   . SER A  134 ? 0.25497 0.26324 0.20765 -0.00093 -0.00096 -0.05920 134 SER A C   
1386 O  O   . SER A  134 ? 0.26791 0.27267 0.22332 -0.00355 -0.00185 -0.05730 134 SER A O   
1387 C  CB  . SER A  134 ? 0.32963 0.33026 0.27812 -0.00656 0.00378  -0.07489 134 SER A CB  
1388 O  OG  . SER A  134 ? 0.35713 0.34240 0.31003 -0.00878 0.00481  -0.07446 134 SER A OG  
1394 N  N   . ARG A  135 ? 0.26679 0.27334 0.21997 0.00541  -0.00055 -0.05375 135 ARG A N   
1395 C  CA  . ARG A  135 ? 0.23548 0.23554 0.19234 0.00950  -0.00141 -0.04560 135 ARG A CA  
1396 C  C   . ARG A  135 ? 0.24222 0.25243 0.19981 0.00920  -0.00394 -0.04132 135 ARG A C   
1397 O  O   . ARG A  135 ? 0.24178 0.24618 0.20186 0.00883  -0.00440 -0.03801 135 ARG A O   
1398 C  CB  . ARG A  135 ? 0.23275 0.23138 0.19015 0.01558  -0.00047 -0.04138 135 ARG A CB  
1399 C  CG  . ARG A  135 ? 0.25949 0.24619 0.21859 0.01669  0.00227  -0.04438 135 ARG A CG  
1400 C  CD  . ARG A  135 ? 0.24972 0.23527 0.21085 0.02243  0.00330  -0.03983 135 ARG A CD  
1401 N  NE  . ARG A  135 ? 0.26814 0.24525 0.23108 0.02304  0.00635  -0.04445 135 ARG A NE  
1402 C  CZ  . ARG A  135 ? 0.26760 0.23245 0.23556 0.02470  0.00704  -0.04281 135 ARG A CZ  
1403 N  NH1 . ARG A  135 ? 0.25442 0.21426 0.22531 0.02589  0.00470  -0.03636 135 ARG A NH1 
1404 N  NH2 . ARG A  135 ? 0.28379 0.24148 0.25393 0.02526  0.01019  -0.04780 135 ARG A NH2 
1418 N  N   . ARG A  136 ? 0.23807 0.26362 0.19359 0.00952  -0.00541 -0.04129 136 ARG A N   
1419 C  CA  . ARG A  136 ? 0.23187 0.26833 0.18937 0.00966  -0.00761 -0.03744 136 ARG A CA  
1420 C  C   . ARG A  136 ? 0.24515 0.27983 0.20481 0.00386  -0.00786 -0.04056 136 ARG A C   
1421 O  O   . ARG A  136 ? 0.23341 0.26667 0.19621 0.00450  -0.00812 -0.03650 136 ARG A O   
1422 C  CB  . ARG A  136 ? 0.23609 0.29060 0.19102 0.01018  -0.00947 -0.03767 136 ARG A CB  
1423 C  CG  . ARG A  136 ? 0.23304 0.30103 0.19119 0.00973  -0.01188 -0.03478 136 ARG A CG  
1424 C  CD  . ARG A  136 ? 0.25243 0.33467 0.20853 0.00407  -0.01380 -0.04089 136 ARG A CD  
1425 N  NE  . ARG A  136 ? 0.26789 0.36420 0.22854 0.00371  -0.01617 -0.03802 136 ARG A NE  
1426 C  CZ  . ARG A  136 ? 0.30220 0.39637 0.26738 0.00008  -0.01581 -0.03925 136 ARG A CZ  
1427 N  NH1 . ARG A  136 ? 0.32501 0.40431 0.28990 -0.00447 -0.01361 -0.04361 136 ARG A NH1 
1428 N  NH2 . ARG A  136 ? 0.32152 0.42880 0.29200 0.00134  -0.01745 -0.03550 136 ARG A NH2 
1442 N  N   . ASP A  137 ? 0.24787 0.28191 0.20583 -0.00216 -0.00730 -0.04809 137 ASP A N   
1443 C  CA  . ASP A  137 ? 0.26708 0.29892 0.22734 -0.00864 -0.00711 -0.05129 137 ASP A CA  
1444 C  C   . ASP A  137 ? 0.26352 0.27861 0.22578 -0.00842 -0.00544 -0.04812 137 ASP A C   
1445 O  O   . ASP A  137 ? 0.27030 0.28495 0.23494 -0.01137 -0.00537 -0.04660 137 ASP A O   
1446 C  CB  . ASP A  137 ? 0.28131 0.31204 0.23939 -0.01544 -0.00617 -0.06050 137 ASP A CB  
1447 C  CG  . ASP A  137 ? 0.41856 0.46788 0.37416 -0.01783 -0.00834 -0.06463 137 ASP A CG  
1448 O  OD1 . ASP A  137 ? 0.31716 0.38143 0.27390 -0.01481 -0.01088 -0.05980 137 ASP A OD1 
1449 O  OD2 . ASP A  137 ? 0.47559 0.52415 0.42813 -0.02274 -0.00739 -0.07283 137 ASP A OD2 
1454 N  N   . GLN A  138 ? 0.23820 0.24023 0.19958 -0.00513 -0.00406 -0.04700 138 GLN A N   
1455 C  CA  . GLN A  138 ? 0.22988 0.21651 0.19275 -0.00502 -0.00298 -0.04371 138 GLN A CA  
1456 C  C   . GLN A  138 ? 0.23894 0.22650 0.20289 -0.00100 -0.00398 -0.03647 138 GLN A C   
1457 O  O   . GLN A  138 ? 0.23725 0.21789 0.20182 -0.00289 -0.00360 -0.03390 138 GLN A O   
1458 C  CB  . GLN A  138 ? 0.25603 0.23018 0.21871 -0.00245 -0.00144 -0.04474 138 GLN A CB  
1459 C  CG  . GLN A  138 ? 0.27110 0.24194 0.23294 -0.00705 0.00045  -0.05305 138 GLN A CG  
1460 C  CD  . GLN A  138 ? 0.29221 0.25023 0.25511 -0.00414 0.00266  -0.05440 138 GLN A CD  
1461 O  OE1 . GLN A  138 ? 0.30830 0.25349 0.27367 -0.00279 0.00322  -0.05072 138 GLN A OE1 
1462 N  NE2 . GLN A  138 ? 0.30402 0.26604 0.26514 -0.00326 0.00407  -0.05987 138 GLN A NE2 
1471 N  N   . ILE A  139 ? 0.22975 0.22555 0.19368 0.00424  -0.00500 -0.03316 139 ILE A N   
1472 C  CA  . ILE A  139 ? 0.22057 0.21804 0.18586 0.00763  -0.00557 -0.02726 139 ILE A CA  
1473 C  C   . ILE A  139 ? 0.22209 0.22745 0.18900 0.00426  -0.00567 -0.02755 139 ILE A C   
1474 O  O   . ILE A  139 ? 0.21899 0.22015 0.18650 0.00380  -0.00502 -0.02478 139 ILE A O   
1475 C  CB  . ILE A  139 ? 0.20939 0.21454 0.17500 0.01354  -0.00627 -0.02376 139 ILE A CB  
1476 C  CG1 . ILE A  139 ? 0.22477 0.22319 0.18944 0.01675  -0.00573 -0.02325 139 ILE A CG1 
1477 C  CG2 . ILE A  139 ? 0.20589 0.21190 0.17342 0.01663  -0.00633 -0.01860 139 ILE A CG2 
1478 C  CD1 . ILE A  139 ? 0.23243 0.24020 0.19674 0.02113  -0.00600 -0.02088 139 ILE A CD1 
1490 N  N   . GLU A  140 ? 0.23469 0.25298 0.20242 0.00195  -0.00645 -0.03084 140 GLU A N   
1491 C  CA  . GLU A  140 ? 0.22472 0.25296 0.19538 -0.00131 -0.00654 -0.03132 140 GLU A CA  
1492 C  C   . GLU A  140 ? 0.23060 0.24961 0.20119 -0.00748 -0.00494 -0.03331 140 GLU A C   
1493 O  O   . GLU A  140 ? 0.24163 0.26152 0.21395 -0.00848 -0.00389 -0.03100 140 GLU A O   
1494 C  CB  . GLU A  140 ? 0.24255 0.28666 0.21405 -0.00350 -0.00822 -0.03508 140 GLU A CB  
1495 C  CG  . GLU A  140 ? 0.24215 0.29942 0.21808 -0.00721 -0.00860 -0.03596 140 GLU A CG  
1496 C  CD  . GLU A  140 ? 0.33048 0.40537 0.30723 -0.00935 -0.01107 -0.03942 140 GLU A CD  
1497 O  OE1 . GLU A  140 ? 0.34388 0.41722 0.31701 -0.01303 -0.01155 -0.04485 140 GLU A OE1 
1498 O  OE2 . GLU A  140 ? 0.55557 0.64614 0.53684 -0.00753 -0.01245 -0.03687 140 GLU A OE2 
1505 N  N   . ALA A  141 ? 0.23429 0.24379 0.20293 -0.01154 -0.00430 -0.03739 141 ALA A N   
1506 C  CA  . ALA A  141 ? 0.23370 0.23276 0.20226 -0.01747 -0.00256 -0.03845 141 ALA A CA  
1507 C  C   . ALA A  141 ? 0.24266 0.23009 0.20974 -0.01505 -0.00176 -0.03276 141 ALA A C   
1508 O  O   . ALA A  141 ? 0.25565 0.24012 0.22271 -0.01886 -0.00040 -0.03124 141 ALA A O   
1509 C  CB  . ALA A  141 ? 0.27945 0.26869 0.24673 -0.02125 -0.00170 -0.04365 141 ALA A CB  
1515 N  N   . ALA A  142 ? 0.24650 0.22780 0.21211 -0.00922 -0.00256 -0.02961 142 ALA A N   
1516 C  CA  . ALA A  142 ? 0.22909 0.20046 0.19292 -0.00714 -0.00240 -0.02449 142 ALA A CA  
1517 C  C   . ALA A  142 ? 0.21552 0.19405 0.17965 -0.00585 -0.00200 -0.02154 142 ALA A C   
1518 O  O   . ALA A  142 ? 0.23636 0.20926 0.19844 -0.00778 -0.00105 -0.01898 142 ALA A O   
1519 C  CB  . ALA A  142 ? 0.22966 0.19500 0.19296 -0.00159 -0.00352 -0.02249 142 ALA A CB  
1525 N  N   . LEU A  143 ? 0.22183 0.21276 0.18844 -0.00249 -0.00248 -0.02177 143 LEU A N   
1526 C  CA  . LEU A  143 ? 0.21751 0.21542 0.18567 -0.00095 -0.00142 -0.01958 143 LEU A CA  
1527 C  C   . LEU A  143 ? 0.21697 0.22002 0.18656 -0.00673 0.00033  -0.02140 143 LEU A C   
1528 O  O   . LEU A  143 ? 0.23421 0.23597 0.20293 -0.00761 0.00222  -0.01958 143 LEU A O   
1529 C  CB  . LEU A  143 ? 0.22752 0.23745 0.19911 0.00437  -0.00226 -0.01878 143 LEU A CB  
1530 C  CG  . LEU A  143 ? 0.21890 0.22407 0.18954 0.01028  -0.00315 -0.01578 143 LEU A CG  
1531 C  CD1 . LEU A  143 ? 0.24121 0.25839 0.21497 0.01474  -0.00404 -0.01476 143 LEU A CD1 
1532 C  CD2 . LEU A  143 ? 0.21137 0.20952 0.18083 0.01235  -0.00203 -0.01277 143 LEU A CD2 
1544 N  N   . GLU A  144 ? 0.23156 0.24037 0.20309 -0.01123 -0.00000 -0.02530 144 GLU A N   
1545 C  CA  . GLU A  144 ? 0.23892 0.25260 0.21246 -0.01773 0.00183  -0.02720 144 GLU A CA  
1546 C  C   . GLU A  144 ? 0.24714 0.24683 0.21662 -0.02193 0.00364  -0.02542 144 GLU A C   
1547 O  O   . GLU A  144 ? 0.24874 0.25054 0.21838 -0.02532 0.00601  -0.02441 144 GLU A O   
1548 C  CB  . GLU A  144 ? 0.27704 0.29809 0.25309 -0.02261 0.00088  -0.03230 144 GLU A CB  
1549 C  CG  . GLU A  144 ? 0.33794 0.37672 0.31812 -0.01937 -0.00112 -0.03347 144 GLU A CG  
1550 C  CD  . GLU A  144 ? 0.70678 0.75350 0.68816 -0.02432 -0.00270 -0.03911 144 GLU A CD  
1551 O  OE1 . GLU A  144 ? 0.64282 0.67905 0.62179 -0.02981 -0.00197 -0.04275 144 GLU A OE1 
1552 O  OE2 . GLU A  144 ? 0.74951 0.81300 0.73427 -0.02270 -0.00469 -0.03988 144 GLU A OE2 
1559 N  N   . TYR A  145 ? 0.25308 0.23889 0.21904 -0.02162 0.00270  -0.02466 145 TYR A N   
1560 C  CA  . TYR A  145 ? 0.25081 0.22301 0.21278 -0.02493 0.00390  -0.02169 145 TYR A CA  
1561 C  C   . TYR A  145 ? 0.25953 0.23045 0.21818 -0.02249 0.00464  -0.01734 145 TYR A C   
1562 O  O   . TYR A  145 ? 0.26686 0.23487 0.22283 -0.02681 0.00670  -0.01543 145 TYR A O   
1563 C  CB  . TYR A  145 ? 0.25877 0.21757 0.21896 -0.02321 0.00241  -0.02108 145 TYR A CB  
1564 C  CG  . TYR A  145 ? 0.27943 0.22431 0.23584 -0.02541 0.00297  -0.01667 145 TYR A CG  
1565 C  CD1 . TYR A  145 ? 0.30412 0.24244 0.26029 -0.03206 0.00489  -0.01684 145 TYR A CD1 
1566 C  CD2 . TYR A  145 ? 0.30113 0.23995 0.25426 -0.02109 0.00147  -0.01197 145 TYR A CD2 
1567 C  CE1 . TYR A  145 ? 0.34551 0.27123 0.29790 -0.03380 0.00527  -0.01148 145 TYR A CE1 
1568 C  CE2 . TYR A  145 ? 0.32214 0.24960 0.27143 -0.02300 0.00141  -0.00711 145 TYR A CE2 
1569 C  CZ  . TYR A  145 ? 0.32604 0.24687 0.27495 -0.02896 0.00325  -0.00656 145 TYR A CZ  
1570 O  OH  . TYR A  145 ? 0.41151 0.32111 0.35635 -0.03061 0.00306  -0.00054 145 TYR A OH  
1580 N  N   . LEU A  146 ? 0.24040 0.21344 0.19887 -0.01609 0.00329  -0.01595 146 LEU A N   
1581 C  CA  . LEU A  146 ? 0.23746 0.20895 0.19252 -0.01420 0.00417  -0.01293 146 LEU A CA  
1582 C  C   . LEU A  146 ? 0.23598 0.21785 0.19282 -0.01627 0.00727  -0.01409 146 LEU A C   
1583 O  O   . LEU A  146 ? 0.24696 0.22622 0.19972 -0.01866 0.00935  -0.01243 146 LEU A O   
1584 C  CB  . LEU A  146 ? 0.24433 0.21615 0.19994 -0.00739 0.00244  -0.01188 146 LEU A CB  
1585 C  CG  . LEU A  146 ? 0.22830 0.19035 0.18240 -0.00501 -0.00023 -0.01021 146 LEU A CG  
1586 C  CD1 . LEU A  146 ? 0.25294 0.21717 0.20861 0.00120  -0.00146 -0.00936 146 LEU A CD1 
1587 C  CD2 . LEU A  146 ? 0.25229 0.20301 0.20119 -0.00750 -0.00089 -0.00677 146 LEU A CD2 
1599 N  N   . VAL A  147 ? 0.23182 0.22644 0.19486 -0.01529 0.00764  -0.01686 147 VAL A N   
1600 C  CA  . VAL A  147 ? 0.23948 0.24581 0.20618 -0.01683 0.01073  -0.01800 147 VAL A CA  
1601 C  C   . VAL A  147 ? 0.26744 0.27189 0.23238 -0.02467 0.01313  -0.01831 147 VAL A C   
1602 O  O   . VAL A  147 ? 0.27314 0.27975 0.23649 -0.02682 0.01650  -0.01753 147 VAL A O   
1603 C  CB  . VAL A  147 ? 0.24605 0.26750 0.22054 -0.01431 0.00985  -0.02026 147 VAL A CB  
1604 C  CG1 . VAL A  147 ? 0.26569 0.30051 0.24566 -0.01712 0.01291  -0.02169 147 VAL A CG1 
1605 C  CG2 . VAL A  147 ? 0.24835 0.27234 0.22471 -0.00620 0.00849  -0.01875 147 VAL A CG2 
1615 N  N   . ASP A  148 ? 0.26050 0.26048 0.22561 -0.02934 0.01189  -0.01958 148 ASP A N   
1616 C  CA  . ASP A  148 ? 0.26800 0.26514 0.23201 -0.03741 0.01438  -0.01958 148 ASP A CA  
1617 C  C   . ASP A  148 ? 0.27875 0.26304 0.23485 -0.03925 0.01564  -0.01515 148 ASP A C   
1618 O  O   . ASP A  148 ? 0.30240 0.28802 0.25668 -0.04438 0.01898  -0.01398 148 ASP A O   
1619 C  CB  . ASP A  148 ? 0.29529 0.28842 0.26135 -0.04181 0.01293  -0.02233 148 ASP A CB  
1620 C  CG  . ASP A  148 ? 0.61110 0.60195 0.57754 -0.05089 0.01583  -0.02273 148 ASP A CG  
1621 O  OD1 . ASP A  148 ? 0.65951 0.66315 0.63044 -0.05465 0.01828  -0.02447 148 ASP A OD1 
1622 O  OD2 . ASP A  148 ? 0.73305 0.70928 0.69594 -0.05419 0.01582  -0.02102 148 ASP A OD2 
1627 N  N   . GLN A  149 ? 0.27572 0.24829 0.22712 -0.03554 0.01295  -0.01244 149 GLN A N   
1628 C  CA  . GLN A  149 ? 0.27211 0.23366 0.21570 -0.03722 0.01335  -0.00762 149 GLN A CA  
1629 C  C   . GLN A  149 ? 0.28921 0.25621 0.22899 -0.03616 0.01575  -0.00675 149 GLN A C   
1630 O  O   . GLN A  149 ? 0.28959 0.25277 0.22315 -0.04041 0.01786  -0.00378 149 GLN A O   
1631 C  CB  . GLN A  149 ? 0.28014 0.23039 0.22099 -0.03295 0.00958  -0.00500 149 GLN A CB  
1632 C  CG  . GLN A  149 ? 0.30491 0.24686 0.24843 -0.03449 0.00813  -0.00549 149 GLN A CG  
1633 C  CD  . GLN A  149 ? 0.37424 0.30809 0.31577 -0.04141 0.01010  -0.00305 149 GLN A CD  
1634 O  OE1 . GLN A  149 ? 0.38070 0.30619 0.31630 -0.04281 0.01007  0.00246  149 GLN A OE1 
1635 N  NE2 . GLN A  149 ? 0.42196 0.35890 0.36830 -0.04634 0.01192  -0.00692 149 GLN A NE2 
1644 N  N   . SER A  150 ? 0.26700 0.24264 0.21025 -0.03066 0.01580  -0.00928 150 SER A N   
1645 C  CA  . SER A  150 ? 0.25059 0.23176 0.19151 -0.02941 0.01893  -0.00978 150 SER A CA  
1646 C  C   . SER A  150 ? 0.27424 0.26385 0.21658 -0.03495 0.02372  -0.01093 150 SER A C   
1647 O  O   . SER A  150 ? 0.29304 0.28429 0.23065 -0.03624 0.02723  -0.01066 150 SER A O   
1648 C  CB  . SER A  150 ? 0.27673 0.26504 0.22310 -0.02228 0.01843  -0.01225 150 SER A CB  
1649 O  OG  . SER A  150 ? 0.27842 0.26976 0.22252 -0.02057 0.02172  -0.01320 150 SER A OG  
1655 N  N   . ASN A  151 ? 0.27981 0.27460 0.22808 -0.03897 0.02417  -0.01238 151 ASN A N   
1656 C  CA  . ASN A  151 ? 0.28360 0.28695 0.23430 -0.04516 0.02873  -0.01333 151 ASN A CA  
1657 C  C   . ASN A  151 ? 0.35810 0.35211 0.30331 -0.05311 0.02990  -0.01009 151 ASN A C   
1658 O  O   . ASN A  151 ? 0.41420 0.41465 0.36147 -0.05935 0.03393  -0.01052 151 ASN A O   
1659 C  CB  . ASN A  151 ? 0.33953 0.35701 0.30132 -0.04517 0.02867  -0.01722 151 ASN A CB  
1660 C  CG  . ASN A  151 ? 0.41089 0.43985 0.37871 -0.03766 0.02887  -0.01932 151 ASN A CG  
1661 O  OD1 . ASN A  151 ? 0.43349 0.46457 0.39943 -0.03492 0.03202  -0.01922 151 ASN A OD1 
1662 N  ND2 . ASN A  151 ? 0.47669 0.51217 0.45120 -0.03407 0.02558  -0.02108 151 ASN A ND2 
1669 N  N   . SER A  152 ? 0.30145 0.28078 0.24007 -0.05305 0.02683  -0.00635 152 SER A N   
1670 C  CA  . SER A  152 ? 0.30210 0.27095 0.23594 -0.05993 0.02770  -0.00217 152 SER A CA  
1671 C  C   . SER A  152 ? 0.33777 0.30049 0.26071 -0.06120 0.02899  0.00287  152 SER A C   
1672 O  O   . SER A  152 ? 0.34254 0.30049 0.26021 -0.05613 0.02611  0.00443  152 SER A O   
1673 C  CB  . SER A  152 ? 0.35355 0.30947 0.28772 -0.05847 0.02336  -0.00060 152 SER A CB  
1674 O  OG  . SER A  152 ? 0.38385 0.32784 0.31293 -0.06423 0.02430  0.00471  152 SER A OG  
1680 N  N   . SER A  153 ? 0.34971 0.31249 0.26901 -0.06843 0.03310  0.00559  153 SER A N   
1681 C  CA  . SER A  153 ? 0.37899 0.33620 0.28652 -0.07042 0.03421  0.01094  153 SER A CA  
1682 C  C   . SER A  153 ? 0.40383 0.34532 0.30521 -0.07020 0.02987  0.01760  153 SER A C   
1683 O  O   . SER A  153 ? 0.49271 0.42952 0.38364 -0.07164 0.02971  0.02297  153 SER A O   
1684 C  CB  . SER A  153 ? 0.50849 0.47094 0.41332 -0.07844 0.04034  0.01253  153 SER A CB  
1685 O  OG  . SER A  153 ? 0.44350 0.40026 0.35224 -0.08470 0.04116  0.01481  153 SER A OG  
1691 N  N   . ARG A  154 ? 0.35023 0.28390 0.25762 -0.06857 0.02652  0.01759  154 ARG A N   
1692 C  CA  . ARG A  154 ? 0.39118 0.31031 0.29475 -0.06703 0.02242  0.02376  154 ARG A CA  
1693 C  C   . ARG A  154 ? 0.38566 0.30287 0.29011 -0.05882 0.01726  0.02261  154 ARG A C   
1694 O  O   . ARG A  154 ? 0.48306 0.38945 0.38641 -0.05639 0.01350  0.02721  154 ARG A O   
1695 C  CB  . ARG A  154 ? 0.60217 0.51189 0.51217 -0.07040 0.02257  0.02446  154 ARG A CB  
1696 C  CG  . ARG A  154 ? 0.77616 0.68916 0.68886 -0.07890 0.02780  0.02352  154 ARG A CG  
1697 C  CD  . ARG A  154 ? 0.85615 0.76991 0.75962 -0.08439 0.03137  0.02944  154 ARG A CD  
1698 N  NE  . ARG A  154 ? 0.97344 0.89493 0.88063 -0.09224 0.03708  0.02711  154 ARG A NE  
1699 C  CZ  . ARG A  154 ? 0.77212 0.68798 0.67586 -0.10014 0.04082  0.03273  154 ARG A CZ  
1700 N  NH1 . ARG A  154 ? 0.95282 0.85510 0.84841 -0.10114 0.03947  0.04186  154 ARG A NH1 
1701 N  NH2 . ARG A  154 ? 0.94509 0.86983 0.85391 -0.10730 0.04608  0.02962  154 ARG A NH2 
1715 N  N   . SER A  155 ? 0.36577 0.29331 0.27313 -0.05426 0.01714  0.01675  155 SER A N   
1716 C  CA  . SER A  155 ? 0.34513 0.27102 0.25438 -0.04701 0.01270  0.01550  155 SER A CA  
1717 C  C   . SER A  155 ? 0.31711 0.24477 0.21864 -0.04439 0.01131  0.01689  155 SER A C   
1718 O  O   . SER A  155 ? 0.34331 0.27867 0.24116 -0.04605 0.01469  0.01465  155 SER A O   
1719 C  CB  . SER A  155 ? 0.32994 0.26546 0.24804 -0.04341 0.01325  0.00844  155 SER A CB  
1720 O  OG  . SER A  155 ? 0.33318 0.26812 0.25294 -0.03661 0.00962  0.00728  155 SER A OG  
1726 N  N   . PRO A  156 ? 0.35090 0.27225 0.25095 -0.04018 0.00655  0.01974  156 PRO A N   
1727 C  CA  . PRO A  156 ? 0.37112 0.29490 0.26488 -0.03776 0.00475  0.01982  156 PRO A CA  
1728 C  C   . PRO A  156 ? 0.32149 0.25370 0.21961 -0.03369 0.00612  0.01307  156 PRO A C   
1729 O  O   . PRO A  156 ? 0.36095 0.29582 0.25373 -0.03285 0.00619  0.01173  156 PRO A O   
1730 C  CB  . PRO A  156 ? 0.42161 0.33749 0.31558 -0.03415 -0.00094 0.02437  156 PRO A CB  
1731 C  CG  . PRO A  156 ? 0.44904 0.36050 0.35248 -0.03213 -0.00152 0.02352  156 PRO A CG  
1732 C  CD  . PRO A  156 ? 0.39433 0.30636 0.29889 -0.03760 0.00284  0.02270  156 PRO A CD  
1740 N  N   . ILE A  157 ? 0.30506 0.24153 0.21249 -0.03127 0.00725  0.00885  157 ILE A N   
1741 C  CA  . ILE A  157 ? 0.29128 0.23604 0.20356 -0.02705 0.00879  0.00340  157 ILE A CA  
1742 C  C   . ILE A  157 ? 0.28881 0.24318 0.20385 -0.02950 0.01404  -0.00020 157 ILE A C   
1743 O  O   . ILE A  157 ? 0.28181 0.24406 0.20360 -0.02582 0.01556  -0.00429 157 ILE A O   
1744 C  CB  . ILE A  157 ? 0.27435 0.21927 0.19487 -0.02150 0.00599  0.00157  157 ILE A CB  
1745 C  CG1 . ILE A  157 ? 0.28365 0.22933 0.21059 -0.02280 0.00624  0.00058  157 ILE A CG1 
1746 C  CG2 . ILE A  157 ? 0.32609 0.26315 0.24456 -0.01867 0.00130  0.00483  157 ILE A CG2 
1747 C  CD1 . ILE A  157 ? 0.27372 0.22345 0.20832 -0.01755 0.00468  -0.00248 157 ILE A CD1 
1759 N  N   . ASN A  158 ? 0.29707 0.25147 0.20736 -0.03558 0.01697  0.00173  158 ASN A N   
1760 C  CA  . ASN A  158 ? 0.29442 0.25891 0.20714 -0.03829 0.02243  -0.00148 158 ASN A CA  
1761 C  C   . ASN A  158 ? 0.28290 0.25447 0.19631 -0.03420 0.02506  -0.00578 158 ASN A C   
1762 O  O   . ASN A  158 ? 0.31616 0.28416 0.22197 -0.03352 0.02482  -0.00561 158 ASN A O   
1763 C  CB  . ASN A  158 ? 0.32461 0.28694 0.22901 -0.04547 0.02540  0.00204  158 ASN A CB  
1764 C  CG  . ASN A  158 ? 0.34856 0.32193 0.25508 -0.04858 0.03165  -0.00118 158 ASN A CG  
1765 O  OD1 . ASN A  158 ? 0.36676 0.34495 0.26936 -0.04777 0.03500  -0.00364 158 ASN A OD1 
1766 N  ND2 . ASN A  158 ? 0.38803 0.36576 0.30113 -0.05243 0.03357  -0.00155 158 ASN A ND2 
1773 N  N   . GLY A  159 ? 0.29229 0.27417 0.21508 -0.03174 0.02771  -0.00970 159 GLY A N   
1774 C  CA  . GLY A  159 ? 0.28022 0.26888 0.20557 -0.02745 0.03110  -0.01371 159 GLY A CA  
1775 C  C   . GLY A  159 ? 0.29226 0.27681 0.21882 -0.02095 0.02816  -0.01474 159 GLY A C   
1776 O  O   . GLY A  159 ? 0.32180 0.30841 0.24817 -0.01796 0.03115  -0.01784 159 GLY A O   
1780 N  N   . MET A  160 ? 0.25828 0.23634 0.18576 -0.01892 0.02283  -0.01237 160 MET A N   
1781 C  CA  . MET A  160 ? 0.26006 0.23384 0.18833 -0.01345 0.02015  -0.01288 160 MET A CA  
1782 C  C   . MET A  160 ? 0.26810 0.24732 0.20665 -0.00753 0.01922  -0.01409 160 MET A C   
1783 O  O   . MET A  160 ? 0.27030 0.24713 0.21049 -0.00284 0.01829  -0.01470 160 MET A O   
1784 C  CB  . MET A  160 ? 0.27804 0.24163 0.20108 -0.01415 0.01485  -0.00925 160 MET A CB  
1785 C  CG  . MET A  160 ? 0.29344 0.25118 0.20540 -0.01888 0.01450  -0.00708 160 MET A CG  
1786 S  SD  . MET A  160 ? 0.31204 0.25979 0.21987 -0.01806 0.00781  -0.00266 160 MET A SD  
1787 C  CE  . MET A  160 ? 0.40898 0.35334 0.30358 -0.02406 0.00785  0.00013  160 MET A CE  
1797 N  N   . VAL A  161 ? 0.23044 0.21676 0.17553 -0.00797 0.01918  -0.01420 161 VAL A N   
1798 C  CA  . VAL A  161 ? 0.22377 0.21554 0.17722 -0.00289 0.01727  -0.01451 161 VAL A CA  
1799 C  C   . VAL A  161 ? 0.24102 0.24563 0.20268 -0.00025 0.02078  -0.01656 161 VAL A C   
1800 O  O   . VAL A  161 ? 0.26602 0.27823 0.22981 -0.00407 0.02335  -0.01767 161 VAL A O   
1801 C  CB  . VAL A  161 ? 0.22836 0.21947 0.18335 -0.00514 0.01388  -0.01346 161 VAL A CB  
1802 C  CG1 . VAL A  161 ? 0.23312 0.23223 0.19593 -0.00038 0.01217  -0.01407 161 VAL A CG1 
1803 C  CG2 . VAL A  161 ? 0.24948 0.22806 0.19823 -0.00632 0.01039  -0.01100 161 VAL A CG2 
1813 N  N   . ASP A  162 ? 0.21616 0.22362 0.18328 0.00635  0.02089  -0.01663 162 ASP A N   
1814 C  CA  . ASP A  162 ? 0.21545 0.23594 0.19227 0.01037  0.02331  -0.01742 162 ASP A CA  
1815 C  C   . ASP A  162 ? 0.21659 0.24440 0.19881 0.01165  0.01942  -0.01603 162 ASP A C   
1816 O  O   . ASP A  162 ? 0.20468 0.22888 0.18716 0.01550  0.01640  -0.01423 162 ASP A O   
1817 C  CB  . ASP A  162 ? 0.22602 0.24475 0.20612 0.01708  0.02549  -0.01752 162 ASP A CB  
1818 C  CG  . ASP A  162 ? 0.21964 0.25151 0.21070 0.02229  0.02834  -0.01757 162 ASP A CG  
1819 O  OD1 . ASP A  162 ? 0.22072 0.26454 0.21748 0.02138  0.02699  -0.01693 162 ASP A OD1 
1820 O  OD2 . ASP A  162 ? 0.22669 0.25698 0.22110 0.02733  0.03180  -0.01824 162 ASP A OD2 
1825 N  N   . PRO A  163 ? 0.20736 0.24585 0.19370 0.00810  0.01946  -0.01703 163 PRO A N   
1826 C  CA  . PRO A  163 ? 0.21681 0.26245 0.20696 0.00829  0.01554  -0.01655 163 PRO A CA  
1827 C  C   . PRO A  163 ? 0.21333 0.26797 0.21070 0.01584  0.01430  -0.01450 163 PRO A C   
1828 O  O   . PRO A  163 ? 0.21567 0.27561 0.21459 0.01647  0.01070  -0.01381 163 PRO A O   
1829 C  CB  . PRO A  163 ? 0.26928 0.32582 0.26312 0.00230  0.01660  -0.01867 163 PRO A CB  
1830 C  CG  . PRO A  163 ? 0.30443 0.36512 0.30061 0.00221  0.02183  -0.01949 163 PRO A CG  
1831 C  CD  . PRO A  163 ? 0.21878 0.26456 0.20695 0.00362  0.02342  -0.01893 163 PRO A CD  
1839 N  N   . ASN A  164 ? 0.19556 0.25282 0.19762 0.02134  0.01752  -0.01356 164 ASN A N   
1840 C  CA  . ASN A  164 ? 0.20334 0.26783 0.21264 0.02916  0.01666  -0.01046 164 ASN A CA  
1841 C  C   . ASN A  164 ? 0.19383 0.24694 0.19899 0.03285  0.01453  -0.00802 164 ASN A C   
1842 O  O   . ASN A  164 ? 0.19609 0.25409 0.20627 0.03894  0.01345  -0.00461 164 ASN A O   
1843 C  CB  . ASN A  164 ? 0.19870 0.26738 0.21495 0.03419  0.02159  -0.01034 164 ASN A CB  
1844 C  CG  . ASN A  164 ? 0.19748 0.28056 0.22043 0.03191  0.02408  -0.01214 164 ASN A CG  
1845 O  OD1 . ASN A  164 ? 0.22057 0.31937 0.25214 0.03425  0.02251  -0.01048 164 ASN A OD1 
1846 N  ND2 . ASN A  164 ? 0.21889 0.29784 0.23821 0.02729  0.02813  -0.01538 164 ASN A ND2 
1853 N  N   . ARG A  165 ? 0.19036 0.22891 0.18697 0.02947  0.01403  -0.00917 165 ARG A N   
1854 C  CA  . ARG A  165 ? 0.19076 0.21828 0.18438 0.03289  0.01297  -0.00713 165 ARG A CA  
1855 C  C   . ARG A  165 ? 0.19006 0.20933 0.17668 0.02893  0.00943  -0.00737 165 ARG A C   
1856 O  O   . ARG A  165 ? 0.20061 0.20956 0.18090 0.02505  0.00957  -0.00874 165 ARG A O   
1857 C  CB  . ARG A  165 ? 0.20026 0.21841 0.19215 0.03402  0.01684  -0.00844 165 ARG A CB  
1858 C  CG  . ARG A  165 ? 0.20123 0.22748 0.20049 0.03760  0.02126  -0.00915 165 ARG A CG  
1859 C  CD  . ARG A  165 ? 0.21487 0.23184 0.21329 0.03975  0.02555  -0.01093 165 ARG A CD  
1860 N  NE  . ARG A  165 ? 0.22252 0.23121 0.21208 0.03366  0.02709  -0.01467 165 ARG A NE  
1861 C  CZ  . ARG A  165 ? 0.21873 0.21490 0.20136 0.03197  0.02678  -0.01579 165 ARG A CZ  
1862 N  NH1 . ARG A  165 ? 0.23834 0.22785 0.22132 0.03479  0.02446  -0.01355 165 ARG A NH1 
1863 N  NH2 . ARG A  165 ? 0.23173 0.22290 0.20692 0.02702  0.02880  -0.01909 165 ARG A NH2 
1877 N  N   . LEU A  166 ? 0.18382 0.20829 0.17170 0.03008  0.00636  -0.00593 166 LEU A N   
1878 C  CA  . LEU A  166 ? 0.17312 0.19162 0.15575 0.02661  0.00348  -0.00675 166 LEU A CA  
1879 C  C   . LEU A  166 ? 0.18726 0.20364 0.16994 0.03077  0.00167  -0.00401 166 LEU A C   
1880 O  O   . LEU A  166 ? 0.19277 0.21764 0.17971 0.03521  0.00135  -0.00146 166 LEU A O   
1881 C  CB  . LEU A  166 ? 0.20796 0.23529 0.19122 0.02237  0.00199  -0.00915 166 LEU A CB  
1882 C  CG  . LEU A  166 ? 0.19955 0.23111 0.18377 0.01749  0.00394  -0.01170 166 LEU A CG  
1883 C  CD1 . LEU A  166 ? 0.25752 0.29852 0.24331 0.01313  0.00224  -0.01426 166 LEU A CD1 
1884 C  CD2 . LEU A  166 ? 0.23642 0.25541 0.21471 0.01335  0.00522  -0.01259 166 LEU A CD2 
1896 N  N   . GLY A  167 ? 0.19057 0.19629 0.16875 0.02932  0.00047  -0.00410 167 GLY A N   
1897 C  CA  . GLY A  167 ? 0.19387 0.19732 0.17210 0.03266  -0.00080 -0.00165 167 GLY A CA  
1898 C  C   . GLY A  167 ? 0.18681 0.18608 0.16151 0.02985  -0.00276 -0.00325 167 GLY A C   
1899 O  O   . GLY A  167 ? 0.18746 0.18224 0.15938 0.02541  -0.00316 -0.00579 167 GLY A O   
1903 N  N   . ALA A  168 ? 0.17576 0.17607 0.15082 0.03266  -0.00359 -0.00149 168 ALA A N   
1904 C  CA  . ALA A  168 ? 0.18949 0.18531 0.16202 0.03088  -0.00475 -0.00315 168 ALA A CA  
1905 C  C   . ALA A  168 ? 0.18563 0.17793 0.15894 0.03424  -0.00468 -0.00023 168 ALA A C   
1906 O  O   . ALA A  168 ? 0.19278 0.18938 0.16827 0.03798  -0.00398 0.00308  168 ALA A O   
1907 C  CB  . ALA A  168 ? 0.23195 0.23634 0.20365 0.02925  -0.00553 -0.00602 168 ALA A CB  
1913 N  N   . VAL A  169 ? 0.19158 0.17625 0.16367 0.03290  -0.00528 -0.00116 169 VAL A N   
1914 C  CA  . VAL A  169 ? 0.17946 0.16081 0.15293 0.03528  -0.00515 0.00108  169 VAL A CA  
1915 C  C   . VAL A  169 ? 0.18076 0.16158 0.15333 0.03437  -0.00534 -0.00157 169 VAL A C   
1916 O  O   . VAL A  169 ? 0.19732 0.17297 0.16876 0.03155  -0.00593 -0.00422 169 VAL A O   
1917 C  CB  . VAL A  169 ? 0.18122 0.15346 0.15534 0.03457  -0.00569 0.00253  169 VAL A CB  
1918 C  CG1 . VAL A  169 ? 0.19053 0.16047 0.16720 0.03650  -0.00565 0.00471  169 VAL A CG1 
1919 C  CG2 . VAL A  169 ? 0.20938 0.18057 0.18372 0.03472  -0.00494 0.00368  169 VAL A CG2 
1929 N  N   . GLY A  170 ? 0.18256 0.16840 0.15557 0.03669  -0.00447 -0.00093 170 GLY A N   
1930 C  CA  . GLY A  170 ? 0.19750 0.18326 0.16954 0.03591  -0.00390 -0.00447 170 GLY A CA  
1931 C  C   . GLY A  170 ? 0.19296 0.17949 0.16683 0.03869  -0.00251 -0.00271 170 GLY A C   
1932 O  O   . GLY A  170 ? 0.18912 0.18125 0.16337 0.04111  -0.00171 0.00082  170 GLY A O   
1936 N  N   . TRP A  171 ? 0.20478 0.18600 0.18030 0.03851  -0.00190 -0.00488 171 TRP A N   
1937 C  CA  . TRP A  171 ? 0.18887 0.17140 0.16698 0.04099  -0.00003 -0.00394 171 TRP A CA  
1938 C  C   . TRP A  171 ? 0.20696 0.19497 0.18226 0.04096  0.00215  -0.00852 171 TRP A C   
1939 O  O   . TRP A  171 ? 0.21549 0.20070 0.18920 0.03881  0.00234  -0.01369 171 TRP A O   
1940 C  CB  . TRP A  171 ? 0.20194 0.17611 0.18482 0.04130  -0.00057 -0.00347 171 TRP A CB  
1941 C  CG  . TRP A  171 ? 0.18938 0.16510 0.17640 0.04379  0.00162  -0.00316 171 TRP A CG  
1942 C  CD1 . TRP A  171 ? 0.19484 0.17686 0.18302 0.04573  0.00355  -0.00043 171 TRP A CD1 
1943 C  CD2 . TRP A  171 ? 0.19658 0.16753 0.18791 0.04475  0.00248  -0.00532 171 TRP A CD2 
1944 N  NE1 . TRP A  171 ? 0.19437 0.17666 0.18727 0.04756  0.00575  -0.00118 171 TRP A NE1 
1945 C  CE2 . TRP A  171 ? 0.18550 0.16108 0.18075 0.04732  0.00511  -0.00432 171 TRP A CE2 
1946 C  CE3 . TRP A  171 ? 0.20555 0.16849 0.19839 0.04388  0.00144  -0.00748 171 TRP A CE3 
1947 C  CZ2 . TRP A  171 ? 0.20715 0.18038 0.20839 0.04938  0.00683  -0.00588 171 TRP A CZ2 
1948 C  CZ3 . TRP A  171 ? 0.23717 0.19685 0.23587 0.04616  0.00291  -0.00851 171 TRP A CZ3 
1949 C  CH2 . TRP A  171 ? 0.21660 0.18163 0.21982 0.04906  0.00560  -0.00795 171 TRP A CH2 
1960 N  N   . SER A  172 ? 0.20322 0.19881 0.17763 0.04302  0.00408  -0.00672 172 SER A N   
1961 C  CA  . SER A  172 ? 0.22088 0.22214 0.19232 0.04318  0.00683  -0.01111 172 SER A CA  
1962 C  C   . SER A  172 ? 0.20655 0.21233 0.17224 0.04018  0.00591  -0.01617 172 SER A C   
1963 O  O   . SER A  172 ? 0.22009 0.23233 0.18315 0.03972  0.00399  -0.01357 172 SER A O   
1964 C  CB  . SER A  172 ? 0.24623 0.24101 0.22246 0.04429  0.00891  -0.01362 172 SER A CB  
1965 O  OG  . SER A  172 ? 0.31797 0.31946 0.29198 0.04533  0.01254  -0.01655 172 SER A OG  
1971 N  N   . MET A  173 ? 0.22145 0.22452 0.18564 0.03805  0.00725  -0.02327 173 MET A N   
1972 C  CA  . MET A  173 ? 0.23251 0.24045 0.19157 0.03428  0.00619  -0.02842 173 MET A CA  
1973 C  C   . MET A  173 ? 0.21393 0.21924 0.17401 0.03219  0.00301  -0.02647 173 MET A C   
1974 O  O   . MET A  173 ? 0.22280 0.23618 0.17952 0.02976  0.00140  -0.02790 173 MET A O   
1975 C  CB  . MET A  173 ? 0.23951 0.24242 0.19758 0.03178  0.00857  -0.03703 173 MET A CB  
1976 C  CG  . MET A  173 ? 0.26182 0.27074 0.21676 0.03293  0.01219  -0.04089 173 MET A CG  
1977 S  SD  . MET A  173 ? 0.28365 0.28638 0.23685 0.02919  0.01530  -0.05265 173 MET A SD  
1978 C  CE  . MET A  173 ? 0.32583 0.33659 0.27549 0.03157  0.02018  -0.05601 173 MET A CE  
1988 N  N   . GLY A  174 ? 0.21255 0.20782 0.17718 0.03294  0.00206  -0.02321 174 GLY A N   
1989 C  CA  . GLY A  174 ? 0.20917 0.20277 0.17432 0.03121  -0.00043 -0.02082 174 GLY A CA  
1990 C  C   . GLY A  174 ? 0.19786 0.19973 0.16262 0.03325  -0.00168 -0.01543 174 GLY A C   
1991 O  O   . GLY A  174 ? 0.20415 0.20975 0.16835 0.03168  -0.00321 -0.01498 174 GLY A O   
1995 N  N   . GLY A  175 ? 0.20525 0.21005 0.17094 0.03682  -0.00071 -0.01117 175 GLY A N   
1996 C  CA  . GLY A  175 ? 0.20299 0.21582 0.16840 0.03919  -0.00134 -0.00581 175 GLY A CA  
1997 C  C   . GLY A  175 ? 0.21541 0.24123 0.17656 0.03863  -0.00187 -0.00708 175 GLY A C   
1998 O  O   . GLY A  175 ? 0.22350 0.25606 0.18494 0.03943  -0.00336 -0.00397 175 GLY A O   
2002 N  N   . GLY A  176 ? 0.20670 0.23685 0.16401 0.03730  -0.00066 -0.01173 176 GLY A N   
2003 C  CA  . GLY A  176 ? 0.21132 0.25464 0.16371 0.03553  -0.00181 -0.01415 176 GLY A CA  
2004 C  C   . GLY A  176 ? 0.22891 0.27389 0.18174 0.03181  -0.00407 -0.01761 176 GLY A C   
2005 O  O   . GLY A  176 ? 0.22266 0.27921 0.17468 0.03168  -0.00618 -0.01576 176 GLY A O   
2009 N  N   . GLY A  177 ? 0.21515 0.24896 0.16992 0.02883  -0.00365 -0.02202 177 GLY A N   
2010 C  CA  . GLY A  177 ? 0.21862 0.25340 0.17429 0.02481  -0.00532 -0.02487 177 GLY A CA  
2011 C  C   . GLY A  177 ? 0.21269 0.24994 0.17193 0.02684  -0.00681 -0.01898 177 GLY A C   
2012 O  O   . GLY A  177 ? 0.21287 0.25923 0.17276 0.02488  -0.00845 -0.01962 177 GLY A O   
2016 N  N   . THR A  178 ? 0.21008 0.23973 0.17211 0.03060  -0.00608 -0.01363 178 THR A N   
2017 C  CA  . THR A  178 ? 0.19043 0.22078 0.15595 0.03289  -0.00670 -0.00851 178 THR A CA  
2018 C  C   . THR A  178 ? 0.20141 0.24528 0.16740 0.03612  -0.00763 -0.00415 178 THR A C   
2019 O  O   . THR A  178 ? 0.21140 0.26196 0.18006 0.03637  -0.00864 -0.00273 178 THR A O   
2020 C  CB  . THR A  178 ? 0.19877 0.21793 0.16657 0.03567  -0.00555 -0.00462 178 THR A CB  
2021 O  OG1 . THR A  178 ? 0.21540 0.22310 0.18334 0.03290  -0.00534 -0.00754 178 THR A OG1 
2022 C  CG2 . THR A  178 ? 0.22532 0.24451 0.19643 0.03834  -0.00549 0.00016  178 THR A CG2 
2030 N  N   . LEU A  179 ? 0.20875 0.25793 0.17233 0.03864  -0.00725 -0.00179 179 LEU A N   
2031 C  CA  . LEU A  179 ? 0.20300 0.26573 0.16653 0.04193  -0.00838 0.00343  179 LEU A CA  
2032 C  C   . LEU A  179 ? 0.22942 0.30639 0.19085 0.03885  -0.01080 -0.00017 179 LEU A C   
2033 O  O   . LEU A  179 ? 0.21840 0.30697 0.18238 0.04100  -0.01257 0.00388  179 LEU A O   
2034 C  CB  . LEU A  179 ? 0.23289 0.29743 0.19338 0.04471  -0.00705 0.00696  179 LEU A CB  
2035 C  CG  . LEU A  179 ? 0.24857 0.30129 0.21257 0.04783  -0.00486 0.01168  179 LEU A CG  
2036 C  CD1 . LEU A  179 ? 0.24363 0.29788 0.20450 0.04931  -0.00295 0.01382  179 LEU A CD1 
2037 C  CD2 . LEU A  179 ? 0.30956 0.36164 0.27859 0.05183  -0.00476 0.01854  179 LEU A CD2 
2049 N  N   . ARG A  180 ? 0.21389 0.29031 0.17138 0.03371  -0.01089 -0.00793 180 ARG A N   
2050 C  CA  . ARG A  180 ? 0.22861 0.31803 0.18436 0.02946  -0.01324 -0.01256 180 ARG A CA  
2051 C  C   . ARG A  180 ? 0.21852 0.30938 0.17992 0.02793  -0.01435 -0.01258 180 ARG A C   
2052 O  O   . ARG A  180 ? 0.23488 0.34062 0.19814 0.02753  -0.01673 -0.01156 180 ARG A O   
2053 C  CB  . ARG A  180 ? 0.22781 0.31364 0.17873 0.02372  -0.01241 -0.02179 180 ARG A CB  
2054 C  CG  . ARG A  180 ? 0.23349 0.32365 0.17791 0.02440  -0.01135 -0.02327 180 ARG A CG  
2055 C  CD  . ARG A  180 ? 0.23750 0.31869 0.17863 0.01977  -0.00910 -0.03260 180 ARG A CD  
2056 N  NE  . ARG A  180 ? 0.23123 0.31803 0.16574 0.02000  -0.00757 -0.03521 180 ARG A NE  
2057 C  CZ  . ARG A  180 ? 0.22189 0.32332 0.15023 0.01668  -0.00909 -0.03945 180 ARG A CZ  
2058 N  NH1 . ARG A  180 ? 0.24910 0.36184 0.17781 0.01284  -0.01252 -0.04146 180 ARG A NH1 
2059 N  NH2 . ARG A  180 ? 0.25264 0.35880 0.17413 0.01690  -0.00712 -0.04192 180 ARG A NH2 
2073 N  N   . LEU A  181 ? 0.21803 0.29458 0.18210 0.02676  -0.01263 -0.01388 181 LEU A N   
2074 C  CA  . LEU A  181 ? 0.21120 0.28883 0.18027 0.02535  -0.01292 -0.01366 181 LEU A CA  
2075 C  C   . LEU A  181 ? 0.18592 0.27055 0.15998 0.03133  -0.01323 -0.00621 181 LEU A C   
2076 O  O   . LEU A  181 ? 0.20808 0.30408 0.18662 0.03122  -0.01440 -0.00535 181 LEU A O   
2077 C  CB  . LEU A  181 ? 0.21480 0.27538 0.18450 0.02320  -0.01086 -0.01565 181 LEU A CB  
2078 C  CG  . LEU A  181 ? 0.20873 0.26976 0.18236 0.02032  -0.01051 -0.01659 181 LEU A CG  
2079 C  CD1 . LEU A  181 ? 0.25396 0.32594 0.22794 0.01452  -0.01189 -0.02179 181 LEU A CD1 
2080 C  CD2 . LEU A  181 ? 0.23520 0.27924 0.20776 0.01835  -0.00866 -0.01770 181 LEU A CD2 
2092 N  N   . ALA A  182 ? 0.21739 0.29580 0.19154 0.03663  -0.01200 -0.00073 182 ALA A N   
2093 C  CA  . ALA A  182 ? 0.22439 0.30814 0.20360 0.04270  -0.01184 0.00658  182 ALA A CA  
2094 C  C   . ALA A  182 ? 0.22279 0.32571 0.20291 0.04466  -0.01452 0.00974  182 ALA A C   
2095 O  O   . ALA A  182 ? 0.24658 0.35796 0.23288 0.04841  -0.01499 0.01427  182 ALA A O   
2096 C  CB  . ALA A  182 ? 0.22699 0.30058 0.20599 0.04722  -0.00993 0.01166  182 ALA A CB  
2102 N  N   . ALA A  183 ? 0.21941 0.33048 0.19360 0.04227  -0.01634 0.00742  183 ALA A N   
2103 C  CA  . ALA A  183 ? 0.21693 0.34778 0.19073 0.04349  -0.01953 0.01036  183 ALA A CA  
2104 C  C   . ALA A  183 ? 0.23938 0.38313 0.21756 0.04008  -0.02186 0.00709  183 ALA A C   
2105 O  O   . ALA A  183 ? 0.26867 0.43033 0.24936 0.04219  -0.02482 0.01105  183 ALA A O   
2106 C  CB  . ALA A  183 ? 0.26280 0.39772 0.22774 0.04049  -0.02039 0.00689  183 ALA A CB  
2112 N  N   . ASP A  184 ? 0.24020 0.37610 0.21974 0.03480  -0.02065 0.00046  184 ASP A N   
2113 C  CA  . ASP A  184 ? 0.23628 0.38383 0.22123 0.03139  -0.02217 -0.00225 184 ASP A CA  
2114 C  C   . ASP A  184 ? 0.24295 0.38715 0.23632 0.03528  -0.02004 0.00163  184 ASP A C   
2115 O  O   . ASP A  184 ? 0.26723 0.42041 0.26625 0.03260  -0.02048 -0.00050 184 ASP A O   
2116 C  CB  . ASP A  184 ? 0.28776 0.42903 0.26963 0.02259  -0.02162 -0.01177 184 ASP A CB  
2117 C  CG  . ASP A  184 ? 0.36502 0.51295 0.33955 0.01745  -0.02371 -0.01766 184 ASP A CG  
2118 O  OD1 . ASP A  184 ? 0.37817 0.54256 0.35097 0.01913  -0.02675 -0.01509 184 ASP A OD1 
2119 O  OD2 . ASP A  184 ? 0.42173 0.55876 0.39230 0.01155  -0.02225 -0.02499 184 ASP A OD2 
2124 N  N   . ASP A  185 ? 0.24278 0.37497 0.23741 0.04118  -0.01747 0.00687  185 ASP A N   
2125 C  CA  . ASP A  185 ? 0.27583 0.40015 0.27672 0.04382  -0.01438 0.00852  185 ASP A CA  
2126 C  C   . ASP A  185 ? 0.25308 0.36744 0.25259 0.03713  -0.01253 0.00159  185 ASP A C   
2127 O  O   . ASP A  185 ? 0.25864 0.37395 0.26348 0.03669  -0.01065 0.00092  185 ASP A O   
2128 C  CB  . ASP A  185 ? 0.28883 0.42819 0.29908 0.04868  -0.01485 0.01333  185 ASP A CB  
2129 C  CG  . ASP A  185 ? 0.55343 0.68311 0.56927 0.05529  -0.01114 0.01813  185 ASP A CG  
2130 O  OD1 . ASP A  185 ? 0.40512 0.52282 0.41808 0.05888  -0.00977 0.02161  185 ASP A OD1 
2131 O  OD2 . ASP A  185 ? 0.44185 0.57568 0.46506 0.05655  -0.00925 0.01795  185 ASP A OD2 
2136 N  N   . GLY A  186 ? 0.25959 0.36313 0.25182 0.03220  -0.01260 -0.00318 186 GLY A N   
2137 C  CA  . GLY A  186 ? 0.27996 0.37286 0.27047 0.02612  -0.01092 -0.00860 186 GLY A CA  
2138 C  C   . GLY A  186 ? 0.24439 0.32047 0.23406 0.02788  -0.00803 -0.00715 186 GLY A C   
2139 O  O   . GLY A  186 ? 0.26931 0.33580 0.25683 0.02309  -0.00669 -0.01068 186 GLY A O   
2143 N  N   . ILE A  187 ? 0.25733 0.32988 0.24866 0.03432  -0.00704 -0.00192 187 ILE A N   
2144 C  CA  . ILE A  187 ? 0.20626 0.26331 0.19658 0.03596  -0.00450 -0.00070 187 ILE A CA  
2145 C  C   . ILE A  187 ? 0.22729 0.28704 0.22323 0.04291  -0.00293 0.00468  187 ILE A C   
2146 O  O   . ILE A  187 ? 0.26149 0.33172 0.26045 0.04725  -0.00423 0.00879  187 ILE A O   
2147 C  CB  . ILE A  187 ? 0.27453 0.31853 0.25928 0.03529  -0.00479 -0.00108 187 ILE A CB  
2148 C  CG1 . ILE A  187 ? 0.25437 0.30461 0.23709 0.03710  -0.00670 0.00036  187 ILE A CG1 
2149 C  CG2 . ILE A  187 ? 0.26114 0.29581 0.24159 0.02908  -0.00481 -0.00591 187 ILE A CG2 
2150 C  CD1 . ILE A  187 ? 0.26478 0.30389 0.24316 0.03673  -0.00655 -0.00012 187 ILE A CD1 
2162 N  N   . GLN A  188 ? 0.18949 0.23882 0.18642 0.04404  -0.00003 0.00483  188 GLN A N   
2163 C  CA  . GLN A  188 ? 0.19074 0.23805 0.19274 0.05011  0.00247  0.00879  188 GLN A CA  
2164 C  C   . GLN A  188 ? 0.19025 0.22559 0.18998 0.05268  0.00302  0.01159  188 GLN A C   
2165 O  O   . GLN A  188 ? 0.21620 0.24916 0.22043 0.05788  0.00513  0.01537  188 GLN A O   
2166 C  CB  . GLN A  188 ? 0.19654 0.23981 0.20061 0.04901  0.00592  0.00599  188 GLN A CB  
2167 C  CG  . GLN A  188 ? 0.20140 0.25886 0.21116 0.04861  0.00650  0.00486  188 GLN A CG  
2168 C  CD  . GLN A  188 ? 0.22248 0.28637 0.22915 0.04207  0.00405  0.00119  188 GLN A CD  
2169 O  OE1 . GLN A  188 ? 0.20140 0.25620 0.20202 0.03635  0.00413  -0.00243 188 GLN A OE1 
2170 N  NE2 . GLN A  188 ? 0.23972 0.31986 0.25086 0.04261  0.00183  0.00214  188 GLN A NE2 
2179 N  N   . ALA A  189 ? 0.17874 0.20684 0.17253 0.04929  0.00138  0.00997  189 ALA A N   
2180 C  CA  . ALA A  189 ? 0.19841 0.21738 0.19069 0.05118  0.00162  0.01266  189 ALA A CA  
2181 C  C   . ALA A  189 ? 0.18253 0.19974 0.16956 0.04773  -0.00064 0.01073  189 ALA A C   
2182 O  O   . ALA A  189 ? 0.19550 0.21159 0.17932 0.04308  -0.00167 0.00644  189 ALA A O   
2183 C  CB  . ALA A  189 ? 0.20505 0.21084 0.19698 0.05064  0.00388  0.01161  189 ALA A CB  
2189 N  N   . ALA A  190 ? 0.18947 0.20616 0.17602 0.05014  -0.00099 0.01409  190 ALA A N   
2190 C  CA  . ALA A  190 ? 0.17596 0.19129 0.15833 0.04775  -0.00239 0.01237  190 ALA A CA  
2191 C  C   . ALA A  190 ? 0.18516 0.19202 0.16783 0.04923  -0.00139 0.01509  190 ALA A C   
2192 O  O   . ALA A  190 ? 0.20156 0.20823 0.18730 0.05300  0.00001  0.01989  190 ALA A O   
2193 C  CB  . ALA A  190 ? 0.21093 0.23909 0.19203 0.04873  -0.00381 0.01332  190 ALA A CB  
2199 N  N   . ILE A  191 ? 0.18134 0.18168 0.16146 0.04628  -0.00204 0.01231  191 ILE A N   
2200 C  CA  . ILE A  191 ? 0.18613 0.18086 0.16700 0.04713  -0.00137 0.01446  191 ILE A CA  
2201 C  C   . ILE A  191 ? 0.18991 0.18757 0.16820 0.04595  -0.00199 0.01236  191 ILE A C   
2202 O  O   . ILE A  191 ? 0.19646 0.19195 0.17267 0.04294  -0.00301 0.00796  191 ILE A O   
2203 C  CB  . ILE A  191 ? 0.17687 0.16056 0.15859 0.04507  -0.00137 0.01336  191 ILE A CB  
2204 C  CG1 . ILE A  191 ? 0.18872 0.16901 0.17236 0.04586  -0.00013 0.01417  191 ILE A CG1 
2205 C  CG2 . ILE A  191 ? 0.19750 0.17740 0.18103 0.04556  -0.00092 0.01545  191 ILE A CG2 
2206 C  CD1 . ILE A  191 ? 0.21694 0.18743 0.20015 0.04311  -0.00033 0.01240  191 ILE A CD1 
2218 N  N   . GLY A  192 ? 0.19450 0.19629 0.17303 0.04826  -0.00093 0.01552  192 GLY A N   
2219 C  CA  . GLY A  192 ? 0.19782 0.20196 0.17421 0.04752  -0.00056 0.01341  192 GLY A CA  
2220 C  C   . GLY A  192 ? 0.20267 0.20000 0.18207 0.04776  0.00056  0.01490  192 GLY A C   
2221 O  O   . GLY A  192 ? 0.21842 0.21408 0.20073 0.04948  0.00176  0.01952  192 GLY A O   
2225 N  N   . LEU A  193 ? 0.19525 0.18857 0.17469 0.04596  0.00022  0.01108  193 LEU A N   
2226 C  CA  . LEU A  193 ? 0.18308 0.17161 0.16642 0.04615  0.00099  0.01211  193 LEU A CA  
2227 C  C   . LEU A  193 ? 0.18843 0.18256 0.17092 0.04718  0.00307  0.01077  193 LEU A C   
2228 O  O   . LEU A  193 ? 0.19425 0.18870 0.17470 0.04616  0.00308  0.00596  193 LEU A O   
2229 C  CB  . LEU A  193 ? 0.19992 0.18049 0.18465 0.04396  -0.00093 0.00921  193 LEU A CB  
2230 C  CG  . LEU A  193 ? 0.17683 0.15229 0.16033 0.04203  -0.00293 0.00885  193 LEU A CG  
2231 C  CD1 . LEU A  193 ? 0.19781 0.16680 0.18157 0.03991  -0.00474 0.00650  193 LEU A CD1 
2232 C  CD2 . LEU A  193 ? 0.19560 0.16855 0.18134 0.04245  -0.00274 0.01235  193 LEU A CD2 
2244 N  N   . ALA A  194 ? 0.19458 0.19313 0.17829 0.04897  0.00528  0.01466  194 ALA A N   
2245 C  CA  . ALA A  194 ? 0.21259 0.21756 0.19476 0.04989  0.00793  0.01339  194 ALA A CA  
2246 C  C   . ALA A  194 ? 0.20243 0.21299 0.17830 0.04900  0.00764  0.00839  194 ALA A C   
2247 O  O   . ALA A  194 ? 0.21278 0.22287 0.18780 0.04820  0.00872  0.00301  194 ALA A O   
2248 C  CB  . ALA A  194 ? 0.20809 0.20918 0.19537 0.04987  0.00915  0.01135  194 ALA A CB  
2254 N  N   . PRO A  195 ? 0.20164 0.21774 0.17358 0.04904  0.00621  0.00992  195 PRO A N   
2255 C  CA  . PRO A  195 ? 0.20779 0.22973 0.17426 0.04725  0.00524  0.00468  195 PRO A CA  
2256 C  C   . PRO A  195 ? 0.21731 0.24754 0.17896 0.04717  0.00762  0.00175  195 PRO A C   
2257 O  O   . PRO A  195 ? 0.22395 0.25926 0.18490 0.04906  0.00989  0.00578  195 PRO A O   
2258 C  CB  . PRO A  195 ? 0.23108 0.25908 0.19605 0.04804  0.00319  0.00867  195 PRO A CB  
2259 C  CG  . PRO A  195 ? 0.22493 0.25341 0.19261 0.05115  0.00457  0.01657  195 PRO A CG  
2260 C  CD  . PRO A  195 ? 0.19794 0.21536 0.17115 0.05080  0.00558  0.01647  195 PRO A CD  
2268 N  N   . TRP A  196 ? 0.22081 0.25222 0.17885 0.04451  0.00738  -0.00569 196 TRP A N   
2269 C  CA  . TRP A  196 ? 0.23169 0.27094 0.18382 0.04340  0.00962  -0.01084 196 TRP A CA  
2270 C  C   . TRP A  196 ? 0.21005 0.25671 0.15668 0.04027  0.00712  -0.01508 196 TRP A C   
2271 O  O   . TRP A  196 ? 0.23245 0.27386 0.18090 0.03796  0.00500  -0.01806 196 TRP A O   
2272 C  CB  . TRP A  196 ? 0.22552 0.25673 0.18008 0.04270  0.01243  -0.01756 196 TRP A CB  
2273 C  CG  . TRP A  196 ? 0.23771 0.27561 0.18680 0.04188  0.01593  -0.02356 196 TRP A CG  
2274 C  CD1 . TRP A  196 ? 0.25536 0.29580 0.20497 0.04402  0.02009  -0.02300 196 TRP A CD1 
2275 C  CD2 . TRP A  196 ? 0.25256 0.29601 0.19467 0.03829  0.01599  -0.03158 196 TRP A CD2 
2276 N  NE1 . TRP A  196 ? 0.29380 0.34076 0.23669 0.04227  0.02300  -0.03029 196 TRP A NE1 
2277 C  CE2 . TRP A  196 ? 0.25430 0.30307 0.19227 0.03856  0.02042  -0.03591 196 TRP A CE2 
2278 C  CE3 . TRP A  196 ? 0.24755 0.29255 0.18662 0.03446  0.01291  -0.03584 196 TRP A CE3 
2279 C  CZ2 . TRP A  196 ? 0.28759 0.34271 0.21778 0.03502  0.02176  -0.04476 196 TRP A CZ2 
2280 C  CZ3 . TRP A  196 ? 0.28799 0.33949 0.22010 0.03071  0.01394  -0.04433 196 TRP A CZ3 
2281 C  CH2 . TRP A  196 ? 0.31003 0.36633 0.23736 0.03092  0.01826  -0.04898 196 TRP A CH2 
2292 N  N   . ASN A  197 ? 0.22489 0.28465 0.16479 0.03995  0.00728  -0.01496 197 ASN A N   
2293 C  CA  . ASN A  197 ? 0.23113 0.30061 0.16539 0.03641  0.00483  -0.01971 197 ASN A CA  
2294 C  C   . ASN A  197 ? 0.24567 0.32784 0.17138 0.03558  0.00656  -0.02211 197 ASN A C   
2295 O  O   . ASN A  197 ? 0.26476 0.35052 0.18900 0.03853  0.00890  -0.01688 197 ASN A O   
2296 C  CB  . ASN A  197 ? 0.25069 0.32726 0.18631 0.03741  0.00080  -0.01326 197 ASN A CB  
2297 C  CG  . ASN A  197 ? 0.24739 0.33060 0.18073 0.03301  -0.00219 -0.01903 197 ASN A CG  
2298 O  OD1 . ASN A  197 ? 0.23241 0.30677 0.16843 0.02986  -0.00232 -0.02483 197 ASN A OD1 
2299 N  ND2 . ASN A  197 ? 0.24270 0.34226 0.17132 0.03264  -0.00472 -0.01694 197 ASN A ND2 
2306 N  N   . THR A  198 ? 0.26523 0.35494 0.18484 0.03103  0.00547  -0.03012 198 THR A N   
2307 C  CA  . THR A  198 ? 0.29649 0.39917 0.20654 0.02956  0.00710  -0.03335 198 THR A CA  
2308 C  C   . THR A  198 ? 0.25988 0.37744 0.16578 0.03240  0.00495  -0.02334 198 THR A C   
2309 O  O   . THR A  198 ? 0.30904 0.43463 0.20845 0.03334  0.00749  -0.02168 198 THR A O   
2310 C  CB  . THR A  198 ? 0.33291 0.44130 0.23712 0.02337  0.00592  -0.04432 198 THR A CB  
2311 O  OG1 . THR A  198 ? 0.41182 0.50524 0.31976 0.02097  0.00882  -0.05346 198 THR A OG1 
2312 C  CG2 . THR A  198 ? 0.37363 0.49695 0.26641 0.02135  0.00749  -0.04814 198 THR A CG2 
2320 N  N   . SER A  199 ? 0.27354 0.39496 0.18332 0.03399  0.00062  -0.01630 199 SER A N   
2321 C  CA  . SER A  199 ? 0.28074 0.41610 0.18759 0.03717  -0.00168 -0.00610 199 SER A CA  
2322 C  C   . SER A  199 ? 0.24702 0.37682 0.16297 0.04155  -0.00368 0.00342  199 SER A C   
2323 O  O   . SER A  199 ? 0.26513 0.38394 0.18802 0.04097  -0.00436 0.00096  199 SER A O   
2324 C  CB  . SER A  199 ? 0.35053 0.50426 0.24999 0.03342  -0.00583 -0.00941 199 SER A CB  
2325 O  OG  . SER A  199 ? 0.44150 0.60763 0.34135 0.03708  -0.00937 0.00150  199 SER A OG  
2331 N  N   . SER A  200 ? 0.27130 0.40891 0.18678 0.04587  -0.00437 0.01435  200 SER A N   
2332 C  CA  . SER A  200 ? 0.25093 0.38594 0.17453 0.05014  -0.00643 0.02330  200 SER A CA  
2333 C  C   . SER A  200 ? 0.27080 0.42154 0.19389 0.05040  -0.01138 0.02617  200 SER A C   
2334 O  O   . SER A  200 ? 0.27306 0.42294 0.20362 0.05414  -0.01309 0.03291  200 SER A O   
2335 C  CB  . SER A  200 ? 0.25267 0.38568 0.17803 0.05524  -0.00413 0.03467  200 SER A CB  
2336 O  OG  . SER A  200 ? 0.28332 0.43226 0.20119 0.05644  -0.00505 0.04070  200 SER A OG  
2342 N  N   . LEU A  201 ? 0.26465 0.43075 0.17926 0.04658  -0.01362 0.02129  201 LEU A N   
2343 C  CA  . LEU A  201 ? 0.26511 0.45020 0.17837 0.04721  -0.01866 0.02583  201 LEU A CA  
2344 C  C   . LEU A  201 ? 0.27133 0.45764 0.19226 0.04586  -0.02204 0.02281  201 LEU A C   
2345 O  O   . LEU A  201 ? 0.32206 0.52268 0.24583 0.04841  -0.02604 0.02938  201 LEU A O   
2346 C  CB  . LEU A  201 ? 0.28544 0.48674 0.18661 0.04240  -0.02007 0.02005  201 LEU A CB  
2347 C  CG  . LEU A  201 ? 0.27714 0.48204 0.16957 0.04407  -0.01693 0.02475  201 LEU A CG  
2348 C  CD1 . LEU A  201 ? 0.30129 0.52064 0.18080 0.03808  -0.01763 0.01596  201 LEU A CD1 
2349 C  CD2 . LEU A  201 ? 0.38128 0.59575 0.27477 0.05045  -0.01871 0.04024  201 LEU A CD2 
2361 N  N   . GLY A  202 ? 0.26317 0.43624 0.18757 0.04203  -0.02054 0.01365  202 GLY A N   
2362 C  CA  . GLY A  202 ? 0.25667 0.42931 0.18858 0.04037  -0.02287 0.01077  202 GLY A CA  
2363 C  C   . GLY A  202 ? 0.28610 0.44805 0.22805 0.04572  -0.02177 0.01785  202 GLY A C   
2364 O  O   . GLY A  202 ? 0.27463 0.43572 0.22322 0.04474  -0.02301 0.01591  202 GLY A O   
2368 N  N   . PHE A  203 ? 0.24989 0.40278 0.19321 0.05087  -0.01897 0.02538  203 PHE A N   
2369 C  CA  . PHE A  203 ? 0.22643 0.36605 0.17860 0.05528  -0.01704 0.03065  203 PHE A CA  
2370 C  C   . PHE A  203 ? 0.26983 0.41750 0.22707 0.06208  -0.01821 0.04242  203 PHE A C   
2371 O  O   . PHE A  203 ? 0.29015 0.42687 0.25477 0.06618  -0.01615 0.04718  203 PHE A O   
2372 C  CB  . PHE A  203 ? 0.23183 0.35429 0.18331 0.05589  -0.01282 0.03052  203 PHE A CB  
2373 C  CG  . PHE A  203 ? 0.21594 0.32860 0.16447 0.05048  -0.01131 0.02013  203 PHE A CG  
2374 C  CD1 . PHE A  203 ? 0.22869 0.34140 0.17781 0.04575  -0.01288 0.01200  203 PHE A CD1 
2375 C  CD2 . PHE A  203 ? 0.23147 0.33446 0.17749 0.05028  -0.00802 0.01888  203 PHE A CD2 
2376 C  CE1 . PHE A  203 ? 0.24051 0.34271 0.18759 0.04125  -0.01118 0.00328  203 PHE A CE1 
2377 C  CE2 . PHE A  203 ? 0.22876 0.32236 0.17331 0.04616  -0.00647 0.00998  203 PHE A CE2 
2378 C  CZ  . PHE A  203 ? 0.25031 0.34287 0.19529 0.04180  -0.00804 0.00236  203 PHE A CZ  
2388 N  N   . ARG A  204 ? 0.25805 0.42473 0.21190 0.06334  -0.02155 0.04708  204 ARG A N   
2389 C  CA  . ARG A  204 ? 0.26634 0.44052 0.22433 0.07047  -0.02242 0.05977  204 ARG A CA  
2390 C  C   . ARG A  204 ? 0.30919 0.48834 0.27774 0.07421  -0.02430 0.06326  204 ARG A C   
2391 O  O   . ARG A  204 ? 0.33349 0.51830 0.30725 0.08094  -0.02486 0.07416  204 ARG A O   
2392 C  CB  . ARG A  204 ? 0.30569 0.49988 0.25513 0.07045  -0.02562 0.06426  204 ARG A CB  
2393 C  CG  . ARG A  204 ? 0.30735 0.49710 0.24702 0.06847  -0.02271 0.06346  204 ARG A CG  
2394 C  CD  . ARG A  204 ? 0.36039 0.57089 0.28948 0.06728  -0.02573 0.06639  204 ARG A CD  
2395 N  NE  . ARG A  204 ? 0.66351 0.86916 0.58498 0.06738  -0.02189 0.06911  204 ARG A NE  
2396 C  CZ  . ARG A  204 ? 0.86790 1.08855 0.77874 0.06649  -0.02294 0.07238  204 ARG A CZ  
2397 N  NH1 . ARG A  204 ? 0.63190 0.87233 0.53922 0.06472  -0.02782 0.07258  204 ARG A NH1 
2398 N  NH2 . ARG A  204 ? 0.83797 1.05281 0.74279 0.06653  -0.01850 0.07470  204 ARG A NH2 
2412 N  N   . SER A  205 ? 0.25205 0.42915 0.22431 0.07023  -0.02489 0.05471  205 SER A N   
2413 C  CA  . SER A  205 ? 0.29637 0.47728 0.27933 0.07343  -0.02573 0.05689  205 SER A CA  
2414 C  C   . SER A  205 ? 0.26548 0.42832 0.25389 0.07198  -0.02217 0.05106  205 SER A C   
2415 O  O   . SER A  205 ? 0.29410 0.46027 0.29073 0.07327  -0.02237 0.05060  205 SER A O   
2416 C  CB  . SER A  205 ? 0.33052 0.53262 0.31365 0.06971  -0.03062 0.05302  205 SER A CB  
2417 O  OG  . SER A  205 ? 0.43875 0.65965 0.41738 0.07182  -0.03443 0.05983  205 SER A OG  
2423 N  N   . ILE A  206 ? 0.24654 0.39113 0.23091 0.06954  -0.01886 0.04700  206 ILE A N   
2424 C  CA  . ILE A  206 ? 0.23641 0.36454 0.22488 0.06795  -0.01587 0.04195  206 ILE A CA  
2425 C  C   . ILE A  206 ? 0.22299 0.34582 0.22080 0.07447  -0.01355 0.04851  206 ILE A C   
2426 O  O   . ILE A  206 ? 0.24528 0.36460 0.24491 0.07988  -0.01205 0.05658  206 ILE A O   
2427 C  CB  . ILE A  206 ? 0.21875 0.32995 0.20178 0.06526  -0.01316 0.03847  206 ILE A CB  
2428 C  CG1 . ILE A  206 ? 0.24336 0.35651 0.21868 0.05851  -0.01446 0.02991  206 ILE A CG1 
2429 C  CG2 . ILE A  206 ? 0.22387 0.31785 0.21144 0.06505  -0.01009 0.03591  206 ILE A CG2 
2430 C  CD1 . ILE A  206 ? 0.24435 0.34370 0.21486 0.05656  -0.01197 0.02709  206 ILE A CD1 
2442 N  N   . GLU A  207 ? 0.20897 0.33079 0.21292 0.07382  -0.01277 0.04488  207 GLU A N   
2443 C  CA  . GLU A  207 ? 0.22489 0.33900 0.23757 0.07916  -0.00951 0.04859  207 GLU A CA  
2444 C  C   . GLU A  207 ? 0.21310 0.30849 0.22512 0.07593  -0.00602 0.04238  207 GLU A C   
2445 O  O   . GLU A  207 ? 0.24339 0.32871 0.26084 0.07979  -0.00259 0.04469  207 GLU A O   
2446 C  CB  . GLU A  207 ? 0.24973 0.37872 0.27102 0.08170  -0.01067 0.04968  207 GLU A CB  
2447 C  CG  . GLU A  207 ? 0.28566 0.43440 0.30920 0.08606  -0.01443 0.05739  207 GLU A CG  
2448 C  CD  . GLU A  207 ? 0.34352 0.50681 0.37862 0.09102  -0.01508 0.06108  207 GLU A CD  
2449 O  OE1 . GLU A  207 ? 0.34459 0.50309 0.38531 0.09022  -0.01233 0.05641  207 GLU A OE1 
2450 O  OE2 . GLU A  207 ? 0.37532 0.55500 0.41324 0.09541  -0.01834 0.06856  207 GLU A OE2 
2457 N  N   . THR A  208 ? 0.19347 0.28415 0.19912 0.06902  -0.00677 0.03469  208 THR A N   
2458 C  CA  . THR A  208 ? 0.20087 0.27447 0.20462 0.06574  -0.00414 0.02967  208 THR A CA  
2459 C  C   . THR A  208 ? 0.20075 0.26075 0.20406 0.06861  -0.00176 0.03352  208 THR A C   
2460 O  O   . THR A  208 ? 0.20868 0.26914 0.20814 0.06908  -0.00263 0.03646  208 THR A O   
2461 C  CB  . THR A  208 ? 0.21134 0.28203 0.20774 0.05870  -0.00573 0.02273  208 THR A CB  
2462 O  OG1 . THR A  208 ? 0.23360 0.31684 0.23004 0.05504  -0.00797 0.01880  208 THR A OG1 
2463 C  CG2 . THR A  208 ? 0.21727 0.27193 0.21141 0.05525  -0.00376 0.01829  208 THR A CG2 
2471 N  N   . PRO A  209 ? 0.19898 0.23354 0.19398 0.05656  0.00161  0.01558  209 PRO A N   
2472 C  CA  . PRO A  209 ? 0.21063 0.23869 0.21517 0.05703  0.00208  0.02148  209 PRO A CA  
2473 C  C   . PRO A  209 ? 0.20913 0.23542 0.20949 0.05507  0.00237  0.01779  209 PRO A C   
2474 O  O   . PRO A  209 ? 0.20910 0.22627 0.20285 0.05238  0.00116  0.00841  209 PRO A O   
2475 C  CB  . PRO A  209 ? 0.21433 0.22541 0.22414 0.05621  0.00060  0.01857  209 PRO A CB  
2476 C  CG  . PRO A  209 ? 0.23495 0.24862 0.24239 0.05703  0.00008  0.01664  209 PRO A CG  
2477 C  CD  . PRO A  209 ? 0.20185 0.22718 0.19792 0.05626  0.00032  0.01172  209 PRO A CD  
2485 N  N   . THR A  210 ? 0.18336 0.21809 0.18781 0.05638  0.00394  0.02522  210 THR A N   
2486 C  CA  . THR A  210 ? 0.18009 0.21670 0.18014 0.05497  0.00461  0.02252  210 THR A CA  
2487 C  C   . THR A  210 ? 0.18200 0.21383 0.19150 0.05529  0.00532  0.02867  210 THR A C   
2488 O  O   . THR A  210 ? 0.20034 0.23859 0.21814 0.05758  0.00649  0.03867  210 THR A O   
2489 C  CB  . THR A  210 ? 0.20058 0.25524 0.19381 0.05612  0.00617  0.02463  210 THR A CB  
2490 O  OG1 . THR A  210 ? 0.21523 0.27412 0.19874 0.05549  0.00532  0.01809  210 THR A OG1 
2491 C  CG2 . THR A  210 ? 0.20659 0.26396 0.19617 0.05503  0.00712  0.02274  210 THR A CG2 
2499 N  N   A LEU A  211 ? 0.18735 0.20733 0.19597 0.05292  0.00442  0.02277  211 LEU A N   
2500 N  N   B LEU A  211 ? 0.16408 0.18513 0.17209 0.05292  0.00454  0.02269  211 LEU A N   
2501 C  CA  A LEU A  211 ? 0.19525 0.21039 0.21171 0.05277  0.00497  0.02732  211 LEU A CA  
2502 C  CA  B LEU A  211 ? 0.17009 0.18490 0.18627 0.05267  0.00493  0.02694  211 LEU A CA  
2503 C  C   A LEU A  211 ? 0.17745 0.19977 0.18778 0.05186  0.00611  0.02464  211 LEU A C   
2504 C  C   B LEU A  211 ? 0.19689 0.21843 0.20739 0.05175  0.00606  0.02445  211 LEU A C   
2505 O  O   A LEU A  211 ? 0.19244 0.21272 0.19313 0.04989  0.00526  0.01537  211 LEU A O   
2506 O  O   B LEU A  211 ? 0.18332 0.20165 0.18468 0.04964  0.00514  0.01506  211 LEU A O   
2507 C  CB  A LEU A  211 ? 0.16831 0.16414 0.18899 0.05077  0.00301  0.02295  211 LEU A CB  
2508 C  CB  B LEU A  211 ? 0.25345 0.24882 0.27263 0.05051  0.00282  0.02148  211 LEU A CB  
2509 C  CG  A LEU A  211 ? 0.21511 0.20491 0.24522 0.05067  0.00333  0.02837  211 LEU A CG  
2510 C  CG  B LEU A  211 ? 0.19510 0.18132 0.22041 0.04932  0.00264  0.02268  211 LEU A CG  
2511 C  CD1 A LEU A  211 ? 0.20709 0.18006 0.24503 0.05011  0.00149  0.02868  211 LEU A CD1 
2512 C  CD1 B LEU A  211 ? 0.26996 0.25871 0.30736 0.05158  0.00366  0.03426  211 LEU A CD1 
2513 C  CD2 A LEU A  211 ? 0.18752 0.17451 0.21296 0.04849  0.00328  0.02253  211 LEU A CD2 
2514 C  CD2 B LEU A  211 ? 0.21778 0.18499 0.24303 0.04677  0.00026  0.01515  211 LEU A CD2 
2537 N  N   . ILE A  212 ? 0.17832 0.20894 0.19423 0.05328  0.00801  0.03269  212 ILE A N   
2538 C  CA  . ILE A  212 ? 0.17972 0.21716 0.19120 0.05265  0.00937  0.03110  212 ILE A CA  
2539 C  C   . ILE A  212 ? 0.19485 0.22407 0.21513 0.05201  0.00956  0.03439  212 ILE A C   
2540 O  O   . ILE A  212 ? 0.19616 0.22609 0.22670 0.05355  0.01031  0.04368  212 ILE A O   
2541 C  CB  . ILE A  212 ? 0.18921 0.24607 0.19782 0.05489  0.01175  0.03725  212 ILE A CB  
2542 C  CG1 . ILE A  212 ? 0.21285 0.27698 0.21081 0.05495  0.01124  0.03188  212 ILE A CG1 
2543 C  CG2 . ILE A  212 ? 0.21164 0.27457 0.21851 0.05454  0.01348  0.03744  212 ILE A CG2 
2544 C  CD1 . ILE A  212 ? 0.26031 0.34266 0.25591 0.05730  0.01318  0.03846  212 ILE A CD1 
2556 N  N   . PHE A  213 ? 0.18385 0.20495 0.20017 0.04967  0.00871  0.02668  213 PHE A N   
2557 C  CA  . PHE A  213 ? 0.17502 0.19101 0.19794 0.04896  0.00917  0.02902  213 PHE A CA  
2558 C  C   . PHE A  213 ? 0.21008 0.24065 0.22908 0.04976  0.01161  0.03078  213 PHE A C   
2559 O  O   . PHE A  213 ? 0.21893 0.25370 0.22767 0.04882  0.01161  0.02336  213 PHE A O   
2560 C  CB  . PHE A  213 ? 0.20315 0.20264 0.22383 0.04596  0.00685  0.01964  213 PHE A CB  
2561 C  CG  . PHE A  213 ? 0.19023 0.17346 0.21603 0.04498  0.00450  0.01830  213 PHE A CG  
2562 C  CD1 . PHE A  213 ? 0.21775 0.19419 0.25535 0.04569  0.00432  0.02581  213 PHE A CD1 
2563 C  CD2 . PHE A  213 ? 0.20923 0.18335 0.22774 0.04319  0.00235  0.00908  213 PHE A CD2 
2564 C  CE1 . PHE A  213 ? 0.20650 0.16760 0.24848 0.04481  0.00212  0.02432  213 PHE A CE1 
2565 C  CE2 . PHE A  213 ? 0.22408 0.18311 0.24691 0.04225  0.00031  0.00755  213 PHE A CE2 
2566 C  CZ  . PHE A  213 ? 0.21499 0.16728 0.24935 0.04307  0.00016  0.01494  213 PHE A CZ  
2576 N  N   . ALA A  214 ? 0.20099 0.23893 0.22821 0.05144  0.01363  0.04054  214 ALA A N   
2577 C  CA  . ALA A  214 ? 0.17470 0.22640 0.20014 0.05242  0.01629  0.04382  214 ALA A CA  
2578 C  C   . ALA A  214 ? 0.22452 0.26913 0.25624 0.05124  0.01652  0.04425  214 ALA A C   
2579 O  O   . ALA A  214 ? 0.23634 0.27007 0.27766 0.05080  0.01545  0.04780  214 ALA A O   
2580 C  CB  . ALA A  214 ? 0.20911 0.27466 0.23979 0.05515  0.01850  0.05522  214 ALA A CB  
2586 N  N   . CYS A  215 ? 0.19083 0.24061 0.21684 0.05061  0.01766  0.03990  215 CYS A N   
2587 C  CA  . CYS A  215 ? 0.18183 0.22599 0.21340 0.04953  0.01801  0.03999  215 CYS A CA  
2588 C  C   . CYS A  215 ? 0.19472 0.25376 0.23074 0.05154  0.02138  0.04917  215 CYS A C   
2589 O  O   . CYS A  215 ? 0.19803 0.27053 0.22664 0.05249  0.02339  0.04828  215 CYS A O   
2590 C  CB  . CYS A  215 ? 0.20343 0.24232 0.22604 0.04739  0.01685  0.02858  215 CYS A CB  
2591 S  SG  . CYS A  215 ? 0.20433 0.22404 0.22222 0.04464  0.01268  0.01775  215 CYS A SG  
2596 N  N   . GLU A  216 ? 0.19121 0.24804 0.23924 0.05224  0.02196  0.05834  216 GLU A N   
2597 C  CA  . GLU A  216 ? 0.19089 0.26251 0.24398 0.05442  0.02508  0.06890  216 GLU A CA  
2598 C  C   . GLU A  216 ? 0.21184 0.29538 0.25943 0.05476  0.02774  0.06727  216 GLU A C   
2599 O  O   . GLU A  216 ? 0.22288 0.32243 0.26736 0.05666  0.03033  0.07229  216 GLU A O   
2600 C  CB  . GLU A  216 ? 0.20661 0.27239 0.27360 0.05457  0.02514  0.07778  216 GLU A CB  
2601 C  CG  . GLU A  216 ? 0.21353 0.29455 0.28619 0.05673  0.02830  0.08930  216 GLU A CG  
2602 C  CD  . GLU A  216 ? 0.28979 0.36510 0.37591 0.05665  0.02833  0.09761  216 GLU A CD  
2603 O  OE1 . GLU A  216 ? 0.27080 0.33235 0.36177 0.05486  0.02661  0.09430  216 GLU A OE1 
2604 O  OE2 . GLU A  216 ? 0.35446 0.43973 0.44685 0.05837  0.03021  0.10816  216 GLU A OE2 
2611 N  N   . ARG A  217 ? 0.20614 0.28235 0.25279 0.05303  0.02720  0.06070  217 ARG A N   
2612 C  CA  . ARG A  217 ? 0.19340 0.27960 0.23675 0.05337  0.02977  0.05964  217 ARG A CA  
2613 C  C   . ARG A  217 ? 0.21384 0.30171 0.24383 0.05252  0.02917  0.04847  217 ARG A C   
2614 O  O   . ARG A  217 ? 0.24417 0.33504 0.27092 0.05211  0.03032  0.04434  217 ARG A O   
2615 C  CB  . ARG A  217 ? 0.22832 0.30635 0.28097 0.05224  0.02979  0.06109  217 ARG A CB  
2616 C  CG  . ARG A  217 ? 0.27848 0.35821 0.34392 0.05337  0.03092  0.07320  217 ARG A CG  
2617 C  CD  . ARG A  217 ? 0.46719 0.54123 0.54182 0.05244  0.03131  0.07553  217 ARG A CD  
2618 N  NE  . ARG A  217 ? 0.46017 0.54694 0.53220 0.05324  0.03453  0.07601  217 ARG A NE  
2619 C  CZ  . ARG A  217 ? 0.42667 0.51368 0.50694 0.05304  0.03597  0.08011  217 ARG A CZ  
2620 N  NH1 . ARG A  217 ? 0.49750 0.57291 0.58908 0.05203  0.03438  0.08426  217 ARG A NH1 
2621 N  NH2 . ARG A  217 ? 0.37340 0.47235 0.45051 0.05385  0.03901  0.07989  217 ARG A NH2 
2635 N  N   . ASP A  218 ? 0.21672 0.30382 0.23885 0.05241  0.02751  0.04393  218 ASP A N   
2636 C  CA  . ASP A  218 ? 0.21720 0.30574 0.22618 0.05155  0.02658  0.03340  218 ASP A CA  
2637 C  C   . ASP A  218 ? 0.24695 0.35306 0.24898 0.05325  0.02965  0.03463  218 ASP A C   
2638 O  O   . ASP A  218 ? 0.24447 0.36336 0.24680 0.05530  0.03170  0.04221  218 ASP A O   
2639 C  CB  . ASP A  218 ? 0.20490 0.29045 0.20885 0.05142  0.02447  0.03080  218 ASP A CB  
2640 C  CG  . ASP A  218 ? 0.20115 0.28406 0.19246 0.04997  0.02259  0.01923  218 ASP A CG  
2641 O  OD1 . ASP A  218 ? 0.22059 0.30946 0.20464 0.04980  0.02351  0.01418  218 ASP A OD1 
2642 O  OD2 . ASP A  218 ? 0.20345 0.27850 0.19208 0.04904  0.02016  0.01531  218 ASP A OD2 
2647 N  N   A SER A  219 ? 0.22290 0.32967 0.21867 0.05242  0.02995  0.02727  219 SER A N   
2648 N  N   B SER A  219 ? 0.22802 0.33455 0.22393 0.05239  0.02992  0.02725  219 SER A N   
2649 C  CA  A SER A  219 ? 0.22362 0.34638 0.21177 0.05396  0.03273  0.02733  219 SER A CA  
2650 C  CA  B SER A  219 ? 0.24258 0.36479 0.23082 0.05387  0.03267  0.02699  219 SER A CA  
2651 C  C   A SER A  219 ? 0.25395 0.37939 0.22807 0.05348  0.03134  0.01797  219 SER A C   
2652 C  C   B SER A  219 ? 0.24639 0.37140 0.22055 0.05340  0.03131  0.01765  219 SER A C   
2653 O  O   A SER A  219 ? 0.25903 0.39796 0.22542 0.05482  0.03340  0.01754  219 SER A O   
2654 O  O   B SER A  219 ? 0.30066 0.43873 0.26713 0.05466  0.03334  0.01687  219 SER A O   
2655 C  CB  A SER A  219 ? 0.33601 0.46015 0.32693 0.05381  0.03454  0.02647  219 SER A CB  
2656 C  CB  B SER A  219 ? 0.32765 0.45051 0.31881 0.05361  0.03436  0.02586  219 SER A CB  
2657 O  OG  A SER A  219 ? 0.29732 0.40900 0.28432 0.05155  0.03191  0.01590  219 SER A OG  
2658 O  OG  B SER A  219 ? 0.31273 0.43538 0.31672 0.05424  0.03602  0.03533  219 SER A OG  
2669 N  N   . ILE A  220 ? 0.24723 0.36022 0.21777 0.05158  0.02791  0.01057  220 ILE A N   
2670 C  CA  . ILE A  220 ? 0.27384 0.38795 0.23137 0.05080  0.02619  0.00135  220 ILE A CA  
2671 C  C   . ILE A  220 ? 0.25827 0.37843 0.21216 0.05185  0.02579  0.00431  220 ILE A C   
2672 O  O   . ILE A  220 ? 0.28212 0.41298 0.22609 0.05269  0.02632  0.00203  220 ILE A O   
2673 C  CB  . ILE A  220 ? 0.27181 0.36851 0.22725 0.04788  0.02259  -0.00892 220 ILE A CB  
2674 C  CG1 . ILE A  220 ? 0.33654 0.42675 0.29649 0.04681  0.02283  -0.01153 220 ILE A CG1 
2675 C  CG2 . ILE A  220 ? 0.31900 0.41634 0.26124 0.04688  0.02064  -0.01848 220 ILE A CG2 
2676 C  CD1 . ILE A  220 ? 0.41913 0.52139 0.37470 0.04803  0.02545  -0.01218 220 ILE A CD1 
2688 N  N   . ALA A  221 ? 0.24376 0.35704 0.20583 0.05184  0.02479  0.00948  221 ALA A N   
2689 C  CA  . ALA A  221 ? 0.22588 0.34503 0.18740 0.05315  0.02469  0.01443  221 ALA A CA  
2690 C  C   . ALA A  221 ? 0.20649 0.32941 0.18008 0.05489  0.02662  0.02664  221 ALA A C   
2691 O  O   . ALA A  221 ? 0.21918 0.33267 0.20071 0.05456  0.02521  0.02987  221 ALA A O   
2692 C  CB  . ALA A  221 ? 0.23667 0.34275 0.19630 0.05138  0.02130  0.00829  221 ALA A CB  
2698 N  N   . PRO A  222 ? 0.22039 0.35631 0.19587 0.05665  0.02979  0.03342  222 PRO A N   
2699 C  CA  . PRO A  222 ? 0.21911 0.35845 0.20638 0.05812  0.03162  0.04511  222 PRO A CA  
2700 C  C   . PRO A  222 ? 0.22570 0.36468 0.21696 0.05902  0.03060  0.05089  222 PRO A C   
2701 O  O   . PRO A  222 ? 0.23544 0.38183 0.21961 0.05983  0.03030  0.05020  222 PRO A O   
2702 C  CB  . PRO A  222 ? 0.24902 0.40566 0.23361 0.06001  0.03518  0.05037  222 PRO A CB  
2703 C  CG  . PRO A  222 ? 0.36585 0.52461 0.33952 0.05920  0.03524  0.04067  222 PRO A CG  
2704 C  CD  . PRO A  222 ? 0.25749 0.40548 0.22379 0.05733  0.03173  0.03034  222 PRO A CD  
2712 N  N   A VAL A  223 ? 0.18509 0.31520 0.18804 0.05891  0.02994  0.05672  223 VAL A N   
2713 N  N   B VAL A  223 ? 0.23036 0.36105 0.23343 0.05897  0.03010  0.05702  223 VAL A N   
2714 C  CA  A VAL A  223 ? 0.21737 0.34538 0.22494 0.05973  0.02870  0.06186  223 VAL A CA  
2715 C  CA  B VAL A  223 ? 0.20049 0.32832 0.20905 0.05974  0.02885  0.06247  223 VAL A CA  
2716 C  C   A VAL A  223 ? 0.21066 0.35537 0.21643 0.06208  0.03069  0.06978  223 VAL A C   
2717 C  C   B VAL A  223 ? 0.20427 0.34836 0.21096 0.06207  0.03069  0.07022  223 VAL A C   
2718 O  O   A VAL A  223 ? 0.21580 0.36236 0.21887 0.06272  0.02951  0.07017  223 VAL A O   
2719 O  O   B VAL A  223 ? 0.22406 0.36905 0.22897 0.06268  0.02942  0.07094  223 VAL A O   
2720 C  CB  A VAL A  223 ? 0.23311 0.34974 0.25403 0.05943  0.02787  0.06773  223 VAL A CB  
2721 C  CB  B VAL A  223 ? 0.25111 0.36868 0.27323 0.05947  0.02841  0.06872  223 VAL A CB  
2722 C  CG1 A VAL A  223 ? 0.24309 0.34257 0.26518 0.05694  0.02565  0.05944  223 VAL A CG1 
2723 C  CG1 B VAL A  223 ? 0.31984 0.43920 0.34941 0.06101  0.02819  0.07783  223 VAL A CG1 
2724 C  CG2 A VAL A  223 ? 0.24128 0.36619 0.27066 0.06074  0.03061  0.07790  223 VAL A CG2 
2725 C  CG2 B VAL A  223 ? 0.25606 0.35497 0.27910 0.05701  0.02553  0.06016  223 VAL A CG2 
2744 N  N   . ARG A  224 ? 0.23746 0.39443 0.24468 0.06337  0.03366  0.07618  224 ARG A N   
2745 C  CA  . ARG A  224 ? 0.22957 0.40209 0.23533 0.06551  0.03547  0.08414  224 ARG A CA  
2746 C  C   . ARG A  224 ? 0.22859 0.40953 0.22137 0.06584  0.03509  0.07846  224 ARG A C   
2747 O  O   . ARG A  224 ? 0.25227 0.44366 0.24363 0.06742  0.03566  0.08422  224 ARG A O   
2748 C  CB  . ARG A  224 ? 0.26541 0.44920 0.27502 0.06666  0.03886  0.09186  224 ARG A CB  
2749 C  CG  . ARG A  224 ? 0.63349 0.81121 0.65702 0.06671  0.03924  0.10004  224 ARG A CG  
2750 C  CD  . ARG A  224 ? 0.89897 1.08864 0.92623 0.06781  0.04274  0.10795  224 ARG A CD  
2751 N  NE  . ARG A  224 ? 1.00259 1.18581 1.04324 0.06762  0.04297  0.11532  224 ARG A NE  
2752 C  CZ  . ARG A  224 ? 1.10506 1.29548 1.15140 0.06819  0.04572  0.12228  224 ARG A CZ  
2753 N  NH1 . ARG A  224 ? 1.15123 1.35575 1.19117 0.06909  0.04871  0.12302  224 ARG A NH1 
2754 N  NH2 . ARG A  224 ? 1.11350 1.29673 1.17223 0.06784  0.04548  0.12864  224 ARG A NH2 
2768 N  N   . SER A  225 ? 0.24108 0.41850 0.22433 0.06442  0.03417  0.06773  225 SER A N   
2769 C  CA  . SER A  225 ? 0.25467 0.43961 0.22524 0.06455  0.03363  0.06180  225 SER A CA  
2770 C  C   . SER A  225 ? 0.23163 0.40546 0.19752 0.06300  0.03031  0.05308  225 SER A C   
2771 O  O   . SER A  225 ? 0.24804 0.42767 0.20427 0.06313  0.02949  0.04893  225 SER A O   
2772 C  CB  . SER A  225 ? 0.29495 0.48568 0.25658 0.06416  0.03506  0.05564  225 SER A CB  
2773 O  OG  . SER A  225 ? 0.33529 0.53805 0.29986 0.06572  0.03841  0.06348  225 SER A OG  
2779 N  N   . HIS A  226 ? 0.21465 0.37286 0.18692 0.06149  0.02836  0.05021  226 HIS A N   
2780 C  CA  . HIS A  226 ? 0.20834 0.35487 0.17632 0.05976  0.02528  0.04144  226 HIS A CA  
2781 C  C   . HIS A  226 ? 0.21213 0.34842 0.19018 0.05980  0.02380  0.04578  226 HIS A C   
2782 O  O   . HIS A  226 ? 0.21969 0.36093 0.19865 0.06111  0.02350  0.05028  226 HIS A O   
2783 C  CB  . HIS A  226 ? 0.21508 0.35172 0.17831 0.05748  0.02414  0.03114  226 HIS A CB  
2784 C  CG  . HIS A  226 ? 0.21641 0.36301 0.16890 0.05753  0.02531  0.02620  226 HIS A CG  
2785 N  ND1 . HIS A  226 ? 0.25145 0.40117 0.19213 0.05693  0.02393  0.01868  226 HIS A ND1 
2786 C  CD2 . HIS A  226 ? 0.23453 0.38874 0.18628 0.05815  0.02771  0.02774  226 HIS A CD2 
2787 C  CE1 . HIS A  226 ? 0.24944 0.40809 0.18238 0.05722  0.02534  0.01573  226 HIS A CE1 
2788 N  NE2 . HIS A  226 ? 0.26947 0.43133 0.20889 0.05804  0.02776  0.02119  226 HIS A NE2 
2796 N  N   . ALA A  227 ? 0.21723 0.27753 0.20774 0.05887  0.01863  0.05123  227 ALA A N   
2797 C  CA  . ALA A  227 ? 0.22524 0.27811 0.21728 0.06026  0.01730  0.05287  227 ALA A CA  
2798 C  C   . ALA A  227 ? 0.22132 0.27532 0.21399 0.06182  0.01884  0.05929  227 ALA A C   
2799 O  O   . ALA A  227 ? 0.22405 0.27576 0.21566 0.06369  0.01804  0.06081  227 ALA A O   
2800 C  CB  . ALA A  227 ? 0.22018 0.26514 0.21750 0.05901  0.01640  0.05087  227 ALA A CB  
2806 N  N   . SER A  228 ? 0.22597 0.28316 0.22072 0.06104  0.02108  0.06313  228 SER A N   
2807 C  CA  . SER A  228 ? 0.22774 0.28492 0.22363 0.06245  0.02243  0.06977  228 SER A CA  
2808 C  C   . SER A  228 ? 0.22410 0.28859 0.21538 0.06405  0.02231  0.07302  228 SER A C   
2809 O  O   . SER A  228 ? 0.23398 0.29609 0.22580 0.06643  0.02171  0.07610  228 SER A O   
2810 C  CB  . SER A  228 ? 0.26331 0.32134 0.26239 0.06078  0.02481  0.07299  228 SER A CB  
2811 O  OG  . SER A  228 ? 0.26457 0.32247 0.26449 0.06209  0.02609  0.07983  228 SER A OG  
2817 N  N   . PRO A  229 ? 0.23151 0.30499 0.21847 0.06282  0.02288  0.07232  229 PRO A N   
2818 C  CA  . PRO A  229 ? 0.24088 0.32175 0.22325 0.06412  0.02245  0.07529  229 PRO A CA  
2819 C  C   . PRO A  229 ? 0.23252 0.31123 0.21287 0.06594  0.02025  0.07199  229 PRO A C   
2820 O  O   . PRO A  229 ? 0.24453 0.32684 0.22324 0.06793  0.01963  0.07550  229 PRO A O   
2821 C  CB  . PRO A  229 ? 0.26844 0.35910 0.24630 0.06154  0.02377  0.07385  229 PRO A CB  
2822 C  CG  . PRO A  229 ? 0.31632 0.40404 0.29664 0.05932  0.02463  0.06871  229 PRO A CG  
2823 C  CD  . PRO A  229 ? 0.27629 0.35429 0.26282 0.05997  0.02442  0.06954  229 PRO A CD  
2831 N  N   . PHE A  230 ? 0.22664 0.30013 0.20699 0.06524  0.01898  0.06560  230 PHE A N   
2832 C  CA  . PHE A  230 ? 0.23523 0.30611 0.21346 0.06664  0.01700  0.06254  230 PHE A CA  
2833 C  C   . PHE A  230 ? 0.25428 0.31870 0.23648 0.06898  0.01667  0.06582  230 PHE A C   
2834 O  O   . PHE A  230 ? 0.23576 0.30191 0.21674 0.07099  0.01595  0.06714  230 PHE A O   
2835 C  CB  . PHE A  230 ? 0.24077 0.30653 0.21809 0.06512  0.01552  0.05537  230 PHE A CB  
2836 C  CG  . PHE A  230 ? 0.22445 0.29569 0.19862 0.06300  0.01605  0.05159  230 PHE A CG  
2837 C  CD1 . PHE A  230 ? 0.22716 0.30828 0.19782 0.06229  0.01769  0.05352  230 PHE A CD1 
2838 C  CD2 . PHE A  230 ? 0.23072 0.29708 0.20578 0.06153  0.01499  0.04613  230 PHE A CD2 
2839 C  CE1 . PHE A  230 ? 0.21734 0.30314 0.18568 0.06002  0.01881  0.04962  230 PHE A CE1 
2840 C  CE2 . PHE A  230 ? 0.23832 0.30907 0.21147 0.05979  0.01575  0.04256  230 PHE A CE2 
2841 C  CZ  . PHE A  230 ? 0.24638 0.32685 0.21625 0.05898  0.01796  0.04411  230 PHE A CZ  
2851 N  N   . TYR A  231 ? 0.22022 0.27700 0.20754 0.06865  0.01735  0.06681  231 TYR A N   
2852 C  CA  . TYR A  231 ? 0.22808 0.27806 0.21962 0.07058  0.01763  0.06962  231 TYR A CA  
2853 C  C   . TYR A  231 ? 0.24009 0.29503 0.23259 0.07300  0.01869  0.07690  231 TYR A C   
2854 O  O   . TYR A  231 ? 0.25100 0.30446 0.24512 0.07548  0.01841  0.07884  231 TYR A O   
2855 C  CB  . TYR A  231 ? 0.24496 0.28647 0.24161 0.06921  0.01859  0.06949  231 TYR A CB  
2856 C  CG  . TYR A  231 ? 0.24627 0.28089 0.24758 0.07096  0.01964  0.07281  231 TYR A CG  
2857 C  CD1 . TYR A  231 ? 0.27917 0.31482 0.28348 0.07253  0.02152  0.07973  231 TYR A CD1 
2858 C  CD2 . TYR A  231 ? 0.24527 0.27214 0.24793 0.07089  0.01887  0.06884  231 TYR A CD2 
2859 C  CE1 . TYR A  231 ? 0.25594 0.28491 0.26511 0.07440  0.02280  0.08289  231 TYR A CE1 
2860 C  CE2 . TYR A  231 ? 0.25049 0.27098 0.25784 0.07236  0.02037  0.07149  231 TYR A CE2 
2861 C  CZ  . TYR A  231 ? 0.27191 0.29311 0.28278 0.07424  0.02237  0.07830  231 TYR A CZ  
2862 O  OH  . TYR A  231 ? 0.30035 0.31461 0.31651 0.07589  0.02416  0.08088  231 TYR A OH  
2872 N  N   . ASN A  232 ? 0.24012 0.30124 0.23185 0.07222  0.01993  0.08114  232 ASN A N   
2873 C  CA  . ASN A  232 ? 0.23987 0.30577 0.23244 0.07425  0.02067  0.08882  232 ASN A CA  
2874 C  C   . ASN A  232 ? 0.27119 0.34587 0.25969 0.07580  0.01931  0.08994  232 ASN A C   
2875 O  O   . ASN A  232 ? 0.31908 0.39615 0.30954 0.07840  0.01924  0.09602  232 ASN A O   
2876 C  CB  . ASN A  232 ? 0.26747 0.33803 0.25943 0.07229  0.02231  0.09286  232 ASN A CB  
2877 C  CG  . ASN A  232 ? 0.28389 0.34626 0.28067 0.07110  0.02394  0.09341  232 ASN A CG  
2878 O  OD1 . ASN A  232 ? 0.30026 0.35348 0.30143 0.07217  0.02408  0.09268  232 ASN A OD1 
2879 N  ND2 . ASN A  232 ? 0.30851 0.37447 0.30449 0.06855  0.02545  0.09470  232 ASN A ND2 
2886 N  N   . ALA A  233 ? 0.25184 0.33108 0.23517 0.07433  0.01824  0.08431  233 ALA A N   
2887 C  CA  . ALA A  233 ? 0.25777 0.34572 0.23687 0.07538  0.01704  0.08480  233 ALA A CA  
2888 C  C   . ALA A  233 ? 0.24915 0.33296 0.23054 0.07816  0.01584  0.08369  233 ALA A C   
2889 O  O   . ALA A  233 ? 0.28611 0.37635 0.26674 0.08017  0.01503  0.08675  233 ALA A O   
2890 C  CB  . ALA A  233 ? 0.25602 0.34866 0.22902 0.07269  0.01661  0.07822  233 ALA A CB  
2896 N  N   . ILE A  234 ? 0.24323 0.31683 0.22744 0.07806  0.01573  0.07919  234 ILE A N   
2897 C  CA  . ILE A  234 ? 0.25088 0.32014 0.23706 0.08009  0.01493  0.07704  234 ILE A CA  
2898 C  C   . ILE A  234 ? 0.25249 0.32082 0.24470 0.08351  0.01573  0.08396  234 ILE A C   
2899 O  O   . ILE A  234 ? 0.26797 0.33225 0.26447 0.08390  0.01715  0.08853  234 ILE A O   
2900 C  CB  . ILE A  234 ? 0.24717 0.30557 0.23475 0.07842  0.01480  0.07083  234 ILE A CB  
2901 C  CG1 . ILE A  234 ? 0.24057 0.30069 0.22230 0.07544  0.01365  0.06445  234 ILE A CG1 
2902 C  CG2 . ILE A  234 ? 0.24208 0.29515 0.23210 0.08003  0.01447  0.06845  234 ILE A CG2 
2903 C  CD1 . ILE A  234 ? 0.25055 0.30064 0.23331 0.07328  0.01307  0.05878  234 ILE A CD1 
2915 N  N   . PRO A  235 ? 0.25966 0.33142 0.25279 0.08607  0.01497  0.08491  235 PRO A N   
2916 C  CA  . PRO A  235 ? 0.27475 0.34578 0.27463 0.08973  0.01572  0.09182  235 PRO A CA  
2917 C  C   . PRO A  235 ? 0.27904 0.33792 0.28580 0.09038  0.01762  0.09240  235 PRO A C   
2918 O  O   . PRO A  235 ? 0.27499 0.32538 0.28211 0.08863  0.01802  0.08616  235 PRO A O   
2919 C  CB  . PRO A  235 ? 0.31327 0.38809 0.31343 0.09190  0.01462  0.08991  235 PRO A CB  
2920 C  CG  . PRO A  235 ? 0.28121 0.36386 0.27310 0.08946  0.01308  0.08505  235 PRO A CG  
2921 C  CD  . PRO A  235 ? 0.26149 0.33961 0.24942 0.08573  0.01341  0.08036  235 PRO A CD  
2929 N  N   . SER A  236 ? 0.31189 0.37006 0.32416 0.09278  0.01882  0.10016  236 SER A N   
2930 C  CA  . SER A  236 ? 0.31391 0.36057 0.33321 0.09353  0.02109  0.10125  236 SER A CA  
2931 C  C   . SER A  236 ? 0.30275 0.34325 0.32712 0.09551  0.02182  0.09801  236 SER A C   
2932 O  O   . SER A  236 ? 0.32088 0.35077 0.35011 0.09506  0.02393  0.09630  236 SER A O   
2933 C  CB  . SER A  236 ? 0.41540 0.46317 0.43913 0.09572  0.02221  0.11082  236 SER A CB  
2934 O  OG  . SER A  236 ? 0.47132 0.52336 0.49931 0.09950  0.02172  0.11558  236 SER A OG  
2940 N  N   . SER A  237 ? 0.28593 0.33292 0.30911 0.09725  0.02035  0.09660  237 SER A N   
2941 C  CA  . SER A  237 ? 0.28148 0.32326 0.30923 0.09875  0.02121  0.09264  237 SER A CA  
2942 C  C   . SER A  237 ? 0.29504 0.33181 0.31807 0.09511  0.02077  0.08286  237 SER A C   
2943 O  O   . SER A  237 ? 0.30001 0.33146 0.32618 0.09538  0.02175  0.07852  237 SER A O   
2944 C  CB  . SER A  237 ? 0.30216 0.35363 0.33110 0.10215  0.01982  0.09530  237 SER A CB  
2945 O  OG  . SER A  237 ? 0.31982 0.38226 0.34056 0.10069  0.01733  0.09447  237 SER A OG  
2951 N  N   . THR A  238 ? 0.25993 0.29843 0.27568 0.09163  0.01936  0.07935  238 THR A N   
2952 C  CA  . THR A  238 ? 0.27429 0.30799 0.28523 0.08796  0.01857  0.07073  238 THR A CA  
2953 C  C   . THR A  238 ? 0.24581 0.26851 0.25934 0.08544  0.02008  0.06869  238 THR A C   
2954 O  O   . THR A  238 ? 0.25973 0.28083 0.27573 0.08554  0.02115  0.07326  238 THR A O   
2955 C  CB  . THR A  238 ? 0.27609 0.31753 0.27874 0.08580  0.01638  0.06868  238 THR A CB  
2956 O  OG1 . THR A  238 ? 0.29285 0.34453 0.29271 0.08763  0.01511  0.06981  238 THR A OG1 
2957 C  CG2 . THR A  238 ? 0.25111 0.28719 0.24877 0.08184  0.01530  0.06051  238 THR A CG2 
2965 N  N   . ASP A  239 ? 0.24456 0.25979 0.25764 0.08300  0.02029  0.06195  239 ASP A N   
2966 C  CA  . ASP A  239 ? 0.27012 0.27561 0.28447 0.07970  0.02130  0.05910  239 ASP A CA  
2967 C  C   . ASP A  239 ? 0.25752 0.26547 0.26624 0.07690  0.01933  0.05762  239 ASP A C   
2968 O  O   . ASP A  239 ? 0.24867 0.25987 0.25122 0.07514  0.01708  0.05306  239 ASP A O   
2969 C  CB  . ASP A  239 ? 0.25787 0.25626 0.27128 0.07689  0.02142  0.05169  239 ASP A CB  
2970 C  CG  . ASP A  239 ? 0.39286 0.38712 0.41288 0.07901  0.02407  0.05200  239 ASP A CG  
2971 O  OD1 . ASP A  239 ? 0.34748 0.34425 0.37328 0.08308  0.02562  0.05820  239 ASP A OD1 
2972 O  OD2 . ASP A  239 ? 0.43184 0.42020 0.45136 0.07639  0.02464  0.04584  239 ASP A OD2 
2977 N  N   . LYS A  240 ? 0.23270 0.23903 0.24372 0.07641  0.02029  0.06130  240 LYS A N   
2978 C  CA  . LYS A  240 ? 0.23167 0.24075 0.23855 0.07399  0.01874  0.06010  240 LYS A CA  
2979 C  C   . LYS A  240 ? 0.22787 0.23037 0.23855 0.07204  0.02021  0.06126  240 LYS A C   
2980 O  O   . LYS A  240 ? 0.24009 0.23792 0.25631 0.07323  0.02267  0.06493  240 LYS A O   
2981 C  CB  . LYS A  240 ? 0.22584 0.24555 0.22979 0.07576  0.01802  0.06433  240 LYS A CB  
2982 C  CG  . LYS A  240 ? 0.24118 0.26369 0.24946 0.07866  0.01986  0.07233  240 LYS A CG  
2983 C  CD  . LYS A  240 ? 0.23906 0.27256 0.24334 0.07935  0.01902  0.07599  240 LYS A CD  
2984 C  CE  . LYS A  240 ? 0.24749 0.28371 0.25551 0.08162  0.02059  0.08438  240 LYS A CE  
2985 N  NZ  . LYS A  240 ? 0.26341 0.31029 0.26707 0.08128  0.01998  0.08790  240 LYS A NZ  
2999 N  N   . ALA A  241 ? 0.22802 0.23030 0.23595 0.06901  0.01872  0.05806  241 ALA A N   
3000 C  CA  . ALA A  241 ? 0.22520 0.22239 0.23641 0.06675  0.01979  0.05869  241 ALA A CA  
3001 C  C   . ALA A  241 ? 0.23999 0.24225 0.24845 0.06513  0.01824  0.05778  241 ALA A C   
3002 O  O   . ALA A  241 ? 0.23023 0.23693 0.23403 0.06464  0.01602  0.05446  241 ALA A O   
3003 C  CB  . ALA A  241 ? 0.25478 0.24267 0.26743 0.06365  0.01984  0.05390  241 ALA A CB  
3009 N  N   . TYR A  242 ? 0.23513 0.23665 0.24682 0.06428  0.01969  0.06070  242 TYR A N   
3010 C  CA  . TYR A  242 ? 0.22322 0.22943 0.23394 0.06276  0.01898  0.06033  242 TYR A CA  
3011 C  C   . TYR A  242 ? 0.22591 0.22584 0.24057 0.05983  0.01956  0.05903  242 TYR A C   
3012 O  O   . TYR A  242 ? 0.24624 0.24194 0.26491 0.05986  0.02201  0.06235  242 TYR A O   
3013 C  CB  . TYR A  242 ? 0.24401 0.25728 0.25482 0.06468  0.02066  0.06615  242 TYR A CB  
3014 C  CG  . TYR A  242 ? 0.22600 0.24509 0.23596 0.06318  0.02064  0.06603  242 TYR A CG  
3015 C  CD1 . TYR A  242 ? 0.23533 0.26155 0.24095 0.06314  0.01920  0.06361  242 TYR A CD1 
3016 C  CD2 . TYR A  242 ? 0.23570 0.25345 0.24937 0.06174  0.02249  0.06842  242 TYR A CD2 
3017 C  CE1 . TYR A  242 ? 0.23513 0.26681 0.24051 0.06174  0.01971  0.06331  242 TYR A CE1 
3018 C  CE2 . TYR A  242 ? 0.23202 0.25547 0.24544 0.06029  0.02288  0.06818  242 TYR A CE2 
3019 C  CZ  . TYR A  242 ? 0.23319 0.26371 0.24256 0.06035  0.02155  0.06556  242 TYR A CZ  
3020 O  OH  . TYR A  242 ? 0.30690 0.34311 0.31649 0.05877  0.02237  0.06487  242 TYR A OH  
3030 N  N   . PHE A  243 ? 0.20952 0.20877 0.22324 0.05726  0.01731  0.05435  243 PHE A N   
3031 C  CA  . PHE A  243 ? 0.23137 0.22624 0.24884 0.05421  0.01738  0.05298  243 PHE A CA  
3032 C  C   . PHE A  243 ? 0.21652 0.21746 0.23425 0.05340  0.01642  0.05221  243 PHE A C   
3033 O  O   . PHE A  243 ? 0.22162 0.22516 0.23678 0.05292  0.01385  0.04856  243 PHE A O   
3034 C  CB  . PHE A  243 ? 0.24058 0.22904 0.25728 0.05150  0.01517  0.04795  243 PHE A CB  
3035 C  CG  . PHE A  243 ? 0.22658 0.20798 0.24417 0.05135  0.01678  0.04798  243 PHE A CG  
3036 C  CD1 . PHE A  243 ? 0.24745 0.22863 0.26204 0.05317  0.01651  0.04708  243 PHE A CD1 
3037 C  CD2 . PHE A  243 ? 0.26616 0.24116 0.28792 0.04916  0.01885  0.04860  243 PHE A CD2 
3038 C  CE1 . PHE A  243 ? 0.27597 0.25073 0.29226 0.05307  0.01844  0.04686  243 PHE A CE1 
3039 C  CE2 . PHE A  243 ? 0.26801 0.23624 0.29101 0.04883  0.02083  0.04821  243 PHE A CE2 
3040 C  CZ  . PHE A  243 ? 0.26984 0.23798 0.29040 0.05086  0.02068  0.04734  243 PHE A CZ  
3050 N  N   . GLU A  244 ? 0.22092 0.22376 0.24199 0.05308  0.01864  0.05542  244 GLU A N   
3051 C  CA  . GLU A  244 ? 0.22670 0.23520 0.24919 0.05203  0.01838  0.05456  244 GLU A CA  
3052 C  C   . GLU A  244 ? 0.23109 0.23537 0.25802 0.04894  0.01755  0.05209  244 GLU A C   
3053 O  O   . GLU A  244 ? 0.23837 0.23785 0.26846 0.04764  0.01938  0.05386  244 GLU A O   
3054 C  CB  . GLU A  244 ? 0.24290 0.25662 0.26630 0.05292  0.02139  0.05924  244 GLU A CB  
3055 C  CG  . GLU A  244 ? 0.24452 0.26483 0.26915 0.05179  0.02144  0.05767  244 GLU A CG  
3056 C  CD  . GLU A  244 ? 0.34097 0.36633 0.36636 0.05179  0.02466  0.06205  244 GLU A CD  
3057 O  OE1 . GLU A  244 ? 0.29365 0.31555 0.32241 0.05062  0.02661  0.06457  244 GLU A OE1 
3058 O  OE2 . GLU A  244 ? 0.47739 0.51002 0.49980 0.05253  0.02529  0.06274  244 GLU A OE2 
3065 N  N   . ILE A  245 ? 0.21524 0.22134 0.24252 0.04773  0.01477  0.04810  245 ILE A N   
3066 C  CA  . ILE A  245 ? 0.21040 0.21358 0.24201 0.04475  0.01318  0.04560  245 ILE A CA  
3067 C  C   . ILE A  245 ? 0.21015 0.21827 0.24658 0.04399  0.01486  0.04665  245 ILE A C   
3068 O  O   . ILE A  245 ? 0.21724 0.23188 0.25362 0.04507  0.01502  0.04612  245 ILE A O   
3069 C  CB  . ILE A  245 ? 0.20900 0.21157 0.23891 0.04391  0.00905  0.04124  245 ILE A CB  
3070 C  CG1 . ILE A  245 ? 0.25843 0.25540 0.28370 0.04389  0.00781  0.04003  245 ILE A CG1 
3071 C  CG2 . ILE A  245 ? 0.23464 0.23593 0.26961 0.04096  0.00703  0.03918  245 ILE A CG2 
3072 C  CD1 . ILE A  245 ? 0.36081 0.35703 0.38275 0.04316  0.00383  0.03605  245 ILE A CD1 
3084 N  N   . SER A  246 ? 0.23577 0.24077 0.27622 0.04201  0.01669  0.04819  246 SER A N   
3085 C  CA  . SER A  246 ? 0.22475 0.23366 0.27004 0.04080  0.01879  0.04931  246 SER A CA  
3086 C  C   . SER A  246 ? 0.22128 0.23489 0.27024 0.03995  0.01646  0.04584  246 SER A C   
3087 O  O   . SER A  246 ? 0.24168 0.25285 0.29188 0.03863  0.01301  0.04283  246 SER A O   
3088 C  CB  . SER A  246 ? 0.25758 0.26082 0.30626 0.03817  0.02035  0.05040  246 SER A CB  
3089 O  OG  . SER A  246 ? 0.31457 0.32143 0.36801 0.03664  0.02245  0.05124  246 SER A OG  
3095 N  N   . GLY A  247 ? 0.22409 0.24455 0.27471 0.04067  0.01835  0.04631  247 GLY A N   
3096 C  CA  . GLY A  247 ? 0.20629 0.23179 0.26158 0.04017  0.01683  0.04305  247 GLY A CA  
3097 C  C   . GLY A  247 ? 0.22510 0.25177 0.27776 0.04174  0.01367  0.04009  247 GLY A C   
3098 O  O   . GLY A  247 ? 0.22485 0.25470 0.28182 0.04152  0.01200  0.03729  247 GLY A O   
3102 N  N   . GLY A  248 ? 0.20702 0.23133 0.25301 0.04337  0.01289  0.04057  248 GLY A N   
3103 C  CA  . GLY A  248 ? 0.21326 0.23661 0.25649 0.04416  0.00935  0.03750  248 GLY A CA  
3104 C  C   . GLY A  248 ? 0.18233 0.21208 0.22587 0.04550  0.00967  0.03547  248 GLY A C   
3105 O  O   . GLY A  248 ? 0.19153 0.22631 0.23305 0.04655  0.01275  0.03676  248 GLY A O   
3109 N  N   . ASN A  249 ? 0.18777 0.21715 0.23365 0.04528  0.00641  0.03225  249 ASN A N   
3110 C  CA  . ASN A  249 ? 0.17027 0.20444 0.21604 0.04661  0.00652  0.02977  249 ASN A CA  
3111 C  C   . ASN A  249 ? 0.18095 0.21342 0.21840 0.04797  0.00533  0.02896  249 ASN A C   
3112 O  O   . ASN A  249 ? 0.18274 0.21033 0.21546 0.04785  0.00405  0.03000  249 ASN A O   
3113 C  CB  . ASN A  249 ? 0.18506 0.21977 0.23809 0.04601  0.00380  0.02702  249 ASN A CB  
3114 C  CG  . ASN A  249 ? 0.18212 0.21092 0.23359 0.04535  -0.00125 0.02562  249 ASN A CG  
3115 O  OD1 . ASN A  249 ? 0.19121 0.21801 0.23656 0.04619  -0.00274 0.02445  249 ASN A OD1 
3116 N  ND2 . ASN A  249 ? 0.18240 0.20882 0.23945 0.04351  -0.00391 0.02569  249 ASN A ND2 
3123 N  N   . HIS A  250 ? 0.18140 0.21804 0.21714 0.04909  0.00604  0.02681  250 HIS A N   
3124 C  CA  . HIS A  250 ? 0.17279 0.20896 0.20046 0.05021  0.00551  0.02591  250 HIS A CA  
3125 C  C   . HIS A  250 ? 0.17249 0.20193 0.19693 0.04976  0.00116  0.02433  250 HIS A C   
3126 O  O   . HIS A  250 ? 0.19365 0.22158 0.21099 0.05037  0.00067  0.02400  250 HIS A O   
3127 C  CB  . HIS A  250 ? 0.18578 0.22748 0.21306 0.05094  0.00715  0.02322  250 HIS A CB  
3128 C  CG  . HIS A  250 ? 0.20655 0.24859 0.22561 0.05179  0.00691  0.02191  250 HIS A CG  
3129 N  ND1 . HIS A  250 ? 0.20711 0.25079 0.21971 0.05240  0.00852  0.02420  250 HIS A ND1 
3130 C  CD2 . HIS A  250 ? 0.21209 0.25343 0.22856 0.05207  0.00538  0.01855  250 HIS A CD2 
3131 C  CE1 . HIS A  250 ? 0.21690 0.26113 0.22320 0.05292  0.00792  0.02212  250 HIS A CE1 
3132 N  NE2 . HIS A  250 ? 0.23120 0.27392 0.23947 0.05263  0.00621  0.01858  250 HIS A NE2 
3140 N  N   . TYR A  251 ? 0.18382 0.20969 0.21320 0.04850  -0.00201 0.02328  251 TYR A N   
3141 C  CA  . TYR A  251 ? 0.17964 0.19919 0.20612 0.04736  -0.00641 0.02184  251 TYR A CA  
3142 C  C   . TYR A  251 ? 0.16872 0.18308 0.19449 0.04564  -0.00736 0.02362  251 TYR A C   
3143 O  O   . TYR A  251 ? 0.19289 0.20190 0.21657 0.04390  -0.01092 0.02247  251 TYR A O   
3144 C  CB  . TYR A  251 ? 0.19184 0.21079 0.22470 0.04663  -0.00974 0.02000  251 TYR A CB  
3145 C  CG  . TYR A  251 ? 0.19374 0.21734 0.22858 0.04830  -0.00845 0.01786  251 TYR A CG  
3146 C  CD1 . TYR A  251 ? 0.20119 0.23100 0.24157 0.04917  -0.00467 0.01803  251 TYR A CD1 
3147 C  CD2 . TYR A  251 ? 0.21322 0.23468 0.24440 0.04866  -0.01080 0.01546  251 TYR A CD2 
3148 C  CE1 . TYR A  251 ? 0.21682 0.25085 0.25888 0.05037  -0.00282 0.01566  251 TYR A CE1 
3149 C  CE2 . TYR A  251 ? 0.23841 0.26378 0.27146 0.05006  -0.00903 0.01325  251 TYR A CE2 
3150 C  CZ  . TYR A  251 ? 0.23150 0.26314 0.26996 0.05087  -0.00493 0.01328  251 TYR A CZ  
3151 O  OH  . TYR A  251 ? 0.27937 0.31495 0.31979 0.05191  -0.00256 0.01068  251 TYR A OH  
3161 N  N   . CYS A  252 ? 0.17766 0.19323 0.20488 0.04579  -0.00415 0.02632  252 CYS A N   
3162 C  CA  . CYS A  252 ? 0.18293 0.19343 0.21135 0.04378  -0.00466 0.02777  252 CYS A CA  
3163 C  C   . CYS A  252 ? 0.18771 0.19241 0.20951 0.04303  -0.00602 0.02720  252 CYS A C   
3164 O  O   . CYS A  252 ? 0.20733 0.20676 0.22973 0.04047  -0.00769 0.02695  252 CYS A O   
3165 C  CB  . CYS A  252 ? 0.20473 0.21733 0.23598 0.04416  -0.00054 0.03099  252 CYS A CB  
3166 S  SG  . CYS A  252 ? 0.22444 0.23682 0.24990 0.04607  0.00307  0.03406  252 CYS A SG  
3171 N  N   . ALA A  253 ? 0.17341 0.17923 0.18910 0.04489  -0.00506 0.02687  253 ALA A N   
3172 C  CA  . ALA A  253 ? 0.17476 0.17565 0.18453 0.04433  -0.00581 0.02614  253 ALA A CA  
3173 C  C   . ALA A  253 ? 0.18908 0.18708 0.19447 0.04306  -0.00963 0.02275  253 ALA A C   
3174 O  O   . ALA A  253 ? 0.20196 0.19623 0.20188 0.04237  -0.01030 0.02149  253 ALA A O   
3175 C  CB  . ALA A  253 ? 0.19680 0.20066 0.20289 0.04694  -0.00257 0.02807  253 ALA A CB  
3181 N  N   . ASN A  254 ? 0.18506 0.18433 0.19302 0.04254  -0.01215 0.02126  254 ASN A N   
3182 C  CA  . ASN A  254 ? 0.18553 0.18181 0.18928 0.04128  -0.01592 0.01840  254 ASN A CA  
3183 C  C   . ASN A  254 ? 0.20181 0.19180 0.20547 0.03755  -0.01947 0.01759  254 ASN A C   
3184 O  O   . ASN A  254 ? 0.22772 0.21403 0.22645 0.03577  -0.02264 0.01541  254 ASN A O   
3185 C  CB  . ASN A  254 ? 0.19023 0.19000 0.19721 0.04233  -0.01725 0.01729  254 ASN A CB  
3186 C  CG  . ASN A  254 ? 0.21897 0.22492 0.22524 0.04524  -0.01379 0.01733  254 ASN A CG  
3187 O  OD1 . ASN A  254 ? 0.26169 0.26970 0.26441 0.04655  -0.01079 0.01847  254 ASN A OD1 
3188 N  ND2 . ASN A  254 ? 0.25565 0.26435 0.26486 0.04605  -0.01439 0.01593  254 ASN A ND2 
3195 N  N   . GLY A  255 ? 0.19123 0.18003 0.19975 0.03598  -0.01893 0.01920  255 GLY A N   
3196 C  CA  . GLY A  255 ? 0.20154 0.18507 0.21010 0.03190  -0.02198 0.01847  255 GLY A CA  
3197 C  C   . GLY A  255 ? 0.22427 0.20814 0.23650 0.03026  -0.02650 0.01790  255 GLY A C   
3198 O  O   . GLY A  255 ? 0.23102 0.21934 0.24762 0.03256  -0.02678 0.01823  255 GLY A O   
3202 N  N   . SER A  256 ? 0.22390 0.20310 0.23453 0.02603  -0.03007 0.01705  256 SER A N   
3203 C  CA  . SER A  256 ? 0.22471 0.20431 0.24017 0.02381  -0.03468 0.01739  256 SER A CA  
3204 C  C   . SER A  256 ? 0.24314 0.22768 0.26805 0.02518  -0.03306 0.01937  256 SER A C   
3205 O  O   . SER A  256 ? 0.27775 0.26590 0.30876 0.02636  -0.03518 0.01986  256 SER A O   
3206 C  CB  . SER A  256 ? 0.28517 0.26533 0.29910 0.02504  -0.03815 0.01639  256 SER A CB  
3207 O  OG  . SER A  256 ? 0.36825 0.34388 0.37286 0.02362  -0.03939 0.01436  256 SER A OG  
3213 N  N   . ASN A  257 ? 0.22041 0.20500 0.24692 0.02494  -0.02916 0.02048  257 ASN A N   
3214 C  CA  . ASN A  257 ? 0.19735 0.18657 0.23218 0.02608  -0.02687 0.02226  257 ASN A CA  
3215 C  C   . ASN A  257 ? 0.21878 0.20548 0.25457 0.02344  -0.02435 0.02320  257 ASN A C   
3216 O  O   . ASN A  257 ? 0.22794 0.20926 0.25871 0.02039  -0.02469 0.02228  257 ASN A O   
3217 C  CB  . ASN A  257 ? 0.19121 0.18541 0.22724 0.03074  -0.02292 0.02291  257 ASN A CB  
3218 C  CG  . ASN A  257 ? 0.18937 0.18225 0.21971 0.03238  -0.01874 0.02345  257 ASN A CG  
3219 O  OD1 . ASN A  257 ? 0.20756 0.19608 0.23513 0.03043  -0.01758 0.02374  257 ASN A OD1 
3220 N  ND2 . ASN A  257 ? 0.19736 0.19435 0.22634 0.03599  -0.01622 0.02365  257 ASN A ND2 
3227 N  N   . ARG A  258 ? 0.20665 0.19714 0.24902 0.02438  -0.02146 0.02484  258 ARG A N   
3228 C  CA  . ARG A  258 ? 0.22122 0.20952 0.26552 0.02179  -0.01877 0.02585  258 ARG A CA  
3229 C  C   . ARG A  258 ? 0.21279 0.19679 0.25162 0.02234  -0.01476 0.02628  258 ARG A C   
3230 O  O   . ARG A  258 ? 0.24985 0.23041 0.28940 0.01971  -0.01254 0.02676  258 ARG A O   
3231 C  CB  . ARG A  258 ? 0.21269 0.20642 0.26489 0.02310  -0.01611 0.02751  258 ARG A CB  
3232 C  CG  . ARG A  258 ? 0.21799 0.21596 0.27031 0.02763  -0.01230 0.02865  258 ARG A CG  
3233 C  CD  . ARG A  258 ? 0.22332 0.22646 0.28310 0.02820  -0.00942 0.03005  258 ARG A CD  
3234 N  NE  . ARG A  258 ? 0.25473 0.25483 0.31458 0.02632  -0.00590 0.03164  258 ARG A NE  
3235 C  CZ  . ARG A  258 ? 0.28664 0.28965 0.35145 0.02616  -0.00252 0.03316  258 ARG A CZ  
3236 N  NH1 . ARG A  258 ? 0.29840 0.30793 0.36906 0.02754  -0.00205 0.03308  258 ARG A NH1 
3237 N  NH2 . ARG A  258 ? 0.33973 0.33884 0.40368 0.02447  0.00076  0.03466  258 ARG A NH2 
3251 N  N   . TYR A  259 ? 0.19824 0.18248 0.23210 0.02568  -0.01354 0.02616  259 TYR A N   
3252 C  CA  . TYR A  259 ? 0.20496 0.18599 0.23453 0.02690  -0.00973 0.02695  259 TYR A CA  
3253 C  C   . TYR A  259 ? 0.20419 0.17977 0.22695 0.02513  -0.01137 0.02465  259 TYR A C   
3254 O  O   . TYR A  259 ? 0.21730 0.19049 0.23660 0.02654  -0.00849 0.02499  259 TYR A O   
3255 C  CB  . TYR A  259 ? 0.21022 0.19593 0.23894 0.03168  -0.00681 0.02868  259 TYR A CB  
3256 C  CG  . TYR A  259 ? 0.19720 0.18889 0.23210 0.03325  -0.00505 0.03052  259 TYR A CG  
3257 C  CD1 . TYR A  259 ? 0.21701 0.20853 0.25618 0.03235  -0.00188 0.03266  259 TYR A CD1 
3258 C  CD2 . TYR A  259 ? 0.19471 0.19193 0.23117 0.03529  -0.00641 0.02978  259 TYR A CD2 
3259 C  CE1 . TYR A  259 ? 0.21977 0.21691 0.26458 0.03329  -0.00023 0.03400  259 TYR A CE1 
3260 C  CE2 . TYR A  259 ? 0.20509 0.20791 0.24757 0.03632  -0.00458 0.03091  259 TYR A CE2 
3261 C  CZ  . TYR A  259 ? 0.18809 0.19097 0.23438 0.03532  -0.00152 0.03301  259 TYR A CZ  
3262 O  OH  . TYR A  259 ? 0.20057 0.20923 0.25273 0.03600  0.00040  0.03381  259 TYR A OH  
3272 N  N   . ASP A  260 ? 0.20603 0.17972 0.22702 0.02191  -0.01595 0.02242  260 ASP A N   
3273 C  CA  . ASP A  260 ? 0.20568 0.17441 0.21961 0.01979  -0.01762 0.01990  260 ASP A CA  
3274 C  C   . ASP A  260 ? 0.21166 0.17491 0.22354 0.01779  -0.01422 0.01937  260 ASP A C   
3275 O  O   . ASP A  260 ? 0.21069 0.17127 0.21735 0.01848  -0.01314 0.01797  260 ASP A O   
3276 C  CB  . ASP A  260 ? 0.21761 0.18469 0.23041 0.01551  -0.02299 0.01809  260 ASP A CB  
3277 C  CG  . ASP A  260 ? 0.23566 0.20649 0.24856 0.01762  -0.02671 0.01794  260 ASP A CG  
3278 O  OD1 . ASP A  260 ? 0.26531 0.24010 0.27879 0.02214  -0.02496 0.01873  260 ASP A OD1 
3279 O  OD2 . ASP A  260 ? 0.33801 0.30766 0.35041 0.01435  -0.03148 0.01704  260 ASP A OD2 
3284 N  N   . ALA A  261 ? 0.21196 0.17318 0.22794 0.01496  -0.01242 0.02010  261 ALA A N   
3285 C  CA  . ALA A  261 ? 0.21053 0.16582 0.22504 0.01273  -0.00881 0.01926  261 ALA A CA  
3286 C  C   . ALA A  261 ? 0.22362 0.17911 0.23790 0.01754  -0.00424 0.02116  261 ALA A C   
3287 O  O   . ALA A  261 ? 0.22669 0.17828 0.23744 0.01752  -0.00245 0.01974  261 ALA A O   
3288 C  CB  . ALA A  261 ? 0.24497 0.19828 0.26413 0.00874  -0.00742 0.01969  261 ALA A CB  
3294 N  N   . LEU A  262 ? 0.21712 0.17752 0.23527 0.02160  -0.00238 0.02441  262 LEU A N   
3295 C  CA  . LEU A  262 ? 0.23642 0.19791 0.25456 0.02613  0.00159  0.02699  262 LEU A CA  
3296 C  C   . LEU A  262 ? 0.19967 0.16346 0.21264 0.02920  0.00034  0.02607  262 LEU A C   
3297 O  O   . LEU A  262 ? 0.21023 0.17217 0.22106 0.03103  0.00269  0.02631  262 LEU A O   
3298 C  CB  . LEU A  262 ? 0.30396 0.27068 0.32708 0.02878  0.00341  0.03059  262 LEU A CB  
3299 C  CG  . LEU A  262 ? 0.34899 0.31925 0.37268 0.03349  0.00677  0.03423  262 LEU A CG  
3300 C  CD1 . LEU A  262 ? 0.37466 0.34789 0.40391 0.03341  0.00857  0.03692  262 LEU A CD1 
3301 C  CD2 . LEU A  262 ? 0.25369 0.22961 0.27390 0.03684  0.00508  0.03408  262 LEU A CD2 
3313 N  N   . LEU A  263 ? 0.20307 0.17102 0.21432 0.02982  -0.00325 0.02498  263 LEU A N   
3314 C  CA  . LEU A  263 ? 0.19332 0.16392 0.19955 0.03259  -0.00426 0.02401  263 LEU A CA  
3315 C  C   . LEU A  263 ? 0.18814 0.15362 0.18905 0.03044  -0.00507 0.02084  263 LEU A C   
3316 O  O   . LEU A  263 ? 0.19165 0.15738 0.18952 0.03279  -0.00336 0.02071  263 LEU A O   
3317 C  CB  . LEU A  263 ? 0.18602 0.16094 0.19160 0.03303  -0.00788 0.02296  263 LEU A CB  
3318 C  CG  . LEU A  263 ? 0.19541 0.17664 0.20585 0.03560  -0.00693 0.02542  263 LEU A CG  
3319 C  CD1 . LEU A  263 ? 0.20959 0.19342 0.22063 0.03503  -0.01078 0.02370  263 LEU A CD1 
3320 C  CD2 . LEU A  263 ? 0.21812 0.20411 0.22718 0.03985  -0.00380 0.02762  263 LEU A CD2 
3332 N  N   . GLY A  264 ? 0.19636 0.15750 0.19597 0.02564  -0.00783 0.01812  264 GLY A N   
3333 C  CA  . GLY A  264 ? 0.19793 0.15419 0.19215 0.02289  -0.00850 0.01472  264 GLY A CA  
3334 C  C   . GLY A  264 ? 0.21173 0.16351 0.20701 0.02249  -0.00419 0.01464  264 GLY A C   
3335 O  O   . GLY A  264 ? 0.21573 0.16549 0.20723 0.02275  -0.00317 0.01259  264 GLY A O   
3339 N  N   . LYS A  265 ? 0.20960 0.15967 0.21027 0.02181  -0.00142 0.01671  265 LYS A N   
3340 C  CA  . LYS A  265 ? 0.22537 0.17067 0.22784 0.02165  0.00312  0.01678  265 LYS A CA  
3341 C  C   . LYS A  265 ? 0.20233 0.15045 0.20486 0.02727  0.00580  0.01903  265 LYS A C   
3342 O  O   . LYS A  265 ? 0.21259 0.15799 0.21320 0.02754  0.00748  0.01721  265 LYS A O   
3343 C  CB  . LYS A  265 ? 0.23125 0.17451 0.23964 0.02032  0.00587  0.01903  265 LYS A CB  
3344 C  CG  . LYS A  265 ? 0.24849 0.18743 0.26015 0.02165  0.01129  0.02039  265 LYS A CG  
3345 C  CD  . LYS A  265 ? 0.27909 0.21447 0.29581 0.01881  0.01400  0.02159  265 LYS A CD  
3346 C  CE  . LYS A  265 ? 0.30935 0.24985 0.32963 0.02111  0.01362  0.02544  265 LYS A CE  
3347 N  NZ  . LYS A  265 ? 0.37506 0.31203 0.40015 0.01814  0.01656  0.02651  265 LYS A NZ  
3361 N  N   . TYR A  266 ? 0.19907 0.15309 0.20390 0.03161  0.00623  0.02297  266 TYR A N   
3362 C  CA  . TYR A  266 ? 0.21440 0.17171 0.21948 0.03668  0.00871  0.02573  266 TYR A CA  
3363 C  C   . TYR A  266 ? 0.20479 0.16538 0.20414 0.03816  0.00645  0.02346  266 TYR A C   
3364 O  O   . TYR A  266 ? 0.21224 0.17337 0.21078 0.04070  0.00830  0.02380  266 TYR A O   
3365 C  CB  . TYR A  266 ? 0.23460 0.19739 0.24326 0.04012  0.00994  0.03058  266 TYR A CB  
3366 C  CG  . TYR A  266 ? 0.22433 0.18384 0.23866 0.03916  0.01299  0.03330  266 TYR A CG  
3367 C  CD1 . TYR A  266 ? 0.24713 0.20092 0.26420 0.03900  0.01665  0.03405  266 TYR A CD1 
3368 C  CD2 . TYR A  266 ? 0.22994 0.19220 0.24713 0.03850  0.01247  0.03506  266 TYR A CD2 
3369 C  CE1 . TYR A  266 ? 0.26915 0.21970 0.29129 0.03816  0.01977  0.03669  266 TYR A CE1 
3370 C  CE2 . TYR A  266 ? 0.26888 0.22846 0.29099 0.03756  0.01545  0.03760  266 TYR A CE2 
3371 C  CZ  . TYR A  266 ? 0.26383 0.21726 0.28809 0.03723  0.01904  0.03833  266 TYR A CZ  
3372 O  OH  . TYR A  266 ? 0.31591 0.26625 0.34494 0.03621  0.02231  0.04093  266 TYR A OH  
3382 N  N   . GLY A  267 ? 0.19214 0.15507 0.18780 0.03669  0.00255  0.02126  267 GLY A N   
3383 C  CA  . GLY A  267 ? 0.21364 0.17953 0.20352 0.03785  0.00054  0.01899  267 GLY A CA  
3384 C  C   . GLY A  267 ? 0.19367 0.15438 0.17959 0.03503  0.00033  0.01479  267 GLY A C   
3385 O  O   . GLY A  267 ? 0.19371 0.15598 0.17686 0.03700  0.00121  0.01383  267 GLY A O   
3389 N  N   . VAL A  268 ? 0.18639 0.14111 0.17191 0.02998  -0.00079 0.01205  268 VAL A N   
3390 C  CA  . VAL A  268 ? 0.20334 0.15279 0.18515 0.02654  -0.00049 0.00774  268 VAL A CA  
3391 C  C   . VAL A  268 ? 0.20927 0.15678 0.19469 0.02875  0.00426  0.00863  268 VAL A C   
3392 O  O   . VAL A  268 ? 0.21288 0.15969 0.19574 0.02910  0.00528  0.00615  268 VAL A O   
3393 C  CB  . VAL A  268 ? 0.19132 0.13500 0.17190 0.02001  -0.00249 0.00479  268 VAL A CB  
3394 C  CG1 . VAL A  268 ? 0.23389 0.17170 0.21131 0.01591  -0.00107 0.00029  268 VAL A CG1 
3395 C  CG2 . VAL A  268 ? 0.21735 0.16307 0.19388 0.01812  -0.00773 0.00380  268 VAL A CG2 
3405 N  N   . ALA A  269 ? 0.20504 0.15130 0.19680 0.03006  0.00735  0.01204  269 ALA A N   
3406 C  CA  . ALA A  269 ? 0.22087 0.16487 0.21690 0.03242  0.01191  0.01333  269 ALA A CA  
3407 C  C   . ALA A  269 ? 0.22107 0.17104 0.21653 0.03795  0.01253  0.01546  269 ALA A C   
3408 O  O   . ALA A  269 ? 0.21324 0.16190 0.20955 0.03919  0.01485  0.01428  269 ALA A O   
3409 C  CB  . ALA A  269 ? 0.22328 0.16518 0.22605 0.03318  0.01499  0.01727  269 ALA A CB  
3415 N  N   . TRP A  270 ? 0.20269 0.15959 0.19694 0.04111  0.01057  0.01848  270 TRP A N   
3416 C  CA  . TRP A  270 ? 0.19196 0.15550 0.18519 0.04593  0.01097  0.02063  270 TRP A CA  
3417 C  C   . TRP A  270 ? 0.20320 0.16702 0.19077 0.04482  0.00955  0.01593  270 TRP A C   
3418 O  O   . TRP A  270 ? 0.21481 0.18064 0.20310 0.04753  0.01134  0.01616  270 TRP A O   
3419 C  CB  . TRP A  270 ? 0.19484 0.16571 0.18681 0.04833  0.00905  0.02372  270 TRP A CB  
3420 C  CG  . TRP A  270 ? 0.19254 0.17075 0.18467 0.05324  0.01018  0.02729  270 TRP A CG  
3421 C  CD1 . TRP A  270 ? 0.19865 0.18307 0.18584 0.05477  0.00854  0.02621  270 TRP A CD1 
3422 C  CD2 . TRP A  270 ? 0.21521 0.19535 0.21270 0.05695  0.01319  0.03275  270 TRP A CD2 
3423 N  NE1 . TRP A  270 ? 0.20121 0.19190 0.19032 0.05909  0.01026  0.03063  270 TRP A NE1 
3424 C  CE2 . TRP A  270 ? 0.20962 0.19769 0.20514 0.06059  0.01299  0.03494  270 TRP A CE2 
3425 C  CE3 . TRP A  270 ? 0.23302 0.20878 0.23671 0.05735  0.01605  0.03607  270 TRP A CE3 
3426 C  CZ2 . TRP A  270 ? 0.22031 0.21233 0.21991 0.06455  0.01517  0.04071  270 TRP A CZ2 
3427 C  CZ3 . TRP A  270 ? 0.23367 0.21275 0.24146 0.06150  0.01840  0.04179  270 TRP A CZ3 
3428 C  CH2 . TRP A  270 ? 0.23595 0.22317 0.24172 0.06509  0.01779  0.04418  270 TRP A CH2 
3439 N  N   . MET A  271 ? 0.19479 0.15710 0.17673 0.04093  0.00617  0.01184  271 MET A N   
3440 C  CA  . MET A  271 ? 0.20575 0.16816 0.18149 0.03939  0.00467  0.00724  271 MET A CA  
3441 C  C   . MET A  271 ? 0.21103 0.16726 0.18746 0.03665  0.00695  0.00357  271 MET A C   
3442 O  O   . MET A  271 ? 0.21158 0.16912 0.18594 0.03749  0.00781  0.00120  271 MET A O   
3443 C  CB  . MET A  271 ? 0.20116 0.16309 0.17075 0.03583  0.00035  0.00429  271 MET A CB  
3444 C  CG  . MET A  271 ? 0.20461 0.17302 0.17378 0.03870  -0.00148 0.00730  271 MET A CG  
3445 S  SD  . MET A  271 ? 0.21816 0.19549 0.18678 0.04444  0.00025  0.00992  271 MET A SD  
3446 C  CE  . MET A  271 ? 0.22771 0.21051 0.19124 0.04472  -0.00294 0.00929  271 MET A CE  
3456 N  N   . LYS A  272 ? 0.20879 0.15843 0.18821 0.03310  0.00819  0.00272  272 LYS A N   
3457 C  CA  . LYS A  272 ? 0.22318 0.16674 0.20408 0.03032  0.01121  -0.00091 272 LYS A CA  
3458 C  C   . LYS A  272 ? 0.23121 0.17660 0.21818 0.03539  0.01535  0.00162  272 LYS A C   
3459 O  O   . LYS A  272 ? 0.22398 0.16847 0.21065 0.03526  0.01710  -0.00160 272 LYS A O   
3460 C  CB  . LYS A  272 ? 0.21981 0.15655 0.20368 0.02584  0.01241  -0.00159 272 LYS A CB  
3461 C  CG  . LYS A  272 ? 0.22746 0.16109 0.20565 0.01954  0.00862  -0.00504 272 LYS A CG  
3462 C  CD  . LYS A  272 ? 0.23650 0.16592 0.20911 0.01431  0.00832  -0.01126 272 LYS A CD  
3463 C  CE  . LYS A  272 ? 0.25552 0.18102 0.22318 0.00721  0.00474  -0.01409 272 LYS A CE  
3464 N  NZ  . LYS A  272 ? 0.25624 0.17733 0.21797 0.00127  0.00456  -0.02015 272 LYS A NZ  
3478 N  N   . LEU A  273 ? 0.23111 0.17888 0.22406 0.03969  0.01704  0.00748  273 LEU A N   
3479 C  CA  . LEU A  273 ? 0.21672 0.16597 0.21623 0.04461  0.02078  0.01085  273 LEU A CA  
3480 C  C   . LEU A  273 ? 0.23714 0.19376 0.23433 0.04851  0.01983  0.01119  273 LEU A C   
3481 O  O   . LEU A  273 ? 0.25502 0.21173 0.25565 0.05057  0.02238  0.01053  273 LEU A O   
3482 C  CB  . LEU A  273 ? 0.23692 0.18755 0.24227 0.04807  0.02222  0.01754  273 LEU A CB  
3483 C  CG  . LEU A  273 ? 0.24252 0.19398 0.25533 0.05313  0.02602  0.02189  273 LEU A CG  
3484 C  CD1 . LEU A  273 ? 0.27804 0.22181 0.29577 0.05138  0.03003  0.01886  273 LEU A CD1 
3485 C  CD2 . LEU A  273 ? 0.28514 0.23800 0.30238 0.05588  0.02694  0.02866  273 LEU A CD2 
3497 N  N   . HIS A  274 ? 0.21794 0.18097 0.20956 0.04944  0.01633  0.01200  274 HIS A N   
3498 C  CA  . HIS A  274 ? 0.23133 0.20229 0.22104 0.05331  0.01570  0.01302  274 HIS A CA  
3499 C  C   . HIS A  274 ? 0.25034 0.22202 0.23275 0.05052  0.01367  0.00703  274 HIS A C   
3500 O  O   . HIS A  274 ? 0.30402 0.27914 0.28657 0.05249  0.01467  0.00586  274 HIS A O   
3501 C  CB  . HIS A  274 ? 0.23258 0.21102 0.22132 0.05650  0.01398  0.01806  274 HIS A CB  
3502 C  CG  . HIS A  274 ? 0.20634 0.18488 0.20213 0.05955  0.01623  0.02436  274 HIS A CG  
3503 N  ND1 . HIS A  274 ? 0.26252 0.24235 0.26476 0.06361  0.01912  0.02836  274 HIS A ND1 
3504 C  CD2 . HIS A  274 ? 0.21193 0.18883 0.20955 0.05883  0.01610  0.02723  274 HIS A CD2 
3505 C  CE1 . HIS A  274 ? 0.23398 0.21275 0.24119 0.06519  0.02061  0.03368  274 HIS A CE1 
3506 N  NE2 . HIS A  274 ? 0.27095 0.24811 0.27535 0.06227  0.01891  0.03291  274 HIS A NE2 
3514 N  N   . LEU A  275 ? 0.22209 0.19044 0.19831 0.04580  0.01088  0.00311  275 LEU A N   
3515 C  CA  . LEU A  275 ? 0.21477 0.18303 0.18360 0.04271  0.00902  -0.00264 275 LEU A CA  
3516 C  C   . LEU A  275 ? 0.23394 0.19519 0.20294 0.03862  0.01093  -0.00788 275 LEU A C   
3517 O  O   . LEU A  275 ? 0.24234 0.20476 0.20784 0.03770  0.01111  -0.01195 275 LEU A O   
3518 C  CB  . LEU A  275 ? 0.21213 0.17967 0.17403 0.03929  0.00495  -0.00442 275 LEU A CB  
3519 C  CG  . LEU A  275 ? 0.21593 0.19036 0.17657 0.04248  0.00302  -0.00060 275 LEU A CG  
3520 C  CD1 . LEU A  275 ? 0.23269 0.20508 0.18740 0.03879  -0.00076 -0.00298 275 LEU A CD1 
3521 C  CD2 . LEU A  275 ? 0.22857 0.21126 0.18746 0.04639  0.00354  0.00028  275 LEU A CD2 
3533 N  N   . ASP A  276 ? 0.20708 0.18969 0.19534 0.06447  -0.00424 0.00320  276 ASP A N   
3534 C  CA  . ASP A  276 ? 0.22571 0.19404 0.21248 0.06132  0.00028  -0.00307 276 ASP A CA  
3535 C  C   . ASP A  276 ? 0.24225 0.19882 0.23145 0.06949  0.01015  0.00305  276 ASP A C   
3536 O  O   . ASP A  276 ? 0.25981 0.20538 0.24811 0.06830  0.01426  -0.00120 276 ASP A O   
3537 C  CB  . ASP A  276 ? 0.22191 0.17633 0.20722 0.04910  0.00040  -0.01057 276 ASP A CB  
3538 C  CG  . ASP A  276 ? 0.23976 0.20237 0.22177 0.03987  -0.00881 -0.01850 276 ASP A CG  
3539 O  OD1 . ASP A  276 ? 0.24226 0.22032 0.22260 0.04215  -0.01529 -0.01945 276 ASP A OD1 
3540 O  OD2 . ASP A  276 ? 0.25183 0.20452 0.23293 0.03068  -0.00893 -0.02369 276 ASP A OD2 
3545 N  N   . GLN A  277 ? 0.24001 0.19844 0.23197 0.07728  0.01380  0.01251  277 GLN A N   
3546 C  CA  . GLN A  277 ? 0.26363 0.20942 0.25753 0.08501  0.02361  0.01864  277 GLN A CA  
3547 C  C   . GLN A  277 ? 0.26930 0.19355 0.26298 0.07699  0.02969  0.01406  277 GLN A C   
3548 O  O   . GLN A  277 ? 0.30575 0.21835 0.29967 0.08050  0.03651  0.01440  277 GLN A O   
3549 C  CB  . GLN A  277 ? 0.28820 0.24048 0.28190 0.09487  0.02499  0.02026  277 GLN A CB  
3550 C  CG  . GLN A  277 ? 0.39812 0.37263 0.39174 0.10050  0.01764  0.02254  277 GLN A CG  
3551 C  CD  . GLN A  277 ? 0.58447 0.56524 0.58062 0.11166  0.02062  0.03326  277 GLN A CD  
3552 O  OE1 . GLN A  277 ? 0.53142 0.51172 0.52835 0.12127  0.02534  0.03741  277 GLN A OE1 
3553 N  NE2 . GLN A  277 ? 0.46394 0.45124 0.46125 0.11062  0.01764  0.03765  277 GLN A NE2 
3562 N  N   . ASP A  278 ? 0.26245 0.18203 0.25578 0.06669  0.02723  0.00999  278 ASP A N   
3563 C  CA  . ASP A  278 ? 0.28145 0.18174 0.27452 0.05786  0.03206  0.00440  278 ASP A CA  
3564 C  C   . ASP A  278 ? 0.27485 0.16304 0.27054 0.05935  0.03958  0.01125  278 ASP A C   
3565 O  O   . ASP A  278 ? 0.28740 0.17727 0.28402 0.05483  0.03755  0.01270  278 ASP A O   
3566 C  CB  . ASP A  278 ? 0.27113 0.17376 0.26216 0.04589  0.02490  -0.00439 278 ASP A CB  
3567 C  CG  . ASP A  278 ? 0.27972 0.16357 0.27025 0.03641  0.02914  -0.01141 278 ASP A CG  
3568 O  OD1 . ASP A  278 ? 0.30490 0.17316 0.29708 0.03830  0.03789  -0.00885 278 ASP A OD1 
3569 O  OD2 . ASP A  278 ? 0.28520 0.17037 0.27347 0.02689  0.02334  -0.01979 278 ASP A OD2 
3574 N  N   . GLN A  279 ? 0.29745 0.17334 0.29419 0.06569  0.04835  0.01541  279 GLN A N   
3575 C  CA  . GLN A  279 ? 0.34598 0.21059 0.34492 0.06898  0.05623  0.02306  279 GLN A CA  
3576 C  C   . GLN A  279 ? 0.32088 0.17012 0.32044 0.05820  0.05936  0.01893  279 GLN A C   
3577 O  O   . GLN A  279 ? 0.34236 0.18449 0.34369 0.05903  0.06434  0.02478  279 GLN A O   
3578 C  CB  . GLN A  279 ? 0.38410 0.23929 0.38349 0.07872  0.06470  0.02812  279 GLN A CB  
3579 C  CG  . GLN A  279 ? 0.47136 0.34219 0.47069 0.09090  0.06248  0.03417  279 GLN A CG  
3580 C  CD  . GLN A  279 ? 0.78819 0.66626 0.78913 0.09840  0.06336  0.04442  279 GLN A CD  
3581 O  OE1 . GLN A  279 ? 0.82815 0.69805 0.83025 0.09503  0.06662  0.04757  279 GLN A OE1 
3582 N  NE2 . GLN A  279 ? 0.99632 0.88986 0.99736 0.10864  0.06054  0.04955  279 GLN A NE2 
3591 N  N   . ARG A  280 ? 0.30946 0.15428 0.30753 0.04809  0.05624  0.00895  280 ARG A N   
3592 C  CA  . ARG A  280 ? 0.32448 0.15626 0.32319 0.03743  0.05841  0.00430  280 ARG A CA  
3593 C  C   . ARG A  280 ? 0.31652 0.15610 0.31637 0.03408  0.05445  0.00712  280 ARG A C   
3594 O  O   . ARG A  280 ? 0.33385 0.16238 0.33500 0.02728  0.05790  0.00597  280 ARG A O   
3595 C  CB  . ARG A  280 ? 0.31118 0.14040 0.30772 0.02730  0.05394  -0.00719 280 ARG A CB  
3596 C  CG  . ARG A  280 ? 0.32980 0.15027 0.32515 0.02902  0.05772  -0.01120 280 ARG A CG  
3597 C  CD  . ARG A  280 ? 0.34144 0.16061 0.33433 0.01913  0.05271  -0.02249 280 ARG A CD  
3598 N  NE  . ARG A  280 ? 0.32063 0.15826 0.31119 0.01805  0.04248  -0.02562 280 ARG A NE  
3599 C  CZ  . ARG A  280 ? 0.30221 0.14225 0.29004 0.00935  0.03623  -0.03503 280 ARG A CZ  
3600 N  NH1 . ARG A  280 ? 0.34322 0.16875 0.33040 0.00085  0.03892  -0.04261 280 ARG A NH1 
3601 N  NH2 . ARG A  280 ? 0.30215 0.15912 0.28768 0.00931  0.02728  -0.03702 280 ARG A NH2 
3615 N  N   . TYR A  281 ? 0.28268 0.14139 0.28207 0.03813  0.04696  0.01012  281 TYR A N   
3616 C  CA  . TYR A  281 ? 0.28470 0.15229 0.28508 0.03498  0.04242  0.01253  281 TYR A CA  
3617 C  C   . TYR A  281 ? 0.28294 0.15123 0.28565 0.04339  0.04733  0.02365  281 TYR A C   
3618 O  O   . TYR A  281 ? 0.29366 0.16603 0.29760 0.04051  0.04537  0.02621  281 TYR A O   
3619 C  CB  . TYR A  281 ? 0.25517 0.14280 0.25365 0.03379  0.03132  0.00916  281 TYR A CB  
3620 C  CG  . TYR A  281 ? 0.24930 0.13491 0.24529 0.02297  0.02615  -0.00217 281 TYR A CG  
3621 C  CD1 . TYR A  281 ? 0.26157 0.14338 0.25547 0.02246  0.02630  -0.00809 281 TYR A CD1 
3622 C  CD2 . TYR A  281 ? 0.25004 0.13590 0.24578 0.01313  0.02191  -0.00703 281 TYR A CD2 
3623 C  CE1 . TYR A  281 ? 0.26329 0.14193 0.25465 0.01235  0.02201  -0.01862 281 TYR A CE1 
3624 C  CE2 . TYR A  281 ? 0.26483 0.14773 0.25811 0.00324  0.01760  -0.01743 281 TYR A CE2 
3625 C  CZ  . TYR A  281 ? 0.27504 0.15426 0.26607 0.00296  0.01769  -0.02306 281 TYR A CZ  
3626 O  OH  . TYR A  281 ? 0.29236 0.16871 0.28066 -0.00704 0.01319  -0.03341 281 TYR A OH  
3636 N  N   . ALA A  282 ? 0.29763 0.16172 0.30085 0.05364  0.05375  0.03025  282 ALA A N   
3637 C  CA  . ALA A  282 ? 0.32286 0.18733 0.32786 0.06212  0.05855  0.04101  282 ALA A CA  
3638 C  C   . ALA A  282 ? 0.31232 0.16251 0.31897 0.05686  0.06475  0.04302  282 ALA A C   
3639 O  O   . ALA A  282 ? 0.32942 0.18547 0.33737 0.05942  0.06439  0.04962  282 ALA A O   
3640 C  CB  . ALA A  282 ? 0.35164 0.21182 0.35652 0.07376  0.06508  0.04708  282 ALA A CB  
3646 N  N   . PRO A  283 ? 0.32938 0.16149 0.33615 0.04943  0.07034  0.03765  283 PRO A N   
3647 C  CA  . PRO A  283 ? 0.33689 0.15531 0.34541 0.04477  0.07684  0.03998  283 PRO A CA  
3648 C  C   . PRO A  283 ? 0.34062 0.16682 0.35006 0.03668  0.07098  0.03784  283 PRO A C   
3649 O  O   . PRO A  283 ? 0.36774 0.18610 0.37883 0.03449  0.07581  0.04156  283 PRO A O   
3650 C  CB  . PRO A  283 ? 0.36981 0.16893 0.37811 0.03790  0.08284  0.03296  283 PRO A CB  
3651 C  CG  . PRO A  283 ? 0.37451 0.17411 0.38119 0.04415  0.08326  0.03154  283 PRO A CG  
3652 C  CD  . PRO A  283 ? 0.33105 0.15287 0.33652 0.04692  0.07275  0.03068  283 PRO A CD  
3660 N  N   . PHE A  284 ? 0.31265 0.15364 0.32094 0.03199  0.06088  0.03184  284 PHE A N   
3661 C  CA  . PHE A  284 ? 0.32619 0.17609 0.33516 0.02500  0.05465  0.02996  284 PHE A CA  
3662 C  C   . PHE A  284 ? 0.31713 0.18212 0.32703 0.03261  0.05156  0.03891  284 PHE A C   
3663 O  O   . PHE A  284 ? 0.34011 0.21013 0.35112 0.02809  0.04860  0.03957  284 PHE A O   
3664 C  CB  . PHE A  284 ? 0.29683 0.15567 0.30378 0.01671  0.04514  0.01963  284 PHE A CB  
3665 C  CG  . PHE A  284 ? 0.32678 0.17073 0.33289 0.00876  0.04813  0.01079  284 PHE A CG  
3666 C  CD1 . PHE A  284 ? 0.35749 0.19024 0.36464 -0.00137 0.05044  0.00568  284 PHE A CD1 
3667 C  CD2 . PHE A  284 ? 0.33206 0.17261 0.33646 0.01154  0.04915  0.00755  284 PHE A CD2 
3668 C  CE1 . PHE A  284 ? 0.40868 0.22689 0.41523 -0.00851 0.05379  -0.00244 284 PHE A CE1 
3669 C  CE2 . PHE A  284 ? 0.39750 0.22365 0.40124 0.00454  0.05246  -0.00026 284 PHE A CE2 
3670 C  CZ  . PHE A  284 ? 0.41352 0.22838 0.41834 -0.00548 0.05480  -0.00530 284 PHE A CZ  
3680 N  N   . LEU A  285 ? 0.30075 0.17295 0.31028 0.04399  0.05228  0.04564  285 LEU A N   
3681 C  CA  . LEU A  285 ? 0.30917 0.19658 0.31948 0.05248  0.04932  0.05439  285 LEU A CA  
3682 C  C   . LEU A  285 ? 0.33234 0.21101 0.34391 0.06134  0.05853  0.06467  285 LEU A C   
3683 O  O   . LEU A  285 ? 0.34707 0.23177 0.35989 0.06427  0.05834  0.07142  285 LEU A O   
3684 C  CB  . LEU A  285 ? 0.28646 0.19039 0.29536 0.05972  0.04289  0.05465  285 LEU A CB  
3685 C  CG  . LEU A  285 ? 0.27777 0.19404 0.28508 0.05204  0.03247  0.04576  285 LEU A CG  
3686 C  CD1 . LEU A  285 ? 0.28946 0.21615 0.29496 0.05770  0.02826  0.04381  285 LEU A CD1 
3687 C  CD2 . LEU A  285 ? 0.28700 0.21821 0.29510 0.05008  0.02538  0.04784  285 LEU A CD2 
3699 N  N   . CYS A  286 ? 0.33157 0.19643 0.34262 0.06605  0.06650  0.06615  286 CYS A N   
3700 C  CA  . CYS A  286 ? 0.34923 0.20484 0.36082 0.07537  0.07563  0.07587  286 CYS A CA  
3701 C  C   . CYS A  286 ? 0.40432 0.23678 0.41627 0.06971  0.08507  0.07383  286 CYS A C   
3702 O  O   . CYS A  286 ? 0.42108 0.24306 0.43220 0.06652  0.08761  0.06770  286 CYS A O   
3703 C  CB  . CYS A  286 ? 0.42709 0.28727 0.43753 0.08700  0.07680  0.07973  286 CYS A CB  
3704 S  SG  . CYS A  286 ? 0.44877 0.33638 0.45901 0.09479  0.06646  0.08286  286 CYS A SG  
3709 N  N   . GLY A  287 ? 0.42352 0.24834 0.43672 0.06820  0.09012  0.07871  287 GLY A N   
3710 C  CA  . GLY A  287 ? 0.44136 0.24427 0.45507 0.06296  0.09957  0.07755  287 GLY A CA  
3711 C  C   . GLY A  287 ? 0.47407 0.27406 0.48943 0.05307  0.09924  0.07551  287 GLY A C   
3712 O  O   . GLY A  287 ? 0.46915 0.25784 0.48531 0.05352  0.10677  0.08088  287 GLY A O   
3716 N  N   . PRO A  288 ? 0.42190 0.23197 0.43763 0.04392  0.09052  0.06757  288 PRO A N   
3717 C  CA  . PRO A  288 ? 0.38883 0.19644 0.40619 0.03385  0.08982  0.06462  288 PRO A CA  
3718 C  C   . PRO A  288 ? 0.43438 0.25039 0.45285 0.03819  0.08951  0.07337  288 PRO A C   
3719 O  O   . PRO A  288 ? 0.39719 0.22817 0.41521 0.04705  0.08528  0.07964  288 PRO A O   
3720 C  CB  . PRO A  288 ? 0.39991 0.21996 0.41681 0.02524  0.07908  0.05472  288 PRO A CB  
3721 C  CG  . PRO A  288 ? 0.45118 0.27098 0.46621 0.02782  0.07759  0.05023  288 PRO A CG  
3722 C  CD  . PRO A  288 ? 0.42504 0.24649 0.43949 0.04133  0.08176  0.05978  288 PRO A CD  
3730 N  N   . ASN A  289 ? 0.43715 0.24389 0.45717 0.03144  0.09380  0.07340  289 ASN A N   
3731 C  CA  . ASN A  289 ? 0.41414 0.22824 0.43535 0.03373  0.09339  0.08071  289 ASN A CA  
3732 C  C   . ASN A  289 ? 0.42483 0.25535 0.44683 0.02605  0.08257  0.07483  289 ASN A C   
3733 O  O   . ASN A  289 ? 0.42402 0.25109 0.44742 0.01635  0.08222  0.07036  289 ASN A O   
3734 C  CB  . ASN A  289 ? 0.46485 0.26066 0.48721 0.03051  0.10374  0.08378  289 ASN A CB  
3735 C  CG  . ASN A  289 ? 0.67085 0.47289 0.69412 0.03450  0.10464  0.09265  289 ASN A CG  
3736 O  OD1 . ASN A  289 ? 0.58318 0.40248 0.60618 0.04143  0.09843  0.09774  289 ASN A OD1 
3737 N  ND2 . ASN A  289 ? 0.73998 0.52777 0.76433 0.03021  0.11264  0.09458  289 ASN A ND2 
3744 N  N   . HIS A  290 ? 0.39724 0.24622 0.41823 0.03081  0.07359  0.07494  290 HIS A N   
3745 C  CA  . HIS A  290 ? 0.39511 0.25991 0.41619 0.02382  0.06258  0.06834  290 HIS A CA  
3746 C  C   . HIS A  290 ? 0.33643 0.20637 0.35935 0.01941  0.06091  0.07056  290 HIS A C   
3747 O  O   . HIS A  290 ? 0.35077 0.22519 0.37418 0.00952  0.05506  0.06304  290 HIS A O   
3748 C  CB  . HIS A  290 ? 0.32818 0.21225 0.34791 0.03152  0.05422  0.07024  290 HIS A CB  
3749 C  CG  . HIS A  290 ? 0.33017 0.21099 0.34815 0.03659  0.05551  0.06853  290 HIS A CG  
3750 N  ND1 . HIS A  290 ? 0.32939 0.20652 0.34606 0.02964  0.05264  0.05857  290 HIS A ND1 
3751 C  CD2 . HIS A  290 ? 0.35556 0.23679 0.37281 0.04811  0.05917  0.07540  290 HIS A CD2 
3752 C  CE1 . HIS A  290 ? 0.34240 0.21749 0.35771 0.03643  0.05467  0.05936  290 HIS A CE1 
3753 N  NE2 . HIS A  290 ? 0.34896 0.22631 0.36465 0.04769  0.05875  0.06944  290 HIS A NE2 
3761 N  N   . GLU A  291 ? 0.37335 0.24287 0.39719 0.02653  0.06587  0.08063  291 GLU A N   
3762 C  CA  . GLU A  291 ? 0.38203 0.25783 0.40760 0.02304  0.06398  0.08326  291 GLU A CA  
3763 C  C   . GLU A  291 ? 0.40021 0.26147 0.42727 0.01178  0.06891  0.07793  291 GLU A C   
3764 O  O   . GLU A  291 ? 0.39755 0.26431 0.42616 0.00683  0.06649  0.07808  291 GLU A O   
3765 C  CB  . GLU A  291 ? 0.38488 0.26328 0.41084 0.03383  0.06848  0.09562  291 GLU A CB  
3766 C  CG  . GLU A  291 ? 0.44622 0.34464 0.47142 0.04384  0.06121  0.10096  291 GLU A CG  
3767 C  CD  . GLU A  291 ? 0.48989 0.38974 0.51531 0.05487  0.06628  0.11320  291 GLU A CD  
3768 O  OE1 . GLU A  291 ? 0.57229 0.45886 0.59842 0.05391  0.07465  0.11752  291 GLU A OE1 
3769 O  OE2 . GLU A  291 ? 0.37486 0.28897 0.39969 0.06451  0.06208  0.11853  291 GLU A OE2 
3776 N  N   . ARG A  292 ? 0.41202 0.25486 0.43880 0.00773  0.07609  0.07344  292 ARG A N   
3777 C  CA  . ARG A  292 ? 0.43767 0.26735 0.46602 -0.00372 0.08029  0.06725  292 ARG A CA  
3778 C  C   . ARG A  292 ? 0.53436 0.37407 0.56302 -0.01427 0.07060  0.05679  292 ARG A C   
3779 O  O   . ARG A  292 ? 0.54107 0.37760 0.57142 -0.02325 0.07099  0.05273  292 ARG A O   
3780 C  CB  . ARG A  292 ? 0.51196 0.32050 0.53991 -0.00590 0.08943  0.06392  292 ARG A CB  
3781 C  CG  . ARG A  292 ? 0.85164 0.64472 0.87960 0.00099  0.10125  0.07294  292 ARG A CG  
3782 C  CD  . ARG A  292 ? 1.01600 0.80079 1.04590 -0.00430 0.10714  0.07526  292 ARG A CD  
3783 N  NE  . ARG A  292 ? 1.17257 0.97148 1.20298 0.00081  0.10361  0.08308  292 ARG A NE  
3784 C  CZ  . ARG A  292 ? 1.13210 0.93140 1.16163 0.01191  0.10802  0.09416  292 ARG A CZ  
3785 N  NH1 . ARG A  292 ? 1.06404 0.84998 1.09204 0.01927  0.11642  0.09905  292 ARG A NH1 
3786 N  NH2 . ARG A  292 ? 1.08038 0.89387 1.11047 0.01588  0.10384  0.10045  292 ARG A NH2 
3800 N  N   A ASP A  293 ? 0.45007 0.30204 0.47699 -0.01321 0.06192  0.05238  293 ASP A N   
3801 N  N   B ASP A  293 ? 0.44575 0.29733 0.47265 -0.01333 0.06202  0.05218  293 ASP A N   
3802 C  CA  A ASP A  293 ? 0.51595 0.37788 0.54259 -0.02265 0.05236  0.04268  293 ASP A CA  
3803 C  CA  B ASP A  293 ? 0.49874 0.36205 0.52522 -0.02199 0.05171  0.04289  293 ASP A CA  
3804 C  C   A ASP A  293 ? 0.47038 0.34807 0.49815 -0.02309 0.04602  0.04585  293 ASP A C   
3805 C  C   B ASP A  293 ? 0.46607 0.34414 0.49383 -0.02289 0.04589  0.04602  293 ASP A C   
3806 O  O   A ASP A  293 ? 0.36703 0.25682 0.39466 -0.01412 0.04355  0.05407  293 ASP A O   
3807 O  O   B ASP A  293 ? 0.35857 0.24858 0.38627 -0.01405 0.04358  0.05435  293 ASP A O   
3808 C  CB  A ASP A  293 ? 0.43519 0.30679 0.45929 -0.02102 0.04454  0.03764  293 ASP A CB  
3809 C  CB  B ASP A  293 ? 0.42586 0.30065 0.44979 -0.01771 0.04411  0.04027  293 ASP A CB  
3810 C  CG  A ASP A  293 ? 0.55388 0.42993 0.57712 -0.03204 0.03668  0.02600  293 ASP A CG  
3811 C  CG  B ASP A  293 ? 0.53988 0.42358 0.56247 -0.02676 0.03422  0.02943  293 ASP A CG  
3812 O  OD1 A ASP A  293 ? 0.37062 0.23271 0.39385 -0.03958 0.04043  0.01847  293 ASP A OD1 
3813 O  OD1 B ASP A  293 ? 0.36695 0.25507 0.39058 -0.03445 0.03035  0.02561  293 ASP A OD1 
3814 O  OD2 A ASP A  293 ? 0.40494 0.29816 0.42745 -0.03313 0.02693  0.02444  293 ASP A OD2 
3815 O  OD2 B ASP A  293 ? 0.46436 0.35055 0.48466 -0.02594 0.03041  0.02480  293 ASP A OD2 
3824 N  N   . ARG A  294 ? 0.40865 0.28625 0.43763 -0.03354 0.04344  0.03919  294 ARG A N   
3825 C  CA  . ARG A  294 ? 0.43357 0.32556 0.46375 -0.03510 0.03739  0.04125  294 ARG A CA  
3826 C  C   . ARG A  294 ? 0.30990 0.22322 0.33838 -0.03093 0.02595  0.04151  294 ARG A C   
3827 O  O   . ARG A  294 ? 0.35130 0.27801 0.38068 -0.02756 0.02188  0.04711  294 ARG A O   
3828 C  CB  . ARG A  294 ? 0.49198 0.38069 0.52351 -0.04775 0.03573  0.03236  294 ARG A CB  
3829 C  CG  . ARG A  294 ? 0.80769 0.67784 0.84158 -0.05225 0.04678  0.03318  294 ARG A CG  
3830 C  CD  . ARG A  294 ? 0.90035 0.77117 0.93605 -0.06373 0.04434  0.02589  294 ARG A CD  
3831 N  NE  . ARG A  294 ? 1.12063 0.99260 1.15505 -0.07251 0.03804  0.01380  294 ARG A NE  
3832 C  CZ  . ARG A  294 ? 1.22441 1.08106 1.25881 -0.07869 0.04296  0.00652  294 ARG A CZ  
3833 N  NH1 . ARG A  294 ? 1.26560 1.10423 1.30116 -0.07717 0.05431  0.00988  294 ARG A NH1 
3834 N  NH2 . ARG A  294 ? 1.13253 0.99190 1.16554 -0.08648 0.03637  -0.00440 294 ARG A NH2 
3848 N  N   . GLN A  295 ? 0.31620 0.23279 0.34223 -0.03040 0.02116  0.03624  295 GLN A N   
3849 C  CA  . GLN A  295 ? 0.25903 0.19535 0.28324 -0.02661 0.01053  0.03617  295 GLN A CA  
3850 C  C   . GLN A  295 ? 0.26950 0.21383 0.29346 -0.01382 0.01131  0.04632  295 GLN A C   
3851 O  O   . GLN A  295 ? 0.27748 0.23931 0.30032 -0.00979 0.00282  0.04752  295 GLN A O   
3852 C  CB  . GLN A  295 ? 0.27485 0.21236 0.29620 -0.03101 0.00473  0.02646  295 GLN A CB  
3853 C  CG  . GLN A  295 ? 0.34017 0.27235 0.36125 -0.04349 0.00220  0.01554  295 GLN A CG  
3854 C  CD  . GLN A  295 ? 0.35184 0.27940 0.37012 -0.04676 -0.00002 0.00706  295 GLN A CD  
3855 O  OE1 . GLN A  295 ? 0.33807 0.27696 0.35380 -0.04962 -0.00934 0.00108  295 GLN A OE1 
3856 N  NE2 . GLN A  295 ? 0.38418 0.29487 0.40270 -0.04590 0.00871  0.00676  295 GLN A NE2 
3865 N  N   . ILE A  296 ? 0.28198 0.21412 0.30678 -0.00711 0.02117  0.05347  296 ILE A N   
3866 C  CA  . ILE A  296 ? 0.29003 0.22865 0.31440 0.00560  0.02252  0.06289  296 ILE A CA  
3867 C  C   . ILE A  296 ? 0.29461 0.23210 0.32104 0.01099  0.02821  0.07309  296 ILE A C   
3868 O  O   . ILE A  296 ? 0.33025 0.25095 0.35764 0.01088  0.03821  0.07614  296 ILE A O   
3869 C  CB  . ILE A  296 ? 0.29127 0.21700 0.31436 0.01019  0.02914  0.06299  296 ILE A CB  
3870 C  CG1 . ILE A  296 ? 0.31299 0.24079 0.33386 0.00510  0.02313  0.05298  296 ILE A CG1 
3871 C  CG2 . ILE A  296 ? 0.30347 0.23522 0.32628 0.02378  0.03134  0.07316  296 ILE A CG2 
3872 C  CD1 . ILE A  296 ? 0.38765 0.33593 0.40690 0.00901  0.01263  0.05245  296 ILE A CD1 
3884 N  N   . SER A  297 ? 0.27107 0.22618 0.29804 0.01604  0.02210  0.07864  297 SER A N   
3885 C  CA  . SER A  297 ? 0.27703 0.23272 0.30574 0.02167  0.02679  0.08862  297 SER A CA  
3886 C  C   . SER A  297 ? 0.27956 0.23402 0.30774 0.03477  0.03235  0.09860  297 SER A C   
3887 O  O   . SER A  297 ? 0.32138 0.26927 0.35053 0.03949  0.03960  0.10685  297 SER A O   
3888 C  CB  . SER A  297 ? 0.28138 0.25651 0.31109 0.02088  0.01782  0.09008  297 SER A CB  
3889 O  OG  . SER A  297 ? 0.28679 0.27919 0.31507 0.02348  0.00788  0.08752  297 SER A OG  
3895 N  N   . GLU A  298 ? 0.28737 0.24748 0.31389 0.04063  0.02934  0.09779  298 GLU A N   
3896 C  CA  . GLU A  298 ? 0.29665 0.25519 0.32253 0.05318  0.03470  0.10656  298 GLU A CA  
3897 C  C   . GLU A  298 ? 0.26354 0.22076 0.28754 0.05554  0.03351  0.10193  298 GLU A C   
3898 O  O   . GLU A  298 ? 0.26118 0.22823 0.28423 0.05092  0.02511  0.09438  298 GLU A O   
3899 C  CB  . GLU A  298 ? 0.28407 0.26159 0.31050 0.06274  0.02976  0.11495  298 GLU A CB  
3900 C  CG  . GLU A  298 ? 0.32474 0.29842 0.35063 0.07563  0.03675  0.12463  298 GLU A CG  
3901 C  CD  . GLU A  298 ? 0.33387 0.32787 0.35974 0.08084  0.03181  0.12520  298 GLU A CD  
3902 O  OE1 . GLU A  298 ? 0.35291 0.36327 0.37928 0.07711  0.02315  0.12139  298 GLU A OE1 
3903 O  OE2 . GLU A  298 ? 0.35239 0.34554 0.37745 0.08746  0.03682  0.12748  298 GLU A OE2 
3910 N  N   . HIS A  299 ? 0.28645 0.23130 0.30972 0.06263  0.04198  0.10636  299 HIS A N   
3911 C  CA  . HIS A  299 ? 0.28260 0.22752 0.30418 0.06709  0.04132  0.10366  299 HIS A CA  
3912 C  C   . HIS A  299 ? 0.29865 0.24472 0.31983 0.08096  0.04625  0.11367  299 HIS A C   
3913 O  O   . HIS A  299 ? 0.32669 0.26199 0.34828 0.08529  0.05464  0.12100  299 HIS A O   
3914 C  CB  . HIS A  299 ? 0.31939 0.24472 0.34019 0.06038  0.04734  0.09673  299 HIS A CB  
3915 C  CG  . HIS A  299 ? 0.29945 0.22294 0.31856 0.06561  0.04806  0.09472  299 HIS A CG  
3916 N  ND1 . HIS A  299 ? 0.39134 0.30171 0.40984 0.07319  0.05720  0.09975  299 HIS A ND1 
3917 C  CD2 . HIS A  299 ? 0.26719 0.20131 0.28498 0.06492  0.04058  0.08864  299 HIS A CD2 
3918 C  CE1 . HIS A  299 ? 0.33265 0.24541 0.34972 0.07649  0.05529  0.09633  299 HIS A CE1 
3919 N  NE2 . HIS A  299 ? 0.31790 0.24480 0.33452 0.07141  0.04537  0.08951  299 HIS A NE2 
3927 N  N   . ARG A  300 ? 0.28135 0.24033 0.30156 0.08794  0.04113  0.11381  300 ARG A N   
3928 C  CA  . ARG A  300 ? 0.29641 0.25932 0.31559 0.09746  0.04445  0.11732  300 ARG A CA  
3929 C  C   . ARG A  300 ? 0.28292 0.24543 0.30062 0.09972  0.04296  0.11277  300 ARG A C   
3930 O  O   . ARG A  300 ? 0.27259 0.24110 0.29013 0.09602  0.03603  0.10777  300 ARG A O   
3931 C  CB  . ARG A  300 ? 0.26724 0.25311 0.28628 0.09936  0.03763  0.11635  300 ARG A CB  
3932 C  CG  . ARG A  300 ? 0.29450 0.28588 0.31511 0.09643  0.03635  0.11923  300 ARG A CG  
3933 C  CD  . ARG A  300 ? 0.30478 0.31756 0.32504 0.09600  0.02883  0.11563  300 ARG A CD  
3934 N  NE  . ARG A  300 ? 0.28472 0.30354 0.30656 0.09184  0.02607  0.11670  300 ARG A NE  
3935 C  CZ  . ARG A  300 ? 0.31534 0.35019 0.33700 0.08850  0.01892  0.11193  300 ARG A CZ  
3936 N  NH1 . ARG A  300 ? 0.28810 0.33339 0.30797 0.08884  0.01495  0.10636  300 ARG A NH1 
3937 N  NH2 . ARG A  300 ? 0.31384 0.35266 0.33697 0.08401  0.01624  0.11230  300 ARG A NH2 
3951 N  N   . SER A  301 ? 0.29827 0.25536 0.31473 0.10580  0.04896  0.11420  301 SER A N   
3952 C  CA  . SER A  301 ? 0.28604 0.24550 0.30106 0.10835  0.04699  0.10975  301 SER A CA  
3953 C  C   . SER A  301 ? 0.31289 0.27146 0.32645 0.11552  0.05259  0.11221  301 SER A C   
3954 O  O   . SER A  301 ? 0.32903 0.28019 0.34256 0.11840  0.05951  0.11739  301 SER A O   
3955 C  CB  . SER A  301 ? 0.30671 0.24707 0.32169 0.10474  0.05061  0.10653  301 SER A CB  
3956 O  OG  . SER A  301 ? 0.37064 0.29083 0.38531 0.10686  0.06149  0.10974  301 SER A OG  
3962 N  N   . THR A  302 ? 0.29748 0.26258 0.30963 0.11817  0.04985  0.10833  302 THR A N   
3963 C  CA  . THR A  302 ? 0.31459 0.27704 0.32506 0.12464  0.05522  0.11012  302 THR A CA  
3964 C  C   . THR A  302 ? 0.36114 0.30500 0.37105 0.12558  0.06149  0.10863  302 THR A C   
3965 O  O   . THR A  302 ? 0.40084 0.34489 0.40918 0.13013  0.06347  0.10774  302 THR A O   
3966 C  CB  . THR A  302 ? 0.31980 0.30142 0.32881 0.12669  0.04888  0.10691  302 THR A CB  
3967 O  OG1 . THR A  302 ? 0.29692 0.28521 0.30591 0.12287  0.04177  0.10046  302 THR A OG1 
3968 C  CG2 . THR A  302 ? 0.31703 0.31399 0.32629 0.12541  0.04457  0.10800  302 THR A CG2 
3976 N  N   . CYS A  303 ? 0.35496 0.28195 0.36598 0.12069  0.06500  0.10790  303 CYS A N   
3977 C  CA  . CYS A  303 ? 0.36973 0.27579 0.38019 0.11999  0.07245  0.10582  303 CYS A CA  
3978 C  C   . CYS A  303 ? 0.45466 0.35200 0.46389 0.12533  0.08112  0.11044  303 CYS A C   
3979 O  O   . CYS A  303 ? 0.45874 0.35898 0.46803 0.12751  0.08348  0.11587  303 CYS A O   
3980 C  CB  . CYS A  303 ? 0.39613 0.28398 0.40790 0.11190  0.07604  0.10446  303 CYS A CB  
3981 S  SG  . CYS A  303 ? 0.41596 0.31353 0.42806 0.09848  0.06550  0.09338  303 CYS A SG  
3986 N  N   . PRO A  304 ? 0.44734 0.33338 0.45531 0.12735  0.08617  0.10823  304 PRO A N   
3987 C  CA  . PRO A  304 ? 0.46651 0.34728 0.47425 0.12492  0.08452  0.10145  304 PRO A CA  
3988 C  C   . PRO A  304 ? 0.53901 0.43979 0.54594 0.12917  0.07670  0.09906  304 PRO A C   
3989 O  O   . PRO A  304 ? 0.69716 0.61033 0.70301 0.13487  0.07576  0.10240  304 PRO A O   
3990 C  CB  . PRO A  304 ? 0.63658 0.49947 0.64307 0.12651  0.09370  0.10124  304 PRO A CB  
3991 C  CG  . PRO A  304 ? 0.77369 0.62968 0.77991 0.12840  0.10060  0.10785  304 PRO A CG  
3992 C  CD  . PRO A  304 ? 0.53031 0.40554 0.53692 0.13172  0.09504  0.11252  304 PRO A CD  
4000 N  N   . PHE A  305 ? 0.51557 0.41875 0.52277 0.12588  0.07145  0.09281  305 PHE A N   
4001 C  CA  . PHE A  305 ? 0.68603 0.60845 0.69241 0.12853  0.06353  0.08949  305 PHE A CA  
4002 C  C   . PHE A  305 ? 0.85867 0.77594 0.86358 0.13257  0.06722  0.08714  305 PHE A C   
4003 O  O   . PHE A  305 ? 0.79319 0.70483 0.79783 0.13053  0.06651  0.08112  305 PHE A O   
4004 C  CB  . PHE A  305 ? 0.58701 0.51475 0.59406 0.12322  0.05610  0.08383  305 PHE A CB  
4005 C  CG  . PHE A  305 ? 0.44166 0.37594 0.44995 0.11839  0.05163  0.08560  305 PHE A CG  
4006 C  CD1 . PHE A  305 ? 0.43017 0.37775 0.43885 0.12099  0.04965  0.09104  305 PHE A CD1 
4007 C  CD2 . PHE A  305 ? 0.42600 0.35650 0.43412 0.10551  0.04800  0.07777  305 PHE A CD2 
4008 C  CE1 . PHE A  305 ? 0.35425 0.30778 0.36420 0.11684  0.04557  0.09265  305 PHE A CE1 
4009 C  CE2 . PHE A  305 ? 0.45884 0.39601 0.46793 0.10022  0.04363  0.07856  305 PHE A CE2 
4010 C  CZ  . PHE A  305 ? 0.41870 0.36648 0.42906 0.10753  0.04278  0.08735  305 PHE A CZ  
4020 N  N   . GLY B  42  ? 0.79116 0.80095 0.81879 0.03254  0.02136  0.03928  42  GLY B N   
4021 C  CA  . GLY B  42  ? 0.63131 0.63985 0.65670 0.03209  0.02163  0.03378  42  GLY B CA  
4022 C  C   . GLY B  42  ? 0.45139 0.46576 0.47230 0.03066  0.02023  0.03228  42  GLY B C   
4023 O  O   . GLY B  42  ? 0.42935 0.44916 0.44941 0.03051  0.01893  0.03552  42  GLY B O   
4027 N  N   . TYR B  43  ? 0.32222 0.33528 0.34024 0.02973  0.02036  0.02726  43  TYR B N   
4028 C  CA  . TYR B  43  ? 0.28825 0.30612 0.30195 0.02835  0.01888  0.02527  43  TYR B CA  
4029 C  C   . TYR B  43  ? 0.27670 0.29676 0.29128 0.02970  0.01845  0.02446  43  TYR B C   
4030 O  O   . TYR B  43  ? 0.26352 0.28781 0.27496 0.02862  0.01700  0.02322  43  TYR B O   
4031 C  CB  . TYR B  43  ? 0.27531 0.29061 0.28496 0.02649  0.01906  0.02014  43  TYR B CB  
4032 C  CG  . TYR B  43  ? 0.28876 0.30193 0.29749 0.02498  0.01959  0.02020  43  TYR B CG  
4033 C  CD1 . TYR B  43  ? 0.28967 0.30686 0.29725 0.02383  0.01876  0.02372  43  TYR B CD1 
4034 C  CD2 . TYR B  43  ? 0.33256 0.33972 0.34167 0.02478  0.02095  0.01666  43  TYR B CD2 
4035 C  CE1 . TYR B  43  ? 0.30685 0.32245 0.31373 0.02236  0.01938  0.02391  43  TYR B CE1 
4036 C  CE2 . TYR B  43  ? 0.36513 0.37053 0.37375 0.02328  0.02147  0.01671  43  TYR B CE2 
4037 C  CZ  . TYR B  43  ? 0.34738 0.35716 0.35491 0.02200  0.02073  0.02040  43  TYR B CZ  
4038 O  OH  . TYR B  43  ? 0.41831 0.42678 0.42543 0.02038  0.02135  0.02059  43  TYR B OH  
4048 N  N   . ALA B  44  ? 0.25323 0.27054 0.27194 0.03201  0.01961  0.02490  44  ALA B N   
4049 C  CA  . ALA B  44  ? 0.22174 0.24132 0.24140 0.03324  0.01941  0.02399  44  ALA B CA  
4050 C  C   . ALA B  44  ? 0.22627 0.25258 0.24648 0.03342  0.01777  0.02770  44  ALA B C   
4051 O  O   . ALA B  44  ? 0.26378 0.29178 0.28584 0.03402  0.01734  0.03193  44  ALA B O   
4052 C  CB  . ALA B  44  ? 0.26582 0.28142 0.29006 0.03600  0.02099  0.02401  44  ALA B CB  
4058 N  N   . ARG B  45  ? 0.21958 0.24958 0.23797 0.03279  0.01675  0.02602  45  ARG B N   
4059 C  CA  . ARG B  45  ? 0.21824 0.25478 0.23708 0.03287  0.01498  0.02884  45  ARG B CA  
4060 C  C   . ARG B  45  ? 0.22507 0.26339 0.24610 0.03407  0.01519  0.02790  45  ARG B C   
4061 O  O   . ARG B  45  ? 0.22830 0.26407 0.24838 0.03390  0.01612  0.02423  45  ARG B O   
4062 C  CB  . ARG B  45  ? 0.21539 0.25592 0.22926 0.03038  0.01286  0.02780  45  ARG B CB  
4063 C  CG  . ARG B  45  ? 0.21447 0.25367 0.22535 0.02889  0.01266  0.02791  45  ARG B CG  
4064 C  CD  . ARG B  45  ? 0.23294 0.27445 0.24555 0.02962  0.01223  0.03286  45  ARG B CD  
4065 N  NE  . ARG B  45  ? 0.23290 0.27317 0.24302 0.02822  0.01235  0.03328  45  ARG B NE  
4066 C  CZ  . ARG B  45  ? 0.30731 0.34320 0.31948 0.02866  0.01399  0.03464  45  ARG B CZ  
4067 N  NH1 . ARG B  45  ? 0.31353 0.34559 0.33013 0.03060  0.01550  0.03559  45  ARG B NH1 
4068 N  NH2 . ARG B  45  ? 0.28008 0.31532 0.28987 0.02713  0.01409  0.03487  45  ARG B NH2 
4082 N  N   . GLY B  46  ? 0.21915 0.26205 0.24315 0.03536  0.01433  0.03133  46  GLY B N   
4083 C  CA  . GLY B  46  ? 0.19889 0.24484 0.22492 0.03616  0.01424  0.03072  46  GLY B CA  
4084 C  C   . GLY B  46  ? 0.20638 0.24967 0.23678 0.03879  0.01621  0.03072  46  GLY B C   
4085 O  O   . GLY B  46  ? 0.23930 0.27762 0.27130 0.04016  0.01768  0.03085  46  GLY B O   
4089 N  N   . PRO B  47  ? 0.20583 0.25258 0.23835 0.03958  0.01620  0.03054  47  PRO B N   
4090 C  CA  . PRO B  47  ? 0.19890 0.24402 0.23568 0.04234  0.01799  0.03055  47  PRO B CA  
4091 C  C   . PRO B  47  ? 0.20954 0.24898 0.24516 0.04265  0.01994  0.02654  47  PRO B C   
4092 O  O   . PRO B  47  ? 0.21117 0.24841 0.24265 0.04060  0.01991  0.02339  47  PRO B O   
4093 C  CB  . PRO B  47  ? 0.21215 0.26338 0.25093 0.04255  0.01726  0.03124  47  PRO B CB  
4094 C  CG  . PRO B  47  ? 0.21158 0.26517 0.24606 0.03948  0.01576  0.02926  47  PRO B CG  
4095 C  CD  . PRO B  47  ? 0.22554 0.27757 0.25645 0.03785  0.01457  0.02982  47  PRO B CD  
4103 N  N   . ASP B  48  ? 0.20302 0.23998 0.24230 0.04547  0.02155  0.02661  48  ASP B N   
4104 C  CA  . ASP B  48  ? 0.19316 0.22496 0.23163 0.04626  0.02340  0.02277  48  ASP B CA  
4105 C  C   . ASP B  48  ? 0.20432 0.23852 0.24065 0.04498  0.02358  0.02003  48  ASP B C   
4106 O  O   . ASP B  48  ? 0.19514 0.23472 0.23356 0.04532  0.02319  0.02144  48  ASP B O   
4107 C  CB  . ASP B  48  ? 0.21049 0.23986 0.25348 0.04988  0.02489  0.02334  48  ASP B CB  
4108 C  CG  . ASP B  48  ? 0.22804 0.25377 0.27303 0.05117  0.02477  0.02565  48  ASP B CG  
4109 O  OD1 . ASP B  48  ? 0.23716 0.26146 0.27967 0.04909  0.02391  0.02637  48  ASP B OD1 
4110 O  OD2 . ASP B  48  ? 0.25876 0.28313 0.30768 0.05415  0.02545  0.02682  48  ASP B OD2 
4115 N  N   . PRO B  49  ? 0.18882 0.21916 0.22118 0.04358  0.02415  0.01617  49  PRO B N   
4116 C  CA  . PRO B  49  ? 0.18630 0.21871 0.21607 0.04203  0.02409  0.01370  49  PRO B CA  
4117 C  C   . PRO B  49  ? 0.19249 0.22456 0.22455 0.04433  0.02604  0.01226  49  PRO B C   
4118 O  O   . PRO B  49  ? 0.20374 0.23214 0.23812 0.04708  0.02763  0.01168  49  PRO B O   
4119 C  CB  . PRO B  49  ? 0.19949 0.22711 0.22394 0.03994  0.02395  0.01003  49  PRO B CB  
4120 C  CG  . PRO B  49  ? 0.21656 0.23835 0.24213 0.04161  0.02508  0.00961  49  PRO B CG  
4121 C  CD  . PRO B  49  ? 0.20059 0.22482 0.23025 0.04288  0.02449  0.01412  49  PRO B CD  
4129 N  N   . THR B  50  ? 0.18475 0.22078 0.21599 0.04311  0.02581  0.01163  50  THR B N   
4130 C  CA  . THR B  50  ? 0.18463 0.22038 0.21647 0.04447  0.02765  0.00957  50  THR B CA  
4131 C  C   . THR B  50  ? 0.18481 0.22084 0.21201 0.04157  0.02704  0.00696  50  THR B C   
4132 O  O   . THR B  50  ? 0.18096 0.21860 0.20536 0.03876  0.02501  0.00722  50  THR B O   
4133 C  CB  . THR B  50  ? 0.20466 0.24629 0.24163 0.04631  0.02813  0.01235  50  THR B CB  
4134 O  OG1 . THR B  50  ? 0.19046 0.23821 0.22759 0.04391  0.02614  0.01454  50  THR B OG1 
4135 C  CG2 . THR B  50  ? 0.20166 0.24294 0.24324 0.04941  0.02853  0.01494  50  THR B CG2 
4143 N  N   . GLU B  51  ? 0.20283 0.23750 0.22922 0.04238  0.02874  0.00452  51  GLU B N   
4144 C  CA  . GLU B  51  ? 0.19434 0.22857 0.21610 0.03978  0.02827  0.00188  51  GLU B CA  
4145 C  C   . GLU B  51  ? 0.19367 0.23443 0.21588 0.03721  0.02633  0.00404  51  GLU B C   
4146 O  O   . GLU B  51  ? 0.19692 0.23765 0.21513 0.03427  0.02436  0.00300  51  GLU B O   
4147 C  CB  . GLU B  51  ? 0.23786 0.26963 0.25910 0.04156  0.03067  -0.00074 51  GLU B CB  
4148 C  CG  . GLU B  51  ? 0.38901 0.41440 0.41039 0.04462  0.03253  -0.00294 51  GLU B CG  
4149 C  CD  . GLU B  51  ? 0.58471 0.61110 0.61186 0.04850  0.03398  -0.00084 51  GLU B CD  
4150 O  OE1 . GLU B  51  ? 0.27297 0.30430 0.30458 0.04918  0.03335  0.00287  51  GLU B OE1 
4151 O  OE2 . GLU B  51  ? 0.71716 0.73889 0.74424 0.05119  0.03573  -0.00323 51  GLU B OE2 
4158 N  N   . SER B  52  ? 0.19748 0.24398 0.22464 0.03833  0.02664  0.00702  52  SER B N   
4159 C  CA  . SER B  52  ? 0.19545 0.24819 0.22340 0.03593  0.02474  0.00893  52  SER B CA  
4160 C  C   . SER B  52  ? 0.19222 0.24668 0.21923 0.03412  0.02196  0.01065  52  SER B C   
4161 O  O   . SER B  52  ? 0.18860 0.24554 0.21331 0.03131  0.01974  0.01056  52  SER B O   
4162 C  CB  . SER B  52  ? 0.22066 0.27948 0.25463 0.03770  0.02562  0.01188  52  SER B CB  
4163 O  OG  . SER B  52  ? 0.32787 0.38634 0.36244 0.03894  0.02800  0.01041  52  SER B OG  
4169 N  N   . PHE B  53  ? 0.18323 0.23619 0.21179 0.03576  0.02196  0.01215  53  PHE B N   
4170 C  CA  . PHE B  53  ? 0.18336 0.23748 0.21060 0.03429  0.01953  0.01375  53  PHE B CA  
4171 C  C   . PHE B  53  ? 0.18403 0.23461 0.20514 0.03165  0.01819  0.01081  53  PHE B C   
4172 O  O   . PHE B  53  ? 0.18798 0.24131 0.20709 0.02947  0.01564  0.01149  53  PHE B O   
4173 C  CB  . PHE B  53  ? 0.18378 0.23591 0.21377 0.03682  0.02034  0.01571  53  PHE B CB  
4174 C  CG  . PHE B  53  ? 0.18000 0.23134 0.20801 0.03576  0.01857  0.01689  53  PHE B CG  
4175 C  CD1 . PHE B  53  ? 0.18004 0.23649 0.20994 0.03545  0.01659  0.02032  53  PHE B CD1 
4176 C  CD2 . PHE B  53  ? 0.18784 0.23330 0.21225 0.03529  0.01900  0.01462  53  PHE B CD2 
4177 C  CE1 . PHE B  53  ? 0.18453 0.24028 0.21239 0.03463  0.01511  0.02151  53  PHE B CE1 
4178 C  CE2 . PHE B  53  ? 0.19085 0.23576 0.21361 0.03440  0.01762  0.01585  53  PHE B CE2 
4179 C  CZ  . PHE B  53  ? 0.18413 0.23425 0.20851 0.03409  0.01572  0.01935  53  PHE B CZ  
4189 N  N   . LEU B  54  ? 0.17694 0.22147 0.19505 0.03201  0.01976  0.00749  54  LEU B N   
4190 C  CA  . LEU B  54  ? 0.17957 0.22039 0.19177 0.02974  0.01860  0.00431  54  LEU B CA  
4191 C  C   . LEU B  54  ? 0.18794 0.23013 0.19694 0.02734  0.01745  0.00236  54  LEU B C   
4192 O  O   . LEU B  54  ? 0.20374 0.24464 0.20801 0.02507  0.01555  0.00040  54  LEU B O   
4193 C  CB  . LEU B  54  ? 0.19860 0.23226 0.20880 0.03111  0.02072  0.00109  54  LEU B CB  
4194 C  CG  . LEU B  54  ? 0.21124 0.24196 0.22202 0.03208  0.02087  0.00191  54  LEU B CG  
4195 C  CD1 . LEU B  54  ? 0.23424 0.25849 0.24483 0.03407  0.02311  -0.00066 54  LEU B CD1 
4196 C  CD2 . LEU B  54  ? 0.25651 0.28712 0.26272 0.02938  0.01852  0.00107  54  LEU B CD2 
4208 N  N   . GLU B  55  ? 0.18596 0.23060 0.19733 0.02780  0.01853  0.00279  55  GLU B N   
4209 C  CA  . GLU B  55  ? 0.19547 0.24156 0.20426 0.02545  0.01745  0.00133  55  GLU B CA  
4210 C  C   . GLU B  55  ? 0.20450 0.25695 0.21467 0.02343  0.01458  0.00387  55  GLU B C   
4211 O  O   . GLU B  55  ? 0.21770 0.27112 0.22514 0.02099  0.01289  0.00262  55  GLU B O   
4212 C  CB  . GLU B  55  ? 0.22040 0.26671 0.23139 0.02680  0.02000  0.00093  55  GLU B CB  
4213 C  CG  . GLU B  55  ? 0.21969 0.25923 0.22807 0.02851  0.02248  -0.00246 55  GLU B CG  
4214 C  CD  . GLU B  55  ? 0.32982 0.36948 0.34066 0.03063  0.02528  -0.00267 55  GLU B CD  
4215 O  OE1 . GLU B  55  ? 0.35655 0.40188 0.37174 0.03094  0.02562  0.00004  55  GLU B OE1 
4216 O  OE2 . GLU B  55  ? 0.35312 0.38735 0.36168 0.03217  0.02718  -0.00558 55  GLU B OE2 
4223 N  N   . ALA B  56  ? 0.19214 0.24889 0.20658 0.02449  0.01391  0.00739  56  ALA B N   
4224 C  CA  . ALA B  56  ? 0.20026 0.26337 0.21661 0.02298  0.01121  0.00989  56  ALA B CA  
4225 C  C   . ALA B  56  ? 0.19368 0.25639 0.20503 0.02038  0.00801  0.00848  56  ALA B C   
4226 O  O   . ALA B  56  ? 0.20264 0.26119 0.21004 0.02019  0.00777  0.00665  56  ALA B O   
4227 C  CB  . ALA B  56  ? 0.20759 0.27458 0.22899 0.02502  0.01118  0.01370  56  ALA B CB  
4233 N  N   . ASP B  57  ? 0.21289 0.28043 0.22478 0.01846  0.00537  0.00949  57  ASP B N   
4234 C  CA  . ASP B  57  ? 0.21226 0.27992 0.21948 0.01609  0.00195  0.00808  57  ASP B CA  
4235 C  C   . ASP B  57  ? 0.24662 0.31504 0.25302 0.01674  0.00049  0.00944  57  ASP B C   
4236 O  O   . ASP B  57  ? 0.25022 0.31693 0.25173 0.01536  -0.00155 0.00753  57  ASP B O   
4237 C  CB  . ASP B  57  ? 0.26363 0.33666 0.27238 0.01415  -0.00078 0.00920  57  ASP B CB  
4238 C  CG  . ASP B  57  ? 0.32736 0.39908 0.33501 0.01253  -0.00021 0.00724  57  ASP B CG  
4239 O  OD1 . ASP B  57  ? 0.32583 0.39196 0.32960 0.01233  0.00142  0.00420  57  ASP B OD1 
4240 O  OD2 . ASP B  57  ? 0.40206 0.47858 0.41289 0.01139  -0.00152 0.00885  57  ASP B OD2 
4245 N  N   . SER B  58  ? 0.23162 0.30283 0.24267 0.01884  0.00137  0.01279  58  SER B N   
4246 C  CA  . SER B  58  ? 0.26580 0.33760 0.27619 0.01962  0.00030  0.01441  58  SER B CA  
4247 C  C   . SER B  58  ? 0.20709 0.27625 0.22020 0.02222  0.00324  0.01587  58  SER B C   
4248 O  O   . SER B  58  ? 0.21595 0.28563 0.23346 0.02395  0.00545  0.01711  58  SER B O   
4249 C  CB  . SER B  58  ? 0.31905 0.39761 0.33249 0.01970  -0.00234 0.01770  58  SER B CB  
4250 O  OG  . SER B  58  ? 0.43245 0.51129 0.44470 0.02051  -0.00326 0.01923  58  SER B OG  
4256 N  N   . GLY B  59  ? 0.21405 0.28038 0.22452 0.02249  0.00321  0.01564  59  GLY B N   
4257 C  CA  . GLY B  59  ? 0.21783 0.28224 0.23098 0.02477  0.00527  0.01763  59  GLY B CA  
4258 C  C   . GLY B  59  ? 0.18783 0.25750 0.20502 0.02611  0.00415  0.02193  59  GLY B C   
4259 O  O   . GLY B  59  ? 0.22132 0.29637 0.23950 0.02535  0.00180  0.02327  59  GLY B O   
4263 N  N   . PRO B  60  ? 0.17859 0.24658 0.19817 0.02819  0.00573  0.02409  60  PRO B N   
4264 C  CA  . PRO B  60  ? 0.19684 0.26930 0.22066 0.02993  0.00504  0.02823  60  PRO B CA  
4265 C  C   . PRO B  60  ? 0.20501 0.28084 0.22705 0.02936  0.00242  0.03030  60  PRO B C   
4266 O  O   . PRO B  60  ? 0.21314 0.29356 0.23842 0.03060  0.00131  0.03351  60  PRO B O   
4267 C  CB  . PRO B  60  ? 0.22657 0.29494 0.25316 0.03236  0.00774  0.02941  60  PRO B CB  
4268 C  CG  . PRO B  60  ? 0.22116 0.28341 0.24355 0.03134  0.00884  0.02641  60  PRO B CG  
4269 C  CD  . PRO B  60  ? 0.19098 0.25266 0.21012 0.02928  0.00837  0.02274  60  PRO B CD  
4277 N  N   . TYR B  61  ? 0.18350 0.25737 0.20051 0.02772  0.00138  0.02858  61  TYR B N   
4278 C  CA  . TYR B  61  ? 0.19414 0.27124 0.20925 0.02746  -0.00096 0.03065  61  TYR B CA  
4279 C  C   . TYR B  61  ? 0.18702 0.26909 0.20030 0.02588  -0.00425 0.02994  61  TYR B C   
4280 O  O   . TYR B  61  ? 0.23596 0.31722 0.24698 0.02411  -0.00490 0.02678  61  TYR B O   
4281 C  CB  . TYR B  61  ? 0.19887 0.27196 0.20951 0.02655  -0.00053 0.02922  61  TYR B CB  
4282 C  CG  . TYR B  61  ? 0.20527 0.27361 0.21782 0.02806  0.00232  0.03032  61  TYR B CG  
4283 C  CD1 . TYR B  61  ? 0.29766 0.36714 0.31263 0.02973  0.00254  0.03425  61  TYR B CD1 
4284 C  CD2 . TYR B  61  ? 0.22164 0.28423 0.23370 0.02792  0.00467  0.02742  61  TYR B CD2 
4285 C  CE1 . TYR B  61  ? 0.31582 0.38073 0.33283 0.03110  0.00496  0.03535  61  TYR B CE1 
4286 C  CE2 . TYR B  61  ? 0.23489 0.29314 0.24893 0.02934  0.00698  0.02832  61  TYR B CE2 
4287 C  CZ  . TYR B  61  ? 0.26591 0.32513 0.28252 0.03086  0.00715  0.03223  61  TYR B CZ  
4288 O  OH  . TYR B  61  ? 0.28871 0.34322 0.30753 0.03228  0.00933  0.03319  61  TYR B OH  
4298 N  N   . THR B  62  ? 0.22701 0.31401 0.24122 0.02662  -0.00642 0.03286  62  THR B N   
4299 C  CA  . THR B  62  ? 0.21828 0.31008 0.23048 0.02536  -0.01000 0.03239  62  THR B CA  
4300 C  C   . THR B  62  ? 0.19788 0.28829 0.20415 0.02402  -0.01135 0.03060  62  THR B C   
4301 O  O   . THR B  62  ? 0.20916 0.29797 0.21414 0.02478  -0.01039 0.03200  62  THR B O   
4302 C  CB  . THR B  62  ? 0.24196 0.33936 0.25738 0.02707  -0.01173 0.03625  62  THR B CB  
4303 O  OG1 . THR B  62  ? 0.26608 0.36517 0.28715 0.02834  -0.01058 0.03774  62  THR B OG1 
4304 C  CG2 . THR B  62  ? 0.26529 0.36786 0.27864 0.02607  -0.01579 0.03589  62  THR B CG2 
4312 N  N   . ILE B  63  ? 0.19344 0.24861 0.23745 0.03351  -0.02493 -0.01723 63  ILE B N   
4313 C  CA  . ILE B  63  ? 0.19280 0.25237 0.22757 0.03435  -0.02518 -0.02061 63  ILE B CA  
4314 C  C   . ILE B  63  ? 0.21225 0.28309 0.24278 0.03513  -0.02916 -0.02674 63  ILE B C   
4315 O  O   . ILE B  63  ? 0.23535 0.30755 0.26946 0.03468  -0.03156 -0.03062 63  ILE B O   
4316 C  CB  . ILE B  63  ? 0.20396 0.24968 0.23569 0.03382  -0.02168 -0.02541 63  ILE B CB  
4317 C  CG1 . ILE B  63  ? 0.21246 0.25085 0.24620 0.03323  -0.02215 -0.03390 63  ILE B CG1 
4318 C  CG2 . ILE B  63  ? 0.21201 0.24683 0.24671 0.03271  -0.01779 -0.01890 63  ILE B CG2 
4319 C  CD1 . ILE B  63  ? 0.26941 0.29479 0.29940 0.03273  -0.01926 -0.03922 63  ILE B CD1 
4331 N  N   . ALA B  64  ? 0.21228 0.29113 0.23474 0.03622  -0.02970 -0.02759 64  ALA B N   
4332 C  CA  . ALA B  64  ? 0.21337 0.30177 0.22967 0.03708  -0.03269 -0.03420 64  ALA B CA  
4333 C  C   . ALA B  64  ? 0.20609 0.29042 0.21551 0.03806  -0.03053 -0.03973 64  ALA B C   
4334 O  O   . ALA B  64  ? 0.21480 0.29104 0.22406 0.03796  -0.02722 -0.03726 64  ALA B O   
4335 C  CB  . ALA B  64  ? 0.23497 0.33935 0.24794 0.03759  -0.03560 -0.02920 64  ALA B CB  
4341 N  N   . THR B  65  ? 0.24596 0.33612 0.24960 0.03897  -0.03249 -0.04710 65  THR B N   
4342 C  CA  . THR B  65  ? 0.23148 0.31923 0.22870 0.04029  -0.03066 -0.05259 65  THR B CA  
4343 C  C   . THR B  65  ? 0.24570 0.34742 0.23516 0.04174  -0.03231 -0.05413 65  THR B C   
4344 O  O   . THR B  65  ? 0.25257 0.36464 0.24069 0.04146  -0.03558 -0.05398 65  THR B O   
4345 C  CB  . THR B  65  ? 0.27542 0.35337 0.27262 0.04022  -0.03056 -0.06192 65  THR B CB  
4346 O  OG1 . THR B  65  ? 0.31926 0.40361 0.31536 0.04000  -0.03411 -0.06691 65  THR B OG1 
4347 C  CG2 . THR B  65  ? 0.28991 0.35334 0.29418 0.03862  -0.02863 -0.06109 65  THR B CG2 
4355 N  N   . SER B  66  ? 0.24028 0.34181 0.22458 0.04319  -0.02996 -0.05595 66  SER B N   
4356 C  CA  . SER B  66  ? 0.24852 0.36196 0.22492 0.04482  -0.03072 -0.05877 66  SER B CA  
4357 C  C   . SER B  66  ? 0.26152 0.36926 0.23400 0.04654  -0.02847 -0.06601 66  SER B C   
4358 O  O   . SER B  66  ? 0.27431 0.37352 0.24867 0.04669  -0.02563 -0.06444 66  SER B O   
4359 C  CB  . SER B  66  ? 0.30316 0.42607 0.27752 0.04503  -0.02987 -0.05035 66  SER B CB  
4360 O  OG  . SER B  66  ? 0.41090 0.54632 0.37750 0.04640  -0.03071 -0.05299 66  SER B OG  
4366 N  N   . ASN B  67  ? 0.28834 0.40088 0.25519 0.04780  -0.02973 -0.07370 67  ASN B N   
4367 C  CA  . ASN B  67  ? 0.29423 0.40165 0.25744 0.04974  -0.02774 -0.08108 67  ASN B CA  
4368 C  C   . ASN B  67  ? 0.28727 0.40336 0.24521 0.05177  -0.02560 -0.07940 67  ASN B C   
4369 O  O   . ASN B  67  ? 0.34112 0.47003 0.29491 0.05202  -0.02655 -0.07651 67  ASN B O   
4370 C  CB  . ASN B  67  ? 0.32266 0.43060 0.28191 0.05025  -0.02986 -0.09053 67  ASN B CB  
4371 C  CG  . ASN B  67  ? 0.50150 0.59988 0.46606 0.04825  -0.03177 -0.09327 67  ASN B CG  
4372 O  OD1 . ASN B  67  ? 0.67076 0.75897 0.64169 0.04701  -0.03058 -0.09009 67  ASN B OD1 
4373 N  ND2 . ASN B  67  ? 0.65361 0.75509 0.61535 0.04776  -0.03467 -0.09920 67  ASN B ND2 
4380 N  N   . VAL B  68  ? 0.29155 0.40063 0.24971 0.05313  -0.02275 -0.08127 68  VAL B N   
4381 C  CA  . VAL B  68  ? 0.30791 0.42406 0.26197 0.05525  -0.02031 -0.08022 68  VAL B CA  
4382 C  C   . VAL B  68  ? 0.29971 0.41309 0.24997 0.05778  -0.01931 -0.08983 68  VAL B C   
4383 O  O   . VAL B  68  ? 0.30886 0.40998 0.26188 0.05794  -0.01859 -0.09403 68  VAL B O   
4384 C  CB  . VAL B  68  ? 0.32193 0.43269 0.27999 0.05461  -0.01782 -0.07325 68  VAL B CB  
4385 C  CG1 . VAL B  68  ? 0.32537 0.44409 0.27964 0.05678  -0.01537 -0.07227 68  VAL B CG1 
4386 C  CG2 . VAL B  68  ? 0.31858 0.43077 0.28045 0.05209  -0.01868 -0.06382 68  VAL B CG2 
4396 N  N   . SER B  69  ? 0.32788 0.45218 0.27164 0.05969  -0.01920 -0.09334 69  SER B N   
4397 C  CA  . SER B  69  ? 0.39215 0.51421 0.33189 0.06229  -0.01819 -0.10274 69  SER B CA  
4398 C  C   . SER B  69  ? 0.40050 0.51736 0.34209 0.06436  -0.01494 -0.10301 69  SER B C   
4399 O  O   . SER B  69  ? 0.33474 0.45475 0.27835 0.06424  -0.01318 -0.09594 69  SER B O   
4400 C  CB  . SER B  69  ? 0.43801 0.57384 0.36991 0.06377  -0.01834 -0.10549 69  SER B CB  
4401 O  OG  . SER B  69  ? 0.40177 0.53809 0.32951 0.06701  -0.01597 -0.11253 69  SER B OG  
4407 N  N   . SER B  70  ? 0.35392 0.46264 0.29481 0.06616  -0.01432 -0.11124 70  SER B N   
4408 C  CA  . SER B  70  ? 0.37074 0.47491 0.31322 0.06845  -0.01148 -0.11233 70  SER B CA  
4409 C  C   . SER B  70  ? 0.38347 0.50029 0.32199 0.07126  -0.00894 -0.11139 70  SER B C   
4410 O  O   . SER B  70  ? 0.39674 0.51213 0.33736 0.07307  -0.00647 -0.11034 70  SER B O   
4411 C  CB  . SER B  70  ? 0.42219 0.51548 0.36429 0.06997  -0.01158 -0.12177 70  SER B CB  
4412 O  OG  . SER B  70  ? 0.48061 0.57978 0.41641 0.07196  -0.01184 -0.12918 70  SER B OG  
4418 N  N   . LEU B  71  ? 0.38315 0.51232 0.31593 0.07164  -0.00946 -0.11192 71  LEU B N   
4419 C  CA  . LEU B  71  ? 0.45778 0.59972 0.38670 0.07394  -0.00684 -0.11026 71  LEU B CA  
4420 C  C   . LEU B  71  ? 0.45246 0.59971 0.38474 0.07262  -0.00571 -0.09989 71  LEU B C   
4421 O  O   . LEU B  71  ? 0.41586 0.57299 0.34606 0.07447  -0.00315 -0.09778 71  LEU B O   
4422 C  CB  . LEU B  71  ? 0.49446 0.64782 0.41577 0.07405  -0.00788 -0.11311 71  LEU B CB  
4423 C  CG  . LEU B  71  ? 0.63300 0.78295 0.54932 0.07590  -0.00824 -0.12398 71  LEU B CG  
4424 C  CD1 . LEU B  71  ? 0.61718 0.77741 0.52578 0.07501  -0.00993 -0.12604 71  LEU B CD1 
4425 C  CD2 . LEU B  71  ? 0.66024 0.80944 0.57637 0.07936  -0.00470 -0.12796 71  LEU B CD2 
4437 N  N   . VAL B  72  ? 0.34289 0.48383 0.28018 0.06945  -0.00738 -0.09345 72  VAL B N   
4438 C  CA  . VAL B  72  ? 0.33899 0.48341 0.27939 0.06794  -0.00633 -0.08357 72  VAL B CA  
4439 C  C   . VAL B  72  ? 0.36117 0.50304 0.30421 0.06983  -0.00341 -0.08298 72  VAL B C   
4440 O  O   . VAL B  72  ? 0.38594 0.51799 0.33106 0.07126  -0.00286 -0.08861 72  VAL B O   
4441 C  CB  . VAL B  72  ? 0.35626 0.49144 0.30179 0.06439  -0.00837 -0.07798 72  VAL B CB  
4442 C  CG1 . VAL B  72  ? 0.34255 0.46181 0.29291 0.06404  -0.00813 -0.08098 72  VAL B CG1 
4443 C  CG2 . VAL B  72  ? 0.41297 0.55323 0.36035 0.06244  -0.00774 -0.06749 72  VAL B CG2 
4453 N  N   . ARG B  73  ? 0.40752 0.55856 0.35054 0.06976  -0.00165 -0.07598 73  ARG B N   
4454 C  CA  . ARG B  73  ? 0.36319 0.51380 0.30897 0.07137  0.00103  -0.07438 73  ARG B CA  
4455 C  C   . ARG B  73  ? 0.35570 0.49393 0.30749 0.06875  0.00057  -0.06912 73  ARG B C   
4456 O  O   . ARG B  73  ? 0.43013 0.56654 0.38353 0.06551  -0.00064 -0.06207 73  ARG B O   
4457 C  CB  . ARG B  73  ? 0.47270 0.63824 0.41614 0.07190  0.00302  -0.06852 73  ARG B CB  
4458 C  CG  . ARG B  73  ? 0.53889 0.71679 0.47610 0.07494  0.00445  -0.07412 73  ARG B CG  
4459 C  CD  . ARG B  73  ? 0.91792 1.10222 0.85573 0.07821  0.00806  -0.07507 73  ARG B CD  
4460 N  NE  . ARG B  73  ? 1.14453 1.31936 1.08492 0.08096  0.00892  -0.08250 73  ARG B NE  
4461 C  CZ  . ARG B  73  ? 0.94196 1.11437 0.88696 0.08261  0.01093  -0.08157 73  ARG B CZ  
4462 N  NH1 . ARG B  73  ? 0.91469 1.09318 0.86246 0.08162  0.01234  -0.07348 73  ARG B NH1 
4463 N  NH2 . ARG B  73  ? 0.79123 0.95474 0.73825 0.08515  0.01136  -0.08874 73  ARG B NH2 
4477 N  N   . GLY B  74  ? 0.32896 0.45837 0.28385 0.07010  0.00155  -0.07256 74  GLY B N   
4478 C  CA  . GLY B  74  ? 0.32770 0.44633 0.28763 0.06766  0.00152  -0.06732 74  GLY B CA  
4479 C  C   . GLY B  74  ? 0.28494 0.38721 0.24751 0.06586  -0.00025 -0.07062 74  GLY B C   
4480 O  O   . GLY B  74  ? 0.30323 0.39514 0.26952 0.06406  -0.00009 -0.06762 74  GLY B O   
4484 N  N   . PHE B  75  ? 0.30108 0.40074 0.26168 0.06607  -0.00191 -0.07660 75  PHE B N   
4485 C  CA  . PHE B  75  ? 0.28512 0.36968 0.24802 0.06450  -0.00349 -0.08065 75  PHE B CA  
4486 C  C   . PHE B  75  ? 0.31298 0.39876 0.27252 0.06615  -0.00486 -0.08929 75  PHE B C   
4487 O  O   . PHE B  75  ? 0.31892 0.41647 0.27416 0.06845  -0.00447 -0.09211 75  PHE B O   
4488 C  CB  . PHE B  75  ? 0.28932 0.36612 0.25527 0.06031  -0.00454 -0.07376 75  PHE B CB  
4489 C  CG  . PHE B  75  ? 0.27667 0.36172 0.24109 0.05890  -0.00577 -0.06978 75  PHE B CG  
4490 C  CD1 . PHE B  75  ? 0.27455 0.37227 0.23723 0.05887  -0.00502 -0.06318 75  PHE B CD1 
4491 C  CD2 . PHE B  75  ? 0.27568 0.35550 0.24075 0.05743  -0.00779 -0.07232 75  PHE B CD2 
4492 C  CE1 . PHE B  75  ? 0.28351 0.38844 0.24486 0.05752  -0.00638 -0.05931 75  PHE B CE1 
4493 C  CE2 . PHE B  75  ? 0.26249 0.34966 0.22678 0.05615  -0.00915 -0.06840 75  PHE B CE2 
4494 C  CZ  . PHE B  75  ? 0.26747 0.36716 0.22978 0.05620  -0.00855 -0.06185 75  PHE B CZ  
4504 N  N   . GLY B  76  ? 0.29424 0.36746 0.25550 0.06471  -0.00644 -0.09350 76  GLY B N   
4505 C  CA  . GLY B  76  ? 0.31312 0.38539 0.27140 0.06613  -0.00779 -0.10239 76  GLY B CA  
4506 C  C   . GLY B  76  ? 0.32807 0.40274 0.28532 0.06404  -0.01013 -0.10212 76  GLY B C   
4507 O  O   . GLY B  76  ? 0.35659 0.42657 0.31261 0.06401  -0.01179 -0.10892 76  GLY B O   
4511 N  N   . GLY B  77  ? 0.29534 0.37776 0.25303 0.06229  -0.01043 -0.09429 77  GLY B N   
4512 C  CA  . GLY B  77  ? 0.29661 0.38169 0.25415 0.06026  -0.01281 -0.09306 77  GLY B CA  
4513 C  C   . GLY B  77  ? 0.28039 0.35343 0.24343 0.05705  -0.01359 -0.08942 77  GLY B C   
4514 O  O   . GLY B  77  ? 0.28558 0.34799 0.25190 0.05614  -0.01229 -0.08775 77  GLY B O   
4518 N  N   . GLY B  78  ? 0.28701 0.36162 0.25112 0.05520  -0.01571 -0.08806 78  GLY B N   
4519 C  CA  . GLY B  78  ? 0.28361 0.34767 0.25325 0.05223  -0.01612 -0.08408 78  GLY B CA  
4520 C  C   . GLY B  78  ? 0.26454 0.33322 0.23565 0.05058  -0.01852 -0.08191 78  GLY B C   
4521 O  O   . GLY B  78  ? 0.27398 0.35375 0.24148 0.05149  -0.02027 -0.08378 78  GLY B O   
4525 N  N   . THR B  79  ? 0.26047 0.32035 0.23702 0.04806  -0.01852 -0.07768 79  THR B N   
4526 C  CA  . THR B  79  ? 0.24135 0.30433 0.22101 0.04636  -0.02058 -0.07448 79  THR B CA  
4527 C  C   . THR B  79  ? 0.22829 0.29030 0.21167 0.04469  -0.01929 -0.06460 79  THR B C   
4528 O  O   . THR B  79  ? 0.23775 0.28819 0.22411 0.04337  -0.01723 -0.06226 79  THR B O   
4529 C  CB  . THR B  79  ? 0.25386 0.30575 0.23739 0.04488  -0.02164 -0.07953 79  THR B CB  
4530 O  OG1 . THR B  79  ? 0.30947 0.36052 0.28916 0.04634  -0.02264 -0.08901 79  THR B OG1 
4531 C  CG2 . THR B  79  ? 0.27357 0.33014 0.26072 0.04337  -0.02402 -0.07655 79  THR B CG2 
4539 N  N   . ILE B  80  ? 0.23400 0.30789 0.21682 0.04461  -0.02056 -0.05878 80  ILE B N   
4540 C  CA  . ILE B  80  ? 0.21665 0.28993 0.20300 0.04301  -0.01957 -0.04922 80  ILE B CA  
4541 C  C   . ILE B  80  ? 0.21788 0.28688 0.21021 0.04130  -0.02097 -0.04745 80  ILE B C   
4542 O  O   . ILE B  80  ? 0.23179 0.30777 0.22424 0.04151  -0.02377 -0.04998 80  ILE B O   
4543 C  CB  . ILE B  80  ? 0.22458 0.31254 0.20742 0.04373  -0.02016 -0.04329 80  ILE B CB  
4544 C  CG1 . ILE B  80  ? 0.22972 0.32394 0.20664 0.04569  -0.01881 -0.04565 80  ILE B CG1 
4545 C  CG2 . ILE B  80  ? 0.25545 0.34156 0.24162 0.04206  -0.01890 -0.03333 80  ILE B CG2 
4546 C  CD1 . ILE B  80  ? 0.25138 0.36113 0.22416 0.04635  -0.01950 -0.04063 80  ILE B CD1 
4558 N  N   . TYR B  81  ? 0.21274 0.27040 0.20998 0.03953  -0.01899 -0.04309 81  TYR B N   
4559 C  CA  . TYR B  81  ? 0.19583 0.24893 0.19965 0.03793  -0.01952 -0.03979 81  TYR B CA  
4560 C  C   . TYR B  81  ? 0.19821 0.25405 0.20387 0.03714  -0.01845 -0.02971 81  TYR B C   
4561 O  O   . TYR B  81  ? 0.19831 0.24946 0.20231 0.03663  -0.01596 -0.02594 81  TYR B O   
4562 C  CB  . TYR B  81  ? 0.20672 0.24288 0.21443 0.03639  -0.01740 -0.04282 81  TYR B CB  
4563 C  CG  . TYR B  81  ? 0.20572 0.23689 0.21197 0.03686  -0.01825 -0.05265 81  TYR B CG  
4564 C  CD1 . TYR B  81  ? 0.23049 0.25874 0.23186 0.03788  -0.01724 -0.05737 81  TYR B CD1 
4565 C  CD2 . TYR B  81  ? 0.24248 0.27201 0.25229 0.03627  -0.02010 -0.05698 81  TYR B CD2 
4566 C  CE1 . TYR B  81  ? 0.24093 0.26414 0.24077 0.03840  -0.01799 -0.06630 81  TYR B CE1 
4567 C  CE2 . TYR B  81  ? 0.25135 0.27619 0.25941 0.03655  -0.02095 -0.06588 81  TYR B CE2 
4568 C  CZ  . TYR B  81  ? 0.29373 0.31507 0.29663 0.03767  -0.01984 -0.07059 81  TYR B CZ  
4569 O  OH  . TYR B  81  ? 0.29311 0.30920 0.29419 0.03801  -0.02069 -0.07943 81  TYR B OH  
4579 N  N   . TYR B  82  ? 0.19636 0.25983 0.20532 0.03695  -0.02044 -0.02510 82  TYR B N   
4580 C  CA  . TYR B  82  ? 0.20077 0.26739 0.21121 0.03634  -0.01963 -0.01533 82  TYR B CA  
4581 C  C   . TYR B  82  ? 0.19617 0.26369 0.21358 0.03568  -0.02099 -0.01094 82  TYR B C   
4582 O  O   . TYR B  82  ? 0.20325 0.27604 0.22280 0.03603  -0.02385 -0.01457 82  TYR B O   
4583 C  CB  . TYR B  82  ? 0.21595 0.29744 0.22021 0.03750  -0.02095 -0.01229 82  TYR B CB  
4584 C  CG  . TYR B  82  ? 0.20047 0.29534 0.20241 0.03858  -0.02464 -0.01549 82  TYR B CG  
4585 C  CD1 . TYR B  82  ? 0.22502 0.32318 0.22220 0.03979  -0.02573 -0.02423 82  TYR B CD1 
4586 C  CD2 . TYR B  82  ? 0.21008 0.31435 0.21435 0.03831  -0.02722 -0.00984 82  TYR B CD2 
4587 C  CE1 . TYR B  82  ? 0.25442 0.36400 0.24893 0.04042  -0.02911 -0.02730 82  TYR B CE1 
4588 C  CE2 . TYR B  82  ? 0.24095 0.35700 0.24287 0.03888  -0.03087 -0.01271 82  TYR B CE2 
4589 C  CZ  . TYR B  82  ? 0.24255 0.36135 0.23912 0.03984  -0.03178 -0.02151 82  TYR B CZ  
4590 O  OH  . TYR B  82  ? 0.30100 0.43151 0.29456 0.04006  -0.03552 -0.02408 82  TYR B OH  
4600 N  N   . PRO B  83  ? 0.19098 0.25367 0.21214 0.03469  -0.01907 -0.00300 83  PRO B N   
4601 C  CA  . PRO B  83  ? 0.20321 0.26813 0.23141 0.03442  -0.02037 0.00209  83  PRO B CA  
4602 C  C   . PRO B  83  ? 0.22016 0.30169 0.24686 0.03533  -0.02412 0.00570  83  PRO B C   
4603 O  O   . PRO B  83  ? 0.24457 0.33466 0.26520 0.03581  -0.02457 0.00842  83  PRO B O   
4604 C  CB  . PRO B  83  ? 0.25670 0.31217 0.28780 0.03328  -0.01695 0.00997  83  PRO B CB  
4605 C  CG  . PRO B  83  ? 0.24955 0.29573 0.27570 0.03251  -0.01392 0.00794  83  PRO B CG  
4606 C  CD  . PRO B  83  ? 0.21977 0.27371 0.23920 0.03366  -0.01555 0.00162  83  PRO B CD  
4614 N  N   . VAL B  84  ? 0.21570 0.30167 0.24812 0.03540  -0.02682 0.00609  84  VAL B N   
4615 C  CA  . VAL B  84  ? 0.21686 0.31798 0.24867 0.03591  -0.03064 0.01059  84  VAL B CA  
4616 C  C   . VAL B  84  ? 0.30394 0.40534 0.34128 0.03564  -0.03017 0.02073  84  VAL B C   
4617 O  O   . VAL B  84  ? 0.29383 0.40760 0.33005 0.03594  -0.03313 0.02599  84  VAL B O   
4618 C  CB  . VAL B  84  ? 0.25152 0.35965 0.28552 0.03602  -0.03469 0.00547  84  VAL B CB  
4619 C  CG1 . VAL B  84  ? 0.31008 0.41788 0.33760 0.03635  -0.03510 -0.00470 84  VAL B CG1 
4620 C  CG2 . VAL B  84  ? 0.26648 0.36728 0.31058 0.03545  -0.03448 0.00617  84  VAL B CG2 
4630 N  N   . ASN B  85  ? 0.22719 0.31528 0.26997 0.03504  -0.02651 0.02367  85  ASN B N   
4631 C  CA  . ASN B  85  ? 0.29887 0.38455 0.34830 0.03489  -0.02553 0.03263  85  ASN B CA  
4632 C  C   . ASN B  85  ? 0.30794 0.38064 0.35660 0.03402  -0.02069 0.03677  85  ASN B C   
4633 O  O   . ASN B  85  ? 0.32534 0.38922 0.38058 0.03367  -0.01830 0.04148  85  ASN B O   
4634 C  CB  . ASN B  85  ? 0.28769 0.37029 0.34727 0.03499  -0.02629 0.03227  85  ASN B CB  
4635 C  CG  . ASN B  85  ? 0.27260 0.34030 0.33557 0.03427  -0.02306 0.02558  85  ASN B CG  
4636 O  OD1 . ASN B  85  ? 0.26792 0.32911 0.32515 0.03377  -0.02124 0.01967  85  ASN B OD1 
4637 N  ND2 . ASN B  85  ? 0.36053 0.42337 0.43308 0.03422  -0.02249 0.02668  85  ASN B ND2 
4644 N  N   . ALA B  86  ? 0.37272 0.44446 0.41338 0.03361  -0.01923 0.03566  86  ALA B N   
4645 C  CA  . ALA B  86  ? 0.28154 0.34235 0.32071 0.03243  -0.01518 0.04052  86  ALA B CA  
4646 C  C   . ALA B  86  ? 0.34286 0.41086 0.38067 0.03240  -0.01580 0.05012  86  ALA B C   
4647 O  O   . ALA B  86  ? 0.35412 0.43656 0.38893 0.03318  -0.01919 0.05203  86  ALA B O   
4648 C  CB  . ALA B  86  ? 0.50078 0.55679 0.53256 0.03177  -0.01334 0.03542  86  ALA B CB  
4654 N  N   . GLU B  87  ? 0.31307 0.37041 0.35266 0.03131  -0.01242 0.05622  87  GLU B N   
4655 C  CA  . GLU B  87  ? 0.29794 0.36022 0.33775 0.03124  -0.01285 0.06589  87  GLU B CA  
4656 C  C   . GLU B  87  ? 0.35741 0.42360 0.38871 0.03028  -0.01234 0.06935  87  GLU B C   
4657 O  O   . GLU B  87  ? 0.40119 0.47128 0.43188 0.02997  -0.01267 0.07759  87  GLU B O   
4658 C  CB  . GLU B  87  ? 0.34581 0.39490 0.39231 0.03065  -0.00950 0.07138  87  GLU B CB  
4659 C  CG  . GLU B  87  ? 0.34083 0.37266 0.38494 0.02870  -0.00459 0.07094  87  GLU B CG  
4660 C  CD  . GLU B  87  ? 0.46429 0.48411 0.51134 0.02826  -0.00237 0.06315  87  GLU B CD  
4661 O  OE1 . GLU B  87  ? 0.35263 0.37790 0.40015 0.02918  -0.00464 0.05584  87  GLU B OE1 
4662 O  OE2 . GLU B  87  ? 0.30543 0.30973 0.35383 0.02677  0.00178  0.06441  87  GLU B OE2 
4669 N  N   . GLY B  88  ? 0.28208 0.34790 0.30708 0.02985  -0.01169 0.06358  88  GLY B N   
4670 C  CA  . GLY B  88  ? 0.26365 0.33386 0.28105 0.02893  -0.01116 0.06675  88  GLY B CA  
4671 C  C   . GLY B  88  ? 0.24263 0.31347 0.25449 0.02901  -0.01078 0.05904  88  GLY B C   
4672 O  O   . GLY B  88  ? 0.25670 0.32436 0.27021 0.02976  -0.01105 0.05116  88  GLY B O   
4676 N  N   A THR B  89  ? 0.23276 0.30778 0.23820 0.02821  -0.01014 0.06154  89  THR B N   
4677 N  N   B THR B  89  ? 0.23516 0.30997 0.24062 0.02818  -0.01009 0.06166  89  THR B N   
4678 C  CA  A THR B  89  ? 0.24163 0.31782 0.24206 0.02845  -0.00963 0.05495  89  THR B CA  
4679 C  CA  B THR B  89  ? 0.23720 0.31311 0.23757 0.02837  -0.00953 0.05525  89  THR B CA  
4680 C  C   A THR B  89  ? 0.24141 0.30082 0.24337 0.02724  -0.00669 0.05075  89  THR B C   
4681 C  C   B THR B  89  ? 0.24316 0.30242 0.24512 0.02721  -0.00665 0.05081  89  THR B C   
4682 O  O   A THR B  89  ? 0.23843 0.28513 0.24317 0.02553  -0.00431 0.05479  89  THR B O   
4683 O  O   B THR B  89  ? 0.24132 0.28779 0.24597 0.02549  -0.00424 0.05478  89  THR B O   
4684 C  CB  A THR B  89  ? 0.25469 0.33853 0.24891 0.02766  -0.00930 0.05973  89  THR B CB  
4685 C  CB  B THR B  89  ? 0.24829 0.33130 0.24241 0.02751  -0.00907 0.05999  89  THR B CB  
4686 O  OG1 A THR B  89  ? 0.29862 0.39807 0.29113 0.02865  -0.01211 0.06341  89  THR B OG1 
4687 O  OG1 B THR B  89  ? 0.23128 0.30418 0.22522 0.02512  -0.00652 0.06710  89  THR B OG1 
4688 C  CG2 A THR B  89  ? 0.31156 0.39842 0.30102 0.02822  -0.00881 0.05354  89  THR B CG2 
4689 C  CG2 B THR B  89  ? 0.33108 0.43052 0.32305 0.02843  -0.01189 0.06428  89  THR B CG2 
4704 N  N   . MET B  90  ? 0.21323 0.27238 0.21329 0.02811  -0.00687 0.04247  90  MET B N   
4705 C  CA  . MET B  90  ? 0.22114 0.26518 0.22273 0.02714  -0.00469 0.03719  90  MET B CA  
4706 C  C   . MET B  90  ? 0.20399 0.24688 0.20055 0.02684  -0.00372 0.03352  90  MET B C   
4707 O  O   . MET B  90  ? 0.20383 0.25908 0.19622 0.02808  -0.00496 0.03288  90  MET B O   
4708 C  CB  . MET B  90  ? 0.22635 0.26946 0.23170 0.02861  -0.00608 0.02944  90  MET B CB  
4709 C  CG  . MET B  90  ? 0.22046 0.26179 0.23223 0.02870  -0.00664 0.03238  90  MET B CG  
4710 S  SD  . MET B  90  ? 0.24006 0.28707 0.25578 0.03067  -0.00967 0.02415  90  MET B SD  
4711 C  CE  . MET B  90  ? 0.24933 0.31742 0.26059 0.03254  -0.01354 0.02481  90  MET B CE  
4721 N  N   . ALA B  91  ? 0.20464 0.23258 0.20174 0.02517  -0.00147 0.03114  91  ALA B N   
4722 C  CA  . ALA B  91  ? 0.19250 0.21805 0.18602 0.02511  -0.00088 0.02627  91  ALA B CA  
4723 C  C   . ALA B  91  ? 0.20578 0.23652 0.19950 0.02764  -0.00268 0.01690  91  ALA B C   
4724 O  O   . ALA B  91  ? 0.20582 0.23641 0.20309 0.02863  -0.00387 0.01324  91  ALA B O   
4725 C  CB  . ALA B  91  ? 0.20550 0.21295 0.19952 0.02233  0.00176  0.02641  91  ALA B CB  
4731 N  N   . ALA B  92  ? 0.19378 0.25559 0.20508 0.03685  -0.00138 0.00938  92  ALA B N   
4732 C  CA  . ALA B  92  ? 0.17807 0.24197 0.19108 0.03927  -0.00175 0.00339  92  ALA B CA  
4733 C  C   . ALA B  92  ? 0.19254 0.24839 0.20676 0.03938  -0.00153 0.00145  92  ALA B C   
4734 O  O   . ALA B  92  ? 0.19653 0.24957 0.20988 0.03810  -0.00106 0.00451  92  ALA B O   
4735 C  CB  . ALA B  92  ? 0.21188 0.28754 0.22390 0.04119  -0.00196 0.00165  92  ALA B CB  
4741 N  N   . ILE B  93  ? 0.18869 0.24046 0.20477 0.04054  -0.00223 -0.00332 93  ILE B N   
4742 C  CA  . ILE B  93  ? 0.19170 0.23500 0.20899 0.04040  -0.00254 -0.00539 93  ILE B CA  
4743 C  C   . ILE B  93  ? 0.17792 0.22317 0.19651 0.04311  -0.00403 -0.01143 93  ILE B C   
4744 O  O   . ILE B  93  ? 0.19623 0.24435 0.21515 0.04414  -0.00495 -0.01443 93  ILE B O   
4745 C  CB  . ILE B  93  ? 0.17224 0.20551 0.19036 0.03823  -0.00220 -0.00459 93  ILE B CB  
4746 C  CG1 . ILE B  93  ? 0.18597 0.21634 0.20240 0.03603  -0.00080 0.00086  93  ILE B CG1 
4747 C  CG2 . ILE B  93  ? 0.19569 0.22046 0.21470 0.03771  -0.00282 -0.00668 93  ILE B CG2 
4748 C  CD1 . ILE B  93  ? 0.19762 0.21961 0.21483 0.03435  0.00005  0.00163  93  ILE B CD1 
4760 N  N   . VAL B  94  ? 0.17610 0.21952 0.19535 0.04432  -0.00458 -0.01322 94  VAL B N   
4761 C  CA  . VAL B  94  ? 0.18325 0.22600 0.20373 0.04705  -0.00641 -0.01916 94  VAL B CA  
4762 C  C   . VAL B  94  ? 0.19040 0.22124 0.21221 0.04541  -0.00762 -0.02009 94  VAL B C   
4763 O  O   . VAL B  94  ? 0.20808 0.23327 0.22981 0.04338  -0.00697 -0.01676 94  VAL B O   
4764 C  CB  . VAL B  94  ? 0.19723 0.24772 0.21783 0.05021  -0.00636 -0.02083 94  VAL B CB  
4765 C  CG1 . VAL B  94  ? 0.20950 0.25657 0.23154 0.05316  -0.00851 -0.02672 94  VAL B CG1 
4766 C  CG2 . VAL B  94  ? 0.20745 0.27029 0.22638 0.05188  -0.00543 -0.02101 94  VAL B CG2 
4776 N  N   . VAL B  95  ? 0.18843 0.21537 0.21111 0.04601  -0.00962 -0.02442 95  VAL B N   
4777 C  CA  . VAL B  95  ? 0.19331 0.20932 0.21717 0.04432  -0.01132 -0.02569 95  VAL B CA  
4778 C  C   . VAL B  95  ? 0.20950 0.22442 0.23412 0.04743  -0.01412 -0.03117 95  VAL B C   
4779 O  O   . VAL B  95  ? 0.21822 0.23764 0.24239 0.05001  -0.01545 -0.03539 95  VAL B O   
4780 C  CB  . VAL B  95  ? 0.20181 0.21337 0.22625 0.04174  -0.01171 -0.02559 95  VAL B CB  
4781 C  CG1 . VAL B  95  ? 0.21775 0.21824 0.24307 0.03903  -0.01300 -0.02553 95  VAL B CG1 
4782 C  CG2 . VAL B  95  ? 0.20636 0.22087 0.23026 0.03980  -0.00901 -0.02092 95  VAL B CG2 
4792 N  N   . ILE B  96  ? 0.21000 0.21853 0.23555 0.04724  -0.01527 -0.03120 96  ILE B N   
4793 C  CA  . ILE B  96  ? 0.23550 0.24276 0.26207 0.05072  -0.01805 -0.03613 96  ILE B CA  
4794 C  C   . ILE B  96  ? 0.23177 0.22676 0.25929 0.04859  -0.02102 -0.03717 96  ILE B C   
4795 O  O   . ILE B  96  ? 0.23054 0.21900 0.25806 0.04486  -0.02030 -0.03309 96  ILE B O   
4796 C  CB  . ILE B  96  ? 0.21644 0.23018 0.24377 0.05347  -0.01688 -0.03520 96  ILE B CB  
4797 C  CG1 . ILE B  96  ? 0.23477 0.24819 0.26358 0.05797  -0.01963 -0.04073 96  ILE B CG1 
4798 C  CG2 . ILE B  96  ? 0.22341 0.23203 0.25113 0.05014  -0.01583 -0.02977 96  ILE B CG2 
4799 C  CD1 . ILE B  96  ? 0.24708 0.26880 0.27745 0.06127  -0.01836 -0.04008 96  ILE B CD1 
4811 N  N   . PRO B  97  ? 0.23312 0.22438 0.26102 0.05066  -0.02462 -0.04256 97  PRO B N   
4812 C  CA  . PRO B  97  ? 0.24225 0.22164 0.27093 0.04848  -0.02814 -0.04357 97  PRO B CA  
4813 C  C   . PRO B  97  ? 0.24991 0.22547 0.28006 0.05029  -0.02989 -0.04411 97  PRO B C   
4814 O  O   . PRO B  97  ? 0.25359 0.23582 0.28450 0.05267  -0.02787 -0.04276 97  PRO B O   
4815 C  CB  . PRO B  97  ? 0.28177 0.25935 0.30986 0.05005  -0.03158 -0.04902 97  PRO B CB  
4816 C  CG  . PRO B  97  ? 0.27276 0.26063 0.30006 0.05547  -0.03069 -0.05271 97  PRO B CG  
4817 C  CD  . PRO B  97  ? 0.25620 0.25366 0.28318 0.05475  -0.02582 -0.04789 97  PRO B CD  
4825 N  N   . GLY B  98  ? 0.28644 0.25131 0.31722 0.04899  -0.03395 -0.04582 98  GLY B N   
4826 C  CA  . GLY B  98  ? 0.29438 0.25389 0.32683 0.05009  -0.03631 -0.04597 98  GLY B CA  
4827 C  C   . GLY B  98  ? 0.29247 0.24989 0.32599 0.05511  -0.04062 -0.05238 98  GLY B C   
4828 O  O   . GLY B  98  ? 0.31062 0.27176 0.34311 0.05829  -0.04148 -0.05708 98  GLY B O   
4832 N  N   . TYR B  99  ? 0.30380 0.25466 0.33922 0.05584  -0.04358 -0.05256 99  TYR B N   
4833 C  CA  . TYR B  99  ? 0.30147 0.24865 0.33828 0.06085  -0.04820 -0.05849 99  TYR B CA  
4834 C  C   . TYR B  99  ? 0.33167 0.27111 0.36658 0.06004  -0.05241 -0.06267 99  TYR B C   
4835 O  O   . TYR B  99  ? 0.38210 0.31319 0.41591 0.05430  -0.05402 -0.06014 99  TYR B O   
4836 C  CB  . TYR B  99  ? 0.33244 0.27154 0.37162 0.05991  -0.05110 -0.05648 99  TYR B CB  
4837 C  CG  . TYR B  99  ? 0.39904 0.33474 0.44062 0.06564  -0.05571 -0.06181 99  TYR B CG  
4838 C  CD1 . TYR B  99  ? 0.37383 0.31985 0.41750 0.07271  -0.05420 -0.06529 99  TYR B CD1 
4839 C  CD2 . TYR B  99  ? 0.50415 0.42628 0.54604 0.06396  -0.06168 -0.06312 99  TYR B CD2 
4840 C  CE1 . TYR B  99  ? 0.43074 0.37365 0.47693 0.07855  -0.05837 -0.07042 99  TYR B CE1 
4841 C  CE2 . TYR B  99  ? 0.49887 0.41702 0.54310 0.06947  -0.06631 -0.06802 99  TYR B CE2 
4842 C  CZ  . TYR B  99  ? 0.51650 0.44508 0.56299 0.07700  -0.06452 -0.07179 99  TYR B CZ  
4843 O  OH  . TYR B  99  ? 0.58704 0.51148 0.63608 0.08297  -0.06915 -0.07695 99  TYR B OH  
4853 N  N   . MET B  100 ? 0.35804 0.30035 0.39244 0.06580  -0.05432 -0.06910 100 MET B N   
4854 C  CA  . MET B  100 ? 0.39375 0.32828 0.42604 0.06583  -0.05918 -0.07387 100 MET B CA  
4855 C  C   . MET B  100 ? 0.41705 0.35245 0.44699 0.06091  -0.05777 -0.07184 100 MET B C   
4856 O  O   . MET B  100 ? 0.48681 0.41374 0.51533 0.05833  -0.06210 -0.07361 100 MET B O   
4857 C  CB  . MET B  100 ? 0.48930 0.40923 0.52251 0.06379  -0.06539 -0.07437 100 MET B CB  
4858 C  CG  . MET B  100 ? 0.51649 0.43503 0.55257 0.06917  -0.06753 -0.07676 100 MET B CG  
4859 S  SD  . MET B  100 ? 0.59720 0.52266 0.63287 0.07921  -0.06843 -0.08563 100 MET B SD  
4860 C  CE  . MET B  100 ? 0.62409 0.53546 0.65645 0.07834  -0.07603 -0.09102 100 MET B CE  
4870 N  N   . SER B  101 ? 0.35707 0.30279 0.38671 0.05969  -0.05209 -0.06820 101 SER B N   
4871 C  CA  A SER B  101 ? 0.36754 0.31514 0.39564 0.05531  -0.05040 -0.06585 101 SER B CA  
4872 C  CA  B SER B  101 ? 0.37113 0.31864 0.39921 0.05533  -0.05047 -0.06592 101 SER B CA  
4873 C  C   . SER B  101 ? 0.36435 0.32438 0.39097 0.05852  -0.04680 -0.06738 101 SER B C   
4874 O  O   . SER B  101 ? 0.34238 0.31129 0.36931 0.06293  -0.04400 -0.06823 101 SER B O   
4875 C  CB  A SER B  101 ? 0.35193 0.29835 0.38094 0.04933  -0.04712 -0.05877 101 SER B CB  
4876 C  CB  B SER B  101 ? 0.35074 0.29684 0.37972 0.04923  -0.04730 -0.05885 101 SER B CB  
4877 O  OG  A SER B  101 ? 0.38291 0.31772 0.41264 0.04557  -0.05057 -0.05715 101 SER B OG  
4878 O  OG  B SER B  101 ? 0.37391 0.32870 0.40354 0.05045  -0.04228 -0.05548 101 SER B OG  
4889 N  N   . TYR B  102 ? 0.34148 0.30247 0.36660 0.05598  -0.04700 -0.06738 102 TYR B N   
4890 C  CA  . TYR B  102 ? 0.35498 0.32687 0.37836 0.05817  -0.04420 -0.06851 102 TYR B CA  
4891 C  C   . TYR B  102 ? 0.33756 0.31484 0.36164 0.05388  -0.03984 -0.06242 102 TYR B C   
4892 O  O   . TYR B  102 ? 0.33371 0.30594 0.35931 0.04914  -0.03905 -0.05780 102 TYR B O   
4893 C  CB  . TYR B  102 ? 0.38519 0.35439 0.40600 0.05915  -0.04838 -0.07379 102 TYR B CB  
4894 C  CG  . TYR B  102 ? 0.34509 0.30938 0.36445 0.06434  -0.05273 -0.08065 102 TYR B CG  
4895 C  CD1 . TYR B  102 ? 0.38858 0.36104 0.40589 0.07052  -0.05153 -0.08535 102 TYR B CD1 
4896 C  CD2 . TYR B  102 ? 0.43674 0.38815 0.45656 0.06306  -0.05817 -0.08249 102 TYR B CD2 
4897 C  CE1 . TYR B  102 ? 0.45548 0.42339 0.47133 0.07594  -0.05544 -0.09217 102 TYR B CE1 
4898 C  CE2 . TYR B  102 ? 0.50868 0.45479 0.52710 0.06821  -0.06255 -0.08903 102 TYR B CE2 
4899 C  CZ  . TYR B  102 ? 0.48964 0.44405 0.50614 0.07486  -0.06102 -0.09399 102 TYR B CZ  
4900 O  OH  . TYR B  102 ? 0.57358 0.52263 0.58861 0.08059  -0.06527 -0.10095 102 TYR B OH  
4910 N  N   . GLN B  103 ? 0.31420 0.30198 0.33688 0.05584  -0.03706 -0.06266 103 GLN B N   
4911 C  CA  . GLN B  103 ? 0.31509 0.30917 0.33826 0.05278  -0.03306 -0.05738 103 GLN B CA  
4912 C  C   . GLN B  103 ? 0.32232 0.31058 0.34675 0.04742  -0.03399 -0.05445 103 GLN B C   
4913 O  O   . GLN B  103 ? 0.31702 0.30613 0.34284 0.04418  -0.03084 -0.04918 103 GLN B O   
4914 C  CB  . GLN B  103 ? 0.44721 0.45167 0.46801 0.05590  -0.03198 -0.05982 103 GLN B CB  
4915 C  CG  . GLN B  103 ? 0.38910 0.40040 0.41000 0.05357  -0.02891 -0.05556 103 GLN B CG  
4916 C  CD  . GLN B  103 ? 0.30462 0.32524 0.32276 0.05606  -0.02871 -0.05812 103 GLN B CD  
4917 O  OE1 . GLN B  103 ? 0.31420 0.34015 0.33243 0.05407  -0.02684 -0.05476 103 GLN B OE1 
4918 N  NE2 . GLN B  103 ? 0.39475 0.41719 0.41032 0.06045  -0.03061 -0.06400 103 GLN B NE2 
4927 N  N   . SER B  104 ? 0.31057 0.29293 0.33452 0.04639  -0.03836 -0.05774 104 SER B N   
4928 C  CA  . SER B  104 ? 0.28716 0.26541 0.31272 0.04117  -0.03932 -0.05485 104 SER B CA  
4929 C  C   . SER B  104 ? 0.29563 0.26715 0.32320 0.03721  -0.03821 -0.05049 104 SER B C   
4930 O  O   . SER B  104 ? 0.31788 0.28905 0.34715 0.03297  -0.03673 -0.04651 104 SER B O   
4931 C  CB  . SER B  104 ? 0.36297 0.33538 0.38744 0.04055  -0.04496 -0.05917 104 SER B CB  
4932 O  OG  . SER B  104 ? 0.42613 0.38942 0.44989 0.04181  -0.04890 -0.06254 104 SER B OG  
4938 N  N   . SER B  105 ? 0.29596 0.26244 0.32338 0.03845  -0.03880 -0.05102 105 SER B N   
4939 C  CA  . SER B  105 ? 0.30275 0.26228 0.33139 0.03438  -0.03804 -0.04689 105 SER B CA  
4940 C  C   . SER B  105 ? 0.29324 0.25754 0.32245 0.03254  -0.03259 -0.04141 105 SER B C   
4941 O  O   . SER B  105 ? 0.30878 0.26793 0.33859 0.02842  -0.03153 -0.03771 105 SER B O   
4942 C  CB  . SER B  105 ? 0.32984 0.28306 0.35824 0.03620  -0.04017 -0.04847 105 SER B CB  
4943 O  OG  . SER B  105 ? 0.33980 0.29977 0.36792 0.04031  -0.03723 -0.04849 105 SER B OG  
4949 N  N   . ILE B  106 ? 0.25382 0.22745 0.28250 0.03536  -0.02927 -0.04077 106 ILE B N   
4950 C  CA  . ILE B  106 ? 0.25646 0.23405 0.28527 0.03389  -0.02454 -0.03567 106 ILE B CA  
4951 C  C   . ILE B  106 ? 0.22951 0.21520 0.25877 0.03393  -0.02246 -0.03444 106 ILE B C   
4952 O  O   . ILE B  106 ? 0.23462 0.22485 0.26369 0.03375  -0.01881 -0.03076 106 ILE B O   
4953 C  CB  . ILE B  106 ? 0.24764 0.22779 0.27546 0.03622  -0.02236 -0.03427 106 ILE B CB  
4954 C  CG1 . ILE B  106 ? 0.25682 0.24405 0.28392 0.04126  -0.02310 -0.03807 106 ILE B CG1 
4955 C  CG2 . ILE B  106 ? 0.28917 0.26011 0.31703 0.03461  -0.02387 -0.03355 106 ILE B CG2 
4956 C  CD1 . ILE B  106 ? 0.23717 0.23442 0.26353 0.04306  -0.02163 -0.03869 106 ILE B CD1 
4968 N  N   . SER B  107 ? 0.25576 0.24244 0.28561 0.03376  -0.02511 -0.03715 107 SER B N   
4969 C  CA  . SER B  107 ? 0.24270 0.23744 0.27303 0.03418  -0.02394 -0.03650 107 SER B CA  
4970 C  C   . SER B  107 ? 0.23450 0.23075 0.26680 0.03122  -0.02061 -0.03144 107 SER B C   
4971 O  O   . SER B  107 ? 0.24065 0.24427 0.27319 0.03219  -0.01856 -0.02967 107 SER B O   
4972 C  CB  . SER B  107 ? 0.28710 0.28131 0.31744 0.03418  -0.02817 -0.04050 107 SER B CB  
4973 O  OG  . SER B  107 ? 0.32950 0.31681 0.36179 0.03013  -0.03029 -0.03967 107 SER B OG  
4979 N  N   . PHE B  108 ? 0.22985 0.21951 0.26345 0.02773  -0.02011 -0.02913 108 PHE B N   
4980 C  CA  . PHE B  108 ? 0.22913 0.22007 0.26437 0.02542  -0.01646 -0.02454 108 PHE B CA  
4981 C  C   . PHE B  108 ? 0.22093 0.21695 0.25489 0.02746  -0.01284 -0.02182 108 PHE B C   
4982 O  O   . PHE B  108 ? 0.21300 0.21377 0.24835 0.02731  -0.01067 -0.01924 108 PHE B O   
4983 C  CB  . PHE B  108 ? 0.22067 0.20331 0.25584 0.02211  -0.01579 -0.02261 108 PHE B CB  
4984 C  CG  . PHE B  108 ? 0.20910 0.19171 0.24454 0.02046  -0.01141 -0.01817 108 PHE B CG  
4985 C  CD1 . PHE B  108 ? 0.22614 0.21075 0.26451 0.01819  -0.00998 -0.01614 108 PHE B CD1 
4986 C  CD2 . PHE B  108 ? 0.21700 0.19740 0.24982 0.02111  -0.00887 -0.01605 108 PHE B CD2 
4987 C  CE1 . PHE B  108 ? 0.21822 0.20236 0.25653 0.01720  -0.00587 -0.01254 108 PHE B CE1 
4988 C  CE2 . PHE B  108 ? 0.21698 0.19615 0.24923 0.01975  -0.00507 -0.01232 108 PHE B CE2 
4989 C  CZ  . PHE B  108 ? 0.22833 0.20913 0.26326 0.01792  -0.00350 -0.01079 108 PHE B CZ  
4999 N  N   . TRP B  109 ? 0.20414 0.19927 0.23563 0.02931  -0.01241 -0.02215 109 TRP B N   
5000 C  CA  . TRP B  109 ? 0.20212 0.20087 0.23205 0.03052  -0.00933 -0.01899 109 TRP B CA  
5001 C  C   . TRP B  109 ? 0.19680 0.20496 0.22657 0.03297  -0.00905 -0.01915 109 TRP B C   
5002 O  O   . TRP B  109 ? 0.20165 0.21292 0.23067 0.03320  -0.00662 -0.01569 109 TRP B O   
5003 C  CB  . TRP B  109 ? 0.18820 0.18362 0.21595 0.03146  -0.00951 -0.01925 109 TRP B CB  
5004 C  CG  . TRP B  109 ? 0.19789 0.18412 0.22516 0.02853  -0.00911 -0.01760 109 TRP B CG  
5005 C  CD1 . TRP B  109 ? 0.20907 0.18842 0.23658 0.02728  -0.01170 -0.01972 109 TRP B CD1 
5006 C  CD2 . TRP B  109 ? 0.19716 0.17966 0.22324 0.02625  -0.00609 -0.01342 109 TRP B CD2 
5007 N  NE1 . TRP B  109 ? 0.21515 0.18722 0.24165 0.02410  -0.01039 -0.01689 109 TRP B NE1 
5008 C  CE2 . TRP B  109 ? 0.19583 0.16964 0.22122 0.02352  -0.00681 -0.01318 109 TRP B CE2 
5009 C  CE3 . TRP B  109 ? 0.21922 0.20456 0.24442 0.02632  -0.00306 -0.00993 109 TRP B CE3 
5010 C  CZ2 . TRP B  109 ? 0.23008 0.19817 0.25353 0.02085  -0.00431 -0.00974 109 TRP B CZ2 
5011 C  CZ3 . TRP B  109 ? 0.24081 0.21999 0.26421 0.02400  -0.00068 -0.00673 109 TRP B CZ3 
5012 C  CH2 . TRP B  109 ? 0.22380 0.19459 0.24613 0.02129  -0.00118 -0.00674 109 TRP B CH2 
5023 N  N   . GLY B  110 ? 0.20130 0.21352 0.23132 0.03460  -0.01166 -0.02290 110 GLY B N   
5024 C  CA  . GLY B  110 ? 0.20451 0.22570 0.23385 0.03661  -0.01158 -0.02305 110 GLY B CA  
5025 C  C   . GLY B  110 ? 0.20212 0.22662 0.23349 0.03528  -0.01023 -0.01978 110 GLY B C   
5026 O  O   . GLY B  110 ? 0.20815 0.23650 0.23881 0.03574  -0.00815 -0.01640 110 GLY B O   
5030 N  N   . PRO B  111 ? 0.19343 0.21641 0.22759 0.03354  -0.01162 -0.02052 111 PRO B N   
5031 C  CA  . PRO B  111 ? 0.20435 0.23096 0.24134 0.03252  -0.01038 -0.01737 111 PRO B CA  
5032 C  C   . PRO B  111 ? 0.18643 0.20958 0.22416 0.03141  -0.00695 -0.01324 111 PRO B C   
5033 O  O   . PRO B  111 ? 0.19393 0.22073 0.23267 0.03187  -0.00530 -0.01014 111 PRO B O   
5034 C  CB  . PRO B  111 ? 0.21247 0.23764 0.25254 0.03056  -0.01282 -0.01914 111 PRO B CB  
5035 C  CG  . PRO B  111 ? 0.24922 0.27190 0.28710 0.03127  -0.01618 -0.02388 111 PRO B CG  
5036 C  CD  . PRO B  111 ? 0.20182 0.22080 0.23675 0.03262  -0.01490 -0.02433 111 PRO B CD  
5044 N  N   . ARG B  112 ? 0.19071 0.20639 0.22778 0.02992  -0.00601 -0.01309 112 ARG B N   
5045 C  CA  . ARG B  112 ? 0.18704 0.19873 0.22422 0.02872  -0.00275 -0.00949 112 ARG B CA  
5046 C  C   . ARG B  112 ? 0.18448 0.19758 0.21883 0.03025  -0.00087 -0.00678 112 ARG B C   
5047 O  O   . ARG B  112 ? 0.19583 0.20929 0.23071 0.03034  0.00129  -0.00367 112 ARG B O   
5048 C  CB  . ARG B  112 ? 0.20284 0.20612 0.23903 0.02653  -0.00244 -0.00996 112 ARG B CB  
5049 C  CG  . ARG B  112 ? 0.18920 0.18768 0.22487 0.02502  0.00101  -0.00662 112 ARG B CG  
5050 C  CD  . ARG B  112 ? 0.18959 0.19179 0.22912 0.02471  0.00271  -0.00483 112 ARG B CD  
5051 N  NE  . ARG B  112 ? 0.19906 0.19606 0.23813 0.02313  0.00596  -0.00256 112 ARG B NE  
5052 C  CZ  . ARG B  112 ? 0.20167 0.19493 0.24190 0.02038  0.00638  -0.00286 112 ARG B CZ  
5053 N  NH1 . ARG B  112 ? 0.21929 0.21282 0.26155 0.01865  0.00343  -0.00510 112 ARG B NH1 
5054 N  NH2 . ARG B  112 ? 0.20125 0.19006 0.24011 0.01920  0.00969  -0.00082 112 ARG B NH2 
5068 N  N   . LEU B  113 ? 0.18208 0.19604 0.21342 0.03151  -0.00178 -0.00784 113 LEU B N   
5069 C  CA  . LEU B  113 ? 0.18082 0.19694 0.20947 0.03254  -0.00044 -0.00487 113 LEU B CA  
5070 C  C   . LEU B  113 ? 0.17222 0.19690 0.20153 0.03403  -0.00108 -0.00395 113 LEU B C   
5071 O  O   . LEU B  113 ? 0.18678 0.21255 0.21547 0.03419  0.00020  -0.00039 113 LEU B O   
5072 C  CB  . LEU B  113 ? 0.18827 0.20353 0.21407 0.03319  -0.00111 -0.00587 113 LEU B CB  
5073 C  CG  . LEU B  113 ? 0.21266 0.21920 0.23706 0.03154  -0.00038 -0.00532 113 LEU B CG  
5074 C  CD1 . LEU B  113 ? 0.21671 0.22355 0.23982 0.03260  -0.00192 -0.00745 113 LEU B CD1 
5075 C  CD2 . LEU B  113 ? 0.23695 0.23990 0.25895 0.03053  0.00191  -0.00091 113 LEU B CD2 
5087 N  N   . ALA B  114 ? 0.17863 0.20904 0.20882 0.03505  -0.00332 -0.00706 114 ALA B N   
5088 C  CA  . ALA B  114 ? 0.18475 0.22343 0.21478 0.03621  -0.00414 -0.00605 114 ALA B CA  
5089 C  C   . ALA B  114 ? 0.17981 0.21947 0.21279 0.03567  -0.00345 -0.00316 114 ALA B C   
5090 O  O   . ALA B  114 ? 0.18186 0.22600 0.21427 0.03627  -0.00343 -0.00031 114 ALA B O   
5091 C  CB  . ALA B  114 ? 0.19192 0.23578 0.22180 0.03728  -0.00675 -0.01025 114 ALA B CB  
5097 N  N   . SER B  115 ? 0.17364 0.20984 0.21009 0.03456  -0.00318 -0.00384 115 SER B N   
5098 C  CA  . SER B  115 ? 0.17274 0.21057 0.21300 0.03436  -0.00245 -0.00140 115 SER B CA  
5099 C  C   . SER B  115 ? 0.16395 0.19795 0.20345 0.03461  0.00022  0.00242  115 SER B C   
5100 O  O   . SER B  115 ? 0.17419 0.20977 0.21674 0.03512  0.00095  0.00468  115 SER B O   
5101 C  CB  . SER B  115 ? 0.20104 0.23716 0.24538 0.03290  -0.00288 -0.00314 115 SER B CB  
5102 O  OG  . SER B  115 ? 0.18987 0.21849 0.23380 0.03153  -0.00095 -0.00320 115 SER B OG  
5108 N  N   . HIS B  116 ? 0.17222 0.20114 0.20768 0.03439  0.00147  0.00321  116 HIS B N   
5109 C  CA  . HIS B  116 ? 0.16952 0.19418 0.20285 0.03460  0.00344  0.00682  116 HIS B CA  
5110 C  C   . HIS B  116 ? 0.20128 0.22916 0.23100 0.03525  0.00244  0.00910  116 HIS B C   
5111 O  O   . HIS B  116 ? 0.22163 0.24513 0.24849 0.03509  0.00347  0.01209  116 HIS B O   
5112 C  CB  . HIS B  116 ? 0.17497 0.19076 0.20607 0.03328  0.00542  0.00668  116 HIS B CB  
5113 C  CG  . HIS B  116 ? 0.15992 0.17234 0.19414 0.03254  0.00717  0.00619  116 HIS B CG  
5114 N  ND1 . HIS B  116 ? 0.18609 0.19647 0.22142 0.03328  0.00931  0.00854  116 HIS B ND1 
5115 C  CD2 . HIS B  116 ? 0.16810 0.17866 0.20440 0.03103  0.00716  0.00376  116 HIS B CD2 
5116 C  CE1 . HIS B  116 ? 0.17205 0.18070 0.21036 0.03235  0.01085  0.00751  116 HIS B CE1 
5117 N  NE2 . HIS B  116 ? 0.17892 0.18753 0.21780 0.03068  0.00948  0.00484  116 HIS B NE2 
5125 N  N   . GLY B  117 ? 0.18294 0.21852 0.21250 0.03583  0.00033  0.00797  117 GLY B N   
5126 C  CA  . GLY B  117 ? 0.18075 0.22069 0.20719 0.03613  -0.00062 0.01074  117 GLY B CA  
5127 C  C   . GLY B  117 ? 0.19143 0.23191 0.21410 0.03577  -0.00073 0.01020  117 GLY B C   
5128 O  O   . GLY B  117 ? 0.19541 0.23464 0.21498 0.03516  -0.00048 0.01353  117 GLY B O   
5132 N  N   . PHE B  118 ? 0.18040 0.22310 0.20345 0.03622  -0.00139 0.00609  118 PHE B N   
5133 C  CA  . PHE B  118 ? 0.16481 0.20982 0.18522 0.03653  -0.00166 0.00490  118 PHE B CA  
5134 C  C   . PHE B  118 ? 0.17400 0.22646 0.19474 0.03795  -0.00326 0.00079  118 PHE B C   
5135 O  O   . PHE B  118 ? 0.19115 0.24394 0.21423 0.03827  -0.00426 -0.00200 118 PHE B O   
5136 C  CB  . PHE B  118 ? 0.17345 0.21036 0.19363 0.03590  -0.00068 0.00343  118 PHE B CB  
5137 C  CG  . PHE B  118 ? 0.17936 0.20822 0.19814 0.03440  0.00090  0.00711  118 PHE B CG  
5138 C  CD1 . PHE B  118 ? 0.19043 0.21880 0.20597 0.03363  0.00113  0.01072  118 PHE B CD1 
5139 C  CD2 . PHE B  118 ? 0.18286 0.20456 0.20327 0.03361  0.00212  0.00703  118 PHE B CD2 
5140 C  CE1 . PHE B  118 ? 0.18555 0.20562 0.19901 0.03219  0.00225  0.01400  118 PHE B CE1 
5141 C  CE2 . PHE B  118 ? 0.20380 0.21779 0.22217 0.03245  0.00368  0.01004  118 PHE B CE2 
5142 C  CZ  . PHE B  118 ? 0.20403 0.21675 0.21868 0.03177  0.00361  0.01340  118 PHE B CZ  
5152 N  N   . VAL B  119 ? 0.17566 0.23407 0.19391 0.03879  -0.00353 0.00037  119 VAL B N   
5153 C  CA  . VAL B  119 ? 0.17854 0.24335 0.19631 0.04061  -0.00480 -0.00429 119 VAL B CA  
5154 C  C   . VAL B  119 ? 0.18674 0.24667 0.20492 0.04152  -0.00469 -0.00786 119 VAL B C   
5155 O  O   . VAL B  119 ? 0.20176 0.26035 0.21891 0.04136  -0.00371 -0.00620 119 VAL B O   
5156 C  CB  . VAL B  119 ? 0.18354 0.25863 0.19842 0.04127  -0.00495 -0.00296 119 VAL B CB  
5157 C  CG1 . VAL B  119 ? 0.21545 0.29649 0.22928 0.04364  -0.00590 -0.00847 119 VAL B CG1 
5158 C  CG2 . VAL B  119 ? 0.20608 0.28551 0.22050 0.04011  -0.00565 0.00074  119 VAL B CG2 
5168 N  N   . VAL B  120 ? 0.18074 0.23732 0.20052 0.04219  -0.00598 -0.01235 120 VAL B N   
5169 C  CA  . VAL B  120 ? 0.16907 0.21842 0.18971 0.04246  -0.00628 -0.01512 120 VAL B CA  
5170 C  C   . VAL B  120 ? 0.19513 0.24682 0.21538 0.04484  -0.00831 -0.02100 120 VAL B C   
5171 O  O   . VAL B  120 ? 0.22267 0.27571 0.24328 0.04504  -0.00997 -0.02355 120 VAL B O   
5172 C  CB  . VAL B  120 ? 0.18303 0.22316 0.20607 0.04028  -0.00619 -0.01452 120 VAL B CB  
5173 C  CG1 . VAL B  120 ? 0.21623 0.24848 0.23974 0.04010  -0.00681 -0.01690 120 VAL B CG1 
5174 C  CG2 . VAL B  120 ? 0.18220 0.21973 0.20539 0.03838  -0.00418 -0.00928 120 VAL B CG2 
5184 N  N   . MET B  121 ? 0.18985 0.24202 0.20930 0.04679  -0.00842 -0.02329 121 MET B N   
5185 C  CA  . MET B  121 ? 0.19613 0.24949 0.21499 0.04960  -0.01050 -0.02937 121 MET B CA  
5186 C  C   . MET B  121 ? 0.20710 0.25110 0.22748 0.04974  -0.01179 -0.03178 121 MET B C   
5187 O  O   . MET B  121 ? 0.19974 0.24183 0.22055 0.04989  -0.01080 -0.03016 121 MET B O   
5188 C  CB  . MET B  121 ? 0.21273 0.27647 0.22933 0.05266  -0.00980 -0.03089 121 MET B CB  
5189 C  CG  . MET B  121 ? 0.21837 0.28359 0.23371 0.05609  -0.01189 -0.03767 121 MET B CG  
5190 S  SD  . MET B  121 ? 0.23387 0.31307 0.24611 0.06002  -0.01063 -0.03994 121 MET B SD  
5191 C  CE  . MET B  121 ? 0.23424 0.31542 0.24828 0.06024  -0.00826 -0.03606 121 MET B CE  
5201 N  N   . THR B  122 ? 0.20608 0.24434 0.22717 0.04955  -0.01439 -0.03557 122 THR B N   
5202 C  CA  . THR B  122 ? 0.20498 0.23451 0.22711 0.04994  -0.01651 -0.03862 122 THR B CA  
5203 C  C   . THR B  122 ? 0.22734 0.26067 0.24798 0.05439  -0.01812 -0.04417 122 THR B C   
5204 O  O   . THR B  122 ? 0.24887 0.28747 0.26759 0.05625  -0.01917 -0.04749 122 THR B O   
5205 C  CB  . THR B  122 ? 0.21572 0.23758 0.23914 0.04738  -0.01892 -0.03985 122 THR B CB  
5206 O  OG1 . THR B  122 ? 0.25423 0.28023 0.27654 0.04826  -0.02077 -0.04290 122 THR B OG1 
5207 C  CG2 . THR B  122 ? 0.23035 0.24913 0.25549 0.04340  -0.01688 -0.03455 122 THR B CG2 
5215 N  N   . ILE B  123 ? 0.22560 0.25647 0.24701 0.05623  -0.01835 -0.04525 123 ILE B N   
5216 C  CA  . ILE B  123 ? 0.23530 0.27106 0.25561 0.06115  -0.01933 -0.05042 123 ILE B CA  
5217 C  C   . ILE B  123 ? 0.24736 0.27384 0.26852 0.06287  -0.02298 -0.05526 123 ILE B C   
5218 O  O   . ILE B  123 ? 0.27712 0.29375 0.30005 0.06017  -0.02440 -0.05373 123 ILE B O   
5219 C  CB  . ILE B  123 ? 0.22675 0.27111 0.24743 0.06331  -0.01652 -0.04825 123 ILE B CB  
5220 C  CG1 . ILE B  123 ? 0.23993 0.27792 0.26311 0.06157  -0.01613 -0.04472 123 ILE B CG1 
5221 C  CG2 . ILE B  123 ? 0.23203 0.28619 0.25123 0.06178  -0.01351 -0.04381 123 ILE B CG2 
5222 C  CD1 . ILE B  123 ? 0.25212 0.29840 0.27623 0.06449  -0.01437 -0.04385 123 ILE B CD1 
5234 N  N   . ASP B  124 ? 0.25609 0.28578 0.27560 0.06753  -0.02466 -0.06129 124 ASP B N   
5235 C  CA  . ASP B  124 ? 0.26763 0.29098 0.28800 0.07089  -0.02770 -0.06612 124 ASP B CA  
5236 C  C   . ASP B  124 ? 0.27368 0.30481 0.29537 0.07497  -0.02548 -0.06625 124 ASP B C   
5237 O  O   . ASP B  124 ? 0.26864 0.31164 0.28944 0.07621  -0.02210 -0.06454 124 ASP B O   
5238 C  CB  . ASP B  124 ? 0.28181 0.30358 0.29926 0.07413  -0.03112 -0.07324 124 ASP B CB  
5239 C  CG  . ASP B  124 ? 0.33960 0.35126 0.35650 0.07020  -0.03469 -0.07372 124 ASP B CG  
5240 O  OD1 . ASP B  124 ? 0.37434 0.37566 0.39341 0.06753  -0.03687 -0.07233 124 ASP B OD1 
5241 O  OD2 . ASP B  124 ? 0.33244 0.34673 0.34668 0.06973  -0.03553 -0.07546 124 ASP B OD2 
5246 N  N   . THR B  125 ? 0.27404 0.29866 0.29812 0.07679  -0.02758 -0.06793 125 THR B N   
5247 C  CA  . THR B  125 ? 0.27596 0.30786 0.30206 0.08121  -0.02603 -0.06864 125 THR B CA  
5248 C  C   . THR B  125 ? 0.28259 0.31842 0.30711 0.08788  -0.02757 -0.07648 125 THR B C   
5249 O  O   . THR B  125 ? 0.31080 0.34121 0.33250 0.08886  -0.03062 -0.08153 125 THR B O   
5250 C  CB  . THR B  125 ? 0.32502 0.34835 0.35477 0.08004  -0.02765 -0.06633 125 THR B CB  
5251 O  OG1 . THR B  125 ? 0.30140 0.31144 0.33113 0.07966  -0.03244 -0.06993 125 THR B OG1 
5252 C  CG2 . THR B  125 ? 0.28555 0.30723 0.31614 0.07402  -0.02527 -0.05849 125 THR B CG2 
5260 N  N   . ASN B  126 ? 0.28811 0.33371 0.31437 0.09256  -0.02548 -0.07754 126 ASN B N   
5261 C  CA  . ASN B  126 ? 0.32570 0.37566 0.35058 0.09967  -0.02654 -0.08531 126 ASN B CA  
5262 C  C   . ASN B  126 ? 0.37705 0.41290 0.40213 0.10191  -0.03204 -0.09106 126 ASN B C   
5263 O  O   . ASN B  126 ? 0.37285 0.40647 0.39438 0.10544  -0.03448 -0.09781 126 ASN B O   
5264 C  CB  . ASN B  126 ? 0.33363 0.39564 0.36175 0.10420  -0.02354 -0.08490 126 ASN B CB  
5265 C  CG  . ASN B  126 ? 0.32392 0.40121 0.35106 0.10267  -0.01852 -0.08017 126 ASN B CG  
5266 O  OD1 . ASN B  126 ? 0.37250 0.45435 0.39540 0.10117  -0.01726 -0.08035 126 ASN B OD1 
5267 N  ND2 . ASN B  126 ? 0.35557 0.44097 0.38662 0.10287  -0.01592 -0.07569 126 ASN B ND2 
5274 N  N   . ARG B  127 ? 0.35051 0.37667 0.37945 0.10004  -0.03432 -0.08856 127 ARG B N   
5275 C  CA  . ARG B  127 ? 0.39265 0.40361 0.42184 0.10053  -0.04011 -0.09254 127 ARG B CA  
5276 C  C   . ARG B  127 ? 0.37503 0.37497 0.40599 0.09331  -0.04159 -0.08638 127 ARG B C   
5277 O  O   . ARG B  127 ? 0.34292 0.34636 0.37625 0.08992  -0.03853 -0.07988 127 ARG B O   
5278 C  CB  . ARG B  127 ? 0.38393 0.39370 0.41647 0.10703  -0.04228 -0.09690 127 ARG B CB  
5279 C  CG  . ARG B  127 ? 0.46165 0.48310 0.49285 0.11493  -0.04042 -0.10325 127 ARG B CG  
5280 C  CD  . ARG B  127 ? 0.69921 0.71612 0.73311 0.12187  -0.04393 -0.10923 127 ARG B CD  
5281 N  NE  . ARG B  127 ? 0.78332 0.81128 0.81514 0.12972  -0.04201 -0.11607 127 ARG B NE  
5282 C  CZ  . ARG B  127 ? 0.88966 0.92263 0.92485 0.13730  -0.04200 -0.12035 127 ARG B CZ  
5283 N  NH1 . ARG B  127 ? 0.84486 0.87282 0.88608 0.13813  -0.04408 -0.11836 127 ARG B NH1 
5284 N  NH2 . ARG B  127 ? 0.94151 0.98502 0.97397 0.14427  -0.03984 -0.12679 127 ARG B NH2 
5298 N  N   . ILE B  128 ? 0.39217 0.37869 0.42166 0.09075  -0.04641 -0.08836 128 ILE B N   
5299 C  CA  . ILE B  128 ? 0.36404 0.34060 0.39477 0.08364  -0.04763 -0.08258 128 ILE B CA  
5300 C  C   . ILE B  128 ? 0.35442 0.32630 0.38919 0.08371  -0.04876 -0.08001 128 ILE B C   
5301 O  O   . ILE B  128 ? 0.37076 0.33738 0.40666 0.07798  -0.04832 -0.07411 128 ILE B O   
5302 C  CB  . ILE B  128 ? 0.36391 0.32804 0.39227 0.08024  -0.05255 -0.08469 128 ILE B CB  
5303 C  CG1 . ILE B  128 ? 0.48475 0.43947 0.51294 0.08474  -0.05855 -0.09137 128 ILE B CG1 
5304 C  CG2 . ILE B  128 ? 0.44648 0.41612 0.47119 0.07920  -0.05108 -0.08588 128 ILE B CG2 
5305 C  CD1 . ILE B  128 ? 0.51725 0.45907 0.54301 0.08100  -0.06413 -0.09317 128 ILE B CD1 
5317 N  N   . SER B  129 ? 0.36708 0.34123 0.40407 0.09018  -0.05010 -0.08426 129 SER B N   
5318 C  CA  . SER B  129 ? 0.35418 0.32448 0.39551 0.09080  -0.05158 -0.08203 129 SER B CA  
5319 C  C   . SER B  129 ? 0.34341 0.32557 0.38756 0.09066  -0.04644 -0.07663 129 SER B C   
5320 O  O   . SER B  129 ? 0.36909 0.34907 0.41704 0.09088  -0.04749 -0.07415 129 SER B O   
5321 C  CB  . SER B  129 ? 0.38071 0.34764 0.42380 0.09815  -0.05582 -0.08907 129 SER B CB  
5322 O  OG  . SER B  129 ? 0.41617 0.39576 0.45858 0.10513  -0.05303 -0.09410 129 SER B OG  
5328 N  N   . ASP B  130 ? 0.30136 0.29549 0.34371 0.08984  -0.04133 -0.07432 130 ASP B N   
5329 C  CA  . ASP B  130 ? 0.30628 0.31186 0.35110 0.08966  -0.03689 -0.06914 130 ASP B CA  
5330 C  C   . ASP B  130 ? 0.28386 0.28235 0.33005 0.08320  -0.03693 -0.06181 130 ASP B C   
5331 O  O   . ASP B  130 ? 0.31545 0.30389 0.35941 0.07756  -0.03817 -0.05940 130 ASP B O   
5332 C  CB  . ASP B  130 ? 0.32127 0.33959 0.36327 0.08907  -0.03200 -0.06757 130 ASP B CB  
5333 C  CG  . ASP B  130 ? 0.33393 0.36167 0.37432 0.09565  -0.03124 -0.07434 130 ASP B CG  
5334 O  OD1 . ASP B  130 ? 0.35393 0.38158 0.39637 0.10179  -0.03345 -0.07982 130 ASP B OD1 
5335 O  OD2 . ASP B  130 ? 0.32196 0.35697 0.35883 0.09474  -0.02855 -0.07427 130 ASP B OD2 
5340 N  N   . GLN B  131 ? 0.29947 0.30352 0.34929 0.08408  -0.03562 -0.05831 131 GLN B N   
5341 C  CA  . GLN B  131 ? 0.29046 0.28846 0.34159 0.07866  -0.03589 -0.05155 131 GLN B CA  
5342 C  C   . GLN B  131 ? 0.27463 0.28035 0.32399 0.07439  -0.03119 -0.04508 131 GLN B C   
5343 O  O   . GLN B  131 ? 0.27675 0.29348 0.32452 0.07594  -0.02781 -0.04565 131 GLN B O   
5344 C  CB  . GLN B  131 ? 0.29945 0.29870 0.35581 0.08222  -0.03788 -0.05154 131 GLN B CB  
5345 C  CG  . GLN B  131 ? 0.39189 0.38236 0.45020 0.08670  -0.04313 -0.05787 131 GLN B CG  
5346 C  CD  . GLN B  131 ? 0.53490 0.50826 0.59114 0.08146  -0.04743 -0.05704 131 GLN B CD  
5347 O  OE1 . GLN B  131 ? 0.48604 0.45228 0.54291 0.07646  -0.04857 -0.05171 131 GLN B OE1 
5348 N  NE2 . GLN B  131 ? 0.58367 0.55046 0.63706 0.08213  -0.04988 -0.06207 131 GLN B NE2 
5357 N  N   . PRO B  132 ? 0.26792 0.26730 0.31688 0.06865  -0.03110 -0.03879 132 PRO B N   
5358 C  CA  . PRO B  132 ? 0.26239 0.26643 0.30859 0.06409  -0.02715 -0.03284 132 PRO B CA  
5359 C  C   . PRO B  132 ? 0.23022 0.24993 0.27784 0.06663  -0.02371 -0.03090 132 PRO B C   
5360 O  O   . PRO B  132 ? 0.24732 0.27327 0.29207 0.06483  -0.02056 -0.02869 132 PRO B O   
5361 C  CB  . PRO B  132 ? 0.25386 0.24729 0.29946 0.05828  -0.02840 -0.02714 132 PRO B CB  
5362 C  CG  . PRO B  132 ? 0.26665 0.24715 0.31272 0.05800  -0.03282 -0.03048 132 PRO B CG  
5363 C  CD  . PRO B  132 ? 0.26626 0.25146 0.31587 0.06524  -0.03498 -0.03714 132 PRO B CD  
5371 N  N   . PRO B  133 ? 0.25678 0.28370 0.30885 0.07055  -0.02420 -0.03124 133 PRO B N   
5372 C  CA  . PRO B  133 ? 0.21975 0.26312 0.27312 0.07262  -0.02068 -0.02909 133 PRO B CA  
5373 C  C   . PRO B  133 ? 0.22754 0.28090 0.27893 0.07642  -0.01838 -0.03372 133 PRO B C   
5374 O  O   . PRO B  133 ? 0.26343 0.32570 0.31246 0.07464  -0.01518 -0.03064 133 PRO B O   
5375 C  CB  . PRO B  133 ? 0.26426 0.31288 0.32358 0.07659  -0.02210 -0.02932 133 PRO B CB  
5376 C  CG  . PRO B  133 ? 0.25488 0.28839 0.31533 0.07413  -0.02616 -0.02849 133 PRO B CG  
5377 C  CD  . PRO B  133 ? 0.27083 0.29203 0.32717 0.07265  -0.02784 -0.03248 133 PRO B CD  
5385 N  N   . SER B  134 ? 0.25322 0.30444 0.30504 0.08142  -0.02030 -0.04110 134 SER B N   
5386 C  CA  . SER B  134 ? 0.26405 0.32298 0.31303 0.08471  -0.01856 -0.04594 134 SER B CA  
5387 C  C   . SER B  134 ? 0.23279 0.28728 0.27683 0.07969  -0.01746 -0.04390 134 SER B C   
5388 O  O   . SER B  134 ? 0.25162 0.31568 0.29306 0.07982  -0.01471 -0.04363 134 SER B O   
5389 C  CB  . SER B  134 ? 0.27459 0.32834 0.32417 0.09029  -0.02174 -0.05422 134 SER B CB  
5390 O  OG  . SER B  134 ? 0.31689 0.37685 0.36299 0.09327  -0.02046 -0.05917 134 SER B OG  
5396 N  N   . ARG B  135 ? 0.23491 0.27539 0.27770 0.07515  -0.01955 -0.04222 135 ARG B N   
5397 C  CA  . ARG B  135 ? 0.23184 0.26768 0.27063 0.07033  -0.01852 -0.04000 135 ARG B CA  
5398 C  C   . ARG B  135 ? 0.22501 0.26866 0.26251 0.06694  -0.01500 -0.03338 135 ARG B C   
5399 O  O   . ARG B  135 ? 0.23090 0.27914 0.26564 0.06588  -0.01315 -0.03283 135 ARG B O   
5400 C  CB  . ARG B  135 ? 0.23448 0.25461 0.27271 0.06618  -0.02128 -0.03912 135 ARG B CB  
5401 C  CG  . ARG B  135 ? 0.23093 0.24309 0.26926 0.06869  -0.02503 -0.04560 135 ARG B CG  
5402 C  CD  . ARG B  135 ? 0.24872 0.24599 0.28630 0.06410  -0.02789 -0.04456 135 ARG B CD  
5403 N  NE  . ARG B  135 ? 0.28862 0.27943 0.32693 0.06730  -0.03211 -0.05074 135 ARG B NE  
5404 C  CZ  . ARG B  135 ? 0.28186 0.26911 0.31810 0.06756  -0.03391 -0.05483 135 ARG B CZ  
5405 N  NH1 . ARG B  135 ? 0.26971 0.25861 0.30341 0.06438  -0.03191 -0.05317 135 ARG B NH1 
5406 N  NH2 . ARG B  135 ? 0.30893 0.29050 0.34569 0.07102  -0.03811 -0.06064 135 ARG B NH2 
5420 N  N   . ARG B  136 ? 0.24028 0.28533 0.27971 0.06527  -0.01447 -0.02842 136 ARG B N   
5421 C  CA  . ARG B  136 ? 0.20925 0.26151 0.24723 0.06201  -0.01165 -0.02201 136 ARG B CA  
5422 C  C   . ARG B  136 ? 0.21760 0.28539 0.25510 0.06515  -0.00919 -0.02322 136 ARG B C   
5423 O  O   . ARG B  136 ? 0.21678 0.28870 0.25125 0.06268  -0.00728 -0.02038 136 ARG B O   
5424 C  CB  . ARG B  136 ? 0.23788 0.28984 0.27841 0.06032  -0.01213 -0.01707 136 ARG B CB  
5425 C  CG  . ARG B  136 ? 0.22118 0.28205 0.26068 0.05747  -0.00977 -0.01047 136 ARG B CG  
5426 C  CD  . ARG B  136 ? 0.30425 0.37808 0.34806 0.06080  -0.00927 -0.00974 136 ARG B CD  
5427 N  NE  . ARG B  136 ? 0.28670 0.37015 0.32951 0.05786  -0.00729 -0.00327 136 ARG B NE  
5428 C  CZ  . ARG B  136 ? 0.31036 0.40622 0.35170 0.05884  -0.00496 -0.00304 136 ARG B CZ  
5429 N  NH1 . ARG B  136 ? 0.33592 0.43750 0.37685 0.06326  -0.00409 -0.00918 136 ARG B NH1 
5430 N  NH2 . ARG B  136 ? 0.37107 0.47332 0.41091 0.05507  -0.00378 0.00362  136 ARG B NH2 
5444 N  N   . ASP B  137 ? 0.24075 0.31704 0.28102 0.07072  -0.00930 -0.02770 137 ASP B N   
5445 C  CA  . ASP B  137 ? 0.22432 0.31620 0.26379 0.07390  -0.00678 -0.02921 137 ASP B CA  
5446 C  C   . ASP B  137 ? 0.22318 0.31463 0.25855 0.07414  -0.00643 -0.03278 137 ASP B C   
5447 O  O   . ASP B  137 ? 0.22769 0.32890 0.26055 0.07333  -0.00422 -0.03092 137 ASP B O   
5448 C  CB  . ASP B  137 ? 0.23809 0.33810 0.28115 0.08057  -0.00701 -0.03452 137 ASP B CB  
5449 C  CG  . ASP B  137 ? 0.34087 0.44467 0.38884 0.08091  -0.00714 -0.03080 137 ASP B CG  
5450 O  OD1 . ASP B  137 ? 0.28741 0.39091 0.33533 0.07588  -0.00650 -0.02358 137 ASP B OD1 
5451 O  OD2 . ASP B  137 ? 0.36316 0.47036 0.41501 0.08642  -0.00805 -0.03523 137 ASP B OD2 
5456 N  N   . GLN B  138 ? 0.22707 0.30710 0.26169 0.07482  -0.00891 -0.03749 138 GLN B N   
5457 C  CA  . GLN B  138 ? 0.22525 0.30439 0.25627 0.07502  -0.00911 -0.04108 138 GLN B CA  
5458 C  C   . GLN B  138 ? 0.21771 0.29337 0.24612 0.06937  -0.00810 -0.03581 138 GLN B C   
5459 O  O   . GLN B  138 ? 0.24027 0.32128 0.26583 0.06903  -0.00708 -0.03626 138 GLN B O   
5460 C  CB  . GLN B  138 ? 0.23668 0.30496 0.26786 0.07731  -0.01250 -0.04750 138 GLN B CB  
5461 C  CG  . GLN B  138 ? 0.24941 0.32225 0.28266 0.08395  -0.01352 -0.05364 138 GLN B CG  
5462 C  CD  . GLN B  138 ? 0.31470 0.37598 0.34771 0.08630  -0.01751 -0.06012 138 GLN B CD  
5463 O  OE1 . GLN B  138 ? 0.28597 0.34401 0.31570 0.08615  -0.01872 -0.06358 138 GLN B OE1 
5464 N  NE2 . GLN B  138 ? 0.30229 0.35691 0.33876 0.08822  -0.01997 -0.06154 138 GLN B NE2 
5473 N  N   . ILE B  139 ? 0.21369 0.28028 0.24282 0.06499  -0.00844 -0.03087 139 ILE B N   
5474 C  CA  . ILE B  139 ? 0.20987 0.27392 0.23665 0.06014  -0.00719 -0.02567 139 ILE B CA  
5475 C  C   . ILE B  139 ? 0.20796 0.28459 0.23342 0.05951  -0.00473 -0.02150 139 ILE B C   
5476 O  O   . ILE B  139 ? 0.21247 0.29222 0.23539 0.05783  -0.00380 -0.01991 139 ILE B O   
5477 C  CB  . ILE B  139 ? 0.20823 0.26068 0.23552 0.05586  -0.00778 -0.02118 139 ILE B CB  
5478 C  CG1 . ILE B  139 ? 0.21229 0.25214 0.24055 0.05566  -0.01035 -0.02470 139 ILE B CG1 
5479 C  CG2 . ILE B  139 ? 0.21554 0.26579 0.24023 0.05147  -0.00630 -0.01604 139 ILE B CG2 
5480 C  CD1 . ILE B  139 ? 0.21685 0.24646 0.24585 0.05227  -0.01119 -0.02093 139 ILE B CD1 
5492 N  N   . GLU B  140 ? 0.21782 0.30176 0.24517 0.06053  -0.00391 -0.01920 140 GLU B N   
5493 C  CA  . GLU B  140 ? 0.20232 0.29873 0.22859 0.05948  -0.00184 -0.01462 140 GLU B CA  
5494 C  C   . GLU B  140 ? 0.21713 0.32468 0.24143 0.06240  -0.00077 -0.01828 140 GLU B C   
5495 O  O   . GLU B  140 ? 0.22325 0.33648 0.24485 0.06012  0.00030  -0.01499 140 GLU B O   
5496 C  CB  . GLU B  140 ? 0.25483 0.35785 0.28424 0.06051  -0.00142 -0.01223 140 GLU B CB  
5497 C  CG  . GLU B  140 ? 0.26510 0.38186 0.29384 0.05912  0.00047  -0.00705 140 GLU B CG  
5498 C  CD  . GLU B  140 ? 0.34713 0.47050 0.37975 0.05991  0.00067  -0.00433 140 GLU B CD  
5499 O  OE1 . GLU B  140 ? 0.38798 0.51453 0.42398 0.06469  0.00042  -0.00923 140 GLU B OE1 
5500 O  OE2 . GLU B  140 ? 0.52031 0.64508 0.55263 0.05574  0.00080  0.00266  140 GLU B OE2 
5507 N  N   . ALA B  141 ? 0.22368 0.33404 0.24896 0.06747  -0.00130 -0.02519 141 ALA B N   
5508 C  CA  . ALA B  141 ? 0.22061 0.34110 0.24327 0.07050  -0.00039 -0.02937 141 ALA B CA  
5509 C  C   . ALA B  141 ? 0.20883 0.32383 0.22816 0.06818  -0.00122 -0.03000 141 ALA B C   
5510 O  O   . ALA B  141 ? 0.23008 0.35376 0.24640 0.06779  -0.00019 -0.02942 141 ALA B O   
5511 C  CB  . ALA B  141 ? 0.24361 0.36543 0.26756 0.07659  -0.00126 -0.03725 141 ALA B CB  
5517 N  N   . ALA B  142 ? 0.20515 0.30627 0.22506 0.06654  -0.00319 -0.03112 142 ALA B N   
5518 C  CA  . ALA B  142 ? 0.22023 0.31633 0.23784 0.06427  -0.00406 -0.03144 142 ALA B CA  
5519 C  C   . ALA B  142 ? 0.20425 0.30224 0.22051 0.05980  -0.00276 -0.02445 142 ALA B C   
5520 O  O   . ALA B  142 ? 0.21581 0.31727 0.22972 0.05877  -0.00273 -0.02405 142 ALA B O   
5521 C  CB  . ALA B  142 ? 0.22745 0.30913 0.24649 0.06340  -0.00638 -0.03389 142 ALA B CB  
5527 N  N   . LEU B  143 ? 0.20456 0.29996 0.22204 0.05706  -0.00200 -0.01886 143 LEU B N   
5528 C  CA  . LEU B  143 ? 0.21194 0.30888 0.22774 0.05309  -0.00110 -0.01227 143 LEU B CA  
5529 C  C   . LEU B  143 ? 0.19965 0.31116 0.21346 0.05356  0.00015  -0.01038 143 LEU B C   
5530 O  O   . LEU B  143 ? 0.22639 0.34073 0.23792 0.05140  0.00020  -0.00754 143 LEU B O   
5531 C  CB  . LEU B  143 ? 0.23218 0.32246 0.24907 0.05007  -0.00090 -0.00691 143 LEU B CB  
5532 C  CG  . LEU B  143 ? 0.20337 0.27897 0.22111 0.04830  -0.00189 -0.00733 143 LEU B CG  
5533 C  CD1 . LEU B  143 ? 0.22494 0.29449 0.24356 0.04615  -0.00191 -0.00331 143 LEU B CD1 
5534 C  CD2 . LEU B  143 ? 0.21525 0.28598 0.23139 0.04562  -0.00182 -0.00503 143 LEU B CD2 
5546 N  N   . GLU B  144 ? 0.21509 0.33632 0.22981 0.05636  0.00110  -0.01189 144 GLU B N   
5547 C  CA  . GLU B  144 ? 0.22425 0.36055 0.23692 0.05685  0.00249  -0.01039 144 GLU B CA  
5548 C  C   . GLU B  144 ? 0.22279 0.36298 0.23254 0.05853  0.00216  -0.01482 144 GLU B C   
5549 O  O   . GLU B  144 ? 0.23286 0.38155 0.23974 0.05686  0.00265  -0.01203 144 GLU B O   
5550 C  CB  . GLU B  144 ? 0.27429 0.42055 0.28910 0.06024  0.00379  -0.01208 144 GLU B CB  
5551 C  CG  . GLU B  144 ? 0.33261 0.47799 0.34993 0.05758  0.00404  -0.00592 144 GLU B CG  
5552 C  CD  . GLU B  144 ? 0.65128 0.80458 0.67214 0.06101  0.00497  -0.00753 144 GLU B CD  
5553 O  OE1 . GLU B  144 ? 0.56180 0.72272 0.58308 0.06598  0.00578  -0.01361 144 GLU B OE1 
5554 O  OE2 . GLU B  144 ? 0.55869 0.71028 0.58189 0.05873  0.00475  -0.00261 144 GLU B OE2 
5561 N  N   . TYR B  145 ? 0.23474 0.36857 0.24491 0.06158  0.00097  -0.02159 145 TYR B N   
5562 C  CA  . TYR B  145 ? 0.22359 0.35976 0.23067 0.06292  0.00015  -0.02596 145 TYR B CA  
5563 C  C   . TYR B  145 ? 0.23229 0.36416 0.23797 0.05880  -0.00078 -0.02190 145 TYR B C   
5564 O  O   . TYR B  145 ? 0.23273 0.37206 0.23529 0.05815  -0.00083 -0.02139 145 TYR B O   
5565 C  CB  . TYR B  145 ? 0.25225 0.38028 0.26012 0.06642  -0.00161 -0.03354 145 TYR B CB  
5566 C  CG  . TYR B  145 ? 0.26306 0.39148 0.26759 0.06730  -0.00308 -0.03797 145 TYR B CG  
5567 C  CD1 . TYR B  145 ? 0.28849 0.42740 0.28954 0.07057  -0.00250 -0.04227 145 TYR B CD1 
5568 C  CD2 . TYR B  145 ? 0.27116 0.38956 0.27598 0.06476  -0.00508 -0.03776 145 TYR B CD2 
5569 C  CE1 . TYR B  145 ? 0.28454 0.42318 0.28193 0.07094  -0.00422 -0.04612 145 TYR B CE1 
5570 C  CE2 . TYR B  145 ? 0.26922 0.38798 0.27119 0.06516  -0.00678 -0.04135 145 TYR B CE2 
5571 C  CZ  . TYR B  145 ? 0.30133 0.42962 0.29945 0.06817  -0.00651 -0.04555 145 TYR B CZ  
5572 O  OH  . TYR B  145 ? 0.39855 0.52691 0.39319 0.06832  -0.00853 -0.04912 145 TYR B OH  
5582 N  N   . LEU B  146 ? 0.21257 0.33297 0.22044 0.05602  -0.00149 -0.01881 146 LEU B N   
5583 C  CA  . LEU B  146 ? 0.20562 0.32209 0.21272 0.05261  -0.00225 -0.01503 146 LEU B CA  
5584 C  C   . LEU B  146 ? 0.19813 0.32281 0.20328 0.04991  -0.00143 -0.00857 146 LEU B C   
5585 O  O   . LEU B  146 ? 0.21876 0.34655 0.22198 0.04837  -0.00220 -0.00682 146 LEU B O   
5586 C  CB  . LEU B  146 ? 0.20776 0.31079 0.21746 0.05047  -0.00278 -0.01313 146 LEU B CB  
5587 C  CG  . LEU B  146 ? 0.20198 0.29578 0.21351 0.05207  -0.00413 -0.01868 146 LEU B CG  
5588 C  CD1 . LEU B  146 ? 0.22204 0.30387 0.23579 0.04953  -0.00418 -0.01599 146 LEU B CD1 
5589 C  CD2 . LEU B  146 ? 0.22726 0.32189 0.23764 0.05272  -0.00572 -0.02239 146 LEU B CD2 
5601 N  N   . VAL B  147 ? 0.21423 0.34295 0.21982 0.04917  -0.00021 -0.00482 147 VAL B N   
5602 C  CA  . VAL B  147 ? 0.23712 0.37386 0.24065 0.04624  0.00017  0.00166  147 VAL B CA  
5603 C  C   . VAL B  147 ? 0.24499 0.39537 0.24547 0.04748  0.00055  -0.00003 147 VAL B C   
5604 O  O   . VAL B  147 ? 0.24408 0.39892 0.24203 0.04503  -0.00020 0.00360  147 VAL B O   
5605 C  CB  . VAL B  147 ? 0.24045 0.37889 0.24526 0.04507  0.00112  0.00589  147 VAL B CB  
5606 C  CG1 . VAL B  147 ? 0.28872 0.43841 0.29104 0.04226  0.00134  0.01207  147 VAL B CG1 
5607 C  CG2 . VAL B  147 ? 0.24690 0.37166 0.25339 0.04282  0.00050  0.00884  147 VAL B CG2 
5617 N  N   . ASP B  148 ? 0.23098 0.38794 0.23138 0.05144  0.00158  -0.00577 148 ASP B N   
5618 C  CA  . ASP B  148 ? 0.24325 0.41353 0.24010 0.05294  0.00225  -0.00798 148 ASP B CA  
5619 C  C   . ASP B  148 ? 0.23769 0.40572 0.23192 0.05256  0.00053  -0.01037 148 ASP B C   
5620 O  O   . ASP B  148 ? 0.26663 0.44388 0.25722 0.05127  0.00036  -0.00875 148 ASP B O   
5621 C  CB  . ASP B  148 ? 0.27471 0.45060 0.27212 0.05804  0.00365  -0.01468 148 ASP B CB  
5622 C  CG  . ASP B  148 ? 0.50893 0.69133 0.50886 0.05852  0.00548  -0.01190 148 ASP B CG  
5623 O  OD1 . ASP B  148 ? 0.44945 0.63605 0.44927 0.05462  0.00582  -0.00457 148 ASP B OD1 
5624 O  OD2 . ASP B  148 ? 0.48701 0.67029 0.48911 0.06279  0.00631  -0.01695 148 ASP B OD2 
5629 N  N   . GLN B  149 ? 0.23636 0.39288 0.23233 0.05365  -0.00088 -0.01437 149 GLN B N   
5630 C  CA  . GLN B  149 ? 0.21846 0.37268 0.21250 0.05306  -0.00282 -0.01640 149 GLN B CA  
5631 C  C   . GLN B  149 ? 0.22564 0.37852 0.21948 0.04875  -0.00388 -0.00953 149 GLN B C   
5632 O  O   . GLN B  149 ? 0.22926 0.38720 0.22027 0.04755  -0.00510 -0.00884 149 GLN B O   
5633 C  CB  . GLN B  149 ? 0.24409 0.38630 0.24047 0.05471  -0.00432 -0.02164 149 GLN B CB  
5634 C  CG  . GLN B  149 ? 0.30385 0.44703 0.29957 0.05931  -0.00415 -0.02929 149 GLN B CG  
5635 C  CD  . GLN B  149 ? 0.35893 0.51348 0.34972 0.06163  -0.00394 -0.03329 149 GLN B CD  
5636 O  OE1 . GLN B  149 ? 0.47738 0.64163 0.46678 0.06413  -0.00194 -0.03469 149 GLN B OE1 
5637 N  NE2 . GLN B  149 ? 0.33595 0.48972 0.32408 0.06081  -0.00594 -0.03507 149 GLN B NE2 
5646 N  N   . SER B  150 ? 0.22118 0.36680 0.21781 0.04644  -0.00368 -0.00451 150 SER B N   
5647 C  CA  . SER B  150 ? 0.21640 0.36044 0.21275 0.04275  -0.00479 0.00206  150 SER B CA  
5648 C  C   . SER B  150 ? 0.21474 0.37103 0.20746 0.04083  -0.00475 0.00640  150 SER B C   
5649 O  O   . SER B  150 ? 0.22540 0.38332 0.21656 0.03845  -0.00644 0.00992  150 SER B O   
5650 C  CB  . SER B  150 ? 0.23428 0.36882 0.23334 0.04094  -0.00435 0.00644  150 SER B CB  
5651 O  OG  . SER B  150 ? 0.22939 0.36070 0.22820 0.03780  -0.00565 0.01246  150 SER B OG  
5657 N  N   . ASN B  151 ? 0.21493 0.38439 0.22947 0.00399  0.01659  0.01338  151 ASN B N   
5658 C  CA  . ASN B  151 ? 0.20491 0.38452 0.21918 0.00197  0.02058  0.01645  151 ASN B CA  
5659 C  C   . ASN B  151 ? 0.24331 0.43375 0.25624 0.00564  0.02085  0.01558  151 ASN B C   
5660 O  O   . ASN B  151 ? 0.31526 0.51523 0.32813 0.00427  0.02404  0.01775  151 ASN B O   
5661 C  CB  . ASN B  151 ? 0.26749 0.45454 0.28592 -0.00044 0.02111  0.01401  151 ASN B CB  
5662 C  CG  . ASN B  151 ? 0.37364 0.55096 0.39306 -0.00482 0.02186  0.01606  151 ASN B CG  
5663 O  OD1 . ASN B  151 ? 0.47044 0.63765 0.48702 -0.00718 0.02367  0.02111  151 ASN B OD1 
5664 N  ND2 . ASN B  151 ? 0.37772 0.55792 0.40117 -0.00595 0.02048  0.01222  151 ASN B ND2 
5671 N  N   . SER B  152 ? 0.21185 0.40101 0.22368 0.01010  0.01770  0.01265  152 SER B N   
5672 C  CA  . SER B  152 ? 0.19975 0.39955 0.21060 0.01392  0.01751  0.01110  152 SER B CA  
5673 C  C   . SER B  152 ? 0.19888 0.39295 0.20524 0.01555  0.01818  0.01493  152 SER B C   
5674 O  O   . SER B  152 ? 0.20103 0.38477 0.20603 0.01704  0.01573  0.01451  152 SER B O   
5675 C  CB  . SER B  152 ? 0.23375 0.43848 0.24725 0.01823  0.01302  0.00391  152 SER B CB  
5676 O  OG  . SER B  152 ? 0.27193 0.48577 0.28402 0.02215  0.01269  0.00267  152 SER B OG  
5682 N  N   . SER B  153 ? 0.22129 0.42276 0.22545 0.01552  0.02137  0.01836  153 SER B N   
5683 C  CA  . SER B  153 ? 0.21244 0.41074 0.21243 0.01755  0.02202  0.02158  153 SER B CA  
5684 C  C   . SER B  153 ? 0.19633 0.39670 0.19607 0.02296  0.01810  0.01692  153 SER B C   
5685 O  O   . SER B  153 ? 0.22479 0.42128 0.22116 0.02503  0.01796  0.01906  153 SER B O   
5686 C  CB  . SER B  153 ? 0.25280 0.46067 0.25102 0.01648  0.02622  0.02560  153 SER B CB  
5687 O  OG  . SER B  153 ? 0.29431 0.51603 0.29459 0.01919  0.02543  0.02140  153 SER B OG  
5693 N  N   . ARG B  154 ? 0.20702 0.41364 0.21016 0.02533  0.01495  0.01071  154 ARG B N   
5694 C  CA  . ARG B  154 ? 0.23934 0.44774 0.24256 0.03044  0.01090  0.00585  154 ARG B CA  
5695 C  C   . ARG B  154 ? 0.22279 0.41920 0.22660 0.03150  0.00701  0.00329  154 ARG B C   
5696 O  O   . ARG B  154 ? 0.25350 0.45046 0.25757 0.03568  0.00332  -0.00095 154 ARG B O   
5697 C  CB  . ARG B  154 ? 0.22461 0.44652 0.23122 0.03264  0.00944  0.00027  154 ARG B CB  
5698 C  CG  . ARG B  154 ? 0.23303 0.46727 0.23930 0.03152  0.01330  0.00265  154 ARG B CG  
5699 C  CD  . ARG B  154 ? 0.25282 0.50027 0.26238 0.03367  0.01191  -0.00275 154 ARG B CD  
5700 N  NE  . ARG B  154 ? 0.29058 0.54183 0.29990 0.03892  0.00833  -0.00733 154 ARG B NE  
5701 C  CZ  . ARG B  154 ? 0.63262 0.88626 0.64486 0.04166  0.00433  -0.01363 154 ARG B CZ  
5702 N  NH1 . ARG B  154 ? 0.51968 0.77284 0.53554 0.03976  0.00326  -0.01651 154 ARG B NH1 
5703 N  NH2 . ARG B  154 ? 0.55229 0.80904 0.56379 0.04645  0.00132  -0.01716 154 ARG B NH2 
5717 N  N   . SER B  155 ? 0.20328 0.38890 0.20725 0.02787  0.00771  0.00580  155 SER B N   
5718 C  CA  . SER B  155 ? 0.23122 0.40570 0.23603 0.02864  0.00408  0.00327  155 SER B CA  
5719 C  C   . SER B  155 ? 0.19872 0.36023 0.19973 0.02805  0.00463  0.00797  155 SER B C   
5720 O  O   . SER B  155 ? 0.22049 0.37822 0.21917 0.02478  0.00832  0.01377  155 SER B O   
5721 C  CB  . SER B  155 ? 0.21302 0.38411 0.22108 0.02504  0.00407  0.00218  155 SER B CB  
5722 O  OG  . SER B  155 ? 0.22670 0.38529 0.23503 0.02510  0.00118  0.00097  155 SER B OG  
5728 N  N   . PRO B  156 ? 0.21688 0.37073 0.21733 0.03096  0.00092  0.00557  156 PRO B N   
5729 C  CA  . PRO B  156 ? 0.24692 0.38732 0.24408 0.03009  0.00127  0.00990  156 PRO B CA  
5730 C  C   . PRO B  156 ? 0.24943 0.38029 0.24682 0.02535  0.00316  0.01332  156 PRO B C   
5731 O  O   . PRO B  156 ? 0.27025 0.39204 0.26444 0.02353  0.00517  0.01862  156 PRO B O   
5732 C  CB  . PRO B  156 ? 0.30176 0.43660 0.29925 0.03406  -0.00356 0.00558  156 PRO B CB  
5733 C  CG  . PRO B  156 ? 0.38404 0.52894 0.38491 0.03691  -0.00643 -0.00090 156 PRO B CG  
5734 C  CD  . PRO B  156 ? 0.28463 0.44161 0.28754 0.03501  -0.00373 -0.00118 156 PRO B CD  
5742 N  N   . ILE B  157 ? 0.21551 0.34770 0.21651 0.02331  0.00253  0.01054  157 ILE B N   
5743 C  CA  . ILE B  157 ? 0.20353 0.32645 0.20497 0.01880  0.00408  0.01346  157 ILE B CA  
5744 C  C   . ILE B  157 ? 0.20935 0.33795 0.21095 0.01466  0.00861  0.01734  157 ILE B C   
5745 O  O   . ILE B  157 ? 0.21897 0.34256 0.22185 0.01077  0.00987  0.01888  157 ILE B O   
5746 C  CB  . ILE B  157 ? 0.20658 0.32507 0.21165 0.01869  0.00061  0.00858  157 ILE B CB  
5747 C  CG1 . ILE B  157 ? 0.19091 0.32138 0.20011 0.01932  -0.00045 0.00335  157 ILE B CG1 
5748 C  CG2 . ILE B  157 ? 0.24179 0.35206 0.24604 0.02226  -0.00352 0.00596  157 ILE B CG2 
5749 C  CD1 . ILE B  157 ? 0.23197 0.35729 0.24467 0.01767  -0.00270 -0.00003 157 ILE B CD1 
5761 N  N   . ASN B  158 ? 0.19198 0.33115 0.19242 0.01542  0.01103  0.01885  158 ASN B N   
5762 C  CA  . ASN B  158 ? 0.20805 0.35284 0.20832 0.01166  0.01545  0.02289  158 ASN B CA  
5763 C  C   . ASN B  158 ? 0.21422 0.34761 0.21231 0.00739  0.01817  0.02882  158 ASN B C   
5764 O  O   . ASN B  158 ? 0.21355 0.33807 0.20815 0.00776  0.01856  0.03240  158 ASN B O   
5765 C  CB  . ASN B  158 ? 0.20292 0.35739 0.20085 0.01367  0.01750  0.02474  158 ASN B CB  
5766 C  CG  . ASN B  158 ? 0.22941 0.39025 0.22676 0.01018  0.02215  0.02917  158 ASN B CG  
5767 O  OD1 . ASN B  158 ? 0.26263 0.42826 0.26280 0.00731  0.02346  0.02854  158 ASN B OD1 
5768 N  ND2 . ASN B  158 ? 0.21645 0.37847 0.21021 0.01053  0.02471  0.03359  158 ASN B ND2 
5775 N  N   . GLY B  159 ? 0.22889 0.36269 0.22910 0.00335  0.02001  0.02979  159 GLY B N   
5776 C  CA  . GLY B  159 ? 0.23084 0.35525 0.22936 -0.00114 0.02291  0.03536  159 GLY B CA  
5777 C  C   . GLY B  159 ? 0.24288 0.35331 0.24155 -0.00225 0.02080  0.03514  159 GLY B C   
5778 O  O   . GLY B  159 ? 0.26044 0.36278 0.25793 -0.00615 0.02309  0.03958  159 GLY B O   
5782 N  N   . MET B  160 ? 0.20847 0.31570 0.20849 0.00101  0.01654  0.03025  160 MET B N   
5783 C  CA  . MET B  160 ? 0.21353 0.30666 0.21300 0.00052  0.01442  0.03041  160 MET B CA  
5784 C  C   . MET B  160 ? 0.22793 0.31716 0.23082 -0.00216 0.01329  0.02808  160 MET B C   
5785 O  O   . MET B  160 ? 0.25605 0.33285 0.25824 -0.00345 0.01228  0.02926  160 MET B O   
5786 C  CB  . MET B  160 ? 0.22701 0.31723 0.22612 0.00524  0.01025  0.02650  160 MET B CB  
5787 C  CG  . MET B  160 ? 0.26050 0.35061 0.25576 0.00785  0.01091  0.02920  160 MET B CG  
5788 S  SD  . MET B  160 ? 0.28244 0.36766 0.27748 0.01322  0.00564  0.02449  160 MET B SD  
5789 C  CE  . MET B  160 ? 0.33783 0.42552 0.32839 0.01564  0.00741  0.02835  160 MET B CE  
5799 N  N   . VAL B  161 ? 0.21448 0.31356 0.22098 -0.00290 0.01330  0.02478  161 VAL B N   
5800 C  CA  . VAL B  161 ? 0.20558 0.30191 0.21572 -0.00483 0.01163  0.02158  161 VAL B CA  
5801 C  C   . VAL B  161 ? 0.25018 0.34800 0.26118 -0.00978 0.01527  0.02505  161 VAL B C   
5802 O  O   . VAL B  161 ? 0.24720 0.35570 0.25859 -0.01075 0.01796  0.02625  161 VAL B O   
5803 C  CB  . VAL B  161 ? 0.21128 0.31708 0.22526 -0.00175 0.00833  0.01453  161 VAL B CB  
5804 C  CG1 . VAL B  161 ? 0.22132 0.32518 0.23922 -0.00407 0.00694  0.01140  161 VAL B CG1 
5805 C  CG2 . VAL B  161 ? 0.21528 0.31841 0.22858 0.00296  0.00445  0.01099  161 VAL B CG2 
5815 N  N   . ASP B  162 ? 0.22787 0.31518 0.23941 -0.01291 0.01517  0.02632  162 ASP B N   
5816 C  CA  . ASP B  162 ? 0.22838 0.31660 0.24152 -0.01761 0.01788  0.02855  162 ASP B CA  
5817 C  C   . ASP B  162 ? 0.24096 0.33489 0.25891 -0.01748 0.01549  0.02270  162 ASP B C   
5818 O  O   . ASP B  162 ? 0.24056 0.32726 0.26013 -0.01672 0.01222  0.01933  162 ASP B O   
5819 C  CB  . ASP B  162 ? 0.23033 0.30408 0.24150 -0.02092 0.01889  0.03287  162 ASP B CB  
5820 C  CG  . ASP B  162 ? 0.25997 0.33353 0.27247 -0.02594 0.02175  0.03563  162 ASP B CG  
5821 O  OD1 . ASP B  162 ? 0.26805 0.35168 0.28386 -0.02687 0.02215  0.03306  162 ASP B OD1 
5822 O  OD2 . ASP B  162 ? 0.26140 0.32478 0.27161 -0.02911 0.02372  0.04053  162 ASP B OD2 
5827 N  N   . PRO B  163 ? 0.22774 0.33450 0.24808 -0.01804 0.01686  0.02119  163 PRO B N   
5828 C  CA  . PRO B  163 ? 0.22259 0.33540 0.24752 -0.01751 0.01439  0.01530  163 PRO B CA  
5829 C  C   . PRO B  163 ? 0.22170 0.32673 0.24879 -0.02115 0.01405  0.01519  163 PRO B C   
5830 O  O   . PRO B  163 ? 0.24513 0.35293 0.27599 -0.02062 0.01149  0.01007  163 PRO B O   
5831 C  CB  . PRO B  163 ? 0.26522 0.39292 0.29166 -0.01807 0.01686  0.01517  163 PRO B CB  
5832 C  CG  . PRO B  163 ? 0.31542 0.44198 0.33854 -0.02101 0.02131  0.02209  163 PRO B CG  
5833 C  CD  . PRO B  163 ? 0.26926 0.38545 0.28829 -0.01942 0.02085  0.02497  163 PRO B CD  
5841 N  N   . ASN B  164 ? 0.23135 0.32695 0.25622 -0.02487 0.01657  0.02064  164 ASN B N   
5842 C  CA  . ASN B  164 ? 0.25156 0.33957 0.27831 -0.02853 0.01645  0.02087  164 ASN B CA  
5843 C  C   . ASN B  164 ? 0.22106 0.29603 0.24750 -0.02737 0.01308  0.01907  164 ASN B C   
5844 O  O   . ASN B  164 ? 0.23920 0.30655 0.26703 -0.03015 0.01261  0.01910  164 ASN B O   
5845 C  CB  . ASN B  164 ? 0.29318 0.37648 0.31760 -0.03317 0.02068  0.02768  164 ASN B CB  
5846 C  CG  . ASN B  164 ? 0.38340 0.47883 0.40811 -0.03480 0.02422  0.02993  164 ASN B CG  
5847 O  OD1 . ASN B  164 ? 0.34947 0.45454 0.37765 -0.03528 0.02410  0.02682  164 ASN B OD1 
5848 N  ND2 . ASN B  164 ? 0.48974 0.58502 0.51077 -0.03553 0.02738  0.03530  164 ASN B ND2 
5855 N  N   . ARG B  165 ? 0.20546 0.27716 0.22993 -0.02344 0.01079  0.01778  165 ARG B N   
5856 C  CA  . ARG B  165 ? 0.19194 0.25039 0.21542 -0.02241 0.00798  0.01705  165 ARG B CA  
5857 C  C   . ARG B  165 ? 0.18980 0.25113 0.21450 -0.01743 0.00381  0.01128  165 ARG B C   
5858 O  O   . ARG B  165 ? 0.20888 0.27114 0.23112 -0.01421 0.00326  0.01168  165 ARG B O   
5859 C  CB  . ARG B  165 ? 0.20390 0.25247 0.22262 -0.02335 0.01013  0.02323  165 ARG B CB  
5860 C  CG  . ARG B  165 ? 0.22643 0.27358 0.24388 -0.02819 0.01446  0.02901  165 ARG B CG  
5861 C  CD  . ARG B  165 ? 0.22276 0.25837 0.23569 -0.02961 0.01645  0.03514  165 ARG B CD  
5862 N  NE  . ARG B  165 ? 0.21766 0.25642 0.22729 -0.02690 0.01741  0.03728  165 ARG B NE  
5863 C  CZ  . ARG B  165 ? 0.22039 0.25153 0.22726 -0.02419 0.01579  0.03789  165 ARG B CZ  
5864 N  NH1 . ARG B  165 ? 0.22263 0.24333 0.22988 -0.02322 0.01265  0.03574  165 ARG B NH1 
5865 N  NH2 . ARG B  165 ? 0.23546 0.26956 0.23909 -0.02241 0.01738  0.04076  165 ARG B NH2 
5879 N  N   . LEU B  166 ? 0.20274 0.24776 0.24340 0.00698  -0.00652 0.00160  166 LEU B N   
5880 C  CA  . LEU B  166 ? 0.17460 0.21771 0.21251 0.01296  -0.00535 -0.00021 166 LEU B CA  
5881 C  C   . LEU B  166 ? 0.18341 0.22257 0.22077 0.01517  -0.00864 -0.00124 166 LEU B C   
5882 O  O   . LEU B  166 ? 0.17980 0.22384 0.22218 0.01393  -0.01112 -0.00040 166 LEU B O   
5883 C  CB  . LEU B  166 ? 0.20294 0.25679 0.24590 0.01634  -0.00270 0.00032  166 LEU B CB  
5884 C  CG  . LEU B  166 ? 0.20555 0.26479 0.24965 0.01480  0.00091  0.00168  166 LEU B CG  
5885 C  CD1 . LEU B  166 ? 0.24988 0.32071 0.29969 0.01831  0.00320  0.00244  166 LEU B CD1 
5886 C  CD2 . LEU B  166 ? 0.23997 0.29136 0.27669 0.01599  0.00301  0.00031  166 LEU B CD2 
5898 N  N   . GLY B  167 ? 0.18513 0.21560 0.21663 0.01867  -0.00869 -0.00305 167 GLY B N   
5899 C  CA  . GLY B  167 ? 0.18775 0.21398 0.21830 0.02131  -0.01144 -0.00386 167 GLY B CA  
5900 C  C   . GLY B  167 ? 0.18265 0.20702 0.21125 0.02739  -0.01012 -0.00545 167 GLY B C   
5901 O  O   . GLY B  167 ? 0.18865 0.21292 0.21535 0.02953  -0.00733 -0.00632 167 GLY B O   
5905 N  N   . ALA B  168 ? 0.17505 0.19770 0.20404 0.03038  -0.01232 -0.00586 168 ALA B N   
5906 C  CA  . ALA B  168 ? 0.17870 0.19851 0.20574 0.03618  -0.01147 -0.00732 168 ALA B CA  
5907 C  C   . ALA B  168 ? 0.19120 0.20274 0.21522 0.03774  -0.01406 -0.00765 168 ALA B C   
5908 O  O   . ALA B  168 ? 0.19588 0.20790 0.22140 0.03585  -0.01676 -0.00670 168 ALA B O   
5909 C  CB  . ALA B  168 ? 0.20083 0.23100 0.23310 0.04006  -0.01036 -0.00732 168 ALA B CB  
5915 N  N   . VAL B  169 ? 0.19779 0.20203 0.21780 0.04152  -0.01319 -0.00901 169 VAL B N   
5916 C  CA  . VAL B  169 ? 0.19549 0.19138 0.21247 0.04392  -0.01498 -0.00928 169 VAL B CA  
5917 C  C   . VAL B  169 ? 0.19482 0.19126 0.21232 0.04999  -0.01385 -0.01041 169 VAL B C   
5918 O  O   . VAL B  169 ? 0.21208 0.20802 0.22840 0.05199  -0.01160 -0.01172 169 VAL B O   
5919 C  CB  . VAL B  169 ? 0.19381 0.17840 0.20494 0.04204  -0.01487 -0.00984 169 VAL B CB  
5920 C  CG1 . VAL B  169 ? 0.23162 0.20776 0.24000 0.04456  -0.01656 -0.00975 169 VAL B CG1 
5921 C  CG2 . VAL B  169 ? 0.19951 0.18366 0.20974 0.03602  -0.01572 -0.00887 169 VAL B CG2 
5931 N  N   . GLY B  170 ? 0.19410 0.19136 0.21313 0.05319  -0.01547 -0.01001 170 GLY B N   
5932 C  CA  . GLY B  170 ? 0.21011 0.20848 0.22990 0.05901  -0.01449 -0.01101 170 GLY B CA  
5933 C  C   . GLY B  170 ? 0.21837 0.21055 0.23658 0.06253  -0.01609 -0.01075 170 GLY B C   
5934 O  O   . GLY B  170 ? 0.21846 0.21104 0.23745 0.06165  -0.01833 -0.00951 170 GLY B O   
5938 N  N   . TRP B  171 ? 0.22184 0.20832 0.23791 0.06677  -0.01498 -0.01191 171 TRP B N   
5939 C  CA  . TRP B  171 ? 0.22444 0.20442 0.23901 0.07064  -0.01607 -0.01156 171 TRP B CA  
5940 C  C   . TRP B  171 ? 0.25074 0.23698 0.26831 0.07593  -0.01593 -0.01188 171 TRP B C   
5941 O  O   . TRP B  171 ? 0.23379 0.22396 0.25253 0.07860  -0.01424 -0.01324 171 TRP B O   
5942 C  CB  . TRP B  171 ? 0.27286 0.24179 0.28347 0.07187  -0.01512 -0.01255 171 TRP B CB  
5943 C  CG  . TRP B  171 ? 0.25515 0.21732 0.26465 0.07632  -0.01577 -0.01214 171 TRP B CG  
5944 C  CD1 . TRP B  171 ? 0.26918 0.22968 0.27863 0.07728  -0.01753 -0.01038 171 TRP B CD1 
5945 C  CD2 . TRP B  171 ? 0.29032 0.24646 0.29868 0.08050  -0.01466 -0.01344 171 TRP B CD2 
5946 N  NE1 . TRP B  171 ? 0.27975 0.23355 0.28811 0.08178  -0.01736 -0.01027 171 TRP B NE1 
5947 C  CE2 . TRP B  171 ? 0.30051 0.25145 0.30837 0.08371  -0.01567 -0.01218 171 TRP B CE2 
5948 C  CE3 . TRP B  171 ? 0.30161 0.25611 0.30932 0.08199  -0.01299 -0.01561 171 TRP B CE3 
5949 C  CZ2 . TRP B  171 ? 0.35090 0.29484 0.35795 0.08803  -0.01502 -0.01288 171 TRP B CZ2 
5950 C  CZ3 . TRP B  171 ? 0.33971 0.28730 0.34657 0.08635  -0.01260 -0.01658 171 TRP B CZ3 
5951 C  CH2 . TRP B  171 ? 0.35429 0.29653 0.36097 0.08916  -0.01358 -0.01516 171 TRP B CH2 
5962 N  N   . SER B  172 ? 0.22759 0.21497 0.24624 0.07764  -0.01777 -0.01066 172 SER B N   
5963 C  CA  . SER B  172 ? 0.24592 0.23710 0.26654 0.08330  -0.01784 -0.01090 172 SER B CA  
5964 C  C   . SER B  172 ? 0.24142 0.24468 0.26630 0.08387  -0.01696 -0.01164 172 SER B C   
5965 O  O   . SER B  172 ? 0.23909 0.24963 0.26683 0.08026  -0.01779 -0.01094 172 SER B O   
5966 C  CB  . SER B  172 ? 0.28480 0.26711 0.30268 0.08766  -0.01686 -0.01165 172 SER B CB  
5967 O  OG  . SER B  172 ? 0.32157 0.30595 0.34075 0.09294  -0.01749 -0.01130 172 SER B OG  
5973 N  N   . MET B  173 ? 0.23454 0.24051 0.26018 0.08817  -0.01537 -0.01298 173 MET B N   
5974 C  CA  . MET B  173 ? 0.26125 0.27924 0.29102 0.08857  -0.01444 -0.01345 173 MET B CA  
5975 C  C   . MET B  173 ? 0.25425 0.27584 0.28489 0.08315  -0.01341 -0.01333 173 MET B C   
5976 O  O   . MET B  173 ? 0.23415 0.26608 0.26894 0.08144  -0.01318 -0.01287 173 MET B O   
5977 C  CB  . MET B  173 ? 0.26050 0.28010 0.29025 0.09406  -0.01279 -0.01503 173 MET B CB  
5978 C  CG  . MET B  173 ? 0.28330 0.30317 0.31358 0.09964  -0.01369 -0.01506 173 MET B CG  
5979 S  SD  . MET B  173 ? 0.32052 0.34597 0.35185 0.10554  -0.01185 -0.01693 173 MET B SD  
5980 C  CE  . MET B  173 ? 0.39801 0.42094 0.42897 0.11179  -0.01318 -0.01675 173 MET B CE  
5990 N  N   . GLY B  174 ? 0.23878 0.25207 0.26568 0.08053  -0.01266 -0.01372 174 GLY B N   
5991 C  CA  . GLY B  174 ? 0.21814 0.23418 0.24546 0.07525  -0.01178 -0.01340 174 GLY B CA  
5992 C  C   . GLY B  174 ? 0.22098 0.23943 0.25007 0.07030  -0.01370 -0.01175 174 GLY B C   
5993 O  O   . GLY B  174 ? 0.21547 0.24015 0.24699 0.06624  -0.01321 -0.01114 174 GLY B O   
5997 N  N   . GLY B  175 ? 0.21408 0.22717 0.24181 0.07057  -0.01592 -0.01098 175 GLY B N   
5998 C  CA  . GLY B  175 ? 0.19238 0.20852 0.22212 0.06684  -0.01822 -0.00960 175 GLY B CA  
5999 C  C   . GLY B  175 ? 0.20432 0.23244 0.23987 0.06785  -0.01900 -0.00925 175 GLY B C   
6000 O  O   . GLY B  175 ? 0.21746 0.25162 0.25633 0.06371  -0.01998 -0.00845 175 GLY B O   
6004 N  N   . GLY B  176 ? 0.20750 0.23916 0.24449 0.07326  -0.01860 -0.00988 176 GLY B N   
6005 C  CA  . GLY B  176 ? 0.21997 0.26392 0.26276 0.07439  -0.01889 -0.00978 176 GLY B CA  
6006 C  C   . GLY B  176 ? 0.20640 0.25838 0.25248 0.07134  -0.01691 -0.00972 176 GLY B C   
6007 O  O   . GLY B  176 ? 0.20327 0.26406 0.25437 0.06844  -0.01768 -0.00892 176 GLY B O   
6011 N  N   . GLY B  177 ? 0.20310 0.25208 0.24650 0.07194  -0.01434 -0.01051 177 GLY B N   
6012 C  CA  . GLY B  177 ? 0.20591 0.26237 0.25206 0.06936  -0.01221 -0.01024 177 GLY B CA  
6013 C  C   . GLY B  177 ? 0.18144 0.23807 0.22854 0.06268  -0.01282 -0.00899 177 GLY B C   
6014 O  O   . GLY B  177 ? 0.19759 0.26352 0.24949 0.05985  -0.01208 -0.00804 177 GLY B O   
6018 N  N   . THR B  178 ? 0.19543 0.24178 0.23804 0.06016  -0.01407 -0.00890 178 THR B N   
6019 C  CA  . THR B  178 ? 0.19338 0.23851 0.23615 0.05393  -0.01502 -0.00780 178 THR B CA  
6020 C  C   . THR B  178 ? 0.18824 0.24081 0.23644 0.05162  -0.01757 -0.00671 178 THR B C   
6021 O  O   . THR B  178 ? 0.18778 0.24621 0.23972 0.04708  -0.01756 -0.00569 178 THR B O   
6022 C  CB  . THR B  178 ? 0.19798 0.23032 0.23454 0.05254  -0.01608 -0.00804 178 THR B CB  
6023 O  OG1 . THR B  178 ? 0.20495 0.23107 0.23715 0.05374  -0.01370 -0.00914 178 THR B OG1 
6024 C  CG2 . THR B  178 ? 0.20379 0.23452 0.24019 0.04638  -0.01752 -0.00696 178 THR B CG2 
6032 N  N   . LEU B  179 ? 0.19674 0.24864 0.24535 0.05464  -0.01992 -0.00690 179 LEU B N   
6033 C  CA  . LEU B  179 ? 0.19631 0.25535 0.25016 0.05300  -0.02264 -0.00620 179 LEU B CA  
6034 C  C   . LEU B  179 ? 0.18984 0.26199 0.25072 0.05344  -0.02155 -0.00597 179 LEU B C   
6035 O  O   . LEU B  179 ? 0.20053 0.27964 0.26676 0.04970  -0.02295 -0.00513 179 LEU B O   
6036 C  CB  . LEU B  179 ? 0.19845 0.25417 0.25086 0.05717  -0.02512 -0.00660 179 LEU B CB  
6037 C  CG  . LEU B  179 ? 0.21492 0.25848 0.26109 0.05655  -0.02655 -0.00643 179 LEU B CG  
6038 C  CD1 . LEU B  179 ? 0.24118 0.28150 0.28565 0.06159  -0.02840 -0.00662 179 LEU B CD1 
6039 C  CD2 . LEU B  179 ? 0.27540 0.31773 0.32196 0.05075  -0.02883 -0.00559 179 LEU B CD2 
6051 N  N   . ARG B  180 ? 0.19023 0.26579 0.25131 0.05783  -0.01909 -0.00666 180 ARG B N   
6052 C  CA  . ARG B  180 ? 0.20357 0.29165 0.27101 0.05832  -0.01758 -0.00629 180 ARG B CA  
6053 C  C   . ARG B  180 ? 0.20365 0.29581 0.27361 0.05302  -0.01580 -0.00508 180 ARG B C   
6054 O  O   . ARG B  180 ? 0.21981 0.32216 0.29654 0.05061  -0.01591 -0.00404 180 ARG B O   
6055 C  CB  . ARG B  180 ? 0.19025 0.27991 0.25626 0.06427  -0.01519 -0.00736 180 ARG B CB  
6056 C  CG  . ARG B  180 ? 0.19358 0.28237 0.25898 0.06971  -0.01691 -0.00830 180 ARG B CG  
6057 C  CD  . ARG B  180 ? 0.21366 0.30159 0.27641 0.07564  -0.01468 -0.00951 180 ARG B CD  
6058 N  NE  . ARG B  180 ? 0.22469 0.31328 0.28751 0.08112  -0.01607 -0.01030 180 ARG B NE  
6059 C  CZ  . ARG B  180 ? 0.23728 0.33635 0.30513 0.08377  -0.01636 -0.01042 180 ARG B CZ  
6060 N  NH1 . ARG B  180 ? 0.24425 0.35443 0.31784 0.08161  -0.01520 -0.00974 180 ARG B NH1 
6061 N  NH2 . ARG B  180 ? 0.25511 0.35359 0.32225 0.08887  -0.01772 -0.01118 180 ARG B NH2 
6075 N  N   . LEU B  181 ? 0.19863 0.28311 0.26340 0.05124  -0.01404 -0.00514 181 LEU B N   
6076 C  CA  . LEU B  181 ? 0.18662 0.27479 0.25342 0.04644  -0.01215 -0.00387 181 LEU B CA  
6077 C  C   . LEU B  181 ? 0.19146 0.27964 0.26092 0.04047  -0.01471 -0.00269 181 LEU B C   
6078 O  O   . LEU B  181 ? 0.21593 0.31200 0.29092 0.03667  -0.01408 -0.00126 181 LEU B O   
6079 C  CB  . LEU B  181 ? 0.19620 0.27567 0.25627 0.04652  -0.00976 -0.00452 181 LEU B CB  
6080 C  CG  . LEU B  181 ? 0.19721 0.28041 0.25857 0.04254  -0.00720 -0.00327 181 LEU B CG  
6081 C  CD1 . LEU B  181 ? 0.21095 0.30652 0.27802 0.04409  -0.00473 -0.00238 181 LEU B CD1 
6082 C  CD2 . LEU B  181 ? 0.21405 0.28759 0.26805 0.04299  -0.00519 -0.00429 181 LEU B CD2 
6094 N  N   . ALA B  182 ? 0.19071 0.27049 0.25661 0.03982  -0.01766 -0.00320 182 ALA B N   
6095 C  CA  . ALA B  182 ? 0.19949 0.27944 0.26800 0.03485  -0.02076 -0.00235 182 ALA B CA  
6096 C  C   . ALA B  182 ? 0.21706 0.30863 0.29408 0.03454  -0.02248 -0.00183 182 ALA B C   
6097 O  O   . ALA B  182 ? 0.24579 0.34273 0.32804 0.02972  -0.02332 -0.00067 182 ALA B O   
6098 C  CB  . ALA B  182 ? 0.21524 0.28468 0.27824 0.03547  -0.02368 -0.00308 182 ALA B CB  
6104 N  N   . ALA B  183 ? 0.19211 0.28808 0.27097 0.03968  -0.02286 -0.00269 183 ALA B N   
6105 C  CA  . ALA B  183 ? 0.21353 0.32067 0.30056 0.03973  -0.02463 -0.00242 183 ALA B CA  
6106 C  C   . ALA B  183 ? 0.25421 0.37234 0.34798 0.03739  -0.02202 -0.00108 183 ALA B C   
6107 O  O   . ALA B  183 ? 0.27837 0.40554 0.37991 0.03493  -0.02354 -0.00035 183 ALA B O   
6108 C  CB  . ALA B  183 ? 0.22505 0.33398 0.31167 0.04630  -0.02514 -0.00371 183 ALA B CB  
6114 N  N   . ASP B  184 ? 0.22020 0.33787 0.31131 0.03826  -0.01814 -0.00071 184 ASP B N   
6115 C  CA  . ASP B  184 ? 0.23118 0.35867 0.32782 0.03629  -0.01513 0.00087  184 ASP B CA  
6116 C  C   . ASP B  184 ? 0.26916 0.39458 0.36602 0.02992  -0.01432 0.00247  184 ASP B C   
6117 O  O   . ASP B  184 ? 0.28634 0.41845 0.38660 0.02824  -0.01126 0.00404  184 ASP B O   
6118 C  CB  . ASP B  184 ? 0.24402 0.37219 0.33723 0.04110  -0.01129 0.00038  184 ASP B CB  
6119 C  CG  . ASP B  184 ? 0.33390 0.46892 0.42972 0.04691  -0.01127 -0.00058 184 ASP B CG  
6120 O  OD1 . ASP B  184 ? 0.38644 0.52809 0.48815 0.04673  -0.01371 -0.00052 184 ASP B OD1 
6121 O  OD2 . ASP B  184 ? 0.29810 0.43174 0.38999 0.05173  -0.00895 -0.00151 184 ASP B OD2 
6126 N  N   . ASP B  185 ? 0.26644 0.38279 0.35955 0.02654  -0.01685 0.00221  185 ASP B N   
6127 C  CA  . ASP B  185 ? 0.30711 0.42059 0.39987 0.02050  -0.01641 0.00361  185 ASP B CA  
6128 C  C   . ASP B  185 ? 0.26979 0.37928 0.35719 0.02077  -0.01237 0.00394  185 ASP B C   
6129 O  O   . ASP B  185 ? 0.28749 0.39895 0.37646 0.01668  -0.01056 0.00556  185 ASP B O   
6130 C  CB  . ASP B  185 ? 0.29564 0.41979 0.39800 0.01606  -0.01689 0.00549  185 ASP B CB  
6131 C  CG  . ASP B  185 ? 0.68632 0.81570 0.79477 0.01638  -0.02090 0.00487  185 ASP B CG  
6132 O  OD1 . ASP B  185 ? 0.71776 0.83994 0.82214 0.01779  -0.02416 0.00333  185 ASP B OD1 
6133 O  OD2 . ASP B  185 ? 0.88890 1.02968 1.00620 0.01543  -0.02079 0.00592  185 ASP B OD2 
6138 N  N   . GLY B  186 ? 0.21787 0.32132 0.29881 0.02560  -0.01106 0.00237  186 GLY B N   
6139 C  CA  . GLY B  186 ? 0.23782 0.33794 0.31382 0.02666  -0.00739 0.00230  186 GLY B CA  
6140 C  C   . GLY B  186 ? 0.21849 0.30628 0.28678 0.02452  -0.00770 0.00162  186 GLY B C   
6141 O  O   . GLY B  186 ? 0.26407 0.34838 0.32784 0.02546  -0.00485 0.00130  186 GLY B O   
6145 N  N   . ILE B  187 ? 0.20638 0.28748 0.27290 0.02188  -0.01117 0.00130  187 ILE B N   
6146 C  CA  . ILE B  187 ? 0.18676 0.25584 0.24592 0.01984  -0.01193 0.00063  187 ILE B CA  
6147 C  C   . ILE B  187 ? 0.19920 0.26626 0.25998 0.01490  -0.01553 0.00137  187 ILE B C   
6148 O  O   . ILE B  187 ? 0.20790 0.28088 0.27439 0.01444  -0.01812 0.00173  187 ILE B O   
6149 C  CB  . ILE B  187 ? 0.20638 0.26610 0.25890 0.02453  -0.01246 -0.00133 187 ILE B CB  
6150 C  CG1 . ILE B  187 ? 0.20368 0.26631 0.25883 0.02853  -0.01465 -0.00199 187 ILE B CG1 
6151 C  CG2 . ILE B  187 ? 0.23848 0.29603 0.28691 0.02810  -0.00888 -0.00234 187 ILE B CG2 
6152 C  CD1 . ILE B  187 ? 0.21193 0.26528 0.26104 0.03292  -0.01524 -0.00357 187 ILE B CD1 
6164 N  N   . GLN B  188 ? 0.17968 0.23817 0.23522 0.01144  -0.01586 0.00141  188 GLN B N   
6165 C  CA  . GLN B  188 ? 0.19533 0.25048 0.25109 0.00664  -0.01913 0.00199  188 GLN B CA  
6166 C  C   . GLN B  188 ? 0.20191 0.24684 0.25169 0.00800  -0.02209 0.00071  188 GLN B C   
6167 O  O   . GLN B  188 ? 0.21494 0.25713 0.26476 0.00484  -0.02539 0.00099  188 GLN B O   
6168 C  CB  . GLN B  188 ? 0.23302 0.28572 0.28691 0.00168  -0.01750 0.00307  188 GLN B CB  
6169 C  CG  . GLN B  188 ? 0.23263 0.29630 0.29397 -0.00102 -0.01537 0.00503  188 GLN B CG  
6170 C  CD  . GLN B  188 ? 0.23923 0.30972 0.30240 0.00302  -0.01148 0.00515  188 GLN B CD  
6171 O  OE1 . GLN B  188 ? 0.21779 0.28412 0.27557 0.00513  -0.00861 0.00446  188 GLN B OE1 
6172 N  NE2 . GLN B  188 ? 0.26120 0.34255 0.33215 0.00413  -0.01138 0.00598  188 GLN B NE2 
6181 N  N   . ALA B  189 ? 0.18186 0.22132 0.22679 0.01277  -0.02104 -0.00061 189 ALA B N   
6182 C  CA  . ALA B  189 ? 0.17545 0.20626 0.21554 0.01485  -0.02361 -0.00154 189 ALA B CA  
6183 C  C   . ALA B  189 ? 0.17340 0.20254 0.21140 0.02090  -0.02204 -0.00271 189 ALA B C   
6184 O  O   . ALA B  189 ? 0.19055 0.22085 0.22772 0.02282  -0.01881 -0.00316 189 ALA B O   
6185 C  CB  . ALA B  189 ? 0.19104 0.21102 0.22418 0.01203  -0.02406 -0.00174 189 ALA B CB  
6191 N  N   . ALA B  190 ? 0.17975 0.20608 0.21683 0.02407  -0.02444 -0.00317 190 ALA B N   
6192 C  CA  . ALA B  190 ? 0.16470 0.18939 0.20020 0.02997  -0.02334 -0.00415 190 ALA B CA  
6193 C  C   . ALA B  190 ? 0.18365 0.19825 0.21376 0.03189  -0.02522 -0.00450 190 ALA B C   
6194 O  O   . ALA B  190 ? 0.20639 0.21912 0.23626 0.03025  -0.02831 -0.00395 190 ALA B O   
6195 C  CB  . ALA B  190 ? 0.20224 0.23663 0.24378 0.03316  -0.02404 -0.00412 190 ALA B CB  
6201 N  N   . ILE B  191 ? 0.18535 0.19354 0.21132 0.03553  -0.02344 -0.00538 191 ILE B N   
6202 C  CA  . ILE B  191 ? 0.19454 0.19368 0.21606 0.03829  -0.02480 -0.00552 191 ILE B CA  
6203 C  C   . ILE B  191 ? 0.19829 0.19825 0.22044 0.04436  -0.02367 -0.00624 191 ILE B C   
6204 O  O   . ILE B  191 ? 0.20552 0.20618 0.22747 0.04633  -0.02101 -0.00718 191 ILE B O   
6205 C  CB  . ILE B  191 ? 0.19519 0.18356 0.21053 0.03642  -0.02400 -0.00583 191 ILE B CB  
6206 C  CG1 . ILE B  191 ? 0.20173 0.18889 0.21600 0.03048  -0.02527 -0.00512 191 ILE B CG1 
6207 C  CG2 . ILE B  191 ? 0.21854 0.19817 0.23000 0.03976  -0.02510 -0.00572 191 ILE B CG2 
6208 C  CD1 . ILE B  191 ? 0.21986 0.19668 0.22793 0.02834  -0.02449 -0.00550 191 ILE B CD1 
6220 N  N   . GLY B  192 ? 0.19973 0.19953 0.22246 0.04761  -0.02570 -0.00585 192 GLY B N   
6221 C  CA  . GLY B  192 ? 0.19966 0.19892 0.22237 0.05353  -0.02482 -0.00639 192 GLY B CA  
6222 C  C   . GLY B  192 ? 0.21464 0.20263 0.23217 0.05568  -0.02520 -0.00615 192 GLY B C   
6223 O  O   . GLY B  192 ? 0.23648 0.22018 0.25199 0.05446  -0.02740 -0.00515 192 GLY B O   
6227 N  N   . LEU B  193 ? 0.21554 0.19873 0.23102 0.05876  -0.02303 -0.00705 193 LEU B N   
6228 C  CA  . LEU B  193 ? 0.22731 0.19970 0.23851 0.06108  -0.02300 -0.00681 193 LEU B CA  
6229 C  C   . LEU B  193 ? 0.22815 0.20173 0.24073 0.06715  -0.02304 -0.00676 193 LEU B C   
6230 O  O   . LEU B  193 ? 0.22913 0.20547 0.24319 0.07033  -0.02132 -0.00791 193 LEU B O   
6231 C  CB  . LEU B  193 ? 0.22155 0.18755 0.22992 0.06052  -0.02071 -0.00806 193 LEU B CB  
6232 C  CG  . LEU B  193 ? 0.21809 0.18437 0.22540 0.05522  -0.01993 -0.00855 193 LEU B CG  
6233 C  CD1 . LEU B  193 ? 0.24199 0.20267 0.24683 0.05610  -0.01762 -0.01018 193 LEU B CD1 
6234 C  CD2 . LEU B  193 ? 0.22830 0.18947 0.23281 0.05086  -0.02176 -0.00739 193 LEU B CD2 
6246 N  N   . ALA B  194 ? 0.23088 0.20263 0.24291 0.06911  -0.02500 -0.00544 194 ALA B N   
6247 C  CA  . ALA B  194 ? 0.23757 0.21042 0.25071 0.07501  -0.02511 -0.00521 194 ALA B CA  
6248 C  C   . ALA B  194 ? 0.24213 0.22539 0.25964 0.07711  -0.02424 -0.00641 194 ALA B C   
6249 O  O   . ALA B  194 ? 0.25355 0.23646 0.27135 0.08122  -0.02265 -0.00729 194 ALA B O   
6250 C  CB  . ALA B  194 ? 0.27200 0.23516 0.28216 0.07833  -0.02365 -0.00523 194 ALA B CB  
6256 N  N   . PRO B  195 ? 0.22790 0.22032 0.24892 0.07434  -0.02528 -0.00644 195 PRO B N   
6257 C  CA  . PRO B  195 ? 0.23375 0.23647 0.25917 0.07562  -0.02416 -0.00748 195 PRO B CA  
6258 C  C   . PRO B  195 ? 0.23725 0.24380 0.26448 0.08167  -0.02442 -0.00767 195 PRO B C   
6259 O  O   . PRO B  195 ? 0.24983 0.25425 0.27623 0.08423  -0.02618 -0.00679 195 PRO B O   
6260 C  CB  . PRO B  195 ? 0.22509 0.23597 0.25416 0.07109  -0.02584 -0.00702 195 PRO B CB  
6261 C  CG  . PRO B  195 ? 0.22643 0.23251 0.25342 0.06995  -0.02856 -0.00585 195 PRO B CG  
6262 C  CD  . PRO B  195 ? 0.23723 0.23128 0.25869 0.07001  -0.02768 -0.00549 195 PRO B CD  
6270 N  N   . TRP B  196 ? 0.22868 0.24148 0.25838 0.08402  -0.02265 -0.00883 196 TRP B N   
6271 C  CA  . TRP B  196 ? 0.23325 0.25115 0.26503 0.08975  -0.02262 -0.00929 196 TRP B CA  
6272 C  C   . TRP B  196 ? 0.23794 0.26835 0.27483 0.08921  -0.02198 -0.01001 196 TRP B C   
6273 O  O   . TRP B  196 ? 0.23857 0.27165 0.27631 0.08650  -0.02024 -0.01054 196 TRP B O   
6274 C  CB  . TRP B  196 ? 0.25599 0.26719 0.28491 0.09425  -0.02072 -0.01014 196 TRP B CB  
6275 C  CG  . TRP B  196 ? 0.29160 0.30590 0.32165 0.10069  -0.02067 -0.01058 196 TRP B CG  
6276 C  CD1 . TRP B  196 ? 0.33126 0.33954 0.35916 0.10501  -0.02140 -0.00988 196 TRP B CD1 
6277 C  CD2 . TRP B  196 ? 0.29911 0.32300 0.33247 0.10363  -0.01969 -0.01173 196 TRP B CD2 
6278 N  NE1 . TRP B  196 ? 0.31234 0.32565 0.34187 0.11054  -0.02102 -0.01063 196 TRP B NE1 
6279 C  CE2 . TRP B  196 ? 0.28717 0.31019 0.32003 0.10977  -0.02002 -0.01184 196 TRP B CE2 
6280 C  CE3 . TRP B  196 ? 0.28073 0.31403 0.31744 0.10183  -0.01850 -0.01254 196 TRP B CE3 
6281 C  CZ2 . TRP B  196 ? 0.31187 0.34307 0.34730 0.11406  -0.01933 -0.01291 196 TRP B CZ2 
6282 C  CZ3 . TRP B  196 ? 0.29011 0.33180 0.32957 0.10617  -0.01775 -0.01347 196 TRP B CZ3 
6283 C  CH2 . TRP B  196 ? 0.29872 0.33926 0.33742 0.11215  -0.01823 -0.01374 196 TRP B CH2 
6294 N  N   . ASN B  197 ? 0.23418 0.27245 0.27455 0.09187  -0.02339 -0.00995 197 ASN B N   
6295 C  CA  . ASN B  197 ? 0.20831 0.25903 0.25403 0.09212  -0.02283 -0.01055 197 ASN B CA  
6296 C  C   . ASN B  197 ? 0.23814 0.29396 0.28585 0.09748  -0.02412 -0.01082 197 ASN B C   
6297 O  O   . ASN B  197 ? 0.25476 0.30593 0.30050 0.09950  -0.02598 -0.01025 197 ASN B O   
6298 C  CB  . ASN B  197 ? 0.22546 0.28280 0.27515 0.08606  -0.02390 -0.00990 197 ASN B CB  
6299 C  CG  . ASN B  197 ? 0.23124 0.29984 0.28600 0.08503  -0.02226 -0.01026 197 ASN B CG  
6300 O  OD1 . ASN B  197 ? 0.24859 0.31686 0.30230 0.08488  -0.01967 -0.01069 197 ASN B OD1 
6301 N  ND2 . ASN B  197 ? 0.22940 0.30833 0.28990 0.08439  -0.02377 -0.01006 197 ASN B ND2 
6308 N  N   . THR B  198 ? 0.22890 0.29472 0.28055 0.09989  -0.02314 -0.01162 198 THR B N   
6309 C  CA  . THR B  198 ? 0.23928 0.31006 0.29265 0.10528  -0.02434 -0.01202 198 THR B CA  
6310 C  C   . THR B  198 ? 0.24040 0.31852 0.29808 0.10359  -0.02716 -0.01164 198 THR B C   
6311 O  O   . THR B  198 ? 0.28900 0.36956 0.34731 0.10801  -0.02869 -0.01192 198 THR B O   
6312 C  CB  . THR B  198 ? 0.28247 0.36161 0.33843 0.10908  -0.02249 -0.01311 198 THR B CB  
6313 O  OG1 . THR B  198 ? 0.28851 0.37770 0.34956 0.10506  -0.02178 -0.01301 198 THR B OG1 
6314 C  CG2 . THR B  198 ? 0.33764 0.40961 0.38928 0.11205  -0.02005 -0.01386 198 THR B CG2 
6322 N  N   . SER B  199 ? 0.21949 0.30089 0.28007 0.09758  -0.02802 -0.01109 199 SER B N   
6323 C  CA  . SER B  199 ? 0.20584 0.29442 0.27110 0.09573  -0.03095 -0.01094 199 SER B CA  
6324 C  C   . SER B  199 ? 0.20586 0.29126 0.27115 0.08915  -0.03221 -0.01008 199 SER B C   
6325 O  O   . SER B  199 ? 0.21957 0.30231 0.28380 0.08516  -0.03031 -0.00968 199 SER B O   
6326 C  CB  . SER B  199 ? 0.24140 0.34388 0.31379 0.09566  -0.03056 -0.01149 199 SER B CB  
6327 O  OG  . SER B  199 ? 0.22189 0.33131 0.29947 0.09327  -0.03362 -0.01146 199 SER B OG  
6333 N  N   . SER B  200 ? 0.20430 0.29013 0.27072 0.08823  -0.03551 -0.00989 200 SER B N   
6334 C  CA  . SER B  200 ? 0.18497 0.26960 0.25244 0.08212  -0.03736 -0.00925 200 SER B CA  
6335 C  C   . SER B  200 ? 0.19499 0.29135 0.27036 0.07832  -0.03857 -0.00943 200 SER B C   
6336 O  O   . SER B  200 ? 0.20050 0.29636 0.27731 0.07263  -0.03973 -0.00885 200 SER B O   
6337 C  CB  . SER B  200 ? 0.21504 0.29403 0.27963 0.08332  -0.04071 -0.00903 200 SER B CB  
6338 O  OG  . SER B  200 ? 0.22436 0.31129 0.29300 0.08689  -0.04305 -0.00985 200 SER B OG  
6344 N  N   . LEU B  201 ? 0.19001 0.29675 0.27059 0.08112  -0.03812 -0.01013 201 LEU B N   
6345 C  CA  . LEU B  201 ? 0.18516 0.30339 0.27394 0.07824  -0.03995 -0.01034 201 LEU B CA  
6346 C  C   . LEU B  201 ? 0.19145 0.31295 0.28369 0.07181  -0.03825 -0.00937 201 LEU B C   
6347 O  O   . LEU B  201 ? 0.25208 0.37830 0.34950 0.06723  -0.04039 -0.00908 201 LEU B O   
6348 C  CB  . LEU B  201 ? 0.19776 0.32622 0.29108 0.08306  -0.03956 -0.01128 201 LEU B CB  
6349 C  CG  . LEU B  201 ? 0.21550 0.35514 0.31714 0.08142  -0.04242 -0.01181 201 LEU B CG  
6350 C  CD1 . LEU B  201 ? 0.22475 0.36110 0.32541 0.08228  -0.04681 -0.01249 201 LEU B CD1 
6351 C  CD2 . LEU B  201 ? 0.22713 0.37753 0.33346 0.08599  -0.04155 -0.01270 201 LEU B CD2 
6363 N  N   . GLY B  202 ? 0.19459 0.31368 0.28415 0.07157  -0.03451 -0.00888 202 GLY B N   
6364 C  CA  . GLY B  202 ? 0.21921 0.34157 0.31171 0.06606  -0.03252 -0.00783 202 GLY B CA  
6365 C  C   . GLY B  202 ? 0.25079 0.36500 0.34018 0.06059  -0.03339 -0.00704 202 GLY B C   
6366 O  O   . GLY B  202 ? 0.29010 0.40651 0.38174 0.05569  -0.03187 -0.00605 202 GLY B O   
6370 N  N   . PHE B  203 ? 0.20283 0.30741 0.28674 0.06141  -0.03557 -0.00733 203 PHE B N   
6371 C  CA  . PHE B  203 ? 0.19281 0.28906 0.27311 0.05657  -0.03657 -0.00664 203 PHE B CA  
6372 C  C   . PHE B  203 ? 0.20801 0.30753 0.29265 0.05288  -0.04052 -0.00657 203 PHE B C   
6373 O  O   . PHE B  203 ? 0.20735 0.30068 0.28951 0.04858  -0.04183 -0.00604 203 PHE B O   
6374 C  CB  . PHE B  203 ? 0.20854 0.29202 0.28024 0.05925  -0.03657 -0.00680 203 PHE B CB  
6375 C  CG  . PHE B  203 ? 0.19269 0.27202 0.26014 0.06278  -0.03295 -0.00705 203 PHE B CG  
6376 C  CD1 . PHE B  203 ? 0.19791 0.28165 0.26719 0.06159  -0.02967 -0.00690 203 PHE B CD1 
6377 C  CD2 . PHE B  203 ? 0.20966 0.28028 0.27116 0.06749  -0.03287 -0.00740 203 PHE B CD2 
6378 C  CE1 . PHE B  203 ? 0.21206 0.29189 0.27735 0.06524  -0.02663 -0.00741 203 PHE B CE1 
6379 C  CE2 . PHE B  203 ? 0.22930 0.29600 0.28732 0.07082  -0.02984 -0.00780 203 PHE B CE2 
6380 C  CZ  . PHE B  203 ? 0.22909 0.30030 0.28890 0.06967  -0.02682 -0.00795 203 PHE B CZ  
6390 N  N   . ARG B  204 ? 0.23629 0.34535 0.32737 0.05456  -0.04262 -0.00722 204 ARG B N   
6391 C  CA  . ARG B  204 ? 0.21720 0.32966 0.31276 0.05193  -0.04691 -0.00755 204 ARG B CA  
6392 C  C   . ARG B  204 ? 0.22104 0.33845 0.32244 0.04504  -0.04705 -0.00664 204 ARG B C   
6393 O  O   . ARG B  204 ? 0.31198 0.43148 0.41718 0.04223  -0.05084 -0.00695 204 ARG B O   
6394 C  CB  . ARG B  204 ? 0.21735 0.33849 0.31801 0.05632  -0.04910 -0.00877 204 ARG B CB  
6395 C  CG  . ARG B  204 ? 0.31138 0.42702 0.40588 0.06326  -0.04884 -0.00948 204 ARG B CG  
6396 C  CD  . ARG B  204 ? 0.57191 0.68526 0.66513 0.06589  -0.05315 -0.01037 204 ARG B CD  
6397 N  NE  . ARG B  204 ? 0.34676 0.47094 0.44817 0.06577  -0.05632 -0.01144 204 ARG B NE  
6398 C  CZ  . ARG B  204 ? 0.61886 0.74332 0.72056 0.06836  -0.06044 -0.01255 204 ARG B CZ  
6399 N  NH1 . ARG B  204 ? 0.69883 0.81401 0.79310 0.07193  -0.06159 -0.01254 204 ARG B NH1 
6400 N  NH2 . ARG B  204 ? 0.60604 0.74052 0.71582 0.06761  -0.06344 -0.01367 204 ARG B NH2 
6414 N  N   . SER B  205 ? 0.24057 0.35968 0.34287 0.04218  -0.04342 -0.00553 205 SER B N   
6415 C  CA  . SER B  205 ? 0.37978 0.50241 0.48720 0.03530  -0.04374 -0.00439 205 SER B CA  
6416 C  C   . SER B  205 ? 0.31343 0.42747 0.41474 0.03197  -0.04093 -0.00331 205 SER B C   
6417 O  O   . SER B  205 ? 0.34671 0.46432 0.45187 0.02705  -0.03972 -0.00209 205 SER B O   
6418 C  CB  . SER B  205 ? 0.53026 0.66580 0.64691 0.03408  -0.04227 -0.00375 205 SER B CB  
6419 O  OG  . SER B  205 ? 0.73975 0.87709 0.85463 0.03674  -0.03772 -0.00325 205 SER B OG  
6425 N  N   . ILE B  206 ? 0.24222 0.34596 0.33479 0.03479  -0.03965 -0.00368 206 ILE B N   
6426 C  CA  . ILE B  206 ? 0.22186 0.31732 0.30878 0.03146  -0.03745 -0.00288 206 ILE B CA  
6427 C  C   . ILE B  206 ? 0.21756 0.31006 0.30514 0.02554  -0.04014 -0.00230 206 ILE B C   
6428 O  O   . ILE B  206 ? 0.22635 0.31498 0.31248 0.02566  -0.04398 -0.00294 206 ILE B O   
6429 C  CB  . ILE B  206 ? 0.19651 0.28066 0.27429 0.03532  -0.03663 -0.00355 206 ILE B CB  
6430 C  CG1 . ILE B  206 ? 0.21878 0.30483 0.29536 0.04046  -0.03322 -0.00400 206 ILE B CG1 
6431 C  CG2 . ILE B  206 ? 0.19969 0.27409 0.27138 0.03149  -0.03558 -0.00298 206 ILE B CG2 
6432 C  CD1 . ILE B  206 ? 0.22743 0.30332 0.29627 0.04485  -0.03266 -0.00472 206 ILE B CD1 
6444 N  N   . GLU B  207 ? 0.18754 0.28145 0.27684 0.02059  -0.03808 -0.00107 207 GLU B N   
6445 C  CA  . GLU B  207 ? 0.21929 0.30917 0.30822 0.01475  -0.04007 -0.00040 207 GLU B CA  
6446 C  C   . GLU B  207 ? 0.22059 0.30009 0.30135 0.01309  -0.03783 -0.00003 207 GLU B C   
6447 O  O   . GLU B  207 ? 0.24048 0.31377 0.31842 0.00925  -0.03982 0.00020  207 GLU B O   
6448 C  CB  . GLU B  207 ? 0.26509 0.36466 0.36288 0.00987  -0.03975 0.00090  207 GLU B CB  
6449 C  CG  . GLU B  207 ? 0.33573 0.44539 0.44228 0.01075  -0.04269 0.00041  207 GLU B CG  
6450 C  CD  . GLU B  207 ? 0.63352 0.75311 0.74965 0.00588  -0.04223 0.00189  207 GLU B CD  
6451 O  OE1 . GLU B  207 ? 0.73116 0.84804 0.84756 0.00044  -0.04245 0.00300  207 GLU B OE1 
6452 O  OE2 . GLU B  207 ? 0.76581 0.89595 0.88927 0.00754  -0.04155 0.00204  207 GLU B OE2 
6459 N  N   . THR B  208 ? 0.21828 0.29541 0.29494 0.01611  -0.03400 -0.00015 208 THR B N   
6460 C  CA  . THR B  208 ? 0.19212 0.25920 0.26090 0.01516  -0.03195 -0.00012 208 THR B CA  
6461 C  C   . THR B  208 ? 0.19630 0.25282 0.25842 0.01615  -0.03478 -0.00091 208 THR B C   
6462 O  O   . THR B  208 ? 0.19678 0.25199 0.25760 0.02075  -0.03619 -0.00175 208 THR B O   
6463 C  CB  . THR B  208 ? 0.22701 0.29336 0.29271 0.01972  -0.02810 -0.00064 208 THR B CB  
6464 O  OG1 . THR B  208 ? 0.27181 0.34861 0.34357 0.01965  -0.02533 0.00014  208 THR B OG1 
6465 C  CG2 . THR B  208 ? 0.22936 0.28577 0.28738 0.01900  -0.02591 -0.00085 208 THR B CG2 
6473 N  N   . PRO B  209 ? 0.19365 0.21293 0.24367 0.02373  -0.01345 -0.00943 209 PRO B N   
6474 C  CA  . PRO B  209 ? 0.21664 0.23286 0.26008 0.02550  -0.01375 -0.00793 209 PRO B CA  
6475 C  C   . PRO B  209 ? 0.20026 0.21180 0.24071 0.02837  -0.01086 -0.00401 209 PRO B C   
6476 O  O   . PRO B  209 ? 0.20387 0.20966 0.24459 0.02694  -0.00762 -0.00294 209 PRO B O   
6477 C  CB  . PRO B  209 ? 0.21434 0.22533 0.25556 0.02139  -0.01317 -0.00995 209 PRO B CB  
6478 C  CG  . PRO B  209 ? 0.23328 0.24788 0.27978 0.01801  -0.01472 -0.01335 209 PRO B CG  
6479 C  CD  . PRO B  209 ? 0.21039 0.22798 0.26235 0.01887  -0.01351 -0.01250 209 PRO B CD  
6487 N  N   . THR B  210 ? 0.18820 0.20192 0.22541 0.03238  -0.01208 -0.00187 210 THR B N   
6488 C  CA  . THR B  210 ? 0.17980 0.19021 0.21477 0.03568  -0.00979 0.00202  210 THR B CA  
6489 C  C   . THR B  210 ? 0.20721 0.21487 0.23524 0.03766  -0.00991 0.00405  210 THR B C   
6490 O  O   . THR B  210 ? 0.20785 0.22001 0.23369 0.03923  -0.01284 0.00345  210 THR B O   
6491 C  CB  . THR B  210 ? 0.20507 0.22148 0.24363 0.03936  -0.01111 0.00322  210 THR B CB  
6492 O  OG1 . THR B  210 ? 0.21744 0.23615 0.26250 0.03760  -0.01054 0.00156  210 THR B OG1 
6493 C  CG2 . THR B  210 ? 0.20057 0.21361 0.23663 0.04310  -0.00909 0.00736  210 THR B CG2 
6501 N  N   A LEU B  211 ? 0.18614 0.18655 0.21076 0.03745  -0.00669 0.00631  211 LEU B N   
6502 N  N   B LEU B  211 ? 0.18939 0.18984 0.21406 0.03749  -0.00669 0.00633  211 LEU B N   
6503 N  N   C LEU B  211 ? 0.19248 0.19285 0.21711 0.03744  -0.00667 0.00631  211 LEU B N   
6504 C  CA  A LEU B  211 ? 0.19769 0.19479 0.21569 0.03936  -0.00614 0.00869  211 LEU B CA  
6505 C  CA  B LEU B  211 ? 0.19682 0.19399 0.21488 0.03940  -0.00615 0.00870  211 LEU B CA  
6506 C  CA  C LEU B  211 ? 0.20176 0.19858 0.21974 0.03927  -0.00600 0.00871  211 LEU B CA  
6507 C  C   A LEU B  211 ? 0.20055 0.19530 0.21760 0.04289  -0.00413 0.01274  211 LEU B C   
6508 C  C   B LEU B  211 ? 0.20183 0.19670 0.21897 0.04293  -0.00417 0.01274  211 LEU B C   
6509 C  C   C LEU B  211 ? 0.20962 0.20426 0.22664 0.04288  -0.00408 0.01278  211 LEU B C   
6510 O  O   A LEU B  211 ? 0.21037 0.20153 0.23013 0.04240  -0.00141 0.01377  211 LEU B O   
6511 O  O   B LEU B  211 ? 0.21328 0.20473 0.23327 0.04247  -0.00150 0.01374  211 LEU B O   
6512 O  O   C LEU B  211 ? 0.20697 0.19795 0.22662 0.04244  -0.00133 0.01386  211 LEU B O   
6513 C  CB  A LEU B  211 ? 0.21716 0.20748 0.23174 0.03618  -0.00397 0.00795  211 LEU B CB  
6514 C  CB  B LEU B  211 ? 0.21162 0.20203 0.22630 0.03621  -0.00399 0.00795  211 LEU B CB  
6515 C  CB  C LEU B  211 ? 0.22836 0.21814 0.24336 0.03599  -0.00358 0.00802  211 LEU B CB  
6516 C  CG  A LEU B  211 ? 0.19900 0.18587 0.20660 0.03748  -0.00333 0.00987  211 LEU B CG  
6517 C  CG  B LEU B  211 ? 0.20897 0.19602 0.21668 0.03755  -0.00339 0.00989  211 LEU B CG  
6518 C  CG  C LEU B  211 ? 0.20907 0.19327 0.21764 0.03709  -0.00161 0.01060  211 LEU B CG  
6519 C  CD1 A LEU B  211 ? 0.26020 0.24375 0.26513 0.03397  -0.00315 0.00731  211 LEU B CD1 
6520 C  CD1 B LEU B  211 ? 0.25975 0.24354 0.26486 0.03405  -0.00322 0.00731  211 LEU B CD1 
6521 C  CD1 C LEU B  211 ? 0.21274 0.20078 0.21701 0.03866  -0.00446 0.01031  211 LEU B CD1 
6522 C  CD2 A LEU B  211 ? 0.21649 0.19755 0.22203 0.03926  0.00013  0.01368  211 LEU B CD2 
6523 C  CD2 B LEU B  211 ? 0.21151 0.19280 0.21722 0.03933  0.00006  0.01368  211 LEU B CD2 
6524 C  CD2 C LEU B  211 ? 0.21648 0.19404 0.22356 0.03354  0.00088  0.00941  211 LEU B CD2 
6558 N  N   . ILE B  212 ? 0.20420 0.20089 0.21732 0.04644  -0.00549 0.01504  212 ILE B N   
6559 C  CA  . ILE B  212 ? 0.20272 0.19704 0.21419 0.05006  -0.00392 0.01910  212 ILE B CA  
6560 C  C   . ILE B  212 ? 0.23891 0.22835 0.24325 0.05087  -0.00260 0.02154  212 ILE B C   
6561 O  O   . ILE B  212 ? 0.23381 0.22571 0.23406 0.05134  -0.00469 0.02103  212 ILE B O   
6562 C  CB  . ILE B  212 ? 0.22038 0.22146 0.23378 0.05396  -0.00673 0.02004  212 ILE B CB  
6563 C  CG1 . ILE B  212 ? 0.24259 0.24753 0.26352 0.05323  -0.00716 0.01807  212 ILE B CG1 
6564 C  CG2 . ILE B  212 ? 0.24184 0.24010 0.25181 0.05806  -0.00555 0.02459  212 ILE B CG2 
6565 C  CD1 . ILE B  212 ? 0.27470 0.28768 0.29860 0.05637  -0.01050 0.01772  212 ILE B CD1 
6577 N  N   . PHE B  213 ? 0.21669 0.19928 0.21960 0.05086  0.00092  0.02401  213 PHE B N   
6578 C  CA  . PHE B  213 ? 0.22194 0.19964 0.21836 0.05214  0.00257  0.02702  213 PHE B CA  
6579 C  C   . PHE B  213 ? 0.25865 0.23702 0.25429 0.05660  0.00242  0.03088  213 PHE B C   
6580 O  O   . PHE B  213 ? 0.26499 0.24185 0.26436 0.05775  0.00391  0.03225  213 PHE B O   
6581 C  CB  . PHE B  213 ? 0.23522 0.20497 0.23063 0.04968  0.00653  0.02756  213 PHE B CB  
6582 C  CG  . PHE B  213 ? 0.21752 0.18552 0.21249 0.04550  0.00688  0.02417  213 PHE B CG  
6583 C  CD1 . PHE B  213 ? 0.24835 0.21654 0.23818 0.04471  0.00579  0.02328  213 PHE B CD1 
6584 C  CD2 . PHE B  213 ? 0.23613 0.20188 0.23541 0.04239  0.00842  0.02198  213 PHE B CD2 
6585 C  CE1 . PHE B  213 ? 0.26863 0.23508 0.25802 0.04104  0.00597  0.02010  213 PHE B CE1 
6586 C  CE2 . PHE B  213 ? 0.25155 0.21525 0.25021 0.03866  0.00870  0.01901  213 PHE B CE2 
6587 C  CZ  . PHE B  213 ? 0.25019 0.21405 0.24378 0.03799  0.00746  0.01803  213 PHE B CZ  
6597 N  N   . ALA B  214 ? 0.25703 0.23777 0.24790 0.05916  0.00054  0.03257  214 ALA B N   
6598 C  CA  . ALA B  214 ? 0.25035 0.23136 0.23921 0.06351  0.00016  0.03649  214 ALA B CA  
6599 C  C   . ALA B  214 ? 0.26915 0.24361 0.25159 0.06404  0.00272  0.03983  214 ALA B C   
6600 O  O   . ALA B  214 ? 0.31013 0.28323 0.28803 0.06224  0.00296  0.03907  214 ALA B O   
6601 C  CB  . ALA B  214 ? 0.26982 0.25831 0.25741 0.06603  -0.00391 0.03609  214 ALA B CB  
6607 N  N   . CYS B  215 ? 0.27084 0.24118 0.25292 0.06642  0.00467  0.04343  215 CYS B N   
6608 C  CA  . CYS B  215 ? 0.30816 0.27190 0.28430 0.06696  0.00731  0.04687  215 CYS B CA  
6609 C  C   . CYS B  215 ? 0.32311 0.28899 0.29462 0.07102  0.00538  0.05028  215 CYS B C   
6610 O  O   . CYS B  215 ? 0.33341 0.30052 0.30681 0.07439  0.00451  0.05249  215 CYS B O   
6611 C  CB  . CYS B  215 ? 0.29527 0.25233 0.27371 0.06676  0.01093  0.04871  215 CYS B CB  
6612 S  SG  . CYS B  215 ? 0.29772 0.25150 0.28053 0.06182  0.01352  0.04494  215 CYS B SG  
6617 N  N   . GLU B  216 ? 0.31313 0.27971 0.27860 0.07073  0.00458  0.05060  216 GLU B N   
6618 C  CA  . GLU B  216 ? 0.33306 0.30339 0.29409 0.07426  0.00198  0.05300  216 GLU B CA  
6619 C  C   . GLU B  216 ? 0.33976 0.30704 0.29964 0.07812  0.00272  0.05767  216 GLU B C   
6620 O  O   . GLU B  216 ? 0.35805 0.32988 0.31822 0.08165  -0.00007 0.05897  216 GLU B O   
6621 C  CB  . GLU B  216 ? 0.33572 0.30508 0.28965 0.07307  0.00224  0.05335  216 GLU B CB  
6622 C  CG  . GLU B  216 ? 0.36047 0.33439 0.30964 0.07652  -0.00068 0.05551  216 GLU B CG  
6623 C  CD  . GLU B  216 ? 0.45087 0.42297 0.39243 0.07577  0.00012  0.05678  216 GLU B CD  
6624 O  OE1 . GLU B  216 ? 0.43758 0.40362 0.37689 0.07323  0.00342  0.05714  216 GLU B OE1 
6625 O  OE2 . GLU B  216 ? 0.50846 0.48542 0.44617 0.07783  -0.00259 0.05744  216 GLU B OE2 
6632 N  N   . ARG B  217 ? 0.35808 0.31761 0.31631 0.07759  0.00638  0.06029  217 ARG B N   
6633 C  CA  . ARG B  217 ? 0.40542 0.36094 0.36146 0.08106  0.00736  0.06505  217 ARG B CA  
6634 C  C   . ARG B  217 ? 0.38981 0.34332 0.35220 0.08214  0.00848  0.06544  217 ARG B C   
6635 O  O   . ARG B  217 ? 0.45379 0.40239 0.41504 0.08445  0.01005  0.06918  217 ARG B O   
6636 C  CB  . ARG B  217 ? 0.39184 0.34002 0.34169 0.08003  0.01064  0.06797  217 ARG B CB  
6637 C  CG  . ARG B  217 ? 0.54435 0.49436 0.48716 0.07964  0.00959  0.06839  217 ARG B CG  
6638 C  CD  . ARG B  217 ? 0.74816 0.69075 0.68491 0.07886  0.01301  0.07168  217 ARG B CD  
6639 N  NE  . ARG B  217 ? 1.03498 0.97685 0.96604 0.08235  0.01218  0.07627  217 ARG B NE  
6640 C  CZ  . ARG B  217 ? 1.06863 1.01181 0.99289 0.08247  0.01147  0.07747  217 ARG B CZ  
6641 N  NH1 . ARG B  217 ? 1.01187 0.95707 0.93408 0.07936  0.01153  0.07440  217 ARG B NH1 
6642 N  NH2 . ARG B  217 ? 1.11422 1.05668 1.03355 0.08583  0.01063  0.08185  217 ARG B NH2 
6656 N  N   . ASP B  218 ? 0.35240 0.30982 0.32143 0.08060  0.00758  0.06166  218 ASP B N   
6657 C  CA  . ASP B  218 ? 0.34049 0.29669 0.31597 0.08127  0.00865  0.06146  218 ASP B CA  
6658 C  C   . ASP B  218 ? 0.37829 0.33622 0.35444 0.08611  0.00679  0.06449  218 ASP B C   
6659 O  O   . ASP B  218 ? 0.35705 0.32146 0.33304 0.08845  0.00323  0.06412  218 ASP B O   
6660 C  CB  . ASP B  218 ? 0.32080 0.28268 0.30263 0.07894  0.00717  0.05670  218 ASP B CB  
6661 C  CG  . ASP B  218 ? 0.32961 0.28976 0.31816 0.07827  0.00898  0.05567  218 ASP B CG  
6662 O  OD1 . ASP B  218 ? 0.34508 0.30218 0.33463 0.08096  0.01003  0.05851  218 ASP B OD1 
6663 O  OD2 . ASP B  218 ? 0.31181 0.27374 0.30461 0.07498  0.00929  0.05193  218 ASP B OD2 
6668 N  N   . SER B  219 ? 0.34780 0.29984 0.32450 0.08774  0.00910  0.06751  219 SER B N   
6669 C  CA  . SER B  219 ? 0.39876 0.35158 0.37631 0.09243  0.00752  0.07048  219 SER B CA  
6670 C  C   . SER B  219 ? 0.39404 0.34815 0.37950 0.09314  0.00773  0.06893  219 SER B C   
6671 O  O   . SER B  219 ? 0.45165 0.40674 0.43888 0.09706  0.00635  0.07091  219 SER B O   
6672 C  CB  . SER B  219 ? 0.49226 0.43740 0.46424 0.09425  0.00971  0.07541  219 SER B CB  
6673 O  OG  . SER B  219 ? 0.55218 0.49041 0.52614 0.09219  0.01362  0.07568  219 SER B OG  
6679 N  N   . ILE B  220 ? 0.36449 0.31860 0.35470 0.08947  0.00943  0.06543  220 ILE B N   
6680 C  CA  . ILE B  220 ? 0.36176 0.31714 0.35959 0.08961  0.00996  0.06366  220 ILE B CA  
6681 C  C   . ILE B  220 ? 0.36683 0.33092 0.36986 0.08895  0.00701  0.05961  220 ILE B C   
6682 O  O   . ILE B  220 ? 0.36075 0.32896 0.36901 0.09130  0.00543  0.05897  220 ILE B O   
6683 C  CB  . ILE B  220 ? 0.39949 0.34866 0.39910 0.08592  0.01407  0.06264  220 ILE B CB  
6684 C  CG1 . ILE B  220 ? 0.47307 0.41373 0.46837 0.08710  0.01695  0.06679  220 ILE B CG1 
6685 C  CG2 . ILE B  220 ? 0.37205 0.32323 0.37955 0.08542  0.01464  0.06021  220 ILE B CG2 
6686 C  CD1 . ILE B  220 ? 0.48333 0.41749 0.47933 0.08359  0.02103  0.06607  220 ILE B CD1 
6698 N  N   . ALA B  221 ? 0.35401 0.32091 0.35578 0.08568  0.00627  0.05676  221 ALA B N   
6699 C  CA  . ALA B  221 ? 0.34492 0.32017 0.35041 0.08486  0.00317  0.05300  221 ALA B CA  
6700 C  C   . ALA B  221 ? 0.31793 0.29638 0.31765 0.08535  0.00061  0.05325  221 ALA B C   
6701 O  O   . ALA B  221 ? 0.31683 0.29625 0.31499 0.08200  0.00053  0.05077  221 ALA B O   
6702 C  CB  . ALA B  221 ? 0.31618 0.29180 0.32592 0.08011  0.00465  0.04896  221 ALA B CB  
6708 N  N   . PRO B  222 ? 0.32089 0.30097 0.31727 0.08953  -0.00154 0.05618  222 PRO B N   
6709 C  CA  . PRO B  222 ? 0.33850 0.32096 0.32863 0.09007  -0.00365 0.05681  222 PRO B CA  
6710 C  C   . PRO B  222 ? 0.30442 0.29410 0.29688 0.08774  -0.00619 0.05235  222 PRO B C   
6711 O  O   . PRO B  222 ? 0.32145 0.31703 0.31987 0.08810  -0.00814 0.04973  222 PRO B O   
6712 C  CB  . PRO B  222 ? 0.41145 0.39628 0.39970 0.09532  -0.00620 0.06001  222 PRO B CB  
6713 C  CG  . PRO B  222 ? 0.43025 0.41045 0.42140 0.09731  -0.00425 0.06234  222 PRO B CG  
6714 C  CD  . PRO B  222 ? 0.37839 0.35791 0.37623 0.09399  -0.00211 0.05913  222 PRO B CD  
6722 N  N   . VAL B  223 ? 0.31263 0.30205 0.30016 0.08558  -0.00634 0.05159  223 VAL B N   
6723 C  CA  . VAL B  223 ? 0.31111 0.30658 0.30033 0.08301  -0.00857 0.04730  223 VAL B CA  
6724 C  C   . VAL B  223 ? 0.33018 0.33429 0.32171 0.08594  -0.01279 0.04614  223 VAL B C   
6725 O  O   . VAL B  223 ? 0.31340 0.32329 0.30999 0.08435  -0.01461 0.04227  223 VAL B O   
6726 C  CB  . VAL B  223 ? 0.34954 0.34299 0.33221 0.08088  -0.00811 0.04720  223 VAL B CB  
6727 C  CG1 . VAL B  223 ? 0.51463 0.51502 0.49811 0.07921  -0.01116 0.04323  223 VAL B CG1 
6728 C  CG2 . VAL B  223 ? 0.34273 0.32870 0.32460 0.07733  -0.00415 0.04713  223 VAL B CG2 
6738 N  N   . ARG B  224 ? 0.32542 0.33054 0.31328 0.09021  -0.01443 0.04944  224 ARG B N   
6739 C  CA  . ARG B  224 ? 0.34494 0.35849 0.33451 0.09318  -0.01863 0.04832  224 ARG B CA  
6740 C  C   . ARG B  224 ? 0.31272 0.33012 0.31015 0.09447  -0.01956 0.04674  224 ARG B C   
6741 O  O   . ARG B  224 ? 0.32978 0.35498 0.33037 0.09579  -0.02292 0.04443  224 ARG B O   
6742 C  CB  . ARG B  224 ? 0.40977 0.42299 0.39315 0.09758  -0.02008 0.05250  224 ARG B CB  
6743 C  CG  . ARG B  224 ? 0.61137 0.61957 0.59486 0.10078  -0.01853 0.05653  224 ARG B CG  
6744 C  CD  . ARG B  224 ? 0.97648 0.97967 0.95172 0.10311  -0.01782 0.06136  224 ARG B CD  
6745 N  NE  . ARG B  224 ? 1.04554 1.04405 1.02095 0.10647  -0.01670 0.06527  224 ARG B NE  
6746 C  CZ  . ARG B  224 ? 1.08610 1.07656 1.05668 0.10685  -0.01388 0.06929  224 ARG B CZ  
6747 N  NH1 . ARG B  224 ? 0.87929 0.86531 0.84459 0.10394  -0.01162 0.06992  224 ARG B NH1 
6748 N  NH2 . ARG B  224 ? 1.04198 1.02876 1.01317 0.11021  -0.01332 0.07265  224 ARG B NH2 
6762 N  N   . SER B  225 ? 0.31043 0.32274 0.31105 0.09420  -0.01669 0.04790  225 SER B N   
6763 C  CA  . SER B  225 ? 0.33102 0.34658 0.33907 0.09542  -0.01723 0.04653  225 SER B CA  
6764 C  C   . SER B  225 ? 0.29237 0.30801 0.30649 0.09095  -0.01540 0.04272  225 SER B C   
6765 O  O   . SER B  225 ? 0.31538 0.33558 0.33624 0.09132  -0.01632 0.04054  225 SER B O   
6766 C  CB  . SER B  225 ? 0.36511 0.37505 0.37292 0.09850  -0.01533 0.05045  225 SER B CB  
6767 O  OG  . SER B  225 ? 0.48684 0.49745 0.48981 0.10308  -0.01747 0.05393  225 SER B OG  
6773 N  N   . HIS B  226 ? 0.27011 0.28107 0.28200 0.08683  -0.01295 0.04183  226 HIS B N   
6774 C  CA  . HIS B  226 ? 0.26074 0.27067 0.27769 0.08250  -0.01092 0.03861  226 HIS B CA  
6775 C  C   . HIS B  226 ? 0.24633 0.25769 0.26194 0.07842  -0.01145 0.03541  226 HIS B C   
6776 O  O   . HIS B  226 ? 0.25843 0.27657 0.27740 0.07746  -0.01407 0.03207  226 HIS B O   
6777 C  CB  . HIS B  226 ? 0.26100 0.26253 0.27784 0.08160  -0.00674 0.04080  226 HIS B CB  
6778 C  CG  . HIS B  226 ? 0.24753 0.24808 0.26692 0.08540  -0.00632 0.04334  226 HIS B CG  
6779 N  ND1 . HIS B  226 ? 0.28816 0.29126 0.31482 0.08529  -0.00599 0.04150  226 HIS B ND1 
6780 C  CD2 . HIS B  226 ? 0.29096 0.28856 0.30673 0.08948  -0.00636 0.04747  226 HIS B CD2 
6781 C  CE1 . HIS B  226 ? 0.32790 0.32964 0.35543 0.08920  -0.00585 0.04426  226 HIS B CE1 
6782 N  NE2 . HIS B  226 ? 0.31652 0.31475 0.33746 0.09183  -0.00611 0.04798  226 HIS B NE2 
6790 N  N   . ALA B  227 ? 0.24263 0.28080 0.25107 0.06510  -0.01153 0.04081  227 ALA B N   
6791 C  CA  . ALA B  227 ? 0.22394 0.26007 0.23331 0.06285  -0.01086 0.03265  227 ALA B CA  
6792 C  C   . ALA B  227 ? 0.23938 0.28372 0.24130 0.06596  -0.01567 0.02403  227 ALA B C   
6793 O  O   . ALA B  227 ? 0.24017 0.28366 0.24632 0.06332  -0.01859 0.01482  227 ALA B O   
6794 C  CB  . ALA B  227 ? 0.23866 0.27092 0.24456 0.06288  -0.00401 0.03715  227 ALA B CB  
6800 N  N   . SER B  228 ? 0.24576 0.29794 0.23627 0.07160  -0.01626 0.02679  228 SER B N   
6801 C  CA  . SER B  228 ? 0.25729 0.31746 0.24011 0.07484  -0.02055 0.01872  228 SER B CA  
6802 C  C   . SER B  228 ? 0.26149 0.32506 0.24872 0.07406  -0.02761 0.01178  228 SER B C   
6803 O  O   . SER B  228 ? 0.25425 0.31878 0.24313 0.07254  -0.03075 0.00213  228 SER B O   
6804 C  CB  . SER B  228 ? 0.25151 0.31920 0.22108 0.08112  -0.01936 0.02354  228 SER B CB  
6805 O  OG  . SER B  228 ? 0.30218 0.37762 0.26459 0.08425  -0.02372 0.01551  228 SER B OG  
6811 N  N   . PRO B  229 ? 0.25907 0.32470 0.24826 0.07503  -0.03043 0.01586  229 PRO B N   
6812 C  CA  . PRO B  229 ? 0.24808 0.31690 0.24193 0.07401  -0.03719 0.00864  229 PRO B CA  
6813 C  C   . PRO B  229 ? 0.24172 0.30325 0.24810 0.06773  -0.03806 0.00298  229 PRO B C   
6814 O  O   . PRO B  229 ? 0.25509 0.31892 0.26454 0.06641  -0.04313 -0.00588 229 PRO B O   
6815 C  CB  . PRO B  229 ? 0.25797 0.32960 0.25159 0.07625  -0.03910 0.01565  229 PRO B CB  
6816 C  CG  . PRO B  229 ? 0.27085 0.33821 0.26314 0.07680  -0.03300 0.02661  229 PRO B CG  
6817 C  CD  . PRO B  229 ? 0.27056 0.33735 0.25601 0.07801  -0.02822 0.02662  229 PRO B CD  
6825 N  N   . PHE B  230 ? 0.22787 0.28060 0.24169 0.06376  -0.03326 0.00777  230 PHE B N   
6826 C  CA  . PHE B  230 ? 0.23135 0.27702 0.25684 0.05780  -0.03388 0.00218  230 PHE B CA  
6827 C  C   . PHE B  230 ? 0.23580 0.28155 0.25990 0.05664  -0.03448 -0.00733 230 PHE B C   
6828 O  O   . PHE B  230 ? 0.24228 0.28739 0.27238 0.05373  -0.03850 -0.01572 230 PHE B O   
6829 C  CB  . PHE B  230 ? 0.21982 0.25594 0.25328 0.05385  -0.02837 0.00894  230 PHE B CB  
6830 C  CG  . PHE B  230 ? 0.22109 0.25599 0.25737 0.05432  -0.02766 0.01813  230 PHE B CG  
6831 C  CD1 . PHE B  230 ? 0.24366 0.28478 0.27805 0.05704  -0.03253 0.01896  230 PHE B CD1 
6832 C  CD2 . PHE B  230 ? 0.23548 0.26309 0.27615 0.05219  -0.02210 0.02612  230 PHE B CD2 
6833 C  CE1 . PHE B  230 ? 0.22496 0.26505 0.26143 0.05772  -0.03178 0.02765  230 PHE B CE1 
6834 C  CE2 . PHE B  230 ? 0.23858 0.26510 0.28135 0.05284  -0.02129 0.03481  230 PHE B CE2 
6835 C  CZ  . PHE B  230 ? 0.22095 0.25352 0.26185 0.05550  -0.02613 0.03558  230 PHE B CZ  
6845 N  N   . TYR B  231 ? 0.22772 0.27376 0.24435 0.05866  -0.03026 -0.00602 231 TYR B N   
6846 C  CA  . TYR B  231 ? 0.23198 0.27856 0.24625 0.05804  -0.03077 -0.01493 231 TYR B CA  
6847 C  C   . TYR B  231 ? 0.24137 0.29645 0.25075 0.06080  -0.03730 -0.02310 231 TYR B C   
6848 O  O   . TYR B  231 ? 0.24752 0.30208 0.26074 0.05834  -0.04053 -0.03244 231 TYR B O   
6849 C  CB  . TYR B  231 ? 0.25382 0.30082 0.25922 0.06073  -0.02540 -0.01152 231 TYR B CB  
6850 C  CG  . TYR B  231 ? 0.23435 0.28317 0.23596 0.06091  -0.02639 -0.02069 231 TYR B CG  
6851 C  CD1 . TYR B  231 ? 0.26462 0.30615 0.27275 0.05640  -0.02399 -0.02492 231 TYR B CD1 
6852 C  CD2 . TYR B  231 ? 0.26472 0.32239 0.25661 0.06545  -0.02993 -0.02542 231 TYR B CD2 
6853 C  CE1 . TYR B  231 ? 0.25310 0.29606 0.25795 0.05648  -0.02496 -0.03347 231 TYR B CE1 
6854 C  CE2 . TYR B  231 ? 0.27087 0.33020 0.25948 0.06559  -0.03104 -0.03407 231 TYR B CE2 
6855 C  CZ  . TYR B  231 ? 0.24445 0.29621 0.23963 0.06103  -0.02845 -0.03797 231 TYR B CZ  
6856 O  OH  . TYR B  231 ? 0.29714 0.35048 0.28901 0.06118  -0.02966 -0.04680 231 TYR B OH  
6866 N  N   . ASN B  232 ? 0.24759 0.31070 0.24816 0.06606  -0.03932 -0.01978 232 ASN B N   
6867 C  CA  . ASN B  232 ? 0.25584 0.32755 0.25073 0.06920  -0.04531 -0.02729 232 ASN B CA  
6868 C  C   . ASN B  232 ? 0.25965 0.33137 0.26333 0.06624  -0.05112 -0.03309 232 ASN B C   
6869 O  O   . ASN B  232 ? 0.31054 0.38693 0.31294 0.06677  -0.05606 -0.04203 232 ASN B O   
6870 C  CB  . ASN B  232 ? 0.27322 0.35319 0.25715 0.07546  -0.04603 -0.02172 232 ASN B CB  
6871 C  CG  . ASN B  232 ? 0.30228 0.38425 0.27576 0.07912  -0.04132 -0.01803 232 ASN B CG  
6872 O  OD1 . ASN B  232 ? 0.29996 0.37871 0.27299 0.07760  -0.03843 -0.02143 232 ASN B OD1 
6873 N  ND2 . ASN B  232 ? 0.33907 0.42646 0.30393 0.08411  -0.04049 -0.01072 232 ASN B ND2 
6880 N  N   . ALA B  233 ? 0.23721 0.30372 0.25002 0.06302  -0.05062 -0.02827 233 ALA B N   
6881 C  CA  . ALA B  233 ? 0.26639 0.33277 0.28793 0.06009  -0.05594 -0.03328 233 ALA B CA  
6882 C  C   . ALA B  233 ? 0.24709 0.30823 0.27690 0.05494  -0.05704 -0.04229 233 ALA B C   
6883 O  O   . ALA B  233 ? 0.26533 0.32857 0.29969 0.05334  -0.06243 -0.04967 233 ALA B O   
6884 C  CB  . ALA B  233 ? 0.24994 0.31172 0.27899 0.05801  -0.05459 -0.02521 233 ALA B CB  
6890 N  N   . ILE B  234 ? 0.23696 0.29126 0.26891 0.05227  -0.05204 -0.04182 234 ILE B N   
6891 C  CA  . ILE B  234 ? 0.23698 0.28545 0.27724 0.04713  -0.05267 -0.04987 234 ILE B CA  
6892 C  C   . ILE B  234 ? 0.25177 0.30605 0.28687 0.04875  -0.05693 -0.06013 234 ILE B C   
6893 O  O   . ILE B  234 ? 0.25656 0.31646 0.28096 0.05324  -0.05631 -0.06034 234 ILE B O   
6894 C  CB  . ILE B  234 ? 0.23678 0.27701 0.27934 0.04448  -0.04606 -0.04655 234 ILE B CB  
6895 C  CG1 . ILE B  234 ? 0.23998 0.27447 0.28836 0.04273  -0.04222 -0.03658 234 ILE B CG1 
6896 C  CG2 . ILE B  234 ? 0.23816 0.27255 0.28817 0.03957  -0.04647 -0.05504 234 ILE B CG2 
6897 C  CD1 . ILE B  234 ? 0.22870 0.25483 0.27981 0.04012  -0.03542 -0.03222 234 ILE B CD1 
6909 N  N   . PRO B  235 ? 0.24544 0.29861 0.28770 0.04530  -0.06124 -0.06871 235 PRO B N   
6910 C  CA  . PRO B  235 ? 0.27739 0.33589 0.31524 0.04664  -0.06550 -0.07883 235 PRO B CA  
6911 C  C   . PRO B  235 ? 0.26663 0.32473 0.29733 0.04810  -0.06208 -0.08118 235 PRO B C   
6912 O  O   . PRO B  235 ? 0.27685 0.32765 0.31062 0.04539  -0.05703 -0.07897 235 PRO B O   
6913 C  CB  . PRO B  235 ? 0.34524 0.39897 0.39457 0.04104  -0.06872 -0.08639 235 PRO B CB  
6914 C  CG  . PRO B  235 ? 0.30794 0.35791 0.36584 0.03848  -0.06853 -0.08032 235 PRO B CG  
6915 C  CD  . PRO B  235 ? 0.25536 0.30259 0.31031 0.04006  -0.06268 -0.06938 235 PRO B CD  
6923 N  N   . SER B  236 ? 0.29553 0.36171 0.31679 0.05239  -0.06513 -0.08621 236 SER B N   
6924 C  CA  . SER B  236 ? 0.32727 0.39378 0.34169 0.05385  -0.06267 -0.08978 236 SER B CA  
6925 C  C   . SER B  236 ? 0.28160 0.34180 0.30324 0.04890  -0.06290 -0.09821 236 SER B C   
6926 O  O   . SER B  236 ? 0.34822 0.40675 0.36587 0.04919  -0.06005 -0.10073 236 SER B O   
6927 C  CB  . SER B  236 ? 0.36819 0.44491 0.37160 0.05936  -0.06654 -0.09414 236 SER B CB  
6928 O  OG  . SER B  236 ? 0.44393 0.52378 0.45100 0.05814  -0.07295 -0.10326 236 SER B OG  
6934 N  N   . SER B  237 ? 0.31229 0.36946 0.34402 0.04462  -0.06653 -0.10298 237 SER B N   
6935 C  CA  . SER B  237 ? 0.30899 0.35964 0.34836 0.03960  -0.06676 -0.11067 237 SER B CA  
6936 C  C   . SER B  237 ? 0.33975 0.38003 0.38741 0.03497  -0.06131 -0.10582 237 SER B C   
6937 O  O   . SER B  237 ? 0.36808 0.40216 0.42205 0.03073  -0.06078 -0.11152 237 SER B O   
6938 C  CB  . SER B  237 ? 0.36905 0.42085 0.41597 0.03686  -0.07301 -0.11785 237 SER B CB  
6939 O  OG  . SER B  237 ? 0.35225 0.40441 0.40407 0.03635  -0.07424 -0.11201 237 SER B OG  
6945 N  N   . THR B  238 ? 0.27983 0.31800 0.32788 0.03560  -0.05738 -0.09561 238 THR B N   
6946 C  CA  . THR B  238 ? 0.26414 0.29282 0.31934 0.03168  -0.05186 -0.09018 238 THR B CA  
6947 C  C   . THR B  238 ? 0.26031 0.28734 0.30847 0.03360  -0.04608 -0.08667 238 THR B C   
6948 O  O   . THR B  238 ? 0.25902 0.29256 0.29657 0.03865  -0.04546 -0.08409 238 THR B O   
6949 C  CB  . THR B  238 ? 0.22939 0.25713 0.28847 0.03160  -0.05092 -0.08094 238 THR B CB  
6950 O  OG1 . THR B  238 ? 0.26719 0.29621 0.33337 0.02950  -0.05636 -0.08481 238 THR B OG1 
6951 C  CG2 . THR B  238 ? 0.26328 0.28181 0.32913 0.02809  -0.04513 -0.07429 238 THR B CG2 
6959 N  N   . ASP B  239 ? 0.26088 0.27934 0.31484 0.02957  -0.04198 -0.08716 239 ASP B N   
6960 C  CA  . ASP B  239 ? 0.24122 0.25710 0.28981 0.03090  -0.03586 -0.08265 239 ASP B CA  
6961 C  C   . ASP B  239 ? 0.21649 0.23207 0.26349 0.03271  -0.03195 -0.07104 239 ASP B C   
6962 O  O   . ASP B  239 ? 0.22780 0.23781 0.28334 0.02954  -0.03055 -0.06612 239 ASP B O   
6963 C  CB  . ASP B  239 ? 0.25778 0.26395 0.31409 0.02586  -0.03224 -0.08502 239 ASP B CB  
6964 C  CG  . ASP B  239 ? 0.30468 0.31012 0.36268 0.02382  -0.03543 -0.09623 239 ASP B CG  
6965 O  OD1 . ASP B  239 ? 0.36781 0.38019 0.42053 0.02635  -0.04015 -0.10256 239 ASP B OD1 
6966 O  OD2 . ASP B  239 ? 0.40053 0.39805 0.46524 0.01958  -0.03298 -0.09874 239 ASP B OD2 
6971 N  N   . LYS B  240 ? 0.21248 0.23402 0.24867 0.03783  -0.03020 -0.06647 240 LYS B N   
6972 C  CA  . LYS B  240 ? 0.21630 0.23809 0.25030 0.03989  -0.02671 -0.05547 240 LYS B CA  
6973 C  C   . LYS B  240 ? 0.21187 0.23662 0.23507 0.04401  -0.02236 -0.05154 240 LYS B C   
6974 O  O   . LYS B  240 ? 0.23437 0.26394 0.24994 0.04666  -0.02362 -0.05721 240 LYS B O   
6975 C  CB  . LYS B  240 ? 0.21838 0.24646 0.25114 0.04241  -0.03113 -0.05278 240 LYS B CB  
6976 C  CG  . LYS B  240 ? 0.23164 0.26991 0.25428 0.04742  -0.03565 -0.05745 240 LYS B CG  
6977 C  CD  . LYS B  240 ? 0.23158 0.27566 0.25312 0.04995  -0.03953 -0.05387 240 LYS B CD  
6978 C  CE  . LYS B  240 ? 0.22697 0.28126 0.23805 0.05521  -0.04374 -0.05797 240 LYS B CE  
6979 N  NZ  . LYS B  240 ? 0.26264 0.32297 0.27104 0.05848  -0.04672 -0.05290 240 LYS B NZ  
6993 N  N   . ALA B  241 ? 0.21122 0.23323 0.23382 0.04461  -0.01729 -0.04162 241 ALA B N   
6994 C  CA  . ALA B  241 ? 0.20653 0.23108 0.21933 0.04844  -0.01270 -0.03648 241 ALA B CA  
6995 C  C   . ALA B  241 ? 0.20780 0.23291 0.21878 0.05049  -0.00980 -0.02517 241 ALA B C   
6996 O  O   . ALA B  241 ? 0.22312 0.24306 0.24257 0.04751  -0.00904 -0.02041 241 ALA B O   
6997 C  CB  . ALA B  241 ? 0.23723 0.25523 0.25154 0.04597  -0.00750 -0.03748 241 ALA B CB  
7003 N  N   . TYR B  242 ? 0.23428 0.26521 0.23427 0.05548  -0.00778 -0.02075 242 TYR B N   
7004 C  CA  . TYR B  242 ? 0.22509 0.25783 0.22130 0.05832  -0.00520 -0.01013 242 TYR B CA  
7005 C  C   . TYR B  242 ? 0.22458 0.25711 0.21335 0.06057  0.00083  -0.00520 242 TYR B C   
7006 O  O   . TYR B  242 ? 0.25109 0.28872 0.23112 0.06367  0.00061  -0.00930 242 TYR B O   
7007 C  CB  . TYR B  242 ? 0.23553 0.27773 0.22423 0.06311  -0.01002 -0.01028 242 TYR B CB  
7008 C  CG  . TYR B  242 ? 0.23160 0.27675 0.21548 0.06657  -0.00822 0.00001  242 TYR B CG  
7009 C  CD1 . TYR B  242 ? 0.23952 0.28232 0.23008 0.06504  -0.00934 0.00525  242 TYR B CD1 
7010 C  CD2 . TYR B  242 ? 0.26311 0.31393 0.23534 0.07166  -0.00574 0.00435  242 TYR B CD2 
7011 C  CE1 . TYR B  242 ? 0.26249 0.30815 0.24847 0.06835  -0.00799 0.01451  242 TYR B CE1 
7012 C  CE2 . TYR B  242 ? 0.25308 0.30691 0.22058 0.07503  -0.00439 0.01376  242 TYR B CE2 
7013 C  CZ  . TYR B  242 ? 0.27183 0.32292 0.24644 0.07326  -0.00561 0.01865  242 TYR B CZ  
7014 O  OH  . TYR B  242 ? 0.31021 0.36409 0.28027 0.07658  -0.00437 0.02798  242 TYR B OH  
7024 N  N   . PHE B  243 ? 0.23410 0.26074 0.22632 0.05898  0.00624  0.00341  243 PHE B N   
7025 C  CA  . PHE B  243 ? 0.23200 0.25833 0.21749 0.06107  0.01227  0.00917  243 PHE B CA  
7026 C  C   . PHE B  243 ? 0.23748 0.26492 0.22039 0.06344  0.01474  0.02024  243 PHE B C   
7027 O  O   . PHE B  243 ? 0.25922 0.28051 0.25031 0.06038  0.01660  0.02577  243 PHE B O   
7028 C  CB  . PHE B  243 ? 0.24087 0.25810 0.23332 0.05655  0.01727  0.00905  243 PHE B CB  
7029 C  CG  . PHE B  243 ? 0.24522 0.26107 0.23896 0.05452  0.01589  -0.00135 243 PHE B CG  
7030 C  CD1 . PHE B  243 ? 0.25369 0.26610 0.25625 0.05055  0.01194  -0.00883 243 PHE B CD1 
7031 C  CD2 . PHE B  243 ? 0.25231 0.26998 0.23857 0.05651  0.01884  -0.00338 243 PHE B CD2 
7032 C  CE1 . PHE B  243 ? 0.28532 0.29633 0.28889 0.04873  0.01071  -0.01835 243 PHE B CE1 
7033 C  CE2 . PHE B  243 ? 0.26054 0.27677 0.24790 0.05470  0.01763  -0.01290 243 PHE B CE2 
7034 C  CZ  . PHE B  243 ? 0.26147 0.27439 0.25729 0.05089  0.01359  -0.02025 243 PHE B CZ  
7044 N  N   . GLU B  244 ? 0.24664 0.28163 0.21832 0.06881  0.01489  0.02357  244 GLU B N   
7045 C  CA  . GLU B  244 ? 0.26840 0.30475 0.23624 0.07151  0.01773  0.03438  244 GLU B CA  
7046 C  C   . GLU B  244 ? 0.26340 0.29638 0.22816 0.07166  0.02481  0.04011  244 GLU B C   
7047 O  O   . GLU B  244 ? 0.28853 0.32457 0.24592 0.07375  0.02644  0.03697  244 GLU B O   
7048 C  CB  . GLU B  244 ? 0.28279 0.32899 0.24002 0.07735  0.01440  0.03560  244 GLU B CB  
7049 C  CG  . GLU B  244 ? 0.29719 0.34410 0.25200 0.07963  0.01672  0.04668  244 GLU B CG  
7050 C  CD  . GLU B  244 ? 0.37103 0.42755 0.31437 0.08575  0.01427  0.04880  244 GLU B CD  
7051 O  OE1 . GLU B  244 ? 0.35915 0.42046 0.29282 0.08927  0.01593  0.04809  244 GLU B OE1 
7052 O  OE2 . GLU B  244 ? 0.38994 0.44927 0.33386 0.08711  0.01071  0.05128  244 GLU B OE2 
7059 N  N   . ILE B  245 ? 0.28201 0.30869 0.25254 0.06938  0.02896  0.04836  245 ILE B N   
7060 C  CA  . ILE B  245 ? 0.27039 0.29250 0.24013 0.06862  0.03591  0.05412  245 ILE B CA  
7061 C  C   . ILE B  245 ? 0.30024 0.32710 0.26053 0.07333  0.03883  0.06335  245 ILE B C   
7062 O  O   . ILE B  245 ? 0.31860 0.34618 0.27948 0.07447  0.03816  0.07018  245 ILE B O   
7063 C  CB  . ILE B  245 ? 0.25905 0.27124 0.24092 0.06325  0.03888  0.05759  245 ILE B CB  
7064 C  CG1 . ILE B  245 ? 0.31650 0.32401 0.30716 0.05865  0.03627  0.04797  245 ILE B CG1 
7065 C  CG2 . ILE B  245 ? 0.33152 0.33939 0.31233 0.06276  0.04604  0.06436  245 ILE B CG2 
7066 C  CD1 . ILE B  245 ? 0.31973 0.31783 0.32301 0.05326  0.03808  0.05020  245 ILE B CD1 
7078 N  N   . SER B  246 ? 0.31746 0.28593 0.28922 0.04297  0.04371  0.09870  246 SER B N   
7079 C  CA  . SER B  246 ? 0.34217 0.29976 0.31606 0.04396  0.05119  0.10951  246 SER B CA  
7080 C  C   . SER B  246 ? 0.32420 0.27132 0.31462 0.03853  0.05266  0.10837  246 SER B C   
7081 O  O   . SER B  246 ? 0.35702 0.30767 0.36104 0.03141  0.05164  0.10278  246 SER B O   
7082 C  CB  . SER B  246 ? 0.38032 0.34387 0.35443 0.04208  0.05743  0.11679  246 SER B CB  
7083 O  OG  . SER B  246 ? 0.40176 0.35531 0.37660 0.04351  0.06492  0.12786  246 SER B OG  
7089 N  N   . GLY B  247 ? 0.34581 0.28011 0.33497 0.04189  0.05511  0.11375  247 GLY B N   
7090 C  CA  . GLY B  247 ? 0.39680 0.31990 0.40052 0.03751  0.05695  0.11368  247 GLY B CA  
7091 C  C   . GLY B  247 ? 0.37045 0.29193 0.38153 0.03480  0.05016  0.10280  247 GLY B C   
7092 O  O   . GLY B  247 ? 0.42042 0.33333 0.44461 0.03047  0.05131  0.10179  247 GLY B O   
7096 N  N   . GLY B  248 ? 0.35449 0.28377 0.35747 0.03725  0.04307  0.09456  248 GLY B N   
7097 C  CA  . GLY B  248 ? 0.34085 0.27024 0.35183 0.03378  0.03653  0.08355  248 GLY B CA  
7098 C  C   . GLY B  248 ? 0.35580 0.27301 0.36551 0.03729  0.03452  0.08279  248 GLY B C   
7099 O  O   . GLY B  248 ? 0.36839 0.28135 0.36516 0.04445  0.03477  0.08739  248 GLY B O   
7103 N  N   . ASN B  249 ? 0.33940 0.25070 0.36307 0.03204  0.03273  0.07715  249 ASN B N   
7104 C  CA  . ASN B  249 ? 0.35668 0.25756 0.38021 0.03465  0.02968  0.07438  249 ASN B CA  
7105 C  C   . ASN B  249 ? 0.32325 0.23120 0.34184 0.03583  0.02101  0.06315  249 ASN B C   
7106 O  O   . ASN B  249 ? 0.30796 0.22840 0.32235 0.03515  0.01777  0.05842  249 ASN B O   
7107 C  CB  . ASN B  249 ? 0.38338 0.27342 0.42361 0.02895  0.03233  0.07450  249 ASN B CB  
7108 C  CG  . ASN B  249 ? 0.40023 0.29576 0.45514 0.02065  0.02943  0.06568  249 ASN B CG  
7109 O  OD1 . ASN B  249 ? 0.35884 0.26434 0.41189 0.01951  0.02347  0.05691  249 ASN B OD1 
7110 N  ND2 . ASN B  249 ? 0.44690 0.33575 0.51679 0.01469  0.03374  0.06808  249 ASN B ND2 
7117 N  N   . HIS B  250 ? 0.33431 0.23420 0.35352 0.03758  0.01722  0.05880  250 HIS B N   
7118 C  CA  . HIS B  250 ? 0.30705 0.21258 0.32001 0.03970  0.00901  0.04874  250 HIS B CA  
7119 C  C   . HIS B  250 ? 0.29207 0.20783 0.31418 0.03306  0.00437  0.03850  250 HIS B C   
7120 O  O   . HIS B  250 ? 0.30085 0.22458 0.31644 0.03471  -0.00223 0.03043  250 HIS B O   
7121 C  CB  . HIS B  250 ? 0.34788 0.24161 0.36246 0.04178  0.00649  0.04624  250 HIS B CB  
7122 C  CG  . HIS B  250 ? 0.33155 0.22947 0.33895 0.04470  -0.00167 0.03667  250 HIS B CG  
7123 N  ND1 . HIS B  250 ? 0.31400 0.21957 0.30524 0.05099  -0.00480 0.03628  250 HIS B ND1 
7124 C  CD2 . HIS B  250 ? 0.32996 0.22513 0.34390 0.04236  -0.00729 0.02730  250 HIS B CD2 
7125 C  CE1 . HIS B  250 ? 0.31775 0.22514 0.30600 0.05238  -0.01205 0.02701  250 HIS B CE1 
7126 N  NE2 . HIS B  250 ? 0.34167 0.24278 0.34341 0.04728  -0.01367 0.02147  250 HIS B NE2 
7134 N  N   . TYR B  251 ? 0.29819 0.21352 0.33546 0.02560  0.00740  0.03832  251 TYR B N   
7135 C  CA  . TYR B  251 ? 0.28813 0.21269 0.33541 0.01873  0.00343  0.02897  251 TYR B CA  
7136 C  C   . TYR B  251 ? 0.26715 0.20442 0.31245 0.01677  0.00524  0.03057  251 TYR B C   
7137 O  O   . TYR B  251 ? 0.29053 0.23590 0.34471 0.01068  0.00263  0.02360  251 TYR B O   
7138 C  CB  . TYR B  251 ? 0.32819 0.24491 0.39385 0.01135  0.00554  0.02749  251 TYR B CB  
7139 C  CG  . TYR B  251 ? 0.37654 0.28072 0.44518 0.01275  0.00370  0.02544  251 TYR B CG  
7140 C  CD1 . TYR B  251 ? 0.45698 0.34916 0.52235 0.01698  0.00850  0.03431  251 TYR B CD1 
7141 C  CD2 . TYR B  251 ? 0.45652 0.36093 0.53107 0.00993  -0.00286 0.01465  251 TYR B CD2 
7142 C  CE1 . TYR B  251 ? 0.59946 0.48005 0.66731 0.01846  0.00682  0.03252  251 TYR B CE1 
7143 C  CE2 . TYR B  251 ? 0.57270 0.46545 0.64981 0.01133  -0.00457 0.01272  251 TYR B CE2 
7144 C  CZ  . TYR B  251 ? 0.52795 0.40896 0.60168 0.01560  0.00031  0.02170  251 TYR B CZ  
7145 O  OH  . TYR B  251 ? 0.72629 0.59565 0.80264 0.01699  -0.00124 0.01997  251 TYR B OH  
7155 N  N   . CYS B  252 ? 0.28059 0.21987 0.31469 0.02163  0.00962  0.03947  252 CYS B N   
7156 C  CA  . CYS B  252 ? 0.26526 0.21480 0.29954 0.01911  0.01292  0.04269  252 CYS B CA  
7157 C  C   . CYS B  252 ? 0.27488 0.23893 0.30546 0.01790  0.00686  0.03381  252 CYS B C   
7158 O  O   . CYS B  252 ? 0.27229 0.24509 0.30913 0.01288  0.00819  0.03286  252 CYS B O   
7159 C  CB  . CYS B  252 ? 0.29633 0.24442 0.31840 0.02509  0.01875  0.05416  252 CYS B CB  
7160 S  SG  . CYS B  252 ? 0.29984 0.25769 0.30017 0.03351  0.01523  0.05429  252 CYS B SG  
7165 N  N   . ALA B  253 ? 0.23684 0.20374 0.25765 0.02228  0.00022  0.02719  253 ALA B N   
7166 C  CA  . ALA B  253 ? 0.22610 0.20683 0.24155 0.02204  -0.00566 0.01910  253 ALA B CA  
7167 C  C   . ALA B  253 ? 0.21582 0.19924 0.24248 0.01621  -0.01175 0.00741  253 ALA B C   
7168 O  O   . ALA B  253 ? 0.23148 0.22607 0.25484 0.01557  -0.01732 -0.00049 253 ALA B O   
7169 C  CB  . ALA B  253 ? 0.26140 0.24536 0.25842 0.03041  -0.00908 0.01924  253 ALA B CB  
7175 N  N   . ASN B  254 ? 0.24004 0.21356 0.28013 0.01179  -0.01075 0.00616  254 ASN B N   
7176 C  CA  . ASN B  254 ? 0.24251 0.21788 0.29435 0.00575  -0.01619 -0.00474 254 ASN B CA  
7177 C  C   . ASN B  254 ? 0.25282 0.23663 0.31671 -0.00207 -0.01502 -0.00733 254 ASN B C   
7178 O  O   . ASN B  254 ? 0.25415 0.24272 0.32625 -0.00706 -0.02009 -0.01701 254 ASN B O   
7179 C  CB  . ASN B  254 ? 0.24418 0.20547 0.30594 0.00391  -0.01525 -0.00473 254 ASN B CB  
7180 C  CG  . ASN B  254 ? 0.30550 0.25857 0.35669 0.01103  -0.01762 -0.00416 254 ASN B CG  
7181 O  OD1 . ASN B  254 ? 0.34633 0.30409 0.38243 0.01754  -0.01992 -0.00355 254 ASN B OD1 
7182 N  ND2 . ASN B  254 ? 0.31933 0.26031 0.37832 0.00983  -0.01720 -0.00452 254 ASN B ND2 
7189 N  N   . GLY B  255 ? 0.22126 0.20691 0.28654 -0.00331 -0.00843 0.00109  255 GLY B N   
7190 C  CA  . GLY B  255 ? 0.22436 0.21759 0.30145 -0.01079 -0.00684 -0.00071 255 GLY B CA  
7191 C  C   . GLY B  255 ? 0.24485 0.22978 0.33971 -0.01783 -0.00457 -0.00151 255 GLY B C   
7192 O  O   . GLY B  255 ? 0.27049 0.24273 0.36904 -0.01697 -0.00280 0.00119  255 GLY B O   
7196 N  N   . SER B  256 ? 0.23021 0.22257 0.33667 -0.02514 -0.00442 -0.00512 256 SER B N   
7197 C  CA  . SER B  256 ? 0.27805 0.26396 0.40176 -0.03238 -0.00072 -0.00396 256 SER B CA  
7198 C  C   . SER B  256 ? 0.26509 0.24068 0.38954 -0.03064 0.00751  0.00810  256 SER B C   
7199 O  O   . SER B  256 ? 0.32069 0.28465 0.45455 -0.03287 0.01003  0.01020  256 SER B O   
7200 C  CB  . SER B  256 ? 0.35794 0.33678 0.49105 -0.03555 -0.00535 -0.01213 256 SER B CB  
7201 O  OG  . SER B  256 ? 0.39770 0.38610 0.53019 -0.03722 -0.01294 -0.02330 256 SER B OG  
7207 N  N   . ASN B  257 ? 0.26548 0.24544 0.37995 -0.02669 0.01175  0.01608  257 ASN B N   
7208 C  CA  . ASN B  257 ? 0.26093 0.23187 0.37350 -0.02396 0.01945  0.02799  257 ASN B CA  
7209 C  C   . ASN B  257 ? 0.27114 0.25082 0.37854 -0.02338 0.02405  0.03467  257 ASN B C   
7210 O  O   . ASN B  257 ? 0.27412 0.26617 0.38149 -0.02594 0.02158  0.03003  257 ASN B O   
7211 C  CB  . ASN B  257 ? 0.28716 0.24903 0.38742 -0.01597 0.01897  0.03153  257 ASN B CB  
7212 C  CG  . ASN B  257 ? 0.27261 0.24253 0.35514 -0.00895 0.01533  0.03047  257 ASN B CG  
7213 O  OD1 . ASN B  257 ? 0.26330 0.24506 0.34061 -0.00895 0.01499  0.03010  257 ASN B OD1 
7214 N  ND2 . ASN B  257 ? 0.29336 0.25689 0.36625 -0.00278 0.01243  0.02981  257 ASN B ND2 
7221 N  N   . ARG B  258 ? 0.27926 0.25249 0.38182 -0.01979 0.03080  0.04575  258 ARG B N   
7222 C  CA  . ARG B  258 ? 0.27355 0.25385 0.37199 -0.01943 0.03594  0.05297  258 ARG B CA  
7223 C  C   . ARG B  258 ? 0.25394 0.24496 0.33595 -0.01371 0.03301  0.05210  258 ARG B C   
7224 O  O   . ARG B  258 ? 0.28129 0.27934 0.35918 -0.01336 0.03684  0.05748  258 ARG B O   
7225 C  CB  . ARG B  258 ? 0.29892 0.26891 0.39591 -0.01674 0.04388  0.06518  258 ARG B CB  
7226 C  CG  . ARG B  258 ? 0.30005 0.26344 0.38200 -0.00808 0.04368  0.06960  258 ARG B CG  
7227 C  CD  . ARG B  258 ? 0.39464 0.34608 0.47716 -0.00601 0.05140  0.08121  258 ARG B CD  
7228 N  NE  . ARG B  258 ? 0.82154 0.76103 0.91646 -0.00938 0.05194  0.08006  258 ARG B NE  
7229 C  CZ  . ARG B  258 ? 1.02698 0.95406 1.12348 -0.00758 0.05725  0.08823  258 ARG B CZ  
7230 N  NH1 . ARG B  258 ? 0.91671 0.84127 1.00312 -0.00235 0.06253  0.09832  258 ARG B NH1 
7231 N  NH2 . ARG B  258 ? 1.01764 0.93459 1.12611 -0.01113 0.05727  0.08621  258 ARG B NH2 
7245 N  N   . TYR B  259 ? 0.22771 0.21995 0.30043 -0.00932 0.02657  0.04575  259 TYR B N   
7246 C  CA  . TYR B  259 ? 0.24089 0.24268 0.29733 -0.00342 0.02326  0.04447  259 TYR B CA  
7247 C  C   . TYR B  259 ? 0.22890 0.24346 0.28640 -0.00643 0.01630  0.03339  259 TYR B C   
7248 O  O   . TYR B  259 ? 0.22595 0.24868 0.27036 -0.00176 0.01252  0.03081  259 TYR B O   
7249 C  CB  . TYR B  259 ? 0.26195 0.25656 0.30525 0.00451  0.02100  0.04576  259 TYR B CB  
7250 C  CG  . TYR B  259 ? 0.25742 0.23972 0.29830 0.00809  0.02762  0.05675  259 TYR B CG  
7251 C  CD1 . TYR B  259 ? 0.27318 0.25689 0.30674 0.01101  0.03370  0.06665  259 TYR B CD1 
7252 C  CD2 . TYR B  259 ? 0.26734 0.23660 0.31318 0.00857  0.02766  0.05705  259 TYR B CD2 
7253 C  CE1 . TYR B  259 ? 0.28711 0.25944 0.31854 0.01425  0.03983  0.07681  259 TYR B CE1 
7254 C  CE2 . TYR B  259 ? 0.27556 0.23349 0.31935 0.01180  0.03373  0.06712  259 TYR B CE2 
7255 C  CZ  . TYR B  259 ? 0.27374 0.23329 0.31022 0.01468  0.03970  0.07689  259 TYR B CZ  
7256 O  OH  . TYR B  259 ? 0.33448 0.28229 0.36909 0.01790  0.04571  0.08692  259 TYR B OH  
7266 N  N   . ASP B  260 ? 0.22368 0.24096 0.25934 0.02815  -0.00154 0.03450  260 ASP B N   
7267 C  CA  . ASP B  260 ? 0.21537 0.23562 0.25308 0.02713  -0.00099 0.03248  260 ASP B CA  
7268 C  C   . ASP B  260 ? 0.22332 0.24439 0.25803 0.02811  0.00163  0.03269  260 ASP B C   
7269 O  O   . ASP B  260 ? 0.22035 0.24259 0.25474 0.02803  0.00157  0.02983  260 ASP B O   
7270 C  CB  . ASP B  260 ? 0.22138 0.24419 0.26377 0.02529  -0.00067 0.03432  260 ASP B CB  
7271 C  CG  . ASP B  260 ? 0.25923 0.28211 0.30548 0.02397  -0.00356 0.03298  260 ASP B CG  
7272 O  OD1 . ASP B  260 ? 0.28501 0.30601 0.33045 0.02443  -0.00583 0.03066  260 ASP B OD1 
7273 O  OD2 . ASP B  260 ? 0.34342 0.36826 0.39359 0.02250  -0.00347 0.03445  260 ASP B OD2 
7278 N  N   . ALA B  261 ? 0.22647 0.24718 0.25922 0.02896  0.00397  0.03613  261 ALA B N   
7279 C  CA  . ALA B  261 ? 0.21633 0.23787 0.24631 0.02994  0.00644  0.03643  261 ALA B CA  
7280 C  C   . ALA B  261 ? 0.22189 0.24145 0.24776 0.03155  0.00586  0.03358  261 ALA B C   
7281 O  O   . ALA B  261 ? 0.21726 0.23797 0.24228 0.03170  0.00651  0.03157  261 ALA B O   
7282 C  CB  . ALA B  261 ? 0.23749 0.25873 0.26578 0.03082  0.00890  0.04064  261 ALA B CB  
7288 N  N   . LEU B  262 ? 0.21445 0.23100 0.23782 0.03274  0.00456  0.03342  262 LEU B N   
7289 C  CA  . LEU B  262 ? 0.21151 0.22584 0.23093 0.03437  0.00378  0.03076  262 LEU B CA  
7290 C  C   . LEU B  262 ? 0.22752 0.24265 0.24867 0.03353  0.00171  0.02653  262 LEU B C   
7291 O  O   . LEU B  262 ? 0.20771 0.22298 0.22700 0.03417  0.00194  0.02419  262 LEU B O   
7292 C  CB  . LEU B  262 ? 0.26275 0.27372 0.27957 0.03566  0.00269  0.03173  262 LEU B CB  
7293 C  CG  . LEU B  262 ? 0.28896 0.29700 0.30171 0.03743  0.00146  0.02927  262 LEU B CG  
7294 C  CD1 . LEU B  262 ? 0.33741 0.34238 0.34712 0.03888  0.00142  0.03169  262 LEU B CD1 
7295 C  CD2 . LEU B  262 ? 0.27712 0.28482 0.29158 0.03672  -0.00141 0.02537  262 LEU B CD2 
7307 N  N   . LEU B  263 ? 0.20374 0.21935 0.22841 0.03214  -0.00039 0.02551  263 LEU B N   
7308 C  CA  . LEU B  263 ? 0.19645 0.21287 0.22285 0.03139  -0.00247 0.02151  263 LEU B CA  
7309 C  C   . LEU B  263 ? 0.19177 0.21131 0.21979 0.03044  -0.00129 0.02025  263 LEU B C   
7310 O  O   . LEU B  263 ? 0.18816 0.20801 0.21524 0.03071  -0.00183 0.01720  263 LEU B O   
7311 C  CB  . LEU B  263 ? 0.20970 0.22638 0.23989 0.03003  -0.00478 0.02103  263 LEU B CB  
7312 C  CG  . LEU B  263 ? 0.20107 0.21453 0.22992 0.03087  -0.00661 0.02147  263 LEU B CG  
7313 C  CD1 . LEU B  263 ? 0.22007 0.23424 0.25326 0.02930  -0.00850 0.02179  263 LEU B CD1 
7314 C  CD2 . LEU B  263 ? 0.22375 0.23512 0.25004 0.03203  -0.00842 0.01803  263 LEU B CD2 
7326 N  N   . GLY B  264 ? 0.19296 0.21491 0.22373 0.02920  0.00017  0.02249  264 GLY B N   
7327 C  CA  . GLY B  264 ? 0.19513 0.22008 0.22765 0.02818  0.00121  0.02137  264 GLY B CA  
7328 C  C   . GLY B  264 ? 0.19239 0.21720 0.22144 0.02940  0.00319  0.02137  264 GLY B C   
7329 O  O   . GLY B  264 ? 0.17821 0.20446 0.20742 0.02909  0.00323  0.01899  264 GLY B O   
7333 N  N   . LYS B  265 ? 0.18411 0.20721 0.20998 0.03084  0.00482  0.02404  265 LYS B N   
7334 C  CA  . LYS B  265 ? 0.18271 0.20548 0.20504 0.03220  0.00662  0.02402  265 LYS B CA  
7335 C  C   . LYS B  265 ? 0.17772 0.19899 0.19767 0.03316  0.00516  0.02046  265 LYS B C   
7336 O  O   . LYS B  265 ? 0.19292 0.21545 0.21262 0.03302  0.00553  0.01853  265 LYS B O   
7337 C  CB  . LYS B  265 ? 0.20505 0.22595 0.22411 0.03381  0.00833  0.02733  265 LYS B CB  
7338 C  CG  . LYS B  265 ? 0.22184 0.24173 0.23660 0.03563  0.00984  0.02714  265 LYS B CG  
7339 C  CD  . LYS B  265 ? 0.22086 0.23949 0.23265 0.03717  0.01189  0.03074  265 LYS B CD  
7340 C  CE  . LYS B  265 ? 0.24477 0.26077 0.25526 0.03797  0.01079  0.03190  265 LYS B CE  
7341 N  NZ  . LYS B  265 ? 0.29489 0.30991 0.30252 0.03947  0.01298  0.03569  265 LYS B NZ  
7355 N  N   . TYR B  266 ? 0.18026 0.19878 0.19845 0.03413  0.00344  0.01960  266 TYR B N   
7356 C  CA  . TYR B  266 ? 0.18622 0.20303 0.20188 0.03524  0.00209  0.01641  266 TYR B CA  
7357 C  C   . TYR B  266 ? 0.18927 0.20781 0.20794 0.03385  0.00023  0.01290  266 TYR B C   
7358 O  O   . TYR B  266 ? 0.18554 0.20428 0.20313 0.03420  -0.00010 0.01035  266 TYR B O   
7359 C  CB  . TYR B  266 ? 0.19329 0.20655 0.20609 0.03676  0.00083  0.01663  266 TYR B CB  
7360 C  CG  . TYR B  266 ? 0.21524 0.22648 0.22403 0.03860  0.00267  0.01958  266 TYR B CG  
7361 C  CD1 . TYR B  266 ? 0.22239 0.23334 0.22799 0.03993  0.00428  0.01964  266 TYR B CD1 
7362 C  CD2 . TYR B  266 ? 0.24468 0.25437 0.25295 0.03900  0.00272  0.02231  266 TYR B CD2 
7363 C  CE1 . TYR B  266 ? 0.26279 0.27204 0.26473 0.04170  0.00594  0.02224  266 TYR B CE1 
7364 C  CE2 . TYR B  266 ? 0.27122 0.27916 0.27572 0.04076  0.00444  0.02504  266 TYR B CE2 
7365 C  CZ  . TYR B  266 ? 0.26618 0.27397 0.26752 0.04213  0.00604  0.02490  266 TYR B CZ  
7366 O  OH  . TYR B  266 ? 0.31310 0.31912 0.31051 0.04404  0.00767  0.02750  266 TYR B OH  
7376 N  N   . GLY B  267 ? 0.17368 0.19367 0.19622 0.03226  -0.00095 0.01278  267 GLY B N   
7377 C  CA  . GLY B  267 ? 0.17909 0.20093 0.20452 0.03100  -0.00269 0.00946  267 GLY B CA  
7378 C  C   . GLY B  267 ? 0.16721 0.19215 0.19417 0.02997  -0.00137 0.00870  267 GLY B C   
7379 O  O   . GLY B  267 ? 0.17731 0.20318 0.20450 0.02976  -0.00215 0.00576  267 GLY B O   
7383 N  N   . VAL B  268 ? 0.16522 0.19195 0.19353 0.02921  0.00057  0.01136  268 VAL B N   
7384 C  CA  . VAL B  268 ? 0.16716 0.19673 0.19673 0.02828  0.00197  0.01093  268 VAL B CA  
7385 C  C   . VAL B  268 ? 0.18215 0.21075 0.20813 0.02963  0.00297  0.01012  268 VAL B C   
7386 O  O   . VAL B  268 ? 0.16883 0.19899 0.19536 0.02912  0.00284  0.00786  268 VAL B O   
7387 C  CB  . VAL B  268 ? 0.16532 0.19682 0.19696 0.02729  0.00385  0.01407  268 VAL B CB  
7388 C  CG1 . VAL B  268 ? 0.18706 0.22102 0.21915 0.02668  0.00554  0.01389  268 VAL B CG1 
7389 C  CG2 . VAL B  268 ? 0.17810 0.21105 0.21390 0.02570  0.00254  0.01416  268 VAL B CG2 
7399 N  N   . ALA B  269 ? 0.18399 0.21005 0.20626 0.03138  0.00401  0.01202  269 ALA B N   
7400 C  CA  . ALA B  269 ? 0.18520 0.21021 0.20399 0.03277  0.00485  0.01120  269 ALA B CA  
7401 C  C   . ALA B  269 ? 0.17348 0.19765 0.19162 0.03308  0.00283  0.00748  269 ALA B C   
7402 O  O   . ALA B  269 ? 0.18090 0.20583 0.19833 0.03317  0.00312  0.00585  269 ALA B O   
7403 C  CB  . ALA B  269 ? 0.19130 0.21347 0.20601 0.03479  0.00596  0.01355  269 ALA B CB  
7409 N  N   . TRP B  270 ? 0.16877 0.19131 0.18713 0.03330  0.00073  0.00615  270 TRP B N   
7410 C  CA  . TRP B  270 ? 0.16859 0.19038 0.18651 0.03360  -0.00128 0.00258  270 TRP B CA  
7411 C  C   . TRP B  270 ? 0.18606 0.21113 0.20728 0.03190  -0.00171 0.00026  270 TRP B C   
7412 O  O   . TRP B  270 ? 0.18322 0.20854 0.20366 0.03214  -0.00211 -0.00204 270 TRP B O   
7413 C  CB  . TRP B  270 ? 0.18021 0.20012 0.19849 0.03384  -0.00347 0.00170  270 TRP B CB  
7414 C  CG  . TRP B  270 ? 0.17791 0.19617 0.19466 0.03473  -0.00542 -0.00162 270 TRP B CG  
7415 C  CD1 . TRP B  270 ? 0.19480 0.21418 0.21389 0.03388  -0.00743 -0.00478 270 TRP B CD1 
7416 C  CD2 . TRP B  270 ? 0.18775 0.20290 0.20024 0.03675  -0.00551 -0.00199 270 TRP B CD2 
7417 N  NE1 . TRP B  270 ? 0.19217 0.20935 0.20880 0.03520  -0.00874 -0.00709 270 TRP B NE1 
7418 C  CE2 . TRP B  270 ? 0.18661 0.20110 0.19917 0.03697  -0.00765 -0.00545 270 TRP B CE2 
7419 C  CE3 . TRP B  270 ? 0.22207 0.23496 0.23066 0.03847  -0.00400 0.00025  270 TRP B CE3 
7420 C  CZ2 . TRP B  270 ? 0.21539 0.22694 0.22433 0.03880  -0.00837 -0.00671 270 TRP B CZ2 
7421 C  CZ3 . TRP B  270 ? 0.20475 0.21472 0.20961 0.04034  -0.00474 -0.00107 270 TRP B CZ3 
7422 C  CH2 . TRP B  270 ? 0.21114 0.22042 0.21624 0.04046  -0.00694 -0.00451 270 TRP B CH2 
7433 N  N   . MET B  271 ? 0.16331 0.19087 0.18832 0.03018  -0.00181 0.00075  271 MET B N   
7434 C  CA  . MET B  271 ? 0.15806 0.18884 0.18625 0.02858  -0.00227 -0.00144 271 MET B CA  
7435 C  C   . MET B  271 ? 0.18239 0.21505 0.21032 0.02820  -0.00032 -0.00090 271 MET B C   
7436 O  O   . MET B  271 ? 0.18361 0.21788 0.21232 0.02764  -0.00069 -0.00319 271 MET B O   
7437 C  CB  . MET B  271 ? 0.16644 0.19924 0.19859 0.02699  -0.00296 -0.00104 271 MET B CB  
7438 C  CG  . MET B  271 ? 0.16926 0.20035 0.20198 0.02726  -0.00523 -0.00205 271 MET B CG  
7439 S  SD  . MET B  271 ? 0.18935 0.21927 0.22094 0.02804  -0.00751 -0.00614 271 MET B SD  
7440 C  CE  . MET B  271 ? 0.21816 0.24853 0.25303 0.02718  -0.01012 -0.00771 271 MET B CE  
7450 N  N   . LYS B  272 ? 0.17438 0.20687 0.20120 0.02852  0.00174  0.00213  272 LYS B N   
7451 C  CA  . LYS B  272 ? 0.16599 0.19991 0.19217 0.02837  0.00356  0.00271  272 LYS B CA  
7452 C  C   . LYS B  272 ? 0.19086 0.22313 0.21388 0.02972  0.00335  0.00101  272 LYS B C   
7453 O  O   . LYS B  272 ? 0.18198 0.21590 0.20563 0.02910  0.00347  -0.00059 272 LYS B O   
7454 C  CB  . LYS B  272 ? 0.17810 0.21167 0.20321 0.02881  0.00572  0.00630  272 LYS B CB  
7455 C  CG  . LYS B  272 ? 0.17756 0.21325 0.20602 0.02732  0.00636  0.00827  272 LYS B CG  
7456 C  CD  . LYS B  272 ? 0.19319 0.23218 0.22424 0.02574  0.00723  0.00786  272 LYS B CD  
7457 C  CE  . LYS B  272 ? 0.19341 0.23421 0.22722 0.02454  0.00830  0.01040  272 LYS B CE  
7458 N  NZ  . LYS B  272 ? 0.19733 0.24128 0.23361 0.02303  0.00909  0.00999  272 LYS B NZ  
7472 N  N   . LEU B  273 ? 0.19038 0.21935 0.21001 0.03155  0.00292  0.00130  273 LEU B N   
7473 C  CA  . LEU B  273 ? 0.20104 0.22818 0.21747 0.03300  0.00270  -0.00015 273 LEU B CA  
7474 C  C   . LEU B  273 ? 0.22101 0.24889 0.23878 0.03241  0.00078  -0.00372 273 LEU B C   
7475 O  O   . LEU B  273 ? 0.24357 0.27205 0.26079 0.03244  0.00090  -0.00515 273 LEU B O   
7476 C  CB  . LEU B  273 ? 0.21217 0.23555 0.22479 0.03511  0.00243  0.00082  273 LEU B CB  
7477 C  CG  . LEU B  273 ? 0.22770 0.24867 0.23660 0.03691  0.00208  -0.00056 273 LEU B CG  
7478 C  CD1 . LEU B  273 ? 0.26076 0.28271 0.26855 0.03711  0.00394  0.00040  273 LEU B CD1 
7479 C  CD2 . LEU B  273 ? 0.26802 0.28526 0.27311 0.03903  0.00182  0.00057  273 LEU B CD2 
7491 N  N   . HIS B  274 ? 0.18639 0.21449 0.20619 0.03177  -0.00100 -0.00520 274 HIS B N   
7492 C  CA  . HIS B  274 ? 0.19683 0.22520 0.21747 0.03155  -0.00295 -0.00862 274 HIS B CA  
7493 C  C   . HIS B  274 ? 0.21042 0.24257 0.23508 0.02953  -0.00329 -0.01019 274 HIS B C   
7494 O  O   . HIS B  274 ? 0.28535 0.31860 0.31057 0.02920  -0.00398 -0.01258 274 HIS B O   
7495 C  CB  . HIS B  274 ? 0.20505 0.23097 0.22492 0.03243  -0.00491 -0.00968 274 HIS B CB  
7496 C  CG  . HIS B  274 ? 0.18436 0.20645 0.19994 0.03457  -0.00474 -0.00854 274 HIS B CG  
7497 N  ND1 . HIS B  274 ? 0.24516 0.26547 0.25773 0.03596  -0.00477 -0.00958 274 HIS B ND1 
7498 C  CD2 . HIS B  274 ? 0.20373 0.22350 0.21746 0.03558  -0.00440 -0.00625 274 HIS B CD2 
7499 C  CE1 . HIS B  274 ? 0.22899 0.24597 0.23794 0.03782  -0.00455 -0.00814 274 HIS B CE1 
7500 N  NE2 . HIS B  274 ? 0.23851 0.25516 0.24807 0.03761  -0.00427 -0.00606 274 HIS B NE2 
7508 N  N   . LEU B  275 ? 0.18550 0.21971 0.21303 0.02818  -0.00292 -0.00901 275 LEU B N   
7509 C  CA  . LEU B  275 ? 0.18429 0.22219 0.21549 0.02632  -0.00315 -0.01045 275 LEU B CA  
7510 C  C   . LEU B  275 ? 0.21051 0.25060 0.24216 0.02551  -0.00124 -0.00943 275 LEU B C   
7511 O  O   . LEU B  275 ? 0.21144 0.25413 0.24505 0.02438  -0.00148 -0.01125 275 LEU B O   
7512 C  CB  . LEU B  275 ? 0.18387 0.22320 0.21817 0.02517  -0.00372 -0.00982 275 LEU B CB  
7513 C  CG  . LEU B  275 ? 0.18585 0.22342 0.22038 0.02569  -0.00590 -0.01109 275 LEU B CG  
7514 C  CD1 . LEU B  275 ? 0.20271 0.24185 0.24047 0.02448  -0.00641 -0.01034 275 LEU B CD1 
7515 C  CD2 . LEU B  275 ? 0.20733 0.24518 0.24218 0.02581  -0.00771 -0.01459 275 LEU B CD2 
7527 N  N   . ASP B  276 ? 0.19231 0.19452 0.23419 0.00952  -0.00264 0.00158  276 ASP B N   
7528 C  CA  . ASP B  276 ? 0.18322 0.18345 0.22528 0.01139  -0.00056 0.00287  276 ASP B CA  
7529 C  C   . ASP B  276 ? 0.19973 0.19277 0.23913 0.01476  -0.00251 -0.00097 276 ASP B C   
7530 O  O   . ASP B  276 ? 0.24734 0.23803 0.28667 0.01652  -0.00103 -0.00022 276 ASP B O   
7531 C  CB  . ASP B  276 ? 0.19083 0.19683 0.22911 0.01387  0.00254  0.00664  276 ASP B CB  
7532 C  CG  . ASP B  276 ? 0.19443 0.20776 0.23548 0.01102  0.00455  0.01052  276 ASP B CG  
7533 O  OD1 . ASP B  276 ? 0.19915 0.21307 0.24512 0.00717  0.00392  0.01068  276 ASP B OD1 
7534 O  OD2 . ASP B  276 ? 0.21397 0.23232 0.25221 0.01290  0.00658  0.01320  276 ASP B OD2 
7539 N  N   . GLN B  277 ? 0.21020 0.19974 0.24775 0.01563  -0.00585 -0.00506 277 GLN B N   
7540 C  CA  . GLN B  277 ? 0.22658 0.20924 0.26145 0.01922  -0.00819 -0.00922 277 GLN B CA  
7541 C  C   . GLN B  277 ? 0.23785 0.22126 0.26651 0.02422  -0.00625 -0.00785 277 GLN B C   
7542 O  O   . GLN B  277 ? 0.27109 0.24913 0.29889 0.02682  -0.00679 -0.00970 277 GLN B O   
7543 C  CB  . GLN B  277 ? 0.28438 0.26069 0.32592 0.01684  -0.00934 -0.01118 277 GLN B CB  
7544 C  CG  . GLN B  277 ? 0.29442 0.26993 0.34174 0.01234  -0.01165 -0.01301 277 GLN B CG  
7545 C  CD  . GLN B  277 ? 0.57071 0.54430 0.61450 0.01406  -0.01546 -0.01753 277 GLN B CD  
7546 O  OE1 . GLN B  277 ? 0.58368 0.55253 0.62385 0.01795  -0.01763 -0.02114 277 GLN B OE1 
7547 N  NE2 . GLN B  277 ? 0.50052 0.47786 0.54497 0.01154  -0.01631 -0.01736 277 GLN B NE2 
7556 N  N   . ASP B  278 ? 0.21566 0.20572 0.24014 0.02564  -0.00410 -0.00465 278 ASP B N   
7557 C  CA  . ASP B  278 ? 0.22341 0.21582 0.24263 0.02995  -0.00156 -0.00229 278 ASP B CA  
7558 C  C   . ASP B  278 ? 0.22326 0.21475 0.23491 0.03522  -0.00317 -0.00468 278 ASP B C   
7559 O  O   . ASP B  278 ? 0.22923 0.22571 0.23745 0.03624  -0.00272 -0.00331 278 ASP B O   
7560 C  CB  . ASP B  278 ? 0.21958 0.22018 0.23970 0.02826  0.00190  0.00288  278 ASP B CB  
7561 C  CG  . ASP B  278 ? 0.22527 0.22893 0.24120 0.03213  0.00482  0.00574  278 ASP B CG  
7562 O  OD1 . ASP B  278 ? 0.23231 0.23228 0.24334 0.03673  0.00427  0.00388  278 ASP B OD1 
7563 O  OD2 . ASP B  278 ? 0.21886 0.22883 0.23661 0.03056  0.00760  0.00982  278 ASP B OD2 
7568 N  N   . GLN B  279 ? 0.25031 0.23535 0.25937 0.03882  -0.00499 -0.00815 279 GLN B N   
7569 C  CA  . GLN B  279 ? 0.28323 0.26642 0.28506 0.04429  -0.00709 -0.01119 279 GLN B CA  
7570 C  C   . GLN B  279 ? 0.24187 0.23078 0.23700 0.04876  -0.00422 -0.00776 279 GLN B C   
7571 O  O   . GLN B  279 ? 0.27406 0.26320 0.26266 0.05349  -0.00544 -0.00938 279 GLN B O   
7572 C  CB  . GLN B  279 ? 0.32076 0.29534 0.32203 0.04703  -0.00991 -0.01590 279 GLN B CB  
7573 C  CG  . GLN B  279 ? 0.35280 0.32162 0.36035 0.04326  -0.01345 -0.02005 279 GLN B CG  
7574 C  CD  . GLN B  279 ? 0.41544 0.38507 0.42140 0.04316  -0.01636 -0.02283 279 GLN B CD  
7575 O  OE1 . GLN B  279 ? 0.43208 0.40332 0.43081 0.04791  -0.01717 -0.02388 279 GLN B OE1 
7576 N  NE2 . GLN B  279 ? 0.59066 0.55940 0.60325 0.03796  -0.01783 -0.02390 279 GLN B NE2 
7585 N  N   . ARG B  280 ? 0.23310 0.22680 0.22971 0.04766  -0.00046 -0.00309 280 ARG B N   
7586 C  CA  . ARG B  280 ? 0.24218 0.24211 0.23322 0.05157  0.00237  0.00046  280 ARG B CA  
7587 C  C   . ARG B  280 ? 0.23468 0.24026 0.22393 0.05133  0.00256  0.00198  280 ARG B C   
7588 O  O   . ARG B  280 ? 0.25534 0.26512 0.23899 0.05561  0.00413  0.00397  280 ARG B O   
7589 C  CB  . ARG B  280 ? 0.24096 0.24582 0.23520 0.04954  0.00618  0.00522  280 ARG B CB  
7590 C  CG  . ARG B  280 ? 0.23904 0.23893 0.23482 0.05006  0.00665  0.00450  280 ARG B CG  
7591 C  CD  . ARG B  280 ? 0.25117 0.25623 0.24992 0.04832  0.01037  0.00913  280 ARG B CD  
7592 N  NE  . ARG B  280 ? 0.22444 0.23286 0.22984 0.04250  0.01089  0.01097  280 ARG B NE  
7593 C  CZ  . ARG B  280 ? 0.20888 0.22288 0.21779 0.04013  0.01368  0.01488  280 ARG B CZ  
7594 N  NH1 . ARG B  280 ? 0.22388 0.24127 0.23048 0.04293  0.01644  0.01766  280 ARG B NH1 
7595 N  NH2 . ARG B  280 ? 0.22641 0.24285 0.24108 0.03513  0.01359  0.01594  280 ARG B NH2 
7609 N  N   . TYR B  281 ? 0.21680 0.22253 0.21065 0.04663  0.00108  0.00117  281 TYR B N   
7610 C  CA  . TYR B  281 ? 0.23526 0.24622 0.22797 0.04601  0.00133  0.00280  281 TYR B CA  
7611 C  C   . TYR B  281 ? 0.24310 0.25048 0.23137 0.04895  -0.00201 -0.00140 281 TYR B C   
7612 O  O   . TYR B  281 ? 0.24176 0.25323 0.22763 0.04974  -0.00167 -0.00006 281 TYR B O   
7613 C  CB  . TYR B  281 ? 0.20729 0.22145 0.20730 0.03940  0.00198  0.00490  281 TYR B CB  
7614 C  CG  . TYR B  281 ? 0.20470 0.22474 0.20760 0.03771  0.00563  0.00979  281 TYR B CG  
7615 C  CD1 . TYR B  281 ? 0.19252 0.21070 0.19895 0.03621  0.00671  0.01035  281 TYR B CD1 
7616 C  CD2 . TYR B  281 ? 0.18834 0.21589 0.19049 0.03798  0.00810  0.01393  281 TYR B CD2 
7617 C  CE1 . TYR B  281 ? 0.20139 0.22511 0.21009 0.03518  0.00991  0.01458  281 TYR B CE1 
7618 C  CE2 . TYR B  281 ? 0.20029 0.23339 0.20537 0.03663  0.01119  0.01811  281 TYR B CE2 
7619 C  CZ  . TYR B  281 ? 0.19081 0.22213 0.19896 0.03533  0.01204  0.01834  281 TYR B CZ  
7620 O  OH  . TYR B  281 ? 0.21554 0.25274 0.22627 0.03445  0.01501  0.02236  281 TYR B OH  
7630 N  N   . ALA B  282 ? 0.24329 0.24328 0.23033 0.05091  -0.00518 -0.00637 282 ALA B N   
7631 C  CA  . ALA B  282 ? 0.24984 0.24644 0.23266 0.05400  -0.00870 -0.01080 282 ALA B CA  
7632 C  C   . ALA B  282 ? 0.25359 0.25355 0.22788 0.06057  -0.00774 -0.00970 282 ALA B C   
7633 O  O   . ALA B  282 ? 0.25924 0.26037 0.23059 0.06201  -0.00914 -0.01083 282 ALA B O   
7634 C  CB  . ALA B  282 ? 0.28884 0.27678 0.27233 0.05521  -0.01240 -0.01650 282 ALA B CB  
7640 N  N   . PRO B  283 ? 0.26969 0.27166 0.23976 0.06479  -0.00526 -0.00730 283 PRO B N   
7641 C  CA  . PRO B  283 ? 0.26792 0.27299 0.22963 0.07158  -0.00442 -0.00635 283 PRO B CA  
7642 C  C   . PRO B  283 ? 0.28410 0.29689 0.24540 0.07078  -0.00176 -0.00172 283 PRO B C   
7643 O  O   . PRO B  283 ? 0.29891 0.31402 0.25367 0.07613  -0.00144 -0.00120 283 PRO B O   
7644 C  CB  . PRO B  283 ? 0.31422 0.32006 0.27284 0.07535  -0.00200 -0.00430 283 PRO B CB  
7645 C  CG  . PRO B  283 ? 0.34891 0.34897 0.31252 0.07220  -0.00318 -0.00657 283 PRO B CG  
7646 C  CD  . PRO B  283 ? 0.28112 0.28118 0.25305 0.06457  -0.00379 -0.00642 283 PRO B CD  
7654 N  N   . PHE B  284 ? 0.24785 0.26476 0.21589 0.06455  0.00019  0.00177  284 PHE B N   
7655 C  CA  . PHE B  284 ? 0.26141 0.28525 0.22995 0.06334  0.00246  0.00601  284 PHE B CA  
7656 C  C   . PHE B  284 ? 0.25518 0.27727 0.22351 0.06222  -0.00033 0.00324  284 PHE B C   
7657 O  O   . PHE B  284 ? 0.28196 0.30891 0.24897 0.06274  0.00112  0.00611  284 PHE B O   
7658 C  CB  . PHE B  284 ? 0.26435 0.29326 0.24034 0.05728  0.00535  0.01056  284 PHE B CB  
7659 C  CG  . PHE B  284 ? 0.25408 0.28510 0.23019 0.05858  0.00812  0.01329  284 PHE B CG  
7660 C  CD1 . PHE B  284 ? 0.28767 0.32436 0.26004 0.06268  0.01130  0.01733  284 PHE B CD1 
7661 C  CD2 . PHE B  284 ? 0.28916 0.31624 0.26910 0.05595  0.00751  0.01171  284 PHE B CD2 
7662 C  CE1 . PHE B  284 ? 0.30035 0.33878 0.27257 0.06416  0.01364  0.01949  284 PHE B CE1 
7663 C  CE2 . PHE B  284 ? 0.29038 0.31910 0.27008 0.05744  0.00996  0.01401  284 PHE B CE2 
7664 C  CZ  . PHE B  284 ? 0.30585 0.34018 0.28150 0.06163  0.01291  0.01772  284 PHE B CZ  
7674 N  N   . LEU B  285 ? 0.24774 0.26317 0.21775 0.06061  -0.00415 -0.00204 285 LEU B N   
7675 C  CA  . LEU B  285 ? 0.25263 0.26603 0.22327 0.05898  -0.00715 -0.00515 285 LEU B CA  
7676 C  C   . LEU B  285 ? 0.25610 0.26443 0.22013 0.06487  -0.01073 -0.01049 285 LEU B C   
7677 O  O   . LEU B  285 ? 0.28784 0.29713 0.24856 0.06679  -0.01193 -0.01147 285 LEU B O   
7678 C  CB  . LEU B  285 ? 0.25464 0.26470 0.23334 0.05209  -0.00896 -0.00714 285 LEU B CB  
7679 C  CG  . LEU B  285 ? 0.25305 0.26848 0.23848 0.04602  -0.00594 -0.00219 285 LEU B CG  
7680 C  CD1 . LEU B  285 ? 0.26603 0.27756 0.25851 0.04071  -0.00728 -0.00406 285 LEU B CD1 
7681 C  CD2 . LEU B  285 ? 0.28090 0.30084 0.26682 0.04418  -0.00543 -0.00006 285 LEU B CD2 
7693 N  N   . CYS B  286 ? 0.27449 0.27736 0.23659 0.06787  -0.01259 -0.01411 286 CYS B N   
7694 C  CA  . CYS B  286 ? 0.29278 0.29020 0.24904 0.07358  -0.01655 -0.01990 286 CYS B CA  
7695 C  C   . CYS B  286 ? 0.31246 0.31038 0.26122 0.08091  -0.01525 -0.01918 286 CYS B C   
7696 O  O   . CYS B  286 ? 0.32518 0.32177 0.27510 0.08093  -0.01398 -0.01833 286 CYS B O   
7697 C  CB  . CYS B  286 ? 0.32768 0.31738 0.28885 0.07075  -0.02058 -0.02555 286 CYS B CB  
7698 S  SG  . CYS B  286 ? 0.36514 0.35392 0.33467 0.06283  -0.02269 -0.02712 286 CYS B SG  
7703 N  N   . GLY B  287 ? 0.30591 0.30591 0.24684 0.08733  -0.01543 -0.01937 287 GLY B N   
7704 C  CA  . GLY B  287 ? 0.32585 0.32725 0.25898 0.09488  -0.01393 -0.01821 287 GLY B CA  
7705 C  C   . GLY B  287 ? 0.38412 0.39310 0.31220 0.09860  -0.01030 -0.01294 287 GLY B C   
7706 O  O   . GLY B  287 ? 0.38611 0.39554 0.30593 0.10617  -0.01089 -0.01400 287 GLY B O   
7710 N  N   . PRO B  288 ? 0.33144 0.34666 0.26449 0.09359  -0.00640 -0.00702 288 PRO B N   
7711 C  CA  . PRO B  288 ? 0.34591 0.36868 0.27514 0.09690  -0.00247 -0.00133 288 PRO B CA  
7712 C  C   . PRO B  288 ? 0.33044 0.35393 0.25587 0.09940  -0.00388 -0.00246 288 PRO B C   
7713 O  O   . PRO B  288 ? 0.33313 0.35300 0.26128 0.09607  -0.00715 -0.00630 288 PRO B O   
7714 C  CB  . PRO B  288 ? 0.33723 0.36559 0.27451 0.08975  0.00131  0.00448  288 PRO B CB  
7715 C  CG  . PRO B  288 ? 0.29940 0.32355 0.24250 0.08492  0.00017  0.00240  288 PRO B CG  
7716 C  CD  . PRO B  288 ? 0.30846 0.32442 0.25082 0.08525  -0.00505 -0.00486 288 PRO B CD  
7724 N  N   . ASN B  289 ? 0.33063 0.35925 0.24972 0.10550  -0.00112 0.00127  289 ASN B N   
7725 C  CA  . ASN B  289 ? 0.31790 0.34884 0.23375 0.10772  -0.00120 0.00197  289 ASN B CA  
7726 C  C   . ASN B  289 ? 0.33555 0.37299 0.25797 0.10170  0.00274  0.00844  289 ASN B C   
7727 O  O   . ASN B  289 ? 0.33132 0.37538 0.25243 0.10399  0.00708  0.01455  289 ASN B O   
7728 C  CB  . ASN B  289 ? 0.34765 0.38092 0.25335 0.11772  -0.00004 0.00299  289 ASN B CB  
7729 C  CG  . ASN B  289 ? 0.44538 0.47182 0.34377 0.12432  -0.00507 -0.00456 289 ASN B CG  
7730 O  OD1 . ASN B  289 ? 0.72593 0.74906 0.62187 0.12735  -0.00632 -0.00715 289 ASN B OD1 
7731 N  ND2 . ASN B  289 ? 0.57101 0.59548 0.46603 0.12667  -0.00798 -0.00806 289 ASN B ND2 
7738 N  N   . HIS B  290 ? 0.29899 0.33440 0.22877 0.09401  0.00099  0.00687  290 HIS B N   
7739 C  CA  . HIS B  290 ? 0.28696 0.32766 0.22423 0.08731  0.00409  0.01225  290 HIS B CA  
7740 C  C   . HIS B  290 ? 0.29730 0.34352 0.23227 0.08958  0.00676  0.01679  290 HIS B C   
7741 O  O   . HIS B  290 ? 0.29611 0.34834 0.23571 0.08652  0.01063  0.02283  290 HIS B O   
7742 C  CB  . HIS B  290 ? 0.27866 0.31579 0.22324 0.07949  0.00125  0.00917  290 HIS B CB  
7743 C  CG  . HIS B  290 ? 0.26942 0.30120 0.21731 0.07667  -0.00113 0.00515  290 HIS B CG  
7744 N  ND1 . HIS B  290 ? 0.27605 0.30964 0.22927 0.07283  0.00114  0.00797  290 HIS B ND1 
7745 C  CD2 . HIS B  290 ? 0.27715 0.30181 0.22403 0.07726  -0.00555 -0.00142 290 HIS B CD2 
7746 C  CE1 . HIS B  290 ? 0.26533 0.29301 0.22037 0.07132  -0.00160 0.00351  290 HIS B CE1 
7747 N  NE2 . HIS B  290 ? 0.26184 0.28402 0.21346 0.07377  -0.00568 -0.00218 290 HIS B NE2 
7755 N  N   . GLU B  291 ? 0.32075 0.36521 0.24859 0.09532  0.00490  0.01416  291 GLU B N   
7756 C  CA  . GLU B  291 ? 0.30731 0.35677 0.23292 0.09763  0.00755  0.01861  291 GLU B CA  
7757 C  C   . GLU B  291 ? 0.33292 0.38881 0.25518 0.10289  0.01248  0.02500  291 GLU B C   
7758 O  O   . GLU B  291 ? 0.37795 0.43900 0.30005 0.10400  0.01566  0.03014  291 GLU B O   
7759 C  CB  . GLU B  291 ? 0.33532 0.38119 0.25393 0.10272  0.00417  0.01394  291 GLU B CB  
7760 C  CG  . GLU B  291 ? 0.30248 0.34330 0.22560 0.09675  -0.00018 0.00867  291 GLU B CG  
7761 C  CD  . GLU B  291 ? 0.38209 0.41877 0.29839 0.10193  -0.00419 0.00300  291 GLU B CD  
7762 O  OE1 . GLU B  291 ? 0.38390 0.42118 0.29148 0.11056  -0.00390 0.00267  291 GLU B OE1 
7763 O  OE2 . GLU B  291 ? 0.35645 0.38937 0.27604 0.09764  -0.00773 -0.00126 291 GLU B OE2 
7770 N  N   . ARG B  292 ? 0.31670 0.37254 0.23659 0.10612  0.01331  0.02502  292 ARG B N   
7771 C  CA  . ARG B  292 ? 0.33974 0.40234 0.25786 0.11015  0.01831  0.03161  292 ARG B CA  
7772 C  C   . ARG B  292 ? 0.37226 0.44089 0.29972 0.10329  0.02219  0.03799  292 ARG B C   
7773 O  O   . ARG B  292 ? 0.44628 0.52158 0.37373 0.10577  0.02667  0.04443  292 ARG B O   
7774 C  CB  . ARG B  292 ? 0.38334 0.44451 0.29763 0.11439  0.01824  0.03015  292 ARG B CB  
7775 C  CG  . ARG B  292 ? 0.36673 0.42357 0.27085 0.12300  0.01533  0.02519  292 ARG B CG  
7776 C  CD  . ARG B  292 ? 0.44721 0.50295 0.34750 0.12741  0.01553  0.02419  292 ARG B CD  
7777 N  NE  . ARG B  292 ? 0.39183 0.44119 0.28393 0.13394  0.01105  0.01732  292 ARG B NE  
7778 C  CZ  . ARG B  292 ? 0.36666 0.41146 0.25582 0.13670  0.00875  0.01318  292 ARG B CZ  
7779 N  NH1 . ARG B  292 ? 0.43996 0.48599 0.33300 0.13396  0.01078  0.01543  292 ARG B NH1 
7780 N  NH2 . ARG B  292 ? 0.44470 0.48357 0.32681 0.14260  0.00425  0.00657  292 ARG B NH2 
7794 N  N   . ASP B  293 ? 0.33346 0.40001 0.26897 0.09498  0.02053  0.03636  293 ASP B N   
7795 C  CA  . ASP B  293 ? 0.34474 0.41659 0.28949 0.08819  0.02353  0.04167  293 ASP B CA  
7796 C  C   . ASP B  293 ? 0.34744 0.42302 0.29326 0.08782  0.02534  0.04551  293 ASP B C   
7797 O  O   . ASP B  293 ? 0.31185 0.38389 0.25565 0.08758  0.02260  0.04220  293 ASP B O   
7798 C  CB  . ASP B  293 ? 0.32847 0.39629 0.28036 0.08019  0.02057  0.03800  293 ASP B CB  
7799 C  CG  . ASP B  293 ? 0.32094 0.39374 0.28254 0.07318  0.02310  0.04263  293 ASP B CG  
7800 O  OD1 . ASP B  293 ? 0.35948 0.43799 0.32416 0.07229  0.02616  0.04799  293 ASP B OD1 
7801 O  OD2 . ASP B  293 ? 0.38327 0.45405 0.34948 0.06873  0.02189  0.04069  293 ASP B OD2 
7806 N  N   . ARG B  294 ? 0.36014 0.44289 0.30950 0.08769  0.02994  0.05251  294 ARG B N   
7807 C  CA  . ARG B  294 ? 0.34667 0.43315 0.29747 0.08751  0.03207  0.05677  294 ARG B CA  
7808 C  C   . ARG B  294 ? 0.31534 0.39981 0.27303 0.07969  0.02983  0.05517  294 ARG B C   
7809 O  O   . ARG B  294 ? 0.33870 0.42391 0.29602 0.07980  0.03016  0.05662  294 ARG B O   
7810 C  CB  . ARG B  294 ? 0.46709 0.56178 0.42164 0.08846  0.03753  0.06483  294 ARG B CB  
7811 C  CG  . ARG B  294 ? 0.84170 0.93886 0.78786 0.09771  0.04007  0.06699  294 ARG B CG  
7812 C  CD  . ARG B  294 ? 0.98417 1.08970 0.93335 0.09965  0.04572  0.07542  294 ARG B CD  
7813 N  NE  . ARG B  294 ? 1.14425 1.25420 1.10280 0.09398  0.04781  0.07888  294 ARG B NE  
7814 C  CZ  . ARG B  294 ? 1.14972 1.26146 1.10790 0.09566  0.04897  0.07942  294 ARG B CZ  
7815 N  NH1 . ARG B  294 ? 1.07799 1.18735 1.02694 0.10279  0.04827  0.07679  294 ARG B NH1 
7816 N  NH2 . ARG B  294 ? 1.16265 1.27867 1.12990 0.09023  0.05075  0.08255  294 ARG B NH2 
7830 N  N   . GLN B  295 ? 0.31135 0.39347 0.27511 0.07323  0.02771  0.05245  295 GLN B N   
7831 C  CA  . GLN B  295 ? 0.28951 0.36993 0.25996 0.06582  0.02556  0.05095  295 GLN B CA  
7832 C  C   . GLN B  295 ? 0.28814 0.36133 0.25508 0.06535  0.02073  0.04393  295 GLN B C   
7833 O  O   . GLN B  295 ? 0.29072 0.36210 0.26278 0.05938  0.01863  0.04219  295 GLN B O   
7834 C  CB  . GLN B  295 ? 0.28180 0.36418 0.26117 0.05911  0.02603  0.05220  295 GLN B CB  
7835 C  CG  . GLN B  295 ? 0.30185 0.39184 0.28684 0.05814  0.03049  0.05924  295 GLN B CG  
7836 C  CD  . GLN B  295 ? 0.34973 0.44187 0.34380 0.05151  0.03063  0.06019  295 GLN B CD  
7837 O  OE1 . GLN B  295 ? 0.40618 0.49493 0.40057 0.04980  0.02853  0.05642  295 GLN B OE1 
7838 N  NE2 . GLN B  295 ? 0.34647 0.44412 0.34807 0.04784  0.03297  0.06515  295 GLN B NE2 
7847 N  N   . ILE B  296 ? 0.28312 0.35213 0.24191 0.07132  0.01872  0.03966  296 ILE B N   
7848 C  CA  . ILE B  296 ? 0.28506 0.34715 0.24073 0.07124  0.01390  0.03266  296 ILE B CA  
7849 C  C   . ILE B  296 ? 0.29728 0.35841 0.24488 0.07771  0.01318  0.03149  296 ILE B C   
7850 O  O   . ILE B  296 ? 0.30405 0.36569 0.24416 0.08524  0.01415  0.03173  296 ILE B O   
7851 C  CB  . ILE B  296 ? 0.27639 0.33346 0.23007 0.07236  0.01127  0.02759  296 ILE B CB  
7852 C  CG1 . ILE B  296 ? 0.30384 0.36204 0.26550 0.06604  0.01214  0.02896  296 ILE B CG1 
7853 C  CG2 . ILE B  296 ? 0.30153 0.35170 0.25189 0.07310  0.00632  0.02045  296 ILE B CG2 
7854 C  CD1 . ILE B  296 ? 0.36665 0.42061 0.32711 0.06697  0.01040  0.02515  296 ILE B CD1 
7866 N  N   . SER B  297 ? 0.27614 0.33579 0.22488 0.07512  0.01135  0.03003  297 SER B N   
7867 C  CA  . SER B  297 ? 0.28995 0.34851 0.23120 0.08099  0.01038  0.02859  297 SER B CA  
7868 C  C   . SER B  297 ? 0.26697 0.31860 0.20355 0.08303  0.00507  0.02053  297 SER B C   
7869 O  O   . SER B  297 ? 0.30784 0.35819 0.23674 0.08947  0.00387  0.01846  297 SER B O   
7870 C  CB  . SER B  297 ? 0.33688 0.39830 0.28139 0.07793  0.01180  0.03217  297 SER B CB  
7871 O  OG  . SER B  297 ? 0.34320 0.40307 0.29583 0.06942  0.00989  0.03069  297 SER B OG  
7877 N  N   . GLU B  298 ? 0.28725 0.33450 0.22831 0.07804  0.00189  0.01597  298 GLU B N   
7878 C  CA  . GLU B  298 ? 0.28263 0.32327 0.22009 0.08001  -0.00315 0.00829  298 GLU B CA  
7879 C  C   . GLU B  298 ? 0.29368 0.33074 0.23673 0.07507  -0.00505 0.00524  298 GLU B C   
7880 O  O   . GLU B  298 ? 0.27320 0.31203 0.22407 0.06815  -0.00372 0.00781  298 GLU B O   
7881 C  CB  . GLU B  298 ? 0.27944 0.31749 0.21739 0.07782  -0.00635 0.00478  298 GLU B CB  
7882 C  CG  . GLU B  298 ? 0.29195 0.32363 0.22521 0.08142  -0.01155 -0.00318 298 GLU B CG  
7883 C  CD  . GLU B  298 ? 0.35719 0.38606 0.29092 0.07948  -0.01517 -0.00736 298 GLU B CD  
7884 O  OE1 . GLU B  298 ? 0.35857 0.38999 0.29632 0.07494  -0.01388 -0.00438 298 GLU B OE1 
7885 O  OE2 . GLU B  298 ? 0.37977 0.40369 0.30998 0.08261  -0.01954 -0.01397 298 GLU B OE2 
7892 N  N   . HIS B  299 ? 0.28518 0.31727 0.22429 0.07881  -0.00813 -0.00014 299 HIS B N   
7893 C  CA  . HIS B  299 ? 0.27747 0.30509 0.22165 0.07449  -0.01051 -0.00386 299 HIS B CA  
7894 C  C   . HIS B  299 ? 0.28021 0.30108 0.22218 0.07614  -0.01594 -0.01165 299 HIS B C   
7895 O  O   . HIS B  299 ? 0.32261 0.34170 0.25696 0.08316  -0.01779 -0.01475 299 HIS B O   
7896 C  CB  . HIS B  299 ? 0.27900 0.30705 0.22185 0.07710  -0.00860 -0.00238 299 HIS B CB  
7897 C  CG  . HIS B  299 ? 0.26938 0.29236 0.21685 0.07344  -0.01104 -0.00631 299 HIS B CG  
7898 N  ND1 . HIS B  299 ? 0.31857 0.33577 0.26222 0.07758  -0.01444 -0.01199 299 HIS B ND1 
7899 C  CD2 . HIS B  299 ? 0.27302 0.29575 0.22878 0.06614  -0.01061 -0.00536 299 HIS B CD2 
7900 C  CE1 . HIS B  299 ? 0.28200 0.29561 0.23167 0.07283  -0.01573 -0.01402 299 HIS B CE1 
7901 N  NE2 . HIS B  299 ? 0.29553 0.31246 0.25235 0.06602  -0.01341 -0.01007 299 HIS B NE2 
7909 N  N   . ARG B  300 ? 0.26859 0.28586 0.21750 0.06972  -0.01853 -0.01482 300 ARG B N   
7910 C  CA  . ARG B  300 ? 0.26801 0.27860 0.21657 0.07055  -0.02366 -0.02224 300 ARG B CA  
7911 C  C   . ARG B  300 ? 0.25829 0.26560 0.21389 0.06539  -0.02439 -0.02361 300 ARG B C   
7912 O  O   . ARG B  300 ? 0.25797 0.26812 0.21983 0.05957  -0.02170 -0.01946 300 ARG B O   
7913 C  CB  . ARG B  300 ? 0.28532 0.29449 0.23621 0.06740  -0.02661 -0.02525 300 ARG B CB  
7914 C  CG  . ARG B  300 ? 0.29779 0.31078 0.24352 0.07067  -0.02538 -0.02294 300 ARG B CG  
7915 C  CD  . ARG B  300 ? 0.30317 0.31510 0.25224 0.06647  -0.02795 -0.02535 300 ARG B CD  
7916 N  NE  . ARG B  300 ? 0.31081 0.32710 0.25590 0.06871  -0.02582 -0.02172 300 ARG B NE  
7917 C  CZ  . ARG B  300 ? 0.28863 0.30618 0.23694 0.06445  -0.02617 -0.02099 300 ARG B CZ  
7918 N  NH1 . ARG B  300 ? 0.30855 0.32318 0.26328 0.05843  -0.02909 -0.02439 300 ARG B NH1 
7919 N  NH2 . ARG B  300 ? 0.35250 0.37435 0.29760 0.06639  -0.02346 -0.01664 300 ARG B NH2 
7933 N  N   . SER B  301 ? 0.27287 0.27409 0.22777 0.06745  -0.02820 -0.02955 301 SER B N   
7934 C  CA  . SER B  301 ? 0.25454 0.25207 0.21681 0.06224  -0.02917 -0.03114 301 SER B CA  
7935 C  C   . SER B  301 ? 0.30013 0.29048 0.26225 0.06429  -0.03428 -0.03857 301 SER B C   
7936 O  O   . SER B  301 ? 0.32554 0.31384 0.28105 0.07057  -0.03701 -0.04256 301 SER B O   
7937 C  CB  . SER B  301 ? 0.28531 0.28457 0.24809 0.06248  -0.02565 -0.02715 301 SER B CB  
7938 O  OG  . SER B  301 ? 0.32905 0.32503 0.28570 0.06922  -0.02702 -0.03013 301 SER B OG  
7944 N  N   . THR B  302 ? 0.27241 0.25898 0.24228 0.05894  -0.03564 -0.04045 302 THR B N   
7945 C  CA  . THR B  302 ? 0.28737 0.26682 0.25869 0.06031  -0.04015 -0.04706 302 THR B CA  
7946 C  C   . THR B  302 ? 0.31845 0.29544 0.28936 0.06232  -0.03899 -0.04659 302 THR B C   
7947 O  O   . THR B  302 ? 0.35748 0.32870 0.33277 0.06103  -0.04166 -0.05057 302 THR B O   
7948 C  CB  . THR B  302 ? 0.29159 0.26797 0.27205 0.05347  -0.04268 -0.04980 302 THR B CB  
7949 O  OG1 . THR B  302 ? 0.27893 0.25803 0.26604 0.04713  -0.03907 -0.04470 302 THR B OG1 
7950 C  CG2 . THR B  302 ? 0.28255 0.26047 0.26231 0.05273  -0.04465 -0.05147 302 THR B CG2 
7958 N  N   . CYS B  303 ? 0.31468 0.29590 0.28035 0.06577  -0.03515 -0.04192 303 CYS B N   
7959 C  CA  . CYS B  303 ? 0.34831 0.32734 0.31205 0.06890  -0.03421 -0.04174 303 CYS B CA  
7960 C  C   . CYS B  303 ? 0.36360 0.33645 0.32254 0.07521  -0.03884 -0.04853 303 CYS B C   
7961 O  O   . CYS B  303 ? 0.40021 0.37277 0.35371 0.07973  -0.04147 -0.05179 303 CYS B O   
7962 C  CB  . CYS B  303 ? 0.31353 0.29866 0.27110 0.07284  -0.02967 -0.03599 303 CYS B CB  
7963 S  SG  . CYS B  303 ? 0.33948 0.33171 0.30265 0.06635  -0.02412 -0.02799 303 CYS B SG  
7968 N  N   . PRO B  304 ? 0.40878 0.37670 0.36927 0.07610  -0.03988 -0.05072 304 PRO B N   
7969 C  CA  . PRO B  304 ? 0.43416 0.40168 0.40074 0.07146  -0.03707 -0.04740 304 PRO B CA  
7970 C  C   . PRO B  304 ? 0.49258 0.45737 0.46940 0.06370  -0.03840 -0.04862 304 PRO B C   
7971 O  O   . PRO B  304 ? 0.53721 0.49756 0.51656 0.06312  -0.04280 -0.05410 304 PRO B O   
7972 C  CB  . PRO B  304 ? 0.59757 0.55963 0.56086 0.07668  -0.03886 -0.05079 304 PRO B CB  
7973 C  CG  . PRO B  304 ? 0.54289 0.50026 0.50241 0.08151  -0.04423 -0.05779 304 PRO B CG  
7974 C  CD  . PRO B  304 ? 0.51478 0.47718 0.46959 0.08323  -0.04402 -0.05681 304 PRO B CD  
7982 N  N   . PHE B  305 ? 0.46851 0.43619 0.45109 0.05811  -0.03471 -0.04364 305 PHE B N   
7983 C  CA  . PHE B  305 ? 0.58769 0.55355 0.57997 0.05080  -0.03538 -0.04398 305 PHE B CA  
7984 C  C   . PHE B  305 ? 0.79834 0.75733 0.79566 0.04990  -0.03711 -0.04699 305 PHE B C   
7985 O  O   . PHE B  305 ? 0.90013 0.85851 0.89630 0.05152  -0.03486 -0.04487 305 PHE B O   
7986 C  CB  . PHE B  305 ? 0.49930 0.47129 0.49549 0.04559  -0.03069 -0.03733 305 PHE B CB  
7987 C  CG  . PHE B  305 ? 0.39497 0.37381 0.38741 0.04581  -0.02867 -0.03380 305 PHE B CG  
7988 C  CD1 . PHE B  305 ? 0.36695 0.34593 0.35684 0.04703  -0.03137 -0.03667 305 PHE B CD1 
7989 C  CD2 . PHE B  305 ? 0.31706 0.30210 0.30897 0.04470  -0.02415 -0.02767 305 PHE B CD2 
7990 C  CE1 . PHE B  305 ? 0.30784 0.29301 0.29455 0.04719  -0.02925 -0.03306 305 PHE B CE1 
7991 C  CE2 . PHE B  305 ? 0.34423 0.33541 0.33336 0.04480  -0.02226 -0.02428 305 PHE B CE2 
7992 C  CZ  . PHE B  305 ? 0.31061 0.30163 0.29713 0.04603  -0.02481 -0.02698 305 PHE B CZ  
8002 N  N   . VAL B  306 ? 0.83139 0.78531 0.83475 0.04715  -0.04100 -0.05174 306 VAL B N   
8003 C  CA  . VAL B  306 ? 0.85494 0.80201 0.86429 0.04586  -0.04277 -0.05462 306 VAL B CA  
8004 C  C   . VAL B  306 ? 0.95122 0.89991 0.96596 0.04145  -0.03842 -0.04921 306 VAL B C   
8005 O  O   . VAL B  306 ? 0.84341 0.79723 0.86144 0.03679  -0.03546 -0.04473 306 VAL B O   
8006 C  CB  . VAL B  306 ? 0.85282 0.79538 0.86926 0.04256  -0.04723 -0.05980 306 VAL B CB  
8007 C  CG1 . VAL B  306 ? 0.87015 0.80593 0.89453 0.04024  -0.04860 -0.06200 306 VAL B CG1 
8008 C  CG2 . VAL B  306 ? 0.76514 0.70556 0.77583 0.04779  -0.05196 -0.06582 306 VAL B CG2 
8018 N  N   . ASP B  307 ? 1.04714 0.99139 1.06257 0.04322  -0.03809 -0.04972 307 ASP B N   
8019 C  CA  . ASP B  307 ? 0.86461 0.80966 0.88491 0.03975  -0.03413 -0.04499 307 ASP B CA  
8020 C  C   . ASP B  307 ? 0.86487 0.80806 0.89580 0.03300  -0.03447 -0.04485 307 ASP B C   
8021 O  O   . ASP B  307 ? 0.92534 0.86324 0.96109 0.03184  -0.03839 -0.04968 307 ASP B O   
8022 C  CB  . ASP B  307 ? 0.88814 0.82789 0.90673 0.04359  -0.03424 -0.04627 307 ASP B CB  
8023 C  CG  . ASP B  307 ? 1.01773 0.96024 1.03742 0.04219  -0.02929 -0.04046 307 ASP B CG  
8024 O  OD1 . ASP B  307 ? 1.01783 0.96629 1.03136 0.04449  -0.02610 -0.03650 307 ASP B OD1 
8025 O  OD2 . ASP B  307 ? 1.08188 1.02075 1.10873 0.03890  -0.02853 -0.03977 307 ASP B OD2 
8191 CL CL  . CL  T  .   ? 0.29541 0.42059 0.20724 0.05747  -0.01083 -0.04646 418 CL  A CL  
8192 CL CL  . CL  U  .   ? 0.24504 0.32420 0.42092 0.05760  0.06400  -0.04988 419 CL  A CL  
8285 CL CL  . CL  GA .   ? 0.55336 0.42841 0.55393 0.04489  0.00166  0.15260  412 CL  B CL  
# 
