data_9EVI
# 
_entry.id   9EVI 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9EVI         pdb_00009evi 10.2210/pdb9evi/pdb 
WWPDB D_1292136991 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-09 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9EVI 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-30 
_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                 3 
_pdbx_contact_author.email              lloyd.ruddock@oulu.fi 
_pdbx_contact_author.name_first         Lloyd 
_pdbx_contact_author.name_last          Ruddock 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6247-686X 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Sohail, A.A.'  1 0000-0002-6137-1011 
'Ruddock, L.W.' 2 0000-0002-6247-686X 
# 
_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                     'Crystal structure of candida antarctica lipase B with the putative pro-peptide region' 
_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 'Sohail, A.A.'  1 ? 
primary 'Recacha, R.'   2 ? 
primary 'Ruddock, L.W.' 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 'Lipase B'              33808.191 2   3.1.1.3 ? ? ? 
2 non-polymer syn 'L(+)-TARTARIC ACID'    150.087   2   ?       ? ? ? 
3 non-polymer syn 'SODIUM ION'            22.990    2   ?       ? ? ? 
4 non-polymer syn 'DI(HYDROXYETHYL)ETHER' 106.120   1   ?       ? ? ? 
5 non-polymer syn 'TETRAETHYLENE GLYCOL'  194.226   1   ?       ? ? ? 
6 water       nat water                   18.015    845 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        CALB 
# 
_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       
;ATPLVKRLPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFML
NDTQVNTEYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPS
VWQQTTGSALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFS
YVVGRSALRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPYARPFAVGKRTCSG
IVTP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATPLVKRLPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFML
NDTQVNTEYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPS
VWQQTTGSALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFS
YVVGRSALRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPYARPFAVGKRTCSG
IVTP
;
_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 'L(+)-TARTARIC ACID'    TLA 
3 'SODIUM ION'            NA  
4 'DI(HYDROXYETHYL)ETHER' PEG 
5 'TETRAETHYLENE GLYCOL'  PG4 
6 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   PRO n 
1 4   LEU n 
1 5   VAL n 
1 6   LYS n 
1 7   ARG n 
1 8   LEU n 
1 9   PRO n 
1 10  SER n 
1 11  GLY n 
1 12  SER n 
1 13  ASP n 
1 14  PRO n 
1 15  ALA n 
1 16  PHE n 
1 17  SER n 
1 18  GLN n 
1 19  PRO n 
1 20  LYS n 
1 21  SER n 
1 22  VAL n 
1 23  LEU n 
1 24  ASP n 
1 25  ALA n 
1 26  GLY n 
1 27  LEU n 
1 28  THR n 
1 29  CYS n 
1 30  GLN n 
1 31  GLY n 
1 32  ALA n 
1 33  SER n 
1 34  PRO n 
1 35  SER n 
1 36  SER n 
1 37  VAL n 
1 38  SER n 
1 39  LYS n 
1 40  PRO n 
1 41  ILE n 
1 42  LEU n 
1 43  LEU n 
1 44  VAL n 
1 45  PRO n 
1 46  GLY n 
1 47  THR n 
1 48  GLY n 
1 49  THR n 
1 50  THR n 
1 51  GLY n 
1 52  PRO n 
1 53  GLN n 
1 54  SER n 
1 55  PHE n 
1 56  ASP n 
1 57  SER n 
1 58  ASN n 
1 59  TRP n 
1 60  ILE n 
1 61  PRO n 
1 62  LEU n 
1 63  SER n 
1 64  THR n 
1 65  GLN n 
1 66  LEU n 
1 67  GLY n 
1 68  TYR n 
1 69  THR n 
1 70  PRO n 
1 71  CYS n 
1 72  TRP n 
1 73  ILE n 
1 74  SER n 
1 75  PRO n 
1 76  PRO n 
1 77  PRO n 
1 78  PHE n 
1 79  MET n 
1 80  LEU n 
1 81  ASN n 
1 82  ASP n 
1 83  THR n 
1 84  GLN n 
1 85  VAL n 
1 86  ASN n 
1 87  THR n 
1 88  GLU n 
1 89  TYR n 
1 90  MET n 
1 91  VAL n 
1 92  ASN n 
1 93  ALA n 
1 94  ILE n 
1 95  THR n 
1 96  ALA n 
1 97  LEU n 
1 98  TYR n 
1 99  ALA n 
1 100 GLY n 
1 101 SER n 
1 102 GLY n 
1 103 ASN n 
1 104 ASN n 
1 105 LYS n 
1 106 LEU n 
1 107 PRO n 
1 108 VAL n 
1 109 LEU n 
1 110 THR n 
1 111 TRP n 
1 112 SER n 
1 113 GLN n 
1 114 GLY n 
1 115 GLY n 
1 116 LEU n 
1 117 VAL n 
1 118 ALA n 
1 119 GLN n 
1 120 TRP n 
1 121 GLY n 
1 122 LEU n 
1 123 THR n 
1 124 PHE n 
1 125 PHE n 
1 126 PRO n 
1 127 SER n 
1 128 ILE n 
1 129 ARG n 
1 130 SER n 
1 131 LYS n 
1 132 VAL n 
1 133 ASP n 
1 134 ARG n 
1 135 LEU n 
1 136 MET n 
1 137 ALA n 
1 138 PHE n 
1 139 ALA n 
1 140 PRO n 
1 141 ASP n 
1 142 TYR n 
1 143 LYS n 
1 144 GLY n 
1 145 THR n 
1 146 VAL n 
1 147 LEU n 
1 148 ALA n 
1 149 GLY n 
1 150 PRO n 
1 151 LEU n 
1 152 ASP n 
1 153 ALA n 
1 154 LEU n 
1 155 ALA n 
1 156 VAL n 
1 157 SER n 
1 158 ALA n 
1 159 PRO n 
1 160 SER n 
1 161 VAL n 
1 162 TRP n 
1 163 GLN n 
1 164 GLN n 
1 165 THR n 
1 166 THR n 
1 167 GLY n 
1 168 SER n 
1 169 ALA n 
1 170 LEU n 
1 171 THR n 
1 172 THR n 
1 173 ALA n 
1 174 LEU n 
1 175 ARG n 
1 176 ASN n 
1 177 ALA n 
1 178 GLY n 
1 179 GLY n 
1 180 LEU n 
1 181 THR n 
1 182 GLN n 
1 183 ILE n 
1 184 VAL n 
1 185 PRO n 
1 186 THR n 
1 187 THR n 
1 188 ASN n 
1 189 LEU n 
1 190 TYR n 
1 191 SER n 
1 192 ALA n 
1 193 THR n 
1 194 ASP n 
1 195 GLU n 
1 196 ILE n 
1 197 VAL n 
1 198 GLN n 
1 199 PRO n 
1 200 GLN n 
1 201 VAL n 
1 202 SER n 
1 203 ASN n 
1 204 SER n 
1 205 PRO n 
1 206 LEU n 
1 207 ASP n 
1 208 SER n 
1 209 SER n 
1 210 TYR n 
1 211 LEU n 
1 212 PHE n 
1 213 ASN n 
1 214 GLY n 
1 215 LYS n 
1 216 ASN n 
1 217 VAL n 
1 218 GLN n 
1 219 ALA n 
1 220 GLN n 
1 221 ALA n 
1 222 VAL n 
1 223 CYS n 
1 224 GLY n 
1 225 PRO n 
1 226 LEU n 
1 227 PHE n 
1 228 VAL n 
1 229 ILE n 
1 230 ASP n 
1 231 HIS n 
1 232 ALA n 
1 233 GLY n 
1 234 SER n 
1 235 LEU n 
1 236 THR n 
1 237 SER n 
1 238 GLN n 
1 239 PHE n 
1 240 SER n 
1 241 TYR n 
1 242 VAL n 
1 243 VAL n 
1 244 GLY n 
1 245 ARG n 
1 246 SER n 
1 247 ALA n 
1 248 LEU n 
1 249 ARG n 
1 250 SER n 
1 251 THR n 
1 252 THR n 
1 253 GLY n 
1 254 GLN n 
1 255 ALA n 
1 256 ARG n 
1 257 SER n 
1 258 ALA n 
1 259 ASP n 
1 260 TYR n 
1 261 GLY n 
1 262 ILE n 
1 263 THR n 
1 264 ASP n 
1 265 CYS n 
1 266 ASN n 
1 267 PRO n 
1 268 LEU n 
1 269 PRO n 
1 270 ALA n 
1 271 ASN n 
1 272 ASP n 
1 273 LEU n 
1 274 THR n 
1 275 PRO n 
1 276 GLU n 
1 277 GLN n 
1 278 LYS n 
1 279 VAL n 
1 280 ALA n 
1 281 ALA n 
1 282 ALA n 
1 283 ALA n 
1 284 LEU n 
1 285 LEU n 
1 286 ALA n 
1 287 PRO n 
1 288 ALA n 
1 289 ALA n 
1 290 ALA n 
1 291 ALA n 
1 292 ILE n 
1 293 VAL n 
1 294 ALA n 
1 295 GLY n 
1 296 PRO n 
1 297 LYS n 
1 298 GLN n 
1 299 ASN n 
1 300 CYS n 
1 301 GLU n 
1 302 PRO n 
1 303 ASP n 
1 304 LEU n 
1 305 MET n 
1 306 PRO n 
1 307 TYR n 
1 308 ALA n 
1 309 ARG n 
1 310 PRO n 
1 311 PHE n 
1 312 ALA n 
1 313 VAL n 
1 314 GLY n 
1 315 LYS n 
1 316 ARG n 
1 317 THR n 
1 318 CYS n 
1 319 SER n 
1 320 GLY n 
1 321 ILE n 
1 322 VAL n 
1 323 THR n 
1 324 PRO 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                   324 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Moesziomyces antarcticus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     84753 
_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 B' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     37762 
_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 
CYS 'L-peptide linking' y CYSTEINE                ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE               ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'         ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                 ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE               ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                   ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE              ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                 ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                  ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ? 'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'            ? 'Na 1'           22.990  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'      106.120 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'  ? 'C8 H18 O5'      194.226 
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 
TLA non-polymer         . 'L(+)-TARTARIC ACID'    ? 'C4 H6 O6'       150.087 
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   ALA 1   19  19  ALA ALA A . n 
A 1 2   THR 2   20  20  THR THR A . n 
A 1 3   PRO 3   21  21  PRO PRO A . n 
A 1 4   LEU 4   22  22  LEU LEU A . n 
A 1 5   VAL 5   23  23  VAL VAL A . n 
A 1 6   LYS 6   24  24  LYS LYS A . n 
A 1 7   ARG 7   25  25  ARG ARG A . n 
A 1 8   LEU 8   26  26  LEU LEU A . n 
A 1 9   PRO 9   27  27  PRO PRO A . n 
A 1 10  SER 10  28  28  SER SER A . n 
A 1 11  GLY 11  29  29  GLY GLY A . n 
A 1 12  SER 12  30  30  SER SER A . n 
A 1 13  ASP 13  31  31  ASP ASP A . n 
A 1 14  PRO 14  32  32  PRO PRO A . n 
A 1 15  ALA 15  33  33  ALA ALA A . n 
A 1 16  PHE 16  34  34  PHE PHE A . n 
A 1 17  SER 17  35  35  SER SER A . n 
A 1 18  GLN 18  36  36  GLN GLN A . n 
A 1 19  PRO 19  37  37  PRO PRO A . n 
A 1 20  LYS 20  38  38  LYS LYS A . n 
A 1 21  SER 21  39  39  SER SER A . n 
A 1 22  VAL 22  40  40  VAL VAL A . n 
A 1 23  LEU 23  41  41  LEU LEU A . n 
A 1 24  ASP 24  42  42  ASP ASP A . n 
A 1 25  ALA 25  43  43  ALA ALA A . n 
A 1 26  GLY 26  44  44  GLY GLY A . n 
A 1 27  LEU 27  45  45  LEU LEU A . n 
A 1 28  THR 28  46  46  THR THR A . n 
A 1 29  CYS 29  47  47  CYS CYS A . n 
A 1 30  GLN 30  48  48  GLN GLN A . n 
A 1 31  GLY 31  49  49  GLY GLY A . n 
A 1 32  ALA 32  50  50  ALA ALA A . n 
A 1 33  SER 33  51  51  SER SER A . n 
A 1 34  PRO 34  52  52  PRO PRO A . n 
A 1 35  SER 35  53  53  SER SER A . n 
A 1 36  SER 36  54  54  SER SER A . n 
A 1 37  VAL 37  55  55  VAL VAL A . n 
A 1 38  SER 38  56  56  SER SER A . n 
A 1 39  LYS 39  57  57  LYS LYS A . n 
A 1 40  PRO 40  58  58  PRO PRO A . n 
A 1 41  ILE 41  59  59  ILE ILE A . n 
A 1 42  LEU 42  60  60  LEU LEU A . n 
A 1 43  LEU 43  61  61  LEU LEU A . n 
A 1 44  VAL 44  62  62  VAL VAL A . n 
A 1 45  PRO 45  63  63  PRO PRO A . n 
A 1 46  GLY 46  64  64  GLY GLY A . n 
A 1 47  THR 47  65  65  THR THR A . n 
A 1 48  GLY 48  66  66  GLY GLY A . n 
A 1 49  THR 49  67  67  THR THR A . n 
A 1 50  THR 50  68  68  THR THR A . n 
A 1 51  GLY 51  69  69  GLY GLY A . n 
A 1 52  PRO 52  70  70  PRO PRO A . n 
A 1 53  GLN 53  71  71  GLN GLN A . n 
A 1 54  SER 54  72  72  SER SER A . n 
A 1 55  PHE 55  73  73  PHE PHE A . n 
A 1 56  ASP 56  74  74  ASP ASP A . n 
A 1 57  SER 57  75  75  SER SER A . n 
A 1 58  ASN 58  76  76  ASN ASN A . n 
A 1 59  TRP 59  77  77  TRP TRP A . n 
A 1 60  ILE 60  78  78  ILE ILE A . n 
A 1 61  PRO 61  79  79  PRO PRO A . n 
A 1 62  LEU 62  80  80  LEU LEU A . n 
A 1 63  SER 63  81  81  SER SER A . n 
A 1 64  THR 64  82  82  THR THR A . n 
A 1 65  GLN 65  83  83  GLN GLN A . n 
A 1 66  LEU 66  84  84  LEU LEU A . n 
A 1 67  GLY 67  85  85  GLY GLY A . n 
A 1 68  TYR 68  86  86  TYR TYR A . n 
A 1 69  THR 69  87  87  THR THR A . n 
A 1 70  PRO 70  88  88  PRO PRO A . n 
A 1 71  CYS 71  89  89  CYS CYS A . n 
A 1 72  TRP 72  90  90  TRP TRP A . n 
A 1 73  ILE 73  91  91  ILE ILE A . n 
A 1 74  SER 74  92  92  SER SER A . n 
A 1 75  PRO 75  93  93  PRO PRO A . n 
A 1 76  PRO 76  94  94  PRO PRO A . n 
A 1 77  PRO 77  95  95  PRO PRO A . n 
A 1 78  PHE 78  96  96  PHE PHE A . n 
A 1 79  MET 79  97  97  MET MET A . n 
A 1 80  LEU 80  98  98  LEU LEU A . n 
A 1 81  ASN 81  99  99  ASN ASN A . n 
A 1 82  ASP 82  100 100 ASP ASP A . n 
A 1 83  THR 83  101 101 THR THR A . n 
A 1 84  GLN 84  102 102 GLN GLN A . n 
A 1 85  VAL 85  103 103 VAL VAL A . n 
A 1 86  ASN 86  104 104 ASN ASN A . n 
A 1 87  THR 87  105 105 THR THR A . n 
A 1 88  GLU 88  106 106 GLU GLU A . n 
A 1 89  TYR 89  107 107 TYR TYR A . n 
A 1 90  MET 90  108 108 MET MET A . n 
A 1 91  VAL 91  109 109 VAL VAL A . n 
A 1 92  ASN 92  110 110 ASN ASN A . n 
A 1 93  ALA 93  111 111 ALA ALA A . n 
A 1 94  ILE 94  112 112 ILE ILE A . n 
A 1 95  THR 95  113 113 THR THR A . n 
A 1 96  ALA 96  114 114 ALA ALA A . n 
A 1 97  LEU 97  115 115 LEU LEU A . n 
A 1 98  TYR 98  116 116 TYR TYR A . n 
A 1 99  ALA 99  117 117 ALA ALA A . n 
A 1 100 GLY 100 118 118 GLY GLY A . n 
A 1 101 SER 101 119 119 SER SER A . n 
A 1 102 GLY 102 120 120 GLY GLY A . n 
A 1 103 ASN 103 121 121 ASN ASN A . n 
A 1 104 ASN 104 122 122 ASN ASN A . n 
A 1 105 LYS 105 123 123 LYS LYS A . n 
A 1 106 LEU 106 124 124 LEU LEU A . n 
A 1 107 PRO 107 125 125 PRO PRO A . n 
A 1 108 VAL 108 126 126 VAL VAL A . n 
A 1 109 LEU 109 127 127 LEU LEU A . n 
A 1 110 THR 110 128 128 THR THR A . n 
A 1 111 TRP 111 129 129 TRP TRP A . n 
A 1 112 SER 112 130 130 SER SER A . n 
A 1 113 GLN 113 131 131 GLN GLN A . n 
A 1 114 GLY 114 132 132 GLY GLY A . n 
A 1 115 GLY 115 133 133 GLY GLY A . n 
A 1 116 LEU 116 134 134 LEU LEU A . n 
A 1 117 VAL 117 135 135 VAL VAL A . n 
A 1 118 ALA 118 136 136 ALA ALA A . n 
A 1 119 GLN 119 137 137 GLN GLN A . n 
A 1 120 TRP 120 138 138 TRP TRP A . n 
A 1 121 GLY 121 139 139 GLY GLY A . n 
A 1 122 LEU 122 140 140 LEU LEU A . n 
A 1 123 THR 123 141 141 THR THR A . n 
A 1 124 PHE 124 142 142 PHE PHE A . n 
A 1 125 PHE 125 143 143 PHE PHE A . n 
A 1 126 PRO 126 144 144 PRO PRO A . n 
A 1 127 SER 127 145 145 SER SER A . n 
A 1 128 ILE 128 146 146 ILE ILE A . n 
A 1 129 ARG 129 147 147 ARG ARG A . n 
A 1 130 SER 130 148 148 SER SER A . n 
A 1 131 LYS 131 149 149 LYS LYS A . n 
A 1 132 VAL 132 150 150 VAL VAL A . n 
A 1 133 ASP 133 151 151 ASP ASP A . n 
A 1 134 ARG 134 152 152 ARG ARG A . n 
A 1 135 LEU 135 153 153 LEU LEU A . n 
A 1 136 MET 136 154 154 MET MET A . n 
A 1 137 ALA 137 155 155 ALA ALA A . n 
A 1 138 PHE 138 156 156 PHE PHE A . n 
A 1 139 ALA 139 157 157 ALA ALA A . n 
A 1 140 PRO 140 158 158 PRO PRO A . n 
A 1 141 ASP 141 159 159 ASP ASP A . n 
A 1 142 TYR 142 160 160 TYR TYR A . n 
A 1 143 LYS 143 161 161 LYS LYS A . n 
A 1 144 GLY 144 162 162 GLY GLY A . n 
A 1 145 THR 145 163 163 THR THR A . n 
A 1 146 VAL 146 164 164 VAL VAL A . n 
A 1 147 LEU 147 165 165 LEU LEU A . n 
A 1 148 ALA 148 166 166 ALA ALA A . n 
A 1 149 GLY 149 167 167 GLY GLY A . n 
A 1 150 PRO 150 168 168 PRO PRO A . n 
A 1 151 LEU 151 169 169 LEU LEU A . n 
A 1 152 ASP 152 170 170 ASP ASP A . n 
A 1 153 ALA 153 171 171 ALA ALA A . n 
A 1 154 LEU 154 172 172 LEU LEU A . n 
A 1 155 ALA 155 173 173 ALA ALA A . n 
A 1 156 VAL 156 174 174 VAL VAL A . n 
A 1 157 SER 157 175 175 SER SER A . n 
A 1 158 ALA 158 176 176 ALA ALA A . n 
A 1 159 PRO 159 177 177 PRO PRO A . n 
A 1 160 SER 160 178 178 SER SER A . n 
A 1 161 VAL 161 179 179 VAL VAL A . n 
A 1 162 TRP 162 180 180 TRP TRP A . n 
A 1 163 GLN 163 181 181 GLN GLN A . n 
A 1 164 GLN 164 182 182 GLN GLN A . n 
A 1 165 THR 165 183 183 THR THR A . n 
A 1 166 THR 166 184 184 THR THR A . n 
A 1 167 GLY 167 185 185 GLY GLY A . n 
A 1 168 SER 168 186 186 SER SER A . n 
A 1 169 ALA 169 187 187 ALA ALA A . n 
A 1 170 LEU 170 188 188 LEU LEU A . n 
A 1 171 THR 171 189 189 THR THR A . n 
A 1 172 THR 172 190 190 THR THR A . n 
A 1 173 ALA 173 191 191 ALA ALA A . n 
A 1 174 LEU 174 192 192 LEU LEU A . n 
A 1 175 ARG 175 193 193 ARG ARG A . n 
A 1 176 ASN 176 194 194 ASN ASN A . n 
A 1 177 ALA 177 195 195 ALA ALA A . n 
A 1 178 GLY 178 196 196 GLY GLY A . n 
A 1 179 GLY 179 197 197 GLY GLY A . n 
A 1 180 LEU 180 198 198 LEU LEU A . n 
A 1 181 THR 181 199 199 THR THR A . n 
A 1 182 GLN 182 200 200 GLN GLN A . n 
A 1 183 ILE 183 201 201 ILE ILE A . n 
A 1 184 VAL 184 202 202 VAL VAL A . n 
A 1 185 PRO 185 203 203 PRO PRO A . n 
A 1 186 THR 186 204 204 THR THR A . n 
A 1 187 THR 187 205 205 THR THR A . n 
A 1 188 ASN 188 206 206 ASN ASN A . n 
A 1 189 LEU 189 207 207 LEU LEU A . n 
A 1 190 TYR 190 208 208 TYR TYR A . n 
A 1 191 SER 191 209 209 SER SER A . n 
A 1 192 ALA 192 210 210 ALA ALA A . n 
A 1 193 THR 193 211 211 THR THR A . n 
A 1 194 ASP 194 212 212 ASP ASP A . n 
A 1 195 GLU 195 213 213 GLU GLU A . n 
A 1 196 ILE 196 214 214 ILE ILE A . n 
A 1 197 VAL 197 215 215 VAL VAL A . n 
A 1 198 GLN 198 216 216 GLN GLN A . n 
A 1 199 PRO 199 217 217 PRO PRO A . n 
A 1 200 GLN 200 218 218 GLN GLN A . n 
A 1 201 VAL 201 219 219 VAL VAL A . n 
A 1 202 SER 202 220 220 SER SER A . n 
A 1 203 ASN 203 221 221 ASN ASN A . n 
A 1 204 SER 204 222 222 SER SER A . n 
A 1 205 PRO 205 223 223 PRO PRO A . n 
A 1 206 LEU 206 224 224 LEU LEU A . n 
A 1 207 ASP 207 225 225 ASP ASP A . n 
A 1 208 SER 208 226 226 SER SER A . n 
A 1 209 SER 209 227 227 SER SER A . n 
A 1 210 TYR 210 228 228 TYR TYR A . n 
A 1 211 LEU 211 229 229 LEU LEU A . n 
A 1 212 PHE 212 230 230 PHE PHE A . n 
A 1 213 ASN 213 231 231 ASN ASN A . n 
A 1 214 GLY 214 232 232 GLY GLY A . n 
A 1 215 LYS 215 233 233 LYS LYS A . n 
A 1 216 ASN 216 234 234 ASN ASN A . n 
A 1 217 VAL 217 235 235 VAL VAL A . n 
A 1 218 GLN 218 236 236 GLN GLN A . n 
A 1 219 ALA 219 237 237 ALA ALA A . n 
A 1 220 GLN 220 238 238 GLN GLN A . n 
A 1 221 ALA 221 239 239 ALA ALA A . n 
A 1 222 VAL 222 240 240 VAL VAL A . n 
A 1 223 CYS 223 241 241 CYS CYS A . n 
A 1 224 GLY 224 242 242 GLY GLY A . n 
A 1 225 PRO 225 243 243 PRO PRO A . n 
A 1 226 LEU 226 244 244 LEU LEU A . n 
A 1 227 PHE 227 245 245 PHE PHE A . n 
A 1 228 VAL 228 246 246 VAL VAL A . n 
A 1 229 ILE 229 247 247 ILE ILE A . n 
A 1 230 ASP 230 248 248 ASP ASP A . n 
A 1 231 HIS 231 249 249 HIS HIS A . n 
A 1 232 ALA 232 250 250 ALA ALA A . n 
A 1 233 GLY 233 251 251 GLY GLY A . n 
A 1 234 SER 234 252 252 SER SER A . n 
A 1 235 LEU 235 253 253 LEU LEU A . n 
A 1 236 THR 236 254 254 THR THR A . n 
A 1 237 SER 237 255 255 SER SER A . n 
A 1 238 GLN 238 256 256 GLN GLN A . n 
A 1 239 PHE 239 257 257 PHE PHE A . n 
A 1 240 SER 240 258 258 SER SER A . n 
A 1 241 TYR 241 259 259 TYR TYR A . n 
A 1 242 VAL 242 260 260 VAL VAL A . n 
A 1 243 VAL 243 261 261 VAL VAL A . n 
A 1 244 GLY 244 262 262 GLY GLY A . n 
A 1 245 ARG 245 263 263 ARG ARG A . n 
A 1 246 SER 246 264 264 SER SER A . n 
A 1 247 ALA 247 265 265 ALA ALA A . n 
A 1 248 LEU 248 266 266 LEU LEU A . n 
A 1 249 ARG 249 267 267 ARG ARG A . n 
A 1 250 SER 250 268 268 SER SER A . n 
A 1 251 THR 251 269 269 THR THR A . n 
A 1 252 THR 252 270 270 THR THR A . n 
A 1 253 GLY 253 271 271 GLY GLY A . n 
A 1 254 GLN 254 272 272 GLN GLN A . n 
A 1 255 ALA 255 273 273 ALA ALA A . n 
A 1 256 ARG 256 274 274 ARG ARG A . n 
A 1 257 SER 257 275 275 SER SER A . n 
A 1 258 ALA 258 276 276 ALA ALA A . n 
A 1 259 ASP 259 277 277 ASP ASP A . n 
A 1 260 TYR 260 278 278 TYR TYR A . n 
A 1 261 GLY 261 279 279 GLY GLY A . n 
A 1 262 ILE 262 280 280 ILE ILE A . n 
A 1 263 THR 263 281 281 THR THR A . n 
A 1 264 ASP 264 282 282 ASP ASP A . n 
A 1 265 CYS 265 283 283 CYS CYS A . n 
A 1 266 ASN 266 284 284 ASN ASN A . n 
A 1 267 PRO 267 285 285 PRO PRO A . n 
A 1 268 LEU 268 286 286 LEU LEU A . n 
A 1 269 PRO 269 287 287 PRO PRO A . n 
A 1 270 ALA 270 288 288 ALA ALA A . n 
A 1 271 ASN 271 289 289 ASN ASN A . n 
A 1 272 ASP 272 290 290 ASP ASP A . n 
A 1 273 LEU 273 291 291 LEU LEU A . n 
A 1 274 THR 274 292 292 THR THR A . n 
A 1 275 PRO 275 293 293 PRO PRO A . n 
A 1 276 GLU 276 294 294 GLU GLU A . n 
A 1 277 GLN 277 295 295 GLN GLN A . n 
A 1 278 LYS 278 296 296 LYS LYS A . n 
A 1 279 VAL 279 297 297 VAL VAL A . n 
A 1 280 ALA 280 298 298 ALA ALA A . n 
A 1 281 ALA 281 299 299 ALA ALA A . n 
A 1 282 ALA 282 300 300 ALA ALA A . n 
A 1 283 ALA 283 301 301 ALA ALA A . n 
A 1 284 LEU 284 302 302 LEU LEU A . n 
A 1 285 LEU 285 303 303 LEU LEU A . n 
A 1 286 ALA 286 304 304 ALA ALA A . n 
A 1 287 PRO 287 305 305 PRO PRO A . n 
A 1 288 ALA 288 306 306 ALA ALA A . n 
A 1 289 ALA 289 307 307 ALA ALA A . n 
A 1 290 ALA 290 308 308 ALA ALA A . n 
A 1 291 ALA 291 309 309 ALA ALA A . n 
A 1 292 ILE 292 310 310 ILE ILE A . n 
A 1 293 VAL 293 311 311 VAL VAL A . n 
A 1 294 ALA 294 312 312 ALA ALA A . n 
A 1 295 GLY 295 313 313 GLY GLY A . n 
A 1 296 PRO 296 314 314 PRO PRO A . n 
A 1 297 LYS 297 315 315 LYS LYS A . n 
A 1 298 GLN 298 316 316 GLN GLN A . n 
A 1 299 ASN 299 317 317 ASN ASN A . n 
A 1 300 CYS 300 318 318 CYS CYS A . n 
A 1 301 GLU 301 319 319 GLU GLU A . n 
A 1 302 PRO 302 320 320 PRO PRO A . n 
A 1 303 ASP 303 321 321 ASP ASP A . n 
A 1 304 LEU 304 322 322 LEU LEU A . n 
A 1 305 MET 305 323 323 MET MET A . n 
A 1 306 PRO 306 324 324 PRO PRO A . n 
A 1 307 TYR 307 325 325 TYR TYR A . n 
A 1 308 ALA 308 326 326 ALA ALA A . n 
A 1 309 ARG 309 327 327 ARG ARG A . n 
A 1 310 PRO 310 328 328 PRO PRO A . n 
A 1 311 PHE 311 329 329 PHE PHE A . n 
A 1 312 ALA 312 330 330 ALA ALA A . n 
A 1 313 VAL 313 331 331 VAL VAL A . n 
A 1 314 GLY 314 332 332 GLY GLY A . n 
A 1 315 LYS 315 333 333 LYS LYS A . n 
A 1 316 ARG 316 334 334 ARG ARG A . n 
A 1 317 THR 317 335 335 THR THR A . n 
A 1 318 CYS 318 336 336 CYS CYS A . n 
A 1 319 SER 319 337 337 SER SER A . n 
A 1 320 GLY 320 338 338 GLY GLY A . n 
A 1 321 ILE 321 339 339 ILE ILE A . n 
A 1 322 VAL 322 340 340 VAL VAL A . n 
A 1 323 THR 323 341 341 THR THR A . n 
A 1 324 PRO 324 342 342 PRO PRO A . n 
B 1 1   ALA 1   19  ?   ?   ?   B . n 
B 1 2   THR 2   20  ?   ?   ?   B . n 
B 1 3   PRO 3   21  ?   ?   ?   B . n 
B 1 4   LEU 4   22  ?   ?   ?   B . n 
B 1 5   VAL 5   23  ?   ?   ?   B . n 
B 1 6   LYS 6   24  ?   ?   ?   B . n 
B 1 7   ARG 7   25  ?   ?   ?   B . n 
B 1 8   LEU 8   26  26  LEU LEU B . n 
B 1 9   PRO 9   27  27  PRO PRO B . n 
B 1 10  SER 10  28  28  SER SER B . n 
B 1 11  GLY 11  29  29  GLY GLY B . n 
B 1 12  SER 12  30  30  SER SER B . n 
B 1 13  ASP 13  31  31  ASP ASP B . n 
B 1 14  PRO 14  32  32  PRO PRO B . n 
B 1 15  ALA 15  33  33  ALA ALA B . n 
B 1 16  PHE 16  34  34  PHE PHE B . n 
B 1 17  SER 17  35  35  SER SER B . n 
B 1 18  GLN 18  36  36  GLN GLN B . n 
B 1 19  PRO 19  37  37  PRO PRO B . n 
B 1 20  LYS 20  38  38  LYS LYS B . n 
B 1 21  SER 21  39  39  SER SER B . n 
B 1 22  VAL 22  40  40  VAL VAL B . n 
B 1 23  LEU 23  41  41  LEU LEU B . n 
B 1 24  ASP 24  42  42  ASP ASP B . n 
B 1 25  ALA 25  43  43  ALA ALA B . n 
B 1 26  GLY 26  44  44  GLY GLY B . n 
B 1 27  LEU 27  45  45  LEU LEU B . n 
B 1 28  THR 28  46  46  THR THR B . n 
B 1 29  CYS 29  47  47  CYS CYS B . n 
B 1 30  GLN 30  48  48  GLN GLN B . n 
B 1 31  GLY 31  49  49  GLY GLY B . n 
B 1 32  ALA 32  50  50  ALA ALA B . n 
B 1 33  SER 33  51  51  SER SER B . n 
B 1 34  PRO 34  52  52  PRO PRO B . n 
B 1 35  SER 35  53  53  SER SER B . n 
B 1 36  SER 36  54  54  SER SER B . n 
B 1 37  VAL 37  55  55  VAL VAL B . n 
B 1 38  SER 38  56  56  SER SER B . n 
B 1 39  LYS 39  57  57  LYS LYS B . n 
B 1 40  PRO 40  58  58  PRO PRO B . n 
B 1 41  ILE 41  59  59  ILE ILE B . n 
B 1 42  LEU 42  60  60  LEU LEU B . n 
B 1 43  LEU 43  61  61  LEU LEU B . n 
B 1 44  VAL 44  62  62  VAL VAL B . n 
B 1 45  PRO 45  63  63  PRO PRO B . n 
B 1 46  GLY 46  64  64  GLY GLY B . n 
B 1 47  THR 47  65  65  THR THR B . n 
B 1 48  GLY 48  66  66  GLY GLY B . n 
B 1 49  THR 49  67  67  THR THR B . n 
B 1 50  THR 50  68  68  THR THR B . n 
B 1 51  GLY 51  69  69  GLY GLY B . n 
B 1 52  PRO 52  70  70  PRO PRO B . n 
B 1 53  GLN 53  71  71  GLN GLN B . n 
B 1 54  SER 54  72  72  SER SER B . n 
B 1 55  PHE 55  73  73  PHE PHE B . n 
B 1 56  ASP 56  74  74  ASP ASP B . n 
B 1 57  SER 57  75  75  SER SER B . n 
B 1 58  ASN 58  76  76  ASN ASN B . n 
B 1 59  TRP 59  77  77  TRP TRP B . n 
B 1 60  ILE 60  78  78  ILE ILE B . n 
B 1 61  PRO 61  79  79  PRO PRO B . n 
B 1 62  LEU 62  80  80  LEU LEU B . n 
B 1 63  SER 63  81  81  SER SER B . n 
B 1 64  THR 64  82  82  THR THR B . n 
B 1 65  GLN 65  83  83  GLN GLN B . n 
B 1 66  LEU 66  84  84  LEU LEU B . n 
B 1 67  GLY 67  85  85  GLY GLY B . n 
B 1 68  TYR 68  86  86  TYR TYR B . n 
B 1 69  THR 69  87  87  THR THR B . n 
B 1 70  PRO 70  88  88  PRO PRO B . n 
B 1 71  CYS 71  89  89  CYS CYS B . n 
B 1 72  TRP 72  90  90  TRP TRP B . n 
B 1 73  ILE 73  91  91  ILE ILE B . n 
B 1 74  SER 74  92  92  SER SER B . n 
B 1 75  PRO 75  93  93  PRO PRO B . n 
B 1 76  PRO 76  94  94  PRO PRO B . n 
B 1 77  PRO 77  95  95  PRO PRO B . n 
B 1 78  PHE 78  96  96  PHE PHE B . n 
B 1 79  MET 79  97  97  MET MET B . n 
B 1 80  LEU 80  98  98  LEU LEU B . n 
B 1 81  ASN 81  99  99  ASN ASN B . n 
B 1 82  ASP 82  100 100 ASP ASP B . n 
B 1 83  THR 83  101 101 THR THR B . n 
B 1 84  GLN 84  102 102 GLN GLN B . n 
B 1 85  VAL 85  103 103 VAL VAL B . n 
B 1 86  ASN 86  104 104 ASN ASN B . n 
B 1 87  THR 87  105 105 THR THR B . n 
B 1 88  GLU 88  106 106 GLU GLU B . n 
B 1 89  TYR 89  107 107 TYR TYR B . n 
B 1 90  MET 90  108 108 MET MET B . n 
B 1 91  VAL 91  109 109 VAL VAL B . n 
B 1 92  ASN 92  110 110 ASN ASN B . n 
B 1 93  ALA 93  111 111 ALA ALA B . n 
B 1 94  ILE 94  112 112 ILE ILE B . n 
B 1 95  THR 95  113 113 THR THR B . n 
B 1 96  ALA 96  114 114 ALA ALA B . n 
B 1 97  LEU 97  115 115 LEU LEU B . n 
B 1 98  TYR 98  116 116 TYR TYR B . n 
B 1 99  ALA 99  117 117 ALA ALA B . n 
B 1 100 GLY 100 118 118 GLY GLY B . n 
B 1 101 SER 101 119 119 SER SER B . n 
B 1 102 GLY 102 120 120 GLY GLY B . n 
B 1 103 ASN 103 121 121 ASN ASN B . n 
B 1 104 ASN 104 122 122 ASN ASN B . n 
B 1 105 LYS 105 123 123 LYS LYS B . n 
B 1 106 LEU 106 124 124 LEU LEU B . n 
B 1 107 PRO 107 125 125 PRO PRO B . n 
B 1 108 VAL 108 126 126 VAL VAL B . n 
B 1 109 LEU 109 127 127 LEU LEU B . n 
B 1 110 THR 110 128 128 THR THR B . n 
B 1 111 TRP 111 129 129 TRP TRP B . n 
B 1 112 SER 112 130 130 SER SER B . n 
B 1 113 GLN 113 131 131 GLN GLN B . n 
B 1 114 GLY 114 132 132 GLY GLY B . n 
B 1 115 GLY 115 133 133 GLY GLY B . n 
B 1 116 LEU 116 134 134 LEU LEU B . n 
B 1 117 VAL 117 135 135 VAL VAL B . n 
B 1 118 ALA 118 136 136 ALA ALA B . n 
B 1 119 GLN 119 137 137 GLN GLN B . n 
B 1 120 TRP 120 138 138 TRP TRP B . n 
B 1 121 GLY 121 139 139 GLY GLY B . n 
B 1 122 LEU 122 140 140 LEU LEU B . n 
B 1 123 THR 123 141 141 THR THR B . n 
B 1 124 PHE 124 142 142 PHE PHE B . n 
B 1 125 PHE 125 143 143 PHE PHE B . n 
B 1 126 PRO 126 144 144 PRO PRO B . n 
B 1 127 SER 127 145 145 SER SER B . n 
B 1 128 ILE 128 146 146 ILE ILE B . n 
B 1 129 ARG 129 147 147 ARG ARG B . n 
B 1 130 SER 130 148 148 SER SER B . n 
B 1 131 LYS 131 149 149 LYS LYS B . n 
B 1 132 VAL 132 150 150 VAL VAL B . n 
B 1 133 ASP 133 151 151 ASP ASP B . n 
B 1 134 ARG 134 152 152 ARG ARG B . n 
B 1 135 LEU 135 153 153 LEU LEU B . n 
B 1 136 MET 136 154 154 MET MET B . n 
B 1 137 ALA 137 155 155 ALA ALA B . n 
B 1 138 PHE 138 156 156 PHE PHE B . n 
B 1 139 ALA 139 157 157 ALA ALA B . n 
B 1 140 PRO 140 158 158 PRO PRO B . n 
B 1 141 ASP 141 159 159 ASP ASP B . n 
B 1 142 TYR 142 160 160 TYR TYR B . n 
B 1 143 LYS 143 161 161 LYS LYS B . n 
B 1 144 GLY 144 162 162 GLY GLY B . n 
B 1 145 THR 145 163 163 THR THR B . n 
B 1 146 VAL 146 164 164 VAL VAL B . n 
B 1 147 LEU 147 165 165 LEU LEU B . n 
B 1 148 ALA 148 166 166 ALA ALA B . n 
B 1 149 GLY 149 167 167 GLY GLY B . n 
B 1 150 PRO 150 168 168 PRO PRO B . n 
B 1 151 LEU 151 169 169 LEU LEU B . n 
B 1 152 ASP 152 170 170 ASP ASP B . n 
B 1 153 ALA 153 171 171 ALA ALA B . n 
B 1 154 LEU 154 172 172 LEU LEU B . n 
B 1 155 ALA 155 173 173 ALA ALA B . n 
B 1 156 VAL 156 174 174 VAL VAL B . n 
B 1 157 SER 157 175 175 SER SER B . n 
B 1 158 ALA 158 176 176 ALA ALA B . n 
B 1 159 PRO 159 177 177 PRO PRO B . n 
B 1 160 SER 160 178 178 SER SER B . n 
B 1 161 VAL 161 179 179 VAL VAL B . n 
B 1 162 TRP 162 180 180 TRP TRP B . n 
B 1 163 GLN 163 181 181 GLN GLN B . n 
B 1 164 GLN 164 182 182 GLN GLN B . n 
B 1 165 THR 165 183 183 THR THR B . n 
B 1 166 THR 166 184 184 THR THR B . n 
B 1 167 GLY 167 185 185 GLY GLY B . n 
B 1 168 SER 168 186 186 SER SER B . n 
B 1 169 ALA 169 187 187 ALA ALA B . n 
B 1 170 LEU 170 188 188 LEU LEU B . n 
B 1 171 THR 171 189 189 THR THR B . n 
B 1 172 THR 172 190 190 THR THR B . n 
B 1 173 ALA 173 191 191 ALA ALA B . n 
B 1 174 LEU 174 192 192 LEU LEU B . n 
B 1 175 ARG 175 193 193 ARG ARG B . n 
B 1 176 ASN 176 194 194 ASN ASN B . n 
B 1 177 ALA 177 195 195 ALA ALA B . n 
B 1 178 GLY 178 196 196 GLY GLY B . n 
B 1 179 GLY 179 197 197 GLY GLY B . n 
B 1 180 LEU 180 198 198 LEU LEU B . n 
B 1 181 THR 181 199 199 THR THR B . n 
B 1 182 GLN 182 200 200 GLN GLN B . n 
B 1 183 ILE 183 201 201 ILE ILE B . n 
B 1 184 VAL 184 202 202 VAL VAL B . n 
B 1 185 PRO 185 203 203 PRO PRO B . n 
B 1 186 THR 186 204 204 THR THR B . n 
B 1 187 THR 187 205 205 THR THR B . n 
B 1 188 ASN 188 206 206 ASN ASN B . n 
B 1 189 LEU 189 207 207 LEU LEU B . n 
B 1 190 TYR 190 208 208 TYR TYR B . n 
B 1 191 SER 191 209 209 SER SER B . n 
B 1 192 ALA 192 210 210 ALA ALA B . n 
B 1 193 THR 193 211 211 THR THR B . n 
B 1 194 ASP 194 212 212 ASP ASP B . n 
B 1 195 GLU 195 213 213 GLU GLU B . n 
B 1 196 ILE 196 214 214 ILE ILE B . n 
B 1 197 VAL 197 215 215 VAL VAL B . n 
B 1 198 GLN 198 216 216 GLN GLN B . n 
B 1 199 PRO 199 217 217 PRO PRO B . n 
B 1 200 GLN 200 218 218 GLN GLN B . n 
B 1 201 VAL 201 219 219 VAL VAL B . n 
B 1 202 SER 202 220 220 SER SER B . n 
B 1 203 ASN 203 221 221 ASN ASN B . n 
B 1 204 SER 204 222 222 SER SER B . n 
B 1 205 PRO 205 223 223 PRO PRO B . n 
B 1 206 LEU 206 224 224 LEU LEU B . n 
B 1 207 ASP 207 225 225 ASP ASP B . n 
B 1 208 SER 208 226 226 SER SER B . n 
B 1 209 SER 209 227 227 SER SER B . n 
B 1 210 TYR 210 228 228 TYR TYR B . n 
B 1 211 LEU 211 229 229 LEU LEU B . n 
B 1 212 PHE 212 230 230 PHE PHE B . n 
B 1 213 ASN 213 231 231 ASN ASN B . n 
B 1 214 GLY 214 232 232 GLY GLY B . n 
B 1 215 LYS 215 233 233 LYS LYS B . n 
B 1 216 ASN 216 234 234 ASN ASN B . n 
B 1 217 VAL 217 235 235 VAL VAL B . n 
B 1 218 GLN 218 236 236 GLN GLN B . n 
B 1 219 ALA 219 237 237 ALA ALA B . n 
B 1 220 GLN 220 238 238 GLN GLN B . n 
B 1 221 ALA 221 239 239 ALA ALA B . n 
B 1 222 VAL 222 240 240 VAL VAL B . n 
B 1 223 CYS 223 241 241 CYS CYS B . n 
B 1 224 GLY 224 242 242 GLY GLY B . n 
B 1 225 PRO 225 243 243 PRO PRO B . n 
B 1 226 LEU 226 244 244 LEU LEU B . n 
B 1 227 PHE 227 245 245 PHE PHE B . n 
B 1 228 VAL 228 246 246 VAL VAL B . n 
B 1 229 ILE 229 247 247 ILE ILE B . n 
B 1 230 ASP 230 248 248 ASP ASP B . n 
B 1 231 HIS 231 249 249 HIS HIS B . n 
B 1 232 ALA 232 250 250 ALA ALA B . n 
B 1 233 GLY 233 251 251 GLY GLY B . n 
B 1 234 SER 234 252 252 SER SER B . n 
B 1 235 LEU 235 253 253 LEU LEU B . n 
B 1 236 THR 236 254 254 THR THR B . n 
B 1 237 SER 237 255 255 SER SER B . n 
B 1 238 GLN 238 256 256 GLN GLN B . n 
B 1 239 PHE 239 257 257 PHE PHE B . n 
B 1 240 SER 240 258 258 SER SER B . n 
B 1 241 TYR 241 259 259 TYR TYR B . n 
B 1 242 VAL 242 260 260 VAL VAL B . n 
B 1 243 VAL 243 261 261 VAL VAL B . n 
B 1 244 GLY 244 262 262 GLY GLY B . n 
B 1 245 ARG 245 263 263 ARG ARG B . n 
B 1 246 SER 246 264 264 SER SER B . n 
B 1 247 ALA 247 265 265 ALA ALA B . n 
B 1 248 LEU 248 266 266 LEU LEU B . n 
B 1 249 ARG 249 267 267 ARG ARG B . n 
B 1 250 SER 250 268 268 SER SER B . n 
B 1 251 THR 251 269 269 THR THR B . n 
B 1 252 THR 252 270 270 THR THR B . n 
B 1 253 GLY 253 271 271 GLY GLY B . n 
B 1 254 GLN 254 272 272 GLN GLN B . n 
B 1 255 ALA 255 273 273 ALA ALA B . n 
B 1 256 ARG 256 274 274 ARG ARG B . n 
B 1 257 SER 257 275 275 SER SER B . n 
B 1 258 ALA 258 276 276 ALA ALA B . n 
B 1 259 ASP 259 277 277 ASP ASP B . n 
B 1 260 TYR 260 278 278 TYR TYR B . n 
B 1 261 GLY 261 279 279 GLY GLY B . n 
B 1 262 ILE 262 280 280 ILE ILE B . n 
B 1 263 THR 263 281 281 THR THR B . n 
B 1 264 ASP 264 282 282 ASP ASP B . n 
B 1 265 CYS 265 283 283 CYS CYS B . n 
B 1 266 ASN 266 284 284 ASN ASN B . n 
B 1 267 PRO 267 285 285 PRO PRO B . n 
B 1 268 LEU 268 286 286 LEU LEU B . n 
B 1 269 PRO 269 287 287 PRO PRO B . n 
B 1 270 ALA 270 288 288 ALA ALA B . n 
B 1 271 ASN 271 289 289 ASN ASN B . n 
B 1 272 ASP 272 290 290 ASP ASP B . n 
B 1 273 LEU 273 291 291 LEU LEU B . n 
B 1 274 THR 274 292 292 THR THR B . n 
B 1 275 PRO 275 293 293 PRO PRO B . n 
B 1 276 GLU 276 294 294 GLU GLU B . n 
B 1 277 GLN 277 295 295 GLN GLN B . n 
B 1 278 LYS 278 296 296 LYS LYS B . n 
B 1 279 VAL 279 297 297 VAL VAL B . n 
B 1 280 ALA 280 298 298 ALA ALA B . n 
B 1 281 ALA 281 299 299 ALA ALA B . n 
B 1 282 ALA 282 300 300 ALA ALA B . n 
B 1 283 ALA 283 301 301 ALA ALA B . n 
B 1 284 LEU 284 302 302 LEU LEU B . n 
B 1 285 LEU 285 303 303 LEU LEU B . n 
B 1 286 ALA 286 304 304 ALA ALA B . n 
B 1 287 PRO 287 305 305 PRO PRO B . n 
B 1 288 ALA 288 306 306 ALA ALA B . n 
B 1 289 ALA 289 307 307 ALA ALA B . n 
B 1 290 ALA 290 308 308 ALA ALA B . n 
B 1 291 ALA 291 309 309 ALA ALA B . n 
B 1 292 ILE 292 310 310 ILE ILE B . n 
B 1 293 VAL 293 311 311 VAL VAL B . n 
B 1 294 ALA 294 312 312 ALA ALA B . n 
B 1 295 GLY 295 313 313 GLY GLY B . n 
B 1 296 PRO 296 314 314 PRO PRO B . n 
B 1 297 LYS 297 315 315 LYS LYS B . n 
B 1 298 GLN 298 316 316 GLN GLN B . n 
B 1 299 ASN 299 317 317 ASN ASN B . n 
B 1 300 CYS 300 318 318 CYS CYS B . n 
B 1 301 GLU 301 319 319 GLU GLU B . n 
B 1 302 PRO 302 320 320 PRO PRO B . n 
B 1 303 ASP 303 321 321 ASP ASP B . n 
B 1 304 LEU 304 322 322 LEU LEU B . n 
B 1 305 MET 305 323 323 MET MET B . n 
B 1 306 PRO 306 324 324 PRO PRO B . n 
B 1 307 TYR 307 325 325 TYR TYR B . n 
B 1 308 ALA 308 326 326 ALA ALA B . n 
B 1 309 ARG 309 327 327 ARG ARG B . n 
B 1 310 PRO 310 328 328 PRO PRO B . n 
B 1 311 PHE 311 329 329 PHE PHE B . n 
B 1 312 ALA 312 330 330 ALA ALA B . n 
B 1 313 VAL 313 331 331 VAL VAL B . n 
B 1 314 GLY 314 332 332 GLY GLY B . n 
B 1 315 LYS 315 333 333 LYS LYS B . n 
B 1 316 ARG 316 334 334 ARG ARG B . n 
B 1 317 THR 317 335 335 THR THR B . n 
B 1 318 CYS 318 336 336 CYS CYS B . n 
B 1 319 SER 319 337 337 SER SER B . n 
B 1 320 GLY 320 338 338 GLY GLY B . n 
B 1 321 ILE 321 339 339 ILE ILE B . n 
B 1 322 VAL 322 340 340 VAL VAL B . n 
B 1 323 THR 323 341 341 THR THR B . n 
B 1 324 PRO 324 342 342 PRO PRO B . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 NA  ? ? NA  ? ? 'SUBJECT OF INVESTIGATION' ? 
2 PEG ? ? PEG ? ? 'SUBJECT OF INVESTIGATION' ? 
3 PG4 ? ? PG4 ? ? 'SUBJECT OF INVESTIGATION' ? 
4 TLA ? ? TLA ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 TLA 1   401 401 TLA TLA A . 
D 3 NA  1   402 2   NA  NA  A . 
E 4 PEG 1   401 401 PEG PEG B . 
F 5 PG4 1   402 501 PG4 PG4 B . 
G 2 TLA 1   403 601 TLA TLA B . 
H 3 NA  1   404 1   NA  NA  B . 
I 6 HOH 1   501 94  HOH HOH A . 
I 6 HOH 2   502 406 HOH HOH A . 
I 6 HOH 3   503 305 HOH HOH A . 
I 6 HOH 4   504 698 HOH HOH A . 
I 6 HOH 5   505 614 HOH HOH A . 
I 6 HOH 6   506 846 HOH HOH A . 
I 6 HOH 7   507 336 HOH HOH A . 
I 6 HOH 8   508 856 HOH HOH A . 
I 6 HOH 9   509 284 HOH HOH A . 
I 6 HOH 10  510 386 HOH HOH A . 
I 6 HOH 11  511 292 HOH HOH A . 
I 6 HOH 12  512 874 HOH HOH A . 
I 6 HOH 13  513 621 HOH HOH A . 
I 6 HOH 14  514 505 HOH HOH A . 
I 6 HOH 15  515 215 HOH HOH A . 
I 6 HOH 16  516 691 HOH HOH A . 
I 6 HOH 17  517 757 HOH HOH A . 
I 6 HOH 18  518 91  HOH HOH A . 
I 6 HOH 19  519 32  HOH HOH A . 
I 6 HOH 20  520 151 HOH HOH A . 
I 6 HOH 21  521 340 HOH HOH A . 
I 6 HOH 22  522 92  HOH HOH A . 
I 6 HOH 23  523 667 HOH HOH A . 
I 6 HOH 24  524 62  HOH HOH A . 
I 6 HOH 25  525 548 HOH HOH A . 
I 6 HOH 26  526 177 HOH HOH A . 
I 6 HOH 27  527 478 HOH HOH A . 
I 6 HOH 28  528 265 HOH HOH A . 
I 6 HOH 29  529 207 HOH HOH A . 
I 6 HOH 30  530 343 HOH HOH A . 
I 6 HOH 31  531 68  HOH HOH A . 
I 6 HOH 32  532 23  HOH HOH A . 
I 6 HOH 33  533 124 HOH HOH A . 
I 6 HOH 34  534 380 HOH HOH A . 
I 6 HOH 35  535 419 HOH HOH A . 
I 6 HOH 36  536 349 HOH HOH A . 
I 6 HOH 37  537 138 HOH HOH A . 
I 6 HOH 38  538 154 HOH HOH A . 
I 6 HOH 39  539 291 HOH HOH A . 
I 6 HOH 40  540 119 HOH HOH A . 
I 6 HOH 41  541 166 HOH HOH A . 
I 6 HOH 42  542 147 HOH HOH A . 
I 6 HOH 43  543 743 HOH HOH A . 
I 6 HOH 44  544 572 HOH HOH A . 
I 6 HOH 45  545 115 HOH HOH A . 
I 6 HOH 46  546 18  HOH HOH A . 
I 6 HOH 47  547 399 HOH HOH A . 
I 6 HOH 48  548 212 HOH HOH A . 
I 6 HOH 49  549 43  HOH HOH A . 
I 6 HOH 50  550 673 HOH HOH A . 
I 6 HOH 51  551 80  HOH HOH A . 
I 6 HOH 52  552 558 HOH HOH A . 
I 6 HOH 53  553 218 HOH HOH A . 
I 6 HOH 54  554 729 HOH HOH A . 
I 6 HOH 55  555 496 HOH HOH A . 
I 6 HOH 56  556 59  HOH HOH A . 
I 6 HOH 57  557 503 HOH HOH A . 
I 6 HOH 58  558 253 HOH HOH A . 
I 6 HOH 59  559 169 HOH HOH A . 
I 6 HOH 60  560 443 HOH HOH A . 
I 6 HOH 61  561 161 HOH HOH A . 
I 6 HOH 62  562 172 HOH HOH A . 
I 6 HOH 63  563 657 HOH HOH A . 
I 6 HOH 64  564 195 HOH HOH A . 
I 6 HOH 65  565 4   HOH HOH A . 
I 6 HOH 66  566 289 HOH HOH A . 
I 6 HOH 67  567 845 HOH HOH A . 
I 6 HOH 68  568 297 HOH HOH A . 
I 6 HOH 69  569 457 HOH HOH A . 
I 6 HOH 70  570 687 HOH HOH A . 
I 6 HOH 71  571 12  HOH HOH A . 
I 6 HOH 72  572 613 HOH HOH A . 
I 6 HOH 73  573 7   HOH HOH A . 
I 6 HOH 74  574 8   HOH HOH A . 
I 6 HOH 75  575 699 HOH HOH A . 
I 6 HOH 76  576 654 HOH HOH A . 
I 6 HOH 77  577 514 HOH HOH A . 
I 6 HOH 78  578 516 HOH HOH A . 
I 6 HOH 79  579 296 HOH HOH A . 
I 6 HOH 80  580 519 HOH HOH A . 
I 6 HOH 81  581 619 HOH HOH A . 
I 6 HOH 82  582 639 HOH HOH A . 
I 6 HOH 83  583 665 HOH HOH A . 
I 6 HOH 84  584 88  HOH HOH A . 
I 6 HOH 85  585 306 HOH HOH A . 
I 6 HOH 86  586 55  HOH HOH A . 
I 6 HOH 87  587 508 HOH HOH A . 
I 6 HOH 88  588 256 HOH HOH A . 
I 6 HOH 89  589 141 HOH HOH A . 
I 6 HOH 90  590 40  HOH HOH A . 
I 6 HOH 91  591 150 HOH HOH A . 
I 6 HOH 92  592 199 HOH HOH A . 
I 6 HOH 93  593 47  HOH HOH A . 
I 6 HOH 94  594 72  HOH HOH A . 
I 6 HOH 95  595 61  HOH HOH A . 
I 6 HOH 96  596 146 HOH HOH A . 
I 6 HOH 97  597 553 HOH HOH A . 
I 6 HOH 98  598 656 HOH HOH A . 
I 6 HOH 99  599 193 HOH HOH A . 
I 6 HOH 100 600 19  HOH HOH A . 
I 6 HOH 101 601 839 HOH HOH A . 
I 6 HOH 102 602 233 HOH HOH A . 
I 6 HOH 103 603 252 HOH HOH A . 
I 6 HOH 104 604 31  HOH HOH A . 
I 6 HOH 105 605 56  HOH HOH A . 
I 6 HOH 106 606 57  HOH HOH A . 
I 6 HOH 107 607 248 HOH HOH A . 
I 6 HOH 108 608 110 HOH HOH A . 
I 6 HOH 109 609 267 HOH HOH A . 
I 6 HOH 110 610 144 HOH HOH A . 
I 6 HOH 111 611 601 HOH HOH A . 
I 6 HOH 112 612 748 HOH HOH A . 
I 6 HOH 113 613 229 HOH HOH A . 
I 6 HOH 114 614 432 HOH HOH A . 
I 6 HOH 115 615 268 HOH HOH A . 
I 6 HOH 116 616 299 HOH HOH A . 
I 6 HOH 117 617 170 HOH HOH A . 
I 6 HOH 118 618 107 HOH HOH A . 
I 6 HOH 119 619 287 HOH HOH A . 
I 6 HOH 120 620 105 HOH HOH A . 
I 6 HOH 121 621 298 HOH HOH A . 
I 6 HOH 122 622 86  HOH HOH A . 
I 6 HOH 123 623 77  HOH HOH A . 
I 6 HOH 124 624 2   HOH HOH A . 
I 6 HOH 125 625 210 HOH HOH A . 
I 6 HOH 126 626 559 HOH HOH A . 
I 6 HOH 127 627 328 HOH HOH A . 
I 6 HOH 128 628 371 HOH HOH A . 
I 6 HOH 129 629 143 HOH HOH A . 
I 6 HOH 130 630 774 HOH HOH A . 
I 6 HOH 131 631 715 HOH HOH A . 
I 6 HOH 132 632 696 HOH HOH A . 
I 6 HOH 133 633 30  HOH HOH A . 
I 6 HOH 134 634 389 HOH HOH A . 
I 6 HOH 135 635 176 HOH HOH A . 
I 6 HOH 136 636 3   HOH HOH A . 
I 6 HOH 137 637 219 HOH HOH A . 
I 6 HOH 138 638 106 HOH HOH A . 
I 6 HOH 139 639 97  HOH HOH A . 
I 6 HOH 140 640 436 HOH HOH A . 
I 6 HOH 141 641 324 HOH HOH A . 
I 6 HOH 142 642 785 HOH HOH A . 
I 6 HOH 143 643 66  HOH HOH A . 
I 6 HOH 144 644 524 HOH HOH A . 
I 6 HOH 145 645 132 HOH HOH A . 
I 6 HOH 146 646 35  HOH HOH A . 
I 6 HOH 147 647 27  HOH HOH A . 
I 6 HOH 148 648 485 HOH HOH A . 
I 6 HOH 149 649 310 HOH HOH A . 
I 6 HOH 150 650 11  HOH HOH A . 
I 6 HOH 151 651 93  HOH HOH A . 
I 6 HOH 152 652 203 HOH HOH A . 
I 6 HOH 153 653 750 HOH HOH A . 
I 6 HOH 154 654 158 HOH HOH A . 
I 6 HOH 155 655 728 HOH HOH A . 
I 6 HOH 156 656 74  HOH HOH A . 
I 6 HOH 157 657 49  HOH HOH A . 
I 6 HOH 158 658 749 HOH HOH A . 
I 6 HOH 159 659 116 HOH HOH A . 
I 6 HOH 160 660 28  HOH HOH A . 
I 6 HOH 161 661 513 HOH HOH A . 
I 6 HOH 162 662 338 HOH HOH A . 
I 6 HOH 163 663 798 HOH HOH A . 
I 6 HOH 164 664 647 HOH HOH A . 
I 6 HOH 165 665 1   HOH HOH A . 
I 6 HOH 166 666 65  HOH HOH A . 
I 6 HOH 167 667 123 HOH HOH A . 
I 6 HOH 168 668 781 HOH HOH A . 
I 6 HOH 169 669 331 HOH HOH A . 
I 6 HOH 170 670 196 HOH HOH A . 
I 6 HOH 171 671 347 HOH HOH A . 
I 6 HOH 172 672 408 HOH HOH A . 
I 6 HOH 173 673 5   HOH HOH A . 
I 6 HOH 174 674 14  HOH HOH A . 
I 6 HOH 175 675 108 HOH HOH A . 
I 6 HOH 176 676 782 HOH HOH A . 
I 6 HOH 177 677 742 HOH HOH A . 
I 6 HOH 178 678 483 HOH HOH A . 
I 6 HOH 179 679 99  HOH HOH A . 
I 6 HOH 180 680 221 HOH HOH A . 
I 6 HOH 181 681 682 HOH HOH A . 
I 6 HOH 182 682 262 HOH HOH A . 
I 6 HOH 183 683 164 HOH HOH A . 
I 6 HOH 184 684 51  HOH HOH A . 
I 6 HOH 185 685 314 HOH HOH A . 
I 6 HOH 186 686 300 HOH HOH A . 
I 6 HOH 187 687 37  HOH HOH A . 
I 6 HOH 188 688 191 HOH HOH A . 
I 6 HOH 189 689 84  HOH HOH A . 
I 6 HOH 190 690 320 HOH HOH A . 
I 6 HOH 191 691 186 HOH HOH A . 
I 6 HOH 192 692 640 HOH HOH A . 
I 6 HOH 193 693 83  HOH HOH A . 
I 6 HOH 194 694 626 HOH HOH A . 
I 6 HOH 195 695 16  HOH HOH A . 
I 6 HOH 196 696 204 HOH HOH A . 
I 6 HOH 197 697 36  HOH HOH A . 
I 6 HOH 198 698 366 HOH HOH A . 
I 6 HOH 199 699 121 HOH HOH A . 
I 6 HOH 200 700 489 HOH HOH A . 
I 6 HOH 201 701 788 HOH HOH A . 
I 6 HOH 202 702 357 HOH HOH A . 
I 6 HOH 203 703 608 HOH HOH A . 
I 6 HOH 204 704 465 HOH HOH A . 
I 6 HOH 205 705 474 HOH HOH A . 
I 6 HOH 206 706 772 HOH HOH A . 
I 6 HOH 207 707 184 HOH HOH A . 
I 6 HOH 208 708 565 HOH HOH A . 
I 6 HOH 209 709 447 HOH HOH A . 
I 6 HOH 210 710 29  HOH HOH A . 
I 6 HOH 211 711 381 HOH HOH A . 
I 6 HOH 212 712 481 HOH HOH A . 
I 6 HOH 213 713 137 HOH HOH A . 
I 6 HOH 214 714 201 HOH HOH A . 
I 6 HOH 215 715 75  HOH HOH A . 
I 6 HOH 216 716 459 HOH HOH A . 
I 6 HOH 217 717 622 HOH HOH A . 
I 6 HOH 218 718 400 HOH HOH A . 
I 6 HOH 219 719 103 HOH HOH A . 
I 6 HOH 220 720 803 HOH HOH A . 
I 6 HOH 221 721 570 HOH HOH A . 
I 6 HOH 222 722 272 HOH HOH A . 
I 6 HOH 223 723 692 HOH HOH A . 
I 6 HOH 224 724 865 HOH HOH A . 
I 6 HOH 225 725 10  HOH HOH A . 
I 6 HOH 226 726 425 HOH HOH A . 
I 6 HOH 227 727 162 HOH HOH A . 
I 6 HOH 228 728 396 HOH HOH A . 
I 6 HOH 229 729 135 HOH HOH A . 
I 6 HOH 230 730 247 HOH HOH A . 
I 6 HOH 231 731 670 HOH HOH A . 
I 6 HOH 232 732 598 HOH HOH A . 
I 6 HOH 233 733 33  HOH HOH A . 
I 6 HOH 234 734 374 HOH HOH A . 
I 6 HOH 235 735 495 HOH HOH A . 
I 6 HOH 236 736 251 HOH HOH A . 
I 6 HOH 237 737 804 HOH HOH A . 
I 6 HOH 238 738 87  HOH HOH A . 
I 6 HOH 239 739 627 HOH HOH A . 
I 6 HOH 240 740 245 HOH HOH A . 
I 6 HOH 241 741 468 HOH HOH A . 
I 6 HOH 242 742 64  HOH HOH A . 
I 6 HOH 243 743 616 HOH HOH A . 
I 6 HOH 244 744 430 HOH HOH A . 
I 6 HOH 245 745 254 HOH HOH A . 
I 6 HOH 246 746 429 HOH HOH A . 
I 6 HOH 247 747 165 HOH HOH A . 
I 6 HOH 248 748 587 HOH HOH A . 
I 6 HOH 249 749 82  HOH HOH A . 
I 6 HOH 250 750 838 HOH HOH A . 
I 6 HOH 251 751 249 HOH HOH A . 
I 6 HOH 252 752 160 HOH HOH A . 
I 6 HOH 253 753 69  HOH HOH A . 
I 6 HOH 254 754 826 HOH HOH A . 
I 6 HOH 255 755 605 HOH HOH A . 
I 6 HOH 256 756 588 HOH HOH A . 
I 6 HOH 257 757 681 HOH HOH A . 
I 6 HOH 258 758 829 HOH HOH A . 
I 6 HOH 259 759 718 HOH HOH A . 
I 6 HOH 260 760 523 HOH HOH A . 
I 6 HOH 261 761 854 HOH HOH A . 
I 6 HOH 262 762 285 HOH HOH A . 
I 6 HOH 263 763 111 HOH HOH A . 
I 6 HOH 264 764 658 HOH HOH A . 
I 6 HOH 265 765 723 HOH HOH A . 
I 6 HOH 266 766 136 HOH HOH A . 
I 6 HOH 267 767 393 HOH HOH A . 
I 6 HOH 268 768 650 HOH HOH A . 
I 6 HOH 269 769 226 HOH HOH A . 
I 6 HOH 270 770 274 HOH HOH A . 
I 6 HOH 271 771 599 HOH HOH A . 
I 6 HOH 272 772 482 HOH HOH A . 
I 6 HOH 273 773 563 HOH HOH A . 
I 6 HOH 274 774 418 HOH HOH A . 
I 6 HOH 275 775 789 HOH HOH A . 
I 6 HOH 276 776 712 HOH HOH A . 
I 6 HOH 277 777 373 HOH HOH A . 
I 6 HOH 278 778 168 HOH HOH A . 
I 6 HOH 279 779 720 HOH HOH A . 
I 6 HOH 280 780 693 HOH HOH A . 
I 6 HOH 281 781 475 HOH HOH A . 
I 6 HOH 282 782 753 HOH HOH A . 
I 6 HOH 283 783 624 HOH HOH A . 
I 6 HOH 284 784 351 HOH HOH A . 
I 6 HOH 285 785 359 HOH HOH A . 
I 6 HOH 286 786 585 HOH HOH A . 
I 6 HOH 287 787 471 HOH HOH A . 
I 6 HOH 288 788 817 HOH HOH A . 
I 6 HOH 289 789 235 HOH HOH A . 
I 6 HOH 290 790 597 HOH HOH A . 
I 6 HOH 291 791 303 HOH HOH A . 
I 6 HOH 292 792 522 HOH HOH A . 
I 6 HOH 293 793 355 HOH HOH A . 
I 6 HOH 294 794 678 HOH HOH A . 
I 6 HOH 295 795 222 HOH HOH A . 
I 6 HOH 296 796 155 HOH HOH A . 
I 6 HOH 297 797 858 HOH HOH A . 
I 6 HOH 298 798 581 HOH HOH A . 
I 6 HOH 299 799 377 HOH HOH A . 
I 6 HOH 300 800 382 HOH HOH A . 
I 6 HOH 301 801 569 HOH HOH A . 
I 6 HOH 302 802 456 HOH HOH A . 
I 6 HOH 303 803 350 HOH HOH A . 
I 6 HOH 304 804 554 HOH HOH A . 
I 6 HOH 305 805 469 HOH HOH A . 
I 6 HOH 306 806 244 HOH HOH A . 
I 6 HOH 307 807 362 HOH HOH A . 
I 6 HOH 308 808 224 HOH HOH A . 
I 6 HOH 309 809 664 HOH HOH A . 
I 6 HOH 310 810 500 HOH HOH A . 
I 6 HOH 311 811 638 HOH HOH A . 
I 6 HOH 312 812 450 HOH HOH A . 
I 6 HOH 313 813 578 HOH HOH A . 
I 6 HOH 314 814 704 HOH HOH A . 
I 6 HOH 315 815 480 HOH HOH A . 
I 6 HOH 316 816 449 HOH HOH A . 
I 6 HOH 317 817 793 HOH HOH A . 
I 6 HOH 318 818 717 HOH HOH A . 
I 6 HOH 319 819 811 HOH HOH A . 
I 6 HOH 320 820 595 HOH HOH A . 
I 6 HOH 321 821 768 HOH HOH A . 
I 6 HOH 322 822 307 HOH HOH A . 
I 6 HOH 323 823 507 HOH HOH A . 
I 6 HOH 324 824 407 HOH HOH A . 
I 6 HOH 325 825 412 HOH HOH A . 
I 6 HOH 326 826 584 HOH HOH A . 
I 6 HOH 327 827 214 HOH HOH A . 
I 6 HOH 328 828 518 HOH HOH A . 
I 6 HOH 329 829 531 HOH HOH A . 
I 6 HOH 330 830 416 HOH HOH A . 
I 6 HOH 331 831 801 HOH HOH A . 
I 6 HOH 332 832 701 HOH HOH A . 
I 6 HOH 333 833 528 HOH HOH A . 
I 6 HOH 334 834 596 HOH HOH A . 
I 6 HOH 335 835 744 HOH HOH A . 
I 6 HOH 336 836 467 HOH HOH A . 
I 6 HOH 337 837 302 HOH HOH A . 
I 6 HOH 338 838 390 HOH HOH A . 
I 6 HOH 339 839 376 HOH HOH A . 
I 6 HOH 340 840 690 HOH HOH A . 
I 6 HOH 341 841 867 HOH HOH A . 
I 6 HOH 342 842 112 HOH HOH A . 
I 6 HOH 343 843 675 HOH HOH A . 
I 6 HOH 344 844 240 HOH HOH A . 
I 6 HOH 345 845 859 HOH HOH A . 
I 6 HOH 346 846 494 HOH HOH A . 
I 6 HOH 347 847 738 HOH HOH A . 
I 6 HOH 348 848 573 HOH HOH A . 
I 6 HOH 349 849 372 HOH HOH A . 
I 6 HOH 350 850 220 HOH HOH A . 
I 6 HOH 351 851 63  HOH HOH A . 
I 6 HOH 352 852 669 HOH HOH A . 
I 6 HOH 353 853 117 HOH HOH A . 
I 6 HOH 354 854 325 HOH HOH A . 
I 6 HOH 355 855 645 HOH HOH A . 
I 6 HOH 356 856 504 HOH HOH A . 
I 6 HOH 357 857 403 HOH HOH A . 
I 6 HOH 358 858 118 HOH HOH A . 
I 6 HOH 359 859 361 HOH HOH A . 
I 6 HOH 360 860 319 HOH HOH A . 
I 6 HOH 361 861 617 HOH HOH A . 
I 6 HOH 362 862 527 HOH HOH A . 
I 6 HOH 363 863 414 HOH HOH A . 
I 6 HOH 364 864 871 HOH HOH A . 
I 6 HOH 365 865 671 HOH HOH A . 
I 6 HOH 366 866 455 HOH HOH A . 
I 6 HOH 367 867 741 HOH HOH A . 
I 6 HOH 368 868 490 HOH HOH A . 
I 6 HOH 369 869 413 HOH HOH A . 
I 6 HOH 370 870 716 HOH HOH A . 
I 6 HOH 371 871 590 HOH HOH A . 
I 6 HOH 372 872 863 HOH HOH A . 
I 6 HOH 373 873 790 HOH HOH A . 
I 6 HOH 374 874 872 HOH HOH A . 
I 6 HOH 375 875 223 HOH HOH A . 
I 6 HOH 376 876 125 HOH HOH A . 
I 6 HOH 377 877 568 HOH HOH A . 
I 6 HOH 378 878 363 HOH HOH A . 
I 6 HOH 379 879 844 HOH HOH A . 
I 6 HOH 380 880 401 HOH HOH A . 
I 6 HOH 381 881 360 HOH HOH A . 
I 6 HOH 382 882 686 HOH HOH A . 
I 6 HOH 383 883 797 HOH HOH A . 
I 6 HOH 384 884 703 HOH HOH A . 
I 6 HOH 385 885 589 HOH HOH A . 
I 6 HOH 386 886 321 HOH HOH A . 
I 6 HOH 387 887 463 HOH HOH A . 
I 6 HOH 388 888 239 HOH HOH A . 
I 6 HOH 389 889 660 HOH HOH A . 
I 6 HOH 390 890 421 HOH HOH A . 
I 6 HOH 391 891 713 HOH HOH A . 
I 6 HOH 392 892 828 HOH HOH A . 
I 6 HOH 393 893 348 HOH HOH A . 
I 6 HOH 394 894 228 HOH HOH A . 
I 6 HOH 395 895 618 HOH HOH A . 
I 6 HOH 396 896 659 HOH HOH A . 
I 6 HOH 397 897 823 HOH HOH A . 
I 6 HOH 398 898 775 HOH HOH A . 
I 6 HOH 399 899 777 HOH HOH A . 
I 6 HOH 400 900 759 HOH HOH A . 
I 6 HOH 401 901 724 HOH HOH A . 
I 6 HOH 402 902 737 HOH HOH A . 
I 6 HOH 403 903 761 HOH HOH A . 
I 6 HOH 404 904 571 HOH HOH A . 
I 6 HOH 405 905 173 HOH HOH A . 
I 6 HOH 406 906 462 HOH HOH A . 
I 6 HOH 407 907 427 HOH HOH A . 
I 6 HOH 408 908 809 HOH HOH A . 
I 6 HOH 409 909 487 HOH HOH A . 
I 6 HOH 410 910 437 HOH HOH A . 
I 6 HOH 411 911 702 HOH HOH A . 
I 6 HOH 412 912 825 HOH HOH A . 
I 6 HOH 413 913 444 HOH HOH A . 
I 6 HOH 414 914 545 HOH HOH A . 
I 6 HOH 415 915 506 HOH HOH A . 
I 6 HOH 416 916 441 HOH HOH A . 
I 6 HOH 417 917 747 HOH HOH A . 
I 6 HOH 418 918 661 HOH HOH A . 
I 6 HOH 419 919 556 HOH HOH A . 
I 6 HOH 420 920 820 HOH HOH A . 
I 6 HOH 421 921 685 HOH HOH A . 
I 6 HOH 422 922 707 HOH HOH A . 
I 6 HOH 423 923 783 HOH HOH A . 
I 6 HOH 424 924 868 HOH HOH A . 
J 6 HOH 1   501 250 HOH HOH B . 
J 6 HOH 2   502 566 HOH HOH B . 
J 6 HOH 3   503 603 HOH HOH B . 
J 6 HOH 4   504 502 HOH HOH B . 
J 6 HOH 5   505 326 HOH HOH B . 
J 6 HOH 6   506 722 HOH HOH B . 
J 6 HOH 7   507 282 HOH HOH B . 
J 6 HOH 8   508 615 HOH HOH B . 
J 6 HOH 9   509 643 HOH HOH B . 
J 6 HOH 10  510 301 HOH HOH B . 
J 6 HOH 11  511 334 HOH HOH B . 
J 6 HOH 12  512 180 HOH HOH B . 
J 6 HOH 13  513 375 HOH HOH B . 
J 6 HOH 14  514 754 HOH HOH B . 
J 6 HOH 15  515 791 HOH HOH B . 
J 6 HOH 16  516 241 HOH HOH B . 
J 6 HOH 17  517 479 HOH HOH B . 
J 6 HOH 18  518 171 HOH HOH B . 
J 6 HOH 19  519 322 HOH HOH B . 
J 6 HOH 20  520 628 HOH HOH B . 
J 6 HOH 21  521 313 HOH HOH B . 
J 6 HOH 22  522 364 HOH HOH B . 
J 6 HOH 23  523 345 HOH HOH B . 
J 6 HOH 24  524 607 HOH HOH B . 
J 6 HOH 25  525 90  HOH HOH B . 
J 6 HOH 26  526 246 HOH HOH B . 
J 6 HOH 27  527 493 HOH HOH B . 
J 6 HOH 28  528 258 HOH HOH B . 
J 6 HOH 29  529 264 HOH HOH B . 
J 6 HOH 30  530 813 HOH HOH B . 
J 6 HOH 31  531 50  HOH HOH B . 
J 6 HOH 32  532 384 HOH HOH B . 
J 6 HOH 33  533 15  HOH HOH B . 
J 6 HOH 34  534 542 HOH HOH B . 
J 6 HOH 35  535 316 HOH HOH B . 
J 6 HOH 36  536 354 HOH HOH B . 
J 6 HOH 37  537 205 HOH HOH B . 
J 6 HOH 38  538 609 HOH HOH B . 
J 6 HOH 39  539 433 HOH HOH B . 
J 6 HOH 40  540 567 HOH HOH B . 
J 6 HOH 41  541 85  HOH HOH B . 
J 6 HOH 42  542 25  HOH HOH B . 
J 6 HOH 43  543 153 HOH HOH B . 
J 6 HOH 44  544 428 HOH HOH B . 
J 6 HOH 45  545 48  HOH HOH B . 
J 6 HOH 46  546 129 HOH HOH B . 
J 6 HOH 47  547 197 HOH HOH B . 
J 6 HOH 48  548 192 HOH HOH B . 
J 6 HOH 49  549 532 HOH HOH B . 
J 6 HOH 50  550 847 HOH HOH B . 
J 6 HOH 51  551 711 HOH HOH B . 
J 6 HOH 52  552 353 HOH HOH B . 
J 6 HOH 53  553 234 HOH HOH B . 
J 6 HOH 54  554 635 HOH HOH B . 
J 6 HOH 55  555 163 HOH HOH B . 
J 6 HOH 56  556 271 HOH HOH B . 
J 6 HOH 57  557 178 HOH HOH B . 
J 6 HOH 58  558 53  HOH HOH B . 
J 6 HOH 59  559 288 HOH HOH B . 
J 6 HOH 60  560 128 HOH HOH B . 
J 6 HOH 61  561 730 HOH HOH B . 
J 6 HOH 62  562 122 HOH HOH B . 
J 6 HOH 63  563 520 HOH HOH B . 
J 6 HOH 64  564 546 HOH HOH B . 
J 6 HOH 65  565 225 HOH HOH B . 
J 6 HOH 66  566 45  HOH HOH B . 
J 6 HOH 67  567 259 HOH HOH B . 
J 6 HOH 68  568 283 HOH HOH B . 
J 6 HOH 69  569 70  HOH HOH B . 
J 6 HOH 70  570 58  HOH HOH B . 
J 6 HOH 71  571 98  HOH HOH B . 
J 6 HOH 72  572 857 HOH HOH B . 
J 6 HOH 73  573 42  HOH HOH B . 
J 6 HOH 74  574 290 HOH HOH B . 
J 6 HOH 75  575 367 HOH HOH B . 
J 6 HOH 76  576 574 HOH HOH B . 
J 6 HOH 77  577 206 HOH HOH B . 
J 6 HOH 78  578 323 HOH HOH B . 
J 6 HOH 79  579 89  HOH HOH B . 
J 6 HOH 80  580 663 HOH HOH B . 
J 6 HOH 81  581 227 HOH HOH B . 
J 6 HOH 82  582 9   HOH HOH B . 
J 6 HOH 83  583 24  HOH HOH B . 
J 6 HOH 84  584 187 HOH HOH B . 
J 6 HOH 85  585 862 HOH HOH B . 
J 6 HOH 86  586 52  HOH HOH B . 
J 6 HOH 87  587 488 HOH HOH B . 
J 6 HOH 88  588 818 HOH HOH B . 
J 6 HOH 89  589 332 HOH HOH B . 
J 6 HOH 90  590 356 HOH HOH B . 
J 6 HOH 91  591 95  HOH HOH B . 
J 6 HOH 92  592 655 HOH HOH B . 
J 6 HOH 93  593 636 HOH HOH B . 
J 6 HOH 94  594 293 HOH HOH B . 
J 6 HOH 95  595 438 HOH HOH B . 
J 6 HOH 96  596 333 HOH HOH B . 
J 6 HOH 97  597 853 HOH HOH B . 
J 6 HOH 98  598 79  HOH HOH B . 
J 6 HOH 99  599 458 HOH HOH B . 
J 6 HOH 100 600 208 HOH HOH B . 
J 6 HOH 101 601 39  HOH HOH B . 
J 6 HOH 102 602 392 HOH HOH B . 
J 6 HOH 103 603 71  HOH HOH B . 
J 6 HOH 104 604 21  HOH HOH B . 
J 6 HOH 105 605 807 HOH HOH B . 
J 6 HOH 106 606 544 HOH HOH B . 
J 6 HOH 107 607 44  HOH HOH B . 
J 6 HOH 108 608 335 HOH HOH B . 
J 6 HOH 109 609 344 HOH HOH B . 
J 6 HOH 110 610 870 HOH HOH B . 
J 6 HOH 111 611 109 HOH HOH B . 
J 6 HOH 112 612 529 HOH HOH B . 
J 6 HOH 113 613 266 HOH HOH B . 
J 6 HOH 114 614 126 HOH HOH B . 
J 6 HOH 115 615 175 HOH HOH B . 
J 6 HOH 116 616 368 HOH HOH B . 
J 6 HOH 117 617 67  HOH HOH B . 
J 6 HOH 118 618 20  HOH HOH B . 
J 6 HOH 119 619 41  HOH HOH B . 
J 6 HOH 120 620 113 HOH HOH B . 
J 6 HOH 121 621 46  HOH HOH B . 
J 6 HOH 122 622 133 HOH HOH B . 
J 6 HOH 123 623 530 HOH HOH B . 
J 6 HOH 124 624 100 HOH HOH B . 
J 6 HOH 125 625 535 HOH HOH B . 
J 6 HOH 126 626 497 HOH HOH B . 
J 6 HOH 127 627 832 HOH HOH B . 
J 6 HOH 128 628 592 HOH HOH B . 
J 6 HOH 129 629 54  HOH HOH B . 
J 6 HOH 130 630 159 HOH HOH B . 
J 6 HOH 131 631 260 HOH HOH B . 
J 6 HOH 132 632 139 HOH HOH B . 
J 6 HOH 133 633 22  HOH HOH B . 
J 6 HOH 134 634 200 HOH HOH B . 
J 6 HOH 135 635 6   HOH HOH B . 
J 6 HOH 136 636 308 HOH HOH B . 
J 6 HOH 137 637 539 HOH HOH B . 
J 6 HOH 138 638 796 HOH HOH B . 
J 6 HOH 139 639 824 HOH HOH B . 
J 6 HOH 140 640 134 HOH HOH B . 
J 6 HOH 141 641 148 HOH HOH B . 
J 6 HOH 142 642 800 HOH HOH B . 
J 6 HOH 143 643 440 HOH HOH B . 
J 6 HOH 144 644 426 HOH HOH B . 
J 6 HOH 145 645 140 HOH HOH B . 
J 6 HOH 146 646 179 HOH HOH B . 
J 6 HOH 147 647 156 HOH HOH B . 
J 6 HOH 148 648 17  HOH HOH B . 
J 6 HOH 149 649 806 HOH HOH B . 
J 6 HOH 150 650 257 HOH HOH B . 
J 6 HOH 151 651 152 HOH HOH B . 
J 6 HOH 152 652 710 HOH HOH B . 
J 6 HOH 153 653 352 HOH HOH B . 
J 6 HOH 154 654 550 HOH HOH B . 
J 6 HOH 155 655 26  HOH HOH B . 
J 6 HOH 156 656 541 HOH HOH B . 
J 6 HOH 157 657 837 HOH HOH B . 
J 6 HOH 158 658 537 HOH HOH B . 
J 6 HOH 159 659 387 HOH HOH B . 
J 6 HOH 160 660 446 HOH HOH B . 
J 6 HOH 161 661 60  HOH HOH B . 
J 6 HOH 162 662 395 HOH HOH B . 
J 6 HOH 163 663 714 HOH HOH B . 
J 6 HOH 164 664 327 HOH HOH B . 
J 6 HOH 165 665 312 HOH HOH B . 
J 6 HOH 166 666 725 HOH HOH B . 
J 6 HOH 167 667 286 HOH HOH B . 
J 6 HOH 168 668 649 HOH HOH B . 
J 6 HOH 169 669 130 HOH HOH B . 
J 6 HOH 170 670 758 HOH HOH B . 
J 6 HOH 171 671 78  HOH HOH B . 
J 6 HOH 172 672 114 HOH HOH B . 
J 6 HOH 173 673 860 HOH HOH B . 
J 6 HOH 174 674 648 HOH HOH B . 
J 6 HOH 175 675 840 HOH HOH B . 
J 6 HOH 176 676 142 HOH HOH B . 
J 6 HOH 177 677 460 HOH HOH B . 
J 6 HOH 178 678 339 HOH HOH B . 
J 6 HOH 179 679 827 HOH HOH B . 
J 6 HOH 180 680 557 HOH HOH B . 
J 6 HOH 181 681 515 HOH HOH B . 
J 6 HOH 182 682 379 HOH HOH B . 
J 6 HOH 183 683 358 HOH HOH B . 
J 6 HOH 184 684 183 HOH HOH B . 
J 6 HOH 185 685 538 HOH HOH B . 
J 6 HOH 186 686 799 HOH HOH B . 
J 6 HOH 187 687 378 HOH HOH B . 
J 6 HOH 188 688 814 HOH HOH B . 
J 6 HOH 189 689 341 HOH HOH B . 
J 6 HOH 190 690 473 HOH HOH B . 
J 6 HOH 191 691 317 HOH HOH B . 
J 6 HOH 192 692 76  HOH HOH B . 
J 6 HOH 193 693 120 HOH HOH B . 
J 6 HOH 194 694 13  HOH HOH B . 
J 6 HOH 195 695 762 HOH HOH B . 
J 6 HOH 196 696 733 HOH HOH B . 
J 6 HOH 197 697 674 HOH HOH B . 
J 6 HOH 198 698 689 HOH HOH B . 
J 6 HOH 199 699 492 HOH HOH B . 
J 6 HOH 200 700 182 HOH HOH B . 
J 6 HOH 201 701 543 HOH HOH B . 
J 6 HOH 202 702 562 HOH HOH B . 
J 6 HOH 203 703 394 HOH HOH B . 
J 6 HOH 204 704 295 HOH HOH B . 
J 6 HOH 205 705 167 HOH HOH B . 
J 6 HOH 206 706 773 HOH HOH B . 
J 6 HOH 207 707 564 HOH HOH B . 
J 6 HOH 208 708 231 HOH HOH B . 
J 6 HOH 209 709 727 HOH HOH B . 
J 6 HOH 210 710 431 HOH HOH B . 
J 6 HOH 211 711 810 HOH HOH B . 
J 6 HOH 212 712 409 HOH HOH B . 
J 6 HOH 213 713 261 HOH HOH B . 
J 6 HOH 214 714 194 HOH HOH B . 
J 6 HOH 215 715 708 HOH HOH B . 
J 6 HOH 216 716 104 HOH HOH B . 
J 6 HOH 217 717 209 HOH HOH B . 
J 6 HOH 218 718 217 HOH HOH B . 
J 6 HOH 219 719 96  HOH HOH B . 
J 6 HOH 220 720 270 HOH HOH B . 
J 6 HOH 221 721 415 HOH HOH B . 
J 6 HOH 222 722 633 HOH HOH B . 
J 6 HOH 223 723 576 HOH HOH B . 
J 6 HOH 224 724 73  HOH HOH B . 
J 6 HOH 225 725 794 HOH HOH B . 
J 6 HOH 226 726 329 HOH HOH B . 
J 6 HOH 227 727 243 HOH HOH B . 
J 6 HOH 228 728 695 HOH HOH B . 
J 6 HOH 229 729 81  HOH HOH B . 
J 6 HOH 230 730 101 HOH HOH B . 
J 6 HOH 231 731 346 HOH HOH B . 
J 6 HOH 232 732 273 HOH HOH B . 
J 6 HOH 233 733 230 HOH HOH B . 
J 6 HOH 234 734 676 HOH HOH B . 
J 6 HOH 235 735 102 HOH HOH B . 
J 6 HOH 236 736 652 HOH HOH B . 
J 6 HOH 237 737 501 HOH HOH B . 
J 6 HOH 238 738 555 HOH HOH B . 
J 6 HOH 239 739 631 HOH HOH B . 
J 6 HOH 240 740 499 HOH HOH B . 
J 6 HOH 241 741 586 HOH HOH B . 
J 6 HOH 242 742 263 HOH HOH B . 
J 6 HOH 243 743 697 HOH HOH B . 
J 6 HOH 244 744 745 HOH HOH B . 
J 6 HOH 245 745 668 HOH HOH B . 
J 6 HOH 246 746 719 HOH HOH B . 
J 6 HOH 247 747 547 HOH HOH B . 
J 6 HOH 248 748 127 HOH HOH B . 
J 6 HOH 249 749 269 HOH HOH B . 
J 6 HOH 250 750 202 HOH HOH B . 
J 6 HOH 251 751 149 HOH HOH B . 
J 6 HOH 252 752 281 HOH HOH B . 
J 6 HOH 253 753 278 HOH HOH B . 
J 6 HOH 254 754 642 HOH HOH B . 
J 6 HOH 255 755 34  HOH HOH B . 
J 6 HOH 256 756 776 HOH HOH B . 
J 6 HOH 257 757 816 HOH HOH B . 
J 6 HOH 258 758 498 HOH HOH B . 
J 6 HOH 259 759 591 HOH HOH B . 
J 6 HOH 260 760 579 HOH HOH B . 
J 6 HOH 261 761 604 HOH HOH B . 
J 6 HOH 262 762 190 HOH HOH B . 
J 6 HOH 263 763 448 HOH HOH B . 
J 6 HOH 264 764 756 HOH HOH B . 
J 6 HOH 265 765 330 HOH HOH B . 
J 6 HOH 266 766 705 HOH HOH B . 
J 6 HOH 267 767 700 HOH HOH B . 
J 6 HOH 268 768 683 HOH HOH B . 
J 6 HOH 269 769 466 HOH HOH B . 
J 6 HOH 270 770 181 HOH HOH B . 
J 6 HOH 271 771 145 HOH HOH B . 
J 6 HOH 272 772 521 HOH HOH B . 
J 6 HOH 273 773 769 HOH HOH B . 
J 6 HOH 274 774 611 HOH HOH B . 
J 6 HOH 275 775 484 HOH HOH B . 
J 6 HOH 276 776 486 HOH HOH B . 
J 6 HOH 277 777 404 HOH HOH B . 
J 6 HOH 278 778 623 HOH HOH B . 
J 6 HOH 279 779 795 HOH HOH B . 
J 6 HOH 280 780 802 HOH HOH B . 
J 6 HOH 281 781 422 HOH HOH B . 
J 6 HOH 282 782 304 HOH HOH B . 
J 6 HOH 283 783 157 HOH HOH B . 
J 6 HOH 284 784 855 HOH HOH B . 
J 6 HOH 285 785 561 HOH HOH B . 
J 6 HOH 286 786 417 HOH HOH B . 
J 6 HOH 287 787 410 HOH HOH B . 
J 6 HOH 288 788 38  HOH HOH B . 
J 6 HOH 289 789 402 HOH HOH B . 
J 6 HOH 290 790 470 HOH HOH B . 
J 6 HOH 291 791 198 HOH HOH B . 
J 6 HOH 292 792 435 HOH HOH B . 
J 6 HOH 293 793 808 HOH HOH B . 
J 6 HOH 294 794 805 HOH HOH B . 
J 6 HOH 295 795 770 HOH HOH B . 
J 6 HOH 296 796 491 HOH HOH B . 
J 6 HOH 297 797 442 HOH HOH B . 
J 6 HOH 298 798 279 HOH HOH B . 
J 6 HOH 299 799 833 HOH HOH B . 
J 6 HOH 300 800 580 HOH HOH B . 
J 6 HOH 301 801 318 HOH HOH B . 
J 6 HOH 302 802 423 HOH HOH B . 
J 6 HOH 303 803 369 HOH HOH B . 
J 6 HOH 304 804 211 HOH HOH B . 
J 6 HOH 305 805 526 HOH HOH B . 
J 6 HOH 306 806 835 HOH HOH B . 
J 6 HOH 307 807 666 HOH HOH B . 
J 6 HOH 308 808 822 HOH HOH B . 
J 6 HOH 309 809 131 HOH HOH B . 
J 6 HOH 310 810 560 HOH HOH B . 
J 6 HOH 311 811 534 HOH HOH B . 
J 6 HOH 312 812 398 HOH HOH B . 
J 6 HOH 313 813 216 HOH HOH B . 
J 6 HOH 314 814 391 HOH HOH B . 
J 6 HOH 315 815 405 HOH HOH B . 
J 6 HOH 316 816 315 HOH HOH B . 
J 6 HOH 317 817 641 HOH HOH B . 
J 6 HOH 318 818 688 HOH HOH B . 
J 6 HOH 319 819 174 HOH HOH B . 
J 6 HOH 320 820 311 HOH HOH B . 
J 6 HOH 321 821 276 HOH HOH B . 
J 6 HOH 322 822 397 HOH HOH B . 
J 6 HOH 323 823 525 HOH HOH B . 
J 6 HOH 324 824 706 HOH HOH B . 
J 6 HOH 325 825 610 HOH HOH B . 
J 6 HOH 326 826 593 HOH HOH B . 
J 6 HOH 327 827 439 HOH HOH B . 
J 6 HOH 328 828 388 HOH HOH B . 
J 6 HOH 329 829 342 HOH HOH B . 
J 6 HOH 330 830 277 HOH HOH B . 
J 6 HOH 331 831 760 HOH HOH B . 
J 6 HOH 332 832 751 HOH HOH B . 
J 6 HOH 333 833 662 HOH HOH B . 
J 6 HOH 334 834 309 HOH HOH B . 
J 6 HOH 335 835 677 HOH HOH B . 
J 6 HOH 336 836 185 HOH HOH B . 
J 6 HOH 337 837 812 HOH HOH B . 
J 6 HOH 338 838 784 HOH HOH B . 
J 6 HOH 339 839 602 HOH HOH B . 
J 6 HOH 340 840 512 HOH HOH B . 
J 6 HOH 341 841 606 HOH HOH B . 
J 6 HOH 342 842 679 HOH HOH B . 
J 6 HOH 343 843 464 HOH HOH B . 
J 6 HOH 344 844 852 HOH HOH B . 
J 6 HOH 345 845 237 HOH HOH B . 
J 6 HOH 346 846 792 HOH HOH B . 
J 6 HOH 347 847 445 HOH HOH B . 
J 6 HOH 348 848 452 HOH HOH B . 
J 6 HOH 349 849 370 HOH HOH B . 
J 6 HOH 350 850 629 HOH HOH B . 
J 6 HOH 351 851 739 HOH HOH B . 
J 6 HOH 352 852 752 HOH HOH B . 
J 6 HOH 353 853 238 HOH HOH B . 
J 6 HOH 354 854 620 HOH HOH B . 
J 6 HOH 355 855 549 HOH HOH B . 
J 6 HOH 356 856 632 HOH HOH B . 
J 6 HOH 357 857 294 HOH HOH B . 
J 6 HOH 358 858 540 HOH HOH B . 
J 6 HOH 359 859 780 HOH HOH B . 
J 6 HOH 360 860 582 HOH HOH B . 
J 6 HOH 361 861 411 HOH HOH B . 
J 6 HOH 362 862 242 HOH HOH B . 
J 6 HOH 363 863 232 HOH HOH B . 
J 6 HOH 364 864 424 HOH HOH B . 
J 6 HOH 365 865 653 HOH HOH B . 
J 6 HOH 366 866 625 HOH HOH B . 
J 6 HOH 367 867 594 HOH HOH B . 
J 6 HOH 368 868 600 HOH HOH B . 
J 6 HOH 369 869 533 HOH HOH B . 
J 6 HOH 370 870 848 HOH HOH B . 
J 6 HOH 371 871 365 HOH HOH B . 
J 6 HOH 372 872 189 HOH HOH B . 
J 6 HOH 373 873 834 HOH HOH B . 
J 6 HOH 374 874 583 HOH HOH B . 
J 6 HOH 375 875 275 HOH HOH B . 
J 6 HOH 376 876 511 HOH HOH B . 
J 6 HOH 377 877 771 HOH HOH B . 
J 6 HOH 378 878 434 HOH HOH B . 
J 6 HOH 379 879 552 HOH HOH B . 
J 6 HOH 380 880 821 HOH HOH B . 
J 6 HOH 381 881 236 HOH HOH B . 
J 6 HOH 382 882 787 HOH HOH B . 
J 6 HOH 383 883 861 HOH HOH B . 
J 6 HOH 384 884 726 HOH HOH B . 
J 6 HOH 385 885 509 HOH HOH B . 
J 6 HOH 386 886 385 HOH HOH B . 
J 6 HOH 387 887 746 HOH HOH B . 
J 6 HOH 388 888 634 HOH HOH B . 
J 6 HOH 389 889 869 HOH HOH B . 
J 6 HOH 390 890 630 HOH HOH B . 
J 6 HOH 391 891 684 HOH HOH B . 
J 6 HOH 392 892 517 HOH HOH B . 
J 6 HOH 393 893 461 HOH HOH B . 
J 6 HOH 394 894 280 HOH HOH B . 
J 6 HOH 395 895 476 HOH HOH B . 
J 6 HOH 396 896 766 HOH HOH B . 
J 6 HOH 397 897 337 HOH HOH B . 
J 6 HOH 398 898 536 HOH HOH B . 
J 6 HOH 399 899 551 HOH HOH B . 
J 6 HOH 400 900 734 HOH HOH B . 
J 6 HOH 401 901 454 HOH HOH B . 
J 6 HOH 402 902 453 HOH HOH B . 
J 6 HOH 403 903 646 HOH HOH B . 
J 6 HOH 404 904 836 HOH HOH B . 
J 6 HOH 405 905 755 HOH HOH B . 
J 6 HOH 406 906 383 HOH HOH B . 
J 6 HOH 407 907 866 HOH HOH B . 
J 6 HOH 408 908 864 HOH HOH B . 
J 6 HOH 409 909 255 HOH HOH B . 
J 6 HOH 410 910 472 HOH HOH B . 
J 6 HOH 411 911 420 HOH HOH B . 
J 6 HOH 412 912 451 HOH HOH B . 
J 6 HOH 413 913 644 HOH HOH B . 
J 6 HOH 414 914 786 HOH HOH B . 
J 6 HOH 415 915 735 HOH HOH B . 
J 6 HOH 416 916 736 HOH HOH B . 
J 6 HOH 417 917 721 HOH HOH B . 
J 6 HOH 418 918 188 HOH HOH B . 
J 6 HOH 419 919 731 HOH HOH B . 
J 6 HOH 420 920 778 HOH HOH B . 
J 6 HOH 421 921 819 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 ? ? ? '(1.17.1_3660)' 1 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot   ? ? ? .               2 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   98.30 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9EVI 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     47.344 
_cell.length_a_esd                 ? 
_cell.length_b                     80.985 
_cell.length_b_esd                 ? 
_cell.length_c                     73.993 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9EVI 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9EVI 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.08 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          40.75 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.2 M potassium sodium tartrate tetrahydrate; 0.1 M Bis-Tris propane, pH 7.5; 25 % w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295.15 
# 
_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 EIGER2 XE 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         2020-01-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   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                        'DIAMOND BEAMLINE I04' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9795 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I04 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9EVI 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.19 
_reflns.d_resolution_low                               54.37 
_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                                     129759 
_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                           73.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.053 
_reflns.pdbx_Rpim_I_all                                0.024 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.9989 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.047 
_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                                    1.19 
_reflns_shell.d_res_low                                     1.21 
_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                             279 
_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                               1.0 
_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                                  0.387 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          3.03 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.642 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9EVI 
_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                            1.45 
_refine.ls_d_res_low                             46.85 
_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                     97613 
_refine.ls_number_reflns_R_free                  4876 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.86 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1375 
_refine.ls_R_factor_R_free                       0.1679 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1359 
_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                          1.38 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 17.43 
_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                            0.13 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4700 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             845 
_refine_hist.number_atoms_total               5587 
_refine_hist.d_res_high                       1.45 
_refine_hist.d_res_low                        46.85 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.005 ? 4920 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.812 ? 6759 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.160 ? 703  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.064 ? 789  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.005 ? 889  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.45 1.47  . . 147 3106 99.00  . . . . 0.2304 . . . . . . . . . . . 0.2746 
'X-RAY DIFFRACTION' 1.47 1.48  . . 160 3092 100.00 . . . . 0.2151 . . . . . . . . . . . 0.2732 
'X-RAY DIFFRACTION' 1.48 1.50  . . 167 3017 100.00 . . . . 0.1832 . . . . . . . . . . . 0.2317 
'X-RAY DIFFRACTION' 1.50 1.52  . . 159 3098 100.00 . . . . 0.1683 . . . . . . . . . . . 0.2253 
'X-RAY DIFFRACTION' 1.52 1.54  . . 161 3087 100.00 . . . . 0.1638 . . . . . . . . . . . 0.2142 
'X-RAY DIFFRACTION' 1.54 1.56  . . 146 3097 100.00 . . . . 0.1539 . . . . . . . . . . . 0.1994 
'X-RAY DIFFRACTION' 1.56 1.58  . . 167 3096 100.00 . . . . 0.1478 . . . . . . . . . . . 0.2407 
'X-RAY DIFFRACTION' 1.58 1.61  . . 163 3041 100.00 . . . . 0.1360 . . . . . . . . . . . 0.1795 
'X-RAY DIFFRACTION' 1.61 1.63  . . 167 3100 100.00 . . . . 0.1292 . . . . . . . . . . . 0.1772 
'X-RAY DIFFRACTION' 1.63 1.66  . . 177 3036 100.00 . . . . 0.1310 . . . . . . . . . . . 0.1839 
'X-RAY DIFFRACTION' 1.66 1.69  . . 167 3117 100.00 . . . . 0.1308 . . . . . . . . . . . 0.1778 
'X-RAY DIFFRACTION' 1.69 1.72  . . 151 3061 100.00 . . . . 0.1314 . . . . . . . . . . . 0.2019 
'X-RAY DIFFRACTION' 1.72 1.75  . . 163 3081 100.00 . . . . 0.1424 . . . . . . . . . . . 0.2082 
'X-RAY DIFFRACTION' 1.75 1.79  . . 178 3046 100.00 . . . . 0.1384 . . . . . . . . . . . 0.1970 
'X-RAY DIFFRACTION' 1.79 1.83  . . 167 3105 100.00 . . . . 0.1370 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 1.83 1.87  . . 160 3074 100.00 . . . . 0.1388 . . . . . . . . . . . 0.1968 
'X-RAY DIFFRACTION' 1.87 1.92  . . 162 3111 100.00 . . . . 0.1335 . . . . . . . . . . . 0.1858 
'X-RAY DIFFRACTION' 1.92 1.97  . . 163 3075 100.00 . . . . 0.1318 . . . . . . . . . . . 0.1765 
'X-RAY DIFFRACTION' 1.97 2.03  . . 154 3093 100.00 . . . . 0.1314 . . . . . . . . . . . 0.1584 
'X-RAY DIFFRACTION' 2.03 2.09  . . 168 3079 100.00 . . . . 0.1288 . . . . . . . . . . . 0.1766 
'X-RAY DIFFRACTION' 2.09 2.17  . . 166 3100 100.00 . . . . 0.1269 . . . . . . . . . . . 0.1735 
'X-RAY DIFFRACTION' 2.17 2.25  . . 177 3099 100.00 . . . . 0.1272 . . . . . . . . . . . 0.1753 
'X-RAY DIFFRACTION' 2.25 2.36  . . 143 3087 100.00 . . . . 0.1240 . . . . . . . . . . . 0.1456 
'X-RAY DIFFRACTION' 2.36 2.48  . . 145 3138 100.00 . . . . 0.1233 . . . . . . . . . . . 0.1607 
'X-RAY DIFFRACTION' 2.48 2.63  . . 190 3069 100.00 . . . . 0.1293 . . . . . . . . . . . 0.1622 
'X-RAY DIFFRACTION' 2.63 2.84  . . 158 3098 100.00 . . . . 0.1337 . . . . . . . . . . . 0.1482 
'X-RAY DIFFRACTION' 2.84 3.12  . . 147 3157 100.00 . . . . 0.1463 . . . . . . . . . . . 0.1884 
'X-RAY DIFFRACTION' 3.12 3.58  . . 181 3065 100.00 . . . . 0.1377 . . . . . . . . . . . 0.1573 
'X-RAY DIFFRACTION' 3.58 4.50  . . 167 3127 100.00 . . . . 0.1228 . . . . . . . . . . . 0.1405 
'X-RAY DIFFRACTION' 4.51 46.85 . . 155 3185 100.00 . . . . 0.1432 . . . . . . . . . . . 0.1369 
# 
_struct.entry_id                     9EVI 
_struct.title                        'Crystal structure of candida antarctica lipase B with the putative pro-peptide region' 
_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        9EVI 
_struct_keywords.text            'Lipase B, putative pro-peptide region, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
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 4 ? 
F N N 5 ? 
G N N 2 ? 
H N N 3 ? 
I N N 6 ? 
J N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    LIPB_PSEA2 
_struct_ref.pdbx_db_accession          P41365 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATPLVKRLPSGSDPAFSQPKSVLDAGLTCQGASPSSVSKPILLVPGTGTTGPQSFDSNWIPLSTQLGYTPCWISPPPFML
NDTQVNTEYMVNAITALYAGSGNNKLPVLTWSQGGLVAQWGLTFFPSIRSKVDRLMAFAPDYKGTVLAGPLDALAVSAPS
VWQQTTGSALTTALRNAGGLTQIVPTTNLYSATDEIVQPQVSNSPLDSSYLFNGKNVQAQAVCGPLFVIDHAGSLTSQFS
YVVGRSALRSTTGQARSADYGITDCNPLPANDLTPEQKVAAAALLAPAAAAIVAGPKQNCEPDLMPYARPFAVGKRTCSG
IVTP
;
_struct_ref.pdbx_align_begin           19 
# 
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 9EVI A 1 ? 324 ? P41365 19 ? 342 ? 19 342 
2 1 9EVI B 1 ? 324 ? P41365 19 ? 342 ? 19 342 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2480  ? 
1 MORE         -28   ? 
1 'SSA (A^2)'  23540 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 PRO A 19  ? GLY A 26  ? PRO A 37  GLY A 44  1 ? 8  
HELX_P HELX_P2  AA2 THR A 50  ? ASP A 56  ? THR A 68  ASP A 74  1 ? 7  
HELX_P HELX_P3  AA3 ASN A 58  ? GLN A 65  ? ASN A 76  GLN A 83  1 ? 8  
HELX_P HELX_P4  AA4 ASP A 82  ? SER A 101 ? ASP A 100 SER A 119 1 ? 20 
HELX_P HELX_P5  AA5 SER A 112 ? PHE A 125 ? SER A 130 PHE A 143 1 ? 14 
HELX_P HELX_P6  AA6 PRO A 126 ? SER A 130 ? PRO A 144 SER A 148 5 ? 5  
HELX_P HELX_P7  AA7 ALA A 158 ? GLN A 164 ? ALA A 176 GLN A 182 1 ? 7  
HELX_P HELX_P8  AA8 SER A 168 ? ALA A 177 ? SER A 186 ALA A 195 1 ? 10 
HELX_P HELX_P9  AA9 ALA A 219 ? GLY A 224 ? ALA A 237 GLY A 242 1 ? 6  
HELX_P HELX_P10 AB1 ALA A 232 ? SER A 237 ? ALA A 250 SER A 255 1 ? 6  
HELX_P HELX_P11 AB2 SER A 237 ? SER A 250 ? SER A 255 SER A 268 1 ? 14 
HELX_P HELX_P12 AB3 ARG A 256 ? TYR A 260 ? ARG A 274 TYR A 278 5 ? 5  
HELX_P HELX_P13 AB4 GLY A 261 ? CYS A 265 ? GLY A 279 CYS A 283 5 ? 5  
HELX_P HELX_P14 AB5 THR A 274 ? ALA A 283 ? THR A 292 ALA A 301 1 ? 10 
HELX_P HELX_P15 AB6 LEU A 285 ? GLY A 295 ? LEU A 303 GLY A 313 1 ? 11 
HELX_P HELX_P16 AB7 ALA A 308 ? ALA A 312 ? ALA A 326 ALA A 330 5 ? 5  
HELX_P HELX_P17 AB8 PRO B 19  ? GLY B 26  ? PRO B 37  GLY B 44  1 ? 8  
HELX_P HELX_P18 AB9 THR B 50  ? ASP B 56  ? THR B 68  ASP B 74  1 ? 7  
HELX_P HELX_P19 AC1 ASN B 58  ? LEU B 66  ? ASN B 76  LEU B 84  1 ? 9  
HELX_P HELX_P20 AC2 ASP B 82  ? SER B 101 ? ASP B 100 SER B 119 1 ? 20 
HELX_P HELX_P21 AC3 SER B 112 ? PHE B 125 ? SER B 130 PHE B 143 1 ? 14 
HELX_P HELX_P22 AC4 PRO B 126 ? ARG B 129 ? PRO B 144 ARG B 147 5 ? 4  
HELX_P HELX_P23 AC5 THR B 145 ? GLY B 149 ? THR B 163 GLY B 167 5 ? 5  
HELX_P HELX_P24 AC6 PRO B 150 ? LEU B 154 ? PRO B 168 LEU B 172 5 ? 5  
HELX_P HELX_P25 AC7 ALA B 158 ? GLN B 164 ? ALA B 176 GLN B 182 1 ? 7  
HELX_P HELX_P26 AC8 SER B 168 ? ALA B 177 ? SER B 186 ALA B 195 1 ? 10 
HELX_P HELX_P27 AC9 ALA B 219 ? GLY B 224 ? ALA B 237 GLY B 242 1 ? 6  
HELX_P HELX_P28 AD1 ALA B 232 ? SER B 237 ? ALA B 250 SER B 255 1 ? 6  
HELX_P HELX_P29 AD2 SER B 237 ? SER B 250 ? SER B 255 SER B 268 1 ? 14 
HELX_P HELX_P30 AD3 ARG B 256 ? TYR B 260 ? ARG B 274 TYR B 278 5 ? 5  
HELX_P HELX_P31 AD4 GLY B 261 ? CYS B 265 ? GLY B 279 CYS B 283 5 ? 5  
HELX_P HELX_P32 AD5 THR B 274 ? ALA B 283 ? THR B 292 ALA B 301 1 ? 10 
HELX_P HELX_P33 AD6 LEU B 285 ? GLY B 295 ? LEU B 303 GLY B 313 1 ? 11 
HELX_P HELX_P34 AD7 ALA B 308 ? ALA B 312 ? ALA B 326 ALA B 330 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 29  SG ? ? ? 1_555 A CYS 71  SG ? ? A CYS 47  A CYS 89  1_555 ? ? ? ? ? ? ? 2.058 ? ? 
disulf2 disulf ? ? A CYS 223 SG ? ? ? 1_555 A CYS 265 SG ? ? A CYS 241 A CYS 283 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
disulf3 disulf ? ? A CYS 300 SG ? ? ? 1_555 A CYS 318 SG ? ? A CYS 318 A CYS 336 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf4 disulf ? ? B CYS 29  SG ? ? ? 1_555 B CYS 71  SG ? ? B CYS 47  B CYS 89  1_555 ? ? ? ? ? ? ? 2.047 ? ? 
disulf5 disulf ? ? B CYS 223 SG ? ? ? 1_555 B CYS 265 SG ? ? B CYS 241 B CYS 283 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
disulf6 disulf ? ? B CYS 300 SG ? ? ? 1_555 B CYS 318 SG ? ? B CYS 318 B CYS 336 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc1 metalc ? ? A PRO 150 O  ? ? ? 1_555 D NA  .   NA ? ? A PRO 168 A NA  402 1_555 ? ? ? ? ? ? ? 2.875 ? ? 
metalc2 metalc ? ? A ASP 152 O  ? ? ? 1_555 D NA  .   NA ? ? A ASP 170 A NA  402 1_555 ? ? ? ? ? ? ? 2.713 ? ? 
metalc3 metalc ? ? A LEU 154 O  ? ? ? 1_555 D NA  .   NA ? ? A LEU 172 A NA  402 1_555 ? ? ? ? ? ? ? 2.410 ? ? 
metalc4 metalc ? ? A VAL 156 O  ? ? ? 1_555 D NA  .   NA ? ? A VAL 174 A NA  402 1_555 ? ? ? ? ? ? ? 3.008 ? ? 
metalc5 metalc ? ? A SER 157 OG ? ? ? 1_555 D NA  .   NA ? ? A SER 175 A NA  402 1_555 ? ? ? ? ? ? ? 2.935 ? ? 
metalc6 metalc ? ? D NA  .   NA ? ? ? 1_555 I HOH .   O  ? ? A NA  402 A HOH 772 1_555 ? ? ? ? ? ? ? 2.548 ? ? 
metalc7 metalc ? ? B ILE 292 O  ? ? ? 1_555 H NA  .   NA ? ? B ILE 310 B NA  404 1_555 ? ? ? ? ? ? ? 2.794 ? ? 
metalc8 metalc ? ? B PRO 296 O  ? ? ? 1_555 H NA  .   NA ? ? B PRO 314 B NA  404 1_555 ? ? ? ? ? ? ? 2.833 ? ? 
metalc9 metalc ? ? H NA  .   NA ? ? ? 1_555 J HOH .   O  ? ? B NA  404 B HOH 671 1_555 ? ? ? ? ? ? ? 2.917 ? ? 
# 
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 PRO 150 ? A PRO 168 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? A ASP 152 ? A ASP 170 ? 1_555 98.7  ? 
2  O  ? A PRO 150 ? A PRO 168 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? A LEU 154 ? A LEU 172 ? 1_555 85.1  ? 
3  O  ? A ASP 152 ? A ASP 170 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? A LEU 154 ? A LEU 172 ? 1_555 79.6  ? 
4  O  ? A PRO 150 ? A PRO 168 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? A VAL 156 ? A VAL 174 ? 1_555 85.8  ? 
5  O  ? A ASP 152 ? A ASP 170 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? A VAL 156 ? A VAL 174 ? 1_555 150.7 ? 
6  O  ? A LEU 154 ? A LEU 172 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? A VAL 156 ? A VAL 174 ? 1_555 71.9  ? 
7  O  ? A PRO 150 ? A PRO 168 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 OG ? A SER 157 ? A SER 175 ? 1_555 51.6  ? 
8  O  ? A ASP 152 ? A ASP 170 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 OG ? A SER 157 ? A SER 175 ? 1_555 140.2 ? 
9  O  ? A LEU 154 ? A LEU 172 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 OG ? A SER 157 ? A SER 175 ? 1_555 117.3 ? 
10 O  ? A VAL 156 ? A VAL 174 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 OG ? A SER 157 ? A SER 175 ? 1_555 63.1  ? 
11 O  ? A PRO 150 ? A PRO 168 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? I HOH .   ? A HOH 772 ? 1_555 91.2  ? 
12 O  ? A ASP 152 ? A ASP 170 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? I HOH .   ? A HOH 772 ? 1_555 78.1  ? 
13 O  ? A LEU 154 ? A LEU 172 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? I HOH .   ? A HOH 772 ? 1_555 156.5 ? 
14 O  ? A VAL 156 ? A VAL 174 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? I HOH .   ? A HOH 772 ? 1_555 131.0 ? 
15 OG ? A SER 157 ? A SER 175 ? 1_555 NA ? D NA . ? A NA 402 ? 1_555 O  ? I HOH .   ? A HOH 772 ? 1_555 77.0  ? 
16 O  ? B ILE 292 ? B ILE 310 ? 1_555 NA ? H NA . ? B NA 404 ? 1_555 O  ? B PRO 296 ? B PRO 314 ? 1_555 129.5 ? 
17 O  ? B ILE 292 ? B ILE 310 ? 1_555 NA ? H NA . ? B NA 404 ? 1_555 O  ? J HOH .   ? B HOH 671 ? 1_555 119.0 ? 
18 O  ? B PRO 296 ? B PRO 314 ? 1_555 NA ? H NA . ? B NA 404 ? 1_555 O  ? J HOH .   ? B HOH 671 ? 1_555 103.0 ? 
# 
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 29  ? CYS A 71  ? CYS A 47  ? 1_555 CYS A 89  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS A 223 ? CYS A 265 ? CYS A 241 ? 1_555 CYS A 283 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3 CYS A 300 ? CYS A 318 ? CYS A 318 ? 1_555 CYS A 336 ? 1_555 SG SG . . . None 'Disulfide bridge' 
4 CYS B 29  ? CYS B 71  ? CYS B 47  ? 1_555 CYS B 89  ? 1_555 SG SG . . . None 'Disulfide bridge' 
5 CYS B 223 ? CYS B 265 ? CYS B 241 ? 1_555 CYS B 283 ? 1_555 SG SG . . . None 'Disulfide bridge' 
6 CYS B 300 ? CYS B 318 ? CYS B 318 ? 1_555 CYS B 336 ? 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 PRO 76  A . ? PRO 94  A PRO 77  A ? PRO 95  A 1 -10.86 
2 GLN 198 A . ? GLN 216 A PRO 199 A ? PRO 217 A 1 4.70   
3 PRO 76  B . ? PRO 94  B PRO 77  B ? PRO 95  B 1 -11.22 
4 GLN 198 B . ? GLN 216 B PRO 199 B ? PRO 217 B 1 1.84   
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 7 ? 
AA2 ? 2 ? 
AA3 ? 7 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 27  ? CYS A 29  ? LEU A 45  CYS A 47  
AA1 2 THR A 69  ? ILE A 73  ? THR A 87  ILE A 91  
AA1 3 PRO A 40  ? VAL A 44  ? PRO A 58  VAL A 62  
AA1 4 LEU A 106 ? TRP A 111 ? LEU A 124 TRP A 129 
AA1 5 VAL A 132 ? PHE A 138 ? VAL A 150 PHE A 156 
AA1 6 THR A 186 ? TYR A 190 ? THR A 204 TYR A 208 
AA1 7 LYS A 215 ? GLN A 218 ? LYS A 233 GLN A 236 
AA2 1 ARG A 316 ? THR A 317 ? ARG A 334 THR A 335 
AA2 2 GLY A 320 ? ILE A 321 ? GLY A 338 ILE A 339 
AA3 1 LEU B 27  ? CYS B 29  ? LEU B 45  CYS B 47  
AA3 2 THR B 69  ? ILE B 73  ? THR B 87  ILE B 91  
AA3 3 PRO B 40  ? VAL B 44  ? PRO B 58  VAL B 62  
AA3 4 LEU B 106 ? TRP B 111 ? LEU B 124 TRP B 129 
AA3 5 VAL B 132 ? PHE B 138 ? VAL B 150 PHE B 156 
AA3 6 THR B 186 ? TYR B 190 ? THR B 204 TYR B 208 
AA3 7 LYS B 215 ? GLN B 218 ? LYS B 233 GLN B 236 
AA4 1 ARG B 316 ? THR B 317 ? ARG B 334 THR B 335 
AA4 2 GLY B 320 ? ILE B 321 ? GLY B 338 ILE B 339 
# 
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 THR A 28  ? N THR A 46  O TRP A 72  ? O TRP A 90  
AA1 2 3 O CYS A 71  ? O CYS A 89  N LEU A 43  ? N LEU A 61  
AA1 3 4 N LEU A 42  ? N LEU A 60  O LEU A 109 ? O LEU A 127 
AA1 4 5 N VAL A 108 ? N VAL A 126 O MET A 136 ? O MET A 154 
AA1 5 6 N ALA A 137 ? N ALA A 155 O THR A 187 ? O THR A 205 
AA1 6 7 N ASN A 188 ? N ASN A 206 O VAL A 217 ? O VAL A 235 
AA2 1 2 N THR A 317 ? N THR A 335 O GLY A 320 ? O GLY A 338 
AA3 1 2 N THR B 28  ? N THR B 46  O TRP B 72  ? O TRP B 90  
AA3 2 3 O CYS B 71  ? O CYS B 89  N LEU B 43  ? N LEU B 61  
AA3 3 4 N LEU B 42  ? N LEU B 60  O LEU B 109 ? O LEU B 127 
AA3 4 5 N VAL B 108 ? N VAL B 126 O MET B 136 ? O MET B 154 
AA3 5 6 N ALA B 137 ? N ALA B 155 O THR B 187 ? O THR B 205 
AA3 6 7 N ASN B 188 ? N ASN B 206 O VAL B 217 ? O VAL B 235 
AA4 1 2 N THR B 317 ? N THR B 335 O GLY B 320 ? O GLY B 338 
# 
_pdbx_entry_details.entry_id                   9EVI 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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 54  ? ? -159.29 88.76   
2  1 ASN A 76  ? ? -149.24 -93.94  
3  1 ASP A 100 ? ? -34.91  118.30  
4  1 ASP A 100 ? ? -31.03  118.30  
5  1 SER A 130 ? ? 58.34   -129.43 
6  1 ASP A 159 ? ? -113.96 67.44   
7  1 ALA A 166 ? ? 51.00   70.55   
8  1 ALA A 171 ? ? 64.09   -129.78 
9  1 ASN A 231 ? ? 71.99   -3.74   
10 1 ALA A 330 ? ? -146.49 31.21   
11 1 ASN B 76  ? ? -147.04 -92.10  
12 1 ASP B 100 ? ? -26.61  116.99  
13 1 SER B 130 ? ? 56.62   -127.60 
14 1 ASP B 159 ? ? -114.93 67.07   
15 1 ASN B 231 ? ? 70.34   -3.16   
16 1 ALA B 330 ? ? -143.25 35.33   
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 920 ? 6.08 . 
2 1 O ? A HOH 921 ? 6.26 . 
3 1 O ? A HOH 922 ? 6.50 . 
4 1 O ? A HOH 923 ? 7.22 . 
5 1 O ? A HOH 924 ? 8.72 . 
6 1 O ? B HOH 919 ? 5.81 . 
7 1 O ? B HOH 920 ? 6.48 . 
8 1 O ? B HOH 921 ? 7.07 . 
# 
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 B ALA 19 ? B ALA 1 
2 1 Y 1 B THR 20 ? B THR 2 
3 1 Y 1 B PRO 21 ? B PRO 3 
4 1 Y 1 B LEU 22 ? B LEU 4 
5 1 Y 1 B VAL 23 ? B VAL 5 
6 1 Y 1 B LYS 24 ? B LYS 6 
7 1 Y 1 B ARG 25 ? B ARG 7 
# 
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  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
HIS N    N  N N 137 
HIS CA   C  N S 138 
HIS C    C  N N 139 
HIS O    O  N N 140 
HIS CB   C  N N 141 
HIS CG   C  Y N 142 
HIS ND1  N  Y N 143 
HIS CD2  C  Y N 144 
HIS CE1  C  Y N 145 
HIS NE2  N  Y N 146 
HIS OXT  O  N N 147 
HIS H    H  N N 148 
HIS H2   H  N N 149 
HIS HA   H  N N 150 
HIS HB2  H  N N 151 
HIS HB3  H  N N 152 
HIS HD1  H  N N 153 
HIS HD2  H  N N 154 
HIS HE1  H  N N 155 
HIS HE2  H  N N 156 
HIS HXT  H  N N 157 
HOH O    O  N N 158 
HOH H1   H  N N 159 
HOH H2   H  N N 160 
ILE N    N  N N 161 
ILE CA   C  N S 162 
ILE C    C  N N 163 
ILE O    O  N N 164 
ILE CB   C  N S 165 
ILE CG1  C  N N 166 
ILE CG2  C  N N 167 
ILE CD1  C  N N 168 
ILE OXT  O  N N 169 
ILE H    H  N N 170 
ILE H2   H  N N 171 
ILE HA   H  N N 172 
ILE HB   H  N N 173 
ILE HG12 H  N N 174 
ILE HG13 H  N N 175 
ILE HG21 H  N N 176 
ILE HG22 H  N N 177 
ILE HG23 H  N N 178 
ILE HD11 H  N N 179 
ILE HD12 H  N N 180 
ILE HD13 H  N N 181 
ILE HXT  H  N N 182 
LEU N    N  N N 183 
LEU CA   C  N S 184 
LEU C    C  N N 185 
LEU O    O  N N 186 
LEU CB   C  N N 187 
LEU CG   C  N N 188 
LEU CD1  C  N N 189 
LEU CD2  C  N N 190 
LEU OXT  O  N N 191 
LEU H    H  N N 192 
LEU H2   H  N N 193 
LEU HA   H  N N 194 
LEU HB2  H  N N 195 
LEU HB3  H  N N 196 
LEU HG   H  N N 197 
LEU HD11 H  N N 198 
LEU HD12 H  N N 199 
LEU HD13 H  N N 200 
LEU HD21 H  N N 201 
LEU HD22 H  N N 202 
LEU HD23 H  N N 203 
LEU HXT  H  N N 204 
LYS N    N  N N 205 
LYS CA   C  N S 206 
LYS C    C  N N 207 
LYS O    O  N N 208 
LYS CB   C  N N 209 
LYS CG   C  N N 210 
LYS CD   C  N N 211 
LYS CE   C  N N 212 
LYS NZ   N  N N 213 
LYS OXT  O  N N 214 
LYS H    H  N N 215 
LYS H2   H  N N 216 
LYS HA   H  N N 217 
LYS HB2  H  N N 218 
LYS HB3  H  N N 219 
LYS HG2  H  N N 220 
LYS HG3  H  N N 221 
LYS HD2  H  N N 222 
LYS HD3  H  N N 223 
LYS HE2  H  N N 224 
LYS HE3  H  N N 225 
LYS HZ1  H  N N 226 
LYS HZ2  H  N N 227 
LYS HZ3  H  N N 228 
LYS HXT  H  N N 229 
MET N    N  N N 230 
MET CA   C  N S 231 
MET C    C  N N 232 
MET O    O  N N 233 
MET CB   C  N N 234 
MET CG   C  N N 235 
MET SD   S  N N 236 
MET CE   C  N N 237 
MET OXT  O  N N 238 
MET H    H  N N 239 
MET H2   H  N N 240 
MET HA   H  N N 241 
MET HB2  H  N N 242 
MET HB3  H  N N 243 
MET HG2  H  N N 244 
MET HG3  H  N N 245 
MET HE1  H  N N 246 
MET HE2  H  N N 247 
MET HE3  H  N N 248 
MET HXT  H  N N 249 
NA  NA   NA N N 250 
PEG C1   C  N N 251 
PEG O1   O  N N 252 
PEG C2   C  N N 253 
PEG O2   O  N N 254 
PEG C3   C  N N 255 
PEG C4   C  N N 256 
PEG O4   O  N N 257 
PEG H11  H  N N 258 
PEG H12  H  N N 259 
PEG HO1  H  N N 260 
PEG H21  H  N N 261 
PEG H22  H  N N 262 
PEG H31  H  N N 263 
PEG H32  H  N N 264 
PEG H41  H  N N 265 
PEG H42  H  N N 266 
PEG HO4  H  N N 267 
PG4 O1   O  N N 268 
PG4 C1   C  N N 269 
PG4 C2   C  N N 270 
PG4 O2   O  N N 271 
PG4 C3   C  N N 272 
PG4 C4   C  N N 273 
PG4 O3   O  N N 274 
PG4 C5   C  N N 275 
PG4 C6   C  N N 276 
PG4 O4   O  N N 277 
PG4 C7   C  N N 278 
PG4 C8   C  N N 279 
PG4 O5   O  N N 280 
PG4 HO1  H  N N 281 
PG4 H11  H  N N 282 
PG4 H12  H  N N 283 
PG4 H21  H  N N 284 
PG4 H22  H  N N 285 
PG4 H31  H  N N 286 
PG4 H32  H  N N 287 
PG4 H41  H  N N 288 
PG4 H42  H  N N 289 
PG4 H51  H  N N 290 
PG4 H52  H  N N 291 
PG4 H61  H  N N 292 
PG4 H62  H  N N 293 
PG4 H71  H  N N 294 
PG4 H72  H  N N 295 
PG4 H81  H  N N 296 
PG4 H82  H  N N 297 
PG4 HO5  H  N N 298 
PHE N    N  N N 299 
PHE CA   C  N S 300 
PHE C    C  N N 301 
PHE O    O  N N 302 
PHE CB   C  N N 303 
PHE CG   C  Y N 304 
PHE CD1  C  Y N 305 
PHE CD2  C  Y N 306 
PHE CE1  C  Y N 307 
PHE CE2  C  Y N 308 
PHE CZ   C  Y N 309 
PHE OXT  O  N N 310 
PHE H    H  N N 311 
PHE H2   H  N N 312 
PHE HA   H  N N 313 
PHE HB2  H  N N 314 
PHE HB3  H  N N 315 
PHE HD1  H  N N 316 
PHE HD2  H  N N 317 
PHE HE1  H  N N 318 
PHE HE2  H  N N 319 
PHE HZ   H  N N 320 
PHE HXT  H  N N 321 
PRO N    N  N N 322 
PRO CA   C  N S 323 
PRO C    C  N N 324 
PRO O    O  N N 325 
PRO CB   C  N N 326 
PRO CG   C  N N 327 
PRO CD   C  N N 328 
PRO OXT  O  N N 329 
PRO H    H  N N 330 
PRO HA   H  N N 331 
PRO HB2  H  N N 332 
PRO HB3  H  N N 333 
PRO HG2  H  N N 334 
PRO HG3  H  N N 335 
PRO HD2  H  N N 336 
PRO HD3  H  N N 337 
PRO HXT  H  N N 338 
SER N    N  N N 339 
SER CA   C  N S 340 
SER C    C  N N 341 
SER O    O  N N 342 
SER CB   C  N N 343 
SER OG   O  N N 344 
SER OXT  O  N N 345 
SER H    H  N N 346 
SER H2   H  N N 347 
SER HA   H  N N 348 
SER HB2  H  N N 349 
SER HB3  H  N N 350 
SER HG   H  N N 351 
SER HXT  H  N N 352 
THR N    N  N N 353 
THR CA   C  N S 354 
THR C    C  N N 355 
THR O    O  N N 356 
THR CB   C  N R 357 
THR OG1  O  N N 358 
THR CG2  C  N N 359 
THR OXT  O  N N 360 
THR H    H  N N 361 
THR H2   H  N N 362 
THR HA   H  N N 363 
THR HB   H  N N 364 
THR HG1  H  N N 365 
THR HG21 H  N N 366 
THR HG22 H  N N 367 
THR HG23 H  N N 368 
THR HXT  H  N N 369 
TLA O1   O  N N 370 
TLA O11  O  N N 371 
TLA C1   C  N N 372 
TLA C2   C  N R 373 
TLA O2   O  N N 374 
TLA C3   C  N R 375 
TLA O3   O  N N 376 
TLA C4   C  N N 377 
TLA O4   O  N N 378 
TLA O41  O  N N 379 
TLA H11  H  N N 380 
TLA H2   H  N N 381 
TLA HA   H  N N 382 
TLA H3   H  N N 383 
TLA HB   H  N N 384 
TLA H41  H  N N 385 
TRP N    N  N N 386 
TRP CA   C  N S 387 
TRP C    C  N N 388 
TRP O    O  N N 389 
TRP CB   C  N N 390 
TRP CG   C  Y N 391 
TRP CD1  C  Y N 392 
TRP CD2  C  Y N 393 
TRP NE1  N  Y N 394 
TRP CE2  C  Y N 395 
TRP CE3  C  Y N 396 
TRP CZ2  C  Y N 397 
TRP CZ3  C  Y N 398 
TRP CH2  C  Y N 399 
TRP OXT  O  N N 400 
TRP H    H  N N 401 
TRP H2   H  N N 402 
TRP HA   H  N N 403 
TRP HB2  H  N N 404 
TRP HB3  H  N N 405 
TRP HD1  H  N N 406 
TRP HE1  H  N N 407 
TRP HE3  H  N N 408 
TRP HZ2  H  N N 409 
TRP HZ3  H  N N 410 
TRP HH2  H  N N 411 
TRP HXT  H  N N 412 
TYR N    N  N N 413 
TYR CA   C  N S 414 
TYR C    C  N N 415 
TYR O    O  N N 416 
TYR CB   C  N N 417 
TYR CG   C  Y N 418 
TYR CD1  C  Y N 419 
TYR CD2  C  Y N 420 
TYR CE1  C  Y N 421 
TYR CE2  C  Y N 422 
TYR CZ   C  Y N 423 
TYR OH   O  N N 424 
TYR OXT  O  N N 425 
TYR H    H  N N 426 
TYR H2   H  N N 427 
TYR HA   H  N N 428 
TYR HB2  H  N N 429 
TYR HB3  H  N N 430 
TYR HD1  H  N N 431 
TYR HD2  H  N N 432 
TYR HE1  H  N N 433 
TYR HE2  H  N N 434 
TYR HH   H  N N 435 
TYR HXT  H  N N 436 
VAL N    N  N N 437 
VAL CA   C  N S 438 
VAL C    C  N N 439 
VAL O    O  N N 440 
VAL CB   C  N N 441 
VAL CG1  C  N N 442 
VAL CG2  C  N N 443 
VAL OXT  O  N N 444 
VAL H    H  N N 445 
VAL H2   H  N N 446 
VAL HA   H  N N 447 
VAL HB   H  N N 448 
VAL HG11 H  N N 449 
VAL HG12 H  N N 450 
VAL HG13 H  N N 451 
VAL HG21 H  N N 452 
VAL HG22 H  N N 453 
VAL HG23 H  N N 454 
VAL HXT  H  N N 455 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PEG C1  O1   sing N N 237 
PEG C1  C2   sing N N 238 
PEG C1  H11  sing N N 239 
PEG C1  H12  sing N N 240 
PEG O1  HO1  sing N N 241 
PEG C2  O2   sing N N 242 
PEG C2  H21  sing N N 243 
PEG C2  H22  sing N N 244 
PEG O2  C3   sing N N 245 
PEG C3  C4   sing N N 246 
PEG C3  H31  sing N N 247 
PEG C3  H32  sing N N 248 
PEG C4  O4   sing N N 249 
PEG C4  H41  sing N N 250 
PEG C4  H42  sing N N 251 
PEG O4  HO4  sing N N 252 
PG4 O1  C1   sing N N 253 
PG4 O1  HO1  sing N N 254 
PG4 C1  C2   sing N N 255 
PG4 C1  H11  sing N N 256 
PG4 C1  H12  sing N N 257 
PG4 C2  O2   sing N N 258 
PG4 C2  H21  sing N N 259 
PG4 C2  H22  sing N N 260 
PG4 O2  C3   sing N N 261 
PG4 C3  C4   sing N N 262 
PG4 C3  H31  sing N N 263 
PG4 C3  H32  sing N N 264 
PG4 C4  O3   sing N N 265 
PG4 C4  H41  sing N N 266 
PG4 C4  H42  sing N N 267 
PG4 O3  C5   sing N N 268 
PG4 C5  C6   sing N N 269 
PG4 C5  H51  sing N N 270 
PG4 C5  H52  sing N N 271 
PG4 C6  O4   sing N N 272 
PG4 C6  H61  sing N N 273 
PG4 C6  H62  sing N N 274 
PG4 O4  C7   sing N N 275 
PG4 C7  C8   sing N N 276 
PG4 C7  H71  sing N N 277 
PG4 C7  H72  sing N N 278 
PG4 C8  O5   sing N N 279 
PG4 C8  H81  sing N N 280 
PG4 C8  H82  sing N N 281 
PG4 O5  HO5  sing N N 282 
PHE N   CA   sing N N 283 
PHE N   H    sing N N 284 
PHE N   H2   sing N N 285 
PHE CA  C    sing N N 286 
PHE CA  CB   sing N N 287 
PHE CA  HA   sing N N 288 
PHE C   O    doub N N 289 
PHE C   OXT  sing N N 290 
PHE CB  CG   sing N N 291 
PHE CB  HB2  sing N N 292 
PHE CB  HB3  sing N N 293 
PHE CG  CD1  doub Y N 294 
PHE CG  CD2  sing Y N 295 
PHE CD1 CE1  sing Y N 296 
PHE CD1 HD1  sing N N 297 
PHE CD2 CE2  doub Y N 298 
PHE CD2 HD2  sing N N 299 
PHE CE1 CZ   doub Y N 300 
PHE CE1 HE1  sing N N 301 
PHE CE2 CZ   sing Y N 302 
PHE CE2 HE2  sing N N 303 
PHE CZ  HZ   sing N N 304 
PHE OXT HXT  sing N N 305 
PRO N   CA   sing N N 306 
PRO N   CD   sing N N 307 
PRO N   H    sing N N 308 
PRO CA  C    sing N N 309 
PRO CA  CB   sing N N 310 
PRO CA  HA   sing N N 311 
PRO C   O    doub N N 312 
PRO C   OXT  sing N N 313 
PRO CB  CG   sing N N 314 
PRO CB  HB2  sing N N 315 
PRO CB  HB3  sing N N 316 
PRO CG  CD   sing N N 317 
PRO CG  HG2  sing N N 318 
PRO CG  HG3  sing N N 319 
PRO CD  HD2  sing N N 320 
PRO CD  HD3  sing N N 321 
PRO OXT HXT  sing N N 322 
SER N   CA   sing N N 323 
SER N   H    sing N N 324 
SER N   H2   sing N N 325 
SER CA  C    sing N N 326 
SER CA  CB   sing N N 327 
SER CA  HA   sing N N 328 
SER C   O    doub N N 329 
SER C   OXT  sing N N 330 
SER CB  OG   sing N N 331 
SER CB  HB2  sing N N 332 
SER CB  HB3  sing N N 333 
SER OG  HG   sing N N 334 
SER OXT HXT  sing N N 335 
THR N   CA   sing N N 336 
THR N   H    sing N N 337 
THR N   H2   sing N N 338 
THR CA  C    sing N N 339 
THR CA  CB   sing N N 340 
THR CA  HA   sing N N 341 
THR C   O    doub N N 342 
THR C   OXT  sing N N 343 
THR CB  OG1  sing N N 344 
THR CB  CG2  sing N N 345 
THR CB  HB   sing N N 346 
THR OG1 HG1  sing N N 347 
THR CG2 HG21 sing N N 348 
THR CG2 HG22 sing N N 349 
THR CG2 HG23 sing N N 350 
THR OXT HXT  sing N N 351 
TLA O1  C1   doub N N 352 
TLA O11 C1   sing N N 353 
TLA O11 H11  sing N N 354 
TLA C1  C2   sing N N 355 
TLA C2  O2   sing N N 356 
TLA C2  C3   sing N N 357 
TLA C2  H2   sing N N 358 
TLA O2  HA   sing N N 359 
TLA C3  O3   sing N N 360 
TLA C3  C4   sing N N 361 
TLA C3  H3   sing N N 362 
TLA O3  HB   sing N N 363 
TLA C4  O4   doub N N 364 
TLA C4  O41  sing N N 365 
TLA O41 H41  sing N N 366 
TRP N   CA   sing N N 367 
TRP N   H    sing N N 368 
TRP N   H2   sing N N 369 
TRP CA  C    sing N N 370 
TRP CA  CB   sing N N 371 
TRP CA  HA   sing N N 372 
TRP C   O    doub N N 373 
TRP C   OXT  sing N N 374 
TRP CB  CG   sing N N 375 
TRP CB  HB2  sing N N 376 
TRP CB  HB3  sing N N 377 
TRP CG  CD1  doub Y N 378 
TRP CG  CD2  sing Y N 379 
TRP CD1 NE1  sing Y N 380 
TRP CD1 HD1  sing N N 381 
TRP CD2 CE2  doub Y N 382 
TRP CD2 CE3  sing Y N 383 
TRP NE1 CE2  sing Y N 384 
TRP NE1 HE1  sing N N 385 
TRP CE2 CZ2  sing Y N 386 
TRP CE3 CZ3  doub Y N 387 
TRP CE3 HE3  sing N N 388 
TRP CZ2 CH2  doub Y N 389 
TRP CZ2 HZ2  sing N N 390 
TRP CZ3 CH2  sing Y N 391 
TRP CZ3 HZ3  sing N N 392 
TRP CH2 HH2  sing N N 393 
TRP OXT HXT  sing N N 394 
TYR N   CA   sing N N 395 
TYR N   H    sing N N 396 
TYR N   H2   sing N N 397 
TYR CA  C    sing N N 398 
TYR CA  CB   sing N N 399 
TYR CA  HA   sing N N 400 
TYR C   O    doub N N 401 
TYR C   OXT  sing N N 402 
TYR CB  CG   sing N N 403 
TYR CB  HB2  sing N N 404 
TYR CB  HB3  sing N N 405 
TYR CG  CD1  doub Y N 406 
TYR CG  CD2  sing Y N 407 
TYR CD1 CE1  sing Y N 408 
TYR CD1 HD1  sing N N 409 
TYR CD2 CE2  doub Y N 410 
TYR CD2 HD2  sing N N 411 
TYR CE1 CZ   doub Y N 412 
TYR CE1 HE1  sing N N 413 
TYR CE2 CZ   sing Y N 414 
TYR CE2 HE2  sing N N 415 
TYR CZ  OH   sing N N 416 
TYR OH  HH   sing N N 417 
TYR OXT HXT  sing N N 418 
VAL N   CA   sing N N 419 
VAL N   H    sing N N 420 
VAL N   H2   sing N N 421 
VAL CA  C    sing N N 422 
VAL CA  CB   sing N N 423 
VAL CA  HA   sing N N 424 
VAL C   O    doub N N 425 
VAL C   OXT  sing N N 426 
VAL CB  CG1  sing N N 427 
VAL CB  CG2  sing N N 428 
VAL CB  HB   sing N N 429 
VAL CG1 HG11 sing N N 430 
VAL CG1 HG12 sing N N 431 
VAL CG1 HG13 sing N N 432 
VAL CG2 HG21 sing N N 433 
VAL CG2 HG22 sing N N 434 
VAL CG2 HG23 sing N N 435 
VAL OXT HXT  sing N N 436 
# 
_pdbx_audit_support.funding_organization   'Academy of Finland' 
_pdbx_audit_support.country                Finland 
_pdbx_audit_support.grant_number           272573 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1TCA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9EVI 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.021122 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003081 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012348 
_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]   0.013658 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
H  
N  
NA 
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N    . ALA A 1 1   ? 28.586  -12.494 3.181   1.00 95.60  ? 19  ALA A N    1 
ATOM   2     C  CA   . ALA A 1 1   ? 27.923  -11.372 3.837   1.00 154.21 ? 19  ALA A CA   1 
ATOM   3     C  C    . ALA A 1 1   ? 26.591  -11.834 4.414   1.00 161.11 ? 19  ALA A C    1 
ATOM   4     O  O    . ALA A 1 1   ? 26.356  -13.032 4.574   1.00 80.56  ? 19  ALA A O    1 
ATOM   5     C  CB   . ALA A 1 1   ? 27.703  -10.236 2.853   1.00 65.04  ? 19  ALA A CB   1 
ATOM   6     H  HA   . ALA A 1 1   ? 28.482  -11.036 4.554   1.00 185.06 ? 19  ALA A HA   1 
ATOM   7     H  HB1  . ALA A 1 1   ? 27.524  -9.421  3.348   1.00 78.05  ? 19  ALA A HB1  1 
ATOM   8     H  HB2  . ALA A 1 1   ? 28.502  -10.127 2.313   1.00 78.05  ? 19  ALA A HB2  1 
ATOM   9     H  HB3  . ALA A 1 1   ? 26.947  -10.452 2.286   1.00 78.05  ? 19  ALA A HB3  1 
ATOM   10    N  N    . THR A 1 2   ? 25.719  -10.881 4.725   1.00 95.37  ? 20  THR A N    1 
ATOM   11    C  CA   . THR A 1 2   ? 24.396  -11.233 5.216   1.00 131.00 ? 20  THR A CA   1 
ATOM   12    C  C    . THR A 1 2   ? 23.609  -11.927 4.106   1.00 153.31 ? 20  THR A C    1 
ATOM   13    O  O    . THR A 1 2   ? 23.705  -11.537 2.938   1.00 41.09  ? 20  THR A O    1 
ATOM   14    C  CB   . THR A 1 2   ? 23.649  -9.978  5.670   1.00 62.32  ? 20  THR A CB   1 
ATOM   15    O  OG1  . THR A 1 2   ? 23.443  -9.105  4.553   1.00 89.64  ? 20  THR A OG1  1 
ATOM   16    C  CG2  . THR A 1 2   ? 24.437  -9.241  6.748   1.00 66.08  ? 20  THR A CG2  1 
ATOM   17    H  H    . THR A 1 2   ? 25.867  -10.036 4.661   1.00 114.44 ? 20  THR A H    1 
ATOM   18    H  HA   . THR A 1 2   ? 24.473  -11.834 5.973   1.00 157.20 ? 20  THR A HA   1 
ATOM   19    H  HB   . THR A 1 2   ? 22.790  -10.235 6.041   1.00 74.79  ? 20  THR A HB   1 
ATOM   20    H  HG1  . THR A 1 2   ? 22.621  -8.965  4.445   1.00 107.57 ? 20  THR A HG1  1 
ATOM   21    H  HG21 . THR A 1 2   ? 23.839  -8.946  7.453   1.00 79.29  ? 20  THR A HG21 1 
ATOM   22    H  HG22 . THR A 1 2   ? 25.107  -9.829  7.130   1.00 79.29  ? 20  THR A HG22 1 
ATOM   23    H  HG23 . THR A 1 2   ? 24.878  -8.467  6.366   1.00 79.29  ? 20  THR A HG23 1 
ATOM   24    N  N    . PRO A 1 3   ? 22.838  -12.961 4.428   1.00 173.89 ? 21  PRO A N    1 
ATOM   25    C  CA   . PRO A 1 3   ? 22.027  -13.623 3.403   1.00 80.68  ? 21  PRO A CA   1 
ATOM   26    C  C    . PRO A 1 3   ? 20.752  -12.840 3.137   1.00 174.84 ? 21  PRO A C    1 
ATOM   27    O  O    . PRO A 1 3   ? 20.352  -11.970 3.911   1.00 33.70  ? 21  PRO A O    1 
ATOM   28    C  CB   . PRO A 1 3   ? 21.701  -14.974 4.046   1.00 40.97  ? 21  PRO A CB   1 
ATOM   29    C  CG   . PRO A 1 3   ? 21.597  -14.642 5.512   1.00 38.76  ? 21  PRO A CG   1 
ATOM   30    C  CD   . PRO A 1 3   ? 22.626  -13.553 5.765   1.00 44.93  ? 21  PRO A CD   1 
ATOM   31    H  HA   . PRO A 1 3   ? 22.523  -13.756 2.580   1.00 96.81  ? 21  PRO A HA   1 
ATOM   32    H  HB2  . PRO A 1 3   ? 20.862  -15.318 3.702   1.00 49.16  ? 21  PRO A HB2  1 
ATOM   33    H  HB3  . PRO A 1 3   ? 22.415  -15.609 3.878   1.00 49.16  ? 21  PRO A HB3  1 
ATOM   34    H  HG2  . PRO A 1 3   ? 20.703  -14.324 5.713   1.00 46.52  ? 21  PRO A HG2  1 
ATOM   35    H  HG3  . PRO A 1 3   ? 21.795  -15.431 6.041   1.00 46.52  ? 21  PRO A HG3  1 
ATOM   36    H  HD2  . PRO A 1 3   ? 22.280  -12.890 6.384   1.00 53.92  ? 21  PRO A HD2  1 
ATOM   37    H  HD3  . PRO A 1 3   ? 23.450  -13.930 6.109   1.00 53.92  ? 21  PRO A HD3  1 
ATOM   38    N  N    . LEU A 1 4   ? 20.111  -13.159 2.015   1.00 40.00  ? 22  LEU A N    1 
ATOM   39    C  CA   . LEU A 1 4   ? 18.796  -12.595 1.735   1.00 120.79 ? 22  LEU A CA   1 
ATOM   40    C  C    . LEU A 1 4   ? 17.758  -13.368 2.538   1.00 115.47 ? 22  LEU A C    1 
ATOM   41    O  O    . LEU A 1 4   ? 17.607  -14.583 2.368   1.00 43.63  ? 22  LEU A O    1 
ATOM   42    C  CB   . LEU A 1 4   ? 18.455  -12.638 0.249   1.00 46.23  ? 22  LEU A CB   1 
ATOM   43    C  CG   . LEU A 1 4   ? 17.399  -11.592 -0.141  1.00 45.45  ? 22  LEU A CG   1 
ATOM   44    C  CD1  . LEU A 1 4   ? 17.419  -11.324 -1.635  1.00 96.60  ? 22  LEU A CD1  1 
ATOM   45    C  CD2  . LEU A 1 4   ? 15.994  -11.997 0.295   1.00 67.04  ? 22  LEU A CD2  1 
ATOM   46    H  H    . LEU A 1 4   ? 20.412  -13.691 1.411   1.00 48.00  ? 22  LEU A H    1 
ATOM   47    H  HA   . LEU A 1 4   ? 18.795  -11.661 1.999   1.00 144.95 ? 22  LEU A HA   1 
ATOM   48    H  HB2  . LEU A 1 4   ? 19.259  -12.463 -0.265  1.00 55.47  ? 22  LEU A HB2  1 
ATOM   49    H  HB3  . LEU A 1 4   ? 18.107  -13.517 0.030   1.00 55.47  ? 22  LEU A HB3  1 
ATOM   50    H  HG   . LEU A 1 4   ? 17.624  -10.772 0.326   1.00 54.54  ? 22  LEU A HG   1 
ATOM   51    H  HD11 . LEU A 1 4   ? 16.761  -10.642 -1.843  1.00 115.92 ? 22  LEU A HD11 1 
ATOM   52    H  HD12 . LEU A 1 4   ? 18.304  -11.018 -1.889  1.00 115.92 ? 22  LEU A HD12 1 
ATOM   53    H  HD13 . LEU A 1 4   ? 17.205  -12.145 -2.106  1.00 115.92 ? 22  LEU A HD13 1 
ATOM   54    H  HD21 . LEU A 1 4   ? 15.358  -11.350 -0.049  1.00 80.44  ? 22  LEU A HD21 1 
ATOM   55    H  HD22 . LEU A 1 4   ? 15.795  -12.877 -0.060  1.00 80.44  ? 22  LEU A HD22 1 
ATOM   56    H  HD23 . LEU A 1 4   ? 15.957  -12.015 1.264   1.00 80.44  ? 22  LEU A HD23 1 
ATOM   57    N  N    . VAL A 1 5   ? 17.049  -12.660 3.414   1.00 41.13  ? 23  VAL A N    1 
ATOM   58    C  CA   . VAL A 1 5   ? 16.035  -13.237 4.286   1.00 105.33 ? 23  VAL A CA   1 
ATOM   59    C  C    . VAL A 1 5   ? 14.902  -12.230 4.365   1.00 89.50  ? 23  VAL A C    1 
ATOM   60    O  O    . VAL A 1 5   ? 15.093  -11.118 4.870   1.00 42.66  ? 23  VAL A O    1 
ATOM   61    C  CB   . VAL A 1 5   ? 16.588  -13.517 5.697   1.00 26.30  ? 23  VAL A CB   1 
ATOM   62    C  CG1  . VAL A 1 5   ? 15.491  -14.072 6.605   1.00 35.20  ? 23  VAL A CG1  1 
ATOM   63    C  CG2  . VAL A 1 5   ? 17.778  -14.470 5.622   1.00 28.61  ? 23  VAL A CG2  1 
ATOM   64    H  H    . VAL A 1 5   ? 17.142  -11.812 3.523   1.00 49.36  ? 23  VAL A H    1 
ATOM   65    H  HA   . VAL A 1 5   ? 15.703  -14.069 3.914   1.00 126.39 ? 23  VAL A HA   1 
ATOM   66    H  HB   . VAL A 1 5   ? 16.897  -12.685 6.088   1.00 31.56  ? 23  VAL A HB   1 
ATOM   67    H  HG11 . VAL A 1 5   ? 14.791  -14.458 6.055   1.00 42.24  ? 23  VAL A HG11 1 
ATOM   68    H  HG12 . VAL A 1 5   ? 15.872  -14.753 7.182   1.00 42.24  ? 23  VAL A HG12 1 
ATOM   69    H  HG13 . VAL A 1 5   ? 15.129  -13.349 7.141   1.00 42.24  ? 23  VAL A HG13 1 
ATOM   70    H  HG21 . VAL A 1 5   ? 18.100  -14.646 6.520   1.00 34.34  ? 23  VAL A HG21 1 
ATOM   71    H  HG22 . VAL A 1 5   ? 17.494  -15.298 5.205   1.00 34.34  ? 23  VAL A HG22 1 
ATOM   72    H  HG23 . VAL A 1 5   ? 18.480  -14.058 5.094   1.00 34.34  ? 23  VAL A HG23 1 
ATOM   73    N  N    . LYS A 1 6   ? 13.733  -12.596 3.852   1.00 36.96  ? 24  LYS A N    1 
ATOM   74    C  CA   . LYS A 1 6   ? 12.593  -11.696 3.946   1.00 43.73  ? 24  LYS A CA   1 
ATOM   75    C  C    . LYS A 1 6   ? 12.214  -11.529 5.411   1.00 39.92  ? 24  LYS A C    1 
ATOM   76    O  O    . LYS A 1 6   ? 11.888  -12.504 6.102   1.00 65.22  ? 24  LYS A O    1 
ATOM   77    C  CB   . LYS A 1 6   ? 11.412  -12.214 3.126   1.00 52.62  ? 24  LYS A CB   1 
ATOM   78    C  CG   . LYS A 1 6   ? 11.323  -11.598 1.719   1.00 88.31  ? 24  LYS A CG   1 
ATOM   79    C  CD   . LYS A 1 6   ? 9.885   -11.449 1.204   1.00 90.64  ? 24  LYS A CD   1 
ATOM   80    C  CE   . LYS A 1 6   ? 9.871   -10.647 -0.097  1.00 88.46  ? 24  LYS A CE   1 
ATOM   81    N  NZ   . LYS A 1 6   ? 8.781   -9.644  -0.155  1.00 52.97  ? 24  LYS A NZ   1 
ATOM   82    H  H    . LYS A 1 6   ? 13.579  -13.342 3.454   1.00 44.35  ? 24  LYS A H    1 
ATOM   83    H  HA   . LYS A 1 6   ? 12.828  -10.831 3.574   1.00 52.47  ? 24  LYS A HA   1 
ATOM   84    H  HB2  . LYS A 1 6   ? 11.500  -13.174 3.025   1.00 63.15  ? 24  LYS A HB2  1 
ATOM   85    H  HB3  . LYS A 1 6   ? 10.590  -12.003 3.596   1.00 63.15  ? 24  LYS A HB3  1 
ATOM   86    H  HG2  . LYS A 1 6   ? 11.724  -10.715 1.738   1.00 105.97 ? 24  LYS A HG2  1 
ATOM   87    H  HG3  . LYS A 1 6   ? 11.803  -12.167 1.097   1.00 105.97 ? 24  LYS A HG3  1 
ATOM   88    H  HD2  . LYS A 1 6   ? 9.507   -12.326 1.032   1.00 108.77 ? 24  LYS A HD2  1 
ATOM   89    H  HD3  . LYS A 1 6   ? 9.349   -10.980 1.863   1.00 108.77 ? 24  LYS A HD3  1 
ATOM   90    H  HE2  . LYS A 1 6   ? 10.714  -10.175 -0.185  1.00 106.15 ? 24  LYS A HE2  1 
ATOM   91    H  HE3  . LYS A 1 6   ? 9.753   -11.257 -0.841  1.00 106.15 ? 24  LYS A HE3  1 
ATOM   92    H  HZ1  . LYS A 1 6   ? 7.990   -10.051 -0.121  1.00 63.57  ? 24  LYS A HZ1  1 
ATOM   93    H  HZ2  . LYS A 1 6   ? 8.835   -9.179  -0.912  1.00 63.57  ? 24  LYS A HZ2  1 
ATOM   94    H  HZ3  . LYS A 1 6   ? 8.847   -9.084  0.534   1.00 63.57  ? 24  LYS A HZ3  1 
ATOM   95    N  N    . ARG A 1 7   ? 12.277  -10.287 5.884   1.00 59.62  ? 25  ARG A N    1 
ATOM   96    C  CA   . ARG A 1 7   ? 12.101  -9.990  7.295   1.00 79.23  ? 25  ARG A CA   1 
ATOM   97    C  C    . ARG A 1 7   ? 10.661  -10.136 7.758   1.00 63.59  ? 25  ARG A C    1 
ATOM   98    O  O    . ARG A 1 7   ? 10.430  -10.151 8.971   1.00 62.61  ? 25  ARG A O    1 
ATOM   99    C  CB   . ARG A 1 7   ? 12.590  -8.566  7.580   1.00 114.53 ? 25  ARG A CB   1 
ATOM   100   C  CG   . ARG A 1 7   ? 11.901  -7.490  6.743   1.00 119.21 ? 25  ARG A CG   1 
ATOM   101   C  CD   . ARG A 1 7   ? 12.873  -6.413  6.277   1.00 94.62  ? 25  ARG A CD   1 
ATOM   102   N  NE   . ARG A 1 7   ? 13.323  -5.568  7.381   1.00 151.43 ? 25  ARG A NE   1 
ATOM   103   C  CZ   . ARG A 1 7   ? 13.654  -4.284  7.262   1.00 112.77 ? 25  ARG A CZ   1 
ATOM   104   N  NH1  . ARG A 1 7   ? 14.054  -3.602  8.329   1.00 47.41  ? 25  ARG A NH1  1 
ATOM   105   N  NH2  . ARG A 1 7   ? 13.585  -3.680  6.084   1.00 52.26  ? 25  ARG A NH2  1 
ATOM   106   H  H    . ARG A 1 7   ? 12.422  -9.592  5.399   1.00 71.54  ? 25  ARG A H    1 
ATOM   107   H  HA   . ARG A 1 7   ? 12.638  -10.610 7.813   1.00 95.08  ? 25  ARG A HA   1 
ATOM   108   H  HB2  . ARG A 1 7   ? 12.426  -8.363  8.514   1.00 137.43 ? 25  ARG A HB2  1 
ATOM   109   H  HB3  . ARG A 1 7   ? 13.541  -8.521  7.393   1.00 137.43 ? 25  ARG A HB3  1 
ATOM   110   H  HG2  . ARG A 1 7   ? 11.507  -7.901  5.958   1.00 143.06 ? 25  ARG A HG2  1 
ATOM   111   H  HG3  . ARG A 1 7   ? 11.212  -7.064  7.277   1.00 143.06 ? 25  ARG A HG3  1 
ATOM   112   H  HD2  . ARG A 1 7   ? 13.652  -6.835  5.882   1.00 113.54 ? 25  ARG A HD2  1 
ATOM   113   H  HD3  . ARG A 1 7   ? 12.434  -5.848  5.623   1.00 113.54 ? 25  ARG A HD3  1 
ATOM   114   H  HE   . ARG A 1 7   ? 13.378  -5.925  8.161   1.00 181.72 ? 25  ARG A HE   1 
ATOM   115   H  HH11 . ARG A 1 7   ? 14.098  -3.990  9.095   1.00 56.89  ? 25  ARG A HH11 1 
ATOM   116   H  HH12 . ARG A 1 7   ? 14.268  -2.773  8.253   1.00 56.89  ? 25  ARG A HH12 1 
ATOM   117   H  HH21 . ARG A 1 7   ? 13.325  -4.118  5.391   1.00 62.72  ? 25  ARG A HH21 1 
ATOM   118   H  HH22 . ARG A 1 7   ? 13.800  -2.851  6.013   1.00 62.72  ? 25  ARG A HH22 1 
ATOM   119   N  N    . LEU A 1 8   ? 9.701   -10.251 6.845   1.00 48.86  ? 26  LEU A N    1 
ATOM   120   C  CA   . LEU A 1 8   ? 8.297   -10.201 7.222   1.00 35.29  ? 26  LEU A CA   1 
ATOM   121   C  C    . LEU A 1 8   ? 7.487   -11.059 6.269   1.00 27.89  ? 26  LEU A C    1 
ATOM   122   O  O    . LEU A 1 8   ? 7.905   -11.298 5.131   1.00 25.68  ? 26  LEU A O    1 
ATOM   123   C  CB   . LEU A 1 8   ? 7.759   -8.767  7.156   1.00 31.76  ? 26  LEU A CB   1 
ATOM   124   C  CG   . LEU A 1 8   ? 8.402   -7.748  8.091   1.00 30.08  ? 26  LEU A CG   1 
ATOM   125   C  CD1  . LEU A 1 8   ? 7.960   -6.351  7.683   1.00 29.69  ? 26  LEU A CD1  1 
ATOM   126   C  CD2  . LEU A 1 8   ? 8.042   -8.048  9.537   1.00 28.84  ? 26  LEU A CD2  1 
ATOM   127   H  H    . LEU A 1 8   ? 9.839   -10.358 6.003   1.00 58.64  ? 26  LEU A H    1 
ATOM   128   H  HA   . LEU A 1 8   ? 8.207   -10.555 8.121   1.00 42.35  ? 26  LEU A HA   1 
ATOM   129   H  HB2  . LEU A 1 8   ? 7.886   -8.441  6.251   1.00 38.11  ? 26  LEU A HB2  1 
ATOM   130   H  HB3  . LEU A 1 8   ? 6.814   -8.792  7.370   1.00 38.11  ? 26  LEU A HB3  1 
ATOM   131   H  HG   . LEU A 1 8   ? 9.369   -7.796  8.027   1.00 36.09  ? 26  LEU A HG   1 
ATOM   132   H  HD11 . LEU A 1 8   ? 7.025   -6.236  7.914   1.00 35.63  ? 26  LEU A HD11 1 
ATOM   133   H  HD12 . LEU A 1 8   ? 8.500   -5.699  8.156   1.00 35.63  ? 26  LEU A HD12 1 
ATOM   134   H  HD13 . LEU A 1 8   ? 8.080   -6.249  6.726   1.00 35.63  ? 26  LEU A HD13 1 
ATOM   135   H  HD21 . LEU A 1 8   ? 8.409   -8.912  9.782   1.00 34.61  ? 26  LEU A HD21 1 
ATOM   136   H  HD22 . LEU A 1 8   ? 8.415   -7.356  10.106  1.00 34.61  ? 26  LEU A HD22 1 
ATOM   137   H  HD23 . LEU A 1 8   ? 7.076   -8.062  9.625   1.00 34.61  ? 26  LEU A HD23 1 
ATOM   138   N  N    . PRO A 1 9   ? 6.301   -11.499 6.689   1.00 23.40  ? 27  PRO A N    1 
ATOM   139   C  CA   . PRO A 1 9   ? 5.361   -12.111 5.744   1.00 23.06  ? 27  PRO A CA   1 
ATOM   140   C  C    . PRO A 1 9   ? 5.125   -11.223 4.530   1.00 22.08  ? 27  PRO A C    1 
ATOM   141   O  O    . PRO A 1 9   ? 5.180   -9.994  4.611   1.00 21.02  ? 27  PRO A O    1 
ATOM   142   C  CB   . PRO A 1 9   ? 4.084   -12.273 6.579   1.00 22.46  ? 27  PRO A CB   1 
ATOM   143   C  CG   . PRO A 1 9   ? 4.594   -12.424 7.987   1.00 22.24  ? 27  PRO A CG   1 
ATOM   144   C  CD   . PRO A 1 9   ? 5.768   -11.482 8.065   1.00 23.34  ? 27  PRO A CD   1 
ATOM   145   H  HA   . PRO A 1 9   ? 5.682   -12.979 5.453   1.00 27.67  ? 27  PRO A HA   1 
ATOM   146   H  HB2  . PRO A 1 9   ? 3.523   -11.486 6.490   1.00 26.95  ? 27  PRO A HB2  1 
ATOM   147   H  HB3  . PRO A 1 9   ? 3.595   -13.062 6.295   1.00 26.95  ? 27  PRO A HB3  1 
ATOM   148   H  HG2  . PRO A 1 9   ? 3.903   -12.174 8.620   1.00 26.69  ? 27  PRO A HG2  1 
ATOM   149   H  HG3  . PRO A 1 9   ? 4.872   -13.341 8.144   1.00 26.69  ? 27  PRO A HG3  1 
ATOM   150   H  HD2  . PRO A 1 9   ? 5.479   -10.590 8.314   1.00 28.01  ? 27  PRO A HD2  1 
ATOM   151   H  HD3  . PRO A 1 9   ? 6.429   -11.805 8.696   1.00 28.01  ? 27  PRO A HD3  1 
ATOM   152   N  N    . SER A 1 10  ? 4.852   -11.870 3.398   1.00 23.75  ? 28  SER A N    1 
ATOM   153   C  CA   . SER A 1 10  ? 4.685   -11.209 2.116   1.00 26.02  ? 28  SER A CA   1 
ATOM   154   C  C    . SER A 1 10  ? 3.409   -11.711 1.452   1.00 27.24  ? 28  SER A C    1 
ATOM   155   O  O    . SER A 1 10  ? 2.750   -12.639 1.929   1.00 28.48  ? 28  SER A O    1 
ATOM   156   C  CB   . SER A 1 10  ? 5.875   -11.501 1.192   1.00 28.32  ? 28  SER A CB   1 
ATOM   157   O  OG   . SER A 1 10  ? 6.030   -12.900 1.007   1.00 30.16  ? 28  SER A OG   1 
ATOM   158   H  H    . SER A 1 10  ? 4.756   -12.723 3.351   1.00 28.49  ? 28  SER A H    1 
ATOM   159   H  HA   . SER A 1 10  ? 4.612   -10.252 2.258   1.00 31.22  ? 28  SER A HA   1 
ATOM   160   H  HB2  . SER A 1 10  ? 5.718   -11.082 0.331   1.00 33.99  ? 28  SER A HB2  1 
ATOM   161   H  HB3  . SER A 1 10  ? 6.683   -11.142 1.592   1.00 33.99  ? 28  SER A HB3  1 
ATOM   162   H  HG   . SER A 1 10  ? 6.675   -13.051 0.490   1.00 36.19  ? 28  SER A HG   1 
ATOM   163   N  N    . GLY A 1 11  ? 3.068   -11.092 0.332   1.00 27.73  ? 29  GLY A N    1 
ATOM   164   C  CA   . GLY A 1 11  ? 1.953   -11.555 -0.463  1.00 28.12  ? 29  GLY A CA   1 
ATOM   165   C  C    . GLY A 1 11  ? 0.642   -10.887 -0.094  1.00 28.08  ? 29  GLY A C    1 
ATOM   166   O  O    . GLY A 1 11  ? 0.586   -9.800  0.489   1.00 29.38  ? 29  GLY A O    1 
ATOM   167   H  H    . GLY A 1 11  ? 3.470   -10.402 0.014   1.00 33.28  ? 29  GLY A H    1 
ATOM   168   H  HA2  . GLY A 1 11  ? 2.132   -11.373 -1.399  1.00 33.74  ? 29  GLY A HA2  1 
ATOM   169   H  HA3  . GLY A 1 11  ? 1.850   -12.511 -0.341  1.00 33.74  ? 29  GLY A HA3  1 
ATOM   170   N  N    . SER A 1 12  ? -0.438  -11.574 -0.449  1.00 27.93  ? 30  SER A N    1 
ATOM   171   C  CA   A SER A 1 12  ? -1.772  -11.043 -0.228  0.56 27.80  ? 30  SER A CA   1 
ATOM   172   C  CA   B SER A 1 12  ? -1.772  -11.042 -0.227  0.44 27.56  ? 30  SER A CA   1 
ATOM   173   C  C    . SER A 1 12  ? -2.118  -11.048 1.259   1.00 26.30  ? 30  SER A C    1 
ATOM   174   O  O    . SER A 1 12  ? -1.584  -11.831 2.051   1.00 26.04  ? 30  SER A O    1 
ATOM   175   C  CB   A SER A 1 12  ? -2.807  -11.881 -0.982  0.56 28.99  ? 30  SER A CB   1 
ATOM   176   C  CB   B SER A 1 12  ? -2.803  -11.880 -0.980  0.44 28.37  ? 30  SER A CB   1 
ATOM   177   O  OG   A SER A 1 12  ? -2.522  -11.938 -2.371  0.56 29.91  ? 30  SER A OG   1 
ATOM   178   O  OG   B SER A 1 12  ? -2.734  -13.238 -0.584  0.44 28.90  ? 30  SER A OG   1 
ATOM   179   H  H    . SER A 1 12  ? -0.426  -12.350 -0.819  1.00 33.51  ? 30  SER A H    1 
ATOM   180   H  HA   . SER A 1 12  ? -1.808  -10.130 -0.553  1.00 33.08  ? 30  SER A HA   1 
ATOM   181   H  HB2  A SER A 1 12  ? -2.799  -12.783 -0.625  0.56 34.79  ? 30  SER A HB2  1 
ATOM   182   H  HB2  B SER A 1 12  ? -3.690  -11.538 -0.786  0.44 34.04  ? 30  SER A HB2  1 
ATOM   183   H  HB3  A SER A 1 12  ? -3.682  -11.483 -0.858  0.56 34.79  ? 30  SER A HB3  1 
ATOM   184   H  HB3  B SER A 1 12  ? -2.626  -11.819 -1.932  0.44 34.04  ? 30  SER A HB3  1 
ATOM   185   H  HG   A SER A 1 12  ? -2.545  -11.166 -2.701  0.56 35.89  ? 30  SER A HG   1 
ATOM   186   H  HG   B SER A 1 12  ? -1.981  -13.556 -0.778  0.44 34.68  ? 30  SER A HG   1 
ATOM   187   N  N    . ASP A 1 13  ? -3.033  -10.159 1.629   1.00 24.36  ? 31  ASP A N    1 
ATOM   188   C  CA   . ASP A 1 13  ? -3.490  -10.108 3.005   1.00 21.86  ? 31  ASP A CA   1 
ATOM   189   C  C    . ASP A 1 13  ? -4.287  -11.371 3.318   1.00 21.71  ? 31  ASP A C    1 
ATOM   190   O  O    . ASP A 1 13  ? -5.029  -11.865 2.460   1.00 23.24  ? 31  ASP A O    1 
ATOM   191   C  CB   . ASP A 1 13  ? -4.417  -8.914  3.210   1.00 23.01  ? 31  ASP A CB   1 
ATOM   192   C  CG   . ASP A 1 13  ? -3.678  -7.601  3.351   1.00 23.31  ? 31  ASP A CG   1 
ATOM   193   O  OD1  . ASP A 1 13  ? -2.448  -7.547  3.140   1.00 23.60  ? 31  ASP A OD1  1 
ATOM   194   O  OD2  . ASP A 1 13  ? -4.357  -6.610  3.681   1.00 25.68  ? 31  ASP A OD2  1 
ATOM   195   H  H    . ASP A 1 13  ? -3.398  -9.582  1.107   1.00 29.24  ? 31  ASP A H    1 
ATOM   196   H  HA   . ASP A 1 13  ? -2.726  -10.035 3.597   1.00 26.24  ? 31  ASP A HA   1 
ATOM   197   H  HB2  . ASP A 1 13  ? -5.009  -8.841  2.445   1.00 27.61  ? 31  ASP A HB2  1 
ATOM   198   H  HB3  . ASP A 1 13  ? -4.934  -9.053  4.018   1.00 27.61  ? 31  ASP A HB3  1 
ATOM   199   N  N    . PRO A 1 14  ? -4.166  -11.912 4.527   1.00 21.44  ? 32  PRO A N    1 
ATOM   200   C  CA   . PRO A 1 14  ? -5.079  -12.985 4.936   1.00 22.00  ? 32  PRO A CA   1 
ATOM   201   C  C    . PRO A 1 14  ? -6.519  -12.492 4.930   1.00 22.01  ? 32  PRO A C    1 
ATOM   202   O  O    . PRO A 1 14  ? -6.794  -11.301 5.097   1.00 21.36  ? 32  PRO A O    1 
ATOM   203   C  CB   . PRO A 1 14  ? -4.611  -13.333 6.355   1.00 22.93  ? 32  PRO A CB   1 
ATOM   204   C  CG   . PRO A 1 14  ? -3.201  -12.815 6.440   1.00 22.30  ? 32  PRO A CG   1 
ATOM   205   C  CD   . PRO A 1 14  ? -3.146  -11.614 5.552   1.00 21.05  ? 32  PRO A CD   1 
ATOM   206   H  HA   . PRO A 1 14  ? -4.987  -13.764 4.365   1.00 26.40  ? 32  PRO A HA   1 
ATOM   207   H  HB2  . PRO A 1 14  ? -5.181  -12.896 7.007   1.00 27.52  ? 32  PRO A HB2  1 
ATOM   208   H  HB3  . PRO A 1 14  ? -4.636  -14.294 6.485   1.00 27.52  ? 32  PRO A HB3  1 
ATOM   209   H  HG2  . PRO A 1 14  ? -2.997  -12.573 7.357   1.00 26.76  ? 32  PRO A HG2  1 
ATOM   210   H  HG3  . PRO A 1 14  ? -2.584  -13.497 6.132   1.00 26.76  ? 32  PRO A HG3  1 
ATOM   211   H  HD2  . PRO A 1 14  ? -3.374  -10.809 6.043   1.00 25.25  ? 32  PRO A HD2  1 
ATOM   212   H  HD3  . PRO A 1 14  ? -2.269  -11.521 5.150   1.00 25.25  ? 32  PRO A HD3  1 
ATOM   213   N  N    . ALA A 1 15  ? -7.444  -13.426 4.728   1.00 22.58  ? 33  ALA A N    1 
ATOM   214   C  CA   . ALA A 1 15  ? -8.856  -13.091 4.781   1.00 23.57  ? 33  ALA A CA   1 
ATOM   215   C  C    . ALA A 1 15  ? -9.249  -12.700 6.200   1.00 24.18  ? 33  ALA A C    1 
ATOM   216   O  O    . ALA A 1 15  ? -8.647  -13.145 7.183   1.00 25.90  ? 33  ALA A O    1 
ATOM   217   C  CB   . ALA A 1 15  ? -9.704  -14.282 4.327   1.00 25.27  ? 33  ALA A CB   1 
ATOM   218   H  H    . ALA A 1 15  ? -7.278  -14.253 4.561   1.00 27.10  ? 33  ALA A H    1 
ATOM   219   H  HA   . ALA A 1 15  ? -9.036  -12.344 4.188   1.00 28.29  ? 33  ALA A HA   1 
ATOM   220   H  HB1  . ALA A 1 15  ? -9.455  -14.519 3.419   1.00 30.33  ? 33  ALA A HB1  1 
ATOM   221   H  HB2  . ALA A 1 15  ? -9.541  -15.031 4.921   1.00 30.33  ? 33  ALA A HB2  1 
ATOM   222   H  HB3  . ALA A 1 15  ? -10.641 -14.033 4.358   1.00 30.33  ? 33  ALA A HB3  1 
ATOM   223   N  N    . PHE A 1 16  ? -10.263 -11.848 6.293   1.00 23.78  ? 34  PHE A N    1 
ATOM   224   C  CA   . PHE A 1 16  ? -10.849 -11.494 7.571   1.00 22.88  ? 34  PHE A CA   1 
ATOM   225   C  C    . PHE A 1 16  ? -11.877 -12.547 7.979   1.00 23.73  ? 34  PHE A C    1 
ATOM   226   O  O    . PHE A 1 16  ? -12.587 -13.115 7.139   1.00 25.69  ? 34  PHE A O    1 
ATOM   227   C  CB   . PHE A 1 16  ? -11.586 -10.156 7.471   1.00 23.86  ? 34  PHE A CB   1 
ATOM   228   C  CG   . PHE A 1 16  ? -10.694 -8.949  7.274   1.00 23.83  ? 34  PHE A CG   1 
ATOM   229   C  CD1  . PHE A 1 16  ? -9.464  -8.843  7.905   1.00 23.74  ? 34  PHE A CD1  1 
ATOM   230   C  CD2  . PHE A 1 16  ? -11.119 -7.900  6.472   1.00 23.57  ? 34  PHE A CD2  1 
ATOM   231   C  CE1  . PHE A 1 16  ? -8.669  -7.718  7.727   1.00 23.92  ? 34  PHE A CE1  1 
ATOM   232   C  CE2  . PHE A 1 16  ? -10.330 -6.768  6.292   1.00 23.24  ? 34  PHE A CE2  1 
ATOM   233   C  CZ   . PHE A 1 16  ? -9.102  -6.681  6.916   1.00 23.57  ? 34  PHE A CZ   1 
ATOM   234   H  H    . PHE A 1 16  ? -10.632 -11.459 5.621   1.00 28.54  ? 34  PHE A H    1 
ATOM   235   H  HA   . PHE A 1 16  ? -10.145 -11.431 8.236   1.00 27.46  ? 34  PHE A HA   1 
ATOM   236   H  HB2  . PHE A 1 16  ? -12.192 -10.196 6.715   1.00 28.64  ? 34  PHE A HB2  1 
ATOM   237   H  HB3  . PHE A 1 16  ? -12.085 -10.019 8.291   1.00 28.64  ? 34  PHE A HB3  1 
ATOM   238   H  HD1  . PHE A 1 16  ? -9.168  -9.534  8.452   1.00 28.49  ? 34  PHE A HD1  1 
ATOM   239   H  HD2  . PHE A 1 16  ? -11.945 -7.954  6.048   1.00 28.29  ? 34  PHE A HD2  1 
ATOM   240   H  HE1  . PHE A 1 16  ? -7.845  -7.661  8.154   1.00 28.71  ? 34  PHE A HE1  1 
ATOM   241   H  HE2  . PHE A 1 16  ? -10.629 -6.073  5.753   1.00 27.88  ? 34  PHE A HE2  1 
ATOM   242   H  HZ   . PHE A 1 16  ? -8.568  -5.930  6.793   1.00 28.29  ? 34  PHE A HZ   1 
ATOM   243   N  N    . SER A 1 17  ? -11.961 -12.792 9.288   1.00 22.37  ? 35  SER A N    1 
ATOM   244   C  CA   . SER A 1 17  ? -13.026 -13.608 9.856   1.00 22.49  ? 35  SER A CA   1 
ATOM   245   C  C    . SER A 1 17  ? -14.334 -12.840 9.975   1.00 23.90  ? 35  SER A C    1 
ATOM   246   O  O    . SER A 1 17  ? -15.408 -13.458 9.980   1.00 25.60  ? 35  SER A O    1 
ATOM   247   C  CB   . SER A 1 17  ? -12.596 -14.128 11.231  1.00 21.40  ? 35  SER A CB   1 
ATOM   248   O  OG   . SER A 1 17  ? -12.470 -13.097 12.190  1.00 21.81  ? 35  SER A OG   1 
ATOM   249   H  H    . SER A 1 17  ? -11.406 -12.491 9.872   1.00 26.84  ? 35  SER A H    1 
ATOM   250   H  HA   . SER A 1 17  ? -13.185 -14.376 9.285   1.00 26.99  ? 35  SER A HA   1 
ATOM   251   H  HB2  . SER A 1 17  ? -13.262 -14.761 11.543  1.00 25.68  ? 35  SER A HB2  1 
ATOM   252   H  HB3  . SER A 1 17  ? -11.737 -14.570 11.138  1.00 25.68  ? 35  SER A HB3  1 
ATOM   253   H  HG   . SER A 1 17  ? -12.395 -13.427 12.959  1.00 26.17  ? 35  SER A HG   1 
ATOM   254   N  N    . GLN A 1 18  ? -14.270 -11.485 10.046  1.00 24.75  ? 36  GLN A N    1 
ATOM   255   C  CA   . GLN A 1 18  ? -15.457 -10.660 10.170  1.00 26.74  ? 36  GLN A CA   1 
ATOM   256   C  C    . GLN A 1 18  ? -15.783 -9.992  8.840   1.00 27.66  ? 36  GLN A C    1 
ATOM   257   O  O    . GLN A 1 18  ? -14.876 -9.624  8.087   1.00 28.68  ? 36  GLN A O    1 
ATOM   258   C  CB   . GLN A 1 18  ? -15.215 -9.561  11.210  1.00 27.92  ? 36  GLN A CB   1 
ATOM   259   C  CG   . GLN A 1 18  ? -15.011 -10.071 12.627  1.00 31.14  ? 36  GLN A CG   1 
ATOM   260   C  CD   . GLN A 1 18  ? -16.301 -10.583 13.242  1.00 35.16  ? 36  GLN A CD   1 
ATOM   261   O  OE1  . GLN A 1 18  ? -17.231 -10.975 12.532  1.00 38.79  ? 36  GLN A OE1  1 
ATOM   262   N  NE2  . GLN A 1 18  ? -16.363 -10.584 14.567  1.00 35.15  ? 36  GLN A NE2  1 
ATOM   263   H  H    . GLN A 1 18  ? -13.537 -11.035 10.024  1.00 29.70  ? 36  GLN A H    1 
ATOM   264   H  HA   . GLN A 1 18  ? -16.212 -11.204 10.444  1.00 32.09  ? 36  GLN A HA   1 
ATOM   265   H  HB2  . GLN A 1 18  ? -14.419 -9.068  10.959  1.00 33.51  ? 36  GLN A HB2  1 
ATOM   266   H  HB3  . GLN A 1 18  ? -15.984 -8.970  11.219  1.00 33.51  ? 36  GLN A HB3  1 
ATOM   267   H  HG2  . GLN A 1 18  ? -14.372 -10.800 12.614  1.00 37.37  ? 36  GLN A HG2  1 
ATOM   268   H  HG3  . GLN A 1 18  ? -14.678 -9.348  13.181  1.00 37.37  ? 36  GLN A HG3  1 
ATOM   269   H  HE21 . GLN A 1 18  ? -15.694 -10.304 15.029  1.00 42.18  ? 36  GLN A HE21 1 
ATOM   270   H  HE22 . GLN A 1 18  ? -17.073 -10.865 14.963  1.00 42.18  ? 36  GLN A HE22 1 
ATOM   271   N  N    . PRO A 1 19  ? -17.065 -9.802  8.532   1.00 30.21  ? 37  PRO A N    1 
ATOM   272   C  CA   . PRO A 1 19  ? -17.429 -9.089  7.303   1.00 30.18  ? 37  PRO A CA   1 
ATOM   273   C  C    . PRO A 1 19  ? -17.061 -7.618  7.386   1.00 29.66  ? 37  PRO A C    1 
ATOM   274   O  O    . PRO A 1 19  ? -16.918 -7.040  8.466   1.00 29.18  ? 37  PRO A O    1 
ATOM   275   C  CB   . PRO A 1 19  ? -18.953 -9.251  7.221   1.00 31.18  ? 37  PRO A CB   1 
ATOM   276   C  CG   . PRO A 1 19  ? -19.319 -10.253 8.260   1.00 32.72  ? 37  PRO A CG   1 
ATOM   277   C  CD   . PRO A 1 19  ? -18.251 -10.212 9.300   1.00 31.62  ? 37  PRO A CD   1 
ATOM   278   H  HA   . PRO A 1 19  ? -17.008 -9.502  6.534   1.00 36.22  ? 37  PRO A HA   1 
ATOM   279   H  HB2  . PRO A 1 19  ? -19.381 -8.399  7.400   1.00 37.42  ? 37  PRO A HB2  1 
ATOM   280   H  HB3  . PRO A 1 19  ? -19.200 -9.567  6.338   1.00 37.42  ? 37  PRO A HB3  1 
ATOM   281   H  HG2  . PRO A 1 19  ? -20.177 -10.018 8.646   1.00 39.26  ? 37  PRO A HG2  1 
ATOM   282   H  HG3  . PRO A 1 19  ? -19.366 -11.133 7.856   1.00 39.26  ? 37  PRO A HG3  1 
ATOM   283   H  HD2  . PRO A 1 19  ? -18.461 -9.562  9.989   1.00 37.94  ? 37  PRO A HD2  1 
ATOM   284   H  HD3  . PRO A 1 19  ? -18.121 -11.087 9.699   1.00 37.94  ? 37  PRO A HD3  1 
ATOM   285   N  N    . LYS A 1 20  ? -16.923 -7.008  6.208   1.00 30.03  ? 38  LYS A N    1 
ATOM   286   C  CA   . LYS A 1 20  ? -16.585 -5.590  6.147   1.00 30.16  ? 38  LYS A CA   1 
ATOM   287   C  C    . LYS A 1 20  ? -17.563 -4.751  6.961   1.00 29.79  ? 38  LYS A C    1 
ATOM   288   O  O    . LYS A 1 20  ? -17.151 -3.847  7.694   1.00 29.43  ? 38  LYS A O    1 
ATOM   289   C  CB   . LYS A 1 20  ? -16.554 -5.125  4.690   1.00 32.60  ? 38  LYS A CB   1 
ATOM   290   C  CG   . LYS A 1 20  ? -16.043 -3.699  4.489   1.00 33.81  ? 38  LYS A CG   1 
ATOM   291   C  CD   . LYS A 1 20  ? -16.045 -3.316  3.012   1.00 34.99  ? 38  LYS A CD   1 
ATOM   292   C  CE   . LYS A 1 20  ? -15.531 -1.901  2.801   1.00 36.42  ? 38  LYS A CE   1 
ATOM   293   N  NZ   . LYS A 1 20  ? -16.479 -0.882  3.335   1.00 37.93  ? 38  LYS A NZ   1 
ATOM   294   H  H    . LYS A 1 20  ? -17.018 -7.387  5.442   1.00 36.04  ? 38  LYS A H    1 
ATOM   295   H  HA   . LYS A 1 20  ? -15.699 -5.460  6.522   1.00 36.19  ? 38  LYS A HA   1 
ATOM   296   H  HB2  . LYS A 1 20  ? -15.973 -5.717  4.188   1.00 39.12  ? 38  LYS A HB2  1 
ATOM   297   H  HB3  . LYS A 1 20  ? -17.456 -5.165  4.334   1.00 39.12  ? 38  LYS A HB3  1 
ATOM   298   H  HG2  . LYS A 1 20  ? -16.616 -3.080  4.967   1.00 40.57  ? 38  LYS A HG2  1 
ATOM   299   H  HG3  . LYS A 1 20  ? -15.134 -3.633  4.821   1.00 40.57  ? 38  LYS A HG3  1 
ATOM   300   H  HD2  . LYS A 1 20  ? -15.471 -3.925  2.522   1.00 41.99  ? 38  LYS A HD2  1 
ATOM   301   H  HD3  . LYS A 1 20  ? -16.951 -3.365  2.669   1.00 41.99  ? 38  LYS A HD3  1 
ATOM   302   H  HE2  . LYS A 1 20  ? -14.683 -1.797  3.260   1.00 43.71  ? 38  LYS A HE2  1 
ATOM   303   H  HE3  . LYS A 1 20  ? -15.416 -1.741  1.851   1.00 43.71  ? 38  LYS A HE3  1 
ATOM   304   H  HZ1  . LYS A 1 20  ? -17.274 -0.971  2.944   1.00 45.52  ? 38  LYS A HZ1  1 
ATOM   305   H  HZ2  . LYS A 1 20  ? -16.576 -0.986  4.213   1.00 45.52  ? 38  LYS A HZ2  1 
ATOM   306   H  HZ3  . LYS A 1 20  ? -16.168 -0.063  3.174   1.00 45.52  ? 38  LYS A HZ3  1 
ATOM   307   N  N    . SER A 1 21  ? -18.866 -5.040  6.855   1.00 28.47  ? 39  SER A N    1 
ATOM   308   C  CA   . SER A 1 21  ? -19.861 -4.210  7.533   1.00 27.78  ? 39  SER A CA   1 
ATOM   309   C  C    . SER A 1 21  ? -19.656 -4.219  9.046   1.00 27.02  ? 39  SER A C    1 
ATOM   310   O  O    . SER A 1 21  ? -19.844 -3.193  9.715   1.00 27.05  ? 39  SER A O    1 
ATOM   311   C  CB   . SER A 1 21  ? -21.276 -4.659  7.152   1.00 29.63  ? 39  SER A CB   1 
ATOM   312   O  OG   . SER A 1 21  ? -21.664 -5.836  7.843   1.00 32.80  ? 39  SER A OG   1 
ATOM   313   H  H    . SER A 1 21  ? -19.190 -5.698  6.406   1.00 34.16  ? 39  SER A H    1 
ATOM   314   H  HA   . SER A 1 21  ? -19.762 -3.293  7.234   1.00 33.34  ? 39  SER A HA   1 
ATOM   315   H  HB2  . SER A 1 21  ? -21.898 -3.948  7.374   1.00 35.56  ? 39  SER A HB2  1 
ATOM   316   H  HB3  . SER A 1 21  ? -21.301 -4.835  6.199   1.00 35.56  ? 39  SER A HB3  1 
ATOM   317   H  HG   . SER A 1 21  ? -22.480 -5.990  7.712   1.00 39.36  ? 39  SER A HG   1 
ATOM   318   N  N    . VAL A 1 22  ? -19.244 -5.359  9.600   1.00 27.11  ? 40  VAL A N    1 
ATOM   319   C  CA   . VAL A 1 22  ? -19.000 -5.439  11.034  1.00 25.92  ? 40  VAL A CA   1 
ATOM   320   C  C    . VAL A 1 22  ? -17.758 -4.641  11.393  1.00 24.16  ? 40  VAL A C    1 
ATOM   321   O  O    . VAL A 1 22  ? -17.745 -3.876  12.367  1.00 23.85  ? 40  VAL A O    1 
ATOM   322   C  CB   . VAL A 1 22  ? -18.877 -6.914  11.462  1.00 26.74  ? 40  VAL A CB   1 
ATOM   323   C  CG1  . VAL A 1 22  ? -18.306 -7.012  12.867  1.00 26.92  ? 40  VAL A CG1  1 
ATOM   324   C  CG2  . VAL A 1 22  ? -20.231 -7.606  11.377  1.00 27.60  ? 40  VAL A CG2  1 
ATOM   325   H  H    . VAL A 1 22  ? -19.101 -6.091  9.172   1.00 32.53  ? 40  VAL A H    1 
ATOM   326   H  HA   . VAL A 1 22  ? -19.753 -5.052  11.508  1.00 31.10  ? 40  VAL A HA   1 
ATOM   327   H  HB   . VAL A 1 22  ? -18.269 -7.369  10.858  1.00 32.08  ? 40  VAL A HB   1 
ATOM   328   H  HG11 . VAL A 1 22  ? -17.356 -6.815  12.837  1.00 32.30  ? 40  VAL A HG11 1 
ATOM   329   H  HG12 . VAL A 1 22  ? -18.758 -6.371  13.438  1.00 32.30  ? 40  VAL A HG12 1 
ATOM   330   H  HG13 . VAL A 1 22  ? -18.447 -7.911  13.203  1.00 32.30  ? 40  VAL A HG13 1 
ATOM   331   H  HG21 . VAL A 1 22  ? -20.854 -7.026  10.912  1.00 33.12  ? 40  VAL A HG21 1 
ATOM   332   H  HG22 . VAL A 1 22  ? -20.129 -8.439  10.890  1.00 33.12  ? 40  VAL A HG22 1 
ATOM   333   H  HG23 . VAL A 1 22  ? -20.551 -7.784  12.275  1.00 33.12  ? 40  VAL A HG23 1 
ATOM   334   N  N    . LEU A 1 23  ? -16.695 -4.799  10.610  1.00 22.71  ? 41  LEU A N    1 
ATOM   335   C  CA   . LEU A 1 23  ? -15.474 -4.058  10.885  1.00 21.38  ? 41  LEU A CA   1 
ATOM   336   C  C    . LEU A 1 23  ? -15.708 -2.558  10.743  1.00 19.50  ? 41  LEU A C    1 
ATOM   337   O  O    . LEU A 1 23  ? -15.223 -1.766  11.561  1.00 19.42  ? 41  LEU A O    1 
ATOM   338   C  CB   . LEU A 1 23  ? -14.356 -4.549  9.967   1.00 22.00  ? 41  LEU A CB   1 
ATOM   339   C  CG   . LEU A 1 23  ? -14.018 -6.037  10.131  1.00 21.92  ? 41  LEU A CG   1 
ATOM   340   C  CD1  . LEU A 1 23  ? -13.013 -6.493  9.082   1.00 22.90  ? 41  LEU A CD1  1 
ATOM   341   C  CD2  . LEU A 1 23  ? -13.492 -6.356  11.539  1.00 20.99  ? 41  LEU A CD2  1 
ATOM   342   H  H    . LEU A 1 23  ? -16.657 -5.319  9.926   1.00 27.25  ? 41  LEU A H    1 
ATOM   343   H  HA   . LEU A 1 23  ? -15.188 -4.220  11.798  1.00 25.66  ? 41  LEU A HA   1 
ATOM   344   H  HB2  . LEU A 1 23  ? -14.626 -4.407  9.047   1.00 26.40  ? 41  LEU A HB2  1 
ATOM   345   H  HB3  . LEU A 1 23  ? -13.552 -4.041  10.159  1.00 26.40  ? 41  LEU A HB3  1 
ATOM   346   H  HG   . LEU A 1 23  ? -14.841 -6.535  10.004  1.00 26.30  ? 41  LEU A HG   1 
ATOM   347   H  HD11 . LEU A 1 23  ? -12.886 -7.452  9.162   1.00 27.48  ? 41  LEU A HD11 1 
ATOM   348   H  HD12 . LEU A 1 23  ? -13.356 -6.277  8.201   1.00 27.48  ? 41  LEU A HD12 1 
ATOM   349   H  HD13 . LEU A 1 23  ? -12.171 -6.035  9.231   1.00 27.48  ? 41  LEU A HD13 1 
ATOM   350   H  HD21 . LEU A 1 23  ? -14.213 -6.245  12.178  1.00 25.19  ? 41  LEU A HD21 1 
ATOM   351   H  HD22 . LEU A 1 23  ? -13.172 -7.272  11.557  1.00 25.19  ? 41  LEU A HD22 1 
ATOM   352   H  HD23 . LEU A 1 23  ? -12.766 -5.749  11.750  1.00 25.19  ? 41  LEU A HD23 1 
ATOM   353   N  N    . ASP A 1 24  ? -16.462 -2.147  9.718   1.00 20.17  ? 42  ASP A N    1 
ATOM   354   C  CA   . ASP A 1 24  ? -16.760 -0.728  9.541   1.00 21.69  ? 42  ASP A CA   1 
ATOM   355   C  C    . ASP A 1 24  ? -17.533 -0.176  10.737  1.00 21.27  ? 42  ASP A C    1 
ATOM   356   O  O    . ASP A 1 24  ? -17.330 0.974   11.140  1.00 21.56  ? 42  ASP A O    1 
ATOM   357   C  CB   . ASP A 1 24  ? -17.586 -0.517  8.268   1.00 22.68  ? 42  ASP A CB   1 
ATOM   358   C  CG   . ASP A 1 24  ? -16.748 -0.496  6.983   1.00 24.10  ? 42  ASP A CG   1 
ATOM   359   O  OD1  . ASP A 1 24  ? -15.510 -0.303  7.016   1.00 24.63  ? 42  ASP A OD1  1 
ATOM   360   O  OD2  . ASP A 1 24  ? -17.370 -0.654  5.909   1.00 25.73  ? 42  ASP A OD2  1 
ATOM   361   H  H    . ASP A 1 24  ? -16.807 -2.662  9.122   1.00 24.20  ? 42  ASP A H    1 
ATOM   362   H  HA   . ASP A 1 24  ? -15.922 -0.247  9.455   1.00 26.03  ? 42  ASP A HA   1 
ATOM   363   H  HB2  . ASP A 1 24  ? -18.228 -1.239  8.190   1.00 27.22  ? 42  ASP A HB2  1 
ATOM   364   H  HB3  . ASP A 1 24  ? -18.048 0.333   8.333   1.00 27.22  ? 42  ASP A HB3  1 
ATOM   365   N  N    . ALA A 1 25  ? -18.444 -0.976  11.305  1.00 21.29  ? 43  ALA A N    1 
ATOM   366   C  CA   . ALA A 1 25  ? -19.243 -0.509  12.434  1.00 21.57  ? 43  ALA A CA   1 
ATOM   367   C  C    . ALA A 1 25  ? -18.385 -0.181  13.649  1.00 21.04  ? 43  ALA A C    1 
ATOM   368   O  O    . ALA A 1 25  ? -18.807 0.607   14.504  1.00 23.42  ? 43  ALA A O    1 
ATOM   369   C  CB   . ALA A 1 25  ? -20.285 -1.566  12.813  1.00 22.45  ? 43  ALA A CB   1 
ATOM   370   H  H    . ALA A 1 25  ? -18.615 -1.781  11.055  1.00 25.54  ? 43  ALA A H    1 
ATOM   371   H  HA   . ALA A 1 25  ? -19.711 0.298   12.168  1.00 25.88  ? 43  ALA A HA   1 
ATOM   372   H  HB1  . ALA A 1 25  ? -20.861 -1.729  12.050  1.00 26.94  ? 43  ALA A HB1  1 
ATOM   373   H  HB2  . ALA A 1 25  ? -19.828 -2.384  13.064  1.00 26.94  ? 43  ALA A HB2  1 
ATOM   374   H  HB3  . ALA A 1 25  ? -20.809 -1.238  13.560  1.00 26.94  ? 43  ALA A HB3  1 
ATOM   375   N  N    . GLY A 1 26  ? -17.193 -0.757  13.746  1.00 19.32  ? 44  GLY A N    1 
ATOM   376   C  CA   . GLY A 1 26  ? -16.314 -0.495  14.860  1.00 18.02  ? 44  GLY A CA   1 
ATOM   377   C  C    . GLY A 1 26  ? -15.440 0.724   14.717  1.00 16.22  ? 44  GLY A C    1 
ATOM   378   O  O    . GLY A 1 26  ? -14.645 1.014   15.619  1.00 16.83  ? 44  GLY A O    1 
ATOM   379   H  H    . GLY A 1 26  ? -16.874 -1.309  13.169  1.00 23.19  ? 44  GLY A H    1 
ATOM   380   H  HA2  . GLY A 1 26  ? -16.852 -0.378  15.658  1.00 21.62  ? 44  GLY A HA2  1 
ATOM   381   H  HA3  . GLY A 1 26  ? -15.732 -1.262  14.981  1.00 21.62  ? 44  GLY A HA3  1 
ATOM   382   N  N    . LEU A 1 27  ? -15.560 1.446   13.606  1.00 16.39  ? 45  LEU A N    1 
ATOM   383   C  CA   . LEU A 1 27  ? -14.721 2.599   13.307  1.00 16.80  ? 45  LEU A CA   1 
ATOM   384   C  C    . LEU A 1 27  ? -15.560 3.868   13.343  1.00 17.67  ? 45  LEU A C    1 
ATOM   385   O  O    . LEU A 1 27  ? -16.619 3.937   12.706  1.00 19.64  ? 45  LEU A O    1 
ATOM   386   C  CB   . LEU A 1 27  ? -14.106 2.459   11.914  1.00 17.64  ? 45  LEU A CB   1 
ATOM   387   C  CG   . LEU A 1 27  ? -13.327 3.658   11.375  1.00 18.24  ? 45  LEU A CG   1 
ATOM   388   C  CD1  . LEU A 1 27  ? -12.139 3.988   12.255  1.00 18.87  ? 45  LEU A CD1  1 
ATOM   389   C  CD2  . LEU A 1 27  ? -12.880 3.346   9.952   1.00 19.58  ? 45  LEU A CD2  1 
ATOM   390   H  H    . LEU A 1 27  ? -16.139 1.281   12.992  1.00 19.67  ? 45  LEU A H    1 
ATOM   391   H  HA   . LEU A 1 27  ? -14.020 2.665   13.974  1.00 20.16  ? 45  LEU A HA   1 
ATOM   392   H  HB2  . LEU A 1 27  ? -13.492 1.708   11.933  1.00 21.17  ? 45  LEU A HB2  1 
ATOM   393   H  HB3  . LEU A 1 27  ? -14.826 2.283   11.287  1.00 21.17  ? 45  LEU A HB3  1 
ATOM   394   H  HG   . LEU A 1 27  ? -13.895 4.444   11.370  1.00 21.88  ? 45  LEU A HG   1 
ATOM   395   H  HD11 . LEU A 1 27  ? -11.558 3.213   12.305  1.00 22.65  ? 45  LEU A HD11 1 
ATOM   396   H  HD12 . LEU A 1 27  ? -11.659 4.738   11.870  1.00 22.65  ? 45  LEU A HD12 1 
ATOM   397   H  HD13 . LEU A 1 27  ? -12.458 4.220   13.142  1.00 22.65  ? 45  LEU A HD13 1 
ATOM   398   H  HD21 . LEU A 1 27  ? -12.300 2.568   9.967   1.00 23.49  ? 45  LEU A HD21 1 
ATOM   399   H  HD22 . LEU A 1 27  ? -13.662 3.165   9.407   1.00 23.49  ? 45  LEU A HD22 1 
ATOM   400   H  HD23 . LEU A 1 27  ? -12.399 4.110   9.597   1.00 23.49  ? 45  LEU A HD23 1 
ATOM   401   N  N    . THR A 1 28  ? -15.057 4.885   14.048  1.00 16.43  ? 46  THR A N    1 
ATOM   402   C  CA   . THR A 1 28  ? -15.731 6.170   14.164  1.00 16.93  ? 46  THR A CA   1 
ATOM   403   C  C    . THR A 1 28  ? -14.696 7.280   14.058  1.00 17.41  ? 46  THR A C    1 
ATOM   404   O  O    . THR A 1 28  ? -13.591 7.146   14.584  1.00 17.63  ? 46  THR A O    1 
ATOM   405   C  CB   . THR A 1 28  ? -16.446 6.284   15.520  1.00 19.04  ? 46  THR A CB   1 
ATOM   406   O  OG1  . THR A 1 28  ? -17.275 5.133   15.732  1.00 20.50  ? 46  THR A OG1  1 
ATOM   407   C  CG2  . THR A 1 28  ? -17.299 7.539   15.592  1.00 20.03  ? 46  THR A CG2  1 
ATOM   408   H  H    . THR A 1 28  ? -14.311 4.849   14.474  1.00 19.72  ? 46  THR A H    1 
ATOM   409   H  HA   . THR A 1 28  ? -16.379 6.273   13.449  1.00 20.32  ? 46  THR A HA   1 
ATOM   410   H  HB   . THR A 1 28  ? -15.778 6.336   16.221  1.00 22.85  ? 46  THR A HB   1 
ATOM   411   H  HG1  . THR A 1 28  ? -17.622 5.165   16.496  1.00 24.60  ? 46  THR A HG1  1 
ATOM   412   H  HG21 . THR A 1 28  ? -17.904 7.573   14.834  1.00 24.04  ? 46  THR A HG21 1 
ATOM   413   H  HG22 . THR A 1 28  ? -17.820 7.539   16.410  1.00 24.04  ? 46  THR A HG22 1 
ATOM   414   H  HG23 . THR A 1 28  ? -16.733 8.326   15.578  1.00 24.04  ? 46  THR A HG23 1 
ATOM   415   N  N    . CYS A 1 29  ? -15.049 8.373   13.378  1.00 17.12  ? 47  CYS A N    1 
ATOM   416   C  CA   . CYS A 1 29  ? -14.231 9.575   13.373  1.00 17.20  ? 47  CYS A CA   1 
ATOM   417   C  C    . CYS A 1 29  ? -15.015 10.716  14.005  1.00 17.81  ? 47  CYS A C    1 
ATOM   418   O  O    . CYS A 1 29  ? -16.245 10.770  13.917  1.00 19.37  ? 47  CYS A O    1 
ATOM   419   C  CB   . CYS A 1 29  ? -13.831 10.009  11.957  1.00 17.33  ? 47  CYS A CB   1 
ATOM   420   S  SG   . CYS A 1 29  ? -12.818 8.870   11.039  1.00 18.51  ? 47  CYS A SG   1 
ATOM   421   H  H    . CYS A 1 29  ? -15.767 8.437   12.909  1.00 20.54  ? 47  CYS A H    1 
ATOM   422   H  HA   . CYS A 1 29  ? -13.422 9.397   13.879  1.00 20.64  ? 47  CYS A HA   1 
ATOM   423   H  HB2  . CYS A 1 29  ? -14.642 10.147  11.444  1.00 20.79  ? 47  CYS A HB2  1 
ATOM   424   H  HB3  . CYS A 1 29  ? -13.336 10.840  12.025  1.00 20.79  ? 47  CYS A HB3  1 
ATOM   425   N  N    . GLN A 1 30  ? -14.290 11.626  14.650  1.00 17.67  ? 48  GLN A N    1 
ATOM   426   C  CA   . GLN A 1 30  ? -14.906 12.810  15.240  1.00 17.84  ? 48  GLN A CA   1 
ATOM   427   C  C    . GLN A 1 30  ? -15.309 13.787  14.143  1.00 20.50  ? 48  GLN A C    1 
ATOM   428   O  O    . GLN A 1 30  ? -14.456 14.303  13.414  1.00 21.33  ? 48  GLN A O    1 
ATOM   429   C  CB   . GLN A 1 30  ? -13.905 13.451  16.196  1.00 19.12  ? 48  GLN A CB   1 
ATOM   430   C  CG   . GLN A 1 30  ? -14.331 14.743  16.839  1.00 20.80  ? 48  GLN A CG   1 
ATOM   431   C  CD   . GLN A 1 30  ? -13.199 15.335  17.659  1.00 21.27  ? 48  GLN A CD   1 
ATOM   432   O  OE1  . GLN A 1 30  ? -13.075 15.071  18.854  1.00 22.82  ? 48  GLN A OE1  1 
ATOM   433   N  NE2  . GLN A 1 30  ? -12.349 16.116  17.009  1.00 20.71  ? 48  GLN A NE2  1 
ATOM   434   H  H    . GLN A 1 30  ? -13.438 11.582  14.759  1.00 21.20  ? 48  GLN A H    1 
ATOM   435   H  HA   . GLN A 1 30  ? -15.707 12.567  15.730  1.00 21.40  ? 48  GLN A HA   1 
ATOM   436   H  HB2  . GLN A 1 30  ? -13.725 12.822  16.912  1.00 22.95  ? 48  GLN A HB2  1 
ATOM   437   H  HB3  . GLN A 1 30  ? -13.090 13.633  15.703  1.00 22.95  ? 48  GLN A HB3  1 
ATOM   438   H  HG2  . GLN A 1 30  ? -14.580 15.380  16.152  1.00 24.96  ? 48  GLN A HG2  1 
ATOM   439   H  HG3  . GLN A 1 30  ? -15.084 14.579  17.428  1.00 24.96  ? 48  GLN A HG3  1 
ATOM   440   H  HE21 . GLN A 1 30  ? -12.456 16.263  16.168  1.00 24.86  ? 48  GLN A HE21 1 
ATOM   441   H  HE22 . GLN A 1 30  ? -11.689 16.477  17.427  1.00 24.86  ? 48  GLN A HE22 1 
ATOM   442   N  N    . GLY A 1 31  ? -16.610 14.038  14.027  1.00 21.18  ? 49  GLY A N    1 
ATOM   443   C  CA   . GLY A 1 31  ? -17.100 15.051  13.112  1.00 22.55  ? 49  GLY A CA   1 
ATOM   444   C  C    . GLY A 1 31  ? -16.935 14.743  11.643  1.00 23.32  ? 49  GLY A C    1 
ATOM   445   O  O    . GLY A 1 31  ? -16.994 15.660  10.816  1.00 25.74  ? 49  GLY A O    1 
ATOM   446   H  H    . GLY A 1 31  ? -17.226 13.633  14.469  1.00 25.42  ? 49  GLY A H    1 
ATOM   447   H  HA2  . GLY A 1 31  ? -18.047 15.182  13.278  1.00 27.06  ? 49  GLY A HA2  1 
ATOM   448   H  HA3  . GLY A 1 31  ? -16.630 15.880  13.291  1.00 27.06  ? 49  GLY A HA3  1 
ATOM   449   N  N    . ALA A 1 32  ? -16.740 13.477  11.288  1.00 21.66  ? 50  ALA A N    1 
ATOM   450   C  CA   . ALA A 1 32  ? -16.528 13.103  9.899   1.00 21.73  ? 50  ALA A CA   1 
ATOM   451   C  C    . ALA A 1 32  ? -16.837 11.625  9.744   1.00 21.15  ? 50  ALA A C    1 
ATOM   452   O  O    . ALA A 1 32  ? -16.850 10.870  10.721  1.00 22.13  ? 50  ALA A O    1 
ATOM   453   C  CB   . ALA A 1 32  ? -15.079 13.364  9.468   1.00 22.57  ? 50  ALA A CB   1 
ATOM   454   H  H    . ALA A 1 32  ? -16.727 12.815  11.837  1.00 25.99  ? 50  ALA A H    1 
ATOM   455   H  HA   . ALA A 1 32  ? -17.128 13.618  9.337   1.00 26.08  ? 50  ALA A HA   1 
ATOM   456   H  HB1  . ALA A 1 32  ? -14.974 13.102  8.540   1.00 27.08  ? 50  ALA A HB1  1 
ATOM   457   H  HB2  . ALA A 1 32  ? -14.885 14.309  9.569   1.00 27.08  ? 50  ALA A HB2  1 
ATOM   458   H  HB3  . ALA A 1 32  ? -14.484 12.842  10.028  1.00 27.08  ? 50  ALA A HB3  1 
ATOM   459   N  N    . SER A 1 33  ? -17.065 11.222  8.493   1.00 21.25  ? 51  SER A N    1 
ATOM   460   C  CA   . SER A 1 33  ? -17.133 9.819   8.120   1.00 21.87  ? 51  SER A CA   1 
ATOM   461   C  C    . SER A 1 33  ? -15.770 9.367   7.611   1.00 21.12  ? 51  SER A C    1 
ATOM   462   O  O    . SER A 1 33  ? -15.055 10.153  6.976   1.00 21.48  ? 51  SER A O    1 
ATOM   463   C  CB   . SER A 1 33  ? -18.172 9.621   7.014   1.00 24.39  ? 51  SER A CB   1 
ATOM   464   O  OG   . SER A 1 33  ? -18.052 8.353   6.389   1.00 27.45  ? 51  SER A OG   1 
ATOM   465   H  H    . SER A 1 33  ? -17.186 11.756  7.830   1.00 25.51  ? 51  SER A H    1 
ATOM   466   H  HA   . SER A 1 33  ? -17.388 9.273   8.880   1.00 26.24  ? 51  SER A HA   1 
ATOM   467   H  HB2  . SER A 1 33  ? -19.057 9.694   7.402   1.00 29.27  ? 51  SER A HB2  1 
ATOM   468   H  HB3  . SER A 1 33  ? -18.046 10.311  6.343   1.00 29.27  ? 51  SER A HB3  1 
ATOM   469   H  HG   . SER A 1 33  ? -18.157 7.743   6.956   1.00 32.94  ? 51  SER A HG   1 
ATOM   470   N  N    . PRO A 1 34  ? -15.360 8.128   7.894   1.00 20.13  ? 52  PRO A N    1 
ATOM   471   C  CA   . PRO A 1 34  ? -14.097 7.630   7.323   1.00 19.85  ? 52  PRO A CA   1 
ATOM   472   C  C    . PRO A 1 34  ? -14.031 7.717   5.809   1.00 21.00  ? 52  PRO A C    1 
ATOM   473   O  O    . PRO A 1 34  ? -12.927 7.743   5.253   1.00 21.75  ? 52  PRO A O    1 
ATOM   474   C  CB   . PRO A 1 34  ? -14.041 6.168   7.793   1.00 20.75  ? 52  PRO A CB   1 
ATOM   475   C  CG   . PRO A 1 34  ? -14.885 6.130   9.030   1.00 20.86  ? 52  PRO A CG   1 
ATOM   476   C  CD   . PRO A 1 34  ? -15.977 7.157   8.818   1.00 19.91  ? 52  PRO A CD   1 
ATOM   477   H  HA   . PRO A 1 34  ? -13.353 8.121   7.705   1.00 23.82  ? 52  PRO A HA   1 
ATOM   478   H  HB2  . PRO A 1 34  ? -14.403 5.586   7.107   1.00 24.90  ? 52  PRO A HB2  1 
ATOM   479   H  HB3  . PRO A 1 34  ? -13.124 5.919   7.990   1.00 24.90  ? 52  PRO A HB3  1 
ATOM   480   H  HG2  . PRO A 1 34  ? -15.264 5.244   9.140   1.00 25.03  ? 52  PRO A HG2  1 
ATOM   481   H  HG3  . PRO A 1 34  ? -14.344 6.358   9.802   1.00 25.03  ? 52  PRO A HG3  1 
ATOM   482   H  HD2  . PRO A 1 34  ? -16.761 6.750   8.417   1.00 23.89  ? 52  PRO A HD2  1 
ATOM   483   H  HD3  . PRO A 1 34  ? -16.217 7.583   9.656   1.00 23.89  ? 52  PRO A HD3  1 
ATOM   484   N  N    . SER A 1 35  ? -15.176 7.745   5.127   1.00 21.45  ? 53  SER A N    1 
ATOM   485   C  CA   A SER A 1 35  ? -15.191 7.792   3.673   0.68 23.06  ? 53  SER A CA   1 
ATOM   486   C  CA   B SER A 1 35  ? -15.205 7.794   3.672   0.32 22.70  ? 53  SER A CA   1 
ATOM   487   C  C    . SER A 1 35  ? -14.761 9.139   3.113   1.00 23.12  ? 53  SER A C    1 
ATOM   488   O  O    . SER A 1 35  ? -14.512 9.234   1.906   1.00 23.54  ? 53  SER A O    1 
ATOM   489   C  CB   A SER A 1 35  ? -16.600 7.485   3.175   0.68 23.34  ? 53  SER A CB   1 
ATOM   490   C  CB   B SER A 1 35  ? -16.622 7.500   3.169   0.32 22.98  ? 53  SER A CB   1 
ATOM   491   O  OG   A SER A 1 35  ? -17.523 8.393   3.745   0.68 23.39  ? 53  SER A OG   1 
ATOM   492   O  OG   B SER A 1 35  ? -17.010 6.163   3.438   0.32 23.07  ? 53  SER A OG   1 
ATOM   493   H  H    A SER A 1 35  ? -15.958 7.738   5.486   0.68 25.73  ? 53  SER A H    1 
ATOM   494   H  H    B SER A 1 35  ? -15.956 7.737   5.489   0.32 25.73  ? 53  SER A H    1 
ATOM   495   H  HA   A SER A 1 35  ? -14.577 7.120   3.338   0.68 27.67  ? 53  SER A HA   1 
ATOM   496   H  HA   B SER A 1 35  ? -14.604 7.111   3.335   0.32 27.24  ? 53  SER A HA   1 
ATOM   497   H  HB2  A SER A 1 35  ? -16.624 7.570   2.209   0.68 28.01  ? 53  SER A HB2  1 
ATOM   498   H  HB2  B SER A 1 35  ? -17.242 8.100   3.613   0.32 27.58  ? 53  SER A HB2  1 
ATOM   499   H  HB3  A SER A 1 35  ? -16.841 6.582   3.434   0.68 28.01  ? 53  SER A HB3  1 
ATOM   500   H  HB3  B SER A 1 35  ? -16.649 7.645   2.210   0.32 27.58  ? 53  SER A HB3  1 
ATOM   501   H  HG   A SER A 1 35  ? -17.318 9.181   3.535   0.68 28.07  ? 53  SER A HG   1 
ATOM   502   H  HG   B SER A 1 35  ? -17.014 6.027   4.267   0.32 27.68  ? 53  SER A HG   1 
ATOM   503   N  N    . SER A 1 36  ? -14.677 10.176  3.943   1.00 22.68  ? 54  SER A N    1 
ATOM   504   C  CA   . SER A 1 36  ? -14.299 11.503  3.450   1.00 23.84  ? 54  SER A CA   1 
ATOM   505   C  C    . SER A 1 36  ? -13.798 12.288  4.665   1.00 23.43  ? 54  SER A C    1 
ATOM   506   O  O    . SER A 1 36  ? -14.574 12.968  5.335   1.00 25.50  ? 54  SER A O    1 
ATOM   507   C  CB   . SER A 1 36  ? -15.461 12.200  2.776   1.00 26.78  ? 54  SER A CB   1 
ATOM   508   O  OG   . SER A 1 36  ? -15.003 13.221  1.912   1.00 28.58  ? 54  SER A OG   1 
ATOM   509   H  H    . SER A 1 36  ? -14.833 10.141  4.788   1.00 27.21  ? 54  SER A H    1 
ATOM   510   H  HA   . SER A 1 36  ? -13.578 11.425  2.806   1.00 28.61  ? 54  SER A HA   1 
ATOM   511   H  HB2  . SER A 1 36  ? -15.962 11.550  2.258   1.00 32.13  ? 54  SER A HB2  1 
ATOM   512   H  HB3  . SER A 1 36  ? -16.031 12.593  3.455   1.00 32.13  ? 54  SER A HB3  1 
ATOM   513   H  HG   . SER A 1 36  ? -15.656 13.648  1.600   1.00 34.30  ? 54  SER A HG   1 
ATOM   514   N  N    . VAL A 1 37  ? -12.505 12.174  4.937   1.00 22.63  ? 55  VAL A N    1 
ATOM   515   C  CA   . VAL A 1 37  ? -11.928 12.717  6.160   1.00 21.15  ? 55  VAL A CA   1 
ATOM   516   C  C    . VAL A 1 37  ? -10.598 13.381  5.842   1.00 23.00  ? 55  VAL A C    1 
ATOM   517   O  O    . VAL A 1 37  ? -9.818  12.883  5.022   1.00 23.99  ? 55  VAL A O    1 
ATOM   518   C  CB   . VAL A 1 37  ? -11.764 11.621  7.235   1.00 20.84  ? 55  VAL A CB   1 
ATOM   519   C  CG1  . VAL A 1 37  ? -10.906 10.467  6.720   1.00 20.05  ? 55  VAL A CG1  1 
ATOM   520   C  CG2  . VAL A 1 37  ? -11.160 12.207  8.496   1.00 21.92  ? 55  VAL A CG2  1 
ATOM   521   H  H    . VAL A 1 37  ? -11.936 11.782  4.425   1.00 27.16  ? 55  VAL A H    1 
ATOM   522   H  HA   . VAL A 1 37  ? -12.515 13.406  6.508   1.00 25.38  ? 55  VAL A HA   1 
ATOM   523   H  HB   . VAL A 1 37  ? -12.642 11.266  7.447   1.00 25.01  ? 55  VAL A HB   1 
ATOM   524   H  HG11 . VAL A 1 37  ? -10.880 9.769   7.393   1.00 24.06  ? 55  VAL A HG11 1 
ATOM   525   H  HG12 . VAL A 1 37  ? -11.298 10.123  5.902   1.00 24.06  ? 55  VAL A HG12 1 
ATOM   526   H  HG13 . VAL A 1 37  ? -10.010 10.794  6.546   1.00 24.06  ? 55  VAL A HG13 1 
ATOM   527   H  HG21 . VAL A 1 37  ? -11.396 13.145  8.553   1.00 26.30  ? 55  VAL A HG21 1 
ATOM   528   H  HG22 . VAL A 1 37  ? -11.510 11.730  9.265   1.00 26.30  ? 55  VAL A HG22 1 
ATOM   529   H  HG23 . VAL A 1 37  ? -10.195 12.110  8.458   1.00 26.30  ? 55  VAL A HG23 1 
ATOM   530   N  N    . SER A 1 38  ? -10.343 14.508  6.499   1.00 23.67  ? 56  SER A N    1 
ATOM   531   C  CA   . SER A 1 38  ? -9.113  15.262  6.327   1.00 24.44  ? 56  SER A CA   1 
ATOM   532   C  C    . SER A 1 38  ? -8.135  14.944  7.454   1.00 22.56  ? 56  SER A C    1 
ATOM   533   O  O    . SER A 1 38  ? -8.491  15.015  8.635   1.00 23.40  ? 56  SER A O    1 
ATOM   534   C  CB   . SER A 1 38  ? -9.427  16.757  6.318   1.00 27.93  ? 56  SER A CB   1 
ATOM   535   O  OG   . SER A 1 38  ? -8.239  17.512  6.346   1.00 32.48  ? 56  SER A OG   1 
ATOM   536   H  H    . SER A 1 38  ? -10.885 14.864  7.065   1.00 28.41  ? 56  SER A H    1 
ATOM   537   H  HA   . SER A 1 38  ? -8.690  15.012  5.490   1.00 29.33  ? 56  SER A HA   1 
ATOM   538   H  HB2  . SER A 1 38  ? -9.920  16.973  5.511   1.00 33.52  ? 56  SER A HB2  1 
ATOM   539   H  HB3  . SER A 1 38  ? -9.959  16.974  7.099   1.00 33.52  ? 56  SER A HB3  1 
ATOM   540   H  HG   . SER A 1 38  ? -7.895  17.478  7.112   1.00 38.98  ? 56  SER A HG   1 
ATOM   541   N  N    . LYS A 1 39  ? -6.904  14.607  7.084   1.00 20.61  ? 57  LYS A N    1 
ATOM   542   C  CA   . LYS A 1 39  ? -5.825  14.361  8.034   1.00 20.46  ? 57  LYS A CA   1 
ATOM   543   C  C    . LYS A 1 39  ? -6.261  13.443  9.179   1.00 19.01  ? 57  LYS A C    1 
ATOM   544   O  O    . LYS A 1 39  ? -6.136  13.806  10.355  1.00 19.21  ? 57  LYS A O    1 
ATOM   545   C  CB   . LYS A 1 39  ? -5.260  15.668  8.570   1.00 23.73  ? 57  LYS A CB   1 
ATOM   546   C  CG   . LYS A 1 39  ? -4.085  16.223  7.767   1.00 29.16  ? 57  LYS A CG   1 
ATOM   547   C  CD   . LYS A 1 39  ? -3.289  17.251  8.572   1.00 31.61  ? 57  LYS A CD   1 
ATOM   548   C  CE   . LYS A 1 39  ? -2.194  16.594  9.419   1.00 33.42  ? 57  LYS A CE   1 
ATOM   549   N  NZ   . LYS A 1 39  ? -1.042  16.099  8.602   1.00 33.56  ? 57  LYS A NZ   1 
ATOM   550   H  H    . LYS A 1 39  ? -6.663  14.511  6.264   1.00 24.73  ? 57  LYS A H    1 
ATOM   551   H  HA   . LYS A 1 39  ? -5.108  13.906  7.566   1.00 24.55  ? 57  LYS A HA   1 
ATOM   552   H  HB2  . LYS A 1 39  ? -5.963  16.336  8.562   1.00 28.48  ? 57  LYS A HB2  1 
ATOM   553   H  HB3  . LYS A 1 39  ? -4.952  15.522  9.479   1.00 28.48  ? 57  LYS A HB3  1 
ATOM   554   H  HG2  . LYS A 1 39  ? -3.488  15.496  7.527   1.00 35.00  ? 57  LYS A HG2  1 
ATOM   555   H  HG3  . LYS A 1 39  ? -4.419  16.656  6.966   1.00 35.00  ? 57  LYS A HG3  1 
ATOM   556   H  HD2  . LYS A 1 39  ? -2.865  17.876  7.962   1.00 37.93  ? 57  LYS A HD2  1 
ATOM   557   H  HD3  . LYS A 1 39  ? -3.890  17.725  9.168   1.00 37.93  ? 57  LYS A HD3  1 
ATOM   558   H  HE2  . LYS A 1 39  ? -1.853  17.243  10.054  1.00 40.11  ? 57  LYS A HE2  1 
ATOM   559   H  HE3  . LYS A 1 39  ? -2.573  15.836  9.892   1.00 40.11  ? 57  LYS A HE3  1 
ATOM   560   H  HZ1  . LYS A 1 39  ? -0.444  15.701  9.128   1.00 40.27  ? 57  LYS A HZ1  1 
ATOM   561   H  HZ2  . LYS A 1 39  ? -1.328  15.514  7.996   1.00 40.27  ? 57  LYS A HZ2  1 
ATOM   562   H  HZ3  . LYS A 1 39  ? -0.650  16.780  8.184   1.00 40.27  ? 57  LYS A HZ3  1 
ATOM   563   N  N    . PRO A 1 40  ? -6.758  12.249  8.873   1.00 17.58  ? 58  PRO A N    1 
ATOM   564   C  CA   . PRO A 1 40  ? -7.120  11.314  9.943   1.00 17.95  ? 58  PRO A CA   1 
ATOM   565   C  C    . PRO A 1 40  ? -5.898  10.848  10.716  1.00 17.31  ? 58  PRO A C    1 
ATOM   566   O  O    . PRO A 1 40  ? -4.801  10.712  10.172  1.00 17.27  ? 58  PRO A O    1 
ATOM   567   C  CB   . PRO A 1 40  ? -7.744  10.137  9.185   1.00 19.11  ? 58  PRO A CB   1 
ATOM   568   C  CG   . PRO A 1 40  ? -7.046  10.164  7.861   1.00 18.36  ? 58  PRO A CG   1 
ATOM   569   C  CD   . PRO A 1 40  ? -6.895  11.636  7.537   1.00 17.71  ? 58  PRO A CD   1 
ATOM   570   H  HA   . PRO A 1 40  ? -7.766  11.715  10.544  1.00 21.54  ? 58  PRO A HA   1 
ATOM   571   H  HB2  . PRO A 1 40  ? -7.574  9.306   9.656   1.00 22.94  ? 58  PRO A HB2  1 
ATOM   572   H  HB3  . PRO A 1 40  ? -8.699  10.271  9.083   1.00 22.94  ? 58  PRO A HB3  1 
ATOM   573   H  HG2  . PRO A 1 40  ? -6.180  9.733   7.933   1.00 22.03  ? 58  PRO A HG2  1 
ATOM   574   H  HG3  . PRO A 1 40  ? -7.585  9.714   7.192   1.00 22.03  ? 58  PRO A HG3  1 
ATOM   575   H  HD2  . PRO A 1 40  ? -6.104  11.794  6.999   1.00 21.25  ? 58  PRO A HD2  1 
ATOM   576   H  HD3  . PRO A 1 40  ? -7.681  11.973  7.079   1.00 21.25  ? 58  PRO A HD3  1 
ATOM   577   N  N    . ILE A 1 41  ? -6.104  10.604  12.004  1.00 16.61  ? 59  ILE A N    1 
ATOM   578   C  CA   . ILE A 1 41  ? -5.199  9.812   12.829  1.00 15.67  ? 59  ILE A CA   1 
ATOM   579   C  C    . ILE A 1 41  ? -6.022  8.666   13.406  1.00 15.65  ? 59  ILE A C    1 
ATOM   580   O  O    . ILE A 1 41  ? -7.147  8.883   13.874  1.00 16.96  ? 59  ILE A O    1 
ATOM   581   C  CB   . ILE A 1 41  ? -4.530  10.665  13.926  1.00 16.28  ? 59  ILE A CB   1 
ATOM   582   C  CG1  . ILE A 1 41  ? -3.577  9.809   14.768  1.00 16.01  ? 59  ILE A CG1  1 
ATOM   583   C  CG2  . ILE A 1 41  ? -5.560  11.347  14.813  1.00 17.69  ? 59  ILE A CG2  1 
ATOM   584   C  CD1  . ILE A 1 41  ? -2.650  10.632  15.667  1.00 16.95  ? 59  ILE A CD1  1 
ATOM   585   H  H    . ILE A 1 41  ? -6.787  10.896  12.439  1.00 19.93  ? 59  ILE A H    1 
ATOM   586   H  HA   . ILE A 1 41  ? -4.482  9.437   12.293  1.00 18.80  ? 59  ILE A HA   1 
ATOM   587   H  HB   . ILE A 1 41  ? -4.017  11.359  13.482  1.00 19.53  ? 59  ILE A HB   1 
ATOM   588   H  HG12 . ILE A 1 41  ? -4.102  9.225   15.338  1.00 19.22  ? 59  ILE A HG12 1 
ATOM   589   H  HG13 . ILE A 1 41  ? -3.022  9.281   14.173  1.00 19.22  ? 59  ILE A HG13 1 
ATOM   590   H  HG21 . ILE A 1 41  ? -5.108  11.974  15.398  1.00 21.23  ? 59  ILE A HG21 1 
ATOM   591   H  HG22 . ILE A 1 41  ? -6.197  11.819  14.252  1.00 21.23  ? 59  ILE A HG22 1 
ATOM   592   H  HG23 . ILE A 1 41  ? -6.019  10.674  15.339  1.00 21.23  ? 59  ILE A HG23 1 
ATOM   593   H  HD11 . ILE A 1 41  ? -1.963  10.051  16.028  1.00 20.34  ? 59  ILE A HD11 1 
ATOM   594   H  HD12 . ILE A 1 41  ? -2.243  11.337  15.139  1.00 20.34  ? 59  ILE A HD12 1 
ATOM   595   H  HD13 . ILE A 1 41  ? -3.171  11.018  16.389  1.00 20.34  ? 59  ILE A HD13 1 
ATOM   596   N  N    . LEU A 1 42  ? -5.492  7.445   13.336  1.00 14.82  ? 60  LEU A N    1 
ATOM   597   C  CA   . LEU A 1 42  ? -6.214  6.277   13.830  1.00 14.22  ? 60  LEU A CA   1 
ATOM   598   C  C    . LEU A 1 42  ? -5.706  5.929   15.223  1.00 14.09  ? 60  LEU A C    1 
ATOM   599   O  O    . LEU A 1 42  ? -4.511  5.682   15.406  1.00 14.89  ? 60  LEU A O    1 
ATOM   600   C  CB   . LEU A 1 42  ? -6.058  5.066   12.915  1.00 14.87  ? 60  LEU A CB   1 
ATOM   601   C  CG   . LEU A 1 42  ? -6.749  3.800   13.439  1.00 15.78  ? 60  LEU A CG   1 
ATOM   602   C  CD1  . LEU A 1 42  ? -8.261  3.941   13.527  1.00 17.17  ? 60  LEU A CD1  1 
ATOM   603   C  CD2  . LEU A 1 42  ? -6.371  2.633   12.549  1.00 17.04  ? 60  LEU A CD2  1 
ATOM   604   H  H    . LEU A 1 42  ? -4.717  7.270   13.007  1.00 17.79  ? 60  LEU A H    1 
ATOM   605   H  HA   . LEU A 1 42  ? -7.156  6.505   13.872  1.00 17.07  ? 60  LEU A HA   1 
ATOM   606   H  HB2  . LEU A 1 42  ? -6.443  5.277   12.051  1.00 17.84  ? 60  LEU A HB2  1 
ATOM   607   H  HB3  . LEU A 1 42  ? -5.113  4.869   12.818  1.00 17.84  ? 60  LEU A HB3  1 
ATOM   608   H  HG   . LEU A 1 42  ? -6.448  3.638   14.347  1.00 18.94  ? 60  LEU A HG   1 
ATOM   609   H  HD11 . LEU A 1 42  ? -8.642  3.093   13.802  1.00 20.60  ? 60  LEU A HD11 1 
ATOM   610   H  HD12 . LEU A 1 42  ? -8.477  4.628   14.177  1.00 20.60  ? 60  LEU A HD12 1 
ATOM   611   H  HD13 . LEU A 1 42  ? -8.606  4.191   12.655  1.00 20.60  ? 60  LEU A HD13 1 
ATOM   612   H  HD21 . LEU A 1 42  ? -6.864  1.847   12.833  1.00 20.44  ? 60  LEU A HD21 1 
ATOM   613   H  HD22 . LEU A 1 42  ? -6.596  2.850   11.631  1.00 20.44  ? 60  LEU A HD22 1 
ATOM   614   H  HD23 . LEU A 1 42  ? -5.418  2.472   12.627  1.00 20.44  ? 60  LEU A HD23 1 
ATOM   615   N  N    . LEU A 1 43  ? -6.621  5.869   16.183  1.00 14.46  ? 61  LEU A N    1 
ATOM   616   C  CA   . LEU A 1 43  ? -6.305  5.585   17.575  1.00 13.95  ? 61  LEU A CA   1 
ATOM   617   C  C    . LEU A 1 43  ? -6.777  4.179   17.926  1.00 13.35  ? 61  LEU A C    1 
ATOM   618   O  O    . LEU A 1 43  ? -7.940  3.834   17.686  1.00 15.46  ? 61  LEU A O    1 
ATOM   619   C  CB   . LEU A 1 43  ? -6.999  6.608   18.476  1.00 14.98  ? 61  LEU A CB   1 
ATOM   620   C  CG   . LEU A 1 43  ? -6.817  8.074   18.095  1.00 15.63  ? 61  LEU A CG   1 
ATOM   621   C  CD1  . LEU A 1 43  ? -7.630  8.963   19.021  1.00 18.55  ? 61  LEU A CD1  1 
ATOM   622   C  CD2  . LEU A 1 43  ? -5.348  8.461   18.135  1.00 16.62  ? 61  LEU A CD2  1 
ATOM   623   H  H    . LEU A 1 43  ? -7.460  5.995   16.047  1.00 17.36  ? 61  LEU A H    1 
ATOM   624   H  HA   . LEU A 1 43  ? -5.347  5.626   17.717  1.00 16.74  ? 61  LEU A HA   1 
ATOM   625   H  HB2  . LEU A 1 43  ? -7.951  6.424   18.463  1.00 17.97  ? 61  LEU A HB2  1 
ATOM   626   H  HB3  . LEU A 1 43  ? -6.652  6.501   19.375  1.00 17.97  ? 61  LEU A HB3  1 
ATOM   627   H  HG   . LEU A 1 43  ? -7.135  8.207   17.188  1.00 18.75  ? 61  LEU A HG   1 
ATOM   628   H  HD11 . LEU A 1 43  ? -8.564  8.710   18.962  1.00 22.26  ? 61  LEU A HD11 1 
ATOM   629   H  HD12 . LEU A 1 43  ? -7.312  8.845   19.930  1.00 22.26  ? 61  LEU A HD12 1 
ATOM   630   H  HD13 . LEU A 1 43  ? -7.519  9.887   18.749  1.00 22.26  ? 61  LEU A HD13 1 
ATOM   631   H  HD21 . LEU A 1 43  ? -4.852  7.884   17.534  1.00 19.94  ? 61  LEU A HD21 1 
ATOM   632   H  HD22 . LEU A 1 43  ? -5.257  9.386   17.856  1.00 19.94  ? 61  LEU A HD22 1 
ATOM   633   H  HD23 . LEU A 1 43  ? -5.018  8.356   19.042  1.00 19.94  ? 61  LEU A HD23 1 
ATOM   634   N  N    . VAL A 1 44  ? -5.883  3.368   18.497  1.00 13.16  ? 62  VAL A N    1 
ATOM   635   C  CA   . VAL A 1 44  ? -6.172  1.979   18.813  1.00 12.78  ? 62  VAL A CA   1 
ATOM   636   C  C    . VAL A 1 44  ? -6.112  1.803   20.328  1.00 12.36  ? 62  VAL A C    1 
ATOM   637   O  O    . VAL A 1 44  ? -5.054  2.013   20.936  1.00 13.33  ? 62  VAL A O    1 
ATOM   638   C  CB   . VAL A 1 44  ? -5.207  0.999   18.113  1.00 13.73  ? 62  VAL A CB   1 
ATOM   639   C  CG1  . VAL A 1 44  ? -5.690  -0.434  18.297  1.00 14.37  ? 62  VAL A CG1  1 
ATOM   640   C  CG2  . VAL A 1 44  ? -5.057  1.341   16.632  1.00 15.03  ? 62  VAL A CG2  1 
ATOM   641   H  H    . VAL A 1 44  ? -5.087  3.611   18.714  1.00 15.79  ? 62  VAL A H    1 
ATOM   642   H  HA   . VAL A 1 44  ? -7.075  1.777   18.520  1.00 15.34  ? 62  VAL A HA   1 
ATOM   643   H  HB   . VAL A 1 44  ? -4.329  1.079   18.518  1.00 16.47  ? 62  VAL A HB   1 
ATOM   644   H  HG11 . VAL A 1 44  ? -5.060  -1.036  17.871  1.00 17.24  ? 62  VAL A HG11 1 
ATOM   645   H  HG12 . VAL A 1 44  ? -5.745  -0.629  19.245  1.00 17.24  ? 62  VAL A HG12 1 
ATOM   646   H  HG13 . VAL A 1 44  ? -6.565  -0.527  17.889  1.00 17.24  ? 62  VAL A HG13 1 
ATOM   647   H  HG21 . VAL A 1 44  ? -4.701  2.239   16.550  1.00 18.04  ? 62  VAL A HG21 1 
ATOM   648   H  HG22 . VAL A 1 44  ? -4.449  0.706   16.221  1.00 18.04  ? 62  VAL A HG22 1 
ATOM   649   H  HG23 . VAL A 1 44  ? -5.926  1.289   16.206  1.00 18.04  ? 62  VAL A HG23 1 
ATOM   650   N  N    . PRO A 1 45  ? -7.213  1.420   20.977  1.00 13.76  ? 63  PRO A N    1 
ATOM   651   C  CA   . PRO A 1 45  ? -7.309  1.494   22.440  1.00 13.24  ? 63  PRO A CA   1 
ATOM   652   C  C    . PRO A 1 45  ? -6.657  0.309   23.149  1.00 14.70  ? 63  PRO A C    1 
ATOM   653   O  O    . PRO A 1 45  ? -6.193  -0.661  22.539  1.00 14.39  ? 63  PRO A O    1 
ATOM   654   C  CB   . PRO A 1 45  ? -8.832  1.481   22.676  1.00 13.88  ? 63  PRO A CB   1 
ATOM   655   C  CG   . PRO A 1 45  ? -9.373  0.693   21.520  1.00 14.45  ? 63  PRO A CG   1 
ATOM   656   C  CD   . PRO A 1 45  ? -8.509  1.083   20.357  1.00 15.24  ? 63  PRO A CD   1 
ATOM   657   H  HA   . PRO A 1 45  ? -6.896  2.315   22.751  1.00 15.89  ? 63  PRO A HA   1 
ATOM   658   H  HB2  . PRO A 1 45  ? -9.036  1.050   23.520  1.00 16.66  ? 63  PRO A HB2  1 
ATOM   659   H  HB3  . PRO A 1 45  ? -9.178  2.388   22.674  1.00 16.66  ? 63  PRO A HB3  1 
ATOM   660   H  HG2  . PRO A 1 45  ? -9.302  -0.257  21.703  1.00 17.34  ? 63  PRO A HG2  1 
ATOM   661   H  HG3  . PRO A 1 45  ? -10.300 0.931   21.360  1.00 17.34  ? 63  PRO A HG3  1 
ATOM   662   H  HD2  . PRO A 1 45  ? -8.412  0.343   19.738  1.00 18.29  ? 63  PRO A HD2  1 
ATOM   663   H  HD3  . PRO A 1 45  ? -8.880  1.853   19.897  1.00 18.29  ? 63  PRO A HD3  1 
ATOM   664   N  N    . GLY A 1 46  ? -6.674  0.397   24.479  1.00 14.10  ? 64  GLY A N    1 
ATOM   665   C  CA   . GLY A 1 46  ? -6.098  -0.628  25.320  1.00 14.03  ? 64  GLY A CA   1 
ATOM   666   C  C    . GLY A 1 46  ? -7.113  -1.672  25.784  1.00 14.10  ? 64  GLY A C    1 
ATOM   667   O  O    . GLY A 1 46  ? -8.327  -1.546  25.615  1.00 15.31  ? 64  GLY A O    1 
ATOM   668   H  H    . GLY A 1 46  ? -7.020  1.052   24.917  1.00 16.92  ? 64  GLY A H    1 
ATOM   669   H  HA2  . GLY A 1 46  ? -5.398  -1.085  24.828  1.00 16.84  ? 64  GLY A HA2  1 
ATOM   670   H  HA3  . GLY A 1 46  ? -5.711  -0.212  26.107  1.00 16.84  ? 64  GLY A HA3  1 
ATOM   671   N  N    . THR A 1 47  ? -6.581  -2.720  26.405  1.00 15.38  ? 65  THR A N    1 
ATOM   672   C  CA   . THR A 1 47  ? -7.410  -3.814  26.889  1.00 15.74  ? 65  THR A CA   1 
ATOM   673   C  C    . THR A 1 47  ? -8.450  -3.295  27.873  1.00 15.41  ? 65  THR A C    1 
ATOM   674   O  O    . THR A 1 47  ? -8.143  -2.505  28.771  1.00 16.49  ? 65  THR A O    1 
ATOM   675   C  CB   . THR A 1 47  ? -6.528  -4.837  27.612  1.00 16.13  ? 65  THR A CB   1 
ATOM   676   O  OG1  . THR A 1 47  ? -5.414  -5.200  26.786  1.00 17.73  ? 65  THR A OG1  1 
ATOM   677   C  CG2  . THR A 1 47  ? -7.324  -6.090  27.974  1.00 17.92  ? 65  THR A CG2  1 
ATOM   678   H  H    . THR A 1 47  ? -5.741  -2.821  26.558  1.00 18.45  ? 65  THR A H    1 
ATOM   679   H  HA   . THR A 1 47  ? -7.860  -4.235  26.140  1.00 18.89  ? 65  THR A HA   1 
ATOM   680   H  HB   . THR A 1 47  ? -6.200  -4.440  28.434  1.00 19.35  ? 65  THR A HB   1 
ATOM   681   H  HG1  . THR A 1 47  ? -4.946  -4.522  26.622  1.00 21.27  ? 65  THR A HG1  1 
ATOM   682   H  HG21 . THR A 1 47  ? -7.989  -5.878  28.647  1.00 21.51  ? 65  THR A HG21 1 
ATOM   683   H  HG22 . THR A 1 47  ? -7.772  -6.437  27.186  1.00 21.51  ? 65  THR A HG22 1 
ATOM   684   H  HG23 . THR A 1 47  ? -6.729  -6.772  28.323  1.00 21.51  ? 65  THR A HG23 1 
ATOM   685   N  N    . GLY A 1 48  ? -9.687  -3.762  27.713  1.00 15.41  ? 66  GLY A N    1 
ATOM   686   C  CA   . GLY A 1 48  ? -10.743 -3.405  28.633  1.00 15.97  ? 66  GLY A CA   1 
ATOM   687   C  C    . GLY A 1 48  ? -11.395 -2.070  28.367  1.00 16.62  ? 66  GLY A C    1 
ATOM   688   O  O    . GLY A 1 48  ? -12.139 -1.585  29.225  1.00 18.55  ? 66  GLY A O    1 
ATOM   689   H  H    . GLY A 1 48  ? -9.932  -4.287  27.078  1.00 18.49  ? 66  GLY A H    1 
ATOM   690   H  HA2  . GLY A 1 48  ? -11.433 -4.084  28.591  1.00 19.16  ? 66  GLY A HA2  1 
ATOM   691   H  HA3  . GLY A 1 48  ? -10.377 -3.381  29.531  1.00 19.16  ? 66  GLY A HA3  1 
ATOM   692   N  N    . THR A 1 49  ? -11.168 -1.474  27.200  1.00 16.60  ? 67  THR A N    1 
ATOM   693   C  CA   . THR A 1 49  ? -11.751 -0.180  26.894  1.00 15.45  ? 67  THR A CA   1 
ATOM   694   C  C    . THR A 1 49  ? -12.238 -0.147  25.454  1.00 15.35  ? 67  THR A C    1 
ATOM   695   O  O    . THR A 1 49  ? -11.847 -0.964  24.617  1.00 16.24  ? 67  THR A O    1 
ATOM   696   C  CB   . THR A 1 49  ? -10.738 0.967   27.040  1.00 16.69  ? 67  THR A CB   1 
ATOM   697   O  OG1  . THR A 1 49  ? -9.744  0.857   26.012  1.00 16.43  ? 67  THR A OG1  1 
ATOM   698   C  CG2  . THR A 1 49  ? -10.072 0.944   28.398  1.00 17.24  ? 67  THR A CG2  1 
ATOM   699   H  H    . THR A 1 49  ? -10.679 -1.801  26.573  1.00 19.92  ? 67  THR A H    1 
ATOM   700   H  HA   . THR A 1 49  ? -12.497 -0.057  27.502  1.00 18.54  ? 67  THR A HA   1 
ATOM   701   H  HB   . THR A 1 49  ? -11.201 1.816   26.957  1.00 20.02  ? 67  THR A HB   1 
ATOM   702   H  HG1  . THR A 1 49  ? -9.290  1.563   25.975  1.00 19.72  ? 67  THR A HG1  1 
ATOM   703   H  HG21 . THR A 1 49  ? -9.538  0.140   28.492  1.00 20.69  ? 67  THR A HG21 1 
ATOM   704   H  HG22 . THR A 1 49  ? -9.496  1.718   28.499  1.00 20.69  ? 67  THR A HG22 1 
ATOM   705   H  HG23 . THR A 1 49  ? -10.744 0.959   29.098  1.00 20.69  ? 67  THR A HG23 1 
ATOM   706   N  N    . THR A 1 50  ? -13.092 0.836   25.185  1.00 15.04  ? 68  THR A N    1 
ATOM   707   C  CA   . THR A 1 50  ? -13.414 1.284   23.843  1.00 14.62  ? 68  THR A CA   1 
ATOM   708   C  C    . THR A 1 50  ? -12.458 2.416   23.465  1.00 15.03  ? 68  THR A C    1 
ATOM   709   O  O    . THR A 1 50  ? -11.715 2.943   24.299  1.00 16.37  ? 68  THR A O    1 
ATOM   710   C  CB   . THR A 1 50  ? -14.836 1.833   23.811  1.00 15.93  ? 68  THR A CB   1 
ATOM   711   O  OG1  . THR A 1 50  ? -14.882 2.987   24.659  1.00 15.91  ? 68  THR A OG1  1 
ATOM   712   C  CG2  . THR A 1 50  ? -15.851 0.775   24.275  1.00 17.98  ? 68  THR A CG2  1 
ATOM   713   H  H    . THR A 1 50  ? -13.515 1.275   25.792  1.00 18.05  ? 68  THR A H    1 
ATOM   714   H  HA   . THR A 1 50  ? -13.337 0.546   23.219  1.00 17.55  ? 68  THR A HA   1 
ATOM   715   H  HB   . THR A 1 50  ? -15.088 2.076   22.907  1.00 19.11  ? 68  THR A HB   1 
ATOM   716   H  HG1  . THR A 1 50  ? -15.661 3.300   24.676  1.00 19.10  ? 68  THR A HG1  1 
ATOM   717   H  HG21 . THR A 1 50  ? -15.781 0.646   25.234  1.00 21.58  ? 68  THR A HG21 1 
ATOM   718   H  HG22 . THR A 1 50  ? -16.752 1.065   24.061  1.00 21.58  ? 68  THR A HG22 1 
ATOM   719   H  HG23 . THR A 1 50  ? -15.678 -0.069  23.830  1.00 21.58  ? 68  THR A HG23 1 
ATOM   720   N  N    . GLY A 1 51  ? -12.511 2.815   22.198  1.00 15.71  ? 69  GLY A N    1 
ATOM   721   C  CA   . GLY A 1 51  ? -11.769 3.961   21.726  1.00 15.73  ? 69  GLY A CA   1 
ATOM   722   C  C    . GLY A 1 51  ? -11.996 5.204   22.568  1.00 15.06  ? 69  GLY A C    1 
ATOM   723   O  O    . GLY A 1 51  ? -11.046 5.832   23.055  1.00 14.87  ? 69  GLY A O    1 
ATOM   724   H  H    . GLY A 1 51  ? -12.978 2.428   21.589  1.00 18.86  ? 69  GLY A H    1 
ATOM   725   H  HA2  . GLY A 1 51  ? -10.822 3.755   21.740  1.00 18.88  ? 69  GLY A HA2  1 
ATOM   726   H  HA3  . GLY A 1 51  ? -12.036 4.159   20.815  1.00 18.88  ? 69  GLY A HA3  1 
ATOM   727   N  N    . PRO A 1 52  ? -13.260 5.588   22.765  1.00 14.91  ? 70  PRO A N    1 
ATOM   728   C  CA   . PRO A 1 52  ? -13.521 6.777   23.600  1.00 15.15  ? 70  PRO A CA   1 
ATOM   729   C  C    . PRO A 1 52  ? -13.021 6.635   25.027  1.00 15.37  ? 70  PRO A C    1 
ATOM   730   O  O    . PRO A 1 52  ? -12.492 7.597   25.596  1.00 16.15  ? 70  PRO A O    1 
ATOM   731   C  CB   . PRO A 1 52  ? -15.048 6.932   23.532  1.00 15.88  ? 70  PRO A CB   1 
ATOM   732   C  CG   . PRO A 1 52  ? -15.439 6.259   22.247  1.00 15.44  ? 70  PRO A CG   1 
ATOM   733   C  CD   . PRO A 1 52  ? -14.478 5.109   22.086  1.00 14.01  ? 70  PRO A CD   1 
ATOM   734   H  HA   . PRO A 1 52  ? -13.107 7.555   23.196  1.00 18.18  ? 70  PRO A HA   1 
ATOM   735   H  HB2  . PRO A 1 52  ? -15.460 6.495   24.294  1.00 19.05  ? 70  PRO A HB2  1 
ATOM   736   H  HB3  . PRO A 1 52  ? -15.286 7.872   23.520  1.00 19.05  ? 70  PRO A HB3  1 
ATOM   737   H  HG2  . PRO A 1 52  ? -16.352 5.938   22.308  1.00 18.53  ? 70  PRO A HG2  1 
ATOM   738   H  HG3  . PRO A 1 52  ? -15.355 6.884   21.510  1.00 18.53  ? 70  PRO A HG3  1 
ATOM   739   H  HD2  . PRO A 1 52  ? -14.820 4.309   22.516  1.00 16.81  ? 70  PRO A HD2  1 
ATOM   740   H  HD3  . PRO A 1 52  ? -14.304 4.932   21.148  1.00 16.81  ? 70  PRO A HD3  1 
ATOM   741   N  N    . GLN A 1 53  ? -13.162 5.455   25.628  1.00 15.12  ? 71  GLN A N    1 
ATOM   742   C  CA   . GLN A 1 53  ? -12.680 5.287   26.997  1.00 15.24  ? 71  GLN A CA   1 
ATOM   743   C  C    . GLN A 1 53  ? -11.164 5.416   27.079  1.00 15.56  ? 71  GLN A C    1 
ATOM   744   O  O    . GLN A 1 53  ? -10.634 5.947   28.066  1.00 16.52  ? 71  GLN A O    1 
ATOM   745   C  CB   . GLN A 1 53  ? -13.157 3.951   27.554  1.00 16.60  ? 71  GLN A CB   1 
ATOM   746   C  CG   . GLN A 1 53  ? -14.652 3.917   27.786  1.00 18.14  ? 71  GLN A CG   1 
ATOM   747   C  CD   . GLN A 1 53  ? -15.155 2.534   28.135  1.00 19.44  ? 71  GLN A CD   1 
ATOM   748   O  OE1  . GLN A 1 53  ? -14.573 1.530   27.729  1.00 19.15  ? 71  GLN A OE1  1 
ATOM   749   N  NE2  . GLN A 1 53  ? -16.240 2.474   28.894  1.00 23.10  ? 71  GLN A NE2  1 
ATOM   750   H  H    . GLN A 1 53  ? -13.521 4.757   25.277  1.00 18.14  ? 71  GLN A H    1 
ATOM   751   H  HA   . GLN A 1 53  ? -13.057 5.988   27.552  1.00 18.29  ? 71  GLN A HA   1 
ATOM   752   H  HB2  . GLN A 1 53  ? -12.934 3.248   26.924  1.00 19.92  ? 71  GLN A HB2  1 
ATOM   753   H  HB3  . GLN A 1 53  ? -12.717 3.787   28.403  1.00 19.92  ? 71  GLN A HB3  1 
ATOM   754   H  HG2  . GLN A 1 53  ? -14.872 4.511   28.521  1.00 21.77  ? 71  GLN A HG2  1 
ATOM   755   H  HG3  . GLN A 1 53  ? -15.105 4.206   26.978  1.00 21.77  ? 71  GLN A HG3  1 
ATOM   756   H  HE21 . GLN A 1 53  ? -16.619 3.199   29.160  1.00 27.72  ? 71  GLN A HE21 1 
ATOM   757   H  HE22 . GLN A 1 53  ? -16.565 1.711   29.119  1.00 27.72  ? 71  GLN A HE22 1 
ATOM   758   N  N    . SER A 1 54  ? -10.443 4.936   26.061  1.00 14.41  ? 72  SER A N    1 
ATOM   759   C  CA   . SER A 1 54  ? -8.992  5.094   26.073  1.00 15.04  ? 72  SER A CA   1 
ATOM   760   C  C    . SER A 1 54  ? -8.579  6.542   25.832  1.00 14.91  ? 72  SER A C    1 
ATOM   761   O  O    . SER A 1 54  ? -7.610  7.014   26.432  1.00 14.87  ? 72  SER A O    1 
ATOM   762   C  CB   . SER A 1 54  ? -8.332  4.202   25.021  1.00 15.42  ? 72  SER A CB   1 
ATOM   763   O  OG   . SER A 1 54  ? -8.092  2.894   25.500  1.00 15.24  ? 72  SER A OG   1 
ATOM   764   H  H    . SER A 1 54  ? -10.762 4.527   25.375  1.00 17.29  ? 72  SER A H    1 
ATOM   765   H  HA   . SER A 1 54  ? -8.680  4.817   26.949  1.00 18.04  ? 72  SER A HA   1 
ATOM   766   H  HB2  . SER A 1 54  ? -8.918  4.147   24.250  1.00 18.50  ? 72  SER A HB2  1 
ATOM   767   H  HB3  . SER A 1 54  ? -7.484  4.599   24.766  1.00 18.50  ? 72  SER A HB3  1 
ATOM   768   H  HG   . SER A 1 54  ? -7.668  2.926   26.225  1.00 18.29  ? 72  SER A HG   1 
ATOM   769   N  N    . PHE A 1 55  ? -9.284  7.267   24.948  1.00 14.05  ? 73  PHE A N    1 
ATOM   770   C  CA   . PHE A 1 55  ? -8.718  8.485   24.375  1.00 13.94  ? 73  PHE A CA   1 
ATOM   771   C  C    . PHE A 1 55  ? -9.519  9.770   24.563  1.00 14.31  ? 73  PHE A C    1 
ATOM   772   O  O    . PHE A 1 55  ? -8.988  10.849  24.258  1.00 14.60  ? 73  PHE A O    1 
ATOM   773   C  CB   . PHE A 1 55  ? -8.448  8.268   22.876  1.00 13.39  ? 73  PHE A CB   1 
ATOM   774   C  CG   . PHE A 1 55  ? -7.514  7.122   22.589  1.00 14.31  ? 73  PHE A CG   1 
ATOM   775   C  CD1  . PHE A 1 55  ? -6.195  7.161   23.010  1.00 15.19  ? 73  PHE A CD1  1 
ATOM   776   C  CD2  . PHE A 1 55  ? -7.958  6.005   21.906  1.00 13.85  ? 73  PHE A CD2  1 
ATOM   777   C  CE1  . PHE A 1 55  ? -5.337  6.113   22.741  1.00 14.16  ? 73  PHE A CE1  1 
ATOM   778   C  CE2  . PHE A 1 55  ? -7.105  4.954   21.635  1.00 14.32  ? 73  PHE A CE2  1 
ATOM   779   C  CZ   . PHE A 1 55  ? -5.794  5.007   22.053  1.00 14.17  ? 73  PHE A CZ   1 
ATOM   780   H  H    . PHE A 1 55  ? -10.076 7.072   24.675  1.00 16.86  ? 73  PHE A H    1 
ATOM   781   H  HA   . PHE A 1 55  ? -7.877  8.651   24.830  1.00 16.73  ? 73  PHE A HA   1 
ATOM   782   H  HB2  . PHE A 1 55  ? -9.289  8.084   22.431  1.00 16.07  ? 73  PHE A HB2  1 
ATOM   783   H  HB3  . PHE A 1 55  ? -8.049  9.074   22.512  1.00 16.07  ? 73  PHE A HB3  1 
ATOM   784   H  HD1  . PHE A 1 55  ? -5.884  7.902   23.478  1.00 18.22  ? 73  PHE A HD1  1 
ATOM   785   H  HD2  . PHE A 1 55  ? -8.844  5.961   21.625  1.00 16.62  ? 73  PHE A HD2  1 
ATOM   786   H  HE1  . PHE A 1 55  ? -4.452  6.152   23.024  1.00 16.99  ? 73  PHE A HE1  1 
ATOM   787   H  HE2  . PHE A 1 55  ? -7.416  4.211   21.170  1.00 17.18  ? 73  PHE A HE2  1 
ATOM   788   H  HZ   . PHE A 1 55  ? -5.218  4.299   21.872  1.00 17.01  ? 73  PHE A HZ   1 
ATOM   789   N  N    . ASP A 1 56  ? -10.753 9.705   25.069  1.00 15.39  ? 74  ASP A N    1 
ATOM   790   C  CA   . ASP A 1 56  ? -11.537 10.925  25.248  1.00 16.69  ? 74  ASP A CA   1 
ATOM   791   C  C    . ASP A 1 56  ? -10.799 11.928  26.124  1.00 17.39  ? 74  ASP A C    1 
ATOM   792   O  O    . ASP A 1 56  ? -10.912 13.145  25.925  1.00 18.57  ? 74  ASP A O    1 
ATOM   793   C  CB   . ASP A 1 56  ? -12.878 10.606  25.908  1.00 18.11  ? 74  ASP A CB   1 
ATOM   794   C  CG   . ASP A 1 56  ? -13.959 10.220  24.921  1.00 19.33  ? 74  ASP A CG   1 
ATOM   795   O  OD1  . ASP A 1 56  ? -13.752 10.330  23.691  1.00 20.23  ? 74  ASP A OD1  1 
ATOM   796   O  OD2  . ASP A 1 56  ? -15.042 9.828   25.401  1.00 20.40  ? 74  ASP A OD2  1 
ATOM   797   H  H    . ASP A 1 56  ? -11.151 8.982   25.311  1.00 18.47  ? 74  ASP A H    1 
ATOM   798   H  HA   . ASP A 1 56  ? -11.695 11.308  24.371  1.00 20.02  ? 74  ASP A HA   1 
ATOM   799   H  HB2  . ASP A 1 56  ? -12.757 9.864   26.521  1.00 21.73  ? 74  ASP A HB2  1 
ATOM   800   H  HB3  . ASP A 1 56  ? -13.183 11.390  26.391  1.00 21.73  ? 74  ASP A HB3  1 
ATOM   801   N  N    . SER A 1 57  ? -10.065 11.436  27.118  1.00 17.61  ? 75  SER A N    1 
ATOM   802   C  CA   . SER A 1 57  ? -9.423  12.294  28.099  1.00 18.16  ? 75  SER A CA   1 
ATOM   803   C  C    . SER A 1 57  ? -8.020  12.706  27.696  1.00 18.57  ? 75  SER A C    1 
ATOM   804   O  O    . SER A 1 57  ? -7.335  13.364  28.486  1.00 19.36  ? 75  SER A O    1 
ATOM   805   C  CB   . SER A 1 57  ? -9.356  11.595  29.460  1.00 17.87  ? 75  SER A CB   1 
ATOM   806   O  OG   . SER A 1 57  ? -8.500  10.463  29.412  1.00 17.86  ? 75  SER A OG   1 
ATOM   807   H  H    . SER A 1 57  ? -9.924  10.598  27.245  1.00 21.13  ? 75  SER A H    1 
ATOM   808   H  HA   . SER A 1 57  ? -9.963  13.094  28.195  1.00 21.79  ? 75  SER A HA   1 
ATOM   809   H  HB2  . SER A 1 57  ? -9.015  12.220  30.118  1.00 21.45  ? 75  SER A HB2  1 
ATOM   810   H  HB3  . SER A 1 57  ? -10.248 11.305  29.708  1.00 21.45  ? 75  SER A HB3  1 
ATOM   811   H  HG   . SER A 1 57  ? -8.805  9.894   28.875  1.00 21.43  ? 75  SER A HG   1 
ATOM   812   N  N    . ASN A 1 58  ? -7.576  12.343  26.496  1.00 16.34  ? 76  ASN A N    1 
ATOM   813   C  CA   . ASN A 1 58  ? -6.193  12.597  26.115  1.00 15.90  ? 76  ASN A CA   1 
ATOM   814   C  C    . ASN A 1 58  ? -6.079  12.829  24.611  1.00 15.12  ? 76  ASN A C    1 
ATOM   815   O  O    . ASN A 1 58  ? -6.266  13.959  24.148  1.00 15.91  ? 76  ASN A O    1 
ATOM   816   C  CB   . ASN A 1 58  ? -5.267  11.484  26.650  1.00 15.39  ? 76  ASN A CB   1 
ATOM   817   C  CG   . ASN A 1 58  ? -5.790  10.082  26.384  1.00 15.91  ? 76  ASN A CG   1 
ATOM   818   O  OD1  . ASN A 1 58  ? -5.560  9.526   25.317  1.00 16.31  ? 76  ASN A OD1  1 
ATOM   819   N  ND2  . ASN A 1 58  ? -6.445  9.485   27.377  1.00 15.95  ? 76  ASN A ND2  1 
ATOM   820   H  H    . ASN A 1 58  ? -8.050  11.952  25.894  1.00 19.61  ? 76  ASN A H    1 
ATOM   821   H  HA   . ASN A 1 58  ? -5.876  13.416  26.528  1.00 19.08  ? 76  ASN A HA   1 
ATOM   822   H  HB2  . ASN A 1 58  ? -4.400  11.564  26.222  1.00 18.47  ? 76  ASN A HB2  1 
ATOM   823   H  HB3  . ASN A 1 58  ? -5.173  11.588  27.610  1.00 18.47  ? 76  ASN A HB3  1 
ATOM   824   H  HD21 . ASN A 1 58  ? -6.556  9.892   28.126  1.00 19.14  ? 76  ASN A HD21 1 
ATOM   825   H  HD22 . ASN A 1 58  ? -6.759  8.691   27.269  1.00 19.14  ? 76  ASN A HD22 1 
ATOM   826   N  N    . TRP A 1 59  ? -5.787  11.789  23.832  1.00 14.75  ? 77  TRP A N    1 
ATOM   827   C  CA   . TRP A 1 59  ? -5.350  12.016  22.454  1.00 15.25  ? 77  TRP A CA   1 
ATOM   828   C  C    . TRP A 1 59  ? -6.462  12.353  21.465  1.00 16.00  ? 77  TRP A C    1 
ATOM   829   O  O    . TRP A 1 59  ? -6.142  12.836  20.378  1.00 15.80  ? 77  TRP A O    1 
ATOM   830   C  CB   . TRP A 1 59  ? -4.479  10.852  21.971  1.00 15.71  ? 77  TRP A CB   1 
ATOM   831   C  CG   . TRP A 1 59  ? -3.136  10.940  22.607  1.00 15.18  ? 77  TRP A CG   1 
ATOM   832   C  CD1  . TRP A 1 59  ? -2.700  10.264  23.713  1.00 15.28  ? 77  TRP A CD1  1 
ATOM   833   C  CD2  . TRP A 1 59  ? -2.064  11.793  22.208  1.00 15.25  ? 77  TRP A CD2  1 
ATOM   834   N  NE1  . TRP A 1 59  ? -1.420  10.646  24.024  1.00 15.50  ? 77  TRP A NE1  1 
ATOM   835   C  CE2  . TRP A 1 59  ? -1.006  11.583  23.112  1.00 15.07  ? 77  TRP A CE2  1 
ATOM   836   C  CE3  . TRP A 1 59  ? -1.895  12.720  21.174  1.00 15.52  ? 77  TRP A CE3  1 
ATOM   837   C  CZ2  . TRP A 1 59  ? 0.201   12.252  23.005  1.00 14.86  ? 77  TRP A CZ2  1 
ATOM   838   C  CZ3  . TRP A 1 59  ? -0.702  13.388  21.078  1.00 16.12  ? 77  TRP A CZ3  1 
ATOM   839   C  CH2  . TRP A 1 59  ? 0.334   13.151  21.986  1.00 15.01  ? 77  TRP A CH2  1 
ATOM   840   H  H    . TRP A 1 59  ? -5.832  10.964  24.071  1.00 17.70  ? 77  TRP A H    1 
ATOM   841   H  HA   . TRP A 1 59  ? -4.784  12.803  22.451  1.00 18.31  ? 77  TRP A HA   1 
ATOM   842   H  HB2  . TRP A 1 59  ? -4.889  10.009  22.219  1.00 18.86  ? 77  TRP A HB2  1 
ATOM   843   H  HB3  . TRP A 1 59  ? -4.374  10.898  21.007  1.00 18.86  ? 77  TRP A HB3  1 
ATOM   844   H  HD1  . TRP A 1 59  ? -3.198  9.637   24.185  1.00 18.34  ? 77  TRP A HD1  1 
ATOM   845   H  HE1  . TRP A 1 59  ? -0.954  10.347  24.682  1.00 18.61  ? 77  TRP A HE1  1 
ATOM   846   H  HE3  . TRP A 1 59  ? -2.578  12.879  20.563  1.00 18.62  ? 77  TRP A HE3  1 
ATOM   847   H  HZ2  . TRP A 1 59  ? 0.895   12.094  23.603  1.00 17.83  ? 77  TRP A HZ2  1 
ATOM   848   H  HZ3  . TRP A 1 59  ? -0.579  14.009  20.397  1.00 19.34  ? 77  TRP A HZ3  1 
ATOM   849   H  HH2  . TRP A 1 59  ? 1.133   13.617  21.894  1.00 18.01  ? 77  TRP A HH2  1 
ATOM   850   N  N    . ILE A 1 60  ? -7.738  12.165  21.796  1.00 16.04  ? 78  ILE A N    1 
ATOM   851   C  CA   . ILE A 1 60  ? -8.797  12.704  20.939  1.00 15.78  ? 78  ILE A CA   1 
ATOM   852   C  C    . ILE A 1 60  ? -8.700  14.227  20.937  1.00 15.29  ? 78  ILE A C    1 
ATOM   853   O  O    . ILE A 1 60  ? -8.473  14.813  19.874  1.00 16.77  ? 78  ILE A O    1 
ATOM   854   C  CB   . ILE A 1 60  ? -10.188 12.170  21.316  1.00 15.37  ? 78  ILE A CB   1 
ATOM   855   C  CG1  . ILE A 1 60  ? -10.323 10.732  20.795  1.00 15.56  ? 78  ILE A CG1  1 
ATOM   856   C  CG2  . ILE A 1 60  ? -11.287 13.060  20.739  1.00 16.80  ? 78  ILE A CG2  1 
ATOM   857   C  CD1  . ILE A 1 60  ? -11.508 9.970   21.334  1.00 16.14  ? 78  ILE A CD1  1 
ATOM   858   H  H    . ILE A 1 60  ? -8.010  11.740  22.493  1.00 19.25  ? 78  ILE A H    1 
ATOM   859   H  HA   . ILE A 1 60  ? -8.648  12.411  20.026  1.00 18.94  ? 78  ILE A HA   1 
ATOM   860   H  HB   . ILE A 1 60  ? -10.282 12.177  22.281  1.00 18.44  ? 78  ILE A HB   1 
ATOM   861   H  HG12 . ILE A 1 60  ? -10.411 10.762  19.830  1.00 18.67  ? 78  ILE A HG12 1 
ATOM   862   H  HG13 . ILE A 1 60  ? -9.524  10.240  21.041  1.00 18.67  ? 78  ILE A HG13 1 
ATOM   863   H  HG21 . ILE A 1 60  ? -11.298 13.901  21.221  1.00 20.16  ? 78  ILE A HG21 1 
ATOM   864   H  HG22 . ILE A 1 60  ? -11.105 13.219  19.800  1.00 20.16  ? 78  ILE A HG22 1 
ATOM   865   H  HG23 . ILE A 1 60  ? -12.141 12.611  20.839  1.00 20.16  ? 78  ILE A HG23 1 
ATOM   866   H  HD11 . ILE A 1 60  ? -11.471 9.058   21.006  1.00 19.36  ? 78  ILE A HD11 1 
ATOM   867   H  HD12 . ILE A 1 60  ? -11.472 9.976   22.303  1.00 19.36  ? 78  ILE A HD12 1 
ATOM   868   H  HD13 . ILE A 1 60  ? -12.323 10.399  21.030  1.00 19.36  ? 78  ILE A HD13 1 
ATOM   869   N  N    . PRO A 1 61  ? -8.828  14.910  22.082  1.00 16.39  ? 79  PRO A N    1 
ATOM   870   C  CA   . PRO A 1 61  ? -8.669  16.377  22.052  1.00 16.84  ? 79  PRO A CA   1 
ATOM   871   C  C    . PRO A 1 61  ? -7.267  16.829  21.671  1.00 16.51  ? 79  PRO A C    1 
ATOM   872   O  O    . PRO A 1 61  ? -7.121  17.820  20.947  1.00 17.47  ? 79  PRO A O    1 
ATOM   873   C  CB   . PRO A 1 61  ? -9.065  16.821  23.471  1.00 16.53  ? 79  PRO A CB   1 
ATOM   874   C  CG   . PRO A 1 61  ? -8.970  15.582  24.314  1.00 16.62  ? 79  PRO A CG   1 
ATOM   875   C  CD   . PRO A 1 61  ? -9.249  14.417  23.406  1.00 16.72  ? 79  PRO A CD   1 
ATOM   876   H  HA   . PRO A 1 61  ? -9.303  16.755  21.422  1.00 20.20  ? 79  PRO A HA   1 
ATOM   877   H  HB2  . PRO A 1 61  ? -8.450  17.502  23.786  1.00 19.84  ? 79  PRO A HB2  1 
ATOM   878   H  HB3  . PRO A 1 61  ? -9.970  17.168  23.467  1.00 19.84  ? 79  PRO A HB3  1 
ATOM   879   H  HG2  . PRO A 1 61  ? -8.078  15.514  24.690  1.00 19.94  ? 79  PRO A HG2  1 
ATOM   880   H  HG3  . PRO A 1 61  ? -9.627  15.624  25.026  1.00 19.94  ? 79  PRO A HG3  1 
ATOM   881   H  HD2  . PRO A 1 61  ? -8.728  13.642  23.668  1.00 20.06  ? 79  PRO A HD2  1 
ATOM   882   H  HD3  . PRO A 1 61  ? -10.194 14.197  23.407  1.00 20.06  ? 79  PRO A HD3  1 
ATOM   883   N  N    . LEU A 1 62  ? -6.220  16.144  22.138  1.00 16.38  ? 80  LEU A N    1 
ATOM   884   C  CA   . LEU A 1 62  ? -4.869  16.627  21.857  1.00 16.84  ? 80  LEU A CA   1 
ATOM   885   C  C    . LEU A 1 62  ? -4.536  16.519  20.371  1.00 17.13  ? 80  LEU A C    1 
ATOM   886   O  O    . LEU A 1 62  ? -3.934  17.433  19.798  1.00 18.75  ? 80  LEU A O    1 
ATOM   887   C  CB   . LEU A 1 62  ? -3.849  15.893  22.726  1.00 16.79  ? 80  LEU A CB   1 
ATOM   888   C  CG   . LEU A 1 62  ? -3.916  16.187  24.225  1.00 17.66  ? 80  LEU A CG   1 
ATOM   889   C  CD1  . LEU A 1 62  ? -3.066  15.178  24.970  1.00 16.90  ? 80  LEU A CD1  1 
ATOM   890   C  CD2  . LEU A 1 62  ? -3.459  17.598  24.536  1.00 18.85  ? 80  LEU A CD2  1 
ATOM   891   H  H    . LEU A 1 62  ? -6.264  15.423  22.604  1.00 19.66  ? 80  LEU A H    1 
ATOM   892   H  HA   . LEU A 1 62  ? -4.815  17.566  22.094  1.00 20.21  ? 80  LEU A HA   1 
ATOM   893   H  HB2  . LEU A 1 62  ? -3.986  14.939  22.614  1.00 20.15  ? 80  LEU A HB2  1 
ATOM   894   H  HB3  . LEU A 1 62  ? -2.961  16.139  22.424  1.00 20.15  ? 80  LEU A HB3  1 
ATOM   895   H  HG   . LEU A 1 62  ? -4.836  16.115  24.523  1.00 21.19  ? 80  LEU A HG   1 
ATOM   896   H  HD11 . LEU A 1 62  ? -2.130  15.371  24.806  1.00 20.28  ? 80  LEU A HD11 1 
ATOM   897   H  HD12 . LEU A 1 62  ? -3.256  15.244  25.919  1.00 20.28  ? 80  LEU A HD12 1 
ATOM   898   H  HD13 . LEU A 1 62  ? -3.281  14.287  24.651  1.00 20.28  ? 80  LEU A HD13 1 
ATOM   899   H  HD21 . LEU A 1 62  ? -2.588  17.744  24.134  1.00 22.62  ? 80  LEU A HD21 1 
ATOM   900   H  HD22 . LEU A 1 62  ? -4.102  18.226  24.171  1.00 22.62  ? 80  LEU A HD22 1 
ATOM   901   H  HD23 . LEU A 1 62  ? -3.401  17.706  25.498  1.00 22.62  ? 80  LEU A HD23 1 
ATOM   902   N  N    . SER A 1 63  ? -4.929  15.423  19.717  1.00 17.35  ? 81  SER A N    1 
ATOM   903   C  CA   . SER A 1 63  ? -4.676  15.328  18.281  1.00 17.46  ? 81  SER A CA   1 
ATOM   904   C  C    . SER A 1 63  ? -5.548  16.307  17.502  1.00 18.27  ? 81  SER A C    1 
ATOM   905   O  O    . SER A 1 63  ? -5.107  16.850  16.484  1.00 18.01  ? 81  SER A O    1 
ATOM   906   C  CB   . SER A 1 63  ? -4.848  13.891  17.787  1.00 18.44  ? 81  SER A CB   1 
ATOM   907   O  OG   . SER A 1 63  ? -6.203  13.513  17.729  1.00 19.12  ? 81  SER A OG   1 
ATOM   908   H  H    . SER A 1 63  ? -5.329  14.747  20.068  1.00 20.82  ? 81  SER A H    1 
ATOM   909   H  HA   . SER A 1 63  ? -3.750  15.560  18.108  1.00 20.96  ? 81  SER A HA   1 
ATOM   910   H  HB2  . SER A 1 63  ? -4.467  13.821  16.897  1.00 22.13  ? 81  SER A HB2  1 
ATOM   911   H  HB3  . SER A 1 63  ? -4.384  13.295  18.395  1.00 22.13  ? 81  SER A HB3  1 
ATOM   912   H  HG   . SER A 1 63  ? -6.510  13.427  18.506  1.00 22.94  ? 81  SER A HG   1 
ATOM   913   N  N    . THR A 1 64  ? -6.769  16.570  17.974  1.00 17.74  ? 82  THR A N    1 
ATOM   914   C  CA   . THR A 1 64  ? -7.593  17.591  17.334  1.00 17.98  ? 82  THR A CA   1 
ATOM   915   C  C    . THR A 1 64  ? -6.885  18.941  17.354  1.00 17.61  ? 82  THR A C    1 
ATOM   916   O  O    . THR A 1 64  ? -6.864  19.653  16.344  1.00 18.86  ? 82  THR A O    1 
ATOM   917   C  CB   . THR A 1 64  ? -8.948  17.688  18.038  1.00 18.82  ? 82  THR A CB   1 
ATOM   918   O  OG1  . THR A 1 64  ? -9.631  16.428  17.970  1.00 17.55  ? 82  THR A OG1  1 
ATOM   919   C  CG2  . THR A 1 64  ? -9.814  18.751  17.382  1.00 20.06  ? 82  THR A CG2  1 
ATOM   920   H  H    . THR A 1 64  ? -7.134  16.179  18.647  1.00 21.29  ? 82  THR A H    1 
ATOM   921   H  HA   . THR A 1 64  ? -7.753  17.340  16.411  1.00 21.58  ? 82  THR A HA   1 
ATOM   922   H  HB   . THR A 1 64  ? -8.805  17.927  18.967  1.00 22.59  ? 82  THR A HB   1 
ATOM   923   H  HG1  . THR A 1 64  ? -9.295  15.889  18.520  1.00 21.06  ? 82  THR A HG1  1 
ATOM   924   H  HG21 . THR A 1 64  ? -9.788  18.651  16.417  1.00 24.07  ? 82  THR A HG21 1 
ATOM   925   H  HG22 . THR A 1 64  ? -10.732 18.663  17.682  1.00 24.07  ? 82  THR A HG22 1 
ATOM   926   H  HG23 . THR A 1 64  ? -9.489  19.634  17.616  1.00 24.07  ? 82  THR A HG23 1 
ATOM   927   N  N    A GLN A 1 65  ? -6.282  19.301  18.485  0.64 17.75  ? 83  GLN A N    1 
ATOM   928   N  N    B GLN A 1 65  ? -6.296  19.307  18.502  0.36 18.49  ? 83  GLN A N    1 
ATOM   929   C  CA   A GLN A 1 65  ? -5.618  20.591  18.603  0.64 18.55  ? 83  GLN A CA   1 
ATOM   930   C  CA   B GLN A 1 65  ? -5.596  20.584  18.613  0.36 19.73  ? 83  GLN A CA   1 
ATOM   931   C  C    A GLN A 1 65  ? -4.297  20.640  17.850  0.64 19.42  ? 83  GLN A C    1 
ATOM   932   C  C    B GLN A 1 65  ? -4.408  20.653  17.664  0.36 19.45  ? 83  GLN A C    1 
ATOM   933   O  O    A GLN A 1 65  ? -3.709  21.725  17.739  0.64 21.21  ? 83  GLN A O    1 
ATOM   934   O  O    B GLN A 1 65  ? -4.039  21.741  17.204  0.36 19.75  ? 83  GLN A O    1 
ATOM   935   C  CB   A GLN A 1 65  ? -5.434  20.933  20.083  0.64 19.47  ? 83  GLN A CB   1 
ATOM   936   C  CB   B GLN A 1 65  ? -5.124  20.817  20.054  0.36 21.87  ? 83  GLN A CB   1 
ATOM   937   C  CG   A GLN A 1 65  ? -6.753  21.026  20.839  0.64 20.53  ? 83  GLN A CG   1 
ATOM   938   C  CG   B GLN A 1 65  ? -4.521  22.206  20.287  0.36 23.47  ? 83  GLN A CG   1 
ATOM   939   C  CD   A GLN A 1 65  ? -6.586  20.963  22.344  0.64 22.46  ? 83  GLN A CD   1 
ATOM   940   C  CD   B GLN A 1 65  ? -3.610  22.301  21.512  0.36 24.22  ? 83  GLN A CD   1 
ATOM   941   O  OE1  A GLN A 1 65  ? -5.581  21.419  22.890  0.64 23.22  ? 83  GLN A OE1  1 
ATOM   942   O  OE1  B GLN A 1 65  ? -3.517  21.374  22.323  0.36 23.10  ? 83  GLN A OE1  1 
ATOM   943   N  NE2  A GLN A 1 65  ? -7.581  20.404  23.025  0.64 22.22  ? 83  GLN A NE2  1 
ATOM   944   N  NE2  B GLN A 1 65  ? -2.930  23.438  21.643  0.36 25.60  ? 83  GLN A NE2  1 
ATOM   945   H  H    A GLN A 1 65  ? -6.245  18.817  19.195  0.64 21.30  ? 83  GLN A H    1 
ATOM   946   H  H    B GLN A 1 65  ? -6.290  18.837  19.221  0.36 22.18  ? 83  GLN A H    1 
ATOM   947   H  HA   A GLN A 1 65  ? -6.176  21.286  18.220  0.64 22.26  ? 83  GLN A HA   1 
ATOM   948   H  HA   B GLN A 1 65  ? -6.217  21.293  18.382  0.36 23.67  ? 83  GLN A HA   1 
ATOM   949   H  HB2  A GLN A 1 65  ? -4.897  20.242  20.501  0.64 23.37  ? 83  GLN A HB2  1 
ATOM   950   H  HB2  B GLN A 1 65  ? -5.883  20.719  20.650  0.36 26.24  ? 83  GLN A HB2  1 
ATOM   951   H  HB3  A GLN A 1 65  ? -4.987  21.791  20.155  0.64 23.37  ? 83  GLN A HB3  1 
ATOM   952   H  HB3  B GLN A 1 65  ? -4.445  20.159  20.270  0.36 26.24  ? 83  GLN A HB3  1 
ATOM   953   H  HG2  A GLN A 1 65  ? -7.181  21.869  20.622  0.64 24.63  ? 83  GLN A HG2  1 
ATOM   954   H  HG2  B GLN A 1 65  ? -3.994  22.450  19.510  0.36 28.16  ? 83  GLN A HG2  1 
ATOM   955   H  HG3  A GLN A 1 65  ? -7.322  20.287  20.572  0.64 24.63  ? 83  GLN A HG3  1 
ATOM   956   H  HG3  B GLN A 1 65  ? -5.244  22.841  20.410  0.36 28.16  ? 83  GLN A HG3  1 
ATOM   957   H  HE21 A GLN A 1 65  ? -8.271  20.103  22.609  0.64 26.67  ? 83  GLN A HE21 1 
ATOM   958   H  HE21 B GLN A 1 65  ? -3.019  24.063  21.059  0.36 30.72  ? 83  GLN A HE21 1 
ATOM   959   H  HE22 A GLN A 1 65  ? -7.535  20.344  23.881  0.64 26.67  ? 83  GLN A HE22 1 
ATOM   960   H  HE22 B GLN A 1 65  ? -2.401  23.548  22.313  0.36 30.72  ? 83  GLN A HE22 1 
ATOM   961   N  N    . LEU A 1 66  ? -3.838  19.507  17.311  1.00 19.56  ? 84  LEU A N    1 
ATOM   962   C  CA   . LEU A 1 66  ? -2.671  19.457  16.445  1.00 19.71  ? 84  LEU A CA   1 
ATOM   963   C  C    . LEU A 1 66  ? -3.072  19.420  14.973  1.00 20.71  ? 84  LEU A C    1 
ATOM   964   O  O    . LEU A 1 66  ? -2.201  19.320  14.105  1.00 22.34  ? 84  LEU A O    1 
ATOM   965   C  CB   . LEU A 1 66  ? -1.795  18.245  16.767  1.00 19.68  ? 84  LEU A CB   1 
ATOM   966   C  CG   . LEU A 1 66  ? -1.035  18.353  18.089  1.00 19.63  ? 84  LEU A CG   1 
ATOM   967   C  CD1  . LEU A 1 66  ? -0.346  17.044  18.404  1.00 21.05  ? 84  LEU A CD1  1 
ATOM   968   C  CD2  . LEU A 1 66  ? -0.028  19.494  18.039  1.00 21.09  ? 84  LEU A CD2  1 
ATOM   969   H  H    . LEU A 1 66  ? -4.198  18.736  17.439  1.00 23.47  ? 84  LEU A H    1 
ATOM   970   H  HA   . LEU A 1 66  ? -2.125  20.243  16.607  1.00 23.65  ? 84  LEU A HA   1 
ATOM   971   H  HB2  . LEU A 1 66  ? -2.362  17.459  16.816  1.00 23.61  ? 84  LEU A HB2  1 
ATOM   972   H  HB3  . LEU A 1 66  ? -1.141  18.139  16.059  1.00 23.61  ? 84  LEU A HB3  1 
ATOM   973   H  HG   . LEU A 1 66  ? -1.664  18.544  18.802  1.00 23.56  ? 84  LEU A HG   1 
ATOM   974   H  HD11 . LEU A 1 66  ? 0.149   17.140  19.233  1.00 25.26  ? 84  LEU A HD11 1 
ATOM   975   H  HD12 . LEU A 1 66  ? -1.016  16.349  18.498  1.00 25.26  ? 84  LEU A HD12 1 
ATOM   976   H  HD13 . LEU A 1 66  ? 0.260   16.824  17.680  1.00 25.26  ? 84  LEU A HD13 1 
ATOM   977   H  HD21 . LEU A 1 66  ? 0.512   19.403  17.238  1.00 25.31  ? 84  LEU A HD21 1 
ATOM   978   H  HD22 . LEU A 1 66  ? -0.507  20.337  18.021  1.00 25.31  ? 84  LEU A HD22 1 
ATOM   979   H  HD23 . LEU A 1 66  ? 0.537   19.451  18.826  1.00 25.31  ? 84  LEU A HD23 1 
ATOM   980   N  N    . GLY A 1 67  ? -4.370  19.485  14.671  1.00 19.84  ? 85  GLY A N    1 
ATOM   981   C  CA   . GLY A 1 67  ? -4.831  19.590  13.303  1.00 19.98  ? 85  GLY A CA   1 
ATOM   982   C  C    . GLY A 1 67  ? -5.322  18.310  12.662  1.00 20.57  ? 85  GLY A C    1 
ATOM   983   O  O    . GLY A 1 67  ? -5.651  18.329  11.469  1.00 23.07  ? 85  GLY A O    1 
ATOM   984   H  H    . GLY A 1 67  ? -5.003  19.469  15.252  1.00 23.81  ? 85  GLY A H    1 
ATOM   985   H  HA2  . GLY A 1 67  ? -5.563  20.227  13.276  1.00 23.98  ? 85  GLY A HA2  1 
ATOM   986   H  HA3  . GLY A 1 67  ? -4.101  19.925  12.760  1.00 23.98  ? 85  GLY A HA3  1 
ATOM   987   N  N    . TYR A 1 68  ? -5.385  17.206  13.403  1.00 18.17  ? 86  TYR A N    1 
ATOM   988   C  CA   . TYR A 1 68  ? -5.862  15.942  12.865  1.00 18.05  ? 86  TYR A CA   1 
ATOM   989   C  C    . TYR A 1 68  ? -7.357  15.788  13.113  1.00 18.06  ? 86  TYR A C    1 
ATOM   990   O  O    . TYR A 1 68  ? -7.945  16.455  13.968  1.00 19.48  ? 86  TYR A O    1 
ATOM   991   C  CB   . TYR A 1 68  ? -5.133  14.759  13.520  1.00 17.57  ? 86  TYR A CB   1 
ATOM   992   C  CG   . TYR A 1 68  ? -3.642  14.787  13.317  1.00 18.51  ? 86  TYR A CG   1 
ATOM   993   C  CD1  . TYR A 1 68  ? -3.057  14.120  12.252  1.00 18.93  ? 86  TYR A CD1  1 
ATOM   994   C  CD2  . TYR A 1 68  ? -2.813  15.505  14.177  1.00 18.96  ? 86  TYR A CD2  1 
ATOM   995   C  CE1  . TYR A 1 68  ? -1.696  14.164  12.046  1.00 20.93  ? 86  TYR A CE1  1 
ATOM   996   C  CE2  . TYR A 1 68  ? -1.450  15.550  13.982  1.00 20.13  ? 86  TYR A CE2  1 
ATOM   997   C  CZ   . TYR A 1 68  ? -0.896  14.877  12.915  1.00 20.62  ? 86  TYR A CZ   1 
ATOM   998   O  OH   . TYR A 1 68  ? 0.464   14.922  12.716  1.00 22.79  ? 86  TYR A OH   1 
ATOM   999   H  H    . TYR A 1 68  ? -5.153  17.166  14.231  1.00 21.81  ? 86  TYR A H    1 
ATOM   1000  H  HA   . TYR A 1 68  ? -5.692  15.928  11.910  1.00 21.66  ? 86  TYR A HA   1 
ATOM   1001  H  HB2  . TYR A 1 68  ? -5.303  14.776  14.475  1.00 21.08  ? 86  TYR A HB2  1 
ATOM   1002  H  HB3  . TYR A 1 68  ? -5.470  13.933  13.138  1.00 21.08  ? 86  TYR A HB3  1 
ATOM   1003  H  HD1  . TYR A 1 68  ? -3.592  13.634  11.667  1.00 22.71  ? 86  TYR A HD1  1 
ATOM   1004  H  HD2  . TYR A 1 68  ? -3.187  15.962  14.896  1.00 22.75  ? 86  TYR A HD2  1 
ATOM   1005  H  HE1  . TYR A 1 68  ? -1.318  13.716  11.324  1.00 25.12  ? 86  TYR A HE1  1 
ATOM   1006  H  HE2  . TYR A 1 68  ? -0.909  16.031  14.565  1.00 24.16  ? 86  TYR A HE2  1 
ATOM   1007  H  HH   . TYR A 1 68  ? 0.665   14.518  12.007  1.00 27.35  ? 86  TYR A HH   1 
ATOM   1008  N  N    . THR A 1 69  ? -7.973  14.890  12.342  1.00 17.66  ? 87  THR A N    1 
ATOM   1009  C  CA   . THR A 1 69  ? -9.293  14.387  12.679  1.00 17.87  ? 87  THR A CA   1 
ATOM   1010  C  C    . THR A 1 69  ? -9.091  13.060  13.393  1.00 16.18  ? 87  THR A C    1 
ATOM   1011  O  O    . THR A 1 69  ? -8.668  12.085  12.752  1.00 17.06  ? 87  THR A O    1 
ATOM   1012  C  CB   . THR A 1 69  ? -10.145 14.187  11.429  1.00 18.55  ? 87  THR A CB   1 
ATOM   1013  O  OG1  . THR A 1 69  ? -10.306 15.431  10.735  1.00 20.32  ? 87  THR A OG1  1 
ATOM   1014  C  CG2  . THR A 1 69  ? -11.512 13.656  11.827  1.00 19.01  ? 87  THR A CG2  1 
ATOM   1015  H  H    . THR A 1 69  ? -7.643  14.561  11.619  1.00 21.19  ? 87  THR A H    1 
ATOM   1016  H  HA   . THR A 1 69  ? -9.757  15.017  13.253  1.00 21.44  ? 87  THR A HA   1 
ATOM   1017  H  HB   . THR A 1 69  ? -9.714  13.552  10.836  1.00 22.26  ? 87  THR A HB   1 
ATOM   1018  H  HG1  . THR A 1 69  ? -10.684 15.991  11.233  1.00 24.38  ? 87  THR A HG1  1 
ATOM   1019  H  HG21 . THR A 1 69  ? -11.890 14.208  12.530  1.00 22.81  ? 87  THR A HG21 1 
ATOM   1020  H  HG22 . THR A 1 69  ? -12.108 13.667  11.062  1.00 22.81  ? 87  THR A HG22 1 
ATOM   1021  H  HG23 . THR A 1 69  ? -11.432 12.745  12.151  1.00 22.81  ? 87  THR A HG23 1 
ATOM   1022  N  N    . PRO A 1 70  ? -9.357  12.965  14.696  1.00 16.26  ? 88  PRO A N    1 
ATOM   1023  C  CA   . PRO A 1 70  ? -9.172  11.679  15.387  1.00 15.67  ? 88  PRO A CA   1 
ATOM   1024  C  C    . PRO A 1 70  ? -10.249 10.685  14.983  1.00 15.02  ? 88  PRO A C    1 
ATOM   1025  O  O    . PRO A 1 70  ? -11.435 11.015  14.929  1.00 16.40  ? 88  PRO A O    1 
ATOM   1026  C  CB   . PRO A 1 70  ? -9.276  12.050  16.869  1.00 17.38  ? 88  PRO A CB   1 
ATOM   1027  C  CG   . PRO A 1 70  ? -10.128 13.280  16.877  1.00 17.58  ? 88  PRO A CG   1 
ATOM   1028  C  CD   . PRO A 1 70  ? -9.794  14.031  15.618  1.00 18.34  ? 88  PRO A CD   1 
ATOM   1029  H  HA   . PRO A 1 70  ? -8.295  11.310  15.200  1.00 18.80  ? 88  PRO A HA   1 
ATOM   1030  H  HB2  . PRO A 1 70  ? -9.696  11.329  17.364  1.00 20.86  ? 88  PRO A HB2  1 
ATOM   1031  H  HB3  . PRO A 1 70  ? -8.394  12.232  17.230  1.00 20.86  ? 88  PRO A HB3  1 
ATOM   1032  H  HG2  . PRO A 1 70  ? -11.064 13.027  16.887  1.00 21.10  ? 88  PRO A HG2  1 
ATOM   1033  H  HG3  . PRO A 1 70  ? -9.920  13.814  17.659  1.00 21.10  ? 88  PRO A HG3  1 
ATOM   1034  H  HD2  . PRO A 1 70  ? -10.576 14.488  15.271  1.00 22.01  ? 88  PRO A HD2  1 
ATOM   1035  H  HD3  . PRO A 1 70  ? -9.079  14.667  15.774  1.00 22.01  ? 88  PRO A HD3  1 
ATOM   1036  N  N    . CYS A 1 71  ? -9.811  9.464   14.696  1.00 14.77  ? 89  CYS A N    1 
ATOM   1037  C  CA   . CYS A 1 71  ? -10.680 8.332   14.436  1.00 15.29  ? 89  CYS A CA   1 
ATOM   1038  C  C    . CYS A 1 71  ? -10.209 7.201   15.335  1.00 15.19  ? 89  CYS A C    1 
ATOM   1039  O  O    . CYS A 1 71  ? -9.032  7.134   15.697  1.00 16.11  ? 89  CYS A O    1 
ATOM   1040  C  CB   . CYS A 1 71  ? -10.600 7.895   12.975  1.00 15.92  ? 89  CYS A CB   1 
ATOM   1041  S  SG   . CYS A 1 71  ? -10.933 9.226   11.783  1.00 17.18  ? 89  CYS A SG   1 
ATOM   1042  H  H    . CYS A 1 71  ? -8.977  9.260   14.646  1.00 17.73  ? 89  CYS A H    1 
ATOM   1043  H  HA   . CYS A 1 71  ? -11.607 8.547   14.626  1.00 18.34  ? 89  CYS A HA   1 
ATOM   1044  H  HB2  . CYS A 1 71  ? -9.706  7.559   12.801  1.00 19.10  ? 89  CYS A HB2  1 
ATOM   1045  H  HB3  . CYS A 1 71  ? -11.253 7.194   12.825  1.00 19.10  ? 89  CYS A HB3  1 
ATOM   1046  N  N    . TRP A 1 72  ? -11.126 6.311   15.699  1.00 14.86  ? 90  TRP A N    1 
ATOM   1047  C  CA   . TRP A 1 72  ? -10.766 5.231   16.602  1.00 14.69  ? 90  TRP A CA   1 
ATOM   1048  C  C    . TRP A 1 72  ? -11.563 3.987   16.254  1.00 14.63  ? 90  TRP A C    1 
ATOM   1049  O  O    . TRP A 1 72  ? -12.645 4.056   15.661  1.00 15.72  ? 90  TRP A O    1 
ATOM   1050  C  CB   . TRP A 1 72  ? -11.042 5.608   18.064  1.00 14.77  ? 90  TRP A CB   1 
ATOM   1051  C  CG   . TRP A 1 72  ? -12.428 6.119   18.243  1.00 15.35  ? 90  TRP A CG   1 
ATOM   1052  C  CD1  . TRP A 1 72  ? -13.546 5.384   18.503  1.00 16.42  ? 90  TRP A CD1  1 
ATOM   1053  C  CD2  . TRP A 1 72  ? -12.852 7.481   18.144  1.00 16.39  ? 90  TRP A CD2  1 
ATOM   1054  N  NE1  . TRP A 1 72  ? -14.642 6.209   18.581  1.00 16.52  ? 90  TRP A NE1  1 
ATOM   1055  C  CE2  . TRP A 1 72  ? -14.242 7.502   18.369  1.00 16.48  ? 90  TRP A CE2  1 
ATOM   1056  C  CE3  . TRP A 1 72  ? -12.185 8.688   17.908  1.00 16.56  ? 90  TRP A CE3  1 
ATOM   1057  C  CZ2  . TRP A 1 72  ? -14.986 8.685   18.350  1.00 17.57  ? 90  TRP A CZ2  1 
ATOM   1058  C  CZ3  . TRP A 1 72  ? -12.925 9.865   17.884  1.00 17.66  ? 90  TRP A CZ3  1 
ATOM   1059  C  CH2  . TRP A 1 72  ? -14.312 9.853   18.104  1.00 18.32  ? 90  TRP A CH2  1 
ATOM   1060  H  H    . TRP A 1 72  ? -11.946 6.314   15.441  1.00 17.84  ? 90  TRP A H    1 
ATOM   1061  H  HA   . TRP A 1 72  ? -9.822  5.039   16.488  1.00 17.63  ? 90  TRP A HA   1 
ATOM   1062  H  HB2  . TRP A 1 72  ? -10.931 4.824   18.623  1.00 17.72  ? 90  TRP A HB2  1 
ATOM   1063  H  HB3  . TRP A 1 72  ? -10.423 6.302   18.338  1.00 17.72  ? 90  TRP A HB3  1 
ATOM   1064  H  HD1  . TRP A 1 72  ? -13.564 4.460   18.611  1.00 19.71  ? 90  TRP A HD1  1 
ATOM   1065  H  HE1  . TRP A 1 72  ? -15.448 5.954   18.738  1.00 19.83  ? 90  TRP A HE1  1 
ATOM   1066  H  HE3  . TRP A 1 72  ? -11.266 8.703   17.769  1.00 19.87  ? 90  TRP A HE3  1 
ATOM   1067  H  HZ2  . TRP A 1 72  ? -15.904 8.679   18.498  1.00 21.08  ? 90  TRP A HZ2  1 
ATOM   1068  H  HZ3  . TRP A 1 72  ? -12.494 10.673  17.719  1.00 21.19  ? 90  TRP A HZ3  1 
ATOM   1069  H  HH2  . TRP A 1 72  ? -14.783 10.654  18.083  1.00 21.99  ? 90  TRP A HH2  1 
ATOM   1070  N  N    . ILE A 1 73  ? -11.008 2.844   16.636  1.00 14.90  ? 91  ILE A N    1 
ATOM   1071  C  CA   . ILE A 1 73  ? -11.728 1.583   16.587  1.00 15.25  ? 91  ILE A CA   1 
ATOM   1072  C  C    . ILE A 1 73  ? -12.086 1.169   18.011  1.00 15.68  ? 91  ILE A C    1 
ATOM   1073  O  O    . ILE A 1 73  ? -11.375 1.477   18.980  1.00 15.47  ? 91  ILE A O    1 
ATOM   1074  C  CB   . ILE A 1 73  ? -10.976 0.446   15.859  1.00 14.92  ? 91  ILE A CB   1 
ATOM   1075  C  CG1  . ILE A 1 73  ? -9.551  0.283   16.393  1.00 15.05  ? 91  ILE A CG1  1 
ATOM   1076  C  CG2  . ILE A 1 73  ? -10.971 0.695   14.357  1.00 15.42  ? 91  ILE A CG2  1 
ATOM   1077  C  CD1  . ILE A 1 73  ? -8.869  -1.007  15.932  1.00 15.16  ? 91  ILE A CD1  1 
ATOM   1078  H  H    . ILE A 1 73  ? -10.204 2.775   16.932  1.00 17.88  ? 91  ILE A H    1 
ATOM   1079  H  HA   . ILE A 1 73  ? -12.543 1.736   16.083  1.00 18.30  ? 91  ILE A HA   1 
ATOM   1080  H  HB   . ILE A 1 73  ? -11.448 -0.383  16.036  1.00 17.90  ? 91  ILE A HB   1 
ATOM   1081  H  HG12 . ILE A 1 73  ? -9.014  1.029   16.085  1.00 18.06  ? 91  ILE A HG12 1 
ATOM   1082  H  HG13 . ILE A 1 73  ? -9.580  0.273   17.363  1.00 18.06  ? 91  ILE A HG13 1 
ATOM   1083  H  HG21 . ILE A 1 73  ? -10.572 1.562   14.182  1.00 18.50  ? 91  ILE A HG21 1 
ATOM   1084  H  HG22 . ILE A 1 73  ? -10.453 -0.001  13.923  1.00 18.50  ? 91  ILE A HG22 1 
ATOM   1085  H  HG23 . ILE A 1 73  ? -11.884 0.679   14.031  1.00 18.50  ? 91  ILE A HG23 1 
ATOM   1086  H  HD11 . ILE A 1 73  ? -9.532  -1.714  15.880  1.00 18.19  ? 91  ILE A HD11 1 
ATOM   1087  H  HD12 . ILE A 1 73  ? -8.474  -0.860  15.058  1.00 18.19  ? 91  ILE A HD12 1 
ATOM   1088  H  HD13 . ILE A 1 73  ? -8.180  -1.246  16.571  1.00 18.19  ? 91  ILE A HD13 1 
ATOM   1089  N  N    . SER A 1 74  ? -13.206 0.459   18.128  1.00 15.27  ? 92  SER A N    1 
ATOM   1090  C  CA   . SER A 1 74  ? -13.678 -0.088  19.396  1.00 14.71  ? 92  SER A CA   1 
ATOM   1091  C  C    . SER A 1 74  ? -14.050 -1.549  19.194  1.00 15.66  ? 92  SER A C    1 
ATOM   1092  O  O    . SER A 1 74  ? -15.233 -1.911  19.201  1.00 16.89  ? 92  SER A O    1 
ATOM   1093  C  CB   . SER A 1 74  ? -14.877 0.698   19.923  1.00 15.24  ? 92  SER A CB   1 
ATOM   1094  O  OG   . SER A 1 74  ? -14.523 2.029   20.237  1.00 16.76  ? 92  SER A OG   1 
ATOM   1095  H  H    . SER A 1 74  ? -13.723 0.276   17.466  1.00 18.32  ? 92  SER A H    1 
ATOM   1096  H  HA   . SER A 1 74  ? -12.962 -0.034  20.048  1.00 17.66  ? 92  SER A HA   1 
ATOM   1097  H  HB2  . SER A 1 74  ? -15.568 0.709   19.243  1.00 18.28  ? 92  SER A HB2  1 
ATOM   1098  H  HB3  . SER A 1 74  ? -15.209 0.264   20.725  1.00 18.28  ? 92  SER A HB3  1 
ATOM   1099  H  HG   . SER A 1 74  ? -14.206 2.410   19.558  1.00 20.11  ? 92  SER A HG   1 
ATOM   1100  N  N    . PRO A 1 75  ? -13.064 -2.420  19.009  1.00 14.96  ? 93  PRO A N    1 
ATOM   1101  C  CA   . PRO A 1 75  ? -13.372 -3.840  18.828  1.00 16.41  ? 93  PRO A CA   1 
ATOM   1102  C  C    . PRO A 1 75  ? -14.100 -4.377  20.044  1.00 17.82  ? 93  PRO A C    1 
ATOM   1103  O  O    . PRO A 1 75  ? -13.640 -4.187  21.181  1.00 17.56  ? 93  PRO A O    1 
ATOM   1104  C  CB   . PRO A 1 75  ? -11.985 -4.488  18.680  1.00 16.19  ? 93  PRO A CB   1 
ATOM   1105  C  CG   . PRO A 1 75  ? -11.085 -3.363  18.212  1.00 15.28  ? 93  PRO A CG   1 
ATOM   1106  C  CD   . PRO A 1 75  ? -11.615 -2.150  18.928  1.00 14.91  ? 93  PRO A CD   1 
ATOM   1107  H  HA   . PRO A 1 75  ? -13.893 -3.992  18.024  1.00 19.69  ? 93  PRO A HA   1 
ATOM   1108  H  HB2  . PRO A 1 75  ? -11.690 -4.838  19.536  1.00 19.43  ? 93  PRO A HB2  1 
ATOM   1109  H  HB3  . PRO A 1 75  ? -12.020 -5.202  18.025  1.00 19.43  ? 93  PRO A HB3  1 
ATOM   1110  H  HG2  . PRO A 1 75  ? -10.166 -3.544  18.463  1.00 18.34  ? 93  PRO A HG2  1 
ATOM   1111  H  HG3  . PRO A 1 75  ? -11.153 -3.260  17.250  1.00 18.34  ? 93  PRO A HG3  1 
ATOM   1112  H  HD2  . PRO A 1 75  ? -11.227 -2.073  19.813  1.00 17.89  ? 93  PRO A HD2  1 
ATOM   1113  H  HD3  . PRO A 1 75  ? -11.441 -1.344  18.417  1.00 17.89  ? 93  PRO A HD3  1 
ATOM   1114  N  N    . PRO A 1 76  ? -15.230 -5.054  19.851  1.00 17.96  ? 94  PRO A N    1 
ATOM   1115  C  CA   . PRO A 1 76  ? -16.006 -5.547  20.993  1.00 17.38  ? 94  PRO A CA   1 
ATOM   1116  C  C    . PRO A 1 76  ? -15.516 -6.910  21.443  1.00 17.19  ? 94  PRO A C    1 
ATOM   1117  O  O    . PRO A 1 76  ? -14.905 -7.650  20.660  1.00 17.20  ? 94  PRO A O    1 
ATOM   1118  C  CB   . PRO A 1 76  ? -17.424 -5.645  20.418  1.00 18.90  ? 94  PRO A CB   1 
ATOM   1119  C  CG   . PRO A 1 76  ? -17.189 -6.009  18.982  1.00 18.66  ? 94  PRO A CG   1 
ATOM   1120  C  CD   . PRO A 1 76  ? -15.942 -5.261  18.574  1.00 19.02  ? 94  PRO A CD   1 
ATOM   1121  H  HA   . PRO A 1 76  ? -15.975 -4.922  21.734  1.00 20.85  ? 94  PRO A HA   1 
ATOM   1122  H  HB2  . PRO A 1 76  ? -17.928 -6.334  20.879  1.00 22.68  ? 94  PRO A HB2  1 
ATOM   1123  H  HB3  . PRO A 1 76  ? -17.880 -4.792  20.497  1.00 22.68  ? 94  PRO A HB3  1 
ATOM   1124  H  HG2  . PRO A 1 76  ? -17.058 -6.967  18.903  1.00 22.39  ? 94  PRO A HG2  1 
ATOM   1125  H  HG3  . PRO A 1 76  ? -17.948 -5.733  18.444  1.00 22.39  ? 94  PRO A HG3  1 
ATOM   1126  H  HD2  . PRO A 1 76  ? -15.407 -5.792  17.964  1.00 22.82  ? 94  PRO A HD2  1 
ATOM   1127  H  HD3  . PRO A 1 76  ? -16.169 -4.412  18.164  1.00 22.82  ? 94  PRO A HD3  1 
ATOM   1128  N  N    . PRO A 1 77  ? -15.729 -7.272  22.712  1.00 17.83  ? 95  PRO A N    1 
ATOM   1129  C  CA   . PRO A 1 77  ? -16.195 -6.416  23.801  1.00 17.69  ? 95  PRO A CA   1 
ATOM   1130  C  C    . PRO A 1 77  ? -14.981 -5.805  24.496  1.00 17.74  ? 95  PRO A C    1 
ATOM   1131  O  O    . PRO A 1 77  ? -14.195 -6.527  25.108  1.00 16.93  ? 95  PRO A O    1 
ATOM   1132  C  CB   . PRO A 1 77  ? -16.917 -7.395  24.719  1.00 18.33  ? 95  PRO A CB   1 
ATOM   1133  C  CG   . PRO A 1 77  ? -16.191 -8.702  24.517  1.00 18.18  ? 95  PRO A CG   1 
ATOM   1134  C  CD   . PRO A 1 77  ? -15.488 -8.650  23.175  1.00 17.84  ? 95  PRO A CD   1 
ATOM   1135  H  HA   . PRO A 1 77  ? -16.826 -5.735  23.522  1.00 21.23  ? 95  PRO A HA   1 
ATOM   1136  H  HB2  . PRO A 1 77  ? -16.851 -7.098  25.640  1.00 21.99  ? 95  PRO A HB2  1 
ATOM   1137  H  HB3  . PRO A 1 77  ? -17.848 -7.468  24.459  1.00 21.99  ? 95  PRO A HB3  1 
ATOM   1138  H  HG2  . PRO A 1 77  ? -15.545 -8.820  25.230  1.00 21.82  ? 95  PRO A HG2  1 
ATOM   1139  H  HG3  . PRO A 1 77  ? -16.835 -9.428  24.529  1.00 21.82  ? 95  PRO A HG3  1 
ATOM   1140  H  HD2  . PRO A 1 77  ? -14.538 -8.817  23.278  1.00 21.41  ? 95  PRO A HD2  1 
ATOM   1141  H  HD3  . PRO A 1 77  ? -15.873 -9.293  22.559  1.00 21.41  ? 95  PRO A HD3  1 
ATOM   1142  N  N    . PHE A 1 78  ? -14.803 -4.493  24.361  1.00 17.46  ? 96  PHE A N    1 
ATOM   1143  C  CA   . PHE A 1 78  ? -13.787 -3.772  25.125  1.00 16.59  ? 96  PHE A CA   1 
ATOM   1144  C  C    . PHE A 1 78  ? -12.385 -4.349  24.947  1.00 16.32  ? 96  PHE A C    1 
ATOM   1145  O  O    . PHE A 1 78  ? -11.605 -4.423  25.899  1.00 16.43  ? 96  PHE A O    1 
ATOM   1146  C  CB   . PHE A 1 78  ? -14.162 -3.722  26.605  1.00 17.42  ? 96  PHE A CB   1 
ATOM   1147  C  CG   . PHE A 1 78  ? -15.559 -3.254  26.856  1.00 18.40  ? 96  PHE A CG   1 
ATOM   1148  C  CD1  . PHE A 1 78  ? -15.872 -1.910  26.779  1.00 20.44  ? 96  PHE A CD1  1 
ATOM   1149  C  CD2  . PHE A 1 78  ? -16.564 -4.153  27.160  1.00 18.77  ? 96  PHE A CD2  1 
ATOM   1150  C  CE1  . PHE A 1 78  ? -17.166 -1.469  27.007  1.00 22.32  ? 96  PHE A CE1  1 
ATOM   1151  C  CE2  . PHE A 1 78  ? -17.855 -3.718  27.392  1.00 20.92  ? 96  PHE A CE2  1 
ATOM   1152  C  CZ   . PHE A 1 78  ? -18.158 -2.378  27.311  1.00 22.25  ? 96  PHE A CZ   1 
ATOM   1153  H  H    . PHE A 1 78  ? -15.260 -3.994  23.830  1.00 20.96  ? 96  PHE A H    1 
ATOM   1154  H  HA   . PHE A 1 78  ? -13.751 -2.868  24.776  1.00 19.90  ? 96  PHE A HA   1 
ATOM   1155  H  HB2  . PHE A 1 78  ? -14.076 -4.613  26.979  1.00 20.90  ? 96  PHE A HB2  1 
ATOM   1156  H  HB3  . PHE A 1 78  ? -13.559 -3.112  27.059  1.00 20.90  ? 96  PHE A HB3  1 
ATOM   1157  H  HD1  . PHE A 1 78  ? -15.207 -1.295  26.573  1.00 24.52  ? 96  PHE A HD1  1 
ATOM   1158  H  HD2  . PHE A 1 78  ? -16.369 -5.061  27.210  1.00 22.53  ? 96  PHE A HD2  1 
ATOM   1159  H  HE1  . PHE A 1 78  ? -17.365 -0.563  26.954  1.00 26.79  ? 96  PHE A HE1  1 
ATOM   1160  H  HE2  . PHE A 1 78  ? -18.521 -4.333  27.604  1.00 25.10  ? 96  PHE A HE2  1 
ATOM   1161  H  HZ   . PHE A 1 78  ? -19.028 -2.086  27.461  1.00 26.70  ? 96  PHE A HZ   1 
ATOM   1162  N  N    . MET A 1 79  ? -12.040 -4.721  23.716  1.00 15.72  ? 97  MET A N    1 
ATOM   1163  C  CA   . MET A 1 79  ? -10.702 -5.217  23.389  1.00 15.61  ? 97  MET A CA   1 
ATOM   1164  C  C    . MET A 1 79  ? -10.357 -6.509  24.121  1.00 16.63  ? 97  MET A C    1 
ATOM   1165  O  O    . MET A 1 79  ? -9.176  -6.871  24.224  1.00 17.02  ? 97  MET A O    1 
ATOM   1166  C  CB   . MET A 1 79  ? -9.618  -4.159  23.651  1.00 15.93  ? 97  MET A CB   1 
ATOM   1167  C  CG   . MET A 1 79  ? -9.631  -2.999  22.657  1.00 16.34  ? 97  MET A CG   1 
ATOM   1168  S  SD   . MET A 1 79  ? -9.040  -3.438  21.012  1.00 15.67  ? 97  MET A SD   1 
ATOM   1169  C  CE   . MET A 1 79  ? -7.274  -3.562  21.268  1.00 16.06  ? 97  MET A CE   1 
ATOM   1170  H  H    . MET A 1 79  ? -12.573 -4.695  23.042  1.00 18.87  ? 97  MET A H    1 
ATOM   1171  H  HA   . MET A 1 79  ? -10.699 -5.406  22.437  1.00 18.73  ? 97  MET A HA   1 
ATOM   1172  H  HB2  . MET A 1 79  ? -9.752  -3.789  24.537  1.00 19.11  ? 97  MET A HB2  1 
ATOM   1173  H  HB3  . MET A 1 79  ? -8.748  -4.584  23.596  1.00 19.11  ? 97  MET A HB3  1 
ATOM   1174  H  HG2  . MET A 1 79  ? -10.541 -2.677  22.567  1.00 19.61  ? 97  MET A HG2  1 
ATOM   1175  H  HG3  . MET A 1 79  ? -9.061  -2.292  22.996  1.00 19.61  ? 97  MET A HG3  1 
ATOM   1176  H  HE1  . MET A 1 79  ? -7.071  -4.430  21.650  1.00 19.28  ? 97  MET A HE1  1 
ATOM   1177  H  HE2  . MET A 1 79  ? -6.824  -3.462  20.415  1.00 19.28  ? 97  MET A HE2  1 
ATOM   1178  H  HE3  . MET A 1 79  ? -6.993  -2.859  21.875  1.00 19.28  ? 97  MET A HE3  1 
ATOM   1179  N  N    . LEU A 1 80  ? -11.369 -7.224  24.620  1.00 15.11  ? 98  LEU A N    1 
ATOM   1180  C  CA   . LEU A 1 80  ? -11.138 -8.439  25.389  1.00 14.97  ? 98  LEU A CA   1 
ATOM   1181  C  C    . LEU A 1 80  ? -11.152 -9.696  24.540  1.00 15.94  ? 98  LEU A C    1 
ATOM   1182  O  O    . LEU A 1 80  ? -10.700 -10.750 25.007  1.00 16.27  ? 98  LEU A O    1 
ATOM   1183  C  CB   . LEU A 1 80  ? -12.195 -8.584  26.482  1.00 15.30  ? 98  LEU A CB   1 
ATOM   1184  C  CG   . LEU A 1 80  ? -12.224 -7.460  27.509  1.00 17.23  ? 98  LEU A CG   1 
ATOM   1185  C  CD1  . LEU A 1 80  ? -13.486 -7.555  28.368  1.00 18.82  ? 98  LEU A CD1  1 
ATOM   1186  C  CD2  . LEU A 1 80  ? -10.973 -7.476  28.377  1.00 18.29  ? 98  LEU A CD2  1 
ATOM   1187  H  H    . LEU A 1 80  ? -12.199 -7.022  24.524  1.00 18.14  ? 98  LEU A H    1 
ATOM   1188  H  HA   . LEU A 1 80  ? -10.268 -8.367  25.811  1.00 17.96  ? 98  LEU A HA   1 
ATOM   1189  H  HB2  . LEU A 1 80  ? -13.068 -8.615  26.061  1.00 18.36  ? 98  LEU A HB2  1 
ATOM   1190  H  HB3  . LEU A 1 80  ? -12.028 -9.411  26.961  1.00 18.36  ? 98  LEU A HB3  1 
ATOM   1191  H  HG   . LEU A 1 80  ? -12.240 -6.610  27.042  1.00 20.68  ? 98  LEU A HG   1 
ATOM   1192  H  HD11 . LEU A 1 80  ? -13.443 -6.885  29.068  1.00 22.59  ? 98  LEU A HD11 1 
ATOM   1193  H  HD12 . LEU A 1 80  ? -14.262 -7.400  27.808  1.00 22.59  ? 98  LEU A HD12 1 
ATOM   1194  H  HD13 . LEU A 1 80  ? -13.533 -8.441  28.761  1.00 22.59  ? 98  LEU A HD13 1 
ATOM   1195  H  HD21 . LEU A 1 80  ? -11.053 -6.791  29.059  1.00 21.95  ? 98  LEU A HD21 1 
ATOM   1196  H  HD22 . LEU A 1 80  ? -10.888 -8.348  28.793  1.00 21.95  ? 98  LEU A HD22 1 
ATOM   1197  H  HD23 . LEU A 1 80  ? -10.199 -7.298  27.820  1.00 21.95  ? 98  LEU A HD23 1 
ATOM   1198  N  N    A ASN A 1 81  ? -11.671 -9.608  23.315  0.61 15.76  ? 99  ASN A N    1 
ATOM   1199  N  N    B ASN A 1 81  ? -11.668 -9.635  23.329  0.39 16.81  ? 99  ASN A N    1 
ATOM   1200  C  CA   A ASN A 1 81  ? -11.691 -10.719 22.376  0.61 15.10  ? 99  ASN A CA   1 
ATOM   1201  C  CA   B ASN A 1 81  ? -11.648 -10.826 22.501  0.39 17.23  ? 99  ASN A CA   1 
ATOM   1202  C  C    A ASN A 1 81  ? -10.304 -10.924 21.765  0.61 14.44  ? 99  ASN A C    1 
ATOM   1203  C  C    B ASN A 1 81  ? -10.346 -10.900 21.707  0.39 16.32  ? 99  ASN A C    1 
ATOM   1204  O  O    A ASN A 1 81  ? -9.383  -10.116 21.942  0.61 14.43  ? 99  ASN A O    1 
ATOM   1205  O  O    B ASN A 1 81  ? -9.522  -9.980  21.712  0.39 16.66  ? 99  ASN A O    1 
ATOM   1206  C  CB   A ASN A 1 81  ? -12.712 -10.447 21.263  0.61 15.86  ? 99  ASN A CB   1 
ATOM   1207  C  CB   B ASN A 1 81  ? -12.892 -10.895 21.621  0.39 18.72  ? 99  ASN A CB   1 
ATOM   1208  C  CG   A ASN A 1 81  ? -13.081 -11.704 20.454  0.61 18.22  ? 99  ASN A CG   1 
ATOM   1209  C  CG   B ASN A 1 81  ? -14.029 -11.647 22.300  0.39 19.73  ? 99  ASN A CG   1 
ATOM   1210  O  OD1  A ASN A 1 81  ? -12.860 -12.833 20.885  0.61 19.70  ? 99  ASN A OD1  1 
ATOM   1211  O  OD1  B ASN A 1 81  ? -13.901 -12.074 23.448  0.39 20.76  ? 99  ASN A OD1  1 
ATOM   1212  N  ND2  A ASN A 1 81  ? -13.667 -11.493 19.277  0.61 18.80  ? 99  ASN A ND2  1 
ATOM   1213  N  ND2  B ASN A 1 81  ? -15.139 -11.810 21.599  0.39 19.14  ? 99  ASN A ND2  1 
ATOM   1214  H  H    A ASN A 1 81  ? -12.027 -8.893  22.997  0.61 18.91  ? 99  ASN A H    1 
ATOM   1215  H  H    B ASN A 1 81  ? -12.025 -8.938  22.973  0.39 20.17  ? 99  ASN A H    1 
ATOM   1216  H  HA   A ASN A 1 81  ? -11.945 -11.529 22.844  0.61 18.12  ? 99  ASN A HA   1 
ATOM   1217  H  HA   B ASN A 1 81  ? -11.674 -11.618 23.061  0.39 20.67  ? 99  ASN A HA   1 
ATOM   1218  H  HB2  A ASN A 1 81  ? -13.526 -10.101 21.661  0.61 19.04  ? 99  ASN A HB2  1 
ATOM   1219  H  HB2  B ASN A 1 81  ? -13.197 -9.995  21.427  0.39 22.46  ? 99  ASN A HB2  1 
ATOM   1220  H  HB3  A ASN A 1 81  ? -12.340 -9.796  20.647  0.61 19.04  ? 99  ASN A HB3  1 
ATOM   1221  H  HB3  B ASN A 1 81  ? -12.674 -11.356 20.796  0.39 22.46  ? 99  ASN A HB3  1 
ATOM   1222  H  HD21 A ASN A 1 81  ? -13.894 -12.160 18.784  0.61 22.56  ? 99  ASN A HD21 1 
ATOM   1223  H  HD21 B ASN A 1 81  ? -15.807 -12.228 21.943  0.39 22.97  ? 99  ASN A HD21 1 
ATOM   1224  H  HD22 A ASN A 1 81  ? -13.818 -10.690 19.009  0.61 22.56  ? 99  ASN A HD22 1 
ATOM   1225  H  HD22 B ASN A 1 81  ? -15.193 -11.497 20.799  0.39 22.97  ? 99  ASN A HD22 1 
ATOM   1226  N  N    . ASP A 1 82  ? -10.174 -12.034 21.034  1.00 16.07  ? 100 ASP A N    1 
ATOM   1227  C  CA   . ASP A 1 82  ? -8.989  -12.381 20.251  1.00 16.39  ? 100 ASP A CA   1 
ATOM   1228  C  C    . ASP A 1 82  ? -8.299  -11.173 19.633  1.00 16.27  ? 100 ASP A C    1 
ATOM   1229  O  O    . ASP A 1 82  ? -8.889  -10.452 18.822  1.00 16.06  ? 100 ASP A O    1 
ATOM   1230  C  CB   . ASP A 1 82  ? -9.499  -13.336 19.159  1.00 16.18  ? 100 ASP A CB   1 
ATOM   1231  C  CG   . ASP A 1 82  ? -8.407  -13.960 18.298  1.00 17.34  ? 100 ASP A CG   1 
ATOM   1232  O  OD1  . ASP A 1 82  ? -7.210  -13.637 18.446  1.00 16.27  ? 100 ASP A OD1  1 
ATOM   1233  O  OD2  . ASP A 1 82  ? -8.795  -14.787 17.430  1.00 20.41  ? 100 ASP A OD2  1 
ATOM   1234  H  H    . ASP A 1 82  ? -10.790 -12.632 20.973  1.00 19.29  ? 100 ASP A H    1 
ATOM   1235  H  HA   . ASP A 1 82  ? -8.307  -12.786 20.810  1.00 19.67  ? 100 ASP A HA   1 
ATOM   1236  H  HB2  . ASP A 1 82  ? -9.984  -14.060 19.584  1.00 19.41  ? 100 ASP A HB2  1 
ATOM   1237  H  HB3  . ASP A 1 82  ? -10.090 -12.842 18.568  1.00 19.41  ? 100 ASP A HB3  1 
ATOM   1238  N  N    . THR A 1 83  ? -7.044  -10.953 20.028  1.00 15.37  ? 101 THR A N    1 
ATOM   1239  C  CA   . THR A 1 83  ? -6.237  -9.871  19.465  1.00 15.34  ? 101 THR A CA   1 
ATOM   1240  C  C    . THR A 1 83  ? -6.173  -9.926  17.943  1.00 15.89  ? 101 THR A C    1 
ATOM   1241  O  O    . THR A 1 83  ? -6.048  -8.882  17.286  1.00 15.48  ? 101 THR A O    1 
ATOM   1242  C  CB   . THR A 1 83  ? -4.837  -9.948  20.085  1.00 17.69  ? 101 THR A CB   1 
ATOM   1243  O  OG1  . THR A 1 83  ? -4.930  -9.686  21.492  1.00 17.69  ? 101 THR A OG1  1 
ATOM   1244  C  CG2  . THR A 1 83  ? -3.888  -8.954  19.454  1.00 17.88  ? 101 THR A CG2  1 
ATOM   1245  H  H    . THR A 1 83  ? -6.633  -11.417 20.624  1.00 18.45  ? 101 THR A H    1 
ATOM   1246  H  HA   . THR A 1 83  ? -6.631  -9.013  19.687  1.00 18.41  ? 101 THR A HA   1 
ATOM   1247  H  HB   . THR A 1 83  ? -4.474  -10.834 19.931  1.00 21.23  ? 101 THR A HB   1 
ATOM   1248  H  HG1  . THR A 1 83  ? -4.166  -9.711  21.840  1.00 21.23  ? 101 THR A HG1  1 
ATOM   1249  H  HG21 . THR A 1 83  ? -3.665  -9.234  18.553  1.00 21.46  ? 101 THR A HG21 1 
ATOM   1250  H  HG22 . THR A 1 83  ? -4.302  -8.077  19.418  1.00 21.46  ? 101 THR A HG22 1 
ATOM   1251  H  HG23 . THR A 1 83  ? -3.073  -8.896  19.976  1.00 21.46  ? 101 THR A HG23 1 
ATOM   1252  N  N    . GLN A 1 84  ? -6.270  -11.122 17.362  1.00 15.47  ? 102 GLN A N    1 
ATOM   1253  C  CA   . GLN A 1 84  ? -6.248  -11.237 15.908  1.00 15.35  ? 102 GLN A CA   1 
ATOM   1254  C  C    . GLN A 1 84  ? -7.505  -10.636 15.285  1.00 15.28  ? 102 GLN A C    1 
ATOM   1255  O  O    . GLN A 1 84  ? -7.443  -10.038 14.204  1.00 16.32  ? 102 GLN A O    1 
ATOM   1256  C  CB   . GLN A 1 84  ? -6.089  -12.701 15.508  1.00 15.03  ? 102 GLN A CB   1 
ATOM   1257  C  CG   . GLN A 1 84  ? -4.812  -13.344 16.042  1.00 14.95  ? 102 GLN A CG   1 
ATOM   1258  C  CD   . GLN A 1 84  ? -4.824  -14.857 15.893  1.00 15.61  ? 102 GLN A CD   1 
ATOM   1259  O  OE1  . GLN A 1 84  ? -4.066  -15.423 15.102  1.00 16.96  ? 102 GLN A OE1  1 
ATOM   1260  N  NE2  . GLN A 1 84  ? -5.709  -15.519 16.637  1.00 17.02  ? 102 GLN A NE2  1 
ATOM   1261  H  H    . GLN A 1 84  ? -6.348  -11.869 17.781  1.00 18.56  ? 102 GLN A H    1 
ATOM   1262  H  HA   . GLN A 1 84  ? -5.485  -10.748 15.563  1.00 18.42  ? 102 GLN A HA   1 
ATOM   1263  H  HB2  . GLN A 1 84  ? -6.842  -13.204 15.856  1.00 18.04  ? 102 GLN A HB2  1 
ATOM   1264  H  HB3  . GLN A 1 84  ? -6.069  -12.760 14.540  1.00 18.04  ? 102 GLN A HB3  1 
ATOM   1265  H  HG2  . GLN A 1 84  ? -4.052  -12.998 15.549  1.00 17.94  ? 102 GLN A HG2  1 
ATOM   1266  H  HG3  . GLN A 1 84  ? -4.721  -13.134 16.984  1.00 17.94  ? 102 GLN A HG3  1 
ATOM   1267  H  HE21 . GLN A 1 84  ? -6.234  -15.088 17.165  1.00 20.43  ? 102 GLN A HE21 1 
ATOM   1268  H  HE22 . GLN A 1 84  ? -5.756  -16.376 16.589  1.00 20.43  ? 102 GLN A HE22 1 
ATOM   1269  N  N    . VAL A 1 85  ? -8.656  -10.798 15.945  1.00 15.61  ? 103 VAL A N    1 
ATOM   1270  C  CA   . VAL A 1 85  ? -9.876  -10.142 15.489  1.00 17.32  ? 103 VAL A CA   1 
ATOM   1271  C  C    . VAL A 1 85  ? -9.787  -8.640  15.724  1.00 16.88  ? 103 VAL A C    1 
ATOM   1272  O  O    . VAL A 1 85  ? -10.178 -7.836  14.868  1.00 16.55  ? 103 VAL A O    1 
ATOM   1273  C  CB   . VAL A 1 85  ? -11.103 -10.763 16.182  1.00 17.25  ? 103 VAL A CB   1 
ATOM   1274  C  CG1  . VAL A 1 85  ? -12.366 -9.986  15.842  1.00 18.45  ? 103 VAL A CG1  1 
ATOM   1275  C  CG2  . VAL A 1 85  ? -11.246 -12.239 15.803  1.00 17.97  ? 103 VAL A CG2  1 
ATOM   1276  H  H    . VAL A 1 85  ? -8.753  -11.279 16.651  1.00 18.73  ? 103 VAL A H    1 
ATOM   1277  H  HA   . VAL A 1 85  ? -9.973  -10.287 14.535  1.00 20.79  ? 103 VAL A HA   1 
ATOM   1278  H  HB   . VAL A 1 85  ? -10.978 -10.713 17.143  1.00 20.69  ? 103 VAL A HB   1 
ATOM   1279  H  HG11 . VAL A 1 85  ? -12.364 -9.149  16.333  1.00 22.14  ? 103 VAL A HG11 1 
ATOM   1280  H  HG12 . VAL A 1 85  ? -12.381 -9.809  14.888  1.00 22.14  ? 103 VAL A HG12 1 
ATOM   1281  H  HG13 . VAL A 1 85  ? -13.139 -10.515 16.092  1.00 22.14  ? 103 VAL A HG13 1 
ATOM   1282  H  HG21 . VAL A 1 85  ? -10.418 -12.543 15.398  1.00 21.57  ? 103 VAL A HG21 1 
ATOM   1283  H  HG22 . VAL A 1 85  ? -11.430 -12.754 16.604  1.00 21.57  ? 103 VAL A HG22 1 
ATOM   1284  H  HG23 . VAL A 1 85  ? -11.977 -12.334 15.173  1.00 21.57  ? 103 VAL A HG23 1 
ATOM   1285  N  N    . ASN A 1 86  ? -9.280  -8.230  16.889  1.00 15.92  ? 104 ASN A N    1 
ATOM   1286  C  CA   . ASN A 1 86  ? -9.097  -6.802  17.125  1.00 15.78  ? 104 ASN A CA   1 
ATOM   1287  C  C    . ASN A 1 86  ? -8.252  -6.189  16.015  1.00 15.46  ? 104 ASN A C    1 
ATOM   1288  O  O    . ASN A 1 86  ? -8.513  -5.064  15.572  1.00 15.58  ? 104 ASN A O    1 
ATOM   1289  C  CB   . ASN A 1 86  ? -8.464  -6.559  18.496  1.00 15.27  ? 104 ASN A CB   1 
ATOM   1290  C  CG   . ASN A 1 86  ? -9.286  -7.134  19.631  1.00 15.08  ? 104 ASN A CG   1 
ATOM   1291  O  OD1  . ASN A 1 86  ? -10.473 -7.403  19.473  1.00 16.99  ? 104 ASN A OD1  1 
ATOM   1292  N  ND2  . ASN A 1 86  ? -8.647  -7.359  20.774  1.00 14.84  ? 104 ASN A ND2  1 
ATOM   1293  H  H    . ASN A 1 86  ? -9.042  -8.743  17.537  1.00 19.11  ? 104 ASN A H    1 
ATOM   1294  H  HA   . ASN A 1 86  ? -9.963  -6.364  17.132  1.00 18.93  ? 104 ASN A HA   1 
ATOM   1295  H  HB2  . ASN A 1 86  ? -7.589  -6.977  18.518  1.00 18.32  ? 104 ASN A HB2  1 
ATOM   1296  H  HB3  . ASN A 1 86  ? -8.380  -5.604  18.641  1.00 18.32  ? 104 ASN A HB3  1 
ATOM   1297  H  HD21 . ASN A 1 86  ? -9.072  -7.685  21.447  1.00 17.81  ? 104 ASN A HD21 1 
ATOM   1298  H  HD22 . ASN A 1 86  ? -7.809  -7.179  20.840  1.00 17.81  ? 104 ASN A HD22 1 
ATOM   1299  N  N    . THR A 1 87  ? -7.266  -6.940  15.514  1.00 15.50  ? 105 THR A N    1 
ATOM   1300  C  CA   . THR A 1 87  ? -6.425  -6.431  14.433  1.00 15.31  ? 105 THR A CA   1 
ATOM   1301  C  C    . THR A 1 87  ? -7.201  -6.279  13.128  1.00 16.14  ? 105 THR A C    1 
ATOM   1302  O  O    . THR A 1 87  ? -6.918  -5.358  12.353  1.00 15.86  ? 105 THR A O    1 
ATOM   1303  C  CB   . THR A 1 87  ? -5.199  -7.335  14.253  1.00 16.48  ? 105 THR A CB   1 
ATOM   1304  O  OG1  . THR A 1 87  ? -4.428  -7.338  15.458  1.00 16.52  ? 105 THR A OG1  1 
ATOM   1305  C  CG2  . THR A 1 87  ? -4.321  -6.840  13.120  1.00 17.52  ? 105 THR A CG2  1 
ATOM   1306  H  H    . THR A 1 87  ? -7.068  -7.734  15.779  1.00 18.60  ? 105 THR A H    1 
ATOM   1307  H  HA   . THR A 1 87  ? -6.101  -5.549  14.674  1.00 18.37  ? 105 THR A HA   1 
ATOM   1308  H  HB   . THR A 1 87  ? -5.497  -8.233  14.043  1.00 19.77  ? 105 THR A HB   1 
ATOM   1309  H  HG1  . THR A 1 87  ? -3.784  -7.872  15.385  1.00 19.83  ? 105 THR A HG1  1 
ATOM   1310  H  HG21 . THR A 1 87  ? -3.518  -7.381  13.062  1.00 21.02  ? 105 THR A HG21 1 
ATOM   1311  H  HG22 . THR A 1 87  ? -4.801  -6.897  12.279  1.00 21.02  ? 105 THR A HG22 1 
ATOM   1312  H  HG23 . THR A 1 87  ? -4.067  -5.917  13.275  1.00 21.02  ? 105 THR A HG23 1 
ATOM   1313  N  N    . GLU A 1 88  ? -8.178  -7.152  12.861  1.00 15.84  ? 106 GLU A N    1 
ATOM   1314  C  CA   . GLU A 1 88  ? -8.982  -6.988  11.650  1.00 16.11  ? 106 GLU A CA   1 
ATOM   1315  C  C    . GLU A 1 88  ? -9.641  -5.617  11.629  1.00 17.03  ? 106 GLU A C    1 
ATOM   1316  O  O    . GLU A 1 88  ? -9.726  -4.973  10.578  1.00 17.51  ? 106 GLU A O    1 
ATOM   1317  C  CB   . GLU A 1 88  ? -10.061 -8.072  11.543  1.00 17.09  ? 106 GLU A CB   1 
ATOM   1318  C  CG   . GLU A 1 88  ? -9.533  -9.493  11.461  1.00 17.87  ? 106 GLU A CG   1 
ATOM   1319  C  CD   . GLU A 1 88  ? -10.644 -10.512 11.262  1.00 20.48  ? 106 GLU A CD   1 
ATOM   1320  O  OE1  . GLU A 1 88  ? -11.784 -10.107 10.937  1.00 21.10  ? 106 GLU A OE1  1 
ATOM   1321  O  OE2  . GLU A 1 88  ? -10.384 -11.720 11.432  1.00 22.19  ? 106 GLU A OE2  1 
ATOM   1322  H  H    . GLU A 1 88  ? -8.388  -7.827  13.351  1.00 19.01  ? 106 GLU A H    1 
ATOM   1323  H  HA   . GLU A 1 88  ? -8.392  -7.083  10.886  1.00 19.33  ? 106 GLU A HA   1 
ATOM   1324  H  HB2  . GLU A 1 88  ? -10.630 -8.018  12.327  1.00 20.50  ? 106 GLU A HB2  1 
ATOM   1325  H  HB3  . GLU A 1 88  ? -10.583 -7.908  10.743  1.00 20.50  ? 106 GLU A HB3  1 
ATOM   1326  H  HG2  . GLU A 1 88  ? -8.923  -9.562  10.710  1.00 21.45  ? 106 GLU A HG2  1 
ATOM   1327  H  HG3  . GLU A 1 88  ? -9.070  -9.708  12.285  1.00 21.45  ? 106 GLU A HG3  1 
ATOM   1328  N  N    . TYR A 1 89  ? -10.121 -5.158  12.787  1.00 15.62  ? 107 TYR A N    1 
ATOM   1329  C  CA   . TYR A 1 89  ? -10.724 -3.836  12.857  1.00 15.25  ? 107 TYR A CA   1 
ATOM   1330  C  C    . TYR A 1 89  ? -9.712  -2.765  12.481  1.00 14.46  ? 107 TYR A C    1 
ATOM   1331  O  O    . TYR A 1 89  ? -10.040 -1.800  11.778  1.00 16.59  ? 107 TYR A O    1 
ATOM   1332  C  CB   . TYR A 1 89  ? -11.244 -3.583  14.263  1.00 15.43  ? 107 TYR A CB   1 
ATOM   1333  C  CG   . TYR A 1 89  ? -12.566 -4.232  14.569  1.00 15.03  ? 107 TYR A CG   1 
ATOM   1334  C  CD1  . TYR A 1 89  ? -12.628 -5.500  15.138  1.00 15.79  ? 107 TYR A CD1  1 
ATOM   1335  C  CD2  . TYR A 1 89  ? -13.753 -3.580  14.295  1.00 16.79  ? 107 TYR A CD2  1 
ATOM   1336  C  CE1  . TYR A 1 89  ? -13.850 -6.092  15.421  1.00 15.56  ? 107 TYR A CE1  1 
ATOM   1337  C  CE2  . TYR A 1 89  ? -14.965 -4.156  14.578  1.00 16.75  ? 107 TYR A CE2  1 
ATOM   1338  C  CZ   . TYR A 1 89  ? -15.016 -5.410  15.129  1.00 16.91  ? 107 TYR A CZ   1 
ATOM   1339  O  OH   . TYR A 1 89  ? -16.245 -5.961  15.402  1.00 18.73  ? 107 TYR A OH   1 
ATOM   1340  H  H    . TYR A 1 89  ? -10.108 -5.588  13.532  1.00 18.75  ? 107 TYR A H    1 
ATOM   1341  H  HA   . TYR A 1 89  ? -11.470 -3.792  12.238  1.00 18.30  ? 107 TYR A HA   1 
ATOM   1342  H  HB2  . TYR A 1 89  ? -10.596 -3.926  14.898  1.00 18.52  ? 107 TYR A HB2  1 
ATOM   1343  H  HB3  . TYR A 1 89  ? -11.353 -2.627  14.385  1.00 18.52  ? 107 TYR A HB3  1 
ATOM   1344  H  HD1  . TYR A 1 89  ? -11.841 -5.956  15.331  1.00 18.95  ? 107 TYR A HD1  1 
ATOM   1345  H  HD2  . TYR A 1 89  ? -13.730 -2.733  13.911  1.00 20.15  ? 107 TYR A HD2  1 
ATOM   1346  H  HE1  . TYR A 1 89  ? -13.884 -6.939  15.803  1.00 18.67  ? 107 TYR A HE1  1 
ATOM   1347  H  HE2  . TYR A 1 89  ? -15.753 -3.696  14.397  1.00 20.09  ? 107 TYR A HE2  1 
ATOM   1348  H  HH   . TYR A 1 89  ? -16.149 -6.717  15.755  1.00 22.48  ? 107 TYR A HH   1 
ATOM   1349  N  N    . MET A 1 90  ? -8.470  -2.917  12.937  1.00 12.58  ? 108 MET A N    1 
ATOM   1350  C  CA   . MET A 1 90  ? -7.457  -1.914  12.631  1.00 13.08  ? 108 MET A CA   1 
ATOM   1351  C  C    . MET A 1 90  ? -7.081  -1.934  11.155  1.00 16.20  ? 108 MET A C    1 
ATOM   1352  O  O    . MET A 1 90  ? -6.968  -0.876  10.520  1.00 16.58  ? 108 MET A O    1 
ATOM   1353  C  CB   . MET A 1 90  ? -6.220  -2.112  13.505  1.00 14.11  ? 108 MET A CB   1 
ATOM   1354  C  CG   . MET A 1 90  ? -5.322  -0.879  13.494  1.00 17.72  ? 108 MET A CG   1 
ATOM   1355  S  SD   . MET A 1 90  ? -3.601  -1.257  13.743  1.00 19.53  ? 108 MET A SD   1 
ATOM   1356  C  CE   . MET A 1 90  ? -3.403  -2.233  12.263  1.00 14.53  ? 108 MET A CE   1 
ATOM   1357  H  H    . MET A 1 90  ? -8.195  -3.578  13.414  1.00 15.09  ? 108 MET A H    1 
ATOM   1358  H  HA   . MET A 1 90  ? -7.828  -1.044  12.846  1.00 15.69  ? 108 MET A HA   1 
ATOM   1359  H  HB2  . MET A 1 90  ? -6.497  -2.279  14.419  1.00 16.93  ? 108 MET A HB2  1 
ATOM   1360  H  HB3  . MET A 1 90  ? -5.708  -2.865  13.170  1.00 16.93  ? 108 MET A HB3  1 
ATOM   1361  H  HG2  . MET A 1 90  ? -5.408  -0.436  12.635  1.00 21.27  ? 108 MET A HG2  1 
ATOM   1362  H  HG3  . MET A 1 90  ? -5.601  -0.281  14.205  1.00 21.27  ? 108 MET A HG3  1 
ATOM   1363  H  HE1  . MET A 1 90  ? -4.138  -2.043  11.659  1.00 17.43  ? 108 MET A HE1  1 
ATOM   1364  H  HE2  . MET A 1 90  ? -2.561  -2.000  11.842  1.00 17.43  ? 108 MET A HE2  1 
ATOM   1365  H  HE3  . MET A 1 90  ? -3.406  -3.173  12.502  1.00 17.43  ? 108 MET A HE3  1 
ATOM   1366  N  N    . VAL A 1 91  ? -6.855  -3.128  10.595  1.00 15.97  ? 109 VAL A N    1 
ATOM   1367  C  CA   . VAL A 1 91  ? -6.487  -3.240  9.186   1.00 16.85  ? 109 VAL A CA   1 
ATOM   1368  C  C    . VAL A 1 91  ? -7.577  -2.643  8.307   1.00 16.75  ? 109 VAL A C    1 
ATOM   1369  O  O    . VAL A 1 91  ? -7.304  -1.830  7.416   1.00 17.62  ? 109 VAL A O    1 
ATOM   1370  C  CB   . VAL A 1 91  ? -6.194  -4.710  8.831   1.00 16.76  ? 109 VAL A CB   1 
ATOM   1371  C  CG1  . VAL A 1 91  ? -5.962  -4.872  7.340   1.00 18.56  ? 109 VAL A CG1  1 
ATOM   1372  C  CG2  . VAL A 1 91  ? -4.983  -5.210  9.638   1.00 17.25  ? 109 VAL A CG2  1 
ATOM   1373  H  H    . VAL A 1 91  ? -6.908  -3.880  11.009  1.00 19.16  ? 109 VAL A H    1 
ATOM   1374  H  HA   . VAL A 1 91  ? -5.676  -2.731  9.030   1.00 20.21  ? 109 VAL A HA   1 
ATOM   1375  H  HB   . VAL A 1 91  ? -6.963  -5.253  9.063   1.00 20.11  ? 109 VAL A HB   1 
ATOM   1376  H  HG11 . VAL A 1 91  ? -6.784  -4.666  6.868   1.00 22.27  ? 109 VAL A HG11 1 
ATOM   1377  H  HG12 . VAL A 1 91  ? -5.259  -4.264  7.062   1.00 22.27  ? 109 VAL A HG12 1 
ATOM   1378  H  HG13 . VAL A 1 91  ? -5.697  -5.788  7.159   1.00 22.27  ? 109 VAL A HG13 1 
ATOM   1379  H  HG21 . VAL A 1 91  ? -4.239  -4.604  9.499   1.00 20.70  ? 109 VAL A HG21 1 
ATOM   1380  H  HG22 . VAL A 1 91  ? -5.218  -5.235  10.579  1.00 20.70  ? 109 VAL A HG22 1 
ATOM   1381  H  HG23 . VAL A 1 91  ? -4.746  -6.100  9.333   1.00 20.70  ? 109 VAL A HG23 1 
ATOM   1382  N  N    . ASN A 1 92  ? -8.830  -3.038  8.541   1.00 16.75  ? 110 ASN A N    1 
ATOM   1383  C  CA   . ASN A 1 92  ? -9.932  -2.469  7.774   1.00 17.30  ? 110 ASN A CA   1 
ATOM   1384  C  C    . ASN A 1 92  ? -9.980  -0.955  7.919   1.00 18.10  ? 110 ASN A C    1 
ATOM   1385  O  O    . ASN A 1 92  ? -10.228 -0.241  6.942   1.00 19.55  ? 110 ASN A O    1 
ATOM   1386  C  CB   . ASN A 1 92  ? -11.256 -3.080  8.230   1.00 19.74  ? 110 ASN A CB   1 
ATOM   1387  C  CG   . ASN A 1 92  ? -12.442 -2.511  7.482   1.00 21.65  ? 110 ASN A CG   1 
ATOM   1388  O  OD1  . ASN A 1 92  ? -12.682 -2.861  6.327   1.00 22.92  ? 110 ASN A OD1  1 
ATOM   1389  N  ND2  . ASN A 1 92  ? -13.193 -1.627  8.137   1.00 20.96  ? 110 ASN A ND2  1 
ATOM   1390  H  H    . ASN A 1 92  ? -9.063  -3.623  9.127   1.00 20.10  ? 110 ASN A H    1 
ATOM   1391  H  HA   . ASN A 1 92  ? -9.800  -2.683  6.838   1.00 20.76  ? 110 ASN A HA   1 
ATOM   1392  H  HB2  . ASN A 1 92  ? -11.233 -4.038  8.075   1.00 23.68  ? 110 ASN A HB2  1 
ATOM   1393  H  HB3  . ASN A 1 92  ? -11.380 -2.900  9.175   1.00 23.68  ? 110 ASN A HB3  1 
ATOM   1394  H  HD21 . ASN A 1 92  ? -13.878 -1.277  7.753   1.00 25.15  ? 110 ASN A HD21 1 
ATOM   1395  H  HD22 . ASN A 1 92  ? -12.993 -1.407  8.944   1.00 25.15  ? 110 ASN A HD22 1 
ATOM   1396  N  N    . ALA A 1 93  ? -9.747  -0.445  9.131   1.00 16.86  ? 111 ALA A N    1 
ATOM   1397  C  CA   . ALA A 1 93  ? -9.825  0.995   9.350   1.00 17.97  ? 111 ALA A CA   1 
ATOM   1398  C  C    . ALA A 1 93  ? -8.733  1.735   8.585   1.00 17.52  ? 111 ALA A C    1 
ATOM   1399  O  O    . ALA A 1 93  ? -8.978  2.813   8.035   1.00 18.02  ? 111 ALA A O    1 
ATOM   1400  C  CB   . ALA A 1 93  ? -9.750  1.306   10.843  1.00 18.36  ? 111 ALA A CB   1 
ATOM   1401  H  H    . ALA A 1 93  ? -9.545  -0.905  9.829   1.00 20.24  ? 111 ALA A H    1 
ATOM   1402  H  HA   . ALA A 1 93  ? -10.682 1.312   9.023   1.00 21.56  ? 111 ALA A HA   1 
ATOM   1403  H  HB1  . ALA A 1 93  ? -9.817  2.265   10.969  1.00 22.03  ? 111 ALA A HB1  1 
ATOM   1404  H  HB2  . ALA A 1 93  ? -10.483 0.861   11.296  1.00 22.03  ? 111 ALA A HB2  1 
ATOM   1405  H  HB3  . ALA A 1 93  ? -8.903  0.985   11.190  1.00 22.03  ? 111 ALA A HB3  1 
ATOM   1406  N  N    . ILE A 1 94  ? -7.517  1.186   8.554   1.00 17.38  ? 112 ILE A N    1 
ATOM   1407  C  CA   . ILE A 1 94  ? -6.449  1.802   7.770   1.00 16.70  ? 112 ILE A CA   1 
ATOM   1408  C  C    . ILE A 1 94  ? -6.830  1.833   6.296   1.00 17.70  ? 112 ILE A C    1 
ATOM   1409  O  O    . ILE A 1 94  ? -6.690  2.857   5.616   1.00 17.32  ? 112 ILE A O    1 
ATOM   1410  C  CB   . ILE A 1 94  ? -5.114  1.069   8.006   1.00 17.16  ? 112 ILE A CB   1 
ATOM   1411  C  CG1  . ILE A 1 94  ? -4.675  1.265   9.462   1.00 17.31  ? 112 ILE A CG1  1 
ATOM   1412  C  CG2  . ILE A 1 94  ? -4.061  1.559   7.020   1.00 17.97  ? 112 ILE A CG2  1 
ATOM   1413  C  CD1  . ILE A 1 94  ? -3.621  0.287   9.947   1.00 20.47  ? 112 ILE A CD1  1 
ATOM   1414  H  H    . ILE A 1 94  ? -7.289  0.469   8.971   1.00 20.86  ? 112 ILE A H    1 
ATOM   1415  H  HA   . ILE A 1 94  ? -6.334  2.718   8.066   1.00 20.04  ? 112 ILE A HA   1 
ATOM   1416  H  HB   . ILE A 1 94  ? -5.231  0.118   7.853   1.00 20.59  ? 112 ILE A HB   1 
ATOM   1417  H  HG12 . ILE A 1 94  ? -4.309  2.159   9.555   1.00 20.77  ? 112 ILE A HG12 1 
ATOM   1418  H  HG13 . ILE A 1 94  ? -5.452  1.164   10.034  1.00 20.77  ? 112 ILE A HG13 1 
ATOM   1419  H  HG21 . ILE A 1 94  ? -3.180  1.351   7.368   1.00 21.56  ? 112 ILE A HG21 1 
ATOM   1420  H  HG22 . ILE A 1 94  ? -4.194  1.113   6.168   1.00 21.56  ? 112 ILE A HG22 1 
ATOM   1421  H  HG23 . ILE A 1 94  ? -4.155  2.518   6.909   1.00 21.56  ? 112 ILE A HG23 1 
ATOM   1422  H  HD11 . ILE A 1 94  ? -2.816  0.404   9.419   1.00 24.57  ? 112 ILE A HD11 1 
ATOM   1423  H  HD12 . ILE A 1 94  ? -3.433  0.464   10.882  1.00 24.57  ? 112 ILE A HD12 1 
ATOM   1424  H  HD13 . ILE A 1 94  ? -3.958  -0.616  9.843   1.00 24.57  ? 112 ILE A HD13 1 
ATOM   1425  N  N    . THR A 1 95  ? -7.324  0.706   5.782   1.00 17.79  ? 113 THR A N    1 
ATOM   1426  C  CA   . THR A 1 95  ? -7.772  0.659   4.393   1.00 18.12  ? 113 THR A CA   1 
ATOM   1427  C  C    . THR A 1 95  ? -8.826  1.726   4.127   1.00 17.75  ? 113 THR A C    1 
ATOM   1428  O  O    . THR A 1 95  ? -8.753  2.448   3.128   1.00 19.02  ? 113 THR A O    1 
ATOM   1429  C  CB   . THR A 1 95  ? -8.322  -0.736  4.084   1.00 19.98  ? 113 THR A CB   1 
ATOM   1430  O  OG1  . THR A 1 95  ? -7.325  -1.716  4.410   1.00 20.74  ? 113 THR A OG1  1 
ATOM   1431  C  CG2  . THR A 1 95  ? -8.722  -0.878  2.595   1.00 20.67  ? 113 THR A CG2  1 
ATOM   1432  H  H    . THR A 1 95  ? -7.410  -0.035  6.210   1.00 21.35  ? 113 THR A H    1 
ATOM   1433  H  HA   . THR A 1 95  ? -7.020  0.827   3.803   1.00 21.75  ? 113 THR A HA   1 
ATOM   1434  H  HB   . THR A 1 95  ? -9.122  -0.887  4.612   1.00 23.98  ? 113 THR A HB   1 
ATOM   1435  H  HG1  . THR A 1 95  ? -6.658  -1.624  3.909   1.00 24.88  ? 113 THR A HG1  1 
ATOM   1436  H  HG21 . THR A 1 95  ? -8.926  -1.804  2.393   1.00 24.80  ? 113 THR A HG21 1 
ATOM   1437  H  HG22 . THR A 1 95  ? -9.505  -0.336  2.409   1.00 24.80  ? 113 THR A HG22 1 
ATOM   1438  H  HG23 . THR A 1 95  ? -7.994  -0.584  2.026   1.00 24.80  ? 113 THR A HG23 1 
ATOM   1439  N  N    . ALA A 1 96  ? -9.786  1.871   5.037   1.00 17.80  ? 114 ALA A N    1 
ATOM   1440  C  CA   . ALA A 1 96  ? -10.872 2.822   4.829   1.00 17.33  ? 114 ALA A CA   1 
ATOM   1441  C  C    . ALA A 1 96  ? -10.384 4.263   4.934   1.00 17.16  ? 114 ALA A C    1 
ATOM   1442  O  O    . ALA A 1 96  ? -10.749 5.111   4.109   1.00 17.87  ? 114 ALA A O    1 
ATOM   1443  C  CB   . ALA A 1 96  ? -11.982 2.564   5.845   1.00 19.12  ? 114 ALA A CB   1 
ATOM   1444  H  H    . ALA A 1 96  ? -9.832  1.435   5.777   1.00 21.36  ? 114 ALA A H    1 
ATOM   1445  H  HA   . ALA A 1 96  ? -11.231 2.694   3.937   1.00 20.80  ? 114 ALA A HA   1 
ATOM   1446  H  HB1  . ALA A 1 96  ? -12.717 3.172   5.671   1.00 22.94  ? 114 ALA A HB1  1 
ATOM   1447  H  HB2  . ALA A 1 96  ? -12.284 1.646   5.757   1.00 22.94  ? 114 ALA A HB2  1 
ATOM   1448  H  HB3  . ALA A 1 96  ? -11.633 2.713   6.738   1.00 22.94  ? 114 ALA A HB3  1 
ATOM   1449  N  N    . LEU A 1 97  ? -9.564  4.560   5.945   1.00 16.44  ? 115 LEU A N    1 
ATOM   1450  C  CA   . LEU A 1 97  ? -9.112  5.933   6.151   1.00 16.93  ? 115 LEU A CA   1 
ATOM   1451  C  C    . LEU A 1 97  ? -8.102  6.362   5.094   1.00 17.17  ? 115 LEU A C    1 
ATOM   1452  O  O    . LEU A 1 97  ? -8.077  7.536   4.700   1.00 18.38  ? 115 LEU A O    1 
ATOM   1453  C  CB   . LEU A 1 97  ? -8.526  6.085   7.553   1.00 17.38  ? 115 LEU A CB   1 
ATOM   1454  C  CG   . LEU A 1 97  ? -9.542  5.877   8.673   1.00 16.20  ? 115 LEU A CG   1 
ATOM   1455  C  CD1  . LEU A 1 97  ? -8.835  5.718   10.016  1.00 16.50  ? 115 LEU A CD1  1 
ATOM   1456  C  CD2  . LEU A 1 97  ? -10.549 7.018   8.722   1.00 17.18  ? 115 LEU A CD2  1 
ATOM   1457  H  H    . LEU A 1 97  ? -9.260  3.993   6.516   1.00 19.73  ? 115 LEU A H    1 
ATOM   1458  H  HA   . LEU A 1 97  ? -9.876  6.527   6.082   1.00 20.32  ? 115 LEU A HA   1 
ATOM   1459  H  HB2  . LEU A 1 97  ? -7.820  5.429   7.667   1.00 20.85  ? 115 LEU A HB2  1 
ATOM   1460  H  HB3  . LEU A 1 97  ? -8.164  6.980   7.643   1.00 20.85  ? 115 LEU A HB3  1 
ATOM   1461  H  HG   . LEU A 1 97  ? -10.036 5.061   8.496   1.00 19.44  ? 115 LEU A HG   1 
ATOM   1462  H  HD11 . LEU A 1 97  ? -8.382  6.547   10.234  1.00 19.79  ? 115 LEU A HD11 1 
ATOM   1463  H  HD12 . LEU A 1 97  ? -9.494  5.511   10.697  1.00 19.79  ? 115 LEU A HD12 1 
ATOM   1464  H  HD13 . LEU A 1 97  ? -8.190  4.996   9.950   1.00 19.79  ? 115 LEU A HD13 1 
ATOM   1465  H  HD21 . LEU A 1 97  ? -10.076 7.850   8.880   1.00 20.62  ? 115 LEU A HD21 1 
ATOM   1466  H  HD22 . LEU A 1 97  ? -11.019 7.060   7.874   1.00 20.62  ? 115 LEU A HD22 1 
ATOM   1467  H  HD23 . LEU A 1 97  ? -11.178 6.853   9.441   1.00 20.62  ? 115 LEU A HD23 1 
ATOM   1468  N  N    . TYR A 1 98  ? -7.256  5.441   4.634   1.00 17.64  ? 116 TYR A N    1 
ATOM   1469  C  CA   . TYR A 1 98  ? -6.361  5.752   3.524   1.00 18.11  ? 116 TYR A CA   1 
ATOM   1470  C  C    . TYR A 1 98  ? -7.171  6.148   2.301   1.00 20.01  ? 116 TYR A C    1 
ATOM   1471  O  O    . TYR A 1 98  ? -6.918  7.186   1.679   1.00 20.25  ? 116 TYR A O    1 
ATOM   1472  C  CB   . TYR A 1 98  ? -5.475  4.536   3.232   1.00 19.05  ? 116 TYR A CB   1 
ATOM   1473  C  CG   . TYR A 1 98  ? -4.445  4.731   2.136   1.00 19.22  ? 116 TYR A CG   1 
ATOM   1474  C  CD1  . TYR A 1 98  ? -3.273  5.438   2.372   1.00 20.16  ? 116 TYR A CD1  1 
ATOM   1475  C  CD2  . TYR A 1 98  ? -4.636  4.188   0.869   1.00 20.50  ? 116 TYR A CD2  1 
ATOM   1476  C  CE1  . TYR A 1 98  ? -2.323  5.617   1.373   1.00 21.47  ? 116 TYR A CE1  1 
ATOM   1477  C  CE2  . TYR A 1 98  ? -3.693  4.357   -0.133  1.00 20.57  ? 116 TYR A CE2  1 
ATOM   1478  C  CZ   . TYR A 1 98  ? -2.540  5.072   0.124   1.00 22.24  ? 116 TYR A CZ   1 
ATOM   1479  O  OH   . TYR A 1 98  ? -1.606  5.234   -0.873  1.00 23.14  ? 116 TYR A OH   1 
ATOM   1480  H  H    . TYR A 1 98  ? -7.182  4.642   4.942   1.00 21.17  ? 116 TYR A H    1 
ATOM   1481  H  HA   . TYR A 1 98  ? -5.781  6.493   3.758   1.00 21.74  ? 116 TYR A HA   1 
ATOM   1482  H  HB2  . TYR A 1 98  ? -4.995  4.306   4.043   1.00 22.86  ? 116 TYR A HB2  1 
ATOM   1483  H  HB3  . TYR A 1 98  ? -6.046  3.799   2.965   1.00 22.86  ? 116 TYR A HB3  1 
ATOM   1484  H  HD1  . TYR A 1 98  ? -3.121  5.799   3.216   1.00 24.20  ? 116 TYR A HD1  1 
ATOM   1485  H  HD2  . TYR A 1 98  ? -5.409  3.703   0.691   1.00 24.60  ? 116 TYR A HD2  1 
ATOM   1486  H  HE1  . TYR A 1 98  ? -1.548  6.101   1.545   1.00 25.77  ? 116 TYR A HE1  1 
ATOM   1487  H  HE2  . TYR A 1 98  ? -3.836  3.991   -0.976  1.00 24.69  ? 116 TYR A HE2  1 
ATOM   1488  H  HH   . TYR A 1 98  ? -0.954  5.680   -0.586  1.00 27.77  ? 116 TYR A HH   1 
ATOM   1489  N  N    . ALA A 1 99  ? -8.192  5.354   1.980   1.00 19.78  ? 117 ALA A N    1 
ATOM   1490  C  CA   . ALA A 1 99  ? -9.024  5.644   0.819   1.00 21.40  ? 117 ALA A CA   1 
ATOM   1491  C  C    . ALA A 1 99  ? -9.858  6.904   1.025   1.00 22.02  ? 117 ALA A C    1 
ATOM   1492  O  O    . ALA A 1 99  ? -10.042 7.690   0.088   1.00 24.60  ? 117 ALA A O    1 
ATOM   1493  C  CB   . ALA A 1 99  ? -9.926  4.443   0.515   1.00 21.98  ? 117 ALA A CB   1 
ATOM   1494  H  H    . ALA A 1 99  ? -8.421  4.648   2.414   1.00 23.74  ? 117 ALA A H    1 
ATOM   1495  H  HA   . ALA A 1 99  ? -8.449  5.795   0.052   1.00 25.68  ? 117 ALA A HA   1 
ATOM   1496  H  HB1  . ALA A 1 99  ? -10.461 4.640   -0.269  1.00 26.37  ? 117 ALA A HB1  1 
ATOM   1497  H  HB2  . ALA A 1 99  ? -9.371  3.665   0.350   1.00 26.37  ? 117 ALA A HB2  1 
ATOM   1498  H  HB3  . ALA A 1 99  ? -10.504 4.281   1.278   1.00 26.37  ? 117 ALA A HB3  1 
ATOM   1499  N  N    . GLY A 1 100 ? -10.375 7.110   2.239   1.00 21.00  ? 118 GLY A N    1 
ATOM   1500  C  CA   . GLY A 1 100 ? -11.223 8.258   2.510   1.00 20.95  ? 118 GLY A CA   1 
ATOM   1501  C  C    . GLY A 1 100 ? -10.498 9.581   2.647   1.00 21.20  ? 118 GLY A C    1 
ATOM   1502  O  O    . GLY A 1 100 ? -11.150 10.629  2.687   1.00 22.52  ? 118 GLY A O    1 
ATOM   1503  H  H    . GLY A 1 100 ? -10.247 6.597   2.917   1.00 25.19  ? 118 GLY A H    1 
ATOM   1504  H  HA2  . GLY A 1 100 ? -11.863 8.348   1.787   1.00 25.14  ? 118 GLY A HA2  1 
ATOM   1505  H  HA3  . GLY A 1 100 ? -11.702 8.099   3.338   1.00 25.14  ? 118 GLY A HA3  1 
ATOM   1506  N  N    . SER A 1 101 ? -9.169  9.559   2.715   1.00 21.02  ? 119 SER A N    1 
ATOM   1507  C  CA   . SER A 1 101 ? -8.364  10.770  2.753   1.00 21.08  ? 119 SER A CA   1 
ATOM   1508  C  C    . SER A 1 101 ? -7.579  10.975  1.463   1.00 23.03  ? 119 SER A C    1 
ATOM   1509  O  O    . SER A 1 101 ? -6.577  11.699  1.462   1.00 25.64  ? 119 SER A O    1 
ATOM   1510  C  CB   . SER A 1 101 ? -7.431  10.783  3.968   1.00 21.39  ? 119 SER A CB   1 
ATOM   1511  O  OG   . SER A 1 101 ? -6.470  9.739   3.930   1.00 21.10  ? 119 SER A OG   1 
ATOM   1512  H  H    . SER A 1 101 ? -8.703  8.836   2.739   1.00 25.23  ? 119 SER A H    1 
ATOM   1513  H  HA   . SER A 1 101 ? -8.964  11.526  2.857   1.00 25.29  ? 119 SER A HA   1 
ATOM   1514  H  HB2  . SER A 1 101 ? -6.964  11.633  3.990   1.00 25.67  ? 119 SER A HB2  1 
ATOM   1515  H  HB3  . SER A 1 101 ? -7.967  10.679  4.770   1.00 25.67  ? 119 SER A HB3  1 
ATOM   1516  H  HG   . SER A 1 101 ? -5.975  9.778   4.608   1.00 25.32  ? 119 SER A HG   1 
ATOM   1517  N  N    . GLY A 1 102 ? -8.011  10.345  0.370   1.00 23.36  ? 120 GLY A N    1 
ATOM   1518  C  CA   . GLY A 1 102 ? -7.403  10.568  -0.927  1.00 23.13  ? 120 GLY A CA   1 
ATOM   1519  C  C    . GLY A 1 102 ? -6.162  9.750   -1.192  1.00 23.73  ? 120 GLY A C    1 
ATOM   1520  O  O    . GLY A 1 102 ? -5.277  10.196  -1.930  1.00 24.03  ? 120 GLY A O    1 
ATOM   1521  H  H    . GLY A 1 102 ? -8.660  9.780   0.359   1.00 28.03  ? 120 GLY A H    1 
ATOM   1522  H  HA2  . GLY A 1 102 ? -8.051  10.354  -1.616  1.00 27.75  ? 120 GLY A HA2  1 
ATOM   1523  H  HA3  . GLY A 1 102 ? -7.161  11.505  -1.001  1.00 27.75  ? 120 GLY A HA3  1 
ATOM   1524  N  N    . ASN A 1 103 ? -6.077  8.553   -0.617  1.00 21.99  ? 121 ASN A N    1 
ATOM   1525  C  CA   . ASN A 1 103 ? -4.885  7.708   -0.719  1.00 22.33  ? 121 ASN A CA   1 
ATOM   1526  C  C    . ASN A 1 103 ? -3.656  8.434   -0.174  1.00 22.51  ? 121 ASN A C    1 
ATOM   1527  O  O    . ASN A 1 103 ? -2.617  8.534   -0.828  1.00 24.03  ? 121 ASN A O    1 
ATOM   1528  C  CB   . ASN A 1 103 ? -4.661  7.216   -2.151  1.00 22.47  ? 121 ASN A CB   1 
ATOM   1529  C  CG   . ASN A 1 103 ? -5.508  6.003   -2.489  1.00 22.76  ? 121 ASN A CG   1 
ATOM   1530  O  OD1  . ASN A 1 103 ? -6.586  5.802   -1.923  1.00 22.14  ? 121 ASN A OD1  1 
ATOM   1531  N  ND2  . ASN A 1 103 ? -5.024  5.188   -3.416  1.00 23.18  ? 121 ASN A ND2  1 
ATOM   1532  H  H    . ASN A 1 103 ? -6.708  8.199   -0.153  1.00 26.39  ? 121 ASN A H    1 
ATOM   1533  H  HA   . ASN A 1 103 ? -5.024  6.921   -0.170  1.00 26.79  ? 121 ASN A HA   1 
ATOM   1534  H  HB2  . ASN A 1 103 ? -4.892  7.926   -2.770  1.00 26.97  ? 121 ASN A HB2  1 
ATOM   1535  H  HB3  . ASN A 1 103 ? -3.729  6.972   -2.259  1.00 26.97  ? 121 ASN A HB3  1 
ATOM   1536  H  HD21 . ASN A 1 103 ? -5.465  4.486   -3.644  1.00 27.82  ? 121 ASN A HD21 1 
ATOM   1537  H  HD22 . ASN A 1 103 ? -4.269  5.362   -3.789  1.00 27.82  ? 121 ASN A HD22 1 
ATOM   1538  N  N    . ASN A 1 104 ? -3.794  8.972   1.032   1.00 21.57  ? 122 ASN A N    1 
ATOM   1539  C  CA   . ASN A 1 104 ? -2.690  9.594   1.745   1.00 21.88  ? 122 ASN A CA   1 
ATOM   1540  C  C    . ASN A 1 104 ? -2.405  8.795   3.004   1.00 20.58  ? 122 ASN A C    1 
ATOM   1541  O  O    . ASN A 1 104 ? -3.329  8.388   3.714   1.00 20.50  ? 122 ASN A O    1 
ATOM   1542  C  CB   . ASN A 1 104 ? -3.023  11.034  2.113   1.00 24.32  ? 122 ASN A CB   1 
ATOM   1543  C  CG   . ASN A 1 104 ? -2.947  11.958  0.925   1.00 26.27  ? 122 ASN A CG   1 
ATOM   1544  O  OD1  . ASN A 1 104 ? -1.870  12.187  0.375   1.00 29.04  ? 122 ASN A OD1  1 
ATOM   1545  N  ND2  . ASN A 1 104 ? -4.089  12.483  0.509   1.00 27.08  ? 122 ASN A ND2  1 
ATOM   1546  H  H    . ASN A 1 104 ? -4.536  8.987   1.467   1.00 25.88  ? 122 ASN A H    1 
ATOM   1547  H  HA   . ASN A 1 104 ? -1.895  9.600   1.189   1.00 26.26  ? 122 ASN A HA   1 
ATOM   1548  H  HB2  . ASN A 1 104 ? -3.926  11.072  2.468   1.00 29.19  ? 122 ASN A HB2  1 
ATOM   1549  H  HB3  . ASN A 1 104 ? -2.392  11.347  2.780   1.00 29.19  ? 122 ASN A HB3  1 
ATOM   1550  H  HD21 . ASN A 1 104 ? -4.824  12.292  0.914   1.00 32.50  ? 122 ASN A HD21 1 
ATOM   1551  H  HD22 . ASN A 1 104 ? -4.097  13.017  -0.166  1.00 32.50  ? 122 ASN A HD22 1 
ATOM   1552  N  N    . LYS A 1 105 ? -1.123  8.559   3.269   1.00 20.45  ? 123 LYS A N    1 
ATOM   1553  C  CA   . LYS A 1 105 ? -0.754  7.814   4.462   1.00 18.82  ? 123 LYS A CA   1 
ATOM   1554  C  C    . LYS A 1 105 ? -1.265  8.537   5.702   1.00 17.91  ? 123 LYS A C    1 
ATOM   1555  O  O    . LYS A 1 105 ? -1.441  9.759   5.707   1.00 18.88  ? 123 LYS A O    1 
ATOM   1556  C  CB   . LYS A 1 105 ? 0.764   7.667   4.557   1.00 20.11  ? 123 LYS A CB   1 
ATOM   1557  C  CG   . LYS A 1 105 ? 1.385   6.784   3.485   1.00 21.77  ? 123 LYS A CG   1 
ATOM   1558  C  CD   . LYS A 1 105 ? 2.843   6.492   3.817   1.00 24.84  ? 123 LYS A CD   1 
ATOM   1559  C  CE   . LYS A 1 105 ? 3.541   5.737   2.703   1.00 26.39  ? 123 LYS A CE   1 
ATOM   1560  N  NZ   . LYS A 1 105 ? 4.983   5.521   3.028   1.00 28.51  ? 123 LYS A NZ   1 
ATOM   1561  H  H    . LYS A 1 105 ? -0.462  8.815   2.782   1.00 24.54  ? 123 LYS A H    1 
ATOM   1562  H  HA   . LYS A 1 105 ? -1.144  6.927   4.422   1.00 22.59  ? 123 LYS A HA   1 
ATOM   1563  H  HB2  . LYS A 1 105 ? 1.164   8.547   4.478   1.00 24.13  ? 123 LYS A HB2  1 
ATOM   1564  H  HB3  . LYS A 1 105 ? 0.983   7.279   5.418   1.00 24.13  ? 123 LYS A HB3  1 
ATOM   1565  H  HG2  . LYS A 1 105 ? 0.904   5.943   3.437   1.00 26.12  ? 123 LYS A HG2  1 
ATOM   1566  H  HG3  . LYS A 1 105 ? 1.347   7.237   2.628   1.00 26.12  ? 123 LYS A HG3  1 
ATOM   1567  H  HD2  . LYS A 1 105 ? 3.313   7.330   3.955   1.00 29.81  ? 123 LYS A HD2  1 
ATOM   1568  H  HD3  . LYS A 1 105 ? 2.886   5.952   4.622   1.00 29.81  ? 123 LYS A HD3  1 
ATOM   1569  H  HE2  . LYS A 1 105 ? 3.119   4.872   2.585   1.00 31.67  ? 123 LYS A HE2  1 
ATOM   1570  H  HE3  . LYS A 1 105 ? 3.485   6.249   1.881   1.00 31.67  ? 123 LYS A HE3  1 
ATOM   1571  H  HZ1  . LYS A 1 105 ? 5.383   5.084   2.364   1.00 34.21  ? 123 LYS A HZ1  1 
ATOM   1572  H  HZ2  . LYS A 1 105 ? 5.390   6.304   3.145   1.00 34.21  ? 123 LYS A HZ2  1 
ATOM   1573  H  HZ3  . LYS A 1 105 ? 5.058   5.042   3.775   1.00 34.21  ? 123 LYS A HZ3  1 
ATOM   1574  N  N    . LEU A 1 106 ? -1.494  7.771   6.766   1.00 17.44  ? 124 LEU A N    1 
ATOM   1575  C  CA   . LEU A 1 106 ? -1.979  8.341   8.011   1.00 17.69  ? 124 LEU A CA   1 
ATOM   1576  C  C    . LEU A 1 106 ? -1.190  7.791   9.189   1.00 16.57  ? 124 LEU A C    1 
ATOM   1577  O  O    . LEU A 1 106 ? -0.634  6.689   9.120   1.00 16.14  ? 124 LEU A O    1 
ATOM   1578  C  CB   . LEU A 1 106 ? -3.468  8.030   8.222   1.00 18.95  ? 124 LEU A CB   1 
ATOM   1579  C  CG   . LEU A 1 106 ? -3.890  6.559   8.214   1.00 19.62  ? 124 LEU A CG   1 
ATOM   1580  C  CD1  . LEU A 1 106 ? -4.988  6.321   9.255   1.00 21.51  ? 124 LEU A CD1  1 
ATOM   1581  C  CD2  . LEU A 1 106 ? -4.356  6.121   6.820   1.00 20.72  ? 124 LEU A CD2  1 
ATOM   1582  H  H    . LEU A 1 106 ? -1.374  6.919   6.787   1.00 20.92  ? 124 LEU A H    1 
ATOM   1583  H  HA   . LEU A 1 106 ? -1.861  9.303   7.985   1.00 21.23  ? 124 LEU A HA   1 
ATOM   1584  H  HB2  . LEU A 1 106 ? -3.727  8.391   9.084   1.00 22.74  ? 124 LEU A HB2  1 
ATOM   1585  H  HB3  . LEU A 1 106 ? -3.965  8.468   7.515   1.00 22.74  ? 124 LEU A HB3  1 
ATOM   1586  H  HG   . LEU A 1 106 ? -3.123  6.011   8.446   1.00 23.54  ? 124 LEU A HG   1 
ATOM   1587  H  HD11 . LEU A 1 106 ? -4.624  6.478   10.140  1.00 25.82  ? 124 LEU A HD11 1 
ATOM   1588  H  HD12 . LEU A 1 106 ? -5.721  6.933   9.086   1.00 25.82  ? 124 LEU A HD12 1 
ATOM   1589  H  HD13 . LEU A 1 106 ? -5.299  5.405   9.183   1.00 25.82  ? 124 LEU A HD13 1 
ATOM   1590  H  HD21 . LEU A 1 106 ? -5.158  6.613   6.587   1.00 24.87  ? 124 LEU A HD21 1 
ATOM   1591  H  HD22 . LEU A 1 106 ? -3.654  6.309   6.178   1.00 24.87  ? 124 LEU A HD22 1 
ATOM   1592  H  HD23 . LEU A 1 106 ? -4.545  5.169   6.835   1.00 24.87  ? 124 LEU A HD23 1 
ATOM   1593  N  N    . PRO A 1 107 ? -1.102  8.553   10.274  1.00 16.18  ? 125 PRO A N    1 
ATOM   1594  C  CA   . PRO A 1 107 ? -0.450  8.048   11.487  1.00 15.64  ? 125 PRO A CA   1 
ATOM   1595  C  C    . PRO A 1 107 ? -1.390  7.187   12.317  1.00 15.34  ? 125 PRO A C    1 
ATOM   1596  O  O    . PRO A 1 107 ? -2.611  7.349   12.289  1.00 15.21  ? 125 PRO A O    1 
ATOM   1597  C  CB   . PRO A 1 107 ? -0.097  9.336   12.243  1.00 15.11  ? 125 PRO A CB   1 
ATOM   1598  C  CG   . PRO A 1 107 ? -1.194  10.269  11.852  1.00 15.46  ? 125 PRO A CG   1 
ATOM   1599  C  CD   . PRO A 1 107 ? -1.511  9.963   10.412  1.00 15.46  ? 125 PRO A CD   1 
ATOM   1600  H  HA   . PRO A 1 107 ? 0.354   7.550   11.273  1.00 18.77  ? 125 PRO A HA   1 
ATOM   1601  H  HB2  . PRO A 1 107 ? -0.092  9.177   13.200  1.00 18.13  ? 125 PRO A HB2  1 
ATOM   1602  H  HB3  . PRO A 1 107 ? 0.769   9.669   11.958  1.00 18.13  ? 125 PRO A HB3  1 
ATOM   1603  H  HG2  . PRO A 1 107 ? -1.970  10.114  12.413  1.00 18.56  ? 125 PRO A HG2  1 
ATOM   1604  H  HG3  . PRO A 1 107 ? -0.893  11.186  11.949  1.00 18.56  ? 125 PRO A HG3  1 
ATOM   1605  H  HD2  . PRO A 1 107 ? -2.459  10.068  10.236  1.00 18.55  ? 125 PRO A HD2  1 
ATOM   1606  H  HD3  . PRO A 1 107 ? -0.998  10.532  9.817   1.00 18.55  ? 125 PRO A HD3  1 
ATOM   1607  N  N    . VAL A 1 108 ? -0.789  6.266   13.069  1.00 15.26  ? 126 VAL A N    1 
ATOM   1608  C  CA   . VAL A 1 108 ? -1.489  5.407   14.015  1.00 14.68  ? 126 VAL A CA   1 
ATOM   1609  C  C    . VAL A 1 108 ? -0.887  5.657   15.391  1.00 13.60  ? 126 VAL A C    1 
ATOM   1610  O  O    . VAL A 1 108 ? 0.338   5.702   15.538  1.00 14.13  ? 126 VAL A O    1 
ATOM   1611  C  CB   . VAL A 1 108 ? -1.372  3.927   13.609  1.00 15.95  ? 126 VAL A CB   1 
ATOM   1612  C  CG1  . VAL A 1 108 ? -2.061  3.029   14.628  1.00 15.32  ? 126 VAL A CG1  1 
ATOM   1613  C  CG2  . VAL A 1 108 ? -1.965  3.737   12.214  1.00 17.15  ? 126 VAL A CG2  1 
ATOM   1614  H  H    . VAL A 1 108 ? 0.058   6.117   13.047  1.00 18.31  ? 126 VAL A H    1 
ATOM   1615  H  HA   . VAL A 1 108 ? -2.431  5.635   14.048  1.00 17.62  ? 126 VAL A HA   1 
ATOM   1616  H  HB   . VAL A 1 108 ? -0.437  3.667   13.588  1.00 19.14  ? 126 VAL A HB   1 
ATOM   1617  H  HG11 . VAL A 1 108 ? -2.069  2.119   14.292  1.00 18.39  ? 126 VAL A HG11 1 
ATOM   1618  H  HG12 . VAL A 1 108 ? -1.573  3.068   15.465  1.00 18.39  ? 126 VAL A HG12 1 
ATOM   1619  H  HG13 . VAL A 1 108 ? -2.970  3.340   14.760  1.00 18.39  ? 126 VAL A HG13 1 
ATOM   1620  H  HG21 . VAL A 1 108 ? -2.302  4.589   11.896  1.00 20.58  ? 126 VAL A HG21 1 
ATOM   1621  H  HG22 . VAL A 1 108 ? -1.272  3.412   11.618  1.00 20.58  ? 126 VAL A HG22 1 
ATOM   1622  H  HG23 . VAL A 1 108 ? -2.688  3.093   12.263  1.00 20.58  ? 126 VAL A HG23 1 
ATOM   1623  N  N    . LEU A 1 109 ? -1.747  5.851   16.383  1.00 14.38  ? 127 LEU A N    1 
ATOM   1624  C  CA   . LEU A 1 109 ? -1.348  6.149   17.752  1.00 13.24  ? 127 LEU A CA   1 
ATOM   1625  C  C    . LEU A 1 109 ? -2.110  5.200   18.666  1.00 13.61  ? 127 LEU A C    1 
ATOM   1626  O  O    . LEU A 1 109 ? -3.321  5.013   18.501  1.00 13.81  ? 127 LEU A O    1 
ATOM   1627  C  CB   . LEU A 1 109 ? -1.632  7.620   18.078  1.00 13.23  ? 127 LEU A CB   1 
ATOM   1628  C  CG   . LEU A 1 109 ? -1.133  8.178   19.409  1.00 14.35  ? 127 LEU A CG   1 
ATOM   1629  C  CD1  . LEU A 1 109 ? -0.912  9.684   19.324  1.00 15.14  ? 127 LEU A CD1  1 
ATOM   1630  C  CD2  . LEU A 1 109 ? -2.108  7.857   20.529  1.00 16.25  ? 127 LEU A CD2  1 
ATOM   1631  H  H    . LEU A 1 109 ? -2.601  5.814   16.283  1.00 17.26  ? 127 LEU A H    1 
ATOM   1632  H  HA   . LEU A 1 109 ? -0.400  6.002   17.896  1.00 15.89  ? 127 LEU A HA   1 
ATOM   1633  H  HB2  . LEU A 1 109 ? -1.224  8.159   17.381  1.00 15.88  ? 127 LEU A HB2  1 
ATOM   1634  H  HB3  . LEU A 1 109 ? -2.594  7.742   18.070  1.00 15.88  ? 127 LEU A HB3  1 
ATOM   1635  H  HG   . LEU A 1 109 ? -0.283  7.759   19.615  1.00 17.22  ? 127 LEU A HG   1 
ATOM   1636  H  HD11 . LEU A 1 109 ? -0.617  10.010  20.188  1.00 18.16  ? 127 LEU A HD11 1 
ATOM   1637  H  HD12 . LEU A 1 109 ? -0.235  9.866   18.653  1.00 18.16  ? 127 LEU A HD12 1 
ATOM   1638  H  HD13 . LEU A 1 109 ? -1.747  10.112  19.076  1.00 18.16  ? 127 LEU A HD13 1 
ATOM   1639  H  HD21 . LEU A 1 109 ? -2.106  6.899   20.684  1.00 19.51  ? 127 LEU A HD21 1 
ATOM   1640  H  HD22 . LEU A 1 109 ? -1.832  8.323   21.333  1.00 19.51  ? 127 LEU A HD22 1 
ATOM   1641  H  HD23 . LEU A 1 109 ? -2.996  8.147   20.267  1.00 19.51  ? 127 LEU A HD23 1 
ATOM   1642  N  N    . THR A 1 110 ? -1.400  4.574   19.605  1.00 13.26  ? 128 THR A N    1 
ATOM   1643  C  CA   . THR A 1 110 ? -1.965  3.437   20.312  1.00 13.63  ? 128 THR A CA   1 
ATOM   1644  C  C    . THR A 1 110 ? -1.639  3.504   21.795  1.00 13.01  ? 128 THR A C    1 
ATOM   1645  O  O    . THR A 1 110 ? -0.679  4.152   22.216  1.00 13.02  ? 128 THR A O    1 
ATOM   1646  C  CB   . THR A 1 110 ? -1.432  2.096   19.759  1.00 13.76  ? 128 THR A CB   1 
ATOM   1647  O  OG1  . THR A 1 110 ? -0.044  1.929   20.088  1.00 13.78  ? 128 THR A OG1  1 
ATOM   1648  C  CG2  . THR A 1 110 ? -1.599  2.019   18.243  1.00 15.52  ? 128 THR A CG2  1 
ATOM   1649  H  H    . THR A 1 110 ? -0.602  4.790   19.843  1.00 15.91  ? 128 THR A H    1 
ATOM   1650  H  HA   . THR A 1 110 ? -2.928  3.480   20.209  1.00 16.35  ? 128 THR A HA   1 
ATOM   1651  H  HB   . THR A 1 110 ? -1.943  1.377   20.161  1.00 16.52  ? 128 THR A HB   1 
ATOM   1652  H  HG1  . THR A 1 110 ? 0.433   2.371   19.556  1.00 16.54  ? 128 THR A HG1  1 
ATOM   1653  H  HG21 . THR A 1 110 ? -1.467  1.107   17.941  1.00 18.62  ? 128 THR A HG21 1 
ATOM   1654  H  HG22 . THR A 1 110 ? -2.491  2.307   17.993  1.00 18.62  ? 128 THR A HG22 1 
ATOM   1655  H  HG23 . THR A 1 110 ? -0.949  2.592   17.808  1.00 18.62  ? 128 THR A HG23 1 
ATOM   1656  N  N    . TRP A 1 111 ? -2.432  2.775   22.580  1.00 13.45  ? 129 TRP A N    1 
ATOM   1657  C  CA   . TRP A 1 111 ? -2.145  2.549   23.988  1.00 12.50  ? 129 TRP A CA   1 
ATOM   1658  C  C    . TRP A 1 111 ? -2.200  1.057   24.270  1.00 13.64  ? 129 TRP A C    1 
ATOM   1659  O  O    . TRP A 1 111 ? -3.119  0.371   23.820  1.00 13.90  ? 129 TRP A O    1 
ATOM   1660  C  CB   . TRP A 1 111 ? -3.168  3.249   24.888  1.00 13.27  ? 129 TRP A CB   1 
ATOM   1661  C  CG   . TRP A 1 111 ? -2.908  3.079   26.353  1.00 12.79  ? 129 TRP A CG   1 
ATOM   1662  C  CD1  . TRP A 1 111 ? -1.703  3.175   26.987  1.00 13.38  ? 129 TRP A CD1  1 
ATOM   1663  C  CD2  . TRP A 1 111 ? -3.875  2.795   27.371  1.00 13.49  ? 129 TRP A CD2  1 
ATOM   1664  N  NE1  . TRP A 1 111 ? -1.859  2.965   28.334  1.00 13.42  ? 129 TRP A NE1  1 
ATOM   1665  C  CE2  . TRP A 1 111 ? -3.184  2.733   28.596  1.00 13.51  ? 129 TRP A CE2  1 
ATOM   1666  C  CE3  . TRP A 1 111 ? -5.258  2.587   27.366  1.00 14.51  ? 129 TRP A CE3  1 
ATOM   1667  C  CZ2  . TRP A 1 111 ? -3.826  2.468   29.801  1.00 14.98  ? 129 TRP A CZ2  1 
ATOM   1668  C  CZ3  . TRP A 1 111 ? -5.893  2.336   28.560  1.00 15.49  ? 129 TRP A CZ3  1 
ATOM   1669  C  CH2  . TRP A 1 111 ? -5.179  2.275   29.763  1.00 15.85  ? 129 TRP A CH2  1 
ATOM   1670  H  H    . TRP A 1 111 ? -3.155  2.396   22.311  1.00 16.15  ? 129 TRP A H    1 
ATOM   1671  H  HA   . TRP A 1 111 ? -1.260  2.889   24.192  1.00 15.00  ? 129 TRP A HA   1 
ATOM   1672  H  HB2  . TRP A 1 111 ? -3.155  4.199   24.694  1.00 15.92  ? 129 TRP A HB2  1 
ATOM   1673  H  HB3  . TRP A 1 111 ? -4.048  2.885   24.701  1.00 15.92  ? 129 TRP A HB3  1 
ATOM   1674  H  HD1  . TRP A 1 111 ? -0.893  3.356   26.567  1.00 16.06  ? 129 TRP A HD1  1 
ATOM   1675  H  HE1  . TRP A 1 111 ? -1.229  2.978   28.918  1.00 16.10  ? 129 TRP A HE1  1 
ATOM   1676  H  HE3  . TRP A 1 111 ? -5.739  2.618   26.571  1.00 17.42  ? 129 TRP A HE3  1 
ATOM   1677  H  HZ2  . TRP A 1 111 ? -3.354  2.425   30.601  1.00 17.98  ? 129 TRP A HZ2  1 
ATOM   1678  H  HZ3  . TRP A 1 111 ? -6.814  2.205   28.569  1.00 18.59  ? 129 TRP A HZ3  1 
ATOM   1679  H  HH2  . TRP A 1 111 ? -5.635  2.098   30.554  1.00 19.02  ? 129 TRP A HH2  1 
ATOM   1680  N  N    . SER A 1 112 ? -1.218  0.560   25.022  1.00 14.22  ? 130 SER A N    1 
ATOM   1681  C  CA   . SER A 1 112 ? -1.275  -0.784  25.612  1.00 15.13  ? 130 SER A CA   1 
ATOM   1682  C  C    . SER A 1 112 ? -1.441  -1.803  24.490  1.00 14.65  ? 130 SER A C    1 
ATOM   1683  O  O    . SER A 1 112 ? -0.658  -1.745  23.526  1.00 15.82  ? 130 SER A O    1 
ATOM   1684  C  CB   . SER A 1 112 ? -2.379  -0.749  26.663  1.00 17.75  ? 130 SER A CB   1 
ATOM   1685  O  OG   . SER A 1 112 ? -2.419  -1.959  27.393  1.00 23.59  ? 130 SER A OG   1 
ATOM   1686  H  H    . SER A 1 112 ? -0.495  0.987   25.210  1.00 17.07  ? 130 SER A H    1 
ATOM   1687  H  HA   . SER A 1 112 ? -0.427  -1.007  26.027  1.00 18.15  ? 130 SER A HA   1 
ATOM   1688  H  HB2  . SER A 1 112 ? -2.209  -0.016  27.275  1.00 21.30  ? 130 SER A HB2  1 
ATOM   1689  H  HB3  . SER A 1 112 ? -3.232  -0.621  26.220  1.00 21.30  ? 130 SER A HB3  1 
ATOM   1690  H  HG   . SER A 1 112 ? -1.643  -2.175  27.633  1.00 28.31  ? 130 SER A HG   1 
ATOM   1691  N  N    . GLN A 1 113 ? -2.414  -2.722  24.578  1.00 14.34  ? 131 GLN A N    1 
ATOM   1692  C  CA   . GLN A 1 113 ? -2.622  -3.747  23.560  1.00 13.93  ? 131 GLN A CA   1 
ATOM   1693  C  C    . GLN A 1 113 ? -2.739  -3.157  22.164  1.00 13.22  ? 131 GLN A C    1 
ATOM   1694  O  O    . GLN A 1 113 ? -2.416  -3.828  21.181  1.00 14.96  ? 131 GLN A O    1 
ATOM   1695  C  CB   . GLN A 1 113 ? -3.902  -4.539  23.863  1.00 14.96  ? 131 GLN A CB   1 
ATOM   1696  C  CG   . GLN A 1 113 ? -4.117  -5.736  22.933  1.00 14.51  ? 131 GLN A CG   1 
ATOM   1697  C  CD   . GLN A 1 113 ? -5.529  -6.318  22.936  1.00 15.65  ? 131 GLN A CD   1 
ATOM   1698  O  OE1  . GLN A 1 113 ? -5.927  -6.981  21.973  1.00 16.94  ? 131 GLN A OE1  1 
ATOM   1699  N  NE2  . GLN A 1 113 ? -6.286  -6.082  24.008  1.00 16.28  ? 131 GLN A NE2  1 
ATOM   1700  H  H    . GLN A 1 113 ? -2.973  -2.771  25.229  1.00 17.20  ? 131 GLN A H    1 
ATOM   1701  H  HA   . GLN A 1 113 ? -1.859  -4.345  23.582  1.00 16.71  ? 131 GLN A HA   1 
ATOM   1702  H  HB2  . GLN A 1 113 ? -3.853  -4.875  24.772  1.00 17.95  ? 131 GLN A HB2  1 
ATOM   1703  H  HB3  . GLN A 1 113 ? -4.665  -3.948  23.768  1.00 17.95  ? 131 GLN A HB3  1 
ATOM   1704  H  HG2  . GLN A 1 113 ? -3.921  -5.457  22.025  1.00 17.41  ? 131 GLN A HG2  1 
ATOM   1705  H  HG3  . GLN A 1 113 ? -3.511  -6.444  23.200  1.00 17.41  ? 131 GLN A HG3  1 
ATOM   1706  H  HE21 . GLN A 1 113 ? -5.974  -5.618  24.661  1.00 19.53  ? 131 GLN A HE21 1 
ATOM   1707  H  HE22 . GLN A 1 113 ? -7.087  -6.394  24.046  1.00 19.53  ? 131 GLN A HE22 1 
ATOM   1708  N  N    . GLY A 1 114 ? -3.223  -1.924  22.050  1.00 13.02  ? 132 GLY A N    1 
ATOM   1709  C  CA   . GLY A 1 114 ? -3.358  -1.312  20.736  1.00 13.62  ? 132 GLY A CA   1 
ATOM   1710  C  C    . GLY A 1 114 ? -2.069  -1.308  19.937  1.00 13.64  ? 132 GLY A C    1 
ATOM   1711  O  O    . GLY A 1 114 ? -2.094  -1.424  18.708  1.00 14.21  ? 132 GLY A O    1 
ATOM   1712  H  H    . GLY A 1 114 ? -3.477  -1.429  22.706  1.00 15.63  ? 132 GLY A H    1 
ATOM   1713  H  HA2  . GLY A 1 114 ? -4.026  -1.798  20.227  1.00 16.34  ? 132 GLY A HA2  1 
ATOM   1714  H  HA3  . GLY A 1 114 ? -3.649  -0.393  20.843  1.00 16.34  ? 132 GLY A HA3  1 
ATOM   1715  N  N    . GLY A 1 115 ? -0.925  -1.205  20.617  1.00 14.01  ? 133 GLY A N    1 
ATOM   1716  C  CA   . GLY A 1 115 ? 0.343   -1.240  19.908  1.00 13.74  ? 133 GLY A CA   1 
ATOM   1717  C  C    . GLY A 1 115 ? 0.692   -2.638  19.437  1.00 13.72  ? 133 GLY A C    1 
ATOM   1718  O  O    . GLY A 1 115 ? 1.202   -2.825  18.329  1.00 13.60  ? 133 GLY A O    1 
ATOM   1719  H  H    . GLY A 1 115 ? -0.861  -1.117  21.470  1.00 16.81  ? 133 GLY A H    1 
ATOM   1720  H  HA2  . GLY A 1 115 ? 0.295   -0.658  19.134  1.00 16.49  ? 133 GLY A HA2  1 
ATOM   1721  H  HA3  . GLY A 1 115 ? 1.049   -0.928  20.495  1.00 16.49  ? 133 GLY A HA3  1 
ATOM   1722  N  N    . LEU A 1 116 ? 0.419   -3.638  20.272  1.00 13.20  ? 134 LEU A N    1 
ATOM   1723  C  CA   . LEU A 1 116 ? 0.545   -5.021  19.830  1.00 12.91  ? 134 LEU A CA   1 
ATOM   1724  C  C    . LEU A 1 116 ? -0.331  -5.283  18.609  1.00 13.17  ? 134 LEU A C    1 
ATOM   1725  O  O    . LEU A 1 116 ? 0.108   -5.920  17.642  1.00 14.34  ? 134 LEU A O    1 
ATOM   1726  C  CB   . LEU A 1 116 ? 0.170   -5.947  20.988  1.00 13.78  ? 134 LEU A CB   1 
ATOM   1727  C  CG   . LEU A 1 116 ? 0.123   -7.443  20.696  1.00 14.60  ? 134 LEU A CG   1 
ATOM   1728  C  CD1  . LEU A 1 116 ? 1.480   -7.975  20.253  1.00 15.86  ? 134 LEU A CD1  1 
ATOM   1729  C  CD2  . LEU A 1 116 ? -0.366  -8.194  21.924  1.00 15.64  ? 134 LEU A CD2  1 
ATOM   1730  H  H    . LEU A 1 116 ? 0.162   -3.544  21.087  1.00 15.84  ? 134 LEU A H    1 
ATOM   1731  H  HA   . LEU A 1 116 ? 1.463   -5.207  19.577  1.00 15.50  ? 134 LEU A HA   1 
ATOM   1732  H  HB2  . LEU A 1 116 ? 0.820   -5.818  21.695  1.00 16.54  ? 134 LEU A HB2  1 
ATOM   1733  H  HB3  . LEU A 1 116 ? -0.713  -5.692  21.298  1.00 16.54  ? 134 LEU A HB3  1 
ATOM   1734  H  HG   . LEU A 1 116 ? -0.495  -7.596  19.964  1.00 17.52  ? 134 LEU A HG   1 
ATOM   1735  H  HD11 . LEU A 1 116 ? 2.121   -7.839  20.968  1.00 19.04  ? 134 LEU A HD11 1 
ATOM   1736  H  HD12 . LEU A 1 116 ? 1.399   -8.922  20.057  1.00 19.04  ? 134 LEU A HD12 1 
ATOM   1737  H  HD13 . LEU A 1 116 ? 1.763   -7.495  19.459  1.00 19.04  ? 134 LEU A HD13 1 
ATOM   1738  H  HD21 . LEU A 1 116 ? -1.299  -7.976  22.077  1.00 18.77  ? 134 LEU A HD21 1 
ATOM   1739  H  HD22 . LEU A 1 116 ? -0.269  -9.147  21.770  1.00 18.77  ? 134 LEU A HD22 1 
ATOM   1740  H  HD23 . LEU A 1 116 ? 0.166   -7.927  22.690  1.00 18.77  ? 134 LEU A HD23 1 
ATOM   1741  N  N    . VAL A 1 117 ? -1.571  -4.790  18.636  1.00 13.12  ? 135 VAL A N    1 
ATOM   1742  C  CA   . VAL A 1 117 ? -2.482  -4.932  17.503  1.00 14.65  ? 135 VAL A CA   1 
ATOM   1743  C  C    . VAL A 1 117 ? -1.898  -4.271  16.259  1.00 14.98  ? 135 VAL A C    1 
ATOM   1744  O  O    . VAL A 1 117 ? -1.932  -4.837  15.163  1.00 16.01  ? 135 VAL A O    1 
ATOM   1745  C  CB   . VAL A 1 117 ? -3.857  -4.342  17.866  1.00 14.83  ? 135 VAL A CB   1 
ATOM   1746  C  CG1  . VAL A 1 117 ? -4.679  -4.063  16.607  1.00 16.07  ? 135 VAL A CG1  1 
ATOM   1747  C  CG2  . VAL A 1 117 ? -4.604  -5.262  18.828  1.00 17.14  ? 135 VAL A CG2  1 
ATOM   1748  H  H    . VAL A 1 117 ? -1.910  -4.366  19.303  1.00 15.74  ? 135 VAL A H    1 
ATOM   1749  H  HA   . VAL A 1 117 ? -2.592  -5.875  17.307  1.00 17.57  ? 135 VAL A HA   1 
ATOM   1750  H  HB   . VAL A 1 117 ? -3.723  -3.494  18.319  1.00 17.80  ? 135 VAL A HB   1 
ATOM   1751  H  HG11 . VAL A 1 117 ? -4.478  -4.740  15.942  1.00 19.28  ? 135 VAL A HG11 1 
ATOM   1752  H  HG12 . VAL A 1 117 ? -5.622  -4.090  16.833  1.00 19.28  ? 135 VAL A HG12 1 
ATOM   1753  H  HG13 . VAL A 1 117 ? -4.446  -3.185  16.266  1.00 19.28  ? 135 VAL A HG13 1 
ATOM   1754  H  HG21 . VAL A 1 117 ? -4.611  -6.161  18.464  1.00 20.57  ? 135 VAL A HG21 1 
ATOM   1755  H  HG22 . VAL A 1 117 ? -4.151  -5.256  19.686  1.00 20.57  ? 135 VAL A HG22 1 
ATOM   1756  H  HG23 . VAL A 1 117 ? -5.513  -4.940  18.931  1.00 20.57  ? 135 VAL A HG23 1 
ATOM   1757  N  N    . ALA A 1 118 ? -1.373  -3.049  16.405  1.00 15.30  ? 136 ALA A N    1 
ATOM   1758  C  CA   . ALA A 1 118 ? -0.805  -2.341  15.260  1.00 15.31  ? 136 ALA A CA   1 
ATOM   1759  C  C    . ALA A 1 118 ? 0.353   -3.121  14.649  1.00 15.40  ? 136 ALA A C    1 
ATOM   1760  O  O    . ALA A 1 118 ? 0.424   -3.305  13.427  1.00 15.83  ? 136 ALA A O    1 
ATOM   1761  C  CB   . ALA A 1 118 ? -0.345  -0.942  15.685  1.00 16.38  ? 136 ALA A CB   1 
ATOM   1762  H  H    . ALA A 1 118 ? -1.335  -2.615  17.147  1.00 18.36  ? 136 ALA A H    1 
ATOM   1763  H  HA   . ALA A 1 118 ? -1.493  -2.243  14.583  1.00 18.37  ? 136 ALA A HA   1 
ATOM   1764  H  HB1  . ALA A 1 118 ? -0.033  -0.461  14.902  1.00 19.65  ? 136 ALA A HB1  1 
ATOM   1765  H  HB2  . ALA A 1 118 ? -1.093  -0.472  16.085  1.00 19.65  ? 136 ALA A HB2  1 
ATOM   1766  H  HB3  . ALA A 1 118 ? 0.374   -1.028  16.329  1.00 19.65  ? 136 ALA A HB3  1 
ATOM   1767  N  N    . GLN A 1 119 ? 1.273   -3.593  15.487  1.00 14.82  ? 137 GLN A N    1 
ATOM   1768  C  CA   . GLN A 1 119 ? 2.426   -4.319  14.972  1.00 14.91  ? 137 GLN A CA   1 
ATOM   1769  C  C    . GLN A 1 119 ? 2.026   -5.681  14.419  1.00 13.71  ? 137 GLN A C    1 
ATOM   1770  O  O    . GLN A 1 119 ? 2.594   -6.132  13.419  1.00 15.21  ? 137 GLN A O    1 
ATOM   1771  C  CB   . GLN A 1 119 ? 3.474   -4.431  16.072  1.00 16.56  ? 137 GLN A CB   1 
ATOM   1772  C  CG   . GLN A 1 119 ? 4.802   -4.943  15.592  1.00 16.98  ? 137 GLN A CG   1 
ATOM   1773  C  CD   . GLN A 1 119 ? 5.554   -3.951  14.722  1.00 16.12  ? 137 GLN A CD   1 
ATOM   1774  O  OE1  . GLN A 1 119 ? 5.045   -2.883  14.359  1.00 16.92  ? 137 GLN A OE1  1 
ATOM   1775  N  NE2  . GLN A 1 119 ? 6.779   -4.305  14.381  1.00 16.89  ? 137 GLN A NE2  1 
ATOM   1776  H  H    . GLN A 1 119 ? 1.253   -3.508  16.343  1.00 17.78  ? 137 GLN A H    1 
ATOM   1777  H  HA   . GLN A 1 119 ? 2.829   -3.831  14.237  1.00 17.90  ? 137 GLN A HA   1 
ATOM   1778  H  HB2  . GLN A 1 119 ? 3.617   -3.553  16.457  1.00 19.87  ? 137 GLN A HB2  1 
ATOM   1779  H  HB3  . GLN A 1 119 ? 3.149   -5.043  16.751  1.00 19.87  ? 137 GLN A HB3  1 
ATOM   1780  H  HG2  . GLN A 1 119 ? 5.358   -5.143  16.361  1.00 20.38  ? 137 GLN A HG2  1 
ATOM   1781  H  HG3  . GLN A 1 119 ? 4.658   -5.747  15.069  1.00 20.38  ? 137 GLN A HG3  1 
ATOM   1782  H  HE21 . GLN A 1 119 ? 7.101   -5.056  14.650  1.00 20.27  ? 137 GLN A HE21 1 
ATOM   1783  H  HE22 . GLN A 1 119 ? 7.256   -3.785  13.889  1.00 20.27  ? 137 GLN A HE22 1 
ATOM   1784  N  N    . TRP A 1 120 ? 1.037   -6.337  15.027  1.00 14.63  ? 138 TRP A N    1 
ATOM   1785  C  CA   . TRP A 1 120 ? 0.524   -7.577  14.456  1.00 14.91  ? 138 TRP A CA   1 
ATOM   1786  C  C    . TRP A 1 120 ? -0.051  -7.336  13.068  1.00 14.62  ? 138 TRP A C    1 
ATOM   1787  O  O    . TRP A 1 120 ? 0.195   -8.117  12.140  1.00 16.05  ? 138 TRP A O    1 
ATOM   1788  C  CB   . TRP A 1 120 ? -0.534  -8.170  15.386  1.00 15.76  ? 138 TRP A CB   1 
ATOM   1789  C  CG   . TRP A 1 120 ? -1.047  -9.522  14.983  1.00 14.39  ? 138 TRP A CG   1 
ATOM   1790  C  CD1  . TRP A 1 120 ? -2.133  -9.784  14.203  1.00 15.60  ? 138 TRP A CD1  1 
ATOM   1791  C  CD2  . TRP A 1 120 ? -0.513  -10.797 15.364  1.00 13.85  ? 138 TRP A CD2  1 
ATOM   1792  N  NE1  . TRP A 1 120 ? -2.303  -11.140 14.059  1.00 14.73  ? 138 TRP A NE1  1 
ATOM   1793  C  CE2  . TRP A 1 120 ? -1.322  -11.785 14.766  1.00 14.49  ? 138 TRP A CE2  1 
ATOM   1794  C  CE3  . TRP A 1 120 ? 0.575   -11.197 16.140  1.00 14.57  ? 138 TRP A CE3  1 
ATOM   1795  C  CZ2  . TRP A 1 120 ? -1.075  -13.146 14.916  1.00 15.27  ? 138 TRP A CZ2  1 
ATOM   1796  C  CZ3  . TRP A 1 120 ? 0.811   -12.549 16.301  1.00 15.65  ? 138 TRP A CZ3  1 
ATOM   1797  C  CH2  . TRP A 1 120 ? -0.015  -13.509 15.693  1.00 15.33  ? 138 TRP A CH2  1 
ATOM   1798  H  H    . TRP A 1 120 ? 0.654   -6.089  15.756  1.00 17.55  ? 138 TRP A H    1 
ATOM   1799  H  HA   . TRP A 1 120 ? 1.246   -8.219  14.374  1.00 17.90  ? 138 TRP A HA   1 
ATOM   1800  H  HB2  . TRP A 1 120 ? -0.150  -8.257  16.273  1.00 18.91  ? 138 TRP A HB2  1 
ATOM   1801  H  HB3  . TRP A 1 120 ? -1.294  -7.567  15.412  1.00 18.91  ? 138 TRP A HB3  1 
ATOM   1802  H  HD1  . TRP A 1 120 ? -2.682  -9.137  13.821  1.00 18.73  ? 138 TRP A HD1  1 
ATOM   1803  H  HE1  . TRP A 1 120 ? -2.923  -11.521 13.600  1.00 17.67  ? 138 TRP A HE1  1 
ATOM   1804  H  HE3  . TRP A 1 120 ? 1.130   -10.567 16.540  1.00 17.48  ? 138 TRP A HE3  1 
ATOM   1805  H  HZ2  . TRP A 1 120 ? -1.612  -13.783 14.503  1.00 18.32  ? 138 TRP A HZ2  1 
ATOM   1806  H  HZ3  . TRP A 1 120 ? 1.529   -12.829 16.821  1.00 18.78  ? 138 TRP A HZ3  1 
ATOM   1807  H  HH2  . TRP A 1 120 ? 0.165   -14.412 15.823  1.00 18.40  ? 138 TRP A HH2  1 
ATOM   1808  N  N    . GLY A 1 121 ? -0.803  -6.249  12.901  1.00 15.08  ? 139 GLY A N    1 
ATOM   1809  C  CA   . GLY A 1 121 ? -1.353  -5.940  11.592  1.00 16.56  ? 139 GLY A CA   1 
ATOM   1810  C  C    . GLY A 1 121 ? -0.280  -5.642  10.564  1.00 16.44  ? 139 GLY A C    1 
ATOM   1811  O  O    . GLY A 1 121 ? -0.339  -6.127  9.433   1.00 16.45  ? 139 GLY A O    1 
ATOM   1812  H  H    . GLY A 1 121 ? -1.004  -5.686  13.519  1.00 18.10  ? 139 GLY A H    1 
ATOM   1813  H  HA2  . GLY A 1 121 ? -1.875  -6.695  11.278  1.00 19.87  ? 139 GLY A HA2  1 
ATOM   1814  H  HA3  . GLY A 1 121 ? -1.931  -5.165  11.663  1.00 19.87  ? 139 GLY A HA3  1 
ATOM   1815  N  N    . LEU A 1 122 ? 0.717   -4.839  10.940  1.00 15.83  ? 140 LEU A N    1 
ATOM   1816  C  CA   . LEU A 1 122 ? 1.789   -4.534  9.999   1.00 16.22  ? 140 LEU A CA   1 
ATOM   1817  C  C    . LEU A 1 122 ? 2.596   -5.780  9.653   1.00 15.99  ? 140 LEU A C    1 
ATOM   1818  O  O    . LEU A 1 122 ? 3.108   -5.893  8.534   1.00 17.68  ? 140 LEU A O    1 
ATOM   1819  C  CB   . LEU A 1 122 ? 2.701   -3.446  10.567  1.00 16.77  ? 140 LEU A CB   1 
ATOM   1820  C  CG   . LEU A 1 122 ? 2.065   -2.063  10.719  1.00 17.68  ? 140 LEU A CG   1 
ATOM   1821  C  CD1  . LEU A 1 122 ? 2.871   -1.179  11.677  1.00 18.49  ? 140 LEU A CD1  1 
ATOM   1822  C  CD2  . LEU A 1 122 ? 1.928   -1.387  9.358   1.00 18.92  ? 140 LEU A CD2  1 
ATOM   1823  H  H    . LEU A 1 122 ? 0.792   -4.468  11.712  1.00 19.00  ? 140 LEU A H    1 
ATOM   1824  H  HA   . LEU A 1 122 ? 1.398   -4.190  9.181   1.00 19.46  ? 140 LEU A HA   1 
ATOM   1825  H  HB2  . LEU A 1 122 ? 2.997   -3.726  11.447  1.00 20.13  ? 140 LEU A HB2  1 
ATOM   1826  H  HB3  . LEU A 1 122 ? 3.464   -3.349  9.976   1.00 20.13  ? 140 LEU A HB3  1 
ATOM   1827  H  HG   . LEU A 1 122 ? 1.179   -2.173  11.099  1.00 21.22  ? 140 LEU A HG   1 
ATOM   1828  H  HD11 . LEU A 1 122 ? 2.898   -1.602  12.549  1.00 22.19  ? 140 LEU A HD11 1 
ATOM   1829  H  HD12 . LEU A 1 122 ? 3.771   -1.077  11.330  1.00 22.19  ? 140 LEU A HD12 1 
ATOM   1830  H  HD13 . LEU A 1 122 ? 2.442   -0.311  11.742  1.00 22.19  ? 140 LEU A HD13 1 
ATOM   1831  H  HD21 . LEU A 1 122 ? 1.458   -0.546  9.468   1.00 22.70  ? 140 LEU A HD21 1 
ATOM   1832  H  HD22 . LEU A 1 122 ? 2.813   -1.226  8.995   1.00 22.70  ? 140 LEU A HD22 1 
ATOM   1833  H  HD23 . LEU A 1 122 ? 1.429   -1.970  8.765   1.00 22.70  ? 140 LEU A HD23 1 
ATOM   1834  N  N    . THR A 1 123 ? 2.706   -6.728  10.585  1.00 16.06  ? 141 THR A N    1 
ATOM   1835  C  CA   . THR A 1 123 ? 3.475   -7.941  10.318  1.00 15.88  ? 141 THR A CA   1 
ATOM   1836  C  C    . THR A 1 123 ? 2.752   -8.861  9.337   1.00 16.30  ? 141 THR A C    1 
ATOM   1837  O  O    . THR A 1 123 ? 3.366   -9.375  8.396   1.00 17.40  ? 141 THR A O    1 
ATOM   1838  C  CB   . THR A 1 123 ? 3.781   -8.662  11.634  1.00 16.29  ? 141 THR A CB   1 
ATOM   1839  O  OG1  . THR A 1 123 ? 4.625   -7.836  12.455  1.00 16.46  ? 141 THR A OG1  1 
ATOM   1840  C  CG2  . THR A 1 123 ? 4.480   -9.988  11.381  1.00 17.31  ? 141 THR A CG2  1 
ATOM   1841  H  H    . THR A 1 123 ? 2.351   -6.693  11.368  1.00 19.27  ? 141 THR A H    1 
ATOM   1842  H  HA   . THR A 1 123 ? 4.320   -7.695  9.910   1.00 19.06  ? 141 THR A HA   1 
ATOM   1843  H  HB   . THR A 1 123 ? 2.948   -8.840  12.097  1.00 19.55  ? 141 THR A HB   1 
ATOM   1844  H  HG1  . THR A 1 123 ? 4.192   -7.173  12.737  1.00 19.76  ? 141 THR A HG1  1 
ATOM   1845  H  HG21 . THR A 1 123 ? 3.853   -10.627 11.006  1.00 20.78  ? 141 THR A HG21 1 
ATOM   1846  H  HG22 . THR A 1 123 ? 5.213   -9.863  10.758  1.00 20.78  ? 141 THR A HG22 1 
ATOM   1847  H  HG23 . THR A 1 123 ? 4.830   -10.343 12.213  1.00 20.78  ? 141 THR A HG23 1 
ATOM   1848  N  N    . PHE A 1 124 ? 1.444   -9.056  9.512   1.00 15.74  ? 142 PHE A N    1 
ATOM   1849  C  CA   . PHE A 1 124 ? 0.736   -10.121 8.811   1.00 16.25  ? 142 PHE A CA   1 
ATOM   1850  C  C    . PHE A 1 124 ? -0.201  -9.641  7.710   1.00 17.53  ? 142 PHE A C    1 
ATOM   1851  O  O    . PHE A 1 124 ? -0.747  -10.483 6.982   1.00 18.31  ? 142 PHE A O    1 
ATOM   1852  C  CB   . PHE A 1 124 ? -0.036  -10.981 9.821   1.00 16.41  ? 142 PHE A CB   1 
ATOM   1853  C  CG   . PHE A 1 124 ? 0.858   -11.776 10.735  1.00 16.14  ? 142 PHE A CG   1 
ATOM   1854  C  CD1  . PHE A 1 124 ? 1.593   -12.839 10.236  1.00 16.84  ? 142 PHE A CD1  1 
ATOM   1855  C  CD2  . PHE A 1 124 ? 0.969   -11.461 12.083  1.00 15.90  ? 142 PHE A CD2  1 
ATOM   1856  C  CE1  . PHE A 1 124 ? 2.436   -13.571 11.057  1.00 16.78  ? 142 PHE A CE1  1 
ATOM   1857  C  CE2  . PHE A 1 124 ? 1.811   -12.200 12.917  1.00 16.30  ? 142 PHE A CE2  1 
ATOM   1858  C  CZ   . PHE A 1 124 ? 2.531   -13.261 12.401  1.00 17.11  ? 142 PHE A CZ   1 
ATOM   1859  H  H    . PHE A 1 124 ? 0.948   -8.584  10.032  1.00 18.88  ? 142 PHE A H    1 
ATOM   1860  H  HA   . PHE A 1 124 ? 1.391   -10.688 8.374   1.00 19.50  ? 142 PHE A HA   1 
ATOM   1861  H  HB2  . PHE A 1 124 ? -0.585  -10.401 10.372  1.00 19.69  ? 142 PHE A HB2  1 
ATOM   1862  H  HB3  . PHE A 1 124 ? -0.597  -11.606 9.336   1.00 19.69  ? 142 PHE A HB3  1 
ATOM   1863  H  HD1  . PHE A 1 124 ? 1.520   -13.065 9.337   1.00 20.21  ? 142 PHE A HD1  1 
ATOM   1864  H  HD2  . PHE A 1 124 ? 0.480   -10.752 12.433  1.00 19.08  ? 142 PHE A HD2  1 
ATOM   1865  H  HE1  . PHE A 1 124 ? 2.937   -14.271 10.704  1.00 20.14  ? 142 PHE A HE1  1 
ATOM   1866  H  HE2  . PHE A 1 124 ? 1.887   -11.980 13.818  1.00 19.56  ? 142 PHE A HE2  1 
ATOM   1867  H  HZ   . PHE A 1 124 ? 3.080   -13.766 12.957  1.00 20.54  ? 142 PHE A HZ   1 
ATOM   1868  N  N    . PHE A 1 125 ? -0.383  -8.329  7.548   1.00 18.38  ? 143 PHE A N    1 
ATOM   1869  C  CA   . PHE A 1 125 ? -1.270  -7.754  6.534   1.00 17.75  ? 143 PHE A CA   1 
ATOM   1870  C  C    . PHE A 1 125 ? -0.462  -6.750  5.721   1.00 18.50  ? 143 PHE A C    1 
ATOM   1871  O  O    . PHE A 1 125 ? -0.519  -5.537  5.969   1.00 18.05  ? 143 PHE A O    1 
ATOM   1872  C  CB   . PHE A 1 125 ? -2.493  -7.098  7.180   1.00 18.07  ? 143 PHE A CB   1 
ATOM   1873  C  CG   . PHE A 1 125 ? -3.443  -8.085  7.793   1.00 18.70  ? 143 PHE A CG   1 
ATOM   1874  C  CD1  . PHE A 1 125 ? -3.179  -8.641  9.036   1.00 18.89  ? 143 PHE A CD1  1 
ATOM   1875  C  CD2  . PHE A 1 125 ? -4.592  -8.470  7.123   1.00 19.91  ? 143 PHE A CD2  1 
ATOM   1876  C  CE1  . PHE A 1 125 ? -4.043  -9.563  9.597   1.00 19.58  ? 143 PHE A CE1  1 
ATOM   1877  C  CE2  . PHE A 1 125 ? -5.458  -9.399  7.683   1.00 20.54  ? 143 PHE A CE2  1 
ATOM   1878  C  CZ   . PHE A 1 125 ? -5.184  -9.941  8.919   1.00 20.50  ? 143 PHE A CZ   1 
ATOM   1879  H  H    . PHE A 1 125 ? 0.009   -7.734  8.030   1.00 22.06  ? 143 PHE A H    1 
ATOM   1880  H  HA   . PHE A 1 125 ? -1.582  -8.452  5.937   1.00 21.31  ? 143 PHE A HA   1 
ATOM   1881  H  HB2  . PHE A 1 125 ? -2.193  -6.499  7.881   1.00 21.69  ? 143 PHE A HB2  1 
ATOM   1882  H  HB3  . PHE A 1 125 ? -2.976  -6.600  6.502   1.00 21.69  ? 143 PHE A HB3  1 
ATOM   1883  H  HD1  . PHE A 1 125 ? -2.412  -8.391  9.498   1.00 22.67  ? 143 PHE A HD1  1 
ATOM   1884  H  HD2  . PHE A 1 125 ? -4.786  -8.103  6.291   1.00 23.89  ? 143 PHE A HD2  1 
ATOM   1885  H  HE1  . PHE A 1 125 ? -3.855  -9.929  10.431  1.00 23.50  ? 143 PHE A HE1  1 
ATOM   1886  H  HE2  . PHE A 1 125 ? -6.224  -9.657  7.223   1.00 24.65  ? 143 PHE A HE2  1 
ATOM   1887  H  HZ   . PHE A 1 125 ? -5.767  -10.559 9.296   1.00 24.60  ? 143 PHE A HZ   1 
ATOM   1888  N  N    . PRO A 1 126 ? 0.297   -7.222  4.731   1.00 19.10  ? 144 PRO A N    1 
ATOM   1889  C  CA   . PRO A 1 126 ? 1.245   -6.325  4.046   1.00 19.22  ? 144 PRO A CA   1 
ATOM   1890  C  C    . PRO A 1 126 ? 0.621   -5.110  3.379   1.00 19.54  ? 144 PRO A C    1 
ATOM   1891  O  O    . PRO A 1 126 ? 1.329   -4.113  3.180   1.00 20.51  ? 144 PRO A O    1 
ATOM   1892  C  CB   . PRO A 1 126 ? 1.926   -7.239  3.019   1.00 19.67  ? 144 PRO A CB   1 
ATOM   1893  C  CG   . PRO A 1 126 ? 1.786   -8.609  3.593   1.00 19.69  ? 144 PRO A CG   1 
ATOM   1894  C  CD   . PRO A 1 126 ? 0.459   -8.624  4.310   1.00 19.86  ? 144 PRO A CD   1 
ATOM   1895  H  HA   . PRO A 1 126 ? 1.899   -6.014  4.691   1.00 23.07  ? 144 PRO A HA   1 
ATOM   1896  H  HB2  . PRO A 1 126 ? 1.476   -7.171  2.162   1.00 23.60  ? 144 PRO A HB2  1 
ATOM   1897  H  HB3  . PRO A 1 126 ? 2.860   -6.994  2.923   1.00 23.60  ? 144 PRO A HB3  1 
ATOM   1898  H  HG2  . PRO A 1 126 ? 1.797   -9.265  2.879   1.00 23.63  ? 144 PRO A HG2  1 
ATOM   1899  H  HG3  . PRO A 1 126 ? 2.512   -8.779  4.213   1.00 23.63  ? 144 PRO A HG3  1 
ATOM   1900  H  HD2  . PRO A 1 126 ? -0.255  -8.892  3.711   1.00 23.83  ? 144 PRO A HD2  1 
ATOM   1901  H  HD3  . PRO A 1 126 ? 0.487   -9.216  5.078   1.00 23.83  ? 144 PRO A HD3  1 
ATOM   1902  N  N    . SER A 1 127 ? -0.667  -5.146  3.029   1.00 19.31  ? 145 SER A N    1 
ATOM   1903  C  CA   . SER A 1 127 ? -1.244  -4.041  2.270   1.00 19.49  ? 145 SER A CA   1 
ATOM   1904  C  C    . SER A 1 127 ? -1.198  -2.731  3.042   1.00 20.15  ? 145 SER A C    1 
ATOM   1905  O  O    . SER A 1 127 ? -1.177  -1.655  2.432   1.00 21.38  ? 145 SER A O    1 
ATOM   1906  C  CB   . SER A 1 127 ? -2.692  -4.351  1.893   1.00 20.81  ? 145 SER A CB   1 
ATOM   1907  O  OG   . SER A 1 127 ? -3.530  -4.311  3.038   1.00 21.70  ? 145 SER A OG   1 
ATOM   1908  H  H    . SER A 1 127 ? -1.214  -5.784  3.215   1.00 23.17  ? 145 SER A H    1 
ATOM   1909  H  HA   . SER A 1 127 ? -0.725  -3.938  1.457   1.00 23.39  ? 145 SER A HA   1 
ATOM   1910  H  HB2  . SER A 1 127 ? -3.001  -3.691  1.253   1.00 24.98  ? 145 SER A HB2  1 
ATOM   1911  H  HB3  . SER A 1 127 ? -2.734  -5.238  1.502   1.00 24.98  ? 145 SER A HB3  1 
ATOM   1912  H  HG   . SER A 1 127 ? -4.312  -4.538  2.830   1.00 26.04  ? 145 SER A HG   1 
ATOM   1913  N  N    . ILE A 1 128 ? -1.204  -2.788  4.375   1.00 20.23  ? 146 ILE A N    1 
ATOM   1914  C  CA   . ILE A 1 128 ? -1.285  -1.551  5.153   1.00 19.28  ? 146 ILE A CA   1 
ATOM   1915  C  C    . ILE A 1 128 ? 0.066   -0.890  5.375   1.00 18.49  ? 146 ILE A C    1 
ATOM   1916  O  O    . ILE A 1 128 ? 0.116   0.252   5.846   1.00 19.17  ? 146 ILE A O    1 
ATOM   1917  C  CB   . ILE A 1 128 ? -2.031  -1.737  6.489   1.00 19.20  ? 146 ILE A CB   1 
ATOM   1918  C  CG1  . ILE A 1 128 ? -1.341  -2.774  7.384   1.00 19.90  ? 146 ILE A CG1  1 
ATOM   1919  C  CG2  . ILE A 1 128 ? -3.474  -2.147  6.224   1.00 19.85  ? 146 ILE A CG2  1 
ATOM   1920  C  CD1  . ILE A 1 128 ? -1.677  -2.599  8.854   1.00 19.69  ? 146 ILE A CD1  1 
ATOM   1921  H  H    . ILE A 1 128 ? -1.163  -3.511  4.841   1.00 24.27  ? 146 ILE A H    1 
ATOM   1922  H  HA   . ILE A 1 128 ? -1.819  -0.929  4.633   1.00 23.13  ? 146 ILE A HA   1 
ATOM   1923  H  HB   . ILE A 1 128 ? -2.014  -0.888  6.958   1.00 23.04  ? 146 ILE A HB   1 
ATOM   1924  H  HG12 . ILE A 1 128 ? -1.625  -3.662  7.114   1.00 23.87  ? 146 ILE A HG12 1 
ATOM   1925  H  HG13 . ILE A 1 128 ? -0.380  -2.689  7.283   1.00 23.87  ? 146 ILE A HG13 1 
ATOM   1926  H  HG21 . ILE A 1 128 ? -3.481  -3.004  5.769   1.00 23.82  ? 146 ILE A HG21 1 
ATOM   1927  H  HG22 . ILE A 1 128 ? -3.942  -2.219  7.071   1.00 23.82  ? 146 ILE A HG22 1 
ATOM   1928  H  HG23 . ILE A 1 128 ? -3.897  -1.474  5.669   1.00 23.82  ? 146 ILE A HG23 1 
ATOM   1929  H  HD11 . ILE A 1 128 ? -1.252  -3.307  9.362   1.00 23.62  ? 146 ILE A HD11 1 
ATOM   1930  H  HD12 . ILE A 1 128 ? -1.351  -1.736  9.152   1.00 23.62  ? 146 ILE A HD12 1 
ATOM   1931  H  HD13 . ILE A 1 128 ? -2.640  -2.645  8.965   1.00 23.62  ? 146 ILE A HD13 1 
ATOM   1932  N  N    . ARG A 1 129 ? 1.166   -1.563  5.038   1.00 19.42  ? 147 ARG A N    1 
ATOM   1933  C  CA   . ARG A 1 129 ? 2.481   -0.991  5.304   1.00 20.44  ? 147 ARG A CA   1 
ATOM   1934  C  C    . ARG A 1 129 ? 2.705   0.298   4.523   1.00 22.44  ? 147 ARG A C    1 
ATOM   1935  O  O    . ARG A 1 129 ? 3.397   1.203   5.005   1.00 24.55  ? 147 ARG A O    1 
ATOM   1936  C  CB   . ARG A 1 129 ? 3.564   -2.012  4.968   1.00 19.90  ? 147 ARG A CB   1 
ATOM   1937  C  CG   . ARG A 1 129 ? 3.539   -3.245  5.851   1.00 19.57  ? 147 ARG A CG   1 
ATOM   1938  C  CD   . ARG A 1 129 ? 4.489   -4.298  5.333   1.00 18.60  ? 147 ARG A CD   1 
ATOM   1939  N  NE   . ARG A 1 129 ? 4.306   -5.562  6.030   1.00 17.58  ? 147 ARG A NE   1 
ATOM   1940  C  CZ   . ARG A 1 129 ? 4.736   -6.735  5.578   1.00 18.38  ? 147 ARG A CZ   1 
ATOM   1941  N  NH1  . ARG A 1 129 ? 5.380   -6.805  4.420   1.00 20.56  ? 147 ARG A NH1  1 
ATOM   1942  N  NH2  . ARG A 1 129 ? 4.516   -7.839  6.284   1.00 18.71  ? 147 ARG A NH2  1 
ATOM   1943  H  H    . ARG A 1 129 ? 1.177   -2.337  4.661   1.00 23.30  ? 147 ARG A H    1 
ATOM   1944  H  HA   . ARG A 1 129 ? 2.546   -0.778  6.248   1.00 24.52  ? 147 ARG A HA   1 
ATOM   1945  H  HB2  . ARG A 1 129 ? 3.444   -2.303  4.051   1.00 23.88  ? 147 ARG A HB2  1 
ATOM   1946  H  HB3  . ARG A 1 129 ? 4.432   -1.592  5.072   1.00 23.88  ? 147 ARG A HB3  1 
ATOM   1947  H  HG2  . ARG A 1 129 ? 3.809   -3.004  6.751   1.00 23.49  ? 147 ARG A HG2  1 
ATOM   1948  H  HG3  . ARG A 1 129 ? 2.643   -3.617  5.862   1.00 23.49  ? 147 ARG A HG3  1 
ATOM   1949  H  HD2  . ARG A 1 129 ? 4.325   -4.443  4.388   1.00 22.33  ? 147 ARG A HD2  1 
ATOM   1950  H  HD3  . ARG A 1 129 ? 5.403   -4.003  5.469   1.00 22.33  ? 147 ARG A HD3  1 
ATOM   1951  H  HE   . ARG A 1 129 ? 3.892   -5.549  6.784   1.00 21.09  ? 147 ARG A HE   1 
ATOM   1952  H  HH11 . ARG A 1 129 ? 5.518   -6.090  3.961   1.00 24.67  ? 147 ARG A HH11 1 
ATOM   1953  H  HH12 . ARG A 1 129 ? 5.658   -7.564  4.127   1.00 24.67  ? 147 ARG A HH12 1 
ATOM   1954  H  HH21 . ARG A 1 129 ? 4.095   -7.794  7.032   1.00 22.46  ? 147 ARG A HH21 1 
ATOM   1955  H  HH22 . ARG A 1 129 ? 4.795   -8.599  5.992   1.00 22.46  ? 147 ARG A HH22 1 
ATOM   1956  N  N    . SER A 1 130 ? 2.124   0.403   3.331   1.00 22.81  ? 148 SER A N    1 
ATOM   1957  C  CA   . SER A 1 130 ? 2.245   1.591   2.497   1.00 23.52  ? 148 SER A CA   1 
ATOM   1958  C  C    . SER A 1 130 ? 1.185   2.639   2.807   1.00 22.60  ? 148 SER A C    1 
ATOM   1959  O  O    . SER A 1 130 ? 1.131   3.669   2.126   1.00 24.95  ? 148 SER A O    1 
ATOM   1960  C  CB   . SER A 1 130 ? 2.143   1.202   1.019   1.00 25.15  ? 148 SER A CB   1 
ATOM   1961  O  OG   . SER A 1 130 ? 0.873   0.640   0.741   1.00 26.65  ? 148 SER A OG   1 
ATOM   1962  H  H    . SER A 1 130 ? 1.642   -0.215  2.977   1.00 27.38  ? 148 SER A H    1 
ATOM   1963  H  HA   . SER A 1 130 ? 3.117   1.989   2.649   1.00 28.23  ? 148 SER A HA   1 
ATOM   1964  H  HB2  . SER A 1 130 ? 2.266   1.994   0.473   1.00 30.18  ? 148 SER A HB2  1 
ATOM   1965  H  HB3  . SER A 1 130 ? 2.830   0.548   0.815   1.00 30.18  ? 148 SER A HB3  1 
ATOM   1966  H  HG   . SER A 1 130 ? 0.764   -0.061  1.191   1.00 31.98  ? 148 SER A HG   1 
ATOM   1967  N  N    . LYS A 1 131 ? 0.353   2.410   3.820   1.00 19.33  ? 149 LYS A N    1 
ATOM   1968  C  CA   . LYS A 1 131 ? -0.734  3.314   4.159   1.00 18.69  ? 149 LYS A CA   1 
ATOM   1969  C  C    . LYS A 1 131 ? -0.576  3.954   5.527   1.00 18.80  ? 149 LYS A C    1 
ATOM   1970  O  O    . LYS A 1 131 ? -1.337  4.871   5.851   1.00 20.77  ? 149 LYS A O    1 
ATOM   1971  C  CB   . LYS A 1 131 ? -2.071  2.560   4.083   1.00 18.74  ? 149 LYS A CB   1 
ATOM   1972  C  CG   . LYS A 1 131 ? -2.279  1.936   2.707   1.00 19.57  ? 149 LYS A CG   1 
ATOM   1973  C  CD   . LYS A 1 131 ? -3.580  1.180   2.566   1.00 20.36  ? 149 LYS A CD   1 
ATOM   1974  C  CE   . LYS A 1 131 ? -3.690  0.621   1.143   1.00 21.94  ? 149 LYS A CE   1 
ATOM   1975  N  NZ   . LYS A 1 131 ? -4.930  -0.155  0.885   1.00 23.71  ? 149 LYS A NZ   1 
ATOM   1976  H  H    . LYS A 1 131 ? 0.402   1.722   4.335   1.00 23.20  ? 149 LYS A H    1 
ATOM   1977  H  HA   . LYS A 1 131 ? -0.773  4.037   3.513   1.00 22.42  ? 149 LYS A HA   1 
ATOM   1978  H  HB2  . LYS A 1 131 ? -2.078  1.851   4.745   1.00 22.49  ? 149 LYS A HB2  1 
ATOM   1979  H  HB3  . LYS A 1 131 ? -2.799  3.179   4.252   1.00 22.49  ? 149 LYS A HB3  1 
ATOM   1980  H  HG2  . LYS A 1 131 ? -2.275  2.642   2.041   1.00 23.48  ? 149 LYS A HG2  1 
ATOM   1981  H  HG3  . LYS A 1 131 ? -1.556  1.313   2.535   1.00 23.48  ? 149 LYS A HG3  1 
ATOM   1982  H  HD2  . LYS A 1 131 ? -3.603  0.442   3.196   1.00 24.43  ? 149 LYS A HD2  1 
ATOM   1983  H  HD3  . LYS A 1 131 ? -4.328  1.777   2.727   1.00 24.43  ? 149 LYS A HD3  1 
ATOM   1984  H  HE2  . LYS A 1 131 ? -3.671  1.361   0.516   1.00 26.32  ? 149 LYS A HE2  1 
ATOM   1985  H  HE3  . LYS A 1 131 ? -2.936  0.031   0.982   1.00 26.32  ? 149 LYS A HE3  1 
ATOM   1986  H  HZ1  . LYS A 1 131 ? -4.898  -0.518  0.073   1.00 28.45  ? 149 LYS A HZ1  1 
ATOM   1987  H  HZ2  . LYS A 1 131 ? -5.014  -0.804  1.488   1.00 28.45  ? 149 LYS A HZ2  1 
ATOM   1988  H  HZ3  . LYS A 1 131 ? -5.639  0.380   0.935   1.00 28.45  ? 149 LYS A HZ3  1 
ATOM   1989  N  N    . VAL A 1 132 ? 0.395   3.516   6.321   1.00 19.00  ? 150 VAL A N    1 
ATOM   1990  C  CA   . VAL A 1 132 ? 0.672   4.054   7.648   1.00 18.57  ? 150 VAL A CA   1 
ATOM   1991  C  C    . VAL A 1 132 ? 2.006   4.783   7.559   1.00 19.28  ? 150 VAL A C    1 
ATOM   1992  O  O    . VAL A 1 132 ? 3.020   4.179   7.203   1.00 20.90  ? 150 VAL A O    1 
ATOM   1993  C  CB   . VAL A 1 132 ? 0.729   2.924   8.687   1.00 17.48  ? 150 VAL A CB   1 
ATOM   1994  C  CG1  . VAL A 1 132 ? 1.185   3.448   10.032  1.00 18.80  ? 150 VAL A CG1  1 
ATOM   1995  C  CG2  . VAL A 1 132 ? -0.630  2.236   8.796   1.00 18.56  ? 150 VAL A CG2  1 
ATOM   1996  H  H    . VAL A 1 132 ? 0.930   2.879   6.103   1.00 22.80  ? 150 VAL A H    1 
ATOM   1997  H  HA   . VAL A 1 132 ? -0.013  4.688   7.912   1.00 22.28  ? 150 VAL A HA   1 
ATOM   1998  H  HB   . VAL A 1 132 ? 1.378   2.264   8.397   1.00 20.97  ? 150 VAL A HB   1 
ATOM   1999  H  HG11 . VAL A 1 132 ? 0.986   2.786   10.713  1.00 22.56  ? 150 VAL A HG11 1 
ATOM   2000  H  HG12 . VAL A 1 132 ? 2.140   3.613   9.999   1.00 22.56  ? 150 VAL A HG12 1 
ATOM   2001  H  HG13 . VAL A 1 132 ? 0.713   4.273   10.226  1.00 22.56  ? 150 VAL A HG13 1 
ATOM   2002  H  HG21 . VAL A 1 132 ? -0.549  1.469   9.384   1.00 22.27  ? 150 VAL A HG21 1 
ATOM   2003  H  HG22 . VAL A 1 132 ? -1.274  2.864   9.157   1.00 22.27  ? 150 VAL A HG22 1 
ATOM   2004  H  HG23 . VAL A 1 132 ? -0.909  1.947   7.913   1.00 22.27  ? 150 VAL A HG23 1 
ATOM   2005  N  N    . ASP A 1 133 ? 2.017   6.083   7.846   1.00 19.24  ? 151 ASP A N    1 
ATOM   2006  C  CA   . ASP A 1 133 ? 3.282   6.806   7.754   1.00 20.11  ? 151 ASP A CA   1 
ATOM   2007  C  C    . ASP A 1 133 ? 4.118   6.702   9.020   1.00 18.87  ? 151 ASP A C    1 
ATOM   2008  O  O    . ASP A 1 133 ? 5.338   6.890   8.953   1.00 19.79  ? 151 ASP A O    1 
ATOM   2009  C  CB   . ASP A 1 133 ? 3.101   8.257   7.275   1.00 22.05  ? 151 ASP A CB   1 
ATOM   2010  C  CG   . ASP A 1 133 ? 2.536   9.191   8.326   1.00 22.69  ? 151 ASP A CG   1 
ATOM   2011  O  OD1  . ASP A 1 133 ? 2.652   10.422  8.104   1.00 23.37  ? 151 ASP A OD1  1 
ATOM   2012  O  OD2  . ASP A 1 133 ? 1.959   8.733   9.336   1.00 23.06  ? 151 ASP A OD2  1 
ATOM   2013  H  H    . ASP A 1 133 ? 1.334   6.549   8.085   1.00 23.09  ? 151 ASP A H    1 
ATOM   2014  H  HA   . ASP A 1 133 ? 3.813   6.406   7.048   1.00 24.13  ? 151 ASP A HA   1 
ATOM   2015  H  HB2  . ASP A 1 133 ? 3.965   8.605   7.006   1.00 26.46  ? 151 ASP A HB2  1 
ATOM   2016  H  HB3  . ASP A 1 133 ? 2.492   8.261   6.520   1.00 26.46  ? 151 ASP A HB3  1 
ATOM   2017  N  N    . ARG A 1 134 ? 3.506   6.355   10.148  1.00 17.37  ? 152 ARG A N    1 
ATOM   2018  C  CA   . ARG A 1 134 ? 4.232   6.262   11.405  1.00 16.05  ? 152 ARG A CA   1 
ATOM   2019  C  C    . ARG A 1 134 ? 3.333   5.615   12.443  1.00 15.95  ? 152 ARG A C    1 
ATOM   2020  O  O    . ARG A 1 134 ? 2.104   5.635   12.331  1.00 16.62  ? 152 ARG A O    1 
ATOM   2021  C  CB   . ARG A 1 134 ? 4.672   7.637   11.903  1.00 16.28  ? 152 ARG A CB   1 
ATOM   2022  C  CG   . ARG A 1 134 ? 3.541   8.482   12.483  1.00 17.17  ? 152 ARG A CG   1 
ATOM   2023  C  CD   . ARG A 1 134 ? 3.914   9.959   12.479  1.00 17.92  ? 152 ARG A CD   1 
ATOM   2024  N  NE   . ARG A 1 134 ? 4.014   10.456  11.110  1.00 18.63  ? 152 ARG A NE   1 
ATOM   2025  C  CZ   . ARG A 1 134 ? 4.849   11.409  10.709  1.00 19.49  ? 152 ARG A CZ   1 
ATOM   2026  N  NH1  . ARG A 1 134 ? 5.670   11.998  11.569  1.00 18.80  ? 152 ARG A NH1  1 
ATOM   2027  N  NH2  . ARG A 1 134 ? 4.858   11.771  9.435   1.00 21.36  ? 152 ARG A NH2  1 
ATOM   2028  H  H    . ARG A 1 134 ? 2.669   6.169   10.210  1.00 20.84  ? 152 ARG A H    1 
ATOM   2029  H  HA   . ARG A 1 134 ? 5.014   5.703   11.273  1.00 19.26  ? 152 ARG A HA   1 
ATOM   2030  H  HB2  . ARG A 1 134 ? 5.337   7.517   12.599  1.00 19.54  ? 152 ARG A HB2  1 
ATOM   2031  H  HB3  . ARG A 1 134 ? 5.055   8.129   11.160  1.00 19.54  ? 152 ARG A HB3  1 
ATOM   2032  H  HG2  . ARG A 1 134 ? 2.741   8.364   11.947  1.00 20.60  ? 152 ARG A HG2  1 
ATOM   2033  H  HG3  . ARG A 1 134 ? 3.370   8.210   13.398  1.00 20.60  ? 152 ARG A HG3  1 
ATOM   2034  H  HD2  . ARG A 1 134 ? 3.231   10.468  12.943  1.00 21.50  ? 152 ARG A HD2  1 
ATOM   2035  H  HD3  . ARG A 1 134 ? 4.771   10.080  12.915  1.00 21.50  ? 152 ARG A HD3  1 
ATOM   2036  H  HE   . ARG A 1 134 ? 3.495   10.107  10.520  1.00 22.35  ? 152 ARG A HE   1 
ATOM   2037  H  HH11 . ARG A 1 134 ? 5.666   11.765  12.397  1.00 22.56  ? 152 ARG A HH11 1 
ATOM   2038  H  HH12 . ARG A 1 134 ? 6.207   12.614  11.299  1.00 22.56  ? 152 ARG A HH12 1 
ATOM   2039  H  HH21 . ARG A 1 134 ? 4.327   11.390  8.876   1.00 25.63  ? 152 ARG A HH21 1 
ATOM   2040  H  HH22 . ARG A 1 134 ? 5.395   12.386  9.167   1.00 25.63  ? 152 ARG A HH22 1 
ATOM   2041  N  N    . LEU A 1 135 ? 3.973   5.062   13.467  1.00 14.68  ? 153 LEU A N    1 
ATOM   2042  C  CA   . LEU A 1 135 ? 3.296   4.461   14.606  1.00 14.80  ? 153 LEU A CA   1 
ATOM   2043  C  C    . LEU A 1 135 ? 3.831   5.134   15.861  1.00 14.60  ? 153 LEU A C    1 
ATOM   2044  O  O    . LEU A 1 135 ? 5.047   5.197   16.060  1.00 15.49  ? 153 LEU A O    1 
ATOM   2045  C  CB   . LEU A 1 135 ? 3.560   2.951   14.651  1.00 15.35  ? 153 LEU A CB   1 
ATOM   2046  C  CG   . LEU A 1 135 ? 3.088   2.187   15.894  1.00 15.62  ? 153 LEU A CG   1 
ATOM   2047  C  CD1  . LEU A 1 135 ? 1.590   2.359   16.111  1.00 15.29  ? 153 LEU A CD1  1 
ATOM   2048  C  CD2  . LEU A 1 135 ? 3.459   0.706   15.790  1.00 16.77  ? 153 LEU A CD2  1 
ATOM   2049  H  H    . LEU A 1 135 ? 4.830   5.022   13.525  1.00 17.61  ? 153 LEU A H    1 
ATOM   2050  H  HA   . LEU A 1 135 ? 2.337   4.598   14.557  1.00 17.76  ? 153 LEU A HA   1 
ATOM   2051  H  HB2  . LEU A 1 135 ? 3.114   2.549   13.889  1.00 18.42  ? 153 LEU A HB2  1 
ATOM   2052  H  HB3  . LEU A 1 135 ? 4.518   2.815   14.585  1.00 18.42  ? 153 LEU A HB3  1 
ATOM   2053  H  HG   . LEU A 1 135 ? 3.537   2.554   16.671  1.00 18.74  ? 153 LEU A HG   1 
ATOM   2054  H  HD11 . LEU A 1 135 ? 1.117   2.000   15.344  1.00 18.35  ? 153 LEU A HD11 1 
ATOM   2055  H  HD12 . LEU A 1 135 ? 1.330   1.879   16.913  1.00 18.35  ? 153 LEU A HD12 1 
ATOM   2056  H  HD13 . LEU A 1 135 ? 1.392   3.303   16.211  1.00 18.35  ? 153 LEU A HD13 1 
ATOM   2057  H  HD21 . LEU A 1 135 ? 3.192   0.256   16.607  1.00 20.12  ? 153 LEU A HD21 1 
ATOM   2058  H  HD22 . LEU A 1 135 ? 2.997   0.317   15.031  1.00 20.12  ? 153 LEU A HD22 1 
ATOM   2059  H  HD23 . LEU A 1 135 ? 4.418   0.629   15.669  1.00 20.12  ? 153 LEU A HD23 1 
ATOM   2060  N  N    . MET A 1 136 ? 2.927   5.665   16.685  1.00 13.75  ? 154 MET A N    1 
ATOM   2061  C  CA   . MET A 1 136 ? 3.267   6.286   17.967  1.00 13.70  ? 154 MET A CA   1 
ATOM   2062  C  C    . MET A 1 136 ? 2.578   5.436   19.031  1.00 13.42  ? 154 MET A C    1 
ATOM   2063  O  O    . MET A 1 136 ? 1.371   5.572   19.253  1.00 14.46  ? 154 MET A O    1 
ATOM   2064  C  CB   . MET A 1 136 ? 2.789   7.738   18.013  1.00 14.49  ? 154 MET A CB   1 
ATOM   2065  C  CG   . MET A 1 136 ? 2.982   8.431   19.372  1.00 14.30  ? 154 MET A CG   1 
ATOM   2066  S  SD   . MET A 1 136 ? 4.708   8.615   19.913  1.00 15.91  ? 154 MET A SD   1 
ATOM   2067  C  CE   . MET A 1 136 ? 4.800   7.442   21.272  1.00 15.76  ? 154 MET A CE   1 
ATOM   2068  H  H    . MET A 1 136 ? 2.084   5.678   16.518  1.00 16.49  ? 154 MET A H    1 
ATOM   2069  H  HA   . MET A 1 136 ? 4.228   6.291   18.103  1.00 16.44  ? 154 MET A HA   1 
ATOM   2070  H  HB2  . MET A 1 136 ? 3.284   8.247   17.352  1.00 17.38  ? 154 MET A HB2  1 
ATOM   2071  H  HB3  . MET A 1 136 ? 1.842   7.758   17.806  1.00 17.38  ? 154 MET A HB3  1 
ATOM   2072  H  HG2  . MET A 1 136 ? 2.599   9.321   19.320  1.00 17.16  ? 154 MET A HG2  1 
ATOM   2073  H  HG3  . MET A 1 136 ? 2.522   7.911   20.049  1.00 17.16  ? 154 MET A HG3  1 
ATOM   2074  H  HE1  . MET A 1 136 ? 3.991   7.508   21.802  1.00 18.91  ? 154 MET A HE1  1 
ATOM   2075  H  HE2  . MET A 1 136 ? 4.886   6.546   20.910  1.00 18.91  ? 154 MET A HE2  1 
ATOM   2076  H  HE3  . MET A 1 136 ? 5.573   7.652   21.819  1.00 18.91  ? 154 MET A HE3  1 
ATOM   2077  N  N    . ALA A 1 137 ? 3.335   4.551   19.674  1.00 13.41  ? 155 ALA A N    1 
ATOM   2078  C  CA   . ALA A 1 137 ? 2.786   3.565   20.594  1.00 14.25  ? 155 ALA A CA   1 
ATOM   2079  C  C    . ALA A 1 137 ? 3.160   3.929   22.024  1.00 13.80  ? 155 ALA A C    1 
ATOM   2080  O  O    . ALA A 1 137 ? 4.345   4.077   22.346  1.00 14.88  ? 155 ALA A O    1 
ATOM   2081  C  CB   . ALA A 1 137 ? 3.309   2.169   20.261  1.00 14.32  ? 155 ALA A CB   1 
ATOM   2082  H  H    . ALA A 1 137 ? 4.189   4.504   19.590  1.00 16.09  ? 155 ALA A H    1 
ATOM   2083  H  HA   . ALA A 1 137 ? 1.818   3.575   20.523  1.00 17.11  ? 155 ALA A HA   1 
ATOM   2084  H  HB1  . ALA A 1 137 ? 2.933   1.532   20.888  1.00 17.19  ? 155 ALA A HB1  1 
ATOM   2085  H  HB2  . ALA A 1 137 ? 3.042   1.939   19.357  1.00 17.19  ? 155 ALA A HB2  1 
ATOM   2086  H  HB3  . ALA A 1 137 ? 4.276   2.169   20.330  1.00 17.19  ? 155 ALA A HB3  1 
ATOM   2087  N  N    . PHE A 1 138 ? 2.151   4.053   22.880  1.00 12.98  ? 156 PHE A N    1 
ATOM   2088  C  CA   . PHE A 1 138 ? 2.348   4.333   24.296  1.00 12.67  ? 156 PHE A CA   1 
ATOM   2089  C  C    . PHE A 1 138 ? 2.159   3.043   25.078  1.00 12.34  ? 156 PHE A C    1 
ATOM   2090  O  O    . PHE A 1 138 ? 1.118   2.383   24.962  1.00 12.98  ? 156 PHE A O    1 
ATOM   2091  C  CB   . PHE A 1 138 ? 1.379   5.415   24.768  1.00 13.54  ? 156 PHE A CB   1 
ATOM   2092  C  CG   . PHE A 1 138 ? 1.628   6.766   24.138  1.00 12.50  ? 156 PHE A CG   1 
ATOM   2093  C  CD1  . PHE A 1 138 ? 2.605   7.614   24.636  1.00 13.76  ? 156 PHE A CD1  1 
ATOM   2094  C  CD2  . PHE A 1 138 ? 0.889   7.178   23.045  1.00 12.97  ? 156 PHE A CD2  1 
ATOM   2095  C  CE1  . PHE A 1 138 ? 2.825   8.845   24.058  1.00 14.93  ? 156 PHE A CE1  1 
ATOM   2096  C  CE2  . PHE A 1 138 ? 1.106   8.418   22.467  1.00 14.15  ? 156 PHE A CE2  1 
ATOM   2097  C  CZ   . PHE A 1 138 ? 2.080   9.248   22.972  1.00 14.89  ? 156 PHE A CZ   1 
ATOM   2098  H  H    . PHE A 1 138 ? 1.324   3.977   22.657  1.00 15.57  ? 156 PHE A H    1 
ATOM   2099  H  HA   . PHE A 1 138 ? 3.251   4.652   24.451  1.00 15.20  ? 156 PHE A HA   1 
ATOM   2100  H  HB2  . PHE A 1 138 ? 0.475   5.144   24.543  1.00 16.25  ? 156 PHE A HB2  1 
ATOM   2101  H  HB3  . PHE A 1 138 ? 1.466   5.514   25.729  1.00 16.25  ? 156 PHE A HB3  1 
ATOM   2102  H  HD1  . PHE A 1 138 ? 3.116   7.349   25.366  1.00 16.52  ? 156 PHE A HD1  1 
ATOM   2103  H  HD2  . PHE A 1 138 ? 0.237   6.615   22.693  1.00 15.57  ? 156 PHE A HD2  1 
ATOM   2104  H  HE1  . PHE A 1 138 ? 3.480   9.407   24.404  1.00 17.92  ? 156 PHE A HE1  1 
ATOM   2105  H  HE2  . PHE A 1 138 ? 0.594   8.689   21.739  1.00 16.98  ? 156 PHE A HE2  1 
ATOM   2106  H  HZ   . PHE A 1 138 ? 2.235   10.077  22.581  1.00 17.87  ? 156 PHE A HZ   1 
ATOM   2107  N  N    . ALA A 1 139 ? 3.172   2.688   25.867  1.00 12.82  ? 157 ALA A N    1 
ATOM   2108  C  CA   . ALA A 1 139 ? 3.195   1.456   26.644  1.00 12.06  ? 157 ALA A CA   1 
ATOM   2109  C  C    . ALA A 1 139 ? 2.791   0.203   25.864  1.00 13.03  ? 157 ALA A C    1 
ATOM   2110  O  O    . ALA A 1 139 ? 2.013   -0.618  26.365  1.00 14.13  ? 157 ALA A O    1 
ATOM   2111  C  CB   . ALA A 1 139 ? 2.344   1.597   27.901  1.00 13.03  ? 157 ALA A CB   1 
ATOM   2112  H  H    . ALA A 1 139 ? 3.880   3.164   25.970  1.00 15.38  ? 157 ALA A H    1 
ATOM   2113  H  HA   . ALA A 1 139 ? 4.117   1.305   26.905  1.00 14.48  ? 157 ALA A HA   1 
ATOM   2114  H  HB1  . ALA A 1 139 ? 1.418   1.724   27.643  1.00 15.63  ? 157 ALA A HB1  1 
ATOM   2115  H  HB2  . ALA A 1 139 ? 2.432   0.791   28.433  1.00 15.63  ? 157 ALA A HB2  1 
ATOM   2116  H  HB3  . ALA A 1 139 ? 2.654   2.364   28.408  1.00 15.63  ? 157 ALA A HB3  1 
ATOM   2117  N  N    . PRO A 1 140 ? 3.338   -0.006  24.661  1.00 13.11  ? 158 PRO A N    1 
ATOM   2118  C  CA   . PRO A 1 140 ? 3.012   -1.228  23.912  1.00 12.91  ? 158 PRO A CA   1 
ATOM   2119  C  C    . PRO A 1 140 ? 3.619   -2.466  24.550  1.00 13.97  ? 158 PRO A C    1 
ATOM   2120  O  O    . PRO A 1 140 ? 4.743   -2.436  25.058  1.00 15.56  ? 158 PRO A O    1 
ATOM   2121  C  CB   . PRO A 1 140 ? 3.637   -0.979  22.536  1.00 13.62  ? 158 PRO A CB   1 
ATOM   2122  C  CG   . PRO A 1 140 ? 4.802   -0.080  22.823  1.00 12.83  ? 158 PRO A CG   1 
ATOM   2123  C  CD   . PRO A 1 140 ? 4.301   0.842   23.926  1.00 12.87  ? 158 PRO A CD   1 
ATOM   2124  H  HA   . PRO A 1 140 ? 2.050   -1.329  23.841  1.00 15.49  ? 158 PRO A HA   1 
ATOM   2125  H  HB2  . PRO A 1 140 ? 3.929   -1.818  22.145  1.00 16.34  ? 158 PRO A HB2  1 
ATOM   2126  H  HB3  . PRO A 1 140 ? 2.995   -0.546  21.951  1.00 16.34  ? 158 PRO A HB3  1 
ATOM   2127  H  HG2  . PRO A 1 140 ? 5.561   -0.604  23.124  1.00 15.40  ? 158 PRO A HG2  1 
ATOM   2128  H  HG3  . PRO A 1 140 ? 5.039   0.423   22.029  1.00 15.40  ? 158 PRO A HG3  1 
ATOM   2129  H  HD2  . PRO A 1 140 ? 5.030   1.117   24.503  1.00 15.45  ? 158 PRO A HD2  1 
ATOM   2130  H  HD3  . PRO A 1 140 ? 3.862   1.621   23.552  1.00 15.45  ? 158 PRO A HD3  1 
ATOM   2131  N  N    . ASP A 1 141 ? 2.893   -3.578  24.470  1.00 14.67  ? 159 ASP A N    1 
ATOM   2132  C  CA   . ASP A 1 141 ? 3.355   -4.834  25.055  1.00 15.21  ? 159 ASP A CA   1 
ATOM   2133  C  C    . ASP A 1 141 ? 3.631   -5.860  23.959  1.00 14.39  ? 159 ASP A C    1 
ATOM   2134  O  O    . ASP A 1 141 ? 2.977   -6.900  23.877  1.00 13.89  ? 159 ASP A O    1 
ATOM   2135  C  CB   . ASP A 1 141 ? 2.346   -5.358  26.124  1.00 15.62  ? 159 ASP A CB   1 
ATOM   2136  C  CG   . ASP A 1 141 ? 0.946   -5.634  25.566  1.00 17.38  ? 159 ASP A CG   1 
ATOM   2137  O  OD1  . ASP A 1 141 ? 0.514   -4.994  24.586  1.00 16.71  ? 159 ASP A OD1  1 
ATOM   2138  O  OD2  . ASP A 1 141 ? 0.260   -6.511  26.134  1.00 18.85  ? 159 ASP A OD2  1 
ATOM   2139  H  H    . ASP A 1 141 ? 2.128   -3.630  24.081  1.00 17.60  ? 159 ASP A H    1 
ATOM   2140  H  HA   . ASP A 1 141 ? 4.197   -4.663  25.505  1.00 18.25  ? 159 ASP A HA   1 
ATOM   2141  H  HB2  . ASP A 1 141 ? 2.686   -6.187  26.494  1.00 18.75  ? 159 ASP A HB2  1 
ATOM   2142  H  HB3  . ASP A 1 141 ? 2.260   -4.693  26.825  1.00 18.75  ? 159 ASP A HB3  1 
ATOM   2143  N  N    . TYR A 1 142 ? 4.667   -5.591  23.146  1.00 14.08  ? 160 TYR A N    1 
ATOM   2144  C  CA   . TYR A 1 142 ? 4.974   -6.488  22.032  1.00 13.82  ? 160 TYR A CA   1 
ATOM   2145  C  C    . TYR A 1 142 ? 5.444   -7.860  22.507  1.00 14.76  ? 160 TYR A C    1 
ATOM   2146  O  O    . TYR A 1 142 ? 5.268   -8.849  21.787  1.00 14.74  ? 160 TYR A O    1 
ATOM   2147  C  CB   . TYR A 1 142 ? 6.032   -5.885  21.103  1.00 13.82  ? 160 TYR A CB   1 
ATOM   2148  C  CG   . TYR A 1 142 ? 5.739   -4.484  20.605  1.00 12.66  ? 160 TYR A CG   1 
ATOM   2149  C  CD1  . TYR A 1 142 ? 4.661   -4.230  19.762  1.00 13.69  ? 160 TYR A CD1  1 
ATOM   2150  C  CD2  . TYR A 1 142 ? 6.553   -3.421  20.958  1.00 12.84  ? 160 TYR A CD2  1 
ATOM   2151  C  CE1  . TYR A 1 142 ? 4.397   -2.958  19.297  1.00 14.12  ? 160 TYR A CE1  1 
ATOM   2152  C  CE2  . TYR A 1 142 ? 6.288   -2.137  20.501  1.00 13.91  ? 160 TYR A CE2  1 
ATOM   2153  C  CZ   . TYR A 1 142 ? 5.215   -1.916  19.669  1.00 13.84  ? 160 TYR A CZ   1 
ATOM   2154  O  OH   . TYR A 1 142 ? 4.950   -0.648  19.206  1.00 15.27  ? 160 TYR A OH   1 
ATOM   2155  H  H    . TYR A 1 142 ? 5.190   -4.913  23.220  1.00 16.89  ? 160 TYR A H    1 
ATOM   2156  H  HA   . TYR A 1 142 ? 4.156   -6.598  21.523  1.00 16.59  ? 160 TYR A HA   1 
ATOM   2157  H  HB2  . TYR A 1 142 ? 6.875   -5.851  21.581  1.00 16.58  ? 160 TYR A HB2  1 
ATOM   2158  H  HB3  . TYR A 1 142 ? 6.116   -6.457  20.324  1.00 16.58  ? 160 TYR A HB3  1 
ATOM   2159  H  HD1  . TYR A 1 142 ? 4.107   -4.932  19.507  1.00 16.42  ? 160 TYR A HD1  1 
ATOM   2160  H  HD2  . TYR A 1 142 ? 7.288   -3.570  21.509  1.00 15.41  ? 160 TYR A HD2  1 
ATOM   2161  H  HE1  . TYR A 1 142 ? 3.672   -2.806  18.735  1.00 16.95  ? 160 TYR A HE1  1 
ATOM   2162  H  HE2  . TYR A 1 142 ? 6.835   -1.429  20.755  1.00 16.70  ? 160 TYR A HE2  1 
ATOM   2163  H  HH   . TYR A 1 142 ? 5.469   -0.095  19.569  1.00 18.32  ? 160 TYR A HH   1 
ATOM   2164  N  N    . LYS A 1 143 ? 6.065   -7.937  23.688  1.00 14.49  ? 161 LYS A N    1 
ATOM   2165  C  CA   . LYS A 1 143 ? 6.438   -9.203  24.306  1.00 14.99  ? 161 LYS A CA   1 
ATOM   2166  C  C    . LYS A 1 143 ? 5.391   -9.694  25.303  1.00 15.68  ? 161 LYS A C    1 
ATOM   2167  O  O    . LYS A 1 143 ? 5.627   -10.685 26.002  1.00 17.99  ? 161 LYS A O    1 
ATOM   2168  C  CB   . LYS A 1 143 ? 7.795   -9.088  25.007  1.00 15.89  ? 161 LYS A CB   1 
ATOM   2169  C  CG   . LYS A 1 143 ? 8.972   -8.766  24.087  1.00 15.76  ? 161 LYS A CG   1 
ATOM   2170  C  CD   . LYS A 1 143 ? 10.283  -8.675  24.881  1.00 16.40  ? 161 LYS A CD   1 
ATOM   2171  C  CE   . LYS A 1 143 ? 11.476  -8.431  23.980  1.00 16.79  ? 161 LYS A CE   1 
ATOM   2172  N  NZ   . LYS A 1 143 ? 11.510  -7.060  23.418  1.00 16.75  ? 161 LYS A NZ   1 
ATOM   2173  H  H    . LYS A 1 143 ? 6.283   -7.251  24.157  1.00 17.39  ? 161 LYS A H    1 
ATOM   2174  H  HA   . LYS A 1 143 ? 6.526   -9.864  23.602  1.00 17.99  ? 161 LYS A HA   1 
ATOM   2175  H  HB2  . LYS A 1 143 ? 7.740   -8.379  25.667  1.00 19.07  ? 161 LYS A HB2  1 
ATOM   2176  H  HB3  . LYS A 1 143 ? 7.988   -9.933  25.442  1.00 19.07  ? 161 LYS A HB3  1 
ATOM   2177  H  HG2  . LYS A 1 143 ? 9.064   -9.466  23.422  1.00 18.91  ? 161 LYS A HG2  1 
ATOM   2178  H  HG3  . LYS A 1 143 ? 8.818   -7.913  23.651  1.00 18.91  ? 161 LYS A HG3  1 
ATOM   2179  H  HD2  . LYS A 1 143 ? 10.224  -7.940  25.511  1.00 19.68  ? 161 LYS A HD2  1 
ATOM   2180  H  HD3  . LYS A 1 143 ? 10.427  -9.509  25.355  1.00 19.68  ? 161 LYS A HD3  1 
ATOM   2181  H  HE2  . LYS A 1 143 ? 12.289  -8.564  24.491  1.00 20.14  ? 161 LYS A HE2  1 
ATOM   2182  H  HE3  . LYS A 1 143 ? 11.444  -9.056  23.239  1.00 20.14  ? 161 LYS A HE3  1 
ATOM   2183  H  HZ1  . LYS A 1 143 ? 10.755  -6.893  22.978  1.00 20.10  ? 161 LYS A HZ1  1 
ATOM   2184  H  HZ2  . LYS A 1 143 ? 11.601  -6.465  24.073  1.00 20.10  ? 161 LYS A HZ2  1 
ATOM   2185  H  HZ3  . LYS A 1 143 ? 12.195  -6.979  22.856  1.00 20.10  ? 161 LYS A HZ3  1 
ATOM   2186  N  N    . GLY A 1 144 ? 4.245   -9.019  25.390  1.00 15.28  ? 162 GLY A N    1 
ATOM   2187  C  CA   . GLY A 1 144 ? 3.303   -9.325  26.443  1.00 15.54  ? 162 GLY A CA   1 
ATOM   2188  C  C    . GLY A 1 144 ? 3.816   -8.809  27.776  1.00 16.04  ? 162 GLY A C    1 
ATOM   2189  O  O    . GLY A 1 144 ? 4.623   -7.872  27.850  1.00 16.79  ? 162 GLY A O    1 
ATOM   2190  H  H    . GLY A 1 144 ? 3.999   -8.390  24.857  1.00 18.34  ? 162 GLY A H    1 
ATOM   2191  H  HA2  . GLY A 1 144 ? 2.449   -8.908  26.252  1.00 18.65  ? 162 GLY A HA2  1 
ATOM   2192  H  HA3  . GLY A 1 144 ? 3.179   -10.285 26.505  1.00 18.65  ? 162 GLY A HA3  1 
ATOM   2193  N  N    . THR A 1 145 ? 3.360   -9.451  28.845  1.00 15.71  ? 163 THR A N    1 
ATOM   2194  C  CA   . THR A 1 145 ? 3.762   -9.076  30.188  1.00 15.67  ? 163 THR A CA   1 
ATOM   2195  C  C    . THR A 1 145 ? 3.885   -10.315 31.063  1.00 17.81  ? 163 THR A C    1 
ATOM   2196  O  O    . THR A 1 145 ? 3.138   -11.286 30.907  1.00 18.07  ? 163 THR A O    1 
ATOM   2197  C  CB   . THR A 1 145 ? 2.771   -8.095  30.819  1.00 16.13  ? 163 THR A CB   1 
ATOM   2198  O  OG1  . THR A 1 145 ? 3.237   -7.752  32.128  1.00 16.36  ? 163 THR A OG1  1 
ATOM   2199  C  CG2  . THR A 1 145 ? 1.373   -8.694  30.907  1.00 18.24  ? 163 THR A CG2  1 
ATOM   2200  H  H    . THR A 1 145 ? 2.812   -10.113 28.815  1.00 18.86  ? 163 THR A H    1 
ATOM   2201  H  HA   . THR A 1 145 ? 4.635   -8.654  30.148  1.00 18.81  ? 163 THR A HA   1 
ATOM   2202  H  HB   . THR A 1 145 ? 2.705   -7.299  30.270  1.00 19.35  ? 163 THR A HB   1 
ATOM   2203  H  HG1  . THR A 1 145 ? 2.747   -7.155  32.460  1.00 19.64  ? 163 THR A HG1  1 
ATOM   2204  H  HG21 . THR A 1 145 ? 1.384   -9.481  31.473  1.00 21.89  ? 163 THR A HG21 1 
ATOM   2205  H  HG22 . THR A 1 145 ? 0.757   -8.045  31.283  1.00 21.89  ? 163 THR A HG22 1 
ATOM   2206  H  HG23 . THR A 1 145 ? 1.063   -8.945  30.023  1.00 21.89  ? 163 THR A HG23 1 
ATOM   2207  N  N    . VAL A 1 146 ? 4.827   -10.253 32.009  1.00 19.47  ? 164 VAL A N    1 
ATOM   2208  C  CA   . VAL A 1 146 ? 5.003   -11.326 32.982  1.00 20.66  ? 164 VAL A CA   1 
ATOM   2209  C  C    . VAL A 1 146 ? 4.109   -11.168 34.210  1.00 24.06  ? 164 VAL A C    1 
ATOM   2210  O  O    . VAL A 1 146 ? 4.043   -12.092 35.039  1.00 26.11  ? 164 VAL A O    1 
ATOM   2211  C  CB   . VAL A 1 146 ? 6.479   -11.464 33.419  1.00 22.65  ? 164 VAL A CB   1 
ATOM   2212  C  CG1  . VAL A 1 146 ? 7.380   -11.768 32.213  1.00 23.32  ? 164 VAL A CG1  1 
ATOM   2213  C  CG2  . VAL A 1 146 ? 6.961   -10.215 34.139  1.00 24.12  ? 164 VAL A CG2  1 
ATOM   2214  H  H    . VAL A 1 146 ? 5.376   -9.598  32.107  1.00 23.37  ? 164 VAL A H    1 
ATOM   2215  H  HA   . VAL A 1 146 ? 4.751   -12.156 32.546  1.00 24.79  ? 164 VAL A HA   1 
ATOM   2216  H  HB   . VAL A 1 146 ? 6.540   -12.207 34.039  1.00 27.18  ? 164 VAL A HB   1 
ATOM   2217  H  HG11 . VAL A 1 146 ? 8.295   -11.866 32.520  1.00 27.98  ? 164 VAL A HG11 1 
ATOM   2218  H  HG12 . VAL A 1 146 ? 7.081   -12.590 31.795  1.00 27.98  ? 164 VAL A HG12 1 
ATOM   2219  H  HG13 . VAL A 1 146 ? 7.320   -11.034 31.581  1.00 27.98  ? 164 VAL A HG13 1 
ATOM   2220  H  HG21 . VAL A 1 146 ? 7.892   -10.331 34.384  1.00 28.94  ? 164 VAL A HG21 1 
ATOM   2221  H  HG22 . VAL A 1 146 ? 6.867   -9.453  33.547  1.00 28.94  ? 164 VAL A HG22 1 
ATOM   2222  H  HG23 . VAL A 1 146 ? 6.423   -10.083 34.936  1.00 28.94  ? 164 VAL A HG23 1 
ATOM   2223  N  N    . LEU A 1 147 ? 3.410   -10.041 34.348  1.00 24.95  ? 165 LEU A N    1 
ATOM   2224  C  CA   . LEU A 1 147 ? 2.586   -9.780  35.521  1.00 27.98  ? 165 LEU A CA   1 
ATOM   2225  C  C    . LEU A 1 147 ? 1.147   -10.251 35.314  1.00 33.04  ? 165 LEU A C    1 
ATOM   2226  O  O    . LEU A 1 147 ? 0.631   -10.278 34.192  1.00 33.84  ? 165 LEU A O    1 
ATOM   2227  C  CB   . LEU A 1 147 ? 2.567   -8.282  35.840  1.00 25.85  ? 165 LEU A CB   1 
ATOM   2228  C  CG   . LEU A 1 147 ? 3.911   -7.581  36.009  1.00 24.63  ? 165 LEU A CG   1 
ATOM   2229  C  CD1  . LEU A 1 147 ? 3.676   -6.076  36.033  1.00 23.82  ? 165 LEU A CD1  1 
ATOM   2230  C  CD2  . LEU A 1 147 ? 4.629   -8.027  37.262  1.00 26.51  ? 165 LEU A CD2  1 
ATOM   2231  H  H    . LEU A 1 147 ? 3.398   -9.406  33.768  1.00 29.94  ? 165 LEU A H    1 
ATOM   2232  H  HA   . LEU A 1 147 ? 2.961   -10.268 36.271  1.00 33.58  ? 165 LEU A HA   1 
ATOM   2233  H  HB2  . LEU A 1 147 ? 2.104   -7.831  35.116  1.00 31.02  ? 165 LEU A HB2  1 
ATOM   2234  H  HB3  . LEU A 1 147 ? 2.081   -8.162  36.670  1.00 31.02  ? 165 LEU A HB3  1 
ATOM   2235  H  HG   . LEU A 1 147 ? 4.489   -7.812  35.266  1.00 29.55  ? 165 LEU A HG   1 
ATOM   2236  H  HD11 . LEU A 1 147 ? 3.005   -5.871  36.704  1.00 28.58  ? 165 LEU A HD11 1 
ATOM   2237  H  HD12 . LEU A 1 147 ? 4.509   -5.629  36.252  1.00 28.58  ? 165 LEU A HD12 1 
ATOM   2238  H  HD13 . LEU A 1 147 ? 3.367   -5.790  35.159  1.00 28.58  ? 165 LEU A HD13 1 
ATOM   2239  H  HD21 . LEU A 1 147 ? 5.098   -8.856  37.078  1.00 31.81  ? 165 LEU A HD21 1 
ATOM   2240  H  HD22 . LEU A 1 147 ? 5.261   -7.340  37.526  1.00 31.81  ? 165 LEU A HD22 1 
ATOM   2241  H  HD23 . LEU A 1 147 ? 3.977   -8.166  37.967  1.00 31.81  ? 165 LEU A HD23 1 
ATOM   2242  N  N    . ALA A 1 148 ? 0.502   -10.621 36.420  1.00 35.56  ? 166 ALA A N    1 
ATOM   2243  C  CA   . ALA A 1 148 ? -0.929  -10.938 36.464  1.00 37.19  ? 166 ALA A CA   1 
ATOM   2244  C  C    . ALA A 1 148 ? -1.320  -11.952 35.381  1.00 38.99  ? 166 ALA A C    1 
ATOM   2245  O  O    . ALA A 1 148 ? -2.025  -11.657 34.414  1.00 40.85  ? 166 ALA A O    1 
ATOM   2246  C  CB   . ALA A 1 148 ? -1.773  -9.661  36.383  1.00 37.35  ? 166 ALA A CB   1 
ATOM   2247  H  H    . ALA A 1 148 ? 0.884   -10.697 37.187  1.00 42.67  ? 166 ALA A H    1 
ATOM   2248  H  HA   . ALA A 1 148 ? -1.110  -11.363 37.317  1.00 44.63  ? 166 ALA A HA   1 
ATOM   2249  H  HB1  . ALA A 1 148 ? -2.701  -9.884  36.556  1.00 44.82  ? 166 ALA A HB1  1 
ATOM   2250  H  HB2  . ALA A 1 148 ? -1.455  -9.030  37.047  1.00 44.82  ? 166 ALA A HB2  1 
ATOM   2251  H  HB3  . ALA A 1 148 ? -1.685  -9.280  35.495  1.00 44.82  ? 166 ALA A HB3  1 
ATOM   2252  N  N    . GLY A 1 149 ? -0.864  -13.179 35.596  1.00 37.70  ? 167 GLY A N    1 
ATOM   2253  C  CA   . GLY A 1 149 ? -1.106  -14.250 34.660  1.00 36.60  ? 167 GLY A CA   1 
ATOM   2254  C  C    . GLY A 1 149 ? -2.563  -14.662 34.582  1.00 34.30  ? 167 GLY A C    1 
ATOM   2255  O  O    . GLY A 1 149 ? -3.362  -14.405 35.489  1.00 33.22  ? 167 GLY A O    1 
ATOM   2256  H  H    . GLY A 1 149 ? -0.408  -13.413 36.286  1.00 45.24  ? 167 GLY A H    1 
ATOM   2257  H  HA2  . GLY A 1 149 ? -0.824  -13.968 33.776  1.00 43.93  ? 167 GLY A HA2  1 
ATOM   2258  H  HA3  . GLY A 1 149 ? -0.587  -15.025 34.925  1.00 43.93  ? 167 GLY A HA3  1 
ATOM   2259  N  N    . PRO A 1 150 ? -2.930  -15.333 33.486  1.00 32.95  ? 168 PRO A N    1 
ATOM   2260  C  CA   . PRO A 1 150 ? -4.337  -15.734 33.299  1.00 32.04  ? 168 PRO A CA   1 
ATOM   2261  C  C    . PRO A 1 150 ? -4.865  -16.708 34.343  1.00 31.75  ? 168 PRO A C    1 
ATOM   2262  O  O    . PRO A 1 150 ? -6.091  -16.834 34.481  1.00 32.35  ? 168 PRO A O    1 
ATOM   2263  C  CB   . PRO A 1 150 ? -4.341  -16.367 31.897  1.00 32.76  ? 168 PRO A CB   1 
ATOM   2264  C  CG   . PRO A 1 150 ? -2.915  -16.783 31.664  1.00 33.59  ? 168 PRO A CG   1 
ATOM   2265  C  CD   . PRO A 1 150 ? -2.082  -15.738 32.349  1.00 33.28  ? 168 PRO A CD   1 
ATOM   2266  H  HA   . PRO A 1 150 ? -4.896  -14.942 33.302  1.00 38.44  ? 168 PRO A HA   1 
ATOM   2267  H  HB2  . PRO A 1 150 ? -4.935  -17.133 31.880  1.00 39.31  ? 168 PRO A HB2  1 
ATOM   2268  H  HB3  . PRO A 1 150 ? -4.625  -15.713 31.239  1.00 39.31  ? 168 PRO A HB3  1 
ATOM   2269  H  HG2  . PRO A 1 150 ? -2.759  -17.658 32.052  1.00 40.31  ? 168 PRO A HG2  1 
ATOM   2270  H  HG3  . PRO A 1 150 ? -2.729  -16.804 30.712  1.00 40.31  ? 168 PRO A HG3  1 
ATOM   2271  H  HD2  . PRO A 1 150 ? -1.242  -16.112 32.658  1.00 39.94  ? 168 PRO A HD2  1 
ATOM   2272  H  HD3  . PRO A 1 150 ? -1.913  -14.987 31.758  1.00 39.94  ? 168 PRO A HD3  1 
ATOM   2273  N  N    . LEU A 1 151 ? -3.998  -17.417 35.060  1.00 29.57  ? 169 LEU A N    1 
ATOM   2274  C  CA   . LEU A 1 151 ? -4.443  -18.367 36.073  1.00 30.35  ? 169 LEU A CA   1 
ATOM   2275  C  C    . LEU A 1 151 ? -4.475  -17.773 37.478  1.00 30.71  ? 169 LEU A C    1 
ATOM   2276  O  O    . LEU A 1 151 ? -4.745  -18.501 38.437  1.00 31.23  ? 169 LEU A O    1 
ATOM   2277  C  CB   . LEU A 1 151 ? -3.562  -19.621 36.058  1.00 30.95  ? 169 LEU A CB   1 
ATOM   2278  C  CG   . LEU A 1 151 ? -3.668  -20.494 34.804  1.00 32.61  ? 169 LEU A CG   1 
ATOM   2279  C  CD1  . LEU A 1 151 ? -2.812  -21.744 34.971  1.00 33.12  ? 169 LEU A CD1  1 
ATOM   2280  C  CD2  . LEU A 1 151 ? -5.108  -20.882 34.490  1.00 32.56  ? 169 LEU A CD2  1 
ATOM   2281  H  H    . LEU A 1 151 ? -3.144  -17.365 34.977  1.00 35.49  ? 169 LEU A H    1 
ATOM   2282  H  HA   . LEU A 1 151 ? -5.346  -18.644 35.852  1.00 36.42  ? 169 LEU A HA   1 
ATOM   2283  H  HB2  . LEU A 1 151 ? -2.636  -19.342 36.137  1.00 37.14  ? 169 LEU A HB2  1 
ATOM   2284  H  HB3  . LEU A 1 151 ? -3.808  -20.174 36.816  1.00 37.14  ? 169 LEU A HB3  1 
ATOM   2285  H  HG   . LEU A 1 151 ? -3.345  -19.978 34.048  1.00 39.13  ? 169 LEU A HG   1 
ATOM   2286  H  HD11 . LEU A 1 151 ? -3.115  -22.232 35.753  1.00 39.74  ? 169 LEU A HD11 1 
ATOM   2287  H  HD12 . LEU A 1 151 ? -2.904  -22.298 34.180  1.00 39.74  ? 169 LEU A HD12 1 
ATOM   2288  H  HD13 . LEU A 1 151 ? -1.886  -21.480 35.085  1.00 39.74  ? 169 LEU A HD13 1 
ATOM   2289  H  HD21 . LEU A 1 151 ? -5.522  -21.233 35.294  1.00 39.07  ? 169 LEU A HD21 1 
ATOM   2290  H  HD22 . LEU A 1 151 ? -5.588  -20.096 34.187  1.00 39.07  ? 169 LEU A HD22 1 
ATOM   2291  H  HD23 . LEU A 1 151 ? -5.108  -21.559 33.795  1.00 39.07  ? 169 LEU A HD23 1 
ATOM   2292  N  N    . ASP A 1 152 ? -4.199  -16.482 37.631  1.00 31.34  ? 170 ASP A N    1 
ATOM   2293  C  CA   . ASP A 1 152 ? -4.347  -15.852 38.935  1.00 33.86  ? 170 ASP A CA   1 
ATOM   2294  C  C    . ASP A 1 152 ? -5.833  -15.713 39.252  1.00 33.07  ? 170 ASP A C    1 
ATOM   2295  O  O    . ASP A 1 152 ? -6.629  -15.302 38.400  1.00 32.33  ? 170 ASP A O    1 
ATOM   2296  C  CB   . ASP A 1 152 ? -3.664  -14.486 38.936  1.00 37.92  ? 170 ASP A CB   1 
ATOM   2297  C  CG   . ASP A 1 152 ? -3.699  -13.812 40.297  1.00 42.34  ? 170 ASP A CG   1 
ATOM   2298  O  OD1  . ASP A 1 152 ? -3.362  -14.469 41.307  1.00 45.01  ? 170 ASP A OD1  1 
ATOM   2299  O  OD2  . ASP A 1 152 ? -4.056  -12.617 40.355  1.00 44.50  ? 170 ASP A OD2  1 
ATOM   2300  H  H    . ASP A 1 152 ? -3.928  -15.958 37.005  1.00 37.60  ? 170 ASP A H    1 
ATOM   2301  H  HA   . ASP A 1 152 ? -3.928  -16.391 39.624  1.00 40.63  ? 170 ASP A HA   1 
ATOM   2302  H  HB2  . ASP A 1 152 ? -2.736  -14.596 38.679  1.00 45.51  ? 170 ASP A HB2  1 
ATOM   2303  H  HB3  . ASP A 1 152 ? -4.117  -13.906 38.303  1.00 45.51  ? 170 ASP A HB3  1 
ATOM   2304  N  N    . ALA A 1 153 ? -6.211  -16.085 40.469  1.00 32.53  ? 171 ALA A N    1 
ATOM   2305  C  CA   . ALA A 1 153 ? -7.612  -16.024 40.918  1.00 32.59  ? 171 ALA A CA   1 
ATOM   2306  C  C    . ALA A 1 153 ? -8.423  -16.990 40.068  1.00 32.48  ? 171 ALA A C    1 
ATOM   2307  O  O    . ALA A 1 153 ? -8.039  -18.169 39.930  1.00 32.00  ? 171 ALA A O    1 
ATOM   2308  C  CB   . ALA A 1 153 ? -8.090  -14.582 40.906  1.00 33.00  ? 171 ALA A CB   1 
ATOM   2309  H  H    . ALA A 1 153 ? -5.671  -16.382 41.068  1.00 39.03  ? 171 ALA A H    1 
ATOM   2310  H  HA   . ALA A 1 153 ? -7.651  -16.351 41.830  1.00 39.11  ? 171 ALA A HA   1 
ATOM   2311  H  HB1  . ALA A 1 153 ? -8.927  -14.522 41.391  1.00 39.60  ? 171 ALA A HB1  1 
ATOM   2312  H  HB2  . ALA A 1 153 ? -7.420  -14.023 41.332  1.00 39.60  ? 171 ALA A HB2  1 
ATOM   2313  H  HB3  . ALA A 1 153 ? -8.220  -14.300 39.987  1.00 39.60  ? 171 ALA A HB3  1 
ATOM   2314  N  N    . LEU A 1 154 ? -9.543  -16.574 39.488  1.00 33.22  ? 172 LEU A N    1 
ATOM   2315  C  CA   . LEU A 1 154 ? -10.335 -17.459 38.653  1.00 31.47  ? 172 LEU A CA   1 
ATOM   2316  C  C    . LEU A 1 154 ? -9.479  -18.024 37.525  1.00 29.65  ? 172 LEU A C    1 
ATOM   2317  O  O    . LEU A 1 154 ? -8.741  -17.293 36.859  1.00 31.98  ? 172 LEU A O    1 
ATOM   2318  C  CB   . LEU A 1 154 ? -11.507 -16.673 38.068  1.00 31.79  ? 172 LEU A CB   1 
ATOM   2319  C  CG   . LEU A 1 154 ? -12.670 -17.442 37.446  1.00 31.35  ? 172 LEU A CG   1 
ATOM   2320  C  CD1  . LEU A 1 154 ? -13.277 -18.404 38.444  1.00 31.83  ? 172 LEU A CD1  1 
ATOM   2321  C  CD2  . LEU A 1 154 ? -13.708 -16.446 36.946  1.00 31.20  ? 172 LEU A CD2  1 
ATOM   2322  H  H    . LEU A 1 154 ? -9.865  -15.780 39.564  1.00 39.87  ? 172 LEU A H    1 
ATOM   2323  H  HA   . LEU A 1 154 ? -10.677 -18.199 39.178  1.00 37.76  ? 172 LEU A HA   1 
ATOM   2324  H  HB2  . LEU A 1 154 ? -11.884 -16.137 38.783  1.00 38.14  ? 172 LEU A HB2  1 
ATOM   2325  H  HB3  . LEU A 1 154 ? -11.154 -16.098 37.372  1.00 38.14  ? 172 LEU A HB3  1 
ATOM   2326  H  HG   . LEU A 1 154 ? -12.354 -17.973 36.698  1.00 37.62  ? 172 LEU A HG   1 
ATOM   2327  H  HD11 . LEU A 1 154 ? -12.727 -19.203 38.488  1.00 38.20  ? 172 LEU A HD11 1 
ATOM   2328  H  HD12 . LEU A 1 154 ? -13.310 -17.977 39.314  1.00 38.20  ? 172 LEU A HD12 1 
ATOM   2329  H  HD13 . LEU A 1 154 ? -14.173 -18.635 38.155  1.00 38.20  ? 172 LEU A HD13 1 
ATOM   2330  H  HD21 . LEU A 1 154 ? -14.122 -16.012 37.709  1.00 37.44  ? 172 LEU A HD21 1 
ATOM   2331  H  HD22 . LEU A 1 154 ? -13.269 -15.785 36.388  1.00 37.44  ? 172 LEU A HD22 1 
ATOM   2332  H  HD23 . LEU A 1 154 ? -14.379 -16.920 36.431  1.00 37.44  ? 172 LEU A HD23 1 
ATOM   2333  N  N    . ALA A 1 155 ? -9.606  -19.337 37.290  1.00 26.45  ? 173 ALA A N    1 
ATOM   2334  C  CA   . ALA A 1 155 ? -8.787  -20.060 36.317  1.00 24.43  ? 173 ALA A CA   1 
ATOM   2335  C  C    . ALA A 1 155 ? -9.214  -19.830 34.862  1.00 22.61  ? 173 ALA A C    1 
ATOM   2336  O  O    . ALA A 1 155 ? -8.779  -20.567 33.971  1.00 23.46  ? 173 ALA A O    1 
ATOM   2337  C  CB   . ALA A 1 155 ? -8.786  -21.561 36.634  1.00 25.20  ? 173 ALA A CB   1 
ATOM   2338  H  H    . ALA A 1 155 ? -10.175 -19.840 37.694  1.00 31.74  ? 173 ALA A H    1 
ATOM   2339  H  HA   . ALA A 1 155 ? -7.875  -19.739 36.400  1.00 29.31  ? 173 ALA A HA   1 
ATOM   2340  H  HB1  . ALA A 1 155 ? -8.434  -21.695 37.528  1.00 30.24  ? 173 ALA A HB1  1 
ATOM   2341  H  HB2  . ALA A 1 155 ? -9.695  -21.895 36.583  1.00 30.24  ? 173 ALA A HB2  1 
ATOM   2342  H  HB3  . ALA A 1 155 ? -8.228  -22.020 35.987  1.00 30.24  ? 173 ALA A HB3  1 
ATOM   2343  N  N    . VAL A 1 156 ? -10.052 -18.841 34.598  1.00 21.44  ? 174 VAL A N    1 
ATOM   2344  C  CA   . VAL A 1 156 ? -10.345 -18.406 33.238  1.00 19.32  ? 174 VAL A CA   1 
ATOM   2345  C  C    . VAL A 1 156 ? -9.991  -16.925 33.129  1.00 20.33  ? 174 VAL A C    1 
ATOM   2346  O  O    . VAL A 1 156 ? -10.027 -16.190 34.122  1.00 23.16  ? 174 VAL A O    1 
ATOM   2347  C  CB   . VAL A 1 156 ? -11.816 -18.692 32.847  1.00 18.97  ? 174 VAL A CB   1 
ATOM   2348  C  CG1  . VAL A 1 156 ? -12.047 -20.208 32.669  1.00 19.29  ? 174 VAL A CG1  1 
ATOM   2349  C  CG2  . VAL A 1 156 ? -12.781 -18.115 33.877  1.00 19.39  ? 174 VAL A CG2  1 
ATOM   2350  H  H    . VAL A 1 156 ? -10.473 -18.395 35.201  1.00 25.72  ? 174 VAL A H    1 
ATOM   2351  H  HA   . VAL A 1 156 ? -9.789  -18.886 32.605  1.00 23.19  ? 174 VAL A HA   1 
ATOM   2352  H  HB   . VAL A 1 156 ? -11.997 -18.257 32.000  1.00 22.77  ? 174 VAL A HB   1 
ATOM   2353  H  HG11 . VAL A 1 156 ? -11.298 -20.587 32.184  1.00 23.14  ? 174 VAL A HG11 1 
ATOM   2354  H  HG12 . VAL A 1 156 ? -12.118 -20.621 33.544  1.00 23.14  ? 174 VAL A HG12 1 
ATOM   2355  H  HG13 . VAL A 1 156 ? -12.868 -20.346 32.171  1.00 23.14  ? 174 VAL A HG13 1 
ATOM   2356  H  HG21 . VAL A 1 156 ? -12.359 -17.362 34.319  1.00 23.27  ? 174 VAL A HG21 1 
ATOM   2357  H  HG22 . VAL A 1 156 ? -13.588 -17.822 33.425  1.00 23.27  ? 174 VAL A HG22 1 
ATOM   2358  H  HG23 . VAL A 1 156 ? -12.997 -18.801 34.527  1.00 23.27  ? 174 VAL A HG23 1 
ATOM   2359  N  N    . SER A 1 157 ? -9.606  -16.503 31.923  1.00 18.70  ? 175 SER A N    1 
ATOM   2360  C  CA   . SER A 1 157 ? -9.227  -15.124 31.647  1.00 20.12  ? 175 SER A CA   1 
ATOM   2361  C  C    . SER A 1 157 ? -9.638  -14.763 30.223  1.00 17.69  ? 175 SER A C    1 
ATOM   2362  O  O    . SER A 1 157 ? -9.848  -15.636 29.377  1.00 16.83  ? 175 SER A O    1 
ATOM   2363  C  CB   . SER A 1 157 ? -7.714  -14.912 31.793  1.00 24.43  ? 175 SER A CB   1 
ATOM   2364  O  OG   . SER A 1 157 ? -7.299  -15.063 33.137  1.00 28.64  ? 175 SER A OG   1 
ATOM   2365  H  H    . SER A 1 157 ? -9.556  -17.012 31.232  1.00 22.44  ? 175 SER A H    1 
ATOM   2366  H  HA   . SER A 1 157 ? -9.694  -14.546 32.270  1.00 24.14  ? 175 SER A HA   1 
ATOM   2367  H  HB2  . SER A 1 157 ? -7.252  -15.567 31.246  1.00 29.31  ? 175 SER A HB2  1 
ATOM   2368  H  HB3  . SER A 1 157 ? -7.493  -14.016 31.495  1.00 29.31  ? 175 SER A HB3  1 
ATOM   2369  H  HG   . SER A 1 157 ? -7.655  -14.471 33.616  1.00 34.37  ? 175 SER A HG   1 
ATOM   2370  N  N    . ALA A 1 158 ? -9.722  -13.457 29.964  1.00 16.73  ? 176 ALA A N    1 
ATOM   2371  C  CA   . ALA A 1 158 ? -10.156 -12.982 28.658  1.00 16.99  ? 176 ALA A CA   1 
ATOM   2372  C  C    . ALA A 1 158 ? -9.234  -13.487 27.558  1.00 16.73  ? 176 ALA A C    1 
ATOM   2373  O  O    . ALA A 1 158 ? -8.018  -13.604 27.766  1.00 15.74  ? 176 ALA A O    1 
ATOM   2374  C  CB   . ALA A 1 158 ? -10.146 -11.451 28.639  1.00 17.71  ? 176 ALA A CB   1 
ATOM   2375  H  H    . ALA A 1 158 ? -9.535  -12.832 30.524  1.00 20.07  ? 176 ALA A H    1 
ATOM   2376  H  HA   . ALA A 1 158 ? -11.051 -13.314 28.485  1.00 20.39  ? 176 ALA A HA   1 
ATOM   2377  H  HB1  . ALA A 1 158 ? -10.437 -11.144 27.767  1.00 21.25  ? 176 ALA A HB1  1 
ATOM   2378  H  HB2  . ALA A 1 158 ? -10.749 -11.123 29.324  1.00 21.25  ? 176 ALA A HB2  1 
ATOM   2379  H  HB3  . ALA A 1 158 ? -9.244  -11.139 28.816  1.00 21.25  ? 176 ALA A HB3  1 
ATOM   2380  N  N    . PRO A 1 159 ? -9.768  -13.784 26.365  1.00 15.85  ? 177 PRO A N    1 
ATOM   2381  C  CA   . PRO A 1 159 ? -8.917  -14.162 25.228  1.00 15.42  ? 177 PRO A CA   1 
ATOM   2382  C  C    . PRO A 1 159 ? -7.661  -13.308 25.057  1.00 15.14  ? 177 PRO A C    1 
ATOM   2383  O  O    . PRO A 1 159 ? -6.556  -13.849 24.943  1.00 14.87  ? 177 PRO A O    1 
ATOM   2384  C  CB   . PRO A 1 159 ? -9.868  -14.036 24.029  1.00 15.84  ? 177 PRO A CB   1 
ATOM   2385  C  CG   . PRO A 1 159 ? -11.227 -14.368 24.611  1.00 15.29  ? 177 PRO A CG   1 
ATOM   2386  C  CD   . PRO A 1 159 ? -11.209 -13.814 26.025  1.00 15.43  ? 177 PRO A CD   1 
ATOM   2387  H  HA   . PRO A 1 159 ? -8.634  -15.084 25.333  1.00 18.50  ? 177 PRO A HA   1 
ATOM   2388  H  HB2  . PRO A 1 159 ? -9.847  -13.131 23.679  1.00 19.01  ? 177 PRO A HB2  1 
ATOM   2389  H  HB3  . PRO A 1 159 ? -9.618  -14.666 23.336  1.00 19.01  ? 177 PRO A HB3  1 
ATOM   2390  H  HG2  . PRO A 1 159 ? -11.922 -13.945 24.083  1.00 18.34  ? 177 PRO A HG2  1 
ATOM   2391  H  HG3  . PRO A 1 159 ? -11.354 -15.330 24.618  1.00 18.34  ? 177 PRO A HG3  1 
ATOM   2392  H  HD2  . PRO A 1 159 ? -11.588 -12.922 26.050  1.00 18.51  ? 177 PRO A HD2  1 
ATOM   2393  H  HD3  . PRO A 1 159 ? -11.693 -14.398 26.630  1.00 18.51  ? 177 PRO A HD3  1 
ATOM   2394  N  N    . SER A 1 160 ? -7.798  -11.978 25.047  1.00 14.51  ? 178 SER A N    1 
ATOM   2395  C  CA   . SER A 1 160 ? -6.628  -11.146 24.784  1.00 14.64  ? 178 SER A CA   1 
ATOM   2396  C  C    . SER A 1 160 ? -5.679  -11.086 25.972  1.00 15.59  ? 178 SER A C    1 
ATOM   2397  O  O    . SER A 1 160 ? -4.514  -10.721 25.798  1.00 16.55  ? 178 SER A O    1 
ATOM   2398  C  CB   . SER A 1 160 ? -7.039  -9.735  24.363  1.00 15.75  ? 178 SER A CB   1 
ATOM   2399  O  OG   . SER A 1 160 ? -7.698  -9.039  25.405  1.00 16.64  ? 178 SER A OG   1 
ATOM   2400  H  H    . SER A 1 160 ? -8.531  -11.552 25.186  1.00 17.41  ? 178 SER A H    1 
ATOM   2401  H  HA   . SER A 1 160 ? -6.147  -11.535 24.037  1.00 17.57  ? 178 SER A HA   1 
ATOM   2402  H  HB2  . SER A 1 160 ? -6.243  -9.240  24.114  1.00 18.90  ? 178 SER A HB2  1 
ATOM   2403  H  HB3  . SER A 1 160 ? -7.640  -9.799  23.604  1.00 18.90  ? 178 SER A HB3  1 
ATOM   2404  H  HG   . SER A 1 160 ? -8.368  -9.475  25.662  1.00 19.97  ? 178 SER A HG   1 
ATOM   2405  N  N    . VAL A 1 161 ? -6.146  -11.427 27.171  1.00 16.36  ? 179 VAL A N    1 
ATOM   2406  C  CA   . VAL A 1 161 ? -5.243  -11.511 28.313  1.00 16.39  ? 179 VAL A CA   1 
ATOM   2407  C  C    . VAL A 1 161 ? -4.330  -12.721 28.170  1.00 16.05  ? 179 VAL A C    1 
ATOM   2408  O  O    . VAL A 1 161 ? -3.120  -12.623 28.388  1.00 16.38  ? 179 VAL A O    1 
ATOM   2409  C  CB   . VAL A 1 161 ? -6.042  -11.503 29.627  1.00 18.71  ? 179 VAL A CB   1 
ATOM   2410  C  CG1  . VAL A 1 161 ? -5.153  -11.829 30.813  1.00 19.07  ? 179 VAL A CG1  1 
ATOM   2411  C  CG2  . VAL A 1 161 ? -6.692  -10.140 29.824  1.00 19.68  ? 179 VAL A CG2  1 
ATOM   2412  H  H    . VAL A 1 161 ? -6.968  -11.611 27.347  1.00 19.63  ? 179 VAL A H    1 
ATOM   2413  H  HA   . VAL A 1 161 ? -4.672  -10.727 28.330  1.00 19.66  ? 179 VAL A HA   1 
ATOM   2414  H  HB   . VAL A 1 161 ? -6.730  -12.185 29.576  1.00 22.45  ? 179 VAL A HB   1 
ATOM   2415  H  HG11 . VAL A 1 161 ? -4.252  -11.521 30.626  1.00 22.88  ? 179 VAL A HG11 1 
ATOM   2416  H  HG12 . VAL A 1 161 ? -5.500  -11.381 31.600  1.00 22.88  ? 179 VAL A HG12 1 
ATOM   2417  H  HG13 . VAL A 1 161 ? -5.152  -12.789 30.952  1.00 22.88  ? 179 VAL A HG13 1 
ATOM   2418  H  HG21 . VAL A 1 161 ? -7.329  -10.196 30.553  1.00 23.62  ? 179 VAL A HG21 1 
ATOM   2419  H  HG22 . VAL A 1 161 ? -6.004  -9.490  30.035  1.00 23.62  ? 179 VAL A HG22 1 
ATOM   2420  H  HG23 . VAL A 1 161 ? -7.147  -9.886  29.006  1.00 23.62  ? 179 VAL A HG23 1 
ATOM   2421  N  N    . TRP A 1 162 ? -4.879  -13.866 27.744  1.00 15.91  ? 180 TRP A N    1 
ATOM   2422  C  CA   . TRP A 1 162 ? -4.023  -15.001 27.409  1.00 15.58  ? 180 TRP A CA   1 
ATOM   2423  C  C    . TRP A 1 162 ? -2.954  -14.588 26.410  1.00 14.82  ? 180 TRP A C    1 
ATOM   2424  O  O    . TRP A 1 162 ? -1.771  -14.913 26.564  1.00 16.22  ? 180 TRP A O    1 
ATOM   2425  C  CB   . TRP A 1 162 ? -4.852  -16.148 26.818  1.00 16.36  ? 180 TRP A CB   1 
ATOM   2426  C  CG   . TRP A 1 162 ? -5.588  -16.928 27.837  1.00 16.87  ? 180 TRP A CG   1 
ATOM   2427  C  CD1  . TRP A 1 162 ? -6.887  -16.766 28.211  1.00 16.85  ? 180 TRP A CD1  1 
ATOM   2428  C  CD2  . TRP A 1 162 ? -5.072  -18.005 28.628  1.00 18.53  ? 180 TRP A CD2  1 
ATOM   2429  N  NE1  . TRP A 1 162 ? -7.212  -17.672 29.189  1.00 17.92  ? 180 TRP A NE1  1 
ATOM   2430  C  CE2  . TRP A 1 162 ? -6.113  -18.442 29.465  1.00 19.19  ? 180 TRP A CE2  1 
ATOM   2431  C  CE3  . TRP A 1 162 ? -3.831  -18.641 28.707  1.00 20.95  ? 180 TRP A CE3  1 
ATOM   2432  C  CZ2  . TRP A 1 162 ? -5.954  -19.490 30.369  1.00 20.67  ? 180 TRP A CZ2  1 
ATOM   2433  C  CZ3  . TRP A 1 162 ? -3.678  -19.688 29.608  1.00 22.39  ? 180 TRP A CZ3  1 
ATOM   2434  C  CH2  . TRP A 1 162 ? -4.729  -20.092 30.430  1.00 22.19  ? 180 TRP A CH2  1 
ATOM   2435  H  H    . TRP A 1 162 ? -5.722  -14.004 27.644  1.00 19.09  ? 180 TRP A H    1 
ATOM   2436  H  HA   . TRP A 1 162 ? -3.603  -15.317 28.225  1.00 18.70  ? 180 TRP A HA   1 
ATOM   2437  H  HB2  . TRP A 1 162 ? -5.502  -15.778 26.200  1.00 19.63  ? 180 TRP A HB2  1 
ATOM   2438  H  HB3  . TRP A 1 162 ? -4.258  -16.755 26.350  1.00 19.63  ? 180 TRP A HB3  1 
ATOM   2439  H  HD1  . TRP A 1 162 ? -7.469  -16.134 27.856  1.00 20.22  ? 180 TRP A HD1  1 
ATOM   2440  H  HE1  . TRP A 1 162 ? -7.981  -17.745 29.567  1.00 21.51  ? 180 TRP A HE1  1 
ATOM   2441  H  HE3  . TRP A 1 162 ? -3.123  -18.370 28.169  1.00 25.14  ? 180 TRP A HE3  1 
ATOM   2442  H  HZ2  . TRP A 1 162 ? -6.657  -19.770 30.911  1.00 24.81  ? 180 TRP A HZ2  1 
ATOM   2443  H  HZ3  . TRP A 1 162 ? -2.860  -20.127 29.663  1.00 26.87  ? 180 TRP A HZ3  1 
ATOM   2444  H  HH2  . TRP A 1 162 ? -4.593  -20.786 31.034  1.00 26.63  ? 180 TRP A HH2  1 
ATOM   2445  N  N    . GLN A 1 163 ? -3.361  -13.866 25.367  1.00 15.09  ? 181 GLN A N    1 
ATOM   2446  C  CA   . GLN A 1 163 ? -2.453  -13.566 24.266  1.00 15.33  ? 181 GLN A CA   1 
ATOM   2447  C  C    . GLN A 1 163 ? -1.388  -12.558 24.665  1.00 14.53  ? 181 GLN A C    1 
ATOM   2448  O  O    . GLN A 1 163 ? -0.289  -12.570 24.104  1.00 16.06  ? 181 GLN A O    1 
ATOM   2449  C  CB   . GLN A 1 163 ? -3.255  -13.094 23.057  1.00 15.15  ? 181 GLN A CB   1 
ATOM   2450  C  CG   . GLN A 1 163 ? -4.163  -14.193 22.537  1.00 14.95  ? 181 GLN A CG   1 
ATOM   2451  C  CD   . GLN A 1 163 ? -5.187  -13.696 21.544  1.00 15.04  ? 181 GLN A CD   1 
ATOM   2452  O  OE1  . GLN A 1 163 ? -5.931  -12.751 21.824  1.00 16.21  ? 181 GLN A OE1  1 
ATOM   2453  N  NE2  . GLN A 1 163 ? -5.235  -14.330 20.371  1.00 16.09  ? 181 GLN A NE2  1 
ATOM   2454  H  H    . GLN A 1 163 ? -4.152  -13.540 25.274  1.00 18.11  ? 181 GLN A H    1 
ATOM   2455  H  HA   . GLN A 1 163 ? -1.983  -14.374 24.007  1.00 18.39  ? 181 GLN A HA   1 
ATOM   2456  H  HB2  . GLN A 1 163 ? -3.805  -12.336 23.311  1.00 18.18  ? 181 GLN A HB2  1 
ATOM   2457  H  HB3  . GLN A 1 163 ? -2.646  -12.838 22.347  1.00 18.18  ? 181 GLN A HB3  1 
ATOM   2458  H  HG2  . GLN A 1 163 ? -3.622  -14.866 22.096  1.00 17.95  ? 181 GLN A HG2  1 
ATOM   2459  H  HG3  . GLN A 1 163 ? -4.639  -14.587 23.284  1.00 17.95  ? 181 GLN A HG3  1 
ATOM   2460  H  HE21 . GLN A 1 163 ? -4.699  -14.984 20.214  1.00 19.31  ? 181 GLN A HE21 1 
ATOM   2461  H  HE22 . GLN A 1 163 ? -5.801  -14.084 19.772  1.00 19.31  ? 181 GLN A HE22 1 
ATOM   2462  N  N    . GLN A 1 164 ? -1.679  -11.701 25.635  1.00 15.58  ? 182 GLN A N    1 
ATOM   2463  C  CA   . GLN A 1 164 ? -0.716  -10.727 26.122  1.00 15.30  ? 182 GLN A CA   1 
ATOM   2464  C  C    . GLN A 1 164 ? 0.158   -11.254 27.256  1.00 15.88  ? 182 GLN A C    1 
ATOM   2465  O  O    . GLN A 1 164 ? 0.942   -10.491 27.820  1.00 16.24  ? 182 GLN A O    1 
ATOM   2466  C  CB   . GLN A 1 164 ? -1.442  -9.464  26.562  1.00 17.24  ? 182 GLN A CB   1 
ATOM   2467  C  CG   . GLN A 1 164 ? -2.065  -8.744  25.407  1.00 18.56  ? 182 GLN A CG   1 
ATOM   2468  C  CD   . GLN A 1 164 ? -2.937  -7.602  25.855  1.00 19.36  ? 182 GLN A CD   1 
ATOM   2469  O  OE1  . GLN A 1 164 ? -4.154  -7.755  26.026  1.00 21.52  ? 182 GLN A OE1  1 
ATOM   2470  N  NE2  . GLN A 1 164 ? -2.326  -6.449  26.061  1.00 17.41  ? 182 GLN A NE2  1 
ATOM   2471  H  H    . GLN A 1 164 ? -2.441  -11.664 26.032  1.00 18.69  ? 182 GLN A H    1 
ATOM   2472  H  HA   . GLN A 1 164 ? -0.120  -10.494 25.393  1.00 18.36  ? 182 GLN A HA   1 
ATOM   2473  H  HB2  . GLN A 1 164 ? -2.145  -9.701  27.186  1.00 20.69  ? 182 GLN A HB2  1 
ATOM   2474  H  HB3  . GLN A 1 164 ? -0.809  -8.864  26.987  1.00 20.69  ? 182 GLN A HB3  1 
ATOM   2475  H  HG2  . GLN A 1 164 ? -1.364  -8.385  24.840  1.00 22.27  ? 182 GLN A HG2  1 
ATOM   2476  H  HG3  . GLN A 1 164 ? -2.614  -9.365  24.903  1.00 22.27  ? 182 GLN A HG3  1 
ATOM   2477  H  HE21 . GLN A 1 164 ? -1.477  -6.384  25.938  1.00 20.89  ? 182 GLN A HE21 1 
ATOM   2478  H  HE22 . GLN A 1 164 ? -2.776  -5.763  26.318  1.00 20.89  ? 182 GLN A HE22 1 
ATOM   2479  N  N    . THR A 1 165 ? 0.054   -12.530 27.595  1.00 16.13  ? 183 THR A N    1 
ATOM   2480  C  CA   . THR A 1 165 ? 0.929   -13.118 28.595  1.00 17.06  ? 183 THR A CA   1 
ATOM   2481  C  C    . THR A 1 165 ? 2.248   -13.492 27.935  1.00 15.82  ? 183 THR A C    1 
ATOM   2482  O  O    . THR A 1 165 ? 2.263   -14.076 26.853  1.00 16.57  ? 183 THR A O    1 
ATOM   2483  C  CB   . THR A 1 165 ? 0.270   -14.363 29.181  1.00 19.91  ? 183 THR A CB   1 
ATOM   2484  O  OG1  . THR A 1 165 ? -1.030  -14.025 29.681  1.00 20.93  ? 183 THR A OG1  1 
ATOM   2485  C  CG2  . THR A 1 165 ? 1.112   -14.930 30.307  1.00 20.72  ? 183 THR A CG2  1 
ATOM   2486  H  H    . THR A 1 165 ? -0.518  -13.078 27.259  1.00 19.36  ? 183 THR A H    1 
ATOM   2487  H  HA   . THR A 1 165 ? 1.099   -12.488 29.313  1.00 20.48  ? 183 THR A HA   1 
ATOM   2488  H  HB   . THR A 1 165 ? 0.185   -15.041 28.493  1.00 23.89  ? 183 THR A HB   1 
ATOM   2489  H  HG1  . THR A 1 165 ? -0.960  -13.509 30.339  1.00 25.12  ? 183 THR A HG1  1 
ATOM   2490  H  HG21 . THR A 1 165 ? 1.258   -14.252 30.985  1.00 24.87  ? 183 THR A HG21 1 
ATOM   2491  H  HG22 . THR A 1 165 ? 0.659   -15.687 30.711  1.00 24.87  ? 183 THR A HG22 1 
ATOM   2492  H  HG23 . THR A 1 165 ? 1.970   -15.223 29.964  1.00 24.87  ? 183 THR A HG23 1 
ATOM   2493  N  N    . THR A 1 166 ? 3.357   -13.142 28.571  1.00 17.98  ? 184 THR A N    1 
ATOM   2494  C  CA   . THR A 1 166 ? 4.649   -13.519 28.016  1.00 19.86  ? 184 THR A CA   1 
ATOM   2495  C  C    . THR A 1 166 ? 4.705   -15.033 27.830  1.00 18.40  ? 184 THR A C    1 
ATOM   2496  O  O    . THR A 1 166 ? 4.210   -15.800 28.660  1.00 20.57  ? 184 THR A O    1 
ATOM   2497  C  CB   . THR A 1 166 ? 5.760   -13.001 28.927  1.00 23.68  ? 184 THR A CB   1 
ATOM   2498  O  OG1  . THR A 1 166 ? 5.753   -11.560 28.890  1.00 26.25  ? 184 THR A OG1  1 
ATOM   2499  C  CG2  . THR A 1 166 ? 7.115   -13.516 28.487  1.00 24.55  ? 184 THR A CG2  1 
ATOM   2500  H  H    . THR A 1 166 ? 3.389   -12.698 29.306  1.00 21.58  ? 184 THR A H    1 
ATOM   2501  H  HA   . THR A 1 166 ? 4.790   -13.120 27.143  1.00 23.83  ? 184 THR A HA   1 
ATOM   2502  H  HB   . THR A 1 166 ? 5.612   -13.312 29.834  1.00 28.41  ? 184 THR A HB   1 
ATOM   2503  H  HG1  . THR A 1 166 ? 5.881   -11.292 28.104  1.00 31.50  ? 184 THR A HG1  1 
ATOM   2504  H  HG21 . THR A 1 166 ? 7.215   -14.446 28.744  1.00 29.46  ? 184 THR A HG21 1 
ATOM   2505  H  HG22 . THR A 1 166 ? 7.200   -13.443 27.524  1.00 29.46  ? 184 THR A HG22 1 
ATOM   2506  H  HG23 . THR A 1 166 ? 7.819   -12.996 28.906  1.00 29.46  ? 184 THR A HG23 1 
ATOM   2507  N  N    . GLY A 1 167 ? 5.261   -15.457 26.698  1.00 17.64  ? 185 GLY A N    1 
ATOM   2508  C  CA   . GLY A 1 167 ? 5.290   -16.855 26.321  1.00 18.04  ? 185 GLY A CA   1 
ATOM   2509  C  C    . GLY A 1 167 ? 4.089   -17.336 25.532  1.00 17.14  ? 185 GLY A C    1 
ATOM   2510  O  O    . GLY A 1 167 ? 4.084   -18.495 25.087  1.00 18.86  ? 185 GLY A O    1 
ATOM   2511  H  H    . GLY A 1 167 ? 5.636   -14.939 26.123  1.00 21.16  ? 185 GLY A H    1 
ATOM   2512  H  HA2  . GLY A 1 167 ? 6.079   -17.013 25.780  1.00 21.65  ? 185 GLY A HA2  1 
ATOM   2513  H  HA3  . GLY A 1 167 ? 5.347   -17.391 27.127  1.00 21.65  ? 185 GLY A HA3  1 
ATOM   2514  N  N    . SER A 1 168 ? 3.086   -16.487 25.330  1.00 16.60  ? 186 SER A N    1 
ATOM   2515  C  CA   . SER A 1 168 ? 1.884   -16.882 24.616  1.00 15.52  ? 186 SER A CA   1 
ATOM   2516  C  C    . SER A 1 168 ? 2.211   -17.270 23.180  1.00 15.06  ? 186 SER A C    1 
ATOM   2517  O  O    . SER A 1 168 ? 3.233   -16.875 22.613  1.00 15.71  ? 186 SER A O    1 
ATOM   2518  C  CB   . SER A 1 168 ? 0.879   -15.725 24.590  1.00 14.94  ? 186 SER A CB   1 
ATOM   2519  O  OG   . SER A 1 168 ? 1.379   -14.621 23.843  1.00 15.09  ? 186 SER A OG   1 
ATOM   2520  H  H    . SER A 1 168 ? 3.079   -15.671 25.600  1.00 19.92  ? 186 SER A H    1 
ATOM   2521  H  HA   . SER A 1 168 ? 1.487   -17.644 25.067  1.00 18.62  ? 186 SER A HA   1 
ATOM   2522  H  HB2  . SER A 1 168 ? 0.056   -16.034 24.180  1.00 17.92  ? 186 SER A HB2  1 
ATOM   2523  H  HB3  . SER A 1 168 ? 0.709   -15.437 25.501  1.00 17.92  ? 186 SER A HB3  1 
ATOM   2524  H  HG   . SER A 1 168 ? 0.807   -14.006 23.822  1.00 18.11  ? 186 SER A HG   1 
ATOM   2525  N  N    . ALA A 1 169 ? 1.304   -18.041 22.580  1.00 15.02  ? 187 ALA A N    1 
ATOM   2526  C  CA   . ALA A 1 169 ? 1.454   -18.380 21.169  1.00 14.94  ? 187 ALA A CA   1 
ATOM   2527  C  C    . ALA A 1 169 ? 1.463   -17.122 20.305  1.00 14.45  ? 187 ALA A C    1 
ATOM   2528  O  O    . ALA A 1 169 ? 2.241   -17.023 19.349  1.00 15.17  ? 187 ALA A O    1 
ATOM   2529  C  CB   . ALA A 1 169 ? 0.343   -19.339 20.733  1.00 15.88  ? 187 ALA A CB   1 
ATOM   2530  H  H    . ALA A 1 169 ? 0.608   -18.373 22.960  1.00 18.03  ? 187 ALA A H    1 
ATOM   2531  H  HA   . ALA A 1 169 ? 2.300   -18.838 21.041  1.00 17.92  ? 187 ALA A HA   1 
ATOM   2532  H  HB1  . ALA A 1 169 ? -0.511  -18.884 20.802  1.00 19.06  ? 187 ALA A HB1  1 
ATOM   2533  H  HB2  . ALA A 1 169 ? 0.500   -19.607 19.814  1.00 19.06  ? 187 ALA A HB2  1 
ATOM   2534  H  HB3  . ALA A 1 169 ? 0.352   -20.117 21.311  1.00 19.06  ? 187 ALA A HB3  1 
ATOM   2535  N  N    . LEU A 1 170 ? 0.620   -16.142 20.640  1.00 14.57  ? 188 LEU A N    1 
ATOM   2536  C  CA   . LEU A 1 170 ? 0.549   -14.924 19.841  1.00 14.65  ? 188 LEU A CA   1 
ATOM   2537  C  C    . LEU A 1 170 ? 1.864   -14.150 19.893  1.00 14.56  ? 188 LEU A C    1 
ATOM   2538  O  O    . LEU A 1 170 ? 2.416   -13.772 18.852  1.00 14.61  ? 188 LEU A O    1 
ATOM   2539  C  CB   . LEU A 1 170 ? -0.620  -14.052 20.307  1.00 15.12  ? 188 LEU A CB   1 
ATOM   2540  C  CG   . LEU A 1 170 ? -0.832  -12.822 19.421  1.00 16.55  ? 188 LEU A CG   1 
ATOM   2541  C  CD1  . LEU A 1 170 ? -2.227  -12.817 18.821  1.00 17.55  ? 188 LEU A CD1  1 
ATOM   2542  C  CD2  . LEU A 1 170 ? -0.572  -11.525 20.189  1.00 19.10  ? 188 LEU A CD2  1 
ATOM   2543  H  H    . LEU A 1 170 ? 0.087   -16.160 21.315  1.00 17.49  ? 188 LEU A H    1 
ATOM   2544  H  HA   . LEU A 1 170 ? 0.386   -15.168 18.917  1.00 17.57  ? 188 LEU A HA   1 
ATOM   2545  H  HB2  . LEU A 1 170 ? -1.433  -14.580 20.289  1.00 18.14  ? 188 LEU A HB2  1 
ATOM   2546  H  HB3  . LEU A 1 170 ? -0.444  -13.745 21.210  1.00 18.14  ? 188 LEU A HB3  1 
ATOM   2547  H  HG   . LEU A 1 170 ? -0.193  -12.863 18.692  1.00 19.87  ? 188 LEU A HG   1 
ATOM   2548  H  HD11 . LEU A 1 170 ? -2.413  -13.692 18.448  1.00 21.06  ? 188 LEU A HD11 1 
ATOM   2549  H  HD12 . LEU A 1 170 ? -2.869  -12.611 19.518  1.00 21.06  ? 188 LEU A HD12 1 
ATOM   2550  H  HD13 . LEU A 1 170 ? -2.268  -12.144 18.124  1.00 21.06  ? 188 LEU A HD13 1 
ATOM   2551  H  HD21 . LEU A 1 170 ? 0.334   -11.540 20.536  1.00 22.92  ? 188 LEU A HD21 1 
ATOM   2552  H  HD22 . LEU A 1 170 ? -0.683  -10.773 19.587  1.00 22.92  ? 188 LEU A HD22 1 
ATOM   2553  H  HD23 . LEU A 1 170 ? -1.205  -11.460 20.922  1.00 22.92  ? 188 LEU A HD23 1 
ATOM   2554  N  N    . THR A 1 171 ? 2.391   -13.901 21.098  1.00 14.12  ? 189 THR A N    1 
ATOM   2555  C  CA   . THR A 1 171 ? 3.640   -13.144 21.173  1.00 14.66  ? 189 THR A CA   1 
ATOM   2556  C  C    . THR A 1 171 ? 4.798   -13.932 20.571  1.00 14.55  ? 189 THR A C    1 
ATOM   2557  O  O    . THR A 1 171 ? 5.701   -13.340 19.971  1.00 15.64  ? 189 THR A O    1 
ATOM   2558  C  CB   . THR A 1 171 ? 3.965   -12.685 22.599  1.00 15.32  ? 189 THR A CB   1 
ATOM   2559  O  OG1  . THR A 1 171 ? 4.066   -13.806 23.482  1.00 16.90  ? 189 THR A OG1  1 
ATOM   2560  C  CG2  . THR A 1 171 ? 2.913   -11.686 23.110  1.00 16.31  ? 189 THR A CG2  1 
ATOM   2561  H  H    . THR A 1 171 ? 2.060   -14.149 21.852  1.00 16.94  ? 189 THR A H    1 
ATOM   2562  H  HA   . THR A 1 171 ? 3.521   -12.328 20.661  1.00 17.60  ? 189 THR A HA   1 
ATOM   2563  H  HB   . THR A 1 171 ? 4.822   -12.231 22.595  1.00 18.38  ? 189 THR A HB   1 
ATOM   2564  H  HG1  . THR A 1 171 ? 3.318   -14.181 23.557  1.00 20.28  ? 189 THR A HG1  1 
ATOM   2565  H  HG21 . THR A 1 171 ? 2.030   -12.085 23.069  1.00 19.58  ? 189 THR A HG21 1 
ATOM   2566  H  HG22 . THR A 1 171 ? 3.107   -11.441 24.028  1.00 19.58  ? 189 THR A HG22 1 
ATOM   2567  H  HG23 . THR A 1 171 ? 2.923   -10.886 22.562  1.00 19.58  ? 189 THR A HG23 1 
ATOM   2568  N  N    . THR A 1 172 ? 4.788   -15.259 20.721  1.00 15.43  ? 190 THR A N    1 
ATOM   2569  C  CA   . THR A 1 172 ? 5.793   -16.088 20.067  1.00 14.84  ? 190 THR A CA   1 
ATOM   2570  C  C    . THR A 1 172 ? 5.739   -15.905 18.555  1.00 14.29  ? 190 THR A C    1 
ATOM   2571  O  O    . THR A 1 172 ? 6.767   -15.695 17.902  1.00 15.31  ? 190 THR A O    1 
ATOM   2572  C  CB   . THR A 1 172 ? 5.555   -17.556 20.420  1.00 16.47  ? 190 THR A CB   1 
ATOM   2573  O  OG1  . THR A 1 172 ? 5.691   -17.735 21.836  1.00 17.62  ? 190 THR A OG1  1 
ATOM   2574  C  CG2  . THR A 1 172 ? 6.542   -18.454 19.677  1.00 17.63  ? 190 THR A CG2  1 
ATOM   2575  H  H    . THR A 1 172 ? 4.216   -15.697 21.192  1.00 18.52  ? 190 THR A H    1 
ATOM   2576  H  HA   . THR A 1 172 ? 6.673   -15.829 20.382  1.00 17.81  ? 190 THR A HA   1 
ATOM   2577  H  HB   . THR A 1 172 ? 4.660   -17.818 20.155  1.00 19.77  ? 190 THR A HB   1 
ATOM   2578  H  HG1  . THR A 1 172 ? 5.526   -18.533 22.041  1.00 21.14  ? 190 THR A HG1  1 
ATOM   2579  H  HG21 . THR A 1 172 ? 7.451   -18.158 19.845  1.00 21.16  ? 190 THR A HG21 1 
ATOM   2580  H  HG22 . THR A 1 172 ? 6.449   -19.371 19.979  1.00 21.16  ? 190 THR A HG22 1 
ATOM   2581  H  HG23 . THR A 1 172 ? 6.370   -18.417 18.723  1.00 21.16  ? 190 THR A HG23 1 
ATOM   2582  N  N    . ALA A 1 173 ? 4.536   -15.986 17.985  1.00 14.69  ? 191 ALA A N    1 
ATOM   2583  C  CA   . ALA A 1 173 ? 4.390   -15.878 16.540  1.00 14.19  ? 191 ALA A CA   1 
ATOM   2584  C  C    . ALA A 1 173 ? 4.848   -14.514 16.039  1.00 14.20  ? 191 ALA A C    1 
ATOM   2585  O  O    . ALA A 1 173 ? 5.505   -14.418 14.995  1.00 16.12  ? 191 ALA A O    1 
ATOM   2586  C  CB   . ALA A 1 173 ? 2.935   -16.141 16.156  1.00 14.91  ? 191 ALA A CB   1 
ATOM   2587  H  H    . ALA A 1 173 ? 3.797   -16.102 18.409  1.00 17.63  ? 191 ALA A H    1 
ATOM   2588  H  HA   . ALA A 1 173 ? 4.944   -16.547 16.109  1.00 17.03  ? 191 ALA A HA   1 
ATOM   2589  H  HB1  . ALA A 1 173 ? 2.371   -15.476 16.581  1.00 17.89  ? 191 ALA A HB1  1 
ATOM   2590  H  HB2  . ALA A 1 173 ? 2.847   -16.083 15.192  1.00 17.89  ? 191 ALA A HB2  1 
ATOM   2591  H  HB3  . ALA A 1 173 ? 2.684   -17.028 16.458  1.00 17.89  ? 191 ALA A HB3  1 
ATOM   2592  N  N    . LEU A 1 174 ? 4.505   -13.444 16.763  1.00 14.08  ? 192 LEU A N    1 
ATOM   2593  C  CA   . LEU A 1 174 ? 4.928   -12.106 16.353  1.00 15.13  ? 192 LEU A CA   1 
ATOM   2594  C  C    . LEU A 1 174 ? 6.448   -12.019 16.281  1.00 15.08  ? 192 LEU A C    1 
ATOM   2595  O  O    . LEU A 1 174 ? 7.016   -11.533 15.296  1.00 16.39  ? 192 LEU A O    1 
ATOM   2596  C  CB   . LEU A 1 174 ? 4.378   -11.063 17.328  1.00 15.14  ? 192 LEU A CB   1 
ATOM   2597  C  CG   . LEU A 1 174 ? 4.739   -9.607  17.016  1.00 16.06  ? 192 LEU A CG   1 
ATOM   2598  C  CD1  . LEU A 1 174 ? 4.126   -9.196  15.680  1.00 17.76  ? 192 LEU A CD1  1 
ATOM   2599  C  CD2  . LEU A 1 174 ? 4.291   -8.655  18.124  1.00 17.56  ? 192 LEU A CD2  1 
ATOM   2600  H  H    . LEU A 1 174 ? 4.035   -13.466 17.483  1.00 16.90  ? 192 LEU A H    1 
ATOM   2601  H  HA   . LEU A 1 174 ? 4.569   -11.916 15.472  1.00 18.16  ? 192 LEU A HA   1 
ATOM   2602  H  HB2  . LEU A 1 174 ? 3.410   -11.127 17.327  1.00 18.16  ? 192 LEU A HB2  1 
ATOM   2603  H  HB3  . LEU A 1 174 ? 4.722   -11.263 18.213  1.00 18.16  ? 192 LEU A HB3  1 
ATOM   2604  H  HG   . LEU A 1 174 ? 5.705   -9.537  16.958  1.00 19.28  ? 192 LEU A HG   1 
ATOM   2605  H  HD11 . LEU A 1 174 ? 3.166   -9.330  15.719  1.00 21.31  ? 192 LEU A HD11 1 
ATOM   2606  H  HD12 . LEU A 1 174 ? 4.322   -8.260  15.517  1.00 21.31  ? 192 LEU A HD12 1 
ATOM   2607  H  HD13 . LEU A 1 174 ? 4.508   -9.742  14.975  1.00 21.31  ? 192 LEU A HD13 1 
ATOM   2608  H  HD21 . LEU A 1 174 ? 4.626   -7.765  17.930  1.00 21.07  ? 192 LEU A HD21 1 
ATOM   2609  H  HD22 . LEU A 1 174 ? 3.322   -8.643  18.158  1.00 21.07  ? 192 LEU A HD22 1 
ATOM   2610  H  HD23 . LEU A 1 174 ? 4.648   -8.966  18.971  1.00 21.07  ? 192 LEU A HD23 1 
ATOM   2611  N  N    . ARG A 1 175 ? 7.124   -12.498 17.319  1.00 15.01  ? 193 ARG A N    1 
ATOM   2612  C  CA   . ARG A 1 175 ? 8.582   -12.448 17.347  1.00 15.16  ? 193 ARG A CA   1 
ATOM   2613  C  C    . ARG A 1 175 ? 9.188   -13.306 16.240  1.00 15.78  ? 193 ARG A C    1 
ATOM   2614  O  O    . ARG A 1 175 ? 10.113  -12.876 15.541  1.00 17.20  ? 193 ARG A O    1 
ATOM   2615  C  CB   . ARG A 1 175 ? 9.061   -12.921 18.717  1.00 16.35  ? 193 ARG A CB   1 
ATOM   2616  C  CG   . ARG A 1 175 ? 10.559  -12.940 18.876  1.00 19.06  ? 193 ARG A CG   1 
ATOM   2617  C  CD   . ARG A 1 175 ? 10.939  -13.380 20.280  1.00 21.44  ? 193 ARG A CD   1 
ATOM   2618  N  NE   . ARG A 1 175 ? 10.821  -14.828 20.425  1.00 24.61  ? 193 ARG A NE   1 
ATOM   2619  C  CZ   . ARG A 1 175 ? 9.915   -15.451 21.174  1.00 27.08  ? 193 ARG A CZ   1 
ATOM   2620  N  NH1  . ARG A 1 175 ? 9.022   -14.769 21.883  1.00 27.33  ? 193 ARG A NH1  1 
ATOM   2621  N  NH2  . ARG A 1 175 ? 9.913   -16.776 21.216  1.00 28.93  ? 193 ARG A NH2  1 
ATOM   2622  H  H    . ARG A 1 175 ? 6.767   -12.856 18.015  1.00 18.02  ? 193 ARG A H    1 
ATOM   2623  H  HA   . ARG A 1 175 ? 8.877   -11.536 17.203  1.00 18.20  ? 193 ARG A HA   1 
ATOM   2624  H  HB2  . ARG A 1 175 ? 8.701   -12.325 19.394  1.00 19.63  ? 193 ARG A HB2  1 
ATOM   2625  H  HB3  . ARG A 1 175 ? 8.738   -13.823 18.865  1.00 19.63  ? 193 ARG A HB3  1 
ATOM   2626  H  HG2  . ARG A 1 175 ? 10.945  -13.563 18.241  1.00 22.87  ? 193 ARG A HG2  1 
ATOM   2627  H  HG3  . ARG A 1 175 ? 10.913  -12.049 18.725  1.00 22.87  ? 193 ARG A HG3  1 
ATOM   2628  H  HD2  . ARG A 1 175 ? 11.858  -13.128 20.459  1.00 25.73  ? 193 ARG A HD2  1 
ATOM   2629  H  HD3  . ARG A 1 175 ? 10.347  -12.958 20.922  1.00 25.73  ? 193 ARG A HD3  1 
ATOM   2630  H  HE   . ARG A 1 175 ? 11.381  -15.316 19.992  1.00 29.53  ? 193 ARG A HE   1 
ATOM   2631  H  HH11 . ARG A 1 175 ? 9.023   -13.909 21.863  1.00 32.80  ? 193 ARG A HH11 1 
ATOM   2632  H  HH12 . ARG A 1 175 ? 8.443   -15.188 22.362  1.00 32.80  ? 193 ARG A HH12 1 
ATOM   2633  H  HH21 . ARG A 1 175 ? 10.492  -17.222 20.763  1.00 34.71  ? 193 ARG A HH21 1 
ATOM   2634  H  HH22 . ARG A 1 175 ? 9.332   -17.190 21.697  1.00 34.71  ? 193 ARG A HH22 1 
ATOM   2635  N  N    . ASN A 1 176 ? 8.686   -14.531 16.070  1.00 15.40  ? 194 ASN A N    1 
ATOM   2636  C  CA   . ASN A 1 176 ? 9.276   -15.436 15.088  1.00 16.09  ? 194 ASN A CA   1 
ATOM   2637  C  C    . ASN A 1 176 ? 9.033   -14.965 13.658  1.00 16.99  ? 194 ASN A C    1 
ATOM   2638  O  O    . ASN A 1 176 ? 9.819   -15.293 12.763  1.00 18.72  ? 194 ASN A O    1 
ATOM   2639  C  CB   . ASN A 1 176 ? 8.744   -16.856 15.290  1.00 16.26  ? 194 ASN A CB   1 
ATOM   2640  C  CG   . ASN A 1 176 ? 9.397   -17.565 16.471  1.00 18.35  ? 194 ASN A CG   1 
ATOM   2641  O  OD1  . ASN A 1 176 ? 10.489  -17.196 16.913  1.00 18.95  ? 194 ASN A OD1  1 
ATOM   2642  N  ND2  . ASN A 1 176 ? 8.729   -18.594 16.982  1.00 19.86  ? 194 ASN A ND2  1 
ATOM   2643  H  H    . ASN A 1 176 ? 8.017   -14.855 16.503  1.00 18.48  ? 194 ASN A H    1 
ATOM   2644  H  HA   . ASN A 1 176 ? 10.236  -15.469 15.224  1.00 19.31  ? 194 ASN A HA   1 
ATOM   2645  H  HB2  . ASN A 1 176 ? 7.789   -16.816 15.454  1.00 19.52  ? 194 ASN A HB2  1 
ATOM   2646  H  HB3  . ASN A 1 176 ? 8.922   -17.378 14.492  1.00 19.52  ? 194 ASN A HB3  1 
ATOM   2647  H  HD21 . ASN A 1 176 ? 9.053   -19.028 17.650  1.00 23.83  ? 194 ASN A HD21 1 
ATOM   2648  H  HD22 . ASN A 1 176 ? 7.972   -18.825 16.645  1.00 23.83  ? 194 ASN A HD22 1 
ATOM   2649  N  N    . ALA A 1 177 ? 7.983   -14.183 13.430  1.00 17.52  ? 195 ALA A N    1 
ATOM   2650  C  CA   . ALA A 1 177 ? 7.690   -13.670 12.102  1.00 18.65  ? 195 ALA A CA   1 
ATOM   2651  C  C    . ALA A 1 177 ? 8.463   -12.400 11.773  1.00 19.50  ? 195 ALA A C    1 
ATOM   2652  O  O    . ALA A 1 177 ? 8.361   -11.911 10.645  1.00 21.05  ? 195 ALA A O    1 
ATOM   2653  C  CB   . ALA A 1 177 ? 6.190   -13.395 11.974  1.00 17.42  ? 195 ALA A CB   1 
ATOM   2654  H  H    . ALA A 1 177 ? 7.423   -13.935 14.033  1.00 21.02  ? 195 ALA A H    1 
ATOM   2655  H  HA   . ALA A 1 177 ? 7.933   -14.345 11.449  1.00 22.38  ? 195 ALA A HA   1 
ATOM   2656  H  HB1  . ALA A 1 177 ? 5.704   -14.222 12.118  1.00 20.90  ? 195 ALA A HB1  1 
ATOM   2657  H  HB2  . ALA A 1 177 ? 5.931   -12.739 12.640  1.00 20.90  ? 195 ALA A HB2  1 
ATOM   2658  H  HB3  . ALA A 1 177 ? 6.006   -13.054 11.084  1.00 20.90  ? 195 ALA A HB3  1 
ATOM   2659  N  N    . GLY A 1 178 ? 9.213   -11.846 12.719  1.00 19.43  ? 196 GLY A N    1 
ATOM   2660  C  CA   . GLY A 1 178 ? 9.977   -10.639 12.487  1.00 19.77  ? 196 GLY A CA   1 
ATOM   2661  C  C    . GLY A 1 178 ? 9.398   -9.377  13.082  1.00 19.32  ? 196 GLY A C    1 
ATOM   2662  O  O    . GLY A 1 178 ? 9.925   -8.288  12.815  1.00 20.17  ? 196 GLY A O    1 
ATOM   2663  H  H    . GLY A 1 178 ? 9.294   -12.160 13.516  1.00 23.32  ? 196 GLY A H    1 
ATOM   2664  H  HA2  . GLY A 1 178 ? 10.864  -10.758 12.861  1.00 23.72  ? 196 GLY A HA2  1 
ATOM   2665  H  HA3  . GLY A 1 178 ? 10.054  -10.502 11.530  1.00 23.72  ? 196 GLY A HA3  1 
ATOM   2666  N  N    . GLY A 1 179 ? 8.357   -9.488  13.904  1.00 19.13  ? 197 GLY A N    1 
ATOM   2667  C  CA   . GLY A 1 179 ? 7.588   -8.352  14.359  1.00 19.20  ? 197 GLY A CA   1 
ATOM   2668  C  C    . GLY A 1 179 ? 8.164   -7.537  15.493  1.00 17.41  ? 197 GLY A C    1 
ATOM   2669  O  O    . GLY A 1 179 ? 7.551   -6.542  15.883  1.00 17.67  ? 197 GLY A O    1 
ATOM   2670  H  H    . GLY A 1 179 ? 8.074   -10.236 14.219  1.00 22.95  ? 197 GLY A H    1 
ATOM   2671  H  HA2  . GLY A 1 179 ? 7.466   -7.750  13.608  1.00 23.04  ? 197 GLY A HA2  1 
ATOM   2672  H  HA3  . GLY A 1 179 ? 6.720   -8.673  14.650  1.00 23.04  ? 197 GLY A HA3  1 
ATOM   2673  N  N    . LEU A 1 180 ? 9.306   -7.911  16.061  1.00 17.14  ? 198 LEU A N    1 
ATOM   2674  C  CA   . LEU A 1 180 ? 9.946   -7.079  17.076  1.00 15.64  ? 198 LEU A CA   1 
ATOM   2675  C  C    . LEU A 1 180 ? 10.987  -6.132  16.482  1.00 15.83  ? 198 LEU A C    1 
ATOM   2676  O  O    . LEU A 1 180 ? 11.745  -5.495  17.228  1.00 15.47  ? 198 LEU A O    1 
ATOM   2677  C  CB   . LEU A 1 180 ? 10.512  -7.938  18.208  1.00 15.47  ? 198 LEU A CB   1 
ATOM   2678  C  CG   . LEU A 1 180 ? 9.463   -8.806  18.914  1.00 16.25  ? 198 LEU A CG   1 
ATOM   2679  C  CD1  . LEU A 1 180 ? 10.006  -9.387  20.207  1.00 16.25  ? 198 LEU A CD1  1 
ATOM   2680  C  CD2  . LEU A 1 180 ? 8.176   -8.040  19.200  1.00 17.81  ? 198 LEU A CD2  1 
ATOM   2681  H  H    . LEU A 1 180 ? 9.727   -8.638  15.877  1.00 20.57  ? 198 LEU A H    1 
ATOM   2682  H  HA   . LEU A 1 180 ? 9.276   -6.517  17.496  1.00 18.76  ? 198 LEU A HA   1 
ATOM   2683  H  HB2  . LEU A 1 180 ? 11.187  -8.530  17.841  1.00 18.56  ? 198 LEU A HB2  1 
ATOM   2684  H  HB3  . LEU A 1 180 ? 10.908  -7.354  18.873  1.00 18.56  ? 198 LEU A HB3  1 
ATOM   2685  H  HG   . LEU A 1 180 ? 9.247   -9.533  18.309  1.00 19.51  ? 198 LEU A HG   1 
ATOM   2686  H  HD11 . LEU A 1 180 ? 10.795  -9.916  20.008  1.00 19.50  ? 198 LEU A HD11 1 
ATOM   2687  H  HD12 . LEU A 1 180 ? 10.237  -8.661  20.807  1.00 19.50  ? 198 LEU A HD12 1 
ATOM   2688  H  HD13 . LEU A 1 180 ? 9.326   -9.947  20.612  1.00 19.50  ? 198 LEU A HD13 1 
ATOM   2689  H  HD21 . LEU A 1 180 ? 7.704   -7.893  18.365  1.00 21.37  ? 198 LEU A HD21 1 
ATOM   2690  H  HD22 . LEU A 1 180 ? 7.625   -8.563  19.803  1.00 21.37  ? 198 LEU A HD22 1 
ATOM   2691  H  HD23 . LEU A 1 180 ? 8.399   -7.190  19.609  1.00 21.37  ? 198 LEU A HD23 1 
ATOM   2692  N  N    . THR A 1 181 ? 11.022  -6.013  15.160  1.00 15.76  ? 199 THR A N    1 
ATOM   2693  C  CA   . THR A 1 181 ? 11.721  -4.942  14.466  1.00 14.52  ? 199 THR A CA   1 
ATOM   2694  C  C    . THR A 1 181 ? 10.664  -4.021  13.866  1.00 15.67  ? 199 THR A C    1 
ATOM   2695  O  O    . THR A 1 181 ? 9.621   -4.486  13.401  1.00 16.79  ? 199 THR A O    1 
ATOM   2696  C  CB   . THR A 1 181 ? 12.614  -5.529  13.371  1.00 16.16  ? 199 THR A CB   1 
ATOM   2697  O  OG1  . THR A 1 181 ? 13.629  -6.350  13.968  1.00 18.07  ? 199 THR A OG1  1 
ATOM   2698  C  CG2  . THR A 1 181 ? 13.270  -4.428  12.561  1.00 17.34  ? 199 THR A CG2  1 
ATOM   2699  H  H    . THR A 1 181 ? 10.633  -6.562  14.624  1.00 18.91  ? 199 THR A H    1 
ATOM   2700  H  HA   . THR A 1 181 ? 12.287  -4.427  15.062  1.00 17.43  ? 199 THR A HA   1 
ATOM   2701  H  HB   . THR A 1 181 ? 12.074  -6.066  12.770  1.00 19.40  ? 199 THR A HB   1 
ATOM   2702  H  HG1  . THR A 1 181 ? 13.274  -6.972  14.406  1.00 21.68  ? 199 THR A HG1  1 
ATOM   2703  H  HG21 . THR A 1 181 ? 13.920  -4.808  11.950  1.00 20.80  ? 199 THR A HG21 1 
ATOM   2704  H  HG22 . THR A 1 181 ? 12.600  -3.949  12.050  1.00 20.80  ? 199 THR A HG22 1 
ATOM   2705  H  HG23 . THR A 1 181 ? 13.720  -3.805  13.153  1.00 20.80  ? 199 THR A HG23 1 
ATOM   2706  N  N    . GLN A 1 182 ? 10.898  -2.713  13.917  1.00 15.96  ? 200 GLN A N    1 
ATOM   2707  C  CA   . GLN A 1 182 ? 9.883   -1.802  13.402  1.00 16.07  ? 200 GLN A CA   1 
ATOM   2708  C  C    . GLN A 1 182 ? 9.667   -2.043  11.912  1.00 16.39  ? 200 GLN A C    1 
ATOM   2709  O  O    . GLN A 1 182 ? 10.573  -2.464  11.186  1.00 16.52  ? 200 GLN A O    1 
ATOM   2710  C  CB   . GLN A 1 182 ? 10.246  -0.338  13.666  1.00 16.61  ? 200 GLN A CB   1 
ATOM   2711  C  CG   . GLN A 1 182 ? 11.344  0.214   12.791  1.00 17.26  ? 200 GLN A CG   1 
ATOM   2712  C  CD   . GLN A 1 182 ? 11.408  1.729   12.823  1.00 17.11  ? 200 GLN A CD   1 
ATOM   2713  O  OE1  . GLN A 1 182 ? 10.884  2.374   13.735  1.00 16.75  ? 200 GLN A OE1  1 
ATOM   2714  N  NE2  . GLN A 1 182 ? 12.068  2.303   11.833  1.00 19.23  ? 200 GLN A NE2  1 
ATOM   2715  H  H    . GLN A 1 182 ? 11.608  -2.343  14.232  1.00 19.15  ? 200 GLN A H    1 
ATOM   2716  H  HA   . GLN A 1 182 ? 9.048   -1.967  13.866  1.00 19.29  ? 200 GLN A HA   1 
ATOM   2717  H  HB2  . GLN A 1 182 ? 9.456   0.205   13.519  1.00 19.93  ? 200 GLN A HB2  1 
ATOM   2718  H  HB3  . GLN A 1 182 ? 10.538  -0.256  14.588  1.00 19.93  ? 200 GLN A HB3  1 
ATOM   2719  H  HG2  . GLN A 1 182 ? 12.198  -0.129  13.100  1.00 20.71  ? 200 GLN A HG2  1 
ATOM   2720  H  HG3  . GLN A 1 182 ? 11.188  -0.061  11.875  1.00 20.71  ? 200 GLN A HG3  1 
ATOM   2721  H  HE21 . GLN A 1 182 ? 12.429  1.820   11.220  1.00 23.08  ? 200 GLN A HE21 1 
ATOM   2722  H  HE22 . GLN A 1 182 ? 12.135  3.160   11.801  1.00 23.08  ? 200 GLN A HE22 1 
ATOM   2723  N  N    . ILE A 1 183 ? 8.445   -1.763  11.469  1.00 17.06  ? 201 ILE A N    1 
ATOM   2724  C  CA   . ILE A 1 183 ? 8.027   -1.976  10.094  1.00 17.82  ? 201 ILE A CA   1 
ATOM   2725  C  C    . ILE A 1 183 ? 7.751   -0.659  9.382   1.00 18.22  ? 201 ILE A C    1 
ATOM   2726  O  O    . ILE A 1 183 ? 8.112   -0.499  8.216   1.00 21.16  ? 201 ILE A O    1 
ATOM   2727  C  CB   . ILE A 1 183 ? 6.803   -2.915  10.033  1.00 17.00  ? 201 ILE A CB   1 
ATOM   2728  C  CG1  . ILE A 1 183 ? 7.190   -4.277  10.599  1.00 17.78  ? 201 ILE A CG1  1 
ATOM   2729  C  CG2  . ILE A 1 183 ? 6.288   -3.024  8.605   1.00 18.64  ? 201 ILE A CG2  1 
ATOM   2730  C  CD1  . ILE A 1 183 ? 6.018   -5.186  10.863  1.00 19.07  ? 201 ILE A CD1  1 
ATOM   2731  H  H    . ILE A 1 183 ? 7.823   -1.437  11.965  1.00 20.47  ? 201 ILE A H    1 
ATOM   2732  H  HA   . ILE A 1 183 ? 8.750   -2.407  9.612   1.00 21.39  ? 201 ILE A HA   1 
ATOM   2733  H  HB   . ILE A 1 183 ? 6.085   -2.550  10.573  1.00 20.40  ? 201 ILE A HB   1 
ATOM   2734  H  HG12 . ILE A 1 183 ? 7.772   -4.724  9.964   1.00 21.33  ? 201 ILE A HG12 1 
ATOM   2735  H  HG13 . ILE A 1 183 ? 7.656   -4.145  11.439  1.00 21.33  ? 201 ILE A HG13 1 
ATOM   2736  H  HG21 . ILE A 1 183 ? 7.035   -3.203  8.013   1.00 22.37  ? 201 ILE A HG21 1 
ATOM   2737  H  HG22 . ILE A 1 183 ? 5.646   -3.749  8.556   1.00 22.37  ? 201 ILE A HG22 1 
ATOM   2738  H  HG23 . ILE A 1 183 ? 5.863   -2.188  8.358   1.00 22.37  ? 201 ILE A HG23 1 
ATOM   2739  H  HD11 . ILE A 1 183 ? 5.638   -5.466  10.015  1.00 22.88  ? 201 ILE A HD11 1 
ATOM   2740  H  HD12 . ILE A 1 183 ? 6.324   -5.961  11.360  1.00 22.88  ? 201 ILE A HD12 1 
ATOM   2741  H  HD13 . ILE A 1 183 ? 5.354   -4.703  11.380  1.00 22.88  ? 201 ILE A HD13 1 
ATOM   2742  N  N    . VAL A 1 184 ? 7.098   0.280   10.063  1.00 16.20  ? 202 VAL A N    1 
ATOM   2743  C  CA   . VAL A 1 184 ? 7.020   1.678   9.651   1.00 16.33  ? 202 VAL A CA   1 
ATOM   2744  C  C    . VAL A 1 184 ? 7.775   2.464   10.718  1.00 16.57  ? 202 VAL A C    1 
ATOM   2745  O  O    . VAL A 1 184 ? 8.065   1.916   11.795  1.00 16.62  ? 202 VAL A O    1 
ATOM   2746  C  CB   . VAL A 1 184 ? 5.564   2.151   9.537   1.00 17.95  ? 202 VAL A CB   1 
ATOM   2747  C  CG1  . VAL A 1 184 ? 4.817   1.312   8.516   1.00 19.18  ? 202 VAL A CG1  1 
ATOM   2748  C  CG2  . VAL A 1 184 ? 4.872   2.105   10.900  1.00 18.32  ? 202 VAL A CG2  1 
ATOM   2749  H  H    . VAL A 1 184 ? 6.675   0.126   10.796  1.00 19.44  ? 202 VAL A H    1 
ATOM   2750  H  HA   . VAL A 1 184 ? 7.429   1.808   8.781   1.00 19.60  ? 202 VAL A HA   1 
ATOM   2751  H  HB   . VAL A 1 184 ? 5.552   3.072   9.234   1.00 21.54  ? 202 VAL A HB   1 
ATOM   2752  H  HG11 . VAL A 1 184 ? 3.919   1.663   8.415   1.00 23.02  ? 202 VAL A HG11 1 
ATOM   2753  H  HG12 . VAL A 1 184 ? 5.287   1.354   7.668   1.00 23.02  ? 202 VAL A HG12 1 
ATOM   2754  H  HG13 . VAL A 1 184 ? 4.781   0.394   8.828   1.00 23.02  ? 202 VAL A HG13 1 
ATOM   2755  H  HG21 . VAL A 1 184 ? 3.927   2.283   10.780  1.00 21.98  ? 202 VAL A HG21 1 
ATOM   2756  H  HG22 . VAL A 1 184 ? 4.997   1.224   11.287  1.00 21.98  ? 202 VAL A HG22 1 
ATOM   2757  H  HG23 . VAL A 1 184 ? 5.266   2.779   11.476  1.00 21.98  ? 202 VAL A HG23 1 
ATOM   2758  N  N    . PRO A 1 185 ? 8.094   3.738   10.491  1.00 15.88  ? 203 PRO A N    1 
ATOM   2759  C  CA   . PRO A 1 185 ? 8.763   4.521   11.543  1.00 16.64  ? 203 PRO A CA   1 
ATOM   2760  C  C    . PRO A 1 185 ? 7.942   4.524   12.821  1.00 15.99  ? 203 PRO A C    1 
ATOM   2761  O  O    . PRO A 1 185 ? 6.778   4.932   12.829  1.00 16.21  ? 203 PRO A O    1 
ATOM   2762  C  CB   . PRO A 1 185 ? 8.856   5.918   10.930  1.00 16.99  ? 203 PRO A CB   1 
ATOM   2763  C  CG   . PRO A 1 185 ? 8.861   5.673   9.460   1.00 17.49  ? 203 PRO A CG   1 
ATOM   2764  C  CD   . PRO A 1 185 ? 7.905   4.530   9.261   1.00 15.93  ? 203 PRO A CD   1 
ATOM   2765  H  HA   . PRO A 1 185 ? 9.652   4.176   11.721  1.00 19.97  ? 203 PRO A HA   1 
ATOM   2766  H  HB2  . PRO A 1 185 ? 8.088   6.449   11.194  1.00 20.39  ? 203 PRO A HB2  1 
ATOM   2767  H  HB3  . PRO A 1 185 ? 9.674   6.353   11.215  1.00 20.39  ? 203 PRO A HB3  1 
ATOM   2768  H  HG2  . PRO A 1 185 ? 8.557   6.466   8.990   1.00 20.98  ? 203 PRO A HG2  1 
ATOM   2769  H  HG3  . PRO A 1 185 ? 9.754   5.435   9.166   1.00 20.98  ? 203 PRO A HG3  1 
ATOM   2770  H  HD2  . PRO A 1 185 ? 6.992   4.848   9.188   1.00 19.12  ? 203 PRO A HD2  1 
ATOM   2771  H  HD3  . PRO A 1 185 ? 8.140   4.013   8.474   1.00 19.12  ? 203 PRO A HD3  1 
ATOM   2772  N  N    . THR A 1 186 ? 8.561   4.074   13.913  1.00 15.34  ? 204 THR A N    1 
ATOM   2773  C  CA   . THR A 1 186 ? 7.838   3.846   15.154  1.00 14.61  ? 204 THR A CA   1 
ATOM   2774  C  C    . THR A 1 186 ? 8.544   4.505   16.326  1.00 14.61  ? 204 THR A C    1 
ATOM   2775  O  O    . THR A 1 186 ? 9.771   4.452   16.442  1.00 15.37  ? 204 THR A O    1 
ATOM   2776  C  CB   . THR A 1 186 ? 7.689   2.343   15.435  1.00 15.59  ? 204 THR A CB   1 
ATOM   2777  O  OG1  . THR A 1 186 ? 6.990   1.729   14.351  1.00 14.58  ? 204 THR A OG1  1 
ATOM   2778  C  CG2  . THR A 1 186 ? 6.918   2.103   16.716  1.00 15.84  ? 204 THR A CG2  1 
ATOM   2779  H  H    . THR A 1 186 ? 9.401   3.894   13.955  1.00 18.41  ? 204 THR A H    1 
ATOM   2780  H  HA   . THR A 1 186 ? 6.960   4.250   15.077  1.00 17.53  ? 204 THR A HA   1 
ATOM   2781  H  HB   . THR A 1 186 ? 8.569   1.946   15.532  1.00 18.71  ? 204 THR A HB   1 
ATOM   2782  H  HG1  . THR A 1 186 ? 7.421   1.828   13.638  1.00 17.50  ? 204 THR A HG1  1 
ATOM   2783  H  HG21 . THR A 1 186 ? 6.093   2.613   16.707  1.00 19.01  ? 204 THR A HG21 1 
ATOM   2784  H  HG22 . THR A 1 186 ? 6.705   1.161   16.804  1.00 19.01  ? 204 THR A HG22 1 
ATOM   2785  H  HG23 . THR A 1 186 ? 7.449   2.378   17.479  1.00 19.01  ? 204 THR A HG23 1 
ATOM   2786  N  N    . THR A 1 187 ? 7.744   5.110   17.195  1.00 14.02  ? 205 THR A N    1 
ATOM   2787  C  CA   . THR A 1 187 ? 8.181   5.620   18.485  1.00 14.06  ? 205 THR A CA   1 
ATOM   2788  C  C    . THR A 1 187 ? 7.410   4.858   19.552  1.00 14.27  ? 205 THR A C    1 
ATOM   2789  O  O    . THR A 1 187 ? 6.182   4.722   19.459  1.00 14.62  ? 205 THR A O    1 
ATOM   2790  C  CB   . THR A 1 187 ? 7.882   7.118   18.614  1.00 15.14  ? 205 THR A CB   1 
ATOM   2791  O  OG1  . THR A 1 187 ? 8.454   7.822   17.504  1.00 16.41  ? 205 THR A OG1  1 
ATOM   2792  C  CG2  . THR A 1 187 ? 8.436   7.682   19.924  1.00 14.82  ? 205 THR A CG2  1 
ATOM   2793  H  H    . THR A 1 187 ? 6.906   5.242   17.053  1.00 16.83  ? 205 THR A H    1 
ATOM   2794  H  HA   . THR A 1 187 ? 9.135   5.489   18.600  1.00 16.87  ? 205 THR A HA   1 
ATOM   2795  H  HB   . THR A 1 187 ? 6.921   7.250   18.617  1.00 18.17  ? 205 THR A HB   1 
ATOM   2796  H  HG1  . THR A 1 187 ? 9.289   7.728   17.503  1.00 19.70  ? 205 THR A HG1  1 
ATOM   2797  H  HG21 . THR A 1 187 ? 8.248   8.632   19.982  1.00 17.78  ? 205 THR A HG21 1 
ATOM   2798  H  HG22 . THR A 1 187 ? 8.024   7.233   20.679  1.00 17.78  ? 205 THR A HG22 1 
ATOM   2799  H  HG23 . THR A 1 187 ? 9.395   7.548   19.964  1.00 17.78  ? 205 THR A HG23 1 
ATOM   2800  N  N    . ASN A 1 188 ? 8.129   4.359   20.551  1.00 14.04  ? 206 ASN A N    1 
ATOM   2801  C  CA   . ASN A 1 188 ? 7.556   3.619   21.669  1.00 13.67  ? 206 ASN A CA   1 
ATOM   2802  C  C    . ASN A 1 188 ? 7.889   4.395   22.934  1.00 13.89  ? 206 ASN A C    1 
ATOM   2803  O  O    . ASN A 1 188 ? 9.062   4.506   23.304  1.00 15.31  ? 206 ASN A O    1 
ATOM   2804  C  CB   . ASN A 1 188 ? 8.149   2.215   21.747  1.00 13.56  ? 206 ASN A CB   1 
ATOM   2805  C  CG   . ASN A 1 188 ? 7.847   1.395   20.520  1.00 14.33  ? 206 ASN A CG   1 
ATOM   2806  O  OD1  . ASN A 1 188 ? 6.686   1.224   20.143  1.00 14.16  ? 206 ASN A OD1  1 
ATOM   2807  N  ND2  . ASN A 1 188 ? 8.892   0.893   19.876  1.00 15.14  ? 206 ASN A ND2  1 
ATOM   2808  H  H    . ASN A 1 188 ? 8.984   4.440   20.605  1.00 16.85  ? 206 ASN A H    1 
ATOM   2809  H  HA   . ASN A 1 188 ? 6.594   3.549   21.566  1.00 16.40  ? 206 ASN A HA   1 
ATOM   2810  H  HB2  . ASN A 1 188 ? 9.112   2.283   21.836  1.00 16.27  ? 206 ASN A HB2  1 
ATOM   2811  H  HB3  . ASN A 1 188 ? 7.776   1.756   22.516  1.00 16.27  ? 206 ASN A HB3  1 
ATOM   2812  H  HD21 . ASN A 1 188 ? 9.688   1.043   20.165  1.00 18.17  ? 206 ASN A HD21 1 
ATOM   2813  H  HD22 . ASN A 1 188 ? 8.774   0.417   19.169  1.00 18.17  ? 206 ASN A HD22 1 
ATOM   2814  N  N    . LEU A 1 189 ? 6.873   4.946   23.583  1.00 13.87  ? 207 LEU A N    1 
ATOM   2815  C  CA   . LEU A 1 189 ? 7.061   5.642   24.846  1.00 14.87  ? 207 LEU A CA   1 
ATOM   2816  C  C    . LEU A 1 189 ? 6.573   4.733   25.964  1.00 13.15  ? 207 LEU A C    1 
ATOM   2817  O  O    . LEU A 1 189 ? 5.417   4.302   25.949  1.00 13.89  ? 207 LEU A O    1 
ATOM   2818  C  CB   . LEU A 1 189 ? 6.300   6.968   24.892  1.00 17.34  ? 207 LEU A CB   1 
ATOM   2819  C  CG   . LEU A 1 189 ? 6.607   7.576   26.265  1.00 22.65  ? 207 LEU A CG   1 
ATOM   2820  C  CD1  . LEU A 1 189 ? 7.630   8.710   26.145  1.00 23.63  ? 207 LEU A CD1  1 
ATOM   2821  C  CD2  . LEU A 1 189 ? 5.418   7.981   27.046  1.00 26.56  ? 207 LEU A CD2  1 
ATOM   2822  H  H    . LEU A 1 189 ? 6.058   4.930   23.309  1.00 16.64  ? 207 LEU A H    1 
ATOM   2823  H  HA   . LEU A 1 189 ? 8.002   5.845   24.965  1.00 17.85  ? 207 LEU A HA   1 
ATOM   2824  H  HB2  . LEU A 1 189 ? 6.608   7.564   24.191  1.00 20.81  ? 207 LEU A HB2  1 
ATOM   2825  H  HB3  . LEU A 1 189 ? 5.346   6.818   24.804  1.00 20.81  ? 207 LEU A HB3  1 
ATOM   2826  H  HG   . LEU A 1 189 ? 7.000   6.864   26.794  1.00 27.18  ? 207 LEU A HG   1 
ATOM   2827  H  HD11 . LEU A 1 189 ? 7.245   9.427   25.617  1.00 28.36  ? 207 LEU A HD11 1 
ATOM   2828  H  HD12 . LEU A 1 189 ? 7.849   9.033   27.032  1.00 28.36  ? 207 LEU A HD12 1 
ATOM   2829  H  HD13 . LEU A 1 189 ? 8.428   8.370   25.710  1.00 28.36  ? 207 LEU A HD13 1 
ATOM   2830  H  HD21 . LEU A 1 189 ? 5.056   8.798   26.669  1.00 31.87  ? 207 LEU A HD21 1 
ATOM   2831  H  HD22 . LEU A 1 189 ? 4.755   7.274   27.001  1.00 31.87  ? 207 LEU A HD22 1 
ATOM   2832  H  HD23 . LEU A 1 189 ? 5.681   8.130   27.968  1.00 31.87  ? 207 LEU A HD23 1 
ATOM   2833  N  N    . TYR A 1 190 ? 7.439   4.480   26.944  1.00 12.34  ? 208 TYR A N    1 
ATOM   2834  C  CA   . TYR A 1 190 ? 7.097   3.566   28.017  1.00 12.33  ? 208 TYR A CA   1 
ATOM   2835  C  C    . TYR A 1 190 ? 7.839   3.935   29.288  1.00 14.27  ? 208 TYR A C    1 
ATOM   2836  O  O    . TYR A 1 190 ? 8.655   4.862   29.321  1.00 14.68  ? 208 TYR A O    1 
ATOM   2837  C  CB   . TYR A 1 190 ? 7.363   2.125   27.608  1.00 12.99  ? 208 TYR A CB   1 
ATOM   2838  C  CG   . TYR A 1 190 ? 8.800   1.744   27.325  1.00 13.92  ? 208 TYR A CG   1 
ATOM   2839  C  CD1  . TYR A 1 190 ? 9.422   2.091   26.125  1.00 14.07  ? 208 TYR A CD1  1 
ATOM   2840  C  CD2  . TYR A 1 190 ? 9.520   0.985   28.238  1.00 14.47  ? 208 TYR A CD2  1 
ATOM   2841  C  CE1  . TYR A 1 190 ? 10.720  1.677   25.847  1.00 14.91  ? 208 TYR A CE1  1 
ATOM   2842  C  CE2  . TYR A 1 190 ? 10.820  0.589   27.982  1.00 15.41  ? 208 TYR A CE2  1 
ATOM   2843  C  CZ   . TYR A 1 190 ? 11.416  0.926   26.788  1.00 14.49  ? 208 TYR A CZ   1 
ATOM   2844  O  OH   . TYR A 1 190 ? 12.703  0.489   26.547  1.00 16.20  ? 208 TYR A OH   1 
ATOM   2845  H  H    . TYR A 1 190 ? 8.224   4.825   27.004  1.00 14.81  ? 208 TYR A H    1 
ATOM   2846  H  HA   . TYR A 1 190 ? 6.152   3.671   28.206  1.00 14.79  ? 208 TYR A HA   1 
ATOM   2847  H  HB2  . TYR A 1 190 ? 7.054   1.549   28.325  1.00 15.58  ? 208 TYR A HB2  1 
ATOM   2848  H  HB3  . TYR A 1 190 ? 6.859   1.946   26.799  1.00 15.58  ? 208 TYR A HB3  1 
ATOM   2849  H  HD1  . TYR A 1 190 ? 8.962   2.606   25.502  1.00 16.88  ? 208 TYR A HD1  1 
ATOM   2850  H  HD2  . TYR A 1 190 ? 9.119   0.737   29.040  1.00 17.36  ? 208 TYR A HD2  1 
ATOM   2851  H  HE1  . TYR A 1 190 ? 11.120  1.901   25.037  1.00 17.89  ? 208 TYR A HE1  1 
ATOM   2852  H  HE2  . TYR A 1 190 ? 11.291  0.097   28.616  1.00 18.49  ? 208 TYR A HE2  1 
ATOM   2853  H  HH   . TYR A 1 190 ? 12.875  0.541   25.727  1.00 19.44  ? 208 TYR A HH   1 
ATOM   2854  N  N    . SER A 1 191 ? 7.523   3.202   30.349  1.00 14.46  ? 209 SER A N    1 
ATOM   2855  C  CA   . SER A 1 191 ? 8.014   3.524   31.675  1.00 14.60  ? 209 SER A CA   1 
ATOM   2856  C  C    . SER A 1 191 ? 8.528   2.286   32.386  1.00 15.36  ? 209 SER A C    1 
ATOM   2857  O  O    . SER A 1 191 ? 7.858   1.247   32.409  1.00 15.01  ? 209 SER A O    1 
ATOM   2858  C  CB   . SER A 1 191 ? 6.905   4.149   32.513  1.00 16.22  ? 209 SER A CB   1 
ATOM   2859  O  OG   . SER A 1 191 ? 7.357   4.341   33.833  1.00 16.60  ? 209 SER A OG   1 
ATOM   2860  H  H    . SER A 1 191 ? 7.020   2.505   30.321  1.00 17.35  ? 209 SER A H    1 
ATOM   2861  H  HA   . SER A 1 191 ? 8.759   4.138   31.581  1.00 17.52  ? 209 SER A HA   1 
ATOM   2862  H  HB2  . SER A 1 191 ? 6.660   5.007   32.131  1.00 19.47  ? 209 SER A HB2  1 
ATOM   2863  H  HB3  . SER A 1 191 ? 6.137   3.558   32.520  1.00 19.47  ? 209 SER A HB3  1 
ATOM   2864  H  HG   . SER A 1 191 ? 6.726   4.616   34.315  1.00 19.91  ? 209 SER A HG   1 
ATOM   2865  N  N    . ALA A 1 192 ? 9.707   2.420   32.999  1.00 16.47  ? 210 ALA A N    1 
ATOM   2866  C  CA   . ALA A 1 192 ? 10.250  1.329   33.798  1.00 17.11  ? 210 ALA A CA   1 
ATOM   2867  C  C    . ALA A 1 192 ? 9.335   0.944   34.951  1.00 16.67  ? 210 ALA A C    1 
ATOM   2868  O  O    . ALA A 1 192 ? 9.422   -0.188  35.438  1.00 18.44  ? 210 ALA A O    1 
ATOM   2869  C  CB   . ALA A 1 192 ? 11.617  1.716   34.364  1.00 18.11  ? 210 ALA A CB   1 
ATOM   2870  H  H    . ALA A 1 192 ? 10.202  3.122   32.967  1.00 19.77  ? 210 ALA A H    1 
ATOM   2871  H  HA   . ALA A 1 192 ? 10.359  0.560   33.217  1.00 20.54  ? 210 ALA A HA   1 
ATOM   2872  H  HB1  . ALA A 1 192 ? 12.000  0.949   34.817  1.00 21.73  ? 210 ALA A HB1  1 
ATOM   2873  H  HB2  . ALA A 1 192 ? 12.195  1.992   33.634  1.00 21.73  ? 210 ALA A HB2  1 
ATOM   2874  H  HB3  . ALA A 1 192 ? 11.504  2.448   34.990  1.00 21.73  ? 210 ALA A HB3  1 
ATOM   2875  N  N    . THR A 1 193 ? 8.475   1.854   35.412  1.00 16.25  ? 211 THR A N    1 
ATOM   2876  C  CA   . THR A 1 193 ? 7.606   1.580   36.547  1.00 17.27  ? 211 THR A CA   1 
ATOM   2877  C  C    . THR A 1 193 ? 6.229   1.077   36.137  1.00 17.66  ? 211 THR A C    1 
ATOM   2878  O  O    . THR A 1 193 ? 5.351   0.957   36.997  1.00 20.05  ? 211 THR A O    1 
ATOM   2879  C  CB   . THR A 1 193 ? 7.478   2.808   37.458  1.00 15.99  ? 211 THR A CB   1 
ATOM   2880  O  OG1  . THR A 1 193 ? 6.928   3.915   36.735  1.00 16.91  ? 211 THR A OG1  1 
ATOM   2881  C  CG2  . THR A 1 193 ? 8.842   3.186   38.021  1.00 17.21  ? 211 THR A CG2  1 
ATOM   2882  H  H    . THR A 1 193 ? 8.380   2.642   35.079  1.00 19.50  ? 211 THR A H    1 
ATOM   2883  H  HA   . THR A 1 193 ? 8.024   0.883   37.076  1.00 20.73  ? 211 THR A HA   1 
ATOM   2884  H  HB   . THR A 1 193 ? 6.883   2.601   38.196  1.00 19.19  ? 211 THR A HB   1 
ATOM   2885  H  HG1  . THR A 1 193 ? 6.104   3.801   36.619  1.00 20.30  ? 211 THR A HG1  1 
ATOM   2886  H  HG21 . THR A 1 193 ? 9.271   2.404   38.402  1.00 20.65  ? 211 THR A HG21 1 
ATOM   2887  H  HG22 . THR A 1 193 ? 9.405   3.542   37.317  1.00 20.65  ? 211 THR A HG22 1 
ATOM   2888  H  HG23 . THR A 1 193 ? 8.740   3.858   38.714  1.00 20.65  ? 211 THR A HG23 1 
ATOM   2889  N  N    . ASP A 1 194 ? 6.028   0.768   34.858  1.00 15.50  ? 212 ASP A N    1 
ATOM   2890  C  CA   . ASP A 1 194 ? 4.755   0.232   34.390  1.00 14.42  ? 212 ASP A CA   1 
ATOM   2891  C  C    . ASP A 1 194 ? 4.321   -0.924  35.279  1.00 15.97  ? 212 ASP A C    1 
ATOM   2892  O  O    . ASP A 1 194 ? 5.075   -1.881  35.484  1.00 16.68  ? 212 ASP A O    1 
ATOM   2893  C  CB   . ASP A 1 194 ? 4.932   -0.224  32.938  1.00 15.00  ? 212 ASP A CB   1 
ATOM   2894  C  CG   . ASP A 1 194 ? 3.614   -0.433  32.218  1.00 14.28  ? 212 ASP A CG   1 
ATOM   2895  O  OD1  . ASP A 1 194 ? 2.698   -1.044  32.809  1.00 14.28  ? 212 ASP A OD1  1 
ATOM   2896  O  OD2  . ASP A 1 194 ? 3.504   -0.011  31.044  1.00 15.21  ? 212 ASP A OD2  1 
ATOM   2897  H  H    . ASP A 1 194 ? 6.616   0.860   34.238  1.00 18.61  ? 212 ASP A H    1 
ATOM   2898  H  HA   . ASP A 1 194 ? 4.060   0.908   34.419  1.00 17.30  ? 212 ASP A HA   1 
ATOM   2899  H  HB2  . ASP A 1 194 ? 5.433   0.452   32.455  1.00 17.99  ? 212 ASP A HB2  1 
ATOM   2900  H  HB3  . ASP A 1 194 ? 5.415   -1.065  32.928  1.00 17.99  ? 212 ASP A HB3  1 
ATOM   2901  N  N    . GLU A 1 195 ? 3.108   -0.818  35.826  1.00 15.80  ? 213 GLU A N    1 
ATOM   2902  C  CA   . GLU A 1 195 ? 2.567   -1.808  36.750  1.00 16.14  ? 213 GLU A CA   1 
ATOM   2903  C  C    . GLU A 1 195 ? 1.743   -2.887  36.059  1.00 15.81  ? 213 GLU A C    1 
ATOM   2904  O  O    . GLU A 1 195 ? 1.278   -3.818  36.731  1.00 18.45  ? 213 GLU A O    1 
ATOM   2905  C  CB   . GLU A 1 195 ? 1.746   -1.108  37.847  1.00 18.24  ? 213 GLU A CB   1 
ATOM   2906  C  CG   . GLU A 1 195 ? 0.269   -0.883  37.539  1.00 18.44  ? 213 GLU A CG   1 
ATOM   2907  C  CD   . GLU A 1 195 ? -0.001  0.241   36.549  1.00 18.83  ? 213 GLU A CD   1 
ATOM   2908  O  OE1  . GLU A 1 195 ? 0.941   0.709   35.878  1.00 18.11  ? 213 GLU A OE1  1 
ATOM   2909  O  OE2  . GLU A 1 195 ? -1.183  0.640   36.432  1.00 20.47  ? 213 GLU A OE2  1 
ATOM   2910  H  H    . GLU A 1 195 ? 2.570   -0.165  35.672  1.00 18.96  ? 213 GLU A H    1 
ATOM   2911  H  HA   . GLU A 1 195 ? 3.302   -2.262  37.190  1.00 19.37  ? 213 GLU A HA   1 
ATOM   2912  H  HB2  . GLU A 1 195 ? 1.791   -1.649  38.650  1.00 21.89  ? 213 GLU A HB2  1 
ATOM   2913  H  HB3  . GLU A 1 195 ? 2.140   -0.237  38.011  1.00 21.89  ? 213 GLU A HB3  1 
ATOM   2914  H  HG2  . GLU A 1 195 ? -0.098  -1.699  37.163  1.00 22.12  ? 213 GLU A HG2  1 
ATOM   2915  H  HG3  . GLU A 1 195 ? -0.190  -0.663  38.365  1.00 22.12  ? 213 GLU A HG3  1 
ATOM   2916  N  N    . ILE A 1 196 ? 1.553   -2.777  34.746  1.00 15.54  ? 214 ILE A N    1 
ATOM   2917  C  CA   . ILE A 1 196 ? 0.819   -3.758  33.961  1.00 15.48  ? 214 ILE A CA   1 
ATOM   2918  C  C    . ILE A 1 196 ? 1.750   -4.567  33.066  1.00 15.84  ? 214 ILE A C    1 
ATOM   2919  O  O    . ILE A 1 196 ? 1.623   -5.791  32.975  1.00 16.48  ? 214 ILE A O    1 
ATOM   2920  C  CB   . ILE A 1 196 ? -0.281  -3.063  33.122  1.00 17.42  ? 214 ILE A CB   1 
ATOM   2921  C  CG1  . ILE A 1 196 ? -1.285  -2.331  34.023  1.00 19.83  ? 214 ILE A CG1  1 
ATOM   2922  C  CG2  . ILE A 1 196 ? -0.978  -4.052  32.183  1.00 17.14  ? 214 ILE A CG2  1 
ATOM   2923  C  CD1  . ILE A 1 196 ? -2.043  -3.205  34.965  1.00 22.07  ? 214 ILE A CD1  1 
ATOM   2924  H  H    . ILE A 1 196 ? 1.850   -2.122  34.276  1.00 18.64  ? 214 ILE A H    1 
ATOM   2925  H  HA   . ILE A 1 196 ? 0.389   -4.385  34.564  1.00 18.58  ? 214 ILE A HA   1 
ATOM   2926  H  HB   . ILE A 1 196 ? 0.152   -2.396  32.566  1.00 20.90  ? 214 ILE A HB   1 
ATOM   2927  H  HG12 . ILE A 1 196 ? -0.802  -1.680  34.556  1.00 23.79  ? 214 ILE A HG12 1 
ATOM   2928  H  HG13 . ILE A 1 196 ? -1.934  -1.881  33.458  1.00 23.79  ? 214 ILE A HG13 1 
ATOM   2929  H  HG21 . ILE A 1 196 ? -1.812  -3.663  31.877  1.00 20.57  ? 214 ILE A HG21 1 
ATOM   2930  H  HG22 . ILE A 1 196 ? -0.399  -4.231  31.426  1.00 20.57  ? 214 ILE A HG22 1 
ATOM   2931  H  HG23 . ILE A 1 196 ? -1.155  -4.875  32.666  1.00 20.57  ? 214 ILE A HG23 1 
ATOM   2932  H  HD11 . ILE A 1 196 ? -2.712  -2.672  35.422  1.00 26.49  ? 214 ILE A HD11 1 
ATOM   2933  H  HD12 . ILE A 1 196 ? -2.473  -3.914  34.461  1.00 26.49  ? 214 ILE A HD12 1 
ATOM   2934  H  HD13 . ILE A 1 196 ? -1.426  -3.584  35.610  1.00 26.49  ? 214 ILE A HD13 1 
ATOM   2935  N  N    . VAL A 1 197 ? 2.704   -3.897  32.422  1.00 15.24  ? 215 VAL A N    1 
ATOM   2936  C  CA   . VAL A 1 197 ? 3.607   -4.502  31.453  1.00 15.74  ? 215 VAL A CA   1 
ATOM   2937  C  C    . VAL A 1 197 ? 5.004   -4.511  32.050  1.00 15.79  ? 215 VAL A C    1 
ATOM   2938  O  O    . VAL A 1 197 ? 5.564   -3.451  32.365  1.00 16.23  ? 215 VAL A O    1 
ATOM   2939  C  CB   . VAL A 1 197 ? 3.599   -3.728  30.126  1.00 15.79  ? 215 VAL A CB   1 
ATOM   2940  C  CG1  . VAL A 1 197 ? 4.580   -4.348  29.131  1.00 16.68  ? 215 VAL A CG1  1 
ATOM   2941  C  CG2  . VAL A 1 197 ? 2.199   -3.684  29.547  1.00 16.54  ? 215 VAL A CG2  1 
ATOM   2942  H  H    . VAL A 1 197 ? 2.851   -3.057  32.536  1.00 18.28  ? 215 VAL A H    1 
ATOM   2943  H  HA   . VAL A 1 197 ? 3.333   -5.418  31.290  1.00 18.89  ? 215 VAL A HA   1 
ATOM   2944  H  HB   . VAL A 1 197 ? 3.885   -2.817  30.294  1.00 18.95  ? 215 VAL A HB   1 
ATOM   2945  H  HG11 . VAL A 1 197 ? 4.425   -3.963  28.254  1.00 20.02  ? 215 VAL A HG11 1 
ATOM   2946  H  HG12 . VAL A 1 197 ? 5.486   -4.158  29.421  1.00 20.02  ? 215 VAL A HG12 1 
ATOM   2947  H  HG13 . VAL A 1 197 ? 4.436   -5.307  29.102  1.00 20.02  ? 215 VAL A HG13 1 
ATOM   2948  H  HG21 . VAL A 1 197 ? 2.226   -3.231  28.689  1.00 19.85  ? 215 VAL A HG21 1 
ATOM   2949  H  HG22 . VAL A 1 197 ? 1.876   -4.591  29.432  1.00 19.85  ? 215 VAL A HG22 1 
ATOM   2950  H  HG23 . VAL A 1 197 ? 1.620   -3.201  30.158  1.00 19.85  ? 215 VAL A HG23 1 
ATOM   2951  N  N    . GLN A 1 198 ? 5.564   -5.705  32.197  1.00 15.60  ? 216 GLN A N    1 
ATOM   2952  C  CA   . GLN A 1 198 ? 6.960   -5.897  32.539  1.00 16.58  ? 216 GLN A CA   1 
ATOM   2953  C  C    . GLN A 1 198 ? 7.471   -7.089  31.741  1.00 17.37  ? 216 GLN A C    1 
ATOM   2954  O  O    . GLN A 1 198 ? 6.684   -7.966  31.363  1.00 17.86  ? 216 GLN A O    1 
ATOM   2955  C  CB   . GLN A 1 198 ? 7.149   -6.144  34.042  1.00 16.96  ? 216 GLN A CB   1 
ATOM   2956  C  CG   . GLN A 1 198 ? 6.991   -4.879  34.900  1.00 16.72  ? 216 GLN A CG   1 
ATOM   2957  C  CD   . GLN A 1 198 ? 8.100   -3.855  34.686  1.00 16.65  ? 216 GLN A CD   1 
ATOM   2958  O  OE1  . GLN A 1 198 ? 9.238   -4.212  34.386  1.00 17.55  ? 216 GLN A OE1  1 
ATOM   2959  N  NE2  . GLN A 1 198 ? 7.766   -2.575  34.830  1.00 17.20  ? 216 GLN A NE2  1 
ATOM   2960  H  H    . GLN A 1 198 ? 5.137   -6.445  32.098  1.00 18.72  ? 216 GLN A H    1 
ATOM   2961  H  HA   . GLN A 1 198 ? 7.483   -5.114  32.308  1.00 19.89  ? 216 GLN A HA   1 
ATOM   2962  H  HB2  . GLN A 1 198 ? 6.487   -6.788  34.338  1.00 20.35  ? 216 GLN A HB2  1 
ATOM   2963  H  HB3  . GLN A 1 198 ? 8.041   -6.494  34.191  1.00 20.35  ? 216 GLN A HB3  1 
ATOM   2964  H  HG2  . GLN A 1 198 ? 6.148   -4.454  34.679  1.00 20.06  ? 216 GLN A HG2  1 
ATOM   2965  H  HG3  . GLN A 1 198 ? 6.998   -5.133  35.837  1.00 20.06  ? 216 GLN A HG3  1 
ATOM   2966  H  HE21 . GLN A 1 198 ? 6.958   -2.361  35.033  1.00 20.64  ? 216 GLN A HE21 1 
ATOM   2967  H  HE22 . GLN A 1 198 ? 8.358   -1.961  34.719  1.00 20.64  ? 216 GLN A HE22 1 
ATOM   2968  N  N    . PRO A 1 199 ? 8.780   -7.153  31.479  1.00 17.64  ? 217 PRO A N    1 
ATOM   2969  C  CA   . PRO A 1 199 ? 9.814   -6.236  31.962  1.00 17.74  ? 217 PRO A CA   1 
ATOM   2970  C  C    . PRO A 1 199 ? 9.965   -5.002  31.090  1.00 16.98  ? 217 PRO A C    1 
ATOM   2971  O  O    . PRO A 1 199 ? 9.853   -5.096  29.867  1.00 18.28  ? 217 PRO A O    1 
ATOM   2972  C  CB   . PRO A 1 199 ? 11.078  -7.090  31.888  1.00 19.15  ? 217 PRO A CB   1 
ATOM   2973  C  CG   . PRO A 1 199 ? 10.835  -7.976  30.720  1.00 19.70  ? 217 PRO A CG   1 
ATOM   2974  C  CD   . PRO A 1 199 ? 9.360   -8.260  30.692  1.00 19.33  ? 217 PRO A CD   1 
ATOM   2975  H  HA   . PRO A 1 199 ? 9.636   -5.966  32.876  1.00 21.29  ? 217 PRO A HA   1 
ATOM   2976  H  HB2  . PRO A 1 199 ? 11.855  -6.527  31.748  1.00 22.99  ? 217 PRO A HB2  1 
ATOM   2977  H  HB3  . PRO A 1 199 ? 11.183  -7.603  32.704  1.00 22.99  ? 217 PRO A HB3  1 
ATOM   2978  H  HG2  . PRO A 1 199 ? 11.111  -7.524  29.908  1.00 23.64  ? 217 PRO A HG2  1 
ATOM   2979  H  HG3  . PRO A 1 199 ? 11.338  -8.799  30.829  1.00 23.64  ? 217 PRO A HG3  1 
ATOM   2980  H  HD2  . PRO A 1 199 ? 9.024   -8.247  29.782  1.00 23.19  ? 217 PRO A HD2  1 
ATOM   2981  H  HD3  . PRO A 1 199 ? 9.165   -9.115  31.105  1.00 23.19  ? 217 PRO A HD3  1 
ATOM   2982  N  N    . GLN A 1 200 ? 10.212  -3.857  31.740  1.00 16.29  ? 218 GLN A N    1 
ATOM   2983  C  CA   . GLN A 1 200 ? 10.376  -2.577  31.062  1.00 16.48  ? 218 GLN A CA   1 
ATOM   2984  C  C    . GLN A 1 200 ? 11.551  -1.791  31.633  1.00 16.73  ? 218 GLN A C    1 
ATOM   2985  O  O    . GLN A 1 200 ? 11.713  -0.608  31.294  1.00 17.22  ? 218 GLN A O    1 
ATOM   2986  C  CB   . GLN A 1 200 ? 9.101   -1.725  31.195  1.00 14.55  ? 218 GLN A CB   1 
ATOM   2987  C  CG   . GLN A 1 200 ? 7.871   -2.343  30.554  1.00 14.18  ? 218 GLN A CG   1 
ATOM   2988  C  CD   . GLN A 1 200 ? 7.759   -1.988  29.089  1.00 14.49  ? 218 GLN A CD   1 
ATOM   2989  O  OE1  . GLN A 1 200 ? 8.605   -2.377  28.281  1.00 15.08  ? 218 GLN A OE1  1 
ATOM   2990  N  NE2  . GLN A 1 200 ? 6.711   -1.244  28.736  1.00 14.21  ? 218 GLN A NE2  1 
ATOM   2991  H  H    . GLN A 1 200 ? 10.289  -3.799  32.594  1.00 19.55  ? 218 GLN A H    1 
ATOM   2992  H  HA   . GLN A 1 200 ? 10.533  -2.738  30.118  1.00 19.78  ? 218 GLN A HA   1 
ATOM   2993  H  HB2  . GLN A 1 200 ? 8.910   -1.599  32.137  1.00 17.46  ? 218 GLN A HB2  1 
ATOM   2994  H  HB3  . GLN A 1 200 ? 9.256   -0.867  30.770  1.00 17.46  ? 218 GLN A HB3  1 
ATOM   2995  H  HG2  . GLN A 1 200 ? 7.923   -3.308  30.628  1.00 17.01  ? 218 GLN A HG2  1 
ATOM   2996  H  HG3  . GLN A 1 200 ? 7.078   -2.017  31.006  1.00 17.01  ? 218 GLN A HG3  1 
ATOM   2997  H  HE21 . GLN A 1 200 ? 6.142   -0.992  29.330  1.00 17.05  ? 218 GLN A HE21 1 
ATOM   2998  H  HE22 . GLN A 1 200 ? 6.603   -1.016  27.913  1.00 17.05  ? 218 GLN A HE22 1 
ATOM   2999  N  N    . VAL A 1 201 ? 12.364  -2.399  32.497  1.00 18.04  ? 219 VAL A N    1 
ATOM   3000  C  CA   . VAL A 1 201 ? 13.301  -1.636  33.311  1.00 18.99  ? 219 VAL A CA   1 
ATOM   3001  C  C    . VAL A 1 201 ? 14.664  -1.421  32.665  1.00 19.77  ? 219 VAL A C    1 
ATOM   3002  O  O    . VAL A 1 201 ? 15.362  -0.460  33.025  1.00 22.08  ? 219 VAL A O    1 
ATOM   3003  C  CB   . VAL A 1 201 ? 13.492  -2.323  34.677  1.00 20.54  ? 219 VAL A CB   1 
ATOM   3004  C  CG1  . VAL A 1 201 ? 12.194  -2.325  35.471  1.00 21.80  ? 219 VAL A CG1  1 
ATOM   3005  C  CG2  . VAL A 1 201 ? 14.009  -3.750  34.493  1.00 23.01  ? 219 VAL A CG2  1 
ATOM   3006  H  H    . VAL A 1 201 ? 12.390  -3.248  32.628  1.00 21.65  ? 219 VAL A H    1 
ATOM   3007  H  HA   . VAL A 1 201 ? 12.917  -0.755  33.440  1.00 22.79  ? 219 VAL A HA   1 
ATOM   3008  H  HB   . VAL A 1 201 ? 14.151  -1.823  35.184  1.00 24.65  ? 219 VAL A HB   1 
ATOM   3009  H  HG11 . VAL A 1 201 ? 12.347  -2.757  36.326  1.00 26.17  ? 219 VAL A HG11 1 
ATOM   3010  H  HG12 . VAL A 1 201 ? 11.907  -1.409  35.609  1.00 26.17  ? 219 VAL A HG12 1 
ATOM   3011  H  HG13 . VAL A 1 201 ? 11.519  -2.811  34.972  1.00 26.17  ? 219 VAL A HG13 1 
ATOM   3012  H  HG21 . VAL A 1 201 ? 14.221  -4.123  35.363  1.00 27.61  ? 219 VAL A HG21 1 
ATOM   3013  H  HG22 . VAL A 1 201 ? 13.322  -4.282  34.063  1.00 27.61  ? 219 VAL A HG22 1 
ATOM   3014  H  HG23 . VAL A 1 201 ? 14.805  -3.728  33.939  1.00 27.61  ? 219 VAL A HG23 1 
ATOM   3015  N  N    . SER A 1 202 ? 15.056  -2.267  31.713  1.00 18.21  ? 220 SER A N    1 
ATOM   3016  C  CA   . SER A 1 202 ? 16.443  -2.307  31.268  1.00 18.90  ? 220 SER A CA   1 
ATOM   3017  C  C    . SER A 1 202 ? 16.820  -1.192  30.296  1.00 18.86  ? 220 SER A C    1 
ATOM   3018  O  O    . SER A 1 202 ? 18.016  -0.958  30.087  1.00 19.97  ? 220 SER A O    1 
ATOM   3019  C  CB   . SER A 1 202 ? 16.740  -3.664  30.622  1.00 20.23  ? 220 SER A CB   1 
ATOM   3020  O  OG   . SER A 1 202 ? 16.127  -3.784  29.347  1.00 21.02  ? 220 SER A OG   1 
ATOM   3021  H  H    . SER A 1 202 ? 14.539  -2.825  31.311  1.00 21.86  ? 220 SER A H    1 
ATOM   3022  H  HA   . SER A 1 202 ? 17.007  -2.199  32.050  1.00 22.68  ? 220 SER A HA   1 
ATOM   3023  H  HB2  . SER A 1 202 ? 17.700  -3.756  30.517  1.00 24.27  ? 220 SER A HB2  1 
ATOM   3024  H  HB3  . SER A 1 202 ? 16.401  -4.366  31.199  1.00 24.27  ? 220 SER A HB3  1 
ATOM   3025  H  HG   . SER A 1 202 ? 15.305  -3.620  29.407  1.00 25.23  ? 220 SER A HG   1 
ATOM   3026  N  N    . ASN A 1 203 ? 15.852  -0.501  29.698  1.00 18.38  ? 221 ASN A N    1 
ATOM   3027  C  CA   . ASN A 1 203 ? 16.148  0.485   28.656  1.00 18.25  ? 221 ASN A CA   1 
ATOM   3028  C  C    . ASN A 1 203 ? 16.963  -0.158  27.538  1.00 18.41  ? 221 ASN A C    1 
ATOM   3029  O  O    . ASN A 1 203 ? 18.017  0.343   27.130  1.00 19.15  ? 221 ASN A O    1 
ATOM   3030  C  CB   . ASN A 1 203 ? 16.874  1.709   29.216  1.00 19.60  ? 221 ASN A CB   1 
ATOM   3031  C  CG   . ASN A 1 203 ? 16.998  2.826   28.194  1.00 19.72  ? 221 ASN A CG   1 
ATOM   3032  O  OD1  . ASN A 1 203 ? 16.123  3.007   27.339  1.00 18.91  ? 221 ASN A OD1  1 
ATOM   3033  N  ND2  . ASN A 1 203 ? 18.087  3.580   28.271  1.00 20.04  ? 221 ASN A ND2  1 
ATOM   3034  H  H    . ASN A 1 203 ? 15.015  -0.585  29.876  1.00 22.05  ? 221 ASN A H    1 
ATOM   3035  H  HA   . ASN A 1 203 ? 15.307  0.796   28.288  1.00 21.90  ? 221 ASN A HA   1 
ATOM   3036  H  HB2  . ASN A 1 203 ? 16.379  2.051   29.977  1.00 23.52  ? 221 ASN A HB2  1 
ATOM   3037  H  HB3  . ASN A 1 203 ? 17.768  1.451   29.490  1.00 23.52  ? 221 ASN A HB3  1 
ATOM   3038  H  HD21 . ASN A 1 203 ? 18.204  4.225   27.715  1.00 24.04  ? 221 ASN A HD21 1 
ATOM   3039  H  HD22 . ASN A 1 203 ? 18.676  3.422   28.878  1.00 24.04  ? 221 ASN A HD22 1 
ATOM   3040  N  N    . SER A 1 204 ? 16.466  -1.294  27.052  1.00 18.07  ? 222 SER A N    1 
ATOM   3041  C  CA   . SER A 1 204 ? 17.194  -2.139  26.115  1.00 18.04  ? 222 SER A CA   1 
ATOM   3042  C  C    . SER A 1 204 ? 16.208  -3.050  25.395  1.00 18.03  ? 222 SER A C    1 
ATOM   3043  O  O    . SER A 1 204 ? 15.013  -3.052  25.721  1.00 18.01  ? 222 SER A O    1 
ATOM   3044  C  CB   . SER A 1 204 ? 18.228  -2.981  26.864  1.00 18.69  ? 222 SER A CB   1 
ATOM   3045  O  OG   . SER A 1 204 ? 17.648  -4.185  27.336  1.00 18.64  ? 222 SER A OG   1 
ATOM   3046  H  H    . SER A 1 204 ? 15.690  -1.602  27.256  1.00 21.68  ? 222 SER A H    1 
ATOM   3047  H  HA   . SER A 1 204 ? 17.654  -1.591  25.461  1.00 21.65  ? 222 SER A HA   1 
ATOM   3048  H  HB2  . SER A 1 204 ? 18.957  -3.196  26.261  1.00 22.43  ? 222 SER A HB2  1 
ATOM   3049  H  HB3  . SER A 1 204 ? 18.562  -2.473  27.620  1.00 22.43  ? 222 SER A HB3  1 
ATOM   3050  H  HG   . SER A 1 204 ? 18.243  -4.682  27.660  1.00 22.37  ? 222 SER A HG   1 
ATOM   3051  N  N    . PRO A 1 205 ? 16.672  -3.844  24.425  1.00 17.25  ? 223 PRO A N    1 
ATOM   3052  C  CA   . PRO A 1 205 ? 15.758  -4.747  23.700  1.00 16.99  ? 223 PRO A CA   1 
ATOM   3053  C  C    . PRO A 1 205 ? 15.055  -5.770  24.576  1.00 16.32  ? 223 PRO A C    1 
ATOM   3054  O  O    . PRO A 1 205 ? 14.104  -6.406  24.102  1.00 17.56  ? 223 PRO A O    1 
ATOM   3055  C  CB   . PRO A 1 205 ? 16.668  -5.423  22.662  1.00 17.27  ? 223 PRO A CB   1 
ATOM   3056  C  CG   . PRO A 1 205 ? 17.834  -4.467  22.503  1.00 17.66  ? 223 PRO A CG   1 
ATOM   3057  C  CD   . PRO A 1 205 ? 18.036  -3.861  23.867  1.00 17.68  ? 223 PRO A CD   1 
ATOM   3058  H  HA   . PRO A 1 205 ? 15.086  -4.221  23.238  1.00 20.38  ? 223 PRO A HA   1 
ATOM   3059  H  HB2  . PRO A 1 205 ? 16.966  -6.285  22.992  1.00 20.72  ? 223 PRO A HB2  1 
ATOM   3060  H  HB3  . PRO A 1 205 ? 16.192  -5.536  21.825  1.00 20.72  ? 223 PRO A HB3  1 
ATOM   3061  H  HG2  . PRO A 1 205 ? 18.624  -4.954  22.220  1.00 21.19  ? 223 PRO A HG2  1 
ATOM   3062  H  HG3  . PRO A 1 205 ? 17.614  -3.784  21.850  1.00 21.19  ? 223 PRO A HG3  1 
ATOM   3063  H  HD2  . PRO A 1 205 ? 18.625  -4.412  24.407  1.00 21.22  ? 223 PRO A HD2  1 
ATOM   3064  H  HD3  . PRO A 1 205 ? 18.394  -2.962  23.797  1.00 21.22  ? 223 PRO A HD3  1 
ATOM   3065  N  N    . LEU A 1 206 ? 15.481  -5.962  25.827  1.00 17.17  ? 224 LEU A N    1 
ATOM   3066  C  CA   . LEU A 1 206 ? 14.734  -6.848  26.708  1.00 17.80  ? 224 LEU A CA   1 
ATOM   3067  C  C    . LEU A 1 206 ? 13.331  -6.322  26.985  1.00 17.10  ? 224 LEU A C    1 
ATOM   3068  O  O    . LEU A 1 206 ? 12.435  -7.110  27.309  1.00 18.81  ? 224 LEU A O    1 
ATOM   3069  C  CB   . LEU A 1 206 ? 15.476  -7.027  28.031  1.00 19.47  ? 224 LEU A CB   1 
ATOM   3070  C  CG   . LEU A 1 206 ? 16.839  -7.722  27.986  1.00 20.88  ? 224 LEU A CG   1 
ATOM   3071  C  CD1  . LEU A 1 206 ? 17.486  -7.656  29.355  1.00 21.60  ? 224 LEU A CD1  1 
ATOM   3072  C  CD2  . LEU A 1 206 ? 16.691  -9.153  27.521  1.00 23.32  ? 224 LEU A CD2  1 
ATOM   3073  H  H    . LEU A 1 206 ? 16.179  -5.600  26.176  1.00 20.60  ? 224 LEU A H    1 
ATOM   3074  H  HA   . LEU A 1 206 ? 14.661  -7.717  26.282  1.00 21.35  ? 224 LEU A HA   1 
ATOM   3075  H  HB2  . LEU A 1 206 ? 15.622  -6.147  28.411  1.00 23.37  ? 224 LEU A HB2  1 
ATOM   3076  H  HB3  . LEU A 1 206 ? 14.911  -7.553  28.619  1.00 23.37  ? 224 LEU A HB3  1 
ATOM   3077  H  HG   . LEU A 1 206 ? 17.417  -7.271  27.352  1.00 25.06  ? 224 LEU A HG   1 
ATOM   3078  H  HD11 . LEU A 1 206 ? 16.879  -8.034  30.011  1.00 25.92  ? 224 LEU A HD11 1 
ATOM   3079  H  HD12 . LEU A 1 206 ? 18.313  -8.163  29.339  1.00 25.92  ? 224 LEU A HD12 1 
ATOM   3080  H  HD13 . LEU A 1 206 ? 17.671  -6.729  29.573  1.00 25.92  ? 224 LEU A HD13 1 
ATOM   3081  H  HD21 . LEU A 1 206 ? 17.541  -9.608  27.625  1.00 27.98  ? 224 LEU A HD21 1 
ATOM   3082  H  HD22 . LEU A 1 206 ? 16.014  -9.592  28.059  1.00 27.98  ? 224 LEU A HD22 1 
ATOM   3083  H  HD23 . LEU A 1 206 ? 16.426  -9.156  26.588  1.00 27.98  ? 224 LEU A HD23 1 
ATOM   3084  N  N    . ASP A 1 207 ? 13.117  -5.016  26.843  1.00 16.07  ? 225 ASP A N    1 
ATOM   3085  C  CA   . ASP A 1 207 ? 11.873  -4.403  27.282  1.00 15.57  ? 225 ASP A CA   1 
ATOM   3086  C  C    . ASP A 1 207 ? 10.723  -4.775  26.356  1.00 14.79  ? 225 ASP A C    1 
ATOM   3087  O  O    . ASP A 1 207 ? 10.882  -4.856  25.134  1.00 14.71  ? 225 ASP A O    1 
ATOM   3088  C  CB   . ASP A 1 207 ? 12.028  -2.879  27.323  1.00 15.74  ? 225 ASP A CB   1 
ATOM   3089  C  CG   . ASP A 1 207 ? 13.097  -2.422  28.308  1.00 16.34  ? 225 ASP A CG   1 
ATOM   3090  O  OD1  . ASP A 1 207 ? 13.470  -3.217  29.193  1.00 18.15  ? 225 ASP A OD1  1 
ATOM   3091  O  OD2  . ASP A 1 207 ? 13.548  -1.257  28.211  1.00 17.38  ? 225 ASP A OD2  1 
ATOM   3092  H  H    . ASP A 1 207 ? 13.679  -4.465  26.495  1.00 19.29  ? 225 ASP A H    1 
ATOM   3093  H  HA   . ASP A 1 207 ? 11.658  -4.722  28.172  1.00 18.69  ? 225 ASP A HA   1 
ATOM   3094  H  HB2  . ASP A 1 207 ? 12.278  -2.562  26.441  1.00 18.89  ? 225 ASP A HB2  1 
ATOM   3095  H  HB3  . ASP A 1 207 ? 11.184  -2.482  27.591  1.00 18.89  ? 225 ASP A HB3  1 
ATOM   3096  N  N    . SER A 1 208 ? 9.546   -4.982  26.946  1.00 14.81  ? 226 SER A N    1 
ATOM   3097  C  CA   . SER A 1 208 ? 8.396   -5.384  26.144  1.00 13.41  ? 226 SER A CA   1 
ATOM   3098  C  C    . SER A 1 208 ? 8.029   -4.340  25.092  1.00 13.51  ? 226 SER A C    1 
ATOM   3099  O  O    . SER A 1 208 ? 7.531   -4.695  24.019  1.00 13.85  ? 226 SER A O    1 
ATOM   3100  C  CB   . SER A 1 208 ? 7.206   -5.711  27.042  1.00 14.68  ? 226 SER A CB   1 
ATOM   3101  O  OG   . SER A 1 208 ? 6.139   -6.231  26.261  1.00 14.98  ? 226 SER A OG   1 
ATOM   3102  H  H    . SER A 1 208 ? 9.392   -4.899  27.788  1.00 17.77  ? 226 SER A H    1 
ATOM   3103  H  HA   . SER A 1 208 ? 8.627   -6.196  25.666  1.00 16.09  ? 226 SER A HA   1 
ATOM   3104  H  HB2  . SER A 1 208 ? 7.474   -6.374  27.698  1.00 17.61  ? 226 SER A HB2  1 
ATOM   3105  H  HB3  . SER A 1 208 ? 6.911   -4.903  27.489  1.00 17.61  ? 226 SER A HB3  1 
ATOM   3106  H  HG   . SER A 1 208 ? 5.493   -6.436  26.757  1.00 17.98  ? 226 SER A HG   1 
ATOM   3107  N  N    . SER A 1 209 ? 8.265   -3.057  25.368  1.00 13.40  ? 227 SER A N    1 
ATOM   3108  C  CA   . SER A 1 209 ? 7.896   -2.004  24.430  1.00 14.62  ? 227 SER A CA   1 
ATOM   3109  C  C    . SER A 1 209 ? 8.943   -1.741  23.346  1.00 14.37  ? 227 SER A C    1 
ATOM   3110  O  O    . SER A 1 209 ? 8.702   -0.896  22.479  1.00 14.28  ? 227 SER A O    1 
ATOM   3111  C  CB   . SER A 1 209 ? 7.665   -0.699  25.197  1.00 13.60  ? 227 SER A CB   1 
ATOM   3112  O  OG   . SER A 1 209 ? 6.502   -0.732  26.006  1.00 14.56  ? 227 SER A OG   1 
ATOM   3113  H  H    . SER A 1 209 ? 8.637   -2.775  26.090  1.00 16.08  ? 227 SER A H    1 
ATOM   3114  H  HA   . SER A 1 209 ? 7.076   -2.276  23.989  1.00 17.55  ? 227 SER A HA   1 
ATOM   3115  H  HB2  . SER A 1 209 ? 8.432   -0.537  25.768  1.00 16.32  ? 227 SER A HB2  1 
ATOM   3116  H  HB3  . SER A 1 209 ? 7.572   0.023   24.555  1.00 16.32  ? 227 SER A HB3  1 
ATOM   3117  H  HG   . SER A 1 209 ? 5.819   -0.812  25.524  1.00 17.48  ? 227 SER A HG   1 
ATOM   3118  N  N    . TYR A 1 210 ? 10.090  -2.421  23.366  1.00 14.32  ? 228 TYR A N    1 
ATOM   3119  C  CA   . TYR A 1 210 ? 11.201  -2.068  22.488  1.00 15.18  ? 228 TYR A CA   1 
ATOM   3120  C  C    . TYR A 1 210 ? 11.054  -2.721  21.117  1.00 14.64  ? 228 TYR A C    1 
ATOM   3121  O  O    . TYR A 1 210 ? 10.742  -3.912  21.013  1.00 15.20  ? 228 TYR A O    1 
ATOM   3122  C  CB   . TYR A 1 210 ? 12.502  -2.522  23.145  1.00 15.27  ? 228 TYR A CB   1 
ATOM   3123  C  CG   . TYR A 1 210 ? 13.793  -2.075  22.497  1.00 15.66  ? 228 TYR A CG   1 
ATOM   3124  C  CD1  . TYR A 1 210 ? 14.253  -2.659  21.322  1.00 15.40  ? 228 TYR A CD1  1 
ATOM   3125  C  CD2  . TYR A 1 210 ? 14.582  -1.108  23.094  1.00 15.10  ? 228 TYR A CD2  1 
ATOM   3126  C  CE1  . TYR A 1 210 ? 15.453  -2.269  20.748  1.00 17.56  ? 228 TYR A CE1  1 
ATOM   3127  C  CE2  . TYR A 1 210 ? 15.783  -0.708  22.531  1.00 16.52  ? 228 TYR A CE2  1 
ATOM   3128  C  CZ   . TYR A 1 210 ? 16.217  -1.294  21.360  1.00 18.20  ? 228 TYR A CZ   1 
ATOM   3129  O  OH   . TYR A 1 210 ? 17.415  -0.893  20.806  1.00 21.68  ? 228 TYR A OH   1 
ATOM   3130  H  H    . TYR A 1 210 ? 10.248  -3.092  23.880  1.00 17.18  ? 228 TYR A H    1 
ATOM   3131  H  HA   . TYR A 1 210 ? 11.214  -1.108  22.347  1.00 18.21  ? 228 TYR A HA   1 
ATOM   3132  H  HB2  . TYR A 1 210 ? 12.511  -2.184  24.054  1.00 18.32  ? 228 TYR A HB2  1 
ATOM   3133  H  HB3  . TYR A 1 210 ? 12.510  -3.492  23.152  1.00 18.32  ? 228 TYR A HB3  1 
ATOM   3134  H  HD1  . TYR A 1 210 ? 13.746  -3.323  20.913  1.00 18.48  ? 228 TYR A HD1  1 
ATOM   3135  H  HD2  . TYR A 1 210 ? 14.301  -0.719  23.890  1.00 18.12  ? 228 TYR A HD2  1 
ATOM   3136  H  HE1  . TYR A 1 210 ? 15.743  -2.661  19.957  1.00 21.07  ? 228 TYR A HE1  1 
ATOM   3137  H  HE2  . TYR A 1 210 ? 16.294  -0.048  22.941  1.00 19.83  ? 228 TYR A HE2  1 
ATOM   3138  H  HH   . TYR A 1 210 ? 17.545  -1.295  20.080  1.00 26.02  ? 228 TYR A HH   1 
ATOM   3139  N  N    . LEU A 1 211 ? 11.289  -1.939  20.061  1.00 15.21  ? 229 LEU A N    1 
ATOM   3140  C  CA   . LEU A 1 211 ? 11.382  -2.464  18.704  1.00 14.68  ? 229 LEU A CA   1 
ATOM   3141  C  C    . LEU A 1 211 ? 12.732  -2.087  18.109  1.00 15.01  ? 229 LEU A C    1 
ATOM   3142  O  O    . LEU A 1 211 ? 13.133  -0.923  18.174  1.00 14.84  ? 229 LEU A O    1 
ATOM   3143  C  CB   . LEU A 1 211 ? 10.288  -1.895  17.796  1.00 14.37  ? 229 LEU A CB   1 
ATOM   3144  C  CG   . LEU A 1 211 ? 8.835   -2.286  18.070  1.00 14.91  ? 229 LEU A CG   1 
ATOM   3145  C  CD1  . LEU A 1 211 ? 7.917   -1.543  17.092  1.00 15.35  ? 229 LEU A CD1  1 
ATOM   3146  C  CD2  . LEU A 1 211 ? 8.602   -3.782  17.970  1.00 15.80  ? 229 LEU A CD2  1 
ATOM   3147  H  H    . LEU A 1 211 ? 11.400  -1.087  20.110  1.00 18.25  ? 229 LEU A H    1 
ATOM   3148  H  HA   . LEU A 1 211 ? 11.294  -3.429  18.746  1.00 17.62  ? 229 LEU A HA   1 
ATOM   3149  H  HB2  . LEU A 1 211 ? 10.330  -0.928  17.858  1.00 17.25  ? 229 LEU A HB2  1 
ATOM   3150  H  HB3  . LEU A 1 211 ? 10.484  -2.179  16.890  1.00 17.25  ? 229 LEU A HB3  1 
ATOM   3151  H  HG   . LEU A 1 211 ? 8.622   -2.035  18.983  1.00 17.89  ? 229 LEU A HG   1 
ATOM   3152  H  HD11 . LEU A 1 211 ? 6.998   -1.638  17.387  1.00 18.42  ? 229 LEU A HD11 1 
ATOM   3153  H  HD12 . LEU A 1 211 ? 8.164   -0.605  17.077  1.00 18.42  ? 229 LEU A HD12 1 
ATOM   3154  H  HD13 . LEU A 1 211 ? 8.022   -1.927  16.207  1.00 18.42  ? 229 LEU A HD13 1 
ATOM   3155  H  HD21 . LEU A 1 211 ? 9.121   -4.229  18.657  1.00 18.96  ? 229 LEU A HD21 1 
ATOM   3156  H  HD22 . LEU A 1 211 ? 7.658   -3.963  18.098  1.00 18.96  ? 229 LEU A HD22 1 
ATOM   3157  H  HD23 . LEU A 1 211 ? 8.882   -4.087  17.093  1.00 18.96  ? 229 LEU A HD23 1 
ATOM   3158  N  N    . PHE A 1 212 ? 13.412  -3.051  17.492  1.00 14.73  ? 230 PHE A N    1 
ATOM   3159  C  CA   . PHE A 1 212 ? 14.675  -2.732  16.837  1.00 15.04  ? 230 PHE A CA   1 
ATOM   3160  C  C    . PHE A 1 212 ? 14.445  -1.689  15.747  1.00 15.80  ? 230 PHE A C    1 
ATOM   3161  O  O    . PHE A 1 212 ? 13.462  -1.746  15.004  1.00 16.13  ? 230 PHE A O    1 
ATOM   3162  C  CB   . PHE A 1 212 ? 15.325  -3.984  16.249  1.00 16.47  ? 230 PHE A CB   1 
ATOM   3163  C  CG   . PHE A 1 212 ? 15.810  -4.950  17.289  1.00 16.88  ? 230 PHE A CG   1 
ATOM   3164  C  CD1  . PHE A 1 212 ? 16.935  -4.673  18.050  1.00 17.58  ? 230 PHE A CD1  1 
ATOM   3165  C  CD2  . PHE A 1 212 ? 15.116  -6.124  17.534  1.00 17.18  ? 230 PHE A CD2  1 
ATOM   3166  C  CE1  . PHE A 1 212 ? 17.369  -5.572  19.019  1.00 18.03  ? 230 PHE A CE1  1 
ATOM   3167  C  CE2  . PHE A 1 212 ? 15.542  -7.012  18.501  1.00 18.67  ? 230 PHE A CE2  1 
ATOM   3168  C  CZ   . PHE A 1 212 ? 16.664  -6.733  19.243  1.00 18.82  ? 230 PHE A CZ   1 
ATOM   3169  H  H    . PHE A 1 212 ? 13.169  -3.875  17.441  1.00 17.68  ? 230 PHE A H    1 
ATOM   3170  H  HA   . PHE A 1 212 ? 15.292  -2.370  17.492  1.00 18.05  ? 230 PHE A HA   1 
ATOM   3171  H  HB2  . PHE A 1 212 ? 14.674  -4.444  15.696  1.00 19.76  ? 230 PHE A HB2  1 
ATOM   3172  H  HB3  . PHE A 1 212 ? 16.087  -3.718  15.712  1.00 19.76  ? 230 PHE A HB3  1 
ATOM   3173  H  HD1  . PHE A 1 212 ? 17.403  -3.881  17.912  1.00 21.10  ? 230 PHE A HD1  1 
ATOM   3174  H  HD2  . PHE A 1 212 ? 14.353  -6.317  17.039  1.00 20.61  ? 230 PHE A HD2  1 
ATOM   3175  H  HE1  . PHE A 1 212 ? 18.134  -5.388  19.514  1.00 21.64  ? 230 PHE A HE1  1 
ATOM   3176  H  HE2  . PHE A 1 212 ? 15.069  -7.799  18.650  1.00 22.40  ? 230 PHE A HE2  1 
ATOM   3177  H  HZ   . PHE A 1 212 ? 16.948  -7.329  19.898  1.00 22.59  ? 230 PHE A HZ   1 
ATOM   3178  N  N    . ASN A 1 213 ? 15.359  -0.724  15.669  1.00 15.82  ? 231 ASN A N    1 
ATOM   3179  C  CA   . ASN A 1 213 ? 15.334  0.408   14.746  1.00 16.95  ? 231 ASN A CA   1 
ATOM   3180  C  C    . ASN A 1 213 ? 14.271  1.437   15.103  1.00 16.82  ? 231 ASN A C    1 
ATOM   3181  O  O    . ASN A 1 213 ? 14.205  2.489   14.460  1.00 18.19  ? 231 ASN A O    1 
ATOM   3182  C  CB   . ASN A 1 213 ? 15.213  -0.013  13.278  1.00 18.20  ? 231 ASN A CB   1 
ATOM   3183  C  CG   . ASN A 1 213 ? 16.363  -0.887  12.839  1.00 18.97  ? 231 ASN A CG   1 
ATOM   3184  O  OD1  . ASN A 1 213 ? 17.484  -0.739  13.328  1.00 20.27  ? 231 ASN A OD1  1 
ATOM   3185  N  ND2  . ASN A 1 213 ? 16.091  -1.823  11.934  1.00 20.56  ? 231 ASN A ND2  1 
ATOM   3186  H  H    . ASN A 1 213 ? 16.051  -0.705  16.179  1.00 18.98  ? 231 ASN A H    1 
ATOM   3187  H  HA   . ASN A 1 213 ? 16.187  0.864   14.818  1.00 20.35  ? 231 ASN A HA   1 
ATOM   3188  H  HB2  . ASN A 1 213 ? 14.391  -0.512  13.156  1.00 21.85  ? 231 ASN A HB2  1 
ATOM   3189  H  HB3  . ASN A 1 213 ? 15.206  0.780   12.719  1.00 21.85  ? 231 ASN A HB3  1 
ATOM   3190  H  HD21 . ASN A 1 213 ? 16.714  -2.345  11.654  1.00 24.67  ? 231 ASN A HD21 1 
ATOM   3191  H  HD22 . ASN A 1 213 ? 15.291  -1.906  11.629  1.00 24.67  ? 231 ASN A HD22 1 
ATOM   3192  N  N    . GLY A 1 214 ? 13.461  1.186   16.114  1.00 15.82  ? 232 GLY A N    1 
ATOM   3193  C  CA   . GLY A 1 214 ? 12.510  2.173   16.564  1.00 16.40  ? 232 GLY A CA   1 
ATOM   3194  C  C    . GLY A 1 214 ? 13.144  3.262   17.411  1.00 15.57  ? 232 GLY A C    1 
ATOM   3195  O  O    . GLY A 1 214 ? 14.302  3.205   17.822  1.00 17.38  ? 232 GLY A O    1 
ATOM   3196  H  H    . GLY A 1 214 ? 13.444  0.448   16.556  1.00 18.98  ? 232 GLY A H    1 
ATOM   3197  H  HA2  . GLY A 1 214 ? 12.096  2.590   15.793  1.00 19.68  ? 232 GLY A HA2  1 
ATOM   3198  H  HA3  . GLY A 1 214 ? 11.824  1.737   17.093  1.00 19.68  ? 232 GLY A HA3  1 
ATOM   3199  N  N    . LYS A 1 215 ? 12.346  4.284   17.685  1.00 14.88  ? 233 LYS A N    1 
ATOM   3200  C  CA   . LYS A 1 215 ? 12.712  5.326   18.641  1.00 14.20  ? 233 LYS A CA   1 
ATOM   3201  C  C    . LYS A 1 215 ? 12.093  4.891   19.960  1.00 14.31  ? 233 LYS A C    1 
ATOM   3202  O  O    . LYS A 1 215 ? 10.899  5.088   20.201  1.00 15.46  ? 233 LYS A O    1 
ATOM   3203  C  CB   . LYS A 1 215 ? 12.199  6.683   18.184  1.00 16.04  ? 233 LYS A CB   1 
ATOM   3204  C  CG   . LYS A 1 215 ? 12.524  7.823   19.135  1.00 17.74  ? 233 LYS A CG   1 
ATOM   3205  C  CD   . LYS A 1 215 ? 14.012  8.039   19.279  1.00 19.58  ? 233 LYS A CD   1 
ATOM   3206  C  CE   . LYS A 1 215 ? 14.298  9.397   19.898  1.00 22.66  ? 233 LYS A CE   1 
ATOM   3207  N  NZ   . LYS A 1 215 ? 15.684  9.473   20.412  1.00 25.17  ? 233 LYS A NZ   1 
ATOM   3208  H  H    . LYS A 1 215 ? 11.573  4.400   17.326  1.00 17.86  ? 233 LYS A H    1 
ATOM   3209  H  HA   . LYS A 1 215 ? 13.675  5.405   18.733  1.00 17.04  ? 233 LYS A HA   1 
ATOM   3210  H  HB2  . LYS A 1 215 ? 12.599  6.893   17.325  1.00 19.25  ? 233 LYS A HB2  1 
ATOM   3211  H  HB3  . LYS A 1 215 ? 11.234  6.637   18.098  1.00 19.25  ? 233 LYS A HB3  1 
ATOM   3212  H  HG2  . LYS A 1 215 ? 12.131  8.643   18.796  1.00 21.29  ? 233 LYS A HG2  1 
ATOM   3213  H  HG3  . LYS A 1 215 ? 12.162  7.620   20.012  1.00 21.29  ? 233 LYS A HG3  1 
ATOM   3214  H  HD2  . LYS A 1 215 ? 14.386  7.353   19.854  1.00 23.50  ? 233 LYS A HD2  1 
ATOM   3215  H  HD3  . LYS A 1 215 ? 14.431  8.004   18.405  1.00 23.50  ? 233 LYS A HD3  1 
ATOM   3216  H  HE2  . LYS A 1 215 ? 14.183  10.087  19.226  1.00 27.20  ? 233 LYS A HE2  1 
ATOM   3217  H  HE3  . LYS A 1 215 ? 13.689  9.549   20.637  1.00 27.20  ? 233 LYS A HE3  1 
ATOM   3218  H  HZ1  . LYS A 1 215 ? 15.852  10.293  20.715  1.00 30.20  ? 233 LYS A HZ1  1 
ATOM   3219  H  HZ2  . LYS A 1 215 ? 15.795  8.891   21.077  1.00 30.20  ? 233 LYS A HZ2  1 
ATOM   3220  H  HZ3  . LYS A 1 215 ? 16.261  9.282   19.762  1.00 30.20  ? 233 LYS A HZ3  1 
ATOM   3221  N  N    . ASN A 1 216 ? 12.902  4.255   20.792  1.00 14.09  ? 234 ASN A N    1 
ATOM   3222  C  CA   . ASN A 1 216 ? 12.443  3.613   22.013  1.00 14.05  ? 234 ASN A CA   1 
ATOM   3223  C  C    . ASN A 1 216 ? 12.769  4.565   23.152  1.00 14.16  ? 234 ASN A C    1 
ATOM   3224  O  O    . ASN A 1 216 ? 13.944  4.794   23.459  1.00 15.73  ? 234 ASN A O    1 
ATOM   3225  C  CB   . ASN A 1 216 ? 13.137  2.267   22.176  1.00 14.86  ? 234 ASN A CB   1 
ATOM   3226  C  CG   . ASN A 1 216 ? 12.816  1.311   21.038  1.00 15.40  ? 234 ASN A CG   1 
ATOM   3227  O  OD1  . ASN A 1 216 ? 11.673  0.884   20.868  1.00 15.12  ? 234 ASN A OD1  1 
ATOM   3228  N  ND2  . ASN A 1 216 ? 13.825  0.976   20.251  1.00 16.35  ? 234 ASN A ND2  1 
ATOM   3229  H  H    . ASN A 1 216 ? 13.749  4.179   20.666  1.00 16.91  ? 234 ASN A H    1 
ATOM   3230  H  HA   . ASN A 1 216 ? 11.485  3.456   22.001  1.00 16.86  ? 234 ASN A HA   1 
ATOM   3231  H  HB2  . ASN A 1 216 ? 14.097  2.405   22.193  1.00 17.84  ? 234 ASN A HB2  1 
ATOM   3232  H  HB3  . ASN A 1 216 ? 12.846  1.858   23.005  1.00 17.84  ? 234 ASN A HB3  1 
ATOM   3233  H  HD21 . ASN A 1 216 ? 13.696  0.438   19.593  1.00 19.62  ? 234 ASN A HD21 1 
ATOM   3234  H  HD22 . ASN A 1 216 ? 14.609  1.297   20.397  1.00 19.62  ? 234 ASN A HD22 1 
ATOM   3235  N  N    . VAL A 1 217 ? 11.729  5.142   23.745  1.00 14.56  ? 235 VAL A N    1 
ATOM   3236  C  CA   . VAL A 1 217 ? 11.858  6.217   24.722  1.00 15.27  ? 235 VAL A CA   1 
ATOM   3237  C  C    . VAL A 1 217 ? 11.319  5.687   26.046  1.00 15.55  ? 235 VAL A C    1 
ATOM   3238  O  O    . VAL A 1 217 ? 10.116  5.733   26.321  1.00 15.69  ? 235 VAL A O    1 
ATOM   3239  C  CB   . VAL A 1 217 ? 11.120  7.487   24.290  1.00 15.55  ? 235 VAL A CB   1 
ATOM   3240  C  CG1  . VAL A 1 217 ? 11.374  8.595   25.303  1.00 16.35  ? 235 VAL A CG1  1 
ATOM   3241  C  CG2  . VAL A 1 217 ? 11.558  7.902   22.898  1.00 17.09  ? 235 VAL A CG2  1 
ATOM   3242  H  H    . VAL A 1 217 ? 10.912  4.919   23.593  1.00 17.47  ? 235 VAL A H    1 
ATOM   3243  H  HA   . VAL A 1 217 ? 12.798  6.425   24.839  1.00 18.32  ? 235 VAL A HA   1 
ATOM   3244  H  HB   . VAL A 1 217 ? 10.166  7.317   24.258  1.00 18.66  ? 235 VAL A HB   1 
ATOM   3245  H  HG11 . VAL A 1 217 ? 12.185  8.394   25.794  1.00 19.62  ? 235 VAL A HG11 1 
ATOM   3246  H  HG12 . VAL A 1 217 ? 11.473  9.437   24.831  1.00 19.62  ? 235 VAL A HG12 1 
ATOM   3247  H  HG13 . VAL A 1 217 ? 10.621  8.644   25.913  1.00 19.62  ? 235 VAL A HG13 1 
ATOM   3248  H  HG21 . VAL A 1 217 ? 11.113  8.731   22.662  1.00 20.50  ? 235 VAL A HG21 1 
ATOM   3249  H  HG22 . VAL A 1 217 ? 12.519  8.031   22.895  1.00 20.50  ? 235 VAL A HG22 1 
ATOM   3250  H  HG23 . VAL A 1 217 ? 11.315  7.205   22.269  1.00 20.50  ? 235 VAL A HG23 1 
ATOM   3251  N  N    . GLN A 1 218 ? 12.211  5.161   26.873  1.00 16.14  ? 236 GLN A N    1 
ATOM   3252  C  CA   . GLN A 1 218 ? 11.878  4.849   28.254  1.00 16.22  ? 236 GLN A CA   1 
ATOM   3253  C  C    . GLN A 1 218 ? 11.974  6.140   29.057  1.00 16.85  ? 236 GLN A C    1 
ATOM   3254  O  O    . GLN A 1 218 ? 13.018  6.800   29.050  1.00 17.89  ? 236 GLN A O    1 
ATOM   3255  C  CB   . GLN A 1 218 ? 12.853  3.814   28.793  1.00 15.88  ? 236 GLN A CB   1 
ATOM   3256  C  CG   . GLN A 1 218 ? 12.457  3.273   30.146  1.00 16.13  ? 236 GLN A CG   1 
ATOM   3257  C  CD   . GLN A 1 218 ? 13.652  2.875   30.972  1.00 18.01  ? 236 GLN A CD   1 
ATOM   3258  O  OE1  . GLN A 1 218 ? 14.555  3.679   31.201  1.00 19.30  ? 236 GLN A OE1  1 
ATOM   3259  N  NE2  . GLN A 1 218 ? 13.675  1.627   31.412  1.00 18.06  ? 236 GLN A NE2  1 
ATOM   3260  H  H    . GLN A 1 218 ? 13.022  4.973   26.657  1.00 19.37  ? 236 GLN A H    1 
ATOM   3261  H  HA   . GLN A 1 218 ? 10.979  4.490   28.323  1.00 19.47  ? 236 GLN A HA   1 
ATOM   3262  H  HB2  . GLN A 1 218 ? 12.894  3.069   28.174  1.00 19.05  ? 236 GLN A HB2  1 
ATOM   3263  H  HB3  . GLN A 1 218 ? 13.729  4.222   28.879  1.00 19.05  ? 236 GLN A HB3  1 
ATOM   3264  H  HG2  . GLN A 1 218 ? 11.968  3.955   30.632  1.00 19.35  ? 236 GLN A HG2  1 
ATOM   3265  H  HG3  . GLN A 1 218 ? 11.899  2.488   30.025  1.00 19.35  ? 236 GLN A HG3  1 
ATOM   3266  H  HE21 . GLN A 1 218 ? 13.029  1.092   31.221  1.00 21.67  ? 236 GLN A HE21 1 
ATOM   3267  H  HE22 . GLN A 1 218 ? 14.336  1.351   31.888  1.00 21.67  ? 236 GLN A HE22 1 
ATOM   3268  N  N    . ALA A 1 219 ? 10.885  6.512   29.730  1.00 16.94  ? 237 ALA A N    1 
ATOM   3269  C  CA   . ALA A 1 219 ? 10.805  7.837   30.336  1.00 16.61  ? 237 ALA A CA   1 
ATOM   3270  C  C    . ALA A 1 219 ? 11.958  8.093   31.301  1.00 16.46  ? 237 ALA A C    1 
ATOM   3271  O  O    . ALA A 1 219 ? 12.481  9.210   31.368  1.00 16.77  ? 237 ALA A O    1 
ATOM   3272  C  CB   . ALA A 1 219 ? 9.468   7.982   31.059  1.00 17.52  ? 237 ALA A CB   1 
ATOM   3273  H  H    . ALA A 1 219 ? 10.188  6.021   29.848  1.00 20.33  ? 237 ALA A H    1 
ATOM   3274  H  HA   . ALA A 1 219 ? 10.858  8.504   29.634  1.00 19.94  ? 237 ALA A HA   1 
ATOM   3275  H  HB1  . ALA A 1 219 ? 9.404   7.298   31.744  1.00 21.02  ? 237 ALA A HB1  1 
ATOM   3276  H  HB2  . ALA A 1 219 ? 9.423   8.862   31.465  1.00 21.02  ? 237 ALA A HB2  1 
ATOM   3277  H  HB3  . ALA A 1 219 ? 8.749   7.876   30.417  1.00 21.02  ? 237 ALA A HB3  1 
ATOM   3278  N  N    . GLN A 1 220 ? 12.364  7.072   32.059  1.00 16.24  ? 238 GLN A N    1 
ATOM   3279  C  CA   . GLN A 1 220 ? 13.407  7.254   33.068  1.00 15.94  ? 238 GLN A CA   1 
ATOM   3280  C  C    . GLN A 1 220 ? 14.767  7.517   32.436  1.00 17.42  ? 238 GLN A C    1 
ATOM   3281  O  O    . GLN A 1 220 ? 15.631  8.147   33.059  1.00 18.84  ? 238 GLN A O    1 
ATOM   3282  C  CB   . GLN A 1 220 ? 13.463  6.013   33.962  1.00 16.15  ? 238 GLN A CB   1 
ATOM   3283  C  CG   . GLN A 1 220 ? 12.258  5.853   34.900  1.00 16.83  ? 238 GLN A CG   1 
ATOM   3284  C  CD   . GLN A 1 220 ? 10.987  5.407   34.190  1.00 16.01  ? 238 GLN A CD   1 
ATOM   3285  O  OE1  . GLN A 1 220 ? 11.028  4.850   33.088  1.00 15.64  ? 238 GLN A OE1  1 
ATOM   3286  N  NE2  . GLN A 1 220 ? 9.850   5.641   34.827  1.00 16.40  ? 238 GLN A NE2  1 
ATOM   3287  H  H    . GLN A 1 220 ? 12.055  6.271   32.010  1.00 19.48  ? 238 GLN A H    1 
ATOM   3288  H  HA   . GLN A 1 220 ? 13.188  8.022   33.618  1.00 19.13  ? 238 GLN A HA   1 
ATOM   3289  H  HB2  . GLN A 1 220 ? 13.502  5.226   33.397  1.00 19.38  ? 238 GLN A HB2  1 
ATOM   3290  H  HB3  . GLN A 1 220 ? 14.260  6.065   34.513  1.00 19.38  ? 238 GLN A HB3  1 
ATOM   3291  H  HG2  . GLN A 1 220 ? 12.471  5.188   35.573  1.00 20.19  ? 238 GLN A HG2  1 
ATOM   3292  H  HG3  . GLN A 1 220 ? 12.076  6.707   35.324  1.00 20.19  ? 238 GLN A HG3  1 
ATOM   3293  H  HE21 . GLN A 1 220 ? 9.859   6.025   35.596  1.00 19.68  ? 238 GLN A HE21 1 
ATOM   3294  H  HE22 . GLN A 1 220 ? 9.102   5.409   34.471  1.00 19.68  ? 238 GLN A HE22 1 
ATOM   3295  N  N    . ALA A 1 221 ? 14.979  7.055   31.205  1.00 17.73  ? 239 ALA A N    1 
ATOM   3296  C  CA   . ALA A 1 221 ? 16.237  7.347   30.534  1.00 19.08  ? 239 ALA A CA   1 
ATOM   3297  C  C    . ALA A 1 221 ? 16.395  8.833   30.243  1.00 20.38  ? 239 ALA A C    1 
ATOM   3298  O  O    . ALA A 1 221 ? 17.529  9.302   30.107  1.00 22.04  ? 239 ALA A O    1 
ATOM   3299  C  CB   . ALA A 1 221 ? 16.340  6.535   29.247  1.00 19.96  ? 239 ALA A CB   1 
ATOM   3300  H  H    . ALA A 1 221 ? 14.423  6.583   30.750  1.00 21.27  ? 239 ALA A H    1 
ATOM   3301  H  HA   . ALA A 1 221 ? 16.973  7.080   31.106  1.00 22.90  ? 239 ALA A HA   1 
ATOM   3302  H  HB1  . ALA A 1 221 ? 15.612  6.786   28.656  1.00 23.95  ? 239 ALA A HB1  1 
ATOM   3303  H  HB2  . ALA A 1 221 ? 17.191  6.724   28.821  1.00 23.95  ? 239 ALA A HB2  1 
ATOM   3304  H  HB3  . ALA A 1 221 ? 16.280  5.591   29.463  1.00 23.95  ? 239 ALA A HB3  1 
ATOM   3305  N  N    . VAL A 1 222 ? 15.294  9.574   30.150  1.00 20.58  ? 240 VAL A N    1 
ATOM   3306  C  CA   . VAL A 1 222 ? 15.329  11.018  29.957  1.00 21.30  ? 240 VAL A CA   1 
ATOM   3307  C  C    . VAL A 1 222 ? 15.175  11.767  31.274  1.00 20.35  ? 240 VAL A C    1 
ATOM   3308  O  O    . VAL A 1 222 ? 15.859  12.763  31.508  1.00 21.78  ? 240 VAL A O    1 
ATOM   3309  C  CB   . VAL A 1 222 ? 14.228  11.437  28.956  1.00 23.26  ? 240 VAL A CB   1 
ATOM   3310  C  CG1  . VAL A 1 222 ? 14.150  12.965  28.857  1.00 23.82  ? 240 VAL A CG1  1 
ATOM   3311  C  CG2  . VAL A 1 222 ? 14.459  10.795  27.601  1.00 24.47  ? 240 VAL A CG2  1 
ATOM   3312  H  H    . VAL A 1 222 ? 14.497  9.255   30.198  1.00 24.69  ? 240 VAL A H    1 
ATOM   3313  H  HA   . VAL A 1 222 ? 16.192  11.260  29.585  1.00 25.56  ? 240 VAL A HA   1 
ATOM   3314  H  HB   . VAL A 1 222 ? 13.369  11.122  29.278  1.00 27.91  ? 240 VAL A HB   1 
ATOM   3315  H  HG11 . VAL A 1 222 ? 13.662  13.205  28.054  1.00 28.58  ? 240 VAL A HG11 1 
ATOM   3316  H  HG12 . VAL A 1 222 ? 13.690  13.309  29.639  1.00 28.58  ? 240 VAL A HG12 1 
ATOM   3317  H  HG13 . VAL A 1 222 ? 15.050  13.325  28.818  1.00 28.58  ? 240 VAL A HG13 1 
ATOM   3318  H  HG21 . VAL A 1 222 ? 15.200  10.173  27.669  1.00 29.36  ? 240 VAL A HG21 1 
ATOM   3319  H  HG22 . VAL A 1 222 ? 13.655  10.324  27.334  1.00 29.36  ? 240 VAL A HG22 1 
ATOM   3320  H  HG23 . VAL A 1 222 ? 14.668  11.488  26.955  1.00 29.36  ? 240 VAL A HG23 1 
ATOM   3321  N  N    . CYS A 1 223 ? 14.271  11.298  32.135  1.00 19.40  ? 241 CYS A N    1 
ATOM   3322  C  CA   . CYS A 1 223 ? 13.819  12.038  33.302  1.00 19.08  ? 241 CYS A CA   1 
ATOM   3323  C  C    . CYS A 1 223 ? 14.501  11.608  34.592  1.00 19.15  ? 241 CYS A C    1 
ATOM   3324  O  O    . CYS A 1 223 ? 14.373  12.309  35.604  1.00 20.66  ? 241 CYS A O    1 
ATOM   3325  C  CB   . CYS A 1 223 ? 12.301  11.879  33.444  1.00 18.86  ? 241 CYS A CB   1 
ATOM   3326  S  SG   . CYS A 1 223 ? 11.395  12.550  32.027  1.00 19.70  ? 241 CYS A SG   1 
ATOM   3327  H  H    . CYS A 1 223 ? 13.896  10.528  32.058  1.00 23.27  ? 241 CYS A H    1 
ATOM   3328  H  HA   . CYS A 1 223 ? 14.017  12.979  33.178  1.00 22.89  ? 241 CYS A HA   1 
ATOM   3329  H  HB2  . CYS A 1 223 ? 12.088  10.936  33.519  1.00 22.64  ? 241 CYS A HB2  1 
ATOM   3330  H  HB3  . CYS A 1 223 ? 12.008  12.350  34.240  1.00 22.64  ? 241 CYS A HB3  1 
ATOM   3331  N  N    . GLY A 1 224 ? 15.214  10.487  34.580  1.00 19.44  ? 242 GLY A N    1 
ATOM   3332  C  CA   . GLY A 1 224 ? 15.930  10.028  35.742  1.00 20.17  ? 242 GLY A CA   1 
ATOM   3333  C  C    . GLY A 1 224 ? 15.313  8.775   36.317  1.00 20.69  ? 242 GLY A C    1 
ATOM   3334  O  O    . GLY A 1 224 ? 14.125  8.485   36.121  1.00 19.51  ? 242 GLY A O    1 
ATOM   3335  H  H    . GLY A 1 224 ? 15.296  9.973   33.896  1.00 23.33  ? 242 GLY A H    1 
ATOM   3336  H  HA2  . GLY A 1 224 ? 16.850  9.837   35.501  1.00 24.21  ? 242 GLY A HA2  1 
ATOM   3337  H  HA3  . GLY A 1 224 ? 15.918  10.718  36.423  1.00 24.21  ? 242 GLY A HA3  1 
ATOM   3338  N  N    . PRO A 1 225 ? 16.119  8.005   37.050  1.00 22.83  ? 243 PRO A N    1 
ATOM   3339  C  CA   . PRO A 1 225 ? 15.656  6.684   37.496  1.00 24.50  ? 243 PRO A CA   1 
ATOM   3340  C  C    . PRO A 1 225 ? 14.502  6.733   38.473  1.00 23.87  ? 243 PRO A C    1 
ATOM   3341  O  O    . PRO A 1 225 ? 13.805  5.723   38.610  1.00 25.23  ? 243 PRO A O    1 
ATOM   3342  C  CB   . PRO A 1 225 ? 16.906  6.055   38.124  1.00 25.34  ? 243 PRO A CB   1 
ATOM   3343  C  CG   . PRO A 1 225 ? 17.787  7.209   38.468  1.00 24.58  ? 243 PRO A CG   1 
ATOM   3344  C  CD   . PRO A 1 225 ? 17.514  8.273   37.443  1.00 24.33  ? 243 PRO A CD   1 
ATOM   3345  H  HA   . PRO A 1 225 ? 15.391  6.154   36.728  1.00 29.40  ? 243 PRO A HA   1 
ATOM   3346  H  HB2  . PRO A 1 225 ? 16.661  5.556   38.919  1.00 30.40  ? 243 PRO A HB2  1 
ATOM   3347  H  HB3  . PRO A 1 225 ? 17.338  5.468   37.483  1.00 30.40  ? 243 PRO A HB3  1 
ATOM   3348  H  HG2  . PRO A 1 225 ? 17.570  7.529   39.358  1.00 29.49  ? 243 PRO A HG2  1 
ATOM   3349  H  HG3  . PRO A 1 225 ? 18.715  6.931   38.433  1.00 29.49  ? 243 PRO A HG3  1 
ATOM   3350  H  HD2  . PRO A 1 225 ? 17.600  9.158   37.830  1.00 29.20  ? 243 PRO A HD2  1 
ATOM   3351  H  HD3  . PRO A 1 225 ? 18.111  8.184   36.683  1.00 29.20  ? 243 PRO A HD3  1 
ATOM   3352  N  N    . LEU A 1 226 ? 14.264  7.858   39.146  1.00 21.81  ? 244 LEU A N    1 
ATOM   3353  C  CA   . LEU A 1 226 ? 13.203  7.955   40.139  1.00 21.72  ? 244 LEU A CA   1 
ATOM   3354  C  C    . LEU A 1 226 ? 11.947  8.641   39.607  1.00 21.86  ? 244 LEU A C    1 
ATOM   3355  O  O    . LEU A 1 226 ? 11.022  8.907   40.383  1.00 23.36  ? 244 LEU A O    1 
ATOM   3356  C  CB   . LEU A 1 226 ? 13.716  8.663   41.396  1.00 22.64  ? 244 LEU A CB   1 
ATOM   3357  C  CG   . LEU A 1 226 ? 15.006  8.097   42.008  1.00 23.74  ? 244 LEU A CG   1 
ATOM   3358  C  CD1  . LEU A 1 226 ? 15.342  8.813   43.304  1.00 25.64  ? 244 LEU A CD1  1 
ATOM   3359  C  CD2  . LEU A 1 226 ? 14.907  6.584   42.241  1.00 24.63  ? 244 LEU A CD2  1 
ATOM   3360  H  H    . LEU A 1 226 ? 14.711  8.586   39.041  1.00 26.17  ? 244 LEU A H    1 
ATOM   3361  H  HA   . LEU A 1 226 ? 12.944  7.057   40.399  1.00 26.06  ? 244 LEU A HA   1 
ATOM   3362  H  HB2  . LEU A 1 226 ? 13.888  9.591   41.171  1.00 27.17  ? 244 LEU A HB2  1 
ATOM   3363  H  HB3  . LEU A 1 226 ? 13.028  8.609   42.077  1.00 27.17  ? 244 LEU A HB3  1 
ATOM   3364  H  HG   . LEU A 1 226 ? 15.729  8.246   41.378  1.00 28.49  ? 244 LEU A HG   1 
ATOM   3365  H  HD11 . LEU A 1 226 ? 15.606  9.724   43.103  1.00 30.77  ? 244 LEU A HD11 1 
ATOM   3366  H  HD12 . LEU A 1 226 ? 14.558  8.815   43.876  1.00 30.77  ? 244 LEU A HD12 1 
ATOM   3367  H  HD13 . LEU A 1 226 ? 16.070  8.347   43.743  1.00 30.77  ? 244 LEU A HD13 1 
ATOM   3368  H  HD21 . LEU A 1 226 ? 14.840  6.136   41.383  1.00 29.55  ? 244 LEU A HD21 1 
ATOM   3369  H  HD22 . LEU A 1 226 ? 15.702  6.284   42.709  1.00 29.55  ? 244 LEU A HD22 1 
ATOM   3370  H  HD23 . LEU A 1 226 ? 14.119  6.398   42.774  1.00 29.55  ? 244 LEU A HD23 1 
ATOM   3371  N  N    . PHE A 1 227 ? 11.896  8.930   38.306  1.00 19.93  ? 245 PHE A N    1 
ATOM   3372  C  CA   . PHE A 1 227 ? 10.684  9.445   37.677  1.00 18.15  ? 245 PHE A CA   1 
ATOM   3373  C  C    . PHE A 1 227 ? 9.657   8.329   37.556  1.00 17.80  ? 245 PHE A C    1 
ATOM   3374  O  O    . PHE A 1 227 ? 9.988   7.216   37.138  1.00 19.26  ? 245 PHE A O    1 
ATOM   3375  C  CB   . PHE A 1 227 ? 11.037  9.983   36.290  1.00 18.34  ? 245 PHE A CB   1 
ATOM   3376  C  CG   . PHE A 1 227 ? 9.892   10.631  35.562  1.00 18.58  ? 245 PHE A CG   1 
ATOM   3377  C  CD1  . PHE A 1 227 ? 9.473   11.901  35.902  1.00 20.38  ? 245 PHE A CD1  1 
ATOM   3378  C  CD2  . PHE A 1 227 ? 9.258   9.982   34.517  1.00 19.36  ? 245 PHE A CD2  1 
ATOM   3379  C  CE1  . PHE A 1 227 ? 8.431   12.506  35.227  1.00 21.19  ? 245 PHE A CE1  1 
ATOM   3380  C  CE2  . PHE A 1 227 ? 8.212   10.584  33.836  1.00 20.41  ? 245 PHE A CE2  1 
ATOM   3381  C  CZ   . PHE A 1 227 ? 7.803   11.851  34.192  1.00 21.09  ? 245 PHE A CZ   1 
ATOM   3382  H  H    . PHE A 1 227 ? 12.556  8.835   37.763  1.00 23.91  ? 245 PHE A H    1 
ATOM   3383  H  HA   . PHE A 1 227 ? 10.302  10.161  38.208  1.00 21.78  ? 245 PHE A HA   1 
ATOM   3384  H  HB2  . PHE A 1 227 ? 11.737  10.648  36.385  1.00 22.01  ? 245 PHE A HB2  1 
ATOM   3385  H  HB3  . PHE A 1 227 ? 11.352  9.246   35.744  1.00 22.01  ? 245 PHE A HB3  1 
ATOM   3386  H  HD1  . PHE A 1 227 ? 9.898   12.354  36.594  1.00 24.46  ? 245 PHE A HD1  1 
ATOM   3387  H  HD2  . PHE A 1 227 ? 9.538   9.131   34.268  1.00 23.23  ? 245 PHE A HD2  1 
ATOM   3388  H  HE1  . PHE A 1 227 ? 8.153   13.359  35.473  1.00 25.43  ? 245 PHE A HE1  1 
ATOM   3389  H  HE2  . PHE A 1 227 ? 7.788   10.135  33.141  1.00 24.50  ? 245 PHE A HE2  1 
ATOM   3390  H  HZ   . PHE A 1 227 ? 7.104   12.261  33.735  1.00 25.31  ? 245 PHE A HZ   1 
ATOM   3391  N  N    . VAL A 1 228 ? 8.410   8.622   37.912  1.00 16.87  ? 246 VAL A N    1 
ATOM   3392  C  CA   . VAL A 1 228 ? 7.356   7.612   37.963  1.00 17.23  ? 246 VAL A CA   1 
ATOM   3393  C  C    . VAL A 1 228 ? 6.177   8.052   37.099  1.00 16.84  ? 246 VAL A C    1 
ATOM   3394  O  O    . VAL A 1 228 ? 5.576   9.103   37.352  1.00 17.43  ? 246 VAL A O    1 
ATOM   3395  C  CB   . VAL A 1 228 ? 6.894   7.355   39.406  1.00 18.23  ? 246 VAL A CB   1 
ATOM   3396  C  CG1  . VAL A 1 228 ? 5.819   6.275   39.442  1.00 18.76  ? 246 VAL A CG1  1 
ATOM   3397  C  CG2  . VAL A 1 228 ? 8.067   6.973   40.287  1.00 18.48  ? 246 VAL A CG2  1 
ATOM   3398  H  H    . VAL A 1 228 ? 8.146   9.410   38.132  1.00 20.24  ? 246 VAL A H    1 
ATOM   3399  H  HA   . VAL A 1 228 ? 7.705   6.791   37.580  1.00 20.68  ? 246 VAL A HA   1 
ATOM   3400  H  HB   . VAL A 1 228 ? 6.510   8.173   39.757  1.00 21.87  ? 246 VAL A HB   1 
ATOM   3401  H  HG11 . VAL A 1 228 ? 5.027   6.603   38.988  1.00 22.51  ? 246 VAL A HG11 1 
ATOM   3402  H  HG12 . VAL A 1 228 ? 6.153   5.482   38.995  1.00 22.51  ? 246 VAL A HG12 1 
ATOM   3403  H  HG13 . VAL A 1 228 ? 5.610   6.070   40.367  1.00 22.51  ? 246 VAL A HG13 1 
ATOM   3404  H  HG21 . VAL A 1 228 ? 8.682   6.426   39.774  1.00 22.18  ? 246 VAL A HG21 1 
ATOM   3405  H  HG22 . VAL A 1 228 ? 8.513   7.781   40.586  1.00 22.18  ? 246 VAL A HG22 1 
ATOM   3406  H  HG23 . VAL A 1 228 ? 7.739   6.473   41.051  1.00 22.18  ? 246 VAL A HG23 1 
ATOM   3407  N  N    . ILE A 1 229 ? 5.845   7.241   36.090  1.00 16.44  ? 247 ILE A N    1 
ATOM   3408  C  CA   . ILE A 1 229 ? 4.530   7.251   35.446  1.00 16.80  ? 247 ILE A CA   1 
ATOM   3409  C  C    . ILE A 1 229 ? 4.100   5.796   35.260  1.00 16.08  ? 247 ILE A C    1 
ATOM   3410  O  O    . ILE A 1 229 ? 4.932   4.924   34.980  1.00 16.05  ? 247 ILE A O    1 
ATOM   3411  C  CB   . ILE A 1 229 ? 4.485   8.027   34.104  1.00 19.05  ? 247 ILE A CB   1 
ATOM   3412  C  CG1  . ILE A 1 229 ? 5.510   7.491   33.099  1.00 19.17  ? 247 ILE A CG1  1 
ATOM   3413  C  CG2  . ILE A 1 229 ? 4.656   9.539   34.333  1.00 19.79  ? 247 ILE A CG2  1 
ATOM   3414  C  CD1  . ILE A 1 229 ? 5.450   8.190   31.741  1.00 19.91  ? 247 ILE A CD1  1 
ATOM   3415  H  H    . ILE A 1 229 ? 6.381   6.660   35.752  1.00 19.73  ? 247 ILE A H    1 
ATOM   3416  H  HA   . ILE A 1 229 ? 3.905   7.704   36.033  1.00 20.16  ? 247 ILE A HA   1 
ATOM   3417  H  HB   . ILE A 1 229 ? 3.607   7.882   33.718  1.00 22.87  ? 247 ILE A HB   1 
ATOM   3418  H  HG12 . ILE A 1 229 ? 6.401   7.621   33.461  1.00 23.01  ? 247 ILE A HG12 1 
ATOM   3419  H  HG13 . ILE A 1 229 ? 5.345   6.547   32.956  1.00 23.01  ? 247 ILE A HG13 1 
ATOM   3420  H  HG21 . ILE A 1 229 ? 5.578   9.720   34.575  1.00 23.75  ? 247 ILE A HG21 1 
ATOM   3421  H  HG22 . ILE A 1 229 ? 4.431   10.010  33.516  1.00 23.75  ? 247 ILE A HG22 1 
ATOM   3422  H  HG23 . ILE A 1 229 ? 4.065   9.819   35.050  1.00 23.75  ? 247 ILE A HG23 1 
ATOM   3423  H  HD11 . ILE A 1 229 ? 6.036   8.963   31.757  1.00 23.90  ? 247 ILE A HD11 1 
ATOM   3424  H  HD12 . ILE A 1 229 ? 5.739   7.570   31.054  1.00 23.90  ? 247 ILE A HD12 1 
ATOM   3425  H  HD13 . ILE A 1 229 ? 4.537   8.470   31.570  1.00 23.90  ? 247 ILE A HD13 1 
ATOM   3426  N  N    . ASP A 1 230 ? 2.807   5.525   35.432  1.00 14.84  ? 248 ASP A N    1 
ATOM   3427  C  CA   . ASP A 1 230 ? 2.313   4.154   35.339  1.00 14.34  ? 248 ASP A CA   1 
ATOM   3428  C  C    . ASP A 1 230 ? 1.851   3.833   33.916  1.00 14.50  ? 248 ASP A C    1 
ATOM   3429  O  O    . ASP A 1 230 ? 2.174   4.537   32.955  1.00 15.23  ? 248 ASP A O    1 
ATOM   3430  C  CB   . ASP A 1 230 ? 1.289   3.849   36.438  1.00 15.94  ? 248 ASP A CB   1 
ATOM   3431  C  CG   . ASP A 1 230 ? 0.025   4.676   36.334  1.00 17.13  ? 248 ASP A CG   1 
ATOM   3432  O  OD1  . ASP A 1 230 ? -0.122  5.453   35.370  1.00 17.95  ? 248 ASP A OD1  1 
ATOM   3433  O  OD2  . ASP A 1 230 ? -0.824  4.546   37.245  1.00 17.37  ? 248 ASP A OD2  1 
ATOM   3434  H  H    . ASP A 1 230 ? 2.203   6.113   35.602  1.00 17.81  ? 248 ASP A H    1 
ATOM   3435  H  HA   . ASP A 1 230 ? 3.063   3.563   35.509  1.00 17.21  ? 248 ASP A HA   1 
ATOM   3436  H  HB2  . ASP A 1 230 ? 1.037   2.914   36.380  1.00 19.13  ? 248 ASP A HB2  1 
ATOM   3437  H  HB3  . ASP A 1 230 ? 1.693   4.031   37.301  1.00 19.13  ? 248 ASP A HB3  1 
ATOM   3438  N  N    . HIS A 1 231 ? 1.112   2.729   33.775  1.00 14.22  ? 249 HIS A N    1 
ATOM   3439  C  CA   . HIS A 1 231 ? 0.686   2.266   32.456  1.00 13.99  ? 249 HIS A CA   1 
ATOM   3440  C  C    . HIS A 1 231 ? -0.191  3.305   31.769  1.00 14.47  ? 249 HIS A C    1 
ATOM   3441  O  O    . HIS A 1 231 ? -0.006  3.607   30.585  1.00 15.42  ? 249 HIS A O    1 
ATOM   3442  C  CB   . HIS A 1 231 ? -0.060  0.937   32.610  1.00 14.80  ? 249 HIS A CB   1 
ATOM   3443  C  CG   . HIS A 1 231 ? -0.286  0.198   31.326  1.00 15.85  ? 249 HIS A CG   1 
ATOM   3444  N  ND1  . HIS A 1 231 ? 0.740   -0.194  30.492  1.00 15.70  ? 249 HIS A ND1  1 
ATOM   3445  C  CD2  . HIS A 1 231 ? -1.429  -0.239  30.743  1.00 16.84  ? 249 HIS A CD2  1 
ATOM   3446  C  CE1  . HIS A 1 231 ? 0.238   -0.830  29.447  1.00 16.91  ? 249 HIS A CE1  1 
ATOM   3447  N  NE2  . HIS A 1 231 ? -1.076  -0.867  29.573  1.00 17.11  ? 249 HIS A NE2  1 
ATOM   3448  H  H    . HIS A 1 231 ? 0.846   2.233   34.425  1.00 17.07  ? 249 HIS A H    1 
ATOM   3449  H  HA   . HIS A 1 231 ? 1.463   2.119   31.893  1.00 16.78  ? 249 HIS A HA   1 
ATOM   3450  H  HB2  . HIS A 1 231 ? 0.456   0.359   33.194  1.00 17.77  ? 249 HIS A HB2  1 
ATOM   3451  H  HB3  . HIS A 1 231 ? -0.929  1.114   33.003  1.00 17.77  ? 249 HIS A HB3  1 
ATOM   3452  H  HD1  . HIS A 1 231 ? 1.576   -0.048  30.631  1.00 18.84  ? 249 HIS A HD1  1 
ATOM   3453  H  HD2  . HIS A 1 231 ? -2.292  -0.134  31.074  1.00 20.21  ? 249 HIS A HD2  1 
ATOM   3454  H  HE1  . HIS A 1 231 ? 0.728   -1.189  28.743  1.00 20.29  ? 249 HIS A HE1  1 
ATOM   3455  N  N    . ALA A 1 232 ? -1.142  3.874   32.506  1.00 14.42  ? 250 ALA A N    1 
ATOM   3456  C  CA   . ALA A 1 232 ? -1.998  4.920   31.956  1.00 14.29  ? 250 ALA A CA   1 
ATOM   3457  C  C    . ALA A 1 232 ? -1.248  6.245   31.807  1.00 14.20  ? 250 ALA A C    1 
ATOM   3458  O  O    . ALA A 1 232 ? -1.424  6.957   30.808  1.00 14.18  ? 250 ALA A O    1 
ATOM   3459  C  CB   . ALA A 1 232 ? -3.213  5.091   32.866  1.00 15.55  ? 250 ALA A CB   1 
ATOM   3460  H  H    . ALA A 1 232 ? -1.313  3.674   33.325  1.00 17.31  ? 250 ALA A H    1 
ATOM   3461  H  HA   . ALA A 1 232 ? -2.297  4.658   31.071  1.00 17.14  ? 250 ALA A HA   1 
ATOM   3462  H  HB1  . ALA A 1 232 ? -2.909  5.316   33.759  1.00 18.66  ? 250 ALA A HB1  1 
ATOM   3463  H  HB2  . ALA A 1 232 ? -3.772  5.803   32.517  1.00 18.66  ? 250 ALA A HB2  1 
ATOM   3464  H  HB3  . ALA A 1 232 ? -3.712  4.259   32.886  1.00 18.66  ? 250 ALA A HB3  1 
ATOM   3465  N  N    . GLY A 1 233 ? -0.405  6.592   32.783  1.00 13.08  ? 251 GLY A N    1 
ATOM   3466  C  CA   . GLY A 1 233 ? 0.375   7.814   32.674  1.00 14.97  ? 251 GLY A CA   1 
ATOM   3467  C  C    . GLY A 1 233 ? 1.297   7.824   31.472  1.00 13.83  ? 251 GLY A C    1 
ATOM   3468  O  O    . GLY A 1 233 ? 1.636   8.894   30.948  1.00 14.71  ? 251 GLY A O    1 
ATOM   3469  H  H    . GLY A 1 233 ? -0.272  6.142   33.504  1.00 15.69  ? 251 GLY A H    1 
ATOM   3470  H  HA2  . GLY A 1 233 ? -0.227  8.571   32.601  1.00 17.96  ? 251 GLY A HA2  1 
ATOM   3471  H  HA3  . GLY A 1 233 ? 0.917   7.918   33.472  1.00 17.96  ? 251 GLY A HA3  1 
ATOM   3472  N  N    . SER A 1 234 ? 1.725   6.640   31.021  1.00 14.32  ? 252 SER A N    1 
ATOM   3473  C  CA   . SER A 1 234 ? 2.512   6.554   29.795  1.00 14.44  ? 252 SER A CA   1 
ATOM   3474  C  C    . SER A 1 234 ? 1.757   7.136   28.609  1.00 14.24  ? 252 SER A C    1 
ATOM   3475  O  O    . SER A 1 234 ? 2.372   7.685   27.689  1.00 14.86  ? 252 SER A O    1 
ATOM   3476  C  CB   . SER A 1 234 ? 2.892   5.098   29.524  1.00 14.69  ? 252 SER A CB   1 
ATOM   3477  O  OG   . SER A 1 234 ? 3.689   4.578   30.574  1.00 15.44  ? 252 SER A OG   1 
ATOM   3478  H  H    . SER A 1 234 ? 1.575   5.884   31.403  1.00 17.18  ? 252 SER A H    1 
ATOM   3479  H  HA   . SER A 1 234 ? 3.330   7.063   29.907  1.00 17.33  ? 252 SER A HA   1 
ATOM   3480  H  HB2  . SER A 1 234 ? 2.082   4.569   29.451  1.00 17.63  ? 252 SER A HB2  1 
ATOM   3481  H  HB3  . SER A 1 234 ? 3.394   5.052   28.695  1.00 17.63  ? 252 SER A HB3  1 
ATOM   3482  H  HG   . SER A 1 234 ? 3.955   3.806   30.377  1.00 18.53  ? 252 SER A HG   1 
ATOM   3483  N  N    . LEU A 1 235 ? 0.429   7.042   28.618  1.00 14.53  ? 253 LEU A N    1 
ATOM   3484  C  CA   . LEU A 1 235 ? -0.390  7.651   27.577  1.00 14.41  ? 253 LEU A CA   1 
ATOM   3485  C  C    . LEU A 1 235 ? -0.711  9.121   27.837  1.00 14.18  ? 253 LEU A C    1 
ATOM   3486  O  O    . LEU A 1 235 ? -0.738  9.914   26.889  1.00 15.91  ? 253 LEU A O    1 
ATOM   3487  C  CB   . LEU A 1 235 ? -1.706  6.876   27.453  1.00 13.49  ? 253 LEU A CB   1 
ATOM   3488  C  CG   . LEU A 1 235 ? -2.686  7.372   26.387  1.00 14.25  ? 253 LEU A CG   1 
ATOM   3489  C  CD1  . LEU A 1 235 ? -2.107  7.117   25.000  1.00 15.38  ? 253 LEU A CD1  1 
ATOM   3490  C  CD2  . LEU A 1 235 ? -4.030  6.690   26.550  1.00 13.71  ? 253 LEU A CD2  1 
ATOM   3491  H  H    . LEU A 1 235 ? -0.023  6.627   29.220  1.00 17.43  ? 253 LEU A H    1 
ATOM   3492  H  HA   . LEU A 1 235 ? 0.100   7.601   26.742  1.00 17.30  ? 253 LEU A HA   1 
ATOM   3493  H  HB2  . LEU A 1 235 ? -1.494  5.954   27.240  1.00 16.18  ? 253 LEU A HB2  1 
ATOM   3494  H  HB3  . LEU A 1 235 ? -2.164  6.923   28.307  1.00 16.18  ? 253 LEU A HB3  1 
ATOM   3495  H  HG   . LEU A 1 235 ? -2.827  8.327   26.486  1.00 17.10  ? 253 LEU A HG   1 
ATOM   3496  H  HD11 . LEU A 1 235 ? -2.775  7.339   24.333  1.00 18.46  ? 253 LEU A HD11 1 
ATOM   3497  H  HD12 . LEU A 1 235 ? -1.321  7.672   24.879  1.00 18.46  ? 253 LEU A HD12 1 
ATOM   3498  H  HD13 . LEU A 1 235 ? -1.864  6.180   24.927  1.00 18.46  ? 253 LEU A HD13 1 
ATOM   3499  H  HD21 . LEU A 1 235 ? -4.397  6.919   27.419  1.00 16.46  ? 253 LEU A HD21 1 
ATOM   3500  H  HD22 . LEU A 1 235 ? -4.626  6.994   25.849  1.00 16.46  ? 253 LEU A HD22 1 
ATOM   3501  H  HD23 . LEU A 1 235 ? -3.907  5.730   26.486  1.00 16.46  ? 253 LEU A HD23 1 
ATOM   3502  N  N    . THR A 1 236 ? -0.956  9.505   29.092  1.00 14.44  ? 254 THR A N    1 
ATOM   3503  C  CA   . THR A 1 236 ? -1.640  10.753  29.401  1.00 13.90  ? 254 THR A CA   1 
ATOM   3504  C  C    . THR A 1 236 ? -0.740  11.881  29.896  1.00 14.53  ? 254 THR A C    1 
ATOM   3505  O  O    . THR A 1 236 ? -1.209  13.020  29.970  1.00 15.61  ? 254 THR A O    1 
ATOM   3506  C  CB   . THR A 1 236 ? -2.682  10.523  30.502  1.00 15.33  ? 254 THR A CB   1 
ATOM   3507  O  OG1  . THR A 1 236 ? -1.998  10.124  31.701  1.00 15.55  ? 254 THR A OG1  1 
ATOM   3508  C  CG2  . THR A 1 236 ? -3.709  9.462   30.103  1.00 15.29  ? 254 THR A CG2  1 
ATOM   3509  H  H    . THR A 1 236 ? -0.731  9.051   29.787  1.00 17.33  ? 254 THR A H    1 
ATOM   3510  H  HA   . THR A 1 236 ? -2.065  11.040  28.578  1.00 16.68  ? 254 THR A HA   1 
ATOM   3511  H  HB   . THR A 1 236 ? -3.178  11.342  30.656  1.00 18.39  ? 254 THR A HB   1 
ATOM   3512  H  HG1  . THR A 1 236 ? -2.555  9.932   32.300  1.00 18.66  ? 254 THR A HG1  1 
ATOM   3513  H  HG21 . THR A 1 236 ? -3.277  8.598   30.016  1.00 18.35  ? 254 THR A HG21 1 
ATOM   3514  H  HG22 . THR A 1 236 ? -4.403  9.401   30.778  1.00 18.35  ? 254 THR A HG22 1 
ATOM   3515  H  HG23 . THR A 1 236 ? -4.117  9.697   29.254  1.00 18.35  ? 254 THR A HG23 1 
ATOM   3516  N  N    . SER A 1 237 ? 0.503   11.604  30.268  1.00 14.43  ? 255 SER A N    1 
ATOM   3517  C  CA   . SER A 1 237 ? 1.320   12.610  30.926  1.00 15.68  ? 255 SER A CA   1 
ATOM   3518  C  C    . SER A 1 237 ? 1.743   13.709  29.954  1.00 16.00  ? 255 SER A C    1 
ATOM   3519  O  O    . SER A 1 237 ? 1.722   13.553  28.725  1.00 16.46  ? 255 SER A O    1 
ATOM   3520  C  CB   . SER A 1 237 ? 2.560   11.965  31.551  1.00 15.82  ? 255 SER A CB   1 
ATOM   3521  O  OG   . SER A 1 237 ? 3.535   11.656  30.571  1.00 15.33  ? 255 SER A OG   1 
ATOM   3522  H  H    . SER A 1 237 ? 0.892   10.846  30.152  1.00 17.31  ? 255 SER A H    1 
ATOM   3523  H  HA   . SER A 1 237 ? 0.798   13.026  31.631  1.00 18.82  ? 255 SER A HA   1 
ATOM   3524  H  HB2  . SER A 1 237 ? 2.945   12.582  32.192  1.00 18.98  ? 255 SER A HB2  1 
ATOM   3525  H  HB3  . SER A 1 237 ? 2.295   11.145  31.998  1.00 18.98  ? 255 SER A HB3  1 
ATOM   3526  H  HG   . SER A 1 237 ? 3.224   11.103  30.020  1.00 18.40  ? 255 SER A HG   1 
ATOM   3527  N  N    . GLN A 1 238 ? 2.139   14.843  30.532  1.00 16.21  ? 256 GLN A N    1 
ATOM   3528  C  CA   . GLN A 1 238 ? 2.675   15.934  29.727  1.00 16.42  ? 256 GLN A CA   1 
ATOM   3529  C  C    . GLN A 1 238 ? 3.957   15.514  29.019  1.00 17.20  ? 256 GLN A C    1 
ATOM   3530  O  O    . GLN A 1 238 ? 4.172   15.866  27.855  1.00 17.72  ? 256 GLN A O    1 
ATOM   3531  C  CB   . GLN A 1 238 ? 2.910   17.153  30.616  1.00 16.64  ? 256 GLN A CB   1 
ATOM   3532  C  CG   . GLN A 1 238 ? 3.658   18.303  29.958  1.00 16.83  ? 256 GLN A CG   1 
ATOM   3533  C  CD   . GLN A 1 238 ? 2.888   18.959  28.828  1.00 18.83  ? 256 GLN A CD   1 
ATOM   3534  O  OE1  . GLN A 1 238 ? 1.678   18.782  28.691  1.00 18.74  ? 256 GLN A OE1  1 
ATOM   3535  N  NE2  . GLN A 1 238 ? 3.595   19.724  28.009  1.00 19.69  ? 256 GLN A NE2  1 
ATOM   3536  H  H    . GLN A 1 238 ? 2.108   15.002  31.376  1.00 19.45  ? 256 GLN A H    1 
ATOM   3537  H  HA   . GLN A 1 238 ? 2.032   16.180  29.044  1.00 19.71  ? 256 GLN A HA   1 
ATOM   3538  H  HB2  . GLN A 1 238 ? 2.048   17.494  30.902  1.00 19.97  ? 256 GLN A HB2  1 
ATOM   3539  H  HB3  . GLN A 1 238 ? 3.429   16.874  31.387  1.00 19.97  ? 256 GLN A HB3  1 
ATOM   3540  H  HG2  . GLN A 1 238 ? 3.840   18.981  30.627  1.00 20.19  ? 256 GLN A HG2  1 
ATOM   3541  H  HG3  . GLN A 1 238 ? 4.491   17.966  29.593  1.00 20.19  ? 256 GLN A HG3  1 
ATOM   3542  H  HE21 . GLN A 1 238 ? 4.440   19.824  28.136  1.00 23.63  ? 256 GLN A HE21 1 
ATOM   3543  H  HE22 . GLN A 1 238 ? 3.209   20.121  27.351  1.00 23.63  ? 256 GLN A HE22 1 
ATOM   3544  N  N    . PHE A 1 239 ? 4.824   14.763  29.703  1.00 17.61  ? 257 PHE A N    1 
ATOM   3545  C  CA   . PHE A 1 239 ? 6.012   14.235  29.041  1.00 17.04  ? 257 PHE A CA   1 
ATOM   3546  C  C    . PHE A 1 239 ? 5.620   13.428  27.810  1.00 16.14  ? 257 PHE A C    1 
ATOM   3547  O  O    . PHE A 1 239 ? 6.202   13.589  26.729  1.00 16.76  ? 257 PHE A O    1 
ATOM   3548  C  CB   . PHE A 1 239 ? 6.814   13.343  29.994  1.00 18.56  ? 257 PHE A CB   1 
ATOM   3549  C  CG   . PHE A 1 239 ? 8.058   12.776  29.374  1.00 18.56  ? 257 PHE A CG   1 
ATOM   3550  C  CD1  . PHE A 1 239 ? 9.140   13.601  29.099  1.00 18.07  ? 257 PHE A CD1  1 
ATOM   3551  C  CD2  . PHE A 1 239 ? 8.146   11.430  29.055  1.00 18.66  ? 257 PHE A CD2  1 
ATOM   3552  C  CE1  . PHE A 1 239 ? 10.287  13.100  28.520  1.00 19.43  ? 257 PHE A CE1  1 
ATOM   3553  C  CE2  . PHE A 1 239 ? 9.289   10.922  28.473  1.00 19.11  ? 257 PHE A CE2  1 
ATOM   3554  C  CZ   . PHE A 1 239 ? 10.365  11.763  28.206  1.00 20.06  ? 257 PHE A CZ   1 
ATOM   3555  H  H    . PHE A 1 239 ? 4.748   14.550  30.533  1.00 21.13  ? 257 PHE A H    1 
ATOM   3556  H  HA   . PHE A 1 239 ? 6.571   14.983  28.778  1.00 20.45  ? 257 PHE A HA   1 
ATOM   3557  H  HB2  . PHE A 1 239 ? 7.079   13.868  30.766  1.00 22.27  ? 257 PHE A HB2  1 
ATOM   3558  H  HB3  . PHE A 1 239 ? 6.256   12.601  30.274  1.00 22.27  ? 257 PHE A HB3  1 
ATOM   3559  H  HD1  . PHE A 1 239 ? 9.090   14.506  29.309  1.00 21.69  ? 257 PHE A HD1  1 
ATOM   3560  H  HD2  . PHE A 1 239 ? 7.429   10.865  29.234  1.00 22.39  ? 257 PHE A HD2  1 
ATOM   3561  H  HE1  . PHE A 1 239 ? 11.005  13.664  28.342  1.00 23.32  ? 257 PHE A HE1  1 
ATOM   3562  H  HE2  . PHE A 1 239 ? 9.341   10.018  28.261  1.00 22.93  ? 257 PHE A HE2  1 
ATOM   3563  H  HZ   . PHE A 1 239 ? 11.137  11.421  27.815  1.00 24.07  ? 257 PHE A HZ   1 
ATOM   3564  N  N    . SER A 1 240 ? 4.625   12.545  27.965  1.00 16.09  ? 258 SER A N    1 
ATOM   3565  C  CA   . SER A 1 240 ? 4.178   11.717  26.848  1.00 15.42  ? 258 SER A CA   1 
ATOM   3566  C  C    . SER A 1 240 ? 3.615   12.570  25.720  1.00 15.69  ? 258 SER A C    1 
ATOM   3567  O  O    . SER A 1 240 ? 3.808   12.259  24.539  1.00 16.54  ? 258 SER A O    1 
ATOM   3568  C  CB   . SER A 1 240 ? 3.130   10.709  27.328  1.00 15.37  ? 258 SER A CB   1 
ATOM   3569  O  OG   . SER A 1 240 ? 3.607   9.975   28.442  1.00 15.77  ? 258 SER A OG   1 
ATOM   3570  H  H    . SER A 1 240 ? 4.198   12.410  28.699  1.00 19.31  ? 258 SER A H    1 
ATOM   3571  H  HA   . SER A 1 240 ? 4.938   11.222  26.503  1.00 18.51  ? 258 SER A HA   1 
ATOM   3572  H  HB2  . SER A 1 240 ? 2.327   11.188  27.586  1.00 18.45  ? 258 SER A HB2  1 
ATOM   3573  H  HB3  . SER A 1 240 ? 2.932   10.093  26.606  1.00 18.45  ? 258 SER A HB3  1 
ATOM   3574  H  HG   . SER A 1 240 ? 3.013   9.447   28.713  1.00 18.93  ? 258 SER A HG   1 
ATOM   3575  N  N    . TYR A 1 241 ? 2.929   13.662  26.062  1.00 15.97  ? 259 TYR A N    1 
ATOM   3576  C  CA   . TYR A 1 241 ? 2.406   14.539  25.024  1.00 16.13  ? 259 TYR A CA   1 
ATOM   3577  C  C    . TYR A 1 241 ? 3.536   15.174  24.222  1.00 16.04  ? 259 TYR A C    1 
ATOM   3578  O  O    . TYR A 1 241 ? 3.463   15.262  22.991  1.00 16.80  ? 259 TYR A O    1 
ATOM   3579  C  CB   . TYR A 1 241 ? 1.525   15.628  25.632  1.00 17.39  ? 259 TYR A CB   1 
ATOM   3580  C  CG   . TYR A 1 241 ? 1.141   16.660  24.613  1.00 17.48  ? 259 TYR A CG   1 
ATOM   3581  C  CD1  . TYR A 1 241 ? 0.264   16.342  23.587  1.00 16.73  ? 259 TYR A CD1  1 
ATOM   3582  C  CD2  . TYR A 1 241 ? 1.684   17.939  24.642  1.00 18.66  ? 259 TYR A CD2  1 
ATOM   3583  C  CE1  . TYR A 1 241 ? -0.077  17.263  22.633  1.00 17.81  ? 259 TYR A CE1  1 
ATOM   3584  C  CE2  . TYR A 1 241 ? 1.343   18.870  23.689  1.00 19.60  ? 259 TYR A CE2  1 
ATOM   3585  C  CZ   . TYR A 1 241 ? 0.458   18.520  22.690  1.00 19.24  ? 259 TYR A CZ   1 
ATOM   3586  O  OH   . TYR A 1 241 ? 0.094   19.412  21.723  1.00 20.06  ? 259 TYR A OH   1 
ATOM   3587  H  H    . TYR A 1 241 ? 2.760   13.910  26.868  1.00 19.17  ? 259 TYR A H    1 
ATOM   3588  H  HA   . TYR A 1 241 ? 1.857   14.008  24.426  1.00 19.36  ? 259 TYR A HA   1 
ATOM   3589  H  HB2  . TYR A 1 241 ? 0.713   15.227  25.980  1.00 20.87  ? 259 TYR A HB2  1 
ATOM   3590  H  HB3  . TYR A 1 241 ? 2.009   16.070  26.347  1.00 20.87  ? 259 TYR A HB3  1 
ATOM   3591  H  HD1  . TYR A 1 241 ? -0.100  15.487  23.546  1.00 20.08  ? 259 TYR A HD1  1 
ATOM   3592  H  HD2  . TYR A 1 241 ? 2.285   18.168  25.314  1.00 22.39  ? 259 TYR A HD2  1 
ATOM   3593  H  HE1  . TYR A 1 241 ? -0.668  17.035  21.952  1.00 21.37  ? 259 TYR A HE1  1 
ATOM   3594  H  HE2  . TYR A 1 241 ? 1.705   19.726  23.718  1.00 23.52  ? 259 TYR A HE2  1 
ATOM   3595  H  HH   . TYR A 1 241 ? 0.571   20.101  21.773  1.00 24.07  ? 259 TYR A HH   1 
ATOM   3596  N  N    . VAL A 1 242 ? 4.591   15.628  24.900  1.00 15.80  ? 260 VAL A N    1 
ATOM   3597  C  CA   . VAL A 1 242 ? 5.697   16.260  24.186  1.00 16.67  ? 260 VAL A CA   1 
ATOM   3598  C  C    . VAL A 1 242 ? 6.351   15.270  23.232  1.00 16.12  ? 260 VAL A C    1 
ATOM   3599  O  O    . VAL A 1 242 ? 6.683   15.615  22.092  1.00 17.72  ? 260 VAL A O    1 
ATOM   3600  C  CB   . VAL A 1 242 ? 6.710   16.867  25.173  1.00 18.88  ? 260 VAL A CB   1 
ATOM   3601  C  CG1  . VAL A 1 242 ? 7.927   17.412  24.437  1.00 20.97  ? 260 VAL A CG1  1 
ATOM   3602  C  CG2  . VAL A 1 242 ? 6.036   17.955  25.959  1.00 18.80  ? 260 VAL A CG2  1 
ATOM   3603  H  H    . VAL A 1 242 ? 4.688   15.584  25.753  1.00 18.96  ? 260 VAL A H    1 
ATOM   3604  H  HA   . VAL A 1 242 ? 5.340   16.988  23.654  1.00 20.01  ? 260 VAL A HA   1 
ATOM   3605  H  HB   . VAL A 1 242 ? 7.023   16.179  25.782  1.00 22.65  ? 260 VAL A HB   1 
ATOM   3606  H  HG11 . VAL A 1 242 ? 8.369   16.683  23.974  1.00 25.17  ? 260 VAL A HG11 1 
ATOM   3607  H  HG12 . VAL A 1 242 ? 7.637   18.082  23.798  1.00 25.17  ? 260 VAL A HG12 1 
ATOM   3608  H  HG13 . VAL A 1 242 ? 8.534   17.810  25.081  1.00 25.17  ? 260 VAL A HG13 1 
ATOM   3609  H  HG21 . VAL A 1 242 ? 5.081   17.784  25.980  1.00 22.56  ? 260 VAL A HG21 1 
ATOM   3610  H  HG22 . VAL A 1 242 ? 6.391   17.959  26.862  1.00 22.56  ? 260 VAL A HG22 1 
ATOM   3611  H  HG23 . VAL A 1 242 ? 6.210   18.808  25.532  1.00 22.56  ? 260 VAL A HG23 1 
ATOM   3612  N  N    . VAL A 1 243 ? 6.568   14.031  23.686  1.00 16.16  ? 261 VAL A N    1 
ATOM   3613  C  CA   . VAL A 1 243 ? 7.169   13.029  22.813  1.00 17.01  ? 261 VAL A CA   1 
ATOM   3614  C  C    . VAL A 1 243 ? 6.232   12.699  21.657  1.00 16.00  ? 261 VAL A C    1 
ATOM   3615  O  O    . VAL A 1 243 ? 6.658   12.576  20.501  1.00 16.16  ? 261 VAL A O    1 
ATOM   3616  C  CB   . VAL A 1 243 ? 7.543   11.770  23.620  1.00 16.15  ? 261 VAL A CB   1 
ATOM   3617  C  CG1  . VAL A 1 243 ? 8.053   10.679  22.694  1.00 17.09  ? 261 VAL A CG1  1 
ATOM   3618  C  CG2  . VAL A 1 243 ? 8.584   12.100  24.693  1.00 18.21  ? 261 VAL A CG2  1 
ATOM   3619  H  H    . VAL A 1 243 ? 6.379   13.754  24.478  1.00 19.39  ? 261 VAL A H    1 
ATOM   3620  H  HA   . VAL A 1 243 ? 7.986   13.396  22.439  1.00 20.41  ? 261 VAL A HA   1 
ATOM   3621  H  HB   . VAL A 1 243 ? 6.749   11.442  24.069  1.00 19.38  ? 261 VAL A HB   1 
ATOM   3622  H  HG11 . VAL A 1 243 ? 7.312   10.341  22.167  1.00 20.51  ? 261 VAL A HG11 1 
ATOM   3623  H  HG12 . VAL A 1 243 ? 8.732   11.051  22.110  1.00 20.51  ? 261 VAL A HG12 1 
ATOM   3624  H  HG13 . VAL A 1 243 ? 8.432   9.963   23.228  1.00 20.51  ? 261 VAL A HG13 1 
ATOM   3625  H  HG21 . VAL A 1 243 ? 8.885   11.275  25.106  1.00 21.85  ? 261 VAL A HG21 1 
ATOM   3626  H  HG22 . VAL A 1 243 ? 9.334   12.554  24.278  1.00 21.85  ? 261 VAL A HG22 1 
ATOM   3627  H  HG23 . VAL A 1 243 ? 8.178   12.675  25.361  1.00 21.85  ? 261 VAL A HG23 1 
ATOM   3628  N  N    . GLY A 1 244 ? 4.943   12.537  21.950  1.00 15.87  ? 262 GLY A N    1 
ATOM   3629  C  CA   . GLY A 1 244 ? 3.990   12.230  20.897  1.00 15.93  ? 262 GLY A CA   1 
ATOM   3630  C  C    . GLY A 1 244 ? 3.864   13.342  19.872  1.00 15.77  ? 262 GLY A C    1 
ATOM   3631  O  O    . GLY A 1 244 ? 3.813   13.083  18.666  1.00 16.58  ? 262 GLY A O    1 
ATOM   3632  H  H    . GLY A 1 244 ? 4.603   12.598  22.738  1.00 19.05  ? 262 GLY A H    1 
ATOM   3633  H  HA2  . GLY A 1 244 ? 4.272   11.424  20.437  1.00 19.12  ? 262 GLY A HA2  1 
ATOM   3634  H  HA3  . GLY A 1 244 ? 3.117   12.080  21.291  1.00 19.12  ? 262 GLY A HA3  1 
ATOM   3635  N  N    . ARG A 1 245 ? 3.792   14.594  20.341  1.00 15.89  ? 263 ARG A N    1 
ATOM   3636  C  CA   . ARG A 1 245 ? 3.790   15.736  19.434  1.00 16.92  ? 263 ARG A CA   1 
ATOM   3637  C  C    . ARG A 1 245 ? 5.019   15.724  18.536  1.00 16.62  ? 263 ARG A C    1 
ATOM   3638  O  O    . ARG A 1 245 ? 4.921   15.977  17.331  1.00 18.10  ? 263 ARG A O    1 
ATOM   3639  C  CB   . ARG A 1 245 ? 3.730   17.035  20.240  1.00 18.08  ? 263 ARG A CB   1 
ATOM   3640  C  CG   . ARG A 1 245 ? 3.672   18.300  19.385  1.00 19.55  ? 263 ARG A CG   1 
ATOM   3641  C  CD   . ARG A 1 245 ? 3.631   19.553  20.252  1.00 20.94  ? 263 ARG A CD   1 
ATOM   3642  N  NE   . ARG A 1 245 ? 4.869   19.737  21.009  1.00 22.37  ? 263 ARG A NE   1 
ATOM   3643  C  CZ   . ARG A 1 245 ? 5.011   20.578  22.026  1.00 23.64  ? 263 ARG A CZ   1 
ATOM   3644  N  NH1  . ARG A 1 245 ? 3.996   21.334  22.410  1.00 24.71  ? 263 ARG A NH1  1 
ATOM   3645  N  NH2  . ARG A 1 245 ? 6.177   20.667  22.656  1.00 26.10  ? 263 ARG A NH2  1 
ATOM   3646  H  H    . ARG A 1 245 ? 3.743   14.803  21.173  1.00 19.07  ? 263 ARG A H    1 
ATOM   3647  H  HA   . ARG A 1 245 ? 3.003   15.691  18.868  1.00 20.31  ? 263 ARG A HA   1 
ATOM   3648  H  HB2  . ARG A 1 245 ? 2.936   17.019  20.796  1.00 21.69  ? 263 ARG A HB2  1 
ATOM   3649  H  HB3  . ARG A 1 245 ? 4.523   17.092  20.796  1.00 21.69  ? 263 ARG A HB3  1 
ATOM   3650  H  HG2  . ARG A 1 245 ? 4.460   18.344  18.821  1.00 23.46  ? 263 ARG A HG2  1 
ATOM   3651  H  HG3  . ARG A 1 245 ? 2.872   18.281  18.837  1.00 23.46  ? 263 ARG A HG3  1 
ATOM   3652  H  HD2  . ARG A 1 245 ? 3.505   20.329  19.684  1.00 25.12  ? 263 ARG A HD2  1 
ATOM   3653  H  HD3  . ARG A 1 245 ? 2.898   19.480  20.883  1.00 25.12  ? 263 ARG A HD3  1 
ATOM   3654  H  HE   . ARG A 1 245 ? 5.552   19.268  20.779  1.00 26.85  ? 263 ARG A HE   1 
ATOM   3655  H  HH11 . ARG A 1 245 ? 3.242   21.281  22.000  1.00 29.66  ? 263 ARG A HH11 1 
ATOM   3656  H  HH12 . ARG A 1 245 ? 4.090   21.878  23.069  1.00 29.66  ? 263 ARG A HH12 1 
ATOM   3657  H  HH21 . ARG A 1 245 ? 6.840   20.181  22.404  1.00 31.32  ? 263 ARG A HH21 1 
ATOM   3658  H  HH22 . ARG A 1 245 ? 6.269   21.212  23.315  1.00 31.32  ? 263 ARG A HH22 1 
ATOM   3659  N  N    . SER A 1 246 ? 6.185   15.421  19.103  1.00 17.08  ? 264 SER A N    1 
ATOM   3660  C  CA   . SER A 1 246 ? 7.400   15.361  18.297  1.00 18.01  ? 264 SER A CA   1 
ATOM   3661  C  C    . SER A 1 246 ? 7.299   14.271  17.236  1.00 17.26  ? 264 SER A C    1 
ATOM   3662  O  O    . SER A 1 246 ? 7.657   14.492  16.074  1.00 17.59  ? 264 SER A O    1 
ATOM   3663  C  CB   . SER A 1 246 ? 8.607   15.123  19.207  1.00 18.37  ? 264 SER A CB   1 
ATOM   3664  O  OG   . SER A 1 246 ? 9.771   14.808  18.461  1.00 19.10  ? 264 SER A OG   1 
ATOM   3665  H  H    . SER A 1 246 ? 6.298   15.248  19.938  1.00 20.49  ? 264 SER A H    1 
ATOM   3666  H  HA   . SER A 1 246 ? 7.526   16.208  17.842  1.00 21.61  ? 264 SER A HA   1 
ATOM   3667  H  HB2  . SER A 1 246 ? 8.774   15.927  19.722  1.00 22.04  ? 264 SER A HB2  1 
ATOM   3668  H  HB3  . SER A 1 246 ? 8.408   14.383  19.803  1.00 22.04  ? 264 SER A HB3  1 
ATOM   3669  H  HG   . SER A 1 246 ? 9.955   15.437  17.936  1.00 22.92  ? 264 SER A HG   1 
ATOM   3670  N  N    . ALA A 1 247 ? 6.800   13.090  17.613  1.00 17.45  ? 265 ALA A N    1 
ATOM   3671  C  CA   . ALA A 1 247 ? 6.688   11.997  16.655  1.00 17.50  ? 265 ALA A CA   1 
ATOM   3672  C  C    . ALA A 1 247 ? 5.727   12.346  15.527  1.00 17.56  ? 265 ALA A C    1 
ATOM   3673  O  O    . ALA A 1 247 ? 5.981   12.023  14.361  1.00 17.66  ? 265 ALA A O    1 
ATOM   3674  C  CB   . ALA A 1 247 ? 6.212   10.731  17.368  1.00 17.76  ? 265 ALA A CB   1 
ATOM   3675  H  H    . ALA A 1 247 ? 6.525   12.901  18.406  1.00 20.94  ? 265 ALA A H    1 
ATOM   3676  H  HA   . ALA A 1 247 ? 7.562   11.828  16.270  1.00 20.99  ? 265 ALA A HA   1 
ATOM   3677  H  HB1  . ALA A 1 247 ? 6.875   10.473  18.028  1.00 21.31  ? 265 ALA A HB1  1 
ATOM   3678  H  HB2  . ALA A 1 247 ? 5.365   10.914  17.804  1.00 21.31  ? 265 ALA A HB2  1 
ATOM   3679  H  HB3  . ALA A 1 247 ? 6.102   10.023  16.715  1.00 21.31  ? 265 ALA A HB3  1 
ATOM   3680  N  N    . LEU A 1 248 ? 4.613   13.001  15.856  1.00 18.32  ? 266 LEU A N    1 
ATOM   3681  C  CA   . LEU A 1 248 ? 3.621   13.312  14.837  1.00 18.85  ? 266 LEU A CA   1 
ATOM   3682  C  C    . LEU A 1 248 ? 4.124   14.378  13.877  1.00 20.01  ? 266 LEU A C    1 
ATOM   3683  O  O    . LEU A 1 248 ? 3.784   14.347  12.687  1.00 20.95  ? 266 LEU A O    1 
ATOM   3684  C  CB   . LEU A 1 248 ? 2.319   13.758  15.498  1.00 19.35  ? 266 LEU A CB   1 
ATOM   3685  C  CG   . LEU A 1 248 ? 1.565   12.668  16.267  1.00 19.50  ? 266 LEU A CG   1 
ATOM   3686  C  CD1  . LEU A 1 248 ? 0.350   13.258  16.966  1.00 20.76  ? 266 LEU A CD1  1 
ATOM   3687  C  CD2  . LEU A 1 248 ? 1.148   11.520  15.363  1.00 19.79  ? 266 LEU A CD2  1 
ATOM   3688  H  H    . LEU A 1 248 ? 4.413   13.270  16.648  1.00 21.98  ? 266 LEU A H    1 
ATOM   3689  H  HA   . LEU A 1 248 ? 3.435   12.511  14.321  1.00 22.62  ? 266 LEU A HA   1 
ATOM   3690  H  HB2  . LEU A 1 248 ? 2.524   14.467  16.127  1.00 23.22  ? 266 LEU A HB2  1 
ATOM   3691  H  HB3  . LEU A 1 248 ? 1.724   14.089  14.807  1.00 23.22  ? 266 LEU A HB3  1 
ATOM   3692  H  HG   . LEU A 1 248 ? 2.165   12.302  16.936  1.00 23.40  ? 266 LEU A HG   1 
ATOM   3693  H  HD11 . LEU A 1 248 ? -0.272  13.584  16.297  1.00 24.91  ? 266 LEU A HD11 1 
ATOM   3694  H  HD12 . LEU A 1 248 ? -0.072  12.569  17.502  1.00 24.91  ? 266 LEU A HD12 1 
ATOM   3695  H  HD13 . LEU A 1 248 ? 0.637   13.990  17.535  1.00 24.91  ? 266 LEU A HD13 1 
ATOM   3696  H  HD21 . LEU A 1 248 ? 1.938   11.027  15.093  1.00 23.74  ? 266 LEU A HD21 1 
ATOM   3697  H  HD22 . LEU A 1 248 ? 0.544   10.937  15.850  1.00 23.74  ? 266 LEU A HD22 1 
ATOM   3698  H  HD23 . LEU A 1 248 ? 0.700   11.881  14.581  1.00 23.74  ? 266 LEU A HD23 1 
ATOM   3699  N  N    . ARG A 1 249 ? 4.937   15.318  14.368  1.00 20.94  ? 267 ARG A N    1 
ATOM   3700  C  CA   . ARG A 1 249 ? 5.430   16.413  13.545  1.00 22.44  ? 267 ARG A CA   1 
ATOM   3701  C  C    . ARG A 1 249 ? 6.692   16.056  12.771  1.00 22.41  ? 267 ARG A C    1 
ATOM   3702  O  O    . ARG A 1 249 ? 6.989   16.704  11.762  1.00 24.09  ? 267 ARG A O    1 
ATOM   3703  C  CB   . ARG A 1 249 ? 5.718   17.644  14.419  1.00 27.21  ? 267 ARG A CB   1 
ATOM   3704  C  CG   . ARG A 1 249 ? 4.549   18.096  15.309  1.00 34.09  ? 267 ARG A CG   1 
ATOM   3705  C  CD   . ARG A 1 249 ? 3.609   19.093  14.626  1.00 38.04  ? 267 ARG A CD   1 
ATOM   3706  N  NE   . ARG A 1 249 ? 3.154   20.147  15.539  1.00 41.04  ? 267 ARG A NE   1 
ATOM   3707  C  CZ   . ARG A 1 249 ? 1.971   20.759  15.466  1.00 44.13  ? 267 ARG A CZ   1 
ATOM   3708  N  NH1  . ARG A 1 249 ? 1.091   20.423  14.524  1.00 44.78  ? 267 ARG A NH1  1 
ATOM   3709  N  NH2  . ARG A 1 249 ? 1.666   21.713  16.343  1.00 44.84  ? 267 ARG A NH2  1 
ATOM   3710  H  H    . ARG A 1 249 ? 5.217   15.338  15.181  1.00 25.12  ? 267 ARG A H    1 
ATOM   3711  H  HA   . ARG A 1 249 ? 4.741   16.650  12.905  1.00 26.93  ? 267 ARG A HA   1 
ATOM   3712  H  HB2  . ARG A 1 249 ? 6.465   17.440  15.002  1.00 32.65  ? 267 ARG A HB2  1 
ATOM   3713  H  HB3  . ARG A 1 249 ? 5.944   18.387  13.838  1.00 32.65  ? 267 ARG A HB3  1 
ATOM   3714  H  HG2  . ARG A 1 249 ? 4.025   17.318  15.558  1.00 40.91  ? 267 ARG A HG2  1 
ATOM   3715  H  HG3  . ARG A 1 249 ? 4.906   18.522  16.104  1.00 40.91  ? 267 ARG A HG3  1 
ATOM   3716  H  HD2  . ARG A 1 249 ? 4.076   19.515  13.887  1.00 45.65  ? 267 ARG A HD2  1 
ATOM   3717  H  HD3  . ARG A 1 249 ? 2.828   18.620  14.298  1.00 45.65  ? 267 ARG A HD3  1 
ATOM   3718  H  HE   . ARG A 1 249 ? 3.689   20.389  16.168  1.00 49.25  ? 267 ARG A HE   1 
ATOM   3719  H  HH11 . ARG A 1 249 ? 1.283   19.808  13.955  1.00 53.73  ? 267 ARG A HH11 1 
ATOM   3720  H  HH12 . ARG A 1 249 ? 0.330   20.823  14.484  1.00 53.73  ? 267 ARG A HH12 1 
ATOM   3721  H  HH21 . ARG A 1 249 ? 2.231   21.932  16.953  1.00 53.81  ? 267 ARG A HH21 1 
ATOM   3722  H  HH22 . ARG A 1 249 ? 0.904   22.109  16.299  1.00 53.81  ? 267 ARG A HH22 1 
ATOM   3723  N  N    . SER A 1 250 ? 7.418   15.029  13.194  1.00 21.73  ? 268 SER A N    1 
ATOM   3724  C  CA   . SER A 1 250 ? 8.748   14.785  12.660  1.00 21.91  ? 268 SER A CA   1 
ATOM   3725  C  C    . SER A 1 250 ? 8.702   14.329  11.210  1.00 22.84  ? 268 SER A C    1 
ATOM   3726  O  O    . SER A 1 250 ? 7.898   13.476  10.833  1.00 23.02  ? 268 SER A O    1 
ATOM   3727  C  CB   . SER A 1 250 ? 9.441   13.702  13.479  1.00 21.56  ? 268 SER A CB   1 
ATOM   3728  O  OG   . SER A 1 250 ? 10.642  13.302  12.850  1.00 21.88  ? 268 SER A OG   1 
ATOM   3729  H  H    . SER A 1 250 ? 7.163   14.461  13.788  1.00 26.08  ? 268 SER A H    1 
ATOM   3730  H  HA   . SER A 1 250 ? 9.250   15.614  12.705  1.00 26.29  ? 268 SER A HA   1 
ATOM   3731  H  HB2  . SER A 1 250 ? 9.646   14.053  14.360  1.00 25.87  ? 268 SER A HB2  1 
ATOM   3732  H  HB3  . SER A 1 250 ? 8.852   12.936  13.556  1.00 25.87  ? 268 SER A HB3  1 
ATOM   3733  H  HG   . SER A 1 250 ? 11.103  13.977  12.656  1.00 26.25  ? 268 SER A HG   1 
ATOM   3734  N  N    . THR A 1 251 ? 9.612   14.871  10.405  1.00 25.07  ? 269 THR A N    1 
ATOM   3735  C  CA   . THR A 1 251 ? 9.720   14.442  9.017   1.00 26.59  ? 269 THR A CA   1 
ATOM   3736  C  C    . THR A 1 251 ? 10.372  13.072  8.873   1.00 25.39  ? 269 THR A C    1 
ATOM   3737  O  O    . THR A 1 251 ? 10.304  12.489  7.787   1.00 27.96  ? 269 THR A O    1 
ATOM   3738  C  CB   . THR A 1 251 ? 10.485  15.485  8.198   1.00 29.87  ? 269 THR A CB   1 
ATOM   3739  O  OG1  . THR A 1 251 ? 11.784  15.687  8.764   1.00 31.19  ? 269 THR A OG1  1 
ATOM   3740  C  CG2  . THR A 1 251 ? 9.736   16.809  8.189   1.00 31.39  ? 269 THR A CG2  1 
ATOM   3741  H  H    . THR A 1 251 ? 10.172  15.481  10.636  1.00 30.08  ? 269 THR A H    1 
ATOM   3742  H  HA   . THR A 1 251 ? 8.828   14.378  8.642   1.00 31.90  ? 269 THR A HA   1 
ATOM   3743  H  HB   . THR A 1 251 ? 10.573  15.173  7.284   1.00 35.85  ? 269 THR A HB   1 
ATOM   3744  H  HG1  . THR A 1 251 ? 12.195  16.280  8.334   1.00 37.43  ? 269 THR A HG1  1 
ATOM   3745  H  HG21 . THR A 1 251 ? 9.840   17.256  9.044   1.00 37.67  ? 269 THR A HG21 1 
ATOM   3746  H  HG22 . THR A 1 251 ? 10.086  17.383  7.489   1.00 37.67  ? 269 THR A HG22 1 
ATOM   3747  H  HG23 . THR A 1 251 ? 8.792   16.656  8.027   1.00 37.67  ? 269 THR A HG23 1 
ATOM   3748  N  N    . THR A 1 252 ? 10.986  12.539  9.931   1.00 23.10  ? 270 THR A N    1 
ATOM   3749  C  CA   . THR A 1 252 ? 11.513  11.182  9.901   1.00 22.06  ? 270 THR A CA   1 
ATOM   3750  C  C    . THR A 1 252 ? 10.473  10.144  10.292  1.00 20.43  ? 270 THR A C    1 
ATOM   3751  O  O    . THR A 1 252 ? 10.733  8.942   10.158  1.00 21.62  ? 270 THR A O    1 
ATOM   3752  C  CB   . THR A 1 252 ? 12.691  11.024  10.872  1.00 22.62  ? 270 THR A CB   1 
ATOM   3753  O  OG1  . THR A 1 252 ? 12.209  11.082  12.222  1.00 22.65  ? 270 THR A OG1  1 
ATOM   3754  C  CG2  . THR A 1 252 ? 13.738  12.100  10.639  1.00 23.82  ? 270 THR A CG2  1 
ATOM   3755  H  H    . THR A 1 252 ? 11.108  12.947  10.678  1.00 27.72  ? 270 THR A H    1 
ATOM   3756  H  HA   . THR A 1 252 ? 11.829  11.013  8.999   1.00 26.48  ? 270 THR A HA   1 
ATOM   3757  H  HB   . THR A 1 252 ? 13.121  10.166  10.725  1.00 27.15  ? 270 THR A HB   1 
ATOM   3758  H  HG1  . THR A 1 252 ? 12.852  11.027  12.759  1.00 27.18  ? 270 THR A HG1  1 
ATOM   3759  H  HG21 . THR A 1 252 ? 14.094  12.028  9.740   1.00 28.58  ? 270 THR A HG21 1 
ATOM   3760  H  HG22 . THR A 1 252 ? 13.341  12.978  10.751  1.00 28.58  ? 270 THR A HG22 1 
ATOM   3761  H  HG23 . THR A 1 252 ? 14.464  12.000  11.274  1.00 28.58  ? 270 THR A HG23 1 
ATOM   3762  N  N    . GLY A 1 253 ? 9.315   10.571  10.790  1.00 18.89  ? 271 GLY A N    1 
ATOM   3763  C  CA   . GLY A 1 253 ? 8.319   9.645   11.284  1.00 17.59  ? 271 GLY A CA   1 
ATOM   3764  C  C    . GLY A 1 253 ? 8.527   9.165   12.706  1.00 17.28  ? 271 GLY A C    1 
ATOM   3765  O  O    . GLY A 1 253 ? 7.679   8.423   13.219  1.00 17.55  ? 271 GLY A O    1 
ATOM   3766  H  H    . GLY A 1 253 ? 9.088   11.399  10.851  1.00 22.67  ? 271 GLY A H    1 
ATOM   3767  H  HA2  . GLY A 1 253 ? 7.450   10.075  11.243  1.00 21.11  ? 271 GLY A HA2  1 
ATOM   3768  H  HA3  . GLY A 1 253 ? 8.312   8.864   10.708  1.00 21.11  ? 271 GLY A HA3  1 
ATOM   3769  N  N    . GLN A 1 254 ? 9.617   9.569   13.360  1.00 16.10  ? 272 GLN A N    1 
ATOM   3770  C  CA   . GLN A 1 254 ? 9.891   9.195   14.740  1.00 16.24  ? 272 GLN A CA   1 
ATOM   3771  C  C    . GLN A 1 254 ? 10.113  10.454  15.563  1.00 16.97  ? 272 GLN A C    1 
ATOM   3772  O  O    . GLN A 1 254 ? 10.556  11.475  15.037  1.00 17.78  ? 272 GLN A O    1 
ATOM   3773  C  CB   . GLN A 1 254 ? 11.174  8.359   14.859  1.00 17.12  ? 272 GLN A CB   1 
ATOM   3774  C  CG   . GLN A 1 254 ? 11.102  6.995   14.225  1.00 17.03  ? 272 GLN A CG   1 
ATOM   3775  C  CD   . GLN A 1 254 ? 12.411  6.247   14.342  1.00 19.22  ? 272 GLN A CD   1 
ATOM   3776  O  OE1  . GLN A 1 254 ? 13.477  6.853   14.452  1.00 23.32  ? 272 GLN A OE1  1 
ATOM   3777  N  NE2  . GLN A 1 254 ? 12.340  4.927   14.336  1.00 18.15  ? 272 GLN A NE2  1 
ATOM   3778  H  H    . GLN A 1 254 ? 10.223  10.071  13.015  1.00 19.32  ? 272 GLN A H    1 
ATOM   3779  H  HA   . GLN A 1 254 ? 9.134   8.692   15.080  1.00 19.49  ? 272 GLN A HA   1 
ATOM   3780  H  HB2  . GLN A 1 254 ? 11.897  8.842   14.429  1.00 20.54  ? 272 GLN A HB2  1 
ATOM   3781  H  HB3  . GLN A 1 254 ? 11.373  8.233   15.800  1.00 20.54  ? 272 GLN A HB3  1 
ATOM   3782  H  HG2  . GLN A 1 254 ? 10.414  6.474   14.668  1.00 20.43  ? 272 GLN A HG2  1 
ATOM   3783  H  HG3  . GLN A 1 254 ? 10.891  7.092   13.283  1.00 20.43  ? 272 GLN A HG3  1 
ATOM   3784  H  HE21 . GLN A 1 254 ? 11.576  4.538   14.268  1.00 21.78  ? 272 GLN A HE21 1 
ATOM   3785  H  HE22 . GLN A 1 254 ? 13.057  4.458   14.401  1.00 21.78  ? 272 GLN A HE22 1 
ATOM   3786  N  N    . ALA A 1 255 ? 9.833   10.370  16.863  1.00 17.39  ? 273 ALA A N    1 
ATOM   3787  C  CA   . ALA A 1 255 ? 10.180  11.470  17.755  1.00 17.01  ? 273 ALA A CA   1 
ATOM   3788  C  C    . ALA A 1 255 ? 11.682  11.738  17.699  1.00 18.45  ? 273 ALA A C    1 
ATOM   3789  O  O    . ALA A 1 255 ? 12.488  10.840  17.439  1.00 18.90  ? 273 ALA A O    1 
ATOM   3790  C  CB   . ALA A 1 255 ? 9.771   11.147  19.192  1.00 16.73  ? 273 ALA A CB   1 
ATOM   3791  H  H    . ALA A 1 255 ? 9.451   9.701   17.244  1.00 20.87  ? 273 ALA A H    1 
ATOM   3792  H  HA   . ALA A 1 255 ? 9.706   12.270  17.478  1.00 20.42  ? 273 ALA A HA   1 
ATOM   3793  H  HB1  . ALA A 1 255 ? 10.253  10.359  19.488  1.00 20.08  ? 273 ALA A HB1  1 
ATOM   3794  H  HB2  . ALA A 1 255 ? 9.991   11.902  19.760  1.00 20.08  ? 273 ALA A HB2  1 
ATOM   3795  H  HB3  . ALA A 1 255 ? 8.816   10.981  19.219  1.00 20.08  ? 273 ALA A HB3  1 
ATOM   3796  N  N    . ARG A 1 256 ? 12.057  12.988  17.962  1.00 18.77  ? 274 ARG A N    1 
ATOM   3797  C  CA   . ARG A 1 256 ? 13.444  13.431  17.894  1.00 20.57  ? 274 ARG A CA   1 
ATOM   3798  C  C    . ARG A 1 256 ? 13.889  13.919  19.264  1.00 19.98  ? 274 ARG A C    1 
ATOM   3799  O  O    . ARG A 1 256 ? 13.192  14.718  19.899  1.00 20.34  ? 274 ARG A O    1 
ATOM   3800  C  CB   . ARG A 1 256 ? 13.594  14.556  16.869  1.00 24.02  ? 274 ARG A CB   1 
ATOM   3801  C  CG   . ARG A 1 256 ? 13.056  14.211  15.488  1.00 28.49  ? 274 ARG A CG   1 
ATOM   3802  C  CD   . ARG A 1 256 ? 12.471  15.441  14.815  1.00 34.67  ? 274 ARG A CD   1 
ATOM   3803  N  NE   . ARG A 1 256 ? 11.162  15.773  15.375  1.00 38.89  ? 274 ARG A NE   1 
ATOM   3804  C  CZ   . ARG A 1 256 ? 10.348  16.707  14.896  1.00 38.73  ? 274 ARG A CZ   1 
ATOM   3805  N  NH1  . ARG A 1 256 ? 10.708  17.432  13.840  1.00 40.17  ? 274 ARG A NH1  1 
ATOM   3806  N  NH2  . ARG A 1 256 ? 9.176   16.917  15.487  1.00 34.70  ? 274 ARG A NH2  1 
ATOM   3807  H  H    . ARG A 1 256 ? 11.511  13.612  18.188  1.00 22.53  ? 274 ARG A H    1 
ATOM   3808  H  HA   . ARG A 1 256 ? 14.012  12.688  17.637  1.00 24.68  ? 274 ARG A HA   1 
ATOM   3809  H  HB2  . ARG A 1 256 ? 13.111  15.334  17.188  1.00 28.82  ? 274 ARG A HB2  1 
ATOM   3810  H  HB3  . ARG A 1 256 ? 14.537  14.767  16.774  1.00 28.82  ? 274 ARG A HB3  1 
ATOM   3811  H  HG2  . ARG A 1 256 ? 13.777  13.871  14.935  1.00 34.19  ? 274 ARG A HG2  1 
ATOM   3812  H  HG3  . ARG A 1 256 ? 12.358  13.543  15.570  1.00 34.19  ? 274 ARG A HG3  1 
ATOM   3813  H  HD2  . ARG A 1 256 ? 13.064  16.197  14.953  1.00 41.61  ? 274 ARG A HD2  1 
ATOM   3814  H  HD3  . ARG A 1 256 ? 12.365  15.271  13.866  1.00 41.61  ? 274 ARG A HD3  1 
ATOM   3815  H  HE   . ARG A 1 256 ? 10.899  15.331  16.065  1.00 46.66  ? 274 ARG A HE   1 
ATOM   3816  H  HH11 . ARG A 1 256 ? 11.470  17.296  13.465  1.00 48.21  ? 274 ARG A HH11 1 
ATOM   3817  H  HH12 . ARG A 1 256 ? 10.179  18.036  13.532  1.00 48.21  ? 274 ARG A HH12 1 
ATOM   3818  H  HH21 . ARG A 1 256 ? 8.951   16.451  16.173  1.00 41.64  ? 274 ARG A HH21 1 
ATOM   3819  H  HH22 . ARG A 1 256 ? 8.643   17.520  15.183  1.00 41.64  ? 274 ARG A HH22 1 
ATOM   3820  N  N    . SER A 1 257 ? 15.054  13.431  19.712  1.00 20.90  ? 275 SER A N    1 
ATOM   3821  C  CA   . SER A 1 257 ? 15.570  13.788  21.031  1.00 21.96  ? 275 SER A CA   1 
ATOM   3822  C  C    . SER A 1 257 ? 15.696  15.295  21.216  1.00 21.50  ? 275 SER A C    1 
ATOM   3823  O  O    . SER A 1 257 ? 15.581  15.793  22.344  1.00 22.19  ? 275 SER A O    1 
ATOM   3824  C  CB   . SER A 1 257 ? 16.947  13.157  21.233  1.00 23.32  ? 275 SER A CB   1 
ATOM   3825  O  OG   . SER A 1 257 ? 16.855  11.754  21.276  1.00 25.06  ? 275 SER A OG   1 
ATOM   3826  H  H    . SER A 1 257 ? 15.560  12.893  19.271  1.00 25.08  ? 275 SER A H    1 
ATOM   3827  H  HA   . SER A 1 257 ? 14.951  13.446  21.694  1.00 26.35  ? 275 SER A HA   1 
ATOM   3828  H  HB2  . SER A 1 257 ? 17.522  13.413  20.495  1.00 27.99  ? 275 SER A HB2  1 
ATOM   3829  H  HB3  . SER A 1 257 ? 17.320  13.475  22.070  1.00 27.99  ? 275 SER A HB3  1 
ATOM   3830  H  HG   . SER A 1 257 ? 17.624  11.415  21.272  1.00 30.07  ? 275 SER A HG   1 
ATOM   3831  N  N    . ALA A 1 258 ? 15.954  16.031  20.132  1.00 22.18  ? 276 ALA A N    1 
ATOM   3832  C  CA   . ALA A 1 258 ? 16.061  17.482  20.208  1.00 23.43  ? 276 ALA A CA   1 
ATOM   3833  C  C    . ALA A 1 258 ? 14.785  18.141  20.717  1.00 23.67  ? 276 ALA A C    1 
ATOM   3834  O  O    . ALA A 1 258 ? 14.852  19.254  21.261  1.00 25.11  ? 276 ALA A O    1 
ATOM   3835  C  CB   . ALA A 1 258 ? 16.393  18.030  18.820  1.00 25.05  ? 276 ALA A CB   1 
ATOM   3836  H  H    . ALA A 1 258 ? 16.071  15.712  19.343  1.00 26.61  ? 276 ALA A H    1 
ATOM   3837  H  HA   . ALA A 1 258 ? 16.774  17.711  20.824  1.00 28.12  ? 276 ALA A HA   1 
ATOM   3838  H  HB1  . ALA A 1 258 ? 15.682  17.787  18.206  1.00 30.06  ? 276 ALA A HB1  1 
ATOM   3839  H  HB2  . ALA A 1 258 ? 16.470  18.996  18.872  1.00 30.06  ? 276 ALA A HB2  1 
ATOM   3840  H  HB3  . ALA A 1 258 ? 17.233  17.647  18.522  1.00 30.06  ? 276 ALA A HB3  1 
ATOM   3841  N  N    . ASP A 1 259 ? 13.637  17.474  20.576  1.00 22.41  ? 277 ASP A N    1 
ATOM   3842  C  CA   . ASP A 1 259 ? 12.336  18.072  20.839  1.00 23.23  ? 277 ASP A CA   1 
ATOM   3843  C  C    . ASP A 1 259 ? 11.854  17.876  22.268  1.00 24.19  ? 277 ASP A C    1 
ATOM   3844  O  O    . ASP A 1 259 ? 10.743  18.308  22.597  1.00 26.68  ? 277 ASP A O    1 
ATOM   3845  C  CB   . ASP A 1 259 ? 11.274  17.472  19.915  1.00 23.71  ? 277 ASP A CB   1 
ATOM   3846  C  CG   . ASP A 1 259 ? 11.509  17.787  18.456  1.00 24.69  ? 277 ASP A CG   1 
ATOM   3847  O  OD1  . ASP A 1 259 ? 12.307  18.698  18.131  1.00 25.47  ? 277 ASP A OD1  1 
ATOM   3848  O  OD2  . ASP A 1 259 ? 10.871  17.113  17.627  1.00 24.42  ? 277 ASP A OD2  1 
ATOM   3849  H  H    . ASP A 1 259 ? 13.589  16.653  20.322  1.00 26.89  ? 277 ASP A H    1 
ATOM   3850  H  HA   . ASP A 1 259 ? 12.419  19.022  20.662  1.00 27.88  ? 277 ASP A HA   1 
ATOM   3851  H  HB2  . ASP A 1 259 ? 11.278  16.507  20.016  1.00 28.45  ? 277 ASP A HB2  1 
ATOM   3852  H  HB3  . ASP A 1 259 ? 10.406  17.828  20.161  1.00 28.45  ? 277 ASP A HB3  1 
ATOM   3853  N  N    . TYR A 1 260 ? 12.636  17.230  23.123  1.00 23.34  ? 278 TYR A N    1 
ATOM   3854  C  CA   . TYR A 1 260 ? 12.203  17.016  24.495  1.00 23.73  ? 278 TYR A CA   1 
ATOM   3855  C  C    . TYR A 1 260 ? 13.429  16.864  25.378  1.00 24.92  ? 278 TYR A C    1 
ATOM   3856  O  O    . TYR A 1 260 ? 14.530  16.581  24.901  1.00 25.44  ? 278 TYR A O    1 
ATOM   3857  C  CB   . TYR A 1 260 ? 11.245  15.819  24.597  1.00 23.56  ? 278 TYR A CB   1 
ATOM   3858  C  CG   . TYR A 1 260 ? 11.804  14.513  24.082  1.00 23.34  ? 278 TYR A CG   1 
ATOM   3859  C  CD1  . TYR A 1 260 ? 12.558  13.694  24.902  1.00 23.95  ? 278 TYR A CD1  1 
ATOM   3860  C  CD2  . TYR A 1 260 ? 11.564  14.090  22.781  1.00 24.59  ? 278 TYR A CD2  1 
ATOM   3861  C  CE1  . TYR A 1 260 ? 13.072  12.496  24.442  1.00 25.61  ? 278 TYR A CE1  1 
ATOM   3862  C  CE2  . TYR A 1 260 ? 12.075  12.889  22.313  1.00 24.87  ? 278 TYR A CE2  1 
ATOM   3863  C  CZ   . TYR A 1 260 ? 12.828  12.097  23.154  1.00 26.27  ? 278 TYR A CZ   1 
ATOM   3864  O  OH   . TYR A 1 260 ? 13.344  10.896  22.715  1.00 29.12  ? 278 TYR A OH   1 
ATOM   3865  H  H    . TYR A 1 260 ? 13.412  16.911  22.935  1.00 28.01  ? 278 TYR A H    1 
ATOM   3866  H  HA   . TYR A 1 260 ? 11.719  17.791  24.822  1.00 28.48  ? 278 TYR A HA   1 
ATOM   3867  H  HB2  . TYR A 1 260 ? 11.014  15.689  25.530  1.00 28.27  ? 278 TYR A HB2  1 
ATOM   3868  H  HB3  . TYR A 1 260 ? 10.447  16.018  24.083  1.00 28.27  ? 278 TYR A HB3  1 
ATOM   3869  H  HD1  . TYR A 1 260 ? 12.723  13.954  25.779  1.00 28.74  ? 278 TYR A HD1  1 
ATOM   3870  H  HD2  . TYR A 1 260 ? 11.052  14.620  22.215  1.00 29.51  ? 278 TYR A HD2  1 
ATOM   3871  H  HE1  . TYR A 1 260 ? 13.583  11.961  25.006  1.00 30.74  ? 278 TYR A HE1  1 
ATOM   3872  H  HE2  . TYR A 1 260 ? 11.912  12.621  21.437  1.00 29.84  ? 278 TYR A HE2  1 
ATOM   3873  H  HH   . TYR A 1 260 ? 12.902  10.617  22.057  1.00 34.95  ? 278 TYR A HH   1 
ATOM   3874  N  N    . GLY A 1 261 ? 13.225  17.085  26.671  1.00 24.63  ? 279 GLY A N    1 
ATOM   3875  C  CA   . GLY A 1 261 ? 14.316  17.006  27.617  1.00 25.16  ? 279 GLY A CA   1 
ATOM   3876  C  C    . GLY A 1 261 ? 13.816  17.057  29.042  1.00 23.73  ? 279 GLY A C    1 
ATOM   3877  O  O    . GLY A 1 261 ? 12.622  16.912  29.312  1.00 22.68  ? 279 GLY A O    1 
ATOM   3878  H  H    . GLY A 1 261 ? 12.465  17.282  27.021  1.00 29.56  ? 279 GLY A H    1 
ATOM   3879  H  HA2  . GLY A 1 261 ? 14.799  16.175  27.488  1.00 30.19  ? 279 GLY A HA2  1 
ATOM   3880  H  HA3  . GLY A 1 261 ? 14.923  17.750  27.476  1.00 30.19  ? 279 GLY A HA3  1 
ATOM   3881  N  N    . ILE A 1 262 ? 14.762  17.285  29.955  1.00 24.21  ? 280 ILE A N    1 
ATOM   3882  C  CA   . ILE A 1 262 ? 14.473  17.188  31.382  1.00 25.00  ? 280 ILE A CA   1 
ATOM   3883  C  C    . ILE A 1 262 ? 13.347  18.127  31.790  1.00 24.09  ? 280 ILE A C    1 
ATOM   3884  O  O    . ILE A 1 262 ? 12.560  17.803  32.686  1.00 23.72  ? 280 ILE A O    1 
ATOM   3885  C  CB   . ILE A 1 262 ? 15.762  17.398  32.208  1.00 25.49  ? 280 ILE A CB   1 
ATOM   3886  C  CG1  . ILE A 1 262 ? 15.515  17.096  33.688  1.00 27.06  ? 280 ILE A CG1  1 
ATOM   3887  C  CG2  . ILE A 1 262 ? 16.285  18.822  32.062  1.00 25.79  ? 280 ILE A CG2  1 
ATOM   3888  C  CD1  . ILE A 1 262 ? 15.311  15.623  34.001  1.00 27.85  ? 280 ILE A CD1  1 
ATOM   3889  H  H    . ILE A 1 262 ? 15.576  17.496  29.773  1.00 29.05  ? 280 ILE A H    1 
ATOM   3890  H  HA   . ILE A 1 262 ? 14.157  16.290  31.570  1.00 30.00  ? 280 ILE A HA   1 
ATOM   3891  H  HB   . ILE A 1 262 ? 16.427  16.782  31.862  1.00 30.59  ? 280 ILE A HB   1 
ATOM   3892  H  HG12 . ILE A 1 262 ? 16.281  17.401  34.199  1.00 32.47  ? 280 ILE A HG12 1 
ATOM   3893  H  HG13 . ILE A 1 262 ? 14.717  17.569  33.972  1.00 32.47  ? 280 ILE A HG13 1 
ATOM   3894  H  HG21 . ILE A 1 262 ? 16.371  19.032  31.119  1.00 30.95  ? 280 ILE A HG21 1 
ATOM   3895  H  HG22 . ILE A 1 262 ? 15.660  19.433  32.481  1.00 30.95  ? 280 ILE A HG22 1 
ATOM   3896  H  HG23 . ILE A 1 262 ? 17.151  18.886  32.495  1.00 30.95  ? 280 ILE A HG23 1 
ATOM   3897  H  HD11 . ILE A 1 262 ? 16.049  15.116  33.628  1.00 33.42  ? 280 ILE A HD11 1 
ATOM   3898  H  HD12 . ILE A 1 262 ? 15.281  15.505  34.963  1.00 33.42  ? 280 ILE A HD12 1 
ATOM   3899  H  HD13 . ILE A 1 262 ? 14.475  15.328  33.606  1.00 33.42  ? 280 ILE A HD13 1 
ATOM   3900  N  N    . THR A 1 263 ? 13.234  19.291  31.144  1.00 23.51  ? 281 THR A N    1 
ATOM   3901  C  CA   . THR A 1 263 ? 12.199  20.245  31.538  1.00 23.51  ? 281 THR A CA   1 
ATOM   3902  C  C    . THR A 1 263 ? 10.800  19.809  31.117  1.00 22.63  ? 281 THR A C    1 
ATOM   3903  O  O    . THR A 1 263 ? 9.817   20.426  31.551  1.00 23.55  ? 281 THR A O    1 
ATOM   3904  C  CB   . THR A 1 263 ? 12.503  21.646  30.992  1.00 25.36  ? 281 THR A CB   1 
ATOM   3905  O  OG1  . THR A 1 263 ? 12.557  21.622  29.561  1.00 27.12  ? 281 THR A OG1  1 
ATOM   3906  C  CG2  . THR A 1 263 ? 13.828  22.162  31.530  1.00 25.64  ? 281 THR A CG2  1 
ATOM   3907  H  H    . THR A 1 263 ? 13.733  19.544  30.491  1.00 28.21  ? 281 THR A H    1 
ATOM   3908  H  HA   . THR A 1 263 ? 12.210  20.312  32.506  1.00 28.21  ? 281 THR A HA   1 
ATOM   3909  H  HB   . THR A 1 263 ? 11.798  22.250  31.275  1.00 30.43  ? 281 THR A HB   1 
ATOM   3910  H  HG1  . THR A 1 263 ? 11.793  21.466  29.247  1.00 32.55  ? 281 THR A HG1  1 
ATOM   3911  H  HG21 . THR A 1 263 ? 13.794  22.218  32.498  1.00 30.77  ? 281 THR A HG21 1 
ATOM   3912  H  HG22 . THR A 1 263 ? 14.546  21.562  31.275  1.00 30.77  ? 281 THR A HG22 1 
ATOM   3913  H  HG23 . THR A 1 263 ? 14.012  23.044  31.170  1.00 30.77  ? 281 THR A HG23 1 
ATOM   3914  N  N    . ASP A 1 264 ? 10.680  18.770  30.300  1.00 21.21  ? 282 ASP A N    1 
ATOM   3915  C  CA   . ASP A 1 264 ? 9.380   18.240  29.921  1.00 20.15  ? 282 ASP A CA   1 
ATOM   3916  C  C    . ASP A 1 264 ? 8.927   17.104  30.823  1.00 19.13  ? 282 ASP A C    1 
ATOM   3917  O  O    . ASP A 1 264 ? 7.866   16.521  30.577  1.00 19.45  ? 282 ASP A O    1 
ATOM   3918  C  CB   . ASP A 1 264 ? 9.430   17.743  28.479  1.00 20.12  ? 282 ASP A CB   1 
ATOM   3919  C  CG   . ASP A 1 264 ? 9.742   18.849  27.507  1.00 20.95  ? 282 ASP A CG   1 
ATOM   3920  O  OD1  . ASP A 1 264 ? 8.964   19.825  27.462  1.00 21.38  ? 282 ASP A OD1  1 
ATOM   3921  O  OD2  . ASP A 1 264 ? 10.770  18.751  26.807  1.00 21.92  ? 282 ASP A OD2  1 
ATOM   3922  H  H    . ASP A 1 264 ? 11.345  18.351  29.949  1.00 25.45  ? 282 ASP A H    1 
ATOM   3923  H  HA   . ASP A 1 264 ? 8.723   18.950  29.979  1.00 24.18  ? 282 ASP A HA   1 
ATOM   3924  H  HB2  . ASP A 1 264 ? 10.121  17.066  28.399  1.00 24.15  ? 282 ASP A HB2  1 
ATOM   3925  H  HB3  . ASP A 1 264 ? 8.568   17.366  28.242  1.00 24.15  ? 282 ASP A HB3  1 
ATOM   3926  N  N    . CYS A 1 265 ? 9.700   16.780  31.859  1.00 19.84  ? 283 CYS A N    1 
ATOM   3927  C  CA   . CYS A 1 265 ? 9.429   15.613  32.696  1.00 20.55  ? 283 CYS A CA   1 
ATOM   3928  C  C    . CYS A 1 265 ? 8.380   15.959  33.750  1.00 21.95  ? 283 CYS A C    1 
ATOM   3929  O  O    . CYS A 1 265 ? 8.641   16.027  34.954  1.00 23.41  ? 283 CYS A O    1 
ATOM   3930  C  CB   . CYS A 1 265 ? 10.715  15.114  33.328  1.00 21.27  ? 283 CYS A CB   1 
ATOM   3931  S  SG   . CYS A 1 265 ? 11.900  14.524  32.123  1.00 21.88  ? 283 CYS A SG   1 
ATOM   3932  H  H    . CYS A 1 265 ? 10.394  17.226  32.100  1.00 23.80  ? 283 CYS A H    1 
ATOM   3933  H  HA   . CYS A 1 265 ? 9.062   14.909  32.139  1.00 24.66  ? 283 CYS A HA   1 
ATOM   3934  H  HB2  . CYS A 1 265 ? 11.126  15.840  33.822  1.00 25.52  ? 283 CYS A HB2  1 
ATOM   3935  H  HB3  . CYS A 1 265 ? 10.507  14.380  33.928  1.00 25.52  ? 283 CYS A HB3  1 
ATOM   3936  N  N    . ASN A 1 266 ? 7.163   16.167  33.263  1.00 20.54  ? 284 ASN A N    1 
ATOM   3937  C  CA   . ASN A 1 266 ? 5.990   16.399  34.091  1.00 19.06  ? 284 ASN A CA   1 
ATOM   3938  C  C    . ASN A 1 266 ? 5.130   15.145  34.011  1.00 17.62  ? 284 ASN A C    1 
ATOM   3939  O  O    . ASN A 1 266 ? 4.614   14.822  32.928  1.00 17.18  ? 284 ASN A O    1 
ATOM   3940  C  CB   . ASN A 1 266 ? 5.227   17.611  33.559  1.00 19.98  ? 284 ASN A CB   1 
ATOM   3941  C  CG   . ASN A 1 266 ? 3.887   17.801  34.231  1.00 20.83  ? 284 ASN A CG   1 
ATOM   3942  O  OD1  . ASN A 1 266 ? 3.520   17.051  35.130  1.00 21.85  ? 284 ASN A OD1  1 
ATOM   3943  N  ND2  . ASN A 1 266 ? 3.138   18.809  33.787  1.00 21.19  ? 284 ASN A ND2  1 
ATOM   3944  H  H    . ASN A 1 266 ? 6.985   16.179  32.422  1.00 24.65  ? 284 ASN A H    1 
ATOM   3945  H  HA   . ASN A 1 266 ? 6.231   16.570  35.015  1.00 22.87  ? 284 ASN A HA   1 
ATOM   3946  H  HB2  . ASN A 1 266 ? 5.756   18.409  33.712  1.00 23.98  ? 284 ASN A HB2  1 
ATOM   3947  H  HB3  . ASN A 1 266 ? 5.072   17.494  32.608  1.00 23.98  ? 284 ASN A HB3  1 
ATOM   3948  H  HD21 . ASN A 1 266 ? 2.367   18.958  34.137  1.00 25.43  ? 284 ASN A HD21 1 
ATOM   3949  H  HD22 . ASN A 1 266 ? 3.426   19.310  33.150  1.00 25.43  ? 284 ASN A HD22 1 
ATOM   3950  N  N    . PRO A 1 267 ? 4.967   14.399  35.110  1.00 17.45  ? 285 PRO A N    1 
ATOM   3951  C  CA   . PRO A 1 267 ? 4.213   13.143  35.054  1.00 18.17  ? 285 PRO A CA   1 
ATOM   3952  C  C    . PRO A 1 267 ? 2.708   13.316  35.107  1.00 17.10  ? 285 PRO A C    1 
ATOM   3953  O  O    . PRO A 1 267 ? 1.986   12.324  34.939  1.00 16.68  ? 285 PRO A O    1 
ATOM   3954  C  CB   . PRO A 1 267 ? 4.701   12.413  36.314  1.00 18.06  ? 285 PRO A CB   1 
ATOM   3955  C  CG   . PRO A 1 267 ? 4.887   13.537  37.294  1.00 18.29  ? 285 PRO A CG   1 
ATOM   3956  C  CD   . PRO A 1 267 ? 5.438   14.686  36.480  1.00 17.27  ? 285 PRO A CD   1 
ATOM   3957  H  HA   . PRO A 1 267 ? 4.453   12.643  34.258  1.00 21.80  ? 285 PRO A HA   1 
ATOM   3958  H  HB2  . PRO A 1 267 ? 4.031   11.781  36.621  1.00 21.67  ? 285 PRO A HB2  1 
ATOM   3959  H  HB3  . PRO A 1 267 ? 5.536   11.952  36.138  1.00 21.67  ? 285 PRO A HB3  1 
ATOM   3960  H  HG2  . PRO A 1 267 ? 4.035   13.772  37.692  1.00 21.94  ? 285 PRO A HG2  1 
ATOM   3961  H  HG3  . PRO A 1 267 ? 5.514   13.271  37.985  1.00 21.94  ? 285 PRO A HG3  1 
ATOM   3962  H  HD2  . PRO A 1 267 ? 5.082   15.532  36.796  1.00 20.73  ? 285 PRO A HD2  1 
ATOM   3963  H  HD3  . PRO A 1 267 ? 6.407   14.700  36.515  1.00 20.73  ? 285 PRO A HD3  1 
ATOM   3964  N  N    . LEU A 1 268 ? 2.207   14.516  35.361  1.00 18.29  ? 286 LEU A N    1 
ATOM   3965  C  CA   . LEU A 1 268 ? 0.774   14.718  35.496  1.00 19.16  ? 286 LEU A CA   1 
ATOM   3966  C  C    . LEU A 1 268 ? 0.127   14.842  34.123  1.00 18.82  ? 286 LEU A C    1 
ATOM   3967  O  O    . LEU A 1 268 ? 0.806   15.000  33.105  1.00 19.19  ? 286 LEU A O    1 
ATOM   3968  C  CB   . LEU A 1 268 ? 0.510   15.947  36.357  1.00 22.01  ? 286 LEU A CB   1 
ATOM   3969  C  CG   . LEU A 1 268 ? 0.975   15.760  37.808  1.00 24.20  ? 286 LEU A CG   1 
ATOM   3970  C  CD1  . LEU A 1 268 ? 0.734   17.015  38.634  1.00 24.03  ? 286 LEU A CD1  1 
ATOM   3971  C  CD2  . LEU A 1 268 ? 0.289   14.554  38.453  1.00 25.43  ? 286 LEU A CD2  1 
ATOM   3972  H  H    . LEU A 1 268 ? 2.677   15.230  35.460  1.00 21.94  ? 286 LEU A H    1 
ATOM   3973  H  HA   . LEU A 1 268 ? 0.374   13.953  35.939  1.00 22.99  ? 286 LEU A HA   1 
ATOM   3974  H  HB2  . LEU A 1 268 ? 0.988   16.703  35.982  1.00 26.41  ? 286 LEU A HB2  1 
ATOM   3975  H  HB3  . LEU A 1 268 ? -0.443  16.128  36.366  1.00 26.41  ? 286 LEU A HB3  1 
ATOM   3976  H  HG   . LEU A 1 268 ? 1.930   15.593  37.797  1.00 29.04  ? 286 LEU A HG   1 
ATOM   3977  H  HD11 . LEU A 1 268 ? 1.145   17.771  38.186  1.00 28.84  ? 286 LEU A HD11 1 
ATOM   3978  H  HD12 . LEU A 1 268 ? -0.221  17.159  38.718  1.00 28.84  ? 286 LEU A HD12 1 
ATOM   3979  H  HD13 . LEU A 1 268 ? 1.129   16.896  39.512  1.00 28.84  ? 286 LEU A HD13 1 
ATOM   3980  H  HD21 . LEU A 1 268 ? -0.614  14.481  38.106  1.00 30.51  ? 286 LEU A HD21 1 
ATOM   3981  H  HD22 . LEU A 1 268 ? 0.792   13.753  38.239  1.00 30.51  ? 286 LEU A HD22 1 
ATOM   3982  H  HD23 . LEU A 1 268 ? 0.264   14.682  39.415  1.00 30.51  ? 286 LEU A HD23 1 
ATOM   3983  N  N    . PRO A 1 269 ? -1.202  14.750  34.060  1.00 18.19  ? 287 PRO A N    1 
ATOM   3984  C  CA   . PRO A 1 269 ? -1.878  14.822  32.762  1.00 17.02  ? 287 PRO A CA   1 
ATOM   3985  C  C    . PRO A 1 269 ? -1.512  16.074  31.977  1.00 16.89  ? 287 PRO A C    1 
ATOM   3986  O  O    . PRO A 1 269 ? -1.311  17.157  32.534  1.00 18.89  ? 287 PRO A O    1 
ATOM   3987  C  CB   . PRO A 1 269 ? -3.365  14.791  33.135  1.00 18.13  ? 287 PRO A CB   1 
ATOM   3988  C  CG   . PRO A 1 269 ? -3.396  14.005  34.411  1.00 18.68  ? 287 PRO A CG   1 
ATOM   3989  C  CD   . PRO A 1 269 ? -2.142  14.415  35.148  1.00 18.87  ? 287 PRO A CD   1 
ATOM   3990  H  HA   . PRO A 1 269 ? -1.654  14.046  32.225  1.00 20.43  ? 287 PRO A HA   1 
ATOM   3991  H  HB2  . PRO A 1 269 ? -3.695  15.693  33.270  1.00 21.76  ? 287 PRO A HB2  1 
ATOM   3992  H  HB3  . PRO A 1 269 ? -3.876  14.351  32.438  1.00 21.76  ? 287 PRO A HB3  1 
ATOM   3993  H  HG2  . PRO A 1 269 ? -4.189  14.233  34.921  1.00 22.42  ? 287 PRO A HG2  1 
ATOM   3994  H  HG3  . PRO A 1 269 ? -3.390  13.055  34.215  1.00 22.42  ? 287 PRO A HG3  1 
ATOM   3995  H  HD2  . PRO A 1 269 ? -2.309  15.187  35.710  1.00 22.64  ? 287 PRO A HD2  1 
ATOM   3996  H  HD3  . PRO A 1 269 ? -1.802  13.682  35.684  1.00 22.64  ? 287 PRO A HD3  1 
ATOM   3997  N  N    . ALA A 1 270 ? -1.449  15.902  30.658  1.00 16.91  ? 288 ALA A N    1 
ATOM   3998  C  CA   . ALA A 1 270 ? -0.970  16.940  29.753  1.00 17.86  ? 288 ALA A CA   1 
ATOM   3999  C  C    . ALA A 1 270 ? -1.638  18.286  30.011  1.00 18.34  ? 288 ALA A C    1 
ATOM   4000  O  O    . ALA A 1 270 ? -2.858  18.379  30.183  1.00 17.84  ? 288 ALA A O    1 
ATOM   4001  C  CB   . ALA A 1 270 ? -1.211  16.485  28.310  1.00 19.30  ? 288 ALA A CB   1 
ATOM   4002  H  H    . ALA A 1 270 ? -1.684  15.179  30.255  1.00 20.29  ? 288 ALA A H    1 
ATOM   4003  H  HA   . ALA A 1 270 ? -0.020  17.075  29.895  1.00 21.44  ? 288 ALA A HA   1 
ATOM   4004  H  HB1  . ALA A 1 270 ? -2.157  16.314  28.186  1.00 23.15  ? 288 ALA A HB1  1 
ATOM   4005  H  HB2  . ALA A 1 270 ? -0.920  17.186  27.705  1.00 23.15  ? 288 ALA A HB2  1 
ATOM   4006  H  HB3  . ALA A 1 270 ? -0.704  15.675  28.146  1.00 23.15  ? 288 ALA A HB3  1 
ATOM   4007  N  N    . ASN A 1 271 ? -0.803  19.334  29.999  1.00 17.61  ? 289 ASN A N    1 
ATOM   4008  C  CA   . ASN A 1 271 ? -1.217  20.676  30.404  1.00 18.25  ? 289 ASN A CA   1 
ATOM   4009  C  C    . ASN A 1 271 ? -2.462  21.155  29.666  1.00 19.41  ? 289 ASN A C    1 
ATOM   4010  O  O    . ASN A 1 271 ? -3.331  21.804  30.257  1.00 20.31  ? 289 ASN A O    1 
ATOM   4011  C  CB   . ASN A 1 271 ? -0.081  21.671  30.131  1.00 19.81  ? 289 ASN A CB   1 
ATOM   4012  C  CG   . ASN A 1 271 ? 1.198   21.354  30.906  1.00 21.08  ? 289 ASN A CG   1 
ATOM   4013  O  OD1  . ASN A 1 271 ? 1.192   20.586  31.864  1.00 21.29  ? 289 ASN A OD1  1 
ATOM   4014  N  ND2  . ASN A 1 271 ? 2.303   21.961  30.487  1.00 22.56  ? 289 ASN A ND2  1 
ATOM   4015  H  H    . ASN A 1 271 ? 0.021   19.291  29.757  1.00 21.13  ? 289 ASN A H    1 
ATOM   4016  H  HA   . ASN A 1 271 ? -1.416  20.644  31.353  1.00 21.90  ? 289 ASN A HA   1 
ATOM   4017  H  HB2  . ASN A 1 271 ? 0.132   21.652  29.185  1.00 23.77  ? 289 ASN A HB2  1 
ATOM   4018  H  HB3  . ASN A 1 271 ? -0.373  22.559  30.388  1.00 23.77  ? 289 ASN A HB3  1 
ATOM   4019  H  HD21 . ASN A 1 271 ? 3.051   21.819  30.887  1.00 27.07  ? 289 ASN A HD21 1 
ATOM   4020  H  HD22 . ASN A 1 271 ? 2.271   22.497  29.814  1.00 27.07  ? 289 ASN A HD22 1 
ATOM   4021  N  N    . ASP A 1 272 ? -2.550  20.881  28.366  1.00 18.92  ? 290 ASP A N    1 
ATOM   4022  C  CA   . ASP A 1 272 ? -3.615  21.451  27.550  1.00 20.22  ? 290 ASP A CA   1 
ATOM   4023  C  C    . ASP A 1 272 ? -4.972  20.793  27.771  1.00 20.62  ? 290 ASP A C    1 
ATOM   4024  O  O    . ASP A 1 272 ? -5.974  21.286  27.242  1.00 21.90  ? 290 ASP A O    1 
ATOM   4025  C  CB   . ASP A 1 272 ? -3.247  21.355  26.070  1.00 20.43  ? 290 ASP A CB   1 
ATOM   4026  C  CG   . ASP A 1 272 ? -2.059  22.229  25.706  1.00 23.18  ? 290 ASP A CG   1 
ATOM   4027  O  OD1  . ASP A 1 272 ? -1.733  23.160  26.476  1.00 25.59  ? 290 ASP A OD1  1 
ATOM   4028  O  OD2  . ASP A 1 272 ? -1.457  21.987  24.639  1.00 24.75  ? 290 ASP A OD2  1 
ATOM   4029  H  H    . ASP A 1 272 ? -2.007  20.372  27.937  1.00 22.71  ? 290 ASP A H    1 
ATOM   4030  H  HA   . ASP A 1 272 ? -3.705  22.388  27.785  1.00 24.26  ? 290 ASP A HA   1 
ATOM   4031  H  HB2  . ASP A 1 272 ? -3.019  20.436  25.859  1.00 24.52  ? 290 ASP A HB2  1 
ATOM   4032  H  HB3  . ASP A 1 272 ? -4.004  21.640  25.536  1.00 24.52  ? 290 ASP A HB3  1 
ATOM   4033  N  N    . LEU A 1 273 ? -5.033  19.701  28.523  1.00 18.32  ? 291 LEU A N    1 
ATOM   4034  C  CA   . LEU A 1 273 ? -6.316  19.097  28.844  1.00 18.69  ? 291 LEU A CA   1 
ATOM   4035  C  C    . LEU A 1 273 ? -7.106  19.989  29.799  1.00 19.08  ? 291 LEU A C    1 
ATOM   4036  O  O    . LEU A 1 273 ? -6.541  20.660  30.670  1.00 19.81  ? 291 LEU A O    1 
ATOM   4037  C  CB   . LEU A 1 273 ? -6.090  17.724  29.475  1.00 18.42  ? 291 LEU A CB   1 
ATOM   4038  C  CG   . LEU A 1 273 ? -5.359  16.711  28.586  1.00 17.43  ? 291 LEU A CG   1 
ATOM   4039  C  CD1  . LEU A 1 273 ? -4.992  15.471  29.378  1.00 18.27  ? 291 LEU A CD1  1 
ATOM   4040  C  CD2  . LEU A 1 273 ? -6.197  16.342  27.369  1.00 17.80  ? 291 LEU A CD2  1 
ATOM   4041  H  H    . LEU A 1 273 ? -4.353  19.295  28.857  1.00 21.98  ? 291 LEU A H    1 
ATOM   4042  H  HA   . LEU A 1 273 ? -6.840  18.987  28.035  1.00 22.43  ? 291 LEU A HA   1 
ATOM   4043  H  HB2  . LEU A 1 273 ? -5.560  17.841  30.279  1.00 22.11  ? 291 LEU A HB2  1 
ATOM   4044  H  HB3  . LEU A 1 273 ? -6.954  17.345  29.700  1.00 22.11  ? 291 LEU A HB3  1 
ATOM   4045  H  HG   . LEU A 1 273 ? -4.540  17.119  28.264  1.00 20.92  ? 291 LEU A HG   1 
ATOM   4046  H  HD11 . LEU A 1 273 ? -4.387  15.722  30.094  1.00 21.92  ? 291 LEU A HD11 1 
ATOM   4047  H  HD12 . LEU A 1 273 ? -5.800  15.082  29.748  1.00 21.92  ? 291 LEU A HD12 1 
ATOM   4048  H  HD13 . LEU A 1 273 ? -4.559  14.835  28.787  1.00 21.92  ? 291 LEU A HD13 1 
ATOM   4049  H  HD21 . LEU A 1 273 ? -6.371  17.143  26.850  1.00 21.36  ? 291 LEU A HD21 1 
ATOM   4050  H  HD22 . LEU A 1 273 ? -5.708  15.699  26.832  1.00 21.36  ? 291 LEU A HD22 1 
ATOM   4051  H  HD23 . LEU A 1 273 ? -7.034  15.953  27.668  1.00 21.36  ? 291 LEU A HD23 1 
ATOM   4052  N  N    . THR A 1 274 ? -8.423  20.002  29.626  1.00 19.68  ? 292 THR A N    1 
ATOM   4053  C  CA   . THR A 1 274 ? -9.277  20.720  30.550  1.00 20.94  ? 292 THR A CA   1 
ATOM   4054  C  C    . THR A 1 274 ? -9.210  20.054  31.922  1.00 20.46  ? 292 THR A C    1 
ATOM   4055  O  O    . THR A 1 274 ? -8.791  18.900  32.041  1.00 19.85  ? 292 THR A O    1 
ATOM   4056  C  CB   . THR A 1 274 ? -10.724 20.675  30.072  1.00 21.94  ? 292 THR A CB   1 
ATOM   4057  O  OG1  . THR A 1 274 ? -11.178 19.317  30.131  1.00 22.72  ? 292 THR A OG1  1 
ATOM   4058  C  CG2  . THR A 1 274 ? -10.862 21.208  28.649  1.00 23.38  ? 292 THR A CG2  1 
ATOM   4059  H  H    . THR A 1 274 ? -8.839  19.605  28.986  1.00 23.62  ? 292 THR A H    1 
ATOM   4060  H  HA   . THR A 1 274 ? -8.989  21.644  30.610  1.00 25.13  ? 292 THR A HA   1 
ATOM   4061  H  HB   . THR A 1 274 ? -11.275 21.237  30.639  1.00 26.33  ? 292 THR A HB   1 
ATOM   4062  H  HG1  . THR A 1 274 ? -11.973 19.268  29.863  1.00 27.26  ? 292 THR A HG1  1 
ATOM   4063  H  HG21 . THR A 1 274 ? -11.794 21.207  28.383  1.00 28.06  ? 292 THR A HG21 1 
ATOM   4064  H  HG22 . THR A 1 274 ? -10.521 22.115  28.600  1.00 28.06  ? 292 THR A HG22 1 
ATOM   4065  H  HG23 . THR A 1 274 ? -10.359 20.650  28.035  1.00 28.06  ? 292 THR A HG23 1 
ATOM   4066  N  N    . PRO A 1 275 ? -9.629  20.755  32.980  1.00 21.67  ? 293 PRO A N    1 
ATOM   4067  C  CA   . PRO A 1 275 ? -9.671  20.099  34.300  1.00 23.21  ? 293 PRO A CA   1 
ATOM   4068  C  C    . PRO A 1 275 ? -10.445 18.793  34.281  1.00 23.68  ? 293 PRO A C    1 
ATOM   4069  O  O    . PRO A 1 275 ? -10.010 17.799  34.874  1.00 23.59  ? 293 PRO A O    1 
ATOM   4070  C  CB   . PRO A 1 275 ? -10.317 21.163  35.197  1.00 23.29  ? 293 PRO A CB   1 
ATOM   4071  C  CG   . PRO A 1 275 ? -9.908  22.453  34.568  1.00 22.83  ? 293 PRO A CG   1 
ATOM   4072  C  CD   . PRO A 1 275 ? -9.914  22.198  33.074  1.00 23.32  ? 293 PRO A CD   1 
ATOM   4073  H  HA   . PRO A 1 275 ? -8.773  19.931  34.626  1.00 27.85  ? 293 PRO A HA   1 
ATOM   4074  H  HB2  . PRO A 1 275 ? -11.282 21.062  35.196  1.00 27.95  ? 293 PRO A HB2  1 
ATOM   4075  H  HB3  . PRO A 1 275 ? -9.977  21.090  36.103  1.00 27.95  ? 293 PRO A HB3  1 
ATOM   4076  H  HG2  . PRO A 1 275 ? -10.544 23.148  34.801  1.00 27.40  ? 293 PRO A HG2  1 
ATOM   4077  H  HG3  . PRO A 1 275 ? -9.021  22.700  34.872  1.00 27.40  ? 293 PRO A HG3  1 
ATOM   4078  H  HD2  . PRO A 1 275 ? -10.782 22.404  32.692  1.00 27.98  ? 293 PRO A HD2  1 
ATOM   4079  H  HD3  . PRO A 1 275 ? -9.225  22.717  32.632  1.00 27.98  ? 293 PRO A HD3  1 
ATOM   4080  N  N    . GLU A 1 276 ? -11.579 18.765  33.586  1.00 24.92  ? 294 GLU A N    1 
ATOM   4081  C  CA   . GLU A 1 276 ? -12.379 17.548  33.537  1.00 25.42  ? 294 GLU A CA   1 
ATOM   4082  C  C    . GLU A 1 276 ? -11.631 16.429  32.824  1.00 23.57  ? 294 GLU A C    1 
ATOM   4083  O  O    . GLU A 1 276 ? -11.679 15.272  33.255  1.00 23.60  ? 294 GLU A O    1 
ATOM   4084  C  CB   . GLU A 1 276 ? -13.717 17.855  32.870  1.00 28.01  ? 294 GLU A CB   1 
ATOM   4085  C  CG   . GLU A 1 276 ? -14.632 18.782  33.693  1.00 33.01  ? 294 GLU A CG   1 
ATOM   4086  C  CD   . GLU A 1 276 ? -14.090 20.209  33.880  1.00 36.82  ? 294 GLU A CD   1 
ATOM   4087  O  OE1  . GLU A 1 276 ? -14.228 20.740  35.003  1.00 40.19  ? 294 GLU A OE1  1 
ATOM   4088  O  OE2  . GLU A 1 276 ? -13.530 20.804  32.923  1.00 35.54  ? 294 GLU A OE2  1 
ATOM   4089  H  H    . GLU A 1 276 ? -11.902 19.426  33.142  1.00 29.90  ? 294 GLU A H    1 
ATOM   4090  H  HA   . GLU A 1 276 ? -12.562 17.235  34.437  1.00 30.51  ? 294 GLU A HA   1 
ATOM   4091  H  HB2  . GLU A 1 276 ? -13.547 18.288  32.019  1.00 33.62  ? 294 GLU A HB2  1 
ATOM   4092  H  HB3  . GLU A 1 276 ? -14.192 17.021  32.729  1.00 33.62  ? 294 GLU A HB3  1 
ATOM   4093  H  HG2  . GLU A 1 276 ? -15.488 18.851  33.242  1.00 39.62  ? 294 GLU A HG2  1 
ATOM   4094  H  HG3  . GLU A 1 276 ? -14.751 18.396  34.575  1.00 39.62  ? 294 GLU A HG3  1 
ATOM   4095  N  N    . GLN A 1 277 ? -10.918 16.757  31.743  1.00 21.40  ? 295 GLN A N    1 
ATOM   4096  C  CA   . GLN A 1 277 ? -10.128 15.749  31.045  1.00 19.92  ? 295 GLN A CA   1 
ATOM   4097  C  C    . GLN A 1 277 ? -8.971  15.255  31.909  1.00 18.75  ? 295 GLN A C    1 
ATOM   4098  O  O    . GLN A 1 277 ? -8.670  14.058  31.922  1.00 18.48  ? 295 GLN A O    1 
ATOM   4099  C  CB   . GLN A 1 277 ? -9.628  16.318  29.717  1.00 18.62  ? 295 GLN A CB   1 
ATOM   4100  C  CG   . GLN A 1 277 ? -10.727 16.481  28.679  1.00 18.70  ? 295 GLN A CG   1 
ATOM   4101  C  CD   . GLN A 1 277 ? -10.362 17.433  27.547  1.00 19.53  ? 295 GLN A CD   1 
ATOM   4102  O  OE1  . GLN A 1 277 ? -9.361  18.147  27.603  1.00 19.26  ? 295 GLN A OE1  1 
ATOM   4103  N  NE2  . GLN A 1 277 ? -11.181 17.436  26.508  1.00 21.14  ? 295 GLN A NE2  1 
ATOM   4104  H  H    . GLN A 1 277 ? -10.876 17.545  31.401  1.00 25.68  ? 295 GLN A H    1 
ATOM   4105  H  HA   . GLN A 1 277 ? -10.688 14.982  30.848  1.00 23.91  ? 295 GLN A HA   1 
ATOM   4106  H  HB2  . GLN A 1 277 ? -9.238  17.192  29.878  1.00 22.34  ? 295 GLN A HB2  1 
ATOM   4107  H  HB3  . GLN A 1 277 ? -8.959  15.719  29.351  1.00 22.34  ? 295 GLN A HB3  1 
ATOM   4108  H  HG2  . GLN A 1 277 ? -10.917 15.614  28.288  1.00 22.44  ? 295 GLN A HG2  1 
ATOM   4109  H  HG3  . GLN A 1 277 ? -11.520 16.829  29.116  1.00 22.44  ? 295 GLN A HG3  1 
ATOM   4110  H  HE21 . GLN A 1 277 ? -11.870 16.921  26.502  1.00 25.37  ? 295 GLN A HE21 1 
ATOM   4111  H  HE22 . GLN A 1 277 ? -11.025 17.954  25.840  1.00 25.37  ? 295 GLN A HE22 1 
ATOM   4112  N  N    . LYS A 1 278 ? -8.313  16.156  32.639  1.00 18.89  ? 296 LYS A N    1 
ATOM   4113  C  CA   . LYS A 1 278 ? -7.214  15.731  33.502  1.00 18.72  ? 296 LYS A CA   1 
ATOM   4114  C  C    . LYS A 1 278 ? -7.692  14.742  34.558  1.00 19.10  ? 296 LYS A C    1 
ATOM   4115  O  O    . LYS A 1 278 ? -7.004  13.755  34.855  1.00 19.16  ? 296 LYS A O    1 
ATOM   4116  C  CB   . LYS A 1 278 ? -6.583  16.946  34.179  1.00 19.41  ? 296 LYS A CB   1 
ATOM   4117  C  CG   . LYS A 1 278 ? -5.758  17.818  33.250  1.00 19.81  ? 296 LYS A CG   1 
ATOM   4118  C  CD   . LYS A 1 278 ? -4.808  18.706  34.060  1.00 20.56  ? 296 LYS A CD   1 
ATOM   4119  C  CE   . LYS A 1 278 ? -3.945  19.563  33.160  1.00 21.41  ? 296 LYS A CE   1 
ATOM   4120  N  NZ   . LYS A 1 278 ? -4.691  20.741  32.633  1.00 22.15  ? 296 LYS A NZ   1 
ATOM   4121  H  H    . LYS A 1 278 ? -8.479  16.999  32.653  1.00 22.66  ? 296 LYS A H    1 
ATOM   4122  H  HA   . LYS A 1 278 ? -6.541  15.296  32.954  1.00 22.46  ? 296 LYS A HA   1 
ATOM   4123  H  HB2  . LYS A 1 278 ? -7.290  17.496  34.549  1.00 23.29  ? 296 LYS A HB2  1 
ATOM   4124  H  HB3  . LYS A 1 278 ? -5.998  16.636  34.888  1.00 23.29  ? 296 LYS A HB3  1 
ATOM   4125  H  HG2  . LYS A 1 278 ? -5.231  17.258  32.659  1.00 23.77  ? 296 LYS A HG2  1 
ATOM   4126  H  HG3  . LYS A 1 278 ? -6.346  18.387  32.730  1.00 23.77  ? 296 LYS A HG3  1 
ATOM   4127  H  HD2  . LYS A 1 278 ? -5.327  19.292  34.633  1.00 24.67  ? 296 LYS A HD2  1 
ATOM   4128  H  HD3  . LYS A 1 278 ? -4.226  18.147  34.598  1.00 24.67  ? 296 LYS A HD3  1 
ATOM   4129  H  HE2  . LYS A 1 278 ? -3.182  19.887  33.663  1.00 25.69  ? 296 LYS A HE2  1 
ATOM   4130  H  HE3  . LYS A 1 278 ? -3.644  19.032  32.406  1.00 25.69  ? 296 LYS A HE3  1 
ATOM   4131  H  HZ1  . LYS A 1 278 ? -4.176  21.199  32.070  1.00 26.58  ? 296 LYS A HZ1  1 
ATOM   4132  H  HZ2  . LYS A 1 278 ? -5.421  20.471  32.203  1.00 26.58  ? 296 LYS A HZ2  1 
ATOM   4133  H  HZ3  . LYS A 1 278 ? -4.931  21.273  33.304  1.00 26.58  ? 296 LYS A HZ3  1 
ATOM   4134  N  N    . VAL A 1 279 ? -8.863  15.002  35.147  1.00 20.59  ? 297 VAL A N    1 
ATOM   4135  C  CA   . VAL A 1 279 ? -9.420  14.098  36.151  1.00 20.43  ? 297 VAL A CA   1 
ATOM   4136  C  C    . VAL A 1 279 ? -9.724  12.741  35.525  1.00 19.98  ? 297 VAL A C    1 
ATOM   4137  O  O    . VAL A 1 279 ? -9.399  11.686  36.088  1.00 20.32  ? 297 VAL A O    1 
ATOM   4138  C  CB   . VAL A 1 279 ? -10.665 14.727  36.806  1.00 21.98  ? 297 VAL A CB   1 
ATOM   4139  C  CG1  . VAL A 1 279 ? -11.401 13.694  37.675  1.00 22.28  ? 297 VAL A CG1  1 
ATOM   4140  C  CG2  . VAL A 1 279 ? -10.276 15.948  37.635  1.00 24.21  ? 297 VAL A CG2  1 
ATOM   4141  H  H    . VAL A 1 279 ? -9.350  15.692  34.984  1.00 24.71  ? 297 VAL A H    1 
ATOM   4142  H  HA   . VAL A 1 279 ? -8.760  13.958  36.848  1.00 24.52  ? 297 VAL A HA   1 
ATOM   4143  H  HB   . VAL A 1 279 ? -11.271 15.017  36.107  1.00 26.37  ? 297 VAL A HB   1 
ATOM   4144  H  HG11 . VAL A 1 279 ? -11.842 13.052  37.097  1.00 26.73  ? 297 VAL A HG11 1 
ATOM   4145  H  HG12 . VAL A 1 279 ? -10.757 13.242  38.242  1.00 26.73  ? 297 VAL A HG12 1 
ATOM   4146  H  HG13 . VAL A 1 279 ? -12.058 14.153  38.222  1.00 26.73  ? 297 VAL A HG13 1 
ATOM   4147  H  HG21 . VAL A 1 279 ? -11.081 16.368  37.975  1.00 29.05  ? 297 VAL A HG21 1 
ATOM   4148  H  HG22 . VAL A 1 279 ? -9.714  15.663  38.372  1.00 29.05  ? 297 VAL A HG22 1 
ATOM   4149  H  HG23 . VAL A 1 279 ? -9.791  16.570  37.071  1.00 29.05  ? 297 VAL A HG23 1 
ATOM   4150  N  N    . ALA A 1 280 ? -10.348 12.749  34.344  1.00 18.89  ? 298 ALA A N    1 
ATOM   4151  C  CA   . ALA A 1 280 ? -10.673 11.495  33.673  1.00 18.79  ? 298 ALA A CA   1 
ATOM   4152  C  C    . ALA A 1 280 ? -9.415  10.761  33.229  1.00 18.73  ? 298 ALA A C    1 
ATOM   4153  O  O    . ALA A 1 280 ? -9.367  9.526   33.261  1.00 20.07  ? 298 ALA A O    1 
ATOM   4154  C  CB   . ALA A 1 280 ? -11.580 11.772  32.475  1.00 19.29  ? 298 ALA A CB   1 
ATOM   4155  H  H    . ALA A 1 280 ? -10.590 13.456  33.919  1.00 22.67  ? 298 ALA A H    1 
ATOM   4156  H  HA   . ALA A 1 280 ? -11.150 10.922  34.293  1.00 22.55  ? 298 ALA A HA   1 
ATOM   4157  H  HB1  . ALA A 1 280 ? -11.137 12.399  31.882  1.00 23.15  ? 298 ALA A HB1  1 
ATOM   4158  H  HB2  . ALA A 1 280 ? -11.750 10.939  32.009  1.00 23.15  ? 298 ALA A HB2  1 
ATOM   4159  H  HB3  . ALA A 1 280 ? -12.415 12.150  32.792  1.00 23.15  ? 298 ALA A HB3  1 
ATOM   4160  N  N    . ALA A 1 281 ? -8.392  11.504  32.805  1.00 17.74  ? 299 ALA A N    1 
ATOM   4161  C  CA   . ALA A 1 281 ? -7.129  10.889  32.416  1.00 18.39  ? 299 ALA A CA   1 
ATOM   4162  C  C    . ALA A 1 281 ? -6.481  10.162  33.587  1.00 17.24  ? 299 ALA A C    1 
ATOM   4163  O  O    . ALA A 1 281 ? -5.955  9.058   33.423  1.00 17.71  ? 299 ALA A O    1 
ATOM   4164  C  CB   . ALA A 1 281 ? -6.187  11.956  31.865  1.00 19.91  ? 299 ALA A CB   1 
ATOM   4165  H  H    . ALA A 1 281 ? -8.404  12.361  32.735  1.00 21.29  ? 299 ALA A H    1 
ATOM   4166  H  HA   . ALA A 1 281 ? -7.299  10.237  31.718  1.00 22.06  ? 299 ALA A HA   1 
ATOM   4167  H  HB1  . ALA A 1 281 ? -5.347  11.539  31.618  1.00 23.90  ? 299 ALA A HB1  1 
ATOM   4168  H  HB2  . ALA A 1 281 ? -6.594  12.365  31.086  1.00 23.90  ? 299 ALA A HB2  1 
ATOM   4169  H  HB3  . ALA A 1 281 ? -6.035  12.627  32.549  1.00 23.90  ? 299 ALA A HB3  1 
ATOM   4170  N  N    . ALA A 1 282 ? -6.498  10.770  34.775  1.00 18.15  ? 300 ALA A N    1 
ATOM   4171  C  CA   . ALA A 1 282 ? -5.901  10.119  35.934  1.00 19.60  ? 300 ALA A CA   1 
ATOM   4172  C  C    . ALA A 1 282 ? -6.635  8.834   36.294  1.00 19.50  ? 300 ALA A C    1 
ATOM   4173  O  O    . ALA A 1 282 ? -6.030  7.904   36.843  1.00 21.43  ? 300 ALA A O    1 
ATOM   4174  C  CB   . ALA A 1 282 ? -5.906  11.080  37.121  1.00 21.23  ? 300 ALA A CB   1 
ATOM   4175  H  H    . ALA A 1 282 ? -6.842  11.542  34.931  1.00 21.79  ? 300 ALA A H    1 
ATOM   4176  H  HA   . ALA A 1 282 ? -4.981  9.890   35.729  1.00 23.52  ? 300 ALA A HA   1 
ATOM   4177  H  HB1  . ALA A 1 282 ? -5.409  11.879  36.883  1.00 25.47  ? 300 ALA A HB1  1 
ATOM   4178  H  HB2  . ALA A 1 282 ? -6.823  11.313  37.335  1.00 25.47  ? 300 ALA A HB2  1 
ATOM   4179  H  HB3  . ALA A 1 282 ? -5.489  10.645  37.881  1.00 25.47  ? 300 ALA A HB3  1 
ATOM   4180  N  N    . ALA A 1 283 ? -7.931  8.764   35.990  1.00 20.01  ? 301 ALA A N    1 
ATOM   4181  C  CA   . ALA A 1 283 ? -8.772  7.609   36.280  1.00 19.98  ? 301 ALA A CA   1 
ATOM   4182  C  C    . ALA A 1 283 ? -8.934  6.685   35.076  1.00 20.56  ? 301 ALA A C    1 
ATOM   4183  O  O    . ALA A 1 283 ? -9.907  5.924   35.011  1.00 21.15  ? 301 ALA A O    1 
ATOM   4184  C  CB   . ALA A 1 283 ? -10.138 8.082   36.782  1.00 21.97  ? 301 ALA A CB   1 
ATOM   4185  H  H    . ALA A 1 283 ? -8.361  9.399   35.601  1.00 24.02  ? 301 ALA A H    1 
ATOM   4186  H  HA   . ALA A 1 283 ? -8.354  7.088   36.984  1.00 23.98  ? 301 ALA A HA   1 
ATOM   4187  H  HB1  . ALA A 1 283 ? -10.018 8.566   37.614  1.00 26.37  ? 301 ALA A HB1  1 
ATOM   4188  H  HB2  . ALA A 1 283 ? -10.535 8.665   36.115  1.00 26.37  ? 301 ALA A HB2  1 
ATOM   4189  H  HB3  . ALA A 1 283 ? -10.706 7.310   36.927  1.00 26.37  ? 301 ALA A HB3  1 
ATOM   4190  N  N    . LEU A 1 284 ? -7.985  6.723   34.140  1.00 19.52  ? 302 LEU A N    1 
ATOM   4191  C  CA   . LEU A 1 284 ? -8.137  6.011   32.876  1.00 19.45  ? 302 LEU A CA   1 
ATOM   4192  C  C    . LEU A 1 284 ? -8.307  4.509   33.073  1.00 19.80  ? 302 LEU A C    1 
ATOM   4193  O  O    . LEU A 1 284 ? -9.075  3.869   32.347  1.00 20.85  ? 302 LEU A O    1 
ATOM   4194  C  CB   . LEU A 1 284 ? -6.921  6.286   31.992  1.00 19.43  ? 302 LEU A CB   1 
ATOM   4195  C  CG   . LEU A 1 284 ? -7.069  5.972   30.507  1.00 19.83  ? 302 LEU A CG   1 
ATOM   4196  C  CD1  . LEU A 1 284 ? -7.950  7.025   29.847  1.00 20.75  ? 302 LEU A CD1  1 
ATOM   4197  C  CD2  . LEU A 1 284 ? -5.713  5.882   29.837  1.00 19.85  ? 302 LEU A CD2  1 
ATOM   4198  H  H    . LEU A 1 284 ? -7.244  7.154   34.213  1.00 23.42  ? 302 LEU A H    1 
ATOM   4199  H  HA   . LEU A 1 284 ? -8.937  6.338   32.436  1.00 23.34  ? 302 LEU A HA   1 
ATOM   4200  H  HB2  . LEU A 1 284 ? -6.706  7.229   32.064  1.00 23.31  ? 302 LEU A HB2  1 
ATOM   4201  H  HB3  . LEU A 1 284 ? -6.182  5.752   32.324  1.00 23.31  ? 302 LEU A HB3  1 
ATOM   4202  H  HG   . LEU A 1 284 ? -7.495  5.108   30.395  1.00 23.80  ? 302 LEU A HG   1 
ATOM   4203  H  HD11 . LEU A 1 284 ? -7.985  6.855   28.893  1.00 24.90  ? 302 LEU A HD11 1 
ATOM   4204  H  HD12 . LEU A 1 284 ? -8.842  6.972   30.225  1.00 24.90  ? 302 LEU A HD12 1 
ATOM   4205  H  HD13 . LEU A 1 284 ? -7.572  7.903   30.013  1.00 24.90  ? 302 LEU A HD13 1 
ATOM   4206  H  HD21 . LEU A 1 284 ? -5.833  5.594   28.918  1.00 23.82  ? 302 LEU A HD21 1 
ATOM   4207  H  HD22 . LEU A 1 284 ? -5.292  6.756   29.857  1.00 23.82  ? 302 LEU A HD22 1 
ATOM   4208  H  HD23 . LEU A 1 284 ? -5.166  5.241   30.316  1.00 23.82  ? 302 LEU A HD23 1 
ATOM   4209  N  N    . LEU A 1 285 ? -7.593  3.923   34.036  1.00 22.02  ? 303 LEU A N    1 
ATOM   4210  C  CA   . LEU A 1 285 ? -7.482  2.470   34.109  1.00 26.34  ? 303 LEU A CA   1 
ATOM   4211  C  C    . LEU A 1 285 ? -8.686  1.808   34.766  1.00 28.39  ? 303 LEU A C    1 
ATOM   4212  O  O    . LEU A 1 285 ? -8.987  0.648   34.461  1.00 28.06  ? 303 LEU A O    1 
ATOM   4213  C  CB   . LEU A 1 285 ? -6.218  2.095   34.886  1.00 29.07  ? 303 LEU A CB   1 
ATOM   4214  C  CG   . LEU A 1 285 ? -5.777  0.633   34.835  1.00 31.46  ? 303 LEU A CG   1 
ATOM   4215  C  CD1  . LEU A 1 285 ? -5.177  0.326   33.482  1.00 32.79  ? 303 LEU A CD1  1 
ATOM   4216  C  CD2  . LEU A 1 285 ? -4.787  0.341   35.950  1.00 31.29  ? 303 LEU A CD2  1 
ATOM   4217  H  H    . LEU A 1 285 ? -7.167  4.343   34.654  1.00 26.43  ? 303 LEU A H    1 
ATOM   4218  H  HA   . LEU A 1 285 ? -7.420  2.129   33.203  1.00 31.61  ? 303 LEU A HA   1 
ATOM   4219  H  HB2  . LEU A 1 285 ? -5.485  2.623   34.534  1.00 34.88  ? 303 LEU A HB2  1 
ATOM   4220  H  HB3  . LEU A 1 285 ? -6.367  2.312   35.819  1.00 34.88  ? 303 LEU A HB3  1 
ATOM   4221  H  HG   . LEU A 1 285 ? -6.544  0.053   34.965  1.00 37.75  ? 303 LEU A HG   1 
ATOM   4222  H  HD11 . LEU A 1 285 ? -4.882  -0.598  33.469  1.00 39.35  ? 303 LEU A HD11 1 
ATOM   4223  H  HD12 . LEU A 1 285 ? -5.851  0.467   32.798  1.00 39.35  ? 303 LEU A HD12 1 
ATOM   4224  H  HD13 . LEU A 1 285 ? -4.423  0.916   33.329  1.00 39.35  ? 303 LEU A HD13 1 
ATOM   4225  H  HD21 . LEU A 1 285 ? -4.518  -0.590  35.899  1.00 37.54  ? 303 LEU A HD21 1 
ATOM   4226  H  HD22 . LEU A 1 285 ? -4.012  0.915   35.844  1.00 37.54  ? 303 LEU A HD22 1 
ATOM   4227  H  HD23 . LEU A 1 285 ? -5.212  0.515   36.804  1.00 37.54  ? 303 LEU A HD23 1 
ATOM   4228  N  N    . ALA A 1 286 ? -9.380  2.505   35.663  1.00 31.31  ? 304 ALA A N    1 
ATOM   4229  C  CA   . ALA A 1 286 ? -10.407 1.844   36.466  1.00 34.20  ? 304 ALA A CA   1 
ATOM   4230  C  C    . ALA A 1 286 ? -11.466 1.150   35.620  1.00 34.39  ? 304 ALA A C    1 
ATOM   4231  O  O    . ALA A 1 286 ? -11.748 -0.035  35.871  1.00 35.34  ? 304 ALA A O    1 
ATOM   4232  C  CB   . ALA A 1 286 ? -11.011 2.838   37.463  1.00 35.45  ? 304 ALA A CB   1 
ATOM   4233  H  H    . ALA A 1 286 ? -9.278  3.344   35.824  1.00 37.57  ? 304 ALA A H    1 
ATOM   4234  H  HA   . ALA A 1 286 ? -9.971  1.149   36.985  1.00 41.04  ? 304 ALA A HA   1 
ATOM   4235  H  HB1  . ALA A 1 286 ? -10.309 3.166   38.047  1.00 42.54  ? 304 ALA A HB1  1 
ATOM   4236  H  HB2  . ALA A 1 286 ? -11.405 3.577   36.973  1.00 42.54  ? 304 ALA A HB2  1 
ATOM   4237  H  HB3  . ALA A 1 286 ? -11.693 2.387   37.986  1.00 42.54  ? 304 ALA A HB3  1 
ATOM   4238  N  N    . PRO A 1 287 ? -12.077 1.795   34.622  1.00 33.95  ? 305 PRO A N    1 
ATOM   4239  C  CA   . PRO A 1 287 ? -13.077 1.083   33.810  1.00 32.48  ? 305 PRO A CA   1 
ATOM   4240  C  C    . PRO A 1 287 ? -12.517 -0.149  33.123  1.00 28.80  ? 305 PRO A C    1 
ATOM   4241  O  O    . PRO A 1 287 ? -13.247 -1.127  32.930  1.00 28.85  ? 305 PRO A O    1 
ATOM   4242  C  CB   . PRO A 1 287 ? -13.539 2.134   32.790  1.00 34.37  ? 305 PRO A CB   1 
ATOM   4243  C  CG   . PRO A 1 287 ? -13.035 3.447   33.298  1.00 34.84  ? 305 PRO A CG   1 
ATOM   4244  C  CD   . PRO A 1 287 ? -11.833 3.165   34.141  1.00 34.88  ? 305 PRO A CD   1 
ATOM   4245  H  HA   . PRO A 1 287 ? -13.831 0.834   34.367  1.00 38.98  ? 305 PRO A HA   1 
ATOM   4246  H  HB2  . PRO A 1 287 ? -13.160 1.934   31.920  1.00 41.24  ? 305 PRO A HB2  1 
ATOM   4247  H  HB3  . PRO A 1 287 ? -14.508 2.135   32.737  1.00 41.24  ? 305 PRO A HB3  1 
ATOM   4248  H  HG2  . PRO A 1 287 ? -12.796 4.012   32.546  1.00 41.81  ? 305 PRO A HG2  1 
ATOM   4249  H  HG3  . PRO A 1 287 ? -13.727 3.874   33.827  1.00 41.81  ? 305 PRO A HG3  1 
ATOM   4250  H  HD2  . PRO A 1 287 ? -11.021 3.207   33.611  1.00 41.85  ? 305 PRO A HD2  1 
ATOM   4251  H  HD3  . PRO A 1 287 ? -11.777 3.787   34.883  1.00 41.85  ? 305 PRO A HD3  1 
ATOM   4252  N  N    . ALA A 1 288 ? -11.236 -0.120  32.743  1.00 26.04  ? 306 ALA A N    1 
ATOM   4253  C  CA   . ALA A 1 288 ? -10.643 -1.231  32.006  1.00 25.63  ? 306 ALA A CA   1 
ATOM   4254  C  C    . ALA A 1 288 ? -10.497 -2.453  32.896  1.00 26.01  ? 306 ALA A C    1 
ATOM   4255  O  O    . ALA A 1 288 ? -10.830 -3.574  32.492  1.00 26.23  ? 306 ALA A O    1 
ATOM   4256  C  CB   . ALA A 1 288 ? -9.280  -0.815  31.450  1.00 26.27  ? 306 ALA A CB   1 
ATOM   4257  H  H    . ALA A 1 288 ? -10.693 0.528   32.901  1.00 31.25  ? 306 ALA A H    1 
ATOM   4258  H  HA   . ALA A 1 288 ? -11.221 -1.460  31.262  1.00 30.76  ? 306 ALA A HA   1 
ATOM   4259  H  HB1  . ALA A 1 288 ? -9.394  -0.039  30.880  1.00 31.52  ? 306 ALA A HB1  1 
ATOM   4260  H  HB2  . ALA A 1 288 ? -8.690  -0.598  32.189  1.00 31.52  ? 306 ALA A HB2  1 
ATOM   4261  H  HB3  . ALA A 1 288 ? -8.910  -1.551  30.937  1.00 31.52  ? 306 ALA A HB3  1 
ATOM   4262  N  N    . ALA A 1 289 ? -9.989  -2.260  34.113  1.00 27.44  ? 307 ALA A N    1 
ATOM   4263  C  CA   . ALA A 1 289 ? -9.885  -3.385  35.034  1.00 29.15  ? 307 ALA A CA   1 
ATOM   4264  C  C    . ALA A 1 289 ? -11.255 -3.996  35.296  1.00 30.33  ? 307 ALA A C    1 
ATOM   4265  O  O    . ALA A 1 289 ? -11.393 -5.222  35.355  1.00 31.98  ? 307 ALA A O    1 
ATOM   4266  C  CB   . ALA A 1 289 ? -9.228  -2.941  36.340  1.00 29.59  ? 307 ALA A CB   1 
ATOM   4267  H  H    . ALA A 1 289 ? -9.705  -1.509  34.420  1.00 32.92  ? 307 ALA A H    1 
ATOM   4268  H  HA   . ALA A 1 289 ? -9.319  -4.067  34.640  1.00 34.98  ? 307 ALA A HA   1 
ATOM   4269  H  HB1  . ALA A 1 289 ? -8.335  -2.615  36.149  1.00 35.51  ? 307 ALA A HB1  1 
ATOM   4270  H  HB2  . ALA A 1 289 ? -9.760  -2.234  36.737  1.00 35.51  ? 307 ALA A HB2  1 
ATOM   4271  H  HB3  . ALA A 1 289 ? -9.182  -3.699  36.944  1.00 35.51  ? 307 ALA A HB3  1 
ATOM   4272  N  N    . ALA A 1 290 ? -12.285 -3.157  35.439  1.00 30.13  ? 308 ALA A N    1 
ATOM   4273  C  CA   . ALA A 1 290 ? -13.621 -3.681  35.714  1.00 31.06  ? 308 ALA A CA   1 
ATOM   4274  C  C    . ALA A 1 290 ? -14.167 -4.461  34.526  1.00 33.43  ? 308 ALA A C    1 
ATOM   4275  O  O    . ALA A 1 290 ? -14.802 -5.505  34.702  1.00 35.16  ? 308 ALA A O    1 
ATOM   4276  C  CB   . ALA A 1 290 ? -14.570 -2.539  36.070  1.00 31.54  ? 308 ALA A CB   1 
ATOM   4277  H  H    . ALA A 1 290 ? -12.237 -2.301  35.383  1.00 36.15  ? 308 ALA A H    1 
ATOM   4278  H  HA   . ALA A 1 290 ? -13.564 -4.281  36.475  1.00 37.28  ? 308 ALA A HA   1 
ATOM   4279  H  HB1  . ALA A 1 290 ? -14.618 -1.923  35.322  1.00 37.85  ? 308 ALA A HB1  1 
ATOM   4280  H  HB2  . ALA A 1 290 ? -15.450 -2.905  36.253  1.00 37.85  ? 308 ALA A HB2  1 
ATOM   4281  H  HB3  . ALA A 1 290 ? -14.233 -2.080  36.855  1.00 37.85  ? 308 ALA A HB3  1 
ATOM   4282  N  N    . ALA A 1 291 ? -13.941 -3.966  33.308  1.00 31.66  ? 309 ALA A N    1 
ATOM   4283  C  CA   . ALA A 1 291 ? -14.473 -4.648  32.132  1.00 30.74  ? 309 ALA A CA   1 
ATOM   4284  C  C    . ALA A 1 291 ? -13.824 -6.011  31.956  1.00 30.05  ? 309 ALA A C    1 
ATOM   4285  O  O    . ALA A 1 291 ? -14.488 -6.975  31.558  1.00 29.52  ? 309 ALA A O    1 
ATOM   4286  C  CB   . ALA A 1 291 ? -14.253 -3.795  30.886  1.00 30.19  ? 309 ALA A CB   1 
ATOM   4287  H  H    . ALA A 1 291 ? -13.493 -3.252  33.139  1.00 37.99  ? 309 ALA A H    1 
ATOM   4288  H  HA   . ALA A 1 291 ? -15.428 -4.774  32.248  1.00 36.89  ? 309 ALA A HA   1 
ATOM   4289  H  HB1  . ALA A 1 291 ? -14.689 -2.937  31.009  1.00 36.23  ? 309 ALA A HB1  1 
ATOM   4290  H  HB2  . ALA A 1 291 ? -13.300 -3.665  30.756  1.00 36.23  ? 309 ALA A HB2  1 
ATOM   4291  H  HB3  . ALA A 1 291 ? -14.632 -4.252  30.119  1.00 36.23  ? 309 ALA A HB3  1 
ATOM   4292  N  N    . ILE A 1 292 ? -12.520 -6.101  32.234  1.00 29.04  ? 310 ILE A N    1 
ATOM   4293  C  CA   . ILE A 1 292 ? -11.835 -7.389  32.203  1.00 31.49  ? 310 ILE A CA   1 
ATOM   4294  C  C    . ILE A 1 292 ? -12.526 -8.373  33.134  1.00 34.56  ? 310 ILE A C    1 
ATOM   4295  O  O    . ILE A 1 292 ? -12.662 -9.561  32.819  1.00 35.84  ? 310 ILE A O    1 
ATOM   4296  C  CB   . ILE A 1 292 ? -10.347 -7.203  32.560  1.00 31.81  ? 310 ILE A CB   1 
ATOM   4297  C  CG1  . ILE A 1 292 ? -9.614  -6.485  31.422  1.00 31.72  ? 310 ILE A CG1  1 
ATOM   4298  C  CG2  . ILE A 1 292 ? -9.685  -8.545  32.857  1.00 33.31  ? 310 ILE A CG2  1 
ATOM   4299  C  CD1  . ILE A 1 292 ? -8.248  -5.953  31.817  1.00 32.85  ? 310 ILE A CD1  1 
ATOM   4300  H  H    . ILE A 1 292 ? -12.016 -5.435  32.442  1.00 34.85  ? 310 ILE A H    1 
ATOM   4301  H  HA   . ILE A 1 292 ? -11.881 -7.750  31.304  1.00 37.79  ? 310 ILE A HA   1 
ATOM   4302  H  HB   . ILE A 1 292 ? -10.296 -6.657  33.359  1.00 38.17  ? 310 ILE A HB   1 
ATOM   4303  H  HG12 . ILE A 1 292 ? -9.490  -7.108  30.689  1.00 38.07  ? 310 ILE A HG12 1 
ATOM   4304  H  HG13 . ILE A 1 292 ? -10.152 -5.732  31.131  1.00 38.07  ? 310 ILE A HG13 1 
ATOM   4305  H  HG21 . ILE A 1 292 ? -9.976  -8.854  33.729  1.00 39.97  ? 310 ILE A HG21 1 
ATOM   4306  H  HG22 . ILE A 1 292 ? -9.947  -9.184  32.175  1.00 39.97  ? 310 ILE A HG22 1 
ATOM   4307  H  HG23 . ILE A 1 292 ? -8.722  -8.430  32.850  1.00 39.97  ? 310 ILE A HG23 1 
ATOM   4308  H  HD11 . ILE A 1 292 ? -7.934  -5.346  31.129  1.00 39.42  ? 310 ILE A HD11 1 
ATOM   4309  H  HD12 . ILE A 1 292 ? -8.323  -5.484  32.662  1.00 39.42  ? 310 ILE A HD12 1 
ATOM   4310  H  HD13 . ILE A 1 292 ? -7.633  -6.698  31.907  1.00 39.42  ? 310 ILE A HD13 1 
ATOM   4311  N  N    . VAL A 1 293 ? -12.994 -7.892  34.287  1.00 36.45  ? 311 VAL A N    1 
ATOM   4312  C  CA   . VAL A 1 293 ? -13.622 -8.789  35.249  1.00 38.98  ? 311 VAL A CA   1 
ATOM   4313  C  C    . VAL A 1 293 ? -14.983 -9.271  34.756  1.00 38.97  ? 311 VAL A C    1 
ATOM   4314  O  O    . VAL A 1 293 ? -15.380 -10.407 35.039  1.00 40.96  ? 311 VAL A O    1 
ATOM   4315  C  CB   . VAL A 1 293 ? -13.718 -8.110  36.628  1.00 40.92  ? 311 VAL A CB   1 
ATOM   4316  C  CG1  . VAL A 1 293 ? -14.403 -9.034  37.626  1.00 41.04  ? 311 VAL A CG1  1 
ATOM   4317  C  CG2  . VAL A 1 293 ? -12.333 -7.710  37.128  1.00 41.78  ? 311 VAL A CG2  1 
ATOM   4318  H  H    . VAL A 1 293 ? -12.959 -7.068  34.529  1.00 43.74  ? 311 VAL A H    1 
ATOM   4319  H  HA   . VAL A 1 293 ? -13.060 -9.574  35.341  1.00 46.78  ? 311 VAL A HA   1 
ATOM   4320  H  HB   . VAL A 1 293 ? -14.249 -7.303  36.546  1.00 49.11  ? 311 VAL A HB   1 
ATOM   4321  H  HG11 . VAL A 1 293 ? -14.370 -9.943  37.288  1.00 49.24  ? 311 VAL A HG11 1 
ATOM   4322  H  HG12 . VAL A 1 293 ? -13.940 -8.980  38.476  1.00 49.24  ? 311 VAL A HG12 1 
ATOM   4323  H  HG13 . VAL A 1 293 ? -15.326 -8.755  37.733  1.00 49.24  ? 311 VAL A HG13 1 
ATOM   4324  H  HG21 . VAL A 1 293 ? -12.431 -7.116  37.888  1.00 50.14  ? 311 VAL A HG21 1 
ATOM   4325  H  HG22 . VAL A 1 293 ? -11.851 -8.509  37.393  1.00 50.14  ? 311 VAL A HG22 1 
ATOM   4326  H  HG23 . VAL A 1 293 ? -11.858 -7.258  36.413  1.00 50.14  ? 311 VAL A HG23 1 
ATOM   4327  N  N    . ALA A 1 294 ? -15.715 -8.440  34.012  1.00 36.87  ? 312 ALA A N    1 
ATOM   4328  C  CA   . ALA A 1 294 ? -17.078 -8.765  33.603  1.00 34.42  ? 312 ALA A CA   1 
ATOM   4329  C  C    . ALA A 1 294 ? -17.183 -9.346  32.196  1.00 31.11  ? 312 ALA A C    1 
ATOM   4330  O  O    . ALA A 1 294 ? -18.293 -9.656  31.749  1.00 31.75  ? 312 ALA A O    1 
ATOM   4331  C  CB   . ALA A 1 294 ? -17.960 -7.514  33.697  1.00 36.50  ? 312 ALA A CB   1 
ATOM   4332  H  H    . ALA A 1 294 ? -15.439 -7.676  33.730  1.00 44.24  ? 312 ALA A H    1 
ATOM   4333  H  HA   . ALA A 1 294 ? -17.420 -9.435  34.216  1.00 41.30  ? 312 ALA A HA   1 
ATOM   4334  H  HB1  . ALA A 1 294 ? -17.981 -7.211  34.618  1.00 43.80  ? 312 ALA A HB1  1 
ATOM   4335  H  HB2  . ALA A 1 294 ? -17.587 -6.822  33.129  1.00 43.80  ? 312 ALA A HB2  1 
ATOM   4336  H  HB3  . ALA A 1 294 ? -18.857 -7.737  33.401  1.00 43.80  ? 312 ALA A HB3  1 
ATOM   4337  N  N    . GLY A 1 295 ? -16.072 -9.513  31.490  1.00 25.29  ? 313 GLY A N    1 
ATOM   4338  C  CA   . GLY A 1 295 ? -16.123 -9.885  30.097  1.00 21.71  ? 313 GLY A CA   1 
ATOM   4339  C  C    . GLY A 1 295 ? -15.963 -11.369 29.836  1.00 19.42  ? 313 GLY A C    1 
ATOM   4340  O  O    . GLY A 1 295 ? -16.056 -12.210 30.734  1.00 19.41  ? 313 GLY A O    1 
ATOM   4341  H  H    . GLY A 1 295 ? -15.276 -9.414  31.802  1.00 30.35  ? 313 GLY A H    1 
ATOM   4342  H  HA2  . GLY A 1 295 ? -16.979 -9.611  29.732  1.00 26.05  ? 313 GLY A HA2  1 
ATOM   4343  H  HA3  . GLY A 1 295 ? -15.415 -9.422  29.623  1.00 26.05  ? 313 GLY A HA3  1 
ATOM   4344  N  N    . PRO A 1 296 ? -15.729 -11.711 28.568  1.00 17.52  ? 314 PRO A N    1 
ATOM   4345  C  CA   . PRO A 1 296 ? -15.514 -13.116 28.204  1.00 16.45  ? 314 PRO A CA   1 
ATOM   4346  C  C    . PRO A 1 296 ? -14.259 -13.659 28.862  1.00 16.03  ? 314 PRO A C    1 
ATOM   4347  O  O    . PRO A 1 296 ? -13.271 -12.941 29.042  1.00 16.77  ? 314 PRO A O    1 
ATOM   4348  C  CB   . PRO A 1 296 ? -15.353 -13.064 26.680  1.00 17.89  ? 314 PRO A CB   1 
ATOM   4349  C  CG   . PRO A 1 296 ? -14.884 -11.668 26.402  1.00 19.02  ? 314 PRO A CG   1 
ATOM   4350  C  CD   . PRO A 1 296 ? -15.553 -10.798 27.422  1.00 18.07  ? 314 PRO A CD   1 
ATOM   4351  H  HA   . PRO A 1 296 ? -16.282 -13.660 28.440  1.00 19.74  ? 314 PRO A HA   1 
ATOM   4352  H  HB2  . PRO A 1 296 ? -14.695 -13.717 26.393  1.00 21.47  ? 314 PRO A HB2  1 
ATOM   4353  H  HB3  . PRO A 1 296 ? -16.204 -13.239 26.249  1.00 21.47  ? 314 PRO A HB3  1 
ATOM   4354  H  HG2  . PRO A 1 296 ? -13.919 -11.623 26.493  1.00 22.82  ? 314 PRO A HG2  1 
ATOM   4355  H  HG3  . PRO A 1 296 ? -15.145 -11.408 25.505  1.00 22.82  ? 314 PRO A HG3  1 
ATOM   4356  H  HD2  . PRO A 1 296 ? -14.988 -10.046 27.661  1.00 21.68  ? 314 PRO A HD2  1 
ATOM   4357  H  HD3  . PRO A 1 296 ? -16.409 -10.479 27.098  1.00 21.68  ? 314 PRO A HD3  1 
ATOM   4358  N  N    . LYS A 1 297 ? -14.306 -14.947 29.218  1.00 14.16  ? 315 LYS A N    1 
ATOM   4359  C  CA   . LYS A 1 297 ? -13.164 -15.608 29.833  1.00 15.47  ? 315 LYS A CA   1 
ATOM   4360  C  C    . LYS A 1 297 ? -13.136 -17.076 29.443  1.00 14.91  ? 315 LYS A C    1 
ATOM   4361  O  O    . LYS A 1 297 ? -14.178 -17.712 29.260  1.00 15.65  ? 315 LYS A O    1 
ATOM   4362  C  CB   . LYS A 1 297 ? -13.190 -15.530 31.360  1.00 17.57  ? 315 LYS A CB   1 
ATOM   4363  C  CG   . LYS A 1 297 ? -13.491 -14.138 31.899  1.00 21.06  ? 315 LYS A CG   1 
ATOM   4364  C  CD   . LYS A 1 297 ? -13.680 -14.146 33.391  1.00 25.56  ? 315 LYS A CD   1 
ATOM   4365  C  CE   . LYS A 1 297 ? -13.781 -12.733 33.942  1.00 29.84  ? 315 LYS A CE   1 
ATOM   4366  N  NZ   . LYS A 1 297 ? -13.417 -12.678 35.392  1.00 33.23  ? 315 LYS A NZ   1 
ATOM   4367  H  H    . LYS A 1 297 ? -14.992 -15.455 29.111  1.00 16.99  ? 315 LYS A H    1 
ATOM   4368  H  HA   . LYS A 1 297 ? -12.367 -15.168 29.499  1.00 18.57  ? 315 LYS A HA   1 
ATOM   4369  H  HB2  . LYS A 1 297 ? -13.876 -16.130 31.691  1.00 21.09  ? 315 LYS A HB2  1 
ATOM   4370  H  HB3  . LYS A 1 297 ? -12.322 -15.798 31.701  1.00 21.09  ? 315 LYS A HB3  1 
ATOM   4371  H  HG2  . LYS A 1 297 ? -12.751 -13.547 31.690  1.00 25.28  ? 315 LYS A HG2  1 
ATOM   4372  H  HG3  . LYS A 1 297 ? -14.307 -13.807 31.492  1.00 25.28  ? 315 LYS A HG3  1 
ATOM   4373  H  HD2  . LYS A 1 297 ? -14.498 -14.619 33.610  1.00 30.67  ? 315 LYS A HD2  1 
ATOM   4374  H  HD3  . LYS A 1 297 ? -12.922 -14.584 33.810  1.00 30.67  ? 315 LYS A HD3  1 
ATOM   4375  H  HE2  . LYS A 1 297 ? -13.174 -12.155 33.454  1.00 35.81  ? 315 LYS A HE2  1 
ATOM   4376  H  HE3  . LYS A 1 297 ? -14.692 -12.416 33.844  1.00 35.81  ? 315 LYS A HE3  1 
ATOM   4377  H  HZ1  . LYS A 1 297 ? -13.480 -11.841 35.690  1.00 39.88  ? 315 LYS A HZ1  1 
ATOM   4378  H  HZ2  . LYS A 1 297 ? -13.967 -13.195 35.864  1.00 39.88  ? 315 LYS A HZ2  1 
ATOM   4379  H  HZ3  . LYS A 1 297 ? -12.582 -12.963 35.508  1.00 39.88  ? 315 LYS A HZ3  1 
ATOM   4380  N  N    . GLN A 1 298 ? -11.925 -17.616 29.365  1.00 14.23  ? 316 GLN A N    1 
ATOM   4381  C  CA   . GLN A 1 298 ? -11.716 -18.996 28.957  1.00 15.03  ? 316 GLN A CA   1 
ATOM   4382  C  C    . GLN A 1 298 ? -10.441 -19.513 29.607  1.00 15.42  ? 316 GLN A C    1 
ATOM   4383  O  O    . GLN A 1 298 ? -9.641  -18.750 30.157  1.00 15.65  ? 316 GLN A O    1 
ATOM   4384  C  CB   . GLN A 1 298 ? -11.686 -19.124 27.430  1.00 14.46  ? 316 GLN A CB   1 
ATOM   4385  C  CG   . GLN A 1 298 ? -10.678 -18.258 26.722  1.00 14.49  ? 316 GLN A CG   1 
ATOM   4386  C  CD   . GLN A 1 298 ? -10.928 -18.225 25.228  1.00 14.75  ? 316 GLN A CD   1 
ATOM   4387  O  OE1  . GLN A 1 298 ? -12.000 -17.810 24.772  1.00 15.83  ? 316 GLN A OE1  1 
ATOM   4388  N  NE2  . GLN A 1 298 ? -9.956  -18.684 24.459  1.00 15.78  ? 316 GLN A NE2  1 
ATOM   4389  H  H    . GLN A 1 298 ? -11.197 -17.195 29.547  1.00 17.07  ? 316 GLN A H    1 
ATOM   4390  H  HA   . GLN A 1 298 ? -12.445 -19.548 29.280  1.00 18.03  ? 316 GLN A HA   1 
ATOM   4391  H  HB2  . GLN A 1 298 ? -11.482 -20.045 27.206  1.00 17.35  ? 316 GLN A HB2  1 
ATOM   4392  H  HB3  . GLN A 1 298 ? -12.561 -18.885 27.088  1.00 17.35  ? 316 GLN A HB3  1 
ATOM   4393  H  HG2  . GLN A 1 298 ? -10.738 -17.352 27.062  1.00 17.39  ? 316 GLN A HG2  1 
ATOM   4394  H  HG3  . GLN A 1 298 ? -9.787  -18.612 26.875  1.00 17.39  ? 316 GLN A HG3  1 
ATOM   4395  H  HE21 . GLN A 1 298 ? -9.230  -18.979 24.813  1.00 18.94  ? 316 GLN A HE21 1 
ATOM   4396  H  HE22 . GLN A 1 298 ? -10.048 -18.686 23.604  1.00 18.94  ? 316 GLN A HE22 1 
ATOM   4397  N  N    . ASN A 1 299 ? -10.260 -20.833 29.542  1.00 14.96  ? 317 ASN A N    1 
ATOM   4398  C  CA   . ASN A 1 299 ? -9.138  -21.500 30.192  1.00 15.08  ? 317 ASN A CA   1 
ATOM   4399  C  C    . ASN A 1 299 ? -7.997  -21.833 29.235  1.00 16.22  ? 317 ASN A C    1 
ATOM   4400  O  O    . ASN A 1 299 ? -7.135  -22.654 29.571  1.00 17.36  ? 317 ASN A O    1 
ATOM   4401  C  CB   . ASN A 1 299 ? -9.615  -22.776 30.881  1.00 15.70  ? 317 ASN A CB   1 
ATOM   4402  C  CG   . ASN A 1 299 ? -9.904  -23.872 29.896  1.00 15.15  ? 317 ASN A CG   1 
ATOM   4403  O  OD1  . ASN A 1 299 ? -10.090 -23.604 28.713  1.00 14.75  ? 317 ASN A OD1  1 
ATOM   4404  N  ND2  . ASN A 1 299 ? -9.959  -25.114 30.371  1.00 17.18  ? 317 ASN A ND2  1 
ATOM   4405  H  H    . ASN A 1 299 ? -10.783 -21.369 29.120  1.00 17.95  ? 317 ASN A H    1 
ATOM   4406  H  HA   . ASN A 1 299 ? -8.788  -20.894 30.864  1.00 18.10  ? 317 ASN A HA   1 
ATOM   4407  H  HB2  . ASN A 1 299 ? -8.925  -23.088 31.488  1.00 18.84  ? 317 ASN A HB2  1 
ATOM   4408  H  HB3  . ASN A 1 299 ? -10.429 -22.588 31.373  1.00 18.84  ? 317 ASN A HB3  1 
ATOM   4409  H  HD21 . ASN A 1 299 ? -10.123 -25.770 29.840  1.00 20.61  ? 317 ASN A HD21 1 
ATOM   4410  H  HD22 . ASN A 1 299 ? -9.832  -25.259 31.209  1.00 20.61  ? 317 ASN A HD22 1 
ATOM   4411  N  N    . CYS A 1 300 ? -7.953  -21.202 28.067  1.00 16.52  ? 318 CYS A N    1 
ATOM   4412  C  CA   . CYS A 1 300 ? -6.952  -21.534 27.063  1.00 16.30  ? 318 CYS A CA   1 
ATOM   4413  C  C    . CYS A 1 300 ? -6.751  -20.325 26.161  1.00 15.86  ? 318 CYS A C    1 
ATOM   4414  O  O    . CYS A 1 300 ? -7.635  -19.476 26.021  1.00 15.08  ? 318 CYS A O    1 
ATOM   4415  C  CB   . CYS A 1 300 ? -7.374  -22.761 26.235  1.00 16.67  ? 318 CYS A CB   1 
ATOM   4416  S  SG   . CYS A 1 300 ? -9.064  -22.685 25.572  1.00 17.78  ? 318 CYS A SG   1 
ATOM   4417  H  H    . CYS A 1 300 ? -8.495  -20.577 27.831  1.00 19.83  ? 318 CYS A H    1 
ATOM   4418  H  HA   . CYS A 1 300 ? -6.110  -21.734 27.499  1.00 19.56  ? 318 CYS A HA   1 
ATOM   4419  H  HB2  . CYS A 1 300 ? -6.769  -22.848 25.482  1.00 20.01  ? 318 CYS A HB2  1 
ATOM   4420  H  HB3  . CYS A 1 300 ? -7.317  -23.548 26.799  1.00 20.01  ? 318 CYS A HB3  1 
ATOM   4421  N  N    . GLU A 1 301 ? -5.589  -20.274 25.537  1.00 16.59  ? 319 GLU A N    1 
ATOM   4422  C  CA   . GLU A 1 301 ? -5.306  -19.194 24.604  1.00 16.29  ? 319 GLU A CA   1 
ATOM   4423  C  C    . GLU A 1 301 ? -6.024  -19.448 23.278  1.00 15.82  ? 319 GLU A C    1 
ATOM   4424  O  O    . GLU A 1 301 ? -6.000  -20.570 22.770  1.00 15.47  ? 319 GLU A O    1 
ATOM   4425  C  CB   . GLU A 1 301 ? -3.805  -19.096 24.349  1.00 16.37  ? 319 GLU A CB   1 
ATOM   4426  C  CG   . GLU A 1 301 ? -3.470  -17.911 23.463  1.00 15.89  ? 319 GLU A CG   1 
ATOM   4427  C  CD   . GLU A 1 301 ? -1.996  -17.738 23.173  1.00 16.43  ? 319 GLU A CD   1 
ATOM   4428  O  OE1  . GLU A 1 301 ? -1.163  -18.402 23.823  1.00 16.62  ? 319 GLU A OE1  1 
ATOM   4429  O  OE2  . GLU A 1 301 ? -1.676  -16.913 22.286  1.00 15.79  ? 319 GLU A OE2  1 
ATOM   4430  H  H    . GLU A 1 301 ? -4.953  -20.844 25.632  1.00 19.91  ? 319 GLU A H    1 
ATOM   4431  H  HA   . GLU A 1 301 ? -5.617  -18.352 24.974  1.00 19.55  ? 319 GLU A HA   1 
ATOM   4432  H  HB2  . GLU A 1 301 ? -3.342  -18.987 25.195  1.00 19.65  ? 319 GLU A HB2  1 
ATOM   4433  H  HB3  . GLU A 1 301 ? -3.501  -19.904 23.907  1.00 19.65  ? 319 GLU A HB3  1 
ATOM   4434  H  HG2  . GLU A 1 301 ? -3.924  -18.022 22.613  1.00 19.07  ? 319 GLU A HG2  1 
ATOM   4435  H  HG3  . GLU A 1 301 ? -3.778  -17.101 23.901  1.00 19.07  ? 319 GLU A HG3  1 
ATOM   4436  N  N    . PRO A 1 302 ? -6.668  -18.432 22.698  1.00 15.34  ? 320 PRO A N    1 
ATOM   4437  C  CA   . PRO A 1 302 ? -7.314  -18.623 21.396  1.00 15.97  ? 320 PRO A CA   1 
ATOM   4438  C  C    . PRO A 1 302 ? -6.355  -19.195 20.362  1.00 16.36  ? 320 PRO A C    1 
ATOM   4439  O  O    . PRO A 1 302 ? -5.158  -18.893 20.353  1.00 16.63  ? 320 PRO A O    1 
ATOM   4440  C  CB   . PRO A 1 302 ? -7.763  -17.208 21.006  1.00 17.14  ? 320 PRO A CB   1 
ATOM   4441  C  CG   . PRO A 1 302 ? -7.855  -16.465 22.261  1.00 17.09  ? 320 PRO A CG   1 
ATOM   4442  C  CD   . PRO A 1 302 ? -6.826  -17.048 23.185  1.00 15.37  ? 320 PRO A CD   1 
ATOM   4443  H  HA   . PRO A 1 302 ? -8.083  -19.207 21.488  1.00 19.16  ? 320 PRO A HA   1 
ATOM   4444  H  HB2  . PRO A 1 302 ? -7.107  -16.807 20.415  1.00 20.57  ? 320 PRO A HB2  1 
ATOM   4445  H  HB3  . PRO A 1 302 ? -8.626  -17.248 20.564  1.00 20.57  ? 320 PRO A HB3  1 
ATOM   4446  H  HG2  . PRO A 1 302 ? -7.672  -15.527 22.095  1.00 20.51  ? 320 PRO A HG2  1 
ATOM   4447  H  HG3  . PRO A 1 302 ? -8.745  -16.569 22.633  1.00 20.51  ? 320 PRO A HG3  1 
ATOM   4448  H  HD2  . PRO A 1 302 ? -5.989  -16.562 23.120  1.00 18.45  ? 320 PRO A HD2  1 
ATOM   4449  H  HD3  . PRO A 1 302 ? -7.143  -17.040 24.102  1.00 18.45  ? 320 PRO A HD3  1 
ATOM   4450  N  N    . ASP A 1 303 ? -6.904  -20.028 19.485  1.00 16.85  ? 321 ASP A N    1 
ATOM   4451  C  CA   . ASP A 1 303 ? -6.127  -20.588 18.395  1.00 17.07  ? 321 ASP A CA   1 
ATOM   4452  C  C    . ASP A 1 303 ? -5.575  -19.471 17.521  1.00 16.65  ? 321 ASP A C    1 
ATOM   4453  O  O    . ASP A 1 303 ? -6.234  -18.453 17.281  1.00 17.06  ? 321 ASP A O    1 
ATOM   4454  C  CB   . ASP A 1 303 ? -7.004  -21.486 17.520  1.00 17.30  ? 321 ASP A CB   1 
ATOM   4455  C  CG   . ASP A 1 303 ? -7.397  -22.783 18.197  1.00 18.87  ? 321 ASP A CG   1 
ATOM   4456  O  OD1  . ASP A 1 303 ? -6.749  -23.183 19.185  1.00 17.95  ? 321 ASP A OD1  1 
ATOM   4457  O  OD2  . ASP A 1 303 ? -8.360  -23.418 17.708  1.00 21.43  ? 321 ASP A OD2  1 
ATOM   4458  H  H    . ASP A 1 303 ? -7.725  -20.284 19.502  1.00 20.22  ? 321 ASP A H    1 
ATOM   4459  H  HA   . ASP A 1 303 ? -5.400  -21.112 18.765  1.00 20.48  ? 321 ASP A HA   1 
ATOM   4460  H  HB2  . ASP A 1 303 ? -7.818  -21.009 17.297  1.00 20.75  ? 321 ASP A HB2  1 
ATOM   4461  H  HB3  . ASP A 1 303 ? -6.517  -21.709 16.711  1.00 20.75  ? 321 ASP A HB3  1 
ATOM   4462  N  N    . LEU A 1 304 ? -4.365  -19.676 17.027  1.00 16.97  ? 322 LEU A N    1 
ATOM   4463  C  CA   . LEU A 1 304 ? -3.827  -18.778 16.024  1.00 16.55  ? 322 LEU A CA   1 
ATOM   4464  C  C    . LEU A 1 304 ? -4.556  -19.003 14.711  1.00 17.30  ? 322 LEU A C    1 
ATOM   4465  O  O    . LEU A 1 304 ? -4.903  -20.132 14.363  1.00 18.47  ? 322 LEU A O    1 
ATOM   4466  C  CB   . LEU A 1 304 ? -2.338  -19.033 15.841  1.00 17.25  ? 322 LEU A CB   1 
ATOM   4467  C  CG   . LEU A 1 304 ? -1.447  -18.569 16.993  1.00 17.38  ? 322 LEU A CG   1 
ATOM   4468  C  CD1  . LEU A 1 304 ? -0.029  -19.016 16.693  1.00 18.13  ? 322 LEU A CD1  1 
ATOM   4469  C  CD2  . LEU A 1 304 ? -1.492  -17.061 17.236  1.00 18.60  ? 322 LEU A CD2  1 
ATOM   4470  H  H    . LEU A 1 304 ? -3.841  -20.320 17.254  1.00 20.37  ? 322 LEU A H    1 
ATOM   4471  H  HA   . LEU A 1 304 ? -3.942  -17.855 16.299  1.00 19.86  ? 322 LEU A HA   1 
ATOM   4472  H  HB2  . LEU A 1 304 ? -2.203  -19.988 15.737  1.00 20.70  ? 322 LEU A HB2  1 
ATOM   4473  H  HB3  . LEU A 1 304 ? -2.045  -18.568 15.042  1.00 20.70  ? 322 LEU A HB3  1 
ATOM   4474  H  HG   . LEU A 1 304 ? -1.773  -18.965 17.816  1.00 20.86  ? 322 LEU A HG   1 
ATOM   4475  H  HD11 . LEU A 1 304 ? -0.006  -19.985 16.651  1.00 21.75  ? 322 LEU A HD11 1 
ATOM   4476  H  HD12 . LEU A 1 304 ? 0.248   -18.642 15.842  1.00 21.75  ? 322 LEU A HD12 1 
ATOM   4477  H  HD13 . LEU A 1 304 ? 0.558   -18.702 17.399  1.00 21.75  ? 322 LEU A HD13 1 
ATOM   4478  H  HD21 . LEU A 1 304 ? -1.158  -16.604 16.448  1.00 22.32  ? 322 LEU A HD21 1 
ATOM   4479  H  HD22 . LEU A 1 304 ? -2.409  -16.796 17.409  1.00 22.32  ? 322 LEU A HD22 1 
ATOM   4480  H  HD23 . LEU A 1 304 ? -0.936  -16.848 18.002  1.00 22.32  ? 322 LEU A HD23 1 
ATOM   4481  N  N    A MET A 1 305 ? -4.821  -17.917 13.992  0.50 18.31  ? 323 MET A N    1 
ATOM   4482  N  N    B MET A 1 305 ? -4.809  -17.917 13.990  0.50 17.51  ? 323 MET A N    1 
ATOM   4483  C  CA   A MET A 1 305 ? -5.353  -18.051 12.650  0.50 19.10  ? 323 MET A CA   1 
ATOM   4484  C  CA   B MET A 1 305 ? -5.354  -18.039 12.649  0.50 17.34  ? 323 MET A CA   1 
ATOM   4485  C  C    A MET A 1 305 ? -4.299  -18.702 11.759  0.50 18.74  ? 323 MET A C    1 
ATOM   4486  C  C    B MET A 1 305 ? -4.297  -18.650 11.730  0.50 17.88  ? 323 MET A C    1 
ATOM   4487  O  O    A MET A 1 305 ? -3.104  -18.679 12.071  0.50 17.88  ? 323 MET A O    1 
ATOM   4488  O  O    B MET A 1 305 ? -3.095  -18.557 12.002  0.50 17.18  ? 323 MET A O    1 
ATOM   4489  C  CB   A MET A 1 305 ? -5.769  -16.690 12.102  0.50 22.26  ? 323 MET A CB   1 
ATOM   4490  C  CB   B MET A 1 305 ? -5.813  -16.674 12.141  0.50 19.22  ? 323 MET A CB   1 
ATOM   4491  C  CG   A MET A 1 305 ? -7.102  -16.207 12.665  0.50 25.15  ? 323 MET A CG   1 
ATOM   4492  C  CG   B MET A 1 305 ? -6.879  -16.055 13.051  0.50 20.71  ? 323 MET A CG   1 
ATOM   4493  S  SD   A MET A 1 305 ? -7.861  -14.903 11.696  0.50 25.89  ? 323 MET A SD   1 
ATOM   4494  S  SD   B MET A 1 305 ? -7.708  -14.581 12.449  0.50 21.05  ? 323 MET A SD   1 
ATOM   4495  C  CE   A MET A 1 305 ? -8.374  -15.798 10.234  0.50 26.59  ? 323 MET A CE   1 
ATOM   4496  C  CE   B MET A 1 305 ? -8.692  -15.229 11.097  0.50 21.19  ? 323 MET A CE   1 
ATOM   4497  H  H    A MET A 1 305 ? -4.701  -17.108 14.257  0.50 21.97  ? 323 MET A H    1 
ATOM   4498  H  H    B MET A 1 305 ? -4.675  -17.109 14.252  0.50 21.01  ? 323 MET A H    1 
ATOM   4499  H  HA   A MET A 1 305 ? -6.152  -18.602 12.657  0.50 22.92  ? 323 MET A HA   1 
ATOM   4500  H  HA   B MET A 1 305 ? -6.136  -18.614 12.647  0.50 20.80  ? 323 MET A HA   1 
ATOM   4501  H  HB2  A MET A 1 305 ? -5.091  -16.036 12.334  0.50 26.71  ? 323 MET A HB2  1 
ATOM   4502  H  HB2  B MET A 1 305 ? -5.053  -16.073 12.110  0.50 23.06  ? 323 MET A HB2  1 
ATOM   4503  H  HB3  A MET A 1 305 ? -5.855  -16.751 11.138  0.50 26.71  ? 323 MET A HB3  1 
ATOM   4504  H  HB3  B MET A 1 305 ? -6.192  -16.775 11.253  0.50 23.06  ? 323 MET A HB3  1 
ATOM   4505  H  HG2  A MET A 1 305 ? -7.719  -16.955 12.691  0.50 30.18  ? 323 MET A HG2  1 
ATOM   4506  H  HG2  B MET A 1 305 ? -7.566  -16.722 13.204  0.50 24.86  ? 323 MET A HG2  1 
ATOM   4507  H  HG3  A MET A 1 305 ? -6.957  -15.865 13.561  0.50 30.18  ? 323 MET A HG3  1 
ATOM   4508  H  HG3  B MET A 1 305 ? -6.455  -15.817 13.890  0.50 24.86  ? 323 MET A HG3  1 
ATOM   4509  H  HE1  A MET A 1 305 ? -9.282  -15.542 10.009  0.50 31.91  ? 323 MET A HE1  1 
ATOM   4510  H  HE1  B MET A 1 305 ? -9.558  -15.501 11.439  0.50 25.43  ? 323 MET A HE1  1 
ATOM   4511  H  HE2  A MET A 1 305 ? -7.777  -15.577 9.502   0.50 31.91  ? 323 MET A HE2  1 
ATOM   4512  H  HE2  B MET A 1 305 ? -8.804  -14.536 10.427  0.50 25.43  ? 323 MET A HE2  1 
ATOM   4513  H  HE3  A MET A 1 305 ? -8.334  -16.750 10.417  0.50 31.91  ? 323 MET A HE3  1 
ATOM   4514  H  HE3  B MET A 1 305 ? -8.235  -15.992 10.711  0.50 25.43  ? 323 MET A HE3  1 
ATOM   4515  N  N    . PRO A 1 306 ? -4.718  -19.320 10.656  1.00 19.08  ? 324 PRO A N    1 
ATOM   4516  C  CA   . PRO A 1 306 ? -3.748  -20.060 9.834   1.00 19.37  ? 324 PRO A CA   1 
ATOM   4517  C  C    . PRO A 1 306 ? -2.539  -19.248 9.400   1.00 18.98  ? 324 PRO A C    1 
ATOM   4518  O  O    . PRO A 1 306 ? -1.439  -19.803 9.327   1.00 19.55  ? 324 PRO A O    1 
ATOM   4519  C  CB   . PRO A 1 306 ? -4.594  -20.560 8.652   1.00 19.90  ? 324 PRO A CB   1 
ATOM   4520  C  CG   . PRO A 1 306 ? -5.988  -20.623 9.192   1.00 20.39  ? 324 PRO A CG   1 
ATOM   4521  C  CD   . PRO A 1 306 ? -6.100  -19.471 10.159  1.00 19.77  ? 324 PRO A CD   1 
ATOM   4522  H  HA   . PRO A 1 306 ? -3.426  -20.831 10.328  1.00 23.24  ? 324 PRO A HA   1 
ATOM   4523  H  HB2  . PRO A 1 306 ? -4.534  -19.935 7.913   1.00 23.88  ? 324 PRO A HB2  1 
ATOM   4524  H  HB3  . PRO A 1 306 ? -4.288  -21.437 8.372   1.00 23.88  ? 324 PRO A HB3  1 
ATOM   4525  H  HG2  . PRO A 1 306 ? -6.625  -20.528 8.468   1.00 24.46  ? 324 PRO A HG2  1 
ATOM   4526  H  HG3  . PRO A 1 306 ? -6.126  -21.469 9.647   1.00 24.46  ? 324 PRO A HG3  1 
ATOM   4527  H  HD2  . PRO A 1 306 ? -6.395  -18.666 9.705   1.00 23.72  ? 324 PRO A HD2  1 
ATOM   4528  H  HD3  . PRO A 1 306 ? -6.708  -19.685 10.884  1.00 23.72  ? 324 PRO A HD3  1 
ATOM   4529  N  N    . TYR A 1 307 ? -2.688  -17.946 9.151   1.00 19.37  ? 325 TYR A N    1 
ATOM   4530  C  CA   . TYR A 1 307 ? -1.544  -17.170 8.682   1.00 18.59  ? 325 TYR A CA   1 
ATOM   4531  C  C    . TYR A 1 307 ? -0.423  -17.092 9.716   1.00 18.81  ? 325 TYR A C    1 
ATOM   4532  O  O    . TYR A 1 307 ? 0.743   -16.894 9.349   1.00 20.09  ? 325 TYR A O    1 
ATOM   4533  C  CB   . TYR A 1 307 ? -1.980  -15.769 8.248   1.00 17.83  ? 325 TYR A CB   1 
ATOM   4534  C  CG   . TYR A 1 307 ? -2.565  -14.886 9.332   1.00 16.22  ? 325 TYR A CG   1 
ATOM   4535  C  CD1  . TYR A 1 307 ? -1.747  -14.222 10.229  1.00 16.63  ? 325 TYR A CD1  1 
ATOM   4536  C  CD2  . TYR A 1 307 ? -3.937  -14.680 9.428   1.00 16.65  ? 325 TYR A CD2  1 
ATOM   4537  C  CE1  . TYR A 1 307 ? -2.270  -13.399 11.197  1.00 16.66  ? 325 TYR A CE1  1 
ATOM   4538  C  CE2  . TYR A 1 307 ? -4.470  -13.853 10.405  1.00 17.05  ? 325 TYR A CE2  1 
ATOM   4539  C  CZ   . TYR A 1 307 ? -3.625  -13.208 11.287  1.00 16.17  ? 325 TYR A CZ   1 
ATOM   4540  O  OH   . TYR A 1 307 ? -4.116  -12.374 12.275  1.00 16.03  ? 325 TYR A OH   1 
ATOM   4541  H  H    . TYR A 1 307 ? -3.419  -17.502 9.243   1.00 23.25  ? 325 TYR A H    1 
ATOM   4542  H  HA   . TYR A 1 307 ? -1.182  -17.618 7.901   1.00 22.31  ? 325 TYR A HA   1 
ATOM   4543  H  HB2  . TYR A 1 307 ? -1.205  -15.308 7.891   1.00 21.39  ? 325 TYR A HB2  1 
ATOM   4544  H  HB3  . TYR A 1 307 ? -2.657  -15.863 7.560   1.00 21.39  ? 325 TYR A HB3  1 
ATOM   4545  H  HD1  . TYR A 1 307 ? -0.826  -14.334 10.175  1.00 19.95  ? 325 TYR A HD1  1 
ATOM   4546  H  HD2  . TYR A 1 307 ? -4.506  -15.103 8.826   1.00 19.98  ? 325 TYR A HD2  1 
ATOM   4547  H  HE1  . TYR A 1 307 ? -1.702  -12.968 11.794  1.00 19.99  ? 325 TYR A HE1  1 
ATOM   4548  H  HE2  . TYR A 1 307 ? -5.390  -13.734 10.466  1.00 20.46  ? 325 TYR A HE2  1 
ATOM   4549  H  HH   . TYR A 1 307 ? -4.950  -12.308 12.207  1.00 19.24  ? 325 TYR A HH   1 
ATOM   4550  N  N    . ALA A 1 308 ? -0.746  -17.233 11.004  1.00 17.97  ? 326 ALA A N    1 
ATOM   4551  C  CA   . ALA A 1 308 ? 0.238   -17.092 12.071  1.00 17.53  ? 326 ALA A CA   1 
ATOM   4552  C  C    . ALA A 1 308 ? 0.755   -18.423 12.596  1.00 18.81  ? 326 ALA A C    1 
ATOM   4553  O  O    . ALA A 1 308 ? 1.808   -18.452 13.241  1.00 17.87  ? 326 ALA A O    1 
ATOM   4554  C  CB   . ALA A 1 308 ? -0.375  -16.305 13.239  1.00 16.92  ? 326 ALA A CB   1 
ATOM   4555  H  H    . ALA A 1 308 ? -1.538  -17.412 11.285  1.00 21.56  ? 326 ALA A H    1 
ATOM   4556  H  HA   . ALA A 1 308 ? 0.998   -16.594 11.732  1.00 21.03  ? 326 ALA A HA   1 
ATOM   4557  H  HB1  . ALA A 1 308 ? -1.176  -16.761 13.541  1.00 20.31  ? 326 ALA A HB1  1 
ATOM   4558  H  HB2  . ALA A 1 308 ? 0.271   -16.258 13.961  1.00 20.31  ? 326 ALA A HB2  1 
ATOM   4559  H  HB3  . ALA A 1 308 ? -0.598  -15.411 12.935  1.00 20.31  ? 326 ALA A HB3  1 
ATOM   4560  N  N    . ARG A 1 309 ? 0.064   -19.522 12.314  1.00 18.87  ? 327 ARG A N    1 
ATOM   4561  C  CA   . ARG A 1 309 ? 0.441   -20.794 12.920  1.00 20.80  ? 327 ARG A CA   1 
ATOM   4562  C  C    . ARG A 1 309 ? 1.868   -21.232 12.629  1.00 20.82  ? 327 ARG A C    1 
ATOM   4563  O  O    . ARG A 1 309 ? 2.500   -21.805 13.534  1.00 21.15  ? 327 ARG A O    1 
ATOM   4564  C  CB   . ARG A 1 309 ? -0.546  -21.882 12.494  1.00 21.95  ? 327 ARG A CB   1 
ATOM   4565  C  CG   . ARG A 1 309 ? -1.854  -21.781 13.210  1.00 22.53  ? 327 ARG A CG   1 
ATOM   4566  C  CD   . ARG A 1 309 ? -2.846  -22.779 12.693  1.00 22.06  ? 327 ARG A CD   1 
ATOM   4567  N  NE   . ARG A 1 309 ? -4.188  -22.289 12.952  1.00 22.98  ? 327 ARG A NE   1 
ATOM   4568  C  CZ   . ARG A 1 309 ? -5.298  -22.877 12.538  1.00 24.11  ? 327 ARG A CZ   1 
ATOM   4569  N  NH1  . ARG A 1 309 ? -5.232  -24.000 11.837  1.00 25.91  ? 327 ARG A NH1  1 
ATOM   4570  N  NH2  . ARG A 1 309 ? -6.471  -22.331 12.831  1.00 25.12  ? 327 ARG A NH2  1 
ATOM   4571  H  H    . ARG A 1 309 ? -0.614  -19.559 11.786  1.00 22.64  ? 327 ARG A H    1 
ATOM   4572  H  HA   . ARG A 1 309 ? 0.378   -20.671 13.880  1.00 24.96  ? 327 ARG A HA   1 
ATOM   4573  H  HB2  . ARG A 1 309 ? -0.717  -21.800 11.543  1.00 26.34  ? 327 ARG A HB2  1 
ATOM   4574  H  HB3  . ARG A 1 309 ? -0.163  -22.751 12.689  1.00 26.34  ? 327 ARG A HB3  1 
ATOM   4575  H  HG2  . ARG A 1 309 ? -1.716  -21.950 14.155  1.00 27.04  ? 327 ARG A HG2  1 
ATOM   4576  H  HG3  . ARG A 1 309 ? -2.221  -20.892 13.082  1.00 27.04  ? 327 ARG A HG3  1 
ATOM   4577  H  HD2  . ARG A 1 309 ? -2.732  -22.894 11.737  1.00 26.47  ? 327 ARG A HD2  1 
ATOM   4578  H  HD3  . ARG A 1 309 ? -2.727  -23.628 13.146  1.00 26.47  ? 327 ARG A HD3  1 
ATOM   4579  H  HE   . ARG A 1 309 ? -4.267  -21.564 13.407  1.00 27.57  ? 327 ARG A HE   1 
ATOM   4580  H  HH11 . ARG A 1 309 ? -4.467  -24.346 11.651  1.00 31.09  ? 327 ARG A HH11 1 
ATOM   4581  H  HH12 . ARG A 1 309 ? -5.954  -24.382 11.568  1.00 31.09  ? 327 ARG A HH12 1 
ATOM   4582  H  HH21 . ARG A 1 309 ? -6.504  -21.601 13.285  1.00 30.14  ? 327 ARG A HH21 1 
ATOM   4583  H  HH22 . ARG A 1 309 ? -7.198  -22.706 12.566  1.00 30.14  ? 327 ARG A HH22 1 
ATOM   4584  N  N    . PRO A 1 310 ? 2.427   -21.029 11.432  1.00 20.97  ? 328 PRO A N    1 
ATOM   4585  C  CA   . PRO A 1 310 ? 3.799   -21.512 11.187  1.00 22.51  ? 328 PRO A CA   1 
ATOM   4586  C  C    . PRO A 1 310 ? 4.835   -20.899 12.110  1.00 21.13  ? 328 PRO A C    1 
ATOM   4587  O  O    . PRO A 1 310 ? 5.934   -21.455 12.246  1.00 22.97  ? 328 PRO A O    1 
ATOM   4588  C  CB   . PRO A 1 310 ? 4.058   -21.139 9.719   1.00 24.12  ? 328 PRO A CB   1 
ATOM   4589  C  CG   . PRO A 1 310 ? 2.701   -20.987 9.119   1.00 24.67  ? 328 PRO A CG   1 
ATOM   4590  C  CD   . PRO A 1 310 ? 1.826   -20.446 10.219  1.00 22.88  ? 328 PRO A CD   1 
ATOM   4591  H  HA   . PRO A 1 310 ? 3.827   -22.477 11.276  1.00 27.01  ? 328 PRO A HA   1 
ATOM   4592  H  HB2  . PRO A 1 310 ? 4.555   -20.308 9.672   1.00 28.94  ? 328 PRO A HB2  1 
ATOM   4593  H  HB3  . PRO A 1 310 ? 4.554   -21.848 9.281   1.00 28.94  ? 328 PRO A HB3  1 
ATOM   4594  H  HG2  . PRO A 1 310 ? 2.741   -20.367 8.374   1.00 29.60  ? 328 PRO A HG2  1 
ATOM   4595  H  HG3  . PRO A 1 310 ? 2.379   -21.850 8.816   1.00 29.60  ? 328 PRO A HG3  1 
ATOM   4596  H  HD2  . PRO A 1 310 ? 1.862   -19.477 10.245  1.00 27.45  ? 328 PRO A HD2  1 
ATOM   4597  H  HD3  . PRO A 1 310 ? 0.909   -20.741 10.109  1.00 27.45  ? 328 PRO A HD3  1 
ATOM   4598  N  N    . PHE A 1 311 ? 4.513   -19.791 12.769  1.00 18.49  ? 329 PHE A N    1 
ATOM   4599  C  CA   . PHE A 1 311 ? 5.476   -19.063 13.579  1.00 18.12  ? 329 PHE A CA   1 
ATOM   4600  C  C    . PHE A 1 311 ? 5.392   -19.402 15.058  1.00 19.35  ? 329 PHE A C    1 
ATOM   4601  O  O    . PHE A 1 311 ? 6.117   -18.804 15.858  1.00 20.47  ? 329 PHE A O    1 
ATOM   4602  C  CB   . PHE A 1 311 ? 5.303   -17.561 13.349  1.00 19.13  ? 329 PHE A CB   1 
ATOM   4603  C  CG   . PHE A 1 311 ? 5.433   -17.169 11.913  1.00 19.07  ? 329 PHE A CG   1 
ATOM   4604  C  CD1  . PHE A 1 311 ? 6.682   -17.017 11.337  1.00 18.96  ? 329 PHE A CD1  1 
ATOM   4605  C  CD2  . PHE A 1 311 ? 4.309   -16.989 11.125  1.00 19.06  ? 329 PHE A CD2  1 
ATOM   4606  C  CE1  . PHE A 1 311 ? 6.806   -16.668 10.004  1.00 19.65  ? 329 PHE A CE1  1 
ATOM   4607  C  CE2  . PHE A 1 311 ? 4.424   -16.646 9.792   1.00 18.28  ? 329 PHE A CE2  1 
ATOM   4608  C  CZ   . PHE A 1 311 ? 5.672   -16.481 9.231   1.00 18.47  ? 329 PHE A CZ   1 
ATOM   4609  H  H    . PHE A 1 311 ? 3.729   -19.437 12.762  1.00 22.19  ? 329 PHE A H    1 
ATOM   4610  H  HA   . PHE A 1 311 ? 6.374   -19.297 13.296  1.00 21.75  ? 329 PHE A HA   1 
ATOM   4611  H  HB2  . PHE A 1 311 ? 4.420   -17.297 13.652  1.00 22.95  ? 329 PHE A HB2  1 
ATOM   4612  H  HB3  . PHE A 1 311 ? 5.983   -17.086 13.852  1.00 22.95  ? 329 PHE A HB3  1 
ATOM   4613  H  HD1  . PHE A 1 311 ? 7.445   -17.151 11.851  1.00 22.76  ? 329 PHE A HD1  1 
ATOM   4614  H  HD2  . PHE A 1 311 ? 3.465   -17.102 11.499  1.00 22.87  ? 329 PHE A HD2  1 
ATOM   4615  H  HE1  . PHE A 1 311 ? 7.650   -16.558 9.628   1.00 23.58  ? 329 PHE A HE1  1 
ATOM   4616  H  HE2  . PHE A 1 311 ? 3.660   -16.526 9.275   1.00 21.94  ? 329 PHE A HE2  1 
ATOM   4617  H  HZ   . PHE A 1 311 ? 5.753   -16.245 8.335   1.00 22.16  ? 329 PHE A HZ   1 
ATOM   4618  N  N    . ALA A 1 312 ? 4.544   -20.366 15.436  1.00 19.52  ? 330 ALA A N    1 
ATOM   4619  C  CA   . ALA A 1 312 ? 4.416   -20.767 16.833  1.00 20.77  ? 330 ALA A CA   1 
ATOM   4620  C  C    . ALA A 1 312 ? 4.115   -22.254 16.935  1.00 22.68  ? 330 ALA A C    1 
ATOM   4621  O  O    . ALA A 1 312 ? 3.415   -22.685 17.859  1.00 21.71  ? 330 ALA A O    1 
ATOM   4622  C  CB   . ALA A 1 312 ? 3.344   -19.942 17.550  1.00 21.94  ? 330 ALA A CB   1 
ATOM   4623  H  H    . ALA A 1 312 ? 4.031   -20.800 14.899  1.00 23.43  ? 330 ALA A H    1 
ATOM   4624  H  HA   . ALA A 1 312 ? 5.252   -20.599 17.296  1.00 24.93  ? 330 ALA A HA   1 
ATOM   4625  H  HB1  . ALA A 1 312 ? 2.489   -20.089 17.116  1.00 26.33  ? 330 ALA A HB1  1 
ATOM   4626  H  HB2  . ALA A 1 312 ? 3.297   -20.222 18.477  1.00 26.33  ? 330 ALA A HB2  1 
ATOM   4627  H  HB3  . ALA A 1 312 ? 3.583   -19.003 17.500  1.00 26.33  ? 330 ALA A HB3  1 
ATOM   4628  N  N    . VAL A 1 313 ? 4.618   -23.043 15.983  1.00 24.89  ? 331 VAL A N    1 
ATOM   4629  C  CA   . VAL A 1 313 ? 4.448   -24.485 16.054  1.00 25.11  ? 331 VAL A CA   1 
ATOM   4630  C  C    . VAL A 1 313 ? 4.971   -24.964 17.393  1.00 24.12  ? 331 VAL A C    1 
ATOM   4631  O  O    . VAL A 1 313 ? 6.034   -24.539 17.855  1.00 24.94  ? 331 VAL A O    1 
ATOM   4632  C  CB   . VAL A 1 313 ? 5.164   -25.179 14.879  1.00 25.81  ? 331 VAL A CB   1 
ATOM   4633  C  CG1  . VAL A 1 313 ? 4.675   -24.618 13.552  1.00 27.14  ? 331 VAL A CG1  1 
ATOM   4634  C  CG2  . VAL A 1 313 ? 6.680   -25.060 15.012  1.00 28.60  ? 331 VAL A CG2  1 
ATOM   4635  H  H    . VAL A 1 313 ? 5.056   -22.767 15.295  1.00 29.86  ? 331 VAL A H    1 
ATOM   4636  H  HA   . VAL A 1 313 ? 3.506   -24.704 15.987  1.00 30.13  ? 331 VAL A HA   1 
ATOM   4637  H  HB   . VAL A 1 313 ? 4.949   -26.125 14.898  1.00 30.97  ? 331 VAL A HB   1 
ATOM   4638  H  HG11 . VAL A 1 313 ? 3.751   -24.340 13.648  1.00 32.57  ? 331 VAL A HG11 1 
ATOM   4639  H  HG12 . VAL A 1 313 ? 5.226   -23.857 13.309  1.00 32.57  ? 331 VAL A HG12 1 
ATOM   4640  H  HG13 . VAL A 1 313 ? 4.745   -25.307 12.873  1.00 32.57  ? 331 VAL A HG13 1 
ATOM   4641  H  HG21 . VAL A 1 313 ? 7.090   -25.278 14.160  1.00 34.33  ? 331 VAL A HG21 1 
ATOM   4642  H  HG22 . VAL A 1 313 ? 6.905   -24.150 15.263  1.00 34.33  ? 331 VAL A HG22 1 
ATOM   4643  H  HG23 . VAL A 1 313 ? 6.987   -25.676 15.695  1.00 34.33  ? 331 VAL A HG23 1 
ATOM   4644  N  N    . GLY A 1 314 ? 4.211   -25.845 18.033  1.00 24.76  ? 332 GLY A N    1 
ATOM   4645  C  CA   . GLY A 1 314 ? 4.617   -26.413 19.296  1.00 25.08  ? 332 GLY A CA   1 
ATOM   4646  C  C    . GLY A 1 314 ? 4.080   -25.701 20.514  1.00 25.31  ? 332 GLY A C    1 
ATOM   4647  O  O    . GLY A 1 314 ? 4.267   -26.199 21.633  1.00 27.00  ? 332 GLY A O    1 
ATOM   4648  H  H    . GLY A 1 314 ? 3.451   -26.128 17.747  1.00 29.72  ? 332 GLY A H    1 
ATOM   4649  H  HA2  . GLY A 1 314 ? 4.314   -27.334 19.334  1.00 30.09  ? 332 GLY A HA2  1 
ATOM   4650  H  HA3  . GLY A 1 314 ? 5.586   -26.397 19.347  1.00 30.09  ? 332 GLY A HA3  1 
ATOM   4651  N  N    . LYS A 1 315 ? 3.440   -24.548 20.341  1.00 23.87  ? 333 LYS A N    1 
ATOM   4652  C  CA   . LYS A 1 315 ? 2.739   -23.910 21.439  1.00 22.72  ? 333 LYS A CA   1 
ATOM   4653  C  C    . LYS A 1 315 ? 1.350   -24.521 21.572  1.00 23.46  ? 333 LYS A C    1 
ATOM   4654  O  O    . LYS A 1 315 ? 0.859   -25.210 20.671  1.00 25.60  ? 333 LYS A O    1 
ATOM   4655  C  CB   . LYS A 1 315 ? 2.637   -22.401 21.217  1.00 24.48  ? 333 LYS A CB   1 
ATOM   4656  C  CG   . LYS A 1 315 ? 3.983   -21.718 21.040  1.00 27.02  ? 333 LYS A CG   1 
ATOM   4657  C  CD   . LYS A 1 315 ? 4.812   -21.740 22.314  1.00 29.38  ? 333 LYS A CD   1 
ATOM   4658  C  CE   . LYS A 1 315 ? 6.304   -21.629 21.992  1.00 32.68  ? 333 LYS A CE   1 
ATOM   4659  N  NZ   . LYS A 1 315 ? 7.158   -21.708 23.207  1.00 35.60  ? 333 LYS A NZ   1 
ATOM   4660  H  H    . LYS A 1 315 ? 3.399   -24.119 19.596  1.00 28.64  ? 333 LYS A H    1 
ATOM   4661  H  HA   . LYS A 1 315 ? 3.224   -24.046 22.268  1.00 27.26  ? 333 LYS A HA   1 
ATOM   4662  H  HB2  . LYS A 1 315 ? 2.115   -22.239 20.416  1.00 29.38  ? 333 LYS A HB2  1 
ATOM   4663  H  HB3  . LYS A 1 315 ? 2.200   -22.001 21.985  1.00 29.38  ? 333 LYS A HB3  1 
ATOM   4664  H  HG2  . LYS A 1 315 ? 4.484   -22.175 20.346  1.00 32.42  ? 333 LYS A HG2  1 
ATOM   4665  H  HG3  . LYS A 1 315 ? 3.840   -20.792 20.790  1.00 32.42  ? 333 LYS A HG3  1 
ATOM   4666  H  HD2  . LYS A 1 315 ? 4.562   -20.991 22.877  1.00 35.25  ? 333 LYS A HD2  1 
ATOM   4667  H  HD3  . LYS A 1 315 ? 4.660   -22.574 22.786  1.00 35.25  ? 333 LYS A HD3  1 
ATOM   4668  H  HE2  . LYS A 1 315 ? 6.555   -22.355 21.400  1.00 39.21  ? 333 LYS A HE2  1 
ATOM   4669  H  HE3  . LYS A 1 315 ? 6.472   -20.777 21.561  1.00 39.21  ? 333 LYS A HE3  1 
ATOM   4670  H  HZ1  . LYS A 1 315 ? 8.017   -21.665 22.978  1.00 42.72  ? 333 LYS A HZ1  1 
ATOM   4671  H  HZ2  . LYS A 1 315 ? 6.971   -21.032 23.755  1.00 42.72  ? 333 LYS A HZ2  1 
ATOM   4672  H  HZ3  . LYS A 1 315 ? 7.011   -22.475 23.633  1.00 42.72  ? 333 LYS A HZ3  1 
ATOM   4673  N  N    . ARG A 1 316 ? 0.724   -24.282 22.719  1.00 22.36  ? 334 ARG A N    1 
ATOM   4674  C  CA   . ARG A 1 316 ? -0.574  -24.862 23.024  1.00 21.86  ? 334 ARG A CA   1 
ATOM   4675  C  C    . ARG A 1 316 ? -1.641  -23.779 23.034  1.00 20.14  ? 334 ARG A C    1 
ATOM   4676  O  O    . ARG A 1 316 ? -1.505  -22.774 23.739  1.00 22.66  ? 334 ARG A O    1 
ATOM   4677  C  CB   . ARG A 1 316 ? -0.566  -25.565 24.381  1.00 22.73  ? 334 ARG A CB   1 
ATOM   4678  C  CG   . ARG A 1 316 ? -1.930  -26.098 24.775  1.00 25.62  ? 334 ARG A CG   1 
ATOM   4679  C  CD   . ARG A 1 316 ? -1.872  -26.941 26.040  1.00 27.97  ? 334 ARG A CD   1 
ATOM   4680  N  NE   . ARG A 1 316 ? -1.009  -28.107 25.902  1.00 31.53  ? 334 ARG A NE   1 
ATOM   4681  C  CZ   . ARG A 1 316 ? -1.361  -29.241 25.302  1.00 35.33  ? 334 ARG A CZ   1 
ATOM   4682  N  NH1  . ARG A 1 316 ? -2.568  -29.379 24.762  1.00 36.38  ? 334 ARG A NH1  1 
ATOM   4683  N  NH2  . ARG A 1 316 ? -0.495  -30.240 25.242  1.00 36.77  ? 334 ARG A NH2  1 
ATOM   4684  H  H    . ARG A 1 316 ? 1.037   -23.780 23.343  1.00 26.83  ? 334 ARG A H    1 
ATOM   4685  H  HA   . ARG A 1 316 ? -0.789  -25.509 22.333  1.00 26.23  ? 334 ARG A HA   1 
ATOM   4686  H  HB2  . ARG A 1 316 ? 0.050   -26.313 24.346  1.00 27.28  ? 334 ARG A HB2  1 
ATOM   4687  H  HB3  . ARG A 1 316 ? -0.282  -24.934 25.061  1.00 27.28  ? 334 ARG A HB3  1 
ATOM   4688  H  HG2  . ARG A 1 316 ? -2.529  -25.353 24.936  1.00 30.74  ? 334 ARG A HG2  1 
ATOM   4689  H  HG3  . ARG A 1 316 ? -2.274  -26.653 24.058  1.00 30.74  ? 334 ARG A HG3  1 
ATOM   4690  H  HD2  . ARG A 1 316 ? -1.528  -26.398 26.767  1.00 33.56  ? 334 ARG A HD2  1 
ATOM   4691  H  HD3  . ARG A 1 316 ? -2.765  -27.252 26.254  1.00 33.56  ? 334 ARG A HD3  1 
ATOM   4692  H  HE   . ARG A 1 316 ? -0.217  -28.059 26.232  1.00 37.84  ? 334 ARG A HE   1 
ATOM   4693  H  HH11 . ARG A 1 316 ? -3.133  -28.731 24.799  1.00 43.66  ? 334 ARG A HH11 1 
ATOM   4694  H  HH12 . ARG A 1 316 ? -2.785  -30.116 24.376  1.00 43.66  ? 334 ARG A HH12 1 
ATOM   4695  H  HH21 . ARG A 1 316 ? 0.286   -30.153 25.590  1.00 44.12  ? 334 ARG A HH21 1 
ATOM   4696  H  HH22 . ARG A 1 316 ? -0.715  -30.976 24.856  1.00 44.12  ? 334 ARG A HH22 1 
ATOM   4697  N  N    . THR A 1 317 ? -2.707  -24.002 22.273  1.00 18.21  ? 335 THR A N    1 
ATOM   4698  C  CA   . THR A 1 317 ? -3.887  -23.150 22.264  1.00 17.25  ? 335 THR A CA   1 
ATOM   4699  C  C    . THR A 1 317 ? -5.112  -24.031 22.495  1.00 16.89  ? 335 THR A C    1 
ATOM   4700  O  O    . THR A 1 317 ? -4.999  -25.238 22.732  1.00 17.78  ? 335 THR A O    1 
ATOM   4701  C  CB   . THR A 1 317 ? -3.980  -22.347 20.960  1.00 17.16  ? 335 THR A CB   1 
ATOM   4702  O  OG1  . THR A 1 317 ? -4.080  -23.238 19.847  1.00 17.10  ? 335 THR A OG1  1 
ATOM   4703  C  CG2  . THR A 1 317 ? -2.742  -21.486 20.767  1.00 18.39  ? 335 THR A CG2  1 
ATOM   4704  H  H    . THR A 1 317 ? -2.772  -24.668 21.733  1.00 21.85  ? 335 THR A H    1 
ATOM   4705  H  HA   . THR A 1 317 ? -3.842  -22.506 22.988  1.00 20.70  ? 335 THR A HA   1 
ATOM   4706  H  HB   . THR A 1 317 ? -4.763  -21.776 21.002  1.00 20.60  ? 335 THR A HB   1 
ATOM   4707  H  HG1  . THR A 1 317 ? -4.785  -23.692 19.904  1.00 20.52  ? 335 THR A HG1  1 
ATOM   4708  H  HG21 . THR A 1 317 ? -1.951  -22.045 20.729  1.00 22.07  ? 335 THR A HG21 1 
ATOM   4709  H  HG22 . THR A 1 317 ? -2.813  -20.984 19.940  1.00 22.07  ? 335 THR A HG22 1 
ATOM   4710  H  HG23 . THR A 1 317 ? -2.652  -20.863 21.506  1.00 22.07  ? 335 THR A HG23 1 
ATOM   4711  N  N    . CYS A 1 318 ? -6.299  -23.426 22.428  1.00 16.44  ? 336 CYS A N    1 
ATOM   4712  C  CA   . CYS A 1 318 ? -7.515  -24.134 22.833  1.00 16.44  ? 336 CYS A CA   1 
ATOM   4713  C  C    . CYS A 1 318 ? -7.699  -25.470 22.114  1.00 17.25  ? 336 CYS A C    1 
ATOM   4714  O  O    . CYS A 1 318 ? -8.136  -26.449 22.728  1.00 18.64  ? 336 CYS A O    1 
ATOM   4715  C  CB   . CYS A 1 318 ? -8.739  -23.248 22.610  1.00 17.65  ? 336 CYS A CB   1 
ATOM   4716  S  SG   . CYS A 1 318 ? -8.856  -21.849 23.732  1.00 18.16  ? 336 CYS A SG   1 
ATOM   4717  H  H    . CYS A 1 318 ? -6.427  -22.621 22.156  1.00 19.73  ? 336 CYS A H    1 
ATOM   4718  H  HA   . CYS A 1 318 ? -7.434  -24.327 23.780  1.00 19.73  ? 336 CYS A HA   1 
ATOM   4719  H  HB2  . CYS A 1 318 ? -8.707  -22.897 21.707  1.00 21.18  ? 336 CYS A HB2  1 
ATOM   4720  H  HB3  . CYS A 1 318 ? -9.537  -23.787 22.729  1.00 21.18  ? 336 CYS A HB3  1 
ATOM   4721  N  N    . SER A 1 319 ? -7.412  -25.529 20.809  1.00 17.62  ? 337 SER A N    1 
ATOM   4722  C  CA   . SER A 1 319 ? -7.638  -26.760 20.054  1.00 17.88  ? 337 SER A CA   1 
ATOM   4723  C  C    . SER A 1 319 ? -6.536  -27.792 20.248  1.00 18.58  ? 337 SER A C    1 
ATOM   4724  O  O    . SER A 1 319 ? -6.703  -28.939 19.813  1.00 20.35  ? 337 SER A O    1 
ATOM   4725  C  CB   . SER A 1 319 ? -7.770  -26.461 18.557  1.00 19.97  ? 337 SER A CB   1 
ATOM   4726  O  OG   . SER A 1 319 ? -8.988  -25.791 18.283  1.00 21.32  ? 337 SER A OG   1 
ATOM   4727  H  H    . SER A 1 319 ? -7.091  -24.878 20.348  1.00 21.14  ? 337 SER A H    1 
ATOM   4728  H  HA   . SER A 1 319 ? -8.475  -27.142 20.361  1.00 21.46  ? 337 SER A HA   1 
ATOM   4729  H  HB2  . SER A 1 319 ? -7.031  -25.898 18.280  1.00 23.96  ? 337 SER A HB2  1 
ATOM   4730  H  HB3  . SER A 1 319 ? -7.753  -27.297 18.065  1.00 23.96  ? 337 SER A HB3  1 
ATOM   4731  H  HG   . SER A 1 319 ? -9.067  -25.123 18.786  1.00 25.59  ? 337 SER A HG   1 
ATOM   4732  N  N    . GLY A 1 320 ? -5.427  -27.417 20.877  1.00 19.08  ? 338 GLY A N    1 
ATOM   4733  C  CA   . GLY A 1 320 ? -4.301  -28.313 21.041  1.00 20.37  ? 338 GLY A CA   1 
ATOM   4734  C  C    . GLY A 1 320 ? -2.986  -27.706 20.592  1.00 20.84  ? 338 GLY A C    1 
ATOM   4735  O  O    . GLY A 1 320 ? -2.826  -26.484 20.610  1.00 21.21  ? 338 GLY A O    1 
ATOM   4736  H  H    . GLY A 1 320 ? -5.305  -26.638 21.220  1.00 22.89  ? 338 GLY A H    1 
ATOM   4737  H  HA2  . GLY A 1 320 ? -4.220  -28.553 21.978  1.00 24.44  ? 338 GLY A HA2  1 
ATOM   4738  H  HA3  . GLY A 1 320 ? -4.456  -29.117 20.522  1.00 24.44  ? 338 GLY A HA3  1 
ATOM   4739  N  N    . ILE A 1 321 ? -2.049  -28.544 20.160  1.00 22.12  ? 339 ILE A N    1 
ATOM   4740  C  CA   . ILE A 1 321 ? -0.711  -28.088 19.796  1.00 24.18  ? 339 ILE A CA   1 
ATOM   4741  C  C    . ILE A 1 321 ? -0.740  -27.460 18.406  1.00 25.50  ? 339 ILE A C    1 
ATOM   4742  O  O    . ILE A 1 321 ? -1.336  -28.009 17.472  1.00 27.83  ? 339 ILE A O    1 
ATOM   4743  C  CB   . ILE A 1 321 ? 0.291   -29.251 19.863  1.00 25.18  ? 339 ILE A CB   1 
ATOM   4744  C  CG1  . ILE A 1 321 ? 0.272   -29.875 21.261  1.00 25.98  ? 339 ILE A CG1  1 
ATOM   4745  C  CG2  . ILE A 1 321 ? 1.693   -28.775 19.498  1.00 26.44  ? 339 ILE A CG2  1 
ATOM   4746  C  CD1  . ILE A 1 321 ? 0.411   -28.874 22.390  1.00 27.15  ? 339 ILE A CD1  1 
ATOM   4747  H  H    . ILE A 1 321 ? -2.164  -29.392 20.068  1.00 26.54  ? 339 ILE A H    1 
ATOM   4748  H  HA   . ILE A 1 321 ? -0.432  -27.402 20.422  1.00 29.02  ? 339 ILE A HA   1 
ATOM   4749  H  HB   . ILE A 1 321 ? 0.027   -29.927 19.219  1.00 30.22  ? 339 ILE A HB   1 
ATOM   4750  H  HG12 . ILE A 1 321 ? -0.571  -30.340 21.382  1.00 31.18  ? 339 ILE A HG12 1 
ATOM   4751  H  HG13 . ILE A 1 321 ? 1.010   -30.501 21.331  1.00 31.18  ? 339 ILE A HG13 1 
ATOM   4752  H  HG21 . ILE A 1 321 ? 2.327   -29.482 19.692  1.00 31.73  ? 339 ILE A HG21 1 
ATOM   4753  H  HG22 . ILE A 1 321 ? 1.717   -28.559 18.553  1.00 31.73  ? 339 ILE A HG22 1 
ATOM   4754  H  HG23 . ILE A 1 321 ? 1.905   -27.987 20.023  1.00 31.73  ? 339 ILE A HG23 1 
ATOM   4755  H  HD11 . ILE A 1 321 ? 0.711   -29.338 23.188  1.00 32.58  ? 339 ILE A HD11 1 
ATOM   4756  H  HD12 . ILE A 1 321 ? 1.059   -28.199 22.136  1.00 32.58  ? 339 ILE A HD12 1 
ATOM   4757  H  HD13 . ILE A 1 321 ? -0.452  -28.460 22.553  1.00 32.58  ? 339 ILE A HD13 1 
ATOM   4758  N  N    . VAL A 1 322 ? -0.086  -26.304 18.269  1.00 24.24  ? 340 VAL A N    1 
ATOM   4759  C  CA   . VAL A 1 322 ? -0.039  -25.605 16.990  1.00 25.02  ? 340 VAL A CA   1 
ATOM   4760  C  C    . VAL A 1 322 ? 0.825   -26.388 16.010  1.00 25.84  ? 340 VAL A C    1 
ATOM   4761  O  O    . VAL A 1 322 ? 1.962   -26.764 16.323  1.00 25.08  ? 340 VAL A O    1 
ATOM   4762  C  CB   . VAL A 1 322 ? 0.516   -24.183 17.175  1.00 25.79  ? 340 VAL A CB   1 
ATOM   4763  C  CG1  . VAL A 1 322 ? 0.635   -23.482 15.815  1.00 26.92  ? 340 VAL A CG1  1 
ATOM   4764  C  CG2  . VAL A 1 322 ? -0.355  -23.365 18.131  1.00 24.92  ? 340 VAL A CG2  1 
ATOM   4765  H  H    . VAL A 1 322 ? 0.337   -25.906 18.903  1.00 29.08  ? 340 VAL A H    1 
ATOM   4766  H  HA   . VAL A 1 322 ? -0.940  -25.548 16.635  1.00 30.03  ? 340 VAL A HA   1 
ATOM   4767  H  HB   . VAL A 1 322 ? 1.400   -24.246 17.570  1.00 30.95  ? 340 VAL A HB   1 
ATOM   4768  H  HG11 . VAL A 1 322 ? 0.051   -23.924 15.179  1.00 32.30  ? 340 VAL A HG11 1 
ATOM   4769  H  HG12 . VAL A 1 322 ? 0.372   -22.553 15.914  1.00 32.30  ? 340 VAL A HG12 1 
ATOM   4770  H  HG13 . VAL A 1 322 ? 1.554   -23.534 15.511  1.00 32.30  ? 340 VAL A HG13 1 
ATOM   4771  H  HG21 . VAL A 1 322 ? -0.726  -23.955 18.805  1.00 29.90  ? 340 VAL A HG21 1 
ATOM   4772  H  HG22 . VAL A 1 322 ? 0.192   -22.684 18.552  1.00 29.90  ? 340 VAL A HG22 1 
ATOM   4773  H  HG23 . VAL A 1 322 ? -1.071  -22.948 17.626  1.00 29.90  ? 340 VAL A HG23 1 
ATOM   4774  N  N    . THR A 1 323 ? 0.299   -26.618 14.814  1.00 27.35  ? 341 THR A N    1 
ATOM   4775  C  CA   . THR A 1 323 ? 1.026   -27.234 13.713  1.00 28.22  ? 341 THR A CA   1 
ATOM   4776  C  C    . THR A 1 323 ? 0.890   -26.349 12.487  1.00 28.33  ? 341 THR A C    1 
ATOM   4777  O  O    . THR A 1 323 ? -0.065  -25.571 12.373  1.00 27.41  ? 341 THR A O    1 
ATOM   4778  C  CB   . THR A 1 323 ? 0.495   -28.641 13.406  1.00 29.17  ? 341 THR A CB   1 
ATOM   4779  O  OG1  . THR A 1 323 ? -0.900  -28.579 13.090  1.00 30.30  ? 341 THR A OG1  1 
ATOM   4780  C  CG2  . THR A 1 323 ? 0.688   -29.561 14.600  1.00 30.54  ? 341 THR A CG2  1 
ATOM   4781  H  H    . THR A 1 323 ? -0.512  -26.418 14.609  1.00 32.82  ? 341 THR A H    1 
ATOM   4782  H  HA   . THR A 1 323 ? 1.966   -27.316 13.940  1.00 33.86  ? 341 THR A HA   1 
ATOM   4783  H  HB   . THR A 1 323 ? 0.983   -29.005 12.651  1.00 35.00  ? 341 THR A HB   1 
ATOM   4784  H  HG1  . THR A 1 323 ? -1.334  -28.305 13.755  1.00 36.37  ? 341 THR A HG1  1 
ATOM   4785  H  HG21 . THR A 1 323 ? 0.407   -30.462 14.374  1.00 36.65  ? 341 THR A HG21 1 
ATOM   4786  H  HG22 . THR A 1 323 ? 1.623   -29.578 14.857  1.00 36.65  ? 341 THR A HG22 1 
ATOM   4787  H  HG23 . THR A 1 323 ? 0.161   -29.246 15.351  1.00 36.65  ? 341 THR A HG23 1 
ATOM   4788  N  N    . PRO A 1 324 ? 1.848   -26.421 11.546  1.00 31.56  ? 342 PRO A N    1 
ATOM   4789  C  CA   . PRO A 1 324 ? 1.826   -25.491 10.406  1.00 34.28  ? 342 PRO A CA   1 
ATOM   4790  C  C    . PRO A 1 324 ? 0.755   -25.824 9.367   1.00 36.71  ? 342 PRO A C    1 
ATOM   4791  O  O    . PRO A 1 324 ? 0.178   -26.909 9.438   1.00 39.20  ? 342 PRO A O    1 
ATOM   4792  C  CB   . PRO A 1 324 ? 3.230   -25.633 9.803   1.00 34.27  ? 342 PRO A CB   1 
ATOM   4793  C  CG   . PRO A 1 324 ? 3.698   -26.993 10.219  1.00 33.46  ? 342 PRO A CG   1 
ATOM   4794  C  CD   . PRO A 1 324 ? 3.026   -27.313 11.527  1.00 31.78  ? 342 PRO A CD   1 
ATOM   4795  H  HA   . PRO A 1 324 ? 1.691   -24.582 10.718  1.00 41.13  ? 342 PRO A HA   1 
ATOM   4796  H  HB2  . PRO A 1 324 ? 3.182   -25.564 8.836   1.00 41.13  ? 342 PRO A HB2  1 
ATOM   4797  H  HB3  . PRO A 1 324 ? 3.812   -24.943 10.156  1.00 41.13  ? 342 PRO A HB3  1 
ATOM   4798  H  HG2  . PRO A 1 324 ? 3.447   -27.640 9.542   1.00 40.15  ? 342 PRO A HG2  1 
ATOM   4799  H  HG3  . PRO A 1 324 ? 4.662   -26.982 10.327  1.00 40.15  ? 342 PRO A HG3  1 
ATOM   4800  H  HD2  . PRO A 1 324 ? 2.752   -28.244 11.554  1.00 38.13  ? 342 PRO A HD2  1 
ATOM   4801  H  HD3  . PRO A 1 324 ? 3.615   -27.119 12.273  1.00 38.13  ? 342 PRO A HD3  1 
ATOM   4802  N  N    . LEU B 1 8   ? 12.783  -22.362 3.077   1.00 29.12  ? 26  LEU B N    1 
ATOM   4803  C  CA   . LEU B 1 8   ? 14.159  -22.610 3.491   1.00 25.48  ? 26  LEU B CA   1 
ATOM   4804  C  C    . LEU B 1 8   ? 15.144  -21.653 2.822   1.00 23.68  ? 26  LEU B C    1 
ATOM   4805  O  O    . LEU B 1 8   ? 14.868  -21.132 1.748   1.00 24.54  ? 26  LEU B O    1 
ATOM   4806  C  CB   . LEU B 1 8   ? 14.555  -24.038 3.115   1.00 24.84  ? 26  LEU B CB   1 
ATOM   4807  C  CG   . LEU B 1 8   ? 13.926  -25.189 3.896   1.00 25.56  ? 26  LEU B CG   1 
ATOM   4808  C  CD1  . LEU B 1 8   ? 14.136  -26.494 3.142   1.00 27.28  ? 26  LEU B CD1  1 
ATOM   4809  C  CD2  . LEU B 1 8   ? 14.509  -25.281 5.293   1.00 25.88  ? 26  LEU B CD2  1 
ATOM   4810  H  H    . LEU B 1 8   ? 12.288  -22.026 3.695   1.00 34.95  ? 26  LEU B H    1 
ATOM   4811  H  HA   . LEU B 1 8   ? 14.214  -22.483 4.451   1.00 30.58  ? 26  LEU B HA   1 
ATOM   4812  H  HB2  . LEU B 1 8   ? 14.319  -24.172 2.184   1.00 29.80  ? 26  LEU B HB2  1 
ATOM   4813  H  HB3  . LEU B 1 8   ? 15.515  -24.116 3.229   1.00 29.80  ? 26  LEU B HB3  1 
ATOM   4814  H  HG   . LEU B 1 8   ? 12.974  -25.031 3.989   1.00 30.68  ? 26  LEU B HG   1 
ATOM   4815  H  HD11 . LEU B 1 8   ? 13.629  -27.197 3.578   1.00 32.74  ? 26  LEU B HD11 1 
ATOM   4816  H  HD12 . LEU B 1 8   ? 13.829  -26.384 2.228   1.00 32.74  ? 26  LEU B HD12 1 
ATOM   4817  H  HD13 . LEU B 1 8   ? 15.081  -26.715 3.149   1.00 32.74  ? 26  LEU B HD13 1 
ATOM   4818  H  HD21 . LEU B 1 8   ? 14.103  -26.031 5.756   1.00 31.06  ? 26  LEU B HD21 1 
ATOM   4819  H  HD22 . LEU B 1 8   ? 15.468  -25.413 5.227   1.00 31.06  ? 26  LEU B HD22 1 
ATOM   4820  H  HD23 . LEU B 1 8   ? 14.320  -24.458 5.769   1.00 31.06  ? 26  LEU B HD23 1 
ATOM   4821  N  N    . PRO B 1 9   ? 16.307  -21.444 3.441   1.00 22.15  ? 27  PRO B N    1 
ATOM   4822  C  CA   . PRO B 1 9   ? 17.374  -20.699 2.758   1.00 22.60  ? 27  PRO B CA   1 
ATOM   4823  C  C    . PRO B 1 9   ? 17.678  -21.301 1.393   1.00 23.93  ? 27  PRO B C    1 
ATOM   4824  O  O    . PRO B 1 9   ? 17.649  -22.520 1.211   1.00 22.89  ? 27  PRO B O    1 
ATOM   4825  C  CB   . PRO B 1 9   ? 18.567  -20.847 3.706   1.00 20.63  ? 27  PRO B CB   1 
ATOM   4826  C  CG   . PRO B 1 9   ? 17.940  -21.031 5.056   1.00 20.30  ? 27  PRO B CG   1 
ATOM   4827  C  CD   . PRO B 1 9   ? 16.696  -21.834 4.811   1.00 21.34  ? 27  PRO B CD   1 
ATOM   4828  H  HA   . PRO B 1 9   ? 17.135  -19.764 2.663   1.00 27.11  ? 27  PRO B HA   1 
ATOM   4829  H  HB2  . PRO B 1 9   ? 19.097  -21.620 3.458   1.00 24.75  ? 27  PRO B HB2  1 
ATOM   4830  H  HB3  . PRO B 1 9   ? 19.115  -20.047 3.681   1.00 24.75  ? 27  PRO B HB3  1 
ATOM   4831  H  HG2  . PRO B 1 9   ? 18.550  -21.509 5.640   1.00 24.36  ? 27  PRO B HG2  1 
ATOM   4832  H  HG3  . PRO B 1 9   ? 17.723  -20.167 5.439   1.00 24.36  ? 27  PRO B HG3  1 
ATOM   4833  H  HD2  . PRO B 1 9   ? 16.883  -22.785 4.860   1.00 25.61  ? 27  PRO B HD2  1 
ATOM   4834  H  HD3  . PRO B 1 9   ? 16.003  -21.600 5.448   1.00 25.61  ? 27  PRO B HD3  1 
ATOM   4835  N  N    . SER B 1 10  ? 17.983  -20.433 0.430   1.00 26.94  ? 28  SER B N    1 
ATOM   4836  C  CA   . SER B 1 10  ? 18.318  -20.839 -0.927  1.00 28.06  ? 28  SER B CA   1 
ATOM   4837  C  C    . SER B 1 10  ? 19.602  -20.138 -1.358  1.00 27.69  ? 28  SER B C    1 
ATOM   4838  O  O    . SER B 1 10  ? 20.212  -19.376 -0.602  1.00 27.79  ? 28  SER B O    1 
ATOM   4839  C  CB   . SER B 1 10  ? 17.174  -20.510 -1.895  1.00 31.67  ? 28  SER B CB   1 
ATOM   4840  O  OG   . SER B 1 10  ? 16.953  -19.110 -1.950  1.00 35.05  ? 28  SER B OG   1 
ATOM   4841  H  H    . SER B 1 10  ? 18.002  -19.581 0.546   1.00 32.33  ? 28  SER B H    1 
ATOM   4842  H  HA   . SER B 1 10  ? 18.472  -21.796 -0.941  1.00 33.68  ? 28  SER B HA   1 
ATOM   4843  H  HB2  . SER B 1 10  ? 17.408  -20.828 -2.781  1.00 38.01  ? 28  SER B HB2  1 
ATOM   4844  H  HB3  . SER B 1 10  ? 16.364  -20.947 -1.589  1.00 38.01  ? 28  SER B HB3  1 
ATOM   4845  H  HG   . SER B 1 10  ? 16.798  -18.814 -1.180  1.00 42.06  ? 28  SER B HG   1 
ATOM   4846  N  N    . GLY B 1 11  ? 20.017  -20.405 -2.584  1.00 28.06  ? 29  GLY B N    1 
ATOM   4847  C  CA   . GLY B 1 11  ? 21.210  -19.782 -3.105  1.00 27.33  ? 29  GLY B CA   1 
ATOM   4848  C  C    . GLY B 1 11  ? 22.483  -20.500 -2.689  1.00 25.55  ? 29  GLY B C    1 
ATOM   4849  O  O    . GLY B 1 11  ? 22.496  -21.683 -2.328  1.00 25.04  ? 29  GLY B O    1 
ATOM   4850  H  H    . GLY B 1 11  ? 19.624  -20.941 -3.130  1.00 33.68  ? 29  GLY B H    1 
ATOM   4851  H  HA2  . GLY B 1 11  ? 21.169  -19.775 -4.074  1.00 32.80  ? 29  GLY B HA2  1 
ATOM   4852  H  HA3  . GLY B 1 11  ? 21.259  -18.868 -2.783  1.00 32.80  ? 29  GLY B HA3  1 
ATOM   4853  N  N    . SER B 1 12  ? 23.576  -19.746 -2.732  1.00 24.54  ? 30  SER B N    1 
ATOM   4854  C  CA   . SER B 1 12  ? 24.896  -20.324 -2.541  1.00 24.02  ? 30  SER B CA   1 
ATOM   4855  C  C    . SER B 1 12  ? 25.114  -20.743 -1.091  1.00 21.05  ? 30  SER B C    1 
ATOM   4856  O  O    . SER B 1 12  ? 24.545  -20.170 -0.159  1.00 21.27  ? 30  SER B O    1 
ATOM   4857  C  CB   . SER B 1 12  ? 25.962  -19.303 -2.932  1.00 26.88  ? 30  SER B CB   1 
ATOM   4858  O  OG   . SER B 1 12  ? 25.791  -18.899 -4.276  1.00 30.40  ? 30  SER B OG   1 
ATOM   4859  H  H    . SER B 1 12  ? 23.578  -18.897 -2.872  1.00 29.45  ? 30  SER B H    1 
ATOM   4860  H  HA   . SER B 1 12  ? 24.983  -21.113 -3.097  1.00 28.82  ? 30  SER B HA   1 
ATOM   4861  H  HB2  . SER B 1 12  ? 25.884  -18.526 -2.356  1.00 32.25  ? 30  SER B HB2  1 
ATOM   4862  H  HB3  . SER B 1 12  ? 26.839  -19.705 -2.831  1.00 32.25  ? 30  SER B HB3  1 
ATOM   4863  H  HG   . SER B 1 12  ? 26.357  -18.311 -4.474  1.00 36.48  ? 30  SER B HG   1 
ATOM   4864  N  N    . ASP B 1 13  ? 25.954  -21.757 -0.909  1.00 19.06  ? 31  ASP B N    1 
ATOM   4865  C  CA   . ASP B 1 13  ? 26.303  -22.185 0.436   1.00 17.93  ? 31  ASP B CA   1 
ATOM   4866  C  C    . ASP B 1 13  ? 27.094  -21.082 1.134   1.00 18.44  ? 31  ASP B C    1 
ATOM   4867  O  O    . ASP B 1 13  ? 27.924  -20.421 0.500   1.00 19.58  ? 31  ASP B O    1 
ATOM   4868  C  CB   . ASP B 1 13  ? 27.211  -23.409 0.388   1.00 17.29  ? 31  ASP B CB   1 
ATOM   4869  C  CG   . ASP B 1 13  ? 26.478  -24.692 0.097   1.00 18.03  ? 31  ASP B CG   1 
ATOM   4870  O  OD1  . ASP B 1 13  ? 25.277  -24.657 -0.237  1.00 17.95  ? 31  ASP B OD1  1 
ATOM   4871  O  OD2  . ASP B 1 13  ? 27.130  -25.747 0.217   1.00 18.18  ? 31  ASP B OD2  1 
ATOM   4872  H  H    . ASP B 1 13  ? 26.331  -22.205 -1.539  1.00 22.88  ? 31  ASP B H    1 
ATOM   4873  H  HA   . ASP B 1 13  ? 25.487  -22.390 0.920   1.00 21.52  ? 31  ASP B HA   1 
ATOM   4874  H  HB2  . ASP B 1 13  ? 27.873  -23.281 -0.310  1.00 20.75  ? 31  ASP B HB2  1 
ATOM   4875  H  HB3  . ASP B 1 13  ? 27.650  -23.507 1.248   1.00 20.75  ? 31  ASP B HB3  1 
ATOM   4876  N  N    . PRO B 1 14  ? 26.891  -20.888 2.438   1.00 17.73  ? 32  PRO B N    1 
ATOM   4877  C  CA   . PRO B 1 14  ? 27.797  -20.014 3.194   1.00 18.22  ? 32  PRO B CA   1 
ATOM   4878  C  C    . PRO B 1 14  ? 29.230  -20.515 3.116   1.00 18.73  ? 32  PRO B C    1 
ATOM   4879  O  O    . PRO B 1 14  ? 29.491  -21.706 2.919   1.00 18.64  ? 32  PRO B O    1 
ATOM   4880  C  CB   . PRO B 1 14  ? 27.263  -20.100 4.630   1.00 19.34  ? 32  PRO B CB   1 
ATOM   4881  C  CG   . PRO B 1 14  ? 25.853  -20.600 4.497   1.00 18.71  ? 32  PRO B CG   1 
ATOM   4882  C  CD   . PRO B 1 14  ? 25.852  -21.490 3.296   1.00 18.06  ? 32  PRO B CD   1 
ATOM   4883  H  HA   . PRO B 1 14  ? 27.742  -19.099 2.875   1.00 21.87  ? 32  PRO B HA   1 
ATOM   4884  H  HB2  . PRO B 1 14  ? 27.803  -20.719 5.145   1.00 23.20  ? 32  PRO B HB2  1 
ATOM   4885  H  HB3  . PRO B 1 14  ? 27.282  -19.222 5.041   1.00 23.20  ? 32  PRO B HB3  1 
ATOM   4886  H  HG2  . PRO B 1 14  ? 25.604  -21.095 5.293   1.00 22.46  ? 32  PRO B HG2  1 
ATOM   4887  H  HG3  . PRO B 1 14  ? 25.250  -19.851 4.371   1.00 22.46  ? 32  PRO B HG3  1 
ATOM   4888  H  HD2  . PRO B 1 14  ? 26.086  -22.399 3.538   1.00 21.67  ? 32  PRO B HD2  1 
ATOM   4889  H  HD3  . PRO B 1 14  ? 24.988  -21.476 2.855   1.00 21.67  ? 32  PRO B HD3  1 
ATOM   4890  N  N    . ALA B 1 15  ? 30.166  -19.587 3.285   1.00 20.26  ? 33  ALA B N    1 
ATOM   4891  C  CA   . ALA B 1 15  ? 31.570  -19.951 3.338   1.00 21.96  ? 33  ALA B CA   1 
ATOM   4892  C  C    . ALA B 1 15  ? 31.863  -20.709 4.627   1.00 20.72  ? 33  ALA B C    1 
ATOM   4893  O  O    . ALA B 1 15  ? 31.228  -20.492 5.664   1.00 21.26  ? 33  ALA B O    1 
ATOM   4894  C  CB   . ALA B 1 15  ? 32.442  -18.698 3.267   1.00 23.97  ? 33  ALA B CB   1 
ATOM   4895  H  H    . ALA B 1 15  ? 30.011  -18.745 3.372   1.00 24.32  ? 33  ALA B H    1 
ATOM   4896  H  HA   . ALA B 1 15  ? 31.794  -20.519 2.584   1.00 26.36  ? 33  ALA B HA   1 
ATOM   4897  H  HB1  . ALA B 1 15  ? 33.375  -18.963 3.248   1.00 28.76  ? 33  ALA B HB1  1 
ATOM   4898  H  HB2  . ALA B 1 15  ? 32.222  -18.205 2.461   1.00 28.76  ? 33  ALA B HB2  1 
ATOM   4899  H  HB3  . ALA B 1 15  ? 32.270  -18.149 4.048   1.00 28.76  ? 33  ALA B HB3  1 
ATOM   4900  N  N    . PHE B 1 16  ? 32.811  -21.634 4.539   1.00 19.20  ? 34  PHE B N    1 
ATOM   4901  C  CA   . PHE B 1 16  ? 33.320  -22.314 5.716   1.00 19.47  ? 34  PHE B CA   1 
ATOM   4902  C  C    . PHE B 1 16  ? 34.294  -21.406 6.461   1.00 19.32  ? 34  PHE B C    1 
ATOM   4903  O  O    . PHE B 1 16  ? 35.018  -20.605 5.856   1.00 21.35  ? 34  PHE B O    1 
ATOM   4904  C  CB   . PHE B 1 16  ? 34.063  -23.585 5.308   1.00 20.18  ? 34  PHE B CB   1 
ATOM   4905  C  CG   . PHE B 1 16  ? 33.176  -24.691 4.778   1.00 19.48  ? 34  PHE B CG   1 
ATOM   4906  C  CD1  . PHE B 1 16  ? 31.896  -24.900 5.272   1.00 19.79  ? 34  PHE B CD1  1 
ATOM   4907  C  CD2  . PHE B 1 16  ? 33.650  -25.541 3.797   1.00 21.04  ? 34  PHE B CD2  1 
ATOM   4908  C  CE1  . PHE B 1 16  ? 31.107  -25.932 4.780   1.00 20.87  ? 34  PHE B CE1  1 
ATOM   4909  C  CE2  . PHE B 1 16  ? 32.867  -26.563 3.301   1.00 21.38  ? 34  PHE B CE2  1 
ATOM   4910  C  CZ   . PHE B 1 16  ? 31.595  -26.764 3.801   1.00 20.38  ? 34  PHE B CZ   1 
ATOM   4911  H  H    . PHE B 1 16  ? 33.176  -21.887 3.803   1.00 23.04  ? 34  PHE B H    1 
ATOM   4912  H  HA   . PHE B 1 16  ? 32.582  -22.549 6.301   1.00 23.36  ? 34  PHE B HA   1 
ATOM   4913  H  HB2  . PHE B 1 16  ? 34.699  -23.361 4.610   1.00 24.22  ? 34  PHE B HB2  1 
ATOM   4914  H  HB3  . PHE B 1 16  ? 34.532  -23.932 6.083   1.00 24.22  ? 34  PHE B HB3  1 
ATOM   4915  H  HD1  . PHE B 1 16  ? 31.563  -24.344 5.938   1.00 23.75  ? 34  PHE B HD1  1 
ATOM   4916  H  HD2  . PHE B 1 16  ? 34.511  -25.423 3.466   1.00 25.24  ? 34  PHE B HD2  1 
ATOM   4917  H  HE1  . PHE B 1 16  ? 30.248  -26.060 5.113   1.00 25.05  ? 34  PHE B HE1  1 
ATOM   4918  H  HE2  . PHE B 1 16  ? 33.195  -27.116 2.630   1.00 25.65  ? 34  PHE B HE2  1 
ATOM   4919  H  HZ   . PHE B 1 16  ? 31.072  -27.461 3.477   1.00 24.45  ? 34  PHE B HZ   1 
ATOM   4920  N  N    . SER B 1 17  ? 34.293  -21.528 7.794   1.00 19.38  ? 35  SER B N    1 
ATOM   4921  C  CA   . SER B 1 17  ? 35.275  -20.843 8.628   1.00 19.64  ? 35  SER B CA   1 
ATOM   4922  C  C    . SER B 1 17  ? 36.578  -21.620 8.774   1.00 19.96  ? 35  SER B C    1 
ATOM   4923  O  O    . SER B 1 17  ? 37.594  -21.028 9.159   1.00 21.05  ? 35  SER B O    1 
ATOM   4924  C  CB   . SER B 1 17  ? 34.701  -20.570 10.022  1.00 21.07  ? 35  SER B CB   1 
ATOM   4925  O  OG   . SER B 1 17  ? 34.529  -21.762 10.779  1.00 21.97  ? 35  SER B OG   1 
ATOM   4926  H  H    . SER B 1 17  ? 33.730  -22.003 8.238   1.00 23.26  ? 35  SER B H    1 
ATOM   4927  H  HA   . SER B 1 17  ? 35.476  -19.990 8.211   1.00 23.56  ? 35  SER B HA   1 
ATOM   4928  H  HB2  . SER B 1 17  ? 35.311  -19.985 10.500  1.00 25.29  ? 35  SER B HB2  1 
ATOM   4929  H  HB3  . SER B 1 17  ? 33.838  -20.138 9.923   1.00 25.29  ? 35  SER B HB3  1 
ATOM   4930  H  HG   . SER B 1 17  ? 33.961  -22.258 10.408  1.00 26.37  ? 35  SER B HG   1 
ATOM   4931  N  N    . GLN B 1 18  ? 36.570  -22.921 8.492   1.00 20.43  ? 36  GLN B N    1 
ATOM   4932  C  CA   . GLN B 1 18  ? 37.759  -23.752 8.572   1.00 22.33  ? 36  GLN B CA   1 
ATOM   4933  C  C    . GLN B 1 18  ? 38.240  -24.117 7.171   1.00 23.87  ? 36  GLN B C    1 
ATOM   4934  O  O    . GLN B 1 18  ? 37.428  -24.283 6.256   1.00 24.36  ? 36  GLN B O    1 
ATOM   4935  C  CB   . GLN B 1 18  ? 37.437  -25.055 9.314   1.00 25.39  ? 36  GLN B CB   1 
ATOM   4936  C  CG   . GLN B 1 18  ? 37.122  -24.888 10.788  1.00 29.36  ? 36  GLN B CG   1 
ATOM   4937  C  CD   . GLN B 1 18  ? 38.367  -24.656 11.631  1.00 33.27  ? 36  GLN B CD   1 
ATOM   4938  O  OE1  . GLN B 1 18  ? 39.447  -24.379 11.108  1.00 35.38  ? 36  GLN B OE1  1 
ATOM   4939  N  NE2  . GLN B 1 18  ? 38.218  -24.769 12.942  1.00 34.41  ? 36  GLN B NE2  1 
ATOM   4940  H  H    . GLN B 1 18  ? 35.868  -23.353 8.246   1.00 24.51  ? 36  GLN B H    1 
ATOM   4941  H  HA   . GLN B 1 18  ? 38.465  -23.278 9.038   1.00 26.80  ? 36  GLN B HA   1 
ATOM   4942  H  HB2  . GLN B 1 18  ? 36.664  -25.465 8.896   1.00 30.47  ? 36  GLN B HB2  1 
ATOM   4943  H  HB3  . GLN B 1 18  ? 38.204  -25.645 9.246   1.00 30.47  ? 36  GLN B HB3  1 
ATOM   4944  H  HG2  . GLN B 1 18  ? 36.536  -24.123 10.902  1.00 35.23  ? 36  GLN B HG2  1 
ATOM   4945  H  HG3  . GLN B 1 18  ? 36.685  -25.691 11.112  1.00 35.23  ? 36  GLN B HG3  1 
ATOM   4946  H  HE21 . GLN B 1 18  ? 37.448  -24.964 13.272  1.00 41.29  ? 36  GLN B HE21 1 
ATOM   4947  H  HE22 . GLN B 1 18  ? 38.891  -24.647 13.463  1.00 41.29  ? 36  GLN B HE22 1 
ATOM   4948  N  N    . PRO B 1 19  ? 39.548  -24.273 6.977   1.00 26.01  ? 37  PRO B N    1 
ATOM   4949  C  CA   . PRO B 1 19  ? 40.054  -24.682 5.661   1.00 26.53  ? 37  PRO B CA   1 
ATOM   4950  C  C    . PRO B 1 19  ? 39.640  -26.102 5.313   1.00 26.60  ? 37  PRO B C    1 
ATOM   4951  O  O    . PRO B 1 19  ? 39.376  -26.937 6.183   1.00 24.58  ? 37  PRO B O    1 
ATOM   4952  C  CB   . PRO B 1 19  ? 41.579  -24.585 5.809   1.00 27.64  ? 37  PRO B CB   1 
ATOM   4953  C  CG   . PRO B 1 19  ? 41.811  -23.774 7.018   1.00 27.45  ? 37  PRO B CG   1 
ATOM   4954  C  CD   . PRO B 1 19  ? 40.640  -23.997 7.923   1.00 27.11  ? 37  PRO B CD   1 
ATOM   4955  H  HA   . PRO B 1 19  ? 39.746  -24.068 4.976   1.00 31.83  ? 37  PRO B HA   1 
ATOM   4956  H  HB2  . PRO B 1 19  ? 41.955  -25.474 5.913   1.00 33.17  ? 37  PRO B HB2  1 
ATOM   4957  H  HB3  . PRO B 1 19  ? 41.958  -24.154 5.027   1.00 33.17  ? 37  PRO B HB3  1 
ATOM   4958  H  HG2  . PRO B 1 19  ? 42.632  -24.062 7.447   1.00 32.94  ? 37  PRO B HG2  1 
ATOM   4959  H  HG3  . PRO B 1 19  ? 41.876  -22.839 6.771   1.00 32.94  ? 37  PRO B HG3  1 
ATOM   4960  H  HD2  . PRO B 1 19  ? 40.792  -24.755 8.508   1.00 32.53  ? 37  PRO B HD2  1 
ATOM   4961  H  HD3  . PRO B 1 19  ? 40.452  -23.204 8.449   1.00 32.53  ? 37  PRO B HD3  1 
ATOM   4962  N  N    A LYS B 1 20  ? 39.587  -26.372 4.007   0.58 28.40  ? 38  LYS B N    1 
ATOM   4963  N  N    B LYS B 1 20  ? 39.600  -26.368 4.005   0.42 27.93  ? 38  LYS B N    1 
ATOM   4964  C  CA   A LYS B 1 20  ? 39.191  -27.698 3.546   0.58 29.71  ? 38  LYS B CA   1 
ATOM   4965  C  CA   B LYS B 1 20  ? 39.201  -27.688 3.528   0.42 28.85  ? 38  LYS B CA   1 
ATOM   4966  C  C    A LYS B 1 20  ? 40.074  -28.783 4.151   0.58 28.60  ? 38  LYS B C    1 
ATOM   4967  C  C    B LYS B 1 20  ? 40.074  -28.783 4.131   0.42 28.34  ? 38  LYS B C    1 
ATOM   4968  O  O    A LYS B 1 20  ? 39.581  -29.848 4.544   0.58 27.80  ? 38  LYS B O    1 
ATOM   4969  O  O    B LYS B 1 20  ? 39.575  -29.850 4.509   0.42 27.79  ? 38  LYS B O    1 
ATOM   4970  C  CB   A LYS B 1 20  ? 39.251  -27.767 2.020   0.58 31.84  ? 38  LYS B CB   1 
ATOM   4971  C  CB   B LYS B 1 20  ? 39.276  -27.736 2.000   0.42 29.93  ? 38  LYS B CB   1 
ATOM   4972  C  CG   A LYS B 1 20  ? 38.669  -29.051 1.447   0.58 32.89  ? 38  LYS B CG   1 
ATOM   4973  C  CG   B LYS B 1 20  ? 38.557  -26.595 1.285   0.42 30.16  ? 38  LYS B CG   1 
ATOM   4974  C  CD   A LYS B 1 20  ? 39.204  -29.349 0.053   0.58 33.97  ? 38  LYS B CD   1 
ATOM   4975  C  CD   B LYS B 1 20  ? 37.048  -26.787 1.282   0.42 30.16  ? 38  LYS B CD   1 
ATOM   4976  C  CE   A LYS B 1 20  ? 38.693  -30.689 -0.461  0.58 34.00  ? 38  LYS B CE   1 
ATOM   4977  C  CE   B LYS B 1 20  ? 36.371  -25.726 0.439   0.42 29.75  ? 38  LYS B CE   1 
ATOM   4978  N  NZ   A LYS B 1 20  ? 37.350  -31.040 0.101   0.58 33.32  ? 38  LYS B NZ   1 
ATOM   4979  N  NZ   B LYS B 1 20  ? 34.948  -26.053 0.175   0.42 29.55  ? 38  LYS B NZ   1 
ATOM   4980  H  H    A LYS B 1 20  ? 39.773  -25.814 3.379   0.58 34.08  ? 38  LYS B H    1 
ATOM   4981  H  H    B LYS B 1 20  ? 39.797  -25.809 3.382   0.42 33.51  ? 38  LYS B H    1 
ATOM   4982  H  HA   A LYS B 1 20  ? 38.276  -27.859 3.824   0.58 35.65  ? 38  LYS B HA   1 
ATOM   4983  H  HA   B LYS B 1 20  ? 38.283  -27.851 3.796   0.42 34.62  ? 38  LYS B HA   1 
ATOM   4984  H  HB2  A LYS B 1 20  ? 38.747  -27.023 1.654   0.58 38.21  ? 38  LYS B HB2  1 
ATOM   4985  H  HB2  B LYS B 1 20  ? 40.209  -27.701 1.737   0.42 35.92  ? 38  LYS B HB2  1 
ATOM   4986  H  HB3  A LYS B 1 20  ? 40.178  -27.709 1.740   0.58 38.21  ? 38  LYS B HB3  1 
ATOM   4987  H  HB3  B LYS B 1 20  ? 38.876  -28.566 1.698   0.42 35.92  ? 38  LYS B HB3  1 
ATOM   4988  H  HG2  A LYS B 1 20  ? 38.904  -29.794 2.026   0.58 39.47  ? 38  LYS B HG2  1 
ATOM   4989  H  HG2  B LYS B 1 20  ? 38.755  -25.760 1.736   0.42 36.19  ? 38  LYS B HG2  1 
ATOM   4990  H  HG3  A LYS B 1 20  ? 37.704  -28.967 1.390   0.58 39.47  ? 38  LYS B HG3  1 
ATOM   4991  H  HG3  B LYS B 1 20  ? 38.858  -26.555 0.364   0.42 36.19  ? 38  LYS B HG3  1 
ATOM   4992  H  HD2  A LYS B 1 20  ? 38.912  -28.655 -0.559  0.58 40.77  ? 38  LYS B HD2  1 
ATOM   4993  H  HD2  B LYS B 1 20  ? 36.833  -27.658 0.913   0.42 36.19  ? 38  LYS B HD2  1 
ATOM   4994  H  HD3  A LYS B 1 20  ? 40.173  -29.381 0.080   0.58 40.77  ? 38  LYS B HD3  1 
ATOM   4995  H  HD3  B LYS B 1 20  ? 36.712  -26.720 2.190   0.42 36.19  ? 38  LYS B HD3  1 
ATOM   4996  H  HE2  A LYS B 1 20  ? 38.614  -30.651 -1.427  0.58 40.80  ? 38  LYS B HE2  1 
ATOM   4997  H  HE2  B LYS B 1 20  ? 36.406  -24.877 0.906   0.42 35.70  ? 38  LYS B HE2  1 
ATOM   4998  H  HE3  A LYS B 1 20  ? 39.317  -31.386 -0.206  0.58 40.80  ? 38  LYS B HE3  1 
ATOM   4999  H  HE3  B LYS B 1 20  ? 36.829  -25.655 -0.413  0.42 35.70  ? 38  LYS B HE3  1 
ATOM   5000  H  HZ1  A LYS B 1 20  ? 36.789  -30.358 -0.005  0.58 39.99  ? 38  LYS B HZ1  1 
ATOM   5001  H  HZ1  B LYS B 1 20  ? 34.499  -26.102 0.942   0.42 35.46  ? 38  LYS B HZ1  1 
ATOM   5002  H  HZ2  A LYS B 1 20  ? 37.022  -31.753 -0.319  0.58 39.99  ? 38  LYS B HZ2  1 
ATOM   5003  H  HZ2  B LYS B 1 20  ? 34.580  -25.423 -0.334  0.42 35.46  ? 38  LYS B HZ2  1 
ATOM   5004  H  HZ3  A LYS B 1 20  ? 37.422  -31.223 0.969   0.58 39.99  ? 38  LYS B HZ3  1 
ATOM   5005  H  HZ3  B LYS B 1 20  ? 34.888  -26.836 -0.245  0.42 35.46  ? 38  LYS B HZ3  1 
ATOM   5006  N  N    . SER B 1 21  ? 41.384  -28.537 4.224   1.00 28.97  ? 39  SER B N    1 
ATOM   5007  C  CA   . SER B 1 21  ? 42.293  -29.542 4.770   1.00 28.40  ? 39  SER B CA   1 
ATOM   5008  C  C    . SER B 1 21  ? 41.924  -29.907 6.204   1.00 25.22  ? 39  SER B C    1 
ATOM   5009  O  O    . SER B 1 21  ? 42.012  -31.076 6.601   1.00 25.92  ? 39  SER B O    1 
ATOM   5010  C  CB   . SER B 1 21  ? 43.732  -29.030 4.698   1.00 31.07  ? 39  SER B CB   1 
ATOM   5011  O  OG   . SER B 1 21  ? 43.853  -27.759 5.310   1.00 34.48  ? 39  SER B OG   1 
ATOM   5012  H  H    . SER B 1 21  ? 41.761  -27.808 3.968   1.00 34.76  ? 39  SER B H    1 
ATOM   5013  H  HA   . SER B 1 21  ? 42.228  -30.348 4.234   1.00 34.08  ? 39  SER B HA   1 
ATOM   5014  H  HB2  . SER B 1 21  ? 44.312  -29.656 5.157   1.00 37.28  ? 39  SER B HB2  1 
ATOM   5015  H  HB3  . SER B 1 21  ? 43.993  -28.956 3.767   1.00 37.28  ? 39  SER B HB3  1 
ATOM   5016  H  HG   . SER B 1 21  ? 43.641  -27.156 4.765   1.00 41.38  ? 39  SER B HG   1 
ATOM   5017  N  N    . VAL B 1 22  ? 41.499  -28.922 6.991   1.00 23.63  ? 40  VAL B N    1 
ATOM   5018  C  CA   . VAL B 1 22  ? 41.078  -29.191 8.361   1.00 21.66  ? 40  VAL B CA   1 
ATOM   5019  C  C    . VAL B 1 22  ? 39.804  -30.027 8.371   1.00 18.76  ? 40  VAL B C    1 
ATOM   5020  O  O    . VAL B 1 22  ? 39.688  -31.009 9.114   1.00 19.40  ? 40  VAL B O    1 
ATOM   5021  C  CB   . VAL B 1 22  ? 40.902  -27.860 9.114   1.00 22.46  ? 40  VAL B CB   1 
ATOM   5022  C  CG1  . VAL B 1 22  ? 40.216  -28.069 10.455  1.00 22.80  ? 40  VAL B CG1  1 
ATOM   5023  C  CG2  . VAL B 1 22  ? 42.252  -27.186 9.299   1.00 25.27  ? 40  VAL B CG2  1 
ATOM   5024  H  H    . VAL B 1 22  ? 41.444  -28.096 6.758   1.00 28.36  ? 40  VAL B H    1 
ATOM   5025  H  HA   . VAL B 1 22  ? 41.764  -29.706 8.813   1.00 25.99  ? 40  VAL B HA   1 
ATOM   5026  H  HB   . VAL B 1 22  ? 40.332  -27.277 8.588   1.00 26.95  ? 40  VAL B HB   1 
ATOM   5027  H  HG11 . VAL B 1 22  ? 40.317  -27.266 10.990  1.00 27.36  ? 40  VAL B HG11 1 
ATOM   5028  H  HG12 . VAL B 1 22  ? 39.276  -28.250 10.303  1.00 27.36  ? 40  VAL B HG12 1 
ATOM   5029  H  HG13 . VAL B 1 22  ? 40.629  -28.821 10.906  1.00 27.36  ? 40  VAL B HG13 1 
ATOM   5030  H  HG21 . VAL B 1 22  ? 42.934  -27.718 8.859   1.00 30.32  ? 40  VAL B HG21 1 
ATOM   5031  H  HG22 . VAL B 1 22  ? 42.220  -26.300 8.904   1.00 30.32  ? 40  VAL B HG22 1 
ATOM   5032  H  HG23 . VAL B 1 22  ? 42.445  -27.119 10.247  1.00 30.32  ? 40  VAL B HG23 1 
ATOM   5033  N  N    . LEU B 1 23  ? 38.830  -29.653 7.542   1.00 18.40  ? 41  LEU B N    1 
ATOM   5034  C  CA   . LEU B 1 23  ? 37.576  -30.397 7.497   1.00 17.90  ? 41  LEU B CA   1 
ATOM   5035  C  C    . LEU B 1 23  ? 37.798  -31.821 6.999   1.00 18.37  ? 41  LEU B C    1 
ATOM   5036  O  O    . LEU B 1 23  ? 37.220  -32.769 7.543   1.00 18.37  ? 41  LEU B O    1 
ATOM   5037  C  CB   . LEU B 1 23  ? 36.566  -29.649 6.627   1.00 17.28  ? 41  LEU B CB   1 
ATOM   5038  C  CG   . LEU B 1 23  ? 36.231  -28.238 7.129   1.00 17.83  ? 41  LEU B CG   1 
ATOM   5039  C  CD1  . LEU B 1 23  ? 35.317  -27.504 6.170   1.00 19.17  ? 41  LEU B CD1  1 
ATOM   5040  C  CD2  . LEU B 1 23  ? 35.602  -28.300 8.520   1.00 17.99  ? 41  LEU B CD2  1 
ATOM   5041  H  H    . LEU B 1 23  ? 38.870  -28.982 7.004   1.00 22.08  ? 41  LEU B H    1 
ATOM   5042  H  HA   . LEU B 1 23  ? 37.205  -30.459 8.391   1.00 21.48  ? 41  LEU B HA   1 
ATOM   5043  H  HB2  . LEU B 1 23  ? 36.930  -29.565 5.732   1.00 20.73  ? 41  LEU B HB2  1 
ATOM   5044  H  HB3  . LEU B 1 23  ? 35.741  -30.157 6.604   1.00 20.73  ? 41  LEU B HB3  1 
ATOM   5045  H  HG   . LEU B 1 23  ? 37.058  -27.734 7.183   1.00 21.40  ? 41  LEU B HG   1 
ATOM   5046  H  HD11 . LEU B 1 23  ? 34.460  -27.958 6.140   1.00 23.00  ? 41  LEU B HD11 1 
ATOM   5047  H  HD12 . LEU B 1 23  ? 35.198  -26.593 6.481   1.00 23.00  ? 41  LEU B HD12 1 
ATOM   5048  H  HD13 . LEU B 1 23  ? 35.720  -27.501 5.287   1.00 23.00  ? 41  LEU B HD13 1 
ATOM   5049  H  HD21 . LEU B 1 23  ? 34.881  -28.949 8.512   1.00 21.58  ? 41  LEU B HD21 1 
ATOM   5050  H  HD22 . LEU B 1 23  ? 36.280  -28.566 9.162   1.00 21.58  ? 41  LEU B HD22 1 
ATOM   5051  H  HD23 . LEU B 1 23  ? 35.256  -27.424 8.750   1.00 21.58  ? 41  LEU B HD23 1 
ATOM   5052  N  N    . ASP B 1 24  ? 38.649  -31.996 5.981   1.00 19.74  ? 42  ASP B N    1 
ATOM   5053  C  CA   . ASP B 1 24  ? 38.934  -33.338 5.475   1.00 20.91  ? 42  ASP B CA   1 
ATOM   5054  C  C    . ASP B 1 24  ? 39.576  -34.210 6.550   1.00 20.39  ? 42  ASP B C    1 
ATOM   5055  O  O    . ASP B 1 24  ? 39.301  -35.414 6.630   1.00 20.86  ? 42  ASP B O    1 
ATOM   5056  C  CB   . ASP B 1 24  ? 39.874  -33.256 4.274   1.00 21.73  ? 42  ASP B CB   1 
ATOM   5057  C  CG   . ASP B 1 24  ? 39.183  -32.800 3.007   1.00 24.46  ? 42  ASP B CG   1 
ATOM   5058  O  OD1  . ASP B 1 24  ? 37.940  -32.924 2.895   1.00 25.11  ? 42  ASP B OD1  1 
ATOM   5059  O  OD2  . ASP B 1 24  ? 39.903  -32.323 2.109   1.00 26.04  ? 42  ASP B OD2  1 
ATOM   5060  H  H    . ASP B 1 24  ? 39.066  -31.364 5.574   1.00 23.68  ? 42  ASP B H    1 
ATOM   5061  H  HA   . ASP B 1 24  ? 38.097  -33.742 5.197   1.00 25.10  ? 42  ASP B HA   1 
ATOM   5062  H  HB2  . ASP B 1 24  ? 40.583  -32.624 4.471   1.00 26.08  ? 42  ASP B HB2  1 
ATOM   5063  H  HB3  . ASP B 1 24  ? 40.251  -34.135 4.108   1.00 26.08  ? 42  ASP B HB3  1 
ATOM   5064  N  N    . ALA B 1 25  ? 40.436  -33.617 7.386   1.00 20.37  ? 43  ALA B N    1 
ATOM   5065  C  CA   . ALA B 1 25  ? 41.119  -34.381 8.423   1.00 21.08  ? 43  ALA B CA   1 
ATOM   5066  C  C    . ALA B 1 25  ? 40.150  -34.956 9.446   1.00 21.08  ? 43  ALA B C    1 
ATOM   5067  O  O    . ALA B 1 25  ? 40.484  -35.938 10.120  1.00 22.32  ? 43  ALA B O    1 
ATOM   5068  C  CB   . ALA B 1 25  ? 42.158  -33.502 9.129   1.00 22.75  ? 43  ALA B CB   1 
ATOM   5069  H  H    . ALA B 1 25  ? 40.636  -32.781 7.372   1.00 24.44  ? 43  ALA B H    1 
ATOM   5070  H  HA   . ALA B 1 25  ? 41.587  -35.121 8.005   1.00 25.29  ? 43  ALA B HA   1 
ATOM   5071  H  HB1  . ALA B 1 25  ? 41.709  -32.735 9.518   1.00 27.30  ? 43  ALA B HB1  1 
ATOM   5072  H  HB2  . ALA B 1 25  ? 42.590  -34.021 9.825   1.00 27.30  ? 43  ALA B HB2  1 
ATOM   5073  H  HB3  . ALA B 1 25  ? 42.815  -33.207 8.479   1.00 27.30  ? 43  ALA B HB3  1 
ATOM   5074  N  N    . GLY B 1 26  ? 38.957  -34.382 9.566   1.00 19.13  ? 44  GLY B N    1 
ATOM   5075  C  CA   . GLY B 1 26  ? 37.962  -34.884 10.487  1.00 19.08  ? 44  GLY B CA   1 
ATOM   5076  C  C    . GLY B 1 26  ? 37.120  -36.022 9.975   1.00 17.65  ? 44  GLY B C    1 
ATOM   5077  O  O    . GLY B 1 26  ? 36.279  -36.537 10.717  1.00 18.30  ? 44  GLY B O    1 
ATOM   5078  H  H    . GLY B 1 26  ? 38.703  -33.694 9.118   1.00 22.96  ? 44  GLY B H    1 
ATOM   5079  H  HA2  . GLY B 1 26  ? 38.413  -35.191 11.289  1.00 22.90  ? 44  GLY B HA2  1 
ATOM   5080  H  HA3  . GLY B 1 26  ? 37.363  -34.157 10.719  1.00 22.90  ? 44  GLY B HA3  1 
ATOM   5081  N  N    . LEU B 1 27  ? 37.319  -36.433 8.726   1.00 18.65  ? 45  LEU B N    1 
ATOM   5082  C  CA   . LEU B 1 27  ? 36.494  -37.442 8.069   1.00 17.83  ? 45  LEU B CA   1 
ATOM   5083  C  C    . LEU B 1 27  ? 37.312  -38.707 7.842   1.00 18.76  ? 45  LEU B C    1 
ATOM   5084  O  O    . LEU B 1 27  ? 38.425  -38.642 7.307   1.00 20.45  ? 45  LEU B O    1 
ATOM   5085  C  CB   . LEU B 1 27  ? 35.995  -36.911 6.724   1.00 19.24  ? 45  LEU B CB   1 
ATOM   5086  C  CG   . LEU B 1 27  ? 35.295  -37.902 5.787   1.00 19.85  ? 45  LEU B CG   1 
ATOM   5087  C  CD1  . LEU B 1 27  ? 34.032  -38.444 6.426   1.00 20.80  ? 45  LEU B CD1  1 
ATOM   5088  C  CD2  . LEU B 1 27  ? 34.993  -37.246 4.446   1.00 21.64  ? 45  LEU B CD2  1 
ATOM   5089  H  H    . LEU B 1 27  ? 37.947  -36.131 8.222   1.00 22.38  ? 45  LEU B H    1 
ATOM   5090  H  HA   . LEU B 1 27  ? 35.737  -37.664 8.634   1.00 21.40  ? 45  LEU B HA   1 
ATOM   5091  H  HB2  . LEU B 1 27  ? 35.362  -36.198 6.902   1.00 23.08  ? 45  LEU B HB2  1 
ATOM   5092  H  HB3  . LEU B 1 27  ? 36.761  -36.562 6.241   1.00 23.08  ? 45  LEU B HB3  1 
ATOM   5093  H  HG   . LEU B 1 27  ? 35.886  -38.654 5.624   1.00 23.81  ? 45  LEU B HG   1 
ATOM   5094  H  HD11 . LEU B 1 27  ? 33.560  -38.989 5.778   1.00 24.96  ? 45  LEU B HD11 1 
ATOM   5095  H  HD12 . LEU B 1 27  ? 34.273  -38.981 7.197   1.00 24.96  ? 45  LEU B HD12 1 
ATOM   5096  H  HD13 . LEU B 1 27  ? 33.474  -37.700 6.702   1.00 24.96  ? 45  LEU B HD13 1 
ATOM   5097  H  HD21 . LEU B 1 27  ? 34.477  -36.439 4.598   1.00 25.97  ? 45  LEU B HD21 1 
ATOM   5098  H  HD22 . LEU B 1 27  ? 35.829  -37.027 4.006   1.00 25.97  ? 45  LEU B HD22 1 
ATOM   5099  H  HD23 . LEU B 1 27  ? 34.484  -37.866 3.899   1.00 25.97  ? 45  LEU B HD23 1 
ATOM   5100  N  N    . THR B 1 28  ? 36.750  -39.853 8.230   1.00 19.17  ? 46  THR B N    1 
ATOM   5101  C  CA   . THR B 1 28  ? 37.379  -41.150 8.017   1.00 20.07  ? 46  THR B CA   1 
ATOM   5102  C  C    . THR B 1 28  ? 36.330  -42.161 7.574   1.00 19.80  ? 46  THR B C    1 
ATOM   5103  O  O    . THR B 1 28  ? 35.173  -42.101 7.994   1.00 20.23  ? 46  THR B O    1 
ATOM   5104  C  CB   . THR B 1 28  ? 38.035  -41.668 9.313   1.00 20.31  ? 46  THR B CB   1 
ATOM   5105  O  OG1  . THR B 1 28  ? 38.876  -40.647 9.877   1.00 22.01  ? 46  THR B OG1  1 
ATOM   5106  C  CG2  . THR B 1 28  ? 38.862  -42.935 9.053   1.00 21.01  ? 46  THR B CG2  1 
ATOM   5107  H  H    . THR B 1 28  ? 35.988  -39.903 8.626   1.00 23.01  ? 46  THR B H    1 
ATOM   5108  H  HA   . THR B 1 28  ? 38.050  -41.067 7.321   1.00 24.08  ? 46  THR B HA   1 
ATOM   5109  H  HB   . THR B 1 28  ? 37.339  -41.897 9.949   1.00 24.37  ? 46  THR B HB   1 
ATOM   5110  H  HG1  . THR B 1 28  ? 38.412  -39.982 10.097  1.00 26.41  ? 46  THR B HG1  1 
ATOM   5111  H  HG21 . THR B 1 28  ? 39.392  -43.152 9.836   1.00 25.21  ? 46  THR B HG21 1 
ATOM   5112  H  HG22 . THR B 1 28  ? 38.274  -43.680 8.855   1.00 25.21  ? 46  THR B HG22 1 
ATOM   5113  H  HG23 . THR B 1 28  ? 39.457  -42.794 8.300   1.00 25.21  ? 46  THR B HG23 1 
ATOM   5114  N  N    . CYS B 1 29  ? 36.740  -43.099 6.727   1.00 21.18  ? 47  CYS B N    1 
ATOM   5115  C  CA   . CYS B 1 29  ? 35.895  -44.221 6.355   1.00 22.08  ? 47  CYS B CA   1 
ATOM   5116  C  C    . CYS B 1 29  ? 36.605  -45.520 6.721   1.00 23.50  ? 47  CYS B C    1 
ATOM   5117  O  O    . CYS B 1 29  ? 37.837  -45.603 6.698   1.00 24.35  ? 47  CYS B O    1 
ATOM   5118  C  CB   . CYS B 1 29  ? 35.589  -44.251 4.853   1.00 23.22  ? 47  CYS B CB   1 
ATOM   5119  S  SG   . CYS B 1 29  ? 34.613  -42.916 4.211   1.00 22.89  ? 47  CYS B SG   1 
ATOM   5120  H  H    . CYS B 1 29  ? 37.514  -43.104 6.351   1.00 25.42  ? 47  CYS B H    1 
ATOM   5121  H  HA   . CYS B 1 29  ? 35.055  -44.150 6.834   1.00 26.49  ? 47  CYS B HA   1 
ATOM   5122  H  HB2  . CYS B 1 29  ? 36.432  -44.241 4.374   1.00 27.87  ? 47  CYS B HB2  1 
ATOM   5123  H  HB3  . CYS B 1 29  ? 35.108  -45.072 4.661   1.00 27.87  ? 47  CYS B HB3  1 
ATOM   5124  N  N    . GLN B 1 30  ? 35.813  -46.538 7.045   1.00 25.08  ? 48  GLN B N    1 
ATOM   5125  C  CA   . GLN B 1 30  ? 36.342  -47.853 7.388   1.00 26.09  ? 48  GLN B CA   1 
ATOM   5126  C  C    . GLN B 1 30  ? 36.903  -48.512 6.135   1.00 27.82  ? 48  GLN B C    1 
ATOM   5127  O  O    . GLN B 1 30  ? 36.156  -48.825 5.203   1.00 28.16  ? 48  GLN B O    1 
ATOM   5128  C  CB   . GLN B 1 30  ? 35.222  -48.698 7.986   1.00 26.71  ? 48  GLN B CB   1 
ATOM   5129  C  CG   . GLN B 1 30  ? 35.604  -50.136 8.310   1.00 27.88  ? 48  GLN B CG   1 
ATOM   5130  C  CD   . GLN B 1 30  ? 34.446  -50.909 8.906   1.00 29.91  ? 48  GLN B CD   1 
ATOM   5131  O  OE1  . GLN B 1 30  ? 34.291  -50.968 10.123  1.00 31.69  ? 48  GLN B OE1  1 
ATOM   5132  N  NE2  . GLN B 1 30  ? 33.615  -51.495 8.047   1.00 30.73  ? 48  GLN B NE2  1 
ATOM   5133  H  H    . GLN B 1 30  ? 34.955  -46.492 7.075   1.00 30.10  ? 48  GLN B H    1 
ATOM   5134  H  HA   . GLN B 1 30  ? 37.059  -47.766 8.036   1.00 31.31  ? 48  GLN B HA   1 
ATOM   5135  H  HB2  . GLN B 1 30  ? 34.931  -48.281 8.812   1.00 32.05  ? 48  GLN B HB2  1 
ATOM   5136  H  HB3  . GLN B 1 30  ? 34.488  -48.727 7.353   1.00 32.05  ? 48  GLN B HB3  1 
ATOM   5137  H  HG2  . GLN B 1 30  ? 35.880  -50.584 7.495   1.00 33.45  ? 48  GLN B HG2  1 
ATOM   5138  H  HG3  . GLN B 1 30  ? 36.331  -50.136 8.952   1.00 33.45  ? 48  GLN B HG3  1 
ATOM   5139  H  HE21 . GLN B 1 30  ? 33.751  -51.423 7.200   1.00 36.87  ? 48  GLN B HE21 1 
ATOM   5140  H  HE22 . GLN B 1 30  ? 32.943  -51.946 8.338   1.00 36.87  ? 48  GLN B HE22 1 
ATOM   5141  N  N    . GLY B 1 31  ? 38.219  -48.719 6.113   1.00 28.22  ? 49  GLY B N    1 
ATOM   5142  C  CA   . GLY B 1 31  ? 38.850  -49.470 5.046   1.00 28.97  ? 49  GLY B CA   1 
ATOM   5143  C  C    . GLY B 1 31  ? 38.806  -48.818 3.688   1.00 29.25  ? 49  GLY B C    1 
ATOM   5144  O  O    . GLY B 1 31  ? 38.986  -49.503 2.677   1.00 31.62  ? 49  GLY B O    1 
ATOM   5145  H  H    . GLY B 1 31  ? 38.768  -48.432 6.710   1.00 33.86  ? 49  GLY B H    1 
ATOM   5146  H  HA2  . GLY B 1 31  ? 39.783  -49.609 5.275   1.00 34.77  ? 49  GLY B HA2  1 
ATOM   5147  H  HA3  . GLY B 1 31  ? 38.411  -50.332 4.973   1.00 34.77  ? 49  GLY B HA3  1 
ATOM   5148  N  N    . ALA B 1 32  ? 38.564  -47.512 3.629   1.00 28.63  ? 50  ALA B N    1 
ATOM   5149  C  CA   . ALA B 1 32  ? 38.483  -46.813 2.359   1.00 27.10  ? 50  ALA B CA   1 
ATOM   5150  C  C    . ALA B 1 32  ? 38.824  -45.347 2.569   1.00 26.87  ? 50  ALA B C    1 
ATOM   5151  O  O    . ALA B 1 32  ? 38.693  -44.806 3.672   1.00 27.80  ? 50  ALA B O    1 
ATOM   5152  C  CB   . ALA B 1 32  ? 37.078  -46.906 1.749   1.00 27.12  ? 50  ALA B CB   1 
ATOM   5153  H  H    . ALA B 1 32  ? 38.444  -47.009 4.316   1.00 34.36  ? 50  ALA B H    1 
ATOM   5154  H  HA   . ALA B 1 32  ? 39.126  -47.208 1.751   1.00 32.53  ? 50  ALA B HA   1 
ATOM   5155  H  HB1  . ALA B 1 32  ? 36.854  -47.840 1.614   1.00 32.54  ? 50  ALA B HB1  1 
ATOM   5156  H  HB2  . ALA B 1 32  ? 36.442  -46.498 2.358   1.00 32.54  ? 50  ALA B HB2  1 
ATOM   5157  H  HB3  . ALA B 1 32  ? 37.070  -46.438 0.900   1.00 32.54  ? 50  ALA B HB3  1 
ATOM   5158  N  N    . SER B 1 33  ? 39.248  -44.723 1.511   1.00 25.56  ? 51  SER B N    1 
ATOM   5159  C  CA   . SER B 1 33  ? 39.376  -43.276 1.519   1.00 27.76  ? 51  SER B CA   1 
ATOM   5160  C  C    . SER B 1 33  ? 38.064  -42.650 1.054   1.00 26.60  ? 51  SER B C    1 
ATOM   5161  O  O    . SER B 1 33  ? 37.357  -43.223 0.218   1.00 26.51  ? 51  SER B O    1 
ATOM   5162  C  CB   . SER B 1 33  ? 40.496  -42.848 0.577   1.00 30.95  ? 51  SER B CB   1 
ATOM   5163  O  OG   . SER B 1 33  ? 40.352  -41.488 0.209   1.00 33.29  ? 51  SER B OG   1 
ATOM   5164  H  H    . SER B 1 33  ? 39.472  -45.101 0.772   1.00 30.68  ? 51  SER B H    1 
ATOM   5165  H  HA   . SER B 1 33  ? 39.585  -42.957 2.411   1.00 33.31  ? 51  SER B HA   1 
ATOM   5166  H  HB2  . SER B 1 33  ? 41.348  -42.965 1.026   1.00 37.14  ? 51  SER B HB2  1 
ATOM   5167  H  HB3  . SER B 1 33  ? 40.464  -43.397 -0.222  1.00 37.14  ? 51  SER B HB3  1 
ATOM   5168  H  HG   . SER B 1 33  ? 40.961  -41.270 -0.327  1.00 39.95  ? 51  SER B HG   1 
ATOM   5169  N  N    . PRO B 1 34  ? 37.694  -41.482 1.585   1.00 25.53  ? 52  PRO B N    1 
ATOM   5170  C  CA   . PRO B 1 34  ? 36.434  -40.854 1.149   1.00 25.84  ? 52  PRO B CA   1 
ATOM   5171  C  C    . PRO B 1 34  ? 36.378  -40.561 -0.336  1.00 27.13  ? 52  PRO B C    1 
ATOM   5172  O  O    . PRO B 1 34  ? 35.274  -40.442 -0.887  1.00 27.62  ? 52  PRO B O    1 
ATOM   5173  C  CB   . PRO B 1 34  ? 36.377  -39.561 1.972   1.00 25.23  ? 52  PRO B CB   1 
ATOM   5174  C  CG   . PRO B 1 34  ? 37.255  -39.814 3.149   1.00 26.01  ? 52  PRO B CG   1 
ATOM   5175  C  CD   . PRO B 1 34  ? 38.349  -40.713 2.659   1.00 24.98  ? 52  PRO B CD   1 
ATOM   5176  H  HA   . PRO B 1 34  ? 35.687  -41.423 1.391   1.00 31.01  ? 52  PRO B HA   1 
ATOM   5177  H  HB2  . PRO B 1 34  ? 36.709  -38.819 1.444   1.00 30.28  ? 52  PRO B HB2  1 
ATOM   5178  H  HB3  . PRO B 1 34  ? 35.464  -39.388 2.251   1.00 30.28  ? 52  PRO B HB3  1 
ATOM   5179  H  HG2  . PRO B 1 34  ? 37.618  -38.974 3.471   1.00 31.22  ? 52  PRO B HG2  1 
ATOM   5180  H  HG3  . PRO B 1 34  ? 36.744  -40.245 3.852   1.00 31.22  ? 52  PRO B HG3  1 
ATOM   5181  H  HD2  . PRO B 1 34  ? 39.092  -40.196 2.311   1.00 29.98  ? 52  PRO B HD2  1 
ATOM   5182  H  HD3  . PRO B 1 34  ? 38.657  -41.301 3.367   1.00 29.98  ? 52  PRO B HD3  1 
ATOM   5183  N  N    . SER B 1 35  ? 37.527  -40.429 -0.998  1.00 28.71  ? 53  SER B N    1 
ATOM   5184  C  CA   . SER B 1 35  ? 37.575  -40.123 -2.422  1.00 29.12  ? 53  SER B CA   1 
ATOM   5185  C  C    . SER B 1 35  ? 37.270  -41.324 -3.311  1.00 27.37  ? 53  SER B C    1 
ATOM   5186  O  O    . SER B 1 35  ? 37.051  -41.137 -4.513  1.00 26.38  ? 53  SER B O    1 
ATOM   5187  C  CB   . SER B 1 35  ? 38.954  -39.564 -2.781  1.00 33.54  ? 53  SER B CB   1 
ATOM   5188  O  OG   . SER B 1 35  ? 39.290  -38.473 -1.944  1.00 37.03  ? 53  SER B OG   1 
ATOM   5189  H  H    . SER B 1 35  ? 38.303  -40.514 -0.637  1.00 34.45  ? 53  SER B H    1 
ATOM   5190  H  HA   . SER B 1 35  ? 36.908  -39.445 -2.612  1.00 34.95  ? 53  SER B HA   1 
ATOM   5191  H  HB2  . SER B 1 35  ? 39.617  -40.263 -2.670  1.00 40.24  ? 53  SER B HB2  1 
ATOM   5192  H  HB3  . SER B 1 35  ? 38.942  -39.262 -3.703  1.00 40.24  ? 53  SER B HB3  1 
ATOM   5193  H  HG   . SER B 1 35  ? 39.340  -38.728 -1.145  1.00 44.44  ? 53  SER B HG   1 
ATOM   5194  N  N    . SER B 1 36  ? 37.250  -42.541 -2.763  1.00 26.15  ? 54  SER B N    1 
ATOM   5195  C  CA   . SER B 1 36  ? 36.896  -43.732 -3.539  1.00 26.39  ? 54  SER B CA   1 
ATOM   5196  C  C    . SER B 1 36  ? 36.258  -44.732 -2.572  1.00 26.01  ? 54  SER B C    1 
ATOM   5197  O  O    . SER B 1 36  ? 36.948  -45.536 -1.943  1.00 26.56  ? 54  SER B O    1 
ATOM   5198  C  CB   . SER B 1 36  ? 38.102  -44.334 -4.242  1.00 28.27  ? 54  SER B CB   1 
ATOM   5199  O  OG   . SER B 1 36  ? 37.702  -45.460 -5.002  1.00 29.39  ? 54  SER B OG   1 
ATOM   5200  H  H    . SER B 1 36  ? 37.439  -42.704 -1.939  1.00 31.37  ? 54  SER B H    1 
ATOM   5201  H  HA   . SER B 1 36  ? 36.243  -43.485 -4.213  1.00 31.67  ? 54  SER B HA   1 
ATOM   5202  H  HB2  . SER B 1 36  ? 38.491  -43.671 -4.834  1.00 33.93  ? 54  SER B HB2  1 
ATOM   5203  H  HB3  . SER B 1 36  ? 38.754  -44.610 -3.579  1.00 33.93  ? 54  SER B HB3  1 
ATOM   5204  H  HG   . SER B 1 36  ? 37.072  -45.251 -5.516  1.00 35.27  ? 54  SER B HG   1 
ATOM   5205  N  N    . VAL B 1 37  ? 34.935  -44.677 -2.470  1.00 25.20  ? 55  VAL B N    1 
ATOM   5206  C  CA   . VAL B 1 37  ? 34.208  -45.452 -1.473  1.00 26.47  ? 55  VAL B CA   1 
ATOM   5207  C  C    . VAL B 1 37  ? 32.891  -45.913 -2.076  1.00 26.81  ? 55  VAL B C    1 
ATOM   5208  O  O    . VAL B 1 37  ? 32.206  -45.146 -2.761  1.00 28.31  ? 55  VAL B O    1 
ATOM   5209  C  CB   . VAL B 1 37  ? 33.994  -44.633 -0.180  1.00 25.97  ? 55  VAL B CB   1 
ATOM   5210  C  CG1  . VAL B 1 37  ? 33.218  -43.357 -0.473  1.00 26.31  ? 55  VAL B CG1  1 
ATOM   5211  C  CG2  . VAL B 1 37  ? 33.294  -45.477 0.877   1.00 26.21  ? 55  VAL B CG2  1 
ATOM   5212  H  H    . VAL B 1 37  ? 34.432  -44.194 -2.973  1.00 30.25  ? 55  VAL B H    1 
ATOM   5213  H  HA   . VAL B 1 37  ? 34.712  -46.249 -1.243  1.00 31.76  ? 55  VAL B HA   1 
ATOM   5214  H  HB   . VAL B 1 37  ? 34.859  -44.373 0.175   1.00 31.17  ? 55  VAL B HB   1 
ATOM   5215  H  HG11 . VAL B 1 37  ? 33.093  -43.277 -1.431  1.00 31.58  ? 55  VAL B HG11 1 
ATOM   5216  H  HG12 . VAL B 1 37  ? 32.356  -43.403 -0.030  1.00 31.58  ? 55  VAL B HG12 1 
ATOM   5217  H  HG13 . VAL B 1 37  ? 33.721  -42.598 -0.140  1.00 31.58  ? 55  VAL B HG13 1 
ATOM   5218  H  HG21 . VAL B 1 37  ? 33.317  -45.005 1.724   1.00 31.46  ? 55  VAL B HG21 1 
ATOM   5219  H  HG22 . VAL B 1 37  ? 32.374  -45.623 0.605   1.00 31.46  ? 55  VAL B HG22 1 
ATOM   5220  H  HG23 . VAL B 1 37  ? 33.754  -46.327 0.958   1.00 31.46  ? 55  VAL B HG23 1 
ATOM   5221  N  N    . SER B 1 38  ? 32.547  -47.175 -1.824  1.00 27.21  ? 56  SER B N    1 
ATOM   5222  C  CA   . SER B 1 38  ? 31.300  -47.764 -2.283  1.00 27.45  ? 56  SER B CA   1 
ATOM   5223  C  C    . SER B 1 38  ? 30.273  -47.700 -1.162  1.00 25.84  ? 56  SER B C    1 
ATOM   5224  O  O    . SER B 1 38  ? 30.574  -48.043 -0.012  1.00 25.63  ? 56  SER B O    1 
ATOM   5225  C  CB   . SER B 1 38  ? 31.513  -49.220 -2.708  1.00 28.42  ? 56  SER B CB   1 
ATOM   5226  O  OG   . SER B 1 38  ? 30.281  -49.865 -3.022  1.00 31.33  ? 56  SER B OG   1 
ATOM   5227  H  H    . SER B 1 38  ? 33.037  -47.721 -1.376  1.00 32.66  ? 56  SER B H    1 
ATOM   5228  H  HA   . SER B 1 38  ? 30.965  -47.266 -3.045  1.00 32.94  ? 56  SER B HA   1 
ATOM   5229  H  HB2  . SER B 1 38  ? 32.082  -49.236 -3.493  1.00 34.10  ? 56  SER B HB2  1 
ATOM   5230  H  HB3  . SER B 1 38  ? 31.938  -49.699 -1.979  1.00 34.10  ? 56  SER B HB3  1 
ATOM   5231  H  HG   . SER B 1 38  ? 29.907  -49.472 -3.664  1.00 37.60  ? 56  SER B HG   1 
ATOM   5232  N  N    . LYS B 1 39  ? 29.070  -47.253 -1.500  1.00 24.93  ? 57  LYS B N    1 
ATOM   5233  C  CA   . LYS B 1 39  ? 27.939  -47.243 -0.582  1.00 24.48  ? 57  LYS B CA   1 
ATOM   5234  C  C    . LYS B 1 39  ? 28.316  -46.623 0.764   1.00 22.47  ? 57  LYS B C    1 
ATOM   5235  O  O    . LYS B 1 39  ? 28.082  -47.223 1.819   1.00 22.13  ? 57  LYS B O    1 
ATOM   5236  C  CB   . LYS B 1 39  ? 27.377  -48.646 -0.396  1.00 26.78  ? 57  LYS B CB   1 
ATOM   5237  C  CG   . LYS B 1 39  ? 26.633  -49.182 -1.623  1.00 30.48  ? 57  LYS B CG   1 
ATOM   5238  C  CD   . LYS B 1 39  ? 25.801  -50.402 -1.275  1.00 33.60  ? 57  LYS B CD   1 
ATOM   5239  C  CE   . LYS B 1 39  ? 24.576  -50.042 -0.437  1.00 35.68  ? 57  LYS B CE   1 
ATOM   5240  N  NZ   . LYS B 1 39  ? 23.972  -51.261 0.189   1.00 38.05  ? 57  LYS B NZ   1 
ATOM   5241  H  H    . LYS B 1 39  ? 28.879  -46.943 -2.279  1.00 29.91  ? 57  LYS B H    1 
ATOM   5242  H  HA   . LYS B 1 39  ? 27.229  -46.700 -0.960  1.00 29.38  ? 57  LYS B HA   1 
ATOM   5243  H  HB2  . LYS B 1 39  ? 28.110  -49.252 -0.207  1.00 32.14  ? 57  LYS B HB2  1 
ATOM   5244  H  HB3  . LYS B 1 39  ? 26.754  -48.636 0.347   1.00 32.14  ? 57  LYS B HB3  1 
ATOM   5245  H  HG2  . LYS B 1 39  ? 26.039  -48.495 -1.964  1.00 36.57  ? 57  LYS B HG2  1 
ATOM   5246  H  HG3  . LYS B 1 39  ? 27.275  -49.434 -2.304  1.00 36.57  ? 57  LYS B HG3  1 
ATOM   5247  H  HD2  . LYS B 1 39  ? 25.494  -50.823 -2.094  1.00 40.32  ? 57  LYS B HD2  1 
ATOM   5248  H  HD3  . LYS B 1 39  ? 26.343  -51.024 -0.766  1.00 40.32  ? 57  LYS B HD3  1 
ATOM   5249  H  HE2  . LYS B 1 39  ? 24.837  -49.432 0.270   1.00 42.82  ? 57  LYS B HE2  1 
ATOM   5250  H  HE3  . LYS B 1 39  ? 23.908  -49.626 -1.005  1.00 42.82  ? 57  LYS B HE3  1 
ATOM   5251  H  HZ1  . LYS B 1 39  ? 23.745  -51.846 -0.442  1.00 45.66  ? 57  LYS B HZ1  1 
ATOM   5252  H  HZ2  . LYS B 1 39  ? 23.245  -51.037 0.651   1.00 45.66  ? 57  LYS B HZ2  1 
ATOM   5253  H  HZ3  . LYS B 1 39  ? 24.558  -51.642 0.739   1.00 45.66  ? 57  LYS B HZ3  1 
ATOM   5254  N  N    . PRO B 1 40  ? 28.902  -45.428 0.769   1.00 20.82  ? 58  PRO B N    1 
ATOM   5255  C  CA   . PRO B 1 40  ? 29.194  -44.782 2.046   1.00 19.98  ? 58  PRO B CA   1 
ATOM   5256  C  C    . PRO B 1 40  ? 27.919  -44.485 2.813   1.00 20.40  ? 58  PRO B C    1 
ATOM   5257  O  O    . PRO B 1 40  ? 26.866  -44.204 2.237   1.00 20.87  ? 58  PRO B O    1 
ATOM   5258  C  CB   . PRO B 1 40  ? 29.893  -43.480 1.636   1.00 19.55  ? 58  PRO B CB   1 
ATOM   5259  C  CG   . PRO B 1 40  ? 29.313  -43.168 0.288   1.00 19.95  ? 58  PRO B CG   1 
ATOM   5260  C  CD   . PRO B 1 40  ? 29.178  -44.531 -0.371  1.00 20.37  ? 58  PRO B CD   1 
ATOM   5261  H  HA   . PRO B 1 40  ? 29.791  -45.330 2.580   1.00 23.98  ? 58  PRO B HA   1 
ATOM   5262  H  HB2  . PRO B 1 40  ? 29.693  -42.778 2.275   1.00 23.46  ? 58  PRO B HB2  1 
ATOM   5263  H  HB3  . PRO B 1 40  ? 30.851  -43.618 1.582   1.00 23.46  ? 58  PRO B HB3  1 
ATOM   5264  H  HG2  . PRO B 1 40  ? 28.449  -42.738 0.386   1.00 23.94  ? 58  PRO B HG2  1 
ATOM   5265  H  HG3  . PRO B 1 40  ? 29.915  -42.594 -0.212  1.00 23.94  ? 58  PRO B HG3  1 
ATOM   5266  H  HD2  . PRO B 1 40  ? 28.442  -44.538 -1.003  1.00 24.45  ? 58  PRO B HD2  1 
ATOM   5267  H  HD3  . PRO B 1 40  ? 30.001  -44.783 -0.818  1.00 24.45  ? 58  PRO B HD3  1 
ATOM   5268  N  N    . ILE B 1 41  ? 28.030  -44.535 4.134   1.00 19.72  ? 59  ILE B N    1 
ATOM   5269  C  CA   . ILE B 1 41  ? 27.031  -43.972 5.031   1.00 18.68  ? 59  ILE B CA   1 
ATOM   5270  C  C    . ILE B 1 41  ? 27.781  -43.051 5.980   1.00 18.37  ? 59  ILE B C    1 
ATOM   5271  O  O    . ILE B 1 41  ? 28.807  -43.444 6.546   1.00 19.29  ? 59  ILE B O    1 
ATOM   5272  C  CB   . ILE B 1 41  ? 26.247  -45.068 5.782   1.00 18.49  ? 59  ILE B CB   1 
ATOM   5273  C  CG1  . ILE B 1 41  ? 25.211  -44.442 6.716   1.00 19.49  ? 59  ILE B CG1  1 
ATOM   5274  C  CG2  . ILE B 1 41  ? 27.180  -46.012 6.527   1.00 18.55  ? 59  ILE B CG2  1 
ATOM   5275  C  CD1  . ILE B 1 41  ? 24.170  -45.440 7.234   1.00 19.96  ? 59  ILE B CD1  1 
ATOM   5276  H  H    . ILE B 1 41  ? 28.692  -44.899 4.545   1.00 23.67  ? 59  ILE B H    1 
ATOM   5277  H  HA   . ILE B 1 41  ? 26.375  -43.451 4.542   1.00 22.42  ? 59  ILE B HA   1 
ATOM   5278  H  HB   . ILE B 1 41  ? 25.773  -45.600 5.124   1.00 22.19  ? 59  ILE B HB   1 
ATOM   5279  H  HG12 . ILE B 1 41  ? 25.670  -44.066 7.484   1.00 23.39  ? 59  ILE B HG12 1 
ATOM   5280  H  HG13 . ILE B 1 41  ? 24.739  -43.744 6.236   1.00 23.39  ? 59  ILE B HG13 1 
ATOM   5281  H  HG21 . ILE B 1 41  ? 26.654  -46.717 6.937   1.00 22.26  ? 59  ILE B HG21 1 
ATOM   5282  H  HG22 . ILE B 1 41  ? 27.810  -46.395 5.897   1.00 22.26  ? 59  ILE B HG22 1 
ATOM   5283  H  HG23 . ILE B 1 41  ? 27.655  -45.514 7.209   1.00 22.26  ? 59  ILE B HG23 1 
ATOM   5284  H  HD11 . ILE B 1 41  ? 23.475  -44.955 7.706   1.00 23.95  ? 59  ILE B HD11 1 
ATOM   5285  H  HD12 . ILE B 1 41  ? 23.788  -45.918 6.482   1.00 23.95  ? 59  ILE B HD12 1 
ATOM   5286  H  HD13 . ILE B 1 41  ? 24.604  -46.065 7.837   1.00 23.95  ? 59  ILE B HD13 1 
ATOM   5287  N  N    . LEU B 1 42  ? 27.307  -41.818 6.124   1.00 17.33  ? 60  LEU B N    1 
ATOM   5288  C  CA   . LEU B 1 42  ? 27.974  -40.854 6.996   1.00 16.94  ? 60  LEU B CA   1 
ATOM   5289  C  C    . LEU B 1 42  ? 27.336  -40.878 8.382   1.00 16.16  ? 60  LEU B C    1 
ATOM   5290  O  O    . LEU B 1 42  ? 26.133  -40.628 8.525   1.00 16.40  ? 60  LEU B O    1 
ATOM   5291  C  CB   . LEU B 1 42  ? 27.924  -39.446 6.411   1.00 17.20  ? 60  LEU B CB   1 
ATOM   5292  C  CG   . LEU B 1 42  ? 28.590  -38.376 7.287   1.00 17.22  ? 60  LEU B CG   1 
ATOM   5293  C  CD1  . LEU B 1 42  ? 30.077  -38.660 7.456   1.00 17.12  ? 60  LEU B CD1  1 
ATOM   5294  C  CD2  . LEU B 1 42  ? 28.366  -36.977 6.723   1.00 17.67  ? 60  LEU B CD2  1 
ATOM   5295  H  H    . LEU B 1 42  ? 26.605  -41.516 5.730   1.00 20.79  ? 60  LEU B H    1 
ATOM   5296  H  HA   . LEU B 1 42  ? 28.905  -41.113 7.083   1.00 20.33  ? 60  LEU B HA   1 
ATOM   5297  H  HB2  . LEU B 1 42  ? 28.380  -39.451 5.554   1.00 20.64  ? 60  LEU B HB2  1 
ATOM   5298  H  HB3  . LEU B 1 42  ? 26.996  -39.194 6.291   1.00 20.64  ? 60  LEU B HB3  1 
ATOM   5299  H  HG   . LEU B 1 42  ? 28.178  -38.405 8.165   1.00 20.67  ? 60  LEU B HG   1 
ATOM   5300  H  HD11 . LEU B 1 42  ? 30.443  -38.945 6.604   1.00 20.55  ? 60  LEU B HD11 1 
ATOM   5301  H  HD12 . LEU B 1 42  ? 30.521  -37.850 7.753   1.00 20.55  ? 60  LEU B HD12 1 
ATOM   5302  H  HD13 . LEU B 1 42  ? 30.192  -39.361 8.116   1.00 20.55  ? 60  LEU B HD13 1 
ATOM   5303  H  HD21 . LEU B 1 42  ? 27.412  -36.804 6.678   1.00 21.20  ? 60  LEU B HD21 1 
ATOM   5304  H  HD22 . LEU B 1 42  ? 28.793  -36.330 7.306   1.00 21.20  ? 60  LEU B HD22 1 
ATOM   5305  H  HD23 . LEU B 1 42  ? 28.753  -36.929 5.835   1.00 21.20  ? 60  LEU B HD23 1 
ATOM   5306  N  N    . LEU B 1 43  ? 28.153  -41.156 9.399   1.00 16.15  ? 61  LEU B N    1 
ATOM   5307  C  CA   . LEU B 1 43  ? 27.724  -41.231 10.789  1.00 16.52  ? 61  LEU B CA   1 
ATOM   5308  C  C    . LEU B 1 43  ? 28.191  -39.967 11.501  1.00 17.08  ? 61  LEU B C    1 
ATOM   5309  O  O    . LEU B 1 43  ? 29.373  -39.614 11.430  1.00 18.15  ? 61  LEU B O    1 
ATOM   5310  C  CB   . LEU B 1 43  ? 28.317  -42.471 11.463  1.00 17.74  ? 61  LEU B CB   1 
ATOM   5311  C  CG   . LEU B 1 43  ? 28.149  -43.779 10.681  1.00 17.81  ? 61  LEU B CG   1 
ATOM   5312  C  CD1  . LEU B 1 43  ? 28.896  -44.903 11.389  1.00 19.95  ? 61  LEU B CD1  1 
ATOM   5313  C  CD2  . LEU B 1 43  ? 26.682  -44.135 10.503  1.00 19.57  ? 61  LEU B CD2  1 
ATOM   5314  H  H    . LEU B 1 43  ? 28.993  -41.310 9.301   1.00 19.38  ? 61  LEU B H    1 
ATOM   5315  H  HA   . LEU B 1 43  ? 26.757  -41.288 10.847  1.00 19.83  ? 61  LEU B HA   1 
ATOM   5316  H  HB2  . LEU B 1 43  ? 29.268  -42.326 11.587  1.00 21.28  ? 61  LEU B HB2  1 
ATOM   5317  H  HB3  . LEU B 1 43  ? 27.884  -42.589 12.323  1.00 21.28  ? 61  LEU B HB3  1 
ATOM   5318  H  HG   . LEU B 1 43  ? 28.524  -43.666 9.793   1.00 21.37  ? 61  LEU B HG   1 
ATOM   5319  H  HD11 . LEU B 1 43  ? 29.849  -44.729 11.341  1.00 23.94  ? 61  LEU B HD11 1 
ATOM   5320  H  HD12 . LEU B 1 43  ? 28.612  -44.936 12.316  1.00 23.94  ? 61  LEU B HD12 1 
ATOM   5321  H  HD13 . LEU B 1 43  ? 28.692  -45.744 10.951  1.00 23.94  ? 61  LEU B HD13 1 
ATOM   5322  H  HD21 . LEU B 1 43  ? 26.223  -43.386 10.091  1.00 23.48  ? 61  LEU B HD21 1 
ATOM   5323  H  HD22 . LEU B 1 43  ? 26.613  -44.918 9.935   1.00 23.48  ? 61  LEU B HD22 1 
ATOM   5324  H  HD23 . LEU B 1 43  ? 26.295  -44.322 11.372  1.00 23.48  ? 61  LEU B HD23 1 
ATOM   5325  N  N    . VAL B 1 44  ? 27.266  -39.276 12.156  1.00 15.58  ? 62  VAL B N    1 
ATOM   5326  C  CA   . VAL B 1 44  ? 27.547  -38.014 12.838  1.00 15.28  ? 62  VAL B CA   1 
ATOM   5327  C  C    . VAL B 1 44  ? 27.366  -38.228 14.337  1.00 14.57  ? 62  VAL B C    1 
ATOM   5328  O  O    . VAL B 1 44  ? 26.253  -38.555 14.777  1.00 14.98  ? 62  VAL B O    1 
ATOM   5329  C  CB   . VAL B 1 44  ? 26.635  -36.886 12.333  1.00 15.58  ? 62  VAL B CB   1 
ATOM   5330  C  CG1  . VAL B 1 44  ? 27.096  -35.549 12.910  1.00 15.99  ? 62  VAL B CG1  1 
ATOM   5331  C  CG2  . VAL B 1 44  ? 26.641  -36.834 10.822  1.00 16.55  ? 62  VAL B CG2  1 
ATOM   5332  H  H    . VAL B 1 44  ? 26.445  -39.524 12.222  1.00 18.70  ? 62  VAL B H    1 
ATOM   5333  H  HA   . VAL B 1 44  ? 28.470  -37.764 12.676  1.00 18.33  ? 62  VAL B HA   1 
ATOM   5334  H  HB   . VAL B 1 44  ? 25.726  -37.057 12.626  1.00 18.70  ? 62  VAL B HB   1 
ATOM   5335  H  HG11 . VAL B 1 44  ? 27.123  -35.615 13.877  1.00 19.19  ? 62  VAL B HG11 1 
ATOM   5336  H  HG12 . VAL B 1 44  ? 27.980  -35.346 12.567  1.00 19.19  ? 62  VAL B HG12 1 
ATOM   5337  H  HG13 . VAL B 1 44  ? 26.470  -34.858 12.643  1.00 19.19  ? 62  VAL B HG13 1 
ATOM   5338  H  HG21 . VAL B 1 44  ? 26.118  -36.072 10.530  1.00 19.86  ? 62  VAL B HG21 1 
ATOM   5339  H  HG22 . VAL B 1 44  ? 27.556  -36.745 10.513  1.00 19.86  ? 62  VAL B HG22 1 
ATOM   5340  H  HG23 . VAL B 1 44  ? 26.253  -37.654 10.477  1.00 19.86  ? 62  VAL B HG23 1 
ATOM   5341  N  N    . PRO B 1 45  ? 28.403  -38.024 15.149  1.00 15.24  ? 63  PRO B N    1 
ATOM   5342  C  CA   . PRO B 1 45  ? 28.379  -38.473 16.545  1.00 15.35  ? 63  PRO B CA   1 
ATOM   5343  C  C    . PRO B 1 45  ? 27.708  -37.483 17.490  1.00 15.32  ? 63  PRO B C    1 
ATOM   5344  O  O    . PRO B 1 45  ? 27.313  -36.373 17.125  1.00 15.22  ? 63  PRO B O    1 
ATOM   5345  C  CB   . PRO B 1 45  ? 29.870  -38.603 16.887  1.00 16.17  ? 63  PRO B CB   1 
ATOM   5346  C  CG   . PRO B 1 45  ? 30.531  -37.555 16.028  1.00 16.46  ? 63  PRO B CG   1 
ATOM   5347  C  CD   . PRO B 1 45  ? 29.735  -37.535 14.744  1.00 16.33  ? 63  PRO B CD   1 
ATOM   5348  H  HA   . PRO B 1 45  ? 27.918  -39.325 16.598  1.00 18.43  ? 63  PRO B HA   1 
ATOM   5349  H  HB2  . PRO B 1 45  ? 30.014  -38.427 17.830  1.00 19.40  ? 63  PRO B HB2  1 
ATOM   5350  H  HB3  . PRO B 1 45  ? 30.188  -39.492 16.664  1.00 19.40  ? 63  PRO B HB3  1 
ATOM   5351  H  HG2  . PRO B 1 45  ? 30.493  -36.693 16.472  1.00 19.75  ? 63  PRO B HG2  1 
ATOM   5352  H  HG3  . PRO B 1 45  ? 31.454  -37.801 15.859  1.00 19.75  ? 63  PRO B HG3  1 
ATOM   5353  H  HD2  . PRO B 1 45  ? 29.677  -36.634 14.390  1.00 19.59  ? 63  PRO B HD2  1 
ATOM   5354  H  HD3  . PRO B 1 45  ? 30.132  -38.125 14.085  1.00 19.59  ? 63  PRO B HD3  1 
ATOM   5355  N  N    . GLY B 1 46  ? 27.597  -37.923 18.742  1.00 15.41  ? 64  GLY B N    1 
ATOM   5356  C  CA   . GLY B 1 46  ? 26.993  -37.135 19.788  1.00 15.08  ? 64  GLY B CA   1 
ATOM   5357  C  C    . GLY B 1 46  ? 27.982  -36.259 20.543  1.00 14.80  ? 64  GLY B C    1 
ATOM   5358  O  O    . GLY B 1 46  ? 29.206  -36.388 20.440  1.00 15.07  ? 64  GLY B O    1 
ATOM   5359  H  H    . GLY B 1 46  ? 27.872  -38.693 19.008  1.00 18.49  ? 64  GLY B H    1 
ATOM   5360  H  HA2  . GLY B 1 46  ? 26.318  -36.557 19.399  1.00 18.10  ? 64  GLY B HA2  1 
ATOM   5361  H  HA3  . GLY B 1 46  ? 26.570  -37.729 20.427  1.00 18.10  ? 64  GLY B HA3  1 
ATOM   5362  N  N    . THR B 1 47  ? 27.413  -35.359 21.338  1.00 14.88  ? 65  THR B N    1 
ATOM   5363  C  CA   . THR B 1 47  ? 28.204  -34.451 22.160  1.00 14.37  ? 65  THR B CA   1 
ATOM   5364  C  C    . THR B 1 47  ? 29.177  -35.218 23.043  1.00 15.65  ? 65  THR B C    1 
ATOM   5365  O  O    . THR B 1 47  ? 28.819  -36.217 23.667  1.00 16.04  ? 65  THR B O    1 
ATOM   5366  C  CB   . THR B 1 47  ? 27.267  -33.640 23.052  1.00 15.58  ? 65  THR B CB   1 
ATOM   5367  O  OG1  . THR B 1 47  ? 26.238  -33.058 22.252  1.00 15.15  ? 65  THR B OG1  1 
ATOM   5368  C  CG2  . THR B 1 47  ? 28.022  -32.543 23.779  1.00 15.85  ? 65  THR B CG2  1 
ATOM   5369  H  H    . THR B 1 47  ? 26.563  -35.252 21.420  1.00 17.86  ? 65  THR B H    1 
ATOM   5370  H  HA   . THR B 1 47  ? 28.711  -33.859 21.582  1.00 17.25  ? 65  THR B HA   1 
ATOM   5371  H  HB   . THR B 1 47  ? 26.873  -34.223 23.719  1.00 18.70  ? 65  THR B HB   1 
ATOM   5372  H  HG1  . THR B 1 47  ? 25.706  -32.627 22.739  1.00 18.18  ? 65  THR B HG1  1 
ATOM   5373  H  HG21 . THR B 1 47  ? 27.410  -32.024 24.325  1.00 19.03  ? 65  THR B HG21 1 
ATOM   5374  H  HG22 . THR B 1 47  ? 28.702  -32.931 24.351  1.00 19.03  ? 65  THR B HG22 1 
ATOM   5375  H  HG23 . THR B 1 47  ? 28.449  -31.953 23.139  1.00 19.03  ? 65  THR B HG23 1 
ATOM   5376  N  N    . GLY B 1 48  ? 30.411  -34.725 23.107  1.00 15.57  ? 66  GLY B N    1 
ATOM   5377  C  CA   . GLY B 1 48  ? 31.415  -35.307 23.970  1.00 15.50  ? 66  GLY B CA   1 
ATOM   5378  C  C    . GLY B 1 48  ? 32.053  -36.572 23.448  1.00 16.45  ? 66  GLY B C    1 
ATOM   5379  O  O    . GLY B 1 48  ? 32.725  -37.273 24.216  1.00 17.61  ? 66  GLY B O    1 
ATOM   5380  H  H    . GLY B 1 48  ? 30.688  -34.048 22.654  1.00 18.69  ? 66  GLY B H    1 
ATOM   5381  H  HA2  . GLY B 1 48  ? 32.120  -34.656 24.108  1.00 18.60  ? 66  GLY B HA2  1 
ATOM   5382  H  HA3  . GLY B 1 48  ? 31.005  -35.515 24.825  1.00 18.60  ? 66  GLY B HA3  1 
ATOM   5383  N  N    . THR B 1 49  ? 31.885  -36.880 22.165  1.00 15.94  ? 67  THR B N    1 
ATOM   5384  C  CA   . THR B 1 49  ? 32.453  -38.087 21.594  1.00 16.31  ? 67  THR B CA   1 
ATOM   5385  C  C    . THR B 1 49  ? 33.043  -37.795 20.221  1.00 16.33  ? 67  THR B C    1 
ATOM   5386  O  O    . THR B 1 49  ? 32.735  -36.779 19.581  1.00 15.84  ? 67  THR B O    1 
ATOM   5387  C  CB   . THR B 1 49  ? 31.408  -39.208 21.423  1.00 17.45  ? 67  THR B CB   1 
ATOM   5388  O  OG1  . THR B 1 49  ? 30.524  -38.874 20.344  1.00 17.69  ? 67  THR B OG1  1 
ATOM   5389  C  CG2  . THR B 1 49  ? 30.599  -39.403 22.698  1.00 19.62  ? 67  THR B CG2  1 
ATOM   5390  H  H    . THR B 1 49  ? 31.444  -36.399 21.605  1.00 19.13  ? 67  THR B H    1 
ATOM   5391  H  HA   . THR B 1 49  ? 33.155  -38.384 22.194  1.00 19.57  ? 67  THR B HA   1 
ATOM   5392  H  HB   . THR B 1 49  ? 31.863  -40.042 21.229  1.00 20.94  ? 67  THR B HB   1 
ATOM   5393  H  HG1  . THR B 1 49  ? 30.118  -38.159 20.516  1.00 21.23  ? 67  THR B HG1  1 
ATOM   5394  H  HG21 . THR B 1 49  ? 29.930  -40.092 22.564  1.00 23.55  ? 67  THR B HG21 1 
ATOM   5395  H  HG22 . THR B 1 49  ? 31.184  -39.670 23.424  1.00 23.55  ? 67  THR B HG22 1 
ATOM   5396  H  HG23 . THR B 1 49  ? 30.155  -38.575 22.939  1.00 23.55  ? 67  THR B HG23 1 
ATOM   5397  N  N    . THR B 1 50  ? 33.900  -38.719 19.787  1.00 17.54  ? 68  THR B N    1 
ATOM   5398  C  CA   . THR B 1 50  ? 34.335  -38.846 18.410  1.00 16.87  ? 68  THR B CA   1 
ATOM   5399  C  C    . THR B 1 50  ? 33.406  -39.810 17.674  1.00 16.21  ? 68  THR B C    1 
ATOM   5400  O  O    . THR B 1 50  ? 32.566  -40.488 18.270  1.00 16.65  ? 68  THR B O    1 
ATOM   5401  C  CB   . THR B 1 50  ? 35.757  -39.402 18.371  1.00 17.88  ? 68  THR B CB   1 
ATOM   5402  O  OG1  . THR B 1 50  ? 35.752  -40.725 18.925  1.00 18.14  ? 68  THR B OG1  1 
ATOM   5403  C  CG2  . THR B 1 50  ? 36.711  -38.506 19.179  1.00 18.44  ? 68  THR B CG2  1 
ATOM   5404  H  H    . THR B 1 50  ? 34.256  -39.310 20.300  1.00 21.04  ? 68  THR B H    1 
ATOM   5405  H  HA   . THR B 1 50  ? 34.317  -37.978 17.976  1.00 20.24  ? 68  THR B HA   1 
ATOM   5406  H  HB   . THR B 1 50  ? 36.078  -39.429 17.456  1.00 21.46  ? 68  THR B HB   1 
ATOM   5407  H  HG1  . THR B 1 50  ? 35.485  -40.702 19.721  1.00 21.77  ? 68  THR B HG1  1 
ATOM   5408  H  HG21 . THR B 1 50  ? 36.513  -38.580 20.126  1.00 22.12  ? 68  THR B HG21 1 
ATOM   5409  H  HG22 . THR B 1 50  ? 37.629  -38.778 19.027  1.00 22.12  ? 68  THR B HG22 1 
ATOM   5410  H  HG23 . THR B 1 50  ? 36.607  -37.581 18.907  1.00 22.12  ? 68  THR B HG23 1 
ATOM   5411  N  N    . GLY B 1 51  ? 33.575  -39.880 16.360  1.00 15.84  ? 69  GLY B N    1 
ATOM   5412  C  CA   . GLY B 1 51  ? 32.863  -40.857 15.576  1.00 16.77  ? 69  GLY B CA   1 
ATOM   5413  C  C    . GLY B 1 51  ? 33.046  -42.272 16.101  1.00 17.10  ? 69  GLY B C    1 
ATOM   5414  O  O    . GLY B 1 51  ? 32.077  -43.004 16.322  1.00 17.43  ? 69  GLY B O    1 
ATOM   5415  H  H    . GLY B 1 51  ? 34.097  -39.370 15.906  1.00 19.01  ? 69  GLY B H    1 
ATOM   5416  H  HA2  . GLY B 1 51  ? 31.916  -40.648 15.586  1.00 20.12  ? 69  GLY B HA2  1 
ATOM   5417  H  HA3  . GLY B 1 51  ? 33.183  -40.828 14.660  1.00 20.12  ? 69  GLY B HA3  1 
ATOM   5418  N  N    . PRO B 1 52  ? 34.294  -42.699 16.298  1.00 18.29  ? 70  PRO B N    1 
ATOM   5419  C  CA   . PRO B 1 52  ? 34.497  -44.058 16.838  1.00 18.43  ? 70  PRO B CA   1 
ATOM   5420  C  C    . PRO B 1 52  ? 33.843  -44.278 18.193  1.00 18.52  ? 70  PRO B C    1 
ATOM   5421  O  O    . PRO B 1 52  ? 33.244  -45.334 18.426  1.00 19.89  ? 70  PRO B O    1 
ATOM   5422  C  CB   . PRO B 1 52  ? 36.027  -44.191 16.883  1.00 19.18  ? 70  PRO B CB   1 
ATOM   5423  C  CG   . PRO B 1 52  ? 36.491  -43.305 15.779  1.00 18.78  ? 70  PRO B CG   1 
ATOM   5424  C  CD   . PRO B 1 52  ? 35.558  -42.107 15.821  1.00 17.98  ? 70  PRO B CD   1 
ATOM   5425  H  HA   . PRO B 1 52  ? 34.146  -44.715 16.217  1.00 22.12  ? 70  PRO B HA   1 
ATOM   5426  H  HB2  . PRO B 1 52  ? 36.364  -43.890 17.742  1.00 23.02  ? 70  PRO B HB2  1 
ATOM   5427  H  HB3  . PRO B 1 52  ? 36.288  -45.112 16.729  1.00 23.02  ? 70  PRO B HB3  1 
ATOM   5428  H  HG2  . PRO B 1 52  ? 37.410  -43.035 15.935  1.00 22.53  ? 70  PRO B HG2  1 
ATOM   5429  H  HG3  . PRO B 1 52  ? 36.421  -43.770 14.930  1.00 22.53  ? 70  PRO B HG3  1 
ATOM   5430  H  HD2  . PRO B 1 52  ? 35.883  -41.435 16.440  1.00 21.58  ? 70  PRO B HD2  1 
ATOM   5431  H  HD3  . PRO B 1 52  ? 35.450  -41.720 14.938  1.00 21.58  ? 70  PRO B HD3  1 
ATOM   5432  N  N    . GLN B 1 53  ? 33.934  -43.313 19.106  1.00 18.12  ? 71  GLN B N    1 
ATOM   5433  C  CA   . GLN B 1 53  ? 33.309  -43.508 20.409  1.00 18.40  ? 71  GLN B CA   1 
ATOM   5434  C  C    . GLN B 1 53  ? 31.793  -43.621 20.296  1.00 17.99  ? 71  GLN B C    1 
ATOM   5435  O  O    . GLN B 1 53  ? 31.175  -44.388 21.045  1.00 18.66  ? 71  GLN B O    1 
ATOM   5436  C  CB   . GLN B 1 53  ? 33.703  -42.376 21.353  1.00 18.29  ? 71  GLN B CB   1 
ATOM   5437  C  CG   . GLN B 1 53  ? 35.164  -42.411 21.771  1.00 18.70  ? 71  GLN B CG   1 
ATOM   5438  C  CD   . GLN B 1 53  ? 35.597  -41.135 22.467  1.00 18.92  ? 71  GLN B CD   1 
ATOM   5439  O  OE1  . GLN B 1 53  ? 35.076  -40.050 22.188  1.00 20.18  ? 71  GLN B OE1  1 
ATOM   5440  N  NE2  . GLN B 1 53  ? 36.559  -41.255 23.381  1.00 20.76  ? 71  GLN B NE2  1 
ATOM   5441  H  H    . GLN B 1 53  ? 34.339  -42.562 18.999  1.00 21.74  ? 71  GLN B H    1 
ATOM   5442  H  HA   . GLN B 1 53  ? 33.634  -44.337 20.793  1.00 22.08  ? 71  GLN B HA   1 
ATOM   5443  H  HB2  . GLN B 1 53  ? 33.542  -41.529 20.910  1.00 21.95  ? 71  GLN B HB2  1 
ATOM   5444  H  HB3  . GLN B 1 53  ? 33.164  -42.438 22.157  1.00 21.95  ? 71  GLN B HB3  1 
ATOM   5445  H  HG2  . GLN B 1 53  ? 35.302  -43.151 22.383  1.00 22.44  ? 71  GLN B HG2  1 
ATOM   5446  H  HG3  . GLN B 1 53  ? 35.717  -42.527 20.982  1.00 22.44  ? 71  GLN B HG3  1 
ATOM   5447  H  HE21 . GLN B 1 53  ? 36.900  -42.027 23.548  1.00 24.91  ? 71  GLN B HE21 1 
ATOM   5448  H  HE22 . GLN B 1 53  ? 36.840  -40.561 23.804  1.00 24.91  ? 71  GLN B HE22 1 
ATOM   5449  N  N    . SER B 1 54  ? 31.175  -42.889 19.362  1.00 17.53  ? 72  SER B N    1 
ATOM   5450  C  CA   . SER B 1 54  ? 29.725  -42.970 19.215  1.00 17.15  ? 72  SER B CA   1 
ATOM   5451  C  C    . SER B 1 54  ? 29.293  -44.284 18.570  1.00 17.29  ? 72  SER B C    1 
ATOM   5452  O  O    . SER B 1 54  ? 28.234  -44.824 18.912  1.00 18.04  ? 72  SER B O    1 
ATOM   5453  C  CB   . SER B 1 54  ? 29.198  -41.803 18.372  1.00 16.31  ? 72  SER B CB   1 
ATOM   5454  O  OG   . SER B 1 54  ? 28.835  -40.674 19.156  1.00 16.13  ? 72  SER B OG   1 
ATOM   5455  H  H    . SER B 1 54  ? 31.565  -42.351 18.816  1.00 21.03  ? 72  SER B H    1 
ATOM   5456  H  HA   . SER B 1 54  ? 29.341  -42.914 20.104  1.00 20.58  ? 72  SER B HA   1 
ATOM   5457  H  HB2  . SER B 1 54  ? 29.892  -41.536 17.749  1.00 19.57  ? 72  SER B HB2  1 
ATOM   5458  H  HB3  . SER B 1 54  ? 28.415  -42.105 17.886  1.00 19.57  ? 72  SER B HB3  1 
ATOM   5459  H  HG   . SER B 1 54  ? 29.508  -40.378 19.563  1.00 19.35  ? 72  SER B HG   1 
ATOM   5460  N  N    . PHE B 1 55  ? 30.086  -44.813 17.623  1.00 18.51  ? 73  PHE B N    1 
ATOM   5461  C  CA   . PHE B 1 55  ? 29.585  -45.820 16.690  1.00 17.60  ? 73  PHE B CA   1 
ATOM   5462  C  C    . PHE B 1 55  ? 30.385  -47.121 16.597  1.00 19.38  ? 73  PHE B C    1 
ATOM   5463  O  O    . PHE B 1 55  ? 29.897  -48.064 15.962  1.00 20.07  ? 73  PHE B O    1 
ATOM   5464  C  CB   . PHE B 1 55  ? 29.451  -45.222 15.274  1.00 17.06  ? 73  PHE B CB   1 
ATOM   5465  C  CG   . PHE B 1 55  ? 28.572  -43.994 15.207  1.00 16.18  ? 73  PHE B CG   1 
ATOM   5466  C  CD1  . PHE B 1 55  ? 27.215  -44.085 15.475  1.00 16.44  ? 73  PHE B CD1  1 
ATOM   5467  C  CD2  . PHE B 1 55  ? 29.101  -42.747 14.869  1.00 16.66  ? 73  PHE B CD2  1 
ATOM   5468  C  CE1  . PHE B 1 55  ? 26.398  -42.960 15.423  1.00 16.33  ? 73  PHE B CE1  1 
ATOM   5469  C  CE2  . PHE B 1 55  ? 28.285  -41.610 14.808  1.00 15.43  ? 73  PHE B CE2  1 
ATOM   5470  C  CZ   . PHE B 1 55  ? 26.934  -41.718 15.081  1.00 16.02  ? 73  PHE B CZ   1 
ATOM   5471  H  H    . PHE B 1 55  ? 30.912  -44.602 17.507  1.00 22.21  ? 73  PHE B H    1 
ATOM   5472  H  HA   . PHE B 1 55  ? 28.704  -46.076 17.005  1.00 21.12  ? 73  PHE B HA   1 
ATOM   5473  H  HB2  . PHE B 1 55  ? 30.333  -44.972 14.957  1.00 20.47  ? 73  PHE B HB2  1 
ATOM   5474  H  HB3  . PHE B 1 55  ? 29.067  -45.893 14.688  1.00 20.47  ? 73  PHE B HB3  1 
ATOM   5475  H  HD1  . PHE B 1 55  ? 26.846  -44.911 15.693  1.00 19.72  ? 73  PHE B HD1  1 
ATOM   5476  H  HD2  . PHE B 1 55  ? 30.008  -42.670 14.680  1.00 19.99  ? 73  PHE B HD2  1 
ATOM   5477  H  HE1  . PHE B 1 55  ? 25.492  -43.036 15.617  1.00 19.60  ? 73  PHE B HE1  1 
ATOM   5478  H  HE2  . PHE B 1 55  ? 28.651  -40.785 14.586  1.00 18.51  ? 73  PHE B HE2  1 
ATOM   5479  H  HZ   . PHE B 1 55  ? 26.386  -40.968 15.036  1.00 19.22  ? 73  PHE B HZ   1 
ATOM   5480  N  N    . ASP B 1 56  ? 31.574  -47.219 17.202  1.00 19.97  ? 74  ASP B N    1 
ATOM   5481  C  CA   . ASP B 1 56  ? 32.342  -48.461 17.106  1.00 21.28  ? 74  ASP B CA   1 
ATOM   5482  C  C    . ASP B 1 56  ? 31.530  -49.655 17.597  1.00 21.75  ? 74  ASP B C    1 
ATOM   5483  O  O    . ASP B 1 56  ? 31.613  -50.754 17.032  1.00 22.81  ? 74  ASP B O    1 
ATOM   5484  C  CB   . ASP B 1 56  ? 33.614  -48.367 17.949  1.00 20.79  ? 74  ASP B CB   1 
ATOM   5485  C  CG   . ASP B 1 56  ? 34.790  -47.778 17.198  1.00 21.71  ? 74  ASP B CG   1 
ATOM   5486  O  OD1  . ASP B 1 56  ? 34.693  -47.559 15.972  1.00 23.03  ? 74  ASP B OD1  1 
ATOM   5487  O  OD2  . ASP B 1 56  ? 35.824  -47.532 17.854  1.00 23.71  ? 74  ASP B OD2  1 
ATOM   5488  H  H    . ASP B 1 56  ? 31.948  -46.596 17.662  1.00 23.97  ? 74  ASP B H    1 
ATOM   5489  H  HA   . ASP B 1 56  ? 32.581  -48.590 16.174  1.00 25.53  ? 74  ASP B HA   1 
ATOM   5490  H  HB2  . ASP B 1 56  ? 33.440  -47.802 18.719  1.00 24.95  ? 74  ASP B HB2  1 
ATOM   5491  H  HB3  . ASP B 1 56  ? 33.864  -49.258 18.241  1.00 24.95  ? 74  ASP B HB3  1 
ATOM   5492  N  N    . SER B 1 57  ? 30.747  -49.461 18.651  1.00 20.81  ? 75  SER B N    1 
ATOM   5493  C  CA   . SER B 1 57  ? 30.011  -50.541 19.289  1.00 21.33  ? 75  SER B CA   1 
ATOM   5494  C  C    . SER B 1 57  ? 28.632  -50.760 18.686  1.00 21.34  ? 75  SER B C    1 
ATOM   5495  O  O    . SER B 1 57  ? 27.874  -51.587 19.200  1.00 22.75  ? 75  SER B O    1 
ATOM   5496  C  CB   . SER B 1 57  ? 29.856  -50.236 20.783  1.00 21.89  ? 75  SER B CB   1 
ATOM   5497  O  OG   . SER B 1 57  ? 29.051  -49.079 20.980  1.00 22.56  ? 75  SER B OG   1 
ATOM   5498  H  H    . SER B 1 57  ? 30.624  -48.695 19.023  1.00 24.98  ? 75  SER B H    1 
ATOM   5499  H  HA   . SER B 1 57  ? 30.515  -51.363 19.186  1.00 25.60  ? 75  SER B HA   1 
ATOM   5500  H  HB2  . SER B 1 57  ? 29.434  -50.993 21.218  1.00 26.27  ? 75  SER B HB2  1 
ATOM   5501  H  HB3  . SER B 1 57  ? 30.734  -50.080 21.166  1.00 26.27  ? 75  SER B HB3  1 
ATOM   5502  H  HG   . SER B 1 57  ? 29.389  -48.422 20.581  1.00 27.07  ? 75  SER B HG   1 
ATOM   5503  N  N    . ASN B 1 58  ? 28.275  -50.043 17.624  1.00 19.60  ? 76  ASN B N    1 
ATOM   5504  C  CA   . ASN B 1 58  ? 26.916  -50.151 17.111  1.00 19.96  ? 76  ASN B CA   1 
ATOM   5505  C  C    . ASN B 1 58  ? 26.868  -49.983 15.594  1.00 19.31  ? 76  ASN B C    1 
ATOM   5506  O  O    . ASN B 1 58  ? 27.045  -50.964 14.864  1.00 20.67  ? 76  ASN B O    1 
ATOM   5507  C  CB   . ASN B 1 58  ? 25.957  -49.225 17.883  1.00 18.54  ? 76  ASN B CB   1 
ATOM   5508  C  CG   . ASN B 1 58  ? 26.480  -47.806 18.035  1.00 17.36  ? 76  ASN B CG   1 
ATOM   5509  O  OD1  . ASN B 1 58  ? 26.334  -46.984 17.132  1.00 17.84  ? 76  ASN B OD1  1 
ATOM   5510  N  ND2  . ASN B 1 58  ? 27.045  -47.497 19.201  1.00 18.84  ? 76  ASN B ND2  1 
ATOM   5511  H  H    . ASN B 1 58  ? 28.788  -49.502 17.195  1.00 23.52  ? 76  ASN B H    1 
ATOM   5512  H  HA   . ASN B 1 58  ? 26.582  -51.047 17.269  1.00 23.95  ? 76  ASN B HA   1 
ATOM   5513  H  HB2  . ASN B 1 58  ? 25.112  -49.182 17.408  1.00 22.25  ? 76  ASN B HB2  1 
ATOM   5514  H  HB3  . ASN B 1 58  ? 25.819  -49.588 18.772  1.00 22.25  ? 76  ASN B HB3  1 
ATOM   5515  H  HD21 . ASN B 1 58  ? 27.355  -46.705 19.333  1.00 22.61  ? 76  ASN B HD21 1 
ATOM   5516  H  HD22 . ASN B 1 58  ? 27.100  -48.088 19.823  1.00 22.61  ? 76  ASN B HD22 1 
ATOM   5517  N  N    . TRP B 1 59  ? 26.664  -48.766 15.096  1.00 18.74  ? 77  TRP B N    1 
ATOM   5518  C  CA   . TRP B 1 59  ? 26.335  -48.609 13.682  1.00 19.35  ? 77  TRP B CA   1 
ATOM   5519  C  C    . TRP B 1 59  ? 27.521  -48.739 12.736  1.00 19.60  ? 77  TRP B C    1 
ATOM   5520  O  O    . TRP B 1 59  ? 27.301  -48.883 11.527  1.00 20.61  ? 77  TRP B O    1 
ATOM   5521  C  CB   . TRP B 1 59  ? 25.540  -47.322 13.451  1.00 17.75  ? 77  TRP B CB   1 
ATOM   5522  C  CG   . TRP B 1 59  ? 24.145  -47.514 13.933  1.00 18.03  ? 77  TRP B CG   1 
ATOM   5523  C  CD1  . TRP B 1 59  ? 23.640  -47.149 15.146  1.00 17.55  ? 77  TRP B CD1  1 
ATOM   5524  C  CD2  . TRP B 1 59  ? 23.089  -48.190 13.245  1.00 17.75  ? 77  TRP B CD2  1 
ATOM   5525  N  NE1  . TRP B 1 59  ? 22.328  -47.535 15.248  1.00 18.25  ? 77  TRP B NE1  1 
ATOM   5526  C  CE2  . TRP B 1 59  ? 21.963  -48.176 14.092  1.00 18.11  ? 77  TRP B CE2  1 
ATOM   5527  C  CE3  . TRP B 1 59  ? 22.982  -48.801 11.990  1.00 18.67  ? 77  TRP B CE3  1 
ATOM   5528  C  CZ2  . TRP B 1 59  ? 20.744  -48.742 13.722  1.00 19.09  ? 77  TRP B CZ2  1 
ATOM   5529  C  CZ3  . TRP B 1 59  ? 21.768  -49.362 11.623  1.00 18.90  ? 77  TRP B CZ3  1 
ATOM   5530  C  CH2  . TRP B 1 59  ? 20.668  -49.330 12.486  1.00 19.70  ? 77  TRP B CH2  1 
ATOM   5531  H  H    . TRP B 1 59  ? 26.709  -48.034 15.545  1.00 22.49  ? 77  TRP B H    1 
ATOM   5532  H  HA   . TRP B 1 59  ? 25.742  -49.334 13.429  1.00 23.22  ? 77  TRP B HA   1 
ATOM   5533  H  HB2  . TRP B 1 59  ? 25.946  -46.592 13.944  1.00 21.30  ? 77  TRP B HB2  1 
ATOM   5534  H  HB3  . TRP B 1 59  ? 25.520  -47.113 12.504  1.00 21.30  ? 77  TRP B HB3  1 
ATOM   5535  H  HD1  . TRP B 1 59  ? 24.117  -46.702 15.808  1.00 21.06  ? 77  TRP B HD1  1 
ATOM   5536  H  HE1  . TRP B 1 59  ? 21.817  -47.398 15.927  1.00 21.90  ? 77  TRP B HE1  1 
ATOM   5537  H  HE3  . TRP B 1 59  ? 23.712  -48.829 11.414  1.00 22.40  ? 77  TRP B HE3  1 
ATOM   5538  H  HZ2  . TRP B 1 59  ? 20.010  -48.721 14.292  1.00 22.90  ? 77  TRP B HZ2  1 
ATOM   5539  H  HZ3  . TRP B 1 59  ? 21.685  -49.767 10.790  1.00 22.68  ? 77  TRP B HZ3  1 
ATOM   5540  H  HH2  . TRP B 1 59  ? 19.867  -49.715 12.214  1.00 23.64  ? 77  TRP B HH2  1 
ATOM   5541  N  N    . ILE B 1 60  ? 28.756  -48.732 13.226  1.00 20.30  ? 78  ILE B N    1 
ATOM   5542  C  CA   . ILE B 1 60  ? 29.888  -49.057 12.355  1.00 20.18  ? 78  ILE B CA   1 
ATOM   5543  C  C    . ILE B 1 60  ? 29.767  -50.524 11.940  1.00 20.77  ? 78  ILE B C    1 
ATOM   5544  O  O    . ILE B 1 60  ? 29.636  -50.806 10.739  1.00 20.49  ? 78  ILE B O    1 
ATOM   5545  C  CB   . ILE B 1 60  ? 31.230  -48.667 12.994  1.00 20.37  ? 78  ILE B CB   1 
ATOM   5546  C  CG1  . ILE B 1 60  ? 31.455  -47.156 12.818  1.00 20.62  ? 78  ILE B CG1  1 
ATOM   5547  C  CG2  . ILE B 1 60  ? 32.378  -49.439 12.355  1.00 21.23  ? 78  ILE B CG2  1 
ATOM   5548  C  CD1  . ILE B 1 60  ? 32.575  -46.583 13.653  1.00 20.87  ? 78  ILE B CD1  1 
ATOM   5549  H  H    . ILE B 1 60  ? 28.962  -48.547 14.040  1.00 24.36  ? 78  ILE B H    1 
ATOM   5550  H  HA   . ILE B 1 60  ? 29.846  -48.542 11.534  1.00 24.22  ? 78  ILE B HA   1 
ATOM   5551  H  HB   . ILE B 1 60  ? 31.201  -48.888 13.938  1.00 24.44  ? 78  ILE B HB   1 
ATOM   5552  H  HG12 . ILE B 1 60  ? 31.667  -46.982 11.888  1.00 24.75  ? 78  ILE B HG12 1 
ATOM   5553  H  HG13 . ILE B 1 60  ? 30.640  -46.692 13.065  1.00 24.75  ? 78  ILE B HG13 1 
ATOM   5554  H  HG21 . ILE B 1 60  ? 32.300  -49.379 11.390  1.00 25.47  ? 78  ILE B HG21 1 
ATOM   5555  H  HG22 . ILE B 1 60  ? 33.219  -49.051 12.644  1.00 25.47  ? 78  ILE B HG22 1 
ATOM   5556  H  HG23 . ILE B 1 60  ? 32.328  -50.366 12.634  1.00 25.47  ? 78  ILE B HG23 1 
ATOM   5557  H  HD11 . ILE B 1 60  ? 33.421  -46.918 13.319  1.00 25.04  ? 78  ILE B HD11 1 
ATOM   5558  H  HD12 . ILE B 1 60  ? 32.553  -45.615 13.589  1.00 25.04  ? 78  ILE B HD12 1 
ATOM   5559  H  HD13 . ILE B 1 60  ? 32.452  -46.856 14.576  1.00 25.04  ? 78  ILE B HD13 1 
ATOM   5560  N  N    . PRO B 1 61  ? 29.750  -51.486 12.869  1.00 20.30  ? 79  PRO B N    1 
ATOM   5561  C  CA   . PRO B 1 61  ? 29.553  -52.884 12.434  1.00 22.27  ? 79  PRO B CA   1 
ATOM   5562  C  C    . PRO B 1 61  ? 28.182  -53.153 11.837  1.00 23.45  ? 79  PRO B C    1 
ATOM   5563  O  O    . PRO B 1 61  ? 28.075  -53.930 10.880  1.00 24.90  ? 79  PRO B O    1 
ATOM   5564  C  CB   . PRO B 1 61  ? 29.806  -53.710 13.706  1.00 22.42  ? 79  PRO B CB   1 
ATOM   5565  C  CG   . PRO B 1 61  ? 29.678  -52.735 14.843  1.00 21.89  ? 79  PRO B CG   1 
ATOM   5566  C  CD   . PRO B 1 61  ? 30.079  -51.384 14.304  1.00 21.30  ? 79  PRO B CD   1 
ATOM   5567  H  HA   . PRO B 1 61  ? 30.231  -53.108 11.777  1.00 26.73  ? 79  PRO B HA   1 
ATOM   5568  H  HB2  . PRO B 1 61  ? 29.144  -54.414 13.778  1.00 26.91  ? 79  PRO B HB2  1 
ATOM   5569  H  HB3  . PRO B 1 61  ? 30.697  -54.093 13.678  1.00 26.91  ? 79  PRO B HB3  1 
ATOM   5570  H  HG2  . PRO B 1 61  ? 28.759  -52.719 15.154  1.00 26.27  ? 79  PRO B HG2  1 
ATOM   5571  H  HG3  . PRO B 1 61  ? 30.267  -53.002 15.566  1.00 26.27  ? 79  PRO B HG3  1 
ATOM   5572  H  HD2  . PRO B 1 61  ? 29.567  -50.677 14.726  1.00 25.56  ? 79  PRO B HD2  1 
ATOM   5573  H  HD3  . PRO B 1 61  ? 31.028  -51.229 14.432  1.00 25.56  ? 79  PRO B HD3  1 
ATOM   5574  N  N    . LEU B 1 62  ? 27.122  -52.539 12.365  1.00 23.16  ? 80  LEU B N    1 
ATOM   5575  C  CA   . LEU B 1 62  ? 25.787  -52.854 11.861  1.00 23.42  ? 80  LEU B CA   1 
ATOM   5576  C  C    . LEU B 1 62  ? 25.596  -52.355 10.431  1.00 24.35  ? 80  LEU B C    1 
ATOM   5577  O  O    . LEU B 1 62  ? 25.003  -53.051 9.601   1.00 24.72  ? 80  LEU B O    1 
ATOM   5578  C  CB   . LEU B 1 62  ? 24.715  -52.287 12.790  1.00 23.26  ? 80  LEU B CB   1 
ATOM   5579  C  CG   . LEU B 1 62  ? 24.655  -52.944 14.173  1.00 22.89  ? 80  LEU B CG   1 
ATOM   5580  C  CD1  . LEU B 1 62  ? 23.809  -52.117 15.130  1.00 23.56  ? 80  LEU B CD1  1 
ATOM   5581  C  CD2  . LEU B 1 62  ? 24.133  -54.377 14.073  1.00 23.91  ? 80  LEU B CD2  1 
ATOM   5582  H  H    . LEU B 1 62  ? 27.148  -51.955 12.995  1.00 27.79  ? 80  LEU B H    1 
ATOM   5583  H  HA   . LEU B 1 62  ? 25.681  -53.818 11.851  1.00 28.10  ? 80  LEU B HA   1 
ATOM   5584  H  HB2  . LEU B 1 62  ? 24.891  -51.343 12.921  1.00 27.92  ? 80  LEU B HB2  1 
ATOM   5585  H  HB3  . LEU B 1 62  ? 23.849  -52.408 12.370  1.00 27.92  ? 80  LEU B HB3  1 
ATOM   5586  H  HG   . LEU B 1 62  ? 25.553  -52.985 14.538  1.00 27.46  ? 80  LEU B HG   1 
ATOM   5587  H  HD11 . LEU B 1 62  ? 24.219  -51.245 15.240  1.00 28.27  ? 80  LEU B HD11 1 
ATOM   5588  H  HD12 . LEU B 1 62  ? 22.918  -52.020 14.760  1.00 28.27  ? 80  LEU B HD12 1 
ATOM   5589  H  HD13 . LEU B 1 62  ? 23.765  -52.572 15.986  1.00 28.27  ? 80  LEU B HD13 1 
ATOM   5590  H  HD21 . LEU B 1 62  ? 24.795  -54.923 13.621  1.00 28.70  ? 80  LEU B HD21 1 
ATOM   5591  H  HD22 . LEU B 1 62  ? 23.976  -54.719 14.967  1.00 28.70  ? 80  LEU B HD22 1 
ATOM   5592  H  HD23 . LEU B 1 62  ? 23.304  -54.377 13.569  1.00 28.70  ? 80  LEU B HD23 1 
ATOM   5593  N  N    . SER B 1 63  ? 26.087  -51.155 10.118  1.00 23.68  ? 81  SER B N    1 
ATOM   5594  C  CA   . SER B 1 63  ? 25.980  -50.683 8.742   1.00 23.61  ? 81  SER B CA   1 
ATOM   5595  C  C    . SER B 1 63  ? 26.857  -51.507 7.809   1.00 24.40  ? 81  SER B C    1 
ATOM   5596  O  O    . SER B 1 63  ? 26.482  -51.741 6.655   1.00 23.92  ? 81  SER B O    1 
ATOM   5597  C  CB   . SER B 1 63  ? 26.307  -49.195 8.641   1.00 24.49  ? 81  SER B CB   1 
ATOM   5598  O  OG   . SER B 1 63  ? 27.684  -48.945 8.824   1.00 25.47  ? 81  SER B OG   1 
ATOM   5599  H  H    . SER B 1 63  ? 26.473  -50.615 10.664  1.00 28.42  ? 81  SER B H    1 
ATOM   5600  H  HA   . SER B 1 63  ? 25.059  -50.780 8.452   1.00 28.33  ? 81  SER B HA   1 
ATOM   5601  H  HB2  . SER B 1 63  ? 26.047  -48.878 7.762   1.00 29.39  ? 81  SER B HB2  1 
ATOM   5602  H  HB3  . SER B 1 63  ? 25.810  -48.720 9.325   1.00 29.39  ? 81  SER B HB3  1 
ATOM   5603  H  HG   . SER B 1 63  ? 28.124  -49.294 8.199   1.00 30.57  ? 81  SER B HG   1 
ATOM   5604  N  N    . THR B 1 64  ? 28.007  -51.981 8.297   1.00 26.00  ? 82  THR B N    1 
ATOM   5605  C  CA   . THR B 1 64  ? 28.842  -52.858 7.483   1.00 27.75  ? 82  THR B CA   1 
ATOM   5606  C  C    . THR B 1 64  ? 28.074  -54.108 7.078   1.00 28.46  ? 82  THR B C    1 
ATOM   5607  O  O    . THR B 1 64  ? 28.093  -54.512 5.908   1.00 29.23  ? 82  THR B O    1 
ATOM   5608  C  CB   . THR B 1 64  ? 30.109  -53.232 8.250   1.00 26.88  ? 82  THR B CB   1 
ATOM   5609  O  OG1  . THR B 1 64  ? 30.835  -52.042 8.573   1.00 26.42  ? 82  THR B OG1  1 
ATOM   5610  C  CG2  . THR B 1 64  ? 30.996  -54.134 7.413   1.00 27.69  ? 82  THR B CG2  1 
ATOM   5611  H  H    . THR B 1 64  ? 28.319  -51.811 9.080   1.00 31.20  ? 82  THR B H    1 
ATOM   5612  H  HA   . THR B 1 64  ? 29.106  -52.387 6.678   1.00 33.30  ? 82  THR B HA   1 
ATOM   5613  H  HB   . THR B 1 64  ? 29.866  -53.704 9.062   1.00 32.25  ? 82  THR B HB   1 
ATOM   5614  H  HG1  . THR B 1 64  ? 31.030  -51.625 7.871   1.00 31.70  ? 82  THR B HG1  1 
ATOM   5615  H  HG21 . THR B 1 64  ? 30.598  -55.015 7.340   1.00 33.23  ? 82  THR B HG21 1 
ATOM   5616  H  HG22 . THR B 1 64  ? 31.870  -54.217 7.827   1.00 33.23  ? 82  THR B HG22 1 
ATOM   5617  H  HG23 . THR B 1 64  ? 31.103  -53.762 6.524   1.00 33.23  ? 82  THR B HG23 1 
ATOM   5618  N  N    . GLN B 1 65  ? 27.375  -54.729 8.031   1.00 28.94  ? 83  GLN B N    1 
ATOM   5619  C  CA   . GLN B 1 65  ? 26.645  -55.957 7.727   1.00 29.39  ? 83  GLN B CA   1 
ATOM   5620  C  C    . GLN B 1 65  ? 25.432  -55.700 6.843   1.00 28.53  ? 83  GLN B C    1 
ATOM   5621  O  O    . GLN B 1 65  ? 24.946  -56.633 6.189   1.00 29.29  ? 83  GLN B O    1 
ATOM   5622  C  CB   . GLN B 1 65  ? 26.253  -56.674 9.023   1.00 32.55  ? 83  GLN B CB   1 
ATOM   5623  C  CG   . GLN B 1 65  ? 24.967  -56.197 9.675   1.00 36.14  ? 83  GLN B CG   1 
ATOM   5624  C  CD   . GLN B 1 65  ? 24.537  -57.083 10.835  1.00 38.79  ? 83  GLN B CD   1 
ATOM   5625  O  OE1  . GLN B 1 65  ? 25.363  -57.737 11.480  1.00 40.78  ? 83  GLN B OE1  1 
ATOM   5626  N  NE2  . GLN B 1 65  ? 23.238  -57.105 11.109  1.00 38.69  ? 83  GLN B NE2  1 
ATOM   5627  H  H    . GLN B 1 65  ? 27.310  -54.463 8.847   0.73 34.73  ? 83  GLN B H    1 
ATOM   5628  H  HA   . GLN B 1 65  ? 27.225  -56.563 7.239   1.00 35.26  ? 83  GLN B HA   1 
ATOM   5629  H  HB2  . GLN B 1 65  ? 26.145  -57.618 8.828   1.00 39.06  ? 83  GLN B HB2  1 
ATOM   5630  H  HB3  . GLN B 1 65  ? 26.967  -56.548 9.668   1.00 39.06  ? 83  GLN B HB3  1 
ATOM   5631  H  HG2  . GLN B 1 65  ? 25.099  -55.299 10.016  1.00 43.37  ? 83  GLN B HG2  1 
ATOM   5632  H  HG3  . GLN B 1 65  ? 24.257  -56.201 9.015   1.00 43.37  ? 83  GLN B HG3  1 
ATOM   5633  H  HE21 . GLN B 1 65  ? 22.942  -57.589 11.755  1.00 46.43  ? 83  GLN B HE21 1 
ATOM   5634  H  HE22 . GLN B 1 65  ? 22.692  -56.634 10.640  1.00 46.43  ? 83  GLN B HE22 1 
ATOM   5635  N  N    . LEU B 1 66  ? 24.939  -54.464 6.804   1.00 27.69  ? 84  LEU B N    1 
ATOM   5636  C  CA   . LEU B 1 66  ? 23.850  -54.081 5.916   1.00 28.38  ? 84  LEU B CA   1 
ATOM   5637  C  C    . LEU B 1 66  ? 24.338  -53.676 4.532   1.00 28.68  ? 84  LEU B C    1 
ATOM   5638  O  O    . LEU B 1 66  ? 23.517  -53.339 3.672   1.00 30.56  ? 84  LEU B O    1 
ATOM   5639  C  CB   . LEU B 1 66  ? 23.035  -52.941 6.535   1.00 28.05  ? 84  LEU B CB   1 
ATOM   5640  C  CG   . LEU B 1 66  ? 22.142  -53.329 7.716   1.00 28.25  ? 84  LEU B CG   1 
ATOM   5641  C  CD1  . LEU B 1 66  ? 21.487  -52.094 8.309   1.00 28.87  ? 84  LEU B CD1  1 
ATOM   5642  C  CD2  . LEU B 1 66  ? 21.092  -54.363 7.298   1.00 28.64  ? 84  LEU B CD2  1 
ATOM   5643  H  H    . LEU B 1 66  ? 25.226  -53.817 7.294   1.00 33.23  ? 84  LEU B H    1 
ATOM   5644  H  HA   . LEU B 1 66  ? 23.254  -54.839 5.810   1.00 34.05  ? 84  LEU B HA   1 
ATOM   5645  H  HB2  . LEU B 1 66  ? 23.653  -52.263 6.851   1.00 33.66  ? 84  LEU B HB2  1 
ATOM   5646  H  HB3  . LEU B 1 66  ? 22.459  -52.571 5.847   1.00 33.66  ? 84  LEU B HB3  1 
ATOM   5647  H  HG   . LEU B 1 66  ? 22.690  -53.738 8.404   1.00 33.90  ? 84  LEU B HG   1 
ATOM   5648  H  HD11 . LEU B 1 66  ? 22.176  -51.455 8.548   1.00 34.64  ? 84  LEU B HD11 1 
ATOM   5649  H  HD12 . LEU B 1 66  ? 20.986  -52.351 9.099   1.00 34.64  ? 84  LEU B HD12 1 
ATOM   5650  H  HD13 . LEU B 1 66  ? 20.890  -51.706 7.650   1.00 34.64  ? 84  LEU B HD13 1 
ATOM   5651  H  HD21 . LEU B 1 66  ? 20.415  -54.423 7.991   1.00 34.37  ? 84  LEU B HD21 1 
ATOM   5652  H  HD22 . LEU B 1 66  ? 20.686  -54.082 6.463   1.00 34.37  ? 84  LEU B HD22 1 
ATOM   5653  H  HD23 . LEU B 1 66  ? 21.524  -55.223 7.183   1.00 34.37  ? 84  LEU B HD23 1 
ATOM   5654  N  N    . GLY B 1 67  ? 25.639  -53.707 4.288   1.00 27.64  ? 85  GLY B N    1 
ATOM   5655  C  CA   . GLY B 1 67  ? 26.172  -53.462 2.973   1.00 28.01  ? 85  GLY B CA   1 
ATOM   5656  C  C    . GLY B 1 67  ? 26.607  -52.046 2.696   1.00 27.96  ? 85  GLY B C    1 
ATOM   5657  O  O    . GLY B 1 67  ? 26.561  -51.622 1.535   1.00 30.14  ? 85  GLY B O    1 
ATOM   5658  H  H    . GLY B 1 67  ? 26.238  -53.870 4.882   1.00 33.17  ? 85  GLY B H    1 
ATOM   5659  H  HA2  . GLY B 1 67  ? 26.943  -54.035 2.843   1.00 33.62  ? 85  GLY B HA2  1 
ATOM   5660  H  HA3  . GLY B 1 67  ? 25.493  -53.692 2.319   1.00 33.62  ? 85  GLY B HA3  1 
ATOM   5661  N  N    . TYR B 1 68  ? 27.021  -51.303 3.714   1.00 24.63  ? 86  TYR B N    1 
ATOM   5662  C  CA   . TYR B 1 68  ? 27.535  -49.959 3.538   1.00 23.34  ? 86  TYR B CA   1 
ATOM   5663  C  C    . TYR B 1 68  ? 28.997  -49.909 3.960   1.00 23.89  ? 86  TYR B C    1 
ATOM   5664  O  O    . TYR B 1 68  ? 29.483  -50.765 4.706   1.00 24.97  ? 86  TYR B O    1 
ATOM   5665  C  CB   . TYR B 1 68  ? 26.754  -48.942 4.387   1.00 22.08  ? 86  TYR B CB   1 
ATOM   5666  C  CG   . TYR B 1 68  ? 25.299  -48.834 4.019   1.00 21.52  ? 86  TYR B CG   1 
ATOM   5667  C  CD1  . TYR B 1 68  ? 24.871  -47.936 3.050   1.00 22.14  ? 86  TYR B CD1  1 
ATOM   5668  C  CD2  . TYR B 1 68  ? 24.348  -49.647 4.626   1.00 23.56  ? 86  TYR B CD2  1 
ATOM   5669  C  CE1  . TYR B 1 68  ? 23.535  -47.852 2.696   1.00 22.86  ? 86  TYR B CE1  1 
ATOM   5670  C  CE2  . TYR B 1 68  ? 23.011  -49.564 4.286   1.00 23.13  ? 86  TYR B CE2  1 
ATOM   5671  C  CZ   . TYR B 1 68  ? 22.610  -48.670 3.318   1.00 22.83  ? 86  TYR B CZ   1 
ATOM   5672  O  OH   . TYR B 1 68  ? 21.281  -48.581 2.974   1.00 25.10  ? 86  TYR B OH   1 
ATOM   5673  H  H    . TYR B 1 68  ? 27.011  -51.564 4.534   1.00 29.55  ? 86  TYR B H    1 
ATOM   5674  H  HA   . TYR B 1 68  ? 27.460  -49.717 2.601   1.00 28.01  ? 86  TYR B HA   1 
ATOM   5675  H  HB2  . TYR B 1 68  ? 26.805  -49.208 5.318   1.00 26.50  ? 86  TYR B HB2  1 
ATOM   5676  H  HB3  . TYR B 1 68  ? 27.154  -48.066 4.270   1.00 26.50  ? 86  TYR B HB3  1 
ATOM   5677  H  HD1  . TYR B 1 68  ? 25.492  -47.383 2.633   1.00 26.57  ? 86  TYR B HD1  1 
ATOM   5678  H  HD2  . TYR B 1 68  ? 24.617  -50.258 5.273   1.00 28.27  ? 86  TYR B HD2  1 
ATOM   5679  H  HE1  . TYR B 1 68  ? 23.262  -47.249 2.043   1.00 27.43  ? 86  TYR B HE1  1 
ATOM   5680  H  HE2  . TYR B 1 68  ? 22.386  -50.108 4.708   1.00 27.76  ? 86  TYR B HE2  1 
ATOM   5681  H  HH   . TYR B 1 68  ? 21.171  -47.974 2.404   1.00 30.12  ? 86  TYR B HH   1 
ATOM   5682  N  N    . THR B 1 69  ? 29.700  -48.885 3.474   1.00 22.87  ? 87  THR B N    1 
ATOM   5683  C  CA   . THR B 1 69  ? 30.992  -48.525 4.041   1.00 23.08  ? 87  THR B CA   1 
ATOM   5684  C  C    . THR B 1 69  ? 30.741  -47.437 5.072   1.00 20.86  ? 87  THR B C    1 
ATOM   5685  O  O    . THR B 1 69  ? 30.374  -46.311 4.693   1.00 21.25  ? 87  THR B O    1 
ATOM   5686  C  CB   . THR B 1 69  ? 31.950  -48.028 2.971   1.00 23.20  ? 87  THR B CB   1 
ATOM   5687  O  OG1  . THR B 1 69  ? 32.109  -49.032 1.963   1.00 24.49  ? 87  THR B OG1  1 
ATOM   5688  C  CG2  . THR B 1 69  ? 33.319  -47.722 3.593   1.00 23.06  ? 87  THR B CG2  1 
ATOM   5689  H  H    . THR B 1 69  ? 29.448  -48.387 2.819   1.00 27.44  ? 87  THR B H    1 
ATOM   5690  H  HA   . THR B 1 69  ? 31.399  -49.299 4.461   1.00 27.70  ? 87  THR B HA   1 
ATOM   5691  H  HB   . THR B 1 69  ? 31.598  -47.218 2.568   1.00 27.85  ? 87  THR B HB   1 
ATOM   5692  H  HG1  . THR B 1 69  ? 31.373  -49.181 1.587   1.00 29.39  ? 87  THR B HG1  1 
ATOM   5693  H  HG21 . THR B 1 69  ? 33.659  -48.507 4.050   1.00 27.67  ? 87  THR B HG21 1 
ATOM   5694  H  HG22 . THR B 1 69  ? 33.948  -47.464 2.901   1.00 27.67  ? 87  THR B HG22 1 
ATOM   5695  H  HG23 . THR B 1 69  ? 33.239  -46.996 4.231   1.00 27.67  ? 87  THR B HG23 1 
ATOM   5696  N  N    . PRO B 1 70  ? 30.895  -47.714 6.365   1.00 20.48  ? 88  PRO B N    1 
ATOM   5697  C  CA   . PRO B 1 70  ? 30.692  -46.653 7.360   1.00 20.26  ? 88  PRO B CA   1 
ATOM   5698  C  C    . PRO B 1 70  ? 31.810  -45.623 7.304   1.00 19.31  ? 88  PRO B C    1 
ATOM   5699  O  O    . PRO B 1 70  ? 32.996  -45.966 7.256   1.00 20.02  ? 88  PRO B O    1 
ATOM   5700  C  CB   . PRO B 1 70  ? 30.683  -47.406 8.697   1.00 21.26  ? 88  PRO B CB   1 
ATOM   5701  C  CG   . PRO B 1 70  ? 31.460  -48.653 8.444   1.00 21.81  ? 88  PRO B CG   1 
ATOM   5702  C  CD   . PRO B 1 70  ? 31.258  -49.001 6.985   1.00 20.38  ? 88  PRO B CD   1 
ATOM   5703  H  HA   . PRO B 1 70  ? 29.836  -46.216 7.223   1.00 24.31  ? 88  PRO B HA   1 
ATOM   5704  H  HB2  . PRO B 1 70  ? 31.107  -46.866 9.382   1.00 25.51  ? 88  PRO B HB2  1 
ATOM   5705  H  HB3  . PRO B 1 70  ? 29.770  -47.612 8.954   1.00 25.51  ? 88  PRO B HB3  1 
ATOM   5706  H  HG2  . PRO B 1 70  ? 32.398  -48.493 8.629   1.00 26.18  ? 88  PRO B HG2  1 
ATOM   5707  H  HG3  . PRO B 1 70  ? 31.125  -49.364 9.013   1.00 26.18  ? 88  PRO B HG3  1 
ATOM   5708  H  HD2  . PRO B 1 70  ? 32.077  -49.350 6.599   1.00 24.46  ? 88  PRO B HD2  1 
ATOM   5709  H  HD3  . PRO B 1 70  ? 30.542  -49.647 6.882   1.00 24.46  ? 88  PRO B HD3  1 
ATOM   5710  N  N    . CYS B 1 71  ? 31.414  -44.354 7.301   1.00 18.59  ? 89  CYS B N    1 
ATOM   5711  C  CA   . CYS B 1 71  ? 32.321  -43.229 7.430   1.00 19.43  ? 89  CYS B CA   1 
ATOM   5712  C  C    . CYS B 1 71  ? 31.790  -42.330 8.539   1.00 18.15  ? 89  CYS B C    1 
ATOM   5713  O  O    . CYS B 1 71  ? 30.603  -42.360 8.866   1.00 18.63  ? 89  CYS B O    1 
ATOM   5714  C  CB   . CYS B 1 71  ? 32.397  -42.428 6.126   1.00 19.97  ? 89  CYS B CB   1 
ATOM   5715  S  SG   . CYS B 1 71  ? 32.674  -43.417 4.636   1.00 20.39  ? 89  CYS B SG   1 
ATOM   5716  H  H    . CYS B 1 71  ? 30.592  -44.114 7.223   1.00 22.31  ? 89  CYS B H    1 
ATOM   5717  H  HA   . CYS B 1 71  ? 33.214  -43.535 7.654   1.00 23.31  ? 89  CYS B HA   1 
ATOM   5718  H  HB2  . CYS B 1 71  ? 31.559  -41.953 6.008   1.00 23.96  ? 89  CYS B HB2  1 
ATOM   5719  H  HB3  . CYS B 1 71  ? 33.129  -41.796 6.195   1.00 23.96  ? 89  CYS B HB3  1 
ATOM   5720  N  N    . TRP B 1 72  ? 32.674  -41.534 9.129   1.00 18.27  ? 90  TRP B N    1 
ATOM   5721  C  CA   . TRP B 1 72  ? 32.274  -40.704 10.257  1.00 17.34  ? 90  TRP B CA   1 
ATOM   5722  C  C    . TRP B 1 72  ? 33.102  -39.429 10.287  1.00 16.74  ? 90  TRP B C    1 
ATOM   5723  O  O    . TRP B 1 72  ? 34.208  -39.366 9.742   1.00 16.73  ? 90  TRP B O    1 
ATOM   5724  C  CB   . TRP B 1 72  ? 32.436  -41.452 11.589  1.00 17.45  ? 90  TRP B CB   1 
ATOM   5725  C  CG   . TRP B 1 72  ? 33.794  -42.032 11.754  1.00 18.78  ? 90  TRP B CG   1 
ATOM   5726  C  CD1  . TRP B 1 72  ? 34.881  -41.431 12.326  1.00 18.45  ? 90  TRP B CD1  1 
ATOM   5727  C  CD2  . TRP B 1 72  ? 34.225  -43.328 11.335  1.00 20.08  ? 90  TRP B CD2  1 
ATOM   5728  N  NE1  . TRP B 1 72  ? 35.961  -42.281 12.294  1.00 20.46  ? 90  TRP B NE1  1 
ATOM   5729  C  CE2  . TRP B 1 72  ? 35.583  -43.451 11.690  1.00 20.14  ? 90  TRP B CE2  1 
ATOM   5730  C  CE3  . TRP B 1 72  ? 33.594  -44.400 10.696  1.00 20.67  ? 90  TRP B CE3  1 
ATOM   5731  C  CZ2  . TRP B 1 72  ? 36.321  -44.600 11.423  1.00 21.42  ? 90  TRP B CZ2  1 
ATOM   5732  C  CZ3  . TRP B 1 72  ? 34.329  -45.542 10.437  1.00 21.16  ? 90  TRP B CZ3  1 
ATOM   5733  C  CH2  . TRP B 1 72  ? 35.680  -45.627 10.787  1.00 21.41  ? 90  TRP B CH2  1 
ATOM   5734  H  H    . TRP B 1 72  ? 33.499  -41.458 8.899   1.00 21.92  ? 90  TRP B H    1 
ATOM   5735  H  HA   . TRP B 1 72  ? 31.343  -40.457 10.138  1.00 20.81  ? 90  TRP B HA   1 
ATOM   5736  H  HB2  . TRP B 1 72  ? 32.282  -40.833 12.320  1.00 20.94  ? 90  TRP B HB2  1 
ATOM   5737  H  HB3  . TRP B 1 72  ? 31.793  -42.177 11.626  1.00 20.94  ? 90  TRP B HB3  1 
ATOM   5738  H  HD1  . TRP B 1 72  ? 34.889  -40.573 12.684  1.00 22.14  ? 90  TRP B HD1  1 
ATOM   5739  H  HE1  . TRP B 1 72  ? 36.745  -42.107 12.602  1.00 24.55  ? 90  TRP B HE1  1 
ATOM   5740  H  HE3  . TRP B 1 72  ? 32.699  -44.345 10.450  1.00 24.81  ? 90  TRP B HE3  1 
ATOM   5741  H  HZ2  . TRP B 1 72  ? 37.216  -44.667 11.668  1.00 25.71  ? 90  TRP B HZ2  1 
ATOM   5742  H  HZ3  . TRP B 1 72  ? 33.917  -46.265 10.023  1.00 25.39  ? 90  TRP B HZ3  1 
ATOM   5743  H  HH2  . TRP B 1 72  ? 36.153  -46.401 10.583  1.00 25.69  ? 90  TRP B HH2  1 
ATOM   5744  N  N    . ILE B 1 73  ? 32.546  -38.403 10.929  1.00 16.26  ? 91  ILE B N    1 
ATOM   5745  C  CA   . ILE B 1 73  ? 33.304  -37.202 11.264  1.00 16.36  ? 91  ILE B CA   1 
ATOM   5746  C  C    . ILE B 1 73  ? 33.552  -37.178 12.767  1.00 15.73  ? 91  ILE B C    1 
ATOM   5747  O  O    . ILE B 1 73  ? 32.755  -37.692 13.560  1.00 15.98  ? 91  ILE B O    1 
ATOM   5748  C  CB   . ILE B 1 73  ? 32.627  -35.892 10.806  1.00 15.86  ? 91  ILE B CB   1 
ATOM   5749  C  CG1  . ILE B 1 73  ? 31.164  -35.842 11.244  1.00 16.31  ? 91  ILE B CG1  1 
ATOM   5750  C  CG2  . ILE B 1 73  ? 32.749  -35.751 9.304   1.00 17.15  ? 91  ILE B CG2  1 
ATOM   5751  C  CD1  . ILE B 1 73  ? 30.551  -34.470 11.123  1.00 15.75  ? 91  ILE B CD1  1 
ATOM   5752  H  H    . ILE B 1 73  ? 31.725  -38.380 11.183  1.00 19.51  ? 91  ILE B H    1 
ATOM   5753  H  HA   . ILE B 1 73  ? 34.155  -37.257 10.803  1.00 19.63  ? 91  ILE B HA   1 
ATOM   5754  H  HB   . ILE B 1 73  ? 33.081  -35.147 11.231  1.00 19.03  ? 91  ILE B HB   1 
ATOM   5755  H  HG12 . ILE B 1 73  ? 30.650  -36.448 10.687  1.00 19.57  ? 91  ILE B HG12 1 
ATOM   5756  H  HG13 . ILE B 1 73  ? 31.106  -36.114 12.173  1.00 19.57  ? 91  ILE B HG13 1 
ATOM   5757  H  HG21 . ILE B 1 73  ? 33.688  -35.691 9.067   1.00 20.58  ? 91  ILE B HG21 1 
ATOM   5758  H  HG22 . ILE B 1 73  ? 32.351  -36.528 8.880   1.00 20.58  ? 91  ILE B HG22 1 
ATOM   5759  H  HG23 . ILE B 1 73  ? 32.285  -34.947 9.023   1.00 20.58  ? 91  ILE B HG23 1 
ATOM   5760  H  HD11 . ILE B 1 73  ? 31.109  -33.832 11.595  1.00 18.90  ? 91  ILE B HD11 1 
ATOM   5761  H  HD12 . ILE B 1 73  ? 30.495  -34.230 10.185  1.00 18.90  ? 91  ILE B HD12 1 
ATOM   5762  H  HD13 . ILE B 1 73  ? 29.663  -34.486 11.514  1.00 18.90  ? 91  ILE B HD13 1 
ATOM   5763  N  N    . SER B 1 74  ? 34.657  -36.549 13.156  1.00 16.13  ? 92  SER B N    1 
ATOM   5764  C  CA   . SER B 1 74  ? 35.023  -36.367 14.560  1.00 15.96  ? 92  SER B CA   1 
ATOM   5765  C  C    . SER B 1 74  ? 35.458  -34.923 14.767  1.00 14.71  ? 92  SER B C    1 
ATOM   5766  O  O    . SER B 1 74  ? 36.648  -34.636 14.951  1.00 16.23  ? 92  SER B O    1 
ATOM   5767  C  CB   . SER B 1 74  ? 36.138  -37.330 14.965  1.00 16.25  ? 92  SER B CB   1 
ATOM   5768  O  OG   . SER B 1 74  ? 35.714  -38.678 14.839  1.00 17.55  ? 92  SER B OG   1 
ATOM   5769  H  H    . SER B 1 74  ? 35.228  -36.209 12.610  1.00 19.36  ? 92  SER B H    1 
ATOM   5770  H  HA   . SER B 1 74  ? 34.248  -36.542 15.117  1.00 19.15  ? 92  SER B HA   1 
ATOM   5771  H  HB2  . SER B 1 74  ? 36.904  -37.185 14.389  1.00 19.50  ? 92  SER B HB2  1 
ATOM   5772  H  HB3  . SER B 1 74  ? 36.380  -37.161 15.889  1.00 19.50  ? 92  SER B HB3  1 
ATOM   5773  H  HG   . SER B 1 74  ? 36.223  -39.181 15.278  1.00 21.06  ? 92  SER B HG   1 
ATOM   5774  N  N    . PRO B 1 75  ? 34.520  -33.983 14.736  1.00 14.61  ? 93  PRO B N    1 
ATOM   5775  C  CA   . PRO B 1 75  ? 34.886  -32.577 14.934  1.00 14.81  ? 93  PRO B CA   1 
ATOM   5776  C  C    . PRO B 1 75  ? 35.493  -32.372 16.309  1.00 15.15  ? 93  PRO B C    1 
ATOM   5777  O  O    . PRO B 1 75  ? 34.943  -32.845 17.313  1.00 16.66  ? 93  PRO B O    1 
ATOM   5778  C  CB   . PRO B 1 75  ? 33.542  -31.842 14.813  1.00 15.53  ? 93  PRO B CB   1 
ATOM   5779  C  CG   . PRO B 1 75  ? 32.675  -32.765 14.002  1.00 14.83  ? 93  PRO B CG   1 
ATOM   5780  C  CD   . PRO B 1 75  ? 33.081  -34.143 14.450  1.00 15.19  ? 93  PRO B CD   1 
ATOM   5781  H  HA   . PRO B 1 75  ? 35.497  -32.271 14.245  1.00 17.77  ? 93  PRO B HA   1 
ATOM   5782  H  HB2  . PRO B 1 75  ? 33.164  -31.694 15.694  1.00 18.63  ? 93  PRO B HB2  1 
ATOM   5783  H  HB3  . PRO B 1 75  ? 33.667  -30.993 14.359  1.00 18.63  ? 93  PRO B HB3  1 
ATOM   5784  H  HG2  . PRO B 1 75  ? 31.739  -32.597 14.193  1.00 17.79  ? 93  PRO B HG2  1 
ATOM   5785  H  HG3  . PRO B 1 75  ? 32.849  -32.640 13.056  1.00 17.79  ? 93  PRO B HG3  1 
ATOM   5786  H  HD2  . PRO B 1 75  ? 32.596  -34.405 15.248  1.00 18.23  ? 93  PRO B HD2  1 
ATOM   5787  H  HD3  . PRO B 1 75  ? 32.937  -34.794 13.745  1.00 18.23  ? 93  PRO B HD3  1 
ATOM   5788  N  N    . PRO B 1 76  ? 36.621  -31.675 16.399  1.00 15.80  ? 94  PRO B N    1 
ATOM   5789  C  CA   . PRO B 1 76  ? 37.279  -31.491 17.699  1.00 15.96  ? 94  PRO B CA   1 
ATOM   5790  C  C    . PRO B 1 76  ? 36.728  -30.281 18.428  1.00 15.25  ? 94  PRO B C    1 
ATOM   5791  O  O    . PRO B 1 76  ? 36.191  -29.358 17.799  1.00 15.59  ? 94  PRO B O    1 
ATOM   5792  C  CB   . PRO B 1 76  ? 38.743  -31.259 17.304  1.00 16.98  ? 94  PRO B CB   1 
ATOM   5793  C  CG   . PRO B 1 76  ? 38.648  -30.549 16.001  1.00 17.44  ? 94  PRO B CG   1 
ATOM   5794  C  CD   . PRO B 1 76  ? 37.450  -31.158 15.291  1.00 16.42  ? 94  PRO B CD   1 
ATOM   5795  H  HA   . PRO B 1 76  ? 37.188  -32.283 18.252  1.00 19.15  ? 94  PRO B HA   1 
ATOM   5796  H  HB2  . PRO B 1 76  ? 39.188  -30.713 17.971  1.00 20.38  ? 94  PRO B HB2  1 
ATOM   5797  H  HB3  . PRO B 1 76  ? 39.203  -32.108 17.210  1.00 20.38  ? 94  PRO B HB3  1 
ATOM   5798  H  HG2  . PRO B 1 76  ? 38.513  -29.600 16.153  1.00 20.93  ? 94  PRO B HG2  1 
ATOM   5799  H  HG3  . PRO B 1 76  ? 39.460  -30.690 15.490  1.00 20.93  ? 94  PRO B HG3  1 
ATOM   5800  H  HD2  . PRO B 1 76  ? 36.969  -30.484 14.786  1.00 19.71  ? 94  PRO B HD2  1 
ATOM   5801  H  HD3  . PRO B 1 76  ? 37.727  -31.878 14.703  1.00 19.71  ? 94  PRO B HD3  1 
ATOM   5802  N  N    . PRO B 1 77  ? 36.821  -30.247 19.768  1.00 14.70  ? 95  PRO B N    1 
ATOM   5803  C  CA   . PRO B 1 77  ? 37.195  -31.349 20.653  1.00 14.78  ? 95  PRO B CA   1 
ATOM   5804  C  C    . PRO B 1 77  ? 35.921  -32.101 21.017  1.00 15.26  ? 95  PRO B C    1 
ATOM   5805  O  O    . PRO B 1 77  ? 35.063  -31.549 21.699  1.00 15.73  ? 95  PRO B O    1 
ATOM   5806  C  CB   . PRO B 1 77  ? 37.800  -30.631 21.862  1.00 16.15  ? 95  PRO B CB   1 
ATOM   5807  C  CG   . PRO B 1 77  ? 37.044  -29.346 21.947  1.00 15.91  ? 95  PRO B CG   1 
ATOM   5808  C  CD   . PRO B 1 77  ? 36.521  -29.024 20.538  1.00 15.67  ? 95  PRO B CD   1 
ATOM   5809  H  HA   . PRO B 1 77  ? 37.874  -31.943 20.295  1.00 17.74  ? 95  PRO B HA   1 
ATOM   5810  H  HB2  . PRO B 1 77  ? 37.675  -31.164 22.663  1.00 19.38  ? 95  PRO B HB2  1 
ATOM   5811  H  HB3  . PRO B 1 77  ? 38.746  -30.471 21.715  1.00 19.38  ? 95  PRO B HB3  1 
ATOM   5812  H  HG2  . PRO B 1 77  ? 36.305  -29.450 22.566  1.00 19.09  ? 95  PRO B HG2  1 
ATOM   5813  H  HG3  . PRO B 1 77  ? 37.639  -28.644 22.255  1.00 19.09  ? 95  PRO B HG3  1 
ATOM   5814  H  HD2  . PRO B 1 77  ? 35.566  -28.854 20.556  1.00 18.81  ? 95  PRO B HD2  1 
ATOM   5815  H  HD3  . PRO B 1 77  ? 36.986  -28.259 20.164  1.00 18.81  ? 95  PRO B HD3  1 
ATOM   5816  N  N    . PHE B 1 78  ? 35.774  -33.330 20.526  1.00 15.63  ? 96  PHE B N    1 
ATOM   5817  C  CA   . PHE B 1 78  ? 34.698  -34.210 20.972  1.00 15.87  ? 96  PHE B CA   1 
ATOM   5818  C  C    . PHE B 1 78  ? 33.317  -33.568 20.844  1.00 15.12  ? 96  PHE B C    1 
ATOM   5819  O  O    . PHE B 1 78  ? 32.474  -33.684 21.735  1.00 15.32  ? 96  PHE B O    1 
ATOM   5820  C  CB   . PHE B 1 78  ? 34.956  -34.655 22.412  1.00 17.13  ? 96  PHE B CB   1 
ATOM   5821  C  CG   . PHE B 1 78  ? 36.317  -35.238 22.622  1.00 20.36  ? 96  PHE B CG   1 
ATOM   5822  C  CD1  . PHE B 1 78  ? 37.315  -34.507 23.238  1.00 20.99  ? 96  PHE B CD1  1 
ATOM   5823  C  CD2  . PHE B 1 78  ? 36.603  -36.519 22.185  1.00 23.04  ? 96  PHE B CD2  1 
ATOM   5824  C  CE1  . PHE B 1 78  ? 38.570  -35.050 23.420  1.00 23.63  ? 96  PHE B CE1  1 
ATOM   5825  C  CE2  . PHE B 1 78  ? 37.858  -37.068 22.373  1.00 25.17  ? 96  PHE B CE2  1 
ATOM   5826  C  CZ   . PHE B 1 78  ? 38.840  -36.333 22.987  1.00 25.08  ? 96  PHE B CZ   1 
ATOM   5827  H  H    . PHE B 1 78  ? 36.288  -33.678 19.930  1.00 18.76  ? 96  PHE B H    1 
ATOM   5828  H  HA   . PHE B 1 78  ? 34.688  -34.986 20.390  1.00 19.05  ? 96  PHE B HA   1 
ATOM   5829  H  HB2  . PHE B 1 78  ? 34.869  -33.887 22.998  1.00 20.56  ? 96  PHE B HB2  1 
ATOM   5830  H  HB3  . PHE B 1 78  ? 34.304  -35.331 22.652  1.00 20.56  ? 96  PHE B HB3  1 
ATOM   5831  H  HD1  . PHE B 1 78  ? 37.139  -33.642 23.532  1.00 25.18  ? 96  PHE B HD1  1 
ATOM   5832  H  HD2  . PHE B 1 78  ? 35.943  -37.017 21.759  1.00 27.64  ? 96  PHE B HD2  1 
ATOM   5833  H  HE1  . PHE B 1 78  ? 39.236  -34.551 23.837  1.00 28.35  ? 96  PHE B HE1  1 
ATOM   5834  H  HE2  . PHE B 1 78  ? 38.036  -37.934 22.084  1.00 30.20  ? 96  PHE B HE2  1 
ATOM   5835  H  HZ   . PHE B 1 78  ? 39.687  -36.697 23.110  1.00 30.09  ? 96  PHE B HZ   1 
ATOM   5836  N  N    . MET B 1 79  ? 33.068  -32.895 19.719  1.00 13.71  ? 97  MET B N    1 
ATOM   5837  C  CA   . MET B 1 79  ? 31.761  -32.307 19.424  1.00 14.18  ? 97  MET B CA   1 
ATOM   5838  C  C    . MET B 1 79  ? 31.347  -31.247 20.443  1.00 14.01  ? 97  MET B C    1 
ATOM   5839  O  O    . MET B 1 79  ? 30.159  -30.901 20.537  1.00 14.47  ? 97  MET B O    1 
ATOM   5840  C  CB   . MET B 1 79  ? 30.666  -33.373 19.296  1.00 14.49  ? 97  MET B CB   1 
ATOM   5841  C  CG   . MET B 1 79  ? 30.764  -34.241 18.043  1.00 15.39  ? 97  MET B CG   1 
ATOM   5842  S  SD   . MET B 1 79  ? 30.302  -33.395 16.516  1.00 15.52  ? 97  MET B SD   1 
ATOM   5843  C  CE   . MET B 1 79  ? 28.527  -33.364 16.688  1.00 15.61  ? 97  MET B CE   1 
ATOM   5844  H  H    . MET B 1 79  ? 33.652  -32.765 19.101  1.00 16.45  ? 97  MET B H    1 
ATOM   5845  H  HA   . MET B 1 79  ? 31.839  -31.871 18.561  1.00 17.02  ? 97  MET B HA   1 
ATOM   5846  H  HB2  . MET B 1 79  ? 30.719  -33.962 20.064  1.00 17.38  ? 97  MET B HB2  1 
ATOM   5847  H  HB3  . MET B 1 79  ? 29.804  -32.929 19.277  1.00 17.38  ? 97  MET B HB3  1 
ATOM   5848  H  HG2  . MET B 1 79  ? 31.680  -34.543 17.945  1.00 18.47  ? 97  MET B HG2  1 
ATOM   5849  H  HG3  . MET B 1 79  ? 30.173  -35.003 18.147  1.00 18.47  ? 97  MET B HG3  1 
ATOM   5850  H  HE1  . MET B 1 79  ? 28.303  -33.130 17.602  1.00 18.73  ? 97  MET B HE1  1 
ATOM   5851  H  HE2  . MET B 1 79  ? 28.174  -34.242 16.475  1.00 18.73  ? 97  MET B HE2  1 
ATOM   5852  H  HE3  . MET B 1 79  ? 28.162  -32.704 16.079  1.00 18.73  ? 97  MET B HE3  1 
ATOM   5853  N  N    . LEU B 1 80  ? 32.307  -30.684 21.183  1.00 13.56  ? 98  LEU B N    1 
ATOM   5854  C  CA   . LEU B 1 80  ? 32.006  -29.673 22.185  1.00 13.75  ? 98  LEU B CA   1 
ATOM   5855  C  C    . LEU B 1 80  ? 32.108  -28.248 21.654  1.00 14.22  ? 98  LEU B C    1 
ATOM   5856  O  O    . LEU B 1 80  ? 31.597  -27.321 22.299  1.00 14.80  ? 98  LEU B O    1 
ATOM   5857  C  CB   . LEU B 1 80  ? 32.941  -29.840 23.384  1.00 14.00  ? 98  LEU B CB   1 
ATOM   5858  C  CG   . LEU B 1 80  ? 32.780  -31.158 24.142  1.00 15.42  ? 98  LEU B CG   1 
ATOM   5859  C  CD1  . LEU B 1 80  ? 33.872  -31.287 25.177  1.00 16.31  ? 98  LEU B CD1  1 
ATOM   5860  C  CD2  . LEU B 1 80  ? 31.406  -31.243 24.786  1.00 17.81  ? 98  LEU B CD2  1 
ATOM   5861  H  H    . LEU B 1 80  ? 33.143  -30.876 21.119  1.00 16.27  ? 98  LEU B H    1 
ATOM   5862  H  HA   . LEU B 1 80  ? 31.095  -29.800 22.493  1.00 16.51  ? 98  LEU B HA   1 
ATOM   5863  H  HB2  . LEU B 1 80  ? 33.857  -29.794 23.068  1.00 16.81  ? 98  LEU B HB2  1 
ATOM   5864  H  HB3  . LEU B 1 80  ? 32.769  -29.120 24.010  1.00 16.81  ? 98  LEU B HB3  1 
ATOM   5865  H  HG   . LEU B 1 80  ? 32.856  -31.901 23.523  1.00 18.51  ? 98  LEU B HG   1 
ATOM   5866  H  HD11 . LEU B 1 80  ? 33.738  -32.107 25.677  1.00 19.58  ? 98  LEU B HD11 1 
ATOM   5867  H  HD12 . LEU B 1 80  ? 34.731  -31.310 24.728  1.00 19.58  ? 98  LEU B HD12 1 
ATOM   5868  H  HD13 . LEU B 1 80  ? 33.832  -30.525 25.775  1.00 19.58  ? 98  LEU B HD13 1 
ATOM   5869  H  HD21 . LEU B 1 80  ? 31.377  -32.018 25.368  1.00 21.37  ? 98  LEU B HD21 1 
ATOM   5870  H  HD22 . LEU B 1 80  ? 31.248  -30.436 25.301  1.00 21.37  ? 98  LEU B HD22 1 
ATOM   5871  H  HD23 . LEU B 1 80  ? 30.736  -31.327 24.090  1.00 21.37  ? 98  LEU B HD23 1 
ATOM   5872  N  N    . ASN B 1 81  ? 32.758  -28.049 20.512  1.00 13.86  ? 99  ASN B N    1 
ATOM   5873  C  CA   . ASN B 1 81  ? 32.810  -26.730 19.903  1.00 14.19  ? 99  ASN B CA   1 
ATOM   5874  C  C    . ASN B 1 81  ? 31.466  -26.390 19.258  1.00 13.68  ? 99  ASN B C    1 
ATOM   5875  O  O    . ASN B 1 81  ? 30.588  -27.240 19.080  1.00 14.12  ? 99  ASN B O    1 
ATOM   5876  C  CB   . ASN B 1 81  ? 33.902  -26.678 18.831  1.00 16.78  ? 99  ASN B CB   1 
ATOM   5877  C  CG   . ASN B 1 81  ? 34.314  -25.261 18.465  1.00 19.69  ? 99  ASN B CG   1 
ATOM   5878  O  OD1  . ASN B 1 81  ? 33.999  -24.300 19.172  1.00 22.11  ? 99  ASN B OD1  1 
ATOM   5879  N  ND2  . ASN B 1 81  ? 35.032  -25.126 17.350  1.00 22.01  ? 99  ASN B ND2  1 
ATOM   5880  H  H    . ASN B 1 81  ? 33.175  -28.660 20.073  1.00 16.63  ? 99  ASN B H    1 
ATOM   5881  H  HA   . ASN B 1 81  ? 33.009  -26.075 20.590  1.00 17.03  ? 99  ASN B HA   1 
ATOM   5882  H  HB2  . ASN B 1 81  ? 34.689  -27.141 19.160  1.00 20.13  ? 99  ASN B HB2  1 
ATOM   5883  H  HB3  . ASN B 1 81  ? 33.575  -27.111 18.026  1.00 20.13  ? 99  ASN B HB3  1 
ATOM   5884  H  HD21 . ASN B 1 81  ? 35.237  -25.819 16.884  1.00 26.41  ? 99  ASN B HD21 1 
ATOM   5885  H  HD22 . ASN B 1 81  ? 35.291  -24.346 17.097  1.00 26.41  ? 99  ASN B HD22 1 
ATOM   5886  N  N    . ASP B 1 82  ? 31.325  -25.108 18.922  1.00 14.14  ? 100 ASP B N    1 
ATOM   5887  C  CA   . ASP B 1 82  ? 30.248  -24.540 18.120  1.00 13.89  ? 100 ASP B CA   1 
ATOM   5888  C  C    . ASP B 1 82  ? 29.636  -25.547 17.163  1.00 12.78  ? 100 ASP B C    1 
ATOM   5889  O  O    . ASP B 1 82  ? 30.308  -26.044 16.252  1.00 13.46  ? 100 ASP B O    1 
ATOM   5890  C  CB   . ASP B 1 82  ? 30.870  -23.370 17.344  1.00 12.71  ? 100 ASP B CB   1 
ATOM   5891  C  CG   . ASP B 1 82  ? 29.862  -22.513 16.574  1.00 14.39  ? 100 ASP B CG   1 
ATOM   5892  O  OD1  . ASP B 1 82  ? 28.660  -22.839 16.524  1.00 14.10  ? 100 ASP B OD1  1 
ATOM   5893  O  OD2  . ASP B 1 82  ? 30.309  -21.481 16.012  1.00 16.70  ? 100 ASP B OD2  1 
ATOM   5894  H  H    . ASP B 1 82  ? 31.884  -24.502 19.165  1.00 16.97  ? 100 ASP B H    1 
ATOM   5895  H  HA   . ASP B 1 82  ? 29.516  -24.248 18.686  1.00 16.67  ? 100 ASP B HA   1 
ATOM   5896  H  HB2  . ASP B 1 82  ? 31.327  -22.790 17.973  1.00 15.26  ? 100 ASP B HB2  1 
ATOM   5897  H  HB3  . ASP B 1 82  ? 31.503  -23.726 16.702  1.00 15.26  ? 100 ASP B HB3  1 
ATOM   5898  N  N    . THR B 1 83  ? 28.347  -25.834 17.367  1.00 12.75  ? 101 THR B N    1 
ATOM   5899  C  CA   . THR B 1 83  ? 27.609  -26.723 16.478  1.00 13.63  ? 101 THR B CA   1 
ATOM   5900  C  C    . THR B 1 83  ? 27.694  -26.276 15.026  1.00 12.23  ? 101 THR B C    1 
ATOM   5901  O  O    . THR B 1 83  ? 27.638  -27.113 14.116  1.00 12.73  ? 101 THR B O    1 
ATOM   5902  C  CB   . THR B 1 83  ? 26.151  -26.784 16.951  1.00 14.91  ? 101 THR B CB   1 
ATOM   5903  O  OG1  . THR B 1 83  ? 26.099  -27.379 18.257  1.00 14.74  ? 101 THR B OG1  1 
ATOM   5904  C  CG2  . THR B 1 83  ? 25.267  -27.565 15.968  1.00 16.15  ? 101 THR B CG2  1 
ATOM   5905  H  H    . THR B 1 83  ? 27.877  -25.523 18.017  1.00 15.30  ? 101 THR B H    1 
ATOM   5906  H  HA   . THR B 1 83  ? 27.986  -27.616 16.518  1.00 16.35  ? 101 THR B HA   1 
ATOM   5907  H  HB   . THR B 1 83  ? 25.792  -25.884 16.994  1.00 17.89  ? 101 THR B HB   1 
ATOM   5908  H  HG1  . THR B 1 83  ? 26.461  -28.136 18.242  1.00 17.68  ? 101 THR B HG1  1 
ATOM   5909  H  HG21 . THR B 1 83  ? 24.461  -27.867 16.414  1.00 19.38  ? 101 THR B HG21 1 
ATOM   5910  H  HG22 . THR B 1 83  ? 25.020  -26.998 15.221  1.00 19.38  ? 101 THR B HG22 1 
ATOM   5911  H  HG23 . THR B 1 83  ? 25.748  -28.337 15.630  1.00 19.38  ? 101 THR B HG23 1 
ATOM   5912  N  N    . GLN B 1 84  ? 27.820  -24.969 14.784  1.00 11.94  ? 102 GLN B N    1 
ATOM   5913  C  CA   . GLN B 1 84  ? 27.941  -24.491 13.411  1.00 12.87  ? 102 GLN B CA   1 
ATOM   5914  C  C    . GLN B 1 84  ? 29.255  -24.932 12.780  1.00 12.63  ? 102 GLN B C    1 
ATOM   5915  O  O    . GLN B 1 84  ? 29.305  -25.190 11.571  1.00 13.03  ? 102 GLN B O    1 
ATOM   5916  C  CB   . GLN B 1 84  ? 27.820  -22.969 13.382  1.00 12.67  ? 102 GLN B CB   1 
ATOM   5917  C  CG   . GLN B 1 84  ? 26.494  -22.454 13.914  1.00 13.71  ? 102 GLN B CG   1 
ATOM   5918  C  CD   . GLN B 1 84  ? 26.506  -20.965 14.159  1.00 13.36  ? 102 GLN B CD   1 
ATOM   5919  O  OE1  . GLN B 1 84  ? 25.818  -20.205 13.475  1.00 14.64  ? 102 GLN B OE1  1 
ATOM   5920  N  NE2  . GLN B 1 84  ? 27.284  -20.537 15.146  1.00 14.17  ? 102 GLN B NE2  1 
ATOM   5921  H  H    . GLN B 1 84  ? 27.838  -24.353 15.385  1.00 14.33  ? 102 GLN B H    1 
ATOM   5922  H  HA   . GLN B 1 84  ? 27.217  -24.862 12.882  1.00 15.44  ? 102 GLN B HA   1 
ATOM   5923  H  HB2  . GLN B 1 84  ? 28.526  -22.589 13.927  1.00 15.20  ? 102 GLN B HB2  1 
ATOM   5924  H  HB3  . GLN B 1 84  ? 27.909  -22.666 12.464  1.00 15.20  ? 102 GLN B HB3  1 
ATOM   5925  H  HG2  . GLN B 1 84  ? 25.797  -22.647 13.268  1.00 16.45  ? 102 GLN B HG2  1 
ATOM   5926  H  HG3  . GLN B 1 84  ? 26.297  -22.895 14.755  1.00 16.45  ? 102 GLN B HG3  1 
ATOM   5927  H  HE21 . GLN B 1 84  ? 27.745  -21.100 15.605  1.00 17.00  ? 102 GLN B HE21 1 
ATOM   5928  H  HE22 . GLN B 1 84  ? 27.327  -19.698 15.327  1.00 17.00  ? 102 GLN B HE22 1 
ATOM   5929  N  N    . VAL B 1 85  ? 30.325  -25.018 13.575  1.00 13.24  ? 103 VAL B N    1 
ATOM   5930  C  CA   . VAL B 1 85  ? 31.591  -25.540 13.067  1.00 14.94  ? 103 VAL B CA   1 
ATOM   5931  C  C    . VAL B 1 85  ? 31.498  -27.044 12.856  1.00 14.10  ? 103 VAL B C    1 
ATOM   5932  O  O    . VAL B 1 85  ? 31.965  -27.575 11.839  1.00 13.69  ? 103 VAL B O    1 
ATOM   5933  C  CB   . VAL B 1 85  ? 32.749  -25.152 14.002  1.00 16.20  ? 103 VAL B CB   1 
ATOM   5934  C  CG1  . VAL B 1 85  ? 34.036  -25.810 13.536  1.00 17.04  ? 103 VAL B CG1  1 
ATOM   5935  C  CG2  . VAL B 1 85  ? 32.901  -23.634 14.055  1.00 17.32  ? 103 VAL B CG2  1 
ATOM   5936  H  H    . VAL B 1 85  ? 30.342  -24.784 14.402  1.00 15.89  ? 103 VAL B H    1 
ATOM   5937  H  HA   . VAL B 1 85  ? 31.769  -25.134 12.204  1.00 17.93  ? 103 VAL B HA   1 
ATOM   5938  H  HB   . VAL B 1 85  ? 32.558  -25.464 14.900  1.00 19.44  ? 103 VAL B HB   1 
ATOM   5939  H  HG11 . VAL B 1 85  ? 34.786  -25.392 13.988  1.00 20.44  ? 103 VAL B HG11 1 
ATOM   5940  H  HG12 . VAL B 1 85  ? 34.004  -26.755 13.753  1.00 20.44  ? 103 VAL B HG12 1 
ATOM   5941  H  HG13 . VAL B 1 85  ? 34.121  -25.693 12.577  1.00 20.44  ? 103 VAL B HG13 1 
ATOM   5942  H  HG21 . VAL B 1 85  ? 32.866  -23.281 13.152  1.00 20.79  ? 103 VAL B HG21 1 
ATOM   5943  H  HG22 . VAL B 1 85  ? 32.177  -23.262 14.583  1.00 20.79  ? 103 VAL B HG22 1 
ATOM   5944  H  HG23 . VAL B 1 85  ? 33.754  -23.415 14.462  1.00 20.79  ? 103 VAL B HG23 1 
ATOM   5945  N  N    . ASN B 1 86  ? 30.882  -27.755 13.806  1.00 14.04  ? 104 ASN B N    1 
ATOM   5946  C  CA   . ASN B 1 86  ? 30.679  -29.192 13.638  1.00 14.23  ? 104 ASN B CA   1 
ATOM   5947  C  C    . ASN B 1 86  ? 29.939  -29.476 12.343  1.00 14.07  ? 104 ASN B C    1 
ATOM   5948  O  O    . ASN B 1 86  ? 30.228  -30.461 11.653  1.00 14.35  ? 104 ASN B O    1 
ATOM   5949  C  CB   . ASN B 1 86  ? 29.905  -29.740 14.833  1.00 14.23  ? 104 ASN B CB   1 
ATOM   5950  C  CG   . ASN B 1 86  ? 30.628  -29.496 16.148  1.00 14.41  ? 104 ASN B CG   1 
ATOM   5951  O  OD1  . ASN B 1 86  ? 31.835  -29.249 16.168  1.00 16.05  ? 104 ASN B OD1  1 
ATOM   5952  N  ND2  . ASN B 1 86  ? 29.894  -29.558 17.251  1.00 13.84  ? 104 ASN B ND2  1 
ATOM   5953  H  H    . ASN B 1 86  ? 30.579  -27.434 14.544  1.00 16.85  ? 104 ASN B H    1 
ATOM   5954  H  HA   . ASN B 1 86  ? 31.537  -29.642 13.602  1.00 17.08  ? 104 ASN B HA   1 
ATOM   5955  H  HB2  . ASN B 1 86  ? 29.039  -29.305 14.878  1.00 17.08  ? 104 ASN B HB2  1 
ATOM   5956  H  HB3  . ASN B 1 86  ? 29.790  -30.697 14.725  1.00 17.08  ? 104 ASN B HB3  1 
ATOM   5957  H  HD21 . ASN B 1 86  ? 30.259  -29.426 18.018  1.00 16.61  ? 104 ASN B HD21 1 
ATOM   5958  H  HD22 . ASN B 1 86  ? 29.053  -29.730 17.199  1.00 16.61  ? 104 ASN B HD22 1 
ATOM   5959  N  N    . THR B 1 87  ? 29.005  -28.595 11.978  1.00 13.03  ? 105 THR B N    1 
ATOM   5960  C  CA   . THR B 1 87  ? 28.248  -28.786 10.751  1.00 13.59  ? 105 THR B CA   1 
ATOM   5961  C  C    . THR B 1 87  ? 29.124  -28.612 9.517   1.00 12.97  ? 105 THR B C    1 
ATOM   5962  O  O    . THR B 1 87  ? 28.904  -29.292 8.512   1.00 13.60  ? 105 THR B O    1 
ATOM   5963  C  CB   . THR B 1 87  ? 27.062  -27.825 10.724  1.00 14.06  ? 105 THR B CB   1 
ATOM   5964  O  OG1  . THR B 1 87  ? 26.197  -28.114 11.829  1.00 14.61  ? 105 THR B OG1  1 
ATOM   5965  C  CG2  . THR B 1 87  ? 26.294  -27.977 9.431   1.00 14.61  ? 105 THR B CG2  1 
ATOM   5966  H  H    . THR B 1 87  ? 28.796  -27.888 12.420  1.00 15.64  ? 105 THR B H    1 
ATOM   5967  H  HA   . THR B 1 87  ? 27.897  -29.690 10.729  1.00 16.31  ? 105 THR B HA   1 
ATOM   5968  H  HB   . THR B 1 87  ? 27.376  -26.909 10.787  1.00 16.87  ? 105 THR B HB   1 
ATOM   5969  H  HG1  . THR B 1 87  ? 25.512  -27.629 11.793  1.00 17.53  ? 105 THR B HG1  1 
ATOM   5970  H  HG21 . THR B 1 87  ? 26.783  -27.563 8.703   1.00 17.53  ? 105 THR B HG21 1 
ATOM   5971  H  HG22 . THR B 1 87  ? 26.166  -28.917 9.229   1.00 17.53  ? 105 THR B HG22 1 
ATOM   5972  H  HG23 . THR B 1 87  ? 25.426  -27.551 9.509   1.00 17.53  ? 105 THR B HG23 1 
ATOM   5973  N  N    . GLU B 1 88  ? 30.117  -27.718 9.564   1.00 13.26  ? 106 GLU B N    1 
ATOM   5974  C  CA   . GLU B 1 88  ? 31.025  -27.600 8.424   1.00 13.62  ? 106 GLU B CA   1 
ATOM   5975  C  C    . GLU B 1 88  ? 31.685  -28.942 8.118   1.00 14.68  ? 106 GLU B C    1 
ATOM   5976  O  O    . GLU B 1 88  ? 31.851  -29.317 6.948   1.00 14.04  ? 106 GLU B O    1 
ATOM   5977  C  CB   . GLU B 1 88  ? 32.100  -26.551 8.701   1.00 14.94  ? 106 GLU B CB   1 
ATOM   5978  C  CG   . GLU B 1 88  ? 31.583  -25.164 9.022   1.00 15.92  ? 106 GLU B CG   1 
ATOM   5979  C  CD   . GLU B 1 88  ? 32.699  -24.131 9.127   1.00 18.70  ? 106 GLU B CD   1 
ATOM   5980  O  OE1  . GLU B 1 88  ? 33.851  -24.432 8.753   1.00 19.76  ? 106 GLU B OE1  1 
ATOM   5981  O  OE2  . GLU B 1 88  ? 32.421  -23.013 9.595   1.00 21.59  ? 106 GLU B OE2  1 
ATOM   5982  H  H    . GLU B 1 88  ? 30.281  -27.188 10.221  1.00 15.91  ? 106 GLU B H    1 
ATOM   5983  H  HA   . GLU B 1 88  ? 30.512  -27.313 7.652   1.00 16.35  ? 106 GLU B HA   1 
ATOM   5984  H  HB2  . GLU B 1 88  ? 32.627  -26.847 9.459   1.00 17.93  ? 106 GLU B HB2  1 
ATOM   5985  H  HB3  . GLU B 1 88  ? 32.662  -26.476 7.914   1.00 17.93  ? 106 GLU B HB3  1 
ATOM   5986  H  HG2  . GLU B 1 88  ? 30.977  -24.881 8.320   1.00 19.10  ? 106 GLU B HG2  1 
ATOM   5987  H  HG3  . GLU B 1 88  ? 31.117  -25.189 9.872   1.00 19.10  ? 106 GLU B HG3  1 
ATOM   5988  N  N    . TYR B 1 89  ? 32.082  -29.675 9.163   1.00 14.18  ? 107 TYR B N    1 
ATOM   5989  C  CA   . TYR B 1 89  ? 32.658  -30.998 8.957   1.00 14.95  ? 107 TYR B CA   1 
ATOM   5990  C  C    . TYR B 1 89  ? 31.679  -31.906 8.231   1.00 14.90  ? 107 TYR B C    1 
ATOM   5991  O  O    . TYR B 1 89  ? 32.070  -32.682 7.355   1.00 15.09  ? 107 TYR B O    1 
ATOM   5992  C  CB   . TYR B 1 89  ? 33.033  -31.624 10.302  1.00 15.64  ? 107 TYR B CB   1 
ATOM   5993  C  CG   . TYR B 1 89  ? 34.331  -31.116 10.880  1.00 14.83  ? 107 TYR B CG   1 
ATOM   5994  C  CD1  . TYR B 1 89  ? 34.350  -30.009 11.712  1.00 14.87  ? 107 TYR B CD1  1 
ATOM   5995  C  CD2  . TYR B 1 89  ? 35.537  -31.746 10.596  1.00 14.96  ? 107 TYR B CD2  1 
ATOM   5996  C  CE1  . TYR B 1 89  ? 35.531  -29.533 12.245  1.00 15.31  ? 107 TYR B CE1  1 
ATOM   5997  C  CE2  . TYR B 1 89  ? 36.728  -31.276 11.120  1.00 14.19  ? 107 TYR B CE2  1 
ATOM   5998  C  CZ   . TYR B 1 89  ? 36.718  -30.171 11.954  1.00 15.53  ? 107 TYR B CZ   1 
ATOM   5999  O  OH   . TYR B 1 89  ? 37.895  -29.695 12.483  1.00 17.51  ? 107 TYR B OH   1 
ATOM   6000  H  H    . TYR B 1 89  ? 32.028  -29.431 9.986   1.00 17.01  ? 107 TYR B H    1 
ATOM   6001  H  HA   . TYR B 1 89  ? 33.462  -30.906 8.423   1.00 17.94  ? 107 TYR B HA   1 
ATOM   6002  H  HB2  . TYR B 1 89  ? 32.330  -31.429 10.942  1.00 18.77  ? 107 TYR B HB2  1 
ATOM   6003  H  HB3  . TYR B 1 89  ? 33.118  -32.583 10.185  1.00 18.77  ? 107 TYR B HB3  1 
ATOM   6004  H  HD1  . TYR B 1 89  ? 33.551  -29.578 11.915  1.00 17.84  ? 107 TYR B HD1  1 
ATOM   6005  H  HD2  . TYR B 1 89  ? 35.543  -32.495 10.045  1.00 17.96  ? 107 TYR B HD2  1 
ATOM   6006  H  HE1  . TYR B 1 89  ? 35.526  -28.786 12.799  1.00 18.38  ? 107 TYR B HE1  1 
ATOM   6007  H  HE2  . TYR B 1 89  ? 37.530  -31.700 10.914  1.00 17.03  ? 107 TYR B HE2  1 
ATOM   6008  H  HH   . TYR B 1 89  ? 38.540  -30.160 12.212  1.00 21.01  ? 107 TYR B HH   1 
ATOM   6009  N  N    . MET B 1 90  ? 30.398  -31.820 8.579   1.00 14.87  ? 108 MET B N    1 
ATOM   6010  C  CA   . MET B 1 90  ? 29.413  -32.697 7.962   1.00 15.01  ? 108 MET B CA   1 
ATOM   6011  C  C    . MET B 1 90  ? 29.157  -32.315 6.508   1.00 15.29  ? 108 MET B C    1 
ATOM   6012  O  O    . MET B 1 90  ? 29.109  -33.181 5.625   1.00 15.79  ? 108 MET B O    1 
ATOM   6013  C  CB   . MET B 1 90  ? 28.116  -32.675 8.764   1.00 16.11  ? 108 MET B CB   1 
ATOM   6014  C  CG   . MET B 1 90  ? 27.208  -33.845 8.403   1.00 17.03  ? 108 MET B CG   1 
ATOM   6015  S  SD   . MET B 1 90  ? 25.470  -33.496 8.544   1.00 20.38  ? 108 MET B SD   1 
ATOM   6016  C  CE   . MET B 1 90  ? 25.459  -32.158 7.373   1.00 12.44  ? 108 MET B CE   1 
ATOM   6017  H  H    . MET B 1 90  ? 30.079  -31.272 9.160   1.00 17.84  ? 108 MET B H    1 
ATOM   6018  H  HA   . MET B 1 90  ? 29.759  -33.603 7.983   1.00 18.02  ? 108 MET B HA   1 
ATOM   6019  H  HB2  . MET B 1 90  ? 28.325  -32.731 9.710   1.00 19.33  ? 108 MET B HB2  1 
ATOM   6020  H  HB3  . MET B 1 90  ? 27.640  -31.850 8.578   1.00 19.33  ? 108 MET B HB3  1 
ATOM   6021  H  HG2  . MET B 1 90  ? 27.382  -34.100 7.484   1.00 20.43  ? 108 MET B HG2  1 
ATOM   6022  H  HG3  . MET B 1 90  ? 27.407  -34.586 8.996   1.00 20.43  ? 108 MET B HG3  1 
ATOM   6023  H  HE1  . MET B 1 90  ? 25.472  -31.316 7.855   1.00 14.92  ? 108 MET B HE1  1 
ATOM   6024  H  HE2  . MET B 1 90  ? 26.244  -32.227 6.807   1.00 14.92  ? 108 MET B HE2  1 
ATOM   6025  H  HE3  . MET B 1 90  ? 24.656  -32.218 6.833   1.00 14.92  ? 108 MET B HE3  1 
ATOM   6026  N  N    . VAL B 1 91  ? 28.972  -31.020 6.245   1.00 14.65  ? 109 VAL B N    1 
ATOM   6027  C  CA   . VAL B 1 91  ? 28.710  -30.557 4.883   1.00 14.98  ? 109 VAL B CA   1 
ATOM   6028  C  C    . VAL B 1 91  ? 29.872  -30.933 3.976   1.00 15.32  ? 109 VAL B C    1 
ATOM   6029  O  O    . VAL B 1 91  ? 29.683  -31.501 2.890   1.00 16.98  ? 109 VAL B O    1 
ATOM   6030  C  CB   . VAL B 1 91  ? 28.450  -29.039 4.879   1.00 15.61  ? 109 VAL B CB   1 
ATOM   6031  C  CG1  . VAL B 1 91  ? 28.300  -28.519 3.451   1.00 15.56  ? 109 VAL B CG1  1 
ATOM   6032  C  CG2  . VAL B 1 91  ? 27.219  -28.706 5.721   1.00 14.41  ? 109 VAL B CG2  1 
ATOM   6033  H  H    . VAL B 1 91  ? 28.992  -30.393 6.834   1.00 17.59  ? 109 VAL B H    1 
ATOM   6034  H  HA   . VAL B 1 91  ? 27.913  -30.996 4.547   1.00 17.97  ? 109 VAL B HA   1 
ATOM   6035  H  HB   . VAL B 1 91  ? 29.212  -28.588 5.275   1.00 18.73  ? 109 VAL B HB   1 
ATOM   6036  H  HG11 . VAL B 1 91  ? 27.904  -27.634 3.477   1.00 18.67  ? 109 VAL B HG11 1 
ATOM   6037  H  HG12 . VAL B 1 91  ? 29.176  -28.477 3.036   1.00 18.67  ? 109 VAL B HG12 1 
ATOM   6038  H  HG13 . VAL B 1 91  ? 27.727  -29.123 2.953   1.00 18.67  ? 109 VAL B HG13 1 
ATOM   6039  H  HG21 . VAL B 1 91  ? 27.091  -27.745 5.728   1.00 17.30  ? 109 VAL B HG21 1 
ATOM   6040  H  HG22 . VAL B 1 91  ? 26.443  -29.140 5.331   1.00 17.30  ? 109 VAL B HG22 1 
ATOM   6041  H  HG23 . VAL B 1 91  ? 27.358  -29.028 6.625   1.00 17.30  ? 109 VAL B HG23 1 
ATOM   6042  N  N    . ASN B 1 92  ? 31.096  -30.624 4.415   1.00 15.52  ? 110 ASN B N    1 
ATOM   6043  C  CA   . ASN B 1 92  ? 32.271  -31.005 3.640   1.00 16.27  ? 110 ASN B CA   1 
ATOM   6044  C  C    . ASN B 1 92  ? 32.306  -32.508 3.390   1.00 15.85  ? 110 ASN B C    1 
ATOM   6045  O  O    . ASN B 1 92  ? 32.632  -32.948 2.282   1.00 16.78  ? 110 ASN B O    1 
ATOM   6046  C  CB   . ASN B 1 92  ? 33.548  -30.548 4.344   1.00 16.90  ? 110 ASN B CB   1 
ATOM   6047  C  CG   . ASN B 1 92  ? 34.795  -30.957 3.590   1.00 19.06  ? 110 ASN B CG   1 
ATOM   6048  O  OD1  . ASN B 1 92  ? 35.156  -30.348 2.583   1.00 21.35  ? 110 ASN B OD1  1 
ATOM   6049  N  ND2  . ASN B 1 92  ? 35.456  -32.001 4.068   1.00 17.44  ? 110 ASN B ND2  1 
ATOM   6050  H  H    . ASN B 1 92  ? 31.267  -30.203 5.145   1.00 18.63  ? 110 ASN B H    1 
ATOM   6051  H  HA   . ASN B 1 92  ? 32.229  -30.557 2.781   1.00 19.52  ? 110 ASN B HA   1 
ATOM   6052  H  HB2  . ASN B 1 92  ? 33.542  -29.581 4.416   1.00 20.28  ? 110 ASN B HB2  1 
ATOM   6053  H  HB3  . ASN B 1 92  ? 33.585  -30.946 5.227   1.00 20.28  ? 110 ASN B HB3  1 
ATOM   6054  H  HD21 . ASN B 1 92  ? 36.171  -32.274 3.676   1.00 20.93  ? 110 ASN B HD21 1 
ATOM   6055  H  HD22 . ASN B 1 92  ? 35.169  -32.406 4.770   1.00 20.93  ? 110 ASN B HD22 1 
ATOM   6056  N  N    . ALA B 1 93  ? 31.955  -33.312 4.398   1.00 15.78  ? 111 ALA B N    1 
ATOM   6057  C  CA   . ALA B 1 93  ? 31.996  -34.765 4.244   1.00 16.00  ? 111 ALA B CA   1 
ATOM   6058  C  C    . ALA B 1 93  ? 30.958  -35.256 3.243   1.00 17.16  ? 111 ALA B C    1 
ATOM   6059  O  O    . ALA B 1 93  ? 31.232  -36.167 2.453   1.00 18.03  ? 111 ALA B O    1 
ATOM   6060  C  CB   . ALA B 1 93  ? 31.778  -35.439 5.597   1.00 15.71  ? 111 ALA B CB   1 
ATOM   6061  H  H    . ALA B 1 93  ? 31.692  -33.044 5.172   1.00 18.93  ? 111 ALA B H    1 
ATOM   6062  H  HA   . ALA B 1 93  ? 32.873  -35.011 3.912   1.00 19.20  ? 111 ALA B HA   1 
ATOM   6063  H  HB1  . ALA B 1 93  ? 30.887  -35.226 5.916   1.00 18.85  ? 111 ALA B HB1  1 
ATOM   6064  H  HB2  . ALA B 1 93  ? 31.870  -36.399 5.490   1.00 18.85  ? 111 ALA B HB2  1 
ATOM   6065  H  HB3  . ALA B 1 93  ? 32.441  -35.111 6.224   1.00 18.85  ? 111 ALA B HB3  1 
ATOM   6066  N  N    . ILE B 1 94  ? 29.753  -34.687 3.267   1.00 16.74  ? 112 ILE B N    1 
ATOM   6067  C  CA   . ILE B 1 94  ? 28.747  -35.078 2.285   1.00 16.85  ? 112 ILE B CA   1 
ATOM   6068  C  C    . ILE B 1 94  ? 29.233  -34.757 0.880   1.00 17.82  ? 112 ILE B C    1 
ATOM   6069  O  O    . ILE B 1 94  ? 29.130  -35.579 -0.038  1.00 18.62  ? 112 ILE B O    1 
ATOM   6070  C  CB   . ILE B 1 94  ? 27.403  -34.398 2.585   1.00 17.50  ? 112 ILE B CB   1 
ATOM   6071  C  CG1  . ILE B 1 94  ? 26.827  -34.947 3.886   1.00 19.18  ? 112 ILE B CG1  1 
ATOM   6072  C  CG2  . ILE B 1 94  ? 26.446  -34.600 1.424   1.00 18.15  ? 112 ILE B CG2  1 
ATOM   6073  C  CD1  . ILE B 1 94  ? 25.780  -34.062 4.504   1.00 20.88  ? 112 ILE B CD1  1 
ATOM   6074  H  H    . ILE B 1 94  ? 29.500  -34.086 3.828   1.00 20.08  ? 112 ILE B H    1 
ATOM   6075  H  HA   . ILE B 1 94  ? 28.613  -36.037 2.347   1.00 20.23  ? 112 ILE B HA   1 
ATOM   6076  H  HB   . ILE B 1 94  ? 27.541  -33.444 2.694   1.00 21.00  ? 112 ILE B HB   1 
ATOM   6077  H  HG12 . ILE B 1 94  ? 26.419  -35.808 3.707   1.00 23.02  ? 112 ILE B HG12 1 
ATOM   6078  H  HG13 . ILE B 1 94  ? 27.547  -35.047 4.528   1.00 23.02  ? 112 ILE B HG13 1 
ATOM   6079  H  HG21 . ILE B 1 94  ? 25.539  -34.445 1.731   1.00 21.78  ? 112 ILE B HG21 1 
ATOM   6080  H  HG22 . ILE B 1 94  ? 26.668  -33.972 0.718   1.00 21.78  ? 112 ILE B HG22 1 
ATOM   6081  H  HG23 . ILE B 1 94  ? 26.534  -35.509 1.097   1.00 21.78  ? 112 ILE B HG23 1 
ATOM   6082  H  HD11 . ILE B 1 94  ? 25.513  -34.437 5.357   1.00 25.06  ? 112 ILE B HD11 1 
ATOM   6083  H  HD12 . ILE B 1 94  ? 26.153  -33.176 4.635   1.00 25.06  ? 112 ILE B HD12 1 
ATOM   6084  H  HD13 . ILE B 1 94  ? 25.015  -34.015 3.909   1.00 25.06  ? 112 ILE B HD13 1 
ATOM   6085  N  N    . THR B 1 95  ? 29.769  -33.551 0.691   1.00 17.91  ? 113 THR B N    1 
ATOM   6086  C  CA   . THR B 1 95  ? 30.307  -33.190 -0.616  1.00 18.80  ? 113 THR B CA   1 
ATOM   6087  C  C    . THR B 1 95  ? 31.372  -34.186 -1.055  1.00 19.03  ? 113 THR B C    1 
ATOM   6088  O  O    . THR B 1 95  ? 31.362  -34.654 -2.202  1.00 19.38  ? 113 THR B O    1 
ATOM   6089  C  CB   . THR B 1 95  ? 30.859  -31.766 -0.553  1.00 19.63  ? 113 THR B CB   1 
ATOM   6090  O  OG1  . THR B 1 95  ? 29.816  -30.872 -0.137  1.00 20.37  ? 113 THR B OG1  1 
ATOM   6091  C  CG2  . THR B 1 95  ? 31.392  -31.331 -1.912  1.00 20.39  ? 113 THR B CG2  1 
ATOM   6092  H  H    . THR B 1 95  ? 29.831  -32.937 1.290   1.00 21.49  ? 113 THR B H    1 
ATOM   6093  H  HA   . THR B 1 95  ? 29.603  -33.207 -1.283  1.00 22.56  ? 113 THR B HA   1 
ATOM   6094  H  HB   . THR B 1 95  ? 31.593  -31.730 0.080   1.00 23.56  ? 113 THR B HB   1 
ATOM   6095  H  HG1  . THR B 1 95  ? 29.171  -30.912 -0.674  1.00 24.45  ? 113 THR B HG1  1 
ATOM   6096  H  HG21 . THR B 1 95  ? 32.119  -31.913 -2.186  1.00 24.46  ? 113 THR B HG21 1 
ATOM   6097  H  HG22 . THR B 1 95  ? 30.686  -31.375 -2.576  1.00 24.46  ? 113 THR B HG22 1 
ATOM   6098  H  HG23 . THR B 1 95  ? 31.721  -30.419 -1.863  1.00 24.46  ? 113 THR B HG23 1 
ATOM   6099  N  N    . ALA B 1 96  ? 32.268  -34.560 -0.139  1.00 18.07  ? 114 ALA B N    1 
ATOM   6100  C  CA   . ALA B 1 96  ? 33.362  -35.458 -0.486  1.00 19.58  ? 114 ALA B CA   1 
ATOM   6101  C  C    . ALA B 1 96  ? 32.864  -36.871 -0.767  1.00 19.60  ? 114 ALA B C    1 
ATOM   6102  O  O    . ALA B 1 96  ? 33.321  -37.509 -1.718  1.00 20.55  ? 114 ALA B O    1 
ATOM   6103  C  CB   . ALA B 1 96  ? 34.400  -35.464 0.637   1.00 19.68  ? 114 ALA B CB   1 
ATOM   6104  H  H    . ALA B 1 96  ? 32.263  -34.308 0.683   1.00 21.69  ? 114 ALA B H    1 
ATOM   6105  H  HA   . ALA B 1 96  ? 33.787  -35.133 -1.294  1.00 23.50  ? 114 ALA B HA   1 
ATOM   6106  H  HB1  . ALA B 1 96  ? 34.752  -34.566 0.745   1.00 23.61  ? 114 ALA B HB1  1 
ATOM   6107  H  HB2  . ALA B 1 96  ? 33.974  -35.754 1.459   1.00 23.61  ? 114 ALA B HB2  1 
ATOM   6108  H  HB3  . ALA B 1 96  ? 35.116  -36.074 0.402   1.00 23.61  ? 114 ALA B HB3  1 
ATOM   6109  N  N    . LEU B 1 97  ? 31.940  -37.383 0.050   1.00 20.09  ? 115 LEU B N    1 
ATOM   6110  C  CA   . LEU B 1 97  ? 31.482  -38.758 -0.122  1.00 19.40  ? 115 LEU B CA   1 
ATOM   6111  C  C    . LEU B 1 97  ? 30.545  -38.902 -1.318  1.00 18.68  ? 115 LEU B C    1 
ATOM   6112  O  O    . LEU B 1 97  ? 30.503  -39.968 -1.937  1.00 19.45  ? 115 LEU B O    1 
ATOM   6113  C  CB   . LEU B 1 97  ? 30.814  -39.254 1.163   1.00 19.32  ? 115 LEU B CB   1 
ATOM   6114  C  CG   . LEU B 1 97  ? 31.726  -39.335 2.390   1.00 19.06  ? 115 LEU B CG   1 
ATOM   6115  C  CD1  . LEU B 1 97  ? 30.922  -39.553 3.652   1.00 19.26  ? 115 LEU B CD1  1 
ATOM   6116  C  CD2  . LEU B 1 97  ? 32.749  -40.447 2.220   1.00 20.03  ? 115 LEU B CD2  1 
ATOM   6117  H  H    . LEU B 1 97  ? 31.570  -36.960 0.701   1.00 24.11  ? 115 LEU B H    1 
ATOM   6118  H  HA   . LEU B 1 97  ? 32.248  -39.330 -0.287  1.00 23.28  ? 115 LEU B HA   1 
ATOM   6119  H  HB2  . LEU B 1 97  ? 30.087  -38.650 1.381   1.00 23.18  ? 115 LEU B HB2  1 
ATOM   6120  H  HB3  . LEU B 1 97  ? 30.467  -40.146 1.001   1.00 23.18  ? 115 LEU B HB3  1 
ATOM   6121  H  HG   . LEU B 1 97  ? 32.198  -38.492 2.479   1.00 22.87  ? 115 LEU B HG   1 
ATOM   6122  H  HD11 . LEU B 1 97  ? 30.516  -40.433 3.620   1.00 23.11  ? 115 LEU B HD11 1 
ATOM   6123  H  HD12 . LEU B 1 97  ? 31.513  -39.489 4.418   1.00 23.11  ? 115 LEU B HD12 1 
ATOM   6124  H  HD13 . LEU B 1 97  ? 30.232  -38.873 3.709   1.00 23.11  ? 115 LEU B HD13 1 
ATOM   6125  H  HD21 . LEU B 1 97  ? 32.285  -41.274 2.016   1.00 24.04  ? 115 LEU B HD21 1 
ATOM   6126  H  HD22 . LEU B 1 97  ? 33.349  -40.216 1.494   1.00 24.04  ? 115 LEU B HD22 1 
ATOM   6127  H  HD23 . LEU B 1 97  ? 33.250  -40.544 3.046   1.00 24.04  ? 115 LEU B HD23 1 
ATOM   6128  N  N    . TYR B 1 98  ? 29.797  -37.850 -1.656  1.00 18.66  ? 116 TYR B N    1 
ATOM   6129  C  CA   . TYR B 1 98  ? 28.992  -37.864 -2.874  1.00 18.27  ? 116 TYR B CA   1 
ATOM   6130  C  C    . TYR B 1 98  ? 29.882  -38.039 -4.099  1.00 19.33  ? 116 TYR B C    1 
ATOM   6131  O  O    . TYR B 1 98  ? 29.643  -38.914 -4.943  1.00 19.69  ? 116 TYR B O    1 
ATOM   6132  C  CB   . TYR B 1 98  ? 28.187  -36.566 -2.955  1.00 17.54  ? 116 TYR B CB   1 
ATOM   6133  C  CG   . TYR B 1 98  ? 27.299  -36.438 -4.176  1.00 18.38  ? 116 TYR B CG   1 
ATOM   6134  C  CD1  . TYR B 1 98  ? 26.038  -37.014 -4.206  1.00 18.77  ? 116 TYR B CD1  1 
ATOM   6135  C  CD2  . TYR B 1 98  ? 27.724  -35.734 -5.295  1.00 19.97  ? 116 TYR B CD2  1 
ATOM   6136  C  CE1  . TYR B 1 98  ? 25.223  -36.892 -5.316  1.00 20.53  ? 116 TYR B CE1  1 
ATOM   6137  C  CE2  . TYR B 1 98  ? 26.917  -35.602 -6.408  1.00 21.04  ? 116 TYR B CE2  1 
ATOM   6138  C  CZ   . TYR B 1 98  ? 25.668  -36.191 -6.416  1.00 21.46  ? 116 TYR B CZ   1 
ATOM   6139  O  OH   . TYR B 1 98  ? 24.854  -36.075 -7.516  1.00 24.26  ? 116 TYR B OH   1 
ATOM   6140  H  H    . TYR B 1 98  ? 29.739  -37.122 -1.201  1.00 22.39  ? 116 TYR B H    1 
ATOM   6141  H  HA   . TYR B 1 98  ? 28.368  -38.607 -2.852  1.00 21.92  ? 116 TYR B HA   1 
ATOM   6142  H  HB2  . TYR B 1 98  ? 27.616  -36.510 -2.173  1.00 21.05  ? 116 TYR B HB2  1 
ATOM   6143  H  HB3  . TYR B 1 98  ? 28.808  -35.821 -2.967  1.00 21.05  ? 116 TYR B HB3  1 
ATOM   6144  H  HD1  . TYR B 1 98  ? 25.735  -37.491 -3.467  1.00 22.52  ? 116 TYR B HD1  1 
ATOM   6145  H  HD2  . TYR B 1 98  ? 28.568  -35.343 -5.294  1.00 23.96  ? 116 TYR B HD2  1 
ATOM   6146  H  HE1  . TYR B 1 98  ? 24.378  -37.280 -5.320  1.00 24.63  ? 116 TYR B HE1  1 
ATOM   6147  H  HE2  . TYR B 1 98  ? 27.213  -35.120 -7.146  1.00 25.25  ? 116 TYR B HE2  1 
ATOM   6148  H  HH   . TYR B 1 98  ? 25.229  -35.604 -8.102  1.00 29.11  ? 116 TYR B HH   1 
ATOM   6149  N  N    . ALA B 1 99  ? 30.946  -37.240 -4.187  1.00 19.56  ? 117 ALA B N    1 
ATOM   6150  C  CA   . ALA B 1 99  ? 31.871  -37.364 -5.307  1.00 22.04  ? 117 ALA B CA   1 
ATOM   6151  C  C    . ALA B 1 99  ? 32.616  -38.690 -5.262  1.00 23.12  ? 117 ALA B C    1 
ATOM   6152  O  O    . ALA B 1 99  ? 32.790  -39.347 -6.296  1.00 24.13  ? 117 ALA B O    1 
ATOM   6153  C  CB   . ALA B 1 99  ? 32.862  -36.202 -5.278  1.00 22.70  ? 117 ALA B CB   1 
ATOM   6154  H  H    . ALA B 1 99  ? 31.150  -36.627 -3.620  1.00 23.47  ? 117 ALA B H    1 
ATOM   6155  H  HA   . ALA B 1 99  ? 31.371  -37.326 -6.137  1.00 26.44  ? 117 ALA B HA   1 
ATOM   6156  H  HB1  . ALA B 1 99  ? 32.375  -35.369 -5.380  1.00 27.24  ? 117 ALA B HB1  1 
ATOM   6157  H  HB2  . ALA B 1 99  ? 33.332  -36.208 -4.430  1.00 27.24  ? 117 ALA B HB2  1 
ATOM   6158  H  HB3  . ALA B 1 99  ? 33.494  -36.307 -6.007  1.00 27.24  ? 117 ALA B HB3  1 
ATOM   6159  N  N    . GLY B 1 100 ? 33.058  -39.103 -4.074  1.00 23.69  ? 118 GLY B N    1 
ATOM   6160  C  CA   . GLY B 1 100 ? 33.870  -40.295 -3.929  1.00 23.79  ? 118 GLY B CA   1 
ATOM   6161  C  C    . GLY B 1 100 ? 33.128  -41.591 -4.149  1.00 24.70  ? 118 GLY B C    1 
ATOM   6162  O  O    . GLY B 1 100 ? 33.770  -42.637 -4.305  1.00 25.00  ? 118 GLY B O    1 
ATOM   6163  H  H    . GLY B 1 100 ? 32.895  -38.701 -3.331  1.00 28.43  ? 118 GLY B H    1 
ATOM   6164  H  HA2  . GLY B 1 100 ? 34.597  -40.257 -4.570  1.00 28.55  ? 118 GLY B HA2  1 
ATOM   6165  H  HA3  . GLY B 1 100 ? 34.241  -40.314 -3.033  1.00 28.55  ? 118 GLY B HA3  1 
ATOM   6166  N  N    . SER B 1 101 ? 31.799  -41.550 -4.163  1.00 23.51  ? 119 SER B N    1 
ATOM   6167  C  CA   . SER B 1 101 ? 30.990  -42.719 -4.474  1.00 23.70  ? 119 SER B CA   1 
ATOM   6168  C  C    . SER B 1 101 ? 30.423  -42.662 -5.889  1.00 24.00  ? 119 SER B C    1 
ATOM   6169  O  O    . SER B 1 101 ? 29.438  -43.345 -6.182  1.00 24.86  ? 119 SER B O    1 
ATOM   6170  C  CB   . SER B 1 101 ? 29.872  -42.893 -3.446  1.00 22.52  ? 119 SER B CB   1 
ATOM   6171  O  OG   . SER B 1 101 ? 29.028  -41.759 -3.393  1.00 21.99  ? 119 SER B OG   1 
ATOM   6172  H  H    . SER B 1 101 ? 31.338  -40.845 -3.992  1.00 28.22  ? 119 SER B H    1 
ATOM   6173  H  HA   . SER B 1 101 ? 31.554  -43.506 -4.414  1.00 28.43  ? 119 SER B HA   1 
ATOM   6174  H  HB2  . SER B 1 101 ? 29.340  -43.667 -3.690  1.00 27.02  ? 119 SER B HB2  1 
ATOM   6175  H  HB3  . SER B 1 101 ? 30.270  -43.027 -2.571  1.00 27.02  ? 119 SER B HB3  1 
ATOM   6176  H  HG   . SER B 1 101 ? 28.412  -41.885 -2.836  1.00 26.39  ? 119 SER B HG   1 
ATOM   6177  N  N    . GLY B 1 102 ? 31.016  -41.853 -6.764  1.00 23.41  ? 120 GLY B N    1 
ATOM   6178  C  CA   . GLY B 1 102 ? 30.558  -41.767 -8.135  1.00 23.05  ? 120 GLY B CA   1 
ATOM   6179  C  C    . GLY B 1 102 ? 29.423  -40.800 -8.359  1.00 23.53  ? 120 GLY B C    1 
ATOM   6180  O  O    . GLY B 1 102 ? 28.593  -41.027 -9.248  1.00 25.16  ? 120 GLY B O    1 
ATOM   6181  H  H    . GLY B 1 102 ? 31.685  -41.344 -6.582  1.00 28.09  ? 120 GLY B H    1 
ATOM   6182  H  HA2  . GLY B 1 102 ? 31.300  -41.489 -8.694  1.00 27.66  ? 120 GLY B HA2  1 
ATOM   6183  H  HA3  . GLY B 1 102 ? 30.260  -42.646 -8.419  1.00 27.66  ? 120 GLY B HA3  1 
ATOM   6184  N  N    . ASN B 1 103 ? 29.361  -39.721 -7.584  1.00 23.01  ? 121 ASN B N    1 
ATOM   6185  C  CA   . ASN B 1 103 ? 28.268  -38.755 -7.650  1.00 22.22  ? 121 ASN B CA   1 
ATOM   6186  C  C    . ASN B 1 103 ? 26.927  -39.423 -7.356  1.00 21.32  ? 121 ASN B C    1 
ATOM   6187  O  O    . ASN B 1 103 ? 25.970  -39.344 -8.129  1.00 22.99  ? 121 ASN B O    1 
ATOM   6188  C  CB   . ASN B 1 103 ? 28.242  -38.022 -8.990  1.00 24.76  ? 121 ASN B CB   1 
ATOM   6189  C  CG   . ASN B 1 103 ? 29.563  -37.389 -9.320  1.00 27.81  ? 121 ASN B CG   1 
ATOM   6190  O  OD1  . ASN B 1 103 ? 30.225  -36.824 -8.450  1.00 28.30  ? 121 ASN B OD1  1 
ATOM   6191  N  ND2  . ASN B 1 103 ? 29.964  -37.485 -10.581 1.00 30.07  ? 121 ASN B ND2  1 
ATOM   6192  H  H    . ASN B 1 103 ? 29.957  -39.522 -6.996  1.00 27.62  ? 121 ASN B H    1 
ATOM   6193  H  HA   . ASN B 1 103 ? 28.421  -38.090 -6.960  1.00 26.66  ? 121 ASN B HA   1 
ATOM   6194  H  HB2  . ASN B 1 103 ? 28.025  -38.653 -9.694  1.00 29.72  ? 121 ASN B HB2  1 
ATOM   6195  H  HB3  . ASN B 1 103 ? 27.572  -37.321 -8.956  1.00 29.72  ? 121 ASN B HB3  1 
ATOM   6196  H  HD21 . ASN B 1 103 ? 29.473  -37.893 -11.158 1.00 36.09  ? 121 ASN B HD21 1 
ATOM   6197  H  HD22 . ASN B 1 103 ? 30.713  -37.140 -10.822 1.00 36.09  ? 121 ASN B HD22 1 
ATOM   6198  N  N    . ASN B 1 104 ? 26.870  -40.058 -6.195  1.00 20.05  ? 122 ASN B N    1 
ATOM   6199  C  CA   . ASN B 1 104 ? 25.703  -40.802 -5.757  1.00 21.38  ? 122 ASN B CA   1 
ATOM   6200  C  C    . ASN B 1 104 ? 25.295  -40.322 -4.377  1.00 18.22  ? 122 ASN B C    1 
ATOM   6201  O  O    . ASN B 1 104 ? 26.146  -40.116 -3.503  1.00 18.58  ? 122 ASN B O    1 
ATOM   6202  C  CB   . ASN B 1 104 ? 26.008  -42.295 -5.698  1.00 23.43  ? 122 ASN B CB   1 
ATOM   6203  C  CG   . ASN B 1 104 ? 25.805  -42.973 -7.028  1.00 26.72  ? 122 ASN B CG   1 
ATOM   6204  O  OD1  . ASN B 1 104 ? 24.731  -42.882 -7.624  1.00 28.47  ? 122 ASN B OD1  1 
ATOM   6205  N  ND2  . ASN B 1 104 ? 26.839  -43.650 -7.511  1.00 27.58  ? 122 ASN B ND2  1 
ATOM   6206  H  H    . ASN B 1 104 ? 27.516  -40.072 -5.626  1.00 24.05  ? 122 ASN B H    1 
ATOM   6207  H  HA   . ASN B 1 104 ? 24.966  -40.653 -6.371  1.00 25.66  ? 122 ASN B HA   1 
ATOM   6208  H  HB2  . ASN B 1 104 ? 26.932  -42.421 -5.433  1.00 28.12  ? 122 ASN B HB2  1 
ATOM   6209  H  HB3  . ASN B 1 104 ? 25.418  -42.715 -5.053  1.00 28.12  ? 122 ASN B HB3  1 
ATOM   6210  H  HD21 . ASN B 1 104 ? 27.575  -43.685 -7.068  1.00 33.10  ? 122 ASN B HD21 1 
ATOM   6211  H  HD22 . ASN B 1 104 ? 26.773  -44.054 -8.268  1.00 33.10  ? 122 ASN B HD22 1 
ATOM   6212  N  N    . LYS B 1 105 ? 23.990  -40.130 -4.197  1.00 18.64  ? 123 LYS B N    1 
ATOM   6213  C  CA   . LYS B 1 105 ? 23.464  -39.746 -2.896  1.00 18.57  ? 123 LYS B CA   1 
ATOM   6214  C  C    . LYS B 1 105 ? 23.851  -40.787 -1.855  1.00 18.30  ? 123 LYS B C    1 
ATOM   6215  O  O    . LYS B 1 105 ? 24.072  -41.962 -2.167  1.00 19.45  ? 123 LYS B O    1 
ATOM   6216  C  CB   . LYS B 1 105 ? 21.937  -39.629 -2.950  1.00 20.61  ? 123 LYS B CB   1 
ATOM   6217  C  CG   . LYS B 1 105 ? 21.409  -38.676 -4.013  1.00 23.84  ? 123 LYS B CG   1 
ATOM   6218  C  CD   . LYS B 1 105 ? 20.039  -38.103 -3.639  1.00 27.70  ? 123 LYS B CD   1 
ATOM   6219  C  CE   . LYS B 1 105 ? 18.971  -38.382 -4.690  1.00 32.31  ? 123 LYS B CE   1 
ATOM   6220  N  NZ   . LYS B 1 105 ? 19.410  -38.078 -6.084  1.00 35.15  ? 123 LYS B NZ   1 
ATOM   6221  H  H    . LYS B 1 105 ? 23.393  -40.216 -4.810  1.00 22.37  ? 123 LYS B H    1 
ATOM   6222  H  HA   . LYS B 1 105 ? 23.829  -38.885 -2.640  1.00 22.29  ? 123 LYS B HA   1 
ATOM   6223  H  HB2  . LYS B 1 105 ? 21.567  -40.507 -3.135  1.00 24.74  ? 123 LYS B HB2  1 
ATOM   6224  H  HB3  . LYS B 1 105 ? 21.621  -39.311 -2.090  1.00 24.74  ? 123 LYS B HB3  1 
ATOM   6225  H  HG2  . LYS B 1 105 ? 22.029  -37.937 -4.115  1.00 28.60  ? 123 LYS B HG2  1 
ATOM   6226  H  HG3  . LYS B 1 105 ? 21.320  -39.153 -4.853  1.00 28.60  ? 123 LYS B HG3  1 
ATOM   6227  H  HD2  . LYS B 1 105 ? 19.748  -38.502 -2.804  1.00 33.24  ? 123 LYS B HD2  1 
ATOM   6228  H  HD3  . LYS B 1 105 ? 20.116  -37.142 -3.539  1.00 33.24  ? 123 LYS B HD3  1 
ATOM   6229  H  HE2  . LYS B 1 105 ? 18.734  -39.322 -4.653  1.00 38.77  ? 123 LYS B HE2  1 
ATOM   6230  H  HE3  . LYS B 1 105 ? 18.194  -37.835 -4.499  1.00 38.77  ? 123 LYS B HE3  1 
ATOM   6231  H  HZ1  . LYS B 1 105 ? 18.708  -38.074 -6.630  1.00 42.18  ? 123 LYS B HZ1  1 
ATOM   6232  H  HZ2  . LYS B 1 105 ? 19.803  -37.280 -6.112  1.00 42.18  ? 123 LYS B HZ2  1 
ATOM   6233  H  HZ3  . LYS B 1 105 ? 19.989  -38.695 -6.362  1.00 42.18  ? 123 LYS B HZ3  1 
ATOM   6234  N  N    . LEU B 1 106 ? 23.930  -40.352 -0.604  1.00 17.77  ? 124 LEU B N    1 
ATOM   6235  C  CA   . LEU B 1 106 ? 24.285  -41.261 0.476   1.00 18.19  ? 124 LEU B CA   1 
ATOM   6236  C  C    . LEU B 1 106 ? 23.413  -40.994 1.691   1.00 17.78  ? 124 LEU B C    1 
ATOM   6237  O  O    . LEU B 1 106 ? 22.938  -39.868 1.886   1.00 18.03  ? 124 LEU B O    1 
ATOM   6238  C  CB   . LEU B 1 106 ? 25.758  -41.119 0.887   1.00 18.43  ? 124 LEU B CB   1 
ATOM   6239  C  CG   . LEU B 1 106 ? 26.191  -39.720 1.323   1.00 19.83  ? 124 LEU B CG   1 
ATOM   6240  C  CD1  . LEU B 1 106 ? 27.136  -39.789 2.504   1.00 19.59  ? 124 LEU B CD1  1 
ATOM   6241  C  CD2  . LEU B 1 106 ? 26.843  -38.975 0.171   1.00 20.53  ? 124 LEU B CD2  1 
ATOM   6242  H  H    . LEU B 1 106 ? 23.784  -39.541 -0.358  1.00 21.32  ? 124 LEU B H    1 
ATOM   6243  H  HA   . LEU B 1 106 ? 24.125  -42.170 0.177   1.00 21.83  ? 124 LEU B HA   1 
ATOM   6244  H  HB2  . LEU B 1 106 ? 25.925  -41.718 1.631   1.00 22.12  ? 124 LEU B HB2  1 
ATOM   6245  H  HB3  . LEU B 1 106 ? 26.310  -41.369 0.129   1.00 22.12  ? 124 LEU B HB3  1 
ATOM   6246  H  HG   . LEU B 1 106 ? 25.403  -39.226 1.598   1.00 23.79  ? 124 LEU B HG   1 
ATOM   6247  H  HD11 . LEU B 1 106 ? 27.483  -38.901 2.683   1.00 23.51  ? 124 LEU B HD11 1 
ATOM   6248  H  HD12 . LEU B 1 106 ? 26.651  -40.116 3.278   1.00 23.51  ? 124 LEU B HD12 1 
ATOM   6249  H  HD13 . LEU B 1 106 ? 27.865  -40.392 2.290   1.00 23.51  ? 124 LEU B HD13 1 
ATOM   6250  H  HD21 . LEU B 1 106 ? 27.074  -38.080 0.464   1.00 24.64  ? 124 LEU B HD21 1 
ATOM   6251  H  HD22 . LEU B 1 106 ? 27.644  -39.452 -0.100  1.00 24.64  ? 124 LEU B HD22 1 
ATOM   6252  H  HD23 . LEU B 1 106 ? 26.219  -38.931 -0.570  1.00 24.64  ? 124 LEU B HD23 1 
ATOM   6253  N  N    . PRO B 1 107 ? 23.190  -42.009 2.523   1.00 17.70  ? 125 PRO B N    1 
ATOM   6254  C  CA   . PRO B 1 107 ? 22.439  -41.802 3.764   1.00 17.50  ? 125 PRO B CA   1 
ATOM   6255  C  C    . PRO B 1 107 ? 23.313  -41.226 4.864   1.00 16.95  ? 125 PRO B C    1 
ATOM   6256  O  O    . PRO B 1 107 ? 24.531  -41.422 4.894   1.00 17.14  ? 125 PRO B O    1 
ATOM   6257  C  CB   . PRO B 1 107 ? 21.991  -43.220 4.138   1.00 18.59  ? 125 PRO B CB   1 
ATOM   6258  C  CG   . PRO B 1 107 ? 23.079  -44.092 3.601   1.00 19.11  ? 125 PRO B CG   1 
ATOM   6259  C  CD   . PRO B 1 107 ? 23.547  -43.428 2.324   1.00 19.31  ? 125 PRO B CD   1 
ATOM   6260  H  HA   . PRO B 1 107 ? 21.670  -41.231 3.612   1.00 21.00  ? 125 PRO B HA   1 
ATOM   6261  H  HB2  . PRO B 1 107 ? 21.917  -43.304 5.102   1.00 22.31  ? 125 PRO B HB2  1 
ATOM   6262  H  HB3  . PRO B 1 107 ? 21.140  -43.423 3.721   1.00 22.31  ? 125 PRO B HB3  1 
ATOM   6263  H  HG2  . PRO B 1 107 ? 23.802  -44.148 4.245   1.00 22.94  ? 125 PRO B HG2  1 
ATOM   6264  H  HG3  . PRO B 1 107 ? 22.728  -44.978 3.419   1.00 22.94  ? 125 PRO B HG3  1 
ATOM   6265  H  HD2  . PRO B 1 107 ? 24.505  -43.531 2.213   1.00 23.18  ? 125 PRO B HD2  1 
ATOM   6266  H  HD3  . PRO B 1 107 ? 23.083  -43.795 1.555   1.00 23.18  ? 125 PRO B HD3  1 
ATOM   6267  N  N    . VAL B 1 108 ? 22.664  -40.507 5.779   1.00 16.06  ? 126 VAL B N    1 
ATOM   6268  C  CA   . VAL B 1 108 ? 23.299  -39.943 6.965   1.00 16.66  ? 126 VAL B CA   1 
ATOM   6269  C  C    . VAL B 1 108 ? 22.569  -40.509 8.175   1.00 16.29  ? 126 VAL B C    1 
ATOM   6270  O  O    . VAL B 1 108 ? 21.334  -40.516 8.210   1.00 17.02  ? 126 VAL B O    1 
ATOM   6271  C  CB   . VAL B 1 108 ? 23.236  -38.404 6.963   1.00 16.23  ? 126 VAL B CB   1 
ATOM   6272  C  CG1  . VAL B 1 108 ? 23.832  -37.823 8.242   1.00 16.56  ? 126 VAL B CG1  1 
ATOM   6273  C  CG2  . VAL B 1 108 ? 23.971  -37.845 5.761   1.00 17.35  ? 126 VAL B CG2  1 
ATOM   6274  H  H    . VAL B 1 108 ? 21.824  -40.328 5.731   1.00 19.28  ? 126 VAL B H    1 
ATOM   6275  H  HA   . VAL B 1 108 ? 24.232  -40.207 7.002   1.00 20.00  ? 126 VAL B HA   1 
ATOM   6276  H  HB   . VAL B 1 108 ? 22.303  -38.143 6.916   1.00 19.47  ? 126 VAL B HB   1 
ATOM   6277  H  HG11 . VAL B 1 108 ? 23.865  -36.856 8.164   1.00 19.87  ? 126 VAL B HG11 1 
ATOM   6278  H  HG12 . VAL B 1 108 ? 23.274  -38.075 8.994   1.00 19.87  ? 126 VAL B HG12 1 
ATOM   6279  H  HG13 . VAL B 1 108 ? 24.728  -38.175 8.362   1.00 19.87  ? 126 VAL B HG13 1 
ATOM   6280  H  HG21 . VAL B 1 108 ? 23.775  -36.899 5.683   1.00 20.82  ? 126 VAL B HG21 1 
ATOM   6281  H  HG22 . VAL B 1 108 ? 24.924  -37.977 5.885   1.00 20.82  ? 126 VAL B HG22 1 
ATOM   6282  H  HG23 . VAL B 1 108 ? 23.674  -38.311 4.964   1.00 20.82  ? 126 VAL B HG23 1 
ATOM   6283  N  N    . LEU B 1 109 ? 23.328  -40.987 9.157   1.00 16.52  ? 127 LEU B N    1 
ATOM   6284  C  CA   . LEU B 1 109 ? 22.782  -41.609 10.358  1.00 15.92  ? 127 LEU B CA   1 
ATOM   6285  C  C    . LEU B 1 109 ? 23.469  -40.972 11.556  1.00 16.25  ? 127 LEU B C    1 
ATOM   6286  O  O    . LEU B 1 109 ? 24.695  -40.820 11.566  1.00 16.23  ? 127 LEU B O    1 
ATOM   6287  C  CB   . LEU B 1 109 ? 23.001  -43.129 10.320  1.00 16.25  ? 127 LEU B CB   1 
ATOM   6288  C  CG   . LEU B 1 109 ? 22.359  -43.976 11.417  1.00 16.43  ? 127 LEU B CG   1 
ATOM   6289  C  CD1  . LEU B 1 109 ? 22.056  -45.386 10.895  1.00 18.76  ? 127 LEU B CD1  1 
ATOM   6290  C  CD2  . LEU B 1 109 ? 23.267  -44.030 12.646  1.00 16.57  ? 127 LEU B CD2  1 
ATOM   6291  H  H    . LEU B 1 109 ? 24.187  -40.961 9.150   1.00 19.82  ? 127 LEU B H    1 
ATOM   6292  H  HA   . LEU B 1 109 ? 21.827  -41.455 10.438  1.00 19.10  ? 127 LEU B HA   1 
ATOM   6293  H  HB2  . LEU B 1 109 ? 22.651  -43.456 9.476   1.00 19.50  ? 127 LEU B HB2  1 
ATOM   6294  H  HB3  . LEU B 1 109 ? 23.956  -43.290 10.368  1.00 19.50  ? 127 LEU B HB3  1 
ATOM   6295  H  HG   . LEU B 1 109 ? 21.519  -43.572 11.685  1.00 19.72  ? 127 LEU B HG   1 
ATOM   6296  H  HD11 . LEU B 1 109 ? 22.864  -45.760 10.509  1.00 22.51  ? 127 LEU B HD11 1 
ATOM   6297  H  HD12 . LEU B 1 109 ? 21.756  -45.939 11.634  1.00 22.51  ? 127 LEU B HD12 1 
ATOM   6298  H  HD13 . LEU B 1 109 ? 21.362  -45.331 10.220  1.00 22.51  ? 127 LEU B HD13 1 
ATOM   6299  H  HD21 . LEU B 1 109 ? 24.166  -44.264 12.365  1.00 19.89  ? 127 LEU B HD21 1 
ATOM   6300  H  HD22 . LEU B 1 109 ? 23.271  -43.159 13.074  1.00 19.89  ? 127 LEU B HD22 1 
ATOM   6301  H  HD23 . LEU B 1 109 ? 22.928  -44.699 13.261  1.00 19.89  ? 127 LEU B HD23 1 
ATOM   6302  N  N    . THR B 1 110 ? 22.687  -40.576 12.555  1.00 16.05  ? 128 THR B N    1 
ATOM   6303  C  CA   . THR B 1 110 ? 23.210  -39.692 13.584  1.00 15.98  ? 128 THR B CA   1 
ATOM   6304  C  C    . THR B 1 110 ? 22.738  -40.102 14.971  1.00 16.13  ? 128 THR B C    1 
ATOM   6305  O  O    . THR B 1 110 ? 21.739  -40.805 15.137  1.00 16.25  ? 128 THR B O    1 
ATOM   6306  C  CB   . THR B 1 110 ? 22.766  -38.242 13.324  1.00 15.85  ? 128 THR B CB   1 
ATOM   6307  O  OG1  . THR B 1 110 ? 21.359  -38.127 13.564  1.00 16.36  ? 128 THR B OG1  1 
ATOM   6308  C  CG2  . THR B 1 110 ? 23.064  -37.831 11.898  1.00 16.01  ? 128 THR B CG2  1 
ATOM   6309  H  H    . THR B 1 110 ? 21.864  -40.803 12.655  1.00 19.26  ? 128 THR B H    1 
ATOM   6310  H  HA   . THR B 1 110 ? 24.178  -39.765 13.577  1.00 19.18  ? 128 THR B HA   1 
ATOM   6311  H  HB   . THR B 1 110 ? 23.252  -37.646 13.916  1.00 19.01  ? 128 THR B HB   1 
ATOM   6312  H  HG1  . THR B 1 110 ? 21.055  -37.450 13.169  1.00 19.63  ? 128 THR B HG1  1 
ATOM   6313  H  HG21 . THR B 1 110 ? 23.948  -38.138 11.642  1.00 19.21  ? 128 THR B HG21 1 
ATOM   6314  H  HG22 . THR B 1 110 ? 22.409  -38.220 11.298  1.00 19.21  ? 128 THR B HG22 1 
ATOM   6315  H  HG23 . THR B 1 110 ? 23.030  -36.865 11.817  1.00 19.21  ? 128 THR B HG23 1 
ATOM   6316  N  N    . TRP B 1 111 ? 23.460  -39.611 15.975  1.00 15.82  ? 129 TRP B N    1 
ATOM   6317  C  CA   . TRP B 1 111 ? 23.070  -39.750 17.370  1.00 15.68  ? 129 TRP B CA   1 
ATOM   6318  C  C    . TRP B 1 111 ? 23.097  -38.373 18.017  1.00 15.31  ? 129 TRP B C    1 
ATOM   6319  O  O    . TRP B 1 111 ? 24.059  -37.617 17.841  1.00 15.17  ? 129 TRP B O    1 
ATOM   6320  C  CB   . TRP B 1 111 ? 24.022  -40.674 18.130  1.00 16.38  ? 129 TRP B CB   1 
ATOM   6321  C  CG   . TRP B 1 111 ? 23.651  -40.870 19.571  1.00 16.62  ? 129 TRP B CG   1 
ATOM   6322  C  CD1  . TRP B 1 111 ? 22.398  -41.079 20.080  1.00 17.45  ? 129 TRP B CD1  1 
ATOM   6323  C  CD2  . TRP B 1 111 ? 24.544  -40.877 20.691  1.00 17.72  ? 129 TRP B CD2  1 
ATOM   6324  N  NE1  . TRP B 1 111 ? 22.459  -41.222 21.446  1.00 16.94  ? 129 TRP B NE1  1 
ATOM   6325  C  CE2  . TRP B 1 111 ? 23.766  -41.100 21.846  1.00 17.46  ? 129 TRP B CE2  1 
ATOM   6326  C  CE3  . TRP B 1 111 ? 25.927  -40.719 20.828  1.00 17.84  ? 129 TRP B CE3  1 
ATOM   6327  C  CZ2  . TRP B 1 111 ? 24.323  -41.160 23.116  1.00 18.19  ? 129 TRP B CZ2  1 
ATOM   6328  C  CZ3  . TRP B 1 111 ? 26.477  -40.781 22.090  1.00 18.91  ? 129 TRP B CZ3  1 
ATOM   6329  C  CH2  . TRP B 1 111 ? 25.677  -41.009 23.217  1.00 19.19  ? 129 TRP B CH2  1 
ATOM   6330  H  H    . TRP B 1 111 ? 24.199  -39.184 15.867  1.00 18.98  ? 129 TRP B H    1 
ATOM   6331  H  HA   . TRP B 1 111 ? 22.174  -40.118 17.417  1.00 18.81  ? 129 TRP B HA   1 
ATOM   6332  H  HB2  . TRP B 1 111 ? 24.019  -41.545 17.703  1.00 19.65  ? 129 TRP B HB2  1 
ATOM   6333  H  HB3  . TRP B 1 111 ? 24.914  -40.294 18.103  1.00 19.65  ? 129 TRP B HB3  1 
ATOM   6334  H  HD1  . TRP B 1 111 ? 21.618  -41.119 19.575  1.00 20.94  ? 129 TRP B HD1  1 
ATOM   6335  H  HE1  . TRP B 1 111 ? 21.788  -41.365 21.965  1.00 20.33  ? 129 TRP B HE1  1 
ATOM   6336  H  HE3  . TRP B 1 111 ? 26.464  -40.574 20.082  1.00 21.41  ? 129 TRP B HE3  1 
ATOM   6337  H  HZ2  . TRP B 1 111 ? 23.795  -41.299 23.869  1.00 21.83  ? 129 TRP B HZ2  1 
ATOM   6338  H  HZ3  . TRP B 1 111 ? 27.395  -40.671 22.196  1.00 22.69  ? 129 TRP B HZ3  1 
ATOM   6339  H  HH2  . TRP B 1 111 ? 26.078  -41.057 24.055  1.00 23.03  ? 129 TRP B HH2  1 
ATOM   6340  N  N    . SER B 1 112 ? 22.033  -38.045 18.744  1.00 16.67  ? 130 SER B N    1 
ATOM   6341  C  CA   . SER B 1 112 ? 22.001  -36.878 19.630  1.00 16.38  ? 130 SER B CA   1 
ATOM   6342  C  C    . SER B 1 112 ? 22.324  -35.624 18.825  1.00 15.80  ? 130 SER B C    1 
ATOM   6343  O  O    . SER B 1 112 ? 21.656  -35.385 17.803  1.00 16.07  ? 130 SER B O    1 
ATOM   6344  C  CB   . SER B 1 112 ? 22.932  -37.176 20.803  1.00 18.13  ? 130 SER B CB   1 
ATOM   6345  O  OG   . SER B 1 112 ? 22.814  -36.189 21.805  1.00 21.35  ? 130 SER B OG   1 
ATOM   6346  H  H    . SER B 1 112 ? 21.299  -38.492 18.742  1.00 20.00  ? 130 SER B H    1 
ATOM   6347  H  HA   . SER B 1 112 ? 21.095  -36.743 19.949  1.00 19.66  ? 130 SER B HA   1 
ATOM   6348  H  HB2  . SER B 1 112 ? 22.698  -38.038 21.180  1.00 21.75  ? 130 SER B HB2  1 
ATOM   6349  H  HB3  . SER B 1 112 ? 23.848  -37.192 20.482  1.00 21.75  ? 130 SER B HB3  1 
ATOM   6350  H  HG   . SER B 1 112 ? 23.274  -36.403 22.475  1.00 25.62  ? 130 SER B HG   1 
ATOM   6351  N  N    . GLN B 1 113 ? 23.295  -34.807 19.256  1.00 15.77  ? 131 GLN B N    1 
ATOM   6352  C  CA   . GLN B 1 113 ? 23.634  -33.576 18.553  1.00 14.72  ? 131 GLN B CA   1 
ATOM   6353  C  C    . GLN B 1 113 ? 23.868  -33.805 17.069  1.00 14.17  ? 131 GLN B C    1 
ATOM   6354  O  O    . GLN B 1 113 ? 23.666  -32.891 16.261  1.00 14.98  ? 131 GLN B O    1 
ATOM   6355  C  CB   . GLN B 1 113 ? 24.896  -32.941 19.163  1.00 14.86  ? 131 GLN B CB   1 
ATOM   6356  C  CG   . GLN B 1 113 ? 25.177  -31.533 18.645  1.00 14.11  ? 131 GLN B CG   1 
ATOM   6357  C  CD   . GLN B 1 113 ? 26.624  -31.050 18.820  1.00 14.37  ? 131 GLN B CD   1 
ATOM   6358  O  OE1  . GLN B 1 113 ? 27.092  -30.202 18.062  1.00 15.53  ? 131 GLN B OE1  1 
ATOM   6359  N  NE2  . GLN B 1 113 ? 27.321  -31.567 19.823  1.00 14.45  ? 131 GLN B NE2  1 
ATOM   6360  H  H    . GLN B 1 113 ? 23.772  -34.948 19.957  1.00 18.92  ? 131 GLN B H    1 
ATOM   6361  H  HA   . GLN B 1 113 ? 22.890  -32.962 18.659  1.00 17.67  ? 131 GLN B HA   1 
ATOM   6362  H  HB2  . GLN B 1 113 ? 24.786  -32.889 20.125  1.00 17.83  ? 131 GLN B HB2  1 
ATOM   6363  H  HB3  . GLN B 1 113 ? 25.661  -33.497 18.946  1.00 17.83  ? 131 GLN B HB3  1 
ATOM   6364  H  HG2  . GLN B 1 113 ? 24.976  -31.508 17.697  1.00 16.94  ? 131 GLN B HG2  1 
ATOM   6365  H  HG3  . GLN B 1 113 ? 24.605  -30.911 19.122  1.00 16.94  ? 131 GLN B HG3  1 
ATOM   6366  H  HE21 . GLN B 1 113 ? 26.959  -32.148 20.344  1.00 17.34  ? 131 GLN B HE21 1 
ATOM   6367  H  HE22 . GLN B 1 113 ? 28.135  -31.322 19.953  1.00 17.34  ? 131 GLN B HE22 1 
ATOM   6368  N  N    . GLY B 1 114 ? 24.334  -34.997 16.688  1.00 15.03  ? 132 GLY B N    1 
ATOM   6369  C  CA   . GLY B 1 114 ? 24.614  -35.240 15.286  1.00 14.87  ? 132 GLY B CA   1 
ATOM   6370  C  C    . GLY B 1 114 ? 23.413  -35.016 14.390  1.00 14.33  ? 132 GLY B C    1 
ATOM   6371  O  O    . GLY B 1 114 ? 23.565  -34.639 13.226  1.00 15.69  ? 132 GLY B O    1 
ATOM   6372  H  H    . GLY B 1 114 ? 24.490  -35.660 17.213  1.00 18.04  ? 132 GLY B H    1 
ATOM   6373  H  HA2  . GLY B 1 114 ? 25.323  -34.646 14.995  1.00 17.85  ? 132 GLY B HA2  1 
ATOM   6374  H  HA3  . GLY B 1 114 ? 24.907  -36.158 15.175  1.00 17.85  ? 132 GLY B HA3  1 
ATOM   6375  N  N    . GLY B 1 115 ? 22.210  -35.269 14.906  1.00 14.79  ? 133 GLY B N    1 
ATOM   6376  C  CA   . GLY B 1 115 ? 21.011  -35.013 14.122  1.00 14.34  ? 133 GLY B CA   1 
ATOM   6377  C  C    . GLY B 1 115 ? 20.704  -33.532 14.004  1.00 13.98  ? 133 GLY B C    1 
ATOM   6378  O  O    . GLY B 1 115 ? 20.238  -33.066 12.960  1.00 14.99  ? 133 GLY B O    1 
ATOM   6379  H  H    . GLY B 1 115 ? 22.065  -35.583 15.694  1.00 17.75  ? 133 GLY B H    1 
ATOM   6380  H  HA2  . GLY B 1 115 ? 21.129  -35.373 13.229  1.00 17.21  ? 133 GLY B HA2  1 
ATOM   6381  H  HA3  . GLY B 1 115 ? 20.254  -35.450 14.541  1.00 17.21  ? 133 GLY B HA3  1 
ATOM   6382  N  N    . LEU B 1 116 ? 20.932  -32.779 15.083  1.00 13.48  ? 134 LEU B N    1 
ATOM   6383  C  CA   . LEU B 1 116 ? 20.838  -31.327 15.018  1.00 14.07  ? 134 LEU B CA   1 
ATOM   6384  C  C    . LEU B 1 116 ? 21.806  -30.777 13.983  1.00 13.96  ? 134 LEU B C    1 
ATOM   6385  O  O    . LEU B 1 116 ? 21.449  -29.896 13.190  1.00 13.75  ? 134 LEU B O    1 
ATOM   6386  C  CB   . LEU B 1 116 ? 21.149  -30.758 16.399  1.00 14.21  ? 134 LEU B CB   1 
ATOM   6387  C  CG   . LEU B 1 116 ? 21.211  -29.238 16.555  1.00 14.25  ? 134 LEU B CG   1 
ATOM   6388  C  CD1  . LEU B 1 116 ? 19.892  -28.595 16.159  1.00 15.67  ? 134 LEU B CD1  1 
ATOM   6389  C  CD2  . LEU B 1 116 ? 21.560  -28.901 17.993  1.00 16.63  ? 134 LEU B CD2  1 
ATOM   6390  H  H    . LEU B 1 116 ? 21.142  -33.086 15.859  1.00 16.18  ? 134 LEU B H    1 
ATOM   6391  H  HA   . LEU B 1 116 ? 19.942  -31.059 14.763  1.00 16.88  ? 134 LEU B HA   1 
ATOM   6392  H  HB2  . LEU B 1 116 ? 20.463  -31.072 17.008  1.00 17.05  ? 134 LEU B HB2  1 
ATOM   6393  H  HB3  . LEU B 1 116 ? 22.015  -31.100 16.670  1.00 17.05  ? 134 LEU B HB3  1 
ATOM   6394  H  HG   . LEU B 1 116 ? 21.893  -28.876 15.968  1.00 17.10  ? 134 LEU B HG   1 
ATOM   6395  H  HD11 . LEU B 1 116 ? 19.747  -28.731 15.209  1.00 18.80  ? 134 LEU B HD11 1 
ATOM   6396  H  HD12 . LEU B 1 116 ? 19.175  -29.008 16.665  1.00 18.80  ? 134 LEU B HD12 1 
ATOM   6397  H  HD13 . LEU B 1 116 ? 19.932  -27.646 16.354  1.00 18.80  ? 134 LEU B HD13 1 
ATOM   6398  H  HD21 . LEU B 1 116 ? 22.465  -29.200 18.176  1.00 19.95  ? 134 LEU B HD21 1 
ATOM   6399  H  HD22 . LEU B 1 116 ? 21.497  -27.942 18.117  1.00 19.95  ? 134 LEU B HD22 1 
ATOM   6400  H  HD23 . LEU B 1 116 ? 20.937  -29.353 18.583  1.00 19.95  ? 134 LEU B HD23 1 
ATOM   6401  N  N    . VAL B 1 117 ? 23.038  -31.300 13.980  1.00 14.97  ? 135 VAL B N    1 
ATOM   6402  C  CA   . VAL B 1 117 ? 24.045  -30.912 12.995  1.00 15.06  ? 135 VAL B CA   1 
ATOM   6403  C  C    . VAL B 1 117 ? 23.559  -31.213 11.580  1.00 14.66  ? 135 VAL B C    1 
ATOM   6404  O  O    . VAL B 1 117 ? 23.674  -30.382 10.670  1.00 15.19  ? 135 VAL B O    1 
ATOM   6405  C  CB   . VAL B 1 117 ? 25.374  -31.624 13.311  1.00 14.59  ? 135 VAL B CB   1 
ATOM   6406  C  CG1  . VAL B 1 117 ? 26.315  -31.594 12.110  1.00 15.36  ? 135 VAL B CG1  1 
ATOM   6407  C  CG2  . VAL B 1 117 ? 26.036  -30.998 14.538  1.00 14.42  ? 135 VAL B CG2  1 
ATOM   6408  H  H    . VAL B 1 117 ? 23.316  -31.886 14.543  1.00 17.97  ? 135 VAL B H    1 
ATOM   6409  H  HA   . VAL B 1 117 ? 24.189  -29.954 13.049  1.00 18.07  ? 135 VAL B HA   1 
ATOM   6410  H  HB   . VAL B 1 117 ? 25.185  -32.555 13.510  1.00 17.51  ? 135 VAL B HB   1 
ATOM   6411  H  HG11 . VAL B 1 117 ? 27.221  -31.756 12.414  1.00 18.43  ? 135 VAL B HG11 1 
ATOM   6412  H  HG12 . VAL B 1 117 ? 26.048  -32.285 11.483  1.00 18.43  ? 135 VAL B HG12 1 
ATOM   6413  H  HG13 . VAL B 1 117 ? 26.258  -30.723 11.686  1.00 18.43  ? 135 VAL B HG13 1 
ATOM   6414  H  HG21 . VAL B 1 117 ? 26.757  -31.573 14.836  1.00 17.30  ? 135 VAL B HG21 1 
ATOM   6415  H  HG22 . VAL B 1 117 ? 26.386  -30.126 14.297  1.00 17.30  ? 135 VAL B HG22 1 
ATOM   6416  H  HG23 . VAL B 1 117 ? 25.374  -30.905 15.241  1.00 17.30  ? 135 VAL B HG23 1 
ATOM   6417  N  N    . ALA B 1 118 ? 23.001  -32.401 11.374  1.00 14.15  ? 136 ALA B N    1 
ATOM   6418  C  CA   . ALA B 1 118 ? 22.552  -32.779 10.037  1.00 13.99  ? 136 ALA B CA   1 
ATOM   6419  C  C    . ALA B 1 118 ? 21.457  -31.839 9.544   1.00 14.39  ? 136 ALA B C    1 
ATOM   6420  O  O    . ALA B 1 118 ? 21.486  -31.363 8.402   1.00 14.81  ? 136 ALA B O    1 
ATOM   6421  C  CB   . ALA B 1 118 ? 22.037  -34.218 10.053  1.00 15.26  ? 136 ALA B CB   1 
ATOM   6422  H  H    . ALA B 1 118 ? 22.872  -32.997 11.980  1.00 16.98  ? 136 ALA B H    1 
ATOM   6423  H  HA   . ALA B 1 118 ? 23.304  -32.725 9.427   1.00 16.78  ? 136 ALA B HA   1 
ATOM   6424  H  HB1  . ALA B 1 118 ? 21.375  -34.309 10.756  1.00 18.31  ? 136 ALA B HB1  1 
ATOM   6425  H  HB2  . ALA B 1 118 ? 21.636  -34.419 9.193   1.00 18.31  ? 136 ALA B HB2  1 
ATOM   6426  H  HB3  . ALA B 1 118 ? 22.781  -34.818 10.219  1.00 18.31  ? 136 ALA B HB3  1 
ATOM   6427  N  N    . GLN B 1 119 ? 20.474  -31.570 10.395  1.00 15.13  ? 137 GLN B N    1 
ATOM   6428  C  CA   . GLN B 1 119 ? 19.369  -30.707 10.004  1.00 15.35  ? 137 GLN B CA   1 
ATOM   6429  C  C    . GLN B 1 119 ? 19.830  -29.261 9.847   1.00 13.59  ? 137 GLN B C    1 
ATOM   6430  O  O    . GLN B 1 119 ? 19.347  -28.555 8.955   1.00 14.37  ? 137 GLN B O    1 
ATOM   6431  C  CB   . GLN B 1 119 ? 18.252  -30.869 11.029  1.00 16.66  ? 137 GLN B CB   1 
ATOM   6432  C  CG   . GLN B 1 119 ? 16.951  -30.215 10.644  1.00 16.87  ? 137 GLN B CG   1 
ATOM   6433  C  CD   . GLN B 1 119 ? 16.239  -30.883 9.478   1.00 18.23  ? 137 GLN B CD   1 
ATOM   6434  O  OE1  . GLN B 1 119 ? 16.742  -31.831 8.857   1.00 18.02  ? 137 GLN B OE1  1 
ATOM   6435  N  NE2  . GLN B 1 119 ? 15.049  -30.393 9.183   1.00 17.55  ? 137 GLN B NE2  1 
ATOM   6436  H  H    . GLN B 1 119 ? 20.424  -31.871 11.199  1.00 18.16  ? 137 GLN B H    1 
ATOM   6437  H  HA   . GLN B 1 119 ? 19.008  -30.965 9.141   1.00 18.41  ? 137 GLN B HA   1 
ATOM   6438  H  HB2  . GLN B 1 119 ? 18.079  -31.816 11.151  1.00 19.99  ? 137 GLN B HB2  1 
ATOM   6439  H  HB3  . GLN B 1 119 ? 18.542  -30.474 11.867  1.00 19.99  ? 137 GLN B HB3  1 
ATOM   6440  H  HG2  . GLN B 1 119 ? 16.353  -30.240 11.407  1.00 20.25  ? 137 GLN B HG2  1 
ATOM   6441  H  HG3  . GLN B 1 119 ? 17.129  -29.295 10.391  1.00 20.25  ? 137 GLN B HG3  1 
ATOM   6442  H  HE21 . GLN B 1 119 ? 14.728  -29.739 9.641   1.00 21.06  ? 137 GLN B HE21 1 
ATOM   6443  H  HE22 . GLN B 1 119 ? 14.595  -30.727 8.534   1.00 21.06  ? 137 GLN B HE22 1 
ATOM   6444  N  N    . TRP B 1 120 ? 20.785  -28.817 10.673  1.00 13.64  ? 138 TRP B N    1 
ATOM   6445  C  CA   . TRP B 1 120 ? 21.370  -27.489 10.488  1.00 13.65  ? 138 TRP B CA   1 
ATOM   6446  C  C    . TRP B 1 120 ? 22.052  -27.379 9.129   1.00 13.90  ? 138 TRP B C    1 
ATOM   6447  O  O    . TRP B 1 120 ? 21.887  -26.381 8.413   1.00 14.61  ? 138 TRP B O    1 
ATOM   6448  C  CB   . TRP B 1 120 ? 22.358  -27.209 11.627  1.00 13.00  ? 138 TRP B CB   1 
ATOM   6449  C  CG   . TRP B 1 120 ? 22.928  -25.809 11.650  1.00 13.41  ? 138 TRP B CG   1 
ATOM   6450  C  CD1  . TRP B 1 120 ? 24.094  -25.384 11.078  1.00 14.40  ? 138 TRP B CD1  1 
ATOM   6451  C  CD2  . TRP B 1 120 ? 22.355  -24.663 12.286  1.00 13.76  ? 138 TRP B CD2  1 
ATOM   6452  N  NE1  . TRP B 1 120 ? 24.276  -24.042 11.312  1.00 14.35  ? 138 TRP B NE1  1 
ATOM   6453  C  CE2  . TRP B 1 120 ? 23.219  -23.575 12.049  1.00 12.88  ? 138 TRP B CE2  1 
ATOM   6454  C  CE3  . TRP B 1 120 ? 21.194  -24.450 13.031  1.00 13.59  ? 138 TRP B CE3  1 
ATOM   6455  C  CZ2  . TRP B 1 120 ? 22.958  -22.295 12.536  1.00 13.53  ? 138 TRP B CZ2  1 
ATOM   6456  C  CZ3  . TRP B 1 120 ? 20.935  -23.184 13.508  1.00 14.09  ? 138 TRP B CZ3  1 
ATOM   6457  C  CH2  . TRP B 1 120 ? 21.815  -22.123 13.265  1.00 14.23  ? 138 TRP B CH2  1 
ATOM   6458  H  H    . TRP B 1 120 ? 21.105  -29.259 11.338  1.00 16.37  ? 138 TRP B H    1 
ATOM   6459  H  HA   . TRP B 1 120 ? 20.673  -26.815 10.520  1.00 16.38  ? 138 TRP B HA   1 
ATOM   6460  H  HB2  . TRP B 1 120 ? 21.901  -27.351 12.471  1.00 15.59  ? 138 TRP B HB2  1 
ATOM   6461  H  HB3  . TRP B 1 120 ? 23.103  -27.825 11.545  1.00 15.59  ? 138 TRP B HB3  1 
ATOM   6462  H  HD1  . TRP B 1 120 ? 24.680  -25.925 10.599  1.00 17.28  ? 138 TRP B HD1  1 
ATOM   6463  H  HE1  . TRP B 1 120 ? 24.944  -23.573 11.041  1.00 17.22  ? 138 TRP B HE1  1 
ATOM   6464  H  HE3  . TRP B 1 120 ? 20.606  -25.150 13.202  1.00 16.31  ? 138 TRP B HE3  1 
ATOM   6465  H  HZ2  . TRP B 1 120 ? 23.539  -21.587 12.372  1.00 16.24  ? 138 TRP B HZ2  1 
ATOM   6466  H  HZ3  . TRP B 1 120 ? 20.161  -23.031 14.000  1.00 16.91  ? 138 TRP B HZ3  1 
ATOM   6467  H  HH2  . TRP B 1 120 ? 21.618  -21.282 13.609  1.00 17.07  ? 138 TRP B HH2  1 
ATOM   6468  N  N    . GLY B 1 121 ? 22.820  -28.400 8.748   1.00 13.97  ? 139 GLY B N    1 
ATOM   6469  C  CA   . GLY B 1 121 ? 23.472  -28.366 7.452   1.00 13.23  ? 139 GLY B CA   1 
ATOM   6470  C  C    . GLY B 1 121 ? 22.488  -28.363 6.296   1.00 13.49  ? 139 GLY B C    1 
ATOM   6471  O  O    . GLY B 1 121 ? 22.650  -27.604 5.341   1.00 14.11  ? 139 GLY B O    1 
ATOM   6472  H  H    . GLY B 1 121 ? 22.975  -29.106 9.214   1.00 16.76  ? 139 GLY B H    1 
ATOM   6473  H  HA2  . GLY B 1 121 ? 24.016  -27.565 7.389   1.00 15.88  ? 139 GLY B HA2  1 
ATOM   6474  H  HA3  . GLY B 1 121 ? 24.043  -29.144 7.361   1.00 15.88  ? 139 GLY B HA3  1 
ATOM   6475  N  N    . LEU B 1 122 ? 21.451  -29.202 6.370   1.00 12.96  ? 140 LEU B N    1 
ATOM   6476  C  CA   . LEU B 1 122 ? 20.444  -29.233 5.308   1.00 12.90  ? 140 LEU B CA   1 
ATOM   6477  C  C    . LEU B 1 122 ? 19.670  -27.924 5.229   1.00 14.59  ? 140 LEU B C    1 
ATOM   6478  O  O    . LEU B 1 122 ? 19.249  -27.516 4.139   1.00 15.31  ? 140 LEU B O    1 
ATOM   6479  C  CB   . LEU B 1 122 ? 19.494  -30.412 5.537   1.00 14.39  ? 140 LEU B CB   1 
ATOM   6480  C  CG   . LEU B 1 122 ? 20.097  -31.798 5.291   1.00 15.45  ? 140 LEU B CG   1 
ATOM   6481  C  CD1  . LEU B 1 122 ? 19.265  -32.908 5.943   1.00 16.77  ? 140 LEU B CD1  1 
ATOM   6482  C  CD2  . LEU B 1 122 ? 20.234  -32.037 3.788   1.00 16.55  ? 140 LEU B CD2  1 
ATOM   6483  H  H    . LEU B 1 122 ? 21.309  -29.754 7.014   1.00 15.55  ? 140 LEU B H    1 
ATOM   6484  H  HA   . LEU B 1 122 ? 20.885  -29.362 4.454   1.00 15.48  ? 140 LEU B HA   1 
ATOM   6485  H  HB2  . LEU B 1 122 ? 19.193  -30.387 6.459   1.00 17.26  ? 140 LEU B HB2  1 
ATOM   6486  H  HB3  . LEU B 1 122 ? 18.737  -30.315 4.939   1.00 17.26  ? 140 LEU B HB3  1 
ATOM   6487  H  HG   . LEU B 1 122 ? 20.976  -31.832 5.700   1.00 18.54  ? 140 LEU B HG   1 
ATOM   6488  H  HD11 . LEU B 1 122 ? 18.379  -32.910 5.550   1.00 20.13  ? 140 LEU B HD11 1 
ATOM   6489  H  HD12 . LEU B 1 122 ? 19.699  -33.761 5.786   1.00 20.13  ? 140 LEU B HD12 1 
ATOM   6490  H  HD13 . LEU B 1 122 ? 19.204  -32.739 6.896   1.00 20.13  ? 140 LEU B HD13 1 
ATOM   6491  H  HD21 . LEU B 1 122 ? 19.353  -32.004 3.382   1.00 19.86  ? 140 LEU B HD21 1 
ATOM   6492  H  HD22 . LEU B 1 122 ? 20.799  -31.347 3.408   1.00 19.86  ? 140 LEU B HD22 1 
ATOM   6493  H  HD23 . LEU B 1 122 ? 20.633  -32.909 3.642   1.00 19.86  ? 140 LEU B HD23 1 
ATOM   6494  N  N    . THR B 1 123 ? 19.496  -27.242 6.361   1.00 13.57  ? 141 THR B N    1 
ATOM   6495  C  CA   . THR B 1 123 ? 18.768  -25.979 6.360   1.00 14.59  ? 141 THR B CA   1 
ATOM   6496  C  C    . THR B 1 123 ? 19.589  -24.877 5.701   1.00 14.77  ? 141 THR B C    1 
ATOM   6497  O  O    . THR B 1 123 ? 19.072  -24.118 4.874   1.00 16.07  ? 141 THR B O    1 
ATOM   6498  C  CB   . THR B 1 123 ? 18.394  -25.597 7.794   1.00 14.96  ? 141 THR B CB   1 
ATOM   6499  O  OG1  . THR B 1 123 ? 17.492  -26.572 8.339   1.00 14.41  ? 141 THR B OG1  1 
ATOM   6500  C  CG2  . THR B 1 123 ? 17.732  -24.230 7.844   1.00 16.41  ? 141 THR B CG2  1 
ATOM   6501  H  H    . THR B 1 123 ? 19.787  -27.487 7.132   1.00 16.29  ? 141 THR B H    1 
ATOM   6502  H  HA   . THR B 1 123 ? 17.948  -26.084 5.852   1.00 17.51  ? 141 THR B HA   1 
ATOM   6503  H  HB   . THR B 1 123 ? 19.202  -25.563 8.329   1.00 17.95  ? 141 THR B HB   1 
ATOM   6504  H  HG1  . THR B 1 123 ? 17.236  -26.331 9.102   1.00 17.30  ? 141 THR B HG1  1 
ATOM   6505  H  HG21 . THR B 1 123 ? 18.400  -23.534 7.745   1.00 19.70  ? 141 THR B HG21 1 
ATOM   6506  H  HG22 . THR B 1 123 ? 17.084  -24.148 7.127   1.00 19.70  ? 141 THR B HG22 1 
ATOM   6507  H  HG23 . THR B 1 123 ? 17.278  -24.111 8.694   1.00 19.70  ? 141 THR B HG23 1 
ATOM   6508  N  N    . PHE B 1 124 ? 20.879  -24.780 6.041   1.00 14.16  ? 142 PHE B N    1 
ATOM   6509  C  CA   . PHE B 1 124 ? 21.663  -23.600 5.695   1.00 14.42  ? 142 PHE B CA   1 
ATOM   6510  C  C    . PHE B 1 124 ? 22.666  -23.796 4.568   1.00 14.90  ? 142 PHE B C    1 
ATOM   6511  O  O    . PHE B 1 124 ? 23.223  -22.799 4.088   1.00 14.60  ? 142 PHE B O    1 
ATOM   6512  C  CB   . PHE B 1 124 ? 22.361  -23.043 6.947   1.00 14.32  ? 142 PHE B CB   1 
ATOM   6513  C  CG   . PHE B 1 124 ? 21.405  -22.448 7.938   1.00 14.20  ? 142 PHE B CG   1 
ATOM   6514  C  CD1  . PHE B 1 124 ? 20.723  -21.277 7.645   1.00 14.30  ? 142 PHE B CD1  1 
ATOM   6515  C  CD2  . PHE B 1 124 ? 21.157  -23.073 9.144   1.00 14.21  ? 142 PHE B CD2  1 
ATOM   6516  C  CE1  . PHE B 1 124 ? 19.820  -20.733 8.546   1.00 14.47  ? 142 PHE B CE1  1 
ATOM   6517  C  CE2  . PHE B 1 124 ? 20.255  -22.537 10.051  1.00 14.66  ? 142 PHE B CE2  1 
ATOM   6518  C  CZ   . PHE B 1 124 ? 19.593  -21.359 9.753   1.00 15.21  ? 142 PHE B CZ   1 
ATOM   6519  H  H    . PHE B 1 124 ? 21.316  -25.384 6.470   1.00 16.99  ? 142 PHE B H    1 
ATOM   6520  H  HA   . PHE B 1 124 ? 21.050  -22.919 5.376   1.00 17.30  ? 142 PHE B HA   1 
ATOM   6521  H  HB2  . PHE B 1 124 ? 22.837  -23.764 7.388   1.00 17.18  ? 142 PHE B HB2  1 
ATOM   6522  H  HB3  . PHE B 1 124 ? 22.983  -22.350 6.678   1.00 17.18  ? 142 PHE B HB3  1 
ATOM   6523  H  HD1  . PHE B 1 124 ? 20.873  -20.850 6.833   1.00 17.16  ? 142 PHE B HD1  1 
ATOM   6524  H  HD2  . PHE B 1 124 ? 21.601  -23.864 9.351   1.00 17.05  ? 142 PHE B HD2  1 
ATOM   6525  H  HE1  . PHE B 1 124 ? 19.369  -19.948 8.336   1.00 17.37  ? 142 PHE B HE1  1 
ATOM   6526  H  HE2  . PHE B 1 124 ? 20.096  -22.968 10.859  1.00 17.59  ? 142 PHE B HE2  1 
ATOM   6527  H  HZ   . PHE B 1 124 ? 18.997  -20.991 10.365  1.00 18.25  ? 142 PHE B HZ   1 
ATOM   6528  N  N    . PHE B 1 125 ? 22.882  -25.030 4.103   1.00 14.06  ? 143 PHE B N    1 
ATOM   6529  C  CA   . PHE B 1 125 ? 23.828  -25.338 3.032   1.00 14.77  ? 143 PHE B CA   1 
ATOM   6530  C  C    . PHE B 1 125 ? 23.050  -26.040 1.925   1.00 15.03  ? 143 PHE B C    1 
ATOM   6531  O  O    . PHE B 1 125 ? 23.018  -27.277 1.860   1.00 15.19  ? 143 PHE B O    1 
ATOM   6532  C  CB   . PHE B 1 125 ? 24.996  -26.178 3.553   1.00 14.09  ? 143 PHE B CB   1 
ATOM   6533  C  CG   . PHE B 1 125 ? 25.882  -25.434 4.510   1.00 14.26  ? 143 PHE B CG   1 
ATOM   6534  C  CD1  . PHE B 1 125 ? 25.485  -25.225 5.820   1.00 14.95  ? 143 PHE B CD1  1 
ATOM   6535  C  CD2  . PHE B 1 125 ? 27.099  -24.919 4.090   1.00 16.02  ? 143 PHE B CD2  1 
ATOM   6536  C  CE1  . PHE B 1 125 ? 26.284  -24.506 6.694   1.00 15.35  ? 143 PHE B CE1  1 
ATOM   6537  C  CE2  . PHE B 1 125 ? 27.904  -24.208 4.957   1.00 16.60  ? 143 PHE B CE2  1 
ATOM   6538  C  CZ   . PHE B 1 125 ? 27.503  -24.010 6.265   1.00 15.88  ? 143 PHE B CZ   1 
ATOM   6539  H  H    . PHE B 1 125 ? 22.477  -25.726 4.404   1.00 16.87  ? 143 PHE B H    1 
ATOM   6540  H  HA   . PHE B 1 125 ? 24.203  -24.523 2.663   1.00 17.72  ? 143 PHE B HA   1 
ATOM   6541  H  HB2  . PHE B 1 125 ? 24.642  -26.954 4.015   1.00 16.91  ? 143 PHE B HB2  1 
ATOM   6542  H  HB3  . PHE B 1 125 ? 25.540  -26.460 2.800   1.00 16.91  ? 143 PHE B HB3  1 
ATOM   6543  H  HD1  . PHE B 1 125 ? 24.673  -25.570 6.116   1.00 17.94  ? 143 PHE B HD1  1 
ATOM   6544  H  HD2  . PHE B 1 125 ? 27.376  -25.054 3.213   1.00 19.23  ? 143 PHE B HD2  1 
ATOM   6545  H  HE1  . PHE B 1 125 ? 26.002  -24.358 7.568   1.00 18.42  ? 143 PHE B HE1  1 
ATOM   6546  H  HE2  . PHE B 1 125 ? 28.716  -23.864 4.662   1.00 19.92  ? 143 PHE B HE2  1 
ATOM   6547  H  HZ   . PHE B 1 125 ? 28.050  -23.543 6.854   1.00 19.06  ? 143 PHE B HZ   1 
ATOM   6548  N  N    . PRO B 1 126 ? 22.385  -25.282 1.050   1.00 15.95  ? 144 PRO B N    1 
ATOM   6549  C  CA   . PRO B 1 126 ? 21.489  -25.919 0.068   1.00 15.79  ? 144 PRO B CA   1 
ATOM   6550  C  C    . PRO B 1 126 ? 22.149  -26.952 -0.829  1.00 15.95  ? 144 PRO B C    1 
ATOM   6551  O  O    . PRO B 1 126 ? 21.449  -27.844 -1.324  1.00 17.45  ? 144 PRO B O    1 
ATOM   6552  C  CB   . PRO B 1 126 ? 20.953  -24.730 -0.745  1.00 17.15  ? 144 PRO B CB   1 
ATOM   6553  C  CG   . PRO B 1 126 ? 21.051  -23.563 0.203   1.00 17.75  ? 144 PRO B CG   1 
ATOM   6554  C  CD   . PRO B 1 126 ? 22.311  -23.809 0.997   1.00 16.83  ? 144 PRO B CD   1 
ATOM   6555  H  HA   . PRO B 1 126 ? 20.758  -26.348 0.540   1.00 18.95  ? 144 PRO B HA   1 
ATOM   6556  H  HB2  . PRO B 1 126 ? 21.503  -24.589 -1.532  1.00 20.58  ? 144 PRO B HB2  1 
ATOM   6557  H  HB3  . PRO B 1 126 ? 20.034  -24.892 -1.007  1.00 20.58  ? 144 PRO B HB3  1 
ATOM   6558  H  HG2  . PRO B 1 126 ? 21.113  -22.735 -0.297  1.00 21.30  ? 144 PRO B HG2  1 
ATOM   6559  H  HG3  . PRO B 1 126 ? 20.274  -23.543 0.784   1.00 21.30  ? 144 PRO B HG3  1 
ATOM   6560  H  HD2  . PRO B 1 126 ? 23.085  -23.439 0.544   1.00 20.20  ? 144 PRO B HD2  1 
ATOM   6561  H  HD3  . PRO B 1 126 ? 22.238  -23.433 1.889   1.00 20.20  ? 144 PRO B HD3  1 
ATOM   6562  N  N    . SER B 1 127 ? 23.467  -26.876 -1.046  1.00 16.38  ? 145 SER B N    1 
ATOM   6563  C  CA   . SER B 1 127 ? 24.097  -27.750 -2.025  1.00 17.16  ? 145 SER B CA   1 
ATOM   6564  C  C    . SER B 1 127 ? 24.018  -29.221 -1.643  1.00 16.64  ? 145 SER B C    1 
ATOM   6565  O  O    . SER B 1 127 ? 24.132  -30.081 -2.523  1.00 18.40  ? 145 SER B O    1 
ATOM   6566  C  CB   . SER B 1 127 ? 25.566  -27.380 -2.213  1.00 18.25  ? 145 SER B CB   1 
ATOM   6567  O  OG   . SER B 1 127 ? 26.335  -27.864 -1.133  1.00 19.80  ? 145 SER B OG   1 
ATOM   6568  H  H    . SER B 1 127 ? 24.003  -26.336 -0.645  1.00 19.65  ? 145 SER B H    1 
ATOM   6569  H  HA   . SER B 1 127 ? 23.631  -27.622 -2.866  1.00 20.60  ? 145 SER B HA   1 
ATOM   6570  H  HB2  . SER B 1 127 ? 25.891  -27.775 -3.037  1.00 21.90  ? 145 SER B HB2  1 
ATOM   6571  H  HB3  . SER B 1 127 ? 25.648  -26.414 -2.253  1.00 21.90  ? 145 SER B HB3  1 
ATOM   6572  H  HG   . SER B 1 127 ? 26.046  -27.549 -0.410  1.00 23.76  ? 145 SER B HG   1 
ATOM   6573  N  N    . ILE B 1 128 ? 23.851  -29.537 -0.354  1.00 16.03  ? 146 ILE B N    1 
ATOM   6574  C  CA   . ILE B 1 128 ? 23.863  -30.939 0.060   1.00 16.16  ? 146 ILE B CA   1 
ATOM   6575  C  C    . ILE B 1 128 ? 22.482  -31.588 0.030   1.00 15.85  ? 146 ILE B C    1 
ATOM   6576  O  O    . ILE B 1 128 ? 22.378  -32.809 0.224   1.00 16.59  ? 146 ILE B O    1 
ATOM   6577  C  CB   . ILE B 1 128 ? 24.508  -31.174 1.446   1.00 16.06  ? 146 ILE B CB   1 
ATOM   6578  C  CG1  . ILE B 1 128 ? 23.753  -30.399 2.527   1.00 16.84  ? 146 ILE B CG1  1 
ATOM   6579  C  CG2  . ILE B 1 128 ? 25.983  -30.818 1.420   1.00 17.22  ? 146 ILE B CG2  1 
ATOM   6580  C  CD1  . ILE B 1 128 ? 24.015  -30.899 3.944   1.00 18.33  ? 146 ILE B CD1  1 
ATOM   6581  H  H    . ILE B 1 128 ? 23.732  -28.971 0.283   1.00 19.24  ? 146 ILE B H    1 
ATOM   6582  H  HA   . ILE B 1 128 ? 24.427  -31.393 -0.586  1.00 19.39  ? 146 ILE B HA   1 
ATOM   6583  H  HB   . ILE B 1 128 ? 24.442  -32.118 1.662   1.00 19.27  ? 146 ILE B HB   1 
ATOM   6584  H  HG12 . ILE B 1 128 ? 24.023  -29.468 2.488   1.00 20.21  ? 146 ILE B HG12 1 
ATOM   6585  H  HG13 . ILE B 1 128 ? 22.801  -30.477 2.358   1.00 20.21  ? 146 ILE B HG13 1 
ATOM   6586  H  HG21 . ILE B 1 128 ? 26.445  -31.428 0.824   1.00 20.66  ? 146 ILE B HG21 1 
ATOM   6587  H  HG22 . ILE B 1 128 ? 26.082  -29.907 1.103   1.00 20.66  ? 146 ILE B HG22 1 
ATOM   6588  H  HG23 . ILE B 1 128 ? 26.343  -30.897 2.318   1.00 20.66  ? 146 ILE B HG23 1 
ATOM   6589  H  HD11 . ILE B 1 128 ? 24.966  -30.840 4.129   1.00 22.00  ? 146 ILE B HD11 1 
ATOM   6590  H  HD12 . ILE B 1 128 ? 23.521  -30.346 4.570   1.00 22.00  ? 146 ILE B HD12 1 
ATOM   6591  H  HD13 . ILE B 1 128 ? 23.721  -31.821 4.013   1.00 22.00  ? 146 ILE B HD13 1 
ATOM   6592  N  N    . ARG B 1 129 ? 21.414  -30.815 -0.187  1.00 16.07  ? 147 ARG B N    1 
ATOM   6593  C  CA   . ARG B 1 129 ? 20.079  -31.406 -0.213  1.00 16.40  ? 147 ARG B CA   1 
ATOM   6594  C  C    . ARG B 1 129 ? 19.948  -32.455 -1.310  1.00 16.07  ? 147 ARG B C    1 
ATOM   6595  O  O    . ARG B 1 129 ? 19.228  -33.447 -1.140  1.00 18.23  ? 147 ARG B O    1 
ATOM   6596  C  CB   . ARG B 1 129 ? 19.023  -30.316 -0.376  1.00 17.35  ? 147 ARG B CB   1 
ATOM   6597  C  CG   . ARG B 1 129 ? 18.985  -29.349 0.788   1.00 17.97  ? 147 ARG B CG   1 
ATOM   6598  C  CD   . ARG B 1 129 ? 18.055  -28.182 0.515   1.00 17.91  ? 147 ARG B CD   1 
ATOM   6599  N  NE   . ARG B 1 129 ? 18.188  -27.174 1.553   1.00 17.86  ? 147 ARG B NE   1 
ATOM   6600  C  CZ   . ARG B 1 129 ? 17.865  -25.894 1.421   1.00 18.67  ? 147 ARG B CZ   1 
ATOM   6601  N  NH1  . ARG B 1 129 ? 17.370  -25.439 0.280   1.00 20.43  ? 147 ARG B NH1  1 
ATOM   6602  N  NH2  . ARG B 1 129 ? 18.042  -25.073 2.442   1.00 20.88  ? 147 ARG B NH2  1 
ATOM   6603  H  H    . ARG B 1 129 ? 21.437  -29.965 -0.318  1.00 19.28  ? 147 ARG B H    1 
ATOM   6604  H  HA   . ARG B 1 129 ? 19.917  -31.848 0.635   1.00 19.68  ? 147 ARG B HA   1 
ATOM   6605  H  HB2  . ARG B 1 129 ? 19.216  -29.810 -1.181  1.00 20.82  ? 147 ARG B HB2  1 
ATOM   6606  H  HB3  . ARG B 1 129 ? 18.150  -30.733 -0.448  1.00 20.82  ? 147 ARG B HB3  1 
ATOM   6607  H  HG2  . ARG B 1 129 ? 18.669  -29.811 1.580   1.00 21.56  ? 147 ARG B HG2  1 
ATOM   6608  H  HG3  . ARG B 1 129 ? 19.876  -28.997 0.942   1.00 21.56  ? 147 ARG B HG3  1 
ATOM   6609  H  HD2  . ARG B 1 129 ? 18.279  -27.780 -0.339  1.00 21.49  ? 147 ARG B HD2  1 
ATOM   6610  H  HD3  . ARG B 1 129 ? 17.137  -28.495 0.503   1.00 21.49  ? 147 ARG B HD3  1 
ATOM   6611  H  HE   . ARG B 1 129 ? 18.502  -27.427 2.313   1.00 21.43  ? 147 ARG B HE   1 
ATOM   6612  H  HH11 . ARG B 1 129 ? 17.256  -25.974 -0.383  1.00 24.51  ? 147 ARG B HH11 1 
ATOM   6613  H  HH12 . ARG B 1 129 ? 17.163  -24.608 0.203   1.00 24.51  ? 147 ARG B HH12 1 
ATOM   6614  H  HH21 . ARG B 1 129 ? 18.363  -25.369 3.182   1.00 25.06  ? 147 ARG B HH21 1 
ATOM   6615  H  HH22 . ARG B 1 129 ? 17.835  -24.241 2.365   1.00 25.06  ? 147 ARG B HH22 1 
ATOM   6616  N  N    . SER B 1 130 ? 20.629  -32.257 -2.436  1.00 16.57  ? 148 SER B N    1 
ATOM   6617  C  CA   . SER B 1 130 ? 20.604  -33.196 -3.551  1.00 18.01  ? 148 SER B CA   1 
ATOM   6618  C  C    . SER B 1 130 ? 21.596  -34.335 -3.377  1.00 17.13  ? 148 SER B C    1 
ATOM   6619  O  O    . SER B 1 130 ? 21.663  -35.217 -4.245  1.00 19.63  ? 148 SER B O    1 
ATOM   6620  C  CB   . SER B 1 130 ? 20.913  -32.452 -4.853  1.00 19.08  ? 148 SER B CB   1 
ATOM   6621  O  OG   . SER B 1 130 ? 22.232  -31.924 -4.846  1.00 20.42  ? 148 SER B OG   1 
ATOM   6622  H  H    . SER B 1 130 ? 21.124  -31.569 -2.581  1.00 19.88  ? 148 SER B H    1 
ATOM   6623  H  HA   . SER B 1 130 ? 19.716  -33.579 -3.620  1.00 21.61  ? 148 SER B HA   1 
ATOM   6624  H  HB2  . SER B 1 130 ? 20.827  -33.070 -5.596  1.00 22.90  ? 148 SER B HB2  1 
ATOM   6625  H  HB3  . SER B 1 130 ? 20.283  -31.721 -4.955  1.00 22.90  ? 148 SER B HB3  1 
ATOM   6626  H  HG   . SER B 1 130 ? 22.310  -31.356 -4.232  1.00 24.50  ? 148 SER B HG   1 
ATOM   6627  N  N    . LYS B 1 131 ? 22.351  -34.346 -2.275  1.00 16.21  ? 149 LYS B N    1 
ATOM   6628  C  CA   . LYS B 1 131 ? 23.395  -35.334 -2.048  1.00 17.07  ? 149 LYS B CA   1 
ATOM   6629  C  C    . LYS B 1 131 ? 23.106  -36.254 -0.872  1.00 17.07  ? 149 LYS B C    1 
ATOM   6630  O  O    . LYS B 1 131 ? 23.739  -37.307 -0.765  1.00 17.32  ? 149 LYS B O    1 
ATOM   6631  C  CB   . LYS B 1 131 ? 24.746  -34.632 -1.837  1.00 18.00  ? 149 LYS B CB   1 
ATOM   6632  C  CG   . LYS B 1 131 ? 25.142  -33.778 -3.031  1.00 18.12  ? 149 LYS B CG   1 
ATOM   6633  C  CD   . LYS B 1 131 ? 26.478  -33.055 -2.878  1.00 19.52  ? 149 LYS B CD   1 
ATOM   6634  C  CE   . LYS B 1 131 ? 26.764  -32.251 -4.148  1.00 22.25  ? 149 LYS B CE   1 
ATOM   6635  N  NZ   . LYS B 1 131 ? 28.029  -31.471 -4.123  1.00 25.60  ? 149 LYS B NZ   1 
ATOM   6636  H  H    . LYS B 1 131 ? 22.272  -33.778 -1.634  1.00 19.45  ? 149 LYS B H    1 
ATOM   6637  H  HA   . LYS B 1 131 ? 23.484  -35.894 -2.834  1.00 20.48  ? 149 LYS B HA   1 
ATOM   6638  H  HB2  . LYS B 1 131 ? 24.687  -34.055 -1.059  1.00 21.60  ? 149 LYS B HB2  1 
ATOM   6639  H  HB3  . LYS B 1 131 ? 25.435  -35.301 -1.702  1.00 21.60  ? 149 LYS B HB3  1 
ATOM   6640  H  HG2  . LYS B 1 131 ? 25.207  -34.350 -3.812  1.00 21.74  ? 149 LYS B HG2  1 
ATOM   6641  H  HG3  . LYS B 1 131 ? 24.459  -33.104 -3.170  1.00 21.74  ? 149 LYS B HG3  1 
ATOM   6642  H  HD2  . LYS B 1 131 ? 26.440  -32.447 -2.123  1.00 23.42  ? 149 LYS B HD2  1 
ATOM   6643  H  HD3  . LYS B 1 131 ? 27.190  -33.701 -2.748  1.00 23.42  ? 149 LYS B HD3  1 
ATOM   6644  H  HE2  . LYS B 1 131 ? 26.817  -32.866 -4.897  1.00 26.70  ? 149 LYS B HE2  1 
ATOM   6645  H  HE3  . LYS B 1 131 ? 26.038  -31.623 -4.285  1.00 26.70  ? 149 LYS B HE3  1 
ATOM   6646  H  HZ1  . LYS B 1 131 ? 28.132  -31.033 -4.890  1.00 30.72  ? 149 LYS B HZ1  1 
ATOM   6647  H  HZ2  . LYS B 1 131 ? 28.011  -30.883 -3.455  1.00 30.72  ? 149 LYS B HZ2  1 
ATOM   6648  H  HZ3  . LYS B 1 131 ? 28.722  -32.018 -4.007  1.00 30.72  ? 149 LYS B HZ3  1 
ATOM   6649  N  N    . VAL B 1 132 ? 22.163  -35.894 -0.010  1.00 17.60  ? 150 VAL B N    1 
ATOM   6650  C  CA   . VAL B 1 132 ? 21.749  -36.731 1.107   1.00 17.27  ? 150 VAL B CA   1 
ATOM   6651  C  C    . VAL B 1 132 ? 20.487  -37.469 0.683   1.00 18.33  ? 150 VAL B C    1 
ATOM   6652  O  O    . VAL B 1 132 ? 19.448  -36.855 0.408   1.00 17.84  ? 150 VAL B O    1 
ATOM   6653  C  CB   . VAL B 1 132 ? 21.516  -35.900 2.377   1.00 17.46  ? 150 VAL B CB   1 
ATOM   6654  C  CG1  . VAL B 1 132 ? 20.990  -36.785 3.496   1.00 17.73  ? 150 VAL B CG1  1 
ATOM   6655  C  CG2  . VAL B 1 132 ? 22.812  -35.227 2.827   1.00 19.12  ? 150 VAL B CG2  1 
ATOM   6656  H  H    . VAL B 1 132 ? 21.736  -35.149 -0.054  1.00 21.13  ? 150 VAL B H    1 
ATOM   6657  H  HA   . VAL B 1 132 ? 22.440  -37.384 1.302   1.00 20.72  ? 150 VAL B HA   1 
ATOM   6658  H  HB   . VAL B 1 132 ? 20.860  -35.213 2.179   1.00 20.95  ? 150 VAL B HB   1 
ATOM   6659  H  HG11 . VAL B 1 132 ? 21.482  -37.621 3.496   1.00 21.28  ? 150 VAL B HG11 1 
ATOM   6660  H  HG12 . VAL B 1 132 ? 21.113  -36.329 4.343   1.00 21.28  ? 150 VAL B HG12 1 
ATOM   6661  H  HG13 . VAL B 1 132 ? 20.047  -36.956 3.346   1.00 21.28  ? 150 VAL B HG13 1 
ATOM   6662  H  HG21 . VAL B 1 132 ? 23.504  -35.901 2.916   1.00 22.94  ? 150 VAL B HG21 1 
ATOM   6663  H  HG22 . VAL B 1 132 ? 23.074  -34.570 2.163   1.00 22.94  ? 150 VAL B HG22 1 
ATOM   6664  H  HG23 . VAL B 1 132 ? 22.662  -34.792 3.681   1.00 22.94  ? 150 VAL B HG23 1 
ATOM   6665  N  N    . ASP B 1 133 ? 20.596  -38.790 0.625   1.00 18.74  ? 151 ASP B N    1 
ATOM   6666  C  CA   . ASP B 1 133 ? 19.495  -39.641 0.208   1.00 21.15  ? 151 ASP B CA   1 
ATOM   6667  C  C    . ASP B 1 133 ? 18.390  -39.676 1.252   1.00 18.59  ? 151 ASP B C    1 
ATOM   6668  O  O    . ASP B 1 133 ? 17.200  -39.700 0.908   1.00 21.41  ? 151 ASP B O    1 
ATOM   6669  C  CB   . ASP B 1 133 ? 20.078  -41.033 0.006   1.00 26.62  ? 151 ASP B CB   1 
ATOM   6670  C  CG   . ASP B 1 133 ? 19.200  -41.912 -0.781  1.00 29.16  ? 151 ASP B CG   1 
ATOM   6671  O  OD1  . ASP B 1 133 ? 18.742  -41.472 -1.857  1.00 30.38  ? 151 ASP B OD1  1 
ATOM   6672  O  OD2  . ASP B 1 133 ? 19.001  -43.052 -0.326  1.00 29.86  ? 151 ASP B OD2  1 
ATOM   6673  H  H    . ASP B 1 133 ? 21.310  -39.226 0.825   1.00 22.48  ? 151 ASP B H    1 
ATOM   6674  H  HA   . ASP B 1 133 ? 19.095  -39.313 -0.613  1.00 25.38  ? 151 ASP B HA   1 
ATOM   6675  H  HB2  . ASP B 1 133 ? 20.923  -40.956 -0.464  1.00 31.95  ? 151 ASP B HB2  1 
ATOM   6676  H  HB3  . ASP B 1 133 ? 20.216  -41.446 0.873   1.00 31.95  ? 151 ASP B HB3  1 
ATOM   6677  N  N    . ARG B 1 134 ? 18.766  -39.700 2.526   1.00 17.71  ? 152 ARG B N    1 
ATOM   6678  C  CA   . ARG B 1 134 ? 17.855  -39.845 3.653   1.00 17.91  ? 152 ARG B CA   1 
ATOM   6679  C  C    . ARG B 1 134 ? 18.642  -39.567 4.925   1.00 16.78  ? 152 ARG B C    1 
ATOM   6680  O  O    . ARG B 1 134 ? 19.873  -39.655 4.941   1.00 16.37  ? 152 ARG B O    1 
ATOM   6681  C  CB   . ARG B 1 134 ? 17.276  -41.255 3.720   1.00 19.02  ? 152 ARG B CB   1 
ATOM   6682  C  CG   . ARG B 1 134 ? 18.332  -42.316 4.025   1.00 20.46  ? 152 ARG B CG   1 
ATOM   6683  C  CD   . ARG B 1 134 ? 17.864  -43.708 3.629   1.00 21.59  ? 152 ARG B CD   1 
ATOM   6684  N  NE   . ARG B 1 134 ? 17.801  -43.852 2.178   1.00 22.68  ? 152 ARG B NE   1 
ATOM   6685  C  CZ   . ARG B 1 134 ? 17.044  -44.736 1.542   1.00 23.44  ? 152 ARG B CZ   1 
ATOM   6686  N  NH1  . ARG B 1 134 ? 16.271  -45.560 2.233   1.00 24.21  ? 152 ARG B NH1  1 
ATOM   6687  N  NH2  . ARG B 1 134 ? 17.050  -44.783 0.214   1.00 24.11  ? 152 ARG B NH2  1 
ATOM   6688  H  H    . ARG B 1 134 ? 19.586  -39.630 2.776   1.00 21.25  ? 152 ARG B H    1 
ATOM   6689  H  HA   . ARG B 1 134 ? 17.131  -39.206 3.569   1.00 21.49  ? 152 ARG B HA   1 
ATOM   6690  H  HB2  . ARG B 1 134 ? 16.607  -41.288 4.422   1.00 22.82  ? 152 ARG B HB2  1 
ATOM   6691  H  HB3  . ARG B 1 134 ? 16.871  -41.471 2.866   1.00 22.82  ? 152 ARG B HB3  1 
ATOM   6692  H  HG2  . ARG B 1 134 ? 19.140  -42.115 3.528   1.00 24.56  ? 152 ARG B HG2  1 
ATOM   6693  H  HG3  . ARG B 1 134 ? 18.519  -42.318 4.976   1.00 24.56  ? 152 ARG B HG3  1 
ATOM   6694  H  HD2  . ARG B 1 134 ? 18.486  -44.367 3.975   1.00 25.91  ? 152 ARG B HD2  1 
ATOM   6695  H  HD3  . ARG B 1 134 ? 16.978  -43.865 3.991   1.00 25.91  ? 152 ARG B HD3  1 
ATOM   6696  H  HE   . ARG B 1 134 ? 18.288  -43.326 1.702   1.00 27.22  ? 152 ARG B HE   1 
ATOM   6697  H  HH11 . ARG B 1 134 ? 16.260  -45.521 3.092   1.00 29.05  ? 152 ARG B HH11 1 
ATOM   6698  H  HH12 . ARG B 1 134 ? 15.779  -46.134 1.822   1.00 29.05  ? 152 ARG B HH12 1 
ATOM   6699  H  HH21 . ARG B 1 134 ? 17.545  -44.240 -0.233  1.00 28.93  ? 152 ARG B HH21 1 
ATOM   6700  H  HH22 . ARG B 1 134 ? 16.560  -45.357 -0.198  1.00 28.93  ? 152 ARG B HH22 1 
ATOM   6701  N  N    . LEU B 1 135 ? 17.910  -39.246 5.996   1.00 16.78  ? 153 LEU B N    1 
ATOM   6702  C  CA   . LEU B 1 135 ? 18.472  -39.000 7.321   1.00 16.91  ? 153 LEU B CA   1 
ATOM   6703  C  C    . LEU B 1 135 ? 17.808  -39.950 8.308   1.00 16.37  ? 153 LEU B C    1 
ATOM   6704  O  O    . LEU B 1 135 ? 16.575  -40.023 8.370   1.00 17.33  ? 153 LEU B O    1 
ATOM   6705  C  CB   . LEU B 1 135 ? 18.220  -37.547 7.742   1.00 16.85  ? 153 LEU B CB   1 
ATOM   6706  C  CG   . LEU B 1 135 ? 18.579  -37.128 9.174   1.00 15.85  ? 153 LEU B CG   1 
ATOM   6707  C  CD1  . LEU B 1 135 ? 20.047  -37.369 9.457   1.00 17.07  ? 153 LEU B CD1  1 
ATOM   6708  C  CD2  . LEU B 1 135 ? 18.227  -35.661 9.425   1.00 16.21  ? 153 LEU B CD2  1 
ATOM   6709  H  H    . LEU B 1 135 ? 17.055  -39.164 5.976   1.00 20.14  ? 153 LEU B H    1 
ATOM   6710  H  HA   . LEU B 1 135 ? 19.428  -39.164 7.322   1.00 20.30  ? 153 LEU B HA   1 
ATOM   6711  H  HB2  . LEU B 1 135 ? 18.735  -36.977 7.150   1.00 20.22  ? 153 LEU B HB2  1 
ATOM   6712  H  HB3  . LEU B 1 135 ? 17.272  -37.371 7.632   1.00 20.22  ? 153 LEU B HB3  1 
ATOM   6713  H  HG   . LEU B 1 135 ? 18.058  -37.670 9.786   1.00 19.03  ? 153 LEU B HG   1 
ATOM   6714  H  HD11 . LEU B 1 135 ? 20.578  -36.885 8.805   1.00 20.48  ? 153 LEU B HD11 1 
ATOM   6715  H  HD12 . LEU B 1 135 ? 20.252  -37.054 10.351  1.00 20.48  ? 153 LEU B HD12 1 
ATOM   6716  H  HD13 . LEU B 1 135 ? 20.229  -38.320 9.391   1.00 20.48  ? 153 LEU B HD13 1 
ATOM   6717  H  HD21 . LEU B 1 135 ? 18.770  -35.102 8.846   1.00 19.45  ? 153 LEU B HD21 1 
ATOM   6718  H  HD22 . LEU B 1 135 ? 17.287  -35.523 9.230   1.00 19.45  ? 153 LEU B HD22 1 
ATOM   6719  H  HD23 . LEU B 1 135 ? 18.408  -35.447 10.354  1.00 19.45  ? 153 LEU B HD23 1 
ATOM   6720  N  N    . MET B 1 136 ? 18.620  -40.694 9.057   1.00 15.91  ? 154 MET B N    1 
ATOM   6721  C  CA   . MET B 1 136 ? 18.140  -41.594 10.110  1.00 16.50  ? 154 MET B CA   1 
ATOM   6722  C  C    . MET B 1 136 ? 18.758  -41.080 11.406  1.00 16.49  ? 154 MET B C    1 
ATOM   6723  O  O    . MET B 1 136 ? 19.941  -41.315 11.663  1.00 17.01  ? 154 MET B O    1 
ATOM   6724  C  CB   . MET B 1 136 ? 18.550  -43.034 9.822   1.00 17.55  ? 154 MET B CB   1 
ATOM   6725  C  CG   . MET B 1 136 ? 18.244  -44.047 10.933  1.00 18.34  ? 154 MET B CG   1 
ATOM   6726  S  SD   . MET B 1 136 ? 16.495  -44.283 11.307  1.00 19.43  ? 154 MET B SD   1 
ATOM   6727  C  CE   . MET B 1 136 ? 16.383  -43.453 12.894  1.00 20.20  ? 154 MET B CE   1 
ATOM   6728  H  H    . MET B 1 136 ? 19.475  -40.695 8.974   1.00 19.09  ? 154 MET B H    1 
ATOM   6729  H  HA   . MET B 1 136 ? 17.172  -41.573 10.164  1.00 19.80  ? 154 MET B HA   1 
ATOM   6730  H  HB2  . MET B 1 136 ? 18.082  -43.331 9.026   1.00 21.06  ? 154 MET B HB2  1 
ATOM   6731  H  HB3  . MET B 1 136 ? 19.508  -43.053 9.670   1.00 21.06  ? 154 MET B HB3  1 
ATOM   6732  H  HG2  . MET B 1 136 ? 18.601  -44.909 10.668  1.00 22.00  ? 154 MET B HG2  1 
ATOM   6733  H  HG3  . MET B 1 136 ? 18.675  -43.746 11.748  1.00 22.00  ? 154 MET B HG3  1 
ATOM   6734  H  HE1  . MET B 1 136 ? 16.513  -42.501 12.762  1.00 24.24  ? 154 MET B HE1  1 
ATOM   6735  H  HE2  . MET B 1 136 ? 15.506  -43.618 13.275  1.00 24.24  ? 154 MET B HE2  1 
ATOM   6736  H  HE3  . MET B 1 136 ? 17.070  -43.802 13.482  1.00 24.24  ? 154 MET B HE3  1 
ATOM   6737  N  N    . ALA B 1 137 ? 17.971  -40.362 12.205  1.00 15.85  ? 155 ALA B N    1 
ATOM   6738  C  CA   . ALA B 1 137 ? 18.458  -39.685 13.400  1.00 15.30  ? 155 ALA B CA   1 
ATOM   6739  C  C    . ALA B 1 137 ? 17.960  -40.395 14.653  1.00 16.06  ? 155 ALA B C    1 
ATOM   6740  O  O    . ALA B 1 137 ? 16.750  -40.560 14.839  1.00 17.62  ? 155 ALA B O    1 
ATOM   6741  C  CB   . ALA B 1 137 ? 17.992  -38.225 13.422  1.00 15.53  ? 155 ALA B CB   1 
ATOM   6742  H  H    . ALA B 1 137 ? 17.129  -40.251 12.070  1.00 19.03  ? 155 ALA B H    1 
ATOM   6743  H  HA   . ALA B 1 137 ? 19.428  -39.715 13.403  1.00 18.36  ? 155 ALA B HA   1 
ATOM   6744  H  HB1  . ALA B 1 137 ? 18.342  -37.770 12.640  1.00 18.64  ? 155 ALA B HB1  1 
ATOM   6745  H  HB2  . ALA B 1 137 ? 17.022  -38.203 13.411  1.00 18.64  ? 155 ALA B HB2  1 
ATOM   6746  H  HB3  . ALA B 1 137 ? 18.324  -37.799 14.228  1.00 18.64  ? 155 ALA B HB3  1 
ATOM   6747  N  N    . PHE B 1 138 ? 18.891  -40.776 15.526  1.00 16.45  ? 156 PHE B N    1 
ATOM   6748  C  CA   . PHE B 1 138 ? 18.559  -41.407 16.798  1.00 16.16  ? 156 PHE B CA   1 
ATOM   6749  C  C    . PHE B 1 138 ? 18.700  -40.366 17.903  1.00 16.64  ? 156 PHE B C    1 
ATOM   6750  O  O    . PHE B 1 138 ? 19.758  -39.747 18.048  1.00 17.43  ? 156 PHE B O    1 
ATOM   6751  C  CB   . PHE B 1 138 ? 19.454  -42.620 17.061  1.00 17.43  ? 156 PHE B CB   1 
ATOM   6752  C  CG   . PHE B 1 138 ? 19.263  -43.731 16.070  1.00 18.46  ? 156 PHE B CG   1 
ATOM   6753  C  CD1  . PHE B 1 138 ? 18.233  -44.642 16.223  1.00 19.44  ? 156 PHE B CD1  1 
ATOM   6754  C  CD2  . PHE B 1 138 ? 20.109  -43.861 14.980  1.00 18.50  ? 156 PHE B CD2  1 
ATOM   6755  C  CE1  . PHE B 1 138 ? 18.046  -45.661 15.310  1.00 19.33  ? 156 PHE B CE1  1 
ATOM   6756  C  CE2  . PHE B 1 138 ? 19.928  -44.888 14.063  1.00 18.70  ? 156 PHE B CE2  1 
ATOM   6757  C  CZ   . PHE B 1 138 ? 18.895  -45.783 14.228  1.00 18.22  ? 156 PHE B CZ   1 
ATOM   6758  H  H    . PHE B 1 138 ? 19.736  -40.676 15.400  1.00 19.74  ? 156 PHE B H    1 
ATOM   6759  H  HA   . PHE B 1 138 ? 17.641  -41.720 16.783  1.00 19.39  ? 156 PHE B HA   1 
ATOM   6760  H  HB2  . PHE B 1 138 ? 20.381  -42.340 17.019  1.00 20.92  ? 156 PHE B HB2  1 
ATOM   6761  H  HB3  . PHE B 1 138 ? 19.253  -42.972 17.943  1.00 20.92  ? 156 PHE B HB3  1 
ATOM   6762  H  HD1  . PHE B 1 138 ? 17.659  -44.567 16.951  1.00 23.33  ? 156 PHE B HD1  1 
ATOM   6763  H  HD2  . PHE B 1 138 ? 20.805  -43.255 14.862  1.00 22.21  ? 156 PHE B HD2  1 
ATOM   6764  H  HE1  . PHE B 1 138 ? 17.348  -46.265 15.424  1.00 23.19  ? 156 PHE B HE1  1 
ATOM   6765  H  HE2  . PHE B 1 138 ? 20.504  -44.971 13.337  1.00 22.44  ? 156 PHE B HE2  1 
ATOM   6766  H  HZ   . PHE B 1 138 ? 18.770  -46.469 13.613  1.00 21.87  ? 156 PHE B HZ   1 
ATOM   6767  N  N    . ALA B 1 139 ? 17.620  -40.148 18.648  1.00 17.31  ? 157 ALA B N    1 
ATOM   6768  C  CA   . ALA B 1 139 ? 17.574  -39.182 19.738  1.00 15.97  ? 157 ALA B CA   1 
ATOM   6769  C  C    . ALA B 1 139 ? 18.042  -37.773 19.344  1.00 15.53  ? 157 ALA B C    1 
ATOM   6770  O  O    . ALA B 1 139 ? 18.795  -37.139 20.082  1.00 17.38  ? 157 ALA B O    1 
ATOM   6771  C  CB   . ALA B 1 139 ? 18.358  -39.680 20.944  1.00 16.68  ? 157 ALA B CB   1 
ATOM   6772  H  H    . ALA B 1 139 ? 16.876  -40.564 18.536  1.00 20.77  ? 157 ALA B H    1 
ATOM   6773  H  HA   . ALA B 1 139 ? 16.643  -39.090 19.995  1.00 19.16  ? 157 ALA B HA   1 
ATOM   6774  H  HB1  . ALA B 1 139 ? 17.971  -40.515 21.250  1.00 20.02  ? 157 ALA B HB1  1 
ATOM   6775  H  HB2  . ALA B 1 139 ? 19.282  -39.819 20.685  1.00 20.02  ? 157 ALA B HB2  1 
ATOM   6776  H  HB3  . ALA B 1 139 ? 18.309  -39.015 21.649  1.00 20.02  ? 157 ALA B HB3  1 
ATOM   6777  N  N    . PRO B 1 140 ? 17.582  -37.246 18.210  1.00 15.39  ? 158 PRO B N    1 
ATOM   6778  C  CA   . PRO B 1 140 ? 18.011  -35.892 17.832  1.00 15.23  ? 158 PRO B CA   1 
ATOM   6779  C  C    . PRO B 1 140 ? 17.344  -34.850 18.712  1.00 15.07  ? 158 PRO B C    1 
ATOM   6780  O  O    . PRO B 1 140 ? 16.195  -35.009 19.129  1.00 16.83  ? 158 PRO B O    1 
ATOM   6781  C  CB   . PRO B 1 140 ? 17.533  -35.762 16.381  1.00 15.84  ? 158 PRO B CB   1 
ATOM   6782  C  CG   . PRO B 1 140 ? 16.293  -36.608 16.341  1.00 16.65  ? 158 PRO B CG   1 
ATOM   6783  C  CD   . PRO B 1 140 ? 16.627  -37.807 17.231  1.00 16.21  ? 158 PRO B CD   1 
ATOM   6784  H  HA   . PRO B 1 140 ? 18.976  -35.804 17.872  1.00 18.27  ? 158 PRO B HA   1 
ATOM   6785  H  HB2  . PRO B 1 140 ? 17.335  -34.835 16.175  1.00 19.01  ? 158 PRO B HB2  1 
ATOM   6786  H  HB3  . PRO B 1 140 ? 18.210  -36.099 15.774  1.00 19.01  ? 158 PRO B HB3  1 
ATOM   6787  H  HG2  . PRO B 1 140 ? 15.539  -36.111 16.693  1.00 19.98  ? 158 PRO B HG2  1 
ATOM   6788  H  HG3  . PRO B 1 140 ? 16.110  -36.888 15.431  1.00 19.98  ? 158 PRO B HG3  1 
ATOM   6789  H  HD2  . PRO B 1 140 ? 15.832  -38.139 17.676  1.00 19.45  ? 158 PRO B HD2  1 
ATOM   6790  H  HD3  . PRO B 1 140 ? 17.039  -38.517 16.714  1.00 19.45  ? 158 PRO B HD3  1 
ATOM   6791  N  N    . ASP B 1 141 ? 18.064  -33.761 18.978  1.00 14.93  ? 159 ASP B N    1 
ATOM   6792  C  CA   . ASP B 1 141 ? 17.541  -32.692 19.831  1.00 13.92  ? 159 ASP B CA   1 
ATOM   6793  C  C    . ASP B 1 141 ? 17.358  -31.403 19.035  1.00 14.68  ? 159 ASP B C    1 
ATOM   6794  O  O    . ASP B 1 141 ? 18.009  -30.389 19.292  1.00 14.74  ? 159 ASP B O    1 
ATOM   6795  C  CB   . ASP B 1 141 ? 18.425  -32.464 21.090  1.00 14.48  ? 159 ASP B CB   1 
ATOM   6796  C  CG   . ASP B 1 141 ? 19.905  -32.219 20.773  1.00 15.23  ? 159 ASP B CG   1 
ATOM   6797  O  OD1  . ASP B 1 141 ? 20.385  -32.567 19.680  1.00 16.05  ? 159 ASP B OD1  1 
ATOM   6798  O  OD2  . ASP B 1 141 ? 20.614  -31.693 21.664  1.00 16.79  ? 159 ASP B OD2  1 
ATOM   6799  H  H    . ASP B 1 141 ? 18.857  -33.619 18.677  1.00 17.92  ? 159 ASP B H    1 
ATOM   6800  H  HA   . ASP B 1 141 ? 16.667  -32.983 20.133  1.00 16.71  ? 159 ASP B HA   1 
ATOM   6801  H  HB2  . ASP B 1 141 ? 18.092  -31.688 21.568  1.00 17.38  ? 159 ASP B HB2  1 
ATOM   6802  H  HB3  . ASP B 1 141 ? 18.370  -33.251 21.655  1.00 17.38  ? 159 ASP B HB3  1 
ATOM   6803  N  N    . TYR B 1 142 ? 16.411  -31.434 18.094  1.00 14.64  ? 160 TYR B N    1 
ATOM   6804  C  CA   . TYR B 1 142 ? 16.185  -30.273 17.237  1.00 15.71  ? 160 TYR B CA   1 
ATOM   6805  C  C    . TYR B 1 142 ? 15.685  -29.072 18.030  1.00 15.38  ? 160 TYR B C    1 
ATOM   6806  O  O    . TYR B 1 142 ? 15.914  -27.928 17.621  1.00 16.21  ? 160 TYR B O    1 
ATOM   6807  C  CB   . TYR B 1 142 ? 15.189  -30.601 16.124  1.00 15.36  ? 160 TYR B CB   1 
ATOM   6808  C  CG   . TYR B 1 142 ? 15.521  -31.827 15.298  1.00 15.58  ? 160 TYR B CG   1 
ATOM   6809  C  CD1  . TYR B 1 142 ? 16.678  -31.881 14.533  1.00 16.16  ? 160 TYR B CD1  1 
ATOM   6810  C  CD2  . TYR B 1 142 ? 14.663  -32.921 15.264  1.00 16.08  ? 160 TYR B CD2  1 
ATOM   6811  C  CE1  . TYR B 1 142 ? 16.978  -32.997 13.762  1.00 15.56  ? 160 TYR B CE1  1 
ATOM   6812  C  CE2  . TYR B 1 142 ? 14.958  -34.048 14.495  1.00 15.94  ? 160 TYR B CE2  1 
ATOM   6813  C  CZ   . TYR B 1 142 ? 16.118  -34.075 13.746  1.00 16.27  ? 160 TYR B CZ   1 
ATOM   6814  O  OH   . TYR B 1 142 ? 16.425  -35.172 12.973  1.00 16.61  ? 160 TYR B OH   1 
ATOM   6815  H  H    . TYR B 1 142 ? 15.895  -32.104 17.935  1.00 17.57  ? 160 TYR B H    1 
ATOM   6816  H  HA   . TYR B 1 142 ? 17.032  -30.041 16.824  1.00 18.85  ? 160 TYR B HA   1 
ATOM   6817  H  HB2  . TYR B 1 142 ? 14.319  -30.750 16.527  1.00 18.43  ? 160 TYR B HB2  1 
ATOM   6818  H  HB3  . TYR B 1 142 ? 15.149  -29.845 15.518  1.00 18.43  ? 160 TYR B HB3  1 
ATOM   6819  H  HD1  . TYR B 1 142 ? 17.263  -31.158 14.536  1.00 19.39  ? 160 TYR B HD1  1 
ATOM   6820  H  HD2  . TYR B 1 142 ? 13.878  -32.901 15.762  1.00 19.30  ? 160 TYR B HD2  1 
ATOM   6821  H  HE1  . TYR B 1 142 ? 17.759  -33.018 13.257  1.00 18.68  ? 160 TYR B HE1  1 
ATOM   6822  H  HE2  . TYR B 1 142 ? 14.378  -34.775 14.488  1.00 19.13  ? 160 TYR B HE2  1 
ATOM   6823  H  HH   . TYR B 1 142 ? 15.813  -35.746 13.033  1.00 19.93  ? 160 TYR B HH   1 
ATOM   6824  N  N    . LYS B 1 143 ? 14.997  -29.308 19.153  1.00 15.41  ? 161 LYS B N    1 
ATOM   6825  C  CA   . LYS B 1 143 ? 14.559  -28.247 20.051  1.00 16.44  ? 161 LYS B CA   1 
ATOM   6826  C  C    . LYS B 1 143 ? 15.504  -28.070 21.233  1.00 15.87  ? 161 LYS B C    1 
ATOM   6827  O  O    . LYS B 1 143 ? 15.184  -27.327 22.168  1.00 17.98  ? 161 LYS B O    1 
ATOM   6828  C  CB   . LYS B 1 143 ? 13.149  -28.531 20.576  1.00 17.06  ? 161 LYS B CB   1 
ATOM   6829  C  CG   . LYS B 1 143 ? 12.046  -28.447 19.539  1.00 18.49  ? 161 LYS B CG   1 
ATOM   6830  C  CD   . LYS B 1 143 ? 10.687  -28.715 20.180  1.00 19.83  ? 161 LYS B CD   1 
ATOM   6831  C  CE   . LYS B 1 143 ? 9.541   -28.650 19.187  1.00 21.15  ? 161 LYS B CE   1 
ATOM   6832  N  NZ   . LYS B 1 143 ? 9.481   -29.860 18.314  1.00 20.60  ? 161 LYS B NZ   1 
ATOM   6833  H  H    . LYS B 1 143 ? 14.769  -30.094 19.417  1.00 18.49  ? 161 LYS B H    1 
ATOM   6834  H  HA   . LYS B 1 143 ? 14.529  -27.419 19.547  1.00 19.72  ? 161 LYS B HA   1 
ATOM   6835  H  HB2  . LYS B 1 143 ? 13.134  -29.429 20.943  1.00 20.47  ? 161 LYS B HB2  1 
ATOM   6836  H  HB3  . LYS B 1 143 ? 12.944  -27.885 21.270  1.00 20.47  ? 161 LYS B HB3  1 
ATOM   6837  H  HG2  . LYS B 1 143 ? 12.034  -27.559 19.149  1.00 22.19  ? 161 LYS B HG2  1 
ATOM   6838  H  HG3  . LYS B 1 143 ? 12.198  -29.111 18.849  1.00 22.19  ? 161 LYS B HG3  1 
ATOM   6839  H  HD2  . LYS B 1 143 ? 10.692  -29.602 20.573  1.00 23.80  ? 161 LYS B HD2  1 
ATOM   6840  H  HD3  . LYS B 1 143 ? 10.525  -28.049 20.867  1.00 23.80  ? 161 LYS B HD3  1 
ATOM   6841  H  HE2  . LYS B 1 143 ? 8.703   -28.584 19.671  1.00 25.38  ? 161 LYS B HE2  1 
ATOM   6842  H  HE3  . LYS B 1 143 ? 9.657   -27.873 18.618  1.00 25.38  ? 161 LYS B HE3  1 
ATOM   6843  H  HZ1  . LYS B 1 143 ? 8.774   -29.812 17.776  1.00 24.72  ? 161 LYS B HZ1  1 
ATOM   6844  H  HZ2  . LYS B 1 143 ? 10.218  -29.915 17.818  1.00 24.72  ? 161 LYS B HZ2  1 
ATOM   6845  H  HZ3  . LYS B 1 143 ? 9.414   -30.593 18.814  1.00 24.72  ? 161 LYS B HZ3  1 
ATOM   6846  N  N    . GLY B 1 144 ? 16.651  -28.748 21.216  1.00 15.45  ? 162 GLY B N    1 
ATOM   6847  C  CA   . GLY B 1 144 ? 17.512  -28.790 22.374  1.00 15.74  ? 162 GLY B CA   1 
ATOM   6848  C  C    . GLY B 1 144 ? 16.894  -29.635 23.476  1.00 15.56  ? 162 GLY B C    1 
ATOM   6849  O  O    . GLY B 1 144 ? 16.050  -30.509 23.250  1.00 16.87  ? 162 GLY B O    1 
ATOM   6850  H  H    . GLY B 1 144 ? 16.947  -29.190 20.541  1.00 18.55  ? 162 GLY B H    1 
ATOM   6851  H  HA2  . GLY B 1 144 ? 18.369  -29.174 22.130  1.00 18.89  ? 162 GLY B HA2  1 
ATOM   6852  H  HA3  . GLY B 1 144 ? 17.653  -27.892 22.710  1.00 18.89  ? 162 GLY B HA3  1 
ATOM   6853  N  N    . THR B 1 145 ? 17.326  -29.350 24.698  1.00 14.85  ? 163 THR B N    1 
ATOM   6854  C  CA   . THR B 1 145 ? 16.794  -30.038 25.859  1.00 15.35  ? 163 THR B CA   1 
ATOM   6855  C  C    . THR B 1 145 ? 16.502  -29.047 26.970  1.00 17.12  ? 163 THR B C    1 
ATOM   6856  O  O    . THR B 1 145 ? 17.278  -28.115 27.208  1.00 16.57  ? 163 THR B O    1 
ATOM   6857  C  CB   . THR B 1 145 ? 17.749  -31.121 26.375  1.00 16.44  ? 163 THR B CB   1 
ATOM   6858  O  OG1  . THR B 1 145 ? 17.125  -31.784 27.477  1.00 15.68  ? 163 THR B OG1  1 
ATOM   6859  C  CG2  . THR B 1 145 ? 19.092  -30.538 26.833  1.00 17.78  ? 163 THR B CG2  1 
ATOM   6860  H  H    . THR B 1 145 ? 17.926  -28.761 24.877  1.00 17.83  ? 163 THR B H    1 
ATOM   6861  H  HA   . THR B 1 145 ? 15.959  -30.462 25.607  1.00 18.42  ? 163 THR B HA   1 
ATOM   6862  H  HB   . THR B 1 145 ? 17.941  -31.744 25.657  1.00 19.72  ? 163 THR B HB   1 
ATOM   6863  H  HG1  . THR B 1 145 ? 17.644  -32.364 27.794  1.00 18.81  ? 163 THR B HG1  1 
ATOM   6864  H  HG21 . THR B 1 145 ? 18.969  -30.019 27.644  1.00 21.34  ? 163 THR B HG21 1 
ATOM   6865  H  HG22 . THR B 1 145 ? 19.722  -31.254 27.011  1.00 21.34  ? 163 THR B HG22 1 
ATOM   6866  H  HG23 . THR B 1 145 ? 19.457  -29.962 26.143  1.00 21.34  ? 163 THR B HG23 1 
ATOM   6867  N  N    . VAL B 1 146 ? 15.376  -29.268 27.657  1.00 18.58  ? 164 VAL B N    1 
ATOM   6868  C  CA   . VAL B 1 146 ? 15.041  -28.458 28.825  1.00 19.89  ? 164 VAL B CA   1 
ATOM   6869  C  C    . VAL B 1 146 ? 15.725  -28.952 30.090  1.00 20.64  ? 164 VAL B C    1 
ATOM   6870  O  O    . VAL B 1 146 ? 15.695  -28.251 31.111  1.00 20.57  ? 164 VAL B O    1 
ATOM   6871  C  CB   . VAL B 1 146 ? 13.521  -28.411 29.076  1.00 21.28  ? 164 VAL B CB   1 
ATOM   6872  C  CG1  . VAL B 1 146 ? 12.799  -27.731 27.915  1.00 21.13  ? 164 VAL B CG1  1 
ATOM   6873  C  CG2  . VAL B 1 146 ? 12.968  -29.813 29.309  1.00 22.21  ? 164 VAL B CG2  1 
ATOM   6874  H  H    . VAL B 1 146 ? 14.798  -29.875 27.467  1.00 22.30  ? 164 VAL B H    1 
ATOM   6875  H  HA   . VAL B 1 146 ? 15.342  -27.554 28.640  1.00 23.87  ? 164 VAL B HA   1 
ATOM   6876  H  HB   . VAL B 1 146 ? 13.358  -27.888 29.877  1.00 25.53  ? 164 VAL B HB   1 
ATOM   6877  H  HG11 . VAL B 1 146 ? 11.886  -27.539 28.180  1.00 25.36  ? 164 VAL B HG11 1 
ATOM   6878  H  HG12 . VAL B 1 146 ? 13.261  -26.907 27.696  1.00 25.36  ? 164 VAL B HG12 1 
ATOM   6879  H  HG13 . VAL B 1 146 ? 12.803  -28.327 27.149  1.00 25.36  ? 164 VAL B HG13 1 
ATOM   6880  H  HG21 . VAL B 1 146 ? 13.662  -30.463 29.116  1.00 26.65  ? 164 VAL B HG21 1 
ATOM   6881  H  HG22 . VAL B 1 146 ? 12.688  -29.893 30.235  1.00 26.65  ? 164 VAL B HG22 1 
ATOM   6882  H  HG23 . VAL B 1 146 ? 12.209  -29.955 28.721  1.00 26.65  ? 164 VAL B HG23 1 
ATOM   6883  N  N    . LEU B 1 147 ? 16.349  -30.135 30.050  1.00 21.22  ? 165 LEU B N    1 
ATOM   6884  C  CA   . LEU B 1 147 ? 17.011  -30.683 31.229  1.00 21.39  ? 165 LEU B CA   1 
ATOM   6885  C  C    . LEU B 1 147 ? 18.300  -29.952 31.560  1.00 24.18  ? 165 LEU B C    1 
ATOM   6886  O  O    . LEU B 1 147 ? 18.850  -30.167 32.643  1.00 26.29  ? 165 LEU B O    1 
ATOM   6887  C  CB   . LEU B 1 147 ? 17.331  -32.165 31.044  1.00 21.70  ? 165 LEU B CB   1 
ATOM   6888  C  CG   . LEU B 1 147 ? 16.127  -33.075 30.817  1.00 21.57  ? 165 LEU B CG   1 
ATOM   6889  C  CD1  . LEU B 1 147 ? 16.553  -34.535 30.855  1.00 23.18  ? 165 LEU B CD1  1 
ATOM   6890  C  CD2  . LEU B 1 147 ? 15.047  -32.813 31.849  1.00 24.18  ? 165 LEU B CD2  1 
ATOM   6891  H  H    . LEU B 1 147 ? 16.400  -30.636 29.353  1.00 25.47  ? 165 LEU B H    1 
ATOM   6892  H  HA   . LEU B 1 147 ? 16.395  -30.603 31.975  1.00 25.67  ? 165 LEU B HA   1 
ATOM   6893  H  HB2  . LEU B 1 147 ? 17.912  -32.256 30.272  1.00 26.04  ? 165 LEU B HB2  1 
ATOM   6894  H  HB3  . LEU B 1 147 ? 17.786  -32.480 31.841  1.00 26.04  ? 165 LEU B HB3  1 
ATOM   6895  H  HG   . LEU B 1 147 ? 15.754  -32.885 29.942  1.00 25.88  ? 165 LEU B HG   1 
ATOM   6896  H  HD11 . LEU B 1 147 ? 16.938  -34.730 31.723  1.00 27.82  ? 165 LEU B HD11 1 
ATOM   6897  H  HD12 . LEU B 1 147 ? 15.775  -35.095 30.705  1.00 27.82  ? 165 LEU B HD12 1 
ATOM   6898  H  HD13 . LEU B 1 147 ? 17.211  -34.690 30.159  1.00 27.82  ? 165 LEU B HD13 1 
ATOM   6899  H  HD21 . LEU B 1 147 ? 15.443  -32.840 32.734  1.00 29.01  ? 165 LEU B HD21 1 
ATOM   6900  H  HD22 . LEU B 1 147 ? 14.660  -31.938 31.687  1.00 29.01  ? 165 LEU B HD22 1 
ATOM   6901  H  HD23 . LEU B 1 147 ? 14.364  -33.497 31.771  1.00 29.01  ? 165 LEU B HD23 1 
ATOM   6902  N  N    . ALA B 1 148 ? 18.808  -29.132 30.639  1.00 25.76  ? 166 ALA B N    1 
ATOM   6903  C  CA   . ALA B 1 148 ? 19.908  -28.234 30.945  1.00 27.76  ? 166 ALA B CA   1 
ATOM   6904  C  C    . ALA B 1 148 ? 19.490  -27.121 31.894  1.00 29.14  ? 166 ALA B C    1 
ATOM   6905  O  O    . ALA B 1 148 ? 20.362  -26.461 32.467  1.00 30.27  ? 166 ALA B O    1 
ATOM   6906  C  CB   . ALA B 1 148 ? 20.441  -27.617 29.647  1.00 28.75  ? 166 ALA B CB   1 
ATOM   6907  H  H    . ALA B 1 148 ? 18.529  -29.081 29.827  1.00 30.91  ? 166 ALA B H    1 
ATOM   6908  H  HA   . ALA B 1 148 ? 20.625  -28.738 31.361  1.00 33.32  ? 166 ALA B HA   1 
ATOM   6909  H  HB1  . ALA B 1 148 ? 20.750  -28.327 29.063  1.00 34.50  ? 166 ALA B HB1  1 
ATOM   6910  H  HB2  . ALA B 1 148 ? 19.726  -27.122 29.217  1.00 34.50  ? 166 ALA B HB2  1 
ATOM   6911  H  HB3  . ALA B 1 148 ? 21.175  -27.020 29.860  1.00 34.50  ? 166 ALA B HB3  1 
ATOM   6912  N  N    . GLY B 1 149 ? 18.184  -26.910 32.078  1.00 28.40  ? 167 GLY B N    1 
ATOM   6913  C  CA   . GLY B 1 149 ? 17.681  -25.784 32.822  1.00 27.03  ? 167 GLY B CA   1 
ATOM   6914  C  C    . GLY B 1 149 ? 17.583  -24.555 31.937  1.00 25.90  ? 167 GLY B C    1 
ATOM   6915  O  O    . GLY B 1 149 ? 17.931  -24.587 30.754  1.00 23.44  ? 167 GLY B O    1 
ATOM   6916  H  H    . GLY B 1 149 ? 17.566  -27.423 31.770  1.00 34.09  ? 167 GLY B H    1 
ATOM   6917  H  HA2  . GLY B 1 149 ? 16.799  -25.989 33.171  1.00 32.44  ? 167 GLY B HA2  1 
ATOM   6918  H  HA3  . GLY B 1 149 ? 18.276  -25.588 33.563  1.00 32.44  ? 167 GLY B HA3  1 
ATOM   6919  N  N    . PRO B 1 150 ? 17.116  -23.444 32.493  1.00 27.85  ? 168 PRO B N    1 
ATOM   6920  C  CA   . PRO B 1 150 ? 17.033  -22.209 31.703  1.00 27.68  ? 168 PRO B CA   1 
ATOM   6921  C  C    . PRO B 1 150 ? 18.413  -21.669 31.357  1.00 26.13  ? 168 PRO B C    1 
ATOM   6922  O  O    . PRO B 1 150 ? 19.381  -21.836 32.103  1.00 25.84  ? 168 PRO B O    1 
ATOM   6923  C  CB   . PRO B 1 150 ? 16.285  -21.240 32.629  1.00 28.93  ? 168 PRO B CB   1 
ATOM   6924  C  CG   . PRO B 1 150 ? 15.681  -22.101 33.708  1.00 29.81  ? 168 PRO B CG   1 
ATOM   6925  C  CD   . PRO B 1 150 ? 16.594  -23.273 33.859  1.00 29.12  ? 168 PRO B CD   1 
ATOM   6926  H  HA   . PRO B 1 150 ? 16.522  -22.357 30.892  1.00 33.21  ? 168 PRO B HA   1 
ATOM   6927  H  HB2  . PRO B 1 150 ? 16.908  -20.599 33.006  1.00 34.72  ? 168 PRO B HB2  1 
ATOM   6928  H  HB3  . PRO B 1 150 ? 15.595  -20.777 32.130  1.00 34.72  ? 168 PRO B HB3  1 
ATOM   6929  H  HG2  . PRO B 1 150 ? 15.629  -21.598 34.536  1.00 35.78  ? 168 PRO B HG2  1 
ATOM   6930  H  HG3  . PRO B 1 150 ? 14.795  -22.389 33.439  1.00 35.78  ? 168 PRO B HG3  1 
ATOM   6931  H  HD2  . PRO B 1 150 ? 17.310  -23.079 34.484  1.00 34.94  ? 168 PRO B HD2  1 
ATOM   6932  H  HD3  . PRO B 1 150 ? 16.107  -24.060 34.147  1.00 34.94  ? 168 PRO B HD3  1 
ATOM   6933  N  N    . LEU B 1 151 ? 18.492  -21.007 30.200  1.00 26.20  ? 169 LEU B N    1 
ATOM   6934  C  CA   . LEU B 1 151 ? 19.757  -20.416 29.774  1.00 27.16  ? 169 LEU B CA   1 
ATOM   6935  C  C    . LEU B 1 151 ? 20.321  -19.482 30.837  1.00 27.66  ? 169 LEU B C    1 
ATOM   6936  O  O    . LEU B 1 151 ? 21.541  -19.414 31.031  1.00 26.73  ? 169 LEU B O    1 
ATOM   6937  C  CB   . LEU B 1 151 ? 19.557  -19.638 28.476  1.00 28.79  ? 169 LEU B CB   1 
ATOM   6938  C  CG   . LEU B 1 151 ? 19.467  -20.443 27.186  1.00 29.26  ? 169 LEU B CG   1 
ATOM   6939  C  CD1  . LEU B 1 151 ? 18.640  -19.672 26.164  1.00 30.70  ? 169 LEU B CD1  1 
ATOM   6940  C  CD2  . LEU B 1 151 ? 20.838  -20.732 26.632  1.00 29.30  ? 169 LEU B CD2  1 
ATOM   6941  H  H    . LEU B 1 151 ? 17.839  -20.888 29.654  1.00 31.44  ? 169 LEU B H    1 
ATOM   6942  H  HA   . LEU B 1 151 ? 20.393  -21.132 29.620  1.00 32.59  ? 169 LEU B HA   1 
ATOM   6943  H  HB2  . LEU B 1 151 ? 18.729  -19.138 28.554  1.00 34.55  ? 169 LEU B HB2  1 
ATOM   6944  H  HB3  . LEU B 1 151 ? 20.305  -19.028 28.377  1.00 34.55  ? 169 LEU B HB3  1 
ATOM   6945  H  HG   . LEU B 1 151 ? 19.039  -21.294 27.369  1.00 35.11  ? 169 LEU B HG   1 
ATOM   6946  H  HD11 . LEU B 1 151 ? 18.859  -18.729 26.227  1.00 36.84  ? 169 LEU B HD11 1 
ATOM   6947  H  HD12 . LEU B 1 151 ? 18.847  -20.001 25.276  1.00 36.84  ? 169 LEU B HD12 1 
ATOM   6948  H  HD13 . LEU B 1 151 ? 17.698  -19.805 26.355  1.00 36.84  ? 169 LEU B HD13 1 
ATOM   6949  H  HD21 . LEU B 1 151 ? 20.745  -21.222 25.800  1.00 35.16  ? 169 LEU B HD21 1 
ATOM   6950  H  HD22 . LEU B 1 151 ? 21.298  -19.893 26.474  1.00 35.16  ? 169 LEU B HD22 1 
ATOM   6951  H  HD23 . LEU B 1 151 ? 21.332  -21.264 27.276  1.00 35.16  ? 169 LEU B HD23 1 
ATOM   6952  N  N    . ASP B 1 152 ? 19.444  -18.751 31.535  1.00 30.74  ? 170 ASP B N    1 
ATOM   6953  C  CA   . ASP B 1 152 ? 19.883  -17.739 32.491  1.00 34.23  ? 170 ASP B CA   1 
ATOM   6954  C  C    . ASP B 1 152 ? 20.557  -18.336 33.719  1.00 33.78  ? 170 ASP B C    1 
ATOM   6955  O  O    . ASP B 1 152 ? 21.227  -17.608 34.461  1.00 34.26  ? 170 ASP B O    1 
ATOM   6956  C  CB   . ASP B 1 152 ? 18.685  -16.897 32.945  1.00 38.39  ? 170 ASP B CB   1 
ATOM   6957  C  CG   . ASP B 1 152 ? 17.638  -17.721 33.683  1.00 43.19  ? 170 ASP B CG   1 
ATOM   6958  O  OD1  . ASP B 1 152 ? 16.470  -17.743 33.235  1.00 45.47  ? 170 ASP B OD1  1 
ATOM   6959  O  OD2  . ASP B 1 152 ? 17.980  -18.349 34.710  1.00 45.00  ? 170 ASP B OD2  1 
ATOM   6960  H  H    . ASP B 1 152 ? 18.590  -18.825 31.472  1.00 36.89  ? 170 ASP B H    1 
ATOM   6961  H  HA   . ASP B 1 152 ? 20.525  -17.164 32.045  1.00 41.08  ? 170 ASP B HA   1 
ATOM   6962  H  HB2  . ASP B 1 152 ? 18.996  -16.200 33.543  1.00 46.07  ? 170 ASP B HB2  1 
ATOM   6963  H  HB3  . ASP B 1 152 ? 18.263  -16.501 32.166  1.00 46.07  ? 170 ASP B HB3  1 
ATOM   6964  N  N    . ALA B 1 153 ? 20.376  -19.627 33.966  1.00 33.06  ? 171 ALA B N    1 
ATOM   6965  C  CA   . ALA B 1 153 ? 20.942  -20.276 35.137  1.00 32.81  ? 171 ALA B CA   1 
ATOM   6966  C  C    . ALA B 1 153 ? 22.027  -21.276 34.782  1.00 32.07  ? 171 ALA B C    1 
ATOM   6967  O  O    . ALA B 1 153 ? 22.602  -21.892 35.686  1.00 32.86  ? 171 ALA B O    1 
ATOM   6968  C  CB   . ALA B 1 153 ? 19.836  -20.980 35.931  1.00 33.17  ? 171 ALA B CB   1 
ATOM   6969  H  H    . ALA B 1 153 ? 19.923  -20.156 33.461  1.00 39.68  ? 171 ALA B H    1 
ATOM   6970  H  HA   . ALA B 1 153 ? 21.334  -19.599 35.710  1.00 39.38  ? 171 ALA B HA   1 
ATOM   6971  H  HB1  . ALA B 1 153 ? 20.225  -21.394 36.717  1.00 39.80  ? 171 ALA B HB1  1 
ATOM   6972  H  HB2  . ALA B 1 153 ? 19.171  -20.325 36.197  1.00 39.80  ? 171 ALA B HB2  1 
ATOM   6973  H  HB3  . ALA B 1 153 ? 19.426  -21.657 35.370  1.00 39.80  ? 171 ALA B HB3  1 
ATOM   6974  N  N    . LEU B 1 154 ? 22.329  -21.444 33.496  1.00 30.94  ? 172 LEU B N    1 
ATOM   6975  C  CA   . LEU B 1 154 ? 23.246  -22.490 33.074  1.00 29.66  ? 172 LEU B CA   1 
ATOM   6976  C  C    . LEU B 1 154 ? 24.636  -22.237 33.640  1.00 28.70  ? 172 LEU B C    1 
ATOM   6977  O  O    . LEU B 1 154 ? 25.166  -21.124 33.555  1.00 29.26  ? 172 LEU B O    1 
ATOM   6978  C  CB   . LEU B 1 154 ? 23.297  -22.542 31.546  1.00 29.82  ? 172 LEU B CB   1 
ATOM   6979  C  CG   . LEU B 1 154 ? 23.798  -23.842 30.917  1.00 29.90  ? 172 LEU B CG   1 
ATOM   6980  C  CD1  . LEU B 1 154 ? 22.827  -24.988 31.171  1.00 31.09  ? 172 LEU B CD1  1 
ATOM   6981  C  CD2  . LEU B 1 154 ? 24.023  -23.659 29.421  1.00 29.35  ? 172 LEU B CD2  1 
ATOM   6982  H  H    . LEU B 1 154 ? 22.016  -20.965 32.854  1.00 37.13  ? 172 LEU B H    1 
ATOM   6983  H  HA   . LEU B 1 154 ? 22.937  -23.348 33.403  1.00 35.60  ? 172 LEU B HA   1 
ATOM   6984  H  HB2  . LEU B 1 154 ? 22.399  -22.392 31.212  1.00 35.78  ? 172 LEU B HB2  1 
ATOM   6985  H  HB3  . LEU B 1 154 ? 23.887  -21.834 31.242  1.00 35.78  ? 172 LEU B HB3  1 
ATOM   6986  H  HG   . LEU B 1 154 ? 24.644  -24.076 31.328  1.00 35.88  ? 172 LEU B HG   1 
ATOM   6987  H  HD11 . LEU B 1 154 ? 21.934  -24.708 30.914  1.00 37.31  ? 172 LEU B HD11 1 
ATOM   6988  H  HD12 . LEU B 1 154 ? 23.098  -25.755 30.643  1.00 37.31  ? 172 LEU B HD12 1 
ATOM   6989  H  HD13 . LEU B 1 154 ? 22.844  -25.213 32.114  1.00 37.31  ? 172 LEU B HD13 1 
ATOM   6990  H  HD21 . LEU B 1 154 ? 24.372  -24.485 29.051  1.00 35.22  ? 172 LEU B HD21 1 
ATOM   6991  H  HD22 . LEU B 1 154 ? 23.178  -23.439 28.999  1.00 35.22  ? 172 LEU B HD22 1 
ATOM   6992  H  HD23 . LEU B 1 154 ? 24.659  -22.940 29.283  1.00 35.22  ? 172 LEU B HD23 1 
ATOM   6993  N  N    . ALA B 1 155 ? 25.215  -23.275 34.236  1.00 27.22  ? 173 ALA B N    1 
ATOM   6994  C  CA   . ALA B 1 155 ? 26.607  -23.216 34.646  1.00 27.88  ? 173 ALA B CA   1 
ATOM   6995  C  C    . ALA B 1 155 ? 27.490  -23.096 33.410  1.00 24.56  ? 173 ALA B C    1 
ATOM   6996  O  O    . ALA B 1 155 ? 27.045  -23.314 32.275  1.00 25.14  ? 173 ALA B O    1 
ATOM   6997  C  CB   . ALA B 1 155 ? 26.980  -24.465 35.444  1.00 29.94  ? 173 ALA B CB   1 
ATOM   6998  H  H    . ALA B 1 155 ? 24.823  -24.020 34.412  1.00 32.66  ? 173 ALA B H    1 
ATOM   6999  H  HA   . ALA B 1 155 ? 26.758  -22.447 35.217  1.00 33.46  ? 173 ALA B HA   1 
ATOM   7000  H  HB1  . ALA B 1 155 ? 26.407  -24.525 36.224  1.00 35.93  ? 173 ALA B HB1  1 
ATOM   7001  H  HB2  . ALA B 1 155 ? 26.858  -25.247 34.883  1.00 35.93  ? 173 ALA B HB2  1 
ATOM   7002  H  HB3  . ALA B 1 155 ? 27.908  -24.398 35.720  1.00 35.93  ? 173 ALA B HB3  1 
ATOM   7003  N  N    . VAL B 1 156 ? 28.754  -22.719 33.632  1.00 22.46  ? 174 VAL B N    1 
ATOM   7004  C  CA   . VAL B 1 156 ? 29.686  -22.660 32.514  1.00 20.55  ? 174 VAL B CA   1 
ATOM   7005  C  C    . VAL B 1 156 ? 29.684  -24.006 31.820  1.00 19.02  ? 174 VAL B C    1 
ATOM   7006  O  O    . VAL B 1 156 ? 29.811  -25.062 32.457  1.00 20.73  ? 174 VAL B O    1 
ATOM   7007  C  CB   . VAL B 1 156 ? 31.096  -22.244 32.965  1.00 21.12  ? 174 VAL B CB   1 
ATOM   7008  C  CG1  . VAL B 1 156 ? 31.103  -20.791 33.409  1.00 21.83  ? 174 VAL B CG1  1 
ATOM   7009  C  CG2  . VAL B 1 156 ? 31.612  -23.174 34.052  1.00 22.24  ? 174 VAL B CG2  1 
ATOM   7010  H  H    . VAL B 1 156 ? 29.081  -22.501 34.397  1.00 26.96  ? 174 VAL B H    1 
ATOM   7011  H  HA   . VAL B 1 156 ? 29.385  -21.979 31.892  1.00 24.66  ? 174 VAL B HA   1 
ATOM   7012  H  HB   . VAL B 1 156 ? 31.707  -22.320 32.216  1.00 25.35  ? 174 VAL B HB   1 
ATOM   7013  H  HG11 . VAL B 1 156 ? 30.236  -20.399 33.221  1.00 26.20  ? 174 VAL B HG11 1 
ATOM   7014  H  HG12 . VAL B 1 156 ? 31.284  -20.753 34.362  1.00 26.20  ? 174 VAL B HG12 1 
ATOM   7015  H  HG13 . VAL B 1 156 ? 31.793  -20.315 32.922  1.00 26.20  ? 174 VAL B HG13 1 
ATOM   7016  H  HG21 . VAL B 1 156 ? 32.512  -22.906 34.296  1.00 26.69  ? 174 VAL B HG21 1 
ATOM   7017  H  HG22 . VAL B 1 156 ? 31.028  -23.112 34.824  1.00 26.69  ? 174 VAL B HG22 1 
ATOM   7018  H  HG23 . VAL B 1 156 ? 31.617  -24.083 33.713  1.00 26.69  ? 174 VAL B HG23 1 
ATOM   7019  N  N    . SER B 1 157 ? 29.534  -23.961 30.502  1.00 18.09  ? 175 SER B N    1 
ATOM   7020  C  CA   . SER B 1 157 ? 29.286  -25.140 29.700  1.00 16.88  ? 175 SER B CA   1 
ATOM   7021  C  C    . SER B 1 157 ? 29.941  -24.970 28.340  1.00 14.96  ? 175 SER B C    1 
ATOM   7022  O  O    . SER B 1 157 ? 30.244  -23.853 27.900  1.00 15.21  ? 175 SER B O    1 
ATOM   7023  C  CB   . SER B 1 157 ? 27.783  -25.360 29.501  1.00 20.46  ? 175 SER B CB   1 
ATOM   7024  O  OG   . SER B 1 157 ? 27.105  -25.408 30.739  1.00 23.00  ? 175 SER B OG   1 
ATOM   7025  H  H    . SER B 1 157 ? 29.574  -23.237 30.039  1.00 21.71  ? 175 SER B H    1 
ATOM   7026  H  HA   . SER B 1 157 ? 29.675  -25.910 30.143  1.00 20.26  ? 175 SER B HA   1 
ATOM   7027  H  HB2  . SER B 1 157 ? 27.426  -24.627 28.976  1.00 24.55  ? 175 SER B HB2  1 
ATOM   7028  H  HB3  . SER B 1 157 ? 27.648  -26.200 29.036  1.00 24.55  ? 175 SER B HB3  1 
ATOM   7029  H  HG   . SER B 1 157 ? 26.276  -25.456 30.610  1.00 27.60  ? 175 SER B HG   1 
ATOM   7030  N  N    . ALA B 1 158 ? 30.129  -26.107 27.675  1.00 15.31  ? 176 ALA B N    1 
ATOM   7031  C  CA   . ALA B 1 158 ? 30.749  -26.138 26.364  1.00 15.60  ? 176 ALA B CA   1 
ATOM   7032  C  C    . ALA B 1 158 ? 29.911  -25.352 25.360  1.00 13.98  ? 176 ALA B C    1 
ATOM   7033  O  O    . ALA B 1 158 ? 28.683  -25.276 25.483  1.00 14.88  ? 176 ALA B O    1 
ATOM   7034  C  CB   . ALA B 1 158 ? 30.858  -27.583 25.879  1.00 16.56  ? 176 ALA B CB   1 
ATOM   7035  H  H    . ALA B 1 158 ? 29.902  -26.883 27.967  1.00 18.37  ? 176 ALA B H    1 
ATOM   7036  H  HA   . ALA B 1 158 ? 31.633  -25.740 26.418  1.00 18.72  ? 176 ALA B HA   1 
ATOM   7037  H  HB1  . ALA B 1 158 ? 31.232  -27.589 24.984  1.00 19.87  ? 176 ALA B HB1  1 
ATOM   7038  H  HB2  . ALA B 1 158 ? 31.436  -28.076 26.482  1.00 19.87  ? 176 ALA B HB2  1 
ATOM   7039  H  HB3  . ALA B 1 158 ? 29.973  -27.980 25.870  1.00 19.87  ? 176 ALA B HB3  1 
ATOM   7040  N  N    . PRO B 1 159 ? 30.552  -24.783 24.337  1.00 13.93  ? 177 PRO B N    1 
ATOM   7041  C  CA   . PRO B 1 159 ? 29.805  -24.113 23.268  1.00 13.82  ? 177 PRO B CA   1 
ATOM   7042  C  C    . PRO B 1 159 ? 28.578  -24.865 22.784  1.00 13.38  ? 177 PRO B C    1 
ATOM   7043  O  O    . PRO B 1 159 ? 27.487  -24.291 22.739  1.00 13.62  ? 177 PRO B O    1 
ATOM   7044  C  CB   . PRO B 1 159 ? 30.855  -23.970 22.159  1.00 13.69  ? 177 PRO B CB   1 
ATOM   7045  C  CG   . PRO B 1 159 ? 32.139  -23.784 22.917  1.00 14.35  ? 177 PRO B CG   1 
ATOM   7046  C  CD   . PRO B 1 159 ? 32.012  -24.633 24.167  1.00 13.72  ? 177 PRO B CD   1 
ATOM   7047  H  HA   . PRO B 1 159 ? 29.517  -23.240 23.577  1.00 16.58  ? 177 PRO B HA   1 
ATOM   7048  H  HB2  . PRO B 1 159 ? 30.880  -24.772 21.614  1.00 16.43  ? 177 PRO B HB2  1 
ATOM   7049  H  HB3  . PRO B 1 159 ? 30.657  -23.199 21.605  1.00 16.43  ? 177 PRO B HB3  1 
ATOM   7050  H  HG2  . PRO B 1 159 ? 32.886  -24.082 22.374  1.00 17.21  ? 177 PRO B HG2  1 
ATOM   7051  H  HG3  . PRO B 1 159 ? 32.250  -22.848 23.148  1.00 17.21  ? 177 PRO B HG3  1 
ATOM   7052  H  HD2  . PRO B 1 159 ? 32.435  -25.497 24.041  1.00 16.47  ? 177 PRO B HD2  1 
ATOM   7053  H  HD3  . PRO B 1 159 ? 32.403  -24.181 24.931  1.00 16.47  ? 177 PRO B HD3  1 
ATOM   7054  N  N    . SER B 1 160 ? 28.724  -26.139 22.421  1.00 13.25  ? 178 SER B N    1 
ATOM   7055  C  CA   . SER B 1 160 ? 27.586  -26.853 21.853  1.00 13.49  ? 178 SER B CA   1 
ATOM   7056  C  C    . SER B 1 160 ? 26.551  -27.235 22.906  1.00 13.51  ? 178 SER B C    1 
ATOM   7057  O  O    . SER B 1 160 ? 25.400  -27.519 22.552  1.00 13.91  ? 178 SER B O    1 
ATOM   7058  C  CB   . SER B 1 160 ? 28.055  -28.097 21.107  1.00 13.15  ? 178 SER B CB   1 
ATOM   7059  O  OG   . SER B 1 160 ? 28.563  -29.044 22.030  1.00 13.98  ? 178 SER B OG   1 
ATOM   7060  H  H    . SER B 1 160 ? 29.448  -26.597 22.492  1.00 15.89  ? 178 SER B H    1 
ATOM   7061  H  HA   . SER B 1 160 ? 27.151  -26.277 21.206  1.00 16.18  ? 178 SER B HA   1 
ATOM   7062  H  HB2  . SER B 1 160 ? 27.305  -28.486 20.630  1.00 15.78  ? 178 SER B HB2  1 
ATOM   7063  H  HB3  . SER B 1 160 ? 28.754  -27.851 20.482  1.00 15.78  ? 178 SER B HB3  1 
ATOM   7064  H  HG   . SER B 1 160 ? 28.918  -29.684 21.619  1.00 16.78  ? 178 SER B HG   1 
ATOM   7065  N  N    . VAL B 1 161 ? 26.927  -27.229 24.187  1.00 13.83  ? 179 VAL B N    1 
ATOM   7066  C  CA   . VAL B 1 161 ? 25.949  -27.467 25.241  1.00 13.96  ? 179 VAL B CA   1 
ATOM   7067  C  C    . VAL B 1 161 ? 25.031  -26.257 25.386  1.00 13.49  ? 179 VAL B C    1 
ATOM   7068  O  O    . VAL B 1 161 ? 23.807  -26.401 25.510  1.00 15.16  ? 179 VAL B O    1 
ATOM   7069  C  CB   . VAL B 1 161 ? 26.656  -27.865 26.551  1.00 17.06  ? 179 VAL B CB   1 
ATOM   7070  C  CG1  . VAL B 1 161 ? 25.674  -27.905 27.711  1.00 17.38  ? 179 VAL B CG1  1 
ATOM   7071  C  CG2  . VAL B 1 161 ? 27.337  -29.230 26.371  1.00 18.30  ? 179 VAL B CG2  1 
ATOM   7072  H  H    . VAL B 1 161 ? 27.729  -27.091 24.465  1.00 16.60  ? 179 VAL B H    1 
ATOM   7073  H  HA   . VAL B 1 161 ? 25.387  -28.218 24.996  1.00 16.75  ? 179 VAL B HA   1 
ATOM   7074  H  HB   . VAL B 1 161 ? 27.330  -27.201 26.764  1.00 20.47  ? 179 VAL B HB   1 
ATOM   7075  H  HG11 . VAL B 1 161 ? 24.841  -28.299 27.406  1.00 20.85  ? 179 VAL B HG11 1 
ATOM   7076  H  HG12 . VAL B 1 161 ? 26.051  -28.442 28.425  1.00 20.85  ? 179 VAL B HG12 1 
ATOM   7077  H  HG13 . VAL B 1 161 ? 25.517  -27.001 28.023  1.00 20.85  ? 179 VAL B HG13 1 
ATOM   7078  H  HG21 . VAL B 1 161 ? 27.664  -29.302 25.460  1.00 21.97  ? 179 VAL B HG21 1 
ATOM   7079  H  HG22 . VAL B 1 161 ? 28.077  -29.299 26.995  1.00 21.97  ? 179 VAL B HG22 1 
ATOM   7080  H  HG23 . VAL B 1 161 ? 26.690  -29.932 26.546  1.00 21.97  ? 179 VAL B HG23 1 
ATOM   7081  N  N    . TRP B 1 162 ? 25.595  -25.046 25.316  1.00 13.45  ? 180 TRP B N    1 
ATOM   7082  C  CA   . TRP B 1 162 ? 24.764  -23.845 25.253  1.00 13.55  ? 180 TRP B CA   1 
ATOM   7083  C  C    . TRP B 1 162 ? 23.773  -23.943 24.105  1.00 14.15  ? 180 TRP B C    1 
ATOM   7084  O  O    . TRP B 1 162 ? 22.581  -23.657 24.259  1.00 14.41  ? 180 TRP B O    1 
ATOM   7085  C  CB   . TRP B 1 162 ? 25.632  -22.600 25.042  1.00 14.62  ? 180 TRP B CB   1 
ATOM   7086  C  CG   . TRP B 1 162 ? 26.236  -22.115 26.289  1.00 15.15  ? 180 TRP B CG   1 
ATOM   7087  C  CD1  . TRP B 1 162 ? 27.473  -22.425 26.764  1.00 15.20  ? 180 TRP B CD1  1 
ATOM   7088  C  CD2  . TRP B 1 162 ? 25.636  -21.244 27.255  1.00 15.81  ? 180 TRP B CD2  1 
ATOM   7089  N  NE1  . TRP B 1 162 ? 27.683  -21.802 27.962  1.00 15.75  ? 180 TRP B NE1  1 
ATOM   7090  C  CE2  . TRP B 1 162 ? 26.574  -21.065 28.285  1.00 16.89  ? 180 TRP B CE2  1 
ATOM   7091  C  CE3  . TRP B 1 162 ? 24.399  -20.591 27.343  1.00 16.58  ? 180 TRP B CE3  1 
ATOM   7092  C  CZ2  . TRP B 1 162 ? 26.314  -20.274 29.404  1.00 19.44  ? 180 TRP B CZ2  1 
ATOM   7093  C  CZ3  . TRP B 1 162 ? 24.144  -19.799 28.456  1.00 18.90  ? 180 TRP B CZ3  1 
ATOM   7094  C  CH2  . TRP B 1 162 ? 25.101  -19.648 29.469  1.00 19.36  ? 180 TRP B CH2  1 
ATOM   7095  H  H    . TRP B 1 162 ? 26.442  -24.898 25.303  1.00 16.15  ? 180 TRP B H    1 
ATOM   7096  H  HA   . TRP B 1 162 ? 24.292  -23.760 26.096  1.00 16.26  ? 180 TRP B HA   1 
ATOM   7097  H  HB2  . TRP B 1 162 ? 26.348  -22.815 24.425  1.00 17.55  ? 180 TRP B HB2  1 
ATOM   7098  H  HB3  . TRP B 1 162 ? 25.082  -21.889 24.678  1.00 17.55  ? 180 TRP B HB3  1 
ATOM   7099  H  HD1  . TRP B 1 162 ? 28.086  -22.979 26.336  1.00 18.24  ? 180 TRP B HD1  1 
ATOM   7100  H  HE1  . TRP B 1 162 ? 28.397  -21.863 28.437  1.00 18.90  ? 180 TRP B HE1  1 
ATOM   7101  H  HE3  . TRP B 1 162 ? 23.763  -20.685 26.671  1.00 19.90  ? 180 TRP B HE3  1 
ATOM   7102  H  HZ2  . TRP B 1 162 ? 26.944  -20.177 30.082  1.00 23.33  ? 180 TRP B HZ2  1 
ATOM   7103  H  HZ3  . TRP B 1 162 ? 23.326  -19.364 28.530  1.00 22.68  ? 180 TRP B HZ3  1 
ATOM   7104  H  HH2  . TRP B 1 162 ? 24.907  -19.109 30.201  1.00 23.23  ? 180 TRP B HH2  1 
ATOM   7105  N  N    . GLN B 1 163 ? 24.262  -24.353 22.936  1.00 13.56  ? 181 GLN B N    1 
ATOM   7106  C  CA   . GLN B 1 163 ? 23.438  -24.328 21.735  1.00 13.80  ? 181 GLN B CA   1 
ATOM   7107  C  C    . GLN B 1 163 ? 22.339  -25.377 21.773  1.00 13.49  ? 181 GLN B C    1 
ATOM   7108  O  O    . GLN B 1 163 ? 21.302  -25.204 21.117  1.00 13.78  ? 181 GLN B O    1 
ATOM   7109  C  CB   . GLN B 1 163 ? 24.332  -24.488 20.509  1.00 14.08  ? 181 GLN B CB   1 
ATOM   7110  C  CG   . GLN B 1 163 ? 25.288  -23.318 20.360  1.00 13.18  ? 181 GLN B CG   1 
ATOM   7111  C  CD   . GLN B 1 163 ? 26.361  -23.546 19.333  1.00 13.27  ? 181 GLN B CD   1 
ATOM   7112  O  OE1  . GLN B 1 163 ? 27.075  -24.545 19.381  1.00 13.86  ? 181 GLN B OE1  1 
ATOM   7113  N  NE2  . GLN B 1 163 ? 26.511  -22.598 18.416  1.00 14.00  ? 181 GLN B NE2  1 
ATOM   7114  H  H    . GLN B 1 163 ? 25.061  -24.648 22.813  1.00 16.28  ? 181 GLN B H    1 
ATOM   7115  H  HA   . GLN B 1 163 ? 22.992  -23.469 21.666  1.00 16.56  ? 181 GLN B HA   1 
ATOM   7116  H  HB2  . GLN B 1 163 ? 24.855  -25.300 20.597  1.00 16.90  ? 181 GLN B HB2  1 
ATOM   7117  H  HB3  . GLN B 1 163 ? 23.779  -24.534 19.713  1.00 16.90  ? 181 GLN B HB3  1 
ATOM   7118  H  HG2  . GLN B 1 163 ? 24.784  -22.534 20.092  1.00 15.81  ? 181 GLN B HG2  1 
ATOM   7119  H  HG3  . GLN B 1 163 ? 25.723  -23.159 21.212  1.00 15.81  ? 181 GLN B HG3  1 
ATOM   7120  H  HE21 . GLN B 1 163 ? 26.007  -21.901 18.433  1.00 16.80  ? 181 GLN B HE21 1 
ATOM   7121  H  HE22 . GLN B 1 163 ? 27.111  -22.681 17.806  1.00 16.80  ? 181 GLN B HE22 1 
ATOM   7122  N  N    . GLN B 1 164 ? 22.538  -26.459 22.529  1.00 13.48  ? 182 GLN B N    1 
ATOM   7123  C  CA   . GLN B 1 164 ? 21.518  -27.483 22.709  1.00 13.64  ? 182 GLN B CA   1 
ATOM   7124  C  C    . GLN B 1 164 ? 20.609  -27.219 23.902  1.00 14.61  ? 182 GLN B C    1 
ATOM   7125  O  O    . GLN B 1 164 ? 19.768  -28.063 24.219  1.00 15.53  ? 182 GLN B O    1 
ATOM   7126  C  CB   . GLN B 1 164 ? 22.184  -28.855 22.842  1.00 14.31  ? 182 GLN B CB   1 
ATOM   7127  C  CG   . GLN B 1 164 ? 22.914  -29.278 21.584  1.00 16.10  ? 182 GLN B CG   1 
ATOM   7128  C  CD   . GLN B 1 164 ? 23.758  -30.501 21.797  1.00 16.78  ? 182 GLN B CD   1 
ATOM   7129  O  OE1  . GLN B 1 164 ? 24.952  -30.409 22.117  1.00 19.21  ? 182 GLN B OE1  1 
ATOM   7130  N  NE2  . GLN B 1 164 ? 23.145  -31.663 21.655  1.00 15.07  ? 182 GLN B NE2  1 
ATOM   7131  H  H    . GLN B 1 164 ? 23.269  -26.621 22.952  1.00 16.18  ? 182 GLN B H    1 
ATOM   7132  H  HA   . GLN B 1 164 ? 20.952  -27.505 21.923  1.00 16.37  ? 182 GLN B HA   1 
ATOM   7133  H  HB2  . GLN B 1 164 ? 22.829  -28.824 23.567  1.00 17.17  ? 182 GLN B HB2  1 
ATOM   7134  H  HB3  . GLN B 1 164 ? 21.503  -29.519 23.032  1.00 17.17  ? 182 GLN B HB3  1 
ATOM   7135  H  HG2  . GLN B 1 164 ? 22.264  -29.476 20.892  1.00 19.32  ? 182 GLN B HG2  1 
ATOM   7136  H  HG3  . GLN B 1 164 ? 23.495  -28.556 21.297  1.00 19.32  ? 182 GLN B HG3  1 
ATOM   7137  H  HE21 . GLN B 1 164 ? 22.309  -31.686 21.453  1.00 18.08  ? 182 GLN B HE21 1 
ATOM   7138  H  HE22 . GLN B 1 164 ? 23.581  -32.396 21.765  1.00 18.08  ? 182 GLN B HE22 1 
ATOM   7139  N  N    . THR B 1 165 ? 20.750  -26.079 24.573  1.00 14.80  ? 183 THR B N    1 
ATOM   7140  C  CA   . THR B 1 165 ? 19.827  -25.714 25.640  1.00 14.77  ? 183 THR B CA   1 
ATOM   7141  C  C    . THR B 1 165 ? 18.569  -25.113 25.029  1.00 15.10  ? 183 THR B C    1 
ATOM   7142  O  O    . THR B 1 165 ? 18.644  -24.194 24.213  1.00 15.91  ? 183 THR B O    1 
ATOM   7143  C  CB   . THR B 1 165 ? 20.502  -24.722 26.585  1.00 15.99  ? 183 THR B CB   1 
ATOM   7144  O  OG1  . THR B 1 165 ? 21.656  -25.345 27.161  1.00 17.06  ? 183 THR B OG1  1 
ATOM   7145  C  CG2  . THR B 1 165 ? 19.552  -24.279 27.698  1.00 16.33  ? 183 THR B CG2  1 
ATOM   7146  H  H    . THR B 1 165 ? 21.371  -25.502 24.429  1.00 17.75  ? 183 THR B H    1 
ATOM   7147  H  HA   . THR B 1 165 ? 19.573  -26.495 26.157  1.00 17.72  ? 183 THR B HA   1 
ATOM   7148  H  HB   . THR B 1 165 ? 20.762  -23.928 26.091  1.00 19.18  ? 183 THR B HB   1 
ATOM   7149  H  HG1  . THR B 1 165 ? 22.114  -24.776 27.576  1.00 20.48  ? 183 THR B HG1  1 
ATOM   7150  H  HG21 . THR B 1 165 ? 18.831  -23.746 27.327  1.00 19.60  ? 183 THR B HG21 1 
ATOM   7151  H  HG22 . THR B 1 165 ? 19.174  -25.056 28.140  1.00 19.60  ? 183 THR B HG22 1 
ATOM   7152  H  HG23 . THR B 1 165 ? 20.032  -23.747 28.352  1.00 19.60  ? 183 THR B HG23 1 
ATOM   7153  N  N    . THR B 1 166 ? 17.409  -25.632 25.415  1.00 15.80  ? 184 THR B N    1 
ATOM   7154  C  CA   . THR B 1 166 ? 16.160  -25.080 24.906  1.00 16.85  ? 184 THR B CA   1 
ATOM   7155  C  C    . THR B 1 166 ? 16.101  -23.592 25.219  1.00 17.07  ? 184 THR B C    1 
ATOM   7156  O  O    . THR B 1 166 ? 16.470  -23.158 26.315  1.00 18.09  ? 184 THR B O    1 
ATOM   7157  C  CB   . THR B 1 166 ? 14.982  -25.831 25.516  1.00 18.93  ? 184 THR B CB   1 
ATOM   7158  O  OG1  . THR B 1 166 ? 15.042  -27.199 25.087  1.00 20.63  ? 184 THR B OG1  1 
ATOM   7159  C  CG2  . THR B 1 166 ? 13.658  -25.219 25.091  1.00 18.57  ? 184 THR B CG2  1 
ATOM   7160  H  H    . THR B 1 166 ? 17.319  -26.291 25.960  1.00 18.96  ? 184 THR B H    1 
ATOM   7161  H  HA   . THR B 1 166 ? 16.100  -25.185 23.944  1.00 20.22  ? 184 THR B HA   1 
ATOM   7162  H  HB   . THR B 1 166 ? 15.025  -25.780 26.484  1.00 22.72  ? 184 THR B HB   1 
ATOM   7163  H  HG1  . THR B 1 166 ? 15.092  -27.236 24.249  1.00 24.75  ? 184 THR B HG1  1 
ATOM   7164  H  HG21 . THR B 1 166 ? 12.931  -25.827 25.296  1.00 22.28  ? 184 THR B HG21 1 
ATOM   7165  H  HG22 . THR B 1 166 ? 13.512  -24.384 25.561  1.00 22.28  ? 184 THR B HG22 1 
ATOM   7166  H  HG23 . THR B 1 166 ? 13.664  -25.046 24.136  1.00 22.28  ? 184 THR B HG23 1 
ATOM   7167  N  N    . GLY B 1 167 ? 15.665  -22.812 24.225  1.00 16.38  ? 185 GLY B N    1 
ATOM   7168  C  CA   . GLY B 1 167 ? 15.716  -21.365 24.260  1.00 17.44  ? 185 GLY B CA   1 
ATOM   7169  C  C    . GLY B 1 167 ? 16.917  -20.759 23.556  1.00 16.25  ? 185 GLY B C    1 
ATOM   7170  O  O    . GLY B 1 167 ? 16.947  -19.538 23.355  1.00 17.46  ? 185 GLY B O    1 
ATOM   7171  H  H    . GLY B 1 167 ? 15.325  -23.117 23.496  1.00 19.66  ? 185 GLY B H    1 
ATOM   7172  H  HA2  . GLY B 1 167 ? 14.916  -21.014 23.838  1.00 20.92  ? 185 GLY B HA2  1 
ATOM   7173  H  HA3  . GLY B 1 167 ? 15.737  -21.076 25.185  1.00 20.92  ? 185 GLY B HA3  1 
ATOM   7174  N  N    . SER B 1 168 ? 17.887  -21.577 23.155  1.00 15.25  ? 186 SER B N    1 
ATOM   7175  C  CA   . SER B 1 168 ? 19.124  -21.070 22.584  1.00 14.19  ? 186 SER B CA   1 
ATOM   7176  C  C    . SER B 1 168 ? 18.880  -20.348 21.265  1.00 14.17  ? 186 SER B C    1 
ATOM   7177  O  O    . SER B 1 168 ? 17.903  -20.604 20.552  1.00 15.04  ? 186 SER B O    1 
ATOM   7178  C  CB   . SER B 1 168 ? 20.102  -22.224 22.349  1.00 14.16  ? 186 SER B CB   1 
ATOM   7179  O  OG   . SER B 1 168 ? 19.667  -23.092 21.298  1.00 14.17  ? 186 SER B OG   1 
ATOM   7180  H  H    . SER B 1 168 ? 17.850  -22.435 23.205  1.00 18.30  ? 186 SER B H    1 
ATOM   7181  H  HA   . SER B 1 168 ? 19.514  -20.436 23.206  1.00 17.03  ? 186 SER B HA   1 
ATOM   7182  H  HB2  . SER B 1 168 ? 20.967  -21.854 22.109  1.00 17.00  ? 186 SER B HB2  1 
ATOM   7183  H  HB3  . SER B 1 168 ? 20.177  -22.739 23.167  1.00 17.00  ? 186 SER B HB3  1 
ATOM   7184  H  HG   . SER B 1 168 ? 18.896  -23.381 21.464  1.00 17.00  ? 186 SER B HG   1 
ATOM   7185  N  N    . ALA B 1 169 ? 19.798  -19.436 20.942  1.00 14.20  ? 187 ALA B N    1 
ATOM   7186  C  CA   . ALA B 1 169 ? 19.759  -18.768 19.648  1.00 14.15  ? 187 ALA B CA   1 
ATOM   7187  C  C    . ALA B 1 169 ? 19.861  -19.774 18.510  1.00 13.69  ? 187 ALA B C    1 
ATOM   7188  O  O    . ALA B 1 169 ? 19.191  -19.634 17.480  1.00 14.06  ? 187 ALA B O    1 
ATOM   7189  C  CB   . ALA B 1 169 ? 20.897  -17.755 19.561  1.00 14.84  ? 187 ALA B CB   1 
ATOM   7190  H  H    . ALA B 1 169 ? 20.447  -19.190 21.450  1.00 17.04  ? 187 ALA B H    1 
ATOM   7191  H  HA   . ALA B 1 169 ? 18.916  -18.295 19.559  1.00 16.98  ? 187 ALA B HA   1 
ATOM   7192  H  HB1  . ALA B 1 169 ? 20.813  -17.256 18.734  1.00 17.80  ? 187 ALA B HB1  1 
ATOM   7193  H  HB2  . ALA B 1 169 ? 20.841  -17.152 20.319  1.00 17.80  ? 187 ALA B HB2  1 
ATOM   7194  H  HB3  . ALA B 1 169 ? 21.743  -18.229 19.578  1.00 17.80  ? 187 ALA B HB3  1 
ATOM   7195  N  N    . LEU B 1 170 ? 20.678  -20.813 18.687  1.00 13.62  ? 188 LEU B N    1 
ATOM   7196  C  CA   . LEU B 1 170 ? 20.840  -21.796 17.625  1.00 12.40  ? 188 LEU B CA   1 
ATOM   7197  C  C    . LEU B 1 170 ? 19.528  -22.517 17.341  1.00 11.94  ? 188 LEU B C    1 
ATOM   7198  O  O    . LEU B 1 170 ? 19.104  -22.617 16.185  1.00 13.22  ? 188 LEU B O    1 
ATOM   7199  C  CB   . LEU B 1 170 ? 21.946  -22.796 17.970  1.00 12.91  ? 188 LEU B CB   1 
ATOM   7200  C  CG   . LEU B 1 170 ? 22.234  -23.746 16.798  1.00 14.52  ? 188 LEU B CG   1 
ATOM   7201  C  CD1  . LEU B 1 170 ? 23.677  -23.624 16.336  1.00 15.12  ? 188 LEU B CD1  1 
ATOM   7202  C  CD2  . LEU B 1 170 ? 21.906  -25.171 17.158  1.00 18.22  ? 188 LEU B CD2  1 
ATOM   7203  H  H    . LEU B 1 170 ? 21.138  -20.966 19.397  1.00 16.35  ? 188 LEU B H    1 
ATOM   7204  H  HA   . LEU B 1 170 ? 21.114  -21.330 16.819  1.00 14.88  ? 188 LEU B HA   1 
ATOM   7205  H  HB2  . LEU B 1 170 ? 22.760  -22.312 18.179  1.00 15.50  ? 188 LEU B HB2  1 
ATOM   7206  H  HB3  . LEU B 1 170 ? 21.669  -23.327 18.734  1.00 15.50  ? 188 LEU B HB3  1 
ATOM   7207  H  HG   . LEU B 1 170 ? 21.664  -23.492 16.056  1.00 17.43  ? 188 LEU B HG   1 
ATOM   7208  H  HD11 . LEU B 1 170 ? 24.264  -23.898 17.058  1.00 18.14  ? 188 LEU B HD11 1 
ATOM   7209  H  HD12 . LEU B 1 170 ? 23.811  -24.198 15.565  1.00 18.14  ? 188 LEU B HD12 1 
ATOM   7210  H  HD13 . LEU B 1 170 ? 23.855  -22.701 16.096  1.00 18.14  ? 188 LEU B HD13 1 
ATOM   7211  H  HD21 . LEU B 1 170 ? 20.992  -25.213 17.481  1.00 21.87  ? 188 LEU B HD21 1 
ATOM   7212  H  HD22 . LEU B 1 170 ? 22.002  -25.726 16.368  1.00 21.87  ? 188 LEU B HD22 1 
ATOM   7213  H  HD23 . LEU B 1 170 ? 22.516  -25.471 17.850  1.00 21.87  ? 188 LEU B HD23 1 
ATOM   7214  N  N    . THR B 1 171 ? 18.877  -23.051 18.380  1.00 12.50  ? 189 THR B N    1 
ATOM   7215  C  CA   . THR B 1 171 ? 17.624  -23.763 18.130  1.00 13.50  ? 189 THR B CA   1 
ATOM   7216  C  C    . THR B 1 171 ? 16.543  -22.808 17.623  1.00 13.37  ? 189 THR B C    1 
ATOM   7217  O  O    . THR B 1 171 ? 15.704  -23.203 16.804  1.00 13.83  ? 189 THR B O    1 
ATOM   7218  C  CB   . THR B 1 171 ? 17.156  -24.544 19.365  1.00 14.64  ? 189 THR B CB   1 
ATOM   7219  O  OG1  . THR B 1 171 ? 17.073  -23.681 20.506  1.00 15.70  ? 189 THR B OG1  1 
ATOM   7220  C  CG2  . THR B 1 171 ? 18.096  -25.711 19.657  1.00 15.42  ? 189 THR B CG2  1 
ATOM   7221  H  H    . THR B 1 171 ? 19.130  -23.017 19.201  1.00 15.00  ? 189 THR B H    1 
ATOM   7222  H  HA   . THR B 1 171 ? 17.781  -24.431 17.445  1.00 16.20  ? 189 THR B HA   1 
ATOM   7223  H  HB   . THR B 1 171 ? 16.273  -24.905 19.192  1.00 17.56  ? 189 THR B HB   1 
ATOM   7224  H  HG1  . THR B 1 171 ? 16.472  -23.106 20.389  1.00 18.83  ? 189 THR B HG1  1 
ATOM   7225  H  HG21 . THR B 1 171 ? 18.054  -26.359 18.936  1.00 18.51  ? 189 THR B HG21 1 
ATOM   7226  H  HG22 . THR B 1 171 ? 19.008  -25.391 19.739  1.00 18.51  ? 189 THR B HG22 1 
ATOM   7227  H  HG23 . THR B 1 171 ? 17.840  -26.145 20.486  1.00 18.51  ? 189 THR B HG23 1 
ATOM   7228  N  N    . THR B 1 172 ? 16.559  -21.554 18.091  1.00 13.90  ? 190 THR B N    1 
ATOM   7229  C  CA   . THR B 1 172 ? 15.643  -20.539 17.577  1.00 14.48  ? 190 THR B CA   1 
ATOM   7230  C  C    . THR B 1 172 ? 15.842  -20.345 16.079  1.00 14.74  ? 190 THR B C    1 
ATOM   7231  O  O    . THR B 1 172 ? 14.878  -20.346 15.300  1.00 14.71  ? 190 THR B O    1 
ATOM   7232  C  CB   . THR B 1 172 ? 15.887  -19.217 18.318  1.00 15.96  ? 190 THR B CB   1 
ATOM   7233  O  OG1  . THR B 1 172 ? 15.584  -19.361 19.713  1.00 16.64  ? 190 THR B OG1  1 
ATOM   7234  C  CG2  . THR B 1 172 ? 15.048  -18.096 17.726  1.00 15.66  ? 190 THR B CG2  1 
ATOM   7235  H  H    . THR B 1 172 ? 17.091  -21.269 18.704  1.00 16.68  ? 190 THR B H    1 
ATOM   7236  H  HA   . THR B 1 172 ? 14.728  -20.822 17.733  1.00 17.38  ? 190 THR B HA   1 
ATOM   7237  H  HB   . THR B 1 172 ? 16.821  -18.976 18.222  1.00 19.15  ? 190 THR B HB   1 
ATOM   7238  H  HG1  . THR B 1 172 ? 14.756  -19.460 19.818  1.00 19.96  ? 190 THR B HG1  1 
ATOM   7239  H  HG21 . THR B 1 172 ? 14.170  -18.430 17.486  1.00 18.80  ? 190 THR B HG21 1 
ATOM   7240  H  HG22 . THR B 1 172 ? 14.947  -17.381 18.374  1.00 18.80  ? 190 THR B HG22 1 
ATOM   7241  H  HG23 . THR B 1 172 ? 15.479  -17.743 16.932  1.00 18.80  ? 190 THR B HG23 1 
ATOM   7242  N  N    . ALA B 1 173 ? 17.099  -20.184 15.657  1.00 13.82  ? 191 ALA B N    1 
ATOM   7243  C  CA   . ALA B 1 173 ? 17.386  -19.940 14.248  1.00 14.49  ? 191 ALA B CA   1 
ATOM   7244  C  C    . ALA B 1 173 ? 17.004  -21.133 13.379  1.00 13.72  ? 191 ALA B C    1 
ATOM   7245  O  O    . ALA B 1 173 ? 16.470  -20.954 12.279  1.00 14.72  ? 191 ALA B O    1 
ATOM   7246  C  CB   . ALA B 1 173 ? 18.863  -19.592 14.063  1.00 14.17  ? 191 ALA B CB   1 
ATOM   7247  H  H    . ALA B 1 173 ? 17.794  -20.213 16.163  1.00 16.59  ? 191 ALA B H    1 
ATOM   7248  H  HA   . ALA B 1 173 ? 16.858  -19.181 13.955  1.00 17.39  ? 191 ALA B HA   1 
ATOM   7249  H  HB1  . ALA B 1 173 ? 19.036  -19.442 13.121  1.00 17.01  ? 191 ALA B HB1  1 
ATOM   7250  H  HB2  . ALA B 1 173 ? 19.063  -18.789 14.569  1.00 17.01  ? 191 ALA B HB2  1 
ATOM   7251  H  HB3  . ALA B 1 173 ? 19.403  -20.330 14.386  1.00 17.01  ? 191 ALA B HB3  1 
ATOM   7252  N  N    . LEU B 1 174 ? 17.290  -22.357 13.841  1.00 14.41  ? 192 LEU B N    1 
ATOM   7253  C  CA   . LEU B 1 174 ? 16.891  -23.544 13.090  1.00 14.09  ? 192 LEU B CA   1 
ATOM   7254  C  C    . LEU B 1 174 ? 15.390  -23.542 12.844  1.00 14.61  ? 192 LEU B C    1 
ATOM   7255  O  O    . LEU B 1 174 ? 14.924  -23.776 11.721  1.00 15.97  ? 192 LEU B O    1 
ATOM   7256  C  CB   . LEU B 1 174 ? 17.285  -24.815 13.850  1.00 13.94  ? 192 LEU B CB   1 
ATOM   7257  C  CG   . LEU B 1 174 ? 16.881  -26.130 13.173  1.00 15.01  ? 192 LEU B CG   1 
ATOM   7258  C  CD1  . LEU B 1 174 ? 17.610  -26.312 11.839  1.00 16.05  ? 192 LEU B CD1  1 
ATOM   7259  C  CD2  . LEU B 1 174 ? 17.124  -27.325 14.096  1.00 16.60  ? 192 LEU B CD2  1 
ATOM   7260  H  H    . LEU B 1 174 ? 17.708  -22.520 14.575  1.00 17.30  ? 192 LEU B H    1 
ATOM   7261  H  HA   . LEU B 1 174 ? 17.356  -23.540 12.239  1.00 16.91  ? 192 LEU B HA   1 
ATOM   7262  H  HB2  . LEU B 1 174 ? 18.249  -24.824 13.952  1.00 16.73  ? 192 LEU B HB2  1 
ATOM   7263  H  HB3  . LEU B 1 174 ? 16.859  -24.794 14.722  1.00 16.73  ? 192 LEU B HB3  1 
ATOM   7264  H  HG   . LEU B 1 174 ? 15.930  -26.094 12.984  1.00 18.02  ? 192 LEU B HG   1 
ATOM   7265  H  HD11 . LEU B 1 174 ? 17.407  -27.192 11.485  1.00 19.26  ? 192 LEU B HD11 1 
ATOM   7266  H  HD12 . LEU B 1 174 ? 17.311  -25.629 11.219  1.00 19.26  ? 192 LEU B HD12 1 
ATOM   7267  H  HD13 . LEU B 1 174 ? 18.565  -26.228 11.987  1.00 19.26  ? 192 LEU B HD13 1 
ATOM   7268  H  HD21 . LEU B 1 174 ? 18.070  -27.373 14.308  1.00 19.92  ? 192 LEU B HD21 1 
ATOM   7269  H  HD22 . LEU B 1 174 ? 16.609  -27.206 14.909  1.00 19.92  ? 192 LEU B HD22 1 
ATOM   7270  H  HD23 . LEU B 1 174 ? 16.845  -28.136 13.643  1.00 19.92  ? 192 LEU B HD23 1 
ATOM   7271  N  N    . ARG B 1 175 ? 14.616  -23.320 13.905  1.00 14.22  ? 193 ARG B N    1 
ATOM   7272  C  CA   . ARG B 1 175 ? 13.163  -23.300 13.782  1.00 15.57  ? 193 ARG B CA   1 
ATOM   7273  C  C    . ARG B 1 175 ? 12.708  -22.211 12.817  1.00 16.26  ? 193 ARG B C    1 
ATOM   7274  O  O    . ARG B 1 175 ? 11.877  -22.452 11.934  1.00 17.70  ? 193 ARG B O    1 
ATOM   7275  C  CB   . ARG B 1 175 ? 12.547  -23.082 15.166  1.00 16.90  ? 193 ARG B CB   1 
ATOM   7276  C  CG   . ARG B 1 175 ? 11.046  -22.830 15.156  1.00 20.22  ? 193 ARG B CG   1 
ATOM   7277  C  CD   . ARG B 1 175 ? 10.553  -22.445 16.548  1.00 20.78  ? 193 ARG B CD   1 
ATOM   7278  N  NE   . ARG B 1 175 ? 10.926  -21.083 16.916  1.00 24.08  ? 193 ARG B NE   1 
ATOM   7279  C  CZ   . ARG B 1 175 ? 11.598  -20.746 18.015  1.00 25.13  ? 193 ARG B CZ   1 
ATOM   7280  N  NH1  . ARG B 1 175 ? 12.003  -21.669 18.882  1.00 25.08  ? 193 ARG B NH1  1 
ATOM   7281  N  NH2  . ARG B 1 175 ? 11.865  -19.469 18.247  1.00 26.71  ? 193 ARG B NH2  1 
ATOM   7282  H  H    . ARG B 1 175 ? 14.905  -23.178 14.703  1.00 17.06  ? 193 ARG B H    1 
ATOM   7283  H  HA   . ARG B 1 175 ? 12.858  -24.152 13.433  1.00 18.69  ? 193 ARG B HA   1 
ATOM   7284  H  HB2  . ARG B 1 175 ? 12.708  -23.874 15.703  1.00 20.28  ? 193 ARG B HB2  1 
ATOM   7285  H  HB3  . ARG B 1 175 ? 12.971  -22.312 15.575  1.00 20.28  ? 193 ARG B HB3  1 
ATOM   7286  H  HG2  . ARG B 1 175 ? 10.843  -22.103 14.546  1.00 24.27  ? 193 ARG B HG2  1 
ATOM   7287  H  HG3  . ARG B 1 175 ? 10.583  -23.636 14.878  1.00 24.27  ? 193 ARG B HG3  1 
ATOM   7288  H  HD2  . ARG B 1 175 ? 9.585   -22.509 16.570  1.00 24.94  ? 193 ARG B HD2  1 
ATOM   7289  H  HD3  . ARG B 1 175 ? 10.940  -23.050 17.200  1.00 24.94  ? 193 ARG B HD3  1 
ATOM   7290  H  HE   . ARG B 1 175 ? 10.694  -20.449 16.383  1.00 28.90  ? 193 ARG B HE   1 
ATOM   7291  H  HH11 . ARG B 1 175 ? 11.833  -22.499 18.737  1.00 30.10  ? 193 ARG B HH11 1 
ATOM   7292  H  HH12 . ARG B 1 175 ? 12.436  -21.436 19.588  1.00 30.10  ? 193 ARG B HH12 1 
ATOM   7293  H  HH21 . ARG B 1 175 ? 11.606  -18.867 17.689  1.00 32.05  ? 193 ARG B HH21 1 
ATOM   7294  H  HH22 . ARG B 1 175 ? 12.299  -19.241 18.954  1.00 32.05  ? 193 ARG B HH22 1 
ATOM   7295  N  N    . ASN B 1 176 ? 13.234  -20.998 12.975  1.00 15.84  ? 194 ASN B N    1 
ATOM   7296  C  CA   . ASN B 1 176 ? 12.706  -19.880 12.201  1.00 15.98  ? 194 ASN B CA   1 
ATOM   7297  C  C    . ASN B 1 176 ? 13.139  -19.917 10.742  1.00 17.29  ? 194 ASN B C    1 
ATOM   7298  O  O    . ASN B 1 176 ? 12.486  -19.286 9.904   1.00 19.78  ? 194 ASN B O    1 
ATOM   7299  C  CB   . ASN B 1 176 ? 13.092  -18.567 12.871  1.00 16.11  ? 194 ASN B CB   1 
ATOM   7300  C  CG   . ASN B 1 176 ? 12.330  -18.337 14.164  1.00 16.79  ? 194 ASN B CG   1 
ATOM   7301  O  OD1  . ASN B 1 176 ? 11.321  -18.993 14.429  1.00 18.35  ? 194 ASN B OD1  1 
ATOM   7302  N  ND2  . ASN B 1 176 ? 12.810  -17.412 14.977  1.00 16.48  ? 194 ASN B ND2  1 
ATOM   7303  H  H    . ASN B 1 176 ? 13.878  -20.802 13.509  1.00 19.01  ? 194 ASN B H    1 
ATOM   7304  H  HA   . ASN B 1 176 ? 11.737  -19.923 12.194  1.00 19.17  ? 194 ASN B HA   1 
ATOM   7305  H  HB2  . ASN B 1 176 ? 14.040  -18.581 13.077  1.00 19.33  ? 194 ASN B HB2  1 
ATOM   7306  H  HB3  . ASN B 1 176 ? 12.895  -17.832 12.269  1.00 19.33  ? 194 ASN B HB3  1 
ATOM   7307  H  HD21 . ASN B 1 176 ? 12.413  -17.246 15.721  1.00 19.77  ? 194 ASN B HD21 1 
ATOM   7308  H  HD22 . ASN B 1 176 ? 13.519  -16.976 14.761  1.00 19.77  ? 194 ASN B HD22 1 
ATOM   7309  N  N    . ALA B 1 177 ? 14.203  -20.649 10.417  1.00 16.05  ? 195 ALA B N    1 
ATOM   7310  C  CA   . ALA B 1 177 ? 14.612  -20.831 9.030   1.00 15.48  ? 195 ALA B CA   1 
ATOM   7311  C  C    . ALA B 1 177 ? 13.869  -21.967 8.340   1.00 17.51  ? 195 ALA B C    1 
ATOM   7312  O  O    . ALA B 1 177 ? 14.073  -22.183 7.139   1.00 20.17  ? 195 ALA B O    1 
ATOM   7313  C  CB   . ALA B 1 177 ? 16.123  -21.073 8.956   1.00 16.02  ? 195 ALA B CB   1 
ATOM   7314  H  H    . ALA B 1 177 ? 14.706  -21.052 10.986  1.00 19.26  ? 195 ALA B H    1 
ATOM   7315  H  HA   . ALA B 1 177 ? 14.422  -20.016 8.539   1.00 18.57  ? 195 ALA B HA   1 
ATOM   7316  H  HB1  . ALA B 1 177 ? 16.580  -20.351 9.416   1.00 19.23  ? 195 ALA B HB1  1 
ATOM   7317  H  HB2  . ALA B 1 177 ? 16.328  -21.919 9.383   1.00 19.23  ? 195 ALA B HB2  1 
ATOM   7318  H  HB3  . ALA B 1 177 ? 16.394  -21.097 8.026   1.00 19.23  ? 195 ALA B HB3  1 
ATOM   7319  N  N    . GLY B 1 178 ? 13.018  -22.693 9.056   1.00 17.65  ? 196 GLY B N    1 
ATOM   7320  C  CA   . GLY B 1 178 ? 12.230  -23.756 8.471   1.00 19.64  ? 196 GLY B CA   1 
ATOM   7321  C  C    . GLY B 1 178 ? 12.680  -25.154 8.820   1.00 19.50  ? 196 GLY B C    1 
ATOM   7322  O  O    . GLY B 1 178 ? 12.130  -26.118 8.267   1.00 19.47  ? 196 GLY B O    1 
ATOM   7323  H  H    . GLY B 1 178 ? 12.882  -22.584 9.898   1.00 21.18  ? 196 GLY B H    1 
ATOM   7324  H  HA2  . GLY B 1 178 ? 11.312  -23.659 8.767   1.00 23.57  ? 196 GLY B HA2  1 
ATOM   7325  H  HA3  . GLY B 1 178 ? 12.261  -23.668 7.505   1.00 23.57  ? 196 GLY B HA3  1 
ATOM   7326  N  N    . GLY B 1 179 ? 13.642  -25.297 9.731   1.00 18.83  ? 197 GLY B N    1 
ATOM   7327  C  CA   . GLY B 1 179 ? 14.331  -26.539 9.977   1.00 18.98  ? 197 GLY B CA   1 
ATOM   7328  C  C    . GLY B 1 179 ? 13.653  -27.531 10.883  1.00 19.07  ? 197 GLY B C    1 
ATOM   7329  O  O    . GLY B 1 179 ? 14.242  -28.583 11.130  1.00 18.98  ? 197 GLY B O    1 
ATOM   7330  H  H    . GLY B 1 179 ? 13.918  -24.656 10.234  1.00 22.60  ? 197 GLY B H    1 
ATOM   7331  H  HA2  . GLY B 1 179 ? 14.471  -26.980 9.125   1.00 22.78  ? 197 GLY B HA2  1 
ATOM   7332  H  HA3  . GLY B 1 179 ? 15.192  -26.333 10.372  1.00 22.78  ? 197 GLY B HA3  1 
ATOM   7333  N  N    . LEU B 1 180 ? 12.459  -27.247 11.402  1.00 19.02  ? 198 LEU B N    1 
ATOM   7334  C  CA   . LEU B 1 180 ? 11.699  -28.246 12.146  1.00 20.23  ? 198 LEU B CA   1 
ATOM   7335  C  C    . LEU B 1 180 ? 10.719  -29.002 11.258  1.00 19.27  ? 198 LEU B C    1 
ATOM   7336  O  O    . LEU B 1 180 ? 9.885   -29.756 11.767  1.00 19.01  ? 198 LEU B O    1 
ATOM   7337  C  CB   . LEU B 1 180 ? 10.995  -27.621 13.350  1.00 21.75  ? 198 LEU B CB   1 
ATOM   7338  C  CG   . LEU B 1 180 ? 11.924  -27.092 14.448  1.00 22.37  ? 198 LEU B CG   1 
ATOM   7339  C  CD1  . LEU B 1 180 ? 11.109  -26.740 15.679  1.00 24.97  ? 198 LEU B CD1  1 
ATOM   7340  C  CD2  . LEU B 1 180 ? 13.027  -28.074 14.806  1.00 22.30  ? 198 LEU B CD2  1 
ATOM   7341  H  H    . LEU B 1 180 ? 12.069  -26.484 11.335  1.00 22.83  ? 198 LEU B H    1 
ATOM   7342  H  HA   . LEU B 1 180 ? 12.318  -28.896 12.514  1.00 24.28  ? 198 LEU B HA   1 
ATOM   7343  H  HB2  . LEU B 1 180 ? 10.461  -26.874 13.038  1.00 26.10  ? 198 LEU B HB2  1 
ATOM   7344  H  HB3  . LEU B 1 180 ? 10.424  -28.293 13.753  1.00 26.10  ? 198 LEU B HB3  1 
ATOM   7345  H  HG   . LEU B 1 180 ? 12.366  -26.297 14.112  1.00 26.84  ? 198 LEU B HG   1 
ATOM   7346  H  HD11 . LEU B 1 180 ? 10.490  -26.027 15.454  1.00 29.96  ? 198 LEU B HD11 1 
ATOM   7347  H  HD12 . LEU B 1 180 ? 10.618  -27.525 15.967  1.00 29.96  ? 198 LEU B HD12 1 
ATOM   7348  H  HD13 . LEU B 1 180 ? 11.709  -26.448 16.382  1.00 29.96  ? 198 LEU B HD13 1 
ATOM   7349  H  HD21 . LEU B 1 180 ? 12.633  -28.945 14.969  1.00 26.76  ? 198 LEU B HD21 1 
ATOM   7350  H  HD22 . LEU B 1 180 ? 13.654  -28.128 14.067  1.00 26.76  ? 198 LEU B HD22 1 
ATOM   7351  H  HD23 . LEU B 1 180 ? 13.482  -27.762 15.603  1.00 26.76  ? 198 LEU B HD23 1 
ATOM   7352  N  N    . THR B 1 181 ? 10.819  -28.827 9.946   1.00 18.55  ? 199 THR B N    1 
ATOM   7353  C  CA   . THR B 1 181 ? 10.166  -29.678 8.962   1.00 18.48  ? 199 THR B CA   1 
ATOM   7354  C  C    . THR B 1 181 ? 11.260  -30.432 8.220   1.00 18.24  ? 199 THR B C    1 
ATOM   7355  O  O    . THR B 1 181 ? 12.345  -29.891 7.990   1.00 19.17  ? 199 THR B O    1 
ATOM   7356  C  CB   . THR B 1 181 ? 9.354   -28.814 7.993   1.00 19.34  ? 199 THR B CB   1 
ATOM   7357  O  OG1  . THR B 1 181 ? 8.352   -28.104 8.734   1.00 20.44  ? 199 THR B OG1  1 
ATOM   7358  C  CG2  . THR B 1 181 ? 8.684   -29.655 6.921   1.00 19.04  ? 199 THR B CG2  1 
ATOM   7359  H  H    . THR B 1 181 ? 11.280  -28.196 9.587   1.00 22.27  ? 199 THR B H    1 
ATOM   7360  H  HA   . THR B 1 181 ? 9.560   -30.316 9.370   1.00 22.18  ? 199 THR B HA   1 
ATOM   7361  H  HB   . THR B 1 181 ? 9.948   -28.191 7.546   1.00 23.21  ? 199 THR B HB   1 
ATOM   7362  H  HG1  . THR B 1 181 ? 7.748   -28.633 8.981   1.00 24.53  ? 199 THR B HG1  1 
ATOM   7363  H  HG21 . THR B 1 181 ? 9.355   -30.052 6.344   1.00 22.85  ? 199 THR B HG21 1 
ATOM   7364  H  HG22 . THR B 1 181 ? 8.164   -30.363 7.332   1.00 22.85  ? 199 THR B HG22 1 
ATOM   7365  H  HG23 . THR B 1 181 ? 8.095   -29.102 6.385   1.00 22.85  ? 199 THR B HG23 1 
ATOM   7366  N  N    . GLN B 1 182 ? 11.005  -31.688 7.870   1.00 17.72  ? 200 GLN B N    1 
ATOM   7367  C  CA   . GLN B 1 182 ? 12.060  -32.446 7.210   1.00 18.12  ? 200 GLN B CA   1 
ATOM   7368  C  C    . GLN B 1 182 ? 12.400  -31.805 5.869   1.00 17.76  ? 200 GLN B C    1 
ATOM   7369  O  O    . GLN B 1 182 ? 11.561  -31.169 5.222   1.00 19.17  ? 200 GLN B O    1 
ATOM   7370  C  CB   . GLN B 1 182 ? 11.669  -33.913 7.027   1.00 18.71  ? 200 GLN B CB   1 
ATOM   7371  C  CG   . GLN B 1 182 ? 10.639  -34.173 5.943   1.00 19.28  ? 200 GLN B CG   1 
ATOM   7372  C  CD   . GLN B 1 182 ? 10.581  -35.630 5.514   1.00 20.12  ? 200 GLN B CD   1 
ATOM   7373  O  OE1  . GLN B 1 182 ? 10.998  -36.537 6.250   1.00 20.29  ? 200 GLN B OE1  1 
ATOM   7374  N  NE2  . GLN B 1 182 ? 10.053  -35.863 4.314   1.00 19.86  ? 200 GLN B NE2  1 
ATOM   7375  H  H    . GLN B 1 182 ? 10.264  -32.105 7.997   1.00 21.27  ? 200 GLN B H    1 
ATOM   7376  H  HA   . GLN B 1 182 ? 12.853  -32.439 7.768   1.00 21.74  ? 200 GLN B HA   1 
ATOM   7377  H  HB2  . GLN B 1 182 ? 12.465  -34.416 6.797   1.00 22.45  ? 200 GLN B HB2  1 
ATOM   7378  H  HB3  . GLN B 1 182 ? 11.300  -34.239 7.862   1.00 22.45  ? 200 GLN B HB3  1 
ATOM   7379  H  HG2  . GLN B 1 182 ? 9.762   -33.924 6.275   1.00 23.13  ? 200 GLN B HG2  1 
ATOM   7380  H  HG3  . GLN B 1 182 ? 10.862  -33.641 5.163   1.00 23.13  ? 200 GLN B HG3  1 
ATOM   7381  H  HE21 . GLN B 1 182 ? 9.771   -35.208 3.834   1.00 23.83  ? 200 GLN B HE21 1 
ATOM   7382  H  HE22 . GLN B 1 182 ? 9.994   -36.669 4.019   1.00 23.83  ? 200 GLN B HE22 1 
ATOM   7383  N  N    . ILE B 1 183 ? 13.659  -31.968 5.470   1.00 17.60  ? 201 ILE B N    1 
ATOM   7384  C  CA   . ILE B 1 183 ? 14.171  -31.439 4.217   1.00 16.98  ? 201 ILE B CA   1 
ATOM   7385  C  C    . ILE B 1 183 ? 14.467  -32.556 3.228   1.00 17.75  ? 201 ILE B C    1 
ATOM   7386  O  O    . ILE B 1 183 ? 14.120  -32.454 2.051   1.00 21.22  ? 201 ILE B O    1 
ATOM   7387  C  CB   . ILE B 1 183 ? 15.423  -30.574 4.490   1.00 17.52  ? 201 ILE B CB   1 
ATOM   7388  C  CG1  . ILE B 1 183 ? 15.044  -29.393 5.391   1.00 17.28  ? 201 ILE B CG1  1 
ATOM   7389  C  CG2  . ILE B 1 183 ? 16.047  -30.082 3.204   1.00 17.84  ? 201 ILE B CG2  1 
ATOM   7390  C  CD1  . ILE B 1 183 ? 16.226  -28.645 5.987   1.00 18.52  ? 201 ILE B CD1  1 
ATOM   7391  H  H    . ILE B 1 183 ? 14.251  -32.395 5.925   1.00 21.12  ? 201 ILE B H    1 
ATOM   7392  H  HA   . ILE B 1 183 ? 13.501  -30.874 3.800   1.00 20.38  ? 201 ILE B HA   1 
ATOM   7393  H  HB   . ILE B 1 183 ? 16.081  -31.125 4.941   1.00 21.03  ? 201 ILE B HB   1 
ATOM   7394  H  HG12 . ILE B 1 183 ? 14.530  -28.758 4.868   1.00 20.73  ? 201 ILE B HG12 1 
ATOM   7395  H  HG13 . ILE B 1 183 ? 14.508  -29.728 6.128   1.00 20.73  ? 201 ILE B HG13 1 
ATOM   7396  H  HG21 . ILE B 1 183 ? 16.750  -29.449 3.416   1.00 21.41  ? 201 ILE B HG21 1 
ATOM   7397  H  HG22 . ILE B 1 183 ? 16.417  -30.839 2.723   1.00 21.41  ? 201 ILE B HG22 1 
ATOM   7398  H  HG23 . ILE B 1 183 ? 15.364  -29.650 2.667   1.00 21.41  ? 201 ILE B HG23 1 
ATOM   7399  H  HD11 . ILE B 1 183 ? 16.828  -29.284 6.399   1.00 22.22  ? 201 ILE B HD11 1 
ATOM   7400  H  HD12 . ILE B 1 183 ? 16.685  -28.166 5.280   1.00 22.22  ? 201 ILE B HD12 1 
ATOM   7401  H  HD13 . ILE B 1 183 ? 15.900  -28.020 6.654   1.00 22.22  ? 201 ILE B HD13 1 
ATOM   7402  N  N    . VAL B 1 184 ? 15.071  -33.641 3.700   1.00 17.39  ? 202 VAL B N    1 
ATOM   7403  C  CA   . VAL B 1 184 ? 15.153  -34.894 2.958   1.00 17.65  ? 202 VAL B CA   1 
ATOM   7404  C  C    . VAL B 1 184 ? 14.330  -35.914 3.738   1.00 17.85  ? 202 VAL B C    1 
ATOM   7405  O  O    . VAL B 1 184 ? 13.970  -35.659 4.901   1.00 17.23  ? 202 VAL B O    1 
ATOM   7406  C  CB   . VAL B 1 184 ? 16.610  -35.352 2.784   1.00 18.02  ? 202 VAL B CB   1 
ATOM   7407  C  CG1  . VAL B 1 184 ? 17.436  -34.253 2.133   1.00 19.23  ? 202 VAL B CG1  1 
ATOM   7408  C  CG2  . VAL B 1 184 ? 17.217  -35.801 4.112   1.00 18.65  ? 202 VAL B CG2  1 
ATOM   7409  H  H    . VAL B 1 184 ? 15.451  -33.678 4.470   1.00 20.86  ? 202 VAL B H    1 
ATOM   7410  H  HA   . VAL B 1 184 ? 14.783  -34.788 2.068   1.00 21.18  ? 202 VAL B HA   1 
ATOM   7411  H  HB   . VAL B 1 184 ? 16.625  -36.123 2.195   1.00 21.62  ? 202 VAL B HB   1 
ATOM   7412  H  HG11 . VAL B 1 184 ? 18.314  -34.604 1.918   1.00 23.07  ? 202 VAL B HG11 1 
ATOM   7413  H  HG12 . VAL B 1 184 ? 16.989  -33.960 1.323   1.00 23.07  ? 202 VAL B HG12 1 
ATOM   7414  H  HG13 . VAL B 1 184 ? 17.518  -33.511 2.752   1.00 23.07  ? 202 VAL B HG13 1 
ATOM   7415  H  HG21 . VAL B 1 184 ? 18.173  -35.922 3.997   1.00 22.38  ? 202 VAL B HG21 1 
ATOM   7416  H  HG22 . VAL B 1 184 ? 17.048  -35.121 4.783   1.00 22.38  ? 202 VAL B HG22 1 
ATOM   7417  H  HG23 . VAL B 1 184 ? 16.808  -36.639 4.379   1.00 22.38  ? 202 VAL B HG23 1 
ATOM   7418  N  N    . PRO B 1 185 ? 14.005  -37.074 3.151   1.00 17.79  ? 203 PRO B N    1 
ATOM   7419  C  CA   . PRO B 1 185 ? 13.277  -38.104 3.908   1.00 17.81  ? 203 PRO B CA   1 
ATOM   7420  C  C    . PRO B 1 185 ? 14.001  -38.444 5.199   1.00 17.62  ? 203 PRO B C    1 
ATOM   7421  O  O    . PRO B 1 185 ? 15.164  -38.852 5.180   1.00 17.14  ? 203 PRO B O    1 
ATOM   7422  C  CB   . PRO B 1 185 ? 13.231  -39.292 2.937   1.00 18.32  ? 203 PRO B CB   1 
ATOM   7423  C  CG   . PRO B 1 185 ? 13.325  -38.649 1.571   1.00 18.47  ? 203 PRO B CG   1 
ATOM   7424  C  CD   . PRO B 1 185 ? 14.261  -37.483 1.759   1.00 18.53  ? 203 PRO B CD   1 
ATOM   7425  H  HA   . PRO B 1 185 ? 12.367  -37.831 4.100   1.00 21.37  ? 203 PRO B HA   1 
ATOM   7426  H  HB2  . PRO B 1 185 ? 13.981  -39.886 3.098   1.00 21.99  ? 203 PRO B HB2  1 
ATOM   7427  H  HB3  . PRO B 1 185 ? 12.397  -39.777 3.040   1.00 21.99  ? 203 PRO B HB3  1 
ATOM   7428  H  HG2  . PRO B 1 185 ? 13.684  -39.283 0.931   1.00 22.16  ? 203 PRO B HG2  1 
ATOM   7429  H  HG3  . PRO B 1 185 ? 12.448  -38.349 1.286   1.00 22.16  ? 203 PRO B HG3  1 
ATOM   7430  H  HD2  . PRO B 1 185 ? 15.184  -37.757 1.642   1.00 22.24  ? 203 PRO B HD2  1 
ATOM   7431  H  HD3  . PRO B 1 185 ? 14.048  -36.765 1.142   1.00 22.24  ? 203 PRO B HD3  1 
ATOM   7432  N  N    . THR B 1 186 ? 13.329  -38.253 6.327   1.00 17.02  ? 204 THR B N    1 
ATOM   7433  C  CA   . THR B 1 186 ? 13.956  -38.365 7.631   1.00 17.53  ? 204 THR B CA   1 
ATOM   7434  C  C    . THR B 1 186 ? 13.136  -39.275 8.524   1.00 17.55  ? 204 THR B C    1 
ATOM   7435  O  O    . THR B 1 186 ? 11.904  -39.228 8.511   1.00 18.79  ? 204 THR B O    1 
ATOM   7436  C  CB   . THR B 1 186 ? 14.067  -36.978 8.277   1.00 17.30  ? 204 THR B CB   1 
ATOM   7437  O  OG1  . THR B 1 186 ? 14.888  -36.146 7.451   1.00 17.68  ? 204 THR B OG1  1 
ATOM   7438  C  CG2  . THR B 1 186 ? 14.666  -37.075 9.683   1.00 17.05  ? 204 THR B CG2  1 
ATOM   7439  H  H    . THR B 1 186 ? 12.492  -38.054 6.360   1.00 20.43  ? 204 THR B H    1 
ATOM   7440  H  HA   . THR B 1 186 ? 14.840  -38.755 7.542   1.00 21.03  ? 204 THR B HA   1 
ATOM   7441  H  HB   . THR B 1 186 ? 13.185  -36.583 8.364   1.00 20.76  ? 204 THR B HB   1 
ATOM   7442  H  HG1  . THR B 1 186 ? 14.596  -36.146 6.663   1.00 21.22  ? 204 THR B HG1  1 
ATOM   7443  H  HG21 . THR B 1 186 ? 14.970  -36.201 9.975   1.00 20.46  ? 204 THR B HG21 1 
ATOM   7444  H  HG22 . THR B 1 186 ? 13.998  -37.401 10.306  1.00 20.46  ? 204 THR B HG22 1 
ATOM   7445  H  HG23 . THR B 1 186 ? 15.420  -37.686 9.681   1.00 20.46  ? 204 THR B HG23 1 
ATOM   7446  N  N    . THR B 1 187 ? 13.836  -40.100 9.300   1.00 17.02  ? 205 THR B N    1 
ATOM   7447  C  CA   . THR B 1 187 ? 13.246  -40.893 10.364  1.00 17.71  ? 205 THR B CA   1 
ATOM   7448  C  C    . THR B 1 187 ? 13.908  -40.462 11.658  1.00 17.61  ? 205 THR B C    1 
ATOM   7449  O  O    . THR B 1 187 ? 15.133  -40.341 11.711  1.00 18.00  ? 205 THR B O    1 
ATOM   7450  C  CB   . THR B 1 187 ? 13.509  -42.381 10.146  1.00 18.30  ? 205 THR B CB   1 
ATOM   7451  O  OG1  . THR B 1 187 ? 13.021  -42.766 8.857   1.00 18.30  ? 205 THR B OG1  1 
ATOM   7452  C  CG2  . THR B 1 187 ? 12.815  -43.223 11.214  1.00 19.80  ? 205 THR B CG2  1 
ATOM   7453  H  H    . THR B 1 187 ? 14.684  -40.218 9.223   1.00 20.43  ? 205 THR B H    1 
ATOM   7454  H  HA   . THR B 1 187 ? 12.288  -40.751 10.405  1.00 21.26  ? 205 THR B HA   1 
ATOM   7455  H  HB   . THR B 1 187 ? 14.463  -42.548 10.202  1.00 21.96  ? 205 THR B HB   1 
ATOM   7456  H  HG1  . THR B 1 187 ? 12.205  -42.576 8.791   1.00 21.96  ? 205 THR B HG1  1 
ATOM   7457  H  HG21 . THR B 1 187 ? 13.167  -43.002 12.091  1.00 23.76  ? 205 THR B HG21 1 
ATOM   7458  H  HG22 . THR B 1 187 ? 11.861  -43.049 11.205  1.00 23.76  ? 205 THR B HG22 1 
ATOM   7459  H  HG23 . THR B 1 187 ? 12.966  -44.166 11.043  1.00 23.76  ? 205 THR B HG23 1 
ATOM   7460  N  N    . ASN B 1 188 ? 13.099  -40.244 12.691  1.00 16.92  ? 206 ASN B N    1 
ATOM   7461  C  CA   . ASN B 1 188 ? 13.570  -39.857 14.015  1.00 15.98  ? 206 ASN B CA   1 
ATOM   7462  C  C    . ASN B 1 188 ? 13.116  -40.924 15.001  1.00 17.78  ? 206 ASN B C    1 
ATOM   7463  O  O    . ASN B 1 188 ? 11.915  -41.069 15.247  1.00 20.05  ? 206 ASN B O    1 
ATOM   7464  C  CB   . ASN B 1 188 ? 12.986  -38.504 14.409  1.00 16.30  ? 206 ASN B CB   1 
ATOM   7465  C  CG   . ASN B 1 188 ? 13.374  -37.409 13.461  1.00 16.86  ? 206 ASN B CG   1 
ATOM   7466  O  OD1  . ASN B 1 188 ? 14.556  -37.167 13.233  1.00 17.04  ? 206 ASN B OD1  1 
ATOM   7467  N  ND2  . ASN B 1 188 ? 12.379  -36.733 12.900  1.00 17.80  ? 206 ASN B ND2  1 
ATOM   7468  H  H    . ASN B 1 188 ? 12.243  -40.316 12.647  1.00 20.31  ? 206 ASN B H    1 
ATOM   7469  H  HA   . ASN B 1 188 ? 14.539  -39.807 14.018  1.00 19.18  ? 206 ASN B HA   1 
ATOM   7470  H  HB2  . ASN B 1 188 ? 12.018  -38.567 14.415  1.00 19.57  ? 206 ASN B HB2  1 
ATOM   7471  H  HB3  . ASN B 1 188 ? 13.308  -38.265 15.292  1.00 19.57  ? 206 ASN B HB3  1 
ATOM   7472  H  HD21 . ASN B 1 188 ? 12.550  -36.095 12.349  1.00 21.36  ? 206 ASN B HD21 1 
ATOM   7473  H  HD22 . ASN B 1 188 ? 11.564  -36.932 13.087  1.00 21.36  ? 206 ASN B HD22 1 
ATOM   7474  N  N    A LEU B 1 189 ? 14.072  -41.639 15.589  0.81 17.04  ? 207 LEU B N    1 
ATOM   7475  N  N    B LEU B 1 189 ? 14.066  -41.666 15.559  0.19 18.20  ? 207 LEU B N    1 
ATOM   7476  C  CA   A LEU B 1 189 ? 13.796  -42.664 16.592  0.81 16.94  ? 207 LEU B CA   1 
ATOM   7477  C  CA   B LEU B 1 189 ? 13.777  -42.654 16.588  0.19 18.63  ? 207 LEU B CA   1 
ATOM   7478  C  C    A LEU B 1 189 ? 14.195  -42.110 17.952  0.81 17.38  ? 207 LEU B C    1 
ATOM   7479  C  C    B LEU B 1 189 ? 14.184  -42.086 17.940  0.19 18.49  ? 207 LEU B C    1 
ATOM   7480  O  O    A LEU B 1 189 ? 15.349  -41.711 18.147  0.81 17.92  ? 207 LEU B O    1 
ATOM   7481  O  O    B LEU B 1 189 ? 15.328  -41.653 18.116  0.19 18.55  ? 207 LEU B O    1 
ATOM   7482  C  CB   A LEU B 1 189 ? 14.578  -43.945 16.293  0.81 18.12  ? 207 LEU B CB   1 
ATOM   7483  C  CB   B LEU B 1 189 ? 14.535  -43.955 16.331  0.19 19.55  ? 207 LEU B CB   1 
ATOM   7484  C  CG   A LEU B 1 189 ? 14.341  -45.190 17.158  0.81 19.83  ? 207 LEU B CG   1 
ATOM   7485  C  CG   B LEU B 1 189 ? 14.207  -45.077 17.318  0.19 20.58  ? 207 LEU B CG   1 
ATOM   7486  C  CD1  A LEU B 1 189 ? 14.913  -45.035 18.559  0.81 19.52  ? 207 LEU B CD1  1 
ATOM   7487  C  CD1  B LEU B 1 189 ? 13.062  -45.932 16.794  0.19 21.11  ? 207 LEU B CD1  1 
ATOM   7488  C  CD2  A LEU B 1 189 ? 12.849  -45.541 17.217  0.81 21.31  ? 207 LEU B CD2  1 
ATOM   7489  C  CD2  B LEU B 1 189 ? 15.434  -45.921 17.587  0.19 20.95  ? 207 LEU B CD2  1 
ATOM   7490  H  H    A LEU B 1 189 ? 14.910  -41.546 15.419  0.81 20.45  ? 207 LEU B H    1 
ATOM   7491  H  H    B LEU B 1 189 ? 14.899  -41.613 15.354  0.19 21.84  ? 207 LEU B H    1 
ATOM   7492  H  HA   A LEU B 1 189 ? 12.850  -42.877 16.597  0.81 20.32  ? 207 LEU B HA   1 
ATOM   7493  H  HA   B LEU B 1 189 ? 12.827  -42.852 16.593  0.19 22.36  ? 207 LEU B HA   1 
ATOM   7494  H  HB2  A LEU B 1 189 ? 14.371  -44.203 15.381  0.81 21.75  ? 207 LEU B HB2  1 
ATOM   7495  H  HB2  B LEU B 1 189 ? 14.315  -44.270 15.441  0.19 23.46  ? 207 LEU B HB2  1 
ATOM   7496  H  HB3  A LEU B 1 189 ? 15.521  -43.733 16.373  0.81 21.75  ? 207 LEU B HB3  1 
ATOM   7497  H  HB3  B LEU B 1 189 ? 15.487  -43.776 16.393  0.19 23.46  ? 207 LEU B HB3  1 
ATOM   7498  H  HG   A LEU B 1 189 ? 14.812  -45.930 16.741  0.81 23.79  ? 207 LEU B HG   1 
ATOM   7499  H  HG   B LEU B 1 189 ? 13.923  -44.686 18.159  0.19 24.69  ? 207 LEU B HG   1 
ATOM   7500  H  HD11 A LEU B 1 189 ? 14.271  -44.561 19.111  0.81 23.43  ? 207 LEU B HD11 1 
ATOM   7501  H  HD11 B LEU B 1 189 ? 12.304  -45.360 16.598  0.19 25.33  ? 207 LEU B HD11 1 
ATOM   7502  H  HD12 A LEU B 1 189 ? 15.082  -45.915 18.930  0.81 23.43  ? 207 LEU B HD12 1 
ATOM   7503  H  HD12 B LEU B 1 189 ? 13.350  -46.387 15.987  0.19 25.33  ? 207 LEU B HD12 1 
ATOM   7504  H  HD13 A LEU B 1 189 ? 15.741  -44.532 18.509  0.81 23.43  ? 207 LEU B HD13 1 
ATOM   7505  H  HD13 B LEU B 1 189 ? 12.818  -46.583 17.471  0.19 25.33  ? 207 LEU B HD13 1 
ATOM   7506  H  HD21 A LEU B 1 189 ? 12.375  -44.827 17.673  0.81 25.57  ? 207 LEU B HD21 1 
ATOM   7507  H  HD21 B LEU B 1 189 ? 16.104  -45.375 18.027  0.19 25.14  ? 207 LEU B HD21 1 
ATOM   7508  H  HD22 A LEU B 1 189 ? 12.511  -45.637 16.313  0.81 25.57  ? 207 LEU B HD22 1 
ATOM   7509  H  HD22 B LEU B 1 189 ? 15.187  -46.665 18.159  0.19 25.14  ? 207 LEU B HD22 1 
ATOM   7510  H  HD23 A LEU B 1 189 ? 12.739  -46.373 17.703  0.81 25.57  ? 207 LEU B HD23 1 
ATOM   7511  H  HD23 B LEU B 1 189 ? 15.781  -46.253 16.744  0.19 25.14  ? 207 LEU B HD23 1 
ATOM   7512  N  N    . TYR B 1 190 ? 13.250  -42.086 18.887  1.00 18.50  ? 208 TYR B N    1 
ATOM   7513  C  CA   . TYR B 1 190 ? 13.506  -41.497 20.188  1.00 17.86  ? 208 TYR B CA   1 
ATOM   7514  C  C    . TYR B 1 190 ? 12.669  -42.160 21.269  1.00 19.15  ? 208 TYR B C    1 
ATOM   7515  O  O    . TYR B 1 190 ? 11.836  -43.026 20.999  1.00 19.48  ? 208 TYR B O    1 
ATOM   7516  C  CB   . TYR B 1 190 ? 13.273  -39.990 20.151  1.00 18.34  ? 208 TYR B CB   1 
ATOM   7517  C  CG   . TYR B 1 190 ? 11.855  -39.525 19.883  1.00 19.35  ? 208 TYR B CG   1 
ATOM   7518  C  CD1  . TYR B 1 190 ? 11.333  -39.502 18.594  1.00 19.74  ? 208 TYR B CD1  1 
ATOM   7519  C  CD2  . TYR B 1 190 ? 11.063  -39.038 20.912  1.00 20.42  ? 208 TYR B CD2  1 
ATOM   7520  C  CE1  . TYR B 1 190 ? 10.056  -39.022 18.347  1.00 20.71  ? 208 TYR B CE1  1 
ATOM   7521  C  CE2  . TYR B 1 190 ? 9.787   -38.559 20.671  1.00 20.48  ? 208 TYR B CE2  1 
ATOM   7522  C  CZ   . TYR B 1 190 ? 9.290   -38.554 19.391  1.00 20.54  ? 208 TYR B CZ   1 
ATOM   7523  O  OH   . TYR B 1 190 ? 8.026   -38.064 19.155  1.00 22.51  ? 208 TYR B OH   1 
ATOM   7524  H  H    . TYR B 1 190 ? 12.457  -42.404 18.789  1.00 22.19  ? 208 TYR B H    1 
ATOM   7525  H  HA   . TYR B 1 190 ? 14.432  -41.679 20.411  1.00 21.43  ? 208 TYR B HA   1 
ATOM   7526  H  HB2  . TYR B 1 190 ? 13.533  -39.625 21.011  1.00 22.01  ? 208 TYR B HB2  1 
ATOM   7527  H  HB3  . TYR B 1 190 ? 13.831  -39.617 19.450  1.00 22.01  ? 208 TYR B HB3  1 
ATOM   7528  H  HD1  . TYR B 1 190 ? 11.850  -39.813 17.886  1.00 23.69  ? 208 TYR B HD1  1 
ATOM   7529  H  HD2  . TYR B 1 190 ? 11.396  -39.033 21.781  1.00 24.50  ? 208 TYR B HD2  1 
ATOM   7530  H  HE1  . TYR B 1 190 ? 9.719   -39.016 17.481  1.00 24.85  ? 208 TYR B HE1  1 
ATOM   7531  H  HE2  . TYR B 1 190 ? 9.268   -38.240 21.374  1.00 24.58  ? 208 TYR B HE2  1 
ATOM   7532  H  HH   . TYR B 1 190 ? 7.929   -37.902 18.337  1.00 27.01  ? 208 TYR B HH   1 
ATOM   7533  N  N    . SER B 1 191 ? 12.904  -41.733 22.510  1.00 18.27  ? 209 SER B N    1 
ATOM   7534  C  CA   . SER B 1 191 ? 12.355  -42.405 23.676  1.00 20.21  ? 209 SER B CA   1 
ATOM   7535  C  C    . SER B 1 191 ? 11.818  -41.405 24.688  1.00 20.64  ? 209 SER B C    1 
ATOM   7536  O  O    . SER B 1 191 ? 12.495  -40.427 25.026  1.00 21.28  ? 209 SER B O    1 
ATOM   7537  C  CB   . SER B 1 191 ? 13.439  -43.250 24.350  1.00 21.24  ? 209 SER B CB   1 
ATOM   7538  O  OG   . SER B 1 191 ? 12.920  -43.851 25.515  1.00 22.35  ? 209 SER B OG   1 
ATOM   7539  H  H    . SER B 1 191 ? 13.386  -41.046 22.700  1.00 21.92  ? 209 SER B H    1 
ATOM   7540  H  HA   . SER B 1 191 ? 11.611  -42.958 23.389  1.00 24.26  ? 209 SER B HA   1 
ATOM   7541  H  HB2  . SER B 1 191 ? 13.732  -43.942 23.737  1.00 25.48  ? 209 SER B HB2  1 
ATOM   7542  H  HB3  . SER B 1 191 ? 14.186  -42.680 24.590  1.00 25.48  ? 209 SER B HB3  1 
ATOM   7543  H  HG   . SER B 1 191 ? 13.529  -44.263 25.921  1.00 26.82  ? 209 SER B HG   1 
ATOM   7544  N  N    . ALA B 1 192 ? 10.608  -41.681 25.187  1.00 20.82  ? 210 ALA B N    1 
ATOM   7545  C  CA   . ALA B 1 192 ? 10.024  -40.861 26.242  1.00 21.00  ? 210 ALA B CA   1 
ATOM   7546  C  C    . ALA B 1 192 ? 10.874  -40.870 27.505  1.00 20.83  ? 210 ALA B C    1 
ATOM   7547  O  O    . ALA B 1 192 ? 10.803  -39.928 28.303  1.00 21.15  ? 210 ALA B O    1 
ATOM   7548  C  CB   . ALA B 1 192 ? 8.618   -41.369 26.570  1.00 21.52  ? 210 ALA B CB   1 
ATOM   7549  H  H    . ALA B 1 192 ? 10.110  -42.334 24.932  1.00 24.98  ? 210 ALA B H    1 
ATOM   7550  H  HA   . ALA B 1 192 ? 9.964   -39.947 25.924  1.00 25.20  ? 210 ALA B HA   1 
ATOM   7551  H  HB1  . ALA B 1 192 ? 8.674   -42.295 26.855  1.00 25.82  ? 210 ALA B HB1  1 
ATOM   7552  H  HB2  . ALA B 1 192 ? 8.244   -40.827 27.282  1.00 25.82  ? 210 ALA B HB2  1 
ATOM   7553  H  HB3  . ALA B 1 192 ? 8.064   -41.300 25.777  1.00 25.82  ? 210 ALA B HB3  1 
ATOM   7554  N  N    . THR B 1 193 ? 11.667  -41.918 27.717  1.00 21.47  ? 211 THR B N    1 
ATOM   7555  C  CA   . THR B 1 193 ? 12.478  -42.037 28.922  1.00 22.17  ? 211 THR B CA   1 
ATOM   7556  C  C    . THR B 1 193 ? 13.901  -41.532 28.730  1.00 21.33  ? 211 THR B C    1 
ATOM   7557  O  O    . THR B 1 193 ? 14.764  -41.802 29.574  1.00 23.11  ? 211 THR B O    1 
ATOM   7558  C  CB   . THR B 1 193 ? 12.480  -43.477 29.443  1.00 22.58  ? 211 THR B CB   1 
ATOM   7559  O  OG1  . THR B 1 193 ? 13.049  -44.363 28.473  1.00 23.77  ? 211 THR B OG1  1 
ATOM   7560  C  CG2  . THR B 1 193 ? 11.066  -43.910 29.753  1.00 23.15  ? 211 THR B CG2  1 
ATOM   7561  H  H    . THR B 1 193 ? 11.752  -42.578 27.171  1.00 25.76  ? 211 THR B H    1 
ATOM   7562  H  HA   . THR B 1 193 ? 12.068  -41.492 29.611  1.00 26.60  ? 211 THR B HA   1 
ATOM   7563  H  HB   . THR B 1 193 ? 13.013  -43.526 30.252  1.00 27.10  ? 211 THR B HB   1 
ATOM   7564  H  HG1  . THR B 1 193 ? 13.860  -44.177 28.355  1.00 28.52  ? 211 THR B HG1  1 
ATOM   7565  H  HG21 . THR B 1 193 ? 10.619  -43.229 30.278  1.00 27.79  ? 211 THR B HG21 1 
ATOM   7566  H  HG22 . THR B 1 193 ? 10.573  -44.047 28.929  1.00 27.79  ? 211 THR B HG22 1 
ATOM   7567  H  HG23 . THR B 1 193 ? 11.076  -44.739 30.256  1.00 27.79  ? 211 THR B HG23 1 
ATOM   7568  N  N    . ASP B 1 194 ? 14.160  -40.797 27.651  1.00 20.23  ? 212 ASP B N    1 
ATOM   7569  C  CA   . ASP B 1 194 ? 15.451  -40.149 27.450  1.00 20.03  ? 212 ASP B CA   1 
ATOM   7570  C  C    . ASP B 1 194 ? 15.800  -39.284 28.656  1.00 20.29  ? 212 ASP B C    1 
ATOM   7571  O  O    . ASP B 1 194 ? 15.025  -38.406 29.051  1.00 20.95  ? 212 ASP B O    1 
ATOM   7572  C  CB   . ASP B 1 194 ? 15.362  -39.302 26.177  1.00 19.85  ? 212 ASP B CB   1 
ATOM   7573  C  CG   . ASP B 1 194 ? 16.720  -38.902 25.632  1.00 18.58  ? 212 ASP B CG   1 
ATOM   7574  O  OD1  . ASP B 1 194 ? 17.594  -38.504 26.431  1.00 18.21  ? 212 ASP B OD1  1 
ATOM   7575  O  OD2  . ASP B 1 194 ? 16.908  -38.959 24.392  1.00 19.61  ? 212 ASP B OD2  1 
ATOM   7576  H  H    . ASP B 1 194 ? 13.599  -40.658 27.014  1.00 24.28  ? 212 ASP B H    1 
ATOM   7577  H  HA   . ASP B 1 194 ? 16.156  -40.807 27.343  1.00 24.03  ? 212 ASP B HA   1 
ATOM   7578  H  HB2  . ASP B 1 194 ? 14.903  -39.811 25.491  1.00 23.82  ? 212 ASP B HB2  1 
ATOM   7579  H  HB3  . ASP B 1 194 ? 14.868  -38.490 26.373  1.00 23.82  ? 212 ASP B HB3  1 
ATOM   7580  N  N    . GLU B 1 195 ? 16.969  -39.534 29.244  1.00 19.71  ? 213 GLU B N    1 
ATOM   7581  C  CA   . GLU B 1 195 ? 17.408  -38.828 30.441  1.00 20.28  ? 213 GLU B CA   1 
ATOM   7582  C  C    . GLU B 1 195 ? 18.270  -37.609 30.132  1.00 20.04  ? 213 GLU B C    1 
ATOM   7583  O  O    . GLU B 1 195 ? 18.680  -36.908 31.068  1.00 20.39  ? 213 GLU B O    1 
ATOM   7584  C  CB   . GLU B 1 195 ? 18.136  -39.797 31.393  1.00 20.06  ? 213 GLU B CB   1 
ATOM   7585  C  CG   . GLU B 1 195 ? 19.644  -39.944 31.198  1.00 21.50  ? 213 GLU B CG   1 
ATOM   7586  C  CD   . GLU B 1 195 ? 20.026  -40.810 30.012  1.00 23.25  ? 213 GLU B CD   1 
ATOM   7587  O  OE1  . GLU B 1 195 ? 19.176  -41.042 29.122  1.00 22.82  ? 213 GLU B OE1  1 
ATOM   7588  O  OE2  . GLU B 1 195 ? 21.192  -41.255 29.970  1.00 24.97  ? 213 GLU B OE2  1 
ATOM   7589  H  H    . GLU B 1 195 ? 17.534  -40.117 28.961  1.00 23.65  ? 213 GLU B H    1 
ATOM   7590  H  HA   . GLU B 1 195 ? 16.629  -38.503 30.919  1.00 24.33  ? 213 GLU B HA   1 
ATOM   7591  H  HB2  . GLU B 1 195 ? 17.996  -39.488 32.302  1.00 24.08  ? 213 GLU B HB2  1 
ATOM   7592  H  HB3  . GLU B 1 195 ? 17.748  -40.679 31.280  1.00 24.08  ? 213 GLU B HB3  1 
ATOM   7593  H  HG2  . GLU B 1 195 ? 20.028  -39.065 31.058  1.00 25.80  ? 213 GLU B HG2  1 
ATOM   7594  H  HG3  . GLU B 1 195 ? 20.024  -40.349 31.993  1.00 25.80  ? 213 GLU B HG3  1 
ATOM   7595  N  N    . ILE B 1 196 ? 18.539  -37.337 28.853  1.00 19.83  ? 214 ILE B N    1 
ATOM   7596  C  CA   . ILE B 1 196 ? 19.350  -36.204 28.420  1.00 18.75  ? 214 ILE B CA   1 
ATOM   7597  C  C    . ILE B 1 196 ? 18.500  -35.170 27.696  1.00 17.94  ? 214 ILE B C    1 
ATOM   7598  O  O    . ILE B 1 196 ? 18.615  -33.966 27.947  1.00 17.78  ? 214 ILE B O    1 
ATOM   7599  C  CB   . ILE B 1 196 ? 20.519  -36.677 27.523  1.00 20.29  ? 214 ILE B CB   1 
ATOM   7600  C  CG1  . ILE B 1 196 ? 21.399  -37.691 28.257  1.00 21.64  ? 214 ILE B CG1  1 
ATOM   7601  C  CG2  . ILE B 1 196 ? 21.351  -35.494 27.023  1.00 19.15  ? 214 ILE B CG2  1 
ATOM   7602  C  CD1  . ILE B 1 196 ? 21.994  -37.185 29.534  1.00 23.73  ? 214 ILE B CD1  1 
ATOM   7603  H  H    . ILE B 1 196 ? 18.250  -37.813 28.197  1.00 23.80  ? 214 ILE B H    1 
ATOM   7604  H  HA   . ILE B 1 196 ? 19.730  -35.780 29.205  1.00 22.50  ? 214 ILE B HA   1 
ATOM   7605  H  HB   . ILE B 1 196 ? 20.132  -37.116 26.750  1.00 24.35  ? 214 ILE B HB   1 
ATOM   7606  H  HG12 . ILE B 1 196 ? 20.861  -38.469 28.473  1.00 25.96  ? 214 ILE B HG12 1 
ATOM   7607  H  HG13 . ILE B 1 196 ? 22.131  -37.946 27.673  1.00 25.96  ? 214 ILE B HG13 1 
ATOM   7608  H  HG21 . ILE B 1 196 ? 20.837  -35.002 26.364  1.00 22.98  ? 214 ILE B HG21 1 
ATOM   7609  H  HG22 . ILE B 1 196 ? 21.564  -34.918 27.774  1.00 22.98  ? 214 ILE B HG22 1 
ATOM   7610  H  HG23 . ILE B 1 196 ? 22.168  -35.830 26.622  1.00 22.98  ? 214 ILE B HG23 1 
ATOM   7611  H  HD11 . ILE B 1 196 ? 22.640  -37.831 29.860  1.00 28.48  ? 214 ILE B HD11 1 
ATOM   7612  H  HD12 . ILE B 1 196 ? 22.432  -36.336 29.363  1.00 28.48  ? 214 ILE B HD12 1 
ATOM   7613  H  HD13 . ILE B 1 196 ? 21.287  -37.066 30.187  1.00 28.48  ? 214 ILE B HD13 1 
ATOM   7614  N  N    . VAL B 1 197 ? 17.649  -35.628 26.778  1.00 17.61  ? 215 VAL B N    1 
ATOM   7615  C  CA   . VAL B 1 197 ? 16.841  -34.772 25.912  1.00 16.44  ? 215 VAL B CA   1 
ATOM   7616  C  C    . VAL B 1 197 ? 15.381  -34.883 26.341  1.00 17.32  ? 215 VAL B C    1 
ATOM   7617  O  O    . VAL B 1 197 ? 14.797  -35.975 26.311  1.00 17.93  ? 215 VAL B O    1 
ATOM   7618  C  CB   . VAL B 1 197 ? 16.989  -35.168 24.431  1.00 15.75  ? 215 VAL B CB   1 
ATOM   7619  C  CG1  . VAL B 1 197 ? 16.019  -34.357 23.576  1.00 17.15  ? 215 VAL B CG1  1 
ATOM   7620  C  CG2  . VAL B 1 197 ? 18.421  -34.979 23.962  1.00 15.61  ? 215 VAL B CG2  1 
ATOM   7621  H  H    . VAL B 1 197 ? 17.518  -36.466 26.633  1.00 21.13  ? 215 VAL B H    1 
ATOM   7622  H  HA   . VAL B 1 197 ? 17.128  -33.853 26.029  1.00 19.73  ? 215 VAL B HA   1 
ATOM   7623  H  HB   . VAL B 1 197 ? 16.772  -36.107 24.330  1.00 18.90  ? 215 VAL B HB   1 
ATOM   7624  H  HG11 . VAL B 1 197 ? 15.876  -33.493 23.993  1.00 20.59  ? 215 VAL B HG11 1 
ATOM   7625  H  HG12 . VAL B 1 197 ? 16.401  -34.239 22.692  1.00 20.59  ? 215 VAL B HG12 1 
ATOM   7626  H  HG13 . VAL B 1 197 ? 15.178  -34.837 23.511  1.00 20.59  ? 215 VAL B HG13 1 
ATOM   7627  H  HG21 . VAL B 1 197 ? 18.464  -35.142 23.007  1.00 18.73  ? 215 VAL B HG21 1 
ATOM   7628  H  HG22 . VAL B 1 197 ? 18.699  -34.070 24.156  1.00 18.73  ? 215 VAL B HG22 1 
ATOM   7629  H  HG23 . VAL B 1 197 ? 18.992  -35.607 24.432  1.00 18.73  ? 215 VAL B HG23 1 
ATOM   7630  N  N    . GLN B 1 198 ? 14.792  -33.760 26.727  1.00 17.06  ? 216 GLN B N    1 
ATOM   7631  C  CA   . GLN B 1 198 ? 13.365  -33.660 26.996  1.00 17.66  ? 216 GLN B CA   1 
ATOM   7632  C  C    . GLN B 1 198 ? 12.889  -32.295 26.522  1.00 19.00  ? 216 GLN B C    1 
ATOM   7633  O  O    . GLN B 1 198 ? 13.691  -31.365 26.389  1.00 18.08  ? 216 GLN B O    1 
ATOM   7634  C  CB   . GLN B 1 198 ? 13.058  -33.830 28.491  1.00 18.70  ? 216 GLN B CB   1 
ATOM   7635  C  CG   . GLN B 1 198 ? 13.220  -35.258 28.989  1.00 19.69  ? 216 GLN B CG   1 
ATOM   7636  C  CD   . GLN B 1 198 ? 12.131  -36.193 28.481  1.00 19.50  ? 216 GLN B CD   1 
ATOM   7637  O  OE1  . GLN B 1 198 ? 10.994  -35.780 28.252  1.00 19.31  ? 216 GLN B OE1  1 
ATOM   7638  N  NE2  . GLN B 1 198 ? 12.480  -37.464 28.305  1.00 19.94  ? 216 GLN B NE2  1 
ATOM   7639  H  H    . GLN B 1 198 ? 15.211  -33.018 26.843  1.00 20.48  ? 216 GLN B H    1 
ATOM   7640  H  HA   . GLN B 1 198 ? 12.885  -34.348 26.509  1.00 21.19  ? 216 GLN B HA   1 
ATOM   7641  H  HB2  . GLN B 1 198 ? 13.663  -33.268 28.999  1.00 22.44  ? 216 GLN B HB2  1 
ATOM   7642  H  HB3  . GLN B 1 198 ? 12.140  -33.561 28.653  1.00 22.44  ? 216 GLN B HB3  1 
ATOM   7643  H  HG2  . GLN B 1 198 ? 14.075  -35.602 28.687  1.00 23.63  ? 216 GLN B HG2  1 
ATOM   7644  H  HG3  . GLN B 1 198 ? 13.186  -35.259 29.959  1.00 23.63  ? 216 GLN B HG3  1 
ATOM   7645  H  HE21 . GLN B 1 198 ? 13.283  -37.718 28.477  1.00 23.93  ? 216 GLN B HE21 1 
ATOM   7646  H  HE22 . GLN B 1 198 ? 11.901  -38.033 28.020  1.00 23.93  ? 216 GLN B HE22 1 
ATOM   7647  N  N    . PRO B 1 199 ? 11.583  -32.144 26.242  1.00 19.65  ? 217 PRO B N    1 
ATOM   7648  C  CA   . PRO B 1 199 ? 10.526  -33.152 26.376  1.00 19.76  ? 217 PRO B CA   1 
ATOM   7649  C  C    . PRO B 1 199 ? 10.454  -34.099 25.192  1.00 19.00  ? 217 PRO B C    1 
ATOM   7650  O  O    . PRO B 1 199 ? 10.634  -33.695 24.043  1.00 19.06  ? 217 PRO B O    1 
ATOM   7651  C  CB   . PRO B 1 199 ? 9.251   -32.307 26.447  1.00 20.83  ? 217 PRO B CB   1 
ATOM   7652  C  CG   . PRO B 1 199 ? 9.562   -31.119 25.600  1.00 20.68  ? 217 PRO B CG   1 
ATOM   7653  C  CD   . PRO B 1 199 ? 11.047  -30.849 25.775  1.00 20.45  ? 217 PRO B CD   1 
ATOM   7654  H  HA   . PRO B 1 199 ? 10.642  -33.661 27.193  1.00 23.71  ? 217 PRO B HA   1 
ATOM   7655  H  HB2  . PRO B 1 199 ? 8.499   -32.805 26.091  1.00 25.00  ? 217 PRO B HB2  1 
ATOM   7656  H  HB3  . PRO B 1 199 ? 9.073   -32.047 27.364  1.00 25.00  ? 217 PRO B HB3  1 
ATOM   7657  H  HG2  . PRO B 1 199 ? 9.357   -31.318 24.673  1.00 24.82  ? 217 PRO B HG2  1 
ATOM   7658  H  HG3  . PRO B 1 199 ? 9.038   -30.359 25.900  1.00 24.82  ? 217 PRO B HG3  1 
ATOM   7659  H  HD2  . PRO B 1 199 ? 11.452  -30.594 24.931  1.00 24.54  ? 217 PRO B HD2  1 
ATOM   7660  H  HD3  . PRO B 1 199 ? 11.195  -30.156 26.437  1.00 24.54  ? 217 PRO B HD3  1 
ATOM   7661  N  N    . GLN B 1 200 ? 10.181  -35.364 25.501  1.00 20.64  ? 218 GLN B N    1 
ATOM   7662  C  CA   . GLN B 1 200 ? 10.058  -36.414 24.501  1.00 19.56  ? 218 GLN B CA   1 
ATOM   7663  C  C    . GLN B 1 200 ? 8.864   -37.316 24.791  1.00 20.76  ? 218 GLN B C    1 
ATOM   7664  O  O    . GLN B 1 200 ? 8.745   -38.378 24.169  1.00 21.88  ? 218 GLN B O    1 
ATOM   7665  C  CB   . GLN B 1 200 ? 11.325  -37.281 24.489  1.00 19.21  ? 218 GLN B CB   1 
ATOM   7666  C  CG   . GLN B 1 200 ? 12.603  -36.549 24.139  1.00 18.95  ? 218 GLN B CG   1 
ATOM   7667  C  CD   . GLN B 1 200 ? 12.827  -36.481 22.648  1.00 18.72  ? 218 GLN B CD   1 
ATOM   7668  O  OE1  . GLN B 1 200 ? 12.045  -35.868 21.917  1.00 19.01  ? 218 GLN B OE1  1 
ATOM   7669  N  NE2  . GLN B 1 200 ? 13.895  -37.113 22.185  1.00 18.11  ? 218 GLN B NE2  1 
ATOM   7670  H  H    . GLN B 1 200 ? 10.060  -35.646 26.304  1.00 24.77  ? 218 GLN B H    1 
ATOM   7671  H  HA   . GLN B 1 200 ? 9.949   -36.011 23.625  1.00 23.47  ? 218 GLN B HA   1 
ATOM   7672  H  HB2  . GLN B 1 200 ? 11.443  -37.663 25.373  1.00 23.06  ? 218 GLN B HB2  1 
ATOM   7673  H  HB3  . GLN B 1 200 ? 11.207  -37.988 23.835  1.00 23.06  ? 218 GLN B HB3  1 
ATOM   7674  H  HG2  . GLN B 1 200 ? 12.554  -35.642 24.479  1.00 22.73  ? 218 GLN B HG2  1 
ATOM   7675  H  HG3  . GLN B 1 200 ? 13.356  -37.013 24.537  1.00 22.73  ? 218 GLN B HG3  1 
ATOM   7676  H  HE21 . GLN B 1 200 ? 14.416  -37.531 22.727  1.00 21.73  ? 218 GLN B HE21 1 
ATOM   7677  H  HE22 . GLN B 1 200 ? 14.068  -37.105 21.343  1.00 21.73  ? 218 GLN B HE22 1 
ATOM   7678  N  N    . VAL B 1 201 ? 7.979   -36.937 25.717  1.00 21.60  ? 219 VAL B N    1 
ATOM   7679  C  CA   . VAL B 1 201 ? 6.990   -37.881 26.236  1.00 22.94  ? 219 VAL B CA   1 
ATOM   7680  C  C    . VAL B 1 201 ? 5.661   -37.861 25.494  1.00 24.21  ? 219 VAL B C    1 
ATOM   7681  O  O    . VAL B 1 201 ? 4.866   -38.802 25.647  1.00 25.75  ? 219 VAL B O    1 
ATOM   7682  C  CB   . VAL B 1 201 ? 6.731   -37.623 27.736  1.00 23.67  ? 219 VAL B CB   1 
ATOM   7683  C  CG1  . VAL B 1 201 ? 8.003   -37.863 28.554  1.00 24.37  ? 219 VAL B CG1  1 
ATOM   7684  C  CG2  . VAL B 1 201 ? 6.211   -36.202 27.954  1.00 25.54  ? 219 VAL B CG2  1 
ATOM   7685  H  H    . VAL B 1 201 ? 7.932   -36.148 26.056  1.00 25.92  ? 219 VAL B H    1 
ATOM   7686  H  HA   . VAL B 1 201 ? 7.360   -38.770 26.120  1.00 27.53  ? 219 VAL B HA   1 
ATOM   7687  H  HB   . VAL B 1 201 ? 6.054   -38.244 28.046  1.00 28.41  ? 219 VAL B HB   1 
ATOM   7688  H  HG11 . VAL B 1 201 ? 8.715   -38.142 27.956  1.00 29.24  ? 219 VAL B HG11 1 
ATOM   7689  H  HG12 . VAL B 1 201 ? 8.252   -37.039 29.002  1.00 29.24  ? 219 VAL B HG12 1 
ATOM   7690  H  HG13 . VAL B 1 201 ? 7.831   -38.557 29.210  1.00 29.24  ? 219 VAL B HG13 1 
ATOM   7691  H  HG21 . VAL B 1 201 ? 5.982   -36.090 28.890  1.00 30.65  ? 219 VAL B HG21 1 
ATOM   7692  H  HG22 . VAL B 1 201 ? 6.904   -35.570 27.705  1.00 30.65  ? 219 VAL B HG22 1 
ATOM   7693  H  HG23 . VAL B 1 201 ? 5.425   -36.065 27.403  1.00 30.65  ? 219 VAL B HG23 1 
ATOM   7694  N  N    . SER B 1 202 ? 5.400   -36.845 24.680  1.00 24.13  ? 220 SER B N    1 
ATOM   7695  C  CA   . SER B 1 202 ? 4.058   -36.594 24.174  1.00 24.43  ? 220 SER B CA   1 
ATOM   7696  C  C    . SER B 1 202 ? 3.715   -37.363 22.904  1.00 24.54  ? 220 SER B C    1 
ATOM   7697  O  O    . SER B 1 202 ? 2.529   -37.449 22.561  1.00 25.03  ? 220 SER B O    1 
ATOM   7698  C  CB   . SER B 1 202 ? 3.878   -35.092 23.912  1.00 25.38  ? 220 SER B CB   1 
ATOM   7699  O  OG   . SER B 1 202 ? 4.555   -34.694 22.727  1.00 27.19  ? 220 SER B OG   1 
ATOM   7700  H  H    . SER B 1 202 ? 5.989   -36.282 24.405  1.00 28.95  ? 220 SER B H    1 
ATOM   7701  H  HA   . SER B 1 202 ? 3.426   -36.873 24.854  1.00 29.32  ? 220 SER B HA   1 
ATOM   7702  H  HB2  . SER B 1 202 ? 2.932   -34.902 23.813  1.00 30.46  ? 220 SER B HB2  1 
ATOM   7703  H  HB3  . SER B 1 202 ? 4.239   -34.596 24.663  1.00 30.46  ? 220 SER B HB3  1 
ATOM   7704  H  HG   . SER B 1 202 ? 5.371   -34.885 22.784  1.00 32.63  ? 220 SER B HG   1 
ATOM   7705  N  N    . ASN B 1 203 ? 4.698   -37.931 22.205  1.00 24.81  ? 221 ASN B N    1 
ATOM   7706  C  CA   . ASN B 1 203 ? 4.456   -38.530 20.892  1.00 25.31  ? 221 ASN B CA   1 
ATOM   7707  C  C    . ASN B 1 203 ? 3.699   -37.540 20.005  1.00 25.53  ? 221 ASN B C    1 
ATOM   7708  O  O    . ASN B 1 203 ? 2.653   -37.852 19.426  1.00 26.03  ? 221 ASN B O    1 
ATOM   7709  C  CB   . ASN B 1 203 ? 3.708   -39.862 21.018  1.00 26.09  ? 221 ASN B CB   1 
ATOM   7710  C  CG   . ASN B 1 203 ? 3.674   -40.645 19.711  1.00 25.84  ? 221 ASN B CG   1 
ATOM   7711  O  OD1  . ASN B 1 203 ? 4.599   -40.567 18.901  1.00 27.81  ? 221 ASN B OD1  1 
ATOM   7712  N  ND2  . ASN B 1 203 ? 2.605   -41.413 19.507  1.00 26.60  ? 221 ASN B ND2  1 
ATOM   7713  H  H    . ASN B 1 203 ? 5.515   -37.982 22.471  1.00 29.77  ? 221 ASN B H    1 
ATOM   7714  H  HA   . ASN B 1 203 ? 5.307   -38.725 20.470  1.00 30.37  ? 221 ASN B HA   1 
ATOM   7715  H  HB2  . ASN B 1 203 ? 4.150   -40.411 21.685  1.00 31.31  ? 221 ASN B HB2  1 
ATOM   7716  H  HB3  . ASN B 1 203 ? 2.793   -39.686 21.286  1.00 31.31  ? 221 ASN B HB3  1 
ATOM   7717  H  HD21 . ASN B 1 203 ? 2.539   -41.874 18.784  1.00 31.92  ? 221 ASN B HD21 1 
ATOM   7718  H  HD22 . ASN B 1 203 ? 1.981   -41.446 20.097  1.00 31.92  ? 221 ASN B HD22 1 
ATOM   7719  N  N    . SER B 1 204 ? 4.244   -36.328 19.919  1.00 24.28  ? 222 SER B N    1 
ATOM   7720  C  CA   . SER B 1 204 ? 3.556   -35.189 19.319  1.00 23.51  ? 222 SER B CA   1 
ATOM   7721  C  C    . SER B 1 204 ? 4.615   -34.195 18.850  1.00 21.98  ? 222 SER B C    1 
ATOM   7722  O  O    . SER B 1 204 ? 5.806   -34.364 19.135  1.00 21.72  ? 222 SER B O    1 
ATOM   7723  C  CB   . SER B 1 204 ? 2.603   -34.527 20.330  1.00 25.09  ? 222 SER B CB   1 
ATOM   7724  O  OG   . SER B 1 204 ? 3.242   -33.478 21.021  1.00 26.67  ? 222 SER B OG   1 
ATOM   7725  H  H    . SER B 1 204 ? 5.031   -36.136 20.208  1.00 29.14  ? 222 SER B H    1 
ATOM   7726  H  HA   . SER B 1 204 ? 3.043   -35.484 18.550  1.00 28.21  ? 222 SER B HA   1 
ATOM   7727  H  HB2  . SER B 1 204 ? 1.838   -34.168 19.853  1.00 30.10  ? 222 SER B HB2  1 
ATOM   7728  H  HB3  . SER B 1 204 ? 2.311   -35.194 20.971  1.00 30.10  ? 222 SER B HB3  1 
ATOM   7729  H  HG   . SER B 1 204 ? 2.750   -33.202 21.644  1.00 32.00  ? 222 SER B HG   1 
ATOM   7730  N  N    . PRO B 1 205 ? 4.204   -33.142 18.131  1.00 22.12  ? 223 PRO B N    1 
ATOM   7731  C  CA   . PRO B 1 205 ? 5.173   -32.111 17.712  1.00 22.43  ? 223 PRO B CA   1 
ATOM   7732  C  C    . PRO B 1 205 ? 5.851   -31.384 18.863  1.00 22.79  ? 223 PRO B C    1 
ATOM   7733  O  O    . PRO B 1 205 ? 6.784   -30.607 18.610  1.00 22.91  ? 223 PRO B O    1 
ATOM   7734  C  CB   . PRO B 1 205 ? 4.323   -31.146 16.869  1.00 22.92  ? 223 PRO B CB   1 
ATOM   7735  C  CG   . PRO B 1 205 ? 3.205   -31.987 16.362  1.00 23.51  ? 223 PRO B CG   1 
ATOM   7736  C  CD   . PRO B 1 205 ? 2.897   -32.961 17.472  1.00 22.92  ? 223 PRO B CD   1 
ATOM   7737  H  HA   . PRO B 1 205 ? 5.855   -32.515 17.152  1.00 26.92  ? 223 PRO B HA   1 
ATOM   7738  H  HB2  . PRO B 1 205 ? 3.993   -30.422 17.424  1.00 27.50  ? 223 PRO B HB2  1 
ATOM   7739  H  HB3  . PRO B 1 205 ? 4.851   -30.789 16.138  1.00 27.50  ? 223 PRO B HB3  1 
ATOM   7740  H  HG2  . PRO B 1 205 ? 2.435   -31.429 16.170  1.00 28.21  ? 223 PRO B HG2  1 
ATOM   7741  H  HG3  . PRO B 1 205 ? 3.483   -32.456 15.560  1.00 28.21  ? 223 PRO B HG3  1 
ATOM   7742  H  HD2  . PRO B 1 205 ? 2.248   -32.589 18.089  1.00 27.51  ? 223 PRO B HD2  1 
ATOM   7743  H  HD3  . PRO B 1 205 ? 2.571   -33.802 17.114  1.00 27.51  ? 223 PRO B HD3  1 
ATOM   7744  N  N    . LEU B 1 206 ? 5.407   -31.584 20.106  1.00 23.00  ? 224 LEU B N    1 
ATOM   7745  C  CA   . LEU B 1 206 ? 6.116   -31.017 21.244  1.00 22.46  ? 224 LEU B CA   1 
ATOM   7746  C  C    . LEU B 1 206 ? 7.491   -31.645 21.427  1.00 21.39  ? 224 LEU B C    1 
ATOM   7747  O  O    . LEU B 1 206 ? 8.375   -31.024 22.031  1.00 21.98  ? 224 LEU B O    1 
ATOM   7748  C  CB   . LEU B 1 206 ? 5.318   -31.242 22.531  1.00 22.08  ? 224 LEU B CB   1 
ATOM   7749  C  CG   . LEU B 1 206 ? 3.948   -30.578 22.669  1.00 24.34  ? 224 LEU B CG   1 
ATOM   7750  C  CD1  . LEU B 1 206 ? 3.274   -31.036 23.950  1.00 24.30  ? 224 LEU B CD1  1 
ATOM   7751  C  CD2  . LEU B 1 206 ? 4.077   -29.069 22.647  1.00 26.05  ? 224 LEU B CD2  1 
ATOM   7752  H  H    . LEU B 1 206 ? 4.706   -32.039 20.311  1.00 27.60  ? 224 LEU B H    1 
ATOM   7753  H  HA   . LEU B 1 206 ? 6.214   -30.064 21.094  1.00 26.96  ? 224 LEU B HA   1 
ATOM   7754  H  HB2  . LEU B 1 206 ? 5.173   -32.197 22.622  1.00 26.49  ? 224 LEU B HB2  1 
ATOM   7755  H  HB3  . LEU B 1 206 ? 5.858   -30.917 23.269  1.00 26.49  ? 224 LEU B HB3  1 
ATOM   7756  H  HG   . LEU B 1 206 ? 3.391   -30.838 21.918  1.00 29.21  ? 224 LEU B HG   1 
ATOM   7757  H  HD11 . LEU B 1 206 ? 3.312   -32.004 23.998  1.00 29.16  ? 224 LEU B HD11 1 
ATOM   7758  H  HD12 . LEU B 1 206 ? 3.739   -30.648 24.707  1.00 29.16  ? 224 LEU B HD12 1 
ATOM   7759  H  HD13 . LEU B 1 206 ? 2.350   -30.742 23.943  1.00 29.16  ? 224 LEU B HD13 1 
ATOM   7760  H  HD21 . LEU B 1 206 ? 4.212   -28.777 21.732  1.00 31.26  ? 224 LEU B HD21 1 
ATOM   7761  H  HD22 . LEU B 1 206 ? 3.263   -28.678 23.002  1.00 31.26  ? 224 LEU B HD22 1 
ATOM   7762  H  HD23 . LEU B 1 206 ? 4.835   -28.809 23.193  1.00 31.26  ? 224 LEU B HD23 1 
ATOM   7763  N  N    . ASP B 1 207 ? 7.689   -32.862 20.933  1.00 20.32  ? 225 ASP B N    1 
ATOM   7764  C  CA   . ASP B 1 207 ? 8.907   -33.598 21.249  1.00 18.91  ? 225 ASP B CA   1 
ATOM   7765  C  C    . ASP B 1 207 ? 10.110  -32.985 20.542  1.00 17.43  ? 225 ASP B C    1 
ATOM   7766  O  O    . ASP B 1 207 ? 10.023  -32.543 19.395  1.00 17.56  ? 225 ASP B O    1 
ATOM   7767  C  CB   . ASP B 1 207 ? 8.740   -35.063 20.853  1.00 20.14  ? 225 ASP B CB   1 
ATOM   7768  C  CG   . ASP B 1 207 ? 7.618   -35.741 21.617  1.00 21.52  ? 225 ASP B CG   1 
ATOM   7769  O  OD1  . ASP B 1 207 ? 7.229   -35.218 22.681  1.00 22.43  ? 225 ASP B OD1  1 
ATOM   7770  O  OD2  . ASP B 1 207 ? 7.120   -36.787 21.159  1.00 21.56  ? 225 ASP B OD2  1 
ATOM   7771  H  H    . ASP B 1 207 ? 7.141   -33.279 20.419  1.00 24.39  ? 225 ASP B H    1 
ATOM   7772  H  HA   . ASP B 1 207 ? 9.078   -33.557 22.203  1.00 22.69  ? 225 ASP B HA   1 
ATOM   7773  H  HB2  . ASP B 1 207 ? 8.536   -35.115 19.906  1.00 24.17  ? 225 ASP B HB2  1 
ATOM   7774  H  HB3  . ASP B 1 207 ? 9.564   -35.539 21.041  1.00 24.17  ? 225 ASP B HB3  1 
ATOM   7775  N  N    . SER B 1 208 ? 11.246  -32.967 21.241  1.00 16.74  ? 226 SER B N    1 
ATOM   7776  C  CA   . SER B 1 208 ? 12.449  -32.369 20.672  1.00 16.75  ? 226 SER B CA   1 
ATOM   7777  C  C    . SER B 1 208 ? 12.918  -33.102 19.417  1.00 16.23  ? 226 SER B C    1 
ATOM   7778  O  O    . SER B 1 208 ? 13.529  -32.483 18.540  1.00 16.47  ? 226 SER B O    1 
ATOM   7779  C  CB   . SER B 1 208 ? 13.554  -32.317 21.727  1.00 17.13  ? 226 SER B CB   1 
ATOM   7780  O  OG   . SER B 1 208 ? 14.685  -31.633 21.233  1.00 16.14  ? 226 SER B OG   1 
ATOM   7781  H  H    . SER B 1 208 ? 11.344  -33.288 22.032  1.00 20.09  ? 226 SER B H    1 
ATOM   7782  H  HA   . SER B 1 208 ? 12.250  -31.457 20.409  1.00 20.10  ? 226 SER B HA   1 
ATOM   7783  H  HB2  . SER B 1 208 ? 13.222  -31.853 22.511  1.00 20.56  ? 226 SER B HB2  1 
ATOM   7784  H  HB3  . SER B 1 208 ? 13.810  -33.223 21.961  1.00 20.56  ? 226 SER B HB3  1 
ATOM   7785  H  HG   . SER B 1 208 ? 15.299  -31.640 21.807  1.00 19.37  ? 226 SER B HG   1 
ATOM   7786  N  N    . SER B 1 209 ? 12.643  -34.407 19.299  1.00 17.85  ? 227 SER B N    1 
ATOM   7787  C  CA   . SER B 1 209 ? 13.084  -35.173 18.139  1.00 17.83  ? 227 SER B CA   1 
ATOM   7788  C  C    . SER B 1 209 ? 12.127  -35.097 16.949  1.00 17.35  ? 227 SER B C    1 
ATOM   7789  O  O    . SER B 1 209 ? 12.402  -35.723 15.921  1.00 18.01  ? 227 SER B O    1 
ATOM   7790  C  CB   . SER B 1 209 ? 13.277  -36.650 18.506  1.00 17.86  ? 227 SER B CB   1 
ATOM   7791  O  OG   . SER B 1 209 ? 14.280  -36.822 19.483  1.00 17.71  ? 227 SER B OG   1 
ATOM   7792  H  H    . SER B 1 209 ? 12.202  -34.865 19.879  1.00 21.43  ? 227 SER B H    1 
ATOM   7793  H  HA   . SER B 1 209 ? 13.939  -34.805 17.866  1.00 21.39  ? 227 SER B HA   1 
ATOM   7794  H  HB2  . SER B 1 209 ? 12.441  -36.997 18.853  1.00 21.43  ? 227 SER B HB2  1 
ATOM   7795  H  HB3  . SER B 1 209 ? 13.533  -37.138 17.707  1.00 21.43  ? 227 SER B HB3  1 
ATOM   7796  H  HG   . SER B 1 209 ? 15.014  -36.532 19.196  1.00 21.26  ? 227 SER B HG   1 
ATOM   7797  N  N    . TYR B 1 210 ? 11.023  -34.355 17.052  1.00 17.85  ? 228 TYR B N    1 
ATOM   7798  C  CA   . TYR B 1 210 ? 9.960   -34.407 16.051  1.00 18.92  ? 228 TYR B CA   1 
ATOM   7799  C  C    . TYR B 1 210 ? 10.244  -33.464 14.887  1.00 17.84  ? 228 TYR B C    1 
ATOM   7800  O  O    . TYR B 1 210 ? 10.655  -32.318 15.084  1.00 19.55  ? 228 TYR B O    1 
ATOM   7801  C  CB   . TYR B 1 210 ? 8.622   -34.027 16.696  1.00 21.61  ? 228 TYR B CB   1 
ATOM   7802  C  CG   . TYR B 1 210 ? 7.390   -34.289 15.855  1.00 23.85  ? 228 TYR B CG   1 
ATOM   7803  C  CD1  . TYR B 1 210 ? 7.038   -33.443 14.809  1.00 24.23  ? 228 TYR B CD1  1 
ATOM   7804  C  CD2  . TYR B 1 210 ? 6.564   -35.368 16.129  1.00 25.07  ? 228 TYR B CD2  1 
ATOM   7805  C  CE1  . TYR B 1 210 ? 5.901   -33.677 14.053  1.00 26.17  ? 228 TYR B CE1  1 
ATOM   7806  C  CE2  . TYR B 1 210 ? 5.432   -35.609 15.382  1.00 26.44  ? 228 TYR B CE2  1 
ATOM   7807  C  CZ   . TYR B 1 210 ? 5.107   -34.763 14.344  1.00 26.85  ? 228 TYR B CZ   1 
ATOM   7808  O  OH   . TYR B 1 210 ? 3.979   -35.009 13.599  1.00 28.80  ? 228 TYR B OH   1 
ATOM   7809  H  H    . TYR B 1 210 ? 10.866  -33.810 17.698  1.00 21.42  ? 228 TYR B H    1 
ATOM   7810  H  HA   . TYR B 1 210 ? 9.907   -35.308 15.694  1.00 22.70  ? 228 TYR B HA   1 
ATOM   7811  H  HB2  . TYR B 1 210 ? 8.524   -34.535 17.516  1.00 25.94  ? 228 TYR B HB2  1 
ATOM   7812  H  HB3  . TYR B 1 210 ? 8.638   -33.077 16.894  1.00 25.94  ? 228 TYR B HB3  1 
ATOM   7813  H  HD1  . TYR B 1 210 ? 7.574   -32.709 14.614  1.00 29.08  ? 228 TYR B HD1  1 
ATOM   7814  H  HD2  . TYR B 1 210 ? 6.778   -35.941 16.830  1.00 30.08  ? 228 TYR B HD2  1 
ATOM   7815  H  HE1  . TYR B 1 210 ? 5.676   -33.106 13.355  1.00 31.40  ? 228 TYR B HE1  1 
ATOM   7816  H  HE2  . TYR B 1 210 ? 4.890   -36.339 15.578  1.00 31.73  ? 228 TYR B HE2  1 
ATOM   7817  H  HH   . TYR B 1 210 ? 3.908   -34.437 12.988  1.00 34.56  ? 228 TYR B HH   1 
ATOM   7818  N  N    . LEU B 1 211 ? 10.016  -33.949 13.668  1.00 17.47  ? 229 LEU B N    1 
ATOM   7819  C  CA   . LEU B 1 211 ? 10.066  -33.100 12.485  1.00 17.69  ? 229 LEU B CA   1 
ATOM   7820  C  C    . LEU B 1 211 ? 8.787   -33.274 11.683  1.00 17.94  ? 229 LEU B C    1 
ATOM   7821  O  O    . LEU B 1 211 ? 8.374   -34.405 11.405  1.00 18.55  ? 229 LEU B O    1 
ATOM   7822  C  CB   . LEU B 1 211 ? 11.235  -33.444 11.566  1.00 18.68  ? 229 LEU B CB   1 
ATOM   7823  C  CG   . LEU B 1 211 ? 12.644  -33.173 12.073  1.00 17.86  ? 229 LEU B CG   1 
ATOM   7824  C  CD1  . LEU B 1 211 ? 13.643  -33.678 11.048  1.00 17.90  ? 229 LEU B CD1  1 
ATOM   7825  C  CD2  . LEU B 1 211 ? 12.865  -31.698 12.356  1.00 17.09  ? 229 LEU B CD2  1 
ATOM   7826  H  H    . LEU B 1 211 ? 9.830   -34.772 13.503  1.00 20.97  ? 229 LEU B H    1 
ATOM   7827  H  HA   . LEU B 1 211 ? 10.155  -32.183 12.788  1.00 21.23  ? 229 LEU B HA   1 
ATOM   7828  H  HB2  . LEU B 1 211 ? 11.187  -34.393 11.370  1.00 22.42  ? 229 LEU B HB2  1 
ATOM   7829  H  HB3  . LEU B 1 211 ? 11.129  -32.932 10.749  1.00 22.42  ? 229 LEU B HB3  1 
ATOM   7830  H  HG   . LEU B 1 211 ? 12.779  -33.640 12.912  1.00 21.44  ? 229 LEU B HG   1 
ATOM   7831  H  HD11 . LEU B 1 211 ? 14.541  -33.543 11.389  1.00 21.47  ? 229 LEU B HD11 1 
ATOM   7832  H  HD12 . LEU B 1 211 ? 13.486  -34.622 10.893  1.00 21.47  ? 229 LEU B HD12 1 
ATOM   7833  H  HD13 . LEU B 1 211 ? 13.525  -33.183 10.222  1.00 21.47  ? 229 LEU B HD13 1 
ATOM   7834  H  HD21 . LEU B 1 211 ? 12.683  -31.191 11.550  1.00 20.51  ? 229 LEU B HD21 1 
ATOM   7835  H  HD22 . LEU B 1 211 ? 12.264  -31.420 13.065  1.00 20.51  ? 229 LEU B HD22 1 
ATOM   7836  H  HD23 . LEU B 1 211 ? 13.785  -31.564 12.631  1.00 20.51  ? 229 LEU B HD23 1 
ATOM   7837  N  N    . PHE B 1 212 ? 8.187   -32.162 11.269  1.00 18.89  ? 230 PHE B N    1 
ATOM   7838  C  CA   . PHE B 1 212 ? 6.992   -32.253 10.445  1.00 19.14  ? 230 PHE B CA   1 
ATOM   7839  C  C    . PHE B 1 212 ? 7.314   -32.959 9.136   1.00 20.09  ? 230 PHE B C    1 
ATOM   7840  O  O    . PHE B 1 212 ? 8.359   -32.724 8.522   1.00 19.67  ? 230 PHE B O    1 
ATOM   7841  C  CB   . PHE B 1 212 ? 6.424   -30.860 10.196  1.00 20.84  ? 230 PHE B CB   1 
ATOM   7842  C  CG   . PHE B 1 212 ? 5.857   -30.238 11.430  1.00 23.90  ? 230 PHE B CG   1 
ATOM   7843  C  CD1  . PHE B 1 212 ? 4.668   -30.706 11.971  1.00 25.27  ? 230 PHE B CD1  1 
ATOM   7844  C  CD2  . PHE B 1 212 ? 6.523   -29.213 12.076  1.00 25.17  ? 230 PHE B CD2  1 
ATOM   7845  C  CE1  . PHE B 1 212 ? 4.153   -30.152 13.126  1.00 26.10  ? 230 PHE B CE1  1 
ATOM   7846  C  CE2  . PHE B 1 212 ? 6.010   -28.655 13.234  1.00 26.13  ? 230 PHE B CE2  1 
ATOM   7847  C  CZ   . PHE B 1 212 ? 4.826   -29.127 13.759  1.00 26.04  ? 230 PHE B CZ   1 
ATOM   7848  H  H    . PHE B 1 212 ? 8.447   -31.362 11.449  1.00 22.67  ? 230 PHE B H    1 
ATOM   7849  H  HA   . PHE B 1 212 ? 6.309   -32.769 10.900  1.00 22.97  ? 230 PHE B HA   1 
ATOM   7850  H  HB2  . PHE B 1 212 ? 7.133   -30.284 9.868   1.00 25.01  ? 230 PHE B HB2  1 
ATOM   7851  H  HB3  . PHE B 1 212 ? 5.715   -30.922 9.537   1.00 25.01  ? 230 PHE B HB3  1 
ATOM   7852  H  HD1  . PHE B 1 212 ? 4.214   -31.401 11.552  1.00 30.32  ? 230 PHE B HD1  1 
ATOM   7853  H  HD2  . PHE B 1 212 ? 7.325   -28.894 11.728  1.00 30.20  ? 230 PHE B HD2  1 
ATOM   7854  H  HE1  . PHE B 1 212 ? 3.352   -30.469 13.477  1.00 31.32  ? 230 PHE B HE1  1 
ATOM   7855  H  HE2  . PHE B 1 212 ? 6.464   -27.963 13.658  1.00 31.35  ? 230 PHE B HE2  1 
ATOM   7856  H  HZ   . PHE B 1 212 ? 4.481   -28.756 14.539  1.00 31.25  ? 230 PHE B HZ   1 
ATOM   7857  N  N    . ASN B 1 213 ? 6.411   -33.853 8.731   1.00 20.10  ? 231 ASN B N    1 
ATOM   7858  C  CA   . ASN B 1 213 ? 6.522   -34.719 7.562   1.00 19.68  ? 231 ASN B CA   1 
ATOM   7859  C  C    . ASN B 1 213 ? 7.570   -35.811 7.721   1.00 20.06  ? 231 ASN B C    1 
ATOM   7860  O  O    . ASN B 1 213 ? 7.712   -36.656 6.819   1.00 22.10  ? 231 ASN B O    1 
ATOM   7861  C  CB   . ASN B 1 213 ? 6.759   -33.938 6.265   1.00 20.58  ? 231 ASN B CB   1 
ATOM   7862  C  CG   . ASN B 1 213 ? 5.650   -32.963 5.983   1.00 21.89  ? 231 ASN B CG   1 
ATOM   7863  O  OD1  . ASN B 1 213 ? 4.483   -33.229 6.283   1.00 23.73  ? 231 ASN B OD1  1 
ATOM   7864  N  ND2  . ASN B 1 213 ? 6.002   -31.825 5.415   1.00 22.11  ? 231 ASN B ND2  1 
ATOM   7865  H  H    . ASN B 1 213 ? 5.672   -33.982 9.152   1.00 24.12  ? 231 ASN B H    1 
ATOM   7866  H  HA   . ASN B 1 213 ? 5.673   -35.176 7.457   1.00 23.62  ? 231 ASN B HA   1 
ATOM   7867  H  HB2  . ASN B 1 213 ? 7.588   -33.441 6.340   1.00 24.70  ? 231 ASN B HB2  1 
ATOM   7868  H  HB3  . ASN B 1 213 ? 6.812   -34.561 5.523   1.00 24.70  ? 231 ASN B HB3  1 
ATOM   7869  H  HD21 . ASN B 1 213 ? 5.405   -31.234 5.232   1.00 26.53  ? 231 ASN B HD21 1 
ATOM   7870  H  HD22 . ASN B 1 213 ? 6.827   -31.675 5.228   1.00 26.53  ? 231 ASN B HD22 1 
ATOM   7871  N  N    . GLY B 1 214 ? 8.302   -35.839 8.827   1.00 19.42  ? 232 GLY B N    1 
ATOM   7872  C  CA   . GLY B 1 214 ? 9.198   -36.941 9.081   1.00 19.02  ? 232 GLY B CA   1 
ATOM   7873  C  C    . GLY B 1 214 ? 8.468   -38.179 9.573   1.00 20.33  ? 232 GLY B C    1 
ATOM   7874  O  O    . GLY B 1 214 ? 7.283   -38.159 9.903   1.00 21.34  ? 232 GLY B O    1 
ATOM   7875  H  H    . GLY B 1 214 ? 8.294   -35.234 9.437   1.00 23.30  ? 232 GLY B H    1 
ATOM   7876  H  HA2  . GLY B 1 214 ? 9.667   -37.168 8.263   1.00 22.82  ? 232 GLY B HA2  1 
ATOM   7877  H  HA3  . GLY B 1 214 ? 9.845   -36.680 9.754   1.00 22.82  ? 232 GLY B HA3  1 
ATOM   7878  N  N    . LYS B 1 215 ? 9.209   -39.282 9.616   1.00 20.55  ? 233 LYS B N    1 
ATOM   7879  C  CA   . LYS B 1 215 ? 8.736   -40.523 10.224  1.00 21.38  ? 233 LYS B CA   1 
ATOM   7880  C  C    . LYS B 1 215 ? 9.211   -40.487 11.669  1.00 20.53  ? 233 LYS B C    1 
ATOM   7881  O  O    . LYS B 1 215 ? 10.358  -40.829 11.971  1.00 20.72  ? 233 LYS B O    1 
ATOM   7882  C  CB   . LYS B 1 215 ? 9.269   -41.733 9.468   1.00 21.41  ? 233 LYS B CB   1 
ATOM   7883  C  CG   . LYS B 1 215 ? 8.873   -43.077 10.071  1.00 21.84  ? 233 LYS B CG   1 
ATOM   7884  C  CD   . LYS B 1 215 ? 7.368   -43.249 10.161  1.00 24.08  ? 233 LYS B CD   1 
ATOM   7885  C  CE   . LYS B 1 215 ? 7.004   -44.647 10.649  1.00 25.55  ? 233 LYS B CE   1 
ATOM   7886  N  NZ   . LYS B 1 215 ? 5.531   -44.820 10.858  1.00 28.22  ? 233 LYS B NZ   1 
ATOM   7887  H  H    . LYS B 1 215 ? 10.004  -39.339 9.294   1.00 24.66  ? 233 LYS B H    1 
ATOM   7888  H  HA   . LYS B 1 215 ? 7.768   -40.578 10.202  1.00 25.65  ? 233 LYS B HA   1 
ATOM   7889  H  HB2  . LYS B 1 215 ? 8.927   -41.707 8.561   1.00 25.69  ? 233 LYS B HB2  1 
ATOM   7890  H  HB3  . LYS B 1 215 ? 10.238  -41.690 9.459   1.00 25.69  ? 233 LYS B HB3  1 
ATOM   7891  H  HG2  . LYS B 1 215 ? 9.225   -43.791 9.517   1.00 26.21  ? 233 LYS B HG2  1 
ATOM   7892  H  HG3  . LYS B 1 215 ? 9.238   -43.143 10.968  1.00 26.21  ? 233 LYS B HG3  1 
ATOM   7893  H  HD2  . LYS B 1 215 ? 7.006   -42.602 10.787  1.00 28.89  ? 233 LYS B HD2  1 
ATOM   7894  H  HD3  . LYS B 1 215 ? 6.974   -43.118 9.284   1.00 28.89  ? 233 LYS B HD3  1 
ATOM   7895  H  HE2  . LYS B 1 215 ? 7.292   -45.298 9.990   1.00 30.67  ? 233 LYS B HE2  1 
ATOM   7896  H  HE3  . LYS B 1 215 ? 7.449   -44.813 11.495  1.00 30.67  ? 233 LYS B HE3  1 
ATOM   7897  H  HZ1  . LYS B 1 215 ? 5.089   -44.582 10.122  1.00 33.86  ? 233 LYS B HZ1  1 
ATOM   7898  H  HZ2  . LYS B 1 215 ? 5.347   -45.671 11.042  1.00 33.86  ? 233 LYS B HZ2  1 
ATOM   7899  H  HZ3  . LYS B 1 215 ? 5.257   -44.312 11.535  1.00 33.86  ? 233 LYS B HZ3  1 
ATOM   7900  N  N    . ASN B 1 216 ? 8.340   -40.029 12.554  1.00 20.73  ? 234 ASN B N    1 
ATOM   7901  C  CA   . ASN B 1 216 ? 8.679   -39.790 13.950  1.00 19.50  ? 234 ASN B CA   1 
ATOM   7902  C  C    . ASN B 1 216 ? 8.239   -40.994 14.767  1.00 20.84  ? 234 ASN B C    1 
ATOM   7903  O  O    . ASN B 1 216 ? 7.039   -41.253 14.914  1.00 22.47  ? 234 ASN B O    1 
ATOM   7904  C  CB   . ASN B 1 216 ? 7.997   -38.517 14.437  1.00 19.92  ? 234 ASN B CB   1 
ATOM   7905  C  CG   . ASN B 1 216 ? 8.415   -37.305 13.646  1.00 19.26  ? 234 ASN B CG   1 
ATOM   7906  O  OD1  . ASN B 1 216 ? 9.572   -36.886 13.700  1.00 18.92  ? 234 ASN B OD1  1 
ATOM   7907  N  ND2  . ASN B 1 216 ? 7.479   -36.732 12.904  1.00 20.97  ? 234 ASN B ND2  1 
ATOM   7908  H  H    . ASN B 1 216 ? 7.522   -39.843 12.365  1.00 24.87  ? 234 ASN B H    1 
ATOM   7909  H  HA   . ASN B 1 216 ? 9.639   -39.692 14.047  1.00 23.40  ? 234 ASN B HA   1 
ATOM   7910  H  HB2  . ASN B 1 216 ? 7.036   -38.618 14.350  1.00 23.91  ? 234 ASN B HB2  1 
ATOM   7911  H  HB3  . ASN B 1 216 ? 8.232   -38.367 15.366  1.00 23.91  ? 234 ASN B HB3  1 
ATOM   7912  H  HD21 . ASN B 1 216 ? 7.668   -36.037 12.434  1.00 25.16  ? 234 ASN B HD21 1 
ATOM   7913  H  HD22 . ASN B 1 216 ? 6.682   -37.054 12.892  1.00 25.16  ? 234 ASN B HD22 1 
ATOM   7914  N  N    . VAL B 1 217 ? 9.213   -41.714 15.311  1.00 20.96  ? 235 VAL B N    1 
ATOM   7915  C  CA   . VAL B 1 217 ? 8.983   -42.990 15.976  1.00 20.89  ? 235 VAL B CA   1 
ATOM   7916  C  C    . VAL B 1 217 ? 9.420   -42.838 17.426  1.00 21.01  ? 235 VAL B C    1 
ATOM   7917  O  O    . VAL B 1 217 ? 10.607  -42.974 17.746  1.00 21.23  ? 235 VAL B O    1 
ATOM   7918  C  CB   . VAL B 1 217 ? 9.737   -44.136 15.293  1.00 21.63  ? 235 VAL B CB   1 
ATOM   7919  C  CG1  . VAL B 1 217 ? 9.395   -45.465 15.951  1.00 21.58  ? 235 VAL B CG1  1 
ATOM   7920  C  CG2  . VAL B 1 217 ? 9.412   -44.174 13.798  1.00 21.64  ? 235 VAL B CG2  1 
ATOM   7921  H  H    . VAL B 1 217 ? 10.039  -41.477 15.307  1.00 25.16  ? 235 VAL B H    1 
ATOM   7922  H  HA   . VAL B 1 217 ? 8.033   -43.184 15.966  1.00 25.07  ? 235 VAL B HA   1 
ATOM   7923  H  HB   . VAL B 1 217 ? 10.691  -43.987 15.390  1.00 25.95  ? 235 VAL B HB   1 
ATOM   7924  H  HG11 . VAL B 1 217 ? 8.431   -45.558 15.993  1.00 25.89  ? 235 VAL B HG11 1 
ATOM   7925  H  HG12 . VAL B 1 217 ? 9.775   -46.185 15.425  1.00 25.89  ? 235 VAL B HG12 1 
ATOM   7926  H  HG13 . VAL B 1 217 ? 9.768   -45.478 16.847  1.00 25.89  ? 235 VAL B HG13 1 
ATOM   7927  H  HG21 . VAL B 1 217 ? 9.852   -44.941 13.399  1.00 25.97  ? 235 VAL B HG21 1 
ATOM   7928  H  HG22 . VAL B 1 217 ? 8.452   -44.247 13.685  1.00 25.97  ? 235 VAL B HG22 1 
ATOM   7929  H  HG23 . VAL B 1 217 ? 9.733   -43.357 13.384  1.00 25.97  ? 235 VAL B HG23 1 
ATOM   7930  N  N    . GLN B 1 218 ? 8.467   -42.547 18.305  1.00 21.30  ? 236 GLN B N    1 
ATOM   7931  C  CA   . GLN B 1 218 ? 8.693   -42.642 19.740  1.00 21.98  ? 236 GLN B CA   1 
ATOM   7932  C  C    . GLN B 1 218 ? 8.536   -44.106 20.127  1.00 22.51  ? 236 GLN B C    1 
ATOM   7933  O  O    . GLN B 1 218 ? 7.485   -44.709 19.880  1.00 22.92  ? 236 GLN B O    1 
ATOM   7934  C  CB   . GLN B 1 218 ? 7.690   -41.771 20.489  1.00 22.98  ? 236 GLN B CB   1 
ATOM   7935  C  CG   . GLN B 1 218 ? 7.959   -41.660 21.978  1.00 23.57  ? 236 GLN B CG   1 
ATOM   7936  C  CD   . GLN B 1 218 ? 6.687   -41.517 22.781  1.00 24.89  ? 236 GLN B CD   1 
ATOM   7937  O  OE1  . GLN B 1 218 ? 5.801   -42.374 22.721  1.00 26.12  ? 236 GLN B OE1  1 
ATOM   7938  N  NE2  . GLN B 1 218 ? 6.581   -40.426 23.533  1.00 24.77  ? 236 GLN B NE2  1 
ATOM   7939  H  H    . GLN B 1 218 ? 7.675   -42.290 18.093  1.00 25.56  ? 236 GLN B H    1 
ATOM   7940  H  HA   . GLN B 1 218 ? 9.582   -42.333 19.975  1.00 26.38  ? 236 GLN B HA   1 
ATOM   7941  H  HB2  . GLN B 1 218 ? 7.717   -40.876 20.117  1.00 27.58  ? 236 GLN B HB2  1 
ATOM   7942  H  HB3  . GLN B 1 218 ? 6.804   -42.150 20.376  1.00 27.58  ? 236 GLN B HB3  1 
ATOM   7943  H  HG2  . GLN B 1 218 ? 8.417   -42.461 22.279  1.00 28.28  ? 236 GLN B HG2  1 
ATOM   7944  H  HG3  . GLN B 1 218 ? 8.511   -40.880 22.144  1.00 28.28  ? 236 GLN B HG3  1 
ATOM   7945  H  HE21 . GLN B 1 218 ? 7.218   -39.847 23.544  1.00 29.73  ? 236 GLN B HE21 1 
ATOM   7946  H  HE22 . GLN B 1 218 ? 5.876   -40.298 24.009  1.00 29.73  ? 236 GLN B HE22 1 
ATOM   7947  N  N    . ALA B 1 219 ? 9.584   -44.684 20.717  1.00 22.73  ? 237 ALA B N    1 
ATOM   7948  C  CA   . ALA B 1 219 ? 9.607   -46.130 20.918  1.00 23.15  ? 237 ALA B CA   1 
ATOM   7949  C  C    . ALA B 1 219 ? 8.398   -46.611 21.711  1.00 23.70  ? 237 ALA B C    1 
ATOM   7950  O  O    . ALA B 1 219 ? 7.850   -47.688 21.432  1.00 23.73  ? 237 ALA B O    1 
ATOM   7951  C  CB   . ALA B 1 219 ? 10.901  -46.534 21.621  1.00 23.39  ? 237 ALA B CB   1 
ATOM   7952  H  H    . ALA B 1 219 ? 10.280  -44.269 21.004  1.00 27.28  ? 237 ALA B H    1 
ATOM   7953  H  HA   . ALA B 1 219 ? 9.581   -46.562 20.050  1.00 27.78  ? 237 ALA B HA   1 
ATOM   7954  H  HB1  . ALA B 1 219 ? 11.656  -46.236 21.090  1.00 28.07  ? 237 ALA B HB1  1 
ATOM   7955  H  HB2  . ALA B 1 219 ? 10.928  -46.118 22.497  1.00 28.07  ? 237 ALA B HB2  1 
ATOM   7956  H  HB3  . ALA B 1 219 ? 10.922  -47.500 21.713  1.00 28.07  ? 237 ALA B HB3  1 
ATOM   7957  N  N    . GLN B 1 220 ? 7.964   -45.831 22.704  1.00 25.25  ? 238 GLN B N    1 
ATOM   7958  C  CA   . GLN B 1 220 ? 6.862   -46.266 23.555  1.00 26.36  ? 238 GLN B CA   1 
ATOM   7959  C  C    . GLN B 1 220 ? 5.540   -46.297 22.799  1.00 26.72  ? 238 GLN B C    1 
ATOM   7960  O  O    . GLN B 1 220 ? 4.648   -47.071 23.154  1.00 27.56  ? 238 GLN B O    1 
ATOM   7961  C  CB   . GLN B 1 220 ? 6.754   -45.359 24.779  1.00 26.34  ? 238 GLN B CB   1 
ATOM   7962  C  CG   . GLN B 1 220 ? 7.876   -45.544 25.787  1.00 25.40  ? 238 GLN B CG   1 
ATOM   7963  C  CD   . GLN B 1 220 ? 9.179   -44.893 25.345  1.00 23.54  ? 238 GLN B CD   1 
ATOM   7964  O  OE1  . GLN B 1 220 ? 9.195   -44.031 24.463  1.00 23.36  ? 238 GLN B OE1  1 
ATOM   7965  N  NE2  . GLN B 1 220 ? 10.280  -45.313 25.953  1.00 23.13  ? 238 GLN B NE2  1 
ATOM   7966  H  H    . GLN B 1 220 ? 8.287   -45.058 22.901  1.00 30.30  ? 238 GLN B H    1 
ATOM   7967  H  HA   . GLN B 1 220 ? 7.048   -47.167 23.864  1.00 31.64  ? 238 GLN B HA   1 
ATOM   7968  H  HB2  . GLN B 1 220 ? 6.772   -44.435 24.483  1.00 31.61  ? 238 GLN B HB2  1 
ATOM   7969  H  HB3  . GLN B 1 220 ? 5.916   -45.546 25.231  1.00 31.61  ? 238 GLN B HB3  1 
ATOM   7970  H  HG2  . GLN B 1 220 ? 7.612   -45.144 26.631  1.00 30.48  ? 238 GLN B HG2  1 
ATOM   7971  H  HG3  . GLN B 1 220 ? 8.040   -46.493 25.907  1.00 30.48  ? 238 GLN B HG3  1 
ATOM   7972  H  HE21 . GLN B 1 220 ? 10.232  -45.920 26.560  1.00 27.76  ? 238 GLN B HE21 1 
ATOM   7973  H  HE22 . GLN B 1 220 ? 11.043  -44.977 25.740  1.00 27.76  ? 238 GLN B HE22 1 
ATOM   7974  N  N    . ALA B 1 221 ? 5.387   -45.464 21.768  1.00 26.61  ? 239 ALA B N    1 
ATOM   7975  C  CA   . ALA B 1 221 ? 4.170   -45.514 20.964  1.00 27.68  ? 239 ALA B CA   1 
ATOM   7976  C  C    . ALA B 1 221 ? 4.010   -46.867 20.285  1.00 28.18  ? 239 ALA B C    1 
ATOM   7977  O  O    . ALA B 1 221 ? 2.881   -47.300 20.023  1.00 28.22  ? 239 ALA B O    1 
ATOM   7978  C  CB   . ALA B 1 221 ? 4.184   -44.396 19.920  1.00 27.22  ? 239 ALA B CB   1 
ATOM   7979  H  H    . ALA B 1 221 ? 5.961   -44.873 21.519  1.00 31.93  ? 239 ALA B H    1 
ATOM   7980  H  HA   . ALA B 1 221 ? 3.405   -45.373 21.543  1.00 33.22  ? 239 ALA B HA   1 
ATOM   7981  H  HB1  . ALA B 1 221 ? 3.355   -44.423 19.417  1.00 32.67  ? 239 ALA B HB1  1 
ATOM   7982  H  HB2  . ALA B 1 221 ? 4.268   -43.542 20.373  1.00 32.67  ? 239 ALA B HB2  1 
ATOM   7983  H  HB3  . ALA B 1 221 ? 4.938   -44.529 19.324  1.00 32.67  ? 239 ALA B HB3  1 
ATOM   7984  N  N    . VAL B 1 222 ? 5.119   -47.545 19.996  1.00 28.22  ? 240 VAL B N    1 
ATOM   7985  C  CA   . VAL B 1 222 ? 5.080   -48.867 19.376  1.00 28.46  ? 240 VAL B CA   1 
ATOM   7986  C  C    . VAL B 1 222 ? 5.145   -49.971 20.421  1.00 28.26  ? 240 VAL B C    1 
ATOM   7987  O  O    . VAL B 1 222 ? 4.435   -50.976 20.319  1.00 29.34  ? 240 VAL B O    1 
ATOM   7988  C  CB   . VAL B 1 222 ? 6.242   -48.988 18.366  1.00 28.50  ? 240 VAL B CB   1 
ATOM   7989  C  CG1  . VAL B 1 222 ? 6.290   -50.379 17.751  1.00 28.79  ? 240 VAL B CG1  1 
ATOM   7990  C  CG2  . VAL B 1 222 ? 6.131   -47.919 17.283  1.00 29.75  ? 240 VAL B CG2  1 
ATOM   7991  H  H    . VAL B 1 222 ? 5.915   -47.258 20.150  1.00 33.87  ? 240 VAL B H    1 
ATOM   7992  H  HA   . VAL B 1 222 ? 4.241   -48.964 18.898  1.00 34.15  ? 240 VAL B HA   1 
ATOM   7993  H  HB   . VAL B 1 222 ? 7.076   -48.848 18.842  1.00 34.20  ? 240 VAL B HB   1 
ATOM   7994  H  HG11 . VAL B 1 222 ? 6.963   -50.393 17.053  1.00 34.54  ? 240 VAL B HG11 1 
ATOM   7995  H  HG12 . VAL B 1 222 ? 6.515   -51.022 18.442  1.00 34.54  ? 240 VAL B HG12 1 
ATOM   7996  H  HG13 . VAL B 1 222 ? 5.420   -50.588 17.376  1.00 34.54  ? 240 VAL B HG13 1 
ATOM   7997  H  HG21 . VAL B 1 222 ? 6.836   -48.056 16.631  1.00 35.70  ? 240 VAL B HG21 1 
ATOM   7998  H  HG22 . VAL B 1 222 ? 5.264   -47.992 16.855  1.00 35.70  ? 240 VAL B HG22 1 
ATOM   7999  H  HG23 . VAL B 1 222 ? 6.225   -47.044 17.692  1.00 35.70  ? 240 VAL B HG23 1 
ATOM   8000  N  N    . CYS B 1 223 ? 5.987   -49.790 21.437  1.00 28.27  ? 241 CYS B N    1 
ATOM   8001  C  CA   . CYS B 1 223 ? 6.367   -50.863 22.343  1.00 28.58  ? 241 CYS B CA   1 
ATOM   8002  C  C    . CYS B 1 223 ? 5.590   -50.866 23.651  1.00 29.73  ? 241 CYS B C    1 
ATOM   8003  O  O    . CYS B 1 223 ? 5.668   -51.853 24.392  1.00 30.81  ? 241 CYS B O    1 
ATOM   8004  C  CB   . CYS B 1 223 ? 7.870   -50.776 22.631  1.00 28.60  ? 241 CYS B CB   1 
ATOM   8005  S  SG   . CYS B 1 223 ? 8.849   -51.111 21.145  1.00 27.28  ? 241 CYS B SG   1 
ATOM   8006  H  H    . CYS B 1 223 ? 6.358   -49.036 21.624  1.00 33.92  ? 241 CYS B H    1 
ATOM   8007  H  HA   . CYS B 1 223 ? 6.189   -51.715 21.915  1.00 34.30  ? 241 CYS B HA   1 
ATOM   8008  H  HB2  . CYS B 1 223 ? 8.085   -49.883 22.944  1.00 34.32  ? 241 CYS B HB2  1 
ATOM   8009  H  HB3  . CYS B 1 223 ? 8.105   -51.430 23.307  1.00 34.32  ? 241 CYS B HB3  1 
ATOM   8010  N  N    . GLY B 1 224 ? 4.832   -49.813 23.938  1.00 30.00  ? 242 GLY B N    1 
ATOM   8011  C  CA   . GLY B 1 224 ? 4.082   -49.728 25.166  1.00 31.74  ? 242 GLY B CA   1 
ATOM   8012  C  C    . GLY B 1 224 ? 4.772   -48.870 26.205  1.00 33.48  ? 242 GLY B C    1 
ATOM   8013  O  O    . GLY B 1 224 ? 5.972   -48.589 26.115  1.00 32.57  ? 242 GLY B O    1 
ATOM   8014  H  H    . GLY B 1 224 ? 4.740   -49.129 23.425  1.00 36.01  ? 242 GLY B H    1 
ATOM   8015  H  HA2  . GLY B 1 224 ? 3.210   -49.344 24.983  1.00 38.09  ? 242 GLY B HA2  1 
ATOM   8016  H  HA3  . GLY B 1 224 ? 3.965   -50.618 25.533  1.00 38.09  ? 242 GLY B HA3  1 
ATOM   8017  N  N    . PRO B 1 225 ? 4.024   -48.448 27.231  1.00 36.25  ? 243 PRO B N    1 
ATOM   8018  C  CA   . PRO B 1 225 ? 4.600   -47.527 28.224  1.00 37.51  ? 243 PRO B CA   1 
ATOM   8019  C  C    . PRO B 1 225 ? 5.662   -48.160 29.105  1.00 36.69  ? 243 PRO B C    1 
ATOM   8020  O  O    . PRO B 1 225 ? 6.409   -47.427 29.765  1.00 37.93  ? 243 PRO B O    1 
ATOM   8021  C  CB   . PRO B 1 225 ? 3.386   -47.072 29.052  1.00 39.01  ? 243 PRO B CB   1 
ATOM   8022  C  CG   . PRO B 1 225 ? 2.166   -47.670 28.376  1.00 39.08  ? 243 PRO B CG   1 
ATOM   8023  C  CD   . PRO B 1 225 ? 2.647   -48.841 27.575  1.00 37.77  ? 243 PRO B CD   1 
ATOM   8024  H  HA   . PRO B 1 225 ? 4.979   -46.757 27.772  1.00 45.01  ? 243 PRO B HA   1 
ATOM   8025  H  HB2  . PRO B 1 225 ? 3.470   -47.401 29.960  1.00 46.81  ? 243 PRO B HB2  1 
ATOM   8026  H  HB3  . PRO B 1 225 ? 3.338   -46.103 29.053  1.00 46.81  ? 243 PRO B HB3  1 
ATOM   8027  H  HG2  . PRO B 1 225 ? 1.530   -47.957 29.051  1.00 46.90  ? 243 PRO B HG2  1 
ATOM   8028  H  HG3  . PRO B 1 225 ? 1.758   -47.006 27.798  1.00 46.90  ? 243 PRO B HG3  1 
ATOM   8029  H  HD2  . PRO B 1 225 ? 2.638   -49.653 28.106  1.00 45.33  ? 243 PRO B HD2  1 
ATOM   8030  H  HD3  . PRO B 1 225 ? 2.109   -48.961 26.776  1.00 45.33  ? 243 PRO B HD3  1 
ATOM   8031  N  N    . LEU B 1 226 ? 5.758   -49.488 29.141  1.00 34.96  ? 244 LEU B N    1 
ATOM   8032  C  CA   . LEU B 1 226 ? 6.769   -50.141 29.960  1.00 34.53  ? 244 LEU B CA   1 
ATOM   8033  C  C    . LEU B 1 226 ? 8.118   -50.250 29.263  1.00 32.83  ? 244 LEU B C    1 
ATOM   8034  O  O    . LEU B 1 226 ? 9.102   -50.629 29.909  1.00 32.75  ? 244 LEU B O    1 
ATOM   8035  C  CB   . LEU B 1 226 ? 6.301   -51.540 30.364  1.00 36.04  ? 244 LEU B CB   1 
ATOM   8036  C  CG   . LEU B 1 226 ? 4.901   -51.629 30.968  1.00 37.04  ? 244 LEU B CG   1 
ATOM   8037  C  CD1  . LEU B 1 226 ? 4.563   -53.078 31.312  1.00 37.08  ? 244 LEU B CD1  1 
ATOM   8038  C  CD2  . LEU B 1 226 ? 4.779   -50.733 32.190  1.00 37.31  ? 244 LEU B CD2  1 
ATOM   8039  H  H    . LEU B 1 226 ? 5.251   -50.027 28.703  1.00 41.96  ? 244 LEU B H    1 
ATOM   8040  H  HA   . LEU B 1 226 ? 6.889   -49.619 30.769  1.00 41.43  ? 244 LEU B HA   1 
ATOM   8041  H  HB2  . LEU B 1 226 ? 6.309   -52.101 29.573  1.00 43.25  ? 244 LEU B HB2  1 
ATOM   8042  H  HB3  . LEU B 1 226 ? 6.922   -51.888 31.023  1.00 43.25  ? 244 LEU B HB3  1 
ATOM   8043  H  HG   . LEU B 1 226 ? 4.254   -51.318 30.316  1.00 44.45  ? 244 LEU B HG   1 
ATOM   8044  H  HD11 . LEU B 1 226 ? 5.221   -53.415 31.939  1.00 44.50  ? 244 LEU B HD11 1 
ATOM   8045  H  HD12 . LEU B 1 226 ? 3.679   -53.110 31.710  1.00 44.50  ? 244 LEU B HD12 1 
ATOM   8046  H  HD13 . LEU B 1 226 ? 4.579   -53.607 30.499  1.00 44.50  ? 244 LEU B HD13 1 
ATOM   8047  H  HD21 . LEU B 1 226 ? 3.948   -50.935 32.648  1.00 44.77  ? 244 LEU B HD21 1 
ATOM   8048  H  HD22 . LEU B 1 226 ? 5.531   -50.900 32.780  1.00 44.77  ? 244 LEU B HD22 1 
ATOM   8049  H  HD23 . LEU B 1 226 ? 4.782   -49.807 31.904  1.00 44.77  ? 244 LEU B HD23 1 
ATOM   8050  N  N    . PHE B 1 227 ? 8.190   -49.930 27.974  1.00 30.35  ? 245 PHE B N    1 
ATOM   8051  C  CA   . PHE B 1 227 ? 9.438   -50.034 27.236  1.00 28.81  ? 245 PHE B CA   1 
ATOM   8052  C  C    . PHE B 1 227 ? 10.335  -48.868 27.617  1.00 28.80  ? 245 PHE B C    1 
ATOM   8053  O  O    . PHE B 1 227 ? 9.907   -47.709 27.585  1.00 30.03  ? 245 PHE B O    1 
ATOM   8054  C  CB   . PHE B 1 227 ? 9.160   -50.014 25.735  1.00 27.65  ? 245 PHE B CB   1 
ATOM   8055  C  CG   . PHE B 1 227 ? 10.371  -50.292 24.895  1.00 27.35  ? 245 PHE B CG   1 
ATOM   8056  C  CD1  . PHE B 1 227 ? 10.880  -51.577 24.802  1.00 28.12  ? 245 PHE B CD1  1 
ATOM   8057  C  CD2  . PHE B 1 227 ? 11.006  -49.271 24.203  1.00 27.22  ? 245 PHE B CD2  1 
ATOM   8058  C  CE1  . PHE B 1 227 ? 11.998  -51.838 24.032  1.00 28.37  ? 245 PHE B CE1  1 
ATOM   8059  C  CE2  . PHE B 1 227 ? 12.122  -49.532 23.431  1.00 26.80  ? 245 PHE B CE2  1 
ATOM   8060  C  CZ   . PHE B 1 227 ? 12.617  -50.818 23.346  1.00 28.08  ? 245 PHE B CZ   1 
ATOM   8061  H  H    . PHE B 1 227 ? 7.526   -49.650 27.505  1.00 36.42  ? 245 PHE B H    1 
ATOM   8062  H  HA   . PHE B 1 227 ? 9.888   -50.866 27.451  1.00 34.57  ? 245 PHE B HA   1 
ATOM   8063  H  HB2  . PHE B 1 227 ? 8.496   -50.690 25.531  1.00 33.19  ? 245 PHE B HB2  1 
ATOM   8064  H  HB3  . PHE B 1 227 ? 8.826   -49.136 25.491  1.00 33.19  ? 245 PHE B HB3  1 
ATOM   8065  H  HD1  . PHE B 1 227 ? 10.465  -52.271 25.262  1.00 33.75  ? 245 PHE B HD1  1 
ATOM   8066  H  HD2  . PHE B 1 227 ? 10.678  -48.403 24.258  1.00 32.66  ? 245 PHE B HD2  1 
ATOM   8067  H  HE1  . PHE B 1 227 ? 12.333  -52.705 23.978  1.00 34.04  ? 245 PHE B HE1  1 
ATOM   8068  H  HE2  . PHE B 1 227 ? 12.540  -48.841 22.968  1.00 32.16  ? 245 PHE B HE2  1 
ATOM   8069  H  HZ   . PHE B 1 227 ? 13.368  -50.995 22.826  1.00 33.70  ? 245 PHE B HZ   1 
ATOM   8070  N  N    . VAL B 1 228 ? 11.577  -49.173 27.987  1.00 28.67  ? 246 VAL B N    1 
ATOM   8071  C  CA   . VAL B 1 228 ? 12.508  -48.174 28.495  1.00 28.20  ? 246 VAL B CA   1 
ATOM   8072  C  C    . VAL B 1 228 ? 13.833  -48.315 27.763  1.00 27.77  ? 246 VAL B C    1 
ATOM   8073  O  O    . VAL B 1 228 ? 14.480  -49.366 27.837  1.00 28.85  ? 246 VAL B O    1 
ATOM   8074  C  CB   . VAL B 1 228 ? 12.724  -48.314 30.013  1.00 29.43  ? 246 VAL B CB   1 
ATOM   8075  C  CG1  . VAL B 1 228 ? 13.755  -47.307 30.482  1.00 29.31  ? 246 VAL B CG1  1 
ATOM   8076  C  CG2  . VAL B 1 228 ? 11.415  -48.134 30.760  1.00 30.15  ? 246 VAL B CG2  1 
ATOM   8077  H  H    . VAL B 1 228 ? 11.906  -49.966 27.952  1.00 34.40  ? 246 VAL B H    1 
ATOM   8078  H  HA   . VAL B 1 228 ? 12.154  -47.292 28.303  1.00 33.84  ? 246 VAL B HA   1 
ATOM   8079  H  HB   . VAL B 1 228 ? 13.053  -49.205 30.207  1.00 35.32  ? 246 VAL B HB   1 
ATOM   8080  H  HG11 . VAL B 1 228 ? 14.631  -47.583 30.169  1.00 35.17  ? 246 VAL B HG11 1 
ATOM   8081  H  HG12 . VAL B 1 228 ? 13.533  -46.435 30.120  1.00 35.17  ? 246 VAL B HG12 1 
ATOM   8082  H  HG13 . VAL B 1 228 ? 13.746  -47.275 31.452  1.00 35.17  ? 246 VAL B HG13 1 
ATOM   8083  H  HG21 . VAL B 1 228 ? 10.747  -47.788 30.149  1.00 36.18  ? 246 VAL B HG21 1 
ATOM   8084  H  HG22 . VAL B 1 228 ? 11.130  -48.994 31.109  1.00 36.18  ? 246 VAL B HG22 1 
ATOM   8085  H  HG23 . VAL B 1 228 ? 11.551  -47.510 31.490  1.00 36.18  ? 246 VAL B HG23 1 
ATOM   8086  N  N    . ILE B 1 229 ? 14.235  -47.262 27.057  1.00 25.88  ? 247 ILE B N    1 
ATOM   8087  C  CA   . ILE B 1 229 ? 15.602  -47.117 26.572  1.00 24.42  ? 247 ILE B CA   1 
ATOM   8088  C  C    . ILE B 1 229 ? 16.027  -45.679 26.821  1.00 23.59  ? 247 ILE B C    1 
ATOM   8089  O  O    . ILE B 1 229 ? 15.226  -44.747 26.676  1.00 23.42  ? 247 ILE B O    1 
ATOM   8090  C  CB   . ILE B 1 229 ? 15.780  -47.503 25.089  1.00 24.70  ? 247 ILE B CB   1 
ATOM   8091  C  CG1  . ILE B 1 229 ? 14.869  -46.671 24.191  1.00 24.96  ? 247 ILE B CG1  1 
ATOM   8092  C  CG2  . ILE B 1 229 ? 15.534  -48.990 24.903  1.00 25.38  ? 247 ILE B CG2  1 
ATOM   8093  C  CD1  . ILE B 1 229 ? 14.929  -47.074 22.720  1.00 24.67  ? 247 ILE B CD1  1 
ATOM   8094  H  H    . ILE B 1 229 ? 13.722  -46.606 26.842  1.00 31.05  ? 247 ILE B H    1 
ATOM   8095  H  HA   . ILE B 1 229 ? 16.174  -47.716 27.077  1.00 29.30  ? 247 ILE B HA   1 
ATOM   8096  H  HB   . ILE B 1 229 ? 16.694  -47.309 24.830  1.00 29.64  ? 247 ILE B HB   1 
ATOM   8097  H  HG12 . ILE B 1 229 ? 13.953  -46.777 24.491  1.00 29.95  ? 247 ILE B HG12 1 
ATOM   8098  H  HG13 . ILE B 1 229 ? 15.133  -45.740 24.255  1.00 29.95  ? 247 ILE B HG13 1 
ATOM   8099  H  HG21 . ILE B 1 229 ? 15.848  -49.255 24.025  1.00 30.46  ? 247 ILE B HG21 1 
ATOM   8100  H  HG22 . ILE B 1 229 ? 16.018  -49.478 25.588  1.00 30.46  ? 247 ILE B HG22 1 
ATOM   8101  H  HG23 . ILE B 1 229 ? 14.584  -49.166 24.982  1.00 30.46  ? 247 ILE B HG23 1 
ATOM   8102  H  HD11 . ILE B 1 229 ? 15.856  -47.203 22.465  1.00 29.61  ? 247 ILE B HD11 1 
ATOM   8103  H  HD12 . ILE B 1 229 ? 14.434  -47.899 22.598  1.00 29.61  ? 247 ILE B HD12 1 
ATOM   8104  H  HD13 . ILE B 1 229 ? 14.534  -46.369 22.183  1.00 29.61  ? 247 ILE B HD13 1 
ATOM   8105  N  N    . ASP B 1 230 ? 17.285  -45.501 27.201  1.00 23.15  ? 248 ASP B N    1 
ATOM   8106  C  CA   . ASP B 1 230 ? 17.804  -44.193 27.570  1.00 21.09  ? 248 ASP B CA   1 
ATOM   8107  C  C    . ASP B 1 230 ? 18.355  -43.480 26.334  1.00 19.66  ? 248 ASP B C    1 
ATOM   8108  O  O    . ASP B 1 230 ? 18.126  -43.892 25.195  1.00 20.50  ? 248 ASP B O    1 
ATOM   8109  C  CB   . ASP B 1 230 ? 18.772  -44.311 28.753  1.00 21.19  ? 248 ASP B CB   1 
ATOM   8110  C  CG   . ASP B 1 230 ? 19.993  -45.172 28.462  1.00 24.01  ? 248 ASP B CG   1 
ATOM   8111  O  OD1  . ASP B 1 230 ? 20.184  -45.626 27.315  1.00 25.98  ? 248 ASP B OD1  1 
ATOM   8112  O  OD2  . ASP B 1 230 ? 20.772  -45.403 29.413  1.00 26.05  ? 248 ASP B OD2  1 
ATOM   8113  H  H    . ASP B 1 230 ? 17.867  -46.132 27.255  1.00 27.78  ? 248 ASP B H    1 
ATOM   8114  H  HA   . ASP B 1 230 ? 17.073  -43.639 27.885  1.00 25.31  ? 248 ASP B HA   1 
ATOM   8115  H  HB2  . ASP B 1 230 ? 19.085  -43.424 28.990  1.00 25.43  ? 248 ASP B HB2  1 
ATOM   8116  H  HB3  . ASP B 1 230 ? 18.301  -44.708 29.503  1.00 25.43  ? 248 ASP B HB3  1 
ATOM   8117  N  N    . HIS B 1 231 ? 19.077  -42.383 26.551  1.00 17.68  ? 249 HIS B N    1 
ATOM   8118  C  CA   . HIS B 1 231 ? 19.587  -41.600 25.427  1.00 17.07  ? 249 HIS B CA   1 
ATOM   8119  C  C    . HIS B 1 231 ? 20.519  -42.433 24.553  1.00 18.08  ? 249 HIS B C    1 
ATOM   8120  O  O    . HIS B 1 231 ? 20.429  -42.390 23.318  1.00 18.62  ? 249 HIS B O    1 
ATOM   8121  C  CB   . HIS B 1 231 ? 20.314  -40.369 25.966  1.00 18.33  ? 249 HIS B CB   1 
ATOM   8122  C  CG   . HIS B 1 231 ? 20.649  -39.344 24.929  1.00 18.96  ? 249 HIS B CG   1 
ATOM   8123  N  ND1  . HIS B 1 231 ? 19.696  -38.745 24.133  1.00 18.72  ? 249 HIS B ND1  1 
ATOM   8124  C  CD2  . HIS B 1 231 ? 21.832  -38.781 24.584  1.00 18.98  ? 249 HIS B CD2  1 
ATOM   8125  C  CE1  . HIS B 1 231 ? 20.280  -37.868 23.333  1.00 19.27  ? 249 HIS B CE1  1 
ATOM   8126  N  NE2  . HIS B 1 231 ? 21.577  -37.875 23.584  1.00 19.93  ? 249 HIS B NE2  1 
ATOM   8127  H  H    . HIS B 1 231 ? 19.282  -42.073 27.326  1.00 21.21  ? 249 HIS B H    1 
ATOM   8128  H  HA   . HIS B 1 231 ? 18.847  -41.308 24.873  1.00 20.48  ? 249 HIS B HA   1 
ATOM   8129  H  HB2  . HIS B 1 231 ? 19.749  -39.942 26.629  1.00 21.99  ? 249 HIS B HB2  1 
ATOM   8130  H  HB3  . HIS B 1 231 ? 21.146  -40.655 26.375  1.00 21.99  ? 249 HIS B HB3  1 
ATOM   8131  H  HD1  . HIS B 1 231 ? 18.854  -38.915 24.153  1.00 22.47  ? 249 HIS B HD1  1 
ATOM   8132  H  HD2  . HIS B 1 231 ? 22.663  -38.974 24.955  1.00 22.78  ? 249 HIS B HD2  1 
ATOM   8133  H  HE1  . HIS B 1 231 ? 19.850  -37.337 22.702  1.00 23.13  ? 249 HIS B HE1  1 
ATOM   8134  N  N    . ALA B 1 232 ? 21.419  -43.198 25.177  1.00 19.57  ? 250 ALA B N    1 
ATOM   8135  C  CA   . ALA B 1 232 ? 22.336  -44.047 24.421  1.00 19.86  ? 250 ALA B CA   1 
ATOM   8136  C  C    . ALA B 1 232 ? 21.619  -45.270 23.858  1.00 20.79  ? 250 ALA B C    1 
ATOM   8137  O  O    . ALA B 1 232 ? 21.900  -45.700 22.730  1.00 20.18  ? 250 ALA B O    1 
ATOM   8138  C  CB   . ALA B 1 232 ? 23.515  -44.454 25.307  1.00 20.49  ? 250 ALA B CB   1 
ATOM   8139  H  H    . ALA B 1 232 ? 21.518  -43.241 26.031  1.00 23.48  ? 250 ALA B H    1 
ATOM   8140  H  HA   . ALA B 1 232 ? 22.690  -43.546 23.670  1.00 23.83  ? 250 ALA B HA   1 
ATOM   8141  H  HB1  . ALA B 1 232 ? 23.176  -44.909 26.094  1.00 24.59  ? 250 ALA B HB1  1 
ATOM   8142  H  HB2  . ALA B 1 232 ? 24.096  -45.048 24.806  1.00 24.59  ? 250 ALA B HB2  1 
ATOM   8143  H  HB3  . ALA B 1 232 ? 24.002  -43.658 25.569  1.00 24.59  ? 250 ALA B HB3  1 
ATOM   8144  N  N    . GLY B 1 233 ? 20.680  -45.837 24.620  1.00 21.30  ? 251 GLY B N    1 
ATOM   8145  C  CA   . GLY B 1 233 ? 19.915  -46.972 24.133  1.00 20.45  ? 251 GLY B CA   1 
ATOM   8146  C  C    . GLY B 1 233 ? 19.068  -46.637 22.927  1.00 19.81  ? 251 GLY B C    1 
ATOM   8147  O  O    . GLY B 1 233 ? 18.736  -47.531 22.140  1.00 20.50  ? 251 GLY B O    1 
ATOM   8148  H  H    . GLY B 1 233 ? 20.472  -45.582 25.414  1.00 25.56  ? 251 GLY B H    1 
ATOM   8149  H  HA2  . GLY B 1 233 ? 20.525  -47.685 23.888  1.00 24.54  ? 251 GLY B HA2  1 
ATOM   8150  H  HA3  . GLY B 1 233 ? 19.329  -47.287 24.839  1.00 24.54  ? 251 GLY B HA3  1 
ATOM   8151  N  N    . SER B 1 234 ? 18.716  -45.360 22.765  1.00 19.39  ? 252 SER B N    1 
ATOM   8152  C  CA   . SER B 1 234 ? 18.005  -44.932 21.570  1.00 19.31  ? 252 SER B CA   1 
ATOM   8153  C  C    . SER B 1 234 ? 18.818  -45.207 20.316  1.00 18.70  ? 252 SER B C    1 
ATOM   8154  O  O    . SER B 1 234 ? 18.244  -45.430 19.246  1.00 18.71  ? 252 SER B O    1 
ATOM   8155  C  CB   . SER B 1 234 ? 17.695  -43.438 21.656  1.00 19.74  ? 252 SER B CB   1 
ATOM   8156  O  OG   . SER B 1 234 ? 16.851  -43.151 22.756  1.00 20.27  ? 252 SER B OG   1 
ATOM   8157  H  H    . SER B 1 234 ? 18.877  -44.730 23.328  1.00 23.26  ? 252 SER B H    1 
ATOM   8158  H  HA   . SER B 1 234 ? 17.169  -45.420 21.513  1.00 23.17  ? 252 SER B HA   1 
ATOM   8159  H  HB2  . SER B 1 234 ? 18.526  -42.950 21.763  1.00 23.69  ? 252 SER B HB2  1 
ATOM   8160  H  HB3  . SER B 1 234 ? 17.251  -43.162 20.839  1.00 23.69  ? 252 SER B HB3  1 
ATOM   8161  H  HG   . SER B 1 234 ? 16.120  -43.556 22.671  1.00 24.33  ? 252 SER B HG   1 
ATOM   8162  N  N    . LEU B 1 235 ? 20.148  -45.182 20.426  1.00 18.77  ? 253 LEU B N    1 
ATOM   8163  C  CA   . LEU B 1 235 ? 21.024  -45.494 19.309  1.00 18.54  ? 253 LEU B CA   1 
ATOM   8164  C  C    . LEU B 1 235 ? 21.291  -46.989 19.176  1.00 18.92  ? 253 LEU B C    1 
ATOM   8165  O  O    . LEU B 1 235 ? 21.343  -47.508 18.056  1.00 19.95  ? 253 LEU B O    1 
ATOM   8166  C  CB   . LEU B 1 235 ? 22.370  -44.781 19.475  1.00 19.14  ? 253 LEU B CB   1 
ATOM   8167  C  CG   . LEU B 1 235 ? 23.408  -44.986 18.368  1.00 18.63  ? 253 LEU B CG   1 
ATOM   8168  C  CD1  . LEU B 1 235 ? 22.921  -44.345 17.071  1.00 18.24  ? 253 LEU B CD1  1 
ATOM   8169  C  CD2  . LEU B 1 235 ? 24.771  -44.423 18.763  1.00 18.75  ? 253 LEU B CD2  1 
ATOM   8170  H  H    . LEU B 1 235 ? 20.568  -44.984 21.150  1.00 22.53  ? 253 LEU B H    1 
ATOM   8171  H  HA   . LEU B 1 235 ? 20.596  -45.178 18.498  1.00 22.25  ? 253 LEU B HA   1 
ATOM   8172  H  HB2  . LEU B 1 235 ? 22.198  -43.828 19.527  1.00 22.96  ? 253 LEU B HB2  1 
ATOM   8173  H  HB3  . LEU B 1 235 ? 22.772  -45.091 20.301  1.00 22.96  ? 253 LEU B HB3  1 
ATOM   8174  H  HG   . LEU B 1 235 ? 23.523  -45.939 18.225  1.00 22.35  ? 253 LEU B HG   1 
ATOM   8175  H  HD11 . LEU B 1 235 ? 23.600  -44.459 16.388  1.00 21.89  ? 253 LEU B HD11 1 
ATOM   8176  H  HD12 . LEU B 1 235 ? 22.098  -44.778 16.795  1.00 21.89  ? 253 LEU B HD12 1 
ATOM   8177  H  HD13 . LEU B 1 235 ? 22.762  -43.401 17.226  1.00 21.89  ? 253 LEU B HD13 1 
ATOM   8178  H  HD21 . LEU B 1 235 ? 25.050  -44.827 19.599  1.00 22.50  ? 253 LEU B HD21 1 
ATOM   8179  H  HD22 . LEU B 1 235 ? 25.412  -44.630 18.066  1.00 22.50  ? 253 LEU B HD22 1 
ATOM   8180  H  HD23 . LEU B 1 235 ? 24.696  -43.462 18.869  1.00 22.50  ? 253 LEU B HD23 1 
ATOM   8181  N  N    . THR B 1 236 ? 21.458  -47.691 20.297  1.00 19.34  ? 254 THR B N    1 
ATOM   8182  C  CA   . THR B 1 236 ? 22.089  -49.003 20.288  1.00 19.57  ? 254 THR B CA   1 
ATOM   8183  C  C    . THR B 1 236 ? 21.128  -50.182 20.389  1.00 19.23  ? 254 THR B C    1 
ATOM   8184  O  O    . THR B 1 236 ? 21.564  -51.317 20.174  1.00 20.54  ? 254 THR B O    1 
ATOM   8185  C  CB   . THR B 1 236 ? 23.077  -49.114 21.456  1.00 21.33  ? 254 THR B CB   1 
ATOM   8186  O  OG1  . THR B 1 236 ? 22.348  -49.042 22.692  1.00 22.05  ? 254 THR B OG1  1 
ATOM   8187  C  CG2  . THR B 1 236 ? 24.114  -48.006 21.403  1.00 21.53  ? 254 THR B CG2  1 
ATOM   8188  H  H    . THR B 1 236 ? 21.211  -47.425 21.077  1.00 23.21  ? 254 THR B H    1 
ATOM   8189  H  HA   . THR B 1 236 ? 22.560  -49.082 19.444  1.00 23.48  ? 254 THR B HA   1 
ATOM   8190  H  HB   . THR B 1 236 ? 23.552  -49.958 21.404  1.00 25.59  ? 254 THR B HB   1 
ATOM   8191  H  HG1  . THR B 1 236 ? 22.064  -48.261 22.813  1.00 26.46  ? 254 THR B HG1  1 
ATOM   8192  H  HG21 . THR B 1 236 ? 23.689  -47.147 21.548  1.00 25.83  ? 254 THR B HG21 1 
ATOM   8193  H  HG22 . THR B 1 236 ? 24.784  -48.146 22.091  1.00 25.83  ? 254 THR B HG22 1 
ATOM   8194  H  HG23 . THR B 1 236 ? 24.549  -48.001 20.536  1.00 25.83  ? 254 THR B HG23 1 
ATOM   8195  N  N    . SER B 1 237 ? 19.855  -49.964 20.716  1.00 20.33  ? 255 SER B N    1 
ATOM   8196  C  CA   . SER B 1 237 ? 18.981  -51.083 21.055  1.00 20.32  ? 255 SER B CA   1 
ATOM   8197  C  C    . SER B 1 237 ? 18.612  -51.911 19.824  1.00 20.19  ? 255 SER B C    1 
ATOM   8198  O  O    . SER B 1 237 ? 18.737  -51.478 18.677  1.00 20.25  ? 255 SER B O    1 
ATOM   8199  C  CB   . SER B 1 237 ? 17.697  -50.590 21.729  1.00 21.89  ? 255 SER B CB   1 
ATOM   8200  O  OG   . SER B 1 237 ? 16.791  -50.017 20.799  1.00 21.93  ? 255 SER B OG   1 
ATOM   8201  H  H    . SER B 1 237 ? 19.480  -49.191 20.748  1.00 24.39  ? 255 SER B H    1 
ATOM   8202  H  HA   . SER B 1 237 ? 19.459  -51.657 21.673  1.00 24.38  ? 255 SER B HA   1 
ATOM   8203  H  HB2  . SER B 1 237 ? 17.264  -51.343 22.160  1.00 26.27  ? 255 SER B HB2  1 
ATOM   8204  H  HB3  . SER B 1 237 ? 17.930  -49.919 22.389  1.00 26.27  ? 255 SER B HB3  1 
ATOM   8205  H  HG   . SER B 1 237 ? 16.114  -49.725 21.201  1.00 26.31  ? 255 SER B HG   1 
ATOM   8206  N  N    . GLN B 1 238 ? 18.161  -53.141 20.081  1.00 20.47  ? 256 GLN B N    1 
ATOM   8207  C  CA   . GLN B 1 238 ? 17.677  -53.972 18.982  1.00 20.38  ? 256 GLN B CA   1 
ATOM   8208  C  C    . GLN B 1 238 ? 16.486  -53.315 18.291  1.00 20.34  ? 256 GLN B C    1 
ATOM   8209  O  O    . GLN B 1 238 ? 16.376  -53.349 17.057  1.00 20.32  ? 256 GLN B O    1 
ATOM   8210  C  CB   . GLN B 1 238 ? 17.335  -55.372 19.494  1.00 22.26  ? 256 GLN B CB   1 
ATOM   8211  C  CG   . GLN B 1 238 ? 16.608  -56.259 18.488  1.00 22.38  ? 256 GLN B CG   1 
ATOM   8212  C  CD   . GLN B 1 238 ? 17.444  -56.585 17.259  1.00 23.09  ? 256 GLN B CD   1 
ATOM   8213  O  OE1  . GLN B 1 238 ? 18.663  -56.415 17.257  1.00 23.03  ? 256 GLN B OE1  1 
ATOM   8214  N  NE2  . GLN B 1 238 ? 16.783  -57.054 16.199  1.00 23.65  ? 256 GLN B NE2  1 
ATOM   8215  H  H    . GLN B 1 238 ? 18.127  -53.506 20.858  1.00 24.57  ? 256 GLN B H    1 
ATOM   8216  H  HA   . GLN B 1 238 ? 18.378  -54.075 18.320  1.00 24.46  ? 256 GLN B HA   1 
ATOM   8217  H  HB2  . GLN B 1 238 ? 18.159  -55.821 19.738  1.00 26.71  ? 256 GLN B HB2  1 
ATOM   8218  H  HB3  . GLN B 1 238 ? 16.762  -55.283 20.273  1.00 26.71  ? 256 GLN B HB3  1 
ATOM   8219  H  HG2  . GLN B 1 238 ? 16.374  -57.096 18.919  1.00 26.85  ? 256 GLN B HG2  1 
ATOM   8220  H  HG3  . GLN B 1 238 ? 15.806  -55.803 18.189  1.00 26.85  ? 256 GLN B HG3  1 
ATOM   8221  H  HE21 . GLN B 1 238 ? 15.930  -57.157 16.235  1.00 28.38  ? 256 GLN B HE21 1 
ATOM   8222  H  HE22 . GLN B 1 238 ? 17.210  -57.253 15.479  1.00 28.38  ? 256 GLN B HE22 1 
ATOM   8223  N  N    . PHE B 1 239 ? 15.583  -52.708 19.062  1.00 20.77  ? 257 PHE B N    1 
ATOM   8224  C  CA   . PHE B 1 239 ? 14.467  -52.004 18.441  1.00 21.49  ? 257 PHE B CA   1 
ATOM   8225  C  C    . PHE B 1 239 ? 14.980  -50.905 17.521  1.00 19.94  ? 257 PHE B C    1 
ATOM   8226  O  O    . PHE B 1 239 ? 14.525  -50.761 16.381  1.00 20.30  ? 257 PHE B O    1 
ATOM   8227  C  CB   . PHE B 1 239 ? 13.549  -51.403 19.500  1.00 23.21  ? 257 PHE B CB   1 
ATOM   8228  C  CG   . PHE B 1 239 ? 12.353  -50.714 18.920  1.00 24.14  ? 257 PHE B CG   1 
ATOM   8229  C  CD1  . PHE B 1 239 ? 11.350  -51.450 18.307  1.00 25.14  ? 257 PHE B CD1  1 
ATOM   8230  C  CD2  . PHE B 1 239 ? 12.237  -49.336 18.961  1.00 24.55  ? 257 PHE B CD2  1 
ATOM   8231  C  CE1  . PHE B 1 239 ? 10.248  -50.824 17.758  1.00 25.51  ? 257 PHE B CE1  1 
ATOM   8232  C  CE2  . PHE B 1 239 ? 11.138  -48.710 18.412  1.00 24.76  ? 257 PHE B CE2  1 
ATOM   8233  C  CZ   . PHE B 1 239 ? 10.142  -49.455 17.809  1.00 25.50  ? 257 PHE B CZ   1 
ATOM   8234  H  H    . PHE B 1 239 ? 15.594  -52.690 19.922  1.00 24.93  ? 257 PHE B H    1 
ATOM   8235  H  HA   . PHE B 1 239 ? 13.950  -52.642 17.925  1.00 25.78  ? 257 PHE B HA   1 
ATOM   8236  H  HB2  . PHE B 1 239 ? 13.232  -52.113 20.080  1.00 27.85  ? 257 PHE B HB2  1 
ATOM   8237  H  HB3  . PHE B 1 239 ? 14.048  -50.751 20.016  1.00 27.85  ? 257 PHE B HB3  1 
ATOM   8238  H  HD1  . PHE B 1 239 ? 11.420  -52.377 18.266  1.00 30.17  ? 257 PHE B HD1  1 
ATOM   8239  H  HD2  . PHE B 1 239 ? 12.905  -48.829 19.362  1.00 29.45  ? 257 PHE B HD2  1 
ATOM   8240  H  HE1  . PHE B 1 239 ? 9.579   -51.329 17.355  1.00 30.62  ? 257 PHE B HE1  1 
ATOM   8241  H  HE2  . PHE B 1 239 ? 11.066  -47.783 18.448  1.00 29.72  ? 257 PHE B HE2  1 
ATOM   8242  H  HZ   . PHE B 1 239 ? 9.402   -49.031 17.438  1.00 30.60  ? 257 PHE B HZ   1 
ATOM   8243  N  N    . SER B 1 240 ? 15.947  -50.127 18.009  1.00 19.59  ? 258 SER B N    1 
ATOM   8244  C  CA   . SER B 1 240 ? 16.550  -49.079 17.196  1.00 18.77  ? 258 SER B CA   1 
ATOM   8245  C  C    . SER B 1 240 ? 17.150  -49.642 15.916  1.00 19.01  ? 258 SER B C    1 
ATOM   8246  O  O    . SER B 1 240 ? 17.049  -49.020 14.850  1.00 19.68  ? 258 SER B O    1 
ATOM   8247  C  CB   . SER B 1 240 ? 17.617  -48.365 18.024  1.00 20.26  ? 258 SER B CB   1 
ATOM   8248  O  OG   . SER B 1 240 ? 17.050  -47.815 19.202  1.00 20.50  ? 258 SER B OG   1 
ATOM   8249  H  H    . SER B 1 240 ? 16.269  -50.187 18.804  1.00 23.50  ? 258 SER B H    1 
ATOM   8250  H  HA   . SER B 1 240 ? 15.870  -48.437 16.939  1.00 22.52  ? 258 SER B HA   1 
ATOM   8251  H  HB2  . SER B 1 240 ? 18.304  -49.003 18.272  1.00 24.32  ? 258 SER B HB2  1 
ATOM   8252  H  HB3  . SER B 1 240 ? 18.002  -47.650 17.495  1.00 24.32  ? 258 SER B HB3  1 
ATOM   8253  H  HG   . SER B 1 240 ? 16.659  -48.416 19.640  1.00 24.60  ? 258 SER B HG   1 
ATOM   8254  N  N    . TYR B 1 241 ? 17.781  -50.820 15.998  1.00 19.53  ? 259 TYR B N    1 
ATOM   8255  C  CA   . TYR B 1 241 ? 18.365  -51.426 14.806  1.00 21.22  ? 259 TYR B CA   1 
ATOM   8256  C  C    . TYR B 1 241 ? 17.291  -51.774 13.779  1.00 21.25  ? 259 TYR B C    1 
ATOM   8257  O  O    . TYR B 1 241 ? 17.453  -51.508 12.580  1.00 19.83  ? 259 TYR B O    1 
ATOM   8258  C  CB   . TYR B 1 241 ? 19.175  -52.671 15.180  1.00 20.65  ? 259 TYR B CB   1 
ATOM   8259  C  CG   . TYR B 1 241 ? 19.597  -53.458 13.963  1.00 21.55  ? 259 TYR B CG   1 
ATOM   8260  C  CD1  . TYR B 1 241 ? 20.552  -52.955 13.091  1.00 22.78  ? 259 TYR B CD1  1 
ATOM   8261  C  CD2  . TYR B 1 241 ? 19.011  -54.679 13.663  1.00 23.77  ? 259 TYR B CD2  1 
ATOM   8262  C  CE1  . TYR B 1 241 ? 20.928  -53.647 11.963  1.00 25.01  ? 259 TYR B CE1  1 
ATOM   8263  C  CE2  . TYR B 1 241 ? 19.381  -55.387 12.535  1.00 24.25  ? 259 TYR B CE2  1 
ATOM   8264  C  CZ   . TYR B 1 241 ? 20.341  -54.865 11.689  1.00 24.92  ? 259 TYR B CZ   1 
ATOM   8265  O  OH   . TYR B 1 241 ? 20.710  -55.564 10.568  1.00 27.63  ? 259 TYR B OH   1 
ATOM   8266  H  H    . TYR B 1 241 ? 17.880  -51.277 16.720  1.00 23.43  ? 259 TYR B H    1 
ATOM   8267  H  HA   . TYR B 1 241 ? 18.973  -50.787 14.403  1.00 25.46  ? 259 TYR B HA   1 
ATOM   8268  H  HB2  . TYR B 1 241 ? 19.975  -52.399 15.657  1.00 24.78  ? 259 TYR B HB2  1 
ATOM   8269  H  HB3  . TYR B 1 241 ? 18.633  -53.247 15.741  1.00 24.78  ? 259 TYR B HB3  1 
ATOM   8270  H  HD1  . TYR B 1 241 ? 20.946  -52.132 13.273  1.00 27.33  ? 259 TYR B HD1  1 
ATOM   8271  H  HD2  . TYR B 1 241 ? 18.360  -55.027 14.228  1.00 28.53  ? 259 TYR B HD2  1 
ATOM   8272  H  HE1  . TYR B 1 241 ? 21.571  -53.297 11.391  1.00 30.01  ? 259 TYR B HE1  1 
ATOM   8273  H  HE2  . TYR B 1 241 ? 18.988  -56.209 12.347  1.00 29.10  ? 259 TYR B HE2  1 
ATOM   8274  H  HH   . TYR B 1 241 ? 21.298  -55.138 10.145  1.00 33.16  ? 259 TYR B HH   1 
ATOM   8275  N  N    . VAL B 1 242 ? 16.184  -52.373 14.222  1.00 21.81  ? 260 VAL B N    1 
ATOM   8276  C  CA   . VAL B 1 242 ? 15.130  -52.736 13.276  1.00 22.71  ? 260 VAL B CA   1 
ATOM   8277  C  C    . VAL B 1 242 ? 14.575  -51.492 12.587  1.00 22.65  ? 260 VAL B C    1 
ATOM   8278  O  O    . VAL B 1 242 ? 14.341  -51.487 11.371  1.00 22.38  ? 260 VAL B O    1 
ATOM   8279  C  CB   . VAL B 1 242 ? 14.034  -53.556 13.982  1.00 23.80  ? 260 VAL B CB   1 
ATOM   8280  C  CG1  . VAL B 1 242 ? 12.902  -53.872 13.020  1.00 25.57  ? 260 VAL B CG1  1 
ATOM   8281  C  CG2  . VAL B 1 242 ? 14.609  -54.846 14.547  1.00 24.34  ? 260 VAL B CG2  1 
ATOM   8282  H  H    . VAL B 1 242 ? 16.024  -52.574 15.043  1.00 26.17  ? 260 VAL B H    1 
ATOM   8283  H  HA   . VAL B 1 242 ? 15.514  -53.300 12.586  1.00 27.25  ? 260 VAL B HA   1 
ATOM   8284  H  HB   . VAL B 1 242 ? 13.679  -53.028 14.715  1.00 28.56  ? 260 VAL B HB   1 
ATOM   8285  H  HG11 . VAL B 1 242 ? 12.247  -54.426 13.473  1.00 30.69  ? 260 VAL B HG11 1 
ATOM   8286  H  HG12 . VAL B 1 242 ? 12.491  -53.043 12.731  1.00 30.69  ? 260 VAL B HG12 1 
ATOM   8287  H  HG13 . VAL B 1 242 ? 13.262  -54.347 12.254  1.00 30.69  ? 260 VAL B HG13 1 
ATOM   8288  H  HG21 . VAL B 1 242 ? 13.890  -55.369 14.934  1.00 29.21  ? 260 VAL B HG21 1 
ATOM   8289  H  HG22 . VAL B 1 242 ? 15.031  -55.344 13.830  1.00 29.21  ? 260 VAL B HG22 1 
ATOM   8290  H  HG23 . VAL B 1 242 ? 15.264  -54.628 15.228  1.00 29.21  ? 260 VAL B HG23 1 
ATOM   8291  N  N    . VAL B 1 243 ? 14.355  -50.418 13.347  1.00 21.83  ? 261 VAL B N    1 
ATOM   8292  C  CA   . VAL B 1 243 ? 13.844  -49.189 12.743  1.00 21.60  ? 261 VAL B CA   1 
ATOM   8293  C  C    . VAL B 1 243 ? 14.858  -48.606 11.768  1.00 20.63  ? 261 VAL B C    1 
ATOM   8294  O  O    . VAL B 1 243 ? 14.503  -48.174 10.663  1.00 21.27  ? 261 VAL B O    1 
ATOM   8295  C  CB   . VAL B 1 243 ? 13.451  -48.175 13.834  1.00 21.10  ? 261 VAL B CB   1 
ATOM   8296  C  CG1  . VAL B 1 243 ? 13.083  -46.823 13.212  1.00 22.01  ? 261 VAL B CG1  1 
ATOM   8297  C  CG2  . VAL B 1 243 ? 12.309  -48.744 14.675  1.00 21.55  ? 261 VAL B CG2  1 
ATOM   8298  H  H    . VAL B 1 243 ? 14.491  -50.375 14.195  1.00 26.19  ? 261 VAL B H    1 
ATOM   8299  H  HA   . VAL B 1 243 ? 13.043  -49.407 12.240  1.00 25.92  ? 261 VAL B HA   1 
ATOM   8300  H  HB   . VAL B 1 243 ? 14.206  -48.017 14.422  1.00 25.32  ? 261 VAL B HB   1 
ATOM   8301  H  HG11 . VAL B 1 243 ? 12.614  -46.977 12.377  1.00 26.41  ? 261 VAL B HG11 1 
ATOM   8302  H  HG12 . VAL B 1 243 ? 12.513  -46.337 13.828  1.00 26.41  ? 261 VAL B HG12 1 
ATOM   8303  H  HG13 . VAL B 1 243 ? 13.896  -46.320 13.047  1.00 26.41  ? 261 VAL B HG13 1 
ATOM   8304  H  HG21 . VAL B 1 243 ? 12.142  -49.660 14.403  1.00 25.86  ? 261 VAL B HG21 1 
ATOM   8305  H  HG22 . VAL B 1 243 ? 12.562  -48.717 15.611  1.00 25.86  ? 261 VAL B HG22 1 
ATOM   8306  H  HG23 . VAL B 1 243 ? 11.513  -48.207 14.532  1.00 25.86  ? 261 VAL B HG23 1 
ATOM   8307  N  N    . GLY B 1 244 ? 16.131  -48.567 12.163  1.00 19.43  ? 262 GLY B N    1 
ATOM   8308  C  CA   . GLY B 1 244 ? 17.143  -48.003 11.288  1.00 19.25  ? 262 GLY B CA   1 
ATOM   8309  C  C    . GLY B 1 244 ? 17.324  -48.821 10.027  1.00 19.71  ? 262 GLY B C    1 
ATOM   8310  O  O    . GLY B 1 244 ? 17.480  -48.271 8.933   1.00 19.15  ? 262 GLY B O    1 
ATOM   8311  H  H    . GLY B 1 244 ? 16.424  -48.855 12.919  1.00 23.31  ? 262 GLY B H    1 
ATOM   8312  H  HA2  . GLY B 1 244 ? 16.885  -47.102 11.035  1.00 23.10  ? 262 GLY B HA2  1 
ATOM   8313  H  HA3  . GLY B 1 244 ? 17.992  -47.968 11.756  1.00 23.10  ? 262 GLY B HA3  1 
ATOM   8314  N  N    . ARG B 1 245 ? 17.288  -50.145 10.160  1.00 21.57  ? 263 ARG B N    1 
ATOM   8315  C  CA   . ARG B 1 245 ? 17.353  -51.013 8.992   1.00 22.37  ? 263 ARG B CA   1 
ATOM   8316  C  C    . ARG B 1 245 ? 16.187  -50.744 8.052   1.00 21.63  ? 263 ARG B C    1 
ATOM   8317  O  O    . ARG B 1 245 ? 16.364  -50.691 6.831   1.00 22.95  ? 263 ARG B O    1 
ATOM   8318  C  CB   . ARG B 1 245 ? 17.372  -52.469 9.448   1.00 23.63  ? 263 ARG B CB   1 
ATOM   8319  C  CG   . ARG B 1 245 ? 17.467  -53.466 8.312   1.00 24.72  ? 263 ARG B CG   1 
ATOM   8320  C  CD   . ARG B 1 245 ? 17.487  -54.894 8.845   1.00 26.56  ? 263 ARG B CD   1 
ATOM   8321  N  NE   . ARG B 1 245 ? 16.189  -55.283 9.388   1.00 28.75  ? 263 ARG B NE   1 
ATOM   8322  C  CZ   . ARG B 1 245 ? 15.964  -56.407 10.062  1.00 31.30  ? 263 ARG B CZ   1 
ATOM   8323  N  NH1  . ARG B 1 245 ? 16.954  -57.258 10.289  1.00 32.14  ? 263 ARG B NH1  1 
ATOM   8324  N  NH2  . ARG B 1 245 ? 14.748  -56.678 10.516  1.00 32.83  ? 263 ARG B NH2  1 
ATOM   8325  H  H    . ARG B 1 245 ? 17.228  -50.562 10.910  1.00 25.88  ? 263 ARG B H    1 
ATOM   8326  H  HA   . ARG B 1 245 ? 18.172  -50.843 8.500   1.00 26.84  ? 263 ARG B HA   1 
ATOM   8327  H  HB2  . ARG B 1 245 ? 18.140  -52.605 10.025  1.00 28.36  ? 263 ARG B HB2  1 
ATOM   8328  H  HB3  . ARG B 1 245 ? 16.554  -52.654 9.936   1.00 28.36  ? 263 ARG B HB3  1 
ATOM   8329  H  HG2  . ARG B 1 245 ? 16.698  -53.366 7.729   1.00 29.66  ? 263 ARG B HG2  1 
ATOM   8330  H  HG3  . ARG B 1 245 ? 18.284  -53.312 7.813   1.00 29.66  ? 263 ARG B HG3  1 
ATOM   8331  H  HD2  . ARG B 1 245 ? 17.711  -55.503 8.124   1.00 31.87  ? 263 ARG B HD2  1 
ATOM   8332  H  HD3  . ARG B 1 245 ? 18.147  -54.962 9.553   1.00 31.87  ? 263 ARG B HD3  1 
ATOM   8333  H  HE   . ARG B 1 245 ? 15.526  -54.750 9.263   1.00 34.50  ? 263 ARG B HE   1 
ATOM   8334  H  HH11 . ARG B 1 245 ? 17.745  -57.084 9.999   1.00 38.56  ? 263 ARG B HH11 1 
ATOM   8335  H  HH12 . ARG B 1 245 ? 16.805  -57.984 10.725  1.00 38.56  ? 263 ARG B HH12 1 
ATOM   8336  H  HH21 . ARG B 1 245 ? 14.103  -56.127 10.374  1.00 39.40  ? 263 ARG B HH21 1 
ATOM   8337  H  HH22 . ARG B 1 245 ? 14.604  -57.406 10.952  1.00 39.40  ? 263 ARG B HH22 1 
ATOM   8338  N  N    . SER B 1 246 ? 14.988  -50.557 8.608   1.00 22.22  ? 264 SER B N    1 
ATOM   8339  C  CA   . SER B 1 246 ? 13.833  -50.206 7.788   1.00 21.80  ? 264 SER B CA   1 
ATOM   8340  C  C    . SER B 1 246 ? 14.078  -48.908 7.031   1.00 20.88  ? 264 SER B C    1 
ATOM   8341  O  O    . SER B 1 246 ? 13.821  -48.814 5.824   1.00 21.96  ? 264 SER B O    1 
ATOM   8342  C  CB   . SER B 1 246 ? 12.600  -50.056 8.679   1.00 23.50  ? 264 SER B CB   1 
ATOM   8343  O  OG   . SER B 1 246 ? 11.469  -49.704 7.899   1.00 23.70  ? 264 SER B OG   1 
ATOM   8344  H  H    . SER B 1 246 ? 14.820  -50.626 9.448   1.00 26.66  ? 264 SER B H    1 
ATOM   8345  H  HA   . SER B 1 246 ? 13.677  -50.917 7.146   1.00 26.16  ? 264 SER B HA   1 
ATOM   8346  H  HB2  . SER B 1 246 ? 12.427  -50.899 9.127   1.00 28.20  ? 264 SER B HB2  1 
ATOM   8347  H  HB3  . SER B 1 246 ? 12.764  -49.360 9.334   1.00 28.20  ? 264 SER B HB3  1 
ATOM   8348  H  HG   . SER B 1 246 ? 11.234  -50.355 7.424   1.00 28.44  ? 264 SER B HG   1 
ATOM   8349  N  N    . ALA B 1 247 ? 14.568  -47.884 7.729   1.00 19.93  ? 265 ALA B N    1 
ATOM   8350  C  CA   . ALA B 1 247 ? 14.794  -46.597 7.090   1.00 19.73  ? 265 ALA B CA   1 
ATOM   8351  C  C    . ALA B 1 247 ? 15.826  -46.702 5.975   1.00 20.15  ? 265 ALA B C    1 
ATOM   8352  O  O    . ALA B 1 247 ? 15.655  -46.106 4.905   1.00 22.00  ? 265 ALA B O    1 
ATOM   8353  C  CB   . ALA B 1 247 ? 15.245  -45.581 8.137   1.00 18.92  ? 265 ALA B CB   1 
ATOM   8354  H  H    . ALA B 1 247 ? 14.774  -47.911 8.564   1.00 23.92  ? 265 ALA B H    1 
ATOM   8355  H  HA   . ALA B 1 247 ? 13.963  -46.289 6.696   1.00 23.68  ? 265 ALA B HA   1 
ATOM   8356  H  HB1  . ALA B 1 247 ? 15.378  -44.722 7.708   1.00 22.71  ? 265 ALA B HB1  1 
ATOM   8357  H  HB2  . ALA B 1 247 ? 14.561  -45.507 8.821   1.00 22.71  ? 265 ALA B HB2  1 
ATOM   8358  H  HB3  . ALA B 1 247 ? 16.077  -45.885 8.534   1.00 22.71  ? 265 ALA B HB3  1 
ATOM   8359  N  N    . LEU B 1 248 ? 16.911  -47.446 6.210   1.00 20.68  ? 266 LEU B N    1 
ATOM   8360  C  CA   . LEU B 1 248 ? 17.987  -47.509 5.222   1.00 22.20  ? 266 LEU B CA   1 
ATOM   8361  C  C    . LEU B 1 248 ? 17.573  -48.272 3.969   1.00 24.04  ? 266 LEU B C    1 
ATOM   8362  O  O    . LEU B 1 248 ? 18.073  -47.982 2.875   1.00 24.05  ? 266 LEU B O    1 
ATOM   8363  C  CB   . LEU B 1 248 ? 19.232  -48.144 5.840   1.00 21.96  ? 266 LEU B CB   1 
ATOM   8364  C  CG   . LEU B 1 248 ? 19.896  -47.307 6.935   1.00 21.76  ? 266 LEU B CG   1 
ATOM   8365  C  CD1  . LEU B 1 248 ? 21.004  -48.083 7.634   1.00 22.23  ? 266 LEU B CD1  1 
ATOM   8366  C  CD2  . LEU B 1 248 ? 20.430  -45.986 6.363   1.00 23.07  ? 266 LEU B CD2  1 
ATOM   8367  H  H    . LEU B 1 248 ? 17.046  -47.915 6.919   1.00 24.82  ? 266 LEU B H    1 
ATOM   8368  H  HA   . LEU B 1 248 ? 18.209  -46.603 4.956   1.00 26.64  ? 266 LEU B HA   1 
ATOM   8369  H  HB2  . LEU B 1 248 ? 18.982  -48.995 6.232   1.00 26.35  ? 266 LEU B HB2  1 
ATOM   8370  H  HB3  . LEU B 1 248 ? 19.888  -48.282 5.138   1.00 26.35  ? 266 LEU B HB3  1 
ATOM   8371  H  HG   . LEU B 1 248 ? 19.226  -47.094 7.604   1.00 26.11  ? 266 LEU B HG   1 
ATOM   8372  H  HD11 . LEU B 1 248 ? 20.696  -48.986 7.806   1.00 26.67  ? 266 LEU B HD11 1 
ATOM   8373  H  HD12 . LEU B 1 248 ? 21.785  -48.103 7.060   1.00 26.67  ? 266 LEU B HD12 1 
ATOM   8374  H  HD13 . LEU B 1 248 ? 21.219  -47.642 8.470   1.00 26.67  ? 266 LEU B HD13 1 
ATOM   8375  H  HD21 . LEU B 1 248 ? 20.962  -45.540 7.041   1.00 27.68  ? 266 LEU B HD21 1 
ATOM   8376  H  HD22 . LEU B 1 248 ? 20.978  -46.177 5.586   1.00 27.68  ? 266 LEU B HD22 1 
ATOM   8377  H  HD23 . LEU B 1 248 ? 19.680  -45.425 6.110   1.00 27.68  ? 266 LEU B HD23 1 
ATOM   8378  N  N    . ARG B 1 249 ? 16.661  -49.233 4.098   1.00 25.20  ? 267 ARG B N    1 
ATOM   8379  C  CA   . ARG B 1 249 ? 16.237  -50.029 2.954   1.00 28.82  ? 267 ARG B CA   1 
ATOM   8380  C  C    . ARG B 1 249 ? 15.014  -49.470 2.239   1.00 29.05  ? 267 ARG B C    1 
ATOM   8381  O  O    . ARG B 1 249 ? 14.744  -49.878 1.104   1.00 30.73  ? 267 ARG B O    1 
ATOM   8382  C  CB   . ARG B 1 249 ? 15.912  -51.459 3.397   1.00 31.58  ? 267 ARG B CB   1 
ATOM   8383  C  CG   . ARG B 1 249 ? 17.084  -52.207 4.011   1.00 35.53  ? 267 ARG B CG   1 
ATOM   8384  C  CD   . ARG B 1 249 ? 16.653  -53.579 4.496   1.00 38.93  ? 267 ARG B CD   1 
ATOM   8385  N  NE   . ARG B 1 249 ? 17.785  -54.450 4.802   1.00 40.65  ? 267 ARG B NE   1 
ATOM   8386  C  CZ   . ARG B 1 249 ? 17.669  -55.634 5.397   1.00 43.90  ? 267 ARG B CZ   1 
ATOM   8387  N  NH1  . ARG B 1 249 ? 16.470  -56.082 5.753   1.00 44.21  ? 267 ARG B NH1  1 
ATOM   8388  N  NH2  . ARG B 1 249 ? 18.749  -56.370 5.635   1.00 45.42  ? 267 ARG B NH2  1 
ATOM   8389  H  H    . ARG B 1 249 ? 16.275  -49.442 4.838   1.00 30.24  ? 267 ARG B H    1 
ATOM   8390  H  HA   . ARG B 1 249 ? 16.972  -50.052 2.321   1.00 34.58  ? 267 ARG B HA   1 
ATOM   8391  H  HB2  . ARG B 1 249 ? 15.206  -51.425 4.061   1.00 37.90  ? 267 ARG B HB2  1 
ATOM   8392  H  HB3  . ARG B 1 249 ? 15.616  -51.963 2.624   1.00 37.90  ? 267 ARG B HB3  1 
ATOM   8393  H  HG2  . ARG B 1 249 ? 17.781  -52.320 3.346   1.00 42.64  ? 267 ARG B HG2  1 
ATOM   8394  H  HG3  . ARG B 1 249 ? 17.427  -51.707 4.769   1.00 42.64  ? 267 ARG B HG3  1 
ATOM   8395  H  HD2  . ARG B 1 249 ? 16.125  -53.478 5.303   1.00 46.71  ? 267 ARG B HD2  1 
ATOM   8396  H  HD3  . ARG B 1 249 ? 16.124  -54.007 3.804   1.00 46.71  ? 267 ARG B HD3  1 
ATOM   8397  H  HE   . ARG B 1 249 ? 18.572  -54.181 4.585   1.00 48.77  ? 267 ARG B HE   1 
ATOM   8398  H  HH11 . ARG B 1 249 ? 15.770  -55.607 5.599   1.00 53.05  ? 267 ARG B HH11 1 
ATOM   8399  H  HH12 . ARG B 1 249 ? 16.394  -56.848 6.137   1.00 53.05  ? 267 ARG B HH12 1 
ATOM   8400  H  HH21 . ARG B 1 249 ? 19.526  -56.081 5.405   1.00 54.51  ? 267 ARG B HH21 1 
ATOM   8401  H  HH22 . ARG B 1 249 ? 18.671  -57.135 6.020   1.00 54.51  ? 267 ARG B HH22 1 
ATOM   8402  N  N    . SER B 1 250 ? 14.271  -48.560 2.860   1.00 27.27  ? 268 SER B N    1 
ATOM   8403  C  CA   . SER B 1 250 ? 12.980  -48.158 2.316   1.00 27.09  ? 268 SER B CA   1 
ATOM   8404  C  C    . SER B 1 250 ? 13.127  -47.371 1.017   1.00 28.09  ? 268 SER B C    1 
ATOM   8405  O  O    . SER B 1 250 ? 13.973  -46.480 0.898   1.00 28.40  ? 268 SER B O    1 
ATOM   8406  C  CB   . SER B 1 250 ? 12.226  -47.310 3.339   1.00 28.08  ? 268 SER B CB   1 
ATOM   8407  O  OG   . SER B 1 250 ? 11.079  -46.718 2.756   1.00 28.37  ? 268 SER B OG   1 
ATOM   8408  H  H    . SER B 1 250 ? 14.490  -48.163 3.591   1.00 32.72  ? 268 SER B H    1 
ATOM   8409  H  HA   . SER B 1 250 ? 12.468  -48.959 2.118   1.00 32.51  ? 268 SER B HA   1 
ATOM   8410  H  HB2  . SER B 1 250 ? 11.949  -47.877 4.076   1.00 33.70  ? 268 SER B HB2  1 
ATOM   8411  H  HB3  . SER B 1 250 ? 12.813  -46.609 3.662   1.00 33.70  ? 268 SER B HB3  1 
ATOM   8412  H  HG   . SER B 1 250 ? 10.588  -47.311 2.420   1.00 34.04  ? 268 SER B HG   1 
ATOM   8413  N  N    . THR B 1 251 ? 12.274  -47.700 0.039   1.00 29.76  ? 269 THR B N    1 
ATOM   8414  C  CA   . THR B 1 251 ? 12.237  -46.925 -1.195  1.00 31.57  ? 269 THR B CA   1 
ATOM   8415  C  C    . THR B 1 251 ? 11.781  -45.487 -0.957  1.00 31.70  ? 269 THR B C    1 
ATOM   8416  O  O    . THR B 1 251 ? 12.061  -44.613 -1.786  1.00 34.17  ? 269 THR B O    1 
ATOM   8417  C  CB   . THR B 1 251 ? 11.319  -47.601 -2.221  1.00 33.71  ? 269 THR B CB   1 
ATOM   8418  O  OG1  . THR B 1 251 ? 9.981   -47.661 -1.712  1.00 34.67  ? 269 THR B OG1  1 
ATOM   8419  C  CG2  . THR B 1 251 ? 11.796  -49.016 -2.533  1.00 35.15  ? 269 THR B CG2  1 
ATOM   8420  H  H    . THR B 1 251 ? 11.719  -48.356 0.068   1.00 35.71  ? 269 THR B H    1 
ATOM   8421  H  HA   . THR B 1 251 ? 13.131  -46.898 -1.571  1.00 37.88  ? 269 THR B HA   1 
ATOM   8422  H  HB   . THR B 1 251 ? 11.334  -47.085 -3.043  1.00 40.45  ? 269 THR B HB   1 
ATOM   8423  H  HG1  . THR B 1 251 ? 9.683   -46.885 -1.596  1.00 41.60  ? 269 THR B HG1  1 
ATOM   8424  H  HG21 . THR B 1 251 ? 11.237  -49.410 -3.221  1.00 42.18  ? 269 THR B HG21 1 
ATOM   8425  H  HG22 . THR B 1 251 ? 12.714  -48.995 -2.846  1.00 42.18  ? 269 THR B HG22 1 
ATOM   8426  H  HG23 . THR B 1 251 ? 11.748  -49.565 -1.735  1.00 42.18  ? 269 THR B HG23 1 
ATOM   8427  N  N    . THR B 1 252 ? 11.084  -45.222 0.149   1.00 30.36  ? 270 THR B N    1 
ATOM   8428  C  CA   . THR B 1 252 ? 10.617  -43.881 0.479   1.00 30.96  ? 270 THR B CA   1 
ATOM   8429  C  C    . THR B 1 252 ? 11.645  -43.059 1.243   1.00 29.41  ? 270 THR B C    1 
ATOM   8430  O  O    . THR B 1 252 ? 11.421  -41.861 1.462   1.00 28.41  ? 270 THR B O    1 
ATOM   8431  C  CB   . THR B 1 252 ? 9.355   -43.967 1.347   1.00 33.21  ? 270 THR B CB   1 
ATOM   8432  O  OG1  . THR B 1 252 ? 9.706   -44.414 2.667   1.00 33.55  ? 270 THR B OG1  1 
ATOM   8433  C  CG2  . THR B 1 252 ? 8.347   -44.920 0.732   1.00 33.58  ? 270 THR B CG2  1 
ATOM   8434  H  H    . THR B 1 252 ? 10.866  -45.815 0.733   1.00 36.44  ? 270 THR B H    1 
ATOM   8435  H  HA   . THR B 1 252 ? 10.406  -43.425 -0.350  1.00 37.16  ? 270 THR B HA   1 
ATOM   8436  H  HB   . THR B 1 252 ? 8.941   -43.091 1.406   1.00 39.86  ? 270 THR B HB   1 
ATOM   8437  H  HG1  . THR B 1 252 ? 9.026   -44.417 3.160   1.00 40.26  ? 270 THR B HG1  1 
ATOM   8438  H  HG21 . THR B 1 252 ? 7.498   -44.849 1.195   1.00 40.29  ? 270 THR B HG21 1 
ATOM   8439  H  HG22 . THR B 1 252 ? 8.215   -44.704 -0.204  1.00 40.29  ? 270 THR B HG22 1 
ATOM   8440  H  HG23 . THR B 1 252 ? 8.669   -45.832 0.803   1.00 40.29  ? 270 THR B HG23 1 
ATOM   8441  N  N    . GLY B 1 253 ? 12.752  -43.665 1.657   1.00 27.16  ? 271 GLY B N    1 
ATOM   8442  C  CA   . GLY B 1 253 ? 13.731  -42.990 2.479   1.00 25.65  ? 271 GLY B CA   1 
ATOM   8443  C  C    . GLY B 1 253 ? 13.366  -42.873 3.941   1.00 24.21  ? 271 GLY B C    1 
ATOM   8444  O  O    . GLY B 1 253 ? 14.136  -42.280 4.702   1.00 24.25  ? 271 GLY B O    1 
ATOM   8445  H  H    . GLY B 1 253 ? 12.957  -44.479 1.468   1.00 32.60  ? 271 GLY B H    1 
ATOM   8446  H  HA2  . GLY B 1 253 ? 14.570  -43.474 2.422   1.00 30.78  ? 271 GLY B HA2  1 
ATOM   8447  H  HA3  . GLY B 1 253 ? 13.860  -42.093 2.134   1.00 30.78  ? 271 GLY B HA3  1 
ATOM   8448  N  N    . GLN B 1 254 ? 12.219  -43.410 4.358   1.00 24.49  ? 272 GLN B N    1 
ATOM   8449  C  CA   . GLN B 1 254 ? 11.810  -43.394 5.753   1.00 24.45  ? 272 GLN B CA   1 
ATOM   8450  C  C    . GLN B 1 254 ? 11.472  -44.806 6.203   1.00 24.63  ? 272 GLN B C    1 
ATOM   8451  O  O    . GLN B 1 254 ? 11.056  -45.642 5.397   1.00 25.69  ? 272 GLN B O    1 
ATOM   8452  C  CB   . GLN B 1 254 ? 10.560  -42.543 5.964   1.00 26.05  ? 272 GLN B CB   1 
ATOM   8453  C  CG   . GLN B 1 254 ? 10.714  -41.086 5.584   1.00 26.38  ? 272 GLN B CG   1 
ATOM   8454  C  CD   . GLN B 1 254 ? 9.434   -40.317 5.796   1.00 27.03  ? 272 GLN B CD   1 
ATOM   8455  O  OE1  . GLN B 1 254 ? 8.349   -40.791 5.456   1.00 29.11  ? 272 GLN B OE1  1 
ATOM   8456  N  NE2  . GLN B 1 254 ? 9.546   -39.131 6.366   1.00 25.91  ? 272 GLN B NE2  1 
ATOM   8457  H  H    . GLN B 1 254 ? 11.653  -43.796 3.838   1.00 29.39  ? 272 GLN B H    1 
ATOM   8458  H  HA   . GLN B 1 254 ? 12.542  -43.043 6.284   1.00 29.34  ? 272 GLN B HA   1 
ATOM   8459  H  HB2  . GLN B 1 254 ? 9.842   -42.911 5.425   1.00 31.26  ? 272 GLN B HB2  1 
ATOM   8460  H  HB3  . GLN B 1 254 ? 10.320  -42.575 6.903   1.00 31.26  ? 272 GLN B HB3  1 
ATOM   8461  H  HG2  . GLN B 1 254 ? 11.405  -40.683 6.132   1.00 31.65  ? 272 GLN B HG2  1 
ATOM   8462  H  HG3  . GLN B 1 254 ? 10.955  -41.023 4.646   1.00 31.65  ? 272 GLN B HG3  1 
ATOM   8463  H  HE21 . GLN B 1 254 ? 10.321  -38.835 6.595   1.00 31.09  ? 272 GLN B HE21 1 
ATOM   8464  H  HE22 . GLN B 1 254 ? 8.845   -38.654 6.508   1.00 31.09  ? 272 GLN B HE22 1 
ATOM   8465  N  N    . ALA B 1 255 ? 11.629  -45.057 7.502   1.00 24.09  ? 273 ALA B N    1 
ATOM   8466  C  CA   . ALA B 1 255 ? 11.226  -46.342 8.061   1.00 24.82  ? 273 ALA B CA   1 
ATOM   8467  C  C    . ALA B 1 255 ? 9.732   -46.561 7.846   1.00 25.39  ? 273 ALA B C    1 
ATOM   8468  O  O    . ALA B 1 255 ? 8.947   -45.610 7.787   1.00 25.58  ? 273 ALA B O    1 
ATOM   8469  C  CB   . ALA B 1 255 ? 11.523  -46.387 9.558   1.00 25.47  ? 273 ALA B CB   1 
ATOM   8470  H  H    . ALA B 1 255 ? 11.962  -44.507 8.073   1.00 28.90  ? 273 ALA B H    1 
ATOM   8471  H  HA   . ALA B 1 255 ? 11.721  -47.051 7.623   1.00 29.78  ? 273 ALA B HA   1 
ATOM   8472  H  HB1  . ALA B 1 255 ? 11.281  -47.262 9.902   1.00 30.56  ? 273 ALA B HB1  1 
ATOM   8473  H  HB2  . ALA B 1 255 ? 12.469  -46.227 9.698   1.00 30.56  ? 273 ALA B HB2  1 
ATOM   8474  H  HB3  . ALA B 1 255 ? 11.001  -45.702 10.005  1.00 30.56  ? 273 ALA B HB3  1 
ATOM   8475  N  N    . ARG B 1 256 ? 9.343   -47.834 7.740   1.00 27.30  ? 274 ARG B N    1 
ATOM   8476  C  CA   . ARG B 1 256 ? 7.965   -48.224 7.474   1.00 28.75  ? 274 ARG B CA   1 
ATOM   8477  C  C    . ARG B 1 256 ? 7.408   -49.024 8.645   1.00 28.13  ? 274 ARG B C    1 
ATOM   8478  O  O    . ARG B 1 256 ? 8.037   -49.982 9.105   1.00 28.44  ? 274 ARG B O    1 
ATOM   8479  C  CB   . ARG B 1 256 ? 7.887   -49.078 6.205   1.00 31.89  ? 274 ARG B CB   1 
ATOM   8480  C  CG   . ARG B 1 256 ? 8.620   -48.499 5.008   1.00 34.82  ? 274 ARG B CG   1 
ATOM   8481  C  CD   . ARG B 1 256 ? 8.144   -47.090 4.692   1.00 37.75  ? 274 ARG B CD   1 
ATOM   8482  N  NE   . ARG B 1 256 ? 6.688   -47.015 4.603   1.00 40.52  ? 274 ARG B NE   1 
ATOM   8483  C  CZ   . ARG B 1 256 ? 5.981   -47.352 3.528   1.00 42.24  ? 274 ARG B CZ   1 
ATOM   8484  N  NH1  . ARG B 1 256 ? 6.591   -47.790 2.435   1.00 42.41  ? 274 ARG B NH1  1 
ATOM   8485  N  NH2  . ARG B 1 256 ? 4.660   -47.250 3.550   1.00 44.31  ? 274 ARG B NH2  1 
ATOM   8486  H  H    . ARG B 1 256 ? 9.876   -48.504 7.820   1.00 32.76  ? 274 ARG B H    1 
ATOM   8487  H  HA   . ARG B 1 256 ? 7.428   -47.423 7.369   1.00 34.50  ? 274 ARG B HA   1 
ATOM   8488  H  HB2  . ARG B 1 256 ? 8.276   -49.947 6.394   1.00 38.27  ? 274 ARG B HB2  1 
ATOM   8489  H  HB3  . ARG B 1 256 ? 6.955   -49.179 5.958   1.00 38.27  ? 274 ARG B HB3  1 
ATOM   8490  H  HG2  . ARG B 1 256 ? 9.570   -48.465 5.198   1.00 41.79  ? 274 ARG B HG2  1 
ATOM   8491  H  HG3  . ARG B 1 256 ? 8.457   -49.057 4.231   1.00 41.79  ? 274 ARG B HG3  1 
ATOM   8492  H  HD2  . ARG B 1 256 ? 8.436   -46.489 5.394   1.00 45.29  ? 274 ARG B HD2  1 
ATOM   8493  H  HD3  . ARG B 1 256 ? 8.515   -46.811 3.840   1.00 45.29  ? 274 ARG B HD3  1 
ATOM   8494  H  HE   . ARG B 1 256 ? 6.258   -46.735 5.293   1.00 48.62  ? 274 ARG B HE   1 
ATOM   8495  H  HH11 . ARG B 1 256 ? 7.448   -47.859 2.418   1.00 50.89  ? 274 ARG B HH11 1 
ATOM   8496  H  HH12 . ARG B 1 256 ? 6.129   -48.007 1.742   1.00 50.89  ? 274 ARG B HH12 1 
ATOM   8497  H  HH21 . ARG B 1 256 ? 4.262   -46.967 4.258   1.00 53.18  ? 274 ARG B HH21 1 
ATOM   8498  H  HH22 . ARG B 1 256 ? 4.200   -47.467 2.856   1.00 53.18  ? 274 ARG B HH22 1 
ATOM   8499  N  N    . SER B 1 257 ? 6.211   -48.648 9.100   1.00 28.64  ? 275 SER B N    1 
ATOM   8500  C  CA   . SER B 1 257 ? 5.580   -49.344 10.220  1.00 30.05  ? 275 SER B CA   1 
ATOM   8501  C  C    . SER B 1 257 ? 5.447   -50.845 9.976   1.00 31.05  ? 275 SER B C    1 
ATOM   8502  O  O    . SER B 1 257 ? 5.510   -51.635 10.927  1.00 31.57  ? 275 SER B O    1 
ATOM   8503  C  CB   . SER B 1 257 ? 4.194   -48.749 10.477  1.00 31.37  ? 275 SER B CB   1 
ATOM   8504  O  OG   . SER B 1 257 ? 4.287   -47.412 10.937  1.00 32.69  ? 275 SER B OG   1 
ATOM   8505  H  H    . SER B 1 257 ? 5.747   -47.997 8.781   1.00 34.37  ? 275 SER B H    1 
ATOM   8506  H  HA   . SER B 1 257 ? 6.137   -49.219 11.004  1.00 36.06  ? 275 SER B HA   1 
ATOM   8507  H  HB2  . SER B 1 257 ? 3.688   -48.763 9.650   1.00 37.64  ? 275 SER B HB2  1 
ATOM   8508  H  HB3  . SER B 1 257 ? 3.744   -49.283 11.151  1.00 37.64  ? 275 SER B HB3  1 
ATOM   8509  H  HG   . SER B 1 257 ? 4.684   -47.390 11.677  1.00 39.23  ? 275 SER B HG   1 
ATOM   8510  N  N    . ALA B 1 258 ? 5.243   -51.258 8.724   1.00 30.85  ? 276 ALA B N    1 
ATOM   8511  C  CA   . ALA B 1 258 ? 5.083   -52.676 8.427   1.00 32.48  ? 276 ALA B CA   1 
ATOM   8512  C  C    . ALA B 1 258 ? 6.345   -53.482 8.705   1.00 32.80  ? 276 ALA B C    1 
ATOM   8513  O  O    . ALA B 1 258 ? 6.267   -54.714 8.789   1.00 32.85  ? 276 ALA B O    1 
ATOM   8514  C  CB   . ALA B 1 258 ? 4.681   -52.852 6.963   1.00 34.13  ? 276 ALA B CB   1 
ATOM   8515  H  H    . ALA B 1 258 ? 5.194   -50.742 8.038   1.00 37.02  ? 276 ALA B H    1 
ATOM   8516  H  HA   . ALA B 1 258 ? 4.376   -53.030 8.989   1.00 38.98  ? 276 ALA B HA   1 
ATOM   8517  H  HB1  . ALA B 1 258 ? 5.396   -52.520 6.397   1.00 40.95  ? 276 ALA B HB1  1 
ATOM   8518  H  HB2  . ALA B 1 258 ? 4.531   -53.794 6.787   1.00 40.95  ? 276 ALA B HB2  1 
ATOM   8519  H  HB3  . ALA B 1 258 ? 3.868   -52.351 6.796   1.00 40.95  ? 276 ALA B HB3  1 
ATOM   8520  N  N    . ASP B 1 259 ? 7.494   -52.820 8.867   1.00 32.44  ? 277 ASP B N    1 
ATOM   8521  C  CA   . ASP B 1 259 ? 8.773   -53.498 9.039   1.00 32.56  ? 277 ASP B CA   1 
ATOM   8522  C  C    . ASP B 1 259 ? 9.123   -53.796 10.493  1.00 33.19  ? 277 ASP B C    1 
ATOM   8523  O  O    . ASP B 1 259 ? 10.137  -54.457 10.747  1.00 33.64  ? 277 ASP B O    1 
ATOM   8524  C  CB   . ASP B 1 259 ? 9.907   -52.640 8.464   1.00 31.82  ? 277 ASP B CB   1 
ATOM   8525  C  CG   . ASP B 1 259 ? 9.912   -52.606 6.953   1.00 31.49  ? 277 ASP B CG   1 
ATOM   8526  O  OD1  . ASP B 1 259 ? 9.197   -53.418 6.318   1.00 32.12  ? 277 ASP B OD1  1 
ATOM   8527  O  OD2  . ASP B 1 259 ? 10.647  -51.760 6.401   1.00 31.73  ? 277 ASP B OD2  1 
ATOM   8528  H  H    . ASP B 1 259 ? 7.556   -51.962 8.880   1.00 38.92  ? 277 ASP B H    1 
ATOM   8529  H  HA   . ASP B 1 259 ? 8.723   -54.337 8.555   1.00 39.08  ? 277 ASP B HA   1 
ATOM   8530  H  HB2  . ASP B 1 259 ? 9.807   -51.729 8.783   1.00 38.18  ? 277 ASP B HB2  1 
ATOM   8531  H  HB3  . ASP B 1 259 ? 10.757  -53.002 8.758   1.00 38.18  ? 277 ASP B HB3  1 
ATOM   8532  N  N    . TYR B 1 260 ? 8.343   -53.309 11.454  1.00 32.62  ? 278 TYR B N    1 
ATOM   8533  C  CA   . TYR B 1 260 ? 8.643   -53.552 12.855  1.00 32.61  ? 278 TYR B CA   1 
ATOM   8534  C  C    . TYR B 1 260 ? 7.350   -53.710 13.638  1.00 32.86  ? 278 TYR B C    1 
ATOM   8535  O  O    . TYR B 1 260 ? 6.281   -53.258 13.221  1.00 33.80  ? 278 TYR B O    1 
ATOM   8536  C  CB   . TYR B 1 260 ? 9.535   -52.450 13.460  1.00 32.30  ? 278 TYR B CB   1 
ATOM   8537  C  CG   . TYR B 1 260 ? 9.073   -51.027 13.217  1.00 32.31  ? 278 TYR B CG   1 
ATOM   8538  C  CD1  . TYR B 1 260 ? 8.163   -50.417 14.071  1.00 32.98  ? 278 TYR B CD1  1 
ATOM   8539  C  CD2  . TYR B 1 260 ? 9.565   -50.284 12.148  1.00 31.97  ? 278 TYR B CD2  1 
ATOM   8540  C  CE1  . TYR B 1 260 ? 7.745   -49.115 13.861  1.00 32.81  ? 278 TYR B CE1  1 
ATOM   8541  C  CE2  . TYR B 1 260 ? 9.146   -48.980 11.927  1.00 31.85  ? 278 TYR B CE2  1 
ATOM   8542  C  CZ   . TYR B 1 260 ? 8.237   -48.404 12.788  1.00 33.01  ? 278 TYR B CZ   1 
ATOM   8543  O  OH   . TYR B 1 260 ? 7.816   -47.110 12.585  1.00 34.88  ? 278 TYR B OH   1 
ATOM   8544  H  H    . TYR B 1 260 ? 7.637   -52.838 11.317  1.00 39.14  ? 278 TYR B H    1 
ATOM   8545  H  HA   . TYR B 1 260 ? 9.129   -54.388 12.934  1.00 39.14  ? 278 TYR B HA   1 
ATOM   8546  H  HB2  . TYR B 1 260 ? 9.573   -52.582 14.420  1.00 38.77  ? 278 TYR B HB2  1 
ATOM   8547  H  HB3  . TYR B 1 260 ? 10.423  -52.534 13.078  1.00 38.77  ? 278 TYR B HB3  1 
ATOM   8548  H  HD1  . TYR B 1 260 ? 7.828   -50.893 14.797  1.00 39.58  ? 278 TYR B HD1  1 
ATOM   8549  H  HD2  . TYR B 1 260 ? 10.186  -50.669 11.572  1.00 38.36  ? 278 TYR B HD2  1 
ATOM   8550  H  HE1  . TYR B 1 260 ? 7.134   -48.722 14.442  1.00 39.38  ? 278 TYR B HE1  1 
ATOM   8551  H  HE2  . TYR B 1 260 ? 9.477   -48.499 11.203  1.00 38.22  ? 278 TYR B HE2  1 
ATOM   8552  H  HH   . TYR B 1 260 ? 7.288   -46.880 13.196  1.00 41.86  ? 278 TYR B HH   1 
ATOM   8553  N  N    . GLY B 1 261 ? 7.462   -54.379 14.776  1.00 32.16  ? 279 GLY B N    1 
ATOM   8554  C  CA   . GLY B 1 261 ? 6.316   -54.617 15.615  1.00 31.96  ? 279 GLY B CA   1 
ATOM   8555  C  C    . GLY B 1 261 ? 6.740   -55.005 17.012  1.00 30.78  ? 279 GLY B C    1 
ATOM   8556  O  O    . GLY B 1 261 ? 7.907   -54.873 17.388  1.00 29.72  ? 279 GLY B O    1 
ATOM   8557  H  H    . GLY B 1 261 ? 8.198   -54.703 15.081  1.00 38.60  ? 279 GLY B H    1 
ATOM   8558  H  HA2  . GLY B 1 261 ? 5.775   -53.814 15.666  1.00 38.35  ? 279 GLY B HA2  1 
ATOM   8559  H  HA3  . GLY B 1 261 ? 5.781   -55.335 15.242  1.00 38.35  ? 279 GLY B HA3  1 
ATOM   8560  N  N    . ILE B 1 262 ? 5.766   -55.518 17.766  1.00 30.33  ? 280 ILE B N    1 
ATOM   8561  C  CA   . ILE B 1 262 ? 5.951   -55.745 19.198  1.00 29.99  ? 280 ILE B CA   1 
ATOM   8562  C  C    . ILE B 1 262 ? 7.100   -56.712 19.459  1.00 28.96  ? 280 ILE B C    1 
ATOM   8563  O  O    . ILE B 1 262 ? 7.817   -56.581 20.457  1.00 29.23  ? 280 ILE B O    1 
ATOM   8564  C  CB   . ILE B 1 262 ? 4.635   -56.221 19.839  1.00 31.37  ? 280 ILE B CB   1 
ATOM   8565  C  CG1  . ILE B 1 262 ? 4.740   -56.180 21.365  1.00 32.09  ? 280 ILE B CG1  1 
ATOM   8566  C  CG2  . ILE B 1 262 ? 4.289   -57.631 19.371  1.00 31.34  ? 280 ILE B CG2  1 
ATOM   8567  C  CD1  . ILE B 1 262 ? 4.999   -54.803 21.925  1.00 32.68  ? 280 ILE B CD1  1 
ATOM   8568  H  H    . ILE B 1 262 ? 4.989   -55.743 17.473  1.00 36.40  ? 280 ILE B H    1 
ATOM   8569  H  HA   . ILE B 1 262 ? 6.193   -54.900 19.608  1.00 35.98  ? 280 ILE B HA   1 
ATOM   8570  H  HB   . ILE B 1 262 ? 3.928   -55.620 19.558  1.00 37.64  ? 280 ILE B HB   1 
ATOM   8571  H  HG12 . ILE B 1 262 ? 3.906   -56.501 21.743  1.00 38.51  ? 280 ILE B HG12 1 
ATOM   8572  H  HG13 . ILE B 1 262 ? 5.472   -56.754 21.642  1.00 38.51  ? 280 ILE B HG13 1 
ATOM   8573  H  HG21 . ILE B 1 262 ? 4.387   -57.677 18.407  1.00 37.61  ? 280 ILE B HG21 1 
ATOM   8574  H  HG22 . ILE B 1 262 ? 4.891   -58.261 19.796  1.00 37.61  ? 280 ILE B HG22 1 
ATOM   8575  H  HG23 . ILE B 1 262 ? 3.372   -57.830 19.620  1.00 37.61  ? 280 ILE B HG23 1 
ATOM   8576  H  HD11 . ILE B 1 262 ? 4.454   -54.159 21.445  1.00 39.21  ? 280 ILE B HD11 1 
ATOM   8577  H  HD12 . ILE B 1 262 ? 4.766   -54.796 22.867  1.00 39.21  ? 280 ILE B HD12 1 
ATOM   8578  H  HD13 . ILE B 1 262 ? 5.938   -54.588 21.815  1.00 39.21  ? 280 ILE B HD13 1 
ATOM   8579  N  N    . THR B 1 263 ? 7.288   -57.710 18.588  1.00 28.62  ? 281 THR B N    1 
ATOM   8580  C  CA   . THR B 1 263 ? 8.362   -58.673 18.822  1.00 28.79  ? 281 THR B CA   1 
ATOM   8581  C  C    . THR B 1 263 ? 9.747   -58.036 18.731  1.00 27.90  ? 281 THR B C    1 
ATOM   8582  O  O    . THR B 1 263 ? 10.710  -58.600 19.260  1.00 29.29  ? 281 THR B O    1 
ATOM   8583  C  CB   . THR B 1 263 ? 8.252   -59.883 17.882  1.00 30.05  ? 281 THR B CB   1 
ATOM   8584  O  OG1  . THR B 1 263 ? 8.278   -59.468 16.512  1.00 31.81  ? 281 THR B OG1  1 
ATOM   8585  C  CG2  . THR B 1 263 ? 6.964   -60.657 18.142  1.00 30.07  ? 281 THR B CG2  1 
ATOM   8586  H  H    . THR B 1 263 ? 6.821   -57.844 17.878  1.00 34.34  ? 281 THR B H    1 
ATOM   8587  H  HA   . THR B 1 263 ? 8.258   -59.021 19.722  1.00 34.55  ? 281 THR B HA   1 
ATOM   8588  H  HB   . THR B 1 263 ? 9.007   -60.469 18.049  1.00 36.06  ? 281 THR B HB   1 
ATOM   8589  H  HG1  . THR B 1 263 ? 9.026   -59.134 16.327  1.00 38.17  ? 281 THR B HG1  1 
ATOM   8590  H  HG21 . THR B 1 263 ? 6.772   -61.243 17.393  1.00 36.08  ? 281 THR B HG21 1 
ATOM   8591  H  HG22 . THR B 1 263 ? 7.056   -61.194 18.945  1.00 36.08  ? 281 THR B HG22 1 
ATOM   8592  H  HG23 . THR B 1 263 ? 6.224   -60.041 18.258  1.00 36.08  ? 281 THR B HG23 1 
ATOM   8593  N  N    . ASP B 1 264 ? 9.868   -56.873 18.088  1.00 27.12  ? 282 ASP B N    1 
ATOM   8594  C  CA   . ASP B 1 264 ? 11.149  -56.187 17.973  1.00 26.56  ? 282 ASP B CA   1 
ATOM   8595  C  C    . ASP B 1 264 ? 11.471  -55.316 19.179  1.00 25.56  ? 282 ASP B C    1 
ATOM   8596  O  O    . ASP B 1 264 ? 12.530  -54.675 19.200  1.00 24.71  ? 282 ASP B O    1 
ATOM   8597  C  CB   . ASP B 1 264 ? 11.157  -55.313 16.714  1.00 26.74  ? 282 ASP B CB   1 
ATOM   8598  C  CG   . ASP B 1 264 ? 10.887  -56.106 15.449  1.00 27.21  ? 282 ASP B CG   1 
ATOM   8599  O  OD1  . ASP B 1 264 ? 11.665  -57.034 15.148  1.00 27.36  ? 282 ASP B OD1  1 
ATOM   8600  O  OD2  . ASP B 1 264 ? 9.892   -55.805 14.759  1.00 28.17  ? 282 ASP B OD2  1 
ATOM   8601  H  H    . ASP B 1 264 ? 9.217   -56.460 17.708  1.00 32.54  ? 282 ASP B H    1 
ATOM   8602  H  HA   . ASP B 1 264 ? 11.847  -56.856 17.891  1.00 31.87  ? 282 ASP B HA   1 
ATOM   8603  H  HB2  . ASP B 1 264 ? 10.469  -54.634 16.795  1.00 32.09  ? 282 ASP B HB2  1 
ATOM   8604  H  HB3  . ASP B 1 264 ? 12.028  -54.893 16.625  1.00 32.09  ? 282 ASP B HB3  1 
ATOM   8605  N  N    . CYS B 1 265 ? 10.599  -55.265 20.183  1.00 25.21  ? 283 CYS B N    1 
ATOM   8606  C  CA   . CYS B 1 265 ? 10.752  -54.296 21.266  1.00 25.36  ? 283 CYS B CA   1 
ATOM   8607  C  C    . CYS B 1 265 ? 11.667  -54.864 22.344  1.00 25.46  ? 283 CYS B C    1 
ATOM   8608  O  O    . CYS B 1 265 ? 11.271  -55.148 23.479  1.00 26.73  ? 283 CYS B O    1 
ATOM   8609  C  CB   . CYS B 1 265 ? 9.407   -53.874 21.818  1.00 26.42  ? 283 CYS B CB   1 
ATOM   8610  S  SG   . CYS B 1 265 ? 8.407   -53.048 20.644  1.00 27.07  ? 283 CYS B SG   1 
ATOM   8611  H  H    . CYS B 1 265 ? 9.914   -55.778 20.259  1.00 30.26  ? 283 CYS B H    1 
ATOM   8612  H  HA   . CYS B 1 265 ? 11.180  -53.504 20.906  1.00 30.43  ? 283 CYS B HA   1 
ATOM   8613  H  HB2  . CYS B 1 265 ? 8.928   -54.664 22.115  1.00 31.71  ? 283 CYS B HB2  1 
ATOM   8614  H  HB3  . CYS B 1 265 ? 9.550   -53.272 22.565  1.00 31.71  ? 283 CYS B HB3  1 
ATOM   8615  N  N    . ASN B 1 266 ? 12.934  -54.986 21.969  1.00 23.74  ? 284 ASN B N    1 
ATOM   8616  C  CA   . ASN B 1 266 ? 14.004  -55.435 22.826  1.00 24.18  ? 284 ASN B CA   1 
ATOM   8617  C  C    . ASN B 1 266 ? 14.903  -54.243 23.118  1.00 23.95  ? 284 ASN B C    1 
ATOM   8618  O  O    . ASN B 1 266 ? 15.490  -53.676 22.183  1.00 23.71  ? 284 ASN B O    1 
ATOM   8619  C  CB   . ASN B 1 266 ? 14.773  -56.526 22.090  1.00 24.75  ? 284 ASN B CB   1 
ATOM   8620  C  CG   . ASN B 1 266 ? 16.030  -56.938 22.809  1.00 24.91  ? 284 ASN B CG   1 
ATOM   8621  O  OD1  . ASN B 1 266 ? 16.300  -56.484 23.920  1.00 24.43  ? 284 ASN B OD1  1 
ATOM   8622  N  ND2  . ASN B 1 266 ? 16.811  -57.806 22.179  1.00 25.64  ? 284 ASN B ND2  1 
ATOM   8623  H  H    . ASN B 1 266 ? 13.208  -54.802 21.176  1.00 28.49  ? 284 ASN B H    1 
ATOM   8624  H  HA   . ASN B 1 266 ? 13.674  -55.787 23.668  1.00 29.01  ? 284 ASN B HA   1 
ATOM   8625  H  HB2  . ASN B 1 266 ? 14.207  -57.309 22.003  1.00 29.70  ? 284 ASN B HB2  1 
ATOM   8626  H  HB3  . ASN B 1 266 ? 15.023  -56.199 21.211  1.00 29.70  ? 284 ASN B HB3  1 
ATOM   8627  H  HD21 . ASN B 1 266 ? 17.541  -58.073 22.546  1.00 30.76  ? 284 ASN B HD21 1 
ATOM   8628  H  HD22 . ASN B 1 266 ? 16.587  -58.101 21.403  1.00 30.76  ? 284 ASN B HD22 1 
ATOM   8629  N  N    . PRO B 1 267 ? 15.034  -53.822 24.383  1.00 24.41  ? 285 PRO B N    1 
ATOM   8630  C  CA   . PRO B 1 267 ? 15.792  -52.598 24.686  1.00 24.93  ? 285 PRO B CA   1 
ATOM   8631  C  C    . PRO B 1 267 ? 17.294  -52.807 24.771  1.00 23.77  ? 285 PRO B C    1 
ATOM   8632  O  O    . PRO B 1 267 ? 18.042  -51.817 24.834  1.00 24.52  ? 285 PRO B O    1 
ATOM   8633  C  CB   . PRO B 1 267 ? 15.235  -52.183 26.055  1.00 25.40  ? 285 PRO B CB   1 
ATOM   8634  C  CG   . PRO B 1 267 ? 14.909  -53.508 26.718  1.00 24.80  ? 285 PRO B CG   1 
ATOM   8635  C  CD   . PRO B 1 267 ? 14.512  -54.466 25.606  1.00 25.40  ? 285 PRO B CD   1 
ATOM   8636  H  HA   . PRO B 1 267 ? 15.596  -51.912 24.030  1.00 29.92  ? 285 PRO B HA   1 
ATOM   8637  H  HB2  . PRO B 1 267 ? 15.905  -51.692 26.557  1.00 30.48  ? 285 PRO B HB2  1 
ATOM   8638  H  HB3  . PRO B 1 267 ? 14.439  -51.639 25.944  1.00 30.48  ? 285 PRO B HB3  1 
ATOM   8639  H  HG2  . PRO B 1 267 ? 15.692  -53.836 27.187  1.00 29.77  ? 285 PRO B HG2  1 
ATOM   8640  H  HG3  . PRO B 1 267 ? 14.176  -53.387 27.342  1.00 29.77  ? 285 PRO B HG3  1 
ATOM   8641  H  HD2  . PRO B 1 267 ? 14.923  -55.335 25.739  1.00 30.48  ? 285 PRO B HD2  1 
ATOM   8642  H  HD3  . PRO B 1 267 ? 13.547  -54.559 25.561  1.00 30.48  ? 285 PRO B HD3  1 
ATOM   8643  N  N    . LEU B 1 268 ? 17.755  -54.048 24.784  1.00 24.37  ? 286 LEU B N    1 
ATOM   8644  C  CA   . LEU B 1 268 ? 19.168  -54.336 24.943  1.00 24.63  ? 286 LEU B CA   1 
ATOM   8645  C  C    . LEU B 1 268 ? 19.903  -54.076 23.637  1.00 23.27  ? 286 LEU B C    1 
ATOM   8646  O  O    . LEU B 1 268 ? 19.294  -53.917 22.572  1.00 23.22  ? 286 LEU B O    1 
ATOM   8647  C  CB   . LEU B 1 268 ? 19.348  -55.785 25.384  1.00 28.24  ? 286 LEU B CB   1 
ATOM   8648  C  CG   . LEU B 1 268 ? 18.758  -56.162 26.747  1.00 32.10  ? 286 LEU B CG   1 
ATOM   8649  C  CD1  . LEU B 1 268 ? 19.047  -57.620 27.085  1.00 33.25  ? 286 LEU B CD1  1 
ATOM   8650  C  CD2  . LEU B 1 268 ? 19.281  -55.247 27.846  1.00 33.33  ? 286 LEU B CD2  1 
ATOM   8651  H  H    . LEU B 1 268 ? 17.263  -54.749 24.702  1.00 29.24  ? 286 LEU B H    1 
ATOM   8652  H  HA   . LEU B 1 268 ? 19.543  -53.759 25.627  1.00 29.56  ? 286 LEU B HA   1 
ATOM   8653  H  HB2  . LEU B 1 268 ? 18.925  -56.355 24.722  1.00 33.88  ? 286 LEU B HB2  1 
ATOM   8654  H  HB3  . LEU B 1 268 ? 20.299  -55.972 25.423  1.00 33.88  ? 286 LEU B HB3  1 
ATOM   8655  H  HG   . LEU B 1 268 ? 17.795  -56.049 26.701  1.00 38.52  ? 286 LEU B HG   1 
ATOM   8656  H  HD11 . LEU B 1 268 ? 18.686  -58.184 26.383  1.00 39.90  ? 286 LEU B HD11 1 
ATOM   8657  H  HD12 . LEU B 1 268 ? 20.007  -57.745 27.149  1.00 39.90  ? 286 LEU B HD12 1 
ATOM   8658  H  HD13 . LEU B 1 268 ? 18.628  -57.837 27.932  1.00 39.90  ? 286 LEU B HD13 1 
ATOM   8659  H  HD21 . LEU B 1 268 ? 18.886  -54.367 27.740  1.00 40.00  ? 286 LEU B HD21 1 
ATOM   8660  H  HD22 . LEU B 1 268 ? 19.037  -55.618 28.709  1.00 40.00  ? 286 LEU B HD22 1 
ATOM   8661  H  HD23 . LEU B 1 268 ? 20.247  -55.186 27.774  1.00 40.00  ? 286 LEU B HD23 1 
ATOM   8662  N  N    . PRO B 1 269 ? 21.230  -54.009 23.686  1.00 22.83  ? 287 PRO B N    1 
ATOM   8663  C  CA   . PRO B 1 269 ? 21.990  -53.738 22.461  1.00 23.76  ? 287 PRO B CA   1 
ATOM   8664  C  C    . PRO B 1 269 ? 21.680  -54.751 21.370  1.00 23.02  ? 287 PRO B C    1 
ATOM   8665  O  O    . PRO B 1 269 ? 21.414  -55.930 21.633  1.00 23.92  ? 287 PRO B O    1 
ATOM   8666  C  CB   . PRO B 1 269 ? 23.449  -53.825 22.921  1.00 23.19  ? 287 PRO B CB   1 
ATOM   8667  C  CG   . PRO B 1 269 ? 23.388  -53.409 24.362  1.00 23.97  ? 287 PRO B CG   1 
ATOM   8668  C  CD   . PRO B 1 269 ? 22.090  -53.991 24.883  1.00 23.76  ? 287 PRO B CD   1 
ATOM   8669  H  HA   . PRO B 1 269 ? 21.803  -52.846 22.130  1.00 28.51  ? 287 PRO B HA   1 
ATOM   8670  H  HB2  . PRO B 1 269 ? 23.777  -54.733 22.830  1.00 27.83  ? 287 PRO B HB2  1 
ATOM   8671  H  HB3  . PRO B 1 269 ? 24.001  -53.219 22.403  1.00 27.83  ? 287 PRO B HB3  1 
ATOM   8672  H  HG2  . PRO B 1 269 ? 24.148  -53.771 24.843  1.00 28.77  ? 287 PRO B HG2  1 
ATOM   8673  H  HG3  . PRO B 1 269 ? 23.385  -52.441 24.427  1.00 28.77  ? 287 PRO B HG3  1 
ATOM   8674  H  HD2  . PRO B 1 269 ? 22.226  -54.888 25.225  1.00 28.51  ? 287 PRO B HD2  1 
ATOM   8675  H  HD3  . PRO B 1 269 ? 21.710  -53.426 25.574  1.00 28.51  ? 287 PRO B HD3  1 
ATOM   8676  N  N    . ALA B 1 270 ? 21.737  -54.262 20.130  1.00 22.38  ? 288 ALA B N    1 
ATOM   8677  C  CA   . ALA B 1 270 ? 21.275  -55.010 18.969  1.00 22.49  ? 288 ALA B CA   1 
ATOM   8678  C  C    . ALA B 1 270 ? 21.850  -56.417 18.947  1.00 22.56  ? 288 ALA B C    1 
ATOM   8679  O  O    . ALA B 1 270 ? 23.043  -56.621 19.188  1.00 22.21  ? 288 ALA B O    1 
ATOM   8680  C  CB   . ALA B 1 270 ? 21.690  -54.269 17.697  1.00 22.14  ? 288 ALA B CB   1 
ATOM   8681  H  H    . ALA B 1 270 ? 22.046  -53.483 19.933  1.00 26.86  ? 288 ALA B H    1 
ATOM   8682  H  HA   . ALA B 1 270 ? 20.308  -55.086 19.002  1.00 26.99  ? 288 ALA B HA   1 
ATOM   8683  H  HB1  . ALA B 1 270 ? 21.395  -54.777 16.925  1.00 26.57  ? 288 ALA B HB1  1 
ATOM   8684  H  HB2  . ALA B 1 270 ? 21.277  -53.391 17.693  1.00 26.57  ? 288 ALA B HB2  1 
ATOM   8685  H  HB3  . ALA B 1 270 ? 22.656  -54.180 17.684  1.00 26.57  ? 288 ALA B HB3  1 
ATOM   8686  N  N    . ASN B 1 271 ? 20.984  -57.378 18.605  1.00 21.33  ? 289 ASN B N    1 
ATOM   8687  C  CA   . ASN B 1 271 ? 21.332  -58.794 18.694  1.00 22.81  ? 289 ASN B CA   1 
ATOM   8688  C  C    . ASN B 1 271 ? 22.594  -59.132 17.908  1.00 23.43  ? 289 ASN B C    1 
ATOM   8689  O  O    . ASN B 1 271 ? 23.377  -59.993 18.324  1.00 24.37  ? 289 ASN B O    1 
ATOM   8690  C  CB   . ASN B 1 271 ? 20.175  -59.645 18.163  1.00 24.35  ? 289 ASN B CB   1 
ATOM   8691  C  CG   . ASN B 1 271 ? 18.912  -59.502 18.981  1.00 26.36  ? 289 ASN B CG   1 
ATOM   8692  O  OD1  . ASN B 1 271 ? 18.961  -59.174 20.165  1.00 28.57  ? 289 ASN B OD1  1 
ATOM   8693  N  ND2  . ASN B 1 271 ? 17.767  -59.761 18.355  1.00 25.78  ? 289 ASN B ND2  1 
ATOM   8694  H  H    . ASN B 1 271 ? 20.186  -57.234 18.316  1.00 25.59  ? 289 ASN B H    1 
ATOM   8695  H  HA   . ASN B 1 271 ? 21.491  -58.999 19.629  1.00 27.37  ? 289 ASN B HA   1 
ATOM   8696  H  HB2  . ASN B 1 271 ? 19.974  -59.372 17.254  1.00 29.21  ? 289 ASN B HB2  1 
ATOM   8697  H  HB3  . ASN B 1 271 ? 20.437  -60.579 18.179  1.00 29.21  ? 289 ASN B HB3  1 
ATOM   8698  H  HD21 . ASN B 1 271 ? 17.021  -59.693 18.777  1.00 30.93  ? 289 ASN B HD21 1 
ATOM   8699  H  HD22 . ASN B 1 271 ? 17.773  -59.995 17.528  1.00 30.93  ? 289 ASN B HD22 1 
ATOM   8700  N  N    . ASP B 1 272 ? 22.783  -58.513 16.744  1.00 23.87  ? 290 ASP B N    1 
ATOM   8701  C  CA   . ASP B 1 272 ? 23.888  -58.891 15.869  1.00 23.40  ? 290 ASP B CA   1 
ATOM   8702  C  C    . ASP B 1 272 ? 25.234  -58.383 16.356  1.00 23.23  ? 290 ASP B C    1 
ATOM   8703  O  O    . ASP B 1 272 ? 26.267  -58.768 15.797  1.00 24.74  ? 290 ASP B O    1 
ATOM   8704  C  CB   . ASP B 1 272 ? 23.628  -58.405 14.446  1.00 25.00  ? 290 ASP B CB   1 
ATOM   8705  C  CG   . ASP B 1 272 ? 22.436  -59.087 13.822  1.00 27.12  ? 290 ASP B CG   1 
ATOM   8706  O  OD1  . ASP B 1 272 ? 22.193  -60.269 14.160  1.00 28.39  ? 290 ASP B OD1  1 
ATOM   8707  O  OD2  . ASP B 1 272 ? 21.736  -58.440 13.012  1.00 28.24  ? 290 ASP B OD2  1 
ATOM   8708  H  H    . ASP B 1 272 ? 22.290  -57.877 16.442  1.00 28.65  ? 290 ASP B H    1 
ATOM   8709  H  HA   . ASP B 1 272 ? 23.939  -59.859 15.839  1.00 28.08  ? 290 ASP B HA   1 
ATOM   8710  H  HB2  . ASP B 1 272 ? 23.457  -57.450 14.462  1.00 29.99  ? 290 ASP B HB2  1 
ATOM   8711  H  HB3  . ASP B 1 272 ? 24.406  -58.593 13.898  1.00 29.99  ? 290 ASP B HB3  1 
ATOM   8712  N  N    . LEU B 1 273 ? 25.256  -57.539 17.376  1.00 22.13  ? 291 LEU B N    1 
ATOM   8713  C  CA   . LEU B 1 273 ? 26.525  -57.146 17.962  1.00 21.35  ? 291 LEU B CA   1 
ATOM   8714  C  C    . LEU B 1 273 ? 27.147  -58.334 18.691  1.00 22.38  ? 291 LEU B C    1 
ATOM   8715  O  O    . LEU B 1 273 ? 26.450  -59.193 19.239  1.00 23.33  ? 291 LEU B O    1 
ATOM   8716  C  CB   . LEU B 1 273 ? 26.307  -55.993 18.935  1.00 20.61  ? 291 LEU B CB   1 
ATOM   8717  C  CG   . LEU B 1 273 ? 25.722  -54.718 18.315  1.00 21.34  ? 291 LEU B CG   1 
ATOM   8718  C  CD1  . LEU B 1 273 ? 25.390  -53.678 19.388  1.00 21.94  ? 291 LEU B CD1  1 
ATOM   8719  C  CD2  . LEU B 1 273 ? 26.676  -54.140 17.284  1.00 20.74  ? 291 LEU B CD2  1 
ATOM   8720  H  H    . LEU B 1 273 ? 24.562  -57.185 17.741  1.00 26.55  ? 291 LEU B H    1 
ATOM   8721  H  HA   . LEU B 1 273 ? 27.139  -56.851 17.272  1.00 25.62  ? 291 LEU B HA   1 
ATOM   8722  H  HB2  . LEU B 1 273 ? 25.695  -56.288 19.627  1.00 24.73  ? 291 LEU B HB2  1 
ATOM   8723  H  HB3  . LEU B 1 273 ? 27.163  -55.759 19.328  1.00 24.73  ? 291 LEU B HB3  1 
ATOM   8724  H  HG   . LEU B 1 273 ? 24.893  -54.948 17.867  1.00 25.61  ? 291 LEU B HG   1 
ATOM   8725  H  HD11 . LEU B 1 273 ? 24.902  -52.947 18.978  1.00 26.33  ? 291 LEU B HD11 1 
ATOM   8726  H  HD12 . LEU B 1 273 ? 24.847  -54.095 20.075  1.00 26.33  ? 291 LEU B HD12 1 
ATOM   8727  H  HD13 . LEU B 1 273 ? 26.216  -53.349 19.774  1.00 26.33  ? 291 LEU B HD13 1 
ATOM   8728  H  HD21 . LEU B 1 273 ? 27.538  -53.987 17.703  1.00 24.89  ? 291 LEU B HD21 1 
ATOM   8729  H  HD22 . LEU B 1 273 ? 26.771  -54.770 16.553  1.00 24.89  ? 291 LEU B HD22 1 
ATOM   8730  H  HD23 . LEU B 1 273 ? 26.315  -53.302 16.955  1.00 24.89  ? 291 LEU B HD23 1 
ATOM   8731  N  N    . THR B 1 274 ? 28.476  -58.392 18.673  1.00 22.61  ? 292 THR B N    1 
ATOM   8732  C  CA   . THR B 1 274 ? 29.177  -59.396 19.448  1.00 23.00  ? 292 THR B CA   1 
ATOM   8733  C  C    . THR B 1 274 ? 28.996  -59.106 20.935  1.00 23.66  ? 292 THR B C    1 
ATOM   8734  O  O    . THR B 1 274 ? 28.620  -57.999 21.321  1.00 23.20  ? 292 THR B O    1 
ATOM   8735  C  CB   . THR B 1 274 ? 30.669  -59.356 19.139  1.00 23.89  ? 292 THR B CB   1 
ATOM   8736  O  OG1  . THR B 1 274 ? 31.189  -58.087 19.546  1.00 24.89  ? 292 THR B OG1  1 
ATOM   8737  C  CG2  . THR B 1 274 ? 30.926  -59.552 17.658  1.00 24.73  ? 292 THR B CG2  1 
ATOM   8738  H  H    . THR B 1 274 ? 28.985  -57.864 18.223  1.00 27.13  ? 292 THR B H    1 
ATOM   8739  H  HA   . THR B 1 274 ? 28.828  -60.274 19.231  1.00 27.60  ? 292 THR B HA   1 
ATOM   8740  H  HB   . THR B 1 274 ? 31.120  -60.071 19.614  1.00 28.67  ? 292 THR B HB   1 
ATOM   8741  H  HG1  . THR B 1 274 ? 32.011  -58.046 19.379  1.00 29.87  ? 292 THR B HG1  1 
ATOM   8742  H  HG21 . THR B 1 274 ? 31.876  -59.657 17.498  1.00 29.68  ? 292 THR B HG21 1 
ATOM   8743  H  HG22 . THR B 1 274 ? 30.464  -60.345 17.344  1.00 29.68  ? 292 THR B HG22 1 
ATOM   8744  H  HG23 . THR B 1 274 ? 30.605  -58.783 17.161  1.00 29.68  ? 292 THR B HG23 1 
ATOM   8745  N  N    . PRO B 1 275 ? 29.262  -60.085 21.796  1.00 24.37  ? 293 PRO B N    1 
ATOM   8746  C  CA   . PRO B 1 275 ? 29.185  -59.798 23.237  1.00 24.18  ? 293 PRO B CA   1 
ATOM   8747  C  C    . PRO B 1 275 ? 30.027  -58.598 23.651  1.00 24.59  ? 293 PRO B C    1 
ATOM   8748  O  O    . PRO B 1 275 ? 29.569  -57.787 24.463  1.00 24.32  ? 293 PRO B O    1 
ATOM   8749  C  CB   . PRO B 1 275 ? 29.634  -61.115 23.885  1.00 24.89  ? 293 PRO B CB   1 
ATOM   8750  C  CG   . PRO B 1 275 ? 29.314  -62.155 22.856  1.00 25.86  ? 293 PRO B CG   1 
ATOM   8751  C  CD   . PRO B 1 275 ? 29.570  -61.501 21.527  1.00 25.94  ? 293 PRO B CD   1 
ATOM   8752  H  HA   . PRO B 1 275 ? 28.265  -59.638 23.503  1.00 29.01  ? 293 PRO B HA   1 
ATOM   8753  H  HB2  . PRO B 1 275 ? 30.585  -61.087 24.072  1.00 29.87  ? 293 PRO B HB2  1 
ATOM   8754  H  HB3  . PRO B 1 275 ? 29.139  -61.269 24.705  1.00 29.87  ? 293 PRO B HB3  1 
ATOM   8755  H  HG2  . PRO B 1 275 ? 29.891  -62.925 22.978  1.00 31.04  ? 293 PRO B HG2  1 
ATOM   8756  H  HG3  . PRO B 1 275 ? 28.385  -62.421 22.936  1.00 31.04  ? 293 PRO B HG3  1 
ATOM   8757  H  HD2  . PRO B 1 275 ? 30.495  -61.611 21.258  1.00 31.13  ? 293 PRO B HD2  1 
ATOM   8758  H  HD3  . PRO B 1 275 ? 28.981  -61.861 20.844  1.00 31.13  ? 293 PRO B HD3  1 
ATOM   8759  N  N    A GLU B 1 276 ? 31.234  -58.449 23.095  0.60 24.21  ? 294 GLU B N    1 
ATOM   8760  N  N    B GLU B 1 276 ? 31.246  -58.465 23.116  0.40 25.12  ? 294 GLU B N    1 
ATOM   8761  C  CA   A GLU B 1 276 ? 32.081  -57.315 23.455  0.60 24.89  ? 294 GLU B CA   1 
ATOM   8762  C  CA   B GLU B 1 276 ? 32.083  -57.312 23.440  0.40 26.20  ? 294 GLU B CA   1 
ATOM   8763  C  C    A GLU B 1 276 ? 31.455  -55.996 23.013  0.60 24.44  ? 294 GLU B C    1 
ATOM   8764  C  C    B GLU B 1 276 ? 31.395  -56.015 23.040  0.40 25.01  ? 294 GLU B C    1 
ATOM   8765  O  O    A GLU B 1 276 ? 31.544  -54.988 23.724  0.60 23.98  ? 294 GLU B O    1 
ATOM   8766  O  O    B GLU B 1 276 ? 31.372  -55.044 23.806  0.40 24.84  ? 294 GLU B O    1 
ATOM   8767  C  CB   A GLU B 1 276 ? 33.466  -57.468 22.821  0.60 25.72  ? 294 GLU B CB   1 
ATOM   8768  C  CB   B GLU B 1 276 ? 33.427  -57.426 22.715  0.40 28.34  ? 294 GLU B CB   1 
ATOM   8769  C  CG   A GLU B 1 276 ? 34.120  -58.827 23.006  0.60 26.46  ? 294 GLU B CG   1 
ATOM   8770  C  CG   B GLU B 1 276 ? 34.500  -56.429 23.179  0.40 30.23  ? 294 GLU B CG   1 
ATOM   8771  C  CD   A GLU B 1 276 ? 33.826  -59.769 21.853  0.60 27.47  ? 294 GLU B CD   1 
ATOM   8772  C  CD   B GLU B 1 276 ? 34.220  -54.978 22.785  0.40 31.82  ? 294 GLU B CD   1 
ATOM   8773  O  OE1  A GLU B 1 276 ? 32.681  -60.251 21.766  0.60 24.25  ? 294 GLU B OE1  1 
ATOM   8774  O  OE1  B GLU B 1 276 ? 33.620  -54.733 21.713  0.40 30.57  ? 294 GLU B OE1  1 
ATOM   8775  O  OE2  A GLU B 1 276 ? 34.735  -60.032 21.033  0.60 31.07  ? 294 GLU B OE2  1 
ATOM   8776  O  OE2  B GLU B 1 276 ? 34.607  -54.072 23.557  0.40 33.05  ? 294 GLU B OE2  1 
ATOM   8777  H  H    A GLU B 1 276 ? 31.579  -58.983 22.515  0.60 29.05  ? 294 GLU B H    1 
ATOM   8778  H  H    B GLU B 1 276 ? 31.605  -59.023 22.568  0.40 30.14  ? 294 GLU B H    1 
ATOM   8779  H  HA   A GLU B 1 276 ? 32.182  -57.303 24.420  0.60 29.87  ? 294 GLU B HA   1 
ATOM   8780  H  HA   B GLU B 1 276 ? 32.242  -57.302 24.396  0.40 31.44  ? 294 GLU B HA   1 
ATOM   8781  H  HB2  A GLU B 1 276 ? 33.384  -57.314 21.867  0.60 30.86  ? 294 GLU B HB2  1 
ATOM   8782  H  HB2  B GLU B 1 276 ? 33.778  -58.319 22.858  0.40 34.00  ? 294 GLU B HB2  1 
ATOM   8783  H  HB3  A GLU B 1 276 ? 34.057  -56.807 23.214  0.60 30.86  ? 294 GLU B HB3  1 
ATOM   8784  H  HB3  B GLU B 1 276 ? 33.279  -57.276 21.768  0.40 34.00  ? 294 GLU B HB3  1 
ATOM   8785  H  HG2  A GLU B 1 276 ? 35.081  -58.711 23.064  0.60 31.75  ? 294 GLU B HG2  1 
ATOM   8786  H  HG2  B GLU B 1 276 ? 34.559  -56.464 24.147  0.40 36.27  ? 294 GLU B HG2  1 
ATOM   8787  H  HG3  A GLU B 1 276 ? 33.784  -59.233 23.821  0.60 31.75  ? 294 GLU B HG3  1 
ATOM   8788  H  HG3  B GLU B 1 276 ? 35.350  -56.681 22.785  0.40 36.27  ? 294 GLU B HG3  1 
ATOM   8789  N  N    . GLN B 1 277 ? 30.832  -55.981 21.833  1.00 23.45  ? 295 GLN B N    1 
ATOM   8790  C  CA   . GLN B 1 277 ? 30.200  -54.762 21.351  1.00 20.91  ? 295 GLN B CA   1 
ATOM   8791  C  C    . GLN B 1 277 ? 28.985  -54.417 22.196  1.00 21.46  ? 295 GLN B C    1 
ATOM   8792  O  O    . GLN B 1 277 ? 28.722  -53.240 22.458  1.00 21.03  ? 295 GLN B O    1 
ATOM   8793  C  CB   . GLN B 1 277 ? 29.819  -54.917 19.878  1.00 21.55  ? 295 GLN B CB   1 
ATOM   8794  C  CG   . GLN B 1 277 ? 31.022  -54.931 18.940  1.00 21.95  ? 295 GLN B CG   1 
ATOM   8795  C  CD   . GLN B 1 277 ? 30.716  -55.489 17.553  1.00 22.54  ? 295 GLN B CD   1 
ATOM   8796  O  OE1  . GLN B 1 277 ? 29.680  -56.118 17.321  1.00 23.27  ? 295 GLN B OE1  1 
ATOM   8797  N  NE2  . GLN B 1 277 ? 31.633  -55.267 16.628  1.00 22.83  ? 295 GLN B NE2  1 
ATOM   8798  H  H    . GLN B 1 277 ? 30.766  -56.657 21.305  1.00 28.14  ? 295 GLN B H    1 
ATOM   8799  H  HA   . GLN B 1 277 ? 30.830  -54.027 21.413  1.00 25.09  ? 295 GLN B HA   1 
ATOM   8800  H  HB2  . GLN B 1 277 ? 29.342  -55.754 19.764  1.00 25.86  ? 295 GLN B HB2  1 
ATOM   8801  H  HB3  . GLN B 1 277 ? 29.250  -54.174 19.622  1.00 25.86  ? 295 GLN B HB3  1 
ATOM   8802  H  HG2  . GLN B 1 277 ? 31.341  -54.022 18.828  1.00 26.34  ? 295 GLN B HG2  1 
ATOM   8803  H  HG3  . GLN B 1 277 ? 31.717  -55.481 19.332  1.00 26.34  ? 295 GLN B HG3  1 
ATOM   8804  H  HE21 . GLN B 1 277 ? 32.348  -54.832 16.827  1.00 27.40  ? 295 GLN B HE21 1 
ATOM   8805  H  HE22 . GLN B 1 277 ? 31.516  -55.558 15.827  1.00 27.40  ? 295 GLN B HE22 1 
ATOM   8806  N  N    . LYS B 1 278 ? 28.236  -55.429 22.645  1.00 21.85  ? 296 LYS B N    1 
ATOM   8807  C  CA   . LYS B 1 278 ? 27.081  -55.154 23.493  1.00 22.44  ? 296 LYS B CA   1 
ATOM   8808  C  C    . LYS B 1 278 ? 27.509  -54.496 24.799  1.00 22.49  ? 296 LYS B C    1 
ATOM   8809  O  O    . LYS B 1 278 ? 26.837  -53.585 25.294  1.00 22.62  ? 296 LYS B O    1 
ATOM   8810  C  CB   . LYS B 1 278 ? 26.307  -56.443 23.774  1.00 22.92  ? 296 LYS B CB   1 
ATOM   8811  C  CG   . LYS B 1 278 ? 25.554  -57.006 22.574  1.00 23.40  ? 296 LYS B CG   1 
ATOM   8812  C  CD   . LYS B 1 278 ? 24.476  -57.996 23.016  1.00 23.98  ? 296 LYS B CD   1 
ATOM   8813  C  CE   . LYS B 1 278 ? 23.662  -58.495 21.839  1.00 24.25  ? 296 LYS B CE   1 
ATOM   8814  N  NZ   . LYS B 1 278 ? 24.401  -59.523 21.063  1.00 26.18  ? 296 LYS B NZ   1 
ATOM   8815  H  H    . LYS B 1 278 ? 28.374  -56.261 22.476  1.00 26.22  ? 296 LYS B H    1 
ATOM   8816  H  HA   . LYS B 1 278 ? 26.487  -54.548 23.023  1.00 26.92  ? 296 LYS B HA   1 
ATOM   8817  H  HB2  . LYS B 1 278 ? 26.935  -57.121 24.069  1.00 27.50  ? 296 LYS B HB2  1 
ATOM   8818  H  HB3  . LYS B 1 278 ? 25.657  -56.266 24.471  1.00 27.50  ? 296 LYS B HB3  1 
ATOM   8819  H  HG2  . LYS B 1 278 ? 25.126  -56.281 22.093  1.00 28.09  ? 296 LYS B HG2  1 
ATOM   8820  H  HG3  . LYS B 1 278 ? 26.176  -57.470 21.992  1.00 28.09  ? 296 LYS B HG3  1 
ATOM   8821  H  HD2  . LYS B 1 278 ? 24.896  -58.760 23.441  1.00 28.78  ? 296 LYS B HD2  1 
ATOM   8822  H  HD3  . LYS B 1 278 ? 23.874  -57.559 23.638  1.00 28.78  ? 296 LYS B HD3  1 
ATOM   8823  H  HE2  . LYS B 1 278 ? 22.838  -58.892 22.163  1.00 29.09  ? 296 LYS B HE2  1 
ATOM   8824  H  HE3  . LYS B 1 278 ? 23.462  -57.752 21.248  1.00 29.09  ? 296 LYS B HE3  1 
ATOM   8825  H  HZ1  . LYS B 1 278 ? 24.529  -60.248 21.563  1.00 31.42  ? 296 LYS B HZ1  1 
ATOM   8826  H  HZ2  . LYS B 1 278 ? 23.937  -59.749 20.338  1.00 31.42  ? 296 LYS B HZ2  1 
ATOM   8827  H  HZ3  . LYS B 1 278 ? 25.193  -59.202 20.811  1.00 31.42  ? 296 LYS B HZ3  1 
ATOM   8828  N  N    . VAL B 1 279 ? 28.624  -54.951 25.378  1.00 22.41  ? 297 VAL B N    1 
ATOM   8829  C  CA   . VAL B 1 279 ? 29.130  -54.335 26.603  1.00 23.00  ? 297 VAL B CA   1 
ATOM   8830  C  C    . VAL B 1 279 ? 29.536  -52.892 26.333  1.00 23.42  ? 297 VAL B C    1 
ATOM   8831  O  O    . VAL B 1 279 ? 29.153  -51.964 27.061  1.00 23.18  ? 297 VAL B O    1 
ATOM   8832  C  CB   . VAL B 1 279 ? 30.304  -55.159 27.161  1.00 23.53  ? 297 VAL B CB   1 
ATOM   8833  C  CG1  . VAL B 1 279 ? 31.040  -54.380 28.243  1.00 23.94  ? 297 VAL B CG1  1 
ATOM   8834  C  CG2  . VAL B 1 279 ? 29.807  -56.500 27.697  1.00 24.54  ? 297 VAL B CG2  1 
ATOM   8835  H  H    . VAL B 1 279 ? 29.098  -55.606 25.085  1.00 26.89  ? 297 VAL B H    1 
ATOM   8836  H  HA   . VAL B 1 279 ? 28.424  -54.328 27.268  1.00 27.59  ? 297 VAL B HA   1 
ATOM   8837  H  HB   . VAL B 1 279 ? 30.933  -55.337 26.444  1.00 28.24  ? 297 VAL B HB   1 
ATOM   8838  H  HG11 . VAL B 1 279 ? 30.401  -53.841 28.734  1.00 28.72  ? 297 VAL B HG11 1 
ATOM   8839  H  HG12 . VAL B 1 279 ? 31.475  -55.006 28.843  1.00 28.72  ? 297 VAL B HG12 1 
ATOM   8840  H  HG13 . VAL B 1 279 ? 31.703  -53.808 27.825  1.00 28.72  ? 297 VAL B HG13 1 
ATOM   8841  H  HG21 . VAL B 1 279 ? 28.882  -56.622 27.433  1.00 29.45  ? 297 VAL B HG21 1 
ATOM   8842  H  HG22 . VAL B 1 279 ? 30.353  -57.211 27.325  1.00 29.45  ? 297 VAL B HG22 1 
ATOM   8843  H  HG23 . VAL B 1 279 ? 29.878  -56.500 28.664  1.00 29.45  ? 297 VAL B HG23 1 
ATOM   8844  N  N    . ALA B 1 280 ? 30.322  -52.681 25.277  1.00 22.58  ? 298 ALA B N    1 
ATOM   8845  C  CA   . ALA B 1 280 ? 30.771  -51.331 24.954  1.00 22.64  ? 298 ALA B CA   1 
ATOM   8846  C  C    . ALA B 1 280 ? 29.593  -50.422 24.620  1.00 21.48  ? 298 ALA B C    1 
ATOM   8847  O  O    . ALA B 1 280 ? 29.600  -49.233 24.963  1.00 21.20  ? 298 ALA B O    1 
ATOM   8848  C  CB   . ALA B 1 280 ? 31.759  -51.388 23.789  1.00 22.54  ? 298 ALA B CB   1 
ATOM   8849  H  H    . ALA B 1 280 ? 30.603  -53.292 24.740  1.00 27.09  ? 298 ALA B H    1 
ATOM   8850  H  HA   . ALA B 1 280 ? 31.227  -50.953 25.722  1.00 27.16  ? 298 ALA B HA   1 
ATOM   8851  H  HB1  . ALA B 1 280 ? 32.516  -51.939 24.043  1.00 27.05  ? 298 ALA B HB1  1 
ATOM   8852  H  HB2  . ALA B 1 280 ? 31.316  -51.770 23.016  1.00 27.05  ? 298 ALA B HB2  1 
ATOM   8853  H  HB3  . ALA B 1 280 ? 32.060  -50.488 23.586  1.00 27.05  ? 298 ALA B HB3  1 
ATOM   8854  N  N    . ALA B 1 281 ? 28.567  -50.965 23.953  1.00 21.45  ? 299 ALA B N    1 
ATOM   8855  C  CA   . ALA B 1 281 ? 27.395  -50.162 23.608  1.00 21.95  ? 299 ALA B CA   1 
ATOM   8856  C  C    . ALA B 1 281 ? 26.637  -49.734 24.858  1.00 23.49  ? 299 ALA B C    1 
ATOM   8857  O  O    . ALA B 1 281 ? 26.158  -48.596 24.944  1.00 23.04  ? 299 ALA B O    1 
ATOM   8858  C  CB   . ALA B 1 281 ? 26.484  -50.938 22.651  1.00 21.61  ? 299 ALA B CB   1 
ATOM   8859  H  H    . ALA B 1 281 ? 28.527  -51.783 23.693  1.00 25.75  ? 299 ALA B H    1 
ATOM   8860  H  HA   . ALA B 1 281 ? 27.688  -49.360 23.147  1.00 26.33  ? 299 ALA B HA   1 
ATOM   8861  H  HB1  . ALA B 1 281 ? 26.172  -51.742 23.095  1.00 25.94  ? 299 ALA B HB1  1 
ATOM   8862  H  HB2  . ALA B 1 281 ? 25.729  -50.379 22.410  1.00 25.94  ? 299 ALA B HB2  1 
ATOM   8863  H  HB3  . ALA B 1 281 ? 26.989  -51.174 21.857  1.00 25.94  ? 299 ALA B HB3  1 
ATOM   8864  N  N    . ALA B 1 282 ? 26.525  -50.628 25.844  1.00 24.78  ? 300 ALA B N    1 
ATOM   8865  C  CA   . ALA B 1 282 ? 25.841  -50.261 27.076  1.00 25.28  ? 300 ALA B CA   1 
ATOM   8866  C  C    . ALA B 1 282 ? 26.572  -49.135 27.791  1.00 25.29  ? 300 ALA B C    1 
ATOM   8867  O  O    . ALA B 1 282 ? 25.942  -48.334 28.492  1.00 27.43  ? 300 ALA B O    1 
ATOM   8868  C  CB   . ALA B 1 282 ? 25.718  -51.479 27.990  1.00 26.12  ? 300 ALA B CB   1 
ATOM   8869  H  H    . ALA B 1 282 ? 26.830  -51.432 25.822  1.00 29.74  ? 300 ALA B H    1 
ATOM   8870  H  HA   . ALA B 1 282 ? 24.945  -49.958 26.864  1.00 30.33  ? 300 ALA B HA   1 
ATOM   8871  H  HB1  . ALA B 1 282 ? 25.192  -52.159 27.540  1.00 31.35  ? 300 ALA B HB1  1 
ATOM   8872  H  HB2  . ALA B 1 282 ? 26.605  -51.821 28.182  1.00 31.35  ? 300 ALA B HB2  1 
ATOM   8873  H  HB3  . ALA B 1 282 ? 25.280  -51.213 28.814  1.00 31.35  ? 300 ALA B HB3  1 
ATOM   8874  N  N    . ALA B 1 283 ? 27.894  -49.046 27.614  1.00 24.82  ? 301 ALA B N    1 
ATOM   8875  C  CA   . ALA B 1 283 ? 28.718  -48.035 28.271  1.00 24.49  ? 301 ALA B CA   1 
ATOM   8876  C  C    . ALA B 1 283 ? 29.014  -46.842 27.365  1.00 24.19  ? 301 ALA B C    1 
ATOM   8877  O  O    . ALA B 1 283 ? 30.009  -46.136 27.573  1.00 25.34  ? 301 ALA B O    1 
ATOM   8878  C  CB   . ALA B 1 283 ? 30.023  -48.656 28.769  1.00 25.96  ? 301 ALA B CB   1 
ATOM   8879  H  H    . ALA B 1 283 ? 28.343  -49.574 27.105  1.00 29.79  ? 301 ALA B H    1 
ATOM   8880  H  HA   . ALA B 1 283 ? 28.229  -47.703 29.040  1.00 29.39  ? 301 ALA B HA   1 
ATOM   8881  H  HB1  . ALA B 1 283 ? 30.516  -49.006 28.010  1.00 31.15  ? 301 ALA B HB1  1 
ATOM   8882  H  HB2  . ALA B 1 283 ? 30.547  -47.973 29.217  1.00 31.15  ? 301 ALA B HB2  1 
ATOM   8883  H  HB3  . ALA B 1 283 ? 29.816  -49.373 29.388  1.00 31.15  ? 301 ALA B HB3  1 
ATOM   8884  N  N    . LEU B 1 284 ? 28.140  -46.582 26.388  1.00 22.55  ? 302 LEU B N    1 
ATOM   8885  C  CA   . LEU B 1 284 ? 28.444  -45.616 25.335  1.00 22.35  ? 302 LEU B CA   1 
ATOM   8886  C  C    . LEU B 1 284 ? 28.672  -44.216 25.885  1.00 22.54  ? 302 LEU B C    1 
ATOM   8887  O  O    . LEU B 1 284 ? 29.491  -43.457 25.354  1.00 23.24  ? 302 LEU B O    1 
ATOM   8888  C  CB   . LEU B 1 284 ? 27.285  -45.571 24.336  1.00 22.47  ? 302 LEU B CB   1 
ATOM   8889  C  CG   . LEU B 1 284 ? 27.581  -44.942 22.977  1.00 22.28  ? 302 LEU B CG   1 
ATOM   8890  C  CD1  . LEU B 1 284 ? 28.476  -45.880 22.174  1.00 23.32  ? 302 LEU B CD1  1 
ATOM   8891  C  CD2  . LEU B 1 284 ? 26.303  -44.629 22.210  1.00 22.27  ? 302 LEU B CD2  1 
ATOM   8892  H  H    . LEU B 1 284 ? 27.367  -46.952 26.313  1.00 27.06  ? 302 LEU B H    1 
ATOM   8893  H  HA   . LEU B 1 284 ? 29.256  -45.905 24.890  1.00 26.82  ? 302 LEU B HA   1 
ATOM   8894  H  HB2  . LEU B 1 284 ? 26.995  -46.481 24.171  1.00 26.96  ? 302 LEU B HB2  1 
ATOM   8895  H  HB3  . LEU B 1 284 ? 26.564  -45.060 24.735  1.00 26.96  ? 302 LEU B HB3  1 
ATOM   8896  H  HG   . LEU B 1 284 ? 28.039  -44.097 23.110  1.00 26.73  ? 302 LEU B HG   1 
ATOM   8897  H  HD11 . LEU B 1 284 ? 29.348  -45.923 22.597  1.00 27.98  ? 302 LEU B HD11 1 
ATOM   8898  H  HD12 . LEU B 1 284 ? 28.074  -46.762 22.156  1.00 27.98  ? 302 LEU B HD12 1 
ATOM   8899  H  HD13 . LEU B 1 284 ? 28.564  -45.537 21.271  1.00 27.98  ? 302 LEU B HD13 1 
ATOM   8900  H  HD21 . LEU B 1 284 ? 26.536  -44.244 21.351  1.00 26.72  ? 302 LEU B HD21 1 
ATOM   8901  H  HD22 . LEU B 1 284 ? 25.803  -45.451 22.080  1.00 26.72  ? 302 LEU B HD22 1 
ATOM   8902  H  HD23 . LEU B 1 284 ? 25.773  -43.998 22.722  1.00 26.72  ? 302 LEU B HD23 1 
ATOM   8903  N  N    . LEU B 1 285 ? 27.944  -43.842 26.929  1.00 22.72  ? 303 LEU B N    1 
ATOM   8904  C  CA   . LEU B 1 285 ? 27.874  -42.437 27.305  1.00 22.93  ? 303 LEU B CA   1 
ATOM   8905  C  C    . LEU B 1 285 ? 29.070  -41.966 28.124  1.00 22.79  ? 303 LEU B C    1 
ATOM   8906  O  O    . LEU B 1 285 ? 29.331  -40.757 28.167  1.00 22.55  ? 303 LEU B O    1 
ATOM   8907  C  CB   . LEU B 1 285 ? 26.576  -42.185 28.075  1.00 24.52  ? 303 LEU B CB   1 
ATOM   8908  C  CG   . LEU B 1 285 ? 26.147  -40.732 28.244  1.00 26.48  ? 303 LEU B CG   1 
ATOM   8909  C  CD1  . LEU B 1 285 ? 25.774  -40.123 26.897  1.00 26.53  ? 303 LEU B CD1  1 
ATOM   8910  C  CD2  . LEU B 1 285 ? 24.991  -40.632 29.228  1.00 28.30  ? 303 LEU B CD2  1 
ATOM   8911  H  H    . LEU B 1 285 ? 27.488  -44.373 27.427  1.00 27.27  ? 303 LEU B H    1 
ATOM   8912  H  HA   . LEU B 1 285 ? 27.863  -41.898 26.499  1.00 27.51  ? 303 LEU B HA   1 
ATOM   8913  H  HB2  . LEU B 1 285 ? 25.858  -42.640 27.608  1.00 29.43  ? 303 LEU B HB2  1 
ATOM   8914  H  HB3  . LEU B 1 285 ? 26.679  -42.556 28.966  1.00 29.43  ? 303 LEU B HB3  1 
ATOM   8915  H  HG   . LEU B 1 285 ? 26.888  -40.219 28.603  1.00 31.77  ? 303 LEU B HG   1 
ATOM   8916  H  HD11 . LEU B 1 285 ? 25.150  -40.713 26.446  1.00 31.83  ? 303 LEU B HD11 1 
ATOM   8917  H  HD12 . LEU B 1 285 ? 25.362  -39.257 27.045  1.00 31.83  ? 303 LEU B HD12 1 
ATOM   8918  H  HD13 . LEU B 1 285 ? 26.577  -40.021 26.363  1.00 31.83  ? 303 LEU B HD13 1 
ATOM   8919  H  HD21 . LEU B 1 285 ? 25.289  -40.941 30.098  1.00 33.96  ? 303 LEU B HD21 1 
ATOM   8920  H  HD22 . LEU B 1 285 ? 24.704  -39.707 29.286  1.00 33.96  ? 303 LEU B HD22 1 
ATOM   8921  H  HD23 . LEU B 1 285 ? 24.259  -41.186 28.913  1.00 33.96  ? 303 LEU B HD23 1 
ATOM   8922  N  N    . ALA B 1 286 ? 29.815  -42.879 28.746  1.00 24.50  ? 304 ALA B N    1 
ATOM   8923  C  CA   . ALA B 1 286 ? 30.819  -42.463 29.721  1.00 24.45  ? 304 ALA B CA   1 
ATOM   8924  C  C    . ALA B 1 286 ? 31.890  -41.537 29.158  1.00 24.28  ? 304 ALA B C    1 
ATOM   8925  O  O    . ALA B 1 286 ? 32.267  -40.583 29.861  1.00 24.97  ? 304 ALA B O    1 
ATOM   8926  C  CB   . ALA B 1 286 ? 31.453  -43.697 30.371  1.00 25.20  ? 304 ALA B CB   1 
ATOM   8927  H  H    . ALA B 1 286 ? 29.760  -43.728 28.624  1.00 29.40  ? 304 ALA B H    1 
ATOM   8928  H  HA   . ALA B 1 286 ? 30.352  -41.960 30.406  1.00 29.34  ? 304 ALA B HA   1 
ATOM   8929  H  HB1  . ALA B 1 286 ? 31.879  -44.233 29.684  1.00 30.24  ? 304 ALA B HB1  1 
ATOM   8930  H  HB2  . ALA B 1 286 ? 32.113  -43.408 31.021  1.00 30.24  ? 304 ALA B HB2  1 
ATOM   8931  H  HB3  . ALA B 1 286 ? 30.760  -44.214 30.811  1.00 30.24  ? 304 ALA B HB3  1 
ATOM   8932  N  N    . PRO B 1 287 ? 32.437  -41.758 27.962  1.00 23.68  ? 305 PRO B N    1 
ATOM   8933  C  CA   . PRO B 1 287 ? 33.460  -40.829 27.452  1.00 23.26  ? 305 PRO B CA   1 
ATOM   8934  C  C    . PRO B 1 287 ? 32.975  -39.398 27.351  1.00 20.95  ? 305 PRO B C    1 
ATOM   8935  O  O    . PRO B 1 287 ? 33.791  -38.470 27.434  1.00 20.36  ? 305 PRO B O    1 
ATOM   8936  C  CB   . PRO B 1 287 ? 33.819  -41.411 26.077  1.00 24.69  ? 305 PRO B CB   1 
ATOM   8937  C  CG   . PRO B 1 287 ? 33.464  -42.845 26.175  1.00 25.23  ? 305 PRO B CG   1 
ATOM   8938  C  CD   . PRO B 1 287 ? 32.260  -42.922 27.080  1.00 24.15  ? 305 PRO B CD   1 
ATOM   8939  H  HA   . PRO B 1 287 ? 34.245  -40.861 28.021  1.00 27.92  ? 305 PRO B HA   1 
ATOM   8940  H  HB2  . PRO B 1 287 ? 33.302  -40.970 25.385  1.00 29.62  ? 305 PRO B HB2  1 
ATOM   8941  H  HB3  . PRO B 1 287 ? 34.767  -41.297 25.905  1.00 29.62  ? 305 PRO B HB3  1 
ATOM   8942  H  HG2  . PRO B 1 287 ? 33.251  -43.188 25.293  1.00 30.28  ? 305 PRO B HG2  1 
ATOM   8943  H  HG3  . PRO B 1 287 ? 34.208  -43.339 26.553  1.00 30.28  ? 305 PRO B HG3  1 
ATOM   8944  H  HD2  . PRO B 1 287 ? 31.437  -42.850 26.570  1.00 28.98  ? 305 PRO B HD2  1 
ATOM   8945  H  HD3  . PRO B 1 287 ? 32.262  -43.747 27.590  1.00 28.98  ? 305 PRO B HD3  1 
ATOM   8946  N  N    . ALA B 1 288 ? 31.667  -39.188 27.171  1.00 20.08  ? 306 ALA B N    1 
ATOM   8947  C  CA   . ALA B 1 288 ? 31.151  -37.831 27.015  1.00 18.81  ? 306 ALA B CA   1 
ATOM   8948  C  C    . ALA B 1 288 ? 31.428  -36.991 28.256  1.00 18.68  ? 306 ALA B C    1 
ATOM   8949  O  O    . ALA B 1 288 ? 31.878  -35.844 28.157  1.00 18.27  ? 306 ALA B O    1 
ATOM   8950  C  CB   . ALA B 1 288 ? 29.655  -37.869 26.703  1.00 18.98  ? 306 ALA B CB   1 
ATOM   8951  H  H    . ALA B 1 288 ? 31.069  -39.805 27.135  1.00 24.09  ? 306 ALA B H    1 
ATOM   8952  H  HA   . ALA B 1 288 ? 31.601  -37.411 26.266  1.00 22.57  ? 306 ALA B HA   1 
ATOM   8953  H  HB1  . ALA B 1 288 ? 29.520  -38.327 25.859  1.00 22.77  ? 306 ALA B HB1  1 
ATOM   8954  H  HB2  . ALA B 1 288 ? 29.196  -38.343 27.414  1.00 22.77  ? 306 ALA B HB2  1 
ATOM   8955  H  HB3  . ALA B 1 288 ? 29.322  -36.960 26.643  1.00 22.77  ? 306 ALA B HB3  1 
ATOM   8956  N  N    . ALA B 1 289 ? 31.171  -37.549 29.441  1.00 18.29  ? 307 ALA B N    1 
ATOM   8957  C  CA   . ALA B 1 289 ? 31.433  -36.805 30.667  1.00 18.51  ? 307 ALA B CA   1 
ATOM   8958  C  C    . ALA B 1 289 ? 32.908  -36.456 30.784  1.00 16.30  ? 307 ALA B C    1 
ATOM   8959  O  O    . ALA B 1 289 ? 33.261  -35.351 31.206  1.00 17.28  ? 307 ALA B O    1 
ATOM   8960  C  CB   . ALA B 1 289 ? 30.991  -37.617 31.881  1.00 20.39  ? 307 ALA B CB   1 
ATOM   8961  H  H    . ALA B 1 289 ? 30.853  -38.340 29.557  1.00 21.95  ? 307 ALA B H    1 
ATOM   8962  H  HA   . ALA B 1 289 ? 30.918  -35.982 30.647  1.00 22.21  ? 307 ALA B HA   1 
ATOM   8963  H  HB1  . ALA B 1 289 ? 30.040  -37.795 31.814  1.00 24.47  ? 307 ALA B HB1  1 
ATOM   8964  H  HB2  . ALA B 1 289 ? 31.483  -38.453 31.898  1.00 24.47  ? 307 ALA B HB2  1 
ATOM   8965  H  HB3  . ALA B 1 289 ? 31.176  -37.108 32.686  1.00 24.47  ? 307 ALA B HB3  1 
ATOM   8966  N  N    . ALA B 1 290 ? 33.789  -37.397 30.437  1.00 17.19  ? 308 ALA B N    1 
ATOM   8967  C  CA   . ALA B 1 290 ? 35.220  -37.135 30.546  1.00 16.09  ? 308 ALA B CA   1 
ATOM   8968  C  C    . ALA B 1 290 ? 35.643  -36.018 29.600  1.00 15.60  ? 308 ALA B C    1 
ATOM   8969  O  O    . ALA B 1 290 ? 36.437  -35.148 29.970  1.00 16.55  ? 308 ALA B O    1 
ATOM   8970  C  CB   . ALA B 1 290 ? 36.013  -38.414 30.271  1.00 16.89  ? 308 ALA B CB   1 
ATOM   8971  H  H    . ALA B 1 290 ? 33.587  -38.179 30.141  1.00 20.63  ? 308 ALA B H    1 
ATOM   8972  H  HA   . ALA B 1 290 ? 35.423  -36.853 31.452  1.00 19.30  ? 308 ALA B HA   1 
ATOM   8973  H  HB1  . ALA B 1 290 ? 35.808  -39.066 30.959  1.00 20.27  ? 308 ALA B HB1  1 
ATOM   8974  H  HB2  . ALA B 1 290 ? 35.760  -38.761 29.401  1.00 20.27  ? 308 ALA B HB2  1 
ATOM   8975  H  HB3  . ALA B 1 290 ? 36.960  -38.207 30.283  1.00 20.27  ? 308 ALA B HB3  1 
ATOM   8976  N  N    . ALA B 1 291 ? 35.117  -36.021 28.374  1.00 16.19  ? 309 ALA B N    1 
ATOM   8977  C  CA   . ALA B 1 291 ? 35.429  -34.942 27.445  1.00 16.70  ? 309 ALA B CA   1 
ATOM   8978  C  C    . ALA B 1 291 ? 34.921  -33.603 27.966  1.00 16.15  ? 309 ALA B C    1 
ATOM   8979  O  O    . ALA B 1 291 ? 35.596  -32.574 27.829  1.00 15.11  ? 309 ALA B O    1 
ATOM   8980  C  CB   . ALA B 1 291 ? 34.825  -35.256 26.078  1.00 17.51  ? 309 ALA B CB   1 
ATOM   8981  H  H    . ALA B 1 291 ? 34.588  -36.625 28.063  1.00 19.43  ? 309 ALA B H    1 
ATOM   8982  H  HA   . ALA B 1 291 ? 36.391  -34.875 27.343  1.00 20.04  ? 309 ALA B HA   1 
ATOM   8983  H  HB1  . ALA B 1 291 ? 33.864  -35.347 26.170  1.00 21.01  ? 309 ALA B HB1  1 
ATOM   8984  H  HB2  . ALA B 1 291 ? 35.031  -34.531 25.467  1.00 21.01  ? 309 ALA B HB2  1 
ATOM   8985  H  HB3  . ALA B 1 291 ? 35.205  -36.085 25.747  1.00 21.01  ? 309 ALA B HB3  1 
ATOM   8986  N  N    . ILE B 1 292 ? 33.736  -33.598 28.579  1.00 15.36  ? 310 ILE B N    1 
ATOM   8987  C  CA   . ILE B 1 292 ? 33.190  -32.360 29.131  1.00 15.76  ? 310 ILE B CA   1 
ATOM   8988  C  C    . ILE B 1 292 ? 34.097  -31.822 30.229  1.00 14.86  ? 310 ILE B C    1 
ATOM   8989  O  O    . ILE B 1 292 ? 34.390  -30.623 30.275  1.00 15.80  ? 310 ILE B O    1 
ATOM   8990  C  CB   . ILE B 1 292 ? 31.747  -32.593 29.620  1.00 17.04  ? 310 ILE B CB   1 
ATOM   8991  C  CG1  . ILE B 1 292 ? 30.798  -32.649 28.419  1.00 19.32  ? 310 ILE B CG1  1 
ATOM   8992  C  CG2  . ILE B 1 292 ? 31.296  -31.511 30.588  1.00 17.61  ? 310 ILE B CG2  1 
ATOM   8993  C  CD1  . ILE B 1 292 ? 29.424  -33.177 28.751  1.00 20.44  ? 310 ILE B CD1  1 
ATOM   8994  H  H    . ILE B 1 292 ? 33.235  -34.289 28.686  1.00 18.43  ? 310 ILE B H    1 
ATOM   8995  H  HA   . ILE B 1 292 ? 33.159  -31.688 28.432  1.00 18.91  ? 310 ILE B HA   1 
ATOM   8996  H  HB   . ILE B 1 292 ? 31.730  -33.439 30.094  1.00 20.45  ? 310 ILE B HB   1 
ATOM   8997  H  HG12 . ILE B 1 292 ? 30.693  -31.753 28.063  1.00 23.18  ? 310 ILE B HG12 1 
ATOM   8998  H  HG13 . ILE B 1 292 ? 31.183  -33.231 27.745  1.00 23.18  ? 310 ILE B HG13 1 
ATOM   8999  H  HG21 . ILE B 1 292 ? 31.467  -30.642 30.192  1.00 21.13  ? 310 ILE B HG21 1 
ATOM   9000  H  HG22 . ILE B 1 292 ? 30.347  -31.616 30.758  1.00 21.13  ? 310 ILE B HG22 1 
ATOM   9001  H  HG23 . ILE B 1 292 ? 31.793  -31.601 31.416  1.00 21.13  ? 310 ILE B HG23 1 
ATOM   9002  H  HD11 . ILE B 1 292 ? 28.987  -32.560 29.359  1.00 24.53  ? 310 ILE B HD11 1 
ATOM   9003  H  HD12 . ILE B 1 292 ? 28.909  -33.255 27.933  1.00 24.53  ? 310 ILE B HD12 1 
ATOM   9004  H  HD13 . ILE B 1 292 ? 29.513  -34.047 29.170  1.00 24.53  ? 310 ILE B HD13 1 
ATOM   9005  N  N    . VAL B 1 293 ? 34.562  -32.697 31.125  1.00 15.28  ? 311 VAL B N    1 
ATOM   9006  C  CA   . VAL B 1 293 ? 35.392  -32.248 32.241  1.00 16.22  ? 311 VAL B CA   1 
ATOM   9007  C  C    . VAL B 1 293 ? 36.649  -31.554 31.732  1.00 16.82  ? 311 VAL B C    1 
ATOM   9008  O  O    . VAL B 1 293 ? 37.056  -30.513 32.260  1.00 18.55  ? 311 VAL B O    1 
ATOM   9009  C  CB   . VAL B 1 293 ? 35.739  -33.432 33.167  1.00 17.11  ? 311 VAL B CB   1 
ATOM   9010  C  CG1  . VAL B 1 293 ? 36.882  -33.054 34.102  1.00 18.75  ? 311 VAL B CG1  1 
ATOM   9011  C  CG2  . VAL B 1 293 ? 34.519  -33.874 33.964  1.00 18.63  ? 311 VAL B CG2  1 
ATOM   9012  H  H    . VAL B 1 293 ? 34.413  -33.544 31.108  1.00 18.33  ? 311 VAL B H    1 
ATOM   9013  H  HA   . VAL B 1 293 ? 34.882  -31.602 32.756  1.00 19.46  ? 311 VAL B HA   1 
ATOM   9014  H  HB   . VAL B 1 293 ? 36.024  -34.181 32.621  1.00 20.54  ? 311 VAL B HB   1 
ATOM   9015  H  HG11 . VAL B 1 293 ? 36.888  -33.663 34.857  1.00 22.50  ? 311 VAL B HG11 1 
ATOM   9016  H  HG12 . VAL B 1 293 ? 37.720  -33.118 33.619  1.00 22.50  ? 311 VAL B HG12 1 
ATOM   9017  H  HG13 . VAL B 1 293 ? 36.749  -32.144 34.413  1.00 22.50  ? 311 VAL B HG13 1 
ATOM   9018  H  HG21 . VAL B 1 293 ? 33.719  -33.672 33.454  1.00 22.36  ? 311 VAL B HG21 1 
ATOM   9019  H  HG22 . VAL B 1 293 ? 34.576  -34.829 34.124  1.00 22.36  ? 311 VAL B HG22 1 
ATOM   9020  H  HG23 . VAL B 1 293 ? 34.503  -33.397 34.808  1.00 22.36  ? 311 VAL B HG23 1 
ATOM   9021  N  N    . ALA B 1 294 ? 37.284  -32.119 30.707  1.00 17.58  ? 312 ALA B N    1 
ATOM   9022  C  CA   . ALA B 1 294 ? 38.531  -31.581 30.178  1.00 17.50  ? 312 ALA B CA   1 
ATOM   9023  C  C    . ALA B 1 294 ? 38.329  -30.522 29.101  1.00 17.40  ? 312 ALA B C    1 
ATOM   9024  O  O    . ALA B 1 294 ? 39.311  -29.908 28.667  1.00 18.84  ? 312 ALA B O    1 
ATOM   9025  C  CB   . ALA B 1 294 ? 39.370  -32.721 29.588  1.00 18.51  ? 312 ALA B CB   1 
ATOM   9026  H  H    . ALA B 1 294 ? 37.009  -32.823 30.298  1.00 21.09  ? 312 ALA B H    1 
ATOM   9027  H  HA   . ALA B 1 294 ? 39.021  -31.171 30.908  1.00 20.99  ? 312 ALA B HA   1 
ATOM   9028  H  HB1  . ALA B 1 294 ? 38.865  -33.151 28.880  1.00 22.22  ? 312 ALA B HB1  1 
ATOM   9029  H  HB2  . ALA B 1 294 ? 40.194  -32.354 29.231  1.00 22.22  ? 312 ALA B HB2  1 
ATOM   9030  H  HB3  . ALA B 1 294 ? 39.570  -33.361 30.289  1.00 22.22  ? 312 ALA B HB3  1 
ATOM   9031  N  N    . GLY B 1 295 ? 37.096  -30.293 28.664  1.00 15.61  ? 313 GLY B N    1 
ATOM   9032  C  CA   . GLY B 1 295 ? 36.849  -29.531 27.467  1.00 14.29  ? 313 GLY B CA   1 
ATOM   9033  C  C    . GLY B 1 295 ? 36.502  -28.075 27.684  1.00 14.78  ? 313 GLY B C    1 
ATOM   9034  O  O    . GLY B 1 295 ? 36.478  -27.554 28.806  1.00 16.05  ? 313 GLY B O    1 
ATOM   9035  H  H    . GLY B 1 295 ? 36.383  -30.574 29.054  1.00 18.73  ? 313 GLY B H    1 
ATOM   9036  H  HA2  . GLY B 1 295 ? 37.644  -29.563 26.911  1.00 17.14  ? 313 GLY B HA2  1 
ATOM   9037  H  HA3  . GLY B 1 295 ? 36.112  -29.940 26.987  1.00 17.14  ? 313 GLY B HA3  1 
ATOM   9038  N  N    . PRO B 1 296 ? 36.217  -27.390 26.583  1.00 13.95  ? 314 PRO B N    1 
ATOM   9039  C  CA   . PRO B 1 296 ? 35.919  -25.958 26.667  1.00 14.14  ? 314 PRO B CA   1 
ATOM   9040  C  C    . PRO B 1 296 ? 34.652  -25.692 27.461  1.00 13.76  ? 314 PRO B C    1 
ATOM   9041  O  O    . PRO B 1 296 ? 33.692  -26.468 27.422  1.00 14.50  ? 314 PRO B O    1 
ATOM   9042  C  CB   . PRO B 1 296 ? 35.753  -25.541 25.204  1.00 15.88  ? 314 PRO B CB   1 
ATOM   9043  C  CG   . PRO B 1 296 ? 35.444  -26.793 24.472  1.00 17.72  ? 314 PRO B CG   1 
ATOM   9044  C  CD   . PRO B 1 296 ? 36.106  -27.915 25.210  1.00 15.15  ? 314 PRO B CD   1 
ATOM   9045  H  HA   . PRO B 1 296 ? 36.662  -25.480 27.068  1.00 16.96  ? 314 PRO B HA   1 
ATOM   9046  H  HB2  . PRO B 1 296 ? 35.025  -24.905 25.124  1.00 19.06  ? 314 PRO B HB2  1 
ATOM   9047  H  HB3  . PRO B 1 296 ? 36.577  -25.145 24.879  1.00 19.06  ? 314 PRO B HB3  1 
ATOM   9048  H  HG2  . PRO B 1 296 ? 34.483  -26.923 24.450  1.00 21.26  ? 314 PRO B HG2  1 
ATOM   9049  H  HG3  . PRO B 1 296 ? 35.791  -26.731 23.569  1.00 21.26  ? 314 PRO B HG3  1 
ATOM   9050  H  HD2  . PRO B 1 296 ? 35.557  -28.714 25.189  1.00 18.18  ? 314 PRO B HD2  1 
ATOM   9051  H  HD3  . PRO B 1 296 ? 36.982  -28.103 24.840  1.00 18.18  ? 314 PRO B HD3  1 
ATOM   9052  N  N    . LYS B 1 297 ? 34.655  -24.561 28.166  1.00 14.45  ? 315 LYS B N    1 
ATOM   9053  C  CA   . LYS B 1 297 ? 33.522  -24.107 28.959  1.00 14.77  ? 315 LYS B CA   1 
ATOM   9054  C  C    . LYS B 1 297 ? 33.446  -22.591 28.871  1.00 14.36  ? 315 LYS B C    1 
ATOM   9055  O  O    . LYS B 1 297 ? 34.478  -21.911 28.861  1.00 15.21  ? 315 LYS B O    1 
ATOM   9056  C  CB   . LYS B 1 297 ? 33.676  -24.488 30.437  1.00 16.23  ? 315 LYS B CB   1 
ATOM   9057  C  CG   . LYS B 1 297 ? 33.641  -25.985 30.712  1.00 18.20  ? 315 LYS B CG   1 
ATOM   9058  C  CD   . LYS B 1 297 ? 34.205  -26.308 32.070  1.00 21.37  ? 315 LYS B CD   1 
ATOM   9059  C  CE   . LYS B 1 297 ? 34.247  -27.809 32.333  1.00 24.48  ? 315 LYS B CE   1 
ATOM   9060  N  NZ   . LYS B 1 297 ? 32.926  -28.476 32.081  1.00 27.07  ? 315 LYS B NZ   1 
ATOM   9061  H  H    . LYS B 1 297 ? 35.326  -24.024 28.200  1.00 17.33  ? 315 LYS B H    1 
ATOM   9062  H  HA   . LYS B 1 297 ? 32.709  -24.504 28.610  1.00 17.72  ? 315 LYS B HA   1 
ATOM   9063  H  HB2  . LYS B 1 297 ? 34.529  -24.153 30.755  1.00 19.48  ? 315 LYS B HB2  1 
ATOM   9064  H  HB3  . LYS B 1 297 ? 32.952  -24.081 30.938  1.00 19.48  ? 315 LYS B HB3  1 
ATOM   9065  H  HG2  . LYS B 1 297 ? 32.722  -26.295 30.681  1.00 21.84  ? 315 LYS B HG2  1 
ATOM   9066  H  HG3  . LYS B 1 297 ? 34.170  -26.447 30.043  1.00 21.84  ? 315 LYS B HG3  1 
ATOM   9067  H  HD2  . LYS B 1 297 ? 35.110  -25.965 32.129  1.00 25.65  ? 315 LYS B HD2  1 
ATOM   9068  H  HD3  . LYS B 1 297 ? 33.650  -25.897 32.751  1.00 25.65  ? 315 LYS B HD3  1 
ATOM   9069  H  HE2  . LYS B 1 297 ? 34.905  -28.215 31.746  1.00 29.38  ? 315 LYS B HE2  1 
ATOM   9070  H  HE3  . LYS B 1 297 ? 34.490  -27.961 33.259  1.00 29.38  ? 315 LYS B HE3  1 
ATOM   9071  H  HZ1  . LYS B 1 297 ? 32.962  -29.329 32.334  1.00 32.49  ? 315 LYS B HZ1  1 
ATOM   9072  H  HZ2  . LYS B 1 297 ? 32.285  -28.065 32.543  1.00 32.49  ? 315 LYS B HZ2  1 
ATOM   9073  H  HZ3  . LYS B 1 297 ? 32.726  -28.440 31.215  1.00 32.49  ? 315 LYS B HZ3  1 
ATOM   9074  N  N    . GLN B 1 298 ? 32.226  -22.060 28.822  1.00 13.63  ? 316 GLN B N    1 
ATOM   9075  C  CA   . GLN B 1 298 ? 32.036  -20.617 28.730  1.00 14.51  ? 316 GLN B CA   1 
ATOM   9076  C  C    . GLN B 1 298 ? 30.701  -20.237 29.357  1.00 14.03  ? 316 GLN B C    1 
ATOM   9077  O  O    . GLN B 1 298 ? 29.872  -21.094 29.678  1.00 14.84  ? 316 GLN B O    1 
ATOM   9078  C  CB   . GLN B 1 298 ? 32.188  -20.124 27.288  1.00 14.14  ? 316 GLN B CB   1 
ATOM   9079  C  CG   . GLN B 1 298 ? 31.234  -20.720 26.286  1.00 14.38  ? 316 GLN B CG   1 
ATOM   9080  C  CD   . GLN B 1 298 ? 31.640  -20.369 24.864  1.00 13.71  ? 316 GLN B CD   1 
ATOM   9081  O  OE1  . GLN B 1 298 ? 32.756  -20.664 24.431  1.00 13.73  ? 316 GLN B OE1  1 
ATOM   9082  N  NE2  . GLN B 1 298 ? 30.753  -19.699 24.147  1.00 14.54  ? 316 GLN B NE2  1 
ATOM   9083  H  H    . GLN B 1 298 ? 31.496  -22.514 28.840  1.00 16.35  ? 316 GLN B H    1 
ATOM   9084  H  HA   . GLN B 1 298 ? 32.716  -20.168 29.255  1.00 17.41  ? 316 GLN B HA   1 
ATOM   9085  H  HB2  . GLN B 1 298 ? 32.050  -19.163 27.280  1.00 16.97  ? 316 GLN B HB2  1 
ATOM   9086  H  HB3  . GLN B 1 298 ? 33.087  -20.332 26.988  1.00 16.97  ? 316 GLN B HB3  1 
ATOM   9087  H  HG2  . GLN B 1 298 ? 31.234  -21.686 26.375  1.00 17.25  ? 316 GLN B HG2  1 
ATOM   9088  H  HG3  . GLN B 1 298 ? 30.342  -20.372 26.444  1.00 17.25  ? 316 GLN B HG3  1 
ATOM   9089  H  HE21 . GLN B 1 298 ? 29.994  -19.486 24.491  1.00 17.44  ? 316 GLN B HE21 1 
ATOM   9090  H  HE22 . GLN B 1 298 ? 30.935  -19.477 23.336  1.00 17.44  ? 316 GLN B HE22 1 
ATOM   9091  N  N    . ASN B 1 299 ? 30.506  -18.928 29.538  1.00 13.77  ? 317 ASN B N    1 
ATOM   9092  C  CA   . ASN B 1 299 ? 29.346  -18.404 30.249  1.00 13.74  ? 317 ASN B CA   1 
ATOM   9093  C  C    . ASN B 1 299 ? 28.315  -17.775 29.319  1.00 13.92  ? 317 ASN B C    1 
ATOM   9094  O  O    . ASN B 1 299 ? 27.443  -17.033 29.787  1.00 15.87  ? 317 ASN B O    1 
ATOM   9095  C  CB   . ASN B 1 299 ? 29.771  -17.374 31.296  1.00 15.22  ? 317 ASN B CB   1 
ATOM   9096  C  CG   . ASN B 1 299 ? 30.176  -16.056 30.678  1.00 15.29  ? 317 ASN B CG   1 
ATOM   9097  O  OD1  . ASN B 1 299 ? 30.423  -15.970 29.476  1.00 15.43  ? 317 ASN B OD1  1 
ATOM   9098  N  ND2  . ASN B 1 299 ? 30.256  -15.020 31.501  1.00 17.80  ? 317 ASN B ND2  1 
ATOM   9099  H  H    . ASN B 1 299 ? 31.041  -18.318 29.253  1.00 16.53  ? 317 ASN B H    1 
ATOM   9100  H  HA   . ASN B 1 299 ? 28.926  -19.152 30.703  1.00 16.49  ? 317 ASN B HA   1 
ATOM   9101  H  HB2  . ASN B 1 299 ? 29.029  -17.209 31.898  1.00 18.27  ? 317 ASN B HB2  1 
ATOM   9102  H  HB3  . ASN B 1 299 ? 30.530  -17.720 31.792  1.00 18.27  ? 317 ASN B HB3  1 
ATOM   9103  H  HD21 . ASN B 1 299 ? 30.483  -14.247 31.198  1.00 21.36  ? 317 ASN B HD21 1 
ATOM   9104  H  HD22 . ASN B 1 299 ? 30.082  -15.120 32.337  1.00 21.36  ? 317 ASN B HD22 1 
ATOM   9105  N  N    . CYS B 1 300 ? 28.387  -18.066 28.020  1.00 12.95  ? 318 CYS B N    1 
ATOM   9106  C  CA   . CYS B 1 300 ? 27.494  -17.463 27.041  1.00 11.91  ? 318 CYS B CA   1 
ATOM   9107  C  C    . CYS B 1 300 ? 27.416  -18.386 25.834  1.00 13.07  ? 318 CYS B C    1 
ATOM   9108  O  O    . CYS B 1 300 ? 28.322  -19.190 25.586  1.00 13.35  ? 318 CYS B O    1 
ATOM   9109  C  CB   . CYS B 1 300 ? 27.991  -16.073 26.623  1.00 14.65  ? 318 CYS B CB   1 
ATOM   9110  S  SG   . CYS B 1 300 ? 29.729  -16.017 26.116  1.00 16.04  ? 318 CYS B SG   1 
ATOM   9111  H  H    . CYS B 1 300 ? 28.953  -18.617 27.680  1.00 15.54  ? 318 CYS B H    1 
ATOM   9112  H  HA   . CYS B 1 300 ? 26.605  -17.372 27.418  1.00 14.29  ? 318 CYS B HA   1 
ATOM   9113  H  HB2  . CYS B 1 300 ? 27.457  -15.767 25.874  1.00 17.58  ? 318 CYS B HB2  1 
ATOM   9114  H  HB3  . CYS B 1 300 ? 27.886  -15.469 27.375  1.00 17.58  ? 318 CYS B HB3  1 
ATOM   9115  N  N    . GLU B 1 301 ? 26.320  -18.253 25.075  1.00 14.18  ? 319 GLU B N    1 
ATOM   9116  C  CA   . GLU B 1 301 ? 26.156  -19.069 23.876  1.00 13.81  ? 319 GLU B CA   1 
ATOM   9117  C  C    . GLU B 1 301 ? 26.982  -18.487 22.730  1.00 13.57  ? 319 GLU B C    1 
ATOM   9118  O  O    . GLU B 1 301 ? 26.975  -17.270 22.518  1.00 13.41  ? 319 GLU B O    1 
ATOM   9119  C  CB   . GLU B 1 301 ? 24.687  -19.109 23.447  1.00 13.93  ? 319 GLU B CB   1 
ATOM   9120  C  CG   . GLU B 1 301 ? 24.453  -19.877 22.151  1.00 13.95  ? 319 GLU B CG   1 
ATOM   9121  C  CD   . GLU B 1 301 ? 22.993  -19.964 21.734  1.00 14.35  ? 319 GLU B CD   1 
ATOM   9122  O  OE1  . GLU B 1 301 ? 22.104  -19.429 22.444  1.00 14.64  ? 319 GLU B OE1  1 
ATOM   9123  O  OE2  . GLU B 1 301 ? 22.744  -20.581 20.675  1.00 14.38  ? 319 GLU B OE2  1 
ATOM   9124  H  H    . GLU B 1 301 ? 25.674  -17.708 25.233  1.00 17.02  ? 319 GLU B H    1 
ATOM   9125  H  HA   . GLU B 1 301 ? 26.455  -19.973 24.062  1.00 16.57  ? 319 GLU B HA   1 
ATOM   9126  H  HB2  . GLU B 1 301 ? 24.169  -19.539 24.146  1.00 16.72  ? 319 GLU B HB2  1 
ATOM   9127  H  HB3  . GLU B 1 301 ? 24.375  -18.200 23.315  1.00 16.72  ? 319 GLU B HB3  1 
ATOM   9128  H  HG2  . GLU B 1 301 ? 24.938  -19.436 21.437  1.00 16.74  ? 319 GLU B HG2  1 
ATOM   9129  H  HG3  . GLU B 1 301 ? 24.781  -20.783 22.264  1.00 16.74  ? 319 GLU B HG3  1 
ATOM   9130  N  N    . PRO B 1 302 ? 27.672  -19.330 21.963  1.00 13.17  ? 320 PRO B N    1 
ATOM   9131  C  CA   . PRO B 1 302 ? 28.428  -18.829 20.806  1.00 13.22  ? 320 PRO B CA   1 
ATOM   9132  C  C    . PRO B 1 302 ? 27.566  -17.987 19.880  1.00 13.20  ? 320 PRO B C    1 
ATOM   9133  O  O    . PRO B 1 302 ? 26.374  -18.250 19.697  1.00 13.79  ? 320 PRO B O    1 
ATOM   9134  C  CB   . PRO B 1 302 ? 28.876  -20.111 20.092  1.00 15.25  ? 320 PRO B CB   1 
ATOM   9135  C  CG   . PRO B 1 302 ? 28.908  -21.156 21.162  1.00 15.00  ? 320 PRO B CG   1 
ATOM   9136  C  CD   . PRO B 1 302 ? 27.812  -20.791 22.128  1.00 13.89  ? 320 PRO B CD   1 
ATOM   9137  H  HA   . PRO B 1 302 ? 29.192  -18.314 21.110  1.00 15.87  ? 320 PRO B HA   1 
ATOM   9138  H  HB2  . PRO B 1 302 ? 28.239  -20.343 19.399  1.00 18.30  ? 320 PRO B HB2  1 
ATOM   9139  H  HB3  . PRO B 1 302 ? 29.756  -19.983 19.705  1.00 18.30  ? 320 PRO B HB3  1 
ATOM   9140  H  HG2  . PRO B 1 302 ? 28.746  -22.029 20.772  1.00 18.00  ? 320 PRO B HG2  1 
ATOM   9141  H  HG3  . PRO B 1 302 ? 29.772  -21.145 21.604  1.00 18.00  ? 320 PRO B HG3  1 
ATOM   9142  H  HD2  . PRO B 1 302 ? 26.985  -21.243 21.896  1.00 16.67  ? 320 PRO B HD2  1 
ATOM   9143  H  HD3  . PRO B 1 302 ? 28.067  -21.011 23.037  1.00 16.67  ? 320 PRO B HD3  1 
ATOM   9144  N  N    . ASP B 1 303 ? 28.199  -16.986 19.267  1.00 13.08  ? 321 ASP B N    1 
ATOM   9145  C  CA   . ASP B 1 303 ? 27.512  -16.164 18.285  1.00 13.65  ? 321 ASP B CA   1 
ATOM   9146  C  C    . ASP B 1 303 ? 27.074  -17.006 17.093  1.00 12.41  ? 321 ASP B C    1 
ATOM   9147  O  O    . ASP B 1 303 ? 27.781  -17.928 16.654  1.00 14.77  ? 321 ASP B O    1 
ATOM   9148  C  CB   . ASP B 1 303 ? 28.439  -15.071 17.758  1.00 14.87  ? 321 ASP B CB   1 
ATOM   9149  C  CG   . ASP B 1 303 ? 28.707  -13.984 18.764  1.00 17.92  ? 321 ASP B CG   1 
ATOM   9150  O  OD1  . ASP B 1 303 ? 27.993  -13.895 19.784  1.00 16.27  ? 321 ASP B OD1  1 
ATOM   9151  O  OD2  . ASP B 1 303 ? 29.655  -13.216 18.519  1.00 21.96  ? 321 ASP B OD2  1 
ATOM   9152  H  H    . ASP B 1 303 ? 29.019  -16.768 19.404  1.00 15.70  ? 321 ASP B H    1 
ATOM   9153  H  HA   . ASP B 1 303 ? 26.740  -15.762 18.712  1.00 16.38  ? 321 ASP B HA   1 
ATOM   9154  H  HB2  . ASP B 1 303 ? 29.290  -15.469 17.517  1.00 17.84  ? 321 ASP B HB2  1 
ATOM   9155  H  HB3  . ASP B 1 303 ? 28.032  -14.661 16.979  1.00 17.84  ? 321 ASP B HB3  1 
ATOM   9156  N  N    . LEU B 1 304 ? 25.914  -16.664 16.557  1.00 13.08  ? 322 LEU B N    1 
ATOM   9157  C  CA   . LEU B 1 304 ? 25.475  -17.243 15.300  1.00 13.90  ? 322 LEU B CA   1 
ATOM   9158  C  C    . LEU B 1 304 ? 26.312  -16.687 14.157  1.00 13.94  ? 322 LEU B C    1 
ATOM   9159  O  O    . LEU B 1 304 ? 26.662  -15.502 14.133  1.00 15.63  ? 322 LEU B O    1 
ATOM   9160  C  CB   . LEU B 1 304 ? 24.011  -16.897 15.046  1.00 14.62  ? 322 LEU B CB   1 
ATOM   9161  C  CG   . LEU B 1 304 ? 22.993  -17.535 15.983  1.00 14.30  ? 322 LEU B CG   1 
ATOM   9162  C  CD1  . LEU B 1 304 ? 21.608  -16.989 15.731  1.00 15.74  ? 322 LEU B CD1  1 
ATOM   9163  C  CD2  . LEU B 1 304 ? 22.995  -19.038 15.813  1.00 15.86  ? 322 LEU B CD2  1 
ATOM   9164  H  H    . LEU B 1 304 ? 25.362  -16.100 16.900  1.00 15.70  ? 322 LEU B H    1 
ATOM   9165  H  HA   . LEU B 1 304 ? 25.572  -18.207 15.336  1.00 16.68  ? 322 LEU B HA   1 
ATOM   9166  H  HB2  . LEU B 1 304 ? 23.911  -15.936 15.127  1.00 17.54  ? 322 LEU B HB2  1 
ATOM   9167  H  HB3  . LEU B 1 304 ? 23.787  -17.180 14.146  1.00 17.54  ? 322 LEU B HB3  1 
ATOM   9168  H  HG   . LEU B 1 304 ? 23.237  -17.322 16.897  1.00 17.16  ? 322 LEU B HG   1 
ATOM   9169  H  HD11 . LEU B 1 304 ? 21.545  -16.100 16.113  1.00 18.89  ? 322 LEU B HD11 1 
ATOM   9170  H  HD12 . LEU B 1 304 ? 21.453  -16.950 14.775  1.00 18.89  ? 322 LEU B HD12 1 
ATOM   9171  H  HD13 . LEU B 1 304 ? 20.957  -17.575 16.148  1.00 18.89  ? 322 LEU B HD13 1 
ATOM   9172  H  HD21 . LEU B 1 304 ? 22.848  -19.251 14.879  1.00 19.04  ? 322 LEU B HD21 1 
ATOM   9173  H  HD22 . LEU B 1 304 ? 23.853  -19.387 16.101  1.00 19.04  ? 322 LEU B HD22 1 
ATOM   9174  H  HD23 . LEU B 1 304 ? 22.286  -19.418 16.355  1.00 19.04  ? 322 LEU B HD23 1 
ATOM   9175  N  N    . MET B 1 305 ? 26.628  -17.552 13.203  1.00 14.18  ? 323 MET B N    1 
ATOM   9176  C  CA   . MET B 1 305 ? 27.288  -17.116 11.989  1.00 15.07  ? 323 MET B CA   1 
ATOM   9177  C  C    . MET B 1 305 ? 26.342  -16.225 11.191  1.00 15.62  ? 323 MET B C    1 
ATOM   9178  O  O    . MET B 1 305 ? 25.125  -16.275 11.374  1.00 14.58  ? 323 MET B O    1 
ATOM   9179  C  CB   . MET B 1 305 ? 27.717  -18.341 11.186  1.00 17.96  ? 323 MET B CB   1 
ATOM   9180  C  CG   . MET B 1 305 ? 28.833  -19.117 11.895  1.00 23.50  ? 323 MET B CG   1 
ATOM   9181  S  SD   . MET B 1 305 ? 29.686  -20.272 10.843  1.00 25.64  ? 323 MET B SD   1 
ATOM   9182  C  CE   . MET B 1 305 ? 30.936  -20.971 11.873  1.00 24.05  ? 323 MET B CE   1 
ATOM   9183  H  H    . MET B 1 305 ? 26.469  -18.396 13.236  1.00 17.01  ? 323 MET B H    1 
ATOM   9184  H  HA   . MET B 1 305 ? 28.089  -16.607 12.187  1.00 18.08  ? 323 MET B HA   1 
ATOM   9185  H  HB2  . MET B 1 305 ? 26.957  -18.933 11.074  1.00 21.55  ? 323 MET B HB2  1 
ATOM   9186  H  HB3  . MET B 1 305 ? 28.046  -18.057 10.319  1.00 21.55  ? 323 MET B HB3  1 
ATOM   9187  H  HG2  . MET B 1 305 ? 29.487  -18.484 12.231  1.00 28.20  ? 323 MET B HG2  1 
ATOM   9188  H  HG3  . MET B 1 305 ? 28.446  -19.617 12.631  1.00 28.20  ? 323 MET B HG3  1 
ATOM   9189  H  HE1  . MET B 1 305 ? 31.418  -21.646 11.370  1.00 28.86  ? 323 MET B HE1  1 
ATOM   9190  H  HE2  . MET B 1 305 ? 31.545  -20.268 12.150  1.00 28.86  ? 323 MET B HE2  1 
ATOM   9191  H  HE3  . MET B 1 305 ? 30.517  -21.372 12.650  1.00 28.86  ? 323 MET B HE3  1 
ATOM   9192  N  N    . PRO B 1 306 ? 26.883  -15.381 10.314  1.00 16.38  ? 324 PRO B N    1 
ATOM   9193  C  CA   . PRO B 1 306 ? 26.020  -14.423 9.598   1.00 16.17  ? 324 PRO B CA   1 
ATOM   9194  C  C    . PRO B 1 306 ? 24.850  -15.054 8.862   1.00 16.91  ? 324 PRO B C    1 
ATOM   9195  O  O    . PRO B 1 306 ? 23.770  -14.452 8.814   1.00 18.02  ? 324 PRO B O    1 
ATOM   9196  C  CB   . PRO B 1 306 ? 26.998  -13.714 8.651   1.00 17.74  ? 324 PRO B CB   1 
ATOM   9197  C  CG   . PRO B 1 306 ? 28.324  -13.827 9.342   1.00 19.26  ? 324 PRO B CG   1 
ATOM   9198  C  CD   . PRO B 1 306 ? 28.311  -15.174 10.009  1.00 18.11  ? 324 PRO B CD   1 
ATOM   9199  H  HA   . PRO B 1 306 ? 25.665  -13.775 10.227  1.00 19.40  ? 324 PRO B HA   1 
ATOM   9200  H  HB2  . PRO B 1 306 ? 27.012  -14.160 7.790   1.00 21.29  ? 324 PRO B HB2  1 
ATOM   9201  H  HB3  . PRO B 1 306 ? 26.740  -12.785 8.540   1.00 21.29  ? 324 PRO B HB3  1 
ATOM   9202  H  HG2  . PRO B 1 306 ? 29.040  -13.772 8.690   1.00 23.11  ? 324 PRO B HG2  1 
ATOM   9203  H  HG3  . PRO B 1 306 ? 28.416  -13.118 9.997   1.00 23.11  ? 324 PRO B HG3  1 
ATOM   9204  H  HD2  . PRO B 1 306 ? 28.639  -15.861 9.408   1.00 21.73  ? 324 PRO B HD2  1 
ATOM   9205  H  HD3  . PRO B 1 306 ? 28.840  -15.163 10.821  1.00 21.73  ? 324 PRO B HD3  1 
ATOM   9206  N  N    . TYR B 1 307 ? 25.007  -16.261 8.314   1.00 17.14  ? 325 TYR B N    1 
ATOM   9207  C  CA   . TYR B 1 307 ? 23.912  -16.858 7.557   1.00 16.10  ? 325 TYR B CA   1 
ATOM   9208  C  C    . TYR B 1 307 ? 22.711  -17.205 8.428   1.00 15.78  ? 325 TYR B C    1 
ATOM   9209  O  O    . TYR B 1 307 ? 21.601  -17.351 7.897   1.00 17.50  ? 325 TYR B O    1 
ATOM   9210  C  CB   . TYR B 1 307 ? 24.394  -18.101 6.810   1.00 16.98  ? 325 TYR B CB   1 
ATOM   9211  C  CG   . TYR B 1 307 ? 24.892  -19.233 7.681   1.00 16.25  ? 325 TYR B CG   1 
ATOM   9212  C  CD1  . TYR B 1 307 ? 24.007  -20.083 8.327   1.00 16.39  ? 325 TYR B CD1  1 
ATOM   9213  C  CD2  . TYR B 1 307 ? 26.248  -19.479 7.823   1.00 16.31  ? 325 TYR B CD2  1 
ATOM   9214  C  CE1  . TYR B 1 307 ? 24.456  -21.129 9.104   1.00 15.70  ? 325 TYR B CE1  1 
ATOM   9215  C  CE2  . TYR B 1 307 ? 26.708  -20.529 8.595   1.00 15.69  ? 325 TYR B CE2  1 
ATOM   9216  C  CZ   . TYR B 1 307 ? 25.802  -21.356 9.230   1.00 15.40  ? 325 TYR B CZ   1 
ATOM   9217  O  OH   . TYR B 1 307 ? 26.241  -22.410 10.007  1.00 16.99  ? 325 TYR B OH   1 
ATOM   9218  H  H    . TYR B 1 307 ? 25.719  -16.740 8.366   1.00 20.57  ? 325 TYR B H    1 
ATOM   9219  H  HA   . TYR B 1 307 ? 23.617  -16.212 6.897   1.00 19.33  ? 325 TYR B HA   1 
ATOM   9220  H  HB2  . TYR B 1 307 ? 23.656  -18.445 6.284   1.00 20.38  ? 325 TYR B HB2  1 
ATOM   9221  H  HB3  . TYR B 1 307 ? 25.125  -17.842 6.228   1.00 20.38  ? 325 TYR B HB3  1 
ATOM   9222  H  HD1  . TYR B 1 307 ? 23.092  -19.945 8.235   1.00 19.67  ? 325 TYR B HD1  1 
ATOM   9223  H  HD2  . TYR B 1 307 ? 26.860  -18.928 7.390   1.00 19.57  ? 325 TYR B HD2  1 
ATOM   9224  H  HE1  . TYR B 1 307 ? 23.848  -21.679 9.542   1.00 18.85  ? 325 TYR B HE1  1 
ATOM   9225  H  HE2  . TYR B 1 307 ? 27.621  -20.678 8.686   1.00 18.83  ? 325 TYR B HE2  1 
ATOM   9226  H  HH   . TYR B 1 307 ? 27.080  -22.428 10.020  1.00 20.39  ? 325 TYR B HH   1 
ATOM   9227  N  N    . ALA B 1 308 ? 22.900  -17.326 9.745   1.00 15.87  ? 326 ALA B N    1 
ATOM   9228  C  CA   . ALA B 1 308 ? 21.831  -17.718 10.651  1.00 14.71  ? 326 ALA B CA   1 
ATOM   9229  C  C    . ALA B 1 308 ? 21.313  -16.577 11.510  1.00 14.90  ? 326 ALA B C    1 
ATOM   9230  O  O    . ALA B 1 308 ? 20.191  -16.674 12.016  1.00 15.02  ? 326 ALA B O    1 
ATOM   9231  C  CB   . ALA B 1 308 ? 22.304  -18.844 11.584  1.00 15.32  ? 326 ALA B CB   1 
ATOM   9232  H  H    . ALA B 1 308 ? 23.651  -17.183 10.138  1.00 19.05  ? 326 ALA B H    1 
ATOM   9233  H  HA   . ALA B 1 308 ? 21.092  -18.058 10.122  1.00 17.65  ? 326 ALA B HA   1 
ATOM   9234  H  HB1  . ALA B 1 308 ? 22.491  -19.635 11.054  1.00 18.39  ? 326 ALA B HB1  1 
ATOM   9235  H  HB2  . ALA B 1 308 ? 23.108  -18.556 12.044  1.00 18.39  ? 326 ALA B HB2  1 
ATOM   9236  H  HB3  . ALA B 1 308 ? 21.605  -19.035 12.228  1.00 18.39  ? 326 ALA B HB3  1 
ATOM   9237  N  N    . ARG B 1 309 ? 22.095  -15.512 11.684  1.00 15.92  ? 327 ARG B N    1 
ATOM   9238  C  CA   . ARG B 1 309 ? 21.683  -14.416 12.556  1.00 17.34  ? 327 ARG B CA   1 
ATOM   9239  C  C    . ARG B 1 309 ? 20.294  -13.866 12.254  1.00 17.29  ? 327 ARG B C    1 
ATOM   9240  O  O    . ARG B 1 309 ? 19.574  -13.527 13.209  1.00 18.48  ? 327 ARG B O    1 
ATOM   9241  C  CB   . ARG B 1 309 ? 22.698  -13.267 12.470  1.00 20.05  ? 327 ARG B CB   1 
ATOM   9242  C  CG   . ARG B 1 309 ? 23.909  -13.466 13.336  1.00 24.27  ? 327 ARG B CG   1 
ATOM   9243  C  CD   . ARG B 1 309 ? 24.915  -12.335 13.164  1.00 28.15  ? 327 ARG B CD   1 
ATOM   9244  N  NE   . ARG B 1 309 ? 24.618  -11.182 14.016  1.00 33.20  ? 327 ARG B NE   1 
ATOM   9245  C  CZ   . ARG B 1 309 ? 23.938  -10.103 13.632  1.00 36.25  ? 327 ARG B CZ   1 
ATOM   9246  N  NH1  . ARG B 1 309 ? 23.462  -10.001 12.395  1.00 38.50  ? 327 ARG B NH1  1 
ATOM   9247  N  NH2  . ARG B 1 309 ? 23.731  -9.118  14.496  1.00 35.68  ? 327 ARG B NH2  1 
ATOM   9248  H  H    . ARG B 1 309 ? 22.863  -15.401 11.312  1.00 19.11  ? 327 ARG B H    1 
ATOM   9249  H  HA   . ARG B 1 309 ? 21.676  -14.775 13.457  1.00 20.81  ? 327 ARG B HA   1 
ATOM   9250  H  HB2  . ARG B 1 309 ? 23.001  -13.185 11.552  1.00 24.06  ? 327 ARG B HB2  1 
ATOM   9251  H  HB3  . ARG B 1 309 ? 22.265  -12.446 12.750  1.00 24.06  ? 327 ARG B HB3  1 
ATOM   9252  H  HG2  . ARG B 1 309 ? 23.637  -13.493 14.266  1.00 29.13  ? 327 ARG B HG2  1 
ATOM   9253  H  HG3  . ARG B 1 309 ? 24.343  -14.299 13.093  1.00 29.13  ? 327 ARG B HG3  1 
ATOM   9254  H  HD2  . ARG B 1 309 ? 25.799  -12.659 13.395  1.00 33.79  ? 327 ARG B HD2  1 
ATOM   9255  H  HD3  . ARG B 1 309 ? 24.901  -12.037 12.241  1.00 33.79  ? 327 ARG B HD3  1 
ATOM   9256  H  HE   . ARG B 1 309 ? 24.905  -11.204 14.827  1.00 39.85  ? 327 ARG B HE   1 
ATOM   9257  H  HH11 . ARG B 1 309 ? 23.591  -10.637 11.830  1.00 46.19  ? 327 ARG B HH11 1 
ATOM   9258  H  HH12 . ARG B 1 309 ? 23.024  -9.300  12.158  1.00 46.19  ? 327 ARG B HH12 1 
ATOM   9259  H  HH21 . ARG B 1 309 ? 24.036  -9.179  15.298  1.00 42.81  ? 327 ARG B HH21 1 
ATOM   9260  H  HH22 . ARG B 1 309 ? 23.293  -8.419  14.255  1.00 42.81  ? 327 ARG B HH22 1 
ATOM   9261  N  N    . PRO B 1 310 ? 19.872  -13.705 10.999  1.00 17.61  ? 328 PRO B N    1 
ATOM   9262  C  CA   . PRO B 1 310 ? 18.553  -13.098 10.748  1.00 18.95  ? 328 PRO B CA   1 
ATOM   9263  C  C    . PRO B 1 310 ? 17.394  -13.889 11.328  1.00 18.25  ? 328 PRO B C    1 
ATOM   9264  O  O    . PRO B 1 310 ? 16.282  -13.354 11.408  1.00 20.48  ? 328 PRO B O    1 
ATOM   9265  C  CB   . PRO B 1 310 ? 18.480  -13.022 9.214   1.00 20.88  ? 328 PRO B CB   1 
ATOM   9266  C  CG   . PRO B 1 310 ? 19.914  -13.007 8.773   1.00 22.14  ? 328 PRO B CG   1 
ATOM   9267  C  CD   . PRO B 1 310 ? 20.642  -13.892 9.755   1.00 19.60  ? 328 PRO B CD   1 
ATOM   9268  H  HA   . PRO B 1 310 ? 18.528  -12.197 11.106  1.00 22.74  ? 328 PRO B HA   1 
ATOM   9269  H  HB2  . PRO B 1 310 ? 18.015  -13.798 8.864   1.00 25.05  ? 328 PRO B HB2  1 
ATOM   9270  H  HB3  . PRO B 1 310 ? 18.022  -12.211 8.942   1.00 25.05  ? 328 PRO B HB3  1 
ATOM   9271  H  HG2  . PRO B 1 310 ? 19.985  -13.359 7.872   1.00 26.57  ? 328 PRO B HG2  1 
ATOM   9272  H  HG3  . PRO B 1 310 ? 20.258  -12.101 8.803   1.00 26.57  ? 328 PRO B HG3  1 
ATOM   9273  H  HD2  . PRO B 1 310 ? 20.621  -14.819 9.470   1.00 23.52  ? 328 PRO B HD2  1 
ATOM   9274  H  HD3  . PRO B 1 310 ? 21.561  -13.601 9.869   1.00 23.52  ? 328 PRO B HD3  1 
ATOM   9275  N  N    . PHE B 1 311 ? 17.621  -15.132 11.740  1.00 16.57  ? 329 PHE B N    1 
ATOM   9276  C  CA   . PHE B 1 311 ? 16.561  -16.006 12.216  1.00 16.16  ? 329 PHE B CA   1 
ATOM   9277  C  C    . PHE B 1 311 ? 16.459  -16.065 13.732  1.00 15.79  ? 329 PHE B C    1 
ATOM   9278  O  O    . PHE B 1 311 ? 15.619  -16.807 14.251  1.00 16.34  ? 329 PHE B O    1 
ATOM   9279  C  CB   . PHE B 1 311 ? 16.758  -17.402 11.622  1.00 15.87  ? 329 PHE B CB   1 
ATOM   9280  C  CG   . PHE B 1 311 ? 16.730  -17.415 10.120  1.00 16.55  ? 329 PHE B CG   1 
ATOM   9281  C  CD1  . PHE B 1 311 ? 15.522  -17.364 9.439   1.00 16.42  ? 329 PHE B CD1  1 
ATOM   9282  C  CD2  . PHE B 1 311 ? 17.905  -17.453 9.388   1.00 16.27  ? 329 PHE B CD2  1 
ATOM   9283  C  CE1  . PHE B 1 311 ? 15.488  -17.379 8.066   1.00 18.14  ? 329 PHE B CE1  1 
ATOM   9284  C  CE2  . PHE B 1 311 ? 17.872  -17.452 8.004   1.00 16.86  ? 329 PHE B CE2  1 
ATOM   9285  C  CZ   . PHE B 1 311 ? 16.663  -17.418 7.347   1.00 18.58  ? 329 PHE B CZ   1 
ATOM   9286  H  H    . PHE B 1 311 ? 18.399  -15.498 11.752  1.00 19.88  ? 329 PHE B H    1 
ATOM   9287  H  HA   . PHE B 1 311 ? 15.705  -15.672 11.905  1.00 19.40  ? 329 PHE B HA   1 
ATOM   9288  H  HB2  . PHE B 1 311 ? 17.618  -17.746 11.907  1.00 19.05  ? 329 PHE B HB2  1 
ATOM   9289  H  HB3  . PHE B 1 311 ? 16.047  -17.981 11.938  1.00 19.05  ? 329 PHE B HB3  1 
ATOM   9290  H  HD1  . PHE B 1 311 ? 14.726  -17.319 9.918   1.00 19.70  ? 329 PHE B HD1  1 
ATOM   9291  H  HD2  . PHE B 1 311 ? 18.723  -17.479 9.830   1.00 19.53  ? 329 PHE B HD2  1 
ATOM   9292  H  HE1  . PHE B 1 311 ? 14.671  -17.363 7.621   1.00 21.77  ? 329 PHE B HE1  1 
ATOM   9293  H  HE2  . PHE B 1 311 ? 18.666  -17.475 7.519   1.00 20.23  ? 329 PHE B HE2  1 
ATOM   9294  H  HZ   . PHE B 1 311 ? 16.639  -17.421 6.417   1.00 22.30  ? 329 PHE B HZ   1 
ATOM   9295  N  N    . ALA B 1 312 ? 17.247  -15.271 14.455  1.00 15.01  ? 330 ALA B N    1 
ATOM   9296  C  CA   . ALA B 1 312 ? 17.200  -15.278 15.917  1.00 14.75  ? 330 ALA B CA   1 
ATOM   9297  C  C    . ALA B 1 312 ? 17.398  -13.875 16.478  1.00 14.85  ? 330 ALA B C    1 
ATOM   9298  O  O    . ALA B 1 312 ? 17.997  -13.689 17.542  1.00 16.21  ? 330 ALA B O    1 
ATOM   9299  C  CB   . ALA B 1 312 ? 18.216  -16.254 16.506  1.00 14.99  ? 330 ALA B CB   1 
ATOM   9300  H  H    . ALA B 1 312 ? 17.817  -14.719 14.122  1.00 18.01  ? 330 ALA B H    1 
ATOM   9301  H  HA   . ALA B 1 312 ? 16.316  -15.572 16.187  1.00 17.70  ? 330 ALA B HA   1 
ATOM   9302  H  HB1  . ALA B 1 312 ? 18.133  -16.251 17.472  1.00 17.98  ? 330 ALA B HB1  1 
ATOM   9303  H  HB2  . ALA B 1 312 ? 18.036  -17.143 16.161  1.00 17.98  ? 330 ALA B HB2  1 
ATOM   9304  H  HB3  . ALA B 1 312 ? 19.108  -15.974 16.249  1.00 17.98  ? 330 ALA B HB3  1 
ATOM   9305  N  N    . VAL B 1 313 ? 16.878  -12.869 15.775  1.00 14.88  ? 331 VAL B N    1 
ATOM   9306  C  CA   . VAL B 1 313 ? 16.929  -11.499 16.270  1.00 15.51  ? 331 VAL B CA   1 
ATOM   9307  C  C    . VAL B 1 313 ? 16.326  -11.440 17.665  1.00 15.41  ? 331 VAL B C    1 
ATOM   9308  O  O    . VAL B 1 313 ? 15.255  -12.001 17.916  1.00 16.52  ? 331 VAL B O    1 
ATOM   9309  C  CB   . VAL B 1 313 ? 16.186  -10.572 15.289  1.00 16.33  ? 331 VAL B CB   1 
ATOM   9310  C  CG1  . VAL B 1 313 ? 15.972  -9.217  15.906  1.00 17.08  ? 331 VAL B CG1  1 
ATOM   9311  C  CG2  . VAL B 1 313 ? 16.963  -10.457 13.994  1.00 17.76  ? 331 VAL B CG2  1 
ATOM   9312  H  H    . VAL B 1 313 ? 16.492  -12.954 15.011  1.00 17.85  ? 331 VAL B H    1 
ATOM   9313  H  HA   . VAL B 1 313 ? 17.854  -11.212 16.332  1.00 18.61  ? 331 VAL B HA   1 
ATOM   9314  H  HB   . VAL B 1 313 ? 15.314  -10.948 15.091  1.00 19.60  ? 331 VAL B HB   1 
ATOM   9315  H  HG11 . VAL B 1 313 ? 15.680  -8.599  15.218  1.00 20.49  ? 331 VAL B HG11 1 
ATOM   9316  H  HG12 . VAL B 1 313 ? 15.295  -9.287  16.597  1.00 20.49  ? 331 VAL B HG12 1 
ATOM   9317  H  HG13 . VAL B 1 313 ? 16.808  -8.910  16.291  1.00 20.49  ? 331 VAL B HG13 1 
ATOM   9318  H  HG21 . VAL B 1 313 ? 16.486  -9.866  13.391  1.00 21.31  ? 331 VAL B HG21 1 
ATOM   9319  H  HG22 . VAL B 1 313 ? 17.843  -10.095 14.185  1.00 21.31  ? 331 VAL B HG22 1 
ATOM   9320  H  HG23 . VAL B 1 313 ? 17.047  -11.338 13.597  1.00 21.31  ? 331 VAL B HG23 1 
ATOM   9321  N  N    . GLY B 1 314 ? 17.011  -10.756 18.583  1.00 15.68  ? 332 GLY B N    1 
ATOM   9322  C  CA   . GLY B 1 314 ? 16.547  -10.604 19.943  1.00 14.93  ? 332 GLY B CA   1 
ATOM   9323  C  C    . GLY B 1 314 ? 17.172  -11.559 20.943  1.00 16.34  ? 332 GLY B C    1 
ATOM   9324  O  O    . GLY B 1 314 ? 17.141  -11.279 22.151  1.00 17.65  ? 332 GLY B O    1 
ATOM   9325  H  H    . GLY B 1 314 ? 17.762  -10.366 18.428  1.00 18.82  ? 332 GLY B H    1 
ATOM   9326  H  HA2  . GLY B 1 314 ? 16.739  -9.700  20.238  1.00 17.92  ? 332 GLY B HA2  1 
ATOM   9327  H  HA3  . GLY B 1 314 ? 15.587  -10.744 19.961  1.00 17.92  ? 332 GLY B HA3  1 
ATOM   9328  N  N    . LYS B 1 315 ? 17.733  -12.668 20.478  1.00 15.65  ? 333 LYS B N    1 
ATOM   9329  C  CA   . LYS B 1 315 ? 18.405  -13.613 21.357  1.00 15.79  ? 333 LYS B CA   1 
ATOM   9330  C  C    . LYS B 1 315 ? 19.788  -13.079 21.725  1.00 16.42  ? 333 LYS B C    1 
ATOM   9331  O  O    . LYS B 1 315 ? 20.378  -12.268 21.008  1.00 18.04  ? 333 LYS B O    1 
ATOM   9332  C  CB   . LYS B 1 315 ? 18.512  -14.976 20.676  1.00 16.93  ? 333 LYS B CB   1 
ATOM   9333  C  CG   . LYS B 1 315 ? 17.172  -15.698 20.554  1.00 19.63  ? 333 LYS B CG   1 
ATOM   9334  C  CD   . LYS B 1 315 ? 16.731  -16.217 21.910  1.00 24.71  ? 333 LYS B CD   1 
ATOM   9335  C  CE   . LYS B 1 315 ? 15.317  -16.751 21.894  1.00 28.72  ? 333 LYS B CE   1 
ATOM   9336  N  NZ   . LYS B 1 315 ? 14.957  -17.297 23.238  1.00 30.45  ? 333 LYS B NZ   1 
ATOM   9337  H  H    . LYS B 1 315 ? 17.738  -12.898 19.649  1.00 18.78  ? 333 LYS B H    1 
ATOM   9338  H  HA   . LYS B 1 315 ? 17.901  -13.734 22.177  1.00 18.95  ? 333 LYS B HA   1 
ATOM   9339  H  HB2  . LYS B 1 315 ? 18.866  -14.853 19.782  1.00 20.31  ? 333 LYS B HB2  1 
ATOM   9340  H  HB3  . LYS B 1 315 ? 19.108  -15.539 21.195  1.00 20.31  ? 333 LYS B HB3  1 
ATOM   9341  H  HG2  . LYS B 1 315 ? 16.499  -15.083 20.223  1.00 23.56  ? 333 LYS B HG2  1 
ATOM   9342  H  HG3  . LYS B 1 315 ? 17.261  -16.450 19.948  1.00 23.56  ? 333 LYS B HG3  1 
ATOM   9343  H  HD2  . LYS B 1 315 ? 17.322  -16.937 22.182  1.00 29.65  ? 333 LYS B HD2  1 
ATOM   9344  H  HD3  . LYS B 1 315 ? 16.772  -15.493 22.555  1.00 29.65  ? 333 LYS B HD3  1 
ATOM   9345  H  HE2  . LYS B 1 315 ? 14.700  -16.036 21.674  1.00 34.46  ? 333 LYS B HE2  1 
ATOM   9346  H  HE3  . LYS B 1 315 ? 15.245  -17.464 21.241  1.00 34.46  ? 333 LYS B HE3  1 
ATOM   9347  H  HZ1  . LYS B 1 315 ? 14.124  -17.610 23.226  1.00 36.54  ? 333 LYS B HZ1  1 
ATOM   9348  H  HZ2  . LYS B 1 315 ? 15.511  -17.959 23.456  1.00 36.54  ? 333 LYS B HZ2  1 
ATOM   9349  H  HZ3  . LYS B 1 315 ? 15.016  -16.656 23.853  1.00 36.54  ? 333 LYS B HZ3  1 
ATOM   9350  N  N    . ARG B 1 316 ? 20.304  -13.532 22.864  1.00 17.27  ? 334 ARG B N    1 
ATOM   9351  C  CA   . ARG B 1 316 ? 21.576  -13.037 23.379  1.00 17.56  ? 334 ARG B CA   1 
ATOM   9352  C  C    . ARG B 1 316 ? 22.644  -14.115 23.261  1.00 16.91  ? 334 ARG B C    1 
ATOM   9353  O  O    . ARG B 1 316 ? 22.504  -15.202 23.836  1.00 18.93  ? 334 ARG B O    1 
ATOM   9354  C  CB   . ARG B 1 316 ? 21.477  -12.562 24.829  1.00 21.28  ? 334 ARG B CB   1 
ATOM   9355  C  CG   . ARG B 1 316 ? 22.784  -11.944 25.350  1.00 24.92  ? 334 ARG B CG   1 
ATOM   9356  C  CD   . ARG B 1 316 ? 22.719  -11.579 26.827  1.00 30.70  ? 334 ARG B CD   1 
ATOM   9357  N  NE   . ARG B 1 316 ? 22.475  -10.154 27.051  1.00 36.95  ? 334 ARG B NE   1 
ATOM   9358  C  CZ   . ARG B 1 316 ? 23.362  -9.183  26.830  1.00 39.91  ? 334 ARG B CZ   1 
ATOM   9359  N  NH1  . ARG B 1 316 ? 24.576  -9.461  26.367  1.00 39.81  ? 334 ARG B NH1  1 
ATOM   9360  N  NH2  . ARG B 1 316 ? 23.032  -7.922  27.077  1.00 41.07  ? 334 ARG B NH2  1 
ATOM   9361  H  H    . ARG B 1 316 ? 19.932  -14.129 23.359  1.00 20.73  ? 334 ARG B H    1 
ATOM   9362  H  HA   . ARG B 1 316 ? 21.836  -12.282 22.827  1.00 21.07  ? 334 ARG B HA   1 
ATOM   9363  H  HB2  . ARG B 1 316 ? 20.781  -11.888 24.893  1.00 25.54  ? 334 ARG B HB2  1 
ATOM   9364  H  HB3  . ARG B 1 316 ? 21.258  -13.319 25.394  1.00 25.54  ? 334 ARG B HB3  1 
ATOM   9365  H  HG2  . ARG B 1 316 ? 23.504  -12.583 25.231  1.00 29.91  ? 334 ARG B HG2  1 
ATOM   9366  H  HG3  . ARG B 1 316 ? 22.973  -11.135 24.849  1.00 29.91  ? 334 ARG B HG3  1 
ATOM   9367  H  HD2  . ARG B 1 316 ? 21.997  -12.075 27.243  1.00 36.84  ? 334 ARG B HD2  1 
ATOM   9368  H  HD3  . ARG B 1 316 ? 23.563  -11.807 27.246  1.00 36.84  ? 334 ARG B HD3  1 
ATOM   9369  H  HE   . ARG B 1 316 ? 21.701  -9.926  27.348  1.00 44.35  ? 334 ARG B HE   1 
ATOM   9370  H  HH11 . ARG B 1 316 ? 24.799  -10.275 26.205  1.00 47.78  ? 334 ARG B HH11 1 
ATOM   9371  H  HH12 . ARG B 1 316 ? 25.140  -8.826  26.228  1.00 47.78  ? 334 ARG B HH12 1 
ATOM   9372  H  HH21 . ARG B 1 316 ? 22.248  -7.734  27.377  1.00 49.28  ? 334 ARG B HH21 1 
ATOM   9373  H  HH22 . ARG B 1 316 ? 23.601  -7.293  26.936  1.00 49.28  ? 334 ARG B HH22 1 
ATOM   9374  N  N    . THR B 1 317 ? 23.718  -13.794 22.557  1.00 14.80  ? 335 THR B N    1 
ATOM   9375  C  CA   . THR B 1 317 ? 24.900  -14.636 22.457  1.00 14.07  ? 335 THR B CA   1 
ATOM   9376  C  C    . THR B 1 317 ? 26.081  -13.867 23.056  1.00 13.87  ? 335 THR B C    1 
ATOM   9377  O  O    . THR B 1 317 ? 25.921  -12.774 23.612  1.00 14.84  ? 335 THR B O    1 
ATOM   9378  C  CB   . THR B 1 317 ? 25.126  -15.070 21.006  1.00 14.55  ? 335 THR B CB   1 
ATOM   9379  O  OG1  . THR B 1 317 ? 25.334  -13.916 20.188  1.00 15.08  ? 335 THR B OG1  1 
ATOM   9380  C  CG2  . THR B 1 317 ? 23.926  -15.832 20.469  1.00 15.13  ? 335 THR B CG2  1 
ATOM   9381  H  H    . THR B 1 317 ? 23.789  -13.063 22.110  1.00 17.77  ? 335 THR B H    1 
ATOM   9382  H  HA   . THR B 1 317 ? 24.779  -15.449 22.972  1.00 16.89  ? 335 THR B HA   1 
ATOM   9383  H  HB   . THR B 1 317 ? 25.902  -15.650 20.969  1.00 17.46  ? 335 THR B HB   1 
ATOM   9384  H  HG1  . THR B 1 317 ? 26.032  -13.515 20.427  1.00 18.10  ? 335 THR B HG1  1 
ATOM   9385  H  HG21 . THR B 1 317 ? 24.134  -16.207 19.599  1.00 18.15  ? 335 THR B HG21 1 
ATOM   9386  H  HG22 . THR B 1 317 ? 23.693  -16.552 21.075  1.00 18.15  ? 335 THR B HG22 1 
ATOM   9387  H  HG23 . THR B 1 317 ? 23.167  -15.235 20.382  1.00 18.15  ? 335 THR B HG23 1 
ATOM   9388  N  N    . CYS B 1 318 ? 27.276  -14.448 22.941  1.00 14.08  ? 336 CYS B N    1 
ATOM   9389  C  CA   . CYS B 1 318 ? 28.435  -13.902 23.645  1.00 13.87  ? 336 CYS B CA   1 
ATOM   9390  C  C    . CYS B 1 318 ? 28.690  -12.436 23.299  1.00 14.61  ? 336 CYS B C    1 
ATOM   9391  O  O    . CYS B 1 318 ? 29.114  -11.657 24.163  1.00 17.28  ? 336 CYS B O    1 
ATOM   9392  C  CB   . CYS B 1 318 ? 29.667  -14.760 23.345  1.00 14.85  ? 336 CYS B CB   1 
ATOM   9393  S  SG   . CYS B 1 318 ? 29.668  -16.407 24.115  1.00 15.66  ? 336 CYS B SG   1 
ATOM   9394  H  H    . CYS B 1 318 ? 27.441  -15.149 22.470  1.00 16.90  ? 336 CYS B H    1 
ATOM   9395  H  HA   . CYS B 1 318 ? 28.261  -13.937 24.599  1.00 16.65  ? 336 CYS B HA   1 
ATOM   9396  H  HB2  . CYS B 1 318 ? 29.725  -14.888 22.385  1.00 17.82  ? 336 CYS B HB2  1 
ATOM   9397  H  HB3  . CYS B 1 318 ? 30.453  -14.290 23.664  1.00 17.82  ? 336 CYS B HB3  1 
ATOM   9398  N  N    . SER B 1 319 ? 28.460  -12.038 22.044  1.00 13.75  ? 337 SER B N    1 
ATOM   9399  C  CA   . SER B 1 319 ? 28.745  -10.668 21.635  1.00 15.94  ? 337 SER B CA   1 
ATOM   9400  C  C    . SER B 1 319 ? 27.613  -9.704  21.968  1.00 15.57  ? 337 SER B C    1 
ATOM   9401  O  O    . SER B 1 319 ? 27.782  -8.489  21.799  1.00 18.23  ? 337 SER B O    1 
ATOM   9402  C  CB   . SER B 1 319 ? 29.039  -10.607 20.137  1.00 19.08  ? 337 SER B CB   1 
ATOM   9403  O  OG   . SER B 1 319 ? 30.319  -11.146 19.853  1.00 22.98  ? 337 SER B OG   1 
ATOM   9404  H  H    . SER B 1 319 ? 28.143  -12.540 21.421  1.00 16.50  ? 337 SER B H    1 
ATOM   9405  H  HA   . SER B 1 319 ? 29.540  -10.370 22.103  1.00 19.13  ? 337 SER B HA   1 
ATOM   9406  H  HB2  . SER B 1 319 ? 28.368  -11.120 19.661  1.00 22.89  ? 337 SER B HB2  1 
ATOM   9407  H  HB3  . SER B 1 319 ? 29.015  -9.681  19.848  1.00 22.89  ? 337 SER B HB3  1 
ATOM   9408  H  HG   . SER B 1 319 ? 30.345  -11.956 20.073  1.00 27.58  ? 337 SER B HG   1 
ATOM   9409  N  N    . GLY B 1 320 ? 26.468  -10.214 22.429  1.00 14.50  ? 338 GLY B N    1 
ATOM   9410  C  CA   . GLY B 1 320 ? 25.340  -9.395  22.806  1.00 16.20  ? 338 GLY B CA   1 
ATOM   9411  C  C    . GLY B 1 320 ? 24.055  -9.843  22.134  1.00 16.20  ? 338 GLY B C    1 
ATOM   9412  O  O    . GLY B 1 320 ? 23.958  -10.945 21.581  1.00 15.04  ? 338 GLY B O    1 
ATOM   9413  H  H    . GLY B 1 320 ? 26.328  -11.056 22.530  1.00 17.40  ? 338 GLY B H    1 
ATOM   9414  H  HA2  . GLY B 1 320 ? 25.215  -9.441  23.767  1.00 19.44  ? 338 GLY B HA2  1 
ATOM   9415  H  HA3  . GLY B 1 320 ? 25.512  -8.474  22.555  1.00 19.44  ? 338 GLY B HA3  1 
ATOM   9416  N  N    . ILE B 1 321 ? 23.062  -8.959  22.186  1.00 15.83  ? 339 ILE B N    1 
ATOM   9417  C  CA   . ILE B 1 321 ? 21.756  -9.236  21.611  1.00 16.48  ? 339 ILE B CA   1 
ATOM   9418  C  C    . ILE B 1 321 ? 21.847  -9.165  20.092  1.00 15.98  ? 339 ILE B C    1 
ATOM   9419  O  O    . ILE B 1 321 ? 22.389  -8.207  19.522  1.00 17.71  ? 339 ILE B O    1 
ATOM   9420  C  CB   . ILE B 1 321 ? 20.721  -8.245  22.168  1.00 19.13  ? 339 ILE B CB   1 
ATOM   9421  C  CG1  . ILE B 1 321 ? 20.540  -8.446  23.680  1.00 21.12  ? 339 ILE B CG1  1 
ATOM   9422  C  CG2  . ILE B 1 321 ? 19.398  -8.400  21.447  1.00 19.09  ? 339 ILE B CG2  1 
ATOM   9423  C  CD1  . ILE B 1 321 ? 19.882  -7.283  24.386  1.00 23.14  ? 339 ILE B CD1  1 
ATOM   9424  H  H    . ILE B 1 321 ? 23.123  -8.183  22.553  1.00 19.00  ? 339 ILE B H    1 
ATOM   9425  H  HA   . ILE B 1 321 ? 21.478  -10.135 21.850  1.00 19.78  ? 339 ILE B HA   1 
ATOM   9426  H  HB   . ILE B 1 321 ? 21.051  -7.346  22.017  1.00 22.96  ? 339 ILE B HB   1 
ATOM   9427  H  HG12 . ILE B 1 321 ? 19.986  -9.230  23.825  1.00 25.34  ? 339 ILE B HG12 1 
ATOM   9428  H  HG13 . ILE B 1 321 ? 21.413  -8.579  24.082  1.00 25.34  ? 339 ILE B HG13 1 
ATOM   9429  H  HG21 . ILE B 1 321 ? 19.474  -8.014  20.561  1.00 22.90  ? 339 ILE B HG21 1 
ATOM   9430  H  HG22 . ILE B 1 321 ? 19.184  -9.344  21.379  1.00 22.90  ? 339 ILE B HG22 1 
ATOM   9431  H  HG23 . ILE B 1 321 ? 18.709  -7.940  21.951  1.00 22.90  ? 339 ILE B HG23 1 
ATOM   9432  H  HD11 . ILE B 1 321 ? 19.194  -6.913  23.812  1.00 27.77  ? 339 ILE B HD11 1 
ATOM   9433  H  HD12 . ILE B 1 321 ? 19.487  -7.599  25.214  1.00 27.77  ? 339 ILE B HD12 1 
ATOM   9434  H  HD13 . ILE B 1 321 ? 20.553  -6.609  24.576  1.00 27.77  ? 339 ILE B HD13 1 
ATOM   9435  N  N    . VAL B 1 322 ? 21.314  -10.187 19.427  1.00 15.28  ? 340 VAL B N    1 
ATOM   9436  C  CA   . VAL B 1 322 ? 21.308  -10.217 17.971  1.00 15.14  ? 340 VAL B CA   1 
ATOM   9437  C  C    . VAL B 1 322 ? 20.374  -9.142  17.438  1.00 15.74  ? 340 VAL B C    1 
ATOM   9438  O  O    . VAL B 1 322 ? 19.189  -9.090  17.797  1.00 15.68  ? 340 VAL B O    1 
ATOM   9439  C  CB   . VAL B 1 322 ? 20.870  -11.603 17.481  1.00 15.06  ? 340 VAL B CB   1 
ATOM   9440  C  CG1  . VAL B 1 322 ? 20.817  -11.632 15.966  1.00 15.93  ? 340 VAL B CG1  1 
ATOM   9441  C  CG2  . VAL B 1 322 ? 21.805  -12.682 18.018  1.00 16.26  ? 340 VAL B CG2  1 
ATOM   9442  H  H    . VAL B 1 322 ? 20.951  -10.873 19.796  1.00 18.34  ? 340 VAL B H    1 
ATOM   9443  H  HA   . VAL B 1 322 ? 22.203  -10.031 17.648  1.00 18.16  ? 340 VAL B HA   1 
ATOM   9444  H  HB   . VAL B 1 322 ? 19.980  -11.792 17.816  1.00 18.08  ? 340 VAL B HB   1 
ATOM   9445  H  HG11 . VAL B 1 322 ? 21.599  -11.179 15.614  1.00 19.12  ? 340 VAL B HG11 1 
ATOM   9446  H  HG12 . VAL B 1 322 ? 20.807  -12.555 15.668  1.00 19.12  ? 340 VAL B HG12 1 
ATOM   9447  H  HG13 . VAL B 1 322 ? 20.011  -11.180 15.670  1.00 19.12  ? 340 VAL B HG13 1 
ATOM   9448  H  HG21 . VAL B 1 322 ? 21.606  -13.522 17.575  1.00 19.51  ? 340 VAL B HG21 1 
ATOM   9449  H  HG22 . VAL B 1 322 ? 22.722  -12.423 17.839  1.00 19.51  ? 340 VAL B HG22 1 
ATOM   9450  H  HG23 . VAL B 1 322 ? 21.666  -12.772 18.974  1.00 19.51  ? 340 VAL B HG23 1 
ATOM   9451  N  N    . THR B 1 323 ? 20.895  -8.299  16.565  1.00 16.58  ? 341 THR B N    1 
ATOM   9452  C  CA   . THR B 1 323 ? 20.131  -7.236  15.934  1.00 17.47  ? 341 THR B CA   1 
ATOM   9453  C  C    . THR B 1 323 ? 19.789  -7.617  14.503  1.00 17.61  ? 341 THR B C    1 
ATOM   9454  O  O    . THR B 1 323 ? 20.425  -8.493  13.906  1.00 18.63  ? 341 THR B O    1 
ATOM   9455  C  CB   . THR B 1 323 ? 20.935  -5.928  15.926  1.00 19.66  ? 341 THR B CB   1 
ATOM   9456  O  OG1  . THR B 1 323 ? 22.232  -6.157  15.364  1.00 22.29  ? 341 THR B OG1  1 
ATOM   9457  C  CG2  . THR B 1 323 ? 21.083  -5.380  17.336  1.00 21.54  ? 341 THR B CG2  1 
ATOM   9458  H  H    . THR B 1 323 ? 21.717  -8.323  16.314  1.00 19.90  ? 341 THR B H    1 
ATOM   9459  H  HA   . THR B 1 323 ? 19.311  -7.086  16.430  1.00 20.96  ? 341 THR B HA   1 
ATOM   9460  H  HB   . THR B 1 323 ? 20.466  -5.268  15.391  1.00 23.60  ? 341 THR B HB   1 
ATOM   9461  H  HG1  . THR B 1 323 ? 22.655  -6.709  15.834  1.00 26.75  ? 341 THR B HG1  1 
ATOM   9462  H  HG21 . THR B 1 323 ? 21.663  -5.958  17.857  1.00 25.85  ? 341 THR B HG21 1 
ATOM   9463  H  HG22 . THR B 1 323 ? 21.468  -4.490  17.308  1.00 25.85  ? 341 THR B HG22 1 
ATOM   9464  H  HG23 . THR B 1 323 ? 20.216  -5.335  17.768  1.00 25.85  ? 341 THR B HG23 1 
ATOM   9465  N  N    . PRO B 1 324 ? 18.766  -6.983  13.921  1.00 17.83  ? 342 PRO B N    1 
ATOM   9466  C  CA   . PRO B 1 324 ? 18.402  -7.274  12.533  1.00 19.34  ? 342 PRO B CA   1 
ATOM   9467  C  C    . PRO B 1 324 ? 19.370  -6.645  11.541  1.00 23.18  ? 342 PRO B C    1 
ATOM   9468  O  O    . PRO B 1 324 ? 19.358  -7.148  10.414  1.00 27.23  ? 342 PRO B O    1 
ATOM   9469  C  CB   . PRO B 1 324 ? 17.009  -6.653  12.391  1.00 19.41  ? 342 PRO B CB   1 
ATOM   9470  C  CG   . PRO B 1 324 ? 16.978  -5.570  13.403  1.00 17.91  ? 342 PRO B CG   1 
ATOM   9471  C  CD   . PRO B 1 324 ? 17.832  -6.041  14.559  1.00 17.67  ? 342 PRO B CD   1 
ATOM   9472  H  HA   . PRO B 1 324 ? 18.348  -8.230  12.382  1.00 23.21  ? 342 PRO B HA   1 
ATOM   9473  H  HB2  . PRO B 1 324 ? 16.893  -6.296  11.496  1.00 23.29  ? 342 PRO B HB2  1 
ATOM   9474  H  HB3  . PRO B 1 324 ? 16.328  -7.319  12.573  1.00 23.29  ? 342 PRO B HB3  1 
ATOM   9475  H  HG2  . PRO B 1 324 ? 17.341  -4.756  13.020  1.00 21.49  ? 342 PRO B HG2  1 
ATOM   9476  H  HG3  . PRO B 1 324 ? 16.064  -5.422  13.693  1.00 21.49  ? 342 PRO B HG3  1 
ATOM   9477  H  HD2  . PRO B 1 324 ? 18.310  -5.298  14.960  1.00 21.21  ? 342 PRO B HD2  1 
ATOM   9478  H  HD3  . PRO B 1 324 ? 17.292  -6.489  15.228  1.00 21.21  ? 342 PRO B HD3  1 
HETATM 9479  O  O1   . TLA C 2 .   ? 17.724  12.653  16.718  1.00 60.68  ? 401 TLA A O1   1 
HETATM 9480  O  O11  . TLA C 2 .   ? 16.320  11.655  18.053  1.00 40.25  ? 401 TLA A O11  1 
HETATM 9481  C  C1   . TLA C 2 .   ? 17.267  11.598  17.225  1.00 30.57  ? 401 TLA A C1   1 
HETATM 9482  C  C2   . TLA C 2 .   ? 17.850  10.246  16.827  1.00 53.56  ? 401 TLA A C2   1 
HETATM 9483  O  O2   . TLA C 2 .   ? 16.943  9.234   17.167  1.00 45.42  ? 401 TLA A O2   1 
HETATM 9484  C  C3   . TLA C 2 .   ? 19.165  10.023  17.567  1.00 119.44 ? 401 TLA A C3   1 
HETATM 9485  O  O3   . TLA C 2 .   ? 19.077  10.573  18.851  1.00 92.28  ? 401 TLA A O3   1 
HETATM 9486  C  C4   . TLA C 2 .   ? 19.433  8.523   17.665  1.00 146.18 ? 401 TLA A C4   1 
HETATM 9487  O  O4   . TLA C 2 .   ? 19.379  7.807   16.630  1.00 93.51  ? 401 TLA A O4   1 
HETATM 9488  O  O41  . TLA C 2 .   ? 19.705  8.002   18.778  1.00 100.74 ? 401 TLA A O41  1 
HETATM 9489  H  H2   . TLA C 2 .   ? 18.031  10.227  15.759  1.00 64.28  ? 401 TLA A H2   1 
HETATM 9490  H  HA   . TLA C 2 .   ? 16.350  9.551   17.828  1.00 54.50  ? 401 TLA A HA   1 
HETATM 9491  H  H3   . TLA C 2 .   ? 19.975  10.502  17.031  1.00 143.33 ? 401 TLA A H3   1 
HETATM 9492  H  HB   . TLA C 2 .   ? 19.021  9.880   19.487  1.00 110.74 ? 401 TLA A HB   1 
HETATM 9493  NA NA   . NA  D 3 .   ? -7.901  -15.201 36.006  1.00 21.98  ? 402 NA  A NA   1 
HETATM 9494  C  C1   . PEG E 4 .   ? 23.975  -32.524 25.374  1.00 49.67  ? 401 PEG B C1   1 
HETATM 9495  O  O1   . PEG E 4 .   ? 22.870  -31.673 25.493  1.00 42.38  ? 401 PEG B O1   1 
HETATM 9496  C  C2   . PEG E 4 .   ? 24.509  -32.867 26.764  1.00 61.11  ? 401 PEG B C2   1 
HETATM 9497  O  O2   . PEG E 4 .   ? 25.383  -33.954 26.664  1.00 64.04  ? 401 PEG B O2   1 
HETATM 9498  C  C3   . PEG E 4 .   ? 25.538  -34.683 27.848  1.00 60.58  ? 401 PEG B C3   1 
HETATM 9499  C  C4   . PEG E 4 .   ? 26.369  -35.932 27.558  1.00 53.23  ? 401 PEG B C4   1 
HETATM 9500  O  O4   . PEG E 4 .   ? 25.980  -36.473 26.326  1.00 84.16  ? 401 PEG B O4   1 
HETATM 9501  H  H11  . PEG E 4 .   ? 24.752  -32.030 24.800  1.00 59.60  ? 401 PEG B H11  1 
HETATM 9502  H  H12  . PEG E 4 .   ? 23.676  -33.436 24.867  1.00 59.60  ? 401 PEG B H12  1 
HETATM 9503  H  HO1  . PEG E 4 .   ? 23.099  -30.937 26.039  1.00 50.85  ? 401 PEG B HO1  1 
HETATM 9504  H  H21  . PEG E 4 .   ? 23.682  -33.124 27.417  1.00 73.33  ? 401 PEG B H21  1 
HETATM 9505  H  H22  . PEG E 4 .   ? 25.038  -32.011 27.170  1.00 73.33  ? 401 PEG B H22  1 
HETATM 9506  H  H31  . PEG E 4 .   ? 24.563  -34.975 28.225  1.00 72.69  ? 401 PEG B H31  1 
HETATM 9507  H  H32  . PEG E 4 .   ? 26.044  -34.073 28.588  1.00 72.69  ? 401 PEG B H32  1 
HETATM 9508  H  H41  . PEG E 4 .   ? 26.208  -36.664 28.343  1.00 63.88  ? 401 PEG B H41  1 
HETATM 9509  H  H42  . PEG E 4 .   ? 27.421  -35.666 27.522  1.00 63.88  ? 401 PEG B H42  1 
HETATM 9510  H  HO4  . PEG E 4 .   ? 25.751  -35.775 25.734  1.00 100.99 ? 401 PEG B HO4  1 
HETATM 9511  O  O1   . PG4 F 5 .   ? 17.527  -32.271 39.882  1.00 95.12  ? 402 PG4 B O1   1 
HETATM 9512  C  C1   . PG4 F 5 .   ? 16.243  -31.718 39.780  1.00 96.90  ? 402 PG4 B C1   1 
HETATM 9513  C  C2   . PG4 F 5 .   ? 16.351  -30.230 39.449  1.00 93.65  ? 402 PG4 B C2   1 
HETATM 9514  O  O2   . PG4 F 5 .   ? 17.204  -29.614 40.373  1.00 67.54  ? 402 PG4 B O2   1 
HETATM 9515  C  C3   . PG4 F 5 .   ? 17.304  -28.223 40.244  1.00 77.85  ? 402 PG4 B C3   1 
HETATM 9516  C  C4   . PG4 F 5 .   ? 18.480  -27.831 39.347  1.00 37.30  ? 402 PG4 B C4   1 
HETATM 9517  O  O3   . PG4 F 5 .   ? 18.332  -28.332 38.046  1.00 72.38  ? 402 PG4 B O3   1 
HETATM 9518  C  C5   . PG4 F 5 .   ? 17.347  -27.715 37.268  1.00 65.12  ? 402 PG4 B C5   1 
HETATM 9519  C  C6   . PG4 F 5 .   ? 17.328  -28.359 35.883  1.00 44.50  ? 402 PG4 B C6   1 
HETATM 9520  O  O4   . PG4 F 5 .   ? 16.014  -28.374 35.408  1.00 75.52  ? 402 PG4 B O4   1 
HETATM 9521  C  C7   . PG4 F 5 .   ? 15.837  -29.120 34.239  1.00 74.26  ? 402 PG4 B C7   1 
HETATM 9522  C  C8   . PG4 F 5 .   ? 14.356  -29.121 33.862  1.00 81.71  ? 402 PG4 B C8   1 
HETATM 9523  O  O5   . PG4 F 5 .   ? 13.818  -27.844 34.071  1.00 88.78  ? 402 PG4 B O5   1 
HETATM 9524  H  HO1  . PG4 F 5 .   ? 17.458  -33.195 40.062  1.00 114.14 ? 402 PG4 B HO1  1 
HETATM 9525  H  H11  . PG4 F 5 .   ? 15.720  -31.842 40.723  1.00 116.28 ? 402 PG4 B H11  1 
HETATM 9526  H  H12  . PG4 F 5 .   ? 15.693  -32.225 38.994  1.00 116.28 ? 402 PG4 B H12  1 
HETATM 9527  H  H21  . PG4 F 5 .   ? 15.368  -29.774 39.502  1.00 112.38 ? 402 PG4 B H21  1 
HETATM 9528  H  H22  . PG4 F 5 .   ? 16.752  -30.110 38.448  1.00 112.38 ? 402 PG4 B H22  1 
HETATM 9529  H  H31  . PG4 F 5 .   ? 17.449  -27.787 41.227  1.00 93.42  ? 402 PG4 B H31  1 
HETATM 9530  H  H32  . PG4 F 5 .   ? 16.386  -27.841 39.811  1.00 93.42  ? 402 PG4 B H32  1 
HETATM 9531  H  H41  . PG4 F 5 .   ? 19.395  -28.227 39.774  1.00 44.76  ? 402 PG4 B H41  1 
HETATM 9532  H  H42  . PG4 F 5 .   ? 18.541  -26.748 39.301  1.00 44.76  ? 402 PG4 B H42  1 
HETATM 9533  H  H51  . PG4 F 5 .   ? 17.567  -26.657 37.174  1.00 78.14  ? 402 PG4 B H51  1 
HETATM 9534  H  H52  . PG4 F 5 .   ? 16.378  -27.841 37.741  1.00 78.14  ? 402 PG4 B H52  1 
HETATM 9535  H  H61  . PG4 F 5 .   ? 17.703  -29.375 35.949  1.00 53.40  ? 402 PG4 B H61  1 
HETATM 9536  H  H62  . PG4 F 5 .   ? 17.954  -27.786 35.207  1.00 53.40  ? 402 PG4 B H62  1 
HETATM 9537  H  H71  . PG4 F 5 .   ? 16.170  -30.140 34.405  1.00 89.12  ? 402 PG4 B H71  1 
HETATM 9538  H  H72  . PG4 F 5 .   ? 16.415  -28.678 33.434  1.00 89.12  ? 402 PG4 B H72  1 
HETATM 9539  H  H81  . PG4 F 5 .   ? 14.250  -29.392 32.817  1.00 98.06  ? 402 PG4 B H81  1 
HETATM 9540  H  H82  . PG4 F 5 .   ? 13.828  -29.841 34.478  1.00 98.06  ? 402 PG4 B H82  1 
HETATM 9541  H  HO5  . PG4 F 5 .   ? 14.250  -27.435 34.804  1.00 106.53 ? 402 PG4 B HO5  1 
HETATM 9542  O  O1   . TLA G 2 .   ? 4.975   -46.707 7.469   1.00 34.78  ? 403 TLA B O1   1 
HETATM 9543  O  O11  . TLA G 2 .   ? 4.579   -44.671 8.139   1.00 104.22 ? 403 TLA B O11  1 
HETATM 9544  C  C1   . TLA G 2 .   ? 4.176   -45.743 7.617   1.00 28.05  ? 403 TLA B C1   1 
HETATM 9545  C  C2   . TLA G 2 .   ? 2.724   -45.863 7.159   1.00 67.20  ? 403 TLA B C2   1 
HETATM 9546  O  O2   . TLA G 2 .   ? 2.690   -46.056 5.770   1.00 98.48  ? 403 TLA B O2   1 
HETATM 9547  C  C3   . TLA G 2 .   ? 1.934   -44.607 7.527   1.00 153.98 ? 403 TLA B C3   1 
HETATM 9548  O  O3   . TLA G 2 .   ? 2.116   -44.331 8.891   1.00 111.29 ? 403 TLA B O3   1 
HETATM 9549  C  C4   . TLA G 2 .   ? 2.386   -43.401 6.704   1.00 164.52 ? 403 TLA B C4   1 
HETATM 9550  O  O4   . TLA G 2 .   ? 3.459   -43.444 6.048   1.00 68.95  ? 403 TLA B O4   1 
HETATM 9551  O  O41  . TLA G 2 .   ? 1.676   -42.361 6.679   1.00 47.29  ? 403 TLA B O41  1 
HETATM 9552  H  H2   . TLA G 2 .   ? 2.270   -46.710 7.659   1.00 80.65  ? 403 TLA B H2   1 
HETATM 9553  H  HA   . TLA G 2 .   ? 3.127   -45.343 5.334   1.00 118.17 ? 403 TLA B HA   1 
HETATM 9554  H  H3   . TLA G 2 .   ? 0.889   -44.790 7.313   1.00 184.78 ? 403 TLA B H3   1 
HETATM 9555  H  HB   . TLA G 2 .   ? 2.691   -43.589 8.987   1.00 133.55 ? 403 TLA B HB   1 
HETATM 9556  NA NA   . NA  H 3 .   ? 32.918  -28.911 28.630  1.00 23.75  ? 404 NA  B NA   1 
HETATM 9557  O  O    . HOH I 6 .   ? -17.758 6.076   5.822   1.00 22.83  ? 501 HOH A O    1 
HETATM 9558  O  O    . HOH I 6 .   ? 7.213   -8.145  0.871   1.00 30.61  ? 502 HOH A O    1 
HETATM 9559  O  O    . HOH I 6 .   ? 11.443  5.093   38.856  1.00 26.51  ? 503 HOH A O    1 
HETATM 9560  O  O    . HOH I 6 .   ? -17.244 10.024  24.324  1.00 34.38  ? 504 HOH A O    1 
HETATM 9561  O  O    . HOH I 6 .   ? 9.073   20.055  22.056  1.00 31.93  ? 505 HOH A O    1 
HETATM 9562  O  O    . HOH I 6 .   ? 17.011  16.574  24.210  1.00 38.74  ? 506 HOH A O    1 
HETATM 9563  O  O    . HOH I 6 .   ? 4.726   3.702   5.424   1.00 35.04  ? 507 HOH A O    1 
HETATM 9564  O  O    . HOH I 6 .   ? 7.391   -9.670  28.647  1.00 44.40  ? 508 HOH A O    1 
HETATM 9565  O  O    . HOH I 6 .   ? -2.367  19.233  21.236  1.00 26.12  ? 509 HOH A O    1 
HETATM 9566  O  O    . HOH I 6 .   ? 14.998  9.599   24.102  1.00 30.59  ? 510 HOH A O    1 
HETATM 9567  O  O    . HOH I 6 .   ? -12.943 -10.543 30.514  1.00 30.79  ? 511 HOH A O    1 
HETATM 9568  O  O    . HOH I 6 .   ? 1.849   16.902  13.467  1.00 28.76  ? 512 HOH A O    1 
HETATM 9569  O  O    . HOH I 6 .   ? -19.747 -11.140 12.762  1.00 40.66  ? 513 HOH A O    1 
HETATM 9570  O  O    . HOH I 6 .   ? 7.579   -16.846 23.274  1.00 40.11  ? 514 HOH A O    1 
HETATM 9571  O  O    . HOH I 6 .   ? -19.714 -1.401  5.298   1.00 30.62  ? 515 HOH A O    1 
HETATM 9572  O  O    . HOH I 6 .   ? 19.533  0.524   12.493  1.00 36.00  ? 516 HOH A O    1 
HETATM 9573  O  O    . HOH I 6 .   ? 11.341  17.049  11.400  1.00 41.22  ? 517 HOH A O    1 
HETATM 9574  O  O    . HOH I 6 .   ? -0.083  -20.758 24.430  1.00 23.63  ? 518 HOH A O    1 
HETATM 9575  O  O    . HOH I 6 .   ? -2.057  2.515   34.910  1.00 18.67  ? 519 HOH A O    1 
HETATM 9576  O  O    . HOH I 6 .   ? -17.013 12.961  6.140   1.00 24.14  ? 520 HOH A O    1 
HETATM 9577  O  O    . HOH I 6 .   ? -5.749  -31.322 19.904  1.00 30.96  ? 521 HOH A O    1 
HETATM 9578  O  O    . HOH I 6 .   ? -17.770 4.702   1.465   1.00 22.32  ? 522 HOH A O    1 
HETATM 9579  O  O    . HOH I 6 .   ? -2.182  -30.265 16.566  1.00 40.08  ? 523 HOH A O    1 
HETATM 9580  O  O    . HOH I 6 .   ? -18.290 3.410   10.819  1.00 24.93  ? 524 HOH A O    1 
HETATM 9581  O  O    . HOH I 6 .   ? 4.783   -25.574 24.083  1.00 47.41  ? 525 HOH A O    1 
HETATM 9582  O  O    . HOH I 6 .   ? -6.502  -11.409 11.959  1.00 22.01  ? 526 HOH A O    1 
HETATM 9583  O  O    . HOH I 6 .   ? -13.381 -17.058 22.710  1.00 30.22  ? 527 HOH A O    1 
HETATM 9584  O  O    . HOH I 6 .   ? 6.414   -14.796 23.975  1.00 28.84  ? 528 HOH A O    1 
HETATM 9585  O  O    . HOH I 6 .   ? 17.202  14.977  17.755  1.00 25.07  ? 529 HOH A O    1 
HETATM 9586  O  O    . HOH I 6 .   ? -15.360 -9.252  18.652  1.00 31.28  ? 530 HOH A O    1 
HETATM 9587  O  O    . HOH I 6 .   ? 12.578  -9.705  27.621  1.00 23.40  ? 531 HOH A O    1 
HETATM 9588  O  O    . HOH I 6 .   ? 1.661   12.783  11.790  1.00 22.57  ? 532 HOH A O    1 
HETATM 9589  O  O    . HOH I 6 .   ? -16.313 -8.499  16.154  1.00 22.90  ? 533 HOH A O    1 
HETATM 9590  O  O    . HOH I 6 .   ? 1.805   -2.100  1.564   1.00 32.17  ? 534 HOH A O    1 
HETATM 9591  O  O    . HOH I 6 .   ? 1.557   4.940   -0.131  1.00 40.80  ? 535 HOH A O    1 
HETATM 9592  O  O    . HOH I 6 .   ? 14.679  20.309  28.728  1.00 31.75  ? 536 HOH A O    1 
HETATM 9593  O  O    . HOH I 6 .   ? 12.782  -8.841  14.093  1.00 27.67  ? 537 HOH A O    1 
HETATM 9594  O  O    . HOH I 6 .   ? -7.183  3.289   -1.380  1.00 24.37  ? 538 HOH A O    1 
HETATM 9595  O  O    . HOH I 6 .   ? 0.970   22.761  23.945  1.00 31.65  ? 539 HOH A O    1 
HETATM 9596  O  O    . HOH I 6 .   ? -16.058 3.146   16.986  1.00 20.43  ? 540 HOH A O    1 
HETATM 9597  O  O    . HOH I 6 .   ? 16.723  2.241   17.361  1.00 27.38  ? 541 HOH A O    1 
HETATM 9598  O  O    . HOH I 6 .   ? -14.929 13.844  20.293  1.00 26.39  ? 542 HOH A O    1 
HETATM 9599  O  O    . HOH I 6 .   ? 17.705  13.972  30.043  1.00 39.47  ? 543 HOH A O    1 
HETATM 9600  O  O    . HOH I 6 .   ? -8.721  -17.537 17.419  1.00 26.87  ? 544 HOH A O    1 
HETATM 9601  O  O    . HOH I 6 .   ? 10.020  22.111  28.304  1.00 29.62  ? 545 HOH A O    1 
HETATM 9602  O  O    . HOH I 6 .   ? -12.180 -7.316  21.505  1.00 16.53  ? 546 HOH A O    1 
HETATM 9603  O  O    . HOH I 6 .   ? 15.719  6.123   15.680  1.00 40.82  ? 547 HOH A O    1 
HETATM 9604  O  O    . HOH I 6 .   ? 7.071   -12.772 25.210  1.00 29.43  ? 548 HOH A O    1 
HETATM 9605  O  O    . HOH I 6 .   ? 9.339   -5.833  22.206  1.00 15.59  ? 549 HOH A O    1 
HETATM 9606  O  O    . HOH I 6 .   ? -5.311  -14.248 1.291   1.00 41.90  ? 550 HOH A O    1 
HETATM 9607  O  O    . HOH I 6 .   ? 0.047   19.166  33.814  1.00 21.33  ? 551 HOH A O    1 
HETATM 9608  O  O    . HOH I 6 .   ? -14.082 16.635  12.165  1.00 38.13  ? 552 HOH A O    1 
HETATM 9609  O  O    . HOH I 6 .   ? -1.021  -7.672  0.720   1.00 24.95  ? 553 HOH A O    1 
HETATM 9610  O  O    . HOH I 6 .   ? 5.924   -20.387 25.545  1.00 34.73  ? 554 HOH A O    1 
HETATM 9611  O  O    . HOH I 6 .   ? 12.678  17.287  35.312  1.00 38.28  ? 555 HOH A O    1 
HETATM 9612  O  O    . HOH I 6 .   ? 8.371   -12.295 22.686  1.00 23.55  ? 556 HOH A O    1 
HETATM 9613  O  O    . HOH I 6 .   ? -11.337 -15.397 16.830  1.00 30.03  ? 557 HOH A O    1 
HETATM 9614  O  O    . HOH I 6 .   ? -18.404 -4.412  15.024  1.00 24.54  ? 558 HOH A O    1 
HETATM 9615  O  O    . HOH I 6 .   ? -8.276  -9.111  4.633   1.00 24.62  ? 559 HOH A O    1 
HETATM 9616  O  O    . HOH I 6 .   ? -23.017 -5.421  10.125  1.00 36.77  ? 560 HOH A O    1 
HETATM 9617  O  O    . HOH I 6 .   ? -14.625 -0.390  29.607  1.00 23.69  ? 561 HOH A O    1 
HETATM 9618  O  O    . HOH I 6 .   ? -17.629 -1.035  18.356  1.00 26.69  ? 562 HOH A O    1 
HETATM 9619  O  O    . HOH I 6 .   ? -16.273 -5.827  36.928  1.00 38.38  ? 563 HOH A O    1 
HETATM 9620  O  O    . HOH I 6 .   ? -8.143  -12.141 10.005  1.00 26.52  ? 564 HOH A O    1 
HETATM 9621  O  O    . HOH I 6 .   ? -0.388  3.100   39.473  1.00 19.37  ? 565 HOH A O    1 
HETATM 9622  O  O    . HOH I 6 .   ? -6.182  14.713  4.491   1.00 31.27  ? 566 HOH A O    1 
HETATM 9623  O  O    . HOH I 6 .   ? 12.746  7.581   11.326  1.00 39.10  ? 567 HOH A O    1 
HETATM 9624  O  O    . HOH I 6 .   ? -5.090  -2.128  2.771   1.00 27.07  ? 568 HOH A O    1 
HETATM 9625  O  O    . HOH I 6 .   ? 14.367  9.907   13.336  1.00 39.84  ? 569 HOH A O    1 
HETATM 9626  O  O    . HOH I 6 .   ? -15.920 -1.027  33.284  1.00 42.65  ? 570 HOH A O    1 
HETATM 9627  O  O    . HOH I 6 .   ? 6.536   7.614   15.527  1.00 15.64  ? 571 HOH A O    1 
HETATM 9628  O  O    . HOH I 6 .   ? 12.434  20.420  25.490  1.00 35.55  ? 572 HOH A O    1 
HETATM 9629  O  O    . HOH I 6 .   ? 4.925   2.034   29.996  1.00 13.98  ? 573 HOH A O    1 
HETATM 9630  O  O    . HOH I 6 .   ? -3.555  11.783  8.026   1.00 18.80  ? 574 HOH A O    1 
HETATM 9631  O  O    . HOH I 6 .   ? -18.932 10.659  13.627  1.00 39.49  ? 575 HOH A O    1 
HETATM 9632  O  O    . HOH I 6 .   ? 1.569   -12.595 32.680  1.00 41.17  ? 576 HOH A O    1 
HETATM 9633  O  O    . HOH I 6 .   ? -7.613  -27.873 24.968  1.00 25.21  ? 577 HOH A O    1 
HETATM 9634  O  O    . HOH I 6 .   ? -13.513 10.323  -0.361  1.00 29.01  ? 578 HOH A O    1 
HETATM 9635  O  O    . HOH I 6 .   ? 0.744   -12.137 3.676   1.00 27.52  ? 579 HOH A O    1 
HETATM 9636  O  O    . HOH I 6 .   ? 8.583   21.229  25.177  1.00 38.50  ? 580 HOH A O    1 
HETATM 9637  O  O    . HOH I 6 .   ? 14.497  9.517   16.031  1.00 29.59  ? 581 HOH A O    1 
HETATM 9638  O  O    . HOH I 6 .   ? -2.033  -16.086 43.031  1.00 48.05  ? 582 HOH A O    1 
HETATM 9639  O  O    . HOH I 6 .   ? -1.369  -22.358 8.419   1.00 42.90  ? 583 HOH A O    1 
HETATM 9640  O  O    . HOH I 6 .   ? -13.633 19.002  29.013  1.00 24.82  ? 584 HOH A O    1 
HETATM 9641  O  O    . HOH I 6 .   ? 12.620  14.298  36.200  1.00 32.18  ? 585 HOH A O    1 
HETATM 9642  O  O    . HOH I 6 .   ? 14.935  1.749   25.243  1.00 19.14  ? 586 HOH A O    1 
HETATM 9643  O  O    . HOH I 6 .   ? -19.145 3.684   13.679  1.00 37.73  ? 587 HOH A O    1 
HETATM 9644  O  O    . HOH I 6 .   ? -11.631 8.159   32.625  1.00 27.09  ? 588 HOH A O    1 
HETATM 9645  O  O    . HOH I 6 .   ? 6.525   20.448  28.512  1.00 22.88  ? 589 HOH A O    1 
HETATM 9646  O  O    . HOH I 6 .   ? -8.484  -4.165  4.733   1.00 22.48  ? 590 HOH A O    1 
HETATM 9647  O  O    . HOH I 6 .   ? -9.262  11.138  38.758  1.00 26.32  ? 591 HOH A O    1 
HETATM 9648  O  O    . HOH I 6 .   ? 16.929  3.787   32.543  1.00 27.75  ? 592 HOH A O    1 
HETATM 9649  O  O    . HOH I 6 .   ? -7.065  -6.450  3.985   1.00 25.46  ? 593 HOH A O    1 
HETATM 9650  O  O    . HOH I 6 .   ? -3.204  8.545   33.573  1.00 20.73  ? 594 HOH A O    1 
HETATM 9651  O  O    . HOH I 6 .   ? -9.036  6.831   -2.552  1.00 20.84  ? 595 HOH A O    1 
HETATM 9652  O  O    . HOH I 6 .   ? 1.097   12.421  9.126   1.00 22.66  ? 596 HOH A O    1 
HETATM 9653  O  O    . HOH I 6 .   ? -4.735  20.282  9.794   1.00 37.01  ? 597 HOH A O    1 
HETATM 9654  O  O    . HOH I 6 .   ? -2.645  -30.487 13.970  1.00 42.19  ? 598 HOH A O    1 
HETATM 9655  O  O    . HOH I 6 .   ? 10.089  -1.149  37.907  1.00 28.25  ? 599 HOH A O    1 
HETATM 9656  O  O    . HOH I 6 .   ? -1.834  7.533   35.831  1.00 18.46  ? 600 HOH A O    1 
HETATM 9657  O  O    . HOH I 6 .   ? -10.763 -22.846 16.535  1.00 35.08  ? 601 HOH A O    1 
HETATM 9658  O  O    . HOH I 6 .   ? -3.587  7.584   38.030  1.00 20.90  ? 602 HOH A O    1 
HETATM 9659  O  O    . HOH I 6 .   ? 7.540   -21.974 14.402  1.00 24.38  ? 603 HOH A O    1 
HETATM 9660  O  O    . HOH I 6 .   ? -3.461  4.108   36.647  1.00 20.46  ? 604 HOH A O    1 
HETATM 9661  O  O    . HOH I 6 .   ? 4.305   3.348   37.833  1.00 19.27  ? 605 HOH A O    1 
HETATM 9662  O  O    . HOH I 6 .   ? -17.402 3.737   25.434  1.00 22.76  ? 606 HOH A O    1 
HETATM 9663  O  O    . HOH I 6 .   ? 3.646   10.142  39.000  1.00 25.48  ? 607 HOH A O    1 
HETATM 9664  O  O    . HOH I 6 .   ? -7.207  1.739   0.976   1.00 22.00  ? 608 HOH A O    1 
HETATM 9665  O  O    . HOH I 6 .   ? 18.929  1.297   24.720  1.00 27.19  ? 609 HOH A O    1 
HETATM 9666  O  O    . HOH I 6 .   ? 15.334  21.656  20.015  1.00 24.38  ? 610 HOH A O    1 
HETATM 9667  O  O    . HOH I 6 .   ? -13.159 -15.557 6.011   1.00 48.11  ? 611 HOH A O    1 
HETATM 9668  O  O    . HOH I 6 .   ? -6.319  23.808  26.197  1.00 43.72  ? 612 HOH A O    1 
HETATM 9669  O  O    . HOH I 6 .   ? -5.761  -1.168  29.108  1.00 33.28  ? 613 HOH A O    1 
HETATM 9670  O  O    . HOH I 6 .   ? -14.456 21.198  30.361  1.00 37.18  ? 614 HOH A O    1 
HETATM 9671  O  O    . HOH I 6 .   ? -13.745 14.241  34.759  1.00 30.23  ? 615 HOH A O    1 
HETATM 9672  O  O    . HOH I 6 .   ? -7.628  -23.055 33.667  1.00 25.50  ? 616 HOH A O    1 
HETATM 9673  O  O    . HOH I 6 .   ? 0.033   11.811  4.600   1.00 25.91  ? 617 HOH A O    1 
HETATM 9674  O  O    . HOH I 6 .   ? 10.916  -6.075  35.536  1.00 23.58  ? 618 HOH A O    1 
HETATM 9675  O  O    . HOH I 6 .   ? -0.437  -5.976  36.873  1.00 29.42  ? 619 HOH A O    1 
HETATM 9676  O  O    . HOH I 6 .   ? -5.568  -23.283 31.756  1.00 24.66  ? 620 HOH A O    1 
HETATM 9677  O  O    . HOH I 6 .   ? -1.229  -1.504  -0.325  1.00 36.10  ? 621 HOH A O    1 
HETATM 9678  O  O    . HOH I 6 .   ? 13.594  -4.970  31.325  1.00 20.84  ? 622 HOH A O    1 
HETATM 9679  O  O    . HOH I 6 .   ? -4.294  -8.606  -0.281  1.00 32.04  ? 623 HOH A O    1 
HETATM 9680  O  O    . HOH I 6 .   ? 6.800   -11.021 21.015  1.00 18.57  ? 624 HOH A O    1 
HETATM 9681  O  O    . HOH I 6 .   ? -1.089  -17.583 26.829  1.00 23.70  ? 625 HOH A O    1 
HETATM 9682  O  O    . HOH I 6 .   ? -9.133  -6.605  36.169  1.00 36.98  ? 626 HOH A O    1 
HETATM 9683  O  O    . HOH I 6 .   ? -2.527  10.486  -2.794  1.00 34.37  ? 627 HOH A O    1 
HETATM 9684  O  O    . HOH I 6 .   ? -14.561 -14.747 23.780  1.00 34.73  ? 628 HOH A O    1 
HETATM 9685  O  O    . HOH I 6 .   ? -11.156 5.450   30.745  1.00 29.38  ? 629 HOH A O    1 
HETATM 9686  O  O    . HOH I 6 .   ? -3.741  -31.392 23.251  1.00 43.07  ? 630 HOH A O    1 
HETATM 9687  O  O    . HOH I 6 .   ? 17.741  0.967   33.163  1.00 49.55  ? 631 HOH A O    1 
HETATM 9688  O  O    . HOH I 6 .   ? -14.269 -9.296  5.396   1.00 39.19  ? 632 HOH A O    1 
HETATM 9689  O  O    . HOH I 6 .   ? 15.017  5.188   26.019  1.00 16.53  ? 633 HOH A O    1 
HETATM 9690  O  O    . HOH I 6 .   ? -8.322  -20.423 13.644  1.00 34.97  ? 634 HOH A O    1 
HETATM 9691  O  O    . HOH I 6 .   ? 1.357   21.874  21.437  1.00 23.06  ? 635 HOH A O    1 
HETATM 9692  O  O    . HOH I 6 .   ? -12.637 -0.927  10.964  1.00 16.88  ? 636 HOH A O    1 
HETATM 9693  O  O    . HOH I 6 .   ? -15.288 9.759   21.441  1.00 27.48  ? 637 HOH A O    1 
HETATM 9694  O  O    . HOH I 6 .   ? -3.402  -22.274 17.310  1.00 21.42  ? 638 HOH A O    1 
HETATM 9695  O  O    . HOH I 6 .   ? -11.819 16.899  20.540  1.00 21.08  ? 639 HOH A O    1 
HETATM 9696  O  O    . HOH I 6 .   ? -12.206 15.554  8.289   1.00 36.65  ? 640 HOH A O    1 
HETATM 9697  O  O    . HOH I 6 .   ? -6.199  23.428  30.636  1.00 24.88  ? 641 HOH A O    1 
HETATM 9698  O  O    . HOH I 6 .   ? 12.436  7.123   8.899   1.00 45.53  ? 642 HOH A O    1 
HETATM 9699  O  O    . HOH I 6 .   ? 6.426   -0.788  13.134  1.00 16.54  ? 643 HOH A O    1 
HETATM 9700  O  O    . HOH I 6 .   ? -18.121 11.126  3.796   1.00 31.63  ? 644 HOH A O    1 
HETATM 9701  O  O    . HOH I 6 .   ? 5.339   -0.642  39.294  1.00 22.23  ? 645 HOH A O    1 
HETATM 9702  O  O    . HOH I 6 .   ? -8.171  20.099  25.976  1.00 22.32  ? 646 HOH A O    1 
HETATM 9703  O  O    . HOH I 6 .   ? 0.318   -12.970 6.258   1.00 22.50  ? 647 HOH A O    1 
HETATM 9704  O  O    . HOH I 6 .   ? 12.040  -11.932 10.415  1.00 38.87  ? 648 HOH A O    1 
HETATM 9705  O  O    . HOH I 6 .   ? -2.078  24.590  28.862  1.00 32.05  ? 649 HOH A O    1 
HETATM 9706  O  O    . HOH I 6 .   ? -13.189 -1.595  22.148  1.00 16.96  ? 650 HOH A O    1 
HETATM 9707  O  O    . HOH I 6 .   ? 7.324   18.118  20.998  1.00 22.54  ? 651 HOH A O    1 
HETATM 9708  O  O    . HOH I 6 .   ? -0.534  -7.255  34.017  1.00 30.43  ? 652 HOH A O    1 
HETATM 9709  O  O    . HOH I 6 .   ? 6.262   16.110  9.116   1.00 45.55  ? 653 HOH A O    1 
HETATM 9710  O  O    . HOH I 6 .   ? -9.997  -11.793 32.209  1.00 26.82  ? 654 HOH A O    1 
HETATM 9711  O  O    . HOH I 6 .   ? 16.310  14.411  25.022  1.00 35.67  ? 655 HOH A O    1 
HETATM 9712  O  O    . HOH I 6 .   ? -15.368 7.612   27.098  1.00 24.33  ? 656 HOH A O    1 
HETATM 9713  O  O    . HOH I 6 .   ? -10.483 8.793   28.319  1.00 16.97  ? 657 HOH A O    1 
HETATM 9714  O  O    . HOH I 6 .   ? -18.664 13.248  15.781  1.00 44.50  ? 658 HOH A O    1 
HETATM 9715  O  O    . HOH I 6 .   ? 11.177  -10.286 15.825  1.00 18.49  ? 659 HOH A O    1 
HETATM 9716  O  O    . HOH I 6 .   ? -0.285  19.727  26.909  1.00 20.15  ? 660 HOH A O    1 
HETATM 9717  O  O    . HOH I 6 .   ? -4.896  -27.060 24.875  1.00 25.55  ? 661 HOH A O    1 
HETATM 9718  O  O    . HOH I 6 .   ? -21.482 -0.956  9.228   1.00 32.03  ? 662 HOH A O    1 
HETATM 9719  O  O    . HOH I 6 .   ? -2.903  13.393  27.752  1.00 28.82  ? 663 HOH A O    1 
HETATM 9720  O  O    . HOH I 6 .   ? 0.649   0.859   22.599  1.00 13.06  ? 664 HOH A O    1 
HETATM 9721  O  O    . HOH I 6 .   ? -0.631  11.594  33.677  1.00 18.14  ? 665 HOH A O    1 
HETATM 9722  O  O    . HOH I 6 .   ? -5.789  5.241   35.949  1.00 20.88  ? 666 HOH A O    1 
HETATM 9723  O  O    . HOH I 6 .   ? -1.413  13.327  8.244   1.00 24.49  ? 667 HOH A O    1 
HETATM 9724  O  O    . HOH I 6 .   ? -12.667 6.423   35.302  1.00 39.54  ? 668 HOH A O    1 
HETATM 9725  O  O    . HOH I 6 .   ? -2.718  -25.759 11.427  1.00 27.31  ? 669 HOH A O    1 
HETATM 9726  O  O    . HOH I 6 .   ? 19.975  -5.694  27.870  1.00 31.20  ? 670 HOH A O    1 
HETATM 9727  O  O    . HOH I 6 .   ? -6.566  -25.377 29.074  1.00 27.79  ? 671 HOH A O    1 
HETATM 9728  O  O    . HOH I 6 .   ? -4.031  -1.722  -1.288  1.00 32.25  ? 672 HOH A O    1 
HETATM 9729  O  O    . HOH I 6 .   ? 12.720  -5.646  19.979  1.00 17.41  ? 673 HOH A O    1 
HETATM 9730  O  O    . HOH I 6 .   ? -3.445  -16.667 20.034  1.00 16.27  ? 674 HOH A O    1 
HETATM 9731  O  O    . HOH I 6 .   ? -6.883  -16.161 4.270   1.00 28.99  ? 675 HOH A O    1 
HETATM 9732  O  O    . HOH I 6 .   ? -5.289  -11.635 38.001  1.00 45.00  ? 676 HOH A O    1 
HETATM 9733  O  O    . HOH I 6 .   ? 17.444  17.519  29.070  1.00 34.40  ? 677 HOH A O    1 
HETATM 9734  O  O    . HOH I 6 .   ? -1.720  -10.665 29.894  1.00 34.30  ? 678 HOH A O    1 
HETATM 9735  O  O    . HOH I 6 .   ? -14.367 12.923  22.711  1.00 24.99  ? 679 HOH A O    1 
HETATM 9736  O  O    . HOH I 6 .   ? 19.265  -0.532  22.932  1.00 34.22  ? 680 HOH A O    1 
HETATM 9737  O  O    . HOH I 6 .   ? -3.361  -4.950  28.735  1.00 36.98  ? 681 HOH A O    1 
HETATM 9738  O  O    . HOH I 6 .   ? -15.867 11.042  27.835  1.00 26.92  ? 682 HOH A O    1 
HETATM 9739  O  O    . HOH I 6 .   ? -3.792  -22.449 25.885  1.00 22.63  ? 683 HOH A O    1 
HETATM 9740  O  O    . HOH I 6 .   ? -13.865 -16.232 26.230  1.00 22.24  ? 684 HOH A O    1 
HETATM 9741  O  O    . HOH I 6 .   ? -12.884 14.351  24.259  1.00 32.32  ? 685 HOH A O    1 
HETATM 9742  O  O    . HOH I 6 .   ? 13.190  0.664   9.788   1.00 30.87  ? 686 HOH A O    1 
HETATM 9743  O  O    . HOH I 6 .   ? 1.526   10.527  37.104  1.00 23.20  ? 687 HOH A O    1 
HETATM 9744  O  O    . HOH I 6 .   ? 2.716   11.417  5.431   1.00 29.25  ? 688 HOH A O    1 
HETATM 9745  O  O    . HOH I 6 .   ? -0.175  12.709  26.764  1.00 18.83  ? 689 HOH A O    1 
HETATM 9746  O  O    . HOH I 6 .   ? 12.641  -15.228 12.317  1.00 29.94  ? 690 HOH A O    1 
HETATM 9747  O  O    . HOH I 6 .   ? 3.651   15.865  10.268  1.00 29.27  ? 691 HOH A O    1 
HETATM 9748  O  O    . HOH I 6 .   ? 0.386   7.266   -0.595  1.00 42.84  ? 692 HOH A O    1 
HETATM 9749  O  O    . HOH I 6 .   ? 18.704  -2.733  14.979  1.00 24.18  ? 693 HOH A O    1 
HETATM 9750  O  O    . HOH I 6 .   ? -8.107  17.989  10.039  1.00 36.53  ? 694 HOH A O    1 
HETATM 9751  O  O    . HOH I 6 .   ? -17.026 3.367   20.610  1.00 23.90  ? 695 HOH A O    1 
HETATM 9752  O  O    . HOH I 6 .   ? -8.295  19.295  13.881  1.00 31.56  ? 696 HOH A O    1 
HETATM 9753  O  O    . HOH I 6 .   ? -4.225  10.597  5.487   1.00 18.41  ? 697 HOH A O    1 
HETATM 9754  O  O    . HOH I 6 .   ? 2.175   -20.511 25.798  1.00 31.19  ? 698 HOH A O    1 
HETATM 9755  O  O    . HOH I 6 .   ? -15.385 2.544   7.349   1.00 28.06  ? 699 HOH A O    1 
HETATM 9756  O  O    . HOH I 6 .   ? -11.928 -11.339 4.011   1.00 34.21  ? 700 HOH A O    1 
HETATM 9757  O  O    . HOH I 6 .   ? -2.222  4.598   -3.617  1.00 51.95  ? 701 HOH A O    1 
HETATM 9758  O  O    . HOH I 6 .   ? -2.349  1.021   39.028  1.00 31.90  ? 702 HOH A O    1 
HETATM 9759  O  O    . HOH I 6 .   ? 0.730   9.573   1.319   1.00 37.18  ? 703 HOH A O    1 
HETATM 9760  O  O    . HOH I 6 .   ? -12.463 17.008  14.274  1.00 34.55  ? 704 HOH A O    1 
HETATM 9761  O  O    . HOH I 6 .   ? 13.329  -1.859  10.603  1.00 23.85  ? 705 HOH A O    1 
HETATM 9762  O  O    . HOH I 6 .   ? 6.632   -23.617 10.472  1.00 41.91  ? 706 HOH A O    1 
HETATM 9763  O  O    . HOH I 6 .   ? -13.538 4.832   3.424   1.00 28.04  ? 707 HOH A O    1 
HETATM 9764  O  O    . HOH I 6 .   ? -17.429 -1.647  21.057  1.00 29.67  ? 708 HOH A O    1 
HETATM 9765  O  O    . HOH I 6 .   ? -1.118  -17.582 34.908  1.00 32.87  ? 709 HOH A O    1 
HETATM 9766  O  O    . HOH I 6 .   ? -17.656 8.381   11.962  1.00 18.55  ? 710 HOH A O    1 
HETATM 9767  O  O    . HOH I 6 .   ? 20.627  0.222   28.388  1.00 35.82  ? 711 HOH A O    1 
HETATM 9768  O  O    . HOH I 6 .   ? 12.672  -14.142 15.025  1.00 29.75  ? 712 HOH A O    1 
HETATM 9769  O  O    . HOH I 6 .   ? 1.813   -15.060 7.370   1.00 24.82  ? 713 HOH A O    1 
HETATM 9770  O  O    . HOH I 6 .   ? 7.489   -8.740  3.370   1.00 26.66  ? 714 HOH A O    1 
HETATM 9771  O  O    . HOH I 6 .   ? 17.284  -0.413  17.828  1.00 23.27  ? 715 HOH A O    1 
HETATM 9772  O  O    . HOH I 6 .   ? 4.579   -14.768 3.433   1.00 31.50  ? 716 HOH A O    1 
HETATM 9773  O  O    . HOH I 6 .   ? 0.587   12.527  1.899   1.00 43.14  ? 717 HOH A O    1 
HETATM 9774  O  O    . HOH I 6 .   ? 2.390   -23.445 24.962  1.00 29.51  ? 718 HOH A O    1 
HETATM 9775  O  O    . HOH I 6 .   ? -10.775 -19.022 21.679  1.00 19.93  ? 719 HOH A O    1 
HETATM 9776  O  O    . HOH I 6 .   ? -17.521 -8.662  3.875   1.00 44.73  ? 720 HOH A O    1 
HETATM 9777  O  O    . HOH I 6 .   ? 1.836   -27.780 26.483  1.00 43.67  ? 721 HOH A O    1 
HETATM 9778  O  O    . HOH I 6 .   ? 13.214  20.953  22.987  1.00 30.03  ? 722 HOH A O    1 
HETATM 9779  O  O    . HOH I 6 .   ? -12.433 -0.656  4.418   1.00 36.48  ? 723 HOH A O    1 
HETATM 9780  O  O    . HOH I 6 .   ? -0.776  2.309   -1.016  1.00 49.98  ? 724 HOH A O    1 
HETATM 9781  O  O    . HOH I 6 .   ? -17.501 5.795   19.088  1.00 23.80  ? 725 HOH A O    1 
HETATM 9782  O  O    . HOH I 6 .   ? 2.144   23.605  28.054  1.00 36.97  ? 726 HOH A O    1 
HETATM 9783  O  O    . HOH I 6 .   ? 5.763   -2.992  38.119  1.00 25.56  ? 727 HOH A O    1 
HETATM 9784  O  O    . HOH I 6 .   ? 18.771  5.706   26.356  1.00 31.19  ? 728 HOH A O    1 
HETATM 9785  O  O    . HOH I 6 .   ? 7.949   11.071  39.481  1.00 29.41  ? 729 HOH A O    1 
HETATM 9786  O  O    . HOH I 6 .   ? -16.844 -6.467  29.863  1.00 31.59  ? 730 HOH A O    1 
HETATM 9787  O  O    . HOH I 6 .   ? -5.079  -13.040 43.228  1.00 45.45  ? 731 HOH A O    1 
HETATM 9788  O  O    . HOH I 6 .   ? -3.017  -31.320 20.363  1.00 26.80  ? 732 HOH A O    1 
HETATM 9789  O  O    . HOH I 6 .   ? 13.576  -7.745  21.431  1.00 20.80  ? 733 HOH A O    1 
HETATM 9790  O  O    . HOH I 6 .   ? -0.763  -11.782 31.751  1.00 38.73  ? 734 HOH A O    1 
HETATM 9791  O  O    . HOH I 6 .   ? 7.161   -26.788 21.570  1.00 35.20  ? 735 HOH A O    1 
HETATM 9792  O  O    . HOH I 6 .   ? 12.785  5.032   10.955  1.00 25.99  ? 736 HOH A O    1 
HETATM 9793  O  O    . HOH I 6 .   ? -10.599 12.910  0.890   1.00 35.19  ? 737 HOH A O    1 
HETATM 9794  O  O    . HOH I 6 .   ? 5.996   -4.716  2.421   1.00 29.49  ? 738 HOH A O    1 
HETATM 9795  O  O    . HOH I 6 .   ? -4.310  -25.873 18.123  1.00 25.52  ? 739 HOH A O    1 
HETATM 9796  O  O    . HOH I 6 .   ? 1.234   8.022   35.949  1.00 17.18  ? 740 HOH A O    1 
HETATM 9797  O  O    . HOH I 6 .   ? 6.771   -0.579  5.573   1.00 32.93  ? 741 HOH A O    1 
HETATM 9798  O  O    . HOH I 6 .   ? 15.806  4.739   20.339  1.00 24.58  ? 742 HOH A O    1 
HETATM 9799  O  O    . HOH I 6 .   ? 26.870  -15.967 4.891   1.00 44.20  ? 743 HOH A O    1 
HETATM 9800  O  O    . HOH I 6 .   ? 4.768   -14.823 31.440  1.00 35.09  ? 744 HOH A O    1 
HETATM 9801  O  O    . HOH I 6 .   ? -17.225 -2.862  23.640  1.00 26.67  ? 745 HOH A O    1 
HETATM 9802  O  O    . HOH I 6 .   ? -11.538 19.709  24.554  1.00 32.17  ? 746 HOH A O    1 
HETATM 9803  O  O    . HOH I 6 .   ? -5.217  -17.188 7.686   1.00 24.01  ? 747 HOH A O    1 
HETATM 9804  O  O    . HOH I 6 .   ? -6.304  14.780  37.609  1.00 31.16  ? 748 HOH A O    1 
HETATM 9805  O  O    . HOH I 6 .   ? -9.820  -20.769 19.807  1.00 21.42  ? 749 HOH A O    1 
HETATM 9806  O  O    . HOH I 6 .   ? 19.968  7.510   30.005  1.00 49.99  ? 750 HOH A O    1 
HETATM 9807  O  O    . HOH I 6 .   ? 2.623   21.610  25.848  1.00 26.33  ? 751 HOH A O    1 
HETATM 9808  O  O    . HOH I 6 .   ? -19.663 6.443   8.105   1.00 28.28  ? 752 HOH A O    1 
HETATM 9809  O  O    . HOH I 6 .   ? 16.546  2.225   20.803  1.00 22.58  ? 753 HOH A O    1 
HETATM 9810  O  O    . HOH I 6 .   ? 8.232   -13.916 3.608   1.00 43.33  ? 754 HOH A O    1 
HETATM 9811  O  O    . HOH I 6 .   ? 6.058   8.074   4.308   1.00 39.25  ? 755 HOH A O    1 
HETATM 9812  O  O    . HOH I 6 .   ? -13.340 15.278  26.487  1.00 41.19  ? 756 HOH A O    1 
HETATM 9813  O  O    . HOH I 6 .   ? 12.730  24.515  28.541  1.00 46.49  ? 757 HOH A O    1 
HETATM 9814  O  O    . HOH I 6 .   ? 0.030   -14.384 -1.646  1.00 47.85  ? 758 HOH A O    1 
HETATM 9815  O  O    . HOH I 6 .   ? -17.748 5.061   29.688  1.00 47.22  ? 759 HOH A O    1 
HETATM 9816  O  O    . HOH I 6 .   ? 16.688  11.634  24.369  1.00 38.97  ? 760 HOH A O    1 
HETATM 9817  O  O    . HOH I 6 .   ? -19.856 -6.780  4.475   1.00 38.86  ? 761 HOH A O    1 
HETATM 9818  O  O    . HOH I 6 .   ? -2.801  -26.374 14.939  1.00 27.12  ? 762 HOH A O    1 
HETATM 9819  O  O    . HOH I 6 .   ? -7.703  4.322   37.559  1.00 24.91  ? 763 HOH A O    1 
HETATM 9820  O  O    . HOH I 6 .   ? 16.463  18.967  23.914  1.00 38.37  ? 764 HOH A O    1 
HETATM 9821  O  O    . HOH I 6 .   ? 9.745   18.939  35.150  1.00 50.35  ? 765 HOH A O    1 
HETATM 9822  O  O    . HOH I 6 .   ? -12.546 -15.295 14.440  1.00 27.38  ? 766 HOH A O    1 
HETATM 9823  O  O    . HOH I 6 .   ? 15.957  7.076   22.432  1.00 31.57  ? 767 HOH A O    1 
HETATM 9824  O  O    . HOH I 6 .   ? 4.965   21.153  32.001  1.00 27.14  ? 768 HOH A O    1 
HETATM 9825  O  O    . HOH I 6 .   ? -18.763 0.586   29.342  1.00 35.29  ? 769 HOH A O    1 
HETATM 9826  O  O    . HOH I 6 .   ? -5.286  1.381   -1.888  1.00 28.26  ? 770 HOH A O    1 
HETATM 9827  O  O    . HOH I 6 .   ? 5.040   23.079  24.868  1.00 42.03  ? 771 HOH A O    1 
HETATM 9828  O  O    . HOH I 6 .   ? -6.321  -13.209 35.846  1.00 41.23  ? 772 HOH A O    1 
HETATM 9829  O  O    . HOH I 6 .   ? -4.775  -10.096 -3.776  1.00 50.87  ? 773 HOH A O    1 
HETATM 9830  O  O    . HOH I 6 .   ? -15.406 3.836   5.008   1.00 30.26  ? 774 HOH A O    1 
HETATM 9831  O  O    . HOH I 6 .   ? 2.165   -10.277 39.204  1.00 47.60  ? 775 HOH A O    1 
HETATM 9832  O  O    . HOH I 6 .   ? -13.001 18.607  37.196  1.00 44.20  ? 776 HOH A O    1 
HETATM 9833  O  O    . HOH I 6 .   ? -18.191 1.455   17.631  1.00 40.39  ? 777 HOH A O    1 
HETATM 9834  O  O    . HOH I 6 .   ? 18.550  -17.300 4.060   1.00 28.17  ? 778 HOH A O    1 
HETATM 9835  O  O    . HOH I 6 .   ? 9.556   8.668   7.020   1.00 45.23  ? 779 HOH A O    1 
HETATM 9836  O  O    . HOH I 6 .   ? 4.152   24.448  31.833  1.00 41.26  ? 780 HOH A O    1 
HETATM 9837  O  O    . HOH I 6 .   ? -19.041 -12.437 29.165  1.00 39.51  ? 781 HOH A O    1 
HETATM 9838  O  O    . HOH I 6 .   ? -17.305 -3.550  33.484  1.00 43.46  ? 782 HOH A O    1 
HETATM 9839  O  O    . HOH I 6 .   ? -5.335  -28.421 16.750  1.00 41.56  ? 783 HOH A O    1 
HETATM 9840  O  O    . HOH I 6 .   ? 0.571   23.018  19.304  1.00 31.26  ? 784 HOH A O    1 
HETATM 9841  O  O    . HOH I 6 .   ? -18.609 5.954   10.785  1.00 31.97  ? 785 HOH A O    1 
HETATM 9842  O  O    . HOH I 6 .   ? -14.064 18.796  15.745  1.00 46.27  ? 786 HOH A O    1 
HETATM 9843  O  O    . HOH I 6 .   ? -20.413 1.583   9.735   1.00 40.97  ? 787 HOH A O    1 
HETATM 9844  O  O    . HOH I 6 .   ? 10.435  2.042   8.439   1.00 41.89  ? 788 HOH A O    1 
HETATM 9845  O  O    . HOH I 6 .   ? 16.722  2.722   23.456  1.00 24.19  ? 789 HOH A O    1 
HETATM 9846  O  O    . HOH I 6 .   ? -21.175 -0.987  16.470  1.00 37.97  ? 790 HOH A O    1 
HETATM 9847  O  O    . HOH I 6 .   ? -14.023 19.428  26.380  1.00 29.01  ? 791 HOH A O    1 
HETATM 9848  O  O    . HOH I 6 .   ? 16.869  5.749   17.901  1.00 35.54  ? 792 HOH A O    1 
HETATM 9849  O  O    . HOH I 6 .   ? -13.467 11.633  35.488  1.00 36.99  ? 793 HOH A O    1 
HETATM 9850  O  O    . HOH I 6 .   ? -14.891 5.001   0.864   1.00 37.71  ? 794 HOH A O    1 
HETATM 9851  O  O    . HOH I 6 .   ? 2.202   14.690  8.332   1.00 30.43  ? 795 HOH A O    1 
HETATM 9852  O  O    . HOH I 6 .   ? -4.282  -24.423 15.797  1.00 25.54  ? 796 HOH A O    1 
HETATM 9853  O  O    . HOH I 6 .   ? -17.985 -4.452  35.962  1.00 47.48  ? 797 HOH A O    1 
HETATM 9854  O  O    . HOH I 6 .   ? 12.367  4.048   8.675   1.00 42.66  ? 798 HOH A O    1 
HETATM 9855  O  O    . HOH I 6 .   ? -1.196  13.952  5.665   1.00 30.86  ? 799 HOH A O    1 
HETATM 9856  O  O    . HOH I 6 .   ? -7.815  8.924   39.855  1.00 30.38  ? 800 HOH A O    1 
HETATM 9857  O  O    . HOH I 6 .   ? -8.491  22.359  18.199  1.00 41.26  ? 801 HOH A O    1 
HETATM 9858  O  O    . HOH I 6 .   ? -4.397  -27.490 13.004  1.00 31.72  ? 802 HOH A O    1 
HETATM 9859  O  O    . HOH I 6 .   ? -11.511 -16.235 21.132  1.00 35.16  ? 803 HOH A O    1 
HETATM 9860  O  O    . HOH I 6 .   ? -12.479 -14.930 40.990  1.00 38.71  ? 804 HOH A O    1 
HETATM 9861  O  O    . HOH I 6 .   ? 18.093  8.470   26.561  1.00 40.03  ? 805 HOH A O    1 
HETATM 9862  O  O    . HOH I 6 .   ? -12.632 13.519  29.211  1.00 31.25  ? 806 HOH A O    1 
HETATM 9863  O  O    . HOH I 6 .   ? 9.635   -25.217 18.588  1.00 32.00  ? 807 HOH A O    1 
HETATM 9864  O  O    . HOH I 6 .   ? -19.131 1.748   26.632  1.00 29.19  ? 808 HOH A O    1 
HETATM 9865  O  O    . HOH I 6 .   ? 8.567   10.752  42.547  1.00 38.73  ? 809 HOH A O    1 
HETATM 9866  O  O    . HOH I 6 .   ? -11.891 0.805   1.859   1.00 34.29  ? 810 HOH A O    1 
HETATM 9867  O  O    . HOH I 6 .   ? 23.433  -5.383  3.933   1.00 42.31  ? 811 HOH A O    1 
HETATM 9868  O  O    . HOH I 6 .   ? 14.751  20.492  25.986  1.00 37.76  ? 812 HOH A O    1 
HETATM 9869  O  O    . HOH I 6 .   ? 7.231   -15.160 6.310   1.00 37.36  ? 813 HOH A O    1 
HETATM 9870  O  O    . HOH I 6 .   ? 19.571  15.667  19.031  1.00 45.02  ? 814 HOH A O    1 
HETATM 9871  O  O    . HOH I 6 .   ? -5.988  -15.349 44.189  1.00 31.09  ? 815 HOH A O    1 
HETATM 9872  O  O    . HOH I 6 .   ? 2.510   -15.267 33.621  1.00 39.97  ? 816 HOH A O    1 
HETATM 9873  O  O    . HOH I 6 .   ? -15.222 13.939  32.671  1.00 55.10  ? 817 HOH A O    1 
HETATM 9874  O  O    . HOH I 6 .   ? -5.073  -31.072 17.036  1.00 47.84  ? 818 HOH A O    1 
HETATM 9875  O  O    . HOH I 6 .   ? -17.761 -8.218  37.283  1.00 48.33  ? 819 HOH A O    1 
HETATM 9876  O  O    . HOH I 6 .   ? 1.305   -16.394 36.036  1.00 39.42  ? 820 HOH A O    1 
HETATM 9877  O  O    . HOH I 6 .   ? 0.449   -7.700  39.029  1.00 39.84  ? 821 HOH A O    1 
HETATM 9878  O  O    . HOH I 6 .   ? -16.194 16.283  20.890  1.00 30.51  ? 822 HOH A O    1 
HETATM 9879  O  O    . HOH I 6 .   ? -18.361 3.692   22.986  1.00 41.92  ? 823 HOH A O    1 
HETATM 9880  O  O    . HOH I 6 .   ? -15.672 17.995  18.448  1.00 29.91  ? 824 HOH A O    1 
HETATM 9881  O  O    . HOH I 6 .   ? 17.843  5.179   23.801  1.00 36.38  ? 825 HOH A O    1 
HETATM 9882  O  O    . HOH I 6 .   ? 17.942  3.508   15.234  1.00 47.93  ? 826 HOH A O    1 
HETATM 9883  O  O    . HOH I 6 .   ? -4.023  13.230  4.722   1.00 29.54  ? 827 HOH A O    1 
HETATM 9884  O  O    . HOH I 6 .   ? 4.522   24.883  28.942  1.00 38.35  ? 828 HOH A O    1 
HETATM 9885  O  O    . HOH I 6 .   ? -2.828  1.880   -2.914  1.00 48.30  ? 829 HOH A O    1 
HETATM 9886  O  O    . HOH I 6 .   ? 16.934  4.662   35.002  1.00 34.92  ? 830 HOH A O    1 
HETATM 9887  O  O    . HOH I 6 .   ? 6.145   22.608  26.863  1.00 41.97  ? 831 HOH A O    1 
HETATM 9888  O  O    . HOH I 6 .   ? 15.951  7.683   25.383  1.00 39.24  ? 832 HOH A O    1 
HETATM 9889  O  O    . HOH I 6 .   ? 15.474  24.221  28.593  1.00 34.17  ? 833 HOH A O    1 
HETATM 9890  O  O    . HOH I 6 .   ? -14.288 5.284   31.075  1.00 36.93  ? 834 HOH A O    1 
HETATM 9891  O  O    . HOH I 6 .   ? -11.640 -13.095 39.491  1.00 41.24  ? 835 HOH A O    1 
HETATM 9892  O  O    . HOH I 6 .   ? -4.500  -30.221 12.157  1.00 34.89  ? 836 HOH A O    1 
HETATM 9893  O  O    . HOH I 6 .   ? -19.000 -8.778  17.112  1.00 25.24  ? 837 HOH A O    1 
HETATM 9894  O  O    . HOH I 6 .   ? 16.647  21.876  29.599  1.00 34.94  ? 838 HOH A O    1 
HETATM 9895  O  O    . HOH I 6 .   ? -12.573 16.476  22.710  1.00 37.24  ? 839 HOH A O    1 
HETATM 9896  O  O    . HOH I 6 .   ? -7.655  -0.248  38.250  1.00 45.11  ? 840 HOH A O    1 
HETATM 9897  O  O    . HOH I 6 .   ? -6.838  24.121  19.060  1.00 53.73  ? 841 HOH A O    1 
HETATM 9898  O  O    . HOH I 6 .   ? -4.194  2.782   38.856  1.00 25.14  ? 842 HOH A O    1 
HETATM 9899  O  O    . HOH I 6 .   ? -8.613  6.139   39.546  1.00 30.56  ? 843 HOH A O    1 
HETATM 9900  O  O    . HOH I 6 .   ? -19.273 -2.633  17.059  1.00 29.99  ? 844 HOH A O    1 
HETATM 9901  O  O    . HOH I 6 .   ? 3.168   18.133  10.912  1.00 52.21  ? 845 HOH A O    1 
HETATM 9902  O  O    . HOH I 6 .   ? -8.009  -11.037 33.951  1.00 41.15  ? 846 HOH A O    1 
HETATM 9903  O  O    . HOH I 6 .   ? 2.128   -20.027 28.439  1.00 37.31  ? 847 HOH A O    1 
HETATM 9904  O  O    . HOH I 6 .   ? 9.745   -8.428  35.334  1.00 36.12  ? 848 HOH A O    1 
HETATM 9905  O  O    . HOH I 6 .   ? -2.072  10.671  35.871  1.00 33.99  ? 849 HOH A O    1 
HETATM 9906  O  O    . HOH I 6 .   ? -12.818 9.050   29.890  1.00 30.51  ? 850 HOH A O    1 
HETATM 9907  O  O    . HOH I 6 .   ? -3.803  5.614   40.032  1.00 22.78  ? 851 HOH A O    1 
HETATM 9908  O  O    . HOH I 6 .   ? -4.447  -4.407  30.836  1.00 43.51  ? 852 HOH A O    1 
HETATM 9909  O  O    . HOH I 6 .   ? 9.905   -10.846 28.388  1.00 25.09  ? 853 HOH A O    1 
HETATM 9910  O  O    . HOH I 6 .   ? -6.788  2.195   39.012  1.00 30.99  ? 854 HOH A O    1 
HETATM 9911  O  O    . HOH I 6 .   ? 3.883   13.856  5.845   1.00 44.38  ? 855 HOH A O    1 
HETATM 9912  O  O    . HOH I 6 .   ? -4.600  -25.158 26.980  1.00 39.57  ? 856 HOH A O    1 
HETATM 9913  O  O    . HOH I 6 .   ? -13.783 2.162   2.020   1.00 34.65  ? 857 HOH A O    1 
HETATM 9914  O  O    . HOH I 6 .   ? 19.560  -1.597  17.152  1.00 26.11  ? 858 HOH A O    1 
HETATM 9915  O  O    . HOH I 6 .   ? -10.700 -19.152 17.674  1.00 32.13  ? 859 HOH A O    1 
HETATM 9916  O  O    . HOH I 6 .   ? -16.927 -1.400  30.642  1.00 33.50  ? 860 HOH A O    1 
HETATM 9917  O  O    . HOH I 6 .   ? -13.730 23.863  29.899  1.00 39.12  ? 861 HOH A O    1 
HETATM 9918  O  O    . HOH I 6 .   ? 4.321   -4.737  39.657  1.00 35.62  ? 862 HOH A O    1 
HETATM 9919  O  O    . HOH I 6 .   ? -18.424 -7.920  27.772  1.00 32.13  ? 863 HOH A O    1 
HETATM 9920  O  O    . HOH I 6 .   ? -2.567  -5.672  37.554  1.00 46.18  ? 864 HOH A O    1 
HETATM 9921  O  O    . HOH I 6 .   ? -16.945 21.732  30.378  1.00 43.46  ? 865 HOH A O    1 
HETATM 9922  O  O    . HOH I 6 .   ? -17.911 9.838   28.687  1.00 39.68  ? 866 HOH A O    1 
HETATM 9923  O  O    . HOH I 6 .   ? -16.824 13.459  27.048  1.00 42.99  ? 867 HOH A O    1 
HETATM 9924  O  O    . HOH I 6 .   ? 9.680   -3.583  38.700  1.00 38.08  ? 868 HOH A O    1 
HETATM 9925  O  O    . HOH I 6 .   ? -6.940  -33.299 20.509  1.00 35.46  ? 869 HOH A O    1 
HETATM 9926  O  O    . HOH I 6 .   ? -12.545 -17.198 9.157   1.00 33.74  ? 870 HOH A O    1 
HETATM 9927  O  O    . HOH I 6 .   ? 4.513   10.158  4.064   1.00 40.18  ? 871 HOH A O    1 
HETATM 9928  O  O    . HOH I 6 .   ? 19.781  4.661   21.732  1.00 45.33  ? 872 HOH A O    1 
HETATM 9929  O  O    . HOH I 6 .   ? 19.919  -5.518  30.946  1.00 43.70  ? 873 HOH A O    1 
HETATM 9930  O  O    . HOH I 6 .   ? -4.439  -32.745 27.054  1.00 52.79  ? 874 HOH A O    1 
HETATM 9931  O  O    . HOH I 6 .   ? 13.824  -10.663 29.672  1.00 35.28  ? 875 HOH A O    1 
HETATM 9932  O  O    . HOH I 6 .   ? -17.567 6.179   26.720  1.00 27.64  ? 876 HOH A O    1 
HETATM 9933  O  O    . HOH I 6 .   ? -11.574 10.688  39.907  1.00 37.07  ? 877 HOH A O    1 
HETATM 9934  O  O    . HOH I 6 .   ? -14.611 7.386   29.690  1.00 31.82  ? 878 HOH A O    1 
HETATM 9935  O  O    . HOH I 6 .   ? 2.250   -18.009 32.120  1.00 38.67  ? 879 HOH A O    1 
HETATM 9936  O  O    . HOH I 6 .   ? -17.880 -3.998  30.963  1.00 31.52  ? 880 HOH A O    1 
HETATM 9937  O  O    . HOH I 6 .   ? 14.813  -7.048  32.237  1.00 32.14  ? 881 HOH A O    1 
HETATM 9938  O  O    . HOH I 6 .   ? 21.148  2.683   24.789  1.00 40.23  ? 882 HOH A O    1 
HETATM 9939  O  O    . HOH I 6 .   ? 10.873  -10.596 33.626  1.00 33.56  ? 883 HOH A O    1 
HETATM 9940  O  O    . HOH I 6 .   ? -0.458  -32.489 17.667  1.00 39.66  ? 884 HOH A O    1 
HETATM 9941  O  O    . HOH I 6 .   ? -7.644  13.581  39.859  1.00 40.14  ? 885 HOH A O    1 
HETATM 9942  O  O    . HOH I 6 .   ? -6.195  -31.953 23.228  1.00 33.48  ? 886 HOH A O    1 
HETATM 9943  O  O    . HOH I 6 .   ? 11.964  -5.471  37.862  1.00 31.01  ? 887 HOH A O    1 
HETATM 9944  O  O    . HOH I 6 .   ? -13.935 11.381  29.636  1.00 26.76  ? 888 HOH A O    1 
HETATM 9945  O  O    . HOH I 6 .   ? -15.689 17.494  25.499  1.00 29.25  ? 889 HOH A O    1 
HETATM 9946  O  O    . HOH I 6 .   ? 7.397   -5.175  38.636  1.00 34.18  ? 890 HOH A O    1 
HETATM 9947  O  O    . HOH I 6 .   ? -2.343  -8.007  30.437  1.00 47.72  ? 891 HOH A O    1 
HETATM 9948  O  O    . HOH I 6 .   ? 1.244   -12.355 40.672  1.00 48.59  ? 892 HOH A O    1 
HETATM 9949  O  O    . HOH I 6 .   ? -14.572 16.142  36.805  1.00 39.99  ? 893 HOH A O    1 
HETATM 9950  O  O    . HOH I 6 .   ? 9.835   -12.656 26.443  1.00 34.68  ? 894 HOH A O    1 
HETATM 9951  O  O    . HOH I 6 .   ? -16.950 12.464  18.759  1.00 38.86  ? 895 HOH A O    1 
HETATM 9952  O  O    . HOH I 6 .   ? -12.563 20.624  15.768  1.00 44.46  ? 896 HOH A O    1 
HETATM 9953  O  O    . HOH I 6 .   ? -0.383  -3.861  -1.627  1.00 47.84  ? 897 HOH A O    1 
HETATM 9954  O  O    . HOH I 6 .   ? 21.184  -2.828  23.649  1.00 47.77  ? 898 HOH A O    1 
HETATM 9955  O  O    . HOH I 6 .   ? -16.775 1.023   35.150  1.00 45.39  ? 899 HOH A O    1 
HETATM 9956  O  O    . HOH I 6 .   ? -13.284 -17.639 13.090  1.00 40.42  ? 900 HOH A O    1 
HETATM 9957  O  O    . HOH I 6 .   ? 11.402  6.223   6.357   1.00 40.16  ? 901 HOH A O    1 
HETATM 9958  O  O    . HOH I 6 .   ? 4.100   -18.465 6.410   1.00 38.96  ? 902 HOH A O    1 
HETATM 9959  O  O    . HOH I 6 .   ? 4.675   -27.286 26.228  1.00 40.85  ? 903 HOH A O    1 
HETATM 9960  O  O    . HOH I 6 .   ? -17.699 8.872   21.038  1.00 37.72  ? 904 HOH A O    1 
HETATM 9961  O  O    . HOH I 6 .   ? 4.229   -15.802 6.034   1.00 30.76  ? 905 HOH A O    1 
HETATM 9962  O  O    . HOH I 6 .   ? -1.445  -0.833  40.972  1.00 33.88  ? 906 HOH A O    1 
HETATM 9963  O  O    . HOH I 6 .   ? 2.974   -32.831 27.270  1.00 36.78  ? 907 HOH A O    1 
HETATM 9964  O  O    . HOH I 6 .   ? -2.841  -22.711 31.711  1.00 43.91  ? 908 HOH A O    1 
HETATM 9965  O  O    . HOH I 6 .   ? 17.600  -6.506  33.028  1.00 39.78  ? 909 HOH A O    1 
HETATM 9966  O  O    . HOH I 6 .   ? -14.154 9.556   34.045  1.00 41.85  ? 910 HOH A O    1 
HETATM 9967  O  O    . HOH I 6 .   ? -5.794  6.274   41.551  1.00 37.27  ? 911 HOH A O    1 
HETATM 9968  O  O    . HOH I 6 .   ? -18.871 7.210   23.391  1.00 42.39  ? 912 HOH A O    1 
HETATM 9969  O  O    . HOH I 6 .   ? 10.695  -11.828 30.695  1.00 34.76  ? 913 HOH A O    1 
HETATM 9970  O  O    . HOH I 6 .   ? -12.850 -15.323 2.426   1.00 38.03  ? 914 HOH A O    1 
HETATM 9971  O  O    . HOH I 6 .   ? 17.318  22.375  32.154  1.00 39.61  ? 915 HOH A O    1 
HETATM 9972  O  O    . HOH I 6 .   ? 13.522  -7.286  34.725  1.00 33.10  ? 916 HOH A O    1 
HETATM 9973  O  O    . HOH I 6 .   ? -15.426 11.332  31.858  1.00 39.82  ? 917 HOH A O    1 
HETATM 9974  O  O    . HOH I 6 .   ? 14.816  -9.646  31.742  1.00 37.45  ? 918 HOH A O    1 
HETATM 9975  O  O    . HOH I 6 .   ? -19.827 -0.053  24.664  1.00 39.86  ? 919 HOH A O    1 
HETATM 9976  O  O    . HOH I 6 .   ? -11.982 17.423  40.608  1.00 50.63  ? 920 HOH A O    1 
HETATM 9977  O  O    . HOH I 6 .   ? -21.279 -1.211  29.358  1.00 48.40  ? 921 HOH A O    1 
HETATM 9978  O  O    . HOH I 6 .   ? 15.712  -12.562 28.655  1.00 47.93  ? 922 HOH A O    1 
HETATM 9979  O  O    . HOH I 6 .   ? -21.577 -2.195  25.332  1.00 40.50  ? 923 HOH A O    1 
HETATM 9980  O  O    . HOH I 6 .   ? -23.085 -2.091  22.995  1.00 50.60  ? 924 HOH A O    1 
HETATM 9981  O  O    . HOH J 6 .   ? 33.531  -54.585 25.591  1.00 26.14  ? 501 HOH B O    1 
HETATM 9982  O  O    . HOH J 6 .   ? 8.517   -46.348 29.781  1.00 33.63  ? 502 HOH B O    1 
HETATM 9983  O  O    . HOH J 6 .   ? 29.127  -39.316 30.058  1.00 32.79  ? 503 HOH B O    1 
HETATM 9984  O  O    . HOH J 6 .   ? 24.948  -35.392 22.560  1.00 27.43  ? 504 HOH B O    1 
HETATM 9985  O  O    . HOH J 6 .   ? 32.843  -38.095 -8.375  1.00 30.57  ? 505 HOH B O    1 
HETATM 9986  O  O    . HOH J 6 .   ? 42.209  -31.568 1.885   1.00 43.95  ? 506 HOH B O    1 
HETATM 9987  O  O    . HOH J 6 .   ? 19.467  -57.478 9.666   1.00 32.16  ? 507 HOH B O    1 
HETATM 9988  O  O    . HOH J 6 .   ? 22.877  -40.746 31.702  1.00 35.43  ? 508 HOH B O    1 
HETATM 9989  O  O    . HOH J 6 .   ? 33.775  -50.867 1.869   1.00 38.60  ? 509 HOH B O    1 
HETATM 9990  O  O    . HOH J 6 .   ? 30.500  -27.832 32.198  1.00 26.28  ? 510 HOH B O    1 
HETATM 9991  O  O    . HOH J 6 .   ? 19.619  -59.106 11.829  1.00 31.55  ? 511 HOH B O    1 
HETATM 9992  O  O    . HOH J 6 .   ? 20.205  -46.317 2.608   1.00 22.90  ? 512 HOH B O    1 
HETATM 9993  O  O    . HOH J 6 .   ? 38.219  -47.338 17.021  1.00 32.91  ? 513 HOH B O    1 
HETATM 9994  O  O    . HOH J 6 .   ? 25.930  -11.611 26.211  1.00 34.61  ? 514 HOH B O    1 
HETATM 9995  O  O    . HOH J 6 .   ? 34.015  -51.658 5.535   1.00 41.82  ? 515 HOH B O    1 
HETATM 9996  O  O    . HOH J 6 .   ? 20.615  -8.478  27.770  1.00 31.81  ? 516 HOH B O    1 
HETATM 9997  O  O    . HOH J 6 .   ? 37.317  -44.228 -7.232  1.00 46.56  ? 517 HOH B O    1 
HETATM 9998  O  O    . HOH J 6 .   ? 6.288   -37.472 4.831   1.00 26.16  ? 518 HOH B O    1 
HETATM 9999  O  O    . HOH J 6 .   ? 18.419  -9.459  9.750   1.00 33.91  ? 519 HOH B O    1 
HETATM 10000 O  O    . HOH J 6 .   ? 33.724  -61.902 19.564  1.00 33.79  ? 520 HOH B O    1 
HETATM 10001 O  O    . HOH J 6 .   ? 30.226  -18.821 16.547  1.00 26.64  ? 521 HOH B O    1 
HETATM 10002 O  O    . HOH J 6 .   ? 22.870  -6.709  12.896  1.00 31.21  ? 522 HOH B O    1 
HETATM 10003 O  O    . HOH J 6 .   ? 33.648  -57.650 18.769  1.00 28.61  ? 523 HOH B O    1 
HETATM 10004 O  O    . HOH J 6 .   ? 21.710  -35.919 -6.766  1.00 36.67  ? 524 HOH B O    1 
HETATM 10005 O  O    . HOH J 6 .   ? 22.112  -42.593 27.915  1.00 24.22  ? 525 HOH B O    1 
HETATM 10006 O  O    . HOH J 6 .   ? 28.578  -23.474 9.482   1.00 21.19  ? 526 HOH B O    1 
HETATM 10007 O  O    . HOH J 6 .   ? 24.396  -5.065  16.370  1.00 38.85  ? 527 HOH B O    1 
HETATM 10008 O  O    . HOH J 6 .   ? 37.964  -27.462 13.862  1.00 19.81  ? 528 HOH B O    1 
HETATM 10009 O  O    . HOH J 6 .   ? 36.853  -27.212 16.439  1.00 23.16  ? 529 HOH B O    1 
HETATM 10010 O  O    . HOH J 6 .   ? 9.947   -50.882 32.384  1.00 46.57  ? 530 HOH B O    1 
HETATM 10011 O  O    . HOH J 6 .   ? 5.711   -42.214 17.177  1.00 22.15  ? 531 HOH B O    1 
HETATM 10012 O  O    . HOH J 6 .   ? 7.270   -44.049 6.484   1.00 32.42  ? 532 HOH B O    1 
HETATM 10013 O  O    . HOH J 6 .   ? 24.007  -23.832 -2.579  1.00 21.41  ? 533 HOH B O    1 
HETATM 10014 O  O    . HOH J 6 .   ? 13.465  -20.756 20.881  1.00 34.36  ? 534 HOH B O    1 
HETATM 10015 O  O    . HOH J 6 .   ? 19.977  -57.979 22.492  1.00 29.75  ? 535 HOH B O    1 
HETATM 10016 O  O    . HOH J 6 .   ? 14.329  -26.136 32.113  1.00 48.82  ? 536 HOH B O    1 
HETATM 10017 O  O    . HOH J 6 .   ? 13.032  -59.679 18.576  1.00 25.65  ? 537 HOH B O    1 
HETATM 10018 O  O    . HOH J 6 .   ? 15.564  -50.775 29.804  1.00 44.81  ? 538 HOH B O    1 
HETATM 10019 O  O    . HOH J 6 .   ? 33.615  -51.641 15.536  1.00 32.67  ? 539 HOH B O    1 
HETATM 10020 O  O    . HOH J 6 .   ? 12.221  -50.809 4.489   1.00 34.21  ? 540 HOH B O    1 
HETATM 10021 O  O    . HOH J 6 .   ? 31.499  -44.210 23.786  1.00 23.53  ? 541 HOH B O    1 
HETATM 10022 O  O    . HOH J 6 .   ? 30.950  -28.714 0.937   1.00 21.63  ? 542 HOH B O    1 
HETATM 10023 O  O    . HOH J 6 .   ? 21.332  -17.554 24.277  1.00 26.49  ? 543 HOH B O    1 
HETATM 10024 O  O    . HOH J 6 .   ? 32.561  -46.619 28.171  1.00 32.87  ? 544 HOH B O    1 
HETATM 10025 O  O    . HOH J 6 .   ? 14.733  -22.983 21.576  1.00 22.10  ? 545 HOH B O    1 
HETATM 10026 O  O    . HOH J 6 .   ? 21.911  -47.658 27.283  1.00 26.37  ? 546 HOH B O    1 
HETATM 10027 O  O    . HOH J 6 .   ? 6.759   -34.191 25.097  1.00 24.60  ? 547 HOH B O    1 
HETATM 10028 O  O    . HOH J 6 .   ? 26.352  -37.359 23.833  1.00 29.25  ? 548 HOH B O    1 
HETATM 10029 O  O    . HOH J 6 .   ? 0.161   -38.167 20.355  1.00 39.95  ? 549 HOH B O    1 
HETATM 10030 O  O    . HOH J 6 .   ? 40.483  -45.667 7.114   1.00 42.45  ? 550 HOH B O    1 
HETATM 10031 O  O    . HOH J 6 .   ? 23.666  -62.647 18.080  1.00 44.01  ? 551 HOH B O    1 
HETATM 10032 O  O    . HOH J 6 .   ? 36.375  -46.516 14.161  1.00 30.79  ? 552 HOH B O    1 
HETATM 10033 O  O    . HOH J 6 .   ? 33.461  -40.547 32.265  1.00 16.70  ? 553 HOH B O    1 
HETATM 10034 O  O    . HOH J 6 .   ? 19.870  -50.851 2.721   1.00 37.17  ? 554 HOH B O    1 
HETATM 10035 O  O    . HOH J 6 .   ? 4.924   -36.960 9.444   1.00 30.98  ? 555 HOH B O    1 
HETATM 10036 O  O    . HOH J 6 .   ? 26.917  -6.347  23.170  1.00 27.26  ? 556 HOH B O    1 
HETATM 10037 O  O    . HOH J 6 .   ? 28.173  -29.663 -1.911  1.00 22.35  ? 557 HOH B O    1 
HETATM 10038 O  O    . HOH J 6 .   ? 25.965  -45.649 28.374  1.00 23.45  ? 558 HOH B O    1 
HETATM 10039 O  O    . HOH J 6 .   ? 34.574  -22.413 25.365  1.00 25.32  ? 559 HOH B O    1 
HETATM 10040 O  O    . HOH J 6 .   ? 10.731  -24.839 11.458  1.00 25.09  ? 560 HOH B O    1 
HETATM 10041 O  O    . HOH J 6 .   ? 16.780  -12.190 24.657  1.00 37.22  ? 561 HOH B O    1 
HETATM 10042 O  O    . HOH J 6 .   ? 11.079  -44.362 -4.281  1.00 27.34  ? 562 HOH B O    1 
HETATM 10043 O  O    . HOH J 6 .   ? 20.348  -23.824 33.642  1.00 29.39  ? 563 HOH B O    1 
HETATM 10044 O  O    . HOH J 6 .   ? 3.447   -42.670 23.999  1.00 35.98  ? 564 HOH B O    1 
HETATM 10045 O  O    . HOH J 6 .   ? 36.042  -49.786 11.797  1.00 37.41  ? 565 HOH B O    1 
HETATM 10046 O  O    . HOH J 6 .   ? 11.791  -30.807 17.010  1.00 18.57  ? 566 HOH B O    1 
HETATM 10047 O  O    . HOH J 6 .   ? 23.501  -47.871 24.836  1.00 22.73  ? 567 HOH B O    1 
HETATM 10048 O  O    . HOH J 6 .   ? 32.841  -52.910 11.327  1.00 30.24  ? 568 HOH B O    1 
HETATM 10049 O  O    . HOH J 6 .   ? 38.176  -41.618 19.733  1.00 21.77  ? 569 HOH B O    1 
HETATM 10050 O  O    . HOH J 6 .   ? 13.866  -58.024 16.375  1.00 26.84  ? 570 HOH B O    1 
HETATM 10051 O  O    . HOH J 6 .   ? 8.320   -28.591 23.222  1.00 23.52  ? 571 HOH B O    1 
HETATM 10052 O  O    . HOH J 6 .   ? 5.078   -51.555 27.522  1.00 43.57  ? 572 HOH B O    1 
HETATM 10053 O  O    . HOH J 6 .   ? 29.798  -26.048 0.607   1.00 20.94  ? 573 HOH B O    1 
HETATM 10054 O  O    . HOH J 6 .   ? 6.027   -38.761 17.451  1.00 26.45  ? 574 HOH B O    1 
HETATM 10055 O  O    . HOH J 6 .   ? 40.355  -37.764 5.607   1.00 31.35  ? 575 HOH B O    1 
HETATM 10056 O  O    . HOH J 6 .   ? 1.989   -38.098 16.802  1.00 37.91  ? 576 HOH B O    1 
HETATM 10057 O  O    . HOH J 6 .   ? 9.867   -39.828 0.545   1.00 24.78  ? 577 HOH B O    1 
HETATM 10058 O  O    . HOH J 6 .   ? 18.541  -50.829 27.318  1.00 32.85  ? 578 HOH B O    1 
HETATM 10059 O  O    . HOH J 6 .   ? 28.659  -52.111 29.736  1.00 27.78  ? 579 HOH B O    1 
HETATM 10060 O  O    . HOH J 6 .   ? 23.513  -5.694  25.585  1.00 47.48  ? 580 HOH B O    1 
HETATM 10061 O  O    . HOH J 6 .   ? 43.543  -33.059 5.529   1.00 33.81  ? 581 HOH B O    1 
HETATM 10062 O  O    . HOH J 6 .   ? 15.524  -40.599 22.711  1.00 17.86  ? 582 HOH B O    1 
HETATM 10063 O  O    . HOH J 6 .   ? 37.549  -38.969 11.570  1.00 21.34  ? 583 HOH B O    1 
HETATM 10064 O  O    . HOH J 6 .   ? 30.953  -23.796 1.950   1.00 25.56  ? 584 HOH B O    1 
HETATM 10065 O  O    . HOH J 6 .   ? 42.821  -26.433 3.160   1.00 53.62  ? 585 HOH B O    1 
HETATM 10066 O  O    . HOH J 6 .   ? 30.932  -47.141 20.582  1.00 18.66  ? 586 HOH B O    1 
HETATM 10067 O  O    . HOH J 6 .   ? 36.912  -41.948 -7.117  1.00 36.45  ? 587 HOH B O    1 
HETATM 10068 O  O    . HOH J 6 .   ? 45.333  -25.469 5.502   1.00 46.76  ? 588 HOH B O    1 
HETATM 10069 O  O    . HOH J 6 .   ? 32.100  -36.790 -12.140 1.00 31.35  ? 589 HOH B O    1 
HETATM 10070 O  O    . HOH J 6 .   ? 24.754  -8.467  18.172  1.00 30.25  ? 590 HOH B O    1 
HETATM 10071 O  O    . HOH J 6 .   ? 40.197  -31.310 11.785  1.00 22.65  ? 591 HOH B O    1 
HETATM 10072 O  O    . HOH J 6 .   ? 37.564  -29.348 34.684  1.00 45.17  ? 592 HOH B O    1 
HETATM 10073 O  O    . HOH J 6 .   ? 32.230  -13.560 17.654  1.00 34.68  ? 593 HOH B O    1 
HETATM 10074 O  O    . HOH J 6 .   ? 20.201  -10.411 11.964  1.00 26.74  ? 594 HOH B O    1 
HETATM 10075 O  O    . HOH J 6 .   ? 16.159  -21.158 28.162  1.00 30.40  ? 595 HOH B O    1 
HETATM 10076 O  O    . HOH J 6 .   ? 23.766  -11.725 9.084   1.00 32.35  ? 596 HOH B O    1 
HETATM 10077 O  O    . HOH J 6 .   ? 37.789  -19.492 11.421  1.00 45.83  ? 597 HOH B O    1 
HETATM 10078 O  O    . HOH J 6 .   ? 22.680  -43.666 -3.802  1.00 27.00  ? 598 HOH B O    1 
HETATM 10079 O  O    . HOH J 6 .   ? 35.882  -18.033 5.461   1.00 38.01  ? 599 HOH B O    1 
HETATM 10080 O  O    . HOH J 6 .   ? 39.469  -46.052 -0.993  1.00 24.43  ? 600 HOH B O    1 
HETATM 10081 O  O    . HOH J 6 .   ? 15.586  -33.432 6.950   1.00 15.88  ? 601 HOH B O    1 
HETATM 10082 O  O    . HOH J 6 .   ? 35.304  -49.763 14.453  1.00 30.79  ? 602 HOH B O    1 
HETATM 10083 O  O    . HOH J 6 .   ? 8.801   -30.371 14.526  1.00 24.67  ? 603 HOH B O    1 
HETATM 10084 O  O    . HOH J 6 .   ? 33.458  -29.821 18.309  1.00 14.34  ? 604 HOH B O    1 
HETATM 10085 O  O    . HOH J 6 .   ? 7.281   -43.682 3.736   1.00 44.72  ? 605 HOH B O    1 
HETATM 10086 O  O    . HOH J 6 .   ? 23.368  -48.278 29.457  1.00 30.58  ? 606 HOH B O    1 
HETATM 10087 O  O    . HOH J 6 .   ? 12.948  -10.506 17.995  1.00 19.31  ? 607 HOH B O    1 
HETATM 10088 O  O    . HOH J 6 .   ? 22.124  -20.097 1.243   1.00 28.64  ? 608 HOH B O    1 
HETATM 10089 O  O    . HOH J 6 .   ? 15.506  -58.197 25.924  1.00 34.45  ? 609 HOH B O    1 
HETATM 10090 O  O    . HOH J 6 .   ? 19.090  -22.519 -4.086  1.00 46.82  ? 610 HOH B O    1 
HETATM 10091 O  O    . HOH J 6 .   ? 14.639  -13.158 13.610  1.00 22.30  ? 611 HOH B O    1 
HETATM 10092 O  O    . HOH J 6 .   ? 16.700  -18.235 30.533  1.00 33.70  ? 612 HOH B O    1 
HETATM 10093 O  O    . HOH J 6 .   ? 26.225  -17.309 32.244  1.00 28.87  ? 613 HOH B O    1 
HETATM 10094 O  O    . HOH J 6 .   ? 35.846  -36.893 -2.642  1.00 27.64  ? 614 HOH B O    1 
HETATM 10095 O  O    . HOH J 6 .   ? 20.733  -56.835 15.479  1.00 22.16  ? 615 HOH B O    1 
HETATM 10096 O  O    . HOH J 6 .   ? 38.649  -35.151 16.788  1.00 31.69  ? 616 HOH B O    1 
HETATM 10097 O  O    . HOH J 6 .   ? 25.736  -44.680 -0.241  1.00 20.00  ? 617 HOH B O    1 
HETATM 10098 O  O    . HOH J 6 .   ? 14.397  -25.610 17.190  1.00 16.14  ? 618 HOH B O    1 
HETATM 10099 O  O    . HOH J 6 .   ? 26.752  -42.989 -2.410  1.00 20.38  ? 619 HOH B O    1 
HETATM 10100 O  O    . HOH J 6 .   ? 35.309  -38.439 24.429  1.00 23.43  ? 620 HOH B O    1 
HETATM 10101 O  O    . HOH J 6 .   ? 20.972  -29.416 -3.559  1.00 21.47  ? 621 HOH B O    1 
HETATM 10102 O  O    . HOH J 6 .   ? 13.813  -53.602 9.655   1.00 25.50  ? 622 HOH B O    1 
HETATM 10103 O  O    . HOH J 6 .   ? 23.758  -32.982 -6.912  1.00 33.70  ? 623 HOH B O    1 
HETATM 10104 O  O    . HOH J 6 .   ? 15.239  -42.240 7.269   1.00 19.90  ? 624 HOH B O    1 
HETATM 10105 O  O    . HOH J 6 .   ? 5.135   -40.727 27.632  1.00 38.78  ? 625 HOH B O    1 
HETATM 10106 O  O    . HOH J 6 .   ? 15.100  -22.836 -0.434  1.00 38.83  ? 626 HOH B O    1 
HETATM 10107 O  O    . HOH J 6 .   ? 10.192  -57.595 24.232  1.00 30.34  ? 627 HOH B O    1 
HETATM 10108 O  O    . HOH J 6 .   ? 10.560  -59.652 14.934  1.00 33.03  ? 628 HOH B O    1 
HETATM 10109 O  O    . HOH J 6 .   ? 20.773  -50.817 24.146  1.00 21.95  ? 629 HOH B O    1 
HETATM 10110 O  O    . HOH J 6 .   ? 32.994  -20.760 15.874  1.00 26.31  ? 630 HOH B O    1 
HETATM 10111 O  O    . HOH J 6 .   ? 9.205   -34.313 29.800  1.00 31.40  ? 631 HOH B O    1 
HETATM 10112 O  O    . HOH J 6 .   ? 8.981   -19.871 13.200  1.00 21.77  ? 632 HOH B O    1 
HETATM 10113 O  O    . HOH J 6 .   ? 38.370  -35.968 31.801  1.00 17.91  ? 633 HOH B O    1 
HETATM 10114 O  O    . HOH J 6 .   ? 24.195  -29.487 -5.246  1.00 28.51  ? 634 HOH B O    1 
HETATM 10115 O  O    . HOH J 6 .   ? 22.322  -20.162 3.993   1.00 19.33  ? 635 HOH B O    1 
HETATM 10116 O  O    . HOH J 6 .   ? 25.567  -11.711 16.584  1.00 32.09  ? 636 HOH B O    1 
HETATM 10117 O  O    . HOH J 6 .   ? 25.783  -34.556 -9.664  1.00 42.69  ? 637 HOH B O    1 
HETATM 10118 O  O    . HOH J 6 .   ? 37.807  -28.027 31.215  1.00 28.29  ? 638 HOH B O    1 
HETATM 10119 O  O    . HOH J 6 .   ? 18.188  -48.265 0.099   1.00 50.13  ? 639 HOH B O    1 
HETATM 10120 O  O    . HOH J 6 .   ? 27.519  -19.773 32.885  1.00 24.64  ? 640 HOH B O    1 
HETATM 10121 O  O    . HOH J 6 .   ? 39.320  -42.917 5.635   1.00 25.13  ? 641 HOH B O    1 
HETATM 10122 O  O    . HOH J 6 .   ? 16.432  -38.942 -1.671  1.00 32.36  ? 642 HOH B O    1 
HETATM 10123 O  O    . HOH J 6 .   ? 20.524  -43.875 31.742  1.00 36.43  ? 643 HOH B O    1 
HETATM 10124 O  O    . HOH J 6 .   ? 25.524  -61.436 22.766  1.00 36.83  ? 644 HOH B O    1 
HETATM 10125 O  O    . HOH J 6 .   ? 30.081  -33.363 -4.364  1.00 20.68  ? 645 HOH B O    1 
HETATM 10126 O  O    . HOH J 6 .   ? 28.694  -57.390 15.027  1.00 26.23  ? 646 HOH B O    1 
HETATM 10127 O  O    . HOH J 6 .   ? 7.726   -28.844 16.378  1.00 23.46  ? 647 HOH B O    1 
HETATM 10128 O  O    . HOH J 6 .   ? 34.675  -33.392 6.526   1.00 17.85  ? 648 HOH B O    1 
HETATM 10129 O  O    . HOH J 6 .   ? 26.680  -60.892 14.003  1.00 38.75  ? 649 HOH B O    1 
HETATM 10130 O  O    . HOH J 6 .   ? 36.505  -49.597 19.637  1.00 29.05  ? 650 HOH B O    1 
HETATM 10131 O  O    . HOH J 6 .   ? 23.062  -5.665  20.522  1.00 22.34  ? 651 HOH B O    1 
HETATM 10132 O  O    . HOH J 6 .   ? 26.038  -61.814 18.303  1.00 39.72  ? 652 HOH B O    1 
HETATM 10133 O  O    . HOH J 6 .   ? 39.128  -35.382 13.848  1.00 32.25  ? 653 HOH B O    1 
HETATM 10134 O  O    . HOH J 6 .   ? 26.792  -14.295 29.845  1.00 41.71  ? 654 HOH B O    1 
HETATM 10135 O  O    . HOH J 6 .   ? 34.365  -35.591 17.540  1.00 17.33  ? 655 HOH B O    1 
HETATM 10136 O  O    . HOH J 6 .   ? 12.112  -51.847 28.687  1.00 35.47  ? 656 HOH B O    1 
HETATM 10137 O  O    . HOH J 6 .   ? 29.698  -56.203 10.511  1.00 38.19  ? 657 HOH B O    1 
HETATM 10138 O  O    . HOH J 6 .   ? 4.210   -54.505 11.774  1.00 43.25  ? 658 HOH B O    1 
HETATM 10139 O  O    . HOH J 6 .   ? 6.225   -26.819 7.405   1.00 36.44  ? 659 HOH B O    1 
HETATM 10140 O  O    . HOH J 6 .   ? 34.982  -59.984 18.226  1.00 36.01  ? 660 HOH B O    1 
HETATM 10141 O  O    . HOH J 6 .   ? 35.826  -46.077 20.268  1.00 25.71  ? 661 HOH B O    1 
HETATM 10142 O  O    . HOH J 6 .   ? 5.687   -58.579 15.831  1.00 34.45  ? 662 HOH B O    1 
HETATM 10143 O  O    . HOH J 6 .   ? 8.233   -57.376 13.096  1.00 41.78  ? 663 HOH B O    1 
HETATM 10144 O  O    . HOH J 6 .   ? 28.792  -43.417 -10.743 1.00 26.95  ? 664 HOH B O    1 
HETATM 10145 O  O    . HOH J 6 .   ? 37.059  -61.600 21.390  1.00 27.99  ? 665 HOH B O    1 
HETATM 10146 O  O    . HOH J 6 .   ? 34.497  -20.847 22.212  1.00 29.09  ? 666 HOH B O    1 
HETATM 10147 O  O    . HOH J 6 .   ? 13.294  -29.254 24.241  1.00 25.36  ? 667 HOH B O    1 
HETATM 10148 O  O    . HOH J 6 .   ? 24.772  -14.197 17.430  1.00 15.99  ? 668 HOH B O    1 
HETATM 10149 O  O    . HOH J 6 .   ? 16.102  -24.879 28.614  1.00 22.41  ? 669 HOH B O    1 
HETATM 10150 O  O    . HOH J 6 .   ? 7.703   -56.996 23.255  1.00 42.20  ? 670 HOH B O    1 
HETATM 10151 O  O    . HOH J 6 .   ? 30.085  -28.499 29.190  1.00 25.59  ? 671 HOH B O    1 
HETATM 10152 O  O    . HOH J 6 .   ? 30.249  -22.143 7.999   1.00 22.52  ? 672 HOH B O    1 
HETATM 10153 O  O    . HOH J 6 .   ? 2.671   -40.220 24.546  1.00 47.32  ? 673 HOH B O    1 
HETATM 10154 O  O    . HOH J 6 .   ? 24.701  -20.292 18.642  1.00 13.27  ? 674 HOH B O    1 
HETATM 10155 O  O    . HOH J 6 .   ? 10.500  -25.805 5.966   1.00 33.04  ? 675 HOH B O    1 
HETATM 10156 O  O    . HOH J 6 .   ? 20.757  -18.380 5.391   1.00 21.73  ? 676 HOH B O    1 
HETATM 10157 O  O    . HOH J 6 .   ? 36.237  -38.476 -5.080  1.00 34.06  ? 677 HOH B O    1 
HETATM 10158 O  O    . HOH J 6 .   ? 34.129  -22.005 2.050   1.00 40.14  ? 678 HOH B O    1 
HETATM 10159 O  O    . HOH J 6 .   ? 22.843  -38.081 -7.582  1.00 47.87  ? 679 HOH B O    1 
HETATM 10160 O  O    . HOH J 6 .   ? 37.221  -59.313 19.860  1.00 37.28  ? 680 HOH B O    1 
HETATM 10161 O  O    . HOH J 6 .   ? 28.345  -13.389 13.240  1.00 31.08  ? 681 HOH B O    1 
HETATM 10162 O  O    . HOH J 6 .   ? 20.739  -50.161 17.130  1.00 30.48  ? 682 HOH B O    1 
HETATM 10163 O  O    . HOH J 6 .   ? 17.823  -60.563 15.614  1.00 34.17  ? 683 HOH B O    1 
HETATM 10164 O  O    . HOH J 6 .   ? 21.300  -29.970 34.102  1.00 24.95  ? 684 HOH B O    1 
HETATM 10165 O  O    . HOH J 6 .   ? 26.472  -27.727 32.285  1.00 42.54  ? 685 HOH B O    1 
HETATM 10166 O  O    . HOH J 6 .   ? 40.924  -38.769 8.695   1.00 34.28  ? 686 HOH B O    1 
HETATM 10167 O  O    . HOH J 6 .   ? 17.589  -58.423 13.819  1.00 35.16  ? 687 HOH B O    1 
HETATM 10168 O  O    . HOH J 6 .   ? 10.054  -39.856 31.065  1.00 39.42  ? 688 HOH B O    1 
HETATM 10169 O  O    . HOH J 6 .   ? 8.989   -25.563 9.890   1.00 31.07  ? 689 HOH B O    1 
HETATM 10170 O  O    . HOH J 6 .   ? 32.189  -48.057 25.303  1.00 38.06  ? 690 HOH B O    1 
HETATM 10171 O  O    . HOH J 6 .   ? 37.168  -24.048 3.411   1.00 35.67  ? 691 HOH B O    1 
HETATM 10172 O  O    . HOH J 6 .   ? 24.544  -16.120 25.796  1.00 18.54  ? 692 HOH B O    1 
HETATM 10173 O  O    . HOH J 6 .   ? 27.439  -22.896 -3.083  1.00 30.15  ? 693 HOH B O    1 
HETATM 10174 O  O    . HOH J 6 .   ? 37.883  -32.524 26.094  1.00 20.85  ? 694 HOH B O    1 
HETATM 10175 O  O    . HOH J 6 .   ? 15.749  -10.705 10.435  1.00 42.38  ? 695 HOH B O    1 
HETATM 10176 O  O    . HOH J 6 .   ? 39.909  -37.552 12.427  1.00 36.10  ? 696 HOH B O    1 
HETATM 10177 O  O    . HOH J 6 .   ? 20.362  -37.597 16.210  1.00 15.19  ? 697 HOH B O    1 
HETATM 10178 O  O    . HOH J 6 .   ? 15.913  -19.431 36.395  1.00 49.06  ? 698 HOH B O    1 
HETATM 10179 O  O    . HOH J 6 .   ? 17.758  -26.149 -2.483  1.00 32.83  ? 699 HOH B O    1 
HETATM 10180 O  O    . HOH J 6 .   ? 30.953  -16.506 19.957  1.00 20.52  ? 700 HOH B O    1 
HETATM 10181 O  O    . HOH J 6 .   ? 17.373  -36.899 33.641  1.00 33.74  ? 701 HOH B O    1 
HETATM 10182 O  O    . HOH J 6 .   ? 2.377   -48.692 2.521   1.00 42.70  ? 702 HOH B O    1 
HETATM 10183 O  O    . HOH J 6 .   ? 37.974  -36.220 -0.702  1.00 39.59  ? 703 HOH B O    1 
HETATM 10184 O  O    . HOH J 6 .   ? 20.895  -45.166 0.223   1.00 27.75  ? 704 HOH B O    1 
HETATM 10185 O  O    . HOH J 6 .   ? 39.424  -27.230 27.582  1.00 27.43  ? 705 HOH B O    1 
HETATM 10186 O  O    . HOH J 6 .   ? 23.847  -18.639 32.867  1.00 47.37  ? 706 HOH B O    1 
HETATM 10187 O  O    . HOH J 6 .   ? 11.215  -58.424 22.108  1.00 36.83  ? 707 HOH B O    1 
HETATM 10188 O  O    . HOH J 6 .   ? 33.584  -29.029 0.527   1.00 30.60  ? 708 HOH B O    1 
HETATM 10189 O  O    . HOH J 6 .   ? 22.814  -27.937 32.974  1.00 33.44  ? 709 HOH B O    1 
HETATM 10190 O  O    . HOH J 6 .   ? 30.431  -34.163 -7.298  1.00 39.10  ? 710 HOH B O    1 
HETATM 10191 O  O    . HOH J 6 .   ? 12.264  -57.665 12.373  1.00 41.79  ? 711 HOH B O    1 
HETATM 10192 O  O    . HOH J 6 .   ? 35.666  -22.821 21.049  1.00 31.68  ? 712 HOH B O    1 
HETATM 10193 O  O    . HOH J 6 .   ? 27.586  -58.914 26.278  1.00 29.17  ? 713 HOH B O    1 
HETATM 10194 O  O    . HOH J 6 .   ? 15.697  -8.880  22.962  1.00 23.56  ? 714 HOH B O    1 
HETATM 10195 O  O    . HOH J 6 .   ? 37.435  -48.187 -4.005  1.00 31.23  ? 715 HOH B O    1 
HETATM 10196 O  O    . HOH J 6 .   ? 38.759  -42.058 13.099  1.00 25.79  ? 716 HOH B O    1 
HETATM 10197 O  O    . HOH J 6 .   ? 23.557  -44.526 29.351  1.00 26.36  ? 717 HOH B O    1 
HETATM 10198 O  O    . HOH J 6 .   ? 18.575  -15.004 24.710  1.00 30.34  ? 718 HOH B O    1 
HETATM 10199 O  O    . HOH J 6 .   ? 25.577  -10.951 19.143  1.00 20.09  ? 719 HOH B O    1 
HETATM 10200 O  O    . HOH J 6 .   ? 28.595  -11.701 16.246  1.00 33.24  ? 720 HOH B O    1 
HETATM 10201 O  O    . HOH J 6 .   ? 25.986  -40.721 -10.719 1.00 34.87  ? 721 HOH B O    1 
HETATM 10202 O  O    . HOH J 6 .   ? 17.837  -61.181 21.986  1.00 35.99  ? 722 HOH B O    1 
HETATM 10203 O  O    . HOH J 6 .   ? 29.510  -16.730 3.423   1.00 41.71  ? 723 HOH B O    1 
HETATM 10204 O  O    . HOH J 6 .   ? 18.645  -48.113 27.558  1.00 28.49  ? 724 HOH B O    1 
HETATM 10205 O  O    . HOH J 6 .   ? 25.377  -17.506 0.751   1.00 47.14  ? 725 HOH B O    1 
HETATM 10206 O  O    . HOH J 6 .   ? 29.377  -22.219 36.459  1.00 26.52  ? 726 HOH B O    1 
HETATM 10207 O  O    . HOH J 6 .   ? 20.008  -43.739 -3.236  1.00 27.61  ? 727 HOH B O    1 
HETATM 10208 O  O    . HOH J 6 .   ? 23.178  -16.972 30.909  1.00 45.15  ? 728 HOH B O    1 
HETATM 10209 O  O    . HOH J 6 .   ? 12.498  -24.562 18.653  1.00 23.79  ? 729 HOH B O    1 
HETATM 10210 O  O    . HOH J 6 .   ? 38.259  -40.130 15.138  1.00 25.03  ? 730 HOH B O    1 
HETATM 10211 O  O    . HOH J 6 .   ? 27.000  -7.356  19.195  1.00 28.56  ? 731 HOH B O    1 
HETATM 10212 O  O    . HOH J 6 .   ? 22.442  -41.572 -6.248  1.00 28.03  ? 732 HOH B O    1 
HETATM 10213 O  O    . HOH J 6 .   ? 4.263   -49.517 6.551   1.00 32.39  ? 733 HOH B O    1 
HETATM 10214 O  O    . HOH J 6 .   ? 29.765  -18.591 7.386   1.00 40.39  ? 734 HOH B O    1 
HETATM 10215 O  O    . HOH J 6 .   ? 31.824  -18.666 21.593  1.00 21.32  ? 735 HOH B O    1 
HETATM 10216 O  O    . HOH J 6 .   ? 33.290  -23.645 0.656   1.00 50.44  ? 736 HOH B O    1 
HETATM 10217 O  O    . HOH J 6 .   ? 5.215   -42.880 13.076  1.00 38.74  ? 737 HOH B O    1 
HETATM 10218 O  O    . HOH J 6 .   ? 37.410  -43.879 24.469  1.00 35.47  ? 738 HOH B O    1 
HETATM 10219 O  O    . HOH J 6 .   ? 20.147  -58.433 7.243   1.00 46.37  ? 739 HOH B O    1 
HETATM 10220 O  O    . HOH J 6 .   ? 25.716  -45.066 -9.869  1.00 32.59  ? 740 HOH B O    1 
HETATM 10221 O  O    . HOH J 6 .   ? 40.262  -24.459 15.076  1.00 34.21  ? 741 HOH B O    1 
HETATM 10222 O  O    . HOH J 6 .   ? 38.249  -34.631 19.513  1.00 27.50  ? 742 HOH B O    1 
HETATM 10223 O  O    . HOH J 6 .   ? 13.946  -14.517 17.005  1.00 31.30  ? 743 HOH B O    1 
HETATM 10224 O  O    . HOH J 6 .   ? 2.037   -42.950 17.011  1.00 39.12  ? 744 HOH B O    1 
HETATM 10225 O  O    . HOH J 6 .   ? 34.465  -31.966 0.131   1.00 41.02  ? 745 HOH B O    1 
HETATM 10226 O  O    . HOH J 6 .   ? 41.861  -30.533 27.232  1.00 45.08  ? 746 HOH B O    1 
HETATM 10227 O  O    . HOH J 6 .   ? 0.582   -33.235 22.376  1.00 37.48  ? 747 HOH B O    1 
HETATM 10228 O  O    . HOH J 6 .   ? 9.265   -38.345 2.825   1.00 21.59  ? 748 HOH B O    1 
HETATM 10229 O  O    . HOH J 6 .   ? 5.470   -40.178 11.669  1.00 28.38  ? 749 HOH B O    1 
HETATM 10230 O  O    . HOH J 6 .   ? 4.141   -34.450 10.616  1.00 29.70  ? 750 HOH B O    1 
HETATM 10231 O  O    . HOH J 6 .   ? 8.711   -31.496 4.143   1.00 22.61  ? 751 HOH B O    1 
HETATM 10232 O  O    . HOH J 6 .   ? 13.465  -24.995 21.331  1.00 29.41  ? 752 HOH B O    1 
HETATM 10233 O  O    . HOH J 6 .   ? 32.940  -52.179 20.250  1.00 29.16  ? 753 HOH B O    1 
HETATM 10234 O  O    . HOH J 6 .   ? 32.360  -56.350 13.886  1.00 38.59  ? 754 HOH B O    1 
HETATM 10235 O  O    . HOH J 6 .   ? 24.062  -6.225  23.056  1.00 22.43  ? 755 HOH B O    1 
HETATM 10236 O  O    . HOH J 6 .   ? 10.294  -17.239 10.417  1.00 46.04  ? 756 HOH B O    1 
HETATM 10237 O  O    . HOH J 6 .   ? 27.370  -29.213 -6.055  1.00 42.92  ? 757 HOH B O    1 
HETATM 10238 O  O    . HOH J 6 .   ? 28.891  -46.529 -4.455  1.00 37.79  ? 758 HOH B O    1 
HETATM 10239 O  O    . HOH J 6 .   ? 23.203  -16.773 -3.292  1.00 33.54  ? 759 HOH B O    1 
HETATM 10240 O  O    . HOH J 6 .   ? 34.231  -20.391 13.489  1.00 32.93  ? 760 HOH B O    1 
HETATM 10241 O  O    . HOH J 6 .   ? 5.498   -46.675 -0.188  1.00 35.67  ? 761 HOH B O    1 
HETATM 10242 O  O    . HOH J 6 .   ? 4.690   -37.981 12.881  1.00 29.02  ? 762 HOH B O    1 
HETATM 10243 O  O    . HOH J 6 .   ? 4.405   -50.904 13.751  1.00 39.66  ? 763 HOH B O    1 
HETATM 10244 O  O    . HOH J 6 .   ? 18.605  -17.609 1.430   1.00 41.38  ? 764 HOH B O    1 
HETATM 10245 O  O    . HOH J 6 .   ? 36.717  -38.801 26.592  1.00 29.86  ? 765 HOH B O    1 
HETATM 10246 O  O    . HOH J 6 .   ? 29.922  -15.646 34.493  1.00 43.62  ? 766 HOH B O    1 
HETATM 10247 O  O    . HOH J 6 .   ? 14.510  -13.265 20.631  1.00 34.51  ? 767 HOH B O    1 
HETATM 10248 O  O    . HOH J 6 .   ? 13.958  -37.639 31.853  1.00 47.40  ? 768 HOH B O    1 
HETATM 10249 O  O    . HOH J 6 .   ? 37.686  -35.936 2.225   1.00 30.98  ? 769 HOH B O    1 
HETATM 10250 O  O    . HOH J 6 .   ? 39.891  -30.655 33.526  1.00 29.05  ? 770 HOH B O    1 
HETATM 10251 O  O    . HOH J 6 .   ? 27.808  -16.714 7.037   1.00 26.03  ? 771 HOH B O    1 
HETATM 10252 O  O    . HOH J 6 .   ? 17.486  -37.322 -8.412  1.00 44.34  ? 772 HOH B O    1 
HETATM 10253 O  O    . HOH J 6 .   ? 40.454  -40.767 12.564  1.00 51.15  ? 773 HOH B O    1 
HETATM 10254 O  O    . HOH J 6 .   ? 36.339  -25.571 20.801  1.00 29.05  ? 774 HOH B O    1 
HETATM 10255 O  O    . HOH J 6 .   ? 4.219   -48.262 13.952  1.00 35.77  ? 775 HOH B O    1 
HETATM 10256 O  O    . HOH J 6 .   ? 4.473   -44.959 1.413   1.00 38.60  ? 776 HOH B O    1 
HETATM 10257 O  O    . HOH J 6 .   ? 24.295  -26.278 34.458  1.00 38.95  ? 777 HOH B O    1 
HETATM 10258 O  O    . HOH J 6 .   ? 22.668  -20.062 38.268  1.00 41.83  ? 778 HOH B O    1 
HETATM 10259 O  O    . HOH J 6 .   ? 17.005  -47.417 -1.602  1.00 28.78  ? 779 HOH B O    1 
HETATM 10260 O  O    . HOH J 6 .   ? 13.839  -19.629 5.216   1.00 35.42  ? 780 HOH B O    1 
HETATM 10261 O  O    . HOH J 6 .   ? 15.437  -14.632 24.962  1.00 41.08  ? 781 HOH B O    1 
HETATM 10262 O  O    . HOH J 6 .   ? 32.508  -63.325 22.816  1.00 33.10  ? 782 HOH B O    1 
HETATM 10263 O  O    . HOH J 6 .   ? 27.956  -45.122 30.249  1.00 26.36  ? 783 HOH B O    1 
HETATM 10264 O  O    . HOH J 6 .   ? 19.929  -62.121 15.644  1.00 41.39  ? 784 HOH B O    1 
HETATM 10265 O  O    . HOH J 6 .   ? 28.476  -32.208 -7.307  1.00 40.18  ? 785 HOH B O    1 
HETATM 10266 O  O    . HOH J 6 .   ? 33.977  -53.196 17.704  1.00 32.32  ? 786 HOH B O    1 
HETATM 10267 O  O    . HOH J 6 .   ? 39.405  -39.792 24.239  1.00 32.76  ? 787 HOH B O    1 
HETATM 10268 O  O    . HOH J 6 .   ? 34.268  -38.099 33.674  1.00 18.28  ? 788 HOH B O    1 
HETATM 10269 O  O    . HOH J 6 .   ? 39.258  -36.953 3.647   1.00 37.52  ? 789 HOH B O    1 
HETATM 10270 O  O    . HOH J 6 .   ? 13.457  -14.056 9.646   1.00 43.23  ? 790 HOH B O    1 
HETATM 10271 O  O    . HOH J 6 .   ? 4.372   -39.134 15.429  1.00 31.25  ? 791 HOH B O    1 
HETATM 10272 O  O    . HOH J 6 .   ? 35.593  -50.763 23.601  1.00 34.04  ? 792 HOH B O    1 
HETATM 10273 O  O    . HOH J 6 .   ? 30.120  -15.212 13.979  1.00 42.97  ? 793 HOH B O    1 
HETATM 10274 O  O    . HOH J 6 .   ? 12.525  -57.524 7.930   1.00 45.03  ? 794 HOH B O    1 
HETATM 10275 O  O    . HOH J 6 .   ? 26.867  -6.759  26.211  1.00 38.66  ? 795 HOH B O    1 
HETATM 10276 O  O    . HOH J 6 .   ? 40.671  -40.336 5.147   1.00 39.48  ? 796 HOH B O    1 
HETATM 10277 O  O    . HOH J 6 .   ? 22.656  -25.453 -4.202  1.00 35.07  ? 797 HOH B O    1 
HETATM 10278 O  O    . HOH J 6 .   ? 32.077  -59.175 26.572  1.00 28.61  ? 798 HOH B O    1 
HETATM 10279 O  O    . HOH J 6 .   ? 12.047  -57.726 25.817  1.00 39.15  ? 799 HOH B O    1 
HETATM 10280 O  O    . HOH J 6 .   ? 7.488   -44.080 29.175  1.00 44.69  ? 800 HOH B O    1 
HETATM 10281 O  O    . HOH J 6 .   ? 35.717  -42.589 29.230  1.00 29.57  ? 801 HOH B O    1 
HETATM 10282 O  O    . HOH J 6 .   ? 27.483  -50.221 31.171  1.00 44.35  ? 802 HOH B O    1 
HETATM 10283 O  O    . HOH J 6 .   ? 40.833  -42.515 -3.294  1.00 33.77  ? 803 HOH B O    1 
HETATM 10284 O  O    . HOH J 6 .   ? 26.753  -45.398 -3.618  1.00 29.27  ? 804 HOH B O    1 
HETATM 10285 O  O    . HOH J 6 .   ? 30.902  -17.035 14.987  1.00 44.42  ? 805 HOH B O    1 
HETATM 10286 O  O    . HOH J 6 .   ? 29.466  -57.687 8.586   1.00 43.59  ? 806 HOH B O    1 
HETATM 10287 O  O    . HOH J 6 .   ? 14.771  -58.933 13.431  1.00 42.66  ? 807 HOH B O    1 
HETATM 10288 O  O    . HOH J 6 .   ? 1.966   -51.313 12.030  1.00 46.97  ? 808 HOH B O    1 
HETATM 10289 O  O    . HOH J 6 .   ? 39.552  -30.686 24.995  1.00 23.38  ? 809 HOH B O    1 
HETATM 10290 O  O    . HOH J 6 .   ? 3.474   -52.587 15.650  1.00 42.78  ? 810 HOH B O    1 
HETATM 10291 O  O    . HOH J 6 .   ? 21.717  -16.993 27.065  1.00 43.58  ? 811 HOH B O    1 
HETATM 10292 O  O    . HOH J 6 .   ? 13.608  -10.823 12.333  1.00 37.50  ? 812 HOH B O    1 
HETATM 10293 O  O    . HOH J 6 .   ? 13.245  -10.429 20.734  1.00 23.88  ? 813 HOH B O    1 
HETATM 10294 O  O    . HOH J 6 .   ? 39.671  -40.084 21.516  1.00 25.57  ? 814 HOH B O    1 
HETATM 10295 O  O    . HOH J 6 .   ? 40.923  -33.565 13.097  1.00 29.65  ? 815 HOH B O    1 
HETATM 10296 O  O    . HOH J 6 .   ? 27.586  -43.262 31.845  1.00 28.55  ? 816 HOH B O    1 
HETATM 10297 O  O    . HOH J 6 .   ? 20.487  -3.657  12.952  1.00 29.52  ? 817 HOH B O    1 
HETATM 10298 O  O    . HOH J 6 .   ? 43.087  -34.939 12.803  1.00 41.64  ? 818 HOH B O    1 
HETATM 10299 O  O    . HOH J 6 .   ? 32.475  -20.897 20.227  1.00 28.55  ? 819 HOH B O    1 
HETATM 10300 O  O    . HOH J 6 .   ? 38.719  -36.990 27.320  1.00 28.70  ? 820 HOH B O    1 
HETATM 10301 O  O    . HOH J 6 .   ? 40.593  -27.258 14.736  1.00 26.40  ? 821 HOH B O    1 
HETATM 10302 O  O    . HOH J 6 .   ? 15.551  -17.659 3.866   1.00 39.13  ? 822 HOH B O    1 
HETATM 10303 O  O    . HOH J 6 .   ? 33.824  -52.307 26.943  1.00 36.71  ? 823 HOH B O    1 
HETATM 10304 O  O    . HOH J 6 .   ? 12.675  -24.151 -0.422  1.00 47.87  ? 824 HOH B O    1 
HETATM 10305 O  O    . HOH J 6 .   ? 8.173   -47.811 33.263  1.00 45.32  ? 825 HOH B O    1 
HETATM 10306 O  O    . HOH J 6 .   ? 19.694  -24.808 35.986  1.00 41.70  ? 826 HOH B O    1 
HETATM 10307 O  O    . HOH J 6 .   ? 24.744  -4.625  12.726  1.00 35.31  ? 827 HOH B O    1 
HETATM 10308 O  O    . HOH J 6 .   ? 29.708  -27.912 -3.552  1.00 35.41  ? 828 HOH B O    1 
HETATM 10309 O  O    . HOH J 6 .   ? 39.404  -41.222 17.432  1.00 35.28  ? 829 HOH B O    1 
HETATM 10310 O  O    . HOH J 6 .   ? 29.671  -60.128 27.706  1.00 30.10  ? 830 HOH B O    1 
HETATM 10311 O  O    . HOH J 6 .   ? 3.037   -41.197 14.886  1.00 43.66  ? 831 HOH B O    1 
HETATM 10312 O  O    . HOH J 6 .   ? 21.602  -4.307  26.066  1.00 44.06  ? 832 HOH B O    1 
HETATM 10313 O  O    . HOH J 6 .   ? 3.471   -44.490 26.016  1.00 43.17  ? 833 HOH B O    1 
HETATM 10314 O  O    . HOH J 6 .   ? 33.338  -47.683 21.893  1.00 29.60  ? 834 HOH B O    1 
HETATM 10315 O  O    . HOH J 6 .   ? 20.782  -63.079 18.114  1.00 42.45  ? 835 HOH B O    1 
HETATM 10316 O  O    . HOH J 6 .   ? 39.816  -37.377 29.884  1.00 28.18  ? 836 HOH B O    1 
HETATM 10317 O  O    . HOH J 6 .   ? 47.227  -29.849 6.113   1.00 43.15  ? 837 HOH B O    1 
HETATM 10318 O  O    . HOH J 6 .   ? 38.845  -42.680 26.416  1.00 42.06  ? 838 HOH B O    1 
HETATM 10319 O  O    . HOH J 6 .   ? 33.012  -46.086 24.251  1.00 38.33  ? 839 HOH B O    1 
HETATM 10320 O  O    . HOH J 6 .   ? 10.407  -31.893 30.150  1.00 39.14  ? 840 HOH B O    1 
HETATM 10321 O  O    . HOH J 6 .   ? 9.243   -45.873 32.284  1.00 39.92  ? 841 HOH B O    1 
HETATM 10322 O  O    . HOH J 6 .   ? 26.031  -32.192 -8.119  1.00 45.70  ? 842 HOH B O    1 
HETATM 10323 O  O    . HOH J 6 .   ? 27.224  -15.875 34.152  1.00 41.14  ? 843 HOH B O    1 
HETATM 10324 O  O    . HOH J 6 .   ? 23.661  -27.348 -5.573  1.00 43.93  ? 844 HOH B O    1 
HETATM 10325 O  O    . HOH J 6 .   ? 14.181  -10.511 24.922  1.00 23.93  ? 845 HOH B O    1 
HETATM 10326 O  O    . HOH J 6 .   ? 31.775  -21.916 -0.545  1.00 47.98  ? 846 HOH B O    1 
HETATM 10327 O  O    . HOH J 6 .   ? 44.497  -30.415 9.871   1.00 34.47  ? 847 HOH B O    1 
HETATM 10328 O  O    . HOH J 6 .   ? 26.312  -5.411  14.868  1.00 35.22  ? 848 HOH B O    1 
HETATM 10329 O  O    . HOH J 6 .   ? 23.915  -17.804 3.260   1.00 34.72  ? 849 HOH B O    1 
HETATM 10330 O  O    . HOH J 6 .   ? 27.213  -54.438 29.863  1.00 38.39  ? 850 HOH B O    1 
HETATM 10331 O  O    . HOH J 6 .   ? 13.807  -24.387 29.862  1.00 37.59  ? 851 HOH B O    1 
HETATM 10332 O  O    . HOH J 6 .   ? 17.231  -24.849 40.173  1.00 43.93  ? 852 HOH B O    1 
HETATM 10333 O  O    . HOH J 6 .   ? 35.682  -42.169 31.789  1.00 23.76  ? 853 HOH B O    1 
HETATM 10334 O  O    . HOH J 6 .   ? 19.739  -38.469 34.855  1.00 40.27  ? 854 HOH B O    1 
HETATM 10335 O  O    . HOH J 6 .   ? 11.113  -54.170 27.606  1.00 39.42  ? 855 HOH B O    1 
HETATM 10336 O  O    . HOH J 6 .   ? 28.916  -40.883 32.469  1.00 35.81  ? 856 HOH B O    1 
HETATM 10337 O  O    . HOH J 6 .   ? 23.418  -45.926 -0.709  1.00 30.00  ? 857 HOH B O    1 
HETATM 10338 O  O    . HOH J 6 .   ? 21.912  -50.514 26.681  1.00 31.12  ? 858 HOH B O    1 
HETATM 10339 O  O    . HOH J 6 .   ? 18.348  -43.111 32.786  1.00 42.86  ? 859 HOH B O    1 
HETATM 10340 O  O    . HOH J 6 .   ? 17.275  -52.291 29.360  1.00 42.96  ? 860 HOH B O    1 
HETATM 10341 O  O    . HOH J 6 .   ? 24.478  -43.508 31.691  1.00 34.96  ? 861 HOH B O    1 
HETATM 10342 O  O    . HOH J 6 .   ? 32.217  -17.474 17.652  1.00 31.66  ? 862 HOH B O    1 
HETATM 10343 O  O    . HOH J 6 .   ? 10.802  -27.712 24.161  1.00 24.99  ? 863 HOH B O    1 
HETATM 10344 O  O    . HOH J 6 .   ? 25.817  -57.520 27.528  1.00 36.21  ? 864 HOH B O    1 
HETATM 10345 O  O    . HOH J 6 .   ? 23.289  -50.848 30.910  1.00 48.83  ? 865 HOH B O    1 
HETATM 10346 O  O    . HOH J 6 .   ? 7.836   -41.824 30.919  1.00 45.68  ? 866 HOH B O    1 
HETATM 10347 O  O    . HOH J 6 .   ? 19.799  -25.117 -4.342  1.00 35.25  ? 867 HOH B O    1 
HETATM 10348 O  O    . HOH J 6 .   ? 23.157  -2.559  12.887  1.00 41.07  ? 868 HOH B O    1 
HETATM 10349 O  O    . HOH J 6 .   ? 17.544  -21.002 38.278  1.00 44.69  ? 869 HOH B O    1 
HETATM 10350 O  O    . HOH J 6 .   ? 31.504  -51.859 30.870  1.00 36.27  ? 870 HOH B O    1 
HETATM 10351 O  O    . HOH J 6 .   ? 33.923  -56.978 26.954  1.00 32.38  ? 871 HOH B O    1 
HETATM 10352 O  O    . HOH J 6 .   ? 38.152  -44.320 20.264  1.00 27.40  ? 872 HOH B O    1 
HETATM 10353 O  O    . HOH J 6 .   ? 10.087  -27.081 4.076   1.00 43.59  ? 873 HOH B O    1 
HETATM 10354 O  O    . HOH J 6 .   ? 5.230   -43.496 27.933  1.00 40.16  ? 874 HOH B O    1 
HETATM 10355 O  O    . HOH J 6 .   ? 34.281  -50.158 21.339  1.00 28.50  ? 875 HOH B O    1 
HETATM 10356 O  O    . HOH J 6 .   ? 39.077  -45.156 13.873  1.00 41.88  ? 876 HOH B O    1 
HETATM 10357 O  O    . HOH J 6 .   ? 9.280   -29.547 29.146  1.00 40.31  ? 877 HOH B O    1 
HETATM 10358 O  O    . HOH J 6 .   ? 20.870  -59.490 24.376  1.00 42.27  ? 878 HOH B O    1 
HETATM 10359 O  O    . HOH J 6 .   ? 20.961  -4.111  20.959  1.00 32.95  ? 879 HOH B O    1 
HETATM 10360 O  O    . HOH J 6 .   ? 37.188  -21.899 2.030   1.00 56.80  ? 880 HOH B O    1 
HETATM 10361 O  O    . HOH J 6 .   ? 37.558  -41.065 27.859  1.00 27.85  ? 881 HOH B O    1 
HETATM 10362 O  O    . HOH J 6 .   ? 30.393  -59.461 13.898  1.00 42.28  ? 882 HOH B O    1 
HETATM 10363 O  O    . HOH J 6 .   ? 28.004  -26.281 -5.112  1.00 46.48  ? 883 HOH B O    1 
HETATM 10364 O  O    . HOH J 6 .   ? 25.772  -4.245  26.674  1.00 44.58  ? 884 HOH B O    1 
HETATM 10365 O  O    . HOH J 6 .   ? 26.494  -63.601 20.618  1.00 41.27  ? 885 HOH B O    1 
HETATM 10366 O  O    . HOH J 6 .   ? 39.515  -34.688 26.541  1.00 31.59  ? 886 HOH B O    1 
HETATM 10367 O  O    . HOH J 6 .   ? 23.616  -56.644 26.661  1.00 39.65  ? 887 HOH B O    1 
HETATM 10368 O  O    . HOH J 6 .   ? 19.388  -15.162 27.275  1.00 38.15  ? 888 HOH B O    1 
HETATM 10369 O  O    . HOH J 6 .   ? 9.967   -37.721 32.341  1.00 51.41  ? 889 HOH B O    1 
HETATM 10370 O  O    . HOH J 6 .   ? 6.903   -28.248 25.455  1.00 37.69  ? 890 HOH B O    1 
HETATM 10371 O  O    . HOH J 6 .   ? 24.371  -4.035  18.907  1.00 37.29  ? 891 HOH B O    1 
HETATM 10372 O  O    . HOH J 6 .   ? 17.778  -23.721 37.715  1.00 35.38  ? 892 HOH B O    1 
HETATM 10373 O  O    . HOH J 6 .   ? 42.460  -30.775 31.996  1.00 39.29  ? 893 HOH B O    1 
HETATM 10374 O  O    . HOH J 6 .   ? 10.964  -25.393 22.634  1.00 30.41  ? 894 HOH B O    1 
HETATM 10375 O  O    . HOH J 6 .   ? 19.911  -19.001 38.916  1.00 35.44  ? 895 HOH B O    1 
HETATM 10376 O  O    . HOH J 6 .   ? 35.921  -45.625 24.976  1.00 41.00  ? 896 HOH B O    1 
HETATM 10377 O  O    . HOH J 6 .   ? 34.316  -50.007 25.905  1.00 34.14  ? 897 HOH B O    1 
HETATM 10378 O  O    . HOH J 6 .   ? 41.175  -33.844 15.955  1.00 43.91  ? 898 HOH B O    1 
HETATM 10379 O  O    . HOH J 6 .   ? 35.782  -17.174 2.684   1.00 37.66  ? 899 HOH B O    1 
HETATM 10380 O  O    . HOH J 6 .   ? 5.739   -40.245 30.076  1.00 40.24  ? 900 HOH B O    1 
HETATM 10381 O  O    . HOH J 6 .   ? 18.281  -12.398 27.170  1.00 36.06  ? 901 HOH B O    1 
HETATM 10382 O  O    . HOH J 6 .   ? 26.101  -61.101 25.262  1.00 38.82  ? 902 HOH B O    1 
HETATM 10383 O  O    . HOH J 6 .   ? 22.065  -41.383 34.690  1.00 46.46  ? 903 HOH B O    1 
HETATM 10384 O  O    . HOH J 6 .   ? 26.877  -4.478  19.237  1.00 32.13  ? 904 HOH B O    1 
HETATM 10385 O  O    . HOH J 6 .   ? 31.445  -47.553 32.069  1.00 38.49  ? 905 HOH B O    1 
HETATM 10386 O  O    . HOH J 6 .   ? 5.756   -32.116 26.802  1.00 34.21  ? 906 HOH B O    1 
HETATM 10387 O  O    . HOH J 6 .   ? 25.030  -47.875 33.376  1.00 44.59  ? 907 HOH B O    1 
HETATM 10388 O  O    . HOH J 6 .   ? 26.157  -24.652 -5.163  1.00 48.90  ? 908 HOH B O    1 
HETATM 10389 O  O    . HOH J 6 .   ? 16.045  -35.302 35.024  1.00 40.74  ? 909 HOH B O    1 
HETATM 10390 O  O    . HOH J 6 .   ? 23.059  -54.738 28.463  1.00 35.87  ? 910 HOH B O    1 
HETATM 10391 O  O    . HOH J 6 .   ? 21.606  -52.216 28.421  1.00 37.13  ? 911 HOH B O    1 
HETATM 10392 O  O    . HOH J 6 .   ? 6.888   -32.810 29.173  1.00 33.06  ? 912 HOH B O    1 
HETATM 10393 O  O    . HOH J 6 .   ? 22.177  -43.855 34.523  1.00 39.64  ? 913 HOH B O    1 
HETATM 10394 O  O    . HOH J 6 .   ? 18.915  -41.158 34.797  1.00 49.26  ? 914 HOH B O    1 
HETATM 10395 O  O    . HOH J 6 .   ? 5.766   -29.767 26.735  1.00 45.51  ? 915 HOH B O    1 
HETATM 10396 O  O    . HOH J 6 .   ? 29.788  -62.843 27.109  1.00 39.04  ? 916 HOH B O    1 
HETATM 10397 O  O    . HOH J 6 .   ? 27.342  -63.710 25.770  1.00 40.69  ? 917 HOH B O    1 
HETATM 10398 O  O    . HOH J 6 .   ? 39.250  -40.210 30.084  1.00 30.66  ? 918 HOH B O    1 
HETATM 10399 O  O    . HOH J 6 .   ? 11.073  -25.093 29.571  1.00 46.70  ? 919 HOH B O    1 
HETATM 10400 O  O    . HOH J 6 .   ? 41.921  -34.491 24.895  1.00 47.90  ? 920 HOH B O    1 
HETATM 10401 O  O    . HOH J 6 .   ? 21.748  -56.828 30.146  1.00 51.01  ? 921 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 
95   N N   . ARG A 7   ? 0.7450 0.7549 0.7653 0.0156  -0.0733 0.0460  25  ARG A N   
96   C CA  . ARG A 7   ? 0.9900 1.0033 1.0172 0.0144  -0.0879 0.0484  25  ARG A CA  
97   C C   . ARG A 7   ? 0.7763 0.8047 0.8353 0.0090  -0.0989 0.0499  25  ARG A C   
98   O O   . ARG A 7   ? 0.7533 0.8022 0.8232 0.0102  -0.1187 0.0455  25  ARG A O   
119  N N   . LEU A 8   ? 0.5882 0.6090 0.6594 0.0017  -0.1036 0.0500  26  LEU A N   
120  C CA  . LEU A 8   ? 0.4170 0.4269 0.4970 0.0083  -0.1016 0.0540  26  LEU A CA  
121  C C   . LEU A 8   ? 0.3426 0.2942 0.4228 0.0259  -0.0420 0.0389  26  LEU A C   
122  O O   . LEU A 8   ? 0.2798 0.2645 0.4315 0.0140  -0.0031 0.0418  26  LEU A O   
123  C CB  . LEU A 8   ? 0.3697 0.3923 0.4445 -0.0127 -0.1093 0.0634  26  LEU A CB  
124  C CG  . LEU A 8   ? 0.3623 0.3810 0.3995 -0.0200 -0.1078 0.0630  26  LEU A CG  
125  C CD1 . LEU A 8   ? 0.3593 0.3845 0.3844 -0.0161 -0.1126 0.0678  26  LEU A CD1 
126  C CD2 . LEU A 8   ? 0.3356 0.3735 0.3867 -0.0063 -0.0944 0.0812  26  LEU A CD2 
138  N N   . PRO A 9   ? 0.3273 0.2284 0.3335 0.0187  -0.0489 0.0262  27  PRO A N   
139  C CA  . PRO A 9   ? 0.3490 0.2102 0.3169 -0.0102 -0.0288 0.0126  27  PRO A CA  
140  C C   . PRO A 9   ? 0.3455 0.1916 0.3020 -0.0143 -0.0483 0.0085  27  PRO A C   
141  O O   . PRO A 9   ? 0.3591 0.1614 0.2782 -0.0323 -0.0636 0.0138  27  PRO A O   
142  C CB  . PRO A 9   ? 0.3543 0.2061 0.2929 0.0006  -0.0320 -0.0028 27  PRO A CB  
143  C CG  . PRO A 9   ? 0.3440 0.2065 0.2946 0.0064  -0.0464 0.0161  27  PRO A CG  
144  C CD  . PRO A 9   ? 0.3403 0.2300 0.3166 0.0224  -0.0408 0.0222  27  PRO A CD  
152  N N   . SER A 10  ? 0.3744 0.2229 0.3049 0.0034  -0.0359 -0.0077 28  SER A N   
153  C CA  . SER A 10  ? 0.3925 0.2565 0.3396 0.0126  -0.0380 -0.0201 28  SER A CA  
154  C C   . SER A 10  ? 0.4288 0.2684 0.3376 0.0092  -0.0288 -0.0268 28  SER A C   
155  O O   . SER A 10  ? 0.4568 0.2779 0.3474 0.0162  -0.0082 -0.0151 28  SER A O   
156  C CB  . SER A 10  ? 0.4046 0.2879 0.3836 0.0138  -0.0358 -0.0268 28  SER A CB  
157  O OG  . SER A 10  ? 0.4269 0.3077 0.4113 0.0243  -0.0160 -0.0388 28  SER A OG  
163  N N   . GLY A 11  ? 0.4386 0.2785 0.3366 0.0040  -0.0365 -0.0446 29  GLY A N   
164  C CA  . GLY A 11  ? 0.4450 0.2883 0.3350 0.0232  -0.0580 -0.0534 29  GLY A CA  
165  C C   . GLY A 11  ? 0.4422 0.2865 0.3381 0.0357  -0.0670 -0.0591 29  GLY A C   
166  O O   . GLY A 11  ? 0.4715 0.2943 0.3506 0.0244  -0.0754 -0.0444 29  GLY A O   
170  N N   . SER A 12  ? 0.4372 0.2785 0.3454 0.0242  -0.0560 -0.0781 30  SER A N   
171  C CA  A SER A 12  ? 0.4379 0.2785 0.3397 0.0213  -0.0519 -0.0832 30  SER A CA  
172  C CA  B SER A 12  ? 0.4295 0.2726 0.3453 0.0231  -0.0564 -0.0765 30  SER A CA  
173  C C   . SER A 12  ? 0.4092 0.2549 0.3352 0.0211  -0.0524 -0.0752 30  SER A C   
174  O O   . SER A 12  ? 0.3964 0.2630 0.3302 0.0494  -0.0580 -0.0799 30  SER A O   
175  C CB  A SER A 12  ? 0.4660 0.3018 0.3338 0.0201  -0.0398 -0.0976 30  SER A CB  
176  C CB  B SER A 12  ? 0.4414 0.2842 0.3523 0.0244  -0.0544 -0.0773 30  SER A CB  
177  O OG  A SER A 12  ? 0.4860 0.3181 0.3324 0.0349  -0.0192 -0.0995 30  SER A OG  
178  O OG  B SER A 12  ? 0.4462 0.2904 0.3616 0.0368  -0.0483 -0.0682 30  SER A OG  
187  N N   . ASP A 13  ? 0.3722 0.2304 0.3232 0.0153  -0.0599 -0.0606 31  ASP A N   
188  C CA  . ASP A 13  ? 0.3340 0.1884 0.3084 0.0061  -0.0884 -0.0466 31  ASP A CA  
189  C C   . ASP A 13  ? 0.3332 0.1854 0.3061 0.0017  -0.0984 -0.0303 31  ASP A C   
190  O O   . ASP A 13  ? 0.3633 0.2075 0.3123 -0.0084 -0.0867 -0.0222 31  ASP A O   
191  C CB  . ASP A 13  ? 0.3636 0.1758 0.3348 0.0193  -0.0813 -0.0456 31  ASP A CB  
192  C CG  . ASP A 13  ? 0.3739 0.1652 0.3467 0.0187  -0.0861 -0.0332 31  ASP A CG  
193  O OD1 . ASP A 13  ? 0.4018 0.1659 0.3288 0.0204  -0.1204 -0.0365 31  ASP A OD1 
194  O OD2 . ASP A 13  ? 0.4120 0.1779 0.3858 0.0125  -0.0325 -0.0442 31  ASP A OD2 
199  N N   . PRO A 14  ? 0.3304 0.1694 0.3150 -0.0262 -0.0998 -0.0267 32  PRO A N   
200  C CA  . PRO A 14  ? 0.3459 0.1726 0.3173 -0.0326 -0.1163 -0.0213 32  PRO A CA  
201  C C   . PRO A 14  ? 0.3446 0.1707 0.3211 -0.0271 -0.1168 -0.0260 32  PRO A C   
202  O O   . PRO A 14  ? 0.3515 0.1621 0.2979 -0.0125 -0.1272 -0.0382 32  PRO A O   
203  C CB  . PRO A 14  ? 0.3712 0.1848 0.3154 -0.0312 -0.1162 -0.0071 32  PRO A CB  
204  C CG  . PRO A 14  ? 0.3782 0.1622 0.3068 -0.0482 -0.1123 -0.0232 32  PRO A CG  
205  C CD  . PRO A 14  ? 0.3346 0.1607 0.3043 -0.0391 -0.1190 -0.0158 32  PRO A CD  
213  N N   . ALA A 15  ? 0.3390 0.2009 0.3181 -0.0277 -0.1396 -0.0353 33  ALA A N   
214  C CA  . ALA A 15  ? 0.3564 0.2132 0.3261 -0.0416 -0.1357 -0.0436 33  ALA A CA  
215  C C   . ALA A 15  ? 0.3576 0.2287 0.3325 -0.0229 -0.1454 -0.0044 33  ALA A C   
216  O O   . ALA A 15  ? 0.3837 0.2723 0.3280 -0.0139 -0.1291 -0.0058 33  ALA A O   
217  C CB  . ALA A 15  ? 0.3823 0.2348 0.3431 -0.0498 -0.1043 -0.0601 33  ALA A CB  
223  N N   . PHE A 16  ? 0.3630 0.1904 0.3501 -0.0153 -0.1293 -0.0030 34  PHE A N   
224  C CA  . PHE A 16  ? 0.3362 0.1816 0.3516 -0.0152 -0.1654 0.0134  34  PHE A CA  
225  C C   . PHE A 16  ? 0.3352 0.1992 0.3672 -0.0448 -0.1582 -0.0026 34  PHE A C   
226  O O   . PHE A 16  ? 0.3783 0.2336 0.3642 -0.0546 -0.1538 0.0081  34  PHE A O   
227  C CB  . PHE A 16  ? 0.3716 0.1721 0.3631 0.0022  -0.1397 0.0242  34  PHE A CB  
228  C CG  . PHE A 16  ? 0.3792 0.1829 0.3431 -0.0193 -0.1318 -0.0025 34  PHE A CG  
229  C CD1 . PHE A 16  ? 0.3944 0.1827 0.3249 -0.0346 -0.1193 -0.0161 34  PHE A CD1 
230  C CD2 . PHE A 16  ? 0.3805 0.1780 0.3372 -0.0229 -0.1339 -0.0018 34  PHE A CD2 
231  C CE1 . PHE A 16  ? 0.4119 0.1850 0.3121 -0.0075 -0.1044 0.0093  34  PHE A CE1 
232  C CE2 . PHE A 16  ? 0.3879 0.1610 0.3340 0.0082  -0.1279 0.0089  34  PHE A CE2 
233  C CZ  . PHE A 16  ? 0.4080 0.1752 0.3124 0.0019  -0.1307 -0.0045 34  PHE A CZ  
243  N N   . SER A 17  ? 0.2909 0.1793 0.3798 -0.0343 -0.1555 -0.0059 35  SER A N   
244  C CA  . SER A 17  ? 0.2825 0.1800 0.3919 -0.0408 -0.1435 -0.0157 35  SER A CA  
245  C C   . SER A 17  ? 0.2932 0.2026 0.4122 -0.0649 -0.1608 -0.0088 35  SER A C   
246  O O   . SER A 17  ? 0.3089 0.2073 0.4564 -0.0826 -0.1411 -0.0128 35  SER A O   
247  C CB  . SER A 17  ? 0.2738 0.1752 0.3641 -0.0077 -0.1185 -0.0040 35  SER A CB  
248  O OG  . SER A 17  ? 0.3135 0.1712 0.3441 -0.0208 -0.1053 -0.0378 35  SER A OG  
254  N N   . GLN A 18  ? 0.2995 0.1920 0.4490 -0.0621 -0.1727 0.0133  36  GLN A N   
255  C CA  . GLN A 18  ? 0.3359 0.2008 0.4792 -0.0348 -0.1554 0.0144  36  GLN A CA  
256  C C   . GLN A 18  ? 0.3593 0.2177 0.4739 -0.0320 -0.2014 0.0010  36  GLN A C   
257  O O   . GLN A 18  ? 0.4085 0.2409 0.4405 -0.0049 -0.2261 0.0131  36  GLN A O   
258  C CB  . GLN A 18  ? 0.3503 0.2180 0.4926 -0.0297 -0.1408 0.0229  36  GLN A CB  
259  C CG  . GLN A 18  ? 0.4230 0.2434 0.5168 -0.0511 -0.0764 0.0151  36  GLN A CG  
260  C CD  . GLN A 18  ? 0.5055 0.2826 0.5477 -0.0902 -0.0553 -0.0004 36  GLN A CD  
261  O OE1 . GLN A 18  ? 0.5749 0.3312 0.5678 -0.0866 -0.0299 0.0008  36  GLN A OE1 
262  N NE2 . GLN A 18  ? 0.5120 0.2751 0.5485 -0.1057 -0.0501 -0.0086 36  GLN A NE2 
271  N N   . PRO A 19  ? 0.3992 0.2289 0.5197 -0.0352 -0.1879 0.0047  37  PRO A N   
272  C CA  . PRO A 19  ? 0.3858 0.2354 0.5256 -0.0374 -0.2246 -0.0084 37  PRO A CA  
273  C C   . PRO A 19  ? 0.3962 0.2148 0.5161 0.0011  -0.2419 -0.0198 37  PRO A C   
274  O O   . PRO A 19  ? 0.3777 0.2078 0.5233 0.0104  -0.2395 -0.0407 37  PRO A O   
275  C CB  . PRO A 19  ? 0.3780 0.2482 0.5585 -0.0486 -0.1947 0.0070  37  PRO A CB  
276  C CG  . PRO A 19  ? 0.4104 0.2647 0.5680 -0.0439 -0.1639 0.0217  37  PRO A CG  
277  C CD  . PRO A 19  ? 0.3940 0.2510 0.5564 -0.0446 -0.1669 0.0172  37  PRO A CD  
285  N N   . LYS A 20  ? 0.4218 0.2081 0.5111 0.0239  -0.2511 -0.0193 38  LYS A N   
286  C CA  . LYS A 20  ? 0.4571 0.2041 0.4847 0.0427  -0.2585 -0.0202 38  LYS A CA  
287  C C   . LYS A 20  ? 0.4366 0.2072 0.4882 0.0265  -0.2576 -0.0300 38  LYS A C   
288  O O   . LYS A 20  ? 0.4382 0.1980 0.4822 0.0247  -0.2485 -0.0565 38  LYS A O   
289  C CB  . LYS A 20  ? 0.5283 0.2227 0.4878 0.0498  -0.2146 -0.0019 38  LYS A CB  
290  C CG  . LYS A 20  ? 0.5662 0.2453 0.4730 0.0389  -0.2022 0.0120  38  LYS A CG  
291  C CD  . LYS A 20  ? 0.5880 0.2581 0.4833 0.0544  -0.1735 0.0123  38  LYS A CD  
292  C CE  . LYS A 20  ? 0.6102 0.2749 0.4988 0.0454  -0.1413 0.0019  38  LYS A CE  
293  N NZ  . LYS A 20  ? 0.6281 0.3000 0.5133 0.0389  -0.1251 -0.0028 38  LYS A NZ  
307  N N   . SER A 21  ? 0.4052 0.1998 0.4766 -0.0011 -0.2614 -0.0057 39  SER A N   
308  C CA  . SER A 21  ? 0.3762 0.1962 0.4832 -0.0266 -0.2497 0.0212  39  SER A CA  
309  C C   . SER A 21  ? 0.3609 0.1875 0.4781 -0.0416 -0.2343 0.0314  39  SER A C   
310  O O   . SER A 21  ? 0.3583 0.1952 0.4745 -0.0461 -0.2342 0.0360  39  SER A O   
311  C CB  . SER A 21  ? 0.3952 0.2224 0.5083 -0.0218 -0.2635 0.0369  39  SER A CB  
312  O OG  . SER A 21  ? 0.4443 0.2519 0.5501 -0.0420 -0.2622 0.0403  39  SER A OG  
318  N N   . VAL A 22  ? 0.3476 0.1979 0.4845 -0.0442 -0.2329 0.0369  40  VAL A N   
319  C CA  . VAL A 22  ? 0.3404 0.1769 0.4676 -0.0548 -0.2060 0.0472  40  VAL A CA  
320  C C   . VAL A 22  ? 0.2936 0.1720 0.4523 -0.0392 -0.1822 0.0383  40  VAL A C   
321  O O   . VAL A 22  ? 0.2497 0.1853 0.4711 -0.0330 -0.1579 0.0351  40  VAL A O   
322  C CB  . VAL A 22  ? 0.3633 0.1844 0.4682 -0.0695 -0.1986 0.0553  40  VAL A CB  
323  C CG1 . VAL A 22  ? 0.3845 0.1799 0.4584 -0.0689 -0.1909 0.0633  40  VAL A CG1 
324  C CG2 . VAL A 22  ? 0.3698 0.1939 0.4850 -0.0878 -0.1686 0.0613  40  VAL A CG2 
334  N N   . LEU A 23  ? 0.3012 0.1500 0.4116 -0.0043 -0.1744 0.0407  41  LEU A N   
335  C CA  . LEU A 23  ? 0.2805 0.1443 0.3876 -0.0012 -0.1654 0.0330  41  LEU A CA  
336  C C   . LEU A 23  ? 0.2729 0.1274 0.3406 -0.0199 -0.1723 0.0313  41  LEU A C   
337  O O   . LEU A 23  ? 0.2814 0.1270 0.3294 -0.0170 -0.1622 0.0167  41  LEU A O   
338  C CB  . LEU A 23  ? 0.2910 0.1521 0.3929 0.0086  -0.1470 0.0242  41  LEU A CB  
339  C CG  . LEU A 23  ? 0.2887 0.1603 0.3838 0.0069  -0.1600 0.0248  41  LEU A CG  
340  C CD1 . LEU A 23  ? 0.3257 0.1584 0.3861 0.0132  -0.1496 0.0251  41  LEU A CD1 
341  C CD2 . LEU A 23  ? 0.2539 0.1646 0.3789 -0.0114 -0.1763 0.0275  41  LEU A CD2 
353  N N   . ASP A 24  ? 0.2903 0.1468 0.3292 0.0046  -0.1604 0.0374  42  ASP A N   
354  C CA  . ASP A 24  ? 0.3093 0.1811 0.3338 0.0244  -0.1620 0.0417  42  ASP A CA  
355  C C   . ASP A 24  ? 0.2774 0.1840 0.3467 -0.0017 -0.1531 0.0439  42  ASP A C   
356  O O   . ASP A 24  ? 0.2812 0.1983 0.3398 -0.0219 -0.1507 0.0158  42  ASP A O   
357  C CB  . ASP A 24  ? 0.3176 0.2176 0.3266 0.0347  -0.1792 0.0219  42  ASP A CB  
358  C CG  . ASP A 24  ? 0.3430 0.2409 0.3317 0.0470  -0.1912 0.0063  42  ASP A CG  
359  O OD1 . ASP A 24  ? 0.3506 0.2550 0.3302 0.0501  -0.1850 0.0077  42  ASP A OD1 
360  O OD2 . ASP A 24  ? 0.3811 0.2517 0.3447 0.0389  -0.2129 -0.0074 42  ASP A OD2 
365  N N   . ALA A 25  ? 0.2578 0.2033 0.3477 -0.0196 -0.1535 0.0467  43  ALA A N   
366  C CA  . ALA A 25  ? 0.2497 0.2082 0.3617 -0.0470 -0.1308 0.0379  43  ALA A CA  
367  C C   . ALA A 25  ? 0.2501 0.2008 0.3484 -0.0259 -0.1157 0.0377  43  ALA A C   
368  O O   . ALA A 25  ? 0.2675 0.2424 0.3799 -0.0146 -0.0834 0.0215  43  ALA A O   
369  C CB  . ALA A 25  ? 0.2552 0.2187 0.3790 -0.0415 -0.1353 0.0243  43  ALA A CB  
375  N N   . GLY A 26  ? 0.2353 0.1766 0.3222 -0.0338 -0.1250 0.0477  44  GLY A N   
376  C CA  . GLY A 26  ? 0.2429 0.1511 0.2906 -0.0401 -0.1365 0.0426  44  GLY A CA  
377  C C   . GLY A 26  ? 0.2061 0.1327 0.2775 -0.0210 -0.1368 0.0410  44  GLY A C   
378  O O   . GLY A 26  ? 0.2266 0.1426 0.2704 -0.0213 -0.1183 0.0449  44  GLY A O   
382  N N   . LEU A 27  ? 0.2276 0.1133 0.2820 -0.0122 -0.1055 0.0399  45  LEU A N   
383  C CA  . LEU A 27  ? 0.2156 0.1233 0.2995 -0.0046 -0.0879 0.0398  45  LEU A CA  
384  C C   . LEU A 27  ? 0.2214 0.1289 0.3211 -0.0058 -0.0959 0.0297  45  LEU A C   
385  O O   . LEU A 27  ? 0.2506 0.1434 0.3523 0.0197  -0.1224 0.0280  45  LEU A O   
386  C CB  . LEU A 27  ? 0.2310 0.1396 0.2998 -0.0052 -0.0924 0.0197  45  LEU A CB  
387  C CG  . LEU A 27  ? 0.2626 0.1525 0.2777 -0.0268 -0.1142 0.0099  45  LEU A CG  
388  C CD1 . LEU A 27  ? 0.2611 0.1514 0.3045 -0.0302 -0.0863 0.0100  45  LEU A CD1 
389  C CD2 . LEU A 27  ? 0.3017 0.1686 0.2735 -0.0229 -0.1207 0.0179  45  LEU A CD2 
401  N N   . THR A 28  ? 0.2212 0.1122 0.2910 -0.0228 -0.1130 0.0359  46  THR A N   
402  C CA  . THR A 28  ? 0.2225 0.1137 0.3072 0.0030  -0.1019 0.0408  46  THR A CA  
403  C C   . THR A 28  ? 0.2440 0.1176 0.2998 -0.0047 -0.1045 0.0217  46  THR A C   
404  O O   . THR A 28  ? 0.2447 0.1230 0.3021 -0.0080 -0.1093 0.0097  46  THR A O   
405  C CB  . THR A 28  ? 0.2505 0.1328 0.3402 0.0137  -0.0627 0.0376  46  THR A CB  
406  O OG1 . THR A 28  ? 0.2464 0.1625 0.3701 0.0043  -0.0470 0.0230  46  THR A OG1 
407  C CG2 . THR A 28  ? 0.2648 0.1499 0.3464 0.0152  -0.0535 0.0479  46  THR A CG2 
415  N N   . CYS A 29  ? 0.2412 0.1067 0.3025 -0.0187 -0.1051 0.0185  47  CYS A N   
416  C CA  . CYS A 29  ? 0.2452 0.1226 0.2858 0.0065  -0.1047 0.0377  47  CYS A CA  
417  C C   . CYS A 29  ? 0.2458 0.1339 0.2970 0.0029  -0.1106 0.0212  47  CYS A C   
418  O O   . CYS A 29  ? 0.2543 0.1583 0.3235 0.0122  -0.1055 0.0233  47  CYS A O   
419  C CB  . CYS A 29  ? 0.2452 0.1220 0.2912 0.0069  -0.0832 0.0511  47  CYS A CB  
420  S SG  . CYS A 29  ? 0.2780 0.1484 0.2770 0.0127  -0.0973 0.0200  47  CYS A SG  
425  N N   . GLN A 30  ? 0.2503 0.1366 0.2845 0.0195  -0.0982 0.0072  48  GLN A N   
426  C CA  . GLN A 30  ? 0.2612 0.1316 0.2849 0.0425  -0.1165 0.0185  48  GLN A CA  
427  C C   . GLN A 30  ? 0.3066 0.1638 0.3085 0.0483  -0.1154 0.0269  48  GLN A C   
428  O O   . GLN A 30  ? 0.3105 0.1706 0.3294 0.0319  -0.1128 0.0164  48  GLN A O   
429  C CB  . GLN A 30  ? 0.2877 0.1269 0.3120 0.0424  -0.1242 -0.0093 48  GLN A CB  
430  C CG  . GLN A 30  ? 0.3101 0.1528 0.3274 0.0415  -0.1270 -0.0323 48  GLN A CG  
431  C CD  . GLN A 30  ? 0.3155 0.1547 0.3378 0.0380  -0.1163 -0.0312 48  GLN A CD  
432  O OE1 . GLN A 30  ? 0.3621 0.1693 0.3359 0.0264  -0.1092 -0.0187 48  GLN A OE1 
433  N NE2 . GLN A 30  ? 0.2833 0.1480 0.3557 0.0374  -0.0963 -0.0296 48  GLN A NE2 
442  N N   . GLY A 31  ? 0.3128 0.1848 0.3072 0.0513  -0.1358 0.0252  49  GLY A N   
443  C CA  . GLY A 31  ? 0.3563 0.1859 0.3148 0.0690  -0.1128 0.0409  49  GLY A CA  
444  C C   . GLY A 31  ? 0.3674 0.2011 0.3176 0.0567  -0.1330 0.0501  49  GLY A C   
445  O O   . GLY A 31  ? 0.4301 0.2249 0.3231 0.0411  -0.1221 0.0680  49  GLY A O   
449  N N   . ALA A 32  ? 0.3219 0.2012 0.2999 0.0574  -0.1438 0.0153  50  ALA A N   
450  C CA  . ALA A 32  ? 0.3143 0.1964 0.3151 0.0260  -0.1238 0.0251  50  ALA A CA  
451  C C   . ALA A 32  ? 0.3004 0.1967 0.3065 0.0169  -0.1321 0.0226  50  ALA A C   
452  O O   . ALA A 32  ? 0.3249 0.2066 0.3093 0.0313  -0.1148 0.0162  50  ALA A O   
453  C CB  . ALA A 32  ? 0.3194 0.2090 0.3292 0.0289  -0.1281 0.0327  50  ALA A CB  
459  N N   . SER A 33  ? 0.2825 0.2169 0.3082 0.0197  -0.1374 0.0295  51  SER A N   
460  C CA  . SER A 33  ? 0.3106 0.2266 0.2936 -0.0160 -0.1435 0.0181  51  SER A CA  
461  C C   . SER A 33  ? 0.3123 0.2215 0.2685 -0.0073 -0.1399 0.0235  51  SER A C   
462  O O   . SER A 33  ? 0.3160 0.2344 0.2658 0.0118  -0.1272 0.0274  51  SER A O   
463  C CB  . SER A 33  ? 0.3533 0.2466 0.3269 -0.0238 -0.1504 0.0139  51  SER A CB  
464  O OG  . SER A 33  ? 0.3865 0.2948 0.3617 -0.0158 -0.1328 0.0296  51  SER A OG  
470  N N   . PRO A 34  ? 0.3001 0.2043 0.2606 -0.0009 -0.1286 0.0317  52  PRO A N   
471  C CA  . PRO A 34  ? 0.2870 0.2023 0.2651 -0.0020 -0.1240 0.0286  52  PRO A CA  
472  C C   . PRO A 34  ? 0.2969 0.2278 0.2734 -0.0048 -0.1257 0.0205  52  PRO A C   
473  O O   . PRO A 34  ? 0.3020 0.2498 0.2747 -0.0098 -0.1003 0.0279  52  PRO A O   
474  C CB  . PRO A 34  ? 0.3192 0.1847 0.2847 -0.0194 -0.0868 0.0112  52  PRO A CB  
475  C CG  . PRO A 34  ? 0.3134 0.1935 0.2857 -0.0141 -0.0862 0.0360  52  PRO A CG  
476  C CD  . PRO A 34  ? 0.2863 0.1960 0.2741 0.0053  -0.0991 0.0502  52  PRO A CD  
484  N N   . SER A 35  ? 0.3129 0.2365 0.2654 -0.0128 -0.1561 -0.0033 53  SER A N   
485  C CA  A SER A 35  ? 0.3441 0.2537 0.2783 -0.0037 -0.1304 0.0084  53  SER A CA  
486  C CA  B SER A 35  ? 0.3453 0.2407 0.2765 0.0014  -0.1396 0.0161  53  SER A CA  
487  C C   . SER A 35  ? 0.3413 0.2529 0.2841 0.0131  -0.1415 0.0249  53  SER A C   
488  O O   . SER A 35  ? 0.3224 0.2718 0.3001 0.0143  -0.1349 0.0079  53  SER A O   
489  C CB  A SER A 35  ? 0.3448 0.2705 0.2717 -0.0153 -0.1371 -0.0108 53  SER A CB  
490  C CB  B SER A 35  ? 0.3663 0.2324 0.2744 0.0016  -0.1410 0.0197  53  SER A CB  
491  O OG  A SER A 35  ? 0.3415 0.2871 0.2602 -0.0086 -0.1362 -0.0035 53  SER A OG  
492  O OG  B SER A 35  ? 0.3845 0.2231 0.2689 0.0083  -0.1406 0.0371  53  SER A OG  
503  N N   . SER A 36  ? 0.3361 0.2475 0.2780 0.0272  -0.1600 0.0541  54  SER A N   
504  C CA  . SER A 36  ? 0.3585 0.2496 0.2978 0.0428  -0.1536 0.0480  54  SER A CA  
505  C C   . SER A 36  ? 0.3647 0.2330 0.2926 0.0334  -0.1353 0.0255  54  SER A C   
506  O O   . SER A 36  ? 0.4014 0.2544 0.3132 0.0403  -0.1099 0.0207  54  SER A O   
507  C CB  . SER A 36  ? 0.4119 0.2768 0.3287 0.0311  -0.1369 0.0499  54  SER A CB  
508  O OG  . SER A 36  ? 0.4681 0.2767 0.3412 0.0274  -0.1039 0.0387  54  SER A OG  
514  N N   . VAL A 37  ? 0.3605 0.2174 0.2821 0.0417  -0.1399 0.0166  55  VAL A N   
515  C CA  . VAL A 37  ? 0.3214 0.2117 0.2704 0.0229  -0.1542 0.0119  55  VAL A CA  
516  C C   . VAL A 37  ? 0.3510 0.2136 0.3094 0.0267  -0.1493 0.0177  55  VAL A C   
517  O O   . VAL A 37  ? 0.3578 0.2261 0.3274 0.0166  -0.1250 0.0342  55  VAL A O   
518  C CB  . VAL A 37  ? 0.3242 0.2076 0.2600 -0.0020 -0.0957 0.0195  55  VAL A CB  
519  C CG1 . VAL A 37  ? 0.2835 0.2185 0.2596 -0.0250 -0.0861 0.0140  55  VAL A CG1 
520  C CG2 . VAL A 37  ? 0.3524 0.2245 0.2560 0.0234  -0.0568 0.0109  55  VAL A CG2 
530  N N   . SER A 38  ? 0.3573 0.2089 0.3332 0.0365  -0.1532 0.0218  56  SER A N   
531  C CA  . SER A 38  ? 0.3866 0.2015 0.3406 0.0229  -0.1526 0.0326  56  SER A CA  
532  C C   . SER A 38  ? 0.3557 0.1867 0.3149 0.0199  -0.1182 0.0510  56  SER A C   
533  O O   . SER A 38  ? 0.3441 0.2044 0.3407 0.0226  -0.1072 0.0347  56  SER A O   
534  C CB  . SER A 38  ? 0.4519 0.2205 0.3889 -0.0007 -0.1539 0.0290  56  SER A CB  
535  O OG  . SER A 38  ? 0.5360 0.2687 0.4295 -0.0024 -0.1358 0.0381  56  SER A OG  
541  N N   . LYS A 39  ? 0.3400 0.1561 0.2868 0.0174  -0.0938 0.0586  57  LYS A N   
542  C CA  . LYS A 39  ? 0.3285 0.1648 0.2841 -0.0128 -0.0642 0.0273  57  LYS A CA  
543  C C   . LYS A 39  ? 0.3008 0.1677 0.2538 0.0026  -0.0769 0.0189  57  LYS A C   
544  O O   . LYS A 39  ? 0.2781 0.1941 0.2580 0.0095  -0.0854 0.0303  57  LYS A O   
545  C CB  . LYS A 39  ? 0.3833 0.1742 0.3442 -0.0344 -0.0271 0.0300  57  LYS A CB  
546  C CG  . LYS A 39  ? 0.4698 0.2274 0.4109 -0.0525 0.0009  -0.0049 57  LYS A CG  
547  C CD  . LYS A 39  ? 0.4955 0.2427 0.4627 -0.0826 0.0294  0.0066  57  LYS A CD  
548  C CE  . LYS A 39  ? 0.5136 0.2621 0.4942 -0.0895 0.0436  0.0043  57  LYS A CE  
549  N NZ  . LYS A 39  ? 0.4962 0.2675 0.5114 -0.0894 0.0362  0.0110  57  LYS A NZ  
563  N N   . PRO A 40  ? 0.2944 0.1544 0.2190 0.0029  -0.1060 0.0428  58  PRO A N   
564  C CA  . PRO A 40  ? 0.2945 0.1463 0.2413 -0.0026 -0.0999 0.0414  58  PRO A CA  
565  C C   . PRO A 40  ? 0.2778 0.1437 0.2364 -0.0064 -0.0923 0.0342  58  PRO A C   
566  O O   . PRO A 40  ? 0.2774 0.1407 0.2380 -0.0148 -0.0700 0.0388  58  PRO A O   
567  C CB  . PRO A 40  ? 0.3135 0.1623 0.2504 -0.0084 -0.1009 0.0401  58  PRO A CB  
568  C CG  . PRO A 40  ? 0.3082 0.1602 0.2291 -0.0079 -0.1014 0.0306  58  PRO A CG  
569  C CD  . PRO A 40  ? 0.3005 0.1538 0.2187 -0.0011 -0.1027 0.0432  58  PRO A CD  
577  N N   . ILE A 41  ? 0.2669 0.1369 0.2272 -0.0078 -0.0855 0.0333  59  ILE A N   
578  C CA  . ILE A 41  ? 0.2484 0.1183 0.2285 0.0006  -0.0997 0.0288  59  ILE A CA  
579  C C   . ILE A 41  ? 0.2507 0.1168 0.2272 0.0066  -0.0798 0.0339  59  ILE A C   
580  O O   . ILE A 41  ? 0.2717 0.1233 0.2494 -0.0022 -0.0484 0.0398  59  ILE A O   
581  C CB  . ILE A 41  ? 0.2452 0.1163 0.2569 0.0131  -0.0884 0.0365  59  ILE A CB  
582  C CG1 . ILE A 41  ? 0.2378 0.1030 0.2677 -0.0200 -0.1072 0.0316  59  ILE A CG1 
583  C CG2 . ILE A 41  ? 0.2652 0.1322 0.2749 0.0110  -0.0712 0.0320  59  ILE A CG2 
584  C CD1 . ILE A 41  ? 0.2600 0.1079 0.2760 -0.0231 -0.0717 0.0257  59  ILE A CD1 
596  N N   . LEU A 42  ? 0.2337 0.1135 0.2160 0.0127  -0.0666 0.0243  60  LEU A N   
597  C CA  . LEU A 42  ? 0.2216 0.1107 0.2081 -0.0077 -0.0776 0.0282  60  LEU A CA  
598  C C   . LEU A 42  ? 0.2096 0.1235 0.2021 0.0003  -0.0691 0.0270  60  LEU A C   
599  O O   . LEU A 42  ? 0.2150 0.1421 0.2086 -0.0025 -0.0781 0.0065  60  LEU A O   
600  C CB  . LEU A 42  ? 0.2345 0.1190 0.2114 -0.0318 -0.0775 0.0395  60  LEU A CB  
601  C CG  . LEU A 42  ? 0.2472 0.1335 0.2190 -0.0093 -0.0876 0.0349  60  LEU A CG  
602  C CD1 . LEU A 42  ? 0.2789 0.1539 0.2194 -0.0129 -0.0963 0.0299  60  LEU A CD1 
603  C CD2 . LEU A 42  ? 0.2827 0.1227 0.2419 -0.0322 -0.0529 -0.0098 60  LEU A CD2 
615  N N   . LEU A 43  ? 0.2155 0.1189 0.2152 -0.0134 -0.0453 0.0225  61  LEU A N   
616  C CA  . LEU A 43  ? 0.2130 0.1112 0.2059 -0.0175 -0.0653 0.0263  61  LEU A CA  
617  C C   . LEU A 43  ? 0.2048 0.0952 0.2074 -0.0261 -0.0868 0.0260  61  LEU A C   
618  O O   . LEU A 43  ? 0.2194 0.1234 0.2445 -0.0259 -0.0708 0.0306  61  LEU A O   
619  C CB  . LEU A 43  ? 0.2356 0.1207 0.2128 -0.0340 -0.0571 0.0449  61  LEU A CB  
620  C CG  . LEU A 43  ? 0.2498 0.1278 0.2161 -0.0227 -0.0620 0.0483  61  LEU A CG  
621  C CD1 . LEU A 43  ? 0.2961 0.1624 0.2463 0.0088  -0.0597 0.0487  61  LEU A CD1 
622  C CD2 . LEU A 43  ? 0.2589 0.1379 0.2346 -0.0406 -0.0525 0.0482  61  LEU A CD2 
634  N N   . VAL A 44  ? 0.2109 0.0821 0.2070 0.0089  -0.0773 0.0083  62  VAL A N   
635  C CA  . VAL A 44  ? 0.1906 0.0883 0.2067 -0.0158 -0.0543 0.0184  62  VAL A CA  
636  C C   . VAL A 44  ? 0.1734 0.0948 0.2014 -0.0143 -0.0718 0.0261  62  VAL A C   
637  O O   . VAL A 44  ? 0.1791 0.1145 0.2129 -0.0176 -0.0822 0.0204  62  VAL A O   
638  C CB  . VAL A 44  ? 0.2185 0.0951 0.2079 -0.0006 -0.0393 0.0376  62  VAL A CB  
639  C CG1 . VAL A 44  ? 0.2154 0.1142 0.2164 -0.0097 -0.0651 0.0339  62  VAL A CG1 
640  C CG2 . VAL A 44  ? 0.2358 0.1095 0.2259 -0.0132 0.0106  0.0318  62  VAL A CG2 
650  N N   . PRO A 45  ? 0.2245 0.0994 0.1990 -0.0141 -0.0608 -0.0038 63  PRO A N   
651  C CA  . PRO A 45  ? 0.1893 0.0979 0.2159 -0.0222 -0.0662 0.0096  63  PRO A CA  
652  C C   . PRO A 45  ? 0.2053 0.1167 0.2364 -0.0124 -0.0400 0.0163  63  PRO A C   
653  O O   . PRO A 45  ? 0.1980 0.1221 0.2265 -0.0142 -0.0554 0.0381  63  PRO A O   
654  C CB  . PRO A 45  ? 0.1983 0.1050 0.2241 -0.0310 -0.0748 -0.0099 63  PRO A CB  
655  C CG  . PRO A 45  ? 0.2132 0.1256 0.2102 -0.0134 -0.0675 0.0227  63  PRO A CG  
656  C CD  . PRO A 45  ? 0.2290 0.1315 0.2186 -0.0115 -0.0589 -0.0024 63  PRO A CD  
664  N N   . GLY A 46  ? 0.2008 0.1101 0.2250 0.0113  -0.0581 0.0103  64  GLY A N   
665  C CA  . GLY A 46  ? 0.2046 0.1073 0.2212 -0.0039 -0.0658 0.0110  64  GLY A CA  
666  C C   . GLY A 46  ? 0.1842 0.1095 0.2419 0.0048  -0.0768 0.0191  64  GLY A C   
667  O O   . GLY A 46  ? 0.1811 0.1273 0.2733 0.0055  -0.0617 0.0211  64  GLY A O   
671  N N   . THR A 47  ? 0.2382 0.0968 0.2492 0.0397  -0.0463 0.0320  65  THR A N   
672  C CA  . THR A 47  ? 0.2546 0.1041 0.2393 0.0215  -0.0493 0.0270  65  THR A CA  
673  C C   . THR A 47  ? 0.2297 0.1195 0.2362 0.0052  -0.0760 0.0141  65  THR A C   
674  O O   . THR A 47  ? 0.2710 0.1238 0.2317 -0.0110 -0.0549 0.0065  65  THR A O   
675  C CB  . THR A 47  ? 0.2821 0.0968 0.2339 0.0314  -0.0430 0.0361  65  THR A CB  
676  O OG1 . THR A 47  ? 0.2904 0.0997 0.2834 0.0390  -0.0179 0.0387  65  THR A OG1 
677  C CG2 . THR A 47  ? 0.3209 0.1135 0.2467 0.0322  -0.0124 0.0426  65  THR A CG2 
685  N N   . GLY A 48  ? 0.2147 0.1210 0.2497 -0.0175 -0.0553 0.0089  66  GLY A N   
686  C CA  . GLY A 48  ? 0.2211 0.1225 0.2631 -0.0040 -0.0688 0.0202  66  GLY A CA  
687  C C   . GLY A 48  ? 0.2286 0.1210 0.2820 -0.0097 -0.0611 0.0102  66  GLY A C   
688  O O   . GLY A 48  ? 0.2590 0.1457 0.2999 -0.0046 -0.0673 0.0087  66  GLY A O   
692  N N   . THR A 49  ? 0.2314 0.1113 0.2879 -0.0070 -0.0389 0.0194  67  THR A N   
693  C CA  . THR A 49  ? 0.2193 0.0952 0.2726 0.0099  -0.0366 0.0306  67  THR A CA  
694  C C   . THR A 49  ? 0.2262 0.0937 0.2634 0.0023  -0.0301 0.0079  67  THR A C   
695  O O   . THR A 49  ? 0.2321 0.1131 0.2720 0.0048  -0.0363 0.0105  67  THR A O   
696  C CB  . THR A 49  ? 0.2313 0.1100 0.2927 -0.0009 -0.0245 0.0220  67  THR A CB  
697  O OG1 . THR A 49  ? 0.2232 0.1076 0.2934 -0.0309 -0.0518 0.0127  67  THR A OG1 
698  C CG2 . THR A 49  ? 0.2307 0.1349 0.2895 -0.0254 -0.0377 0.0190  67  THR A CG2 
706  N N   . THR A 50  ? 0.2118 0.0995 0.2603 0.0080  -0.0377 0.0152  68  THR A N   
707  C CA  . THR A 50  ? 0.1921 0.0967 0.2667 0.0036  -0.0391 0.0300  68  THR A CA  
708  C C   . THR A 50  ? 0.1728 0.1133 0.2848 -0.0149 -0.0504 0.0145  68  THR A C   
709  O O   . THR A 50  ? 0.1903 0.1392 0.2923 -0.0136 -0.0484 0.0178  68  THR A O   
710  C CB  . THR A 50  ? 0.2365 0.1072 0.2614 -0.0337 -0.0392 0.0281  68  THR A CB  
711  O OG1 . THR A 50  ? 0.2330 0.1267 0.2450 -0.0106 -0.0285 0.0228  68  THR A OG1 
712  C CG2 . THR A 50  ? 0.2692 0.1229 0.2911 -0.0056 -0.0481 0.0330  68  THR A CG2 
720  N N   . GLY A 51  ? 0.1960 0.1230 0.2780 -0.0027 -0.0655 0.0106  69  GLY A N   
721  C CA  . GLY A 51  ? 0.2069 0.1275 0.2632 0.0052  -0.0616 0.0291  69  GLY A CA  
722  C C   . GLY A 51  ? 0.2114 0.1196 0.2413 0.0059  -0.0583 0.0384  69  GLY A C   
723  O O   . GLY A 51  ? 0.2273 0.1168 0.2210 -0.0062 -0.0523 0.0279  69  GLY A O   
727  N N   . PRO A 52  ? 0.2024 0.1270 0.2372 -0.0032 -0.0651 0.0271  70  PRO A N   
728  C CA  . PRO A 52  ? 0.1986 0.1384 0.2386 0.0154  -0.0681 0.0215  70  PRO A CA  
729  C C   . PRO A 52  ? 0.2090 0.1347 0.2403 0.0070  -0.0477 0.0204  70  PRO A C   
730  O O   . PRO A 52  ? 0.2481 0.1207 0.2448 0.0062  -0.0664 0.0173  70  PRO A O   
731  C CB  . PRO A 52  ? 0.1983 0.1575 0.2476 0.0190  -0.0929 0.0127  70  PRO A CB  
732  C CG  . PRO A 52  ? 0.1872 0.1490 0.2506 0.0147  -0.0849 0.0193  70  PRO A CG  
733  C CD  . PRO A 52  ? 0.1675 0.1300 0.2349 0.0121  -0.0555 0.0282  70  PRO A CD  
741  N N   . GLN A 53  ? 0.2050 0.1372 0.2321 0.0009  -0.0457 0.0329  71  GLN A N   
742  C CA  . GLN A 53  ? 0.2163 0.1197 0.2432 -0.0014 -0.0323 0.0345  71  GLN A CA  
743  C C   . GLN A 53  ? 0.2318 0.1168 0.2426 -0.0080 -0.0381 0.0216  71  GLN A C   
744  O O   . GLN A 53  ? 0.2432 0.1299 0.2545 -0.0013 -0.0456 0.0101  71  GLN A O   
745  C CB  . GLN A 53  ? 0.2277 0.1304 0.2726 -0.0337 -0.0385 0.0447  71  GLN A CB  
746  C CG  . GLN A 53  ? 0.2483 0.1313 0.3096 -0.0081 -0.0195 0.0316  71  GLN A CG  
747  C CD  . GLN A 53  ? 0.2595 0.1469 0.3323 -0.0343 -0.0035 0.0152  71  GLN A CD  
748  O OE1 . GLN A 53  ? 0.2473 0.1415 0.3387 -0.0102 -0.0230 0.0250  71  GLN A OE1 
749  N NE2 . GLN A 53  ? 0.3399 0.1816 0.3560 -0.0059 0.0235  -0.0011 71  GLN A NE2 
758  N N   . SER A 54  ? 0.2119 0.1032 0.2323 -0.0109 -0.0567 0.0052  72  SER A N   
759  C CA  . SER A 54  ? 0.2257 0.1031 0.2425 -0.0028 -0.0541 0.0082  72  SER A CA  
760  C C   . SER A 54  ? 0.2222 0.1016 0.2425 0.0126  -0.0389 0.0031  72  SER A C   
761  O O   . SER A 54  ? 0.2149 0.1119 0.2384 0.0046  -0.0662 0.0037  72  SER A O   
762  C CB  . SER A 54  ? 0.2251 0.1068 0.2539 -0.0174 -0.0511 0.0171  72  SER A CB  
763  O OG  . SER A 54  ? 0.2092 0.0949 0.2751 0.0041  -0.0563 0.0207  72  SER A OG  
769  N N   . PHE A 55  ? 0.2066 0.0826 0.2445 0.0057  -0.0479 0.0088  73  PHE A N   
770  C CA  . PHE A 55  ? 0.2213 0.0877 0.2205 0.0175  -0.0332 0.0113  73  PHE A CA  
771  C C   . PHE A 55  ? 0.2188 0.0910 0.2340 0.0018  -0.0511 0.0119  73  PHE A C   
772  O O   . PHE A 55  ? 0.2510 0.0853 0.2184 0.0039  -0.0434 -0.0075 73  PHE A O   
773  C CB  . PHE A 55  ? 0.2161 0.0956 0.1972 -0.0109 -0.0346 -0.0111 73  PHE A CB  
774  C CG  . PHE A 55  ? 0.2184 0.1153 0.2099 -0.0196 -0.0373 0.0309  73  PHE A CG  
775  C CD1 . PHE A 55  ? 0.2357 0.1241 0.2172 -0.0167 -0.0560 0.0255  73  PHE A CD1 
776  C CD2 . PHE A 55  ? 0.2173 0.1117 0.1972 0.0010  -0.0545 0.0524  73  PHE A CD2 
777  C CE1 . PHE A 55  ? 0.2060 0.1214 0.2104 -0.0311 -0.0725 0.0356  73  PHE A CE1 
778  C CE2 . PHE A 55  ? 0.2234 0.1157 0.2050 -0.0046 -0.0551 0.0375  73  PHE A CE2 
779  C CZ  . PHE A 55  ? 0.2194 0.1154 0.2038 -0.0197 -0.0624 0.0402  73  PHE A CZ  
789  N N   . ASP A 56  ? 0.2123 0.1118 0.2607 0.0120  -0.0546 0.0234  74  ASP A N   
790  C CA  . ASP A 56  ? 0.2398 0.1200 0.2741 0.0115  -0.0521 -0.0036 74  ASP A CA  
791  C C   . ASP A 56  ? 0.2579 0.1170 0.2860 0.0141  -0.0611 0.0075  74  ASP A C   
792  O O   . ASP A 56  ? 0.2869 0.1084 0.3103 0.0107  -0.0414 -0.0010 74  ASP A O   
793  C CB  . ASP A 56  ? 0.2477 0.1452 0.2952 0.0119  -0.0394 -0.0105 74  ASP A CB  
794  C CG  . ASP A 56  ? 0.2645 0.1586 0.3115 0.0291  -0.0300 -0.0036 74  ASP A CG  
795  O OD1 . ASP A 56  ? 0.2660 0.1905 0.3121 0.0377  -0.0438 0.0076  74  ASP A OD1 
796  O OD2 . ASP A 56  ? 0.2868 0.1518 0.3365 0.0295  -0.0236 -0.0025 74  ASP A OD2 
801  N N   . SER A 57  ? 0.2650 0.1314 0.2727 -0.0156 -0.0655 0.0063  75  SER A N   
802  C CA  . SER A 57  ? 0.2869 0.1321 0.2709 -0.0273 -0.0434 -0.0140 75  SER A CA  
803  C C   . SER A 57  ? 0.3008 0.1433 0.2614 -0.0070 -0.0242 -0.0159 75  SER A C   
804  O O   . SER A 57  ? 0.3401 0.1510 0.2443 -0.0342 -0.0127 -0.0316 75  SER A O   
805  C CB  . SER A 57  ? 0.2627 0.1336 0.2827 -0.0067 -0.0693 -0.0001 75  SER A CB  
806  O OG  . SER A 57  ? 0.2475 0.1340 0.2972 -0.0058 -0.0685 -0.0012 75  SER A OG  
812  N N   . ASN A 58  ? 0.2639 0.1246 0.2323 -0.0078 -0.0487 0.0074  76  ASN A N   
813  C CA  . ASN A 58  ? 0.2627 0.1123 0.2292 -0.0173 -0.0669 0.0096  76  ASN A CA  
814  C C   . ASN A 58  ? 0.2483 0.1081 0.2182 -0.0186 -0.0643 -0.0075 76  ASN A C   
815  O O   . ASN A 58  ? 0.2667 0.1143 0.2235 0.0054  -0.0528 0.0103  76  ASN A O   
816  C CB  . ASN A 58  ? 0.2239 0.1204 0.2405 -0.0252 -0.0732 0.0167  76  ASN A CB  
817  C CG  . ASN A 58  ? 0.2292 0.1302 0.2451 -0.0188 -0.0662 0.0134  76  ASN A CG  
818  O OD1 . ASN A 58  ? 0.2490 0.1197 0.2512 -0.0116 -0.0491 0.0002  76  ASN A OD1 
819  N ND2 . ASN A 58  ? 0.2730 0.1109 0.2221 -0.0313 -0.0686 0.0076  76  ASN A ND2 
826  N N   . TRP A 59  ? 0.2437 0.0981 0.2187 -0.0086 -0.0818 0.0060  77  TRP A N   
827  C CA  . TRP A 59  ? 0.2349 0.1256 0.2191 0.0028  -0.1021 0.0241  77  TRP A CA  
828  C C   . TRP A 59  ? 0.2461 0.1352 0.2264 -0.0079 -0.0775 0.0062  77  TRP A C   
829  O O   . TRP A 59  ? 0.2431 0.1466 0.2107 -0.0061 -0.0775 0.0359  77  TRP A O   
830  C CB  . TRP A 59  ? 0.2435 0.1259 0.2276 0.0002  -0.0938 0.0088  77  TRP A CB  
831  C CG  . TRP A 59  ? 0.2257 0.1098 0.2413 -0.0013 -0.0852 0.0067  77  TRP A CG  
832  C CD1 . TRP A 59  ? 0.2136 0.1183 0.2488 -0.0049 -0.0718 0.0067  77  TRP A CD1 
833  C CD2 . TRP A 59  ? 0.2412 0.0999 0.2384 -0.0134 -0.0721 0.0177  77  TRP A CD2 
834  N NE1 . TRP A 59  ? 0.2372 0.0962 0.2557 0.0030  -0.0693 0.0078  77  TRP A NE1 
835  C CE2 . TRP A 59  ? 0.2348 0.0957 0.2423 -0.0056 -0.0585 0.0295  77  TRP A CE2 
836  C CE3 . TRP A 59  ? 0.2482 0.1063 0.2352 -0.0188 -0.0699 0.0293  77  TRP A CE3 
837  C CZ2 . TRP A 59  ? 0.2278 0.1024 0.2343 -0.0203 -0.0709 0.0292  77  TRP A CZ2 
838  C CZ3 . TRP A 59  ? 0.2546 0.1193 0.2386 -0.0106 -0.0456 0.0241  77  TRP A CZ3 
839  C CH2 . TRP A 59  ? 0.2269 0.1068 0.2366 -0.0072 -0.0530 0.0290  77  TRP A CH2 
850  N N   . ILE A 60  ? 0.2438 0.1342 0.2316 0.0059  -0.0886 0.0063  78  ILE A N   
851  C CA  . ILE A 60  ? 0.2514 0.1163 0.2320 0.0217  -0.0751 0.0133  78  ILE A CA  
852  C C   . ILE A 60  ? 0.2277 0.1174 0.2360 0.0174  -0.1008 0.0080  78  ILE A C   
853  O O   . ILE A 60  ? 0.2752 0.1232 0.2386 0.0362  -0.0919 0.0152  78  ILE A O   
854  C CB  . ILE A 60  ? 0.2297 0.1239 0.2304 0.0419  -0.0737 0.0144  78  ILE A CB  
855  C CG1 . ILE A 60  ? 0.2448 0.1276 0.2187 0.0112  -0.0666 0.0107  78  ILE A CG1 
856  C CG2 . ILE A 60  ? 0.2360 0.1410 0.2613 0.0253  -0.0509 0.0090  78  ILE A CG2 
857  C CD1 . ILE A 60  ? 0.2600 0.1256 0.2275 -0.0018 -0.0742 0.0076  78  ILE A CD1 
869  N N   . PRO A 61  ? 0.2611 0.1096 0.2521 0.0018  -0.0638 0.0191  79  PRO A N   
870  C CA  . PRO A 61  ? 0.2626 0.1119 0.2652 0.0162  -0.0607 0.0022  79  PRO A CA  
871  C C   . PRO A 61  ? 0.2535 0.1183 0.2555 0.0105  -0.0470 0.0274  79  PRO A C   
872  O O   . PRO A 61  ? 0.2677 0.1347 0.2615 -0.0217 -0.0493 0.0372  79  PRO A O   
873  C CB  . PRO A 61  ? 0.2500 0.1032 0.2750 0.0199  -0.0611 0.0013  79  PRO A CB  
874  C CG  . PRO A 61  ? 0.2451 0.1199 0.2665 0.0137  -0.0785 0.0117  79  PRO A CG  
875  C CD  . PRO A 61  ? 0.2568 0.1219 0.2564 -0.0017 -0.0747 0.0124  79  PRO A CD  
883  N N   . LEU A 62  ? 0.2551 0.1125 0.2548 -0.0020 -0.0470 0.0203  80  LEU A N   
884  C CA  . LEU A 62  ? 0.2669 0.1244 0.2487 0.0098  -0.0599 0.0290  80  LEU A CA  
885  C C   . LEU A 62  ? 0.2673 0.1272 0.2566 -0.0050 -0.0739 0.0376  80  LEU A C   
886  O O   . LEU A 62  ? 0.2712 0.1662 0.2749 -0.0296 -0.0671 0.0435  80  LEU A O   
887  C CB  . LEU A 62  ? 0.2480 0.1432 0.2468 -0.0054 -0.0693 0.0130  80  LEU A CB  
888  C CG  . LEU A 62  ? 0.2690 0.1369 0.2650 -0.0108 -0.0609 0.0011  80  LEU A CG  
889  C CD1 . LEU A 62  ? 0.2526 0.1521 0.2373 -0.0075 -0.1029 0.0248  80  LEU A CD1 
890  C CD2 . LEU A 62  ? 0.3103 0.1361 0.2697 -0.0157 -0.0692 -0.0130 80  LEU A CD2 
902  N N   . SER A 63  ? 0.2795 0.1330 0.2468 0.0031  -0.0844 0.0323  81  SER A N   
903  C CA  . SER A 63  ? 0.2838 0.1285 0.2513 -0.0028 -0.0935 0.0380  81  SER A CA  
904  C C   . SER A 63  ? 0.2941 0.1403 0.2599 -0.0088 -0.0979 0.0273  81  SER A C   
905  O O   . SER A 63  ? 0.2986 0.1458 0.2399 -0.0153 -0.1016 0.0185  81  SER A O   
906  C CB  . SER A 63  ? 0.2767 0.1453 0.2787 -0.0292 -0.0551 0.0159  81  SER A CB  
907  O OG  . SER A 63  ? 0.2865 0.1626 0.2774 -0.0104 -0.0786 0.0113  81  SER A OG  
913  N N   . THR A 64  ? 0.2735 0.1335 0.2672 -0.0080 -0.1027 0.0393  82  THR A N   
914  C CA  . THR A 64  ? 0.2807 0.1186 0.2839 -0.0102 -0.0738 0.0282  82  THR A CA  
915  C C   . THR A 64  ? 0.2851 0.1098 0.2741 -0.0055 -0.0680 0.0444  82  THR A C   
916  O O   . THR A 64  ? 0.3125 0.1087 0.2954 0.0030  -0.0460 0.0402  82  THR A O   
917  C CB  . THR A 64  ? 0.2934 0.1308 0.2910 0.0131  -0.0941 0.0211  82  THR A CB  
918  O OG1 . THR A 64  ? 0.2559 0.1370 0.2738 -0.0098 -0.0940 0.0461  82  THR A OG1 
919  C CG2 . THR A 64  ? 0.3127 0.1293 0.3200 0.0398  -0.0665 0.0216  82  THR A CG2 
927  N N   A GLN A 65  ? 0.2778 0.1235 0.2733 -0.0053 -0.0820 0.0447  83  GLN A N   
928  N N   B GLN A 65  ? 0.2939 0.1211 0.2873 -0.0025 -0.0770 0.0492  83  GLN A N   
929  C CA  A GLN A 65  ? 0.2732 0.1404 0.2913 -0.0143 -0.0892 0.0298  83  GLN A CA  
930  C CA  B GLN A 65  ? 0.3049 0.1324 0.3123 -0.0038 -0.0807 0.0470  83  GLN A CA  
931  C C   A GLN A 65  ? 0.2792 0.1412 0.3176 -0.0265 -0.0706 0.0392  83  GLN A C   
932  C C   B GLN A 65  ? 0.2988 0.1278 0.3123 -0.0242 -0.0819 0.0593  83  GLN A C   
933  O O   A GLN A 65  ? 0.2859 0.1732 0.3466 -0.0438 -0.0650 0.0364  83  GLN A O   
934  O O   B GLN A 65  ? 0.3051 0.1385 0.3069 -0.0425 -0.0925 0.0801  83  GLN A O   
935  C CB  A GLN A 65  ? 0.2927 0.1595 0.2876 -0.0175 -0.0797 0.0111  83  GLN A CB  
936  C CB  B GLN A 65  ? 0.3387 0.1509 0.3412 0.0080  -0.0623 0.0344  83  GLN A CB  
937  C CG  A GLN A 65  ? 0.3291 0.1766 0.2742 -0.0407 -0.0845 -0.0210 83  GLN A CG  
938  C CG  B GLN A 65  ? 0.3675 0.1627 0.3614 0.0242  -0.0577 0.0191  83  GLN A CG  
939  C CD  A GLN A 65  ? 0.3877 0.1938 0.2719 -0.0348 -0.0458 -0.0292 83  GLN A CD  
940  C CD  B GLN A 65  ? 0.3888 0.1620 0.3697 0.0157  -0.0507 0.0003  83  GLN A CD  
941  O OE1 A GLN A 65  ? 0.4150 0.2180 0.2492 -0.0455 -0.0788 -0.0457 83  GLN A OE1 
942  O OE1 B GLN A 65  ? 0.3829 0.1556 0.3391 0.0201  -0.0601 0.0032  83  GLN A OE1 
943  N NE2 A GLN A 65  ? 0.3854 0.1856 0.2734 -0.0260 -0.0175 -0.0372 83  GLN A NE2 
944  N NE2 B GLN A 65  ? 0.4036 0.1734 0.3957 0.0195  -0.0467 0.0052  83  GLN A NE2 
961  N N   . LEU A 66  ? 0.2913 0.1405 0.3114 -0.0297 -0.0728 0.0384  84  LEU A N   
962  C CA  . LEU A 66  ? 0.2946 0.1411 0.3132 -0.0429 -0.0634 0.0549  84  LEU A CA  
963  C C   . LEU A 66  ? 0.3143 0.1616 0.3109 -0.0267 -0.0621 0.0500  84  LEU A C   
964  O O   . LEU A 66  ? 0.3183 0.2000 0.3305 -0.0172 -0.0253 0.0584  84  LEU A O   
965  C CB  . LEU A 66  ? 0.2870 0.1358 0.3248 -0.0494 -0.0514 0.0441  84  LEU A CB  
966  C CG  . LEU A 66  ? 0.2674 0.1506 0.3278 -0.0416 -0.0785 0.0419  84  LEU A CG  
967  C CD1 . LEU A 66  ? 0.3083 0.1623 0.3290 -0.0485 -0.0629 0.0369  84  LEU A CD1 
968  C CD2 . LEU A 66  ? 0.2771 0.1793 0.3450 -0.0208 -0.0761 0.0349  84  LEU A CD2 
980  N N   . GLY A 67  ? 0.3159 0.1417 0.2963 -0.0071 -0.0805 0.0529  85  GLY A N   
981  C CA  . GLY A 67  ? 0.3333 0.1544 0.2716 -0.0036 -0.0841 0.0535  85  GLY A CA  
982  C C   . GLY A 67  ? 0.3578 0.1568 0.2672 -0.0023 -0.1037 0.0550  85  GLY A C   
983  O O   . GLY A 67  ? 0.4261 0.1891 0.2614 -0.0207 -0.0873 0.0621  85  GLY A O   
987  N N   . TYR A 68  ? 0.2898 0.1419 0.2588 -0.0133 -0.1136 0.0477  86  TYR A N   
988  C CA  . TYR A 68  ? 0.2794 0.1351 0.2713 -0.0041 -0.0899 0.0353  86  TYR A CA  
989  C C   . TYR A 68  ? 0.2819 0.1393 0.2651 0.0052  -0.0885 0.0313  86  TYR A C   
990  O O   . TYR A 68  ? 0.3038 0.1644 0.2721 -0.0228 -0.0762 0.0105  86  TYR A O   
991  C CB  . TYR A 68  ? 0.2667 0.1434 0.2574 0.0151  -0.1237 0.0372  86  TYR A CB  
992  C CG  . TYR A 68  ? 0.2734 0.1529 0.2771 -0.0147 -0.1168 0.0357  86  TYR A CG  
993  C CD1 . TYR A 68  ? 0.2855 0.1453 0.2883 -0.0134 -0.1349 0.0406  86  TYR A CD1 
994  C CD2 . TYR A 68  ? 0.2666 0.1674 0.2862 -0.0051 -0.1221 0.0215  86  TYR A CD2 
995  C CE1 . TYR A 68  ? 0.3029 0.1801 0.3124 0.0160  -0.0936 0.0381  86  TYR A CE1 
996  C CE2 . TYR A 68  ? 0.2847 0.1802 0.2999 0.0043  -0.1141 0.0254  86  TYR A CE2 
997  C CZ  . TYR A 68  ? 0.2806 0.1910 0.3119 0.0152  -0.1019 0.0330  86  TYR A CZ  
998  O OH  . TYR A 68  ? 0.3024 0.2280 0.3356 0.0201  -0.0735 0.0292  86  TYR A OH  
1008 N N   . THR A 69  ? 0.2759 0.1272 0.2678 -0.0064 -0.0934 0.0584  87  THR A N   
1009 C CA  . THR A 69  ? 0.2867 0.1291 0.2632 0.0158  -0.1054 0.0505  87  THR A CA  
1010 C C   . THR A 69  ? 0.2533 0.1073 0.2543 0.0081  -0.1072 0.0336  87  THR A C   
1011 O O   . THR A 69  ? 0.2703 0.1313 0.2465 0.0004  -0.0894 0.0191  87  THR A O   
1012 C CB  . THR A 69  ? 0.3068 0.1381 0.2598 0.0057  -0.1064 0.0472  87  THR A CB  
1013 O OG1 . THR A 69  ? 0.3495 0.1629 0.2595 0.0305  -0.1004 0.0526  87  THR A OG1 
1014 C CG2 . THR A 69  ? 0.3135 0.1453 0.2633 0.0133  -0.1002 0.0406  87  THR A CG2 
1022 N N   . PRO A 70  ? 0.2733 0.0955 0.2489 -0.0045 -0.0957 0.0270  88  PRO A N   
1023 C CA  . PRO A 70  ? 0.2451 0.1032 0.2470 -0.0216 -0.0945 0.0249  88  PRO A CA  
1024 C C   . PRO A 70  ? 0.2359 0.1023 0.2325 0.0064  -0.0985 0.0347  88  PRO A C   
1025 O O   . PRO A 70  ? 0.2535 0.1217 0.2480 -0.0051 -0.0901 0.0293  88  PRO A O   
1026 C CB  . PRO A 70  ? 0.2603 0.1384 0.2617 -0.0213 -0.1090 0.0218  88  PRO A CB  
1027 C CG  . PRO A 70  ? 0.2791 0.1341 0.2548 0.0042  -0.0959 0.0233  88  PRO A CG  
1028 C CD  . PRO A 70  ? 0.3014 0.1260 0.2695 -0.0040 -0.0741 0.0189  88  PRO A CD  
1036 N N   . CYS A 71  ? 0.2362 0.0956 0.2295 -0.0025 -0.0802 0.0432  89  CYS A N   
1037 C CA  . CYS A 71  ? 0.2458 0.0927 0.2423 -0.0056 -0.0847 0.0224  89  CYS A CA  
1038 C C   . CYS A 71  ? 0.2329 0.1084 0.2359 -0.0265 -0.0894 0.0262  89  CYS A C   
1039 O O   . CYS A 71  ? 0.2238 0.1286 0.2595 0.0073  -0.0726 0.0299  89  CYS A O   
1040 C CB  . CYS A 71  ? 0.2553 0.1078 0.2417 -0.0035 -0.0823 0.0329  89  CYS A CB  
1041 S SG  . CYS A 71  ? 0.2682 0.1368 0.2479 0.0129  -0.0957 0.0246  89  CYS A SG  
1046 N N   . TRP A 72  ? 0.2257 0.0909 0.2482 -0.0046 -0.0825 0.0273  90  TRP A N   
1047 C CA  . TRP A 72  ? 0.2184 0.0931 0.2468 -0.0047 -0.0895 0.0303  90  TRP A CA  
1048 C C   . TRP A 72  ? 0.1921 0.1107 0.2529 -0.0099 -0.1008 0.0322  90  TRP A C   
1049 O O   . TRP A 72  ? 0.2227 0.1242 0.2503 -0.0262 -0.1093 0.0559  90  TRP A O   
1050 C CB  . TRP A 72  ? 0.2155 0.1087 0.2370 -0.0107 -0.1001 0.0263  90  TRP A CB  
1051 C CG  . TRP A 72  ? 0.2090 0.1193 0.2551 -0.0103 -0.1044 0.0303  90  TRP A CG  
1052 C CD1 . TRP A 72  ? 0.2172 0.1277 0.2791 -0.0046 -0.0688 0.0379  90  TRP A CD1 
1053 C CD2 . TRP A 72  ? 0.2336 0.1294 0.2599 0.0082  -0.1007 0.0311  90  TRP A CD2 
1054 N NE1 . TRP A 72  ? 0.2051 0.1442 0.2785 0.0044  -0.0808 0.0314  90  TRP A NE1 
1055 C CE2 . TRP A 72  ? 0.2340 0.1328 0.2595 0.0078  -0.0794 0.0233  90  TRP A CE2 
1056 C CE3 . TRP A 72  ? 0.2408 0.1181 0.2702 -0.0007 -0.0911 0.0315  90  TRP A CE3 
1057 C CZ2 . TRP A 72  ? 0.2652 0.1321 0.2701 0.0022  -0.0677 0.0035  90  TRP A CZ2 
1058 C CZ3 . TRP A 72  ? 0.2613 0.1334 0.2763 0.0095  -0.0739 0.0228  90  TRP A CZ3 
1059 C CH2 . TRP A 72  ? 0.2752 0.1419 0.2791 0.0112  -0.0585 0.0199  90  TRP A CH2 
1070 N N   . ILE A 73  ? 0.1944 0.1244 0.2473 -0.0224 -0.0826 0.0435  91  ILE A N   
1071 C CA  . ILE A 73  ? 0.2098 0.1144 0.2552 -0.0329 -0.0743 0.0294  91  ILE A CA  
1072 C C   . ILE A 73  ? 0.2167 0.1124 0.2667 -0.0232 -0.0835 0.0222  91  ILE A C   
1073 O O   . ILE A 73  ? 0.2188 0.1028 0.2661 -0.0305 -0.0649 0.0192  91  ILE A O   
1074 C CB  . ILE A 73  ? 0.2071 0.1198 0.2399 -0.0158 -0.0624 0.0303  91  ILE A CB  
1075 C CG1 . ILE A 73  ? 0.2022 0.1287 0.2411 -0.0272 -0.0623 0.0252  91  ILE A CG1 
1076 C CG2 . ILE A 73  ? 0.2298 0.1265 0.2295 -0.0150 -0.0597 0.0504  91  ILE A CG2 
1077 C CD1 . ILE A 73  ? 0.1933 0.1520 0.2307 -0.0012 -0.0767 0.0187  91  ILE A CD1 
1089 N N   . SER A 74  ? 0.2039 0.0992 0.2771 -0.0291 -0.0745 0.0398  92  SER A N   
1090 C CA  . SER A 74  ? 0.1981 0.0935 0.2675 -0.0234 -0.0706 0.0478  92  SER A CA  
1091 C C   . SER A 74  ? 0.2153 0.1141 0.2656 -0.0312 -0.0732 0.0392  92  SER A C   
1092 O O   . SER A 74  ? 0.2303 0.1282 0.2832 -0.0296 -0.0611 0.0438  92  SER A O   
1093 C CB  . SER A 74  ? 0.1913 0.0996 0.2880 -0.0291 -0.0555 0.0388  92  SER A CB  
1094 O OG  . SER A 74  ? 0.1994 0.1267 0.3107 -0.0387 -0.0578 0.0250  92  SER A OG  
1100 N N   . PRO A 75  ? 0.2078 0.1164 0.2440 -0.0093 -0.0628 0.0202  93  PRO A N   
1101 C CA  . PRO A 75  ? 0.2412 0.1201 0.2623 -0.0160 -0.0500 0.0280  93  PRO A CA  
1102 C C   . PRO A 75  ? 0.2594 0.1430 0.2745 -0.0163 -0.0501 0.0347  93  PRO A C   
1103 O O   . PRO A 75  ? 0.2624 0.1383 0.2666 -0.0109 -0.0546 0.0402  93  PRO A O   
1104 C CB  . PRO A 75  ? 0.2564 0.0979 0.2610 -0.0015 -0.0357 0.0162  93  PRO A CB  
1105 C CG  . PRO A 75  ? 0.2380 0.0938 0.2488 -0.0185 -0.0499 0.0185  93  PRO A CG  
1106 C CD  . PRO A 75  ? 0.2173 0.1063 0.2429 -0.0164 -0.0528 0.0082  93  PRO A CD  
1114 N N   . PRO A 76  ? 0.2514 0.1507 0.2802 -0.0222 -0.0647 0.0327  94  PRO A N   
1115 C CA  . PRO A 76  ? 0.2299 0.1389 0.2915 -0.0119 -0.0757 0.0339  94  PRO A CA  
1116 C C   . PRO A 76  ? 0.2333 0.1277 0.2921 -0.0253 -0.0647 0.0219  94  PRO A C   
1117 O O   . PRO A 76  ? 0.2328 0.1356 0.2852 -0.0252 -0.0481 -0.0041 94  PRO A O   
1118 C CB  . PRO A 76  ? 0.2439 0.1659 0.3085 -0.0004 -0.0550 0.0524  94  PRO A CB  
1119 C CG  . PRO A 76  ? 0.2303 0.1710 0.3076 -0.0371 -0.0606 0.0306  94  PRO A CG  
1120 C CD  . PRO A 76  ? 0.2513 0.1732 0.2982 -0.0547 -0.0569 0.0226  94  PRO A CD  
1128 N N   . PRO A 77  ? 0.2492 0.1228 0.3054 -0.0120 -0.0777 0.0230  95  PRO A N   
1129 C CA  . PRO A 77  ? 0.2544 0.1051 0.3128 -0.0093 -0.0718 0.0331  95  PRO A CA  
1130 C C   . PRO A 77  ? 0.2611 0.0936 0.3192 -0.0217 -0.0517 0.0289  95  PRO A C   
1131 O O   . PRO A 77  ? 0.2405 0.0976 0.3053 -0.0104 -0.0306 0.0572  95  PRO A O   
1132 C CB  . PRO A 77  ? 0.2729 0.1184 0.3050 -0.0130 -0.0803 0.0323  95  PRO A CB  
1133 C CG  . PRO A 77  ? 0.2745 0.1111 0.3053 -0.0189 -0.0680 0.0414  95  PRO A CG  
1134 C CD  . PRO A 77  ? 0.2587 0.1208 0.2984 -0.0098 -0.0830 0.0400  95  PRO A CD  
1142 N N   . PHE A 78  ? 0.2379 0.1059 0.3197 -0.0425 -0.0245 0.0234  96  PHE A N   
1143 C CA  . PHE A 78  ? 0.2252 0.1029 0.3021 -0.0309 -0.0355 0.0410  96  PHE A CA  
1144 C C   . PHE A 78  ? 0.2213 0.1101 0.2885 -0.0169 -0.0418 0.0296  96  PHE A C   
1145 O O   . PHE A 78  ? 0.2105 0.1365 0.2773 -0.0101 -0.0602 0.0071  96  PHE A O   
1146 C CB  . PHE A 78  ? 0.2471 0.1119 0.3028 -0.0214 -0.0168 0.0589  96  PHE A CB  
1147 C CG  . PHE A 78  ? 0.2246 0.1476 0.3268 0.0044  0.0075  0.0478  96  PHE A CG  
1148 C CD1 . PHE A 78  ? 0.2385 0.1615 0.3765 0.0106  0.0382  0.0454  96  PHE A CD1 
1149 C CD2 . PHE A 78  ? 0.2080 0.1696 0.3357 0.0168  -0.0024 0.0364  96  PHE A CD2 
1150 C CE1 . PHE A 78  ? 0.2618 0.1858 0.4005 0.0369  0.0559  0.0561  96  PHE A CE1 
1151 C CE2 . PHE A 78  ? 0.2367 0.1844 0.3737 0.0143  0.0353  0.0394  96  PHE A CE2 
1152 C CZ  . PHE A 78  ? 0.2445 0.2000 0.4008 0.0432  0.0367  0.0427  96  PHE A CZ  
1162 N N   . MET A 79  ? 0.2142 0.1035 0.2798 -0.0124 -0.0631 0.0275  97  MET A N   
1163 C CA  . MET A 79  ? 0.1943 0.1121 0.2867 -0.0281 -0.0542 0.0262  97  MET A CA  
1164 C C   . MET A 79  ? 0.2030 0.1277 0.3012 -0.0162 -0.0457 0.0257  97  MET A C   
1165 O O   . MET A 79  ? 0.1938 0.1440 0.3088 -0.0278 -0.0390 0.0108  97  MET A O   
1166 C CB  . MET A 79  ? 0.2072 0.1206 0.2773 -0.0174 -0.0517 0.0036  97  MET A CB  
1167 C CG  . MET A 79  ? 0.2222 0.1294 0.2692 -0.0053 -0.0715 0.0072  97  MET A CG  
1168 S SD  . MET A 79  ? 0.2126 0.1300 0.2528 -0.0159 -0.0594 0.0268  97  MET A SD  
1169 C CE  . MET A 79  ? 0.2295 0.1272 0.2536 -0.0160 -0.0539 0.0103  97  MET A CE  
1179 N N   . LEU A 80  ? 0.1920 0.0976 0.2848 -0.0198 -0.0589 0.0339  98  LEU A N   
1180 C CA  . LEU A 80  ? 0.2059 0.0906 0.2722 -0.0183 -0.0403 0.0252  98  LEU A CA  
1181 C C   . LEU A 80  ? 0.2167 0.1116 0.2775 -0.0058 -0.0330 0.0189  98  LEU A C   
1182 O O   . LEU A 80  ? 0.2151 0.1171 0.2859 0.0169  -0.0257 0.0331  98  LEU A O   
1183 C CB  . LEU A 80  ? 0.2069 0.1082 0.2664 -0.0089 -0.0328 0.0346  98  LEU A CB  
1184 C CG  . LEU A 80  ? 0.2691 0.1257 0.2601 -0.0143 -0.0028 0.0232  98  LEU A CG  
1185 C CD1 . LEU A 80  ? 0.3147 0.1338 0.2666 -0.0233 0.0510  0.0235  98  LEU A CD1 
1186 C CD2 . LEU A 80  ? 0.2914 0.1446 0.2592 -0.0116 -0.0105 0.0230  98  LEU A CD2 
1198 N N   A ASN A 81  ? 0.2101 0.1199 0.2687 -0.0180 -0.0617 -0.0109 99  ASN A N   
1199 N N   B ASN A 81  ? 0.2321 0.1142 0.2924 -0.0039 -0.0464 0.0073  99  ASN A N   
1200 C CA  A ASN A 81  ? 0.2144 0.1086 0.2506 -0.0372 -0.0660 -0.0126 99  ASN A CA  
1201 C CA  B ASN A 81  ? 0.2522 0.1023 0.3001 -0.0065 -0.0484 0.0111  99  ASN A CA  
1202 C C   A ASN A 81  ? 0.1991 0.1062 0.2432 -0.0359 -0.0696 0.0110  99  ASN A C   
1203 C C   B ASN A 81  ? 0.2386 0.1033 0.2784 -0.0169 -0.0538 0.0198  99  ASN A C   
1204 O O   A ASN A 81  ? 0.2132 0.1079 0.2273 -0.0171 -0.0568 0.0251  99  ASN A O   
1205 O O   B ASN A 81  ? 0.2607 0.0992 0.2729 -0.0055 -0.0528 0.0277  99  ASN A O   
1206 C CB  A ASN A 81  ? 0.2116 0.1336 0.2575 -0.0524 -0.0527 -0.0267 99  ASN A CB  
1207 C CB  B ASN A 81  ? 0.2674 0.1062 0.3376 0.0163  -0.0444 0.0102  99  ASN A CB  
1208 C CG  A ASN A 81  ? 0.2488 0.1641 0.2795 -0.0603 -0.0316 -0.0358 99  ASN A CG  
1209 C CG  B ASN A 81  ? 0.2649 0.1127 0.3720 0.0197  -0.0424 0.0125  99  ASN A CG  
1210 O OD1 A ASN A 81  ? 0.2574 0.1877 0.3033 -0.0785 -0.0372 -0.0289 99  ASN A OD1 
1211 O OD1 B ASN A 81  ? 0.2739 0.1311 0.3836 0.0228  -0.0206 0.0287  99  ASN A OD1 
1212 N ND2 A ASN A 81  ? 0.2658 0.1719 0.2764 -0.0820 -0.0128 -0.0755 99  ASN A ND2 
1213 N ND2 B ASN A 81  ? 0.2329 0.1038 0.3904 -0.0025 -0.0631 -0.0109 99  ASN A ND2 
1226 N N   . ASP A 82  ? 0.2320 0.1116 0.2670 -0.0245 -0.0417 0.0159  100 ASP A N   
1227 C CA  . ASP A 82  ? 0.2288 0.1107 0.2832 -0.0002 -0.0319 0.0158  100 ASP A CA  
1228 C C   . ASP A 82  ? 0.2205 0.1176 0.2800 -0.0160 -0.0296 0.0064  100 ASP A C   
1229 O O   . ASP A 82  ? 0.2126 0.1249 0.2726 -0.0024 -0.0394 0.0118  100 ASP A O   
1230 C CB  . ASP A 82  ? 0.2103 0.1138 0.2904 -0.0221 -0.0610 -0.0131 100 ASP A CB  
1231 C CG  . ASP A 82  ? 0.2343 0.1205 0.3040 -0.0063 -0.0854 -0.0205 100 ASP A CG  
1232 O OD1 . ASP A 82  ? 0.2259 0.1082 0.2843 0.0084  -0.0903 0.0136  100 ASP A OD1 
1233 O OD2 . ASP A 82  ? 0.2780 0.1435 0.3539 -0.0143 -0.0728 -0.0470 100 ASP A OD2 
1238 N N   . THR A 83  ? 0.2189 0.1117 0.2534 -0.0002 -0.0618 0.0011  101 THR A N   
1239 C CA  . THR A 83  ? 0.2107 0.1149 0.2573 0.0026  -0.0780 -0.0079 101 THR A CA  
1240 C C   . THR A 83  ? 0.2109 0.1139 0.2790 -0.0118 -0.0618 -0.0120 101 THR A C   
1241 O O   . THR A 83  ? 0.1995 0.1115 0.2772 -0.0023 -0.0630 -0.0226 101 THR A O   
1242 C CB  . THR A 83  ? 0.2351 0.1581 0.2791 -0.0149 -0.0691 0.0023  101 THR A CB  
1243 O OG1 . THR A 83  ? 0.2106 0.1697 0.2920 -0.0040 -0.0802 0.0181  101 THR A OG1 
1244 C CG2 . THR A 83  ? 0.2677 0.1359 0.2758 -0.0219 -0.0696 -0.0044 101 THR A CG2 
1252 N N   . GLN A 84  ? 0.1980 0.1230 0.2667 -0.0073 -0.0860 -0.0217 102 GLN A N   
1253 C CA  . GLN A 84  ? 0.2250 0.1091 0.2491 -0.0045 -0.0692 -0.0283 102 GLN A CA  
1254 C C   . GLN A 84  ? 0.2148 0.1083 0.2574 0.0001  -0.0646 0.0050  102 GLN A C   
1255 O O   . GLN A 84  ? 0.2366 0.1178 0.2656 -0.0024 -0.0550 0.0176  102 GLN A O   
1256 C CB  . GLN A 84  ? 0.2284 0.1009 0.2418 0.0003  -0.0584 -0.0202 102 GLN A CB  
1257 C CG  . GLN A 84  ? 0.2124 0.0884 0.2672 0.0229  -0.0739 -0.0136 102 GLN A CG  
1258 C CD  . GLN A 84  ? 0.2292 0.0967 0.2674 0.0015  -0.0710 -0.0031 102 GLN A CD  
1259 O OE1 . GLN A 84  ? 0.2448 0.1096 0.2902 0.0021  -0.0507 -0.0056 102 GLN A OE1 
1260 N NE2 . GLN A 84  ? 0.2604 0.1154 0.2711 -0.0147 -0.0525 0.0009  102 GLN A NE2 
1269 N N   . VAL A 85  ? 0.2185 0.1003 0.2742 -0.0159 -0.0758 0.0068  103 VAL A N   
1270 C CA  . VAL A 85  ? 0.2383 0.1362 0.2837 -0.0131 -0.0638 0.0139  103 VAL A CA  
1271 C C   . VAL A 85  ? 0.2322 0.1404 0.2688 -0.0334 -0.0741 0.0060  103 VAL A C   
1272 O O   . VAL A 85  ? 0.2288 0.1374 0.2624 -0.0093 -0.0861 -0.0029 103 VAL A O   
1273 C CB  . VAL A 85  ? 0.2160 0.1436 0.2957 -0.0088 -0.0763 -0.0171 103 VAL A CB  
1274 C CG1 . VAL A 85  ? 0.2178 0.1828 0.3005 0.0167  -0.0893 -0.0069 103 VAL A CG1 
1275 C CG2 . VAL A 85  ? 0.2419 0.1414 0.2996 -0.0211 -0.0551 -0.0500 103 VAL A CG2 
1285 N N   . ASN A 86  ? 0.2400 0.1256 0.2395 -0.0379 -0.0801 0.0017  104 ASN A N   
1286 C CA  . ASN A 86  ? 0.2199 0.1243 0.2554 -0.0074 -0.0840 0.0021  104 ASN A CA  
1287 C C   . ASN A 86  ? 0.2103 0.1221 0.2551 0.0053  -0.0830 0.0087  104 ASN A C   
1288 O O   . ASN A 86  ? 0.2219 0.1165 0.2535 0.0192  -0.0750 0.0182  104 ASN A O   
1289 C CB  . ASN A 86  ? 0.2002 0.1200 0.2599 -0.0183 -0.0656 -0.0117 104 ASN A CB  
1290 C CG  . ASN A 86  ? 0.2056 0.1139 0.2533 0.0136  -0.0701 0.0030  104 ASN A CG  
1291 O OD1 . ASN A 86  ? 0.2362 0.1377 0.2717 -0.0088 -0.0721 0.0194  104 ASN A OD1 
1292 N ND2 . ASN A 86  ? 0.1968 0.1206 0.2465 -0.0130 -0.0760 0.0020  104 ASN A ND2 
1299 N N   . THR A 87  ? 0.2255 0.1289 0.2346 0.0005  -0.0729 0.0045  105 THR A N   
1300 C CA  . THR A 87  ? 0.2297 0.1060 0.2460 -0.0050 -0.0601 0.0097  105 THR A CA  
1301 C C   . THR A 87  ? 0.2448 0.1103 0.2582 0.0028  -0.0736 0.0014  105 THR A C   
1302 O O   . THR A 87  ? 0.2444 0.1092 0.2489 0.0112  -0.0798 -0.0061 105 THR A O   
1303 C CB  . THR A 87  ? 0.2343 0.1320 0.2598 0.0049  -0.0621 0.0256  105 THR A CB  
1304 O OG1 . THR A 87  ? 0.2363 0.1186 0.2729 0.0080  -0.0882 0.0062  105 THR A OG1 
1305 C CG2 . THR A 87  ? 0.2364 0.1705 0.2587 0.0281  -0.0506 0.0203  105 THR A CG2 
1313 N N   . GLU A 88  ? 0.2298 0.1203 0.2518 -0.0399 -0.0970 0.0071  106 GLU A N   
1314 C CA  . GLU A 88  ? 0.2256 0.1303 0.2560 -0.0218 -0.1028 0.0144  106 GLU A CA  
1315 C C   . GLU A 88  ? 0.2347 0.1462 0.2663 -0.0308 -0.0947 0.0065  106 GLU A C   
1316 O O   . GLU A 88  ? 0.2406 0.1591 0.2656 -0.0111 -0.0862 0.0086  106 GLU A O   
1317 C CB  . GLU A 88  ? 0.2626 0.1242 0.2625 -0.0277 -0.1114 0.0037  106 GLU A CB  
1318 C CG  . GLU A 88  ? 0.2708 0.1214 0.2869 -0.0487 -0.1061 0.0148  106 GLU A CG  
1319 C CD  . GLU A 88  ? 0.3021 0.1520 0.3240 -0.0408 -0.1148 0.0025  106 GLU A CD  
1320 O OE1 . GLU A 88  ? 0.2810 0.1626 0.3580 -0.0514 -0.0954 -0.0244 106 GLU A OE1 
1321 O OE2 . GLU A 88  ? 0.3340 0.1755 0.3338 -0.0135 -0.1043 0.0279  106 GLU A OE2 
1328 N N   . TYR A 89  ? 0.2205 0.1328 0.2403 -0.0176 -0.0842 0.0089  107 TYR A N   
1329 C CA  . TYR A 89  ? 0.2080 0.1375 0.2339 -0.0229 -0.0845 0.0061  107 TYR A CA  
1330 C C   . TYR A 89  ? 0.1866 0.1481 0.2148 -0.0334 -0.0680 0.0276  107 TYR A C   
1331 O O   . TYR A 89  ? 0.2708 0.1350 0.2244 -0.0136 -0.0742 0.0440  107 TYR A O   
1332 C CB  . TYR A 89  ? 0.2016 0.1578 0.2270 -0.0267 -0.0778 0.0167  107 TYR A CB  
1333 C CG  . TYR A 89  ? 0.1867 0.1535 0.2310 -0.0329 -0.0683 0.0080  107 TYR A CG  
1334 C CD1 . TYR A 89  ? 0.2095 0.1600 0.2304 -0.0202 -0.0750 0.0230  107 TYR A CD1 
1335 C CD2 . TYR A 89  ? 0.1992 0.1683 0.2706 -0.0322 -0.0513 0.0345  107 TYR A CD2 
1336 C CE1 . TYR A 89  ? 0.1893 0.1565 0.2455 -0.0207 -0.0821 0.0164  107 TYR A CE1 
1337 C CE2 . TYR A 89  ? 0.1894 0.1679 0.2790 -0.0145 -0.0664 0.0377  107 TYR A CE2 
1338 C CZ  . TYR A 89  ? 0.1954 0.1656 0.2814 -0.0195 -0.0607 0.0285  107 TYR A CZ  
1339 O OH  . TYR A 89  ? 0.2258 0.1796 0.3062 -0.0222 -0.0554 0.0241  107 TYR A OH  
1366 N N   . VAL A 91  ? 0.2454 0.1642 0.1971 0.0150  -0.0699 -0.0304 109 VAL A N   
1367 C CA  . VAL A 91  ? 0.2769 0.1359 0.2272 0.0242  -0.0783 -0.0016 109 VAL A CA  
1368 C C   . VAL A 91  ? 0.2531 0.1279 0.2554 -0.0007 -0.0966 0.0006  109 VAL A C   
1369 O O   . VAL A 91  ? 0.2660 0.1302 0.2732 -0.0036 -0.0780 0.0074  109 VAL A O   
1370 C CB  . VAL A 91  ? 0.2882 0.1188 0.2297 0.0108  -0.0671 0.0030  109 VAL A CB  
1371 C CG1 . VAL A 91  ? 0.3199 0.1227 0.2626 0.0298  -0.0309 -0.0012 109 VAL A CG1 
1372 C CG2 . VAL A 91  ? 0.2747 0.1405 0.2402 0.0090  -0.0544 -0.0137 109 VAL A CG2 
1382 N N   . ASN A 92  ? 0.2581 0.1163 0.2619 -0.0220 -0.1392 0.0079  110 ASN A N   
1383 C CA  . ASN A 92  ? 0.2668 0.1267 0.2639 -0.0089 -0.1372 0.0073  110 ASN A CA  
1384 C C   . ASN A 92  ? 0.3093 0.1288 0.2497 -0.0185 -0.1093 0.0039  110 ASN A C   
1385 O O   . ASN A 92  ? 0.3448 0.1430 0.2550 0.0009  -0.0950 0.0079  110 ASN A O   
1386 C CB  . ASN A 92  ? 0.2942 0.1650 0.2907 -0.0033 -0.1343 -0.0007 110 ASN A CB  
1387 C CG  . ASN A 92  ? 0.3399 0.1864 0.2963 0.0016  -0.1267 -0.0127 110 ASN A CG  
1388 O OD1 . ASN A 92  ? 0.3516 0.2203 0.2988 0.0126  -0.1161 -0.0113 110 ASN A OD1 
1389 N ND2 . ASN A 92  ? 0.3492 0.1615 0.2855 0.0010  -0.1510 -0.0244 110 ASN A ND2 
1396 N N   . ALA A 93  ? 0.2954 0.1155 0.2298 0.0048  -0.1080 -0.0001 111 ALA A N   
1397 C CA  . ALA A 93  ? 0.3051 0.1291 0.2485 0.0087  -0.0907 0.0067  111 ALA A CA  
1398 C C   . ALA A 93  ? 0.2822 0.1353 0.2483 0.0072  -0.0930 0.0032  111 ALA A C   
1399 O O   . ALA A 93  ? 0.2979 0.1348 0.2520 0.0257  -0.1038 0.0131  111 ALA A O   
1400 C CB  . ALA A 93  ? 0.3093 0.1382 0.2498 -0.0007 -0.1021 0.0257  111 ALA A CB  
1406 N N   . ILE A 94  ? 0.2701 0.1455 0.2449 -0.0131 -0.0956 -0.0040 112 ILE A N   
1407 C CA  . ILE A 94  ? 0.2643 0.1431 0.2271 0.0035  -0.0897 0.0166  112 ILE A CA  
1408 C C   . ILE A 94  ? 0.2884 0.1511 0.2332 0.0232  -0.0821 0.0060  112 ILE A C   
1409 O O   . ILE A 94  ? 0.2714 0.1650 0.2218 0.0140  -0.0822 0.0311  112 ILE A O   
1410 C CB  . ILE A 94  ? 0.2897 0.1460 0.2163 0.0112  -0.0560 0.0191  112 ILE A CB  
1411 C CG1 . ILE A 94  ? 0.2883 0.1627 0.2065 0.0044  -0.0739 0.0263  112 ILE A CG1 
1412 C CG2 . ILE A 94  ? 0.3458 0.1208 0.2161 0.0230  -0.0550 -0.0031 112 ILE A CG2 
1413 C CD1 . ILE A 94  ? 0.3291 0.2012 0.2476 0.0085  -0.0460 0.0149  112 ILE A CD1 
1425 N N   . THR A 95  ? 0.3128 0.1332 0.2300 0.0179  -0.1172 -0.0186 113 THR A N   
1426 C CA  . THR A 95  ? 0.3332 0.1362 0.2191 0.0124  -0.1274 -0.0148 113 THR A CA  
1427 C C   . THR A 95  ? 0.3075 0.1432 0.2237 0.0028  -0.1306 -0.0043 113 THR A C   
1428 O O   . THR A 95  ? 0.3356 0.1610 0.2259 0.0190  -0.1040 0.0207  113 THR A O   
1429 C CB  . THR A 95  ? 0.3507 0.1702 0.2383 0.0090  -0.1469 -0.0025 113 THR A CB  
1430 O OG1 . THR A 95  ? 0.3302 0.1823 0.2754 0.0317  -0.1137 0.0069  113 THR A OG1 
1431 C CG2 . THR A 95  ? 0.3856 0.1798 0.2200 0.0099  -0.1578 -0.0155 113 THR A CG2 
1439 N N   . ALA A 96  ? 0.2877 0.1450 0.2436 -0.0109 -0.1185 0.0079  114 ALA A N   
1440 C CA  . ALA A 96  ? 0.2723 0.1504 0.2358 0.0169  -0.1169 0.0183  114 ALA A CA  
1441 C C   . ALA A 96  ? 0.2760 0.1505 0.2255 0.0163  -0.1131 0.0227  114 ALA A C   
1442 O O   . ALA A 96  ? 0.2939 0.1582 0.2270 0.0229  -0.1083 0.0010  114 ALA A O   
1443 C CB  . ALA A 96  ? 0.3063 0.1521 0.2680 0.0091  -0.0851 0.0258  114 ALA A CB  
1449 N N   . LEU A 97  ? 0.2919 0.1390 0.1938 0.0155  -0.0995 0.0175  115 LEU A N   
1450 C CA  . LEU A 97  ? 0.2873 0.1358 0.2202 -0.0095 -0.1027 0.0110  115 LEU A CA  
1451 C C   . LEU A 97  ? 0.2994 0.1411 0.2119 0.0125  -0.1103 0.0444  115 LEU A C   
1452 O O   . LEU A 97  ? 0.3333 0.1394 0.2257 -0.0030 -0.0782 0.0410  115 LEU A O   
1453 C CB  . LEU A 97  ? 0.2997 0.1320 0.2285 0.0147  -0.0705 0.0157  115 LEU A CB  
1454 C CG  . LEU A 97  ? 0.2673 0.1299 0.2182 -0.0049 -0.0579 0.0050  115 LEU A CG  
1455 C CD1 . LEU A 97  ? 0.2771 0.1409 0.2088 -0.0443 -0.0498 0.0214  115 LEU A CD1 
1456 C CD2 . LEU A 97  ? 0.2582 0.1546 0.2401 0.0006  -0.0356 -0.0013 115 LEU A CD2 
1468 N N   . TYR A 98  ? 0.3189 0.1417 0.2098 0.0226  -0.0867 0.0499  116 TYR A N   
1469 C CA  . TYR A 98  ? 0.3227 0.1653 0.2003 0.0185  -0.1060 0.0521  116 TYR A CA  
1470 C C   . TYR A 98  ? 0.3609 0.1919 0.2073 0.0130  -0.0811 0.0467  116 TYR A C   
1471 O O   . TYR A 98  ? 0.3513 0.1893 0.2289 0.0340  -0.0734 0.0590  116 TYR A O   
1472 C CB  . TYR A 98  ? 0.3465 0.1631 0.2143 0.0183  -0.0836 0.0529  116 TYR A CB  
1473 C CG  . TYR A 98  ? 0.3439 0.1753 0.2111 -0.0129 -0.0871 0.0544  116 TYR A CG  
1474 C CD1 . TYR A 98  ? 0.3690 0.1769 0.2201 -0.0413 -0.0731 0.0442  116 TYR A CD1 
1475 C CD2 . TYR A 98  ? 0.3415 0.1987 0.2387 -0.0160 -0.0948 0.0510  116 TYR A CD2 
1476 C CE1 . TYR A 98  ? 0.3786 0.1967 0.2405 -0.0372 -0.0668 0.0371  116 TYR A CE1 
1477 C CE2 . TYR A 98  ? 0.3305 0.2094 0.2418 -0.0289 -0.1206 0.0540  116 TYR A CE2 
1478 C CZ  . TYR A 98  ? 0.3614 0.2254 0.2582 -0.0246 -0.0690 0.0644  116 TYR A CZ  
1479 O OH  . TYR A 98  ? 0.3372 0.2555 0.2865 -0.0112 -0.0593 0.0770  116 TYR A OH  
1489 N N   . ALA A 99  ? 0.3360 0.2106 0.2052 -0.0050 -0.1054 0.0227  117 ALA A N   
1490 C CA  . ALA A 99  ? 0.3472 0.2405 0.2255 0.0195  -0.1352 0.0258  117 ALA A CA  
1491 C C   . ALA A 99  ? 0.3531 0.2522 0.2316 0.0349  -0.1319 0.0387  117 ALA A C   
1492 O O   . ALA A 99  ? 0.3995 0.2789 0.2563 0.0658  -0.1139 0.0649  117 ALA A O   
1493 C CB  . ALA A 99  ? 0.3664 0.2371 0.2315 0.0457  -0.1243 0.0223  117 ALA A CB  
1499 N N   . GLY A 100 ? 0.3312 0.2342 0.2324 0.0228  -0.1208 0.0328  118 GLY A N   
1500 C CA  . GLY A 100 ? 0.3292 0.2184 0.2485 0.0184  -0.1020 0.0545  118 GLY A CA  
1501 C C   . GLY A 100 ? 0.3262 0.2159 0.2633 0.0317  -0.1046 0.0557  118 GLY A C   
1502 O O   . GLY A 100 ? 0.3255 0.2503 0.2797 0.0455  -0.0958 0.0631  118 GLY A O   
1506 N N   . SER A 101 ? 0.3226 0.2107 0.2654 0.0060  -0.0915 0.0626  119 SER A N   
1507 C CA  . SER A 101 ? 0.3093 0.2113 0.2802 0.0056  -0.0954 0.0727  119 SER A CA  
1508 C C   . SER A 101 ? 0.3381 0.2515 0.2853 -0.0393 -0.0866 0.0882  119 SER A C   
1509 O O   . SER A 101 ? 0.3815 0.2897 0.3030 -0.0873 -0.0783 0.0850  119 SER A O   
1510 C CB  . SER A 101 ? 0.3398 0.2023 0.2707 0.0193  -0.0939 0.0595  119 SER A CB  
1511 O OG  . SER A 101 ? 0.3416 0.1963 0.2637 -0.0054 -0.1273 0.0509  119 SER A OG  
1517 N N   . GLY A 102 ? 0.3353 0.2594 0.2928 -0.0231 -0.0924 0.0996  120 GLY A N   
1518 C CA  . GLY A 102 ? 0.3329 0.2583 0.2876 -0.0084 -0.0947 0.0717  120 GLY A CA  
1519 C C   . GLY A 102 ? 0.3640 0.2519 0.2856 -0.0031 -0.0676 0.0655  120 GLY A C   
1520 O O   . GLY A 102 ? 0.3699 0.2456 0.2975 -0.0119 -0.0456 0.0835  120 GLY A O   
1524 N N   . ASN A 103 ? 0.3414 0.2361 0.2581 -0.0116 -0.0869 0.0652  121 ASN A N   
1525 C CA  . ASN A 103 ? 0.3508 0.2486 0.2490 -0.0069 -0.0636 0.0478  121 ASN A CA  
1526 C C   . ASN A 103 ? 0.3545 0.2494 0.2516 -0.0141 -0.0651 0.0481  121 ASN A C   
1527 O O   . ASN A 103 ? 0.3608 0.2719 0.2801 -0.0087 -0.0568 0.0208  121 ASN A O   
1528 C CB  . ASN A 103 ? 0.3640 0.2515 0.2384 0.0015  -0.0648 0.0272  121 ASN A CB  
1529 C CG  . ASN A 103 ? 0.3651 0.2587 0.2411 0.0185  -0.0909 0.0131  121 ASN A CG  
1530 O OD1 . ASN A 103 ? 0.3491 0.2526 0.2393 0.0174  -0.1050 0.0044  121 ASN A OD1 
1531 N ND2 . ASN A 103 ? 0.3611 0.2667 0.2529 0.0351  -0.1102 -0.0043 121 ASN A ND2 
1538 N N   . ASN A 104 ? 0.3480 0.2370 0.2345 -0.0282 -0.0855 0.0874  122 ASN A N   
1539 C CA  . ASN A 104 ? 0.3643 0.2146 0.2526 -0.0378 -0.0885 0.0777  122 ASN A CA  
1540 C C   . ASN A 104 ? 0.3419 0.2090 0.2310 -0.0232 -0.0781 0.0626  122 ASN A C   
1541 O O   . ASN A 104 ? 0.3584 0.1954 0.2250 -0.0140 -0.0739 0.0378  122 ASN A O   
1542 C CB  . ASN A 104 ? 0.4042 0.2265 0.2935 -0.0590 -0.0777 0.0960  122 ASN A CB  
1543 C CG  . ASN A 104 ? 0.4168 0.2593 0.3219 -0.0804 -0.0930 0.1110  122 ASN A CG  
1544 O OD1 . ASN A 104 ? 0.4620 0.3015 0.3398 -0.0661 -0.0681 0.1282  122 ASN A OD1 
1545 N ND2 . ASN A 104 ? 0.4194 0.2609 0.3487 -0.0752 -0.1076 0.1052  122 ASN A ND2 
1552 N N   . LYS A 105 ? 0.3179 0.2212 0.2381 -0.0150 -0.0732 0.0548  123 LYS A N   
1553 C CA  . LYS A 105 ? 0.2793 0.2158 0.2202 -0.0124 -0.0647 0.0450  123 LYS A CA  
1554 C C   . LYS A 105 ? 0.2816 0.1835 0.2154 -0.0195 -0.0470 0.0328  123 LYS A C   
1555 O O   . LYS A 105 ? 0.2951 0.1946 0.2276 -0.0094 -0.0486 0.0175  123 LYS A O   
1556 C CB  . LYS A 105 ? 0.2875 0.2427 0.2339 -0.0064 -0.0614 0.0259  123 LYS A CB  
1557 C CG  . LYS A 105 ? 0.2992 0.2717 0.2562 0.0114  -0.0652 0.0123  123 LYS A CG  
1558 C CD  . LYS A 105 ? 0.3372 0.3023 0.3044 0.0038  -0.0379 -0.0106 123 LYS A CD  
1559 C CE  . LYS A 105 ? 0.3401 0.3085 0.3540 -0.0070 -0.0305 -0.0166 123 LYS A CE  
1560 N NZ  . LYS A 105 ? 0.3764 0.3297 0.3772 -0.0284 -0.0236 -0.0190 123 LYS A NZ  
1574 N N   . LEU A 106 ? 0.2896 0.1665 0.2063 -0.0178 -0.0402 0.0323  124 LEU A N   
1575 C CA  . LEU A 106 ? 0.3057 0.1576 0.2088 -0.0074 -0.0588 0.0312  124 LEU A CA  
1576 C C   . LEU A 106 ? 0.2835 0.1376 0.2085 -0.0022 -0.0414 0.0560  124 LEU A C   
1577 O O   . LEU A 106 ? 0.2696 0.1365 0.2069 -0.0341 -0.0610 0.0364  124 LEU A O   
1578 C CB  . LEU A 106 ? 0.3209 0.1648 0.2345 -0.0135 -0.0639 0.0273  124 LEU A CB  
1579 C CG  . LEU A 106 ? 0.3245 0.1969 0.2239 -0.0358 -0.0827 0.0173  124 LEU A CG  
1580 C CD1 . LEU A 106 ? 0.3624 0.2240 0.2309 -0.0192 -0.0808 0.0104  124 LEU A CD1 
1581 C CD2 . LEU A 106 ? 0.3458 0.2202 0.2213 -0.0386 -0.0719 0.0172  124 LEU A CD2 
1593 N N   . PRO A 107 ? 0.2597 0.1355 0.2194 0.0070  -0.0425 0.0551  125 PRO A N   
1594 C CA  . PRO A 107 ? 0.2490 0.1272 0.2182 -0.0141 -0.0496 0.0477  125 PRO A CA  
1595 C C   . PRO A 107 ? 0.2452 0.1377 0.2000 0.0064  -0.0594 0.0535  125 PRO A C   
1596 O O   . PRO A 107 ? 0.2392 0.1470 0.1918 0.0011  -0.0594 0.0429  125 PRO A O   
1597 C CB  . PRO A 107 ? 0.2254 0.1205 0.2281 -0.0179 -0.0747 0.0284  125 PRO A CB  
1598 C CG  . PRO A 107 ? 0.2342 0.1236 0.2298 -0.0184 -0.0768 0.0238  125 PRO A CG  
1599 C CD  . PRO A 107 ? 0.2462 0.1164 0.2246 -0.0061 -0.0427 0.0423  125 PRO A CD  
1607 N N   . VAL A 108 ? 0.2317 0.1331 0.2148 -0.0224 -0.0670 0.0326  126 VAL A N   
1608 C CA  . VAL A 108 ? 0.2113 0.1386 0.2079 -0.0002 -0.0600 0.0104  126 VAL A CA  
1609 C C   . VAL A 108 ? 0.1872 0.1278 0.2018 -0.0013 -0.0470 0.0164  126 VAL A C   
1610 O O   . VAL A 108 ? 0.1911 0.1401 0.2058 -0.0004 -0.0551 0.0120  126 VAL A O   
1611 C CB  . VAL A 108 ? 0.2353 0.1513 0.2193 -0.0069 -0.0587 0.0319  126 VAL A CB  
1612 C CG1 . VAL A 108 ? 0.2280 0.1471 0.2071 0.0054  -0.0452 0.0475  126 VAL A CG1 
1613 C CG2 . VAL A 108 ? 0.2529 0.1721 0.2266 -0.0116 -0.0572 0.0076  126 VAL A CG2 
1623 N N   . LEU A 109 ? 0.2055 0.1290 0.2119 -0.0204 -0.0542 0.0201  127 LEU A N   
1624 C CA  . LEU A 109 ? 0.2097 0.1029 0.1904 -0.0112 -0.0690 0.0163  127 LEU A CA  
1625 C C   . LEU A 109 ? 0.1974 0.1224 0.1974 -0.0047 -0.0808 0.0207  127 LEU A C   
1626 O O   . LEU A 109 ? 0.1967 0.1159 0.2121 -0.0071 -0.0678 0.0110  127 LEU A O   
1627 C CB  . LEU A 109 ? 0.2096 0.0972 0.1961 0.0030  -0.0656 0.0212  127 LEU A CB  
1628 C CG  . LEU A 109 ? 0.2384 0.0907 0.2161 0.0028  -0.0812 0.0205  127 LEU A CG  
1629 C CD1 . LEU A 109 ? 0.2542 0.0863 0.2346 0.0189  -0.0489 0.0228  127 LEU A CD1 
1630 C CD2 . LEU A 109 ? 0.2770 0.1075 0.2331 -0.0085 -0.0654 0.0299  127 LEU A CD2 
1642 N N   . THR A 110 ? 0.2056 0.1248 0.1734 -0.0163 -0.0538 0.0049  128 THR A N   
1643 C CA  . THR A 110 ? 0.2086 0.1135 0.1956 -0.0310 -0.0538 0.0129  128 THR A CA  
1644 C C   . THR A 110 ? 0.1943 0.1012 0.1987 -0.0103 -0.0608 0.0363  128 THR A C   
1645 O O   . THR A 110 ? 0.2057 0.0956 0.1933 -0.0028 -0.0431 0.0237  128 THR A O   
1646 C CB  . THR A 110 ? 0.1936 0.1161 0.2133 -0.0239 -0.0567 0.0101  128 THR A CB  
1647 O OG1 . THR A 110 ? 0.2086 0.1107 0.2043 -0.0221 -0.0417 0.0144  128 THR A OG1 
1648 C CG2 . THR A 110 ? 0.2121 0.1356 0.2420 -0.0387 -0.0463 0.0112  128 THR A CG2 
1656 N N   . TRP A 111 ? 0.1875 0.1164 0.2074 -0.0273 -0.0707 0.0412  129 TRP A N   
1657 C CA  . TRP A 111 ? 0.1856 0.1021 0.1873 -0.0203 -0.0788 0.0303  129 TRP A CA  
1658 C C   . TRP A 111 ? 0.2202 0.1118 0.1862 -0.0207 -0.0782 0.0280  129 TRP A C   
1659 O O   . TRP A 111 ? 0.2260 0.1109 0.1915 -0.0421 -0.0690 0.0051  129 TRP A O   
1660 C CB  . TRP A 111 ? 0.1822 0.1268 0.1951 -0.0122 -0.0776 0.0268  129 TRP A CB  
1661 C CG  . TRP A 111 ? 0.1934 0.1048 0.1878 -0.0102 -0.0617 0.0079  129 TRP A CG  
1662 C CD1 . TRP A 111 ? 0.2061 0.1147 0.1876 -0.0015 -0.0445 0.0149  129 TRP A CD1 
1663 C CD2 . TRP A 111 ? 0.2045 0.1103 0.1980 -0.0063 -0.0641 0.0059  129 TRP A CD2 
1664 N NE1 . TRP A 111 ? 0.1979 0.1228 0.1890 -0.0039 -0.0547 -0.0151 129 TRP A NE1 
1665 C CE2 . TRP A 111 ? 0.2036 0.1190 0.1905 0.0042  -0.0500 0.0007  129 TRP A CE2 
1666 C CE3 . TRP A 111 ? 0.2187 0.1242 0.2085 -0.0141 -0.0451 0.0159  129 TRP A CE3 
1667 C CZ2 . TRP A 111 ? 0.2281 0.1332 0.2081 -0.0116 -0.0523 0.0471  129 TRP A CZ2 
1668 C CZ3 . TRP A 111 ? 0.2152 0.1438 0.2295 -0.0197 -0.0551 0.0408  129 TRP A CZ3 
1669 C CH2 . TRP A 111 ? 0.2256 0.1529 0.2236 -0.0105 -0.0308 0.0422  129 TRP A CH2 
1680 N N   . SER A 112 ? 0.2130 0.1229 0.2045 -0.0045 -0.0560 0.0291  130 SER A N   
1681 C CA  . SER A 112 ? 0.2371 0.1215 0.2162 -0.0140 -0.0580 0.0238  130 SER A CA  
1682 C C   . SER A 112 ? 0.2138 0.1132 0.2295 -0.0089 -0.0443 0.0227  130 SER A C   
1683 O O   . SER A 112 ? 0.2179 0.1291 0.2542 -0.0235 -0.0782 0.0341  130 SER A O   
1684 C CB  . SER A 112 ? 0.3289 0.1177 0.2278 -0.0323 -0.0365 0.0399  130 SER A CB  
1685 O OG  . SER A 112 ? 0.4718 0.1552 0.2693 -0.0317 0.0445  0.0515  130 SER A OG  
1691 N N   . GLN A 113 ? 0.2014 0.0997 0.2436 0.0027  -0.0373 0.0140  131 GLN A N   
1692 C CA  . GLN A 113 ? 0.1781 0.1077 0.2434 -0.0064 -0.0585 0.0083  131 GLN A CA  
1693 C C   . GLN A 113 ? 0.1594 0.1047 0.2384 -0.0032 -0.0514 0.0224  131 GLN A C   
1694 O O   . GLN A 113 ? 0.1809 0.1194 0.2680 -0.0164 -0.0290 0.0150  131 GLN A O   
1695 C CB  . GLN A 113 ? 0.2073 0.1004 0.2608 -0.0031 -0.0383 0.0108  131 GLN A CB  
1696 C CG  . GLN A 113 ? 0.1925 0.0886 0.2702 -0.0077 -0.0417 0.0026  131 GLN A CG  
1697 C CD  . GLN A 113 ? 0.2104 0.1175 0.2667 -0.0071 -0.0345 0.0066  131 GLN A CD  
1698 O OE1 . GLN A 113 ? 0.2335 0.1320 0.2781 -0.0249 -0.0454 0.0003  131 GLN A OE1 
1699 N NE2 . GLN A 113 ? 0.2045 0.1318 0.2821 -0.0240 -0.0532 0.0079  131 GLN A NE2 
1708 N N   . GLY A 114 ? 0.1692 0.0964 0.2293 -0.0040 -0.0507 0.0046  132 GLY A N   
1709 C CA  . GLY A 114 ? 0.1789 0.1128 0.2256 0.0025  -0.0605 0.0092  132 GLY A CA  
1710 C C   . GLY A 114 ? 0.1883 0.1203 0.2095 0.0099  -0.0632 0.0060  132 GLY A C   
1711 O O   . GLY A 114 ? 0.2018 0.1274 0.2108 -0.0098 -0.0489 -0.0095 132 GLY A O   
1715 N N   . GLY A 115 ? 0.1833 0.1101 0.2389 0.0057  -0.0583 0.0123  133 GLY A N   
1716 C CA  . GLY A 115 ? 0.1995 0.1119 0.2107 0.0062  -0.0432 0.0057  133 GLY A CA  
1717 C C   . GLY A 115 ? 0.2032 0.1173 0.2007 0.0170  -0.0362 0.0037  133 GLY A C   
1718 O O   . GLY A 115 ? 0.1909 0.1319 0.1939 -0.0253 -0.0497 0.0022  133 GLY A O   
1722 N N   . LEU A 116 ? 0.2010 0.0997 0.2010 0.0048  -0.0452 -0.0061 134 LEU A N   
1723 C CA  . LEU A 116 ? 0.1975 0.0931 0.2001 -0.0132 -0.0654 -0.0027 134 LEU A CA  
1724 C C   . LEU A 116 ? 0.2021 0.1026 0.1957 -0.0117 -0.0659 -0.0069 134 LEU A C   
1725 O O   . LEU A 116 ? 0.2271 0.1137 0.2042 -0.0061 -0.0580 0.0021  134 LEU A O   
1726 C CB  . LEU A 116 ? 0.1985 0.1157 0.2094 -0.0235 -0.0390 0.0056  134 LEU A CB  
1727 C CG  . LEU A 116 ? 0.2004 0.1312 0.2230 -0.0191 -0.0431 0.0006  134 LEU A CG  
1728 C CD1 . LEU A 116 ? 0.2062 0.1407 0.2559 -0.0059 -0.0343 0.0027  134 LEU A CD1 
1729 C CD2 . LEU A 116 ? 0.2248 0.1436 0.2260 -0.0286 -0.0643 0.0172  134 LEU A CD2 
1741 N N   . VAL A 117 ? 0.1857 0.1116 0.2011 -0.0183 -0.0574 -0.0093 135 VAL A N   
1742 C CA  . VAL A 117 ? 0.2061 0.1151 0.2353 -0.0338 -0.0636 0.0194  135 VAL A CA  
1743 C C   . VAL A 117 ? 0.2193 0.1310 0.2188 -0.0137 -0.0683 0.0161  135 VAL A C   
1744 O O   . VAL A 117 ? 0.2396 0.1413 0.2274 -0.0081 -0.0701 0.0153  135 VAL A O   
1745 C CB  . VAL A 117 ? 0.1981 0.1126 0.2529 -0.0323 -0.0641 -0.0012 135 VAL A CB  
1746 C CG1 . VAL A 117 ? 0.1844 0.1527 0.2736 -0.0341 -0.0910 -0.0094 135 VAL A CG1 
1747 C CG2 . VAL A 117 ? 0.2259 0.1443 0.2811 -0.0435 -0.0433 0.0087  135 VAL A CG2 
1757 N N   . ALA A 118 ? 0.2240 0.1355 0.2219 -0.0051 -0.0762 0.0132  136 ALA A N   
1758 C CA  . ALA A 118 ? 0.2479 0.1179 0.2159 0.0040  -0.0565 0.0057  136 ALA A CA  
1759 C C   . ALA A 118 ? 0.2451 0.1340 0.2061 -0.0156 -0.0567 0.0013  136 ALA A C   
1760 O O   . ALA A 118 ? 0.2436 0.1362 0.2216 -0.0087 -0.0457 0.0121  136 ALA A O   
1761 C CB  . ALA A 118 ? 0.2730 0.1314 0.2179 -0.0197 -0.0561 -0.0065 136 ALA A CB  
1767 N N   . GLN A 119 ? 0.2343 0.1258 0.2029 -0.0125 -0.0496 -0.0122 137 GLN A N   
1768 C CA  . GLN A 119 ? 0.2231 0.1453 0.1982 -0.0111 -0.0380 0.0082  137 GLN A CA  
1769 C C   . GLN A 119 ? 0.2133 0.1278 0.1799 0.0001  -0.0153 0.0182  137 GLN A C   
1770 O O   . GLN A 119 ? 0.2269 0.1458 0.2053 0.0042  -0.0368 0.0142  137 GLN A O   
1771 C CB  . GLN A 119 ? 0.2520 0.1743 0.2029 -0.0032 -0.0460 0.0149  137 GLN A CB  
1772 C CG  . GLN A 119 ? 0.2272 0.1977 0.2204 -0.0137 -0.0386 0.0145  137 GLN A CG  
1773 C CD  . GLN A 119 ? 0.2074 0.1840 0.2213 -0.0152 -0.0577 0.0282  137 GLN A CD  
1774 O OE1 . GLN A 119 ? 0.2132 0.1803 0.2495 -0.0162 -0.0057 -0.0007 137 GLN A OE1 
1775 N NE2 . GLN A 119 ? 0.2060 0.1983 0.2375 -0.0238 -0.0778 0.0414  137 GLN A NE2 
1784 N N   . TRP A 120 ? 0.2431 0.1212 0.1914 -0.0109 -0.0117 0.0078  138 TRP A N   
1785 C CA  . TRP A 120 ? 0.2350 0.1373 0.1943 -0.0150 -0.0424 0.0077  138 TRP A CA  
1786 C C   . TRP A 120 ? 0.2265 0.1333 0.1956 -0.0203 -0.0423 -0.0015 138 TRP A C   
1787 O O   . TRP A 120 ? 0.2787 0.1339 0.1970 -0.0387 -0.0288 -0.0189 138 TRP A O   
1788 C CB  . TRP A 120 ? 0.2541 0.1364 0.2082 -0.0040 -0.0213 0.0217  138 TRP A CB  
1789 C CG  . TRP A 120 ? 0.2245 0.1269 0.1953 0.0051  -0.0545 0.0193  138 TRP A CG  
1790 C CD1 . TRP A 120 ? 0.2384 0.1378 0.2167 -0.0100 -0.0462 0.0087  138 TRP A CD1 
1791 C CD2 . TRP A 120 ? 0.1945 0.1217 0.2102 -0.0046 -0.0548 0.0115  138 TRP A CD2 
1792 N NE1 . TRP A 120 ? 0.2368 0.1203 0.2025 -0.0172 -0.0406 0.0265  138 TRP A NE1 
1793 C CE2 . TRP A 120 ? 0.2216 0.1061 0.2228 0.0082  -0.0546 0.0100  138 TRP A CE2 
1794 C CE3 . TRP A 120 ? 0.2106 0.1225 0.2204 -0.0059 -0.0650 0.0248  138 TRP A CE3 
1795 C CZ2 . TRP A 120 ? 0.2252 0.1120 0.2429 -0.0032 -0.0581 0.0043  138 TRP A CZ2 
1796 C CZ3 . TRP A 120 ? 0.2254 0.1186 0.2506 -0.0101 -0.0805 0.0165  138 TRP A CZ3 
1797 C CH2 . TRP A 120 ? 0.2230 0.1163 0.2433 0.0091  -0.0762 -0.0008 138 TRP A CH2 
1808 N N   . GLY A 121 ? 0.2493 0.1310 0.1928 -0.0218 -0.0646 0.0035  139 GLY A N   
1809 C CA  . GLY A 121 ? 0.2662 0.1415 0.2214 -0.0131 -0.0524 0.0319  139 GLY A CA  
1810 C C   . GLY A 121 ? 0.2592 0.1325 0.2330 -0.0168 -0.0617 0.0235  139 GLY A C   
1811 O O   . GLY A 121 ? 0.2557 0.1334 0.2358 -0.0226 -0.0666 0.0147  139 GLY A O   
1815 N N   . LEU A 122 ? 0.2353 0.1277 0.2384 -0.0282 -0.0621 0.0178  140 LEU A N   
1816 C CA  . LEU A 122 ? 0.2476 0.1251 0.2435 -0.0289 -0.0293 0.0185  140 LEU A CA  
1817 C C   . LEU A 122 ? 0.2443 0.1399 0.2231 0.0032  -0.0518 0.0133  140 LEU A C   
1818 O O   . LEU A 122 ? 0.2910 0.1603 0.2207 -0.0139 -0.0489 0.0213  140 LEU A O   
1819 C CB  . LEU A 122 ? 0.2591 0.1379 0.2403 -0.0307 -0.0497 0.0249  140 LEU A CB  
1820 C CG  . LEU A 122 ? 0.2870 0.1454 0.2394 -0.0142 -0.0425 0.0265  140 LEU A CG  
1821 C CD1 . LEU A 122 ? 0.3026 0.1525 0.2474 -0.0424 -0.0432 0.0138  140 LEU A CD1 
1822 C CD2 . LEU A 122 ? 0.3105 0.1563 0.2520 -0.0096 -0.0219 0.0187  140 LEU A CD2 
1834 N N   . THR A 123 ? 0.2620 0.1327 0.2156 -0.0033 -0.0358 0.0114  141 THR A N   
1835 C CA  . THR A 123 ? 0.2573 0.1451 0.2009 0.0030  -0.0480 0.0145  141 THR A CA  
1836 C C   . THR A 123 ? 0.2609 0.1524 0.2061 0.0185  -0.0234 0.0141  141 THR A C   
1837 O O   . THR A 123 ? 0.2747 0.1719 0.2144 0.0070  -0.0105 -0.0162 141 THR A O   
1838 C CB  . THR A 123 ? 0.2545 0.1435 0.2211 -0.0042 -0.0457 -0.0097 141 THR A CB  
1839 O OG1 . THR A 123 ? 0.2552 0.1449 0.2254 -0.0088 -0.0386 -0.0067 141 THR A OG1 
1840 C CG2 . THR A 123 ? 0.2524 0.1649 0.2405 0.0150  -0.0199 -0.0176 141 THR A CG2 
1848 N N   . PHE A 124 ? 0.2494 0.1547 0.1938 0.0244  -0.0351 0.0039  142 PHE A N   
1849 C CA  . PHE A 124 ? 0.2472 0.1531 0.2171 -0.0062 -0.0711 0.0071  142 PHE A CA  
1850 C C   . PHE A 124 ? 0.3026 0.1426 0.2210 0.0070  -0.0707 -0.0049 142 PHE A C   
1851 O O   . PHE A 124 ? 0.3366 0.1352 0.2238 -0.0198 -0.0606 -0.0039 142 PHE A O   
1852 C CB  . PHE A 124 ? 0.2283 0.1579 0.2373 -0.0121 -0.0588 -0.0022 142 PHE A CB  
1853 C CG  . PHE A 124 ? 0.2256 0.1582 0.2293 -0.0223 -0.0401 0.0042  142 PHE A CG  
1854 C CD1 . PHE A 124 ? 0.2344 0.1634 0.2421 -0.0162 -0.0347 0.0079  142 PHE A CD1 
1855 C CD2 . PHE A 124 ? 0.2165 0.1510 0.2366 -0.0130 -0.0376 0.0044  142 PHE A CD2 
1856 C CE1 . PHE A 124 ? 0.2309 0.1534 0.2533 -0.0042 -0.0347 0.0094  142 PHE A CE1 
1857 C CE2 . PHE A 124 ? 0.2266 0.1530 0.2397 -0.0086 -0.0367 0.0056  142 PHE A CE2 
1858 C CZ  . PHE A 124 ? 0.2425 0.1609 0.2468 -0.0146 -0.0391 0.0143  142 PHE A CZ  
1868 N N   . PHE A 125 ? 0.3077 0.1588 0.2319 0.0339  -0.0738 0.0014  143 PHE A N   
1869 C CA  . PHE A 125 ? 0.3027 0.1544 0.2175 0.0118  -0.0818 -0.0028 143 PHE A CA  
1870 C C   . PHE A 125 ? 0.3327 0.1476 0.2226 -0.0033 -0.0510 0.0029  143 PHE A C   
1871 O O   . PHE A 125 ? 0.3455 0.1283 0.2121 0.0164  -0.0464 -0.0056 143 PHE A O   
1872 C CB  . PHE A 125 ? 0.3052 0.1389 0.2426 -0.0019 -0.0618 -0.0135 143 PHE A CB  
1873 C CG  . PHE A 125 ? 0.2904 0.1551 0.2650 -0.0159 -0.0664 -0.0168 143 PHE A CG  
1874 C CD1 . PHE A 125 ? 0.2897 0.1613 0.2669 -0.0140 -0.0731 -0.0233 143 PHE A CD1 
1875 C CD2 . PHE A 125 ? 0.3136 0.1717 0.2711 -0.0296 -0.0933 -0.0141 143 PHE A CD2 
1876 C CE1 . PHE A 125 ? 0.3106 0.1643 0.2690 -0.0131 -0.0771 -0.0063 143 PHE A CE1 
1877 C CE2 . PHE A 125 ? 0.3122 0.1840 0.2844 -0.0464 -0.0924 -0.0045 143 PHE A CE2 
1878 C CZ  . PHE A 125 ? 0.3121 0.1784 0.2886 -0.0370 -0.0773 -0.0023 143 PHE A CZ  
1888 N N   . PRO A 126 ? 0.3374 0.1548 0.2334 -0.0087 -0.0652 -0.0067 144 PRO A N   
1889 C CA  . PRO A 126 ? 0.3260 0.1584 0.2460 -0.0135 -0.0386 0.0196  144 PRO A CA  
1890 C C   . PRO A 126 ? 0.3241 0.1684 0.2500 0.0091  -0.0549 0.0148  144 PRO A C   
1891 O O   . PRO A 126 ? 0.3185 0.1975 0.2634 -0.0057 -0.0600 0.0277  144 PRO A O   
1892 C CB  . PRO A 126 ? 0.3326 0.1617 0.2531 -0.0283 -0.0417 0.0143  144 PRO A CB  
1893 C CG  . PRO A 126 ? 0.3330 0.1767 0.2384 -0.0260 -0.0501 0.0124  144 PRO A CG  
1894 C CD  . PRO A 126 ? 0.3435 0.1796 0.2315 -0.0150 -0.0607 -0.0150 144 PRO A CD  
1902 N N   . SER A 127 ? 0.3254 0.1582 0.2502 0.0216  -0.0630 -0.0025 145 SER A N   
1903 C CA  . SER A 127 ? 0.3306 0.1684 0.2415 0.0193  -0.0604 0.0047  145 SER A CA  
1904 C C   . SER A 127 ? 0.3493 0.1719 0.2442 0.0062  -0.0729 0.0111  145 SER A C   
1905 O O   . SER A 127 ? 0.3872 0.1764 0.2489 0.0071  -0.0346 0.0235  145 SER A O   
1906 C CB  . SER A 127 ? 0.3270 0.2031 0.2607 0.0344  -0.0431 0.0068  145 SER A CB  
1907 O OG  . SER A 127 ? 0.3170 0.2204 0.2873 0.0008  -0.0326 0.0007  145 SER A OG  
1913 N N   . ILE A 128 ? 0.3536 0.1639 0.2510 -0.0045 -0.0692 0.0111  146 ILE A N   
1914 C CA  . ILE A 128 ? 0.3499 0.1492 0.2334 -0.0216 -0.0618 -0.0096 146 ILE A CA  
1915 C C   . ILE A 128 ? 0.3272 0.1542 0.2212 -0.0156 -0.0699 0.0204  146 ILE A C   
1916 O O   . ILE A 128 ? 0.3559 0.1537 0.2189 -0.0226 -0.0550 0.0311  146 ILE A O   
1917 C CB  . ILE A 128 ? 0.3419 0.1399 0.2477 0.0000  -0.0360 0.0029  146 ILE A CB  
1918 C CG1 . ILE A 128 ? 0.3564 0.1566 0.2429 0.0086  -0.0083 0.0063  146 ILE A CG1 
1919 C CG2 . ILE A 128 ? 0.3439 0.1464 0.2638 0.0129  -0.0396 -0.0111 146 ILE A CG2 
1920 C CD1 . ILE A 128 ? 0.3469 0.1559 0.2452 -0.0054 -0.0418 -0.0012 146 ILE A CD1 
1932 N N   . ARG A 129 ? 0.3345 0.1756 0.2277 -0.0219 -0.0592 0.0065  147 ARG A N   
1933 C CA  . ARG A 129 ? 0.3573 0.1825 0.2367 -0.0164 -0.0699 0.0103  147 ARG A CA  
1934 C C   . ARG A 129 ? 0.4099 0.1874 0.2553 -0.0251 -0.0648 0.0178  147 ARG A C   
1935 O O   . ARG A 129 ? 0.4614 0.2015 0.2699 -0.0247 -0.0755 0.0383  147 ARG A O   
1936 C CB  . ARG A 129 ? 0.3507 0.1667 0.2387 -0.0053 -0.0441 0.0102  147 ARG A CB  
1937 C CG  . ARG A 129 ? 0.3274 0.1776 0.2386 -0.0221 -0.0272 0.0168  147 ARG A CG  
1938 C CD  . ARG A 129 ? 0.3086 0.1743 0.2241 -0.0231 -0.0378 0.0264  147 ARG A CD  
1939 N NE  . ARG A 129 ? 0.2797 0.1676 0.2206 -0.0323 -0.0327 0.0082  147 ARG A NE  
1940 C CZ  . ARG A 129 ? 0.2749 0.1935 0.2299 0.0168  -0.0212 0.0080  147 ARG A CZ  
1941 N NH1 . ARG A 129 ? 0.2993 0.2199 0.2618 0.0044  -0.0135 0.0133  147 ARG A NH1 
1942 N NH2 . ARG A 129 ? 0.2781 0.2112 0.2218 0.0185  -0.0196 0.0250  147 ARG A NH2 
1956 N N   . SER A 130 ? 0.4229 0.1922 0.2518 -0.0346 -0.0481 0.0168  148 SER A N   
1957 C CA  . SER A 130 ? 0.4530 0.1868 0.2540 -0.0176 -0.0340 0.0228  148 SER A CA  
1958 C C   . SER A 130 ? 0.4237 0.1750 0.2601 -0.0035 -0.0205 0.0308  148 SER A C   
1959 O O   . SER A 130 ? 0.4659 0.1859 0.2962 0.0068  -0.0065 0.0369  148 SER A O   
1960 C CB  . SER A 130 ? 0.4932 0.2051 0.2573 -0.0232 -0.0206 0.0161  148 SER A CB  
1961 O OG  . SER A 130 ? 0.5365 0.2283 0.2477 -0.0203 -0.0300 0.0082  148 SER A OG  
1967 N N   . LYS A 131 ? 0.3483 0.1535 0.2327 -0.0070 -0.0554 0.0260  149 LYS A N   
1968 C CA  . LYS A 131 ? 0.3305 0.1571 0.2224 -0.0121 -0.0894 0.0179  149 LYS A CA  
1969 C C   . LYS A 131 ? 0.3174 0.1576 0.2391 -0.0058 -0.0831 0.0190  149 LYS A C   
1970 O O   . LYS A 131 ? 0.3388 0.1813 0.2691 0.0170  -0.0843 0.0279  149 LYS A O   
1971 C CB  . LYS A 131 ? 0.3265 0.1627 0.2228 -0.0044 -0.1069 0.0123  149 LYS A CB  
1972 C CG  . LYS A 131 ? 0.3598 0.1643 0.2193 -0.0134 -0.1020 0.0100  149 LYS A CG  
1973 C CD  . LYS A 131 ? 0.3611 0.1776 0.2349 -0.0034 -0.1179 -0.0024 149 LYS A CD  
1974 C CE  . LYS A 131 ? 0.3768 0.2008 0.2559 -0.0124 -0.1118 -0.0109 149 LYS A CE  
1975 N NZ  . LYS A 131 ? 0.3861 0.2208 0.2938 -0.0277 -0.0751 -0.0211 149 LYS A NZ  
1989 N N   . VAL A 132 ? 0.3196 0.1699 0.2323 0.0084  -0.0913 0.0284  150 VAL A N   
1990 C CA  . VAL A 132 ? 0.2957 0.1695 0.2402 -0.0131 -0.0710 0.0393  150 VAL A CA  
1991 C C   . VAL A 132 ? 0.3096 0.1814 0.2416 0.0031  -0.0768 0.0298  150 VAL A C   
1992 O O   . VAL A 132 ? 0.3209 0.2093 0.2641 0.0057  -0.0597 0.0265  150 VAL A O   
1993 C CB  . VAL A 132 ? 0.2573 0.1525 0.2543 -0.0351 -0.0700 0.0278  150 VAL A CB  
1994 C CG1 . VAL A 132 ? 0.2963 0.1508 0.2674 -0.0267 -0.0732 0.0301  150 VAL A CG1 
1995 C CG2 . VAL A 132 ? 0.2777 0.1720 0.2554 -0.0169 -0.0728 0.0062  150 VAL A CG2 
2005 N N   . ASP A 133 ? 0.3043 0.1717 0.2552 0.0204  -0.0457 0.0311  151 ASP A N   
2006 C CA  . ASP A 133 ? 0.3024 0.1975 0.2643 -0.0038 -0.0692 0.0347  151 ASP A CA  
2007 C C   . ASP A 133 ? 0.2897 0.1885 0.2386 -0.0228 -0.0454 0.0412  151 ASP A C   
2008 O O   . ASP A 133 ? 0.3145 0.1931 0.2442 -0.0014 -0.0171 0.0349  151 ASP A O   
2009 C CB  . ASP A 133 ? 0.3309 0.2099 0.2971 -0.0020 -0.0673 0.0443  151 ASP A CB  
2010 C CG  . ASP A 133 ? 0.3441 0.2051 0.3127 -0.0200 -0.0463 0.0687  151 ASP A CG  
2011 O OD1 . ASP A 133 ? 0.3552 0.2082 0.3246 -0.0463 -0.0147 0.0717  151 ASP A OD1 
2012 O OD2 . ASP A 133 ? 0.3519 0.1960 0.3283 -0.0246 -0.0257 0.0695  151 ASP A OD2 
2017 N N   . ARG A 134 ? 0.2493 0.1783 0.2323 -0.0222 -0.0361 0.0335  152 ARG A N   
2018 C CA  . ARG A 134 ? 0.2142 0.1714 0.2244 -0.0302 -0.0414 0.0269  152 ARG A CA  
2019 C C   . ARG A 134 ? 0.2255 0.1543 0.2261 -0.0164 -0.0367 0.0205  152 ARG A C   
2020 O O   . ARG A 134 ? 0.2356 0.1629 0.2331 -0.0144 -0.0441 0.0246  152 ARG A O   
2021 C CB  . ARG A 134 ? 0.2201 0.1726 0.2260 -0.0369 -0.0552 0.0109  152 ARG A CB  
2022 C CG  . ARG A 134 ? 0.2508 0.1710 0.2305 -0.0544 -0.0299 0.0136  152 ARG A CG  
2023 C CD  . ARG A 134 ? 0.2723 0.1815 0.2270 -0.0481 -0.0185 0.0243  152 ARG A CD  
2024 N NE  . ARG A 134 ? 0.2877 0.1854 0.2346 -0.0112 -0.0121 0.0542  152 ARG A NE  
2025 C CZ  . ARG A 134 ? 0.3142 0.1836 0.2427 -0.0059 -0.0280 0.0557  152 ARG A CZ  
2026 N NH1 . ARG A 134 ? 0.2835 0.1846 0.2461 -0.0102 -0.0462 0.0589  152 ARG A NH1 
2027 N NH2 . ARG A 134 ? 0.3516 0.2065 0.2535 0.0057  -0.0070 0.0435  152 ARG A NH2 
2041 N N   . LEU A 135 ? 0.2160 0.1283 0.2133 -0.0194 -0.0483 0.0136  153 LEU A N   
2042 C CA  . LEU A 135 ? 0.2214 0.1265 0.2146 -0.0108 -0.0516 0.0324  153 LEU A CA  
2043 C C   . LEU A 135 ? 0.2199 0.1185 0.2165 -0.0074 -0.0480 0.0207  153 LEU A C   
2044 O O   . LEU A 135 ? 0.2248 0.1247 0.2392 0.0000  -0.0720 0.0202  153 LEU A O   
2045 C CB  . LEU A 135 ? 0.2270 0.1311 0.2251 -0.0178 -0.0660 0.0067  153 LEU A CB  
2046 C CG  . LEU A 135 ? 0.2093 0.1369 0.2471 -0.0428 -0.0702 -0.0154 153 LEU A CG  
2047 C CD1 . LEU A 135 ? 0.1943 0.1513 0.2354 -0.0332 -0.0638 -0.0055 153 LEU A CD1 
2048 C CD2 . LEU A 135 ? 0.2343 0.1350 0.2677 -0.0302 -0.0688 -0.0069 153 LEU A CD2 
2060 N N   . MET A 136 ? 0.2020 0.1143 0.2060 -0.0102 -0.0504 -0.0027 154 MET A N   
2061 C CA  . MET A 136 ? 0.1919 0.1124 0.2162 -0.0104 -0.0390 0.0069  154 MET A CA  
2062 C C   . MET A 136 ? 0.1958 0.1090 0.2050 0.0155  -0.0423 0.0162  154 MET A C   
2063 O O   . MET A 136 ? 0.2163 0.1288 0.2042 0.0125  -0.0447 0.0120  154 MET A O   
2064 C CB  . MET A 136 ? 0.1999 0.1246 0.2260 -0.0076 -0.0513 0.0071  154 MET A CB  
2065 C CG  . MET A 136 ? 0.2130 0.1144 0.2160 -0.0402 -0.0518 0.0108  154 MET A CG  
2066 S SD  . MET A 136 ? 0.2326 0.1325 0.2395 -0.0277 -0.0659 0.0273  154 MET A SD  
2067 C CE  . MET A 136 ? 0.2271 0.1500 0.2217 -0.0101 -0.0783 0.0447  154 MET A CE  
2077 N N   . ALA A 137 ? 0.1889 0.1111 0.2096 0.0018  -0.0479 0.0191  155 ALA A N   
2078 C CA  . ALA A 137 ? 0.2104 0.1139 0.2173 0.0027  -0.0512 0.0195  155 ALA A CA  
2079 C C   . ALA A 137 ? 0.1982 0.1074 0.2189 -0.0253 -0.0559 0.0048  155 ALA A C   
2080 O O   . ALA A 137 ? 0.2069 0.1175 0.2412 -0.0171 -0.0458 0.0079  155 ALA A O   
2081 C CB  . ALA A 137 ? 0.1867 0.1220 0.2355 0.0169  -0.0460 -0.0102 155 ALA A CB  
2087 N N   . PHE A 138 ? 0.1772 0.1096 0.2062 -0.0269 -0.0601 0.0264  156 PHE A N   
2088 C CA  . PHE A 138 ? 0.1692 0.1056 0.2065 -0.0228 -0.0618 0.0099  156 PHE A CA  
2089 C C   . PHE A 138 ? 0.1585 0.1065 0.2038 -0.0102 -0.0511 0.0089  156 PHE A C   
2090 O O   . PHE A 138 ? 0.1688 0.1133 0.2109 -0.0112 -0.0550 0.0029  156 PHE A O   
2091 C CB  . PHE A 138 ? 0.1989 0.1036 0.2120 -0.0272 -0.0422 0.0206  156 PHE A CB  
2092 C CG  . PHE A 138 ? 0.1712 0.1021 0.2016 -0.0240 -0.0657 0.0296  156 PHE A CG  
2093 C CD1 . PHE A 138 ? 0.2029 0.1126 0.2075 -0.0341 -0.0654 0.0343  156 PHE A CD1 
2094 C CD2 . PHE A 138 ? 0.1830 0.1016 0.2084 0.0145  -0.0823 0.0254  156 PHE A CD2 
2095 C CE1 . PHE A 138 ? 0.2261 0.1137 0.2274 -0.0221 -0.0661 0.0093  156 PHE A CE1 
2096 C CE2 . PHE A 138 ? 0.2153 0.1166 0.2059 -0.0069 -0.0998 0.0331  156 PHE A CE2 
2097 C CZ  . PHE A 138 ? 0.2208 0.1127 0.2324 -0.0149 -0.0714 0.0242  156 PHE A CZ  
2107 N N   . ALA A 139 ? 0.1856 0.1045 0.1970 -0.0191 -0.0524 0.0204  157 ALA A N   
2108 C CA  . ALA A 139 ? 0.1709 0.0935 0.1939 -0.0057 -0.0486 0.0119  157 ALA A CA  
2109 C C   . ALA A 139 ? 0.1750 0.1065 0.2138 -0.0051 -0.0575 0.0115  157 ALA A C   
2110 O O   . ALA A 139 ? 0.2094 0.1037 0.2239 -0.0068 -0.0589 0.0096  157 ALA A O   
2111 C CB  . ALA A 139 ? 0.2036 0.0940 0.1973 -0.0311 -0.0717 0.0079  157 ALA A CB  
2117 N N   . PRO A 140 ? 0.1687 0.1056 0.2238 -0.0302 -0.0480 0.0087  158 PRO A N   
2118 C CA  . PRO A 140 ? 0.1733 0.0947 0.2225 -0.0131 -0.0520 0.0010  158 PRO A CA  
2119 C C   . PRO A 140 ? 0.2089 0.0999 0.2219 -0.0191 -0.0619 0.0110  158 PRO A C   
2120 O O   . PRO A 140 ? 0.2156 0.1146 0.2610 -0.0231 -0.0791 0.0314  158 PRO A O   
2121 C CB  . PRO A 140 ? 0.1911 0.1108 0.2156 -0.0086 -0.0649 0.0151  158 PRO A CB  
2122 C CG  . PRO A 140 ? 0.1795 0.1131 0.1950 -0.0051 -0.0657 0.0204  158 PRO A CG  
2123 C CD  . PRO A 140 ? 0.1776 0.1105 0.2010 -0.0172 -0.0382 0.0108  158 PRO A CD  
2131 N N   . ASP A 141 ? 0.2220 0.0953 0.2400 -0.0171 -0.0641 0.0127  159 ASP A N   
2132 C CA  . ASP A 141 ? 0.2162 0.1125 0.2491 -0.0076 -0.0547 0.0126  159 ASP A CA  
2133 C C   . ASP A 141 ? 0.2004 0.1164 0.2301 -0.0051 -0.0432 0.0042  159 ASP A C   
2134 O O   . ASP A 141 ? 0.1988 0.1236 0.2053 -0.0139 -0.0343 0.0087  159 ASP A O   
2135 C CB  . ASP A 141 ? 0.2225 0.1129 0.2582 0.0118  -0.0585 0.0123  159 ASP A CB  
2136 C CG  . ASP A 141 ? 0.2469 0.1199 0.2937 -0.0062 -0.0413 0.0040  159 ASP A CG  
2137 O OD1 . ASP A 141 ? 0.2024 0.1333 0.2993 -0.0016 -0.0624 -0.0218 159 ASP A OD1 
2138 O OD2 . ASP A 141 ? 0.2631 0.1335 0.3197 -0.0418 -0.0507 0.0411  159 ASP A OD2 
2143 N N   . TYR A 142 ? 0.2044 0.0998 0.2307 -0.0145 -0.0380 -0.0048 160 TYR A N   
2144 C CA  . TYR A 142 ? 0.1968 0.1055 0.2229 -0.0104 -0.0270 0.0048  160 TYR A CA  
2145 C C   . TYR A 142 ? 0.2065 0.1223 0.2319 -0.0215 -0.0281 -0.0039 160 TYR A C   
2146 O O   . TYR A 142 ? 0.2064 0.1203 0.2335 -0.0174 -0.0498 -0.0039 160 TYR A O   
2147 C CB  . TYR A 142 ? 0.2019 0.1078 0.2153 -0.0265 -0.0380 0.0113  160 TYR A CB  
2148 C CG  . TYR A 142 ? 0.1884 0.1061 0.1866 -0.0176 -0.0544 0.0207  160 TYR A CG  
2149 C CD1 . TYR A 142 ? 0.2029 0.1142 0.2030 -0.0079 -0.0506 0.0126  160 TYR A CD1 
2150 C CD2 . TYR A 142 ? 0.1844 0.1136 0.1900 -0.0306 -0.0497 0.0166  160 TYR A CD2 
2151 C CE1 . TYR A 142 ? 0.1838 0.1322 0.2207 -0.0190 -0.0592 0.0157  160 TYR A CE1 
2152 C CE2 . TYR A 142 ? 0.1917 0.1253 0.2117 -0.0180 -0.0411 0.0102  160 TYR A CE2 
2153 C CZ  . TYR A 142 ? 0.1758 0.1242 0.2257 0.0020  -0.0440 0.0087  160 TYR A CZ  
2154 O OH  . TYR A 142 ? 0.1959 0.1412 0.2430 0.0049  -0.0414 0.0121  160 TYR A OH  
2164 N N   . LYS A 143 ? 0.2033 0.1138 0.2336 -0.0053 -0.0680 -0.0180 161 LYS A N   
2165 C CA  . LYS A 143 ? 0.2099 0.1153 0.2444 -0.0032 -0.0551 -0.0179 161 LYS A CA  
2166 C C   . LYS A 143 ? 0.2159 0.1174 0.2626 0.0026  -0.0493 -0.0073 161 LYS A C   
2167 O O   . LYS A 143 ? 0.2530 0.1484 0.2823 -0.0138 -0.0473 -0.0025 161 LYS A O   
2168 C CB  . LYS A 143 ? 0.2349 0.1187 0.2503 -0.0160 -0.0289 -0.0155 161 LYS A CB  
2169 C CG  . LYS A 143 ? 0.2114 0.1353 0.2520 0.0143  -0.0507 0.0070  161 LYS A CG  
2170 C CD  . LYS A 143 ? 0.1969 0.1448 0.2815 0.0267  -0.0548 0.0022  161 LYS A CD  
2171 C CE  . LYS A 143 ? 0.2009 0.1388 0.2982 0.0198  -0.0399 0.0069  161 LYS A CE  
2172 N NZ  . LYS A 143 ? 0.2001 0.1407 0.2955 -0.0061 -0.0182 0.0047  161 LYS A NZ  
2186 N N   . GLY A 144 ? 0.1913 0.1221 0.2673 0.0084  -0.0396 0.0014  162 GLY A N   
2187 C CA  . GLY A 144 ? 0.2209 0.1215 0.2481 0.0154  -0.0564 -0.0160 162 GLY A CA  
2188 C C   . GLY A 144 ? 0.2318 0.1250 0.2527 -0.0137 -0.0528 -0.0192 162 GLY A C   
2189 O O   . GLY A 144 ? 0.2373 0.1377 0.2631 -0.0136 -0.0398 -0.0166 162 GLY A O   
2193 N N   . THR A 145 ? 0.2313 0.1242 0.2415 -0.0042 -0.0523 -0.0043 163 THR A N   
2194 C CA  . THR A 145 ? 0.2674 0.1005 0.2275 -0.0157 -0.0608 0.0115  163 THR A CA  
2195 C C   . THR A 145 ? 0.3257 0.1045 0.2464 -0.0295 -0.0925 0.0243  163 THR A C   
2196 O O   . THR A 145 ? 0.3462 0.1123 0.2281 -0.0537 -0.0784 0.0277  163 THR A O   
2197 C CB  . THR A 145 ? 0.2717 0.1154 0.2257 -0.0281 -0.0307 -0.0051 163 THR A CB  
2198 O OG1 . THR A 145 ? 0.2821 0.1214 0.2182 -0.0170 -0.0332 -0.0039 163 THR A OG1 
2199 C CG2 . THR A 145 ? 0.3107 0.1312 0.2511 -0.0155 -0.0025 -0.0184 163 THR A CG2 
2207 N N   . VAL A 146 ? 0.3322 0.1264 0.2813 -0.0124 -0.1165 0.0217  164 VAL A N   
2208 C CA  . VAL A 146 ? 0.3774 0.1303 0.2774 -0.0067 -0.1248 0.0311  164 VAL A CA  
2209 C C   . VAL A 146 ? 0.4662 0.1568 0.2913 -0.0178 -0.0586 0.0396  164 VAL A C   
2210 O O   . VAL A 146 ? 0.5130 0.1721 0.3070 -0.0052 -0.0152 0.0496  164 VAL A O   
2211 C CB  . VAL A 146 ? 0.4148 0.1358 0.3101 -0.0328 -0.1242 0.0325  164 VAL A CB  
2212 C CG1 . VAL A 146 ? 0.4227 0.1480 0.3154 -0.0460 -0.1441 0.0508  164 VAL A CG1 
2213 C CG2 . VAL A 146 ? 0.4413 0.1453 0.3296 -0.0430 -0.0990 0.0410  164 VAL A CG2 
2223 N N   . LEU A 147 ? 0.4889 0.1631 0.2961 -0.0474 -0.0538 0.0213  165 LEU A N   
2224 C CA  . LEU A 147 ? 0.5383 0.1983 0.3265 -0.0826 -0.0417 0.0092  165 LEU A CA  
2225 C C   . LEU A 147 ? 0.6004 0.2835 0.3715 -0.1240 -0.0054 0.0030  165 LEU A C   
2226 O O   . LEU A 147 ? 0.5998 0.3169 0.3692 -0.1382 -0.0121 0.0039  165 LEU A O   
2227 C CB  . LEU A 147 ? 0.5014 0.1732 0.3076 -0.0323 -0.0787 0.0368  165 LEU A CB  
2228 C CG  . LEU A 147 ? 0.4671 0.1724 0.2962 0.0049  -0.1083 0.0446  165 LEU A CG  
2229 C CD1 . LEU A 147 ? 0.4509 0.1599 0.2941 -0.0037 -0.1282 0.0278  165 LEU A CD1 
2230 C CD2 . LEU A 147 ? 0.4915 0.2035 0.3123 0.0180  -0.1057 0.0496  165 LEU A CD2 
2242 N N   . ALA A 148 ? 0.6528 0.2932 0.4051 -0.1375 0.0148  0.0022  166 ALA A N   
2243 C CA  . ALA A 148 ? 0.6743 0.3074 0.4315 -0.1348 0.0129  -0.0102 166 ALA A CA  
2244 C C   . ALA A 148 ? 0.7065 0.3219 0.4531 -0.1240 0.0269  -0.0114 166 ALA A C   
2245 O O   . ALA A 148 ? 0.7547 0.3329 0.4644 -0.1207 0.0492  -0.0273 166 ALA A O   
2246 C CB  . ALA A 148 ? 0.6738 0.3074 0.4379 -0.1395 0.0114  -0.0110 166 ALA A CB  
2252 N N   . GLY A 149 ? 0.6700 0.3054 0.4572 -0.1269 0.0089  -0.0238 167 GLY A N   
2253 C CA  . GLY A 149 ? 0.6302 0.3083 0.4523 -0.1201 -0.0226 -0.0094 167 GLY A CA  
2254 C C   . GLY A 149 ? 0.5757 0.2956 0.4320 -0.1232 -0.0478 0.0214  167 GLY A C   
2255 O O   . GLY A 149 ? 0.5590 0.2696 0.4337 -0.1389 -0.0486 0.0085  167 GLY A O   
2259 N N   . PRO A 150 ? 0.5400 0.3209 0.3910 -0.0958 -0.0942 0.0606  168 PRO A N   
2260 C CA  . PRO A 150 ? 0.5180 0.3329 0.3663 -0.0964 -0.1174 0.0790  168 PRO A CA  
2261 C C   . PRO A 150 ? 0.5037 0.3362 0.3663 -0.1030 -0.1288 0.0892  168 PRO A C   
2262 O O   . PRO A 150 ? 0.4927 0.3595 0.3771 -0.0774 -0.1173 0.1125  168 PRO A O   
2263 C CB  . PRO A 150 ? 0.5270 0.3415 0.3762 -0.0734 -0.1077 0.0716  168 PRO A CB  
2264 C CG  . PRO A 150 ? 0.5393 0.3475 0.3895 -0.0685 -0.0967 0.0667  168 PRO A CG  
2265 C CD  . PRO A 150 ? 0.5444 0.3355 0.3845 -0.0682 -0.0964 0.0748  168 PRO A CD  
2273 N N   . LEU A 151 ? 0.4719 0.3112 0.3405 -0.1196 -0.1665 0.0767  169 LEU A N   
2274 C CA  . LEU A 151 ? 0.5137 0.2886 0.3509 -0.1274 -0.1226 0.0513  169 LEU A CA  
2275 C C   . LEU A 151 ? 0.5465 0.2758 0.3447 -0.1239 -0.1276 0.0462  169 LEU A C   
2276 O O   . LEU A 151 ? 0.5760 0.2766 0.3338 -0.1585 -0.0870 0.0508  169 LEU A O   
2277 C CB  . LEU A 151 ? 0.5250 0.2934 0.3575 -0.1022 -0.0967 0.0565  169 LEU A CB  
2278 C CG  . LEU A 151 ? 0.5427 0.3014 0.3950 -0.0973 -0.0523 0.0444  169 LEU A CG  
2279 C CD1 . LEU A 151 ? 0.5561 0.2904 0.4119 -0.0849 -0.0203 0.0599  169 LEU A CD1 
2280 C CD2 . LEU A 151 ? 0.5398 0.3048 0.3925 -0.1069 -0.0491 0.0470  169 LEU A CD2 
2292 N N   . ASP A 152 ? 0.5554 0.2742 0.3611 -0.1093 -0.1441 0.0298  170 ASP A N   
2293 C CA  . ASP A 152 ? 0.6377 0.2743 0.3745 -0.0762 -0.1193 0.0432  170 ASP A CA  
2294 C C   . ASP A 152 ? 0.6419 0.2513 0.3631 -0.0448 -0.1136 0.0517  170 ASP A C   
2295 O O   . ASP A 152 ? 0.6268 0.2450 0.3567 -0.0235 -0.1218 0.0766  170 ASP A O   
2296 C CB  . ASP A 152 ? 0.7268 0.3020 0.4122 -0.0667 -0.0948 0.0330  170 ASP A CB  
2297 C CG  . ASP A 152 ? 0.8052 0.3455 0.4581 -0.0475 -0.0740 0.0340  170 ASP A CG  
2298 O OD1 . ASP A 152 ? 0.8431 0.3777 0.4892 -0.0456 -0.0639 0.0148  170 ASP A OD1 
2299 O OD2 . ASP A 152 ? 0.8385 0.3741 0.4784 -0.0334 -0.0615 0.0418  170 ASP A OD2 
2304 N N   . ALA A 153 ? 0.6425 0.2325 0.3608 -0.0361 -0.1076 0.0341  171 ALA A N   
2305 C CA  . ALA A 153 ? 0.6536 0.2241 0.3605 0.0010  -0.0978 0.0450  171 ALA A CA  
2306 C C   . ALA A 153 ? 0.6324 0.2246 0.3772 0.0048  -0.1166 0.0453  171 ALA A C   
2307 O O   . ALA A 153 ? 0.6376 0.1994 0.3789 0.0204  -0.1049 0.0400  171 ALA A O   
2308 C CB  . ALA A 153 ? 0.6685 0.2269 0.3584 0.0004  -0.0894 0.0321  171 ALA A CB  
2314 N N   . LEU A 154 ? 0.6368 0.2396 0.3859 -0.0102 -0.1074 0.0202  172 LEU A N   
2315 C CA  . LEU A 154 ? 0.5915 0.2362 0.3679 -0.0230 -0.1110 0.0212  172 LEU A CA  
2316 C C   . LEU A 154 ? 0.5675 0.2237 0.3352 -0.0670 -0.1002 0.0019  172 LEU A C   
2317 O O   . LEU A 154 ? 0.6098 0.2479 0.3572 -0.1090 -0.0741 -0.0257 172 LEU A O   
2318 C CB  . LEU A 154 ? 0.5852 0.2425 0.3800 0.0259  -0.1032 0.0474  172 LEU A CB  
2319 C CG  . LEU A 154 ? 0.5636 0.2476 0.3797 0.0587  -0.1040 0.0534  172 LEU A CG  
2320 C CD1 . LEU A 154 ? 0.5533 0.2646 0.3914 0.0493  -0.1079 0.0642  172 LEU A CD1 
2321 C CD2 . LEU A 154 ? 0.5637 0.2537 0.3680 0.0823  -0.0809 0.0643  172 LEU A CD2 
2333 N N   . ALA A 155 ? 0.5074 0.1971 0.3006 -0.0363 -0.0941 0.0170  173 ALA A N   
2334 C CA  . ALA A 155 ? 0.4521 0.2048 0.2713 -0.0004 -0.0940 0.0307  173 ALA A CA  
2335 C C   . ALA A 155 ? 0.3951 0.1938 0.2703 0.0049  -0.0757 0.0150  173 ALA A C   
2336 O O   . ALA A 155 ? 0.3896 0.2192 0.2825 -0.0016 -0.0948 0.0098  173 ALA A O   
2337 C CB  . ALA A 155 ? 0.4659 0.2251 0.2663 0.0420  -0.0953 0.0284  173 ALA A CB  
2343 N N   . VAL A 156 ? 0.3613 0.1758 0.2774 0.0224  -0.0771 0.0178  174 VAL A N   
2344 C CA  . VAL A 156 ? 0.3314 0.1387 0.2641 0.0222  -0.0716 0.0248  174 VAL A CA  
2345 C C   . VAL A 156 ? 0.3503 0.1364 0.2858 0.0153  -0.0639 0.0048  174 VAL A C   
2346 O O   . VAL A 156 ? 0.4104 0.1481 0.3216 0.0002  -0.0010 0.0105  174 VAL A O   
2347 C CB  . VAL A 156 ? 0.3159 0.1448 0.2601 0.0191  -0.0506 0.0245  174 VAL A CB  
2348 C CG1 . VAL A 156 ? 0.3073 0.1567 0.2687 0.0195  -0.0290 -0.0006 174 VAL A CG1 
2349 C CG2 . VAL A 156 ? 0.3138 0.1706 0.2524 0.0180  -0.0542 0.0356  174 VAL A CG2 
2359 N N   . SER A 157 ? 0.3238 0.1287 0.2581 0.0302  -0.1074 0.0084  175 SER A N   
2360 C CA  . SER A 157 ? 0.3533 0.1550 0.2562 0.0203  -0.0891 0.0120  175 SER A CA  
2361 C C   . SER A 157 ? 0.3034 0.1216 0.2472 0.0125  -0.0604 0.0289  175 SER A C   
2362 O O   . SER A 157 ? 0.2542 0.1318 0.2532 -0.0159 -0.0690 0.0311  175 SER A O   
2363 C CB  . SER A 157 ? 0.4214 0.2248 0.2820 0.0151  -0.1130 0.0120  175 SER A CB  
2364 O OG  . SER A 157 ? 0.4985 0.2666 0.3231 -0.0169 -0.1029 -0.0205 175 SER A OG  
2370 N N   . ALA A 158 ? 0.2733 0.1115 0.2508 -0.0087 -0.0729 0.0218  176 ALA A N   
2371 C CA  . ALA A 158 ? 0.2621 0.1087 0.2748 0.0016  -0.0312 0.0233  176 ALA A CA  
2372 C C   . ALA A 158 ? 0.2561 0.1131 0.2663 -0.0168 -0.0493 0.0264  176 ALA A C   
2373 O O   . ALA A 158 ? 0.2361 0.1088 0.2532 -0.0111 -0.0691 0.0249  176 ALA A O   
2374 C CB  . ALA A 158 ? 0.2759 0.1052 0.2918 0.0086  -0.0237 0.0169  176 ALA A CB  
2380 N N   . PRO A 159 ? 0.2249 0.1253 0.2521 0.0006  -0.0497 0.0071  177 PRO A N   
2381 C CA  . PRO A 159 ? 0.2068 0.1204 0.2587 -0.0256 -0.0634 -0.0078 177 PRO A CA  
2382 C C   . PRO A 159 ? 0.1993 0.1016 0.2745 -0.0219 -0.0380 0.0002  177 PRO A C   
2383 O O   . PRO A 159 ? 0.2024 0.1025 0.2603 -0.0090 -0.0450 -0.0014 177 PRO A O   
2384 C CB  . PRO A 159 ? 0.2141 0.1273 0.2606 -0.0137 -0.0422 0.0048  177 PRO A CB  
2385 C CG  . PRO A 159 ? 0.2090 0.1279 0.2438 -0.0085 -0.0516 0.0038  177 PRO A CG  
2386 C CD  . PRO A 159 ? 0.2270 0.1120 0.2472 0.0027  -0.0270 0.0315  177 PRO A CD  
2394 N N   . SER A 160 ? 0.1733 0.0923 0.2856 -0.0205 -0.0384 0.0073  178 SER A N   
2395 C CA  . SER A 160 ? 0.1638 0.1030 0.2894 -0.0177 -0.0600 0.0237  178 SER A CA  
2396 C C   . SER A 160 ? 0.1857 0.1125 0.2941 -0.0234 -0.0413 0.0075  178 SER A C   
2397 O O   . SER A 160 ? 0.1900 0.1250 0.3137 -0.0073 -0.0344 0.0224  178 SER A O   
2398 C CB  . SER A 160 ? 0.2158 0.0938 0.2887 -0.0032 -0.0327 0.0063  178 SER A CB  
2399 O OG  . SER A 160 ? 0.2392 0.1076 0.2855 -0.0130 -0.0167 0.0031  178 SER A OG  
2405 N N   . VAL A 161 ? 0.1964 0.1390 0.2863 -0.0033 -0.0428 -0.0047 179 VAL A N   
2406 C CA  . VAL A 161 ? 0.1891 0.1436 0.2899 -0.0162 -0.0461 -0.0206 179 VAL A CA  
2407 C C   . VAL A 161 ? 0.2010 0.1389 0.2699 -0.0204 -0.0515 -0.0092 179 VAL A C   
2408 O O   . VAL A 161 ? 0.2110 0.1522 0.2593 -0.0081 -0.0662 0.0196  179 VAL A O   
2409 C CB  . VAL A 161 ? 0.2409 0.1664 0.3037 0.0044  -0.0235 -0.0257 179 VAL A CB  
2410 C CG1 . VAL A 161 ? 0.2417 0.1957 0.2870 0.0081  -0.0219 -0.0289 179 VAL A CG1 
2411 C CG2 . VAL A 161 ? 0.2546 0.1727 0.3206 0.0299  0.0005  -0.0350 179 VAL A CG2 
2421 N N   . TRP A 162 ? 0.1982 0.1352 0.2710 -0.0157 -0.0531 -0.0118 180 TRP A N   
2422 C CA  . TRP A 162 ? 0.1953 0.1271 0.2697 -0.0143 -0.0642 0.0047  180 TRP A CA  
2423 C C   . TRP A 162 ? 0.1892 0.1125 0.2616 -0.0258 -0.0851 0.0076  180 TRP A C   
2424 O O   . TRP A 162 ? 0.2011 0.1463 0.2690 -0.0188 -0.0737 0.0296  180 TRP A O   
2425 C CB  . TRP A 162 ? 0.2260 0.1266 0.2691 -0.0057 -0.0563 0.0102  180 TRP A CB  
2426 C CG  . TRP A 162 ? 0.2253 0.1303 0.2855 -0.0120 -0.0891 0.0401  180 TRP A CG  
2427 C CD1 . TRP A 162 ? 0.2419 0.1222 0.2761 -0.0328 -0.0621 0.0348  180 TRP A CD1 
2428 C CD2 . TRP A 162 ? 0.2428 0.1504 0.3107 -0.0328 -0.1020 0.0462  180 TRP A CD2 
2429 N NE1 . TRP A 162 ? 0.2718 0.1313 0.2778 -0.0440 -0.0636 0.0236  180 TRP A NE1 
2430 C CE2 . TRP A 162 ? 0.2738 0.1552 0.3000 -0.0418 -0.0857 0.0379  180 TRP A CE2 
2431 C CE3 . TRP A 162 ? 0.2555 0.1952 0.3454 -0.0117 -0.0938 0.0668  180 TRP A CE3 
2432 C CZ2 . TRP A 162 ? 0.2873 0.1741 0.3241 -0.0457 -0.0839 0.0600  180 TRP A CZ2 
2433 C CZ3 . TRP A 162 ? 0.2675 0.2147 0.3686 -0.0173 -0.0758 0.0774  180 TRP A CZ3 
2434 C CH2 . TRP A 162 ? 0.3023 0.1980 0.3428 -0.0281 -0.0705 0.0803  180 TRP A CH2 
2445 N N   . GLN A 163 ? 0.2007 0.1072 0.2656 -0.0091 -0.0509 0.0183  181 GLN A N   
2446 C CA  . GLN A 163 ? 0.2070 0.1272 0.2481 -0.0080 -0.0334 0.0123  181 GLN A CA  
2447 C C   . GLN A 163 ? 0.1929 0.1231 0.2361 -0.0063 -0.0369 0.0227  181 GLN A C   
2448 O O   . GLN A 163 ? 0.2174 0.1408 0.2520 0.0053  -0.0243 -0.0086 181 GLN A O   
2449 C CB  . GLN A 163 ? 0.1997 0.1142 0.2617 -0.0151 -0.0357 -0.0006 181 GLN A CB  
2450 C CG  . GLN A 163 ? 0.1764 0.1101 0.2817 -0.0084 -0.0459 -0.0065 181 GLN A CG  
2451 C CD  . GLN A 163 ? 0.2003 0.1031 0.2680 0.0029  -0.0627 0.0046  181 GLN A CD  
2452 O OE1 . GLN A 163 ? 0.2262 0.1060 0.2839 -0.0081 -0.0427 0.0220  181 GLN A OE1 
2453 N NE2 . GLN A 163 ? 0.2174 0.1153 0.2787 -0.0107 -0.0671 0.0160  181 GLN A NE2 
2462 N N   . GLN A 164 ? 0.2042 0.1396 0.2480 -0.0129 -0.0386 0.0069  182 GLN A N   
2463 C CA  . GLN A 164 ? 0.1972 0.1206 0.2635 -0.0170 -0.0808 0.0095  182 GLN A CA  
2464 C C   . GLN A 164 ? 0.2176 0.1108 0.2750 -0.0180 -0.0695 0.0234  182 GLN A C   
2465 O O   . GLN A 164 ? 0.2224 0.1163 0.2781 -0.0202 -0.0862 0.0189  182 GLN A O   
2466 C CB  . GLN A 164 ? 0.2106 0.1401 0.3044 -0.0093 -0.0929 0.0164  182 GLN A CB  
2467 C CG  . GLN A 164 ? 0.2267 0.1462 0.3323 0.0102  -0.0924 0.0229  182 GLN A CG  
2468 C CD  . GLN A 164 ? 0.2289 0.1446 0.3621 0.0365  -0.0938 0.0115  182 GLN A CD  
2469 O OE1 . GLN A 164 ? 0.2542 0.1835 0.3798 0.0097  -0.0880 0.0097  182 GLN A OE1 
2470 N NE2 . GLN A 164 ? 0.1927 0.1143 0.3544 0.0366  -0.0726 0.0042  182 GLN A NE2 
2479 N N   . THR A 165 ? 0.2369 0.1027 0.2734 -0.0249 -0.0810 0.0119  183 THR A N   
2480 C CA  . THR A 165 ? 0.2311 0.1375 0.2798 -0.0067 -0.0656 0.0277  183 THR A CA  
2481 C C   . THR A 165 ? 0.2165 0.1116 0.2731 -0.0055 -0.0737 0.0163  183 THR A C   
2482 O O   . THR A 165 ? 0.2524 0.1110 0.2661 -0.0003 -0.0524 0.0041  183 THR A O   
2483 C CB  . THR A 165 ? 0.2798 0.1781 0.2985 -0.0068 -0.0586 0.0335  183 THR A CB  
2484 O OG1 . THR A 165 ? 0.3209 0.1819 0.2925 -0.0080 -0.0520 0.0544  183 THR A OG1 
2485 C CG2 . THR A 165 ? 0.2619 0.1923 0.3331 -0.0016 -0.0491 0.0569  183 THR A CG2 
2493 N N   . THR A 166 ? 0.2473 0.1377 0.2983 0.0003  -0.0634 -0.0099 184 THR A N   
2494 C CA  . THR A 166 ? 0.2663 0.1599 0.3285 0.0085  -0.0875 -0.0185 184 THR A CA  
2495 C C   . THR A 166 ? 0.2519 0.1590 0.2880 0.0306  -0.0946 0.0162  184 THR A C   
2496 O O   . THR A 166 ? 0.2828 0.1885 0.3103 0.0506  -0.0681 0.0442  184 THR A O   
2497 C CB  . THR A 166 ? 0.3001 0.1940 0.4055 0.0049  -0.0759 -0.0626 184 THR A CB  
2498 O OG1 . THR A 166 ? 0.3297 0.2235 0.4441 0.0014  -0.0431 -0.0625 184 THR A OG1 
2499 C CG2 . THR A 166 ? 0.2930 0.2123 0.4276 0.0019  -0.1031 -0.0793 184 THR A CG2 
2507 N N   . GLY A 167 ? 0.2436 0.1592 0.2673 0.0080  -0.0905 -0.0120 185 GLY A N   
2508 C CA  . GLY A 167 ? 0.2561 0.1648 0.2647 0.0196  -0.0732 -0.0217 185 GLY A CA  
2509 C C   . GLY A 167 ? 0.2340 0.1558 0.2616 0.0241  -0.0835 -0.0058 185 GLY A C   
2510 O O   . GLY A 167 ? 0.2656 0.1677 0.2834 0.0213  -0.0871 -0.0078 185 GLY A O   
2514 N N   . SER A 168 ? 0.2132 0.1580 0.2594 0.0075  -0.0524 0.0126  186 SER A N   
2515 C CA  . SER A 168 ? 0.2226 0.1233 0.2437 0.0048  -0.0471 0.0090  186 SER A CA  
2516 C C   . SER A 168 ? 0.1962 0.1315 0.2444 0.0128  -0.0658 0.0053  186 SER A C   
2517 O O   . SER A 168 ? 0.2208 0.1400 0.2359 0.0088  -0.0338 0.0065  186 SER A O   
2518 C CB  . SER A 168 ? 0.2124 0.1124 0.2427 -0.0128 -0.0396 0.0088  186 SER A CB  
2519 O OG  . SER A 168 ? 0.2001 0.1218 0.2513 -0.0198 -0.0369 -0.0020 186 SER A OG  
2525 N N   . ALA A 169 ? 0.1925 0.1276 0.2506 0.0010  -0.0762 -0.0043 187 ALA A N   
2526 C CA  . ALA A 169 ? 0.2012 0.1246 0.2417 -0.0154 -0.0463 -0.0021 187 ALA A CA  
2527 C C   . ALA A 169 ? 0.1874 0.1266 0.2351 0.0088  -0.0285 0.0045  187 ALA A C   
2528 O O   . ALA A 169 ? 0.1931 0.1494 0.2339 0.0028  -0.0332 -0.0165 187 ALA A O   
2529 C CB  . ALA A 169 ? 0.2253 0.1213 0.2568 -0.0073 -0.0532 -0.0099 187 ALA A CB  
2535 N N   . LEU A 170 ? 0.1871 0.1312 0.2353 -0.0152 -0.0415 0.0022  188 LEU A N   
2536 C CA  . LEU A 170 ? 0.1943 0.1207 0.2415 -0.0098 -0.0518 0.0141  188 LEU A CA  
2537 C C   . LEU A 170 ? 0.1900 0.1145 0.2485 -0.0269 -0.0490 0.0206  188 LEU A C   
2538 O O   . LEU A 170 ? 0.1639 0.1222 0.2690 -0.0128 -0.0368 0.0333  188 LEU A O   
2539 C CB  . LEU A 170 ? 0.2181 0.1120 0.2442 -0.0196 -0.0269 0.0255  188 LEU A CB  
2540 C CG  . LEU A 170 ? 0.2386 0.1347 0.2557 -0.0099 -0.0341 0.0369  188 LEU A CG  
2541 C CD1 . LEU A 170 ? 0.2455 0.1350 0.2863 -0.0323 -0.0508 0.0181  188 LEU A CD1 
2542 C CD2 . LEU A 170 ? 0.2947 0.1646 0.2666 -0.0083 -0.0414 0.0403  188 LEU A CD2 
2554 N N   . THR A 171 ? 0.1859 0.1220 0.2286 -0.0203 -0.0523 0.0149  189 THR A N   
2555 C CA  . THR A 171 ? 0.1932 0.1291 0.2348 -0.0286 -0.0407 -0.0050 189 THR A CA  
2556 C C   . THR A 171 ? 0.1875 0.1400 0.2255 -0.0162 -0.0287 0.0076  189 THR A C   
2557 O O   . THR A 171 ? 0.2194 0.1579 0.2170 0.0126  -0.0158 0.0274  189 THR A O   
2558 C CB  . THR A 171 ? 0.2091 0.1359 0.2370 -0.0154 -0.0396 0.0017  189 THR A CB  
2559 O OG1 . THR A 171 ? 0.2486 0.1614 0.2322 -0.0307 -0.0467 0.0079  189 THR A OG1 
2560 C CG2 . THR A 171 ? 0.2335 0.1455 0.2408 0.0091  -0.0374 -0.0025 189 THR A CG2 
2568 N N   . THR A 172 ? 0.2086 0.1451 0.2326 -0.0161 -0.0116 -0.0021 190 THR A N   
2569 C CA  . THR A 172 ? 0.1977 0.1331 0.2330 -0.0001 -0.0083 0.0173  190 THR A CA  
2570 C C   . THR A 172 ? 0.1878 0.1307 0.2244 -0.0062 -0.0155 0.0137  190 THR A C   
2571 O O   . THR A 172 ? 0.2002 0.1263 0.2550 0.0187  -0.0227 0.0066  190 THR A O   
2572 C CB  . THR A 172 ? 0.2230 0.1440 0.2589 0.0252  -0.0254 0.0324  190 THR A CB  
2573 O OG1 . THR A 172 ? 0.2633 0.1391 0.2671 0.0167  -0.0163 0.0642  190 THR A OG1 
2574 C CG2 . THR A 172 ? 0.2473 0.1479 0.2749 0.0224  -0.0240 0.0445  190 THR A CG2 
2582 N N   . ALA A 173 ? 0.2026 0.1401 0.2157 -0.0117 -0.0088 0.0233  191 ALA A N   
2583 C CA  . ALA A 173 ? 0.1980 0.1348 0.2064 0.0025  -0.0312 0.0042  191 ALA A CA  
2584 C C   . ALA A 173 ? 0.1851 0.1442 0.2103 0.0006  -0.0302 0.0130  191 ALA A C   
2585 O O   . ALA A 173 ? 0.2086 0.1740 0.2301 -0.0032 -0.0303 0.0057  191 ALA A O   
2586 C CB  . ALA A 173 ? 0.2328 0.1265 0.2071 -0.0031 -0.0304 0.0106  191 ALA A CB  
2592 N N   . LEU A 174 ? 0.1956 0.1274 0.2121 -0.0053 -0.0084 0.0156  192 LEU A N   
2593 C CA  . LEU A 174 ? 0.2086 0.1422 0.2243 -0.0085 -0.0191 0.0098  192 LEU A CA  
2594 C C   . LEU A 174 ? 0.2001 0.1391 0.2339 -0.0055 -0.0316 -0.0079 192 LEU A C   
2595 O O   . LEU A 174 ? 0.2355 0.1601 0.2272 -0.0003 -0.0365 0.0063  192 LEU A O   
2596 C CB  . LEU A 174 ? 0.2000 0.1509 0.2242 -0.0085 -0.0352 0.0299  192 LEU A CB  
2597 C CG  . LEU A 174 ? 0.2148 0.1648 0.2307 -0.0251 -0.0555 0.0163  192 LEU A CG  
2598 C CD1 . LEU A 174 ? 0.2484 0.1845 0.2420 -0.0186 -0.0847 0.0204  192 LEU A CD1 
2599 C CD2 . LEU A 174 ? 0.2522 0.1660 0.2490 -0.0332 -0.0553 0.0010  192 LEU A CD2 
2611 N N   . ARG A 175 ? 0.1888 0.1379 0.2439 -0.0141 -0.0277 -0.0143 193 ARG A N   
2612 C CA  . ARG A 175 ? 0.1735 0.1585 0.2441 -0.0052 -0.0418 -0.0184 193 ARG A CA  
2613 C C   . ARG A 175 ? 0.1881 0.1752 0.2363 -0.0015 -0.0273 0.0022  193 ARG A C   
2614 O O   . ARG A 175 ? 0.2251 0.1910 0.2374 -0.0026 -0.0084 -0.0080 193 ARG A O   
2615 C CB  . ARG A 175 ? 0.1920 0.1793 0.2501 -0.0025 -0.0535 -0.0254 193 ARG A CB  
2616 C CG  . ARG A 175 ? 0.2298 0.2118 0.2827 -0.0067 -0.0683 -0.0107 193 ARG A CG  
2617 C CD  . ARG A 175 ? 0.2684 0.2454 0.3008 -0.0034 -0.0783 -0.0161 193 ARG A CD  
2618 N NE  . ARG A 175 ? 0.3146 0.2777 0.3427 0.0060  -0.0588 0.0012  193 ARG A NE  
2619 C CZ  . ARG A 175 ? 0.3599 0.3004 0.3687 0.0344  -0.0774 -0.0093 193 ARG A CZ  
2620 N NH1 . ARG A 175 ? 0.3620 0.3139 0.3625 0.0303  -0.1156 -0.0146 193 ARG A NH1 
2621 N NH2 . ARG A 175 ? 0.4014 0.3028 0.3949 0.0522  -0.0448 -0.0274 193 ARG A NH2 
2635 N N   . ASN A 176 ? 0.1815 0.1680 0.2357 -0.0016 -0.0215 0.0009  194 ASN A N   
2636 C CA  . ASN A 176 ? 0.2107 0.1721 0.2285 0.0025  -0.0383 -0.0270 194 ASN A CA  
2637 C C   . ASN A 176 ? 0.2242 0.1968 0.2245 0.0147  -0.0274 -0.0331 194 ASN A C   
2638 O O   . ASN A 176 ? 0.2540 0.2226 0.2346 0.0122  -0.0304 -0.0372 194 ASN A O   
2639 C CB  . ASN A 176 ? 0.2253 0.1609 0.2317 0.0140  -0.0285 -0.0296 194 ASN A CB  
2640 C CG  . ASN A 176 ? 0.2295 0.1890 0.2788 0.0241  -0.0376 -0.0310 194 ASN A CG  
2641 O OD1 . ASN A 176 ? 0.2475 0.2116 0.2609 0.0379  -0.0552 -0.0459 194 ASN A OD1 
2642 N ND2 . ASN A 176 ? 0.2337 0.2083 0.3125 0.0607  -0.0223 0.0107  194 ASN A ND2 
2649 N N   . ALA A 177 ? 0.2481 0.1947 0.2227 0.0140  -0.0239 -0.0196 195 ALA A N   
2650 C CA  . ALA A 177 ? 0.2691 0.2014 0.2380 -0.0112 -0.0317 -0.0125 195 ALA A CA  
2651 C C   . ALA A 177 ? 0.2841 0.2077 0.2490 -0.0469 -0.0364 -0.0155 195 ALA A C   
2652 O O   . ALA A 177 ? 0.3193 0.2299 0.2506 -0.0667 -0.0395 -0.0136 195 ALA A O   
2653 C CB  . ALA A 177 ? 0.2370 0.1919 0.2328 -0.0163 -0.0486 -0.0239 195 ALA A CB  
2659 N N   . GLY A 178 ? 0.2777 0.2080 0.2527 -0.0391 -0.0606 0.0081  196 GLY A N   
2660 C CA  . GLY A 178 ? 0.2825 0.2175 0.2512 -0.0658 -0.0337 0.0154  196 GLY A CA  
2661 C C   . GLY A 178 ? 0.2719 0.2117 0.2506 -0.0708 -0.0288 0.0184  196 GLY A C   
2662 O O   . GLY A 178 ? 0.3001 0.2176 0.2485 -0.0854 -0.0172 0.0066  196 GLY A O   
2666 N N   . GLY A 179 ? 0.2518 0.2109 0.2639 -0.0428 -0.0380 0.0165  197 GLY A N   
2667 C CA  . GLY A 179 ? 0.2543 0.2048 0.2705 -0.0407 -0.0227 0.0045  197 GLY A CA  
2668 C C   . GLY A 179 ? 0.2143 0.1928 0.2544 -0.0489 -0.0365 0.0212  197 GLY A C   
2669 O O   . GLY A 179 ? 0.2115 0.2125 0.2472 -0.0217 -0.0417 0.0298  197 GLY A O   
2673 N N   . LEU A 180 ? 0.2167 0.1708 0.2637 -0.0385 -0.0278 0.0152  198 LEU A N   
2674 C CA  . LEU A 180 ? 0.2027 0.1548 0.2366 -0.0348 -0.0243 0.0070  198 LEU A CA  
2675 C C   . LEU A 180 ? 0.2024 0.1714 0.2276 -0.0209 -0.0216 0.0039  198 LEU A C   
2676 O O   . LEU A 180 ? 0.1926 0.1695 0.2257 -0.0073 -0.0306 -0.0016 198 LEU A O   
2677 C CB  . LEU A 180 ? 0.2158 0.1486 0.2233 -0.0257 -0.0133 0.0166  198 LEU A CB  
2678 C CG  . LEU A 180 ? 0.2336 0.1581 0.2258 -0.0249 -0.0200 0.0117  198 LEU A CG  
2679 C CD1 . LEU A 180 ? 0.2201 0.1608 0.2365 -0.0192 -0.0449 0.0060  198 LEU A CD1 
2680 C CD2 . LEU A 180 ? 0.2716 0.1738 0.2314 -0.0149 -0.0026 0.0054  198 LEU A CD2 
2692 N N   . THR A 181 ? 0.1947 0.1713 0.2329 -0.0110 0.0108  0.0091  199 THR A N   
2693 C CA  . THR A 181 ? 0.1616 0.1650 0.2252 0.0058  -0.0114 0.0218  199 THR A CA  
2694 C C   . THR A 181 ? 0.2065 0.1664 0.2225 -0.0160 -0.0256 0.0141  199 THR A C   
2695 O O   . THR A 181 ? 0.2426 0.1697 0.2256 -0.0393 -0.0179 0.0223  199 THR A O   
2696 C CB  . THR A 181 ? 0.1968 0.1894 0.2280 0.0036  -0.0312 0.0123  199 THR A CB  
2697 O OG1 . THR A 181 ? 0.2231 0.2127 0.2507 0.0007  0.0031  0.0037  199 THR A OG1 
2698 C CG2 . THR A 181 ? 0.2210 0.1993 0.2385 0.0005  -0.0143 0.0121  199 THR A CG2 
2706 N N   . GLN A 182 ? 0.2239 0.1667 0.2158 -0.0060 -0.0338 0.0170  200 GLN A N   
2707 C CA  . GLN A 182 ? 0.2382 0.1682 0.2043 0.0032  -0.0184 0.0206  200 GLN A CA  
2708 C C   . GLN A 182 ? 0.2431 0.1776 0.2020 0.0002  -0.0212 0.0155  200 GLN A C   
2709 O O   . GLN A 182 ? 0.2381 0.1741 0.2154 -0.0069 -0.0424 0.0279  200 GLN A O   
2710 C CB  . GLN A 182 ? 0.2219 0.1745 0.2347 -0.0245 -0.0462 0.0202  200 GLN A CB  
2711 C CG  . GLN A 182 ? 0.2191 0.1818 0.2548 -0.0055 -0.0326 0.0021  200 GLN A CG  
2712 C CD  . GLN A 182 ? 0.2190 0.1785 0.2526 0.0162  -0.0329 -0.0075 200 GLN A CD  
2713 O OE1 . GLN A 182 ? 0.2069 0.1859 0.2436 0.0107  -0.0346 -0.0074 200 GLN A OE1 
2714 N NE2 . GLN A 182 ? 0.2589 0.1990 0.2729 -0.0023 -0.0354 -0.0234 200 GLN A NE2 
2723 N N   . ILE A 183 ? 0.2437 0.2025 0.2020 -0.0192 -0.0435 0.0060  201 ILE A N   
2724 C CA  . ILE A 183 ? 0.2617 0.1950 0.2205 -0.0159 -0.0410 0.0273  201 ILE A CA  
2725 C C   . ILE A 183 ? 0.2639 0.1984 0.2299 0.0009  -0.0333 0.0363  201 ILE A C   
2726 O O   . ILE A 183 ? 0.3336 0.2166 0.2536 0.0097  -0.0113 0.0334  201 ILE A O   
2727 C CB  . ILE A 183 ? 0.2527 0.1819 0.2112 -0.0284 -0.0506 0.0383  201 ILE A CB  
2728 C CG1 . ILE A 183 ? 0.2591 0.1826 0.2337 -0.0483 -0.0656 0.0190  201 ILE A CG1 
2729 C CG2 . ILE A 183 ? 0.3115 0.1941 0.2026 -0.0376 -0.0451 0.0178  201 ILE A CG2 
2730 C CD1 . ILE A 183 ? 0.2749 0.1846 0.2649 -0.0677 -0.0446 0.0233  201 ILE A CD1 
2742 N N   . VAL A 184 ? 0.2080 0.1901 0.2175 -0.0247 -0.0189 0.0112  202 VAL A N   
2743 C CA  . VAL A 184 ? 0.2122 0.1845 0.2239 -0.0043 -0.0224 0.0209  202 VAL A CA  
2744 C C   . VAL A 184 ? 0.2457 0.1582 0.2257 -0.0171 -0.0253 0.0187  202 VAL A C   
2745 O O   . VAL A 184 ? 0.2458 0.1614 0.2244 -0.0427 -0.0167 0.0147  202 VAL A O   
2746 C CB  . VAL A 184 ? 0.2504 0.1799 0.2519 -0.0139 -0.0474 0.0320  202 VAL A CB  
2747 C CG1 . VAL A 184 ? 0.2835 0.1694 0.2759 -0.0020 -0.0415 0.0266  202 VAL A CG1 
2748 C CG2 . VAL A 184 ? 0.2569 0.1710 0.2682 -0.0169 -0.0363 0.0160  202 VAL A CG2 
2758 N N   . PRO A 185 ? 0.2559 0.1376 0.2100 -0.0061 -0.0241 0.0152  203 PRO A N   
2759 C CA  . PRO A 185 ? 0.2530 0.1536 0.2258 -0.0172 -0.0287 0.0100  203 PRO A CA  
2760 C C   . PRO A 185 ? 0.2307 0.1512 0.2257 -0.0196 -0.0198 0.0226  203 PRO A C   
2761 O O   . PRO A 185 ? 0.2369 0.1548 0.2240 -0.0113 -0.0221 0.0249  203 PRO A O   
2762 C CB  . PRO A 185 ? 0.2582 0.1440 0.2435 -0.0019 0.0048  0.0050  203 PRO A CB  
2763 C CG  . PRO A 185 ? 0.2771 0.1587 0.2286 -0.0186 0.0057  0.0233  203 PRO A CG  
2764 C CD  . PRO A 185 ? 0.2556 0.1429 0.2069 -0.0095 -0.0294 0.0112  203 PRO A CD  
2772 N N   . THR A 186 ? 0.2189 0.1491 0.2148 -0.0228 -0.0338 0.0062  204 THR A N   
2773 C CA  . THR A 186 ? 0.2199 0.1357 0.1996 -0.0131 -0.0461 0.0033  204 THR A CA  
2774 C C   . THR A 186 ? 0.2088 0.1276 0.2188 -0.0156 -0.0348 -0.0079 204 THR A C   
2775 O O   . THR A 186 ? 0.2123 0.1307 0.2409 -0.0149 -0.0201 -0.0029 204 THR A O   
2776 C CB  . THR A 186 ? 0.2439 0.1411 0.2075 0.0058  -0.0366 0.0015  204 THR A CB  
2777 O OG1 . THR A 186 ? 0.2492 0.1335 0.1714 -0.0132 -0.0184 0.0106  204 THR A OG1 
2778 C CG2 . THR A 186 ? 0.2394 0.1394 0.2230 -0.0059 -0.0439 0.0135  204 THR A CG2 
2786 N N   . THR A 187 ? 0.2026 0.1203 0.2099 -0.0116 -0.0407 0.0204  205 THR A N   
2787 C CA  . THR A 187 ? 0.1892 0.1216 0.2233 -0.0123 -0.0554 0.0243  205 THR A CA  
2788 C C   . THR A 187 ? 0.1992 0.1184 0.2245 -0.0334 -0.0504 0.0115  205 THR A C   
2789 O O   . THR A 187 ? 0.1860 0.1326 0.2370 -0.0369 -0.0511 0.0156  205 THR A O   
2790 C CB  . THR A 187 ? 0.2120 0.1285 0.2349 -0.0163 -0.0364 0.0110  205 THR A CB  
2791 O OG1 . THR A 187 ? 0.2346 0.1347 0.2544 -0.0351 -0.0336 0.0319  205 THR A OG1 
2792 C CG2 . THR A 187 ? 0.2095 0.1245 0.2291 -0.0287 -0.0171 -0.0031 205 THR A CG2 
2800 N N   . ASN A 188 ? 0.1965 0.1237 0.2134 -0.0164 -0.0382 0.0028  206 ASN A N   
2801 C CA  . ASN A 188 ? 0.1911 0.1093 0.2190 -0.0273 -0.0481 -0.0025 206 ASN A CA  
2802 C C   . ASN A 188 ? 0.1857 0.1200 0.2220 -0.0147 -0.0657 -0.0131 206 ASN A C   
2803 O O   . ASN A 188 ? 0.1770 0.1588 0.2459 -0.0261 -0.0524 -0.0161 206 ASN A O   
2804 C CB  . ASN A 188 ? 0.1903 0.1050 0.2197 0.0064  -0.0375 -0.0018 206 ASN A CB  
2805 C CG  . ASN A 188 ? 0.2075 0.1144 0.2224 -0.0024 -0.0093 0.0118  206 ASN A CG  
2806 O OD1 . ASN A 188 ? 0.2108 0.1054 0.2219 -0.0021 -0.0345 0.0066  206 ASN A OD1 
2807 N ND2 . ASN A 188 ? 0.2026 0.1533 0.2194 -0.0065 0.0107  0.0425  206 ASN A ND2 
2814 N N   . LEU A 189 ? 0.1881 0.1147 0.2241 -0.0025 -0.0645 0.0006  207 LEU A N   
2815 C CA  . LEU A 189 ? 0.1688 0.1418 0.2545 -0.0099 -0.0711 0.0088  207 LEU A CA  
2816 C C   . LEU A 189 ? 0.1613 0.1146 0.2239 -0.0167 -0.0666 0.0138  207 LEU A C   
2817 O O   . LEU A 189 ? 0.1887 0.1233 0.2159 -0.0413 -0.0474 0.0170  207 LEU A O   
2818 C CB  . LEU A 189 ? 0.1892 0.1702 0.2997 -0.0279 -0.1036 -0.0014 207 LEU A CB  
2819 C CG  . LEU A 189 ? 0.2480 0.2298 0.3829 -0.0452 -0.0955 -0.0840 207 LEU A CG  
2820 C CD1 . LEU A 189 ? 0.2686 0.2343 0.3951 -0.0510 -0.0548 -0.0718 207 LEU A CD1 
2821 C CD2 . LEU A 189 ? 0.2898 0.2795 0.4398 -0.0680 -0.0918 -0.1022 207 LEU A CD2 
2833 N N   . TYR A 190 ? 0.1675 0.0774 0.2240 -0.0139 -0.0561 0.0233  208 TYR A N   
2834 C CA  . TYR A 190 ? 0.1819 0.0845 0.2020 -0.0078 -0.0731 0.0126  208 TYR A CA  
2835 C C   . TYR A 190 ? 0.2224 0.0976 0.2223 -0.0030 -0.0356 -0.0001 208 TYR A C   
2836 O O   . TYR A 190 ? 0.2227 0.1070 0.2279 -0.0185 -0.0129 -0.0113 208 TYR A O   
2837 C CB  . TYR A 190 ? 0.2053 0.0945 0.1936 0.0104  -0.0692 -0.0057 208 TYR A CB  
2838 C CG  . TYR A 190 ? 0.2287 0.1006 0.1997 -0.0014 -0.0565 -0.0153 208 TYR A CG  
2839 C CD1 . TYR A 190 ? 0.2157 0.1191 0.1997 0.0070  -0.0703 -0.0051 208 TYR A CD1 
2840 C CD2 . TYR A 190 ? 0.2180 0.1120 0.2198 -0.0010 -0.0676 -0.0123 208 TYR A CD2 
2841 C CE1 . TYR A 190 ? 0.1995 0.1550 0.2120 -0.0079 -0.0676 0.0039  208 TYR A CE1 
2842 C CE2 . TYR A 190 ? 0.2174 0.1322 0.2358 -0.0187 -0.0482 -0.0047 208 TYR A CE2 
2843 C CZ  . TYR A 190 ? 0.1808 0.1427 0.2269 -0.0109 -0.0614 0.0047  208 TYR A CZ  
2844 O OH  . TYR A 190 ? 0.2251 0.1387 0.2518 0.0019  -0.0407 -0.0055 208 TYR A OH  
2854 N N   . SER A 191 ? 0.2340 0.0936 0.2218 0.0073  -0.0500 -0.0091 209 SER A N   
2855 C CA  . SER A 191 ? 0.2280 0.1224 0.2044 0.0088  -0.0645 -0.0168 209 SER A CA  
2856 C C   . SER A 191 ? 0.2211 0.1291 0.2334 -0.0128 -0.0719 -0.0099 209 SER A C   
2857 O O   . SER A 191 ? 0.1993 0.1223 0.2487 -0.0068 -0.0838 -0.0057 209 SER A O   
2858 C CB  . SER A 191 ? 0.2355 0.1425 0.2384 0.0247  -0.0679 0.0037  209 SER A CB  
2859 O OG  . SER A 191 ? 0.2521 0.1513 0.2272 0.0043  -0.0768 -0.0112 209 SER A OG  
2865 N N   . ALA A 192 ? 0.2368 0.1397 0.2493 -0.0285 -0.0909 0.0138  210 ALA A N   
2866 C CA  . ALA A 192 ? 0.2497 0.1359 0.2646 -0.0092 -0.0991 0.0006  210 ALA A CA  
2867 C C   . ALA A 192 ? 0.2437 0.1346 0.2551 -0.0042 -0.1127 0.0043  210 ALA A C   
2868 O O   . ALA A 192 ? 0.2754 0.1382 0.2872 -0.0146 -0.0933 0.0015  210 ALA A O   
2869 C CB  . ALA A 192 ? 0.2734 0.1427 0.2719 -0.0278 -0.1312 -0.0162 210 ALA A CB  
2875 N N   . THR A 193 ? 0.2347 0.1397 0.2431 -0.0064 -0.1106 -0.0019 211 THR A N   
2876 C CA  . THR A 193 ? 0.2645 0.1542 0.2376 -0.0058 -0.0840 -0.0106 211 THR A CA  
2877 C C   . THR A 193 ? 0.2629 0.1741 0.2340 -0.0306 -0.0710 -0.0248 211 THR A C   
2878 O O   . THR A 193 ? 0.2908 0.2162 0.2547 -0.0498 -0.0625 -0.0383 211 THR A O   
2879 C CB  . THR A 193 ? 0.2437 0.1366 0.2272 -0.0027 -0.0902 -0.0054 211 THR A CB  
2880 O OG1 . THR A 193 ? 0.2651 0.1519 0.2257 0.0044  -0.0681 0.0067  211 THR A OG1 
2881 C CG2 . THR A 193 ? 0.2562 0.1624 0.2354 0.0072  -0.0883 -0.0079 211 THR A CG2 
2889 N N   . ASP A 194 ? 0.2422 0.1352 0.2117 -0.0336 -0.0762 -0.0288 212 ASP A N   
2890 C CA  . ASP A 194 ? 0.2448 0.1100 0.1929 -0.0220 -0.0476 -0.0134 212 ASP A CA  
2891 C C   . ASP A 194 ? 0.2603 0.1284 0.2182 -0.0254 -0.0426 0.0089  212 ASP A C   
2892 O O   . ASP A 194 ? 0.2527 0.1463 0.2348 -0.0265 -0.0563 0.0290  212 ASP A O   
2893 C CB  . ASP A 194 ? 0.2468 0.1253 0.1977 -0.0339 -0.0399 -0.0156 212 ASP A CB  
2894 C CG  . ASP A 194 ? 0.2149 0.1219 0.2056 -0.0213 -0.0358 0.0049  212 ASP A CG  
2895 O OD1 . ASP A 194 ? 0.2049 0.1264 0.2114 -0.0144 -0.0382 0.0000  212 ASP A OD1 
2896 O OD2 . ASP A 194 ? 0.2448 0.1239 0.2091 -0.0353 -0.0676 0.0352  212 ASP A OD2 
2901 N N   . GLU A 195 ? 0.2492 0.1260 0.2251 -0.0334 -0.0453 0.0019  213 GLU A N   
2902 C CA  . GLU A 195 ? 0.2403 0.1416 0.2314 -0.0065 -0.0512 0.0054  213 GLU A CA  
2903 C C   . GLU A 195 ? 0.2412 0.1340 0.2255 -0.0053 -0.0581 0.0309  213 GLU A C   
2904 O O   . GLU A 195 ? 0.2998 0.1665 0.2347 -0.0176 -0.0299 0.0301  213 GLU A O   
2905 C CB  . GLU A 195 ? 0.2912 0.1656 0.2362 -0.0186 -0.0281 -0.0001 213 GLU A CB  
2906 C CG  . GLU A 195 ? 0.2884 0.1726 0.2394 0.0093  -0.0430 0.0204  213 GLU A CG  
2907 C CD  . GLU A 195 ? 0.2808 0.1740 0.2607 0.0038  -0.0489 0.0142  213 GLU A CD  
2908 O OE1 . GLU A 195 ? 0.2646 0.1777 0.2458 -0.0164 -0.0841 0.0090  213 GLU A OE1 
2909 O OE2 . GLU A 195 ? 0.2975 0.1873 0.2929 0.0201  -0.0377 0.0227  213 GLU A OE2 
2916 N N   . ILE A 196 ? 0.2568 0.1219 0.2115 -0.0242 -0.0348 0.0284  214 ILE A N   
2917 C CA  . ILE A 196 ? 0.2373 0.1294 0.2215 -0.0490 -0.0553 0.0184  214 ILE A CA  
2918 C C   . ILE A 196 ? 0.2637 0.1116 0.2265 -0.0308 -0.0477 0.0165  214 ILE A C   
2919 O O   . ILE A 196 ? 0.2743 0.1150 0.2368 -0.0285 -0.0391 0.0276  214 ILE A O   
2920 C CB  . ILE A 196 ? 0.2627 0.1668 0.2323 -0.0338 -0.0590 -0.0045 214 ILE A CB  
2921 C CG1 . ILE A 196 ? 0.2973 0.2022 0.2539 -0.0309 -0.0382 -0.0094 214 ILE A CG1 
2922 C CG2 . ILE A 196 ? 0.2566 0.1665 0.2282 -0.0525 -0.0519 0.0123  214 ILE A CG2 
2923 C CD1 . ILE A 196 ? 0.3402 0.2261 0.2724 -0.0151 -0.0336 0.0028  214 ILE A CD1 
2935 N N   . VAL A 197 ? 0.2779 0.1021 0.1990 -0.0083 -0.0449 0.0098  215 VAL A N   
2936 C CA  . VAL A 197 ? 0.2569 0.1043 0.2368 -0.0121 -0.0607 0.0034  215 VAL A CA  
2937 C C   . VAL A 197 ? 0.2571 0.0975 0.2451 -0.0131 -0.0685 0.0075  215 VAL A C   
2938 O O   . VAL A 197 ? 0.2470 0.1018 0.2680 -0.0142 -0.0621 0.0058  215 VAL A O   
2939 C CB  . VAL A 197 ? 0.2430 0.1074 0.2496 -0.0075 -0.0574 0.0094  215 VAL A CB  
2940 C CG1 . VAL A 197 ? 0.2793 0.1195 0.2350 -0.0151 -0.0670 0.0003  215 VAL A CG1 
2941 C CG2 . VAL A 197 ? 0.2431 0.1241 0.2611 0.0113  -0.0720 0.0285  215 VAL A CG2 
2951 N N   . GLN A 198 ? 0.2543 0.1066 0.2320 -0.0150 -0.0705 0.0261  216 GLN A N   
2952 C CA  . GLN A 198 ? 0.2867 0.1177 0.2255 -0.0160 -0.0926 0.0081  216 GLN A CA  
2953 C C   . GLN A 198 ? 0.3062 0.1199 0.2339 0.0145  -0.0869 -0.0070 216 GLN A C   
2954 O O   . GLN A 198 ? 0.3106 0.1130 0.2551 0.0053  -0.0829 -0.0162 216 GLN A O   
2955 C CB  . GLN A 198 ? 0.2970 0.1200 0.2273 -0.0256 -0.0738 0.0117  216 GLN A CB  
2956 C CG  . GLN A 198 ? 0.2903 0.1090 0.2358 -0.0216 -0.0686 0.0149  216 GLN A CG  
2957 C CD  . GLN A 198 ? 0.2697 0.1213 0.2416 0.0021  -0.0830 0.0069  216 GLN A CD  
2958 O OE1 . GLN A 198 ? 0.2674 0.1403 0.2592 0.0103  -0.0854 -0.0014 216 GLN A OE1 
2959 N NE2 . GLN A 198 ? 0.2900 0.1270 0.2365 -0.0235 -0.0811 0.0014  216 GLN A NE2 
2968 N N   . PRO A 199 ? 0.3100 0.1226 0.2375 0.0344  -0.0665 -0.0093 217 PRO A N   
2969 C CA  . PRO A 199 ? 0.2899 0.1262 0.2580 0.0462  -0.0701 -0.0059 217 PRO A CA  
2970 C C   . PRO A 199 ? 0.2676 0.1279 0.2496 0.0461  -0.0781 0.0001  217 PRO A C   
2971 O O   . PRO A 199 ? 0.2959 0.1314 0.2674 0.0388  -0.0464 -0.0186 217 PRO A O   
2972 C CB  . PRO A 199 ? 0.3201 0.1297 0.2780 0.0514  -0.0396 0.0074  217 PRO A CB  
2973 C CG  . PRO A 199 ? 0.3367 0.1254 0.2864 0.0433  -0.0183 -0.0010 217 PRO A CG  
2974 C CD  . PRO A 199 ? 0.3297 0.1277 0.2769 0.0379  -0.0323 -0.0139 217 PRO A CD  
2982 N N   . GLN A 200 ? 0.2599 0.1272 0.2320 0.0119  -0.0887 -0.0016 218 GLN A N   
2983 C CA  . GLN A 200 ? 0.2408 0.1409 0.2446 0.0161  -0.0700 0.0089  218 GLN A CA  
2984 C C   . GLN A 200 ? 0.2401 0.1472 0.2482 0.0195  -0.0892 -0.0054 218 GLN A C   
2985 O O   . GLN A 200 ? 0.2399 0.1514 0.2631 0.0069  -0.0933 0.0002  218 GLN A O   
2986 C CB  . GLN A 200 ? 0.2209 0.1185 0.2134 -0.0030 -0.0641 0.0040  218 GLN A CB  
2987 C CG  . GLN A 200 ? 0.1841 0.1254 0.2291 0.0059  -0.0529 0.0068  218 GLN A CG  
2988 C CD  . GLN A 200 ? 0.1940 0.1235 0.2332 0.0041  -0.0425 0.0033  218 GLN A CD  
2989 O OE1 . GLN A 200 ? 0.2112 0.1311 0.2307 0.0130  -0.0345 -0.0053 218 GLN A OE1 
2990 N NE2 . GLN A 200 ? 0.1894 0.1138 0.2367 -0.0092 -0.0522 0.0070  218 GLN A NE2 
2999 N N   . VAL A 201 ? 0.2352 0.1722 0.2781 0.0044  -0.1142 0.0151  219 VAL A N   
3000 C CA  . VAL A 201 ? 0.2517 0.1918 0.2782 -0.0018 -0.1094 0.0103  219 VAL A CA  
3001 C C   . VAL A 201 ? 0.2705 0.1931 0.2876 -0.0109 -0.0963 -0.0151 219 VAL A C   
3002 O O   . VAL A 201 ? 0.3014 0.2256 0.3118 -0.0234 -0.0915 -0.0166 219 VAL A O   
3003 C CB  . VAL A 201 ? 0.2737 0.2193 0.2876 0.0148  -0.1099 0.0333  219 VAL A CB  
3004 C CG1 . VAL A 201 ? 0.2997 0.2305 0.2982 -0.0114 -0.0989 0.0360  219 VAL A CG1 
3005 C CG2 . VAL A 201 ? 0.3292 0.2339 0.3110 0.0194  -0.0728 0.0391  219 VAL A CG2 
3015 N N   . SER A 202 ? 0.2303 0.1727 0.2891 0.0107  -0.1068 -0.0262 220 SER A N   
3016 C CA  . SER A 202 ? 0.2232 0.1814 0.3134 0.0038  -0.0960 -0.0132 220 SER A CA  
3017 C C   . SER A 202 ? 0.2152 0.1807 0.3206 0.0190  -0.1004 0.0061  220 SER A C   
3018 O O   . SER A 202 ? 0.2276 0.1925 0.3385 0.0056  -0.0875 0.0011  220 SER A O   
3019 C CB  . SER A 202 ? 0.2594 0.1950 0.3141 0.0088  -0.0666 -0.0290 220 SER A CB  
3020 O OG  . SER A 202 ? 0.2941 0.1942 0.3105 -0.0079 -0.0590 0.0015  220 SER A OG  
3026 N N   . ASN A 203 ? 0.2153 0.1768 0.3062 0.0062  -0.0984 0.0051  221 ASN A N   
3027 C CA  . ASN A 203 ? 0.2190 0.1636 0.3110 -0.0040 -0.0921 -0.0092 221 ASN A CA  
3028 C C   . ASN A 203 ? 0.2351 0.1521 0.3122 0.0001  -0.0520 -0.0077 221 ASN A C   
3029 O O   . ASN A 203 ? 0.2524 0.1555 0.3197 -0.0013 -0.0292 -0.0218 221 ASN A O   
3030 C CB  . ASN A 203 ? 0.2378 0.1737 0.3332 -0.0020 -0.1031 -0.0307 221 ASN A CB  
3031 C CG  . ASN A 203 ? 0.2426 0.1625 0.3443 -0.0195 -0.0841 -0.0230 221 ASN A CG  
3032 O OD1 . ASN A 203 ? 0.2405 0.1472 0.3310 0.0097  -0.0934 -0.0130 221 ASN A OD1 
3033 N ND2 . ASN A 203 ? 0.2618 0.1522 0.3474 -0.0425 -0.0854 -0.0202 221 ASN A ND2 
3040 N N   . SER A 204 ? 0.2412 0.1482 0.2971 -0.0068 -0.0752 -0.0027 222 SER A N   
3041 C CA  . SER A 204 ? 0.2243 0.1482 0.3128 0.0058  -0.0849 0.0065  222 SER A CA  
3042 C C   . SER A 204 ? 0.2316 0.1462 0.3074 0.0246  -0.0749 0.0066  222 SER A C   
3043 O O   . SER A 204 ? 0.2183 0.1580 0.3082 0.0269  -0.0848 -0.0063 222 SER A O   
3044 C CB  . SER A 204 ? 0.2330 0.1430 0.3344 0.0052  -0.0760 0.0043  222 SER A CB  
3045 O OG  . SER A 204 ? 0.2515 0.1338 0.3230 0.0114  -0.0879 0.0007  222 SER A OG  
3051 N N   . PRO A 205 ? 0.2266 0.1398 0.2891 0.0196  -0.0493 -0.0021 223 PRO A N   
3052 C CA  . PRO A 205 ? 0.2230 0.1313 0.2912 0.0133  -0.0458 -0.0075 223 PRO A CA  
3053 C C   . PRO A 205 ? 0.1938 0.1362 0.2899 0.0114  -0.0731 -0.0203 223 PRO A C   
3054 O O   . PRO A 205 ? 0.2174 0.1554 0.2945 0.0108  -0.0681 -0.0345 223 PRO A O   
3055 C CB  . PRO A 205 ? 0.2258 0.1456 0.2846 -0.0050 -0.0305 -0.0063 223 PRO A CB  
3056 C CG  . PRO A 205 ? 0.2344 0.1538 0.2827 0.0048  -0.0394 -0.0142 223 PRO A CG  
3057 C CD  . PRO A 205 ? 0.2357 0.1392 0.2970 0.0180  -0.0364 -0.0076 223 PRO A CD  
3065 N N   . LEU A 206 ? 0.2193 0.1249 0.3080 0.0131  -0.0567 -0.0096 224 LEU A N   
3066 C CA  . LEU A 206 ? 0.2179 0.1482 0.3101 0.0348  -0.0800 0.0120  224 LEU A CA  
3067 C C   . LEU A 206 ? 0.2082 0.1379 0.3037 0.0210  -0.0840 -0.0087 224 LEU A C   
3068 O O   . LEU A 206 ? 0.2112 0.1566 0.3469 0.0299  -0.0674 0.0078  224 LEU A O   
3069 C CB  . LEU A 206 ? 0.2207 0.1794 0.3398 0.0344  -0.0946 0.0215  224 LEU A CB  
3070 C CG  . LEU A 206 ? 0.2478 0.1790 0.3668 0.0287  -0.1057 0.0282  224 LEU A CG  
3071 C CD1 . LEU A 206 ? 0.2465 0.1893 0.3848 0.0129  -0.1113 0.0367  224 LEU A CD1 
3072 C CD2 . LEU A 206 ? 0.2992 0.1910 0.3958 0.0277  -0.0853 0.0096  224 LEU A CD2 
3084 N N   . ASP A 207 ? 0.2213 0.1245 0.2648 0.0169  -0.0925 -0.0082 225 ASP A N   
3085 C CA  . ASP A 207 ? 0.2012 0.1382 0.2522 0.0220  -0.0679 -0.0048 225 ASP A CA  
3086 C C   . ASP A 207 ? 0.1901 0.1339 0.2381 0.0313  -0.0482 0.0040  225 ASP A C   
3087 O O   . ASP A 207 ? 0.1889 0.1417 0.2282 0.0070  -0.0342 -0.0107 225 ASP A O   
3088 C CB  . ASP A 207 ? 0.1920 0.1476 0.2584 0.0343  -0.0620 0.0067  225 ASP A CB  
3089 C CG  . ASP A 207 ? 0.1887 0.1515 0.2808 0.0248  -0.0835 0.0104  225 ASP A CG  
3090 O OD1 . ASP A 207 ? 0.2352 0.1739 0.2804 0.0235  -0.0931 0.0101  225 ASP A OD1 
3091 O OD2 . ASP A 207 ? 0.2104 0.1555 0.2942 -0.0026 -0.0473 -0.0054 225 ASP A OD2 
3096 N N   . SER A 208 ? 0.2117 0.1273 0.2237 0.0288  -0.0470 0.0022  226 SER A N   
3097 C CA  . SER A 208 ? 0.1648 0.1143 0.2302 0.0148  -0.0688 0.0110  226 SER A CA  
3098 C C   . SER A 208 ? 0.1767 0.1061 0.2305 -0.0023 -0.0536 -0.0011 226 SER A C   
3099 O O   . SER A 208 ? 0.1913 0.1036 0.2315 -0.0105 -0.0435 -0.0009 226 SER A O   
3100 C CB  . SER A 208 ? 0.2024 0.1158 0.2394 -0.0039 -0.0637 0.0052  226 SER A CB  
3101 O OG  . SER A 208 ? 0.2261 0.1210 0.2220 -0.0189 -0.0662 -0.0119 226 SER A OG  
3107 N N   . SER A 209 ? 0.1784 0.1136 0.2171 -0.0031 -0.0396 -0.0104 227 SER A N   
3108 C CA  . SER A 209 ? 0.1864 0.1304 0.2389 -0.0029 -0.0334 -0.0020 227 SER A CA  
3109 C C   . SER A 209 ? 0.1829 0.1347 0.2285 -0.0047 -0.0607 -0.0061 227 SER A C   
3110 O O   . SER A 209 ? 0.1753 0.1327 0.2345 -0.0077 -0.0512 0.0188  227 SER A O   
3111 C CB  . SER A 209 ? 0.1756 0.1070 0.2343 0.0022  -0.0482 0.0155  227 SER A CB  
3112 O OG  . SER A 209 ? 0.1843 0.1184 0.2507 0.0147  -0.0382 0.0036  227 SER A OG  
3118 N N   . TYR A 210 ? 0.1954 0.1263 0.2223 0.0078  -0.0478 -0.0113 228 TYR A N   
3119 C CA  . TYR A 210 ? 0.1976 0.1457 0.2335 0.0264  -0.0414 -0.0074 228 TYR A CA  
3120 C C   . TYR A 210 ? 0.1971 0.1316 0.2278 -0.0010 -0.0480 -0.0089 228 TYR A C   
3121 O O   . TYR A 210 ? 0.2156 0.1310 0.2311 0.0051  -0.0304 -0.0082 228 TYR A O   
3122 C CB  . TYR A 210 ? 0.1931 0.1597 0.2274 0.0117  -0.0339 0.0016  228 TYR A CB  
3123 C CG  . TYR A 210 ? 0.1781 0.1643 0.2524 -0.0020 -0.0347 0.0011  228 TYR A CG  
3124 C CD1 . TYR A 210 ? 0.1551 0.1628 0.2674 -0.0062 -0.0361 -0.0062 228 TYR A CD1 
3125 C CD2 . TYR A 210 ? 0.1620 0.1449 0.2668 -0.0244 -0.0407 0.0037  228 TYR A CD2 
3126 C CE1 . TYR A 210 ? 0.2005 0.1775 0.2892 -0.0098 -0.0277 0.0211  228 TYR A CE1 
3127 C CE2 . TYR A 210 ? 0.1798 0.1658 0.2821 -0.0138 -0.0181 -0.0028 228 TYR A CE2 
3128 C CZ  . TYR A 210 ? 0.2024 0.1908 0.2985 -0.0227 -0.0249 0.0056  228 TYR A CZ  
3129 O OH  . TYR A 210 ? 0.2563 0.2228 0.3447 -0.0323 -0.0232 -0.0041 228 TYR A OH  
3139 N N   . LEU A 211 ? 0.2075 0.1370 0.2333 -0.0124 -0.0516 -0.0077 229 LEU A N   
3140 C CA  . LEU A 211 ? 0.2004 0.1310 0.2265 0.0125  -0.0195 -0.0009 229 LEU A CA  
3141 C C   . LEU A 211 ? 0.1964 0.1403 0.2337 -0.0066 -0.0447 -0.0085 229 LEU A C   
3142 O O   . LEU A 211 ? 0.1911 0.1347 0.2382 -0.0194 -0.0150 0.0082  229 LEU A O   
3143 C CB  . LEU A 211 ? 0.1804 0.1296 0.2360 0.0197  -0.0485 0.0005  229 LEU A CB  
3144 C CG  . LEU A 211 ? 0.1887 0.1362 0.2414 -0.0028 -0.0502 0.0094  229 LEU A CG  
3145 C CD1 . LEU A 211 ? 0.1844 0.1450 0.2540 0.0180  -0.0830 0.0085  229 LEU A CD1 
3146 C CD2 . LEU A 211 ? 0.1920 0.1419 0.2665 -0.0242 -0.0373 0.0068  229 LEU A CD2 
3158 N N   . PHE A 212 ? 0.1909 0.1380 0.2310 -0.0008 -0.0101 -0.0099 230 PHE A N   
3159 C CA  . PHE A 212 ? 0.1903 0.1373 0.2438 -0.0128 -0.0265 -0.0056 230 PHE A CA  
3160 C C   . PHE A 212 ? 0.2016 0.1509 0.2477 -0.0048 -0.0319 0.0156  230 PHE A C   
3161 O O   . PHE A 212 ? 0.2253 0.1630 0.2246 0.0118  -0.0183 0.0192  230 PHE A O   
3162 C CB  . PHE A 212 ? 0.2211 0.1407 0.2640 -0.0033 -0.0349 -0.0201 230 PHE A CB  
3163 C CG  . PHE A 212 ? 0.2145 0.1419 0.2848 0.0046  -0.0369 0.0005  230 PHE A CG  
3164 C CD1 . PHE A 212 ? 0.2419 0.1443 0.2817 0.0109  -0.0435 0.0115  230 PHE A CD1 
3165 C CD2 . PHE A 212 ? 0.2286 0.1235 0.3005 0.0177  -0.0578 0.0083  230 PHE A CD2 
3166 C CE1 . PHE A 212 ? 0.2668 0.1356 0.2826 0.0260  -0.0413 0.0033  230 PHE A CE1 
3167 C CE2 . PHE A 212 ? 0.2613 0.1470 0.3009 0.0312  -0.0420 0.0020  230 PHE A CE2 
3168 C CZ  . PHE A 212 ? 0.2758 0.1462 0.2933 0.0465  -0.0487 -0.0040 230 PHE A CZ  
3178 N N   . ASN A 213 ? 0.1971 0.1402 0.2638 -0.0129 -0.0084 0.0151  231 ASN A N   
3179 C CA  . ASN A 213 ? 0.2166 0.1539 0.2737 0.0078  -0.0164 0.0317  231 ASN A CA  
3180 C C   . ASN A 213 ? 0.2237 0.1522 0.2630 -0.0055 -0.0219 0.0371  231 ASN A C   
3181 O O   . ASN A 213 ? 0.2600 0.1458 0.2853 -0.0069 -0.0140 0.0271  231 ASN A O   
3182 C CB  . ASN A 213 ? 0.2241 0.1734 0.2942 -0.0060 -0.0056 0.0215  231 ASN A CB  
3183 C CG  . ASN A 213 ? 0.2264 0.2069 0.2874 -0.0030 0.0083  0.0163  231 ASN A CG  
3184 O OD1 . ASN A 213 ? 0.2338 0.2322 0.3041 0.0025  0.0307  0.0179  231 ASN A OD1 
3185 N ND2 . ASN A 213 ? 0.2918 0.2230 0.2662 0.0013  0.0312  0.0245  231 ASN A ND2 
3192 N N   . GLY A 214 ? 0.2122 0.1488 0.2401 -0.0279 -0.0249 0.0492  232 GLY A N   
3193 C CA  . GLY A 214 ? 0.2185 0.1694 0.2351 -0.0053 -0.0170 0.0229  232 GLY A CA  
3194 C C   . GLY A 214 ? 0.1962 0.1546 0.2407 -0.0093 -0.0367 0.0238  232 GLY A C   
3195 O O   . GLY A 214 ? 0.2286 0.1815 0.2503 -0.0086 -0.0257 0.0216  232 GLY A O   
3199 N N   . LYS A 215 ? 0.2125 0.1235 0.2296 -0.0106 -0.0269 0.0064  233 LYS A N   
3200 C CA  . LYS A 215 ? 0.1902 0.1154 0.2340 -0.0233 -0.0479 -0.0023 233 LYS A CA  
3201 C C   . LYS A 215 ? 0.1862 0.1193 0.2381 -0.0049 -0.0268 -0.0053 233 LYS A C   
3202 O O   . LYS A 215 ? 0.2067 0.1339 0.2466 -0.0022 -0.0243 0.0084  233 LYS A O   
3203 C CB  . LYS A 215 ? 0.2031 0.1310 0.2756 -0.0261 -0.0453 0.0073  233 LYS A CB  
3204 C CG  . LYS A 215 ? 0.2142 0.1400 0.3198 -0.0025 -0.0749 -0.0080 233 LYS A CG  
3205 C CD  . LYS A 215 ? 0.2550 0.1367 0.3523 -0.0094 -0.0924 -0.0114 233 LYS A CD  
3206 C CE  . LYS A 215 ? 0.2990 0.1669 0.3953 -0.0274 -0.1071 -0.0126 233 LYS A CE  
3207 N NZ  . LYS A 215 ? 0.3343 0.1941 0.4279 -0.0288 -0.1258 -0.0023 233 LYS A NZ  
3221 N N   . ASN A 216 ? 0.1945 0.1131 0.2278 -0.0138 -0.0257 0.0039  234 ASN A N   
3222 C CA  . ASN A 216 ? 0.1673 0.1285 0.2381 -0.0152 -0.0431 -0.0003 234 ASN A CA  
3223 C C   . ASN A 216 ? 0.1683 0.1360 0.2338 -0.0097 -0.0611 -0.0100 234 ASN A C   
3224 O O   . ASN A 216 ? 0.1933 0.1475 0.2568 -0.0233 -0.0498 -0.0105 234 ASN A O   
3225 C CB  . ASN A 216 ? 0.1745 0.1478 0.2424 -0.0050 -0.0561 -0.0007 234 ASN A CB  
3226 C CG  . ASN A 216 ? 0.1912 0.1423 0.2516 0.0072  -0.0472 0.0166  234 ASN A CG  
3227 O OD1 . ASN A 216 ? 0.1762 0.1463 0.2522 -0.0049 -0.0328 0.0051  234 ASN A OD1 
3228 N ND2 . ASN A 216 ? 0.2049 0.1476 0.2689 -0.0100 -0.0236 0.0299  234 ASN A ND2 
3235 N N   . VAL A 217 ? 0.1882 0.1219 0.2429 -0.0104 -0.0442 -0.0069 235 VAL A N   
3236 C CA  . VAL A 217 ? 0.2135 0.1171 0.2495 -0.0117 -0.0648 0.0080  235 VAL A CA  
3237 C C   . VAL A 217 ? 0.2145 0.1231 0.2533 -0.0317 -0.0791 0.0058  235 VAL A C   
3238 O O   . VAL A 217 ? 0.2176 0.1285 0.2503 -0.0236 -0.0685 0.0177  235 VAL A O   
3239 C CB  . VAL A 217 ? 0.2166 0.1186 0.2556 -0.0090 -0.0488 -0.0001 235 VAL A CB  
3240 C CG1 . VAL A 217 ? 0.2287 0.1222 0.2703 -0.0355 -0.0498 -0.0030 235 VAL A CG1 
3241 C CG2 . VAL A 217 ? 0.2485 0.1340 0.2666 -0.0083 -0.0398 -0.0168 235 VAL A CG2 
3251 N N   . GLN A 218 ? 0.2303 0.1252 0.2579 -0.0295 -0.0974 -0.0055 236 GLN A N   
3252 C CA  . GLN A 218 ? 0.2312 0.1324 0.2528 -0.0187 -0.0985 0.0029  236 GLN A CA  
3253 C C   . GLN A 218 ? 0.2356 0.1370 0.2679 -0.0230 -0.0956 -0.0017 236 GLN A C   
3254 O O   . GLN A 218 ? 0.2364 0.1654 0.2781 -0.0348 -0.0922 -0.0072 236 GLN A O   
3255 C CB  . GLN A 218 ? 0.2325 0.1322 0.2386 0.0012  -0.0936 0.0076  236 GLN A CB  
3256 C CG  . GLN A 218 ? 0.2569 0.1302 0.2257 -0.0024 -0.0904 0.0092  236 GLN A CG  
3257 C CD  . GLN A 218 ? 0.2788 0.1491 0.2564 -0.0040 -0.0723 0.0030  236 GLN A CD  
3258 O OE1 . GLN A 218 ? 0.2749 0.1785 0.2799 -0.0317 -0.0955 0.0108  236 GLN A OE1 
3259 N NE2 . GLN A 218 ? 0.2881 0.1521 0.2459 -0.0173 -0.0600 0.0057  236 GLN A NE2 
3268 N N   . ALA A 219 ? 0.2401 0.1217 0.2819 -0.0242 -0.0758 -0.0077 237 ALA A N   
3269 C CA  . ALA A 219 ? 0.2145 0.1287 0.2880 -0.0062 -0.0956 -0.0172 237 ALA A CA  
3270 C C   . ALA A 219 ? 0.2106 0.1349 0.2801 -0.0113 -0.0888 -0.0324 237 ALA A C   
3271 O O   . ALA A 219 ? 0.2194 0.1401 0.2778 -0.0408 -0.0733 -0.0264 237 ALA A O   
3272 C CB  . ALA A 219 ? 0.2151 0.1450 0.3055 0.0032  -0.0988 -0.0272 237 ALA A CB  
3278 N N   . GLN A 220 ? 0.2044 0.1438 0.2688 -0.0024 -0.0996 -0.0290 238 GLN A N   
3279 C CA  . GLN A 220 ? 0.1985 0.1286 0.2785 -0.0156 -0.0751 -0.0436 238 GLN A CA  
3280 C C   . GLN A 220 ? 0.2194 0.1497 0.2927 0.0081  -0.0781 -0.0525 238 GLN A C   
3281 O O   . GLN A 220 ? 0.2533 0.1551 0.3073 -0.0119 -0.0624 -0.0414 238 GLN A O   
3282 C CB  . GLN A 220 ? 0.2124 0.1375 0.2638 0.0029  -0.0736 -0.0101 238 GLN A CB  
3283 C CG  . GLN A 220 ? 0.2367 0.1446 0.2581 -0.0144 -0.0483 -0.0036 238 GLN A CG  
3284 C CD  . GLN A 220 ? 0.2264 0.1417 0.2401 -0.0096 -0.0495 -0.0102 238 GLN A CD  
3285 O OE1 . GLN A 220 ? 0.2431 0.1343 0.2169 -0.0302 -0.0528 -0.0256 238 GLN A OE1 
3286 N NE2 . GLN A 220 ? 0.2431 0.1395 0.2407 -0.0072 -0.0629 -0.0251 238 GLN A NE2 
3295 N N   . ALA A 221 ? 0.2000 0.1560 0.3176 -0.0072 -0.0441 -0.0574 239 ALA A N   
3296 C CA  . ALA A 221 ? 0.2287 0.1627 0.3336 -0.0145 -0.0720 -0.0372 239 ALA A CA  
3297 C C   . ALA A 221 ? 0.2537 0.1676 0.3529 -0.0251 -0.0648 -0.0287 239 ALA A C   
3298 O O   . ALA A 221 ? 0.2804 0.1770 0.3799 -0.0401 -0.0418 -0.0184 239 ALA A O   
3299 C CB  . ALA A 221 ? 0.2629 0.1563 0.3391 0.0089  -0.0675 -0.0516 239 ALA A CB  
3305 N N   . VAL A 222 ? 0.2696 0.1718 0.3404 -0.0170 -0.0723 -0.0043 240 VAL A N   
3306 C CA  . VAL A 222 ? 0.2707 0.1821 0.3566 -0.0125 -0.0596 -0.0204 240 VAL A CA  
3307 C C   . VAL A 222 ? 0.2439 0.1698 0.3595 -0.0460 -0.0678 -0.0243 240 VAL A C   
3308 O O   . VAL A 222 ? 0.2759 0.1686 0.3832 -0.0578 -0.0538 -0.0139 240 VAL A O   
3309 C CB  . VAL A 222 ? 0.3220 0.1912 0.3706 0.0154  -0.0398 -0.0021 240 VAL A CB  
3310 C CG1 . VAL A 222 ? 0.3396 0.1868 0.3786 0.0016  -0.0256 0.0078  240 VAL A CG1 
3311 C CG2 . VAL A 222 ? 0.3283 0.2336 0.3678 0.0273  -0.0402 0.0138  240 VAL A CG2 
3321 N N   . CYS A 223 ? 0.2531 0.1588 0.3250 -0.0501 -0.0412 -0.0223 241 CYS A N   
3322 C CA  . CYS A 223 ? 0.2627 0.1520 0.3100 -0.0275 -0.0504 -0.0177 241 CYS A CA  
3323 C C   . CYS A 223 ? 0.2665 0.1627 0.2983 -0.0052 -0.0747 -0.0242 241 CYS A C   
3324 O O   . CYS A 223 ? 0.2929 0.1901 0.3021 0.0063  -0.0554 -0.0265 241 CYS A O   
3325 C CB  . CYS A 223 ? 0.2683 0.1391 0.3093 -0.0212 -0.0502 -0.0066 241 CYS A CB  
3326 S SG  . CYS A 223 ? 0.2688 0.1600 0.3196 -0.0311 -0.0680 -0.0037 241 CYS A SG  
3331 N N   . GLY A 224 ? 0.2562 0.1732 0.3091 -0.0160 -0.1024 -0.0302 242 GLY A N   
3332 C CA  . GLY A 224 ? 0.2738 0.1807 0.3120 -0.0187 -0.1204 -0.0453 242 GLY A CA  
3333 C C   . GLY A 224 ? 0.2871 0.1863 0.3126 -0.0124 -0.1395 -0.0352 242 GLY A C   
3334 O O   . GLY A 224 ? 0.2628 0.1594 0.3193 -0.0248 -0.1234 -0.0430 242 GLY A O   
3338 N N   . PRO A 225 ? 0.3242 0.2013 0.3421 -0.0015 -0.1351 -0.0311 243 PRO A N   
3339 C CA  . PRO A 225 ? 0.3642 0.2192 0.3475 0.0058  -0.1115 -0.0120 243 PRO A CA  
3340 C C   . PRO A 225 ? 0.3512 0.2130 0.3426 -0.0143 -0.1072 -0.0030 243 PRO A C   
3341 O O   . PRO A 225 ? 0.3781 0.2078 0.3726 -0.0339 -0.0781 -0.0122 243 PRO A O   
3342 C CB  . PRO A 225 ? 0.3741 0.2332 0.3553 0.0223  -0.1134 -0.0175 243 PRO A CB  
3343 C CG  . PRO A 225 ? 0.3596 0.2225 0.3518 0.0379  -0.1379 -0.0307 243 PRO A CG  
3344 C CD  . PRO A 225 ? 0.3476 0.2213 0.3555 0.0137  -0.1436 -0.0320 243 PRO A CD  
3352 N N   . LEU A 226 ? 0.3246 0.1960 0.3081 -0.0295 -0.1391 -0.0015 244 LEU A N   
3353 C CA  . LEU A 226 ? 0.3263 0.2087 0.2903 -0.0555 -0.1313 -0.0002 244 LEU A CA  
3354 C C   . LEU A 226 ? 0.3321 0.2196 0.2790 -0.0537 -0.0991 -0.0137 244 LEU A C   
3355 O O   . LEU A 226 ? 0.3514 0.2598 0.2763 -0.0813 -0.0976 0.0073  244 LEU A O   
3356 C CB  . LEU A 226 ? 0.3399 0.2266 0.2937 -0.0636 -0.1411 0.0106  244 LEU A CB  
3357 C CG  . LEU A 226 ? 0.3754 0.2324 0.2944 -0.0597 -0.1403 0.0147  244 LEU A CG  
3358 C CD1 . LEU A 226 ? 0.3972 0.2658 0.3113 -0.0538 -0.1055 0.0185  244 LEU A CD1 
3359 C CD2 . LEU A 226 ? 0.4110 0.2244 0.3004 -0.0522 -0.1259 0.0325  244 LEU A CD2 
3371 N N   . PHE A 227 ? 0.2970 0.1924 0.2676 -0.0550 -0.0966 -0.0363 245 PHE A N   
3372 C CA  . PHE A 227 ? 0.2521 0.1753 0.2623 -0.0390 -0.0683 -0.0442 245 PHE A CA  
3373 C C   . PHE A 227 ? 0.2500 0.1683 0.2581 -0.0216 -0.0845 -0.0360 245 PHE A C   
3374 O O   . PHE A 227 ? 0.2938 0.1708 0.2674 -0.0102 -0.0784 -0.0663 245 PHE A O   
3375 C CB  . PHE A 227 ? 0.2363 0.1749 0.2856 -0.0269 -0.0413 -0.0069 245 PHE A CB  
3376 C CG  . PHE A 227 ? 0.2295 0.1709 0.3055 -0.0169 -0.0525 -0.0243 245 PHE A CG  
3377 C CD1 . PHE A 227 ? 0.2870 0.1580 0.3294 -0.0001 -0.0347 0.0025  245 PHE A CD1 
3378 C CD2 . PHE A 227 ? 0.2313 0.1898 0.3144 0.0019  -0.0607 -0.0226 245 PHE A CD2 
3379 C CE1 . PHE A 227 ? 0.2911 0.1691 0.3450 0.0121  -0.0322 -0.0013 245 PHE A CE1 
3380 C CE2 . PHE A 227 ? 0.2651 0.1863 0.3243 0.0055  -0.0429 -0.0127 245 PHE A CE2 
3381 C CZ  . PHE A 227 ? 0.2816 0.1890 0.3307 0.0221  -0.0504 0.0028  245 PHE A CZ  
3391 N N   . VAL A 228 ? 0.2226 0.1655 0.2527 -0.0135 -0.0628 -0.0223 246 VAL A N   
3392 C CA  . VAL A 228 ? 0.2481 0.1618 0.2450 -0.0156 -0.0701 -0.0201 246 VAL A CA  
3393 C C   . VAL A 228 ? 0.2416 0.1666 0.2318 0.0023  -0.0660 -0.0181 246 VAL A C   
3394 O O   . VAL A 228 ? 0.2686 0.1764 0.2174 0.0128  -0.0611 -0.0174 246 VAL A O   
3395 C CB  . VAL A 228 ? 0.2790 0.1713 0.2422 -0.0270 -0.0574 -0.0049 246 VAL A CB  
3396 C CG1 . VAL A 228 ? 0.2658 0.2038 0.2433 -0.0304 -0.0756 0.0118  246 VAL A CG1 
3397 C CG2 . VAL A 228 ? 0.2914 0.1807 0.2301 -0.0423 -0.0437 -0.0031 246 VAL A CG2 
3407 N N   . ILE A 229 ? 0.2362 0.1486 0.2400 -0.0127 -0.0600 -0.0358 247 ILE A N   
3408 C CA  . ILE A 229 ? 0.2627 0.1399 0.2357 -0.0143 -0.0729 -0.0129 247 ILE A CA  
3409 C C   . ILE A 229 ? 0.2583 0.1320 0.2204 -0.0038 -0.0824 0.0051  247 ILE A C   
3410 O O   . ILE A 229 ? 0.2365 0.1447 0.2287 0.0075  -0.0731 0.0153  247 ILE A O   
3411 C CB  . ILE A 229 ? 0.3266 0.1365 0.2609 -0.0053 -0.0447 0.0143  247 ILE A CB  
3412 C CG1 . ILE A 229 ? 0.3515 0.1360 0.2410 -0.0158 -0.0417 0.0357  247 ILE A CG1 
3413 C CG2 . ILE A 229 ? 0.3489 0.1347 0.2684 -0.0016 -0.0640 0.0194  247 ILE A CG2 
3414 C CD1 . ILE A 229 ? 0.3308 0.1727 0.2532 -0.0083 -0.0767 0.0341  247 ILE A CD1 
3426 N N   . ASP A 230 ? 0.2504 0.1065 0.2069 -0.0201 -0.0815 0.0117  248 ASP A N   
3427 C CA  . ASP A 230 ? 0.2355 0.1163 0.1932 -0.0286 -0.0789 -0.0110 248 ASP A CA  
3428 C C   . ASP A 230 ? 0.2069 0.1247 0.2192 -0.0078 -0.0717 -0.0095 248 ASP A C   
3429 O O   . ASP A 230 ? 0.2188 0.1267 0.2331 -0.0130 -0.0508 -0.0101 248 ASP A O   
3430 C CB  . ASP A 230 ? 0.2467 0.1350 0.2241 -0.0216 -0.0690 -0.0052 248 ASP A CB  
3431 C CG  . ASP A 230 ? 0.2574 0.1489 0.2445 -0.0128 -0.0520 -0.0079 248 ASP A CG  
3432 O OD1 . ASP A 230 ? 0.2522 0.1799 0.2499 0.0236  -0.0266 0.0019  248 ASP A OD1 
3433 O OD2 . ASP A 230 ? 0.2806 0.1344 0.2450 -0.0116 -0.0754 0.0011  248 ASP A OD2 
3438 N N   . HIS A 231 ? 0.2074 0.1116 0.2215 -0.0217 -0.0716 -0.0067 249 HIS A N   
3439 C CA  . HIS A 231 ? 0.2114 0.1172 0.2028 -0.0170 -0.0760 -0.0119 249 HIS A CA  
3440 C C   . HIS A 231 ? 0.2124 0.1253 0.2121 -0.0103 -0.0812 0.0004  249 HIS A C   
3441 O O   . HIS A 231 ? 0.2267 0.1376 0.2215 -0.0258 -0.0729 0.0260  249 HIS A O   
3442 C CB  . HIS A 231 ? 0.2270 0.1228 0.2128 -0.0104 -0.0768 -0.0059 249 HIS A CB  
3443 C CG  . HIS A 231 ? 0.2538 0.1157 0.2326 0.0012  -0.0804 0.0117  249 HIS A CG  
3444 N ND1 . HIS A 231 ? 0.2588 0.1061 0.2317 -0.0224 -0.0835 0.0252  249 HIS A ND1 
3445 C CD2 . HIS A 231 ? 0.2663 0.1256 0.2480 -0.0263 -0.0765 0.0150  249 HIS A CD2 
3446 C CE1 . HIS A 231 ? 0.2919 0.1062 0.2442 -0.0268 -0.0775 0.0470  249 HIS A CE1 
3447 N NE2 . HIS A 231 ? 0.2917 0.1178 0.2405 -0.0180 -0.0956 0.0401  249 HIS A NE2 
3455 N N   . ALA A 232 ? 0.2131 0.1186 0.2162 0.0023  -0.0626 0.0005  250 ALA A N   
3456 C CA  . ALA A 232 ? 0.2067 0.1105 0.2256 -0.0092 -0.0812 0.0111  250 ALA A CA  
3457 C C   . ALA A 232 ? 0.2000 0.1235 0.2159 -0.0138 -0.0653 0.0192  250 ALA A C   
3458 O O   . ALA A 232 ? 0.2252 0.1137 0.1998 -0.0135 -0.0449 0.0259  250 ALA A O   
3459 C CB  . ALA A 232 ? 0.2266 0.1366 0.2275 -0.0329 -0.0787 0.0184  250 ALA A CB  
3465 N N   . GLY A 233 ? 0.1967 0.1079 0.1924 -0.0082 -0.0556 -0.0061 251 GLY A N   
3466 C CA  . GLY A 233 ? 0.2274 0.1136 0.2278 -0.0049 -0.0656 -0.0048 251 GLY A CA  
3467 C C   . GLY A 233 ? 0.2191 0.0918 0.2145 -0.0268 -0.0694 0.0059  251 GLY A C   
3468 O O   . GLY A 233 ? 0.2420 0.0922 0.2247 -0.0130 -0.0563 0.0048  251 GLY A O   
3472 N N   . SER A 234 ? 0.2245 0.1111 0.2085 -0.0212 -0.0750 -0.0068 252 SER A N   
3473 C CA  . SER A 234 ? 0.2186 0.1142 0.2159 -0.0120 -0.0748 0.0078  252 SER A CA  
3474 C C   . SER A 234 ? 0.2091 0.1077 0.2242 0.0095  -0.0856 0.0028  252 SER A C   
3475 O O   . SER A 234 ? 0.2218 0.0979 0.2448 -0.0050 -0.0695 -0.0010 252 SER A O   
3476 C CB  . SER A 234 ? 0.2269 0.1148 0.2165 -0.0110 -0.0771 0.0145  252 SER A CB  
3477 O OG  . SER A 234 ? 0.2230 0.1122 0.2514 -0.0121 -0.0845 0.0285  252 SER A OG  
3483 N N   . LEU A 235 ? 0.2118 0.1209 0.2192 -0.0031 -0.0909 0.0237  253 LEU A N   
3484 C CA  . LEU A 235 ? 0.2175 0.1053 0.2248 -0.0017 -0.0716 -0.0021 253 LEU A CA  
3485 C C   . LEU A 235 ? 0.2130 0.1048 0.2211 -0.0234 -0.0896 0.0047  253 LEU A C   
3486 O O   . LEU A 235 ? 0.2697 0.1146 0.2203 -0.0359 -0.0932 0.0075  253 LEU A O   
3487 C CB  . LEU A 235 ? 0.1953 0.1005 0.2166 -0.0113 -0.0816 0.0065  253 LEU A CB  
3488 C CG  . LEU A 235 ? 0.2218 0.0990 0.2208 -0.0032 -0.0727 0.0226  253 LEU A CG  
3489 C CD1 . LEU A 235 ? 0.2599 0.0970 0.2275 -0.0216 -0.0805 0.0198  253 LEU A CD1 
3490 C CD2 . LEU A 235 ? 0.2126 0.0927 0.2158 -0.0066 -0.0549 0.0090  253 LEU A CD2 
3502 N N   . THR A 236 ? 0.2108 0.1121 0.2257 -0.0156 -0.0822 0.0110  254 THR A N   
3503 C CA  . THR A 236 ? 0.2041 0.0998 0.2243 -0.0246 -0.0708 0.0060  254 THR A CA  
3504 C C   . THR A 236 ? 0.2060 0.1173 0.2288 -0.0208 -0.0385 -0.0056 254 THR A C   
3505 O O   . THR A 236 ? 0.2380 0.1247 0.2306 -0.0051 -0.0392 -0.0063 254 THR A O   
3506 C CB  . THR A 236 ? 0.2293 0.1158 0.2373 -0.0167 -0.0437 0.0047  254 THR A CB  
3507 O OG1 . THR A 236 ? 0.2193 0.1218 0.2497 -0.0078 -0.0441 0.0107  254 THR A OG1 
3508 C CG2 . THR A 236 ? 0.2142 0.1164 0.2503 -0.0122 -0.0448 0.0269  254 THR A CG2 
3516 N N   . SER A 237 ? 0.2113 0.1086 0.2282 -0.0235 -0.0397 -0.0261 255 SER A N   
3517 C CA  . SER A 237 ? 0.2269 0.1257 0.2433 -0.0059 -0.0618 -0.0064 255 SER A CA  
3518 C C   . SER A 237 ? 0.2449 0.1168 0.2462 -0.0011 -0.0633 -0.0052 255 SER A C   
3519 O O   . SER A 237 ? 0.2563 0.1235 0.2456 -0.0189 -0.0536 0.0048  255 SER A O   
3520 C CB  . SER A 237 ? 0.2375 0.1290 0.2345 -0.0115 -0.0410 -0.0163 255 SER A CB  
3521 O OG  . SER A 237 ? 0.2392 0.1240 0.2193 -0.0267 -0.0192 -0.0314 255 SER A OG  
3527 N N   . GLN A 238 ? 0.2617 0.1010 0.2531 -0.0315 -0.0836 0.0022  256 GLN A N   
3528 C CA  . GLN A 238 ? 0.2673 0.0871 0.2697 -0.0274 -0.0497 -0.0045 256 GLN A CA  
3529 C C   . GLN A 238 ? 0.2840 0.1003 0.2692 -0.0424 -0.0633 -0.0050 256 GLN A C   
3530 O O   . GLN A 238 ? 0.3057 0.1138 0.2538 -0.0374 -0.0680 -0.0036 256 GLN A O   
3531 C CB  . GLN A 238 ? 0.2731 0.0851 0.2740 -0.0240 -0.0370 -0.0245 256 GLN A CB  
3532 C CG  . GLN A 238 ? 0.2622 0.0902 0.2870 -0.0156 -0.0717 -0.0119 256 GLN A CG  
3533 C CD  . GLN A 238 ? 0.3036 0.0963 0.3157 -0.0243 -0.0582 -0.0103 256 GLN A CD  
3534 O OE1 . GLN A 238 ? 0.2935 0.0951 0.3233 -0.0187 -0.0511 -0.0046 256 GLN A OE1 
3535 N NE2 . GLN A 238 ? 0.3282 0.1021 0.3180 -0.0357 -0.0584 -0.0031 256 GLN A NE2 
3544 N N   . PHE A 239 ? 0.2863 0.1194 0.2634 -0.0424 -0.0837 -0.0048 257 PHE A N   
3545 C CA  . PHE A 239 ? 0.2641 0.1302 0.2533 -0.0284 -0.0853 0.0023  257 PHE A CA  
3546 C C   . PHE A 239 ? 0.2452 0.1293 0.2387 -0.0346 -0.0525 -0.0077 257 PHE A C   
3547 O O   . PHE A 239 ? 0.2321 0.1430 0.2615 -0.0372 -0.0259 0.0095  257 PHE A O   
3548 C CB  . PHE A 239 ? 0.2764 0.1435 0.2853 -0.0208 -0.0834 -0.0009 257 PHE A CB  
3549 C CG  . PHE A 239 ? 0.2777 0.1387 0.2886 -0.0126 -0.0852 0.0079  257 PHE A CG  
3550 C CD1 . PHE A 239 ? 0.2382 0.1506 0.2980 -0.0011 -0.0889 0.0200  257 PHE A CD1 
3551 C CD2 . PHE A 239 ? 0.2713 0.1551 0.2826 -0.0039 -0.1003 0.0205  257 PHE A CD2 
3552 C CE1 . PHE A 239 ? 0.2643 0.1606 0.3134 0.0032  -0.0661 0.0342  257 PHE A CE1 
3553 C CE2 . PHE A 239 ? 0.2760 0.1570 0.2930 0.0018  -0.1001 0.0273  257 PHE A CE2 
3554 C CZ  . PHE A 239 ? 0.2838 0.1617 0.3168 0.0143  -0.0756 0.0232  257 PHE A CZ  
3564 N N   . SER A 240 ? 0.2432 0.1208 0.2472 -0.0586 -0.0394 -0.0194 258 SER A N   
3565 C CA  . SER A 240 ? 0.2296 0.1139 0.2424 -0.0286 -0.0372 -0.0045 258 SER A CA  
3566 C C   . SER A 240 ? 0.2390 0.1093 0.2478 -0.0290 -0.0495 -0.0080 258 SER A C   
3567 O O   . SER A 240 ? 0.2654 0.1087 0.2545 -0.0384 -0.0177 -0.0032 258 SER A O   
3568 C CB  . SER A 240 ? 0.2406 0.1092 0.2342 -0.0297 -0.0541 -0.0022 258 SER A CB  
3569 O OG  . SER A 240 ? 0.2463 0.1226 0.2304 -0.0248 -0.0533 0.0148  258 SER A OG  
3575 N N   . TYR A 241 ? 0.2612 0.1045 0.2412 -0.0260 -0.0582 -0.0209 259 TYR A N   
3576 C CA  . TYR A 241 ? 0.2462 0.1263 0.2404 -0.0117 -0.0665 -0.0036 259 TYR A CA  
3577 C C   . TYR A 241 ? 0.2548 0.1156 0.2391 -0.0200 -0.0678 0.0042  259 TYR A C   
3578 O O   . TYR A 241 ? 0.2720 0.1181 0.2483 -0.0430 -0.0478 0.0108  259 TYR A O   
3579 C CB  . TYR A 241 ? 0.2438 0.1420 0.2751 -0.0066 -0.0549 0.0159  259 TYR A CB  
3580 C CG  . TYR A 241 ? 0.2423 0.1260 0.2959 -0.0302 -0.0447 0.0255  259 TYR A CG  
3581 C CD1 . TYR A 241 ? 0.2419 0.1215 0.2724 -0.0138 -0.0536 0.0392  259 TYR A CD1 
3582 C CD2 . TYR A 241 ? 0.2709 0.1260 0.3121 -0.0170 -0.0500 0.0468  259 TYR A CD2 
3583 C CE1 . TYR A 241 ? 0.2670 0.1180 0.2916 -0.0153 -0.0684 0.0321  259 TYR A CE1 
3584 C CE2 . TYR A 241 ? 0.3062 0.1307 0.3077 -0.0011 -0.0510 0.0375  259 TYR A CE2 
3585 C CZ  . TYR A 241 ? 0.2839 0.1363 0.3107 -0.0164 -0.0732 0.0306  259 TYR A CZ  
3586 O OH  . TYR A 241 ? 0.3127 0.1299 0.3193 -0.0219 -0.0787 0.0387  259 TYR A OH  
3596 N N   . VAL A 242 ? 0.2653 0.1119 0.2231 -0.0382 -0.0645 -0.0063 260 VAL A N   
3597 C CA  . VAL A 242 ? 0.2780 0.1195 0.2359 -0.0561 -0.0550 -0.0016 260 VAL A CA  
3598 C C   . VAL A 242 ? 0.2595 0.1253 0.2276 -0.0380 -0.0607 0.0254  260 VAL A C   
3599 O O   . VAL A 242 ? 0.2811 0.1605 0.2315 -0.0327 -0.0471 0.0230  260 VAL A O   
3600 C CB  . VAL A 242 ? 0.3329 0.1269 0.2574 -0.0591 -0.0473 -0.0289 260 VAL A CB  
3601 C CG1 . VAL A 242 ? 0.3683 0.1518 0.2768 -0.0669 -0.0659 -0.0225 260 VAL A CG1 
3602 C CG2 . VAL A 242 ? 0.3410 0.1302 0.2431 -0.0242 -0.0594 -0.0639 260 VAL A CG2 
3612 N N   . VAL A 243 ? 0.2561 0.1197 0.2382 -0.0510 -0.0365 0.0309  261 VAL A N   
3613 C CA  . VAL A 243 ? 0.2615 0.1285 0.2564 -0.0211 -0.0592 0.0343  261 VAL A CA  
3614 C C   . VAL A 243 ? 0.2526 0.1201 0.2353 -0.0196 -0.0723 0.0429  261 VAL A C   
3615 O O   . VAL A 243 ? 0.2428 0.1320 0.2391 -0.0230 -0.0753 0.0024  261 VAL A O   
3616 C CB  . VAL A 243 ? 0.2494 0.1143 0.2500 -0.0510 -0.0824 0.0272  261 VAL A CB  
3617 C CG1 . VAL A 243 ? 0.2520 0.1413 0.2561 -0.0481 -0.0664 0.0145  261 VAL A CG1 
3618 C CG2 . VAL A 243 ? 0.2815 0.1385 0.2719 -0.0564 -0.0601 0.0425  261 VAL A CG2 
3628 N N   . GLY A 244 ? 0.2422 0.1184 0.2426 -0.0243 -0.0681 0.0305  262 GLY A N   
3629 C CA  . GLY A 244 ? 0.2624 0.1194 0.2236 -0.0278 -0.0797 0.0249  262 GLY A CA  
3630 C C   . GLY A 244 ? 0.2544 0.1268 0.2181 -0.0169 -0.0628 0.0301  262 GLY A C   
3631 O O   . GLY A 244 ? 0.2484 0.1463 0.2352 -0.0248 -0.0395 0.0244  262 GLY A O   
3635 N N   . ARG A 245 ? 0.2673 0.1115 0.2249 -0.0045 -0.0509 0.0422  263 ARG A N   
3636 C CA  . ARG A 245 ? 0.2837 0.1022 0.2571 -0.0151 -0.0455 0.0386  263 ARG A CA  
3637 C C   . ARG A 245 ? 0.2592 0.1210 0.2513 -0.0173 -0.0678 0.0495  263 ARG A C   
3638 O O   . ARG A 245 ? 0.2905 0.1489 0.2484 -0.0296 -0.0441 0.0508  263 ARG A O   
3639 C CB  . ARG A 245 ? 0.2989 0.1080 0.2800 -0.0223 -0.0299 0.0396  263 ARG A CB  
3640 C CG  . ARG A 245 ? 0.3136 0.1106 0.3186 -0.0050 -0.0569 0.0578  263 ARG A CG  
3641 C CD  . ARG A 245 ? 0.3297 0.1150 0.3508 -0.0267 -0.0687 0.0478  263 ARG A CD  
3642 N NE  . ARG A 245 ? 0.3622 0.1223 0.3656 -0.0259 -0.0690 0.0265  263 ARG A NE  
3643 C CZ  . ARG A 245 ? 0.3617 0.1611 0.3756 -0.0507 -0.0702 0.0210  263 ARG A CZ  
3644 N NH1 . ARG A 245 ? 0.3804 0.1695 0.3891 -0.0368 -0.0512 0.0117  263 ARG A NH1 
3645 N NH2 . ARG A 245 ? 0.4031 0.1944 0.3941 -0.0331 -0.0499 0.0223  263 ARG A NH2 
3659 N N   . SER A 246 ? 0.2535 0.1364 0.2589 -0.0249 -0.0716 0.0391  264 SER A N   
3660 C CA  . SER A 246 ? 0.2713 0.1398 0.2733 -0.0266 -0.0291 0.0401  264 SER A CA  
3661 C C   . SER A 246 ? 0.2606 0.1374 0.2579 -0.0324 -0.0289 0.0423  264 SER A C   
3662 O O   . SER A 246 ? 0.2690 0.1412 0.2583 -0.0062 -0.0309 0.0527  264 SER A O   
3663 C CB  . SER A 246 ? 0.2744 0.1351 0.2884 -0.0451 -0.0288 0.0307  264 SER A CB  
3664 O OG  . SER A 246 ? 0.2756 0.1378 0.3124 -0.0195 -0.0265 0.0451  264 SER A OG  
3670 N N   . ALA A 247 ? 0.2592 0.1501 0.2537 -0.0225 -0.0292 0.0365  265 ALA A N   
3671 C CA  . ALA A 247 ? 0.2765 0.1601 0.2281 -0.0156 -0.0381 0.0464  265 ALA A CA  
3672 C C   . ALA A 247 ? 0.2661 0.1590 0.2420 -0.0156 -0.0422 0.0504  265 ALA A C   
3673 O O   . ALA A 247 ? 0.2725 0.1597 0.2388 -0.0218 -0.0480 0.0422  265 ALA A O   
3674 C CB  . ALA A 247 ? 0.2819 0.1600 0.2328 -0.0209 -0.0379 0.0353  265 ALA A CB  
3680 N N   . LEU A 248 ? 0.2750 0.1731 0.2480 -0.0122 -0.0480 0.0399  266 LEU A N   
3681 C CA  . LEU A 248 ? 0.2690 0.1961 0.2512 0.0012  -0.0541 0.0516  266 LEU A CA  
3682 C C   . LEU A 248 ? 0.2984 0.2055 0.2563 0.0078  -0.0599 0.0770  266 LEU A C   
3683 O O   . LEU A 248 ? 0.3075 0.2314 0.2570 -0.0006 -0.0437 0.0600  266 LEU A O   
3684 C CB  . LEU A 248 ? 0.2696 0.2103 0.2552 0.0079  -0.0548 0.0549  266 LEU A CB  
3685 C CG  . LEU A 248 ? 0.2691 0.1942 0.2777 -0.0032 -0.0479 0.0389  266 LEU A CG  
3686 C CD1 . LEU A 248 ? 0.2769 0.2071 0.3046 -0.0153 -0.0132 0.0410  266 LEU A CD1 
3687 C CD2 . LEU A 248 ? 0.2626 0.2103 0.2789 -0.0188 -0.0685 0.0348  266 LEU A CD2 
3699 N N   . ARG A 249 ? 0.3413 0.1936 0.2605 -0.0033 -0.0458 0.1084  267 ARG A N   
3700 C CA  . ARG A 249 ? 0.3658 0.1906 0.2962 -0.0014 -0.0085 0.1187  267 ARG A CA  
3701 C C   . ARG A 249 ? 0.3552 0.1945 0.3017 -0.0053 -0.0181 0.1022  267 ARG A C   
3702 O O   . ARG A 249 ? 0.3817 0.2101 0.3235 -0.0115 -0.0133 0.0973  267 ARG A O   
3703 C CB  . ARG A 249 ? 0.4469 0.2283 0.3587 -0.0119 0.0459  0.1021  267 ARG A CB  
3704 C CG  . ARG A 249 ? 0.5611 0.2982 0.4360 0.0067  0.0548  0.0836  267 ARG A CG  
3705 C CD  . ARG A 249 ? 0.6105 0.3413 0.4935 0.0320  0.0724  0.0891  267 ARG A CD  
3706 N NE  . ARG A 249 ? 0.6312 0.3868 0.5413 0.0780  0.0693  0.0917  267 ARG A NE  
3707 C CZ  . ARG A 249 ? 0.6679 0.4457 0.5631 0.0745  0.0567  0.0759  267 ARG A CZ  
3708 N NH1 . ARG A 249 ? 0.6731 0.4646 0.5635 0.0726  0.0332  0.0708  267 ARG A NH1 
3709 N NH2 . ARG A 249 ? 0.6756 0.4614 0.5668 0.0704  0.0462  0.0819  267 ARG A NH2 
3723 N N   . SER A 250 ? 0.3355 0.1802 0.3101 0.0003  -0.0051 0.0786  268 SER A N   
3724 C CA  . SER A 250 ? 0.3137 0.2024 0.3162 0.0028  -0.0098 0.0817  268 SER A CA  
3725 C C   . SER A 250 ? 0.3359 0.2124 0.3195 -0.0066 0.0150  0.0935  268 SER A C   
3726 O O   . SER A 250 ? 0.3336 0.2214 0.3198 -0.0291 0.0089  0.0833  268 SER A O   
3727 C CB  . SER A 250 ? 0.2909 0.2115 0.3167 -0.0003 -0.0122 0.0698  268 SER A CB  
3728 O OG  . SER A 250 ? 0.2726 0.2434 0.3152 -0.0152 -0.0108 0.0477  268 SER A OG  
3734 N N   . THR A 251 ? 0.3813 0.2377 0.3335 -0.0117 0.0316  0.0972  269 THR A N   
3735 C CA  . THR A 251 ? 0.4310 0.2604 0.3187 -0.0319 0.0614  0.0834  269 THR A CA  
3736 C C   . THR A 251 ? 0.4141 0.2663 0.2844 -0.0308 0.0281  0.0652  269 THR A C   
3737 O O   . THR A 251 ? 0.4696 0.3070 0.2858 -0.0131 0.0620  0.0637  269 THR A O   
3738 C CB  . THR A 251 ? 0.4932 0.2819 0.3599 -0.0297 0.0920  0.0969  269 THR A CB  
3739 O OG1 . THR A 251 ? 0.4950 0.3125 0.3775 -0.0418 0.1232  0.1140  269 THR A OG1 
3740 C CG2 . THR A 251 ? 0.5395 0.2751 0.3781 -0.0245 0.0956  0.0949  269 THR A CG2 
3748 N N   . THR A 252 ? 0.3798 0.2305 0.2673 -0.0389 0.0088  0.0697  270 THR A N   
3749 C CA  . THR A 252 ? 0.3296 0.2310 0.2778 -0.0350 -0.0059 0.0390  270 THR A CA  
3750 C C   . THR A 252 ? 0.3122 0.2039 0.2603 -0.0369 0.0256  0.0404  270 THR A C   
3751 O O   . THR A 252 ? 0.3096 0.2268 0.2850 -0.0337 0.0416  0.0237  270 THR A O   
3752 C CB  . THR A 252 ? 0.3226 0.2371 0.2998 -0.0676 -0.0110 0.0263  270 THR A CB  
3753 O OG1 . THR A 252 ? 0.3325 0.2150 0.3131 -0.0771 -0.0158 0.0446  270 THR A OG1 
3754 C CG2 . THR A 252 ? 0.3235 0.2595 0.3220 -0.0833 0.0041  0.0379  270 THR A CG2 
3762 N N   . GLY A 253 ? 0.2963 0.1786 0.2430 -0.0118 -0.0002 0.0310  271 GLY A N   
3763 C CA  . GLY A 253 ? 0.2764 0.1746 0.2174 -0.0218 -0.0125 0.0349  271 GLY A CA  
3764 C C   . GLY A 253 ? 0.2703 0.1719 0.2145 -0.0196 -0.0296 0.0433  271 GLY A C   
3765 O O   . GLY A 253 ? 0.2679 0.1895 0.2096 -0.0343 -0.0416 0.0349  271 GLY A O   
3769 N N   . GLN A 254 ? 0.2389 0.1553 0.2174 -0.0206 -0.0472 0.0354  272 GLN A N   
3770 C CA  . GLN A 254 ? 0.2363 0.1370 0.2436 -0.0239 -0.0326 0.0420  272 GLN A CA  
3771 C C   . GLN A 254 ? 0.2481 0.1373 0.2592 -0.0237 -0.0360 0.0307  272 GLN A C   
3772 O O   . GLN A 254 ? 0.2840 0.1271 0.2643 -0.0558 -0.0198 0.0269  272 GLN A O   
3773 C CB  . GLN A 254 ? 0.2309 0.1405 0.2790 -0.0277 -0.0052 0.0483  272 GLN A CB  
3774 C CG  . GLN A 254 ? 0.2087 0.1305 0.3078 -0.0250 -0.0400 0.0407  272 GLN A CG  
3775 C CD  . GLN A 254 ? 0.2285 0.1352 0.3664 -0.0275 -0.0353 0.0420  272 GLN A CD  
3776 O OE1 . GLN A 254 ? 0.2764 0.1677 0.4419 -0.0285 -0.0043 0.0501  272 GLN A OE1 
3777 N NE2 . GLN A 254 ? 0.2322 0.1167 0.3405 -0.0116 -0.0455 0.0307  272 GLN A NE2 
3786 N N   . ALA A 255 ? 0.2350 0.1345 0.2914 -0.0323 -0.0444 0.0129  273 ALA A N   
3787 C CA  . ALA A 255 ? 0.2294 0.1185 0.2986 -0.0406 -0.0391 0.0180  273 ALA A CA  
3788 C C   . ALA A 255 ? 0.2330 0.1384 0.3295 -0.0350 -0.0461 0.0380  273 ALA A C   
3789 O O   . ALA A 255 ? 0.2220 0.1495 0.3466 -0.0526 -0.0337 0.0448  273 ALA A O   
3790 C CB  . ALA A 255 ? 0.2239 0.1284 0.2834 -0.0313 -0.0287 -0.0031 273 ALA A CB  
3796 N N   . ARG A 256 ? 0.2132 0.1450 0.3550 -0.0598 -0.0337 0.0321  274 ARG A N   
3797 C CA  . ARG A 256 ? 0.2475 0.1657 0.3684 -0.0721 -0.0623 0.0423  274 ARG A CA  
3798 C C   . ARG A 256 ? 0.2439 0.1528 0.3626 -0.0489 -0.0671 0.0311  274 ARG A C   
3799 O O   . ARG A 256 ? 0.2697 0.1522 0.3509 -0.0619 -0.0578 0.0340  274 ARG A O   
3800 C CB  . ARG A 256 ? 0.2970 0.2078 0.4077 -0.0610 -0.0378 0.0659  274 ARG A CB  
3801 C CG  . ARG A 256 ? 0.3507 0.2783 0.4535 -0.0492 -0.0349 0.0894  274 ARG A CG  
3802 C CD  . ARG A 256 ? 0.4676 0.3434 0.5064 -0.0249 0.0014  0.0917  274 ARG A CD  
3803 N NE  . ARG A 256 ? 0.5672 0.3733 0.5370 -0.0072 0.0087  0.1123  274 ARG A NE  
3804 C CZ  . ARG A 256 ? 0.5871 0.3610 0.5233 -0.0263 0.0002  0.1450  274 ARG A CZ  
3805 N NH1 . ARG A 256 ? 0.6018 0.3904 0.5343 -0.0624 0.0201  0.1442  274 ARG A NH1 
3806 N NH2 . ARG A 256 ? 0.5187 0.3151 0.4847 -0.0430 -0.0100 0.1692  274 ARG A NH2 
3820 N N   . SER A 257 ? 0.2464 0.1690 0.3787 -0.0376 -0.0733 0.0199  275 SER A N   
3821 C CA  . SER A 257 ? 0.2881 0.1646 0.3817 -0.0502 -0.0755 -0.0106 275 SER A CA  
3822 C C   . SER A 257 ? 0.2957 0.1539 0.3672 -0.0606 -0.0624 -0.0485 275 SER A C   
3823 O O   . SER A 257 ? 0.2912 0.1775 0.3743 -0.0397 -0.0433 -0.0652 275 SER A O   
3824 C CB  . SER A 257 ? 0.3122 0.1693 0.4047 -0.0344 -0.0806 -0.0126 275 SER A CB  
3825 O OG  . SER A 257 ? 0.3409 0.1835 0.4278 -0.0383 -0.0945 -0.0084 275 SER A OG  
3831 N N   . ALA A 258 ? 0.3159 0.1488 0.3780 -0.0701 -0.0462 -0.0324 276 ALA A N   
3832 C CA  . ALA A 258 ? 0.3413 0.1594 0.3897 -0.0976 -0.0341 -0.0068 276 ALA A CA  
3833 C C   . ALA A 258 ? 0.3571 0.1593 0.3829 -0.0904 -0.0432 0.0070  276 ALA A C   
3834 O O   . ALA A 258 ? 0.3794 0.1736 0.4011 -0.1048 -0.0361 0.0059  276 ALA A O   
3835 C CB  . ALA A 258 ? 0.3891 0.1537 0.4089 -0.1029 -0.0193 -0.0069 276 ALA A CB  
3841 N N   . ASP A 259 ? 0.3094 0.1853 0.3567 -0.0787 -0.0742 0.0272  277 ASP A N   
3842 C CA  . ASP A 259 ? 0.3224 0.1959 0.3644 -0.0530 -0.0537 0.0408  277 ASP A CA  
3843 C C   . ASP A 259 ? 0.3355 0.2101 0.3735 -0.0505 -0.0478 0.0302  277 ASP A C   
3844 O O   . ASP A 259 ? 0.3812 0.2419 0.3906 -0.0439 0.0034  0.0418  277 ASP A O   
3845 C CB  . ASP A 259 ? 0.3226 0.2029 0.3754 -0.0602 -0.0550 0.0591  277 ASP A CB  
3846 C CG  . ASP A 259 ? 0.3272 0.2176 0.3932 -0.0737 -0.0520 0.0719  277 ASP A CG  
3847 O OD1 . ASP A 259 ? 0.3304 0.2311 0.4062 -0.0694 -0.0446 0.0827  277 ASP A OD1 
3848 O OD2 . ASP A 259 ? 0.3323 0.2047 0.3909 -0.0798 -0.0598 0.0636  277 ASP A OD2 
3853 N N   . TYR A 260 ? 0.3271 0.1978 0.3619 -0.0556 -0.0572 0.0173  278 TYR A N   
3854 C CA  . TYR A 260 ? 0.3214 0.2258 0.3544 -0.0417 -0.0659 0.0099  278 TYR A CA  
3855 C C   . TYR A 260 ? 0.3166 0.2534 0.3770 -0.0281 -0.0620 -0.0209 278 TYR A C   
3856 O O   . TYR A 260 ? 0.3062 0.2722 0.3880 -0.0106 -0.0670 -0.0391 278 TYR A O   
3857 C CB  . TYR A 260 ? 0.3266 0.2316 0.3370 -0.0663 -0.0713 0.0317  278 TYR A CB  
3858 C CG  . TYR A 260 ? 0.3341 0.2298 0.3228 -0.1121 -0.0650 0.0277  278 TYR A CG  
3859 C CD1 . TYR A 260 ? 0.3620 0.2250 0.3228 -0.1053 -0.0641 0.0417  278 TYR A CD1 
3860 C CD2 . TYR A 260 ? 0.3723 0.2342 0.3280 -0.1342 -0.0430 0.0481  278 TYR A CD2 
3861 C CE1 . TYR A 260 ? 0.4137 0.2253 0.3343 -0.1218 -0.0495 0.0370  278 TYR A CE1 
3862 C CE2 . TYR A 260 ? 0.3905 0.2261 0.3282 -0.1477 -0.0408 0.0458  278 TYR A CE2 
3863 C CZ  . TYR A 260 ? 0.4304 0.2282 0.3395 -0.1348 -0.0249 0.0391  278 TYR A CZ  
3864 O OH  . TYR A 260 ? 0.5014 0.2558 0.3493 -0.1387 0.0044  0.0222  278 TYR A OH  
3874 N N   . GLY A 261 ? 0.3032 0.2566 0.3761 -0.0415 -0.0827 -0.0271 279 GLY A N   
3875 C CA  . GLY A 261 ? 0.3410 0.2388 0.3760 -0.0351 -0.0692 -0.0215 279 GLY A CA  
3876 C C   . GLY A 261 ? 0.3017 0.2277 0.3724 -0.0536 -0.0856 0.0024  279 GLY A C   
3877 O O   . GLY A 261 ? 0.2806 0.2102 0.3711 -0.0556 -0.0884 -0.0148 279 GLY A O   
3881 N N   . ILE A 262 ? 0.3080 0.2416 0.3701 -0.0776 -0.0970 0.0053  280 ILE A N   
3882 C CA  . ILE A 262 ? 0.3302 0.2323 0.3873 -0.0686 -0.1020 0.0074  280 ILE A CA  
3883 C C   . ILE A 262 ? 0.3397 0.1962 0.3794 -0.0681 -0.1028 -0.0048 280 ILE A C   
3884 O O   . ILE A 262 ? 0.3384 0.1922 0.3707 -0.0623 -0.1057 -0.0005 280 ILE A O   
3885 C CB  . ILE A 262 ? 0.3274 0.2341 0.4069 -0.0773 -0.1293 0.0114  280 ILE A CB  
3886 C CG1 . ILE A 262 ? 0.3730 0.2351 0.4200 -0.0625 -0.1250 0.0258  280 ILE A CG1 
3887 C CG2 . ILE A 262 ? 0.3245 0.2394 0.4162 -0.0760 -0.1307 0.0102  280 ILE A CG2 
3888 C CD1 . ILE A 262 ? 0.3816 0.2403 0.4363 -0.0363 -0.1237 0.0310  280 ILE A CD1 
3900 N N   . THR A 263 ? 0.3313 0.1814 0.3805 -0.0793 -0.1110 -0.0047 281 THR A N   
3901 C CA  . THR A 263 ? 0.3439 0.1639 0.3854 -0.0859 -0.0734 -0.0242 281 THR A CA  
3902 C C   . THR A 263 ? 0.3399 0.1498 0.3700 -0.0505 -0.0742 -0.0285 281 THR A C   
3903 O O   . THR A 263 ? 0.3573 0.1603 0.3770 -0.0455 -0.0646 -0.0196 281 THR A O   
3904 C CB  . THR A 263 ? 0.3782 0.1896 0.3956 -0.1102 -0.0746 -0.0238 281 THR A CB  
3905 O OG1 . THR A 263 ? 0.4211 0.2122 0.3972 -0.1025 -0.1017 -0.0154 281 THR A OG1 
3906 C CG2 . THR A 263 ? 0.3677 0.2039 0.4028 -0.1197 -0.0699 -0.0302 281 THR A CG2 
3914 N N   . ASP A 264 ? 0.3090 0.1475 0.3495 -0.0548 -0.0911 -0.0303 282 ASP A N   
3915 C CA  . ASP A 264 ? 0.2922 0.1386 0.3346 -0.0428 -0.0742 -0.0313 282 ASP A CA  
3916 C C   . ASP A 264 ? 0.2878 0.1251 0.3140 -0.0520 -0.0681 -0.0198 282 ASP A C   
3917 O O   . ASP A 264 ? 0.3035 0.1351 0.3005 -0.0404 -0.0774 -0.0220 282 ASP A O   
3918 C CB  . ASP A 264 ? 0.2836 0.1491 0.3319 -0.0428 -0.0828 -0.0337 282 ASP A CB  
3919 C CG  . ASP A 264 ? 0.2993 0.1517 0.3448 -0.0548 -0.0594 -0.0302 282 ASP A CG  
3920 O OD1 . ASP A 264 ? 0.3158 0.1583 0.3383 -0.0049 -0.0694 -0.0167 282 ASP A OD1 
3921 O OD2 . ASP A 264 ? 0.3043 0.1714 0.3573 -0.0621 -0.0558 -0.0157 282 ASP A OD2 
3926 N N   . CYS A 265 ? 0.2880 0.1343 0.3314 -0.0398 -0.0546 -0.0078 283 CYS A N   
3927 C CA  . CYS A 265 ? 0.2986 0.1564 0.3260 -0.0181 -0.0615 -0.0030 283 CYS A CA  
3928 C C   . CYS A 265 ? 0.3233 0.1959 0.3148 -0.0144 -0.0603 -0.0205 283 CYS A C   
3929 O O   . CYS A 265 ? 0.3245 0.2463 0.3188 0.0318  -0.0502 -0.0556 283 CYS A O   
3930 C CB  . CYS A 265 ? 0.3089 0.1636 0.3355 -0.0341 -0.0754 0.0059  283 CYS A CB  
3931 S SG  . CYS A 265 ? 0.3044 0.1800 0.3469 -0.0418 -0.0640 0.0104  283 CYS A SG  
3936 N N   . ASN A 266 ? 0.3019 0.1776 0.3010 -0.0302 -0.0783 -0.0119 284 ASN A N   
3937 C CA  . ASN A 266 ? 0.3001 0.1398 0.2844 -0.0287 -0.0811 -0.0395 284 ASN A CA  
3938 C C   . ASN A 266 ? 0.2834 0.1291 0.2571 -0.0092 -0.0661 -0.0305 284 ASN A C   
3939 O O   . ASN A 266 ? 0.2983 0.1186 0.2358 -0.0018 -0.0591 -0.0123 284 ASN A O   
3940 C CB  . ASN A 266 ? 0.3100 0.1403 0.3089 -0.0324 -0.1012 -0.0350 284 ASN A CB  
3941 C CG  . ASN A 266 ? 0.3246 0.1586 0.3082 0.0097  -0.0919 -0.0568 284 ASN A CG  
3942 O OD1 . ASN A 266 ? 0.3185 0.1910 0.3209 0.0098  -0.0847 -0.0723 284 ASN A OD1 
3943 N ND2 . ASN A 266 ? 0.3298 0.1665 0.3089 0.0535  -0.0983 -0.0607 284 ASN A ND2 
3950 N N   . PRO A 267 ? 0.2794 0.1350 0.2485 0.0097  -0.0671 -0.0173 285 PRO A N   
3951 C CA  . PRO A 267 ? 0.2832 0.1504 0.2568 0.0119  -0.0550 -0.0071 285 PRO A CA  
3952 C C   . PRO A 267 ? 0.2584 0.1427 0.2488 -0.0014 -0.0503 -0.0211 285 PRO A C   
3953 O O   . PRO A 267 ? 0.2246 0.1517 0.2573 -0.0080 -0.0387 -0.0147 285 PRO A O   
3954 C CB  . PRO A 267 ? 0.2760 0.1618 0.2482 -0.0132 -0.0560 -0.0094 285 PRO A CB  
3955 C CG  . PRO A 267 ? 0.2785 0.1712 0.2451 0.0189  -0.0732 -0.0040 285 PRO A CG  
3956 C CD  . PRO A 267 ? 0.2719 0.1458 0.2386 0.0192  -0.1011 -0.0170 285 PRO A CD  
3964 N N   . LEU A 268 ? 0.2702 0.1574 0.2672 0.0089  -0.0468 -0.0241 286 LEU A N   
3965 C CA  . LEU A 268 ? 0.2972 0.1601 0.2707 0.0044  -0.0731 -0.0308 286 LEU A CA  
3966 C C   . LEU A 268 ? 0.2964 0.1394 0.2793 -0.0050 -0.0825 -0.0145 286 LEU A C   
3967 O O   . LEU A 268 ? 0.2945 0.1395 0.2950 -0.0061 -0.0993 -0.0176 286 LEU A O   
3968 C CB  . LEU A 268 ? 0.3570 0.1953 0.2839 -0.0101 -0.0839 -0.0548 286 LEU A CB  
3969 C CG  . LEU A 268 ? 0.4042 0.2169 0.2983 -0.0094 -0.1015 -0.0481 286 LEU A CG  
3970 C CD1 . LEU A 268 ? 0.4187 0.1942 0.3002 -0.0037 -0.1069 -0.0546 286 LEU A CD1 
3971 C CD2 . LEU A 268 ? 0.4159 0.2435 0.3068 -0.0146 -0.1114 -0.0407 286 LEU A CD2 
3983 N N   . PRO A 269 ? 0.2808 0.1381 0.2725 0.0039  -0.0689 0.0038  287 PRO A N   
3984 C CA  . PRO A 269 ? 0.2528 0.1249 0.2690 0.0233  -0.0952 -0.0037 287 PRO A CA  
3985 C C   . PRO A 269 ? 0.2566 0.1153 0.2700 0.0284  -0.0987 -0.0187 287 PRO A C   
3986 O O   . PRO A 269 ? 0.3020 0.1206 0.2950 0.0305  -0.0668 -0.0365 287 PRO A O   
3987 C CB  . PRO A 269 ? 0.2665 0.1354 0.2869 0.0155  -0.0736 -0.0093 287 PRO A CB  
3988 C CG  . PRO A 269 ? 0.2751 0.1474 0.2873 0.0020  -0.0553 -0.0210 287 PRO A CG  
3989 C CD  . PRO A 269 ? 0.2963 0.1534 0.2672 0.0009  -0.0559 -0.0173 287 PRO A CD  
3997 N N   . ALA A 270 ? 0.2697 0.1154 0.2574 -0.0041 -0.0907 0.0021  288 ALA A N   
3998 C CA  . ALA A 270 ? 0.3133 0.1126 0.2528 -0.0142 -0.1003 0.0173  288 ALA A CA  
3999 C C   . ALA A 270 ? 0.3247 0.1208 0.2514 0.0028  -0.0963 -0.0009 288 ALA A C   
4000 O O   . ALA A 270 ? 0.3229 0.1099 0.2452 0.0076  -0.0865 -0.0048 288 ALA A O   
4001 C CB  . ALA A 270 ? 0.3473 0.1225 0.2633 -0.0156 -0.0874 0.0390  288 ALA A CB  
4007 N N   . ASN A 271 ? 0.3258 0.1041 0.2391 -0.0150 -0.0844 -0.0263 289 ASN A N   
4008 C CA  . ASN A 271 ? 0.3147 0.1141 0.2647 -0.0132 -0.1128 -0.0283 289 ASN A CA  
4009 C C   . ASN A 271 ? 0.3359 0.1248 0.2768 -0.0113 -0.0988 -0.0134 289 ASN A C   
4010 O O   . ASN A 271 ? 0.3467 0.1284 0.2966 -0.0207 -0.0875 -0.0230 289 ASN A O   
4011 C CB  . ASN A 271 ? 0.3277 0.1439 0.2812 -0.0320 -0.1101 -0.0116 289 ASN A CB  
4012 C CG  . ASN A 271 ? 0.3431 0.1581 0.2999 -0.0417 -0.1033 -0.0044 289 ASN A CG  
4013 O OD1 . ASN A 271 ? 0.3494 0.1729 0.2867 -0.0424 -0.1006 -0.0110 289 ASN A OD1 
4014 N ND2 . ASN A 271 ? 0.3738 0.1535 0.3298 -0.0290 -0.0892 -0.0026 289 ASN A ND2 
4021 N N   . ASP A 272 ? 0.3389 0.1213 0.2587 0.0214  -0.0993 -0.0133 290 ASP A N   
4022 C CA  . ASP A 272 ? 0.3412 0.1518 0.2751 0.0196  -0.0929 0.0079  290 ASP A CA  
4023 C C   . ASP A 272 ? 0.3488 0.1604 0.2743 0.0250  -0.0803 0.0230  290 ASP A C   
4024 O O   . ASP A 272 ? 0.3528 0.1899 0.2894 0.0100  -0.0978 0.0107  290 ASP A O   
4025 C CB  . ASP A 272 ? 0.3486 0.1527 0.2749 0.0121  -0.0901 0.0085  290 ASP A CB  
4026 C CG  . ASP A 272 ? 0.3678 0.1870 0.3260 -0.0376 -0.0807 -0.0104 290 ASP A CG  
4027 O OD1 . ASP A 272 ? 0.4251 0.1801 0.3670 -0.0497 -0.0269 -0.0144 290 ASP A OD1 
4028 O OD2 . ASP A 272 ? 0.3714 0.2198 0.3491 -0.0692 -0.0566 -0.0116 290 ASP A OD2 
4033 N N   . LEU A 273 ? 0.3155 0.1273 0.2531 0.0265  -0.0677 0.0211  291 LEU A N   
4034 C CA  . LEU A 273 ? 0.3142 0.1328 0.2630 0.0230  -0.0510 -0.0070 291 LEU A CA  
4035 C C   . LEU A 273 ? 0.2956 0.1445 0.2848 0.0237  -0.0713 -0.0067 291 LEU A C   
4036 O O   . LEU A 273 ? 0.2835 0.1671 0.3023 0.0217  -0.0746 -0.0222 291 LEU A O   
4037 C CB  . LEU A 273 ? 0.3210 0.1271 0.2518 0.0326  -0.0378 -0.0224 291 LEU A CB  
4038 C CG  . LEU A 273 ? 0.2828 0.1383 0.2412 0.0367  -0.0707 -0.0044 291 LEU A CG  
4039 C CD1 . LEU A 273 ? 0.2953 0.1362 0.2626 0.0162  -0.0726 -0.0026 291 LEU A CD1 
4040 C CD2 . LEU A 273 ? 0.2877 0.1446 0.2441 0.0004  -0.0913 -0.0087 291 LEU A CD2 
4052 N N   . THR A 274 ? 0.2968 0.1545 0.2966 0.0237  -0.0610 0.0053  292 THR A N   
4053 C CA  . THR A 274 ? 0.3147 0.1727 0.3084 0.0492  -0.0639 -0.0093 292 THR A CA  
4054 C C   . THR A 274 ? 0.3140 0.1733 0.2899 0.0406  -0.0810 -0.0155 292 THR A C   
4055 O O   . THR A 274 ? 0.3113 0.1629 0.2801 0.0755  -0.0643 -0.0003 292 THR A O   
4056 C CB  . THR A 274 ? 0.3283 0.1883 0.3171 0.0553  -0.0602 0.0047  292 THR A CB  
4057 O OG1 . THR A 274 ? 0.3308 0.1937 0.3386 0.0580  -0.0646 -0.0025 292 THR A OG1 
4058 C CG2 . THR A 274 ? 0.3653 0.1933 0.3298 0.0675  -0.0456 0.0343  292 THR A CG2 
4066 N N   . PRO A 275 ? 0.3368 0.1884 0.2984 0.0523  -0.0928 -0.0138 293 PRO A N   
4067 C CA  . PRO A 275 ? 0.3582 0.2048 0.3189 0.0599  -0.0686 -0.0093 293 PRO A CA  
4068 C C   . PRO A 275 ? 0.3609 0.2171 0.3218 0.0807  -0.0539 -0.0040 293 PRO A C   
4069 O O   . PRO A 275 ? 0.3886 0.2097 0.2981 0.0989  -0.0342 0.0121  293 PRO A O   
4070 C CB  . PRO A 275 ? 0.3579 0.2106 0.3163 0.0622  -0.0782 -0.0038 293 PRO A CB  
4071 C CG  . PRO A 275 ? 0.3680 0.1942 0.3054 0.0689  -0.0791 -0.0208 293 PRO A CG  
4072 C CD  . PRO A 275 ? 0.3798 0.1991 0.3070 0.0679  -0.0669 -0.0236 293 PRO A CD  
4080 N N   . GLU A 276 ? 0.3707 0.2298 0.3464 0.0581  -0.0483 -0.0196 294 GLU A N   
4081 C CA  . GLU A 276 ? 0.3674 0.2432 0.3553 0.0836  -0.0567 -0.0337 294 GLU A CA  
4082 C C   . GLU A 276 ? 0.3376 0.2260 0.3318 0.0830  -0.0379 -0.0159 294 GLU A C   
4083 O O   . GLU A 276 ? 0.3296 0.2321 0.3348 0.0979  -0.0315 -0.0165 294 GLU A O   
4084 C CB  . GLU A 276 ? 0.4120 0.2697 0.3827 0.1152  -0.0612 -0.0358 294 GLU A CB  
4085 C CG  . GLU A 276 ? 0.5184 0.3178 0.4182 0.0982  -0.0401 -0.0635 294 GLU A CG  
4086 C CD  . GLU A 276 ? 0.6001 0.3619 0.4370 0.1111  -0.0468 -0.0733 294 GLU A CD  
4087 O OE1 . GLU A 276 ? 0.6593 0.3989 0.4688 0.0928  -0.0254 -0.0806 294 GLU A OE1 
4088 O OE2 . GLU A 276 ? 0.5773 0.3517 0.4215 0.1456  -0.1024 -0.0572 294 GLU A OE2 
4095 N N   . GLN A 277 ? 0.3184 0.2009 0.2937 0.0869  -0.0404 -0.0156 295 GLN A N   
4096 C CA  . GLN A 277 ? 0.2916 0.1824 0.2830 0.0690  -0.0604 -0.0035 295 GLN A CA  
4097 C C   . GLN A 277 ? 0.2696 0.1632 0.2797 0.0598  -0.0624 -0.0128 295 GLN A C   
4098 O O   . GLN A 277 ? 0.2803 0.1528 0.2690 0.0528  -0.0571 -0.0139 295 GLN A O   
4099 C CB  . GLN A 277 ? 0.2635 0.1652 0.2787 0.0565  -0.0672 -0.0007 295 GLN A CB  
4100 C CG  . GLN A 277 ? 0.2542 0.1739 0.2825 0.0451  -0.0731 -0.0035 295 GLN A CG  
4101 C CD  . GLN A 277 ? 0.2660 0.1802 0.2959 0.0463  -0.0816 -0.0039 295 GLN A CD  
4102 O OE1 . GLN A 277 ? 0.2730 0.1601 0.2985 0.0453  -0.0663 -0.0073 295 GLN A OE1 
4103 N NE2 . GLN A 277 ? 0.2910 0.2130 0.2992 0.0426  -0.0797 -0.0159 295 GLN A NE2 
4112 N N   . LYS A 278 ? 0.2875 0.1468 0.2832 0.0617  -0.0796 -0.0093 296 LYS A N   
4113 C CA  . LYS A 278 ? 0.2901 0.1445 0.2767 0.0383  -0.0779 0.0062  296 LYS A CA  
4114 C C   . LYS A 278 ? 0.3013 0.1533 0.2712 0.0582  -0.0431 0.0005  296 LYS A C   
4115 O O   . LYS A 278 ? 0.3327 0.1407 0.2548 0.0452  -0.0526 -0.0260 296 LYS A O   
4116 C CB  . LYS A 278 ? 0.3033 0.1510 0.2832 0.0407  -0.0765 -0.0179 296 LYS A CB  
4117 C CG  . LYS A 278 ? 0.3134 0.1520 0.2872 0.0305  -0.0945 -0.0116 296 LYS A CG  
4118 C CD  . LYS A 278 ? 0.3460 0.1445 0.2906 0.0081  -0.0874 -0.0175 296 LYS A CD  
4119 C CE  . LYS A 278 ? 0.3360 0.1722 0.3052 0.0064  -0.0875 -0.0032 296 LYS A CE  
4120 N NZ  . LYS A 278 ? 0.3529 0.1665 0.3220 0.0219  -0.0822 0.0129  296 LYS A NZ  
4134 N N   . VAL A 279 ? 0.3353 0.1737 0.2734 0.0439  -0.0312 -0.0137 297 VAL A N   
4135 C CA  . VAL A 279 ? 0.3221 0.2038 0.2504 0.0420  -0.0340 -0.0095 297 VAL A CA  
4136 C C   . VAL A 279 ? 0.2869 0.2090 0.2633 0.0385  -0.0398 -0.0071 297 VAL A C   
4137 O O   . VAL A 279 ? 0.2680 0.2286 0.2756 0.0365  -0.0526 -0.0161 297 VAL A O   
4138 C CB  . VAL A 279 ? 0.3795 0.2120 0.2434 0.0493  -0.0264 -0.0033 297 VAL A CB  
4139 C CG1 . VAL A 279 ? 0.3989 0.2202 0.2273 0.0584  -0.0306 0.0117  297 VAL A CG1 
4140 C CG2 . VAL A 279 ? 0.4168 0.2328 0.2701 0.0667  0.0163  -0.0021 297 VAL A CG2 
4150 N N   . ALA A 280 ? 0.2531 0.2052 0.2595 0.0457  -0.0405 -0.0179 298 ALA A N   
4151 C CA  . ALA A 280 ? 0.2261 0.2092 0.2787 0.0388  -0.0550 -0.0078 298 ALA A CA  
4152 C C   . ALA A 280 ? 0.2311 0.1939 0.2868 0.0420  -0.0545 -0.0011 298 ALA A C   
4153 O O   . ALA A 280 ? 0.2496 0.2041 0.3090 0.0332  -0.0194 0.0044  298 ALA A O   
4154 C CB  . ALA A 280 ? 0.2043 0.2302 0.2984 0.0482  -0.0609 -0.0173 298 ALA A CB  
4160 N N   . ALA A 281 ? 0.2192 0.1788 0.2762 0.0398  -0.0770 -0.0019 299 ALA A N   
4161 C CA  . ALA A 281 ? 0.2442 0.1841 0.2703 0.0169  -0.0549 0.0152  299 ALA A CA  
4162 C C   . ALA A 281 ? 0.2213 0.1759 0.2578 0.0166  -0.0551 0.0065  299 ALA A C   
4163 O O   . ALA A 281 ? 0.2327 0.1700 0.2701 0.0148  -0.0424 0.0064  299 ALA A O   
4164 C CB  . ALA A 281 ? 0.2888 0.1853 0.2826 0.0233  -0.0434 0.0291  299 ALA A CB  
4170 N N   . ALA A 282 ? 0.2481 0.1870 0.2547 0.0188  -0.0660 -0.0021 300 ALA A N   
4171 C CA  . ALA A 282 ? 0.2684 0.2157 0.2606 0.0194  -0.0726 -0.0282 300 ALA A CA  
4172 C C   . ALA A 282 ? 0.2663 0.2205 0.2543 0.0447  -0.0709 -0.0083 300 ALA A C   
4173 O O   . ALA A 282 ? 0.2917 0.2506 0.2718 0.0501  -0.0771 -0.0007 300 ALA A O   
4174 C CB  . ALA A 282 ? 0.3132 0.2238 0.2696 0.0301  -0.0458 -0.0378 300 ALA A CB  
4180 N N   . ALA A 283 ? 0.2675 0.2339 0.2590 0.0458  -0.0664 -0.0140 301 ALA A N   
4181 C CA  . ALA A 283 ? 0.2668 0.2379 0.2545 0.0346  -0.0648 -0.0225 301 ALA A CA  
4182 C C   . ALA A 283 ? 0.2671 0.2430 0.2709 0.0480  -0.0525 -0.0137 301 ALA A C   
4183 O O   . ALA A 283 ? 0.2794 0.2497 0.2745 0.0190  -0.0339 -0.0105 301 ALA A O   
4184 C CB  . ALA A 283 ? 0.3047 0.2533 0.2767 0.0128  -0.0586 -0.0267 301 ALA A CB  
4190 N N   . LEU A 284 ? 0.2365 0.2338 0.2712 0.0506  -0.0546 -0.0076 302 LEU A N   
4191 C CA  . LEU A 284 ? 0.2476 0.2220 0.2695 0.0220  -0.0421 -0.0168 302 LEU A CA  
4192 C C   . LEU A 284 ? 0.2652 0.2261 0.2610 -0.0184 -0.0225 -0.0299 302 LEU A C   
4193 O O   . LEU A 284 ? 0.2775 0.2456 0.2690 -0.0370 -0.0055 -0.0423 302 LEU A O   
4194 C CB  . LEU A 284 ? 0.2534 0.2035 0.2814 0.0269  -0.0403 -0.0086 302 LEU A CB  
4195 C CG  . LEU A 284 ? 0.2772 0.1967 0.2796 -0.0066 -0.0398 -0.0099 302 LEU A CG  
4196 C CD1 . LEU A 284 ? 0.2782 0.2417 0.2686 0.0063  -0.0742 -0.0032 302 LEU A CD1 
4197 C CD2 . LEU A 284 ? 0.2862 0.1886 0.2795 -0.0356 -0.0370 0.0022  302 LEU A CD2 
4209 N N   . LEU A 285 ? 0.3408 0.2263 0.2697 -0.0462 -0.0231 -0.0301 303 LEU A N   
4210 C CA  . LEU A 285 ? 0.4381 0.2479 0.3148 -0.0811 0.0078  -0.0387 303 LEU A CA  
4211 C C   . LEU A 285 ? 0.4857 0.2579 0.3352 -0.1327 0.0243  -0.0467 303 LEU A C   
4212 O O   . LEU A 285 ? 0.4958 0.2577 0.3127 -0.1370 -0.0030 -0.0282 303 LEU A O   
4213 C CB  . LEU A 285 ? 0.5039 0.2489 0.3517 -0.0580 0.0167  -0.0276 303 LEU A CB  
4214 C CG  . LEU A 285 ? 0.5406 0.2764 0.3782 -0.0355 0.0374  -0.0434 303 LEU A CG  
4215 C CD1 . LEU A 285 ? 0.5670 0.2942 0.3847 -0.0261 0.0447  -0.0566 303 LEU A CD1 
4216 C CD2 . LEU A 285 ? 0.5359 0.2747 0.3782 -0.0171 0.0434  -0.0318 303 LEU A CD2 
4228 N N   . ALA A 286 ? 0.5204 0.2761 0.3931 -0.1577 0.0890  -0.0620 304 ALA A N   
4229 C CA  . ALA A 286 ? 0.5762 0.2857 0.4377 -0.1375 0.1243  -0.0612 304 ALA A CA  
4230 C C   . ALA A 286 ? 0.5670 0.2747 0.4650 -0.1111 0.1172  -0.0549 304 ALA A C   
4231 O O   . ALA A 286 ? 0.5618 0.3071 0.4740 -0.1118 0.1446  -0.0528 304 ALA A O   
4232 C CB  . ALA A 286 ? 0.6026 0.2953 0.4492 -0.1374 0.1456  -0.0696 304 ALA A CB  
4238 N N   . PRO A 287 ? 0.5527 0.2550 0.4822 -0.0658 0.1040  -0.0471 305 PRO A N   
4239 C CA  . PRO A 287 ? 0.5230 0.2421 0.4691 -0.0237 0.0667  -0.0415 305 PRO A CA  
4240 C C   . PRO A 287 ? 0.4807 0.1951 0.4184 -0.0067 -0.0068 -0.0526 305 PRO A C   
4241 O O   . PRO A 287 ? 0.4797 0.2002 0.4163 0.0040  -0.0296 -0.0368 305 PRO A O   
4242 C CB  . PRO A 287 ? 0.5470 0.2503 0.5085 -0.0063 0.0906  -0.0465 305 PRO A CB  
4243 C CG  . PRO A 287 ? 0.5548 0.2591 0.5101 -0.0332 0.1024  -0.0451 305 PRO A CG  
4244 C CD  . PRO A 287 ? 0.5565 0.2575 0.5112 -0.0326 0.1165  -0.0433 305 PRO A CD  
4252 N N   . ALA A 288 ? 0.4410 0.1697 0.3787 0.0222  -0.0660 -0.0660 306 ALA A N   
4253 C CA  . ALA A 288 ? 0.4335 0.2005 0.3399 0.0127  -0.0800 -0.0561 306 ALA A CA  
4254 C C   . ALA A 288 ? 0.4658 0.2068 0.3157 0.0074  -0.1011 -0.0306 306 ALA A C   
4255 O O   . ALA A 288 ? 0.4714 0.1976 0.3277 0.0558  -0.1160 -0.0106 306 ALA A O   
4256 C CB  . ALA A 288 ? 0.4326 0.2257 0.3397 0.0288  -0.0758 -0.0551 306 ALA A CB  
4262 N N   . ALA A 289 ? 0.4823 0.2348 0.3253 -0.0371 -0.0831 -0.0123 307 ALA A N   
4263 C CA  . ALA A 289 ? 0.5442 0.2465 0.3169 -0.0518 -0.0621 -0.0030 307 ALA A CA  
4264 C C   . ALA A 289 ? 0.5789 0.2526 0.3210 -0.0582 -0.0485 -0.0227 307 ALA A C   
4265 O O   . ALA A 289 ? 0.6340 0.2506 0.3304 -0.0597 -0.0362 0.0056  307 ALA A O   
4266 C CB  . ALA A 289 ? 0.5661 0.2542 0.3039 -0.0607 -0.0807 -0.0023 307 ALA A CB  
4272 N N   . ALA A 290 ? 0.5638 0.2493 0.3317 -0.0419 -0.0012 -0.0517 308 ALA A N   
4273 C CA  . ALA A 290 ? 0.5869 0.2404 0.3530 -0.0667 0.0642  -0.0432 308 ALA A CA  
4274 C C   . ALA A 290 ? 0.6438 0.2422 0.3842 -0.0564 0.0861  -0.0024 308 ALA A C   
4275 O O   . ALA A 290 ? 0.6670 0.2493 0.4197 -0.0946 0.1288  0.0142  308 ALA A O   
4276 C CB  . ALA A 290 ? 0.5690 0.2562 0.3733 -0.0702 0.0844  -0.0297 308 ALA A CB  
4282 N N   . ALA A 291 ? 0.6537 0.2162 0.3330 -0.0270 0.0620  0.0229  309 ALA A N   
4283 C CA  . ALA A 291 ? 0.6362 0.1920 0.3397 -0.0132 0.0137  0.0221  309 ALA A CA  
4284 C C   . ALA A 291 ? 0.6373 0.1749 0.3296 -0.0212 -0.0392 0.0088  309 ALA A C   
4285 O O   . ALA A 291 ? 0.6273 0.1675 0.3268 -0.0130 -0.0207 0.0217  309 ALA A O   
4286 C CB  . ALA A 291 ? 0.6203 0.1869 0.3400 -0.0253 -0.0003 0.0356  309 ALA A CB  
4292 N N   . ILE A 292 ? 0.6145 0.1763 0.3125 -0.0554 -0.1133 -0.0109 310 ILE A N   
4293 C CA  . ILE A 292 ? 0.6570 0.2052 0.3345 -0.0409 -0.1229 0.0097  310 ILE A CA  
4294 C C   . ILE A 292 ? 0.7307 0.2409 0.3417 -0.0639 -0.0744 0.0134  310 ILE A C   
4295 O O   . ILE A 292 ? 0.7705 0.2539 0.3375 -0.0392 -0.0875 0.0217  310 ILE A O   
4296 C CB  . ILE A 292 ? 0.6288 0.2156 0.3642 -0.0462 -0.1598 -0.0057 310 ILE A CB  
4297 C CG1 . ILE A 292 ? 0.5955 0.2291 0.3807 -0.0536 -0.2141 -0.0277 310 ILE A CG1 
4298 C CG2 . ILE A 292 ? 0.6438 0.2368 0.3849 -0.0227 -0.1561 -0.0164 310 ILE A CG2 
4299 C CD1 . ILE A 292 ? 0.5980 0.2462 0.4039 -0.0598 -0.2140 -0.0451 310 ILE A CD1 
4311 N N   . VAL A 293 ? 0.7665 0.2715 0.3470 -0.0850 -0.0514 0.0279  311 VAL A N   
4312 C CA  . VAL A 293 ? 0.7997 0.3167 0.3648 -0.0946 0.0058  0.0245  311 VAL A CA  
4313 C C   . VAL A 293 ? 0.7897 0.3120 0.3790 -0.0578 0.0457  0.0325  311 VAL A C   
4314 O O   . VAL A 293 ? 0.8320 0.3356 0.3889 -0.0463 0.0742  0.0289  311 VAL A O   
4315 C CB  . VAL A 293 ? 0.8321 0.3512 0.3716 -0.1210 0.0274  0.0210  311 VAL A CB  
4316 C CG1 . VAL A 293 ? 0.8340 0.3545 0.3707 -0.1419 0.0427  0.0181  311 VAL A CG1 
4317 C CG2 . VAL A 293 ? 0.8467 0.3701 0.3708 -0.1196 0.0226  0.0193  311 VAL A CG2 
4327 N N   . ALA A 294 ? 0.7344 0.2815 0.3850 -0.0187 0.0708  0.0450  312 ALA A N   
4328 C CA  . ALA A 294 ? 0.6546 0.2536 0.3995 -0.0131 0.0962  0.0429  312 ALA A CA  
4329 C C   . ALA A 294 ? 0.5678 0.2204 0.3937 -0.0050 0.0757  0.0412  312 ALA A C   
4330 O O   . ALA A 294 ? 0.5516 0.2298 0.4248 -0.0206 0.0805  0.0172  312 ALA A O   
4331 C CB  . ALA A 294 ? 0.6785 0.2819 0.4265 -0.0167 0.1219  0.0345  312 ALA A CB  
4337 N N   . GLY A 295 ? 0.4715 0.1602 0.3292 0.0014  0.0712  0.0584  313 GLY A N   
4338 C CA  . GLY A 295 ? 0.4036 0.1224 0.2988 0.0071  0.0318  0.0423  313 GLY A CA  
4339 C C   . GLY A 295 ? 0.3408 0.1297 0.2674 0.0140  -0.0173 0.0442  313 GLY A C   
4340 O O   . GLY A 295 ? 0.3206 0.1473 0.2695 0.0066  -0.0155 0.0218  313 GLY A O   
4344 N N   . PRO A 296 ? 0.3041 0.1231 0.2385 0.0057  -0.0187 0.0286  314 PRO A N   
4345 C CA  . PRO A 296 ? 0.2793 0.1140 0.2318 -0.0042 -0.0389 0.0059  314 PRO A CA  
4346 C C   . PRO A 296 ? 0.2525 0.1074 0.2490 -0.0060 -0.0346 -0.0076 314 PRO A C   
4347 O O   . PRO A 296 ? 0.2208 0.1411 0.2752 0.0039  -0.0126 0.0011  314 PRO A O   
4348 C CB  . PRO A 296 ? 0.3030 0.1263 0.2503 0.0109  -0.0080 0.0307  314 PRO A CB  
4349 C CG  . PRO A 296 ? 0.3464 0.1234 0.2527 0.0197  0.0001  0.0184  314 PRO A CG  
4350 C CD  . PRO A 296 ? 0.3223 0.1184 0.2459 -0.0084 -0.0155 0.0336  314 PRO A CD  
4358 N N   . LYS A 297 ? 0.2218 0.0861 0.2300 0.0108  -0.0520 0.0190  315 LYS A N   
4359 C CA  . LYS A 297 ? 0.2567 0.0968 0.2344 -0.0012 -0.0549 -0.0091 315 LYS A CA  
4360 C C   . LYS A 297 ? 0.2510 0.1085 0.2069 -0.0054 -0.0505 -0.0036 315 LYS A C   
4361 O O   . LYS A 297 ? 0.2502 0.1245 0.2197 -0.0008 -0.0339 -0.0012 315 LYS A O   
4362 C CB  . LYS A 297 ? 0.3250 0.1130 0.2297 -0.0187 -0.0650 -0.0314 315 LYS A CB  
4363 C CG  . LYS A 297 ? 0.4286 0.1422 0.2295 0.0013  -0.0528 -0.0349 315 LYS A CG  
4364 C CD  . LYS A 297 ? 0.5133 0.1920 0.2660 -0.0088 -0.0523 -0.0388 315 LYS A CD  
4365 C CE  . LYS A 297 ? 0.5914 0.2432 0.2993 -0.0019 -0.0068 -0.0256 315 LYS A CE  
4366 N NZ  . LYS A 297 ? 0.6578 0.2796 0.3252 -0.0377 0.0442  -0.0252 315 LYS A NZ  
4380 N N   . GLN A 298 ? 0.2262 0.1098 0.2046 -0.0041 -0.0464 0.0126  316 GLN A N   
4381 C CA  . GLN A 298 ? 0.2305 0.1193 0.2212 0.0026  -0.0379 0.0177  316 GLN A CA  
4382 C C   . GLN A 298 ? 0.2420 0.1202 0.2238 -0.0255 -0.0336 0.0066  316 GLN A C   
4383 O O   . GLN A 298 ? 0.2591 0.1115 0.2242 -0.0224 -0.0402 0.0004  316 GLN A O   
4384 C CB  . GLN A 298 ? 0.2234 0.1115 0.2146 -0.0150 -0.0376 0.0342  316 GLN A CB  
4385 C CG  . GLN A 298 ? 0.2394 0.1061 0.2050 -0.0045 -0.0375 0.0071  316 GLN A CG  
4386 C CD  . GLN A 298 ? 0.2197 0.1283 0.2125 0.0067  -0.0352 0.0243  316 GLN A CD  
4387 O OE1 . GLN A 298 ? 0.2338 0.1453 0.2225 0.0332  -0.0273 0.0315  316 GLN A OE1 
4388 N NE2 . GLN A 298 ? 0.2234 0.1388 0.2374 0.0009  -0.0380 0.0205  316 GLN A NE2 
4397 N N   . ASN A 299 ? 0.2264 0.1073 0.2347 -0.0184 -0.0434 -0.0050 317 ASN A N   
4398 C CA  . ASN A 299 ? 0.2339 0.1125 0.2266 -0.0086 -0.0761 0.0034  317 ASN A CA  
4399 C C   . ASN A 299 ? 0.2357 0.1200 0.2605 -0.0299 -0.0799 0.0048  317 ASN A C   
4400 O O   . ASN A 299 ? 0.2459 0.1396 0.2741 -0.0219 -0.0694 0.0373  317 ASN A O   
4401 C CB  . ASN A 299 ? 0.2503 0.1301 0.2163 -0.0005 -0.0810 0.0063  317 ASN A CB  
4402 C CG  . ASN A 299 ? 0.2491 0.1117 0.2148 -0.0277 -0.0529 -0.0017 317 ASN A CG  
4403 O OD1 . ASN A 299 ? 0.2112 0.1228 0.2265 -0.0217 -0.0389 0.0085  317 ASN A OD1 
4404 N ND2 . ASN A 299 ? 0.3022 0.1179 0.2325 -0.0147 -0.0324 0.0065  317 ASN A ND2 
4411 N N   . CYS A 300 ? 0.2201 0.1364 0.2712 -0.0297 -0.0711 0.0016  318 CYS A N   
4412 C CA  . CYS A 300 ? 0.2109 0.1353 0.2730 -0.0420 -0.0733 0.0127  318 CYS A CA  
4413 C C   . CYS A 300 ? 0.1948 0.1405 0.2672 -0.0256 -0.0578 0.0237  318 CYS A C   
4414 O O   . CYS A 300 ? 0.1904 0.1412 0.2414 -0.0004 -0.0408 0.0016  318 CYS A O   
4415 C CB  . CYS A 300 ? 0.2354 0.1368 0.2612 -0.0426 -0.0725 0.0170  318 CYS A CB  
4416 S SG  . CYS A 300 ? 0.2648 0.1523 0.2583 -0.0401 -0.0656 0.0255  318 CYS A SG  
4421 N N   . GLU A 301 ? 0.2082 0.1370 0.2853 -0.0388 -0.0512 0.0235  319 GLU A N   
4422 C CA  . GLU A 301 ? 0.2092 0.1256 0.2842 -0.0289 -0.0526 0.0097  319 GLU A CA  
4423 C C   . GLU A 301 ? 0.2244 0.1067 0.2701 -0.0381 -0.0452 0.0025  319 GLU A C   
4424 O O   . GLU A 301 ? 0.2219 0.0865 0.2795 -0.0256 -0.0454 0.0160  319 GLU A O   
4425 C CB  . GLU A 301 ? 0.2128 0.1277 0.2816 -0.0406 -0.0369 -0.0096 319 GLU A CB  
4426 C CG  . GLU A 301 ? 0.2141 0.1177 0.2719 -0.0324 -0.0468 0.0205  319 GLU A CG  
4427 C CD  . GLU A 301 ? 0.2347 0.1181 0.2714 -0.0322 -0.0549 0.0118  319 GLU A CD  
4428 O OE1 . GLU A 301 ? 0.2185 0.1268 0.2861 -0.0408 -0.0531 0.0160  319 GLU A OE1 
4429 O OE2 . GLU A 301 ? 0.2221 0.1190 0.2589 -0.0154 -0.0299 0.0306  319 GLU A OE2 
4436 N N   . PRO A 302 ? 0.2262 0.1094 0.2473 -0.0305 -0.0494 0.0069  320 PRO A N   
4437 C CA  . PRO A 302 ? 0.2219 0.1132 0.2716 -0.0154 -0.0506 0.0079  320 PRO A CA  
4438 C C   . PRO A 302 ? 0.2189 0.1155 0.2872 -0.0250 -0.0579 -0.0033 320 PRO A C   
4439 O O   . PRO A 302 ? 0.2391 0.1200 0.2730 -0.0145 -0.0635 0.0005  320 PRO A O   
4440 C CB  . PRO A 302 ? 0.2648 0.1217 0.2649 0.0094  -0.0344 0.0189  320 PRO A CB  
4441 C CG  . PRO A 302 ? 0.2605 0.1294 0.2593 -0.0043 -0.0380 0.0080  320 PRO A CG  
4442 C CD  . PRO A 302 ? 0.2185 0.1200 0.2456 0.0067  -0.0653 -0.0007 320 PRO A CD  
4450 N N   . ASP A 303 ? 0.2291 0.1177 0.2934 -0.0261 -0.0491 0.0058  321 ASP A N   
4451 C CA  . ASP A 303 ? 0.2262 0.1213 0.3009 -0.0135 -0.0548 0.0197  321 ASP A CA  
4452 C C   . ASP A 303 ? 0.2273 0.1195 0.2858 0.0050  -0.0640 0.0126  321 ASP A C   
4453 O O   . ASP A 303 ? 0.2661 0.1156 0.2664 0.0251  -0.0525 0.0316  321 ASP A O   
4454 C CB  . ASP A 303 ? 0.2273 0.1299 0.2999 -0.0055 -0.0739 0.0067  321 ASP A CB  
4455 C CG  . ASP A 303 ? 0.2445 0.1480 0.3244 -0.0107 -0.0998 -0.0009 321 ASP A CG  
4456 O OD1 . ASP A 303 ? 0.2277 0.1428 0.3116 -0.0074 -0.0677 -0.0044 321 ASP A OD1 
4457 O OD2 . ASP A 303 ? 0.2739 0.1713 0.3692 -0.0241 -0.1184 0.0313  321 ASP A OD2 
4462 N N   . LEU A 304 ? 0.2258 0.1355 0.2836 -0.0078 -0.0635 -0.0070 322 LEU A N   
4463 C CA  . LEU A 304 ? 0.2177 0.1290 0.2820 -0.0137 -0.0525 -0.0139 322 LEU A CA  
4464 C C   . LEU A 304 ? 0.2260 0.1385 0.2926 -0.0253 -0.0633 -0.0094 322 LEU A C   
4465 O O   . LEU A 304 ? 0.2756 0.1344 0.2918 -0.0178 -0.0767 -0.0062 322 LEU A O   
4466 C CB  . LEU A 304 ? 0.2287 0.1399 0.2869 -0.0170 -0.0531 0.0015  322 LEU A CB  
4467 C CG  . LEU A 304 ? 0.2375 0.1497 0.2732 0.0002  -0.0686 -0.0252 322 LEU A CG  
4468 C CD1 . LEU A 304 ? 0.2472 0.1707 0.2710 0.0254  -0.0770 -0.0241 322 LEU A CD1 
4469 C CD2 . LEU A 304 ? 0.2578 0.1641 0.2846 -0.0106 -0.0625 -0.0342 322 LEU A CD2 
4481 N N   A MET A 305 ? 0.2342 0.1577 0.3037 -0.0150 -0.0406 -0.0281 323 MET A N   
4482 N N   B MET A 305 ? 0.2387 0.1310 0.2954 -0.0147 -0.0597 -0.0129 323 MET A N   
4483 C CA  A MET A 305 ? 0.2387 0.1839 0.3029 -0.0044 -0.0413 -0.0439 323 MET A CA  
4484 C CA  B MET A 305 ? 0.2423 0.1317 0.2846 -0.0049 -0.0845 -0.0141 323 MET A CA  
4485 C C   A MET A 305 ? 0.2460 0.1768 0.2892 -0.0101 -0.0559 -0.0494 323 MET A C   
4486 C C   B MET A 305 ? 0.2444 0.1542 0.2806 -0.0161 -0.0788 -0.0359 323 MET A C   
4487 O O   A MET A 305 ? 0.2297 0.1694 0.2803 -0.0033 -0.0469 -0.0552 323 MET A O   
4488 O O   B MET A 305 ? 0.2247 0.1545 0.2736 -0.0207 -0.0702 -0.0465 323 MET A O   
4489 C CB  A MET A 305 ? 0.2861 0.2356 0.3240 0.0219  0.0055  -0.0592 323 MET A CB  
4490 C CB  B MET A 305 ? 0.3044 0.1376 0.2883 0.0247  -0.0750 -0.0031 323 MET A CB  
4491 C CG  A MET A 305 ? 0.3235 0.2860 0.3461 0.0328  0.0381  -0.0746 323 MET A CG  
4492 C CG  B MET A 305 ? 0.3599 0.1380 0.2891 0.0257  -0.0816 0.0002  323 MET A CG  
4493 S SD  A MET A 305 ? 0.2834 0.3371 0.3634 0.0369  0.0218  -0.1029 323 MET A SD  
4494 S SD  B MET A 305 ? 0.3828 0.1422 0.2750 0.0037  -0.1409 -0.0072 323 MET A SD  
4495 C CE  A MET A 305 ? 0.2929 0.3437 0.3736 0.0366  0.0235  -0.0916 323 MET A CE  
4496 C CE  B MET A 305 ? 0.3959 0.1462 0.2631 -0.0069 -0.1308 0.0002  323 MET A CE  
4515 N N   . PRO A 306 ? 0.2538 0.1795 0.2917 -0.0067 -0.0864 -0.0436 324 PRO A N   
4516 C CA  . PRO A 306 ? 0.2611 0.1823 0.2925 -0.0088 -0.0795 -0.0521 324 PRO A CA  
4517 C C   . PRO A 306 ? 0.2422 0.1819 0.2971 0.0029  -0.0652 -0.0614 324 PRO A C   
4518 O O   . PRO A 306 ? 0.2248 0.1977 0.3204 0.0046  -0.0494 -0.0655 324 PRO A O   
4519 C CB  . PRO A 306 ? 0.2721 0.1970 0.2869 -0.0067 -0.0843 -0.0687 324 PRO A CB  
4520 C CG  . PRO A 306 ? 0.2927 0.1904 0.2915 -0.0292 -0.0712 -0.0649 324 PRO A CG  
4521 C CD  . PRO A 306 ? 0.2705 0.1923 0.2881 -0.0190 -0.0976 -0.0581 324 PRO A CD  
4529 N N   . TYR A 307 ? 0.2689 0.1796 0.2877 -0.0033 -0.0559 -0.0490 325 TYR A N   
4530 C CA  . TYR A 307 ? 0.2540 0.1692 0.2833 -0.0035 -0.0541 -0.0301 325 TYR A CA  
4531 C C   . TYR A 307 ? 0.2480 0.1853 0.2813 -0.0057 -0.0536 -0.0255 325 TYR A C   
4532 O O   . TYR A 307 ? 0.2429 0.2181 0.3024 -0.0089 -0.0510 -0.0402 325 TYR A O   
4533 C CB  . TYR A 307 ? 0.2554 0.1467 0.2751 0.0074  -0.0510 0.0019  325 TYR A CB  
4534 C CG  . TYR A 307 ? 0.2156 0.1363 0.2642 -0.0030 -0.0757 0.0050  325 TYR A CG  
4535 C CD1 . TYR A 307 ? 0.2436 0.1258 0.2625 -0.0159 -0.0789 0.0018  325 TYR A CD1 
4536 C CD2 . TYR A 307 ? 0.2059 0.1445 0.2821 0.0023  -0.0857 -0.0009 325 TYR A CD2 
4537 C CE1 . TYR A 307 ? 0.2321 0.1469 0.2540 -0.0214 -0.0805 -0.0097 325 TYR A CE1 
4538 C CE2 . TYR A 307 ? 0.2120 0.1662 0.2696 -0.0053 -0.0695 -0.0044 325 TYR A CE2 
4539 C CZ  . TYR A 307 ? 0.2330 0.1381 0.2433 -0.0065 -0.0618 -0.0173 325 TYR A CZ  
4540 O OH  . TYR A 307 ? 0.2285 0.1438 0.2370 0.0101  -0.0685 -0.0226 325 TYR A OH  
4550 N N   . ALA A 308 ? 0.2488 0.1607 0.2732 -0.0093 -0.0511 -0.0273 326 ALA A N   
4551 C CA  . ALA A 308 ? 0.2558 0.1411 0.2691 0.0131  -0.0366 -0.0222 326 ALA A CA  
4552 C C   . ALA A 308 ? 0.2735 0.1536 0.2874 -0.0096 -0.0500 -0.0212 326 ALA A C   
4553 O O   . ALA A 308 ? 0.2603 0.1544 0.2642 -0.0110 -0.0531 -0.0416 326 ALA A O   
4554 C CB  . ALA A 308 ? 0.2502 0.1251 0.2676 0.0266  -0.0492 -0.0101 326 ALA A CB  
4560 N N   . ARG A 309 ? 0.2682 0.1400 0.3087 -0.0245 -0.0655 -0.0174 327 ARG A N   
4561 C CA  . ARG A 309 ? 0.2940 0.1573 0.3391 -0.0314 -0.0832 -0.0229 327 ARG A CA  
4562 C C   . ARG A 309 ? 0.2951 0.1541 0.3420 -0.0095 -0.0940 -0.0316 327 ARG A C   
4563 O O   . ARG A 309 ? 0.3050 0.1435 0.3552 -0.0011 -0.0817 0.0202  327 ARG A O   
4564 C CB  . ARG A 309 ? 0.3010 0.1804 0.3527 -0.0252 -0.0782 -0.0301 327 ARG A CB  
4565 C CG  . ARG A 309 ? 0.2894 0.1999 0.3669 -0.0097 -0.0940 -0.0370 327 ARG A CG  
4566 C CD  . ARG A 309 ? 0.2798 0.1933 0.3651 0.0048  -0.0946 -0.0429 327 ARG A CD  
4567 N NE  . ARG A 309 ? 0.2811 0.2179 0.3741 0.0251  -0.1066 -0.0207 327 ARG A NE  
4568 C CZ  . ARG A 309 ? 0.3052 0.2328 0.3780 -0.0073 -0.1092 -0.0544 327 ARG A CZ  
4569 N NH1 . ARG A 309 ? 0.3450 0.2376 0.4018 -0.0081 -0.0765 -0.0672 327 ARG A NH1 
4570 N NH2 . ARG A 309 ? 0.3223 0.2536 0.3784 0.0081  -0.1133 -0.0412 327 ARG A NH2 
4584 N N   . PRO A 310 ? 0.2860 0.1829 0.3278 0.0079  -0.1021 -0.0410 328 PRO A N   
4585 C CA  . PRO A 310 ? 0.3078 0.2078 0.3396 0.0488  -0.0725 -0.0356 328 PRO A CA  
4586 C C   . PRO A 310 ? 0.2691 0.2028 0.3310 0.0545  -0.0660 -0.0349 328 PRO A C   
4587 O O   . PRO A 310 ? 0.2927 0.2268 0.3534 0.0375  -0.0488 -0.0625 328 PRO A O   
4588 C CB  . PRO A 310 ? 0.3292 0.2394 0.3477 0.0561  -0.0628 -0.0227 328 PRO A CB  
4589 C CG  . PRO A 310 ? 0.3364 0.2538 0.3472 0.0297  -0.0832 -0.0425 328 PRO A CG  
4590 C CD  . PRO A 310 ? 0.3032 0.2271 0.3389 0.0134  -0.0935 -0.0581 328 PRO A CD  
4598 N N   . PHE A 311 ? 0.2315 0.1790 0.2922 0.0230  -0.0606 -0.0312 329 PHE A N   
4599 C CA  . PHE A 311 ? 0.2459 0.1637 0.2790 0.0278  -0.0627 -0.0302 329 PHE A CA  
4600 C C   . PHE A 311 ? 0.2532 0.1770 0.3050 0.0326  -0.0364 -0.0215 329 PHE A C   
4601 O O   . PHE A 311 ? 0.2611 0.2085 0.3081 0.0319  -0.0630 -0.0183 329 PHE A O   
4602 C CB  . PHE A 311 ? 0.2670 0.1736 0.2861 0.0352  -0.0327 -0.0191 329 PHE A CB  
4603 C CG  . PHE A 311 ? 0.2720 0.1907 0.2620 0.0302  -0.0355 -0.0428 329 PHE A CG  
4604 C CD1 . PHE A 311 ? 0.2574 0.2124 0.2508 0.0112  -0.0609 -0.0269 329 PHE A CD1 
4605 C CD2 . PHE A 311 ? 0.2762 0.1897 0.2582 0.0410  -0.0272 -0.0284 329 PHE A CD2 
4606 C CE1 . PHE A 311 ? 0.2678 0.2268 0.2521 0.0138  -0.0408 -0.0181 329 PHE A CE1 
4607 C CE2 . PHE A 311 ? 0.2451 0.1994 0.2503 0.0409  -0.0188 -0.0339 329 PHE A CE2 
4608 C CZ  . PHE A 311 ? 0.2375 0.2143 0.2499 0.0290  -0.0372 -0.0251 329 PHE A CZ  
4618 N N   . ALA A 312 ? 0.2555 0.1712 0.3150 0.0299  -0.0392 -0.0165 330 ALA A N   
4619 C CA  . ALA A 312 ? 0.2902 0.1613 0.3378 0.0001  -0.0393 -0.0002 330 ALA A CA  
4620 C C   . ALA A 312 ? 0.3147 0.1806 0.3664 -0.0104 -0.0446 0.0203  330 ALA A C   
4621 O O   . ALA A 312 ? 0.2794 0.1822 0.3632 -0.0317 -0.0825 0.0286  330 ALA A O   
4622 C CB  . ALA A 312 ? 0.3256 0.1736 0.3345 -0.0379 -0.0212 -0.0032 330 ALA A CB  
4628 N N   . VAL A 313 ? 0.3456 0.1875 0.4124 0.0241  -0.0322 0.0241  331 VAL A N   
4629 C CA  . VAL A 313 ? 0.3239 0.1990 0.4309 0.0263  -0.0566 0.0277  331 VAL A CA  
4630 C C   . VAL A 313 ? 0.2811 0.1915 0.4440 0.0291  -0.0968 0.0308  331 VAL A C   
4631 O O   . VAL A 313 ? 0.2774 0.2006 0.4698 0.0356  -0.0803 0.0135  331 VAL A O   
4632 C CB  . VAL A 313 ? 0.2892 0.2495 0.4419 0.0472  -0.0808 0.0323  331 VAL A CB  
4633 C CG1 . VAL A 313 ? 0.3133 0.2688 0.4490 0.0529  -0.0668 0.0194  331 VAL A CG1 
4634 C CG2 . VAL A 313 ? 0.3516 0.2761 0.4592 0.0304  -0.0392 0.0268  331 VAL A CG2 
4644 N N   . GLY A 314 ? 0.2924 0.2049 0.4436 -0.0179 -0.1027 0.0499  332 GLY A N   
4645 C CA  . GLY A 314 ? 0.3087 0.2093 0.4348 -0.0149 -0.1116 0.0655  332 GLY A CA  
4646 C C   . GLY A 314 ? 0.3202 0.2095 0.4320 -0.0185 -0.0995 0.0713  332 GLY A C   
4647 O O   . GLY A 314 ? 0.3623 0.2278 0.4358 -0.0010 -0.0875 0.0607  332 GLY A O   
4651 N N   . LYS A 315 ? 0.2658 0.2047 0.4364 -0.0528 -0.1249 0.0768  333 LYS A N   
4652 C CA  . LYS A 315 ? 0.2446 0.1879 0.4307 -0.0471 -0.1257 0.0743  333 LYS A CA  
4653 C C   . LYS A 315 ? 0.2672 0.2008 0.4236 -0.0456 -0.1194 0.0428  333 LYS A C   
4654 O O   . LYS A 315 ? 0.3107 0.2307 0.4312 -0.0510 -0.1044 0.0336  333 LYS A O   
4655 C CB  . LYS A 315 ? 0.2741 0.2059 0.4502 -0.0498 -0.1059 0.0783  333 LYS A CB  
4656 C CG  . LYS A 315 ? 0.3102 0.2480 0.4683 -0.0588 -0.1130 0.0839  333 LYS A CG  
4657 C CD  . LYS A 315 ? 0.3271 0.2922 0.4969 -0.1173 -0.1373 0.0749  333 LYS A CD  
4658 C CE  . LYS A 315 ? 0.3927 0.3351 0.5138 -0.1001 -0.1366 0.0942  333 LYS A CE  
4659 N NZ  . LYS A 315 ? 0.4459 0.3646 0.5419 -0.1054 -0.1028 0.0959  333 LYS A NZ  
4673 N N   . ARG A 316 ? 0.2563 0.1827 0.4107 -0.0281 -0.1166 0.0237  334 ARG A N   
4674 C CA  . ARG A 316 ? 0.2673 0.1775 0.3858 -0.0103 -0.1275 0.0193  334 ARG A CA  
4675 C C   . ARG A 316 ? 0.2555 0.1444 0.3653 -0.0023 -0.1254 -0.0099 334 ARG A C   
4676 O O   . ARG A 316 ? 0.3053 0.1639 0.3918 0.0218  -0.1367 -0.0191 334 ARG A O   
4677 C CB  . ARG A 316 ? 0.3082 0.1885 0.3671 -0.0109 -0.1389 0.0263  334 ARG A CB  
4678 C CG  . ARG A 316 ? 0.3680 0.2235 0.3820 0.0137  -0.1041 0.0280  334 ARG A CG  
4679 C CD  . ARG A 316 ? 0.4221 0.2385 0.4021 0.0378  -0.0799 0.0316  334 ARG A CD  
4680 N NE  . ARG A 316 ? 0.4986 0.2662 0.4334 0.0269  -0.0449 0.0076  334 ARG A NE  
4681 C CZ  . ARG A 316 ? 0.5746 0.3025 0.4652 0.0384  -0.0085 0.0135  334 ARG A CZ  
4682 N NH1 . ARG A 316 ? 0.6010 0.3148 0.4666 0.0262  -0.0085 0.0157  334 ARG A NH1 
4683 N NH2 . ARG A 316 ? 0.6012 0.3093 0.4864 0.0597  0.0183  0.0180  334 ARG A NH2 
4697 N N   . THR A 317 ? 0.2277 0.1312 0.3329 -0.0002 -0.1033 -0.0054 335 THR A N   
4698 C CA  . THR A 317 ? 0.2306 0.1132 0.3118 -0.0139 -0.0903 0.0055  335 THR A CA  
4699 C C   . THR A 317 ? 0.2326 0.1169 0.2923 -0.0144 -0.0956 0.0070  335 THR A C   
4700 O O   . THR A 317 ? 0.2623 0.1104 0.3030 -0.0079 -0.0737 0.0033  335 THR A O   
4701 C CB  . THR A 317 ? 0.2212 0.1204 0.3106 -0.0313 -0.0661 0.0050  335 THR A CB  
4702 O OG1 . THR A 317 ? 0.2173 0.1255 0.3069 -0.0215 -0.0320 0.0049  335 THR A OG1 
4703 C CG2 . THR A 317 ? 0.2404 0.1364 0.3220 -0.0247 -0.0709 0.0030  335 THR A CG2 
4711 N N   . CYS A 318 ? 0.2448 0.0949 0.2849 -0.0270 -0.0810 0.0086  336 CYS A N   
4712 C CA  . CYS A 318 ? 0.2425 0.1011 0.2811 -0.0381 -0.0548 0.0100  336 CYS A CA  
4713 C C   . CYS A 318 ? 0.2644 0.1115 0.2793 -0.0216 -0.0695 0.0073  336 CYS A C   
4714 O O   . CYS A 318 ? 0.3055 0.0983 0.3042 -0.0069 -0.0438 0.0159  336 CYS A O   
4715 C CB  . CYS A 318 ? 0.2673 0.1229 0.2806 -0.0298 -0.0452 -0.0032 336 CYS A CB  
4716 S SG  . CYS A 318 ? 0.2572 0.1437 0.2893 -0.0208 -0.0593 0.0022  336 CYS A SG  
4721 N N   . SER A 319 ? 0.2669 0.1151 0.2873 -0.0238 -0.0776 -0.0269 337 SER A N   
4722 C CA  . SER A 319 ? 0.2486 0.1221 0.3088 0.0142  -0.0968 -0.0088 337 SER A CA  
4723 C C   . SER A 319 ? 0.2476 0.1103 0.3479 0.0047  -0.0887 -0.0202 337 SER A C   
4724 O O   . SER A 319 ? 0.2874 0.1184 0.3675 0.0052  -0.0846 -0.0229 337 SER A O   
4725 C CB  . SER A 319 ? 0.2856 0.1509 0.3222 0.0168  -0.1002 -0.0137 337 SER A CB  
4726 O OG  . SER A 319 ? 0.3013 0.1663 0.3426 0.0085  -0.0867 0.0017  337 SER A OG  
4732 N N   . GLY A 320 ? 0.2197 0.1282 0.3770 0.0022  -0.0901 -0.0181 338 GLY A N   
4733 C CA  . GLY A 320 ? 0.2299 0.1313 0.4128 -0.0008 -0.0915 -0.0053 338 GLY A CA  
4734 C C   . GLY A 320 ? 0.2304 0.1500 0.4116 -0.0116 -0.0992 -0.0055 338 GLY A C   
4735 O O   . GLY A 320 ? 0.2589 0.1427 0.4042 -0.0150 -0.1074 -0.0149 338 GLY A O   
4739 N N   . ILE A 321 ? 0.2417 0.1795 0.4191 0.0132  -0.1175 0.0159  339 ILE A N   
4740 C CA  . ILE A 321 ? 0.2623 0.2170 0.4394 0.0031  -0.0899 0.0107  339 ILE A CA  
4741 C C   . ILE A 321 ? 0.2876 0.2548 0.4264 -0.0299 -0.0918 -0.0065 339 ILE A C   
4742 O O   . ILE A 321 ? 0.3224 0.2910 0.4441 -0.0569 -0.0878 -0.0161 339 ILE A O   
4743 C CB  . ILE A 321 ? 0.2381 0.2522 0.4666 0.0068  -0.0830 0.0253  339 ILE A CB  
4744 C CG1 . ILE A 321 ? 0.2412 0.2605 0.4855 0.0083  -0.0573 0.0443  339 ILE A CG1 
4745 C CG2 . ILE A 321 ? 0.2673 0.2607 0.4766 -0.0041 -0.0669 -0.0053 339 ILE A CG2 
4746 C CD1 . ILE A 321 ? 0.2492 0.2773 0.5051 0.0201  -0.0434 0.0577  339 ILE A CD1 
4758 N N   . VAL A 322 ? 0.2561 0.2530 0.4117 -0.0261 -0.0881 0.0043  340 VAL A N   
4759 C CA  . VAL A 322 ? 0.2755 0.2774 0.3978 0.0050  -0.0935 0.0143  340 VAL A CA  
4760 C C   . VAL A 322 ? 0.3043 0.2874 0.3903 0.0174  -0.1151 -0.0038 340 VAL A C   
4761 O O   . VAL A 322 ? 0.3023 0.2695 0.3811 0.0239  -0.1183 -0.0030 340 VAL A O   
4762 C CB  . VAL A 322 ? 0.2905 0.2876 0.4019 -0.0033 -0.0377 0.0500  340 VAL A CB  
4763 C CG1 . VAL A 322 ? 0.3138 0.3070 0.4020 -0.0071 -0.0240 0.0614  340 VAL A CG1 
4764 C CG2 . VAL A 322 ? 0.2538 0.2850 0.4079 -0.0028 -0.0344 0.0507  340 VAL A CG2 
4774 N N   . THR A 323 ? 0.3309 0.3048 0.4034 0.0170  -0.1035 -0.0216 341 THR A N   
4775 C CA  . THR A 323 ? 0.3404 0.3229 0.4089 0.0238  -0.1121 -0.0105 341 THR A CA  
4776 C C   . THR A 323 ? 0.3283 0.3411 0.4072 0.0308  -0.1150 -0.0052 341 THR A C   
4777 O O   . THR A 323 ? 0.3019 0.3365 0.4030 0.0277  -0.0843 -0.0096 341 THR A O   
4778 C CB  . THR A 323 ? 0.3795 0.3140 0.4149 0.0385  -0.1202 -0.0244 341 THR A CB  
4779 O OG1 . THR A 323 ? 0.4117 0.3081 0.4316 -0.0005 -0.1147 -0.0398 341 THR A OG1 
4780 C CG2 . THR A 323 ? 0.4077 0.3197 0.4330 0.0392  -0.0892 -0.0375 341 THR A CG2 
4788 N N   . PRO A 324 ? 0.3991 0.3713 0.4289 0.0634  -0.0989 0.0109  342 PRO A N   
4789 C CA  . PRO A 324 ? 0.4406 0.4065 0.4552 0.0656  -0.0835 0.0058  342 PRO A CA  
4790 C C   . PRO A 324 ? 0.4694 0.4411 0.4842 0.0455  -0.0819 -0.0126 342 PRO A C   
4791 O O   . PRO A 324 ? 0.5055 0.4755 0.5084 0.0281  -0.0745 -0.0297 342 PRO A O   
4792 C CB  . PRO A 324 ? 0.4438 0.4017 0.4567 0.0784  -0.0636 0.0143  342 PRO A CB  
4793 C CG  . PRO A 324 ? 0.4378 0.3859 0.4477 0.0800  -0.0762 0.0094  342 PRO A CG  
4794 C CD  . PRO A 324 ? 0.4083 0.3739 0.4252 0.0836  -0.1109 0.0136  342 PRO A CD  
4802 N N   . LEU B 8   ? 0.3605 0.3149 0.4311 0.0427  -0.0640 0.0639  26  LEU B N   
4803 C CA  . LEU B 8   ? 0.3034 0.2943 0.3705 0.0494  -0.1036 0.0549  26  LEU B CA  
4804 C C   . LEU B 8   ? 0.2921 0.2678 0.3397 0.0645  -0.0914 0.0468  26  LEU B C   
4805 O O   . LEU B 8   ? 0.2887 0.2915 0.3522 0.0738  -0.1044 0.0407  26  LEU B O   
4806 C CB  . LEU B 8   ? 0.3070 0.2896 0.3471 0.0402  -0.1264 0.0424  26  LEU B CB  
4807 C CG  . LEU B 8   ? 0.3371 0.2832 0.3511 0.0521  -0.0959 0.0343  26  LEU B CG  
4808 C CD1 . LEU B 8   ? 0.3883 0.2991 0.3491 0.0389  -0.0642 0.0202  26  LEU B CD1 
4809 C CD2 . LEU B 8   ? 0.3292 0.2901 0.3640 0.0713  -0.0793 0.0297  26  LEU B CD2 
4821 N N   . PRO B 9   ? 0.2931 0.2496 0.2988 0.0420  -0.0744 0.0511  27  PRO B N   
4822 C CA  . PRO B 9   ? 0.3124 0.2498 0.2963 0.0388  -0.0592 0.0518  27  PRO B CA  
4823 C C   . PRO B 9   ? 0.3324 0.2681 0.3087 0.0547  -0.0469 0.0660  27  PRO B C   
4824 O O   . PRO B 9   ? 0.3356 0.2496 0.2844 0.0493  -0.0533 0.0613  27  PRO B O   
4825 C CB  . PRO B 9   ? 0.2810 0.2303 0.2725 0.0318  -0.0576 0.0578  27  PRO B CB  
4826 C CG  . PRO B 9   ? 0.2884 0.2162 0.2668 0.0303  -0.0366 0.0566  27  PRO B CG  
4827 C CD  . PRO B 9   ? 0.2851 0.2462 0.2795 0.0356  -0.0657 0.0366  27  PRO B CD  
4835 N N   . SER B 10  ? 0.3698 0.3095 0.3444 0.0667  -0.0343 0.0579  28  SER B N   
4836 C CA  . SER B 10  ? 0.3890 0.3201 0.3572 0.0732  -0.0537 0.0595  28  SER B CA  
4837 C C   . SER B 10  ? 0.3913 0.2964 0.3644 0.0744  -0.0441 0.0750  28  SER B C   
4838 O O   . SER B 10  ? 0.3778 0.2972 0.3810 0.0380  -0.0278 0.0780  28  SER B O   
4839 C CB  . SER B 10  ? 0.4650 0.3532 0.3852 0.0704  -0.0363 0.0509  28  SER B CB  
4840 O OG  . SER B 10  ? 0.5246 0.3938 0.4133 0.0598  -0.0189 0.0438  28  SER B OG  
4846 N N   . GLY B 11  ? 0.3917 0.2882 0.3864 0.0868  -0.0313 0.0881  29  GLY B N   
4847 C CA  . GLY B 11  ? 0.3936 0.2746 0.3702 0.0582  -0.0479 0.0980  29  GLY B CA  
4848 C C   . GLY B 11  ? 0.3784 0.2661 0.3262 0.0412  -0.0706 0.0976  29  GLY B C   
4849 O O   . GLY B 11  ? 0.3638 0.2675 0.3202 0.0163  -0.0687 0.1212  29  GLY B O   
4853 N N   . SER B 12  ? 0.3944 0.2576 0.2804 0.0271  -0.0925 0.0589  30  SER B N   
4854 C CA  . SER B 12  ? 0.3901 0.2502 0.2722 0.0199  -0.0710 0.0403  30  SER B CA  
4855 C C   . SER B 12  ? 0.3438 0.2027 0.2531 0.0053  -0.0517 0.0321  30  SER B C   
4856 O O   . SER B 12  ? 0.3348 0.2062 0.2670 0.0177  -0.0201 0.0353  30  SER B O   
4857 C CB  . SER B 12  ? 0.4483 0.2857 0.2872 0.0159  -0.0574 0.0616  30  SER B CB  
4858 O OG  . SER B 12  ? 0.4990 0.3251 0.3310 0.0155  -0.0315 0.0692  30  SER B OG  
4864 N N   . ASP B 13  ? 0.3171 0.1723 0.2350 0.0087  -0.0402 0.0195  31  ASP B N   
4865 C CA  . ASP B 13  ? 0.2746 0.1698 0.2370 -0.0049 -0.0532 0.0304  31  ASP B CA  
4866 C C   . ASP B 13  ? 0.2839 0.1720 0.2449 -0.0085 -0.0342 0.0263  31  ASP B C   
4867 O O   . ASP B 13  ? 0.3118 0.1957 0.2365 -0.0274 -0.0158 0.0307  31  ASP B O   
4868 C CB  . ASP B 13  ? 0.2586 0.1647 0.2336 0.0199  -0.0485 0.0380  31  ASP B CB  
4869 C CG  . ASP B 13  ? 0.2642 0.1785 0.2424 0.0068  -0.0617 0.0005  31  ASP B CG  
4870 O OD1 . ASP B 13  ? 0.2567 0.1874 0.2380 0.0146  -0.0541 -0.0078 31  ASP B OD1 
4871 O OD2 . ASP B 13  ? 0.2589 0.1624 0.2696 0.0081  -0.0611 -0.0194 31  ASP B OD2 
4876 N N   . PRO B 14  ? 0.2476 0.1644 0.2616 -0.0200 -0.0445 0.0002  32  PRO B N   
4877 C CA  . PRO B 14  ? 0.2399 0.1854 0.2671 -0.0360 -0.0454 0.0022  32  PRO B CA  
4878 C C   . PRO B 14  ? 0.2413 0.1880 0.2822 -0.0286 -0.0315 0.0142  32  PRO B C   
4879 O O   . PRO B 14  ? 0.2226 0.1827 0.3029 -0.0152 -0.0167 0.0161  32  PRO B O   
4880 C CB  . PRO B 14  ? 0.2785 0.1997 0.2565 -0.0355 -0.0233 -0.0201 32  PRO B CB  
4881 C CG  . PRO B 14  ? 0.2714 0.1971 0.2426 -0.0289 -0.0320 -0.0066 32  PRO B CG  
4882 C CD  . PRO B 14  ? 0.2593 0.1745 0.2524 -0.0048 -0.0307 0.0098  32  PRO B CD  
4890 N N   . ALA B 15  ? 0.2482 0.2267 0.2950 -0.0399 -0.0363 0.0340  33  ALA B N   
4891 C CA  . ALA B 15  ? 0.2734 0.2324 0.3288 -0.0422 -0.0256 0.0299  33  ALA B CA  
4892 C C   . ALA B 15  ? 0.2618 0.2154 0.3100 -0.0314 -0.0321 0.0139  33  ALA B C   
4893 O O   . ALA B 15  ? 0.2658 0.2160 0.3262 0.0132  -0.0319 0.0146  33  ALA B O   
4894 C CB  . ALA B 15  ? 0.2869 0.2631 0.3607 -0.0352 -0.0351 0.0413  33  ALA B CB  
4900 N N   . PHE B 16  ? 0.2581 0.1813 0.2902 -0.0441 -0.0305 0.0086  34  PHE B N   
4901 C CA  . PHE B 16  ? 0.2624 0.1757 0.3015 -0.0304 -0.0427 0.0111  34  PHE B CA  
4902 C C   . PHE B 16  ? 0.2403 0.1938 0.2999 -0.0422 -0.0471 0.0183  34  PHE B C   
4903 O O   . PHE B 16  ? 0.2790 0.2246 0.3075 -0.0664 -0.0009 0.0257  34  PHE B O   
4904 C CB  . PHE B 16  ? 0.2785 0.1857 0.3027 -0.0184 -0.0342 -0.0097 34  PHE B CB  
4905 C CG  . PHE B 16  ? 0.2525 0.2044 0.2834 -0.0417 -0.0493 0.0100  34  PHE B CG  
4906 C CD1 . PHE B 16  ? 0.2665 0.2037 0.2818 -0.0450 -0.0462 0.0040  34  PHE B CD1 
4907 C CD2 . PHE B 16  ? 0.2808 0.2185 0.3000 -0.0320 -0.0363 0.0176  34  PHE B CD2 
4908 C CE1 . PHE B 16  ? 0.2646 0.2342 0.2942 -0.0432 -0.0315 0.0061  34  PHE B CE1 
4909 C CE2 . PHE B 16  ? 0.2542 0.2454 0.3126 -0.0359 -0.0579 0.0115  34  PHE B CE2 
4910 C CZ  . PHE B 16  ? 0.2304 0.2387 0.3052 -0.0442 -0.0366 0.0113  34  PHE B CZ  
4920 N N   . SER B 17  ? 0.2502 0.1886 0.2977 -0.0351 -0.0661 -0.0054 35  SER B N   
4921 C CA  . SER B 17  ? 0.2513 0.1805 0.3143 -0.0365 -0.0520 -0.0246 35  SER B CA  
4922 C C   . SER B 17  ? 0.2415 0.1803 0.3364 -0.0446 -0.0435 -0.0446 35  SER B C   
4923 O O   . SER B 17  ? 0.2321 0.2004 0.3672 -0.0498 -0.0322 -0.0567 35  SER B O   
4924 C CB  . SER B 17  ? 0.2936 0.1933 0.3139 -0.0333 -0.0225 -0.0274 35  SER B CB  
4925 O OG  . SER B 17  ? 0.3190 0.2144 0.3015 -0.0358 -0.0320 -0.0285 35  SER B OG  
4931 N N   . GLN B 18  ? 0.2371 0.1824 0.3567 -0.0308 -0.0554 -0.0418 36  GLN B N   
4932 C CA  . GLN B 18  ? 0.2634 0.2077 0.3775 0.0016  -0.0595 -0.0553 36  GLN B CA  
4933 C C   . GLN B 18  ? 0.2933 0.2229 0.3906 -0.0023 -0.0422 -0.0366 36  GLN B C   
4934 O O   . GLN B 18  ? 0.3163 0.2299 0.3793 0.0197  -0.0421 -0.0349 36  GLN B O   
4935 C CB  . GLN B 18  ? 0.3315 0.2446 0.3887 0.0330  -0.0565 -0.0572 36  GLN B CB  
4936 C CG  . GLN B 18  ? 0.4005 0.2913 0.4238 0.0343  -0.0523 -0.0650 36  GLN B CG  
4937 C CD  . GLN B 18  ? 0.4706 0.3339 0.4597 0.0160  -0.0363 -0.0703 36  GLN B CD  
4938 O OE1 . GLN B 18  ? 0.4957 0.3601 0.4884 0.0121  -0.0344 -0.0721 36  GLN B OE1 
4939 N NE2 . GLN B 18  ? 0.5006 0.3450 0.4618 0.0256  -0.0437 -0.0560 36  GLN B NE2 
4948 N N   . PRO B 19  ? 0.3237 0.2356 0.4291 -0.0275 -0.0161 -0.0504 37  PRO B N   
4949 C CA  . PRO B 19  ? 0.3198 0.2494 0.4387 -0.0217 -0.0139 -0.0550 37  PRO B CA  
4950 C C   . PRO B 19  ? 0.3283 0.2551 0.4274 -0.0004 -0.0003 -0.0455 37  PRO B C   
4951 O O   . PRO B 19  ? 0.2752 0.2407 0.4182 -0.0072 -0.0177 -0.0408 37  PRO B O   
4952 C CB  . PRO B 19  ? 0.3367 0.2547 0.4588 -0.0243 -0.0070 -0.0593 37  PRO B CB  
4953 C CG  . PRO B 19  ? 0.3311 0.2566 0.4554 -0.0341 -0.0039 -0.0671 37  PRO B CG  
4954 C CD  . PRO B 19  ? 0.3313 0.2476 0.4513 -0.0319 -0.0228 -0.0601 37  PRO B CD  
4962 N N   A LYS B 20  ? 0.3819 0.2704 0.4268 0.0007  0.0185  -0.0461 38  LYS B N   
4963 N N   B LYS B 20  ? 0.3623 0.2674 0.4314 0.0038  0.0188  -0.0336 38  LYS B N   
4964 C CA  A LYS B 20  ? 0.4282 0.2777 0.4228 0.0111  0.0266  -0.0597 38  LYS B CA  
4965 C CA  B LYS B 20  ? 0.3896 0.2738 0.4328 0.0156  0.0296  -0.0316 38  LYS B CA  
4966 C C   A LYS B 20  ? 0.3858 0.2739 0.4270 0.0183  0.0363  -0.0706 38  LYS B C   
4967 C C   B LYS B 20  ? 0.3701 0.2736 0.4333 0.0187  0.0384  -0.0535 38  LYS B C   
4968 O O   A LYS B 20  ? 0.3735 0.2615 0.4214 0.0257  0.0323  -0.0925 38  LYS B O   
4969 O O   B LYS B 20  ? 0.3619 0.2648 0.4293 0.0240  0.0349  -0.0694 38  LYS B O   
4970 C CB  A LYS B 20  ? 0.4925 0.2943 0.4232 0.0094  0.0293  -0.0532 38  LYS B CB  
4971 C CB  B LYS B 20  ? 0.4139 0.2839 0.4396 0.0206  0.0340  -0.0006 38  LYS B CB  
4972 C CG  A LYS B 20  ? 0.5277 0.3051 0.4170 0.0049  0.0282  -0.0693 38  LYS B CG  
4973 C CG  B LYS B 20  ? 0.4117 0.2911 0.4430 0.0245  0.0360  0.0137  38  LYS B CG  
4974 C CD  A LYS B 20  ? 0.5485 0.3219 0.4204 -0.0001 0.0130  -0.0698 38  LYS B CD  
4975 C CD  B LYS B 20  ? 0.4078 0.2939 0.4441 0.0325  0.0294  0.0247  38  LYS B CD  
4976 C CE  A LYS B 20  ? 0.5446 0.3286 0.4186 -0.0036 -0.0071 -0.0796 38  LYS B CE  
4977 C CE  B LYS B 20  ? 0.3990 0.2867 0.4447 0.0391  0.0323  0.0279  38  LYS B CE  
4978 N NZ  A LYS B 20  ? 0.5196 0.3317 0.4147 0.0016  -0.0365 -0.0871 38  LYS B NZ  
4979 N NZ  B LYS B 20  ? 0.3933 0.2838 0.4458 0.0389  0.0390  0.0311  38  LYS B NZ  
5006 N N   . SER B 21  ? 0.3749 0.2826 0.4432 0.0103  0.0553  -0.0606 39  SER B N   
5007 C CA  . SER B 21  ? 0.3265 0.2930 0.4597 0.0090  0.0560  -0.0578 39  SER B CA  
5008 C C   . SER B 21  ? 0.2689 0.2619 0.4274 0.0086  0.0261  -0.0665 39  SER B C   
5009 O O   . SER B 21  ? 0.2660 0.2789 0.4398 0.0140  0.0234  -0.0658 39  SER B O   
5010 C CB  . SER B 21  ? 0.3652 0.3283 0.4871 -0.0087 0.0654  -0.0528 39  SER B CB  
5011 O OG  . SER B 21  ? 0.4222 0.3736 0.5144 -0.0243 0.0667  -0.0415 39  SER B OG  
5017 N N   . VAL B 22  ? 0.2396 0.2465 0.4119 0.0009  0.0042  -0.0619 40  VAL B N   
5018 C CA  . VAL B 22  ? 0.2250 0.2244 0.3737 -0.0126 -0.0323 -0.0803 40  VAL B CA  
5019 C C   . VAL B 22  ? 0.1874 0.2017 0.3238 0.0081  -0.0526 -0.0701 40  VAL B C   
5020 O O   . VAL B 22  ? 0.2004 0.2067 0.3300 0.0173  -0.0472 -0.0659 40  VAL B O   
5021 C CB  . VAL B 22  ? 0.2470 0.2072 0.3993 -0.0305 -0.0382 -0.0944 40  VAL B CB  
5022 C CG1 . VAL B 22  ? 0.2815 0.1905 0.3943 -0.0505 -0.0450 -0.1073 40  VAL B CG1 
5023 C CG2 . VAL B 22  ? 0.2988 0.2294 0.4319 -0.0461 -0.0128 -0.0955 40  VAL B CG2 
5033 N N   . LEU B 23  ? 0.2020 0.2021 0.2951 0.0103  -0.0324 -0.0562 41  LEU B N   
5034 C CA  . LEU B 23  ? 0.2039 0.2027 0.2735 0.0249  -0.0459 -0.0680 41  LEU B CA  
5035 C C   . LEU B 23  ? 0.2062 0.2057 0.2861 0.0345  -0.0376 -0.0676 41  LEU B C   
5036 O O   . LEU B 23  ? 0.2086 0.2118 0.2775 0.0320  -0.0148 -0.0607 41  LEU B O   
5037 C CB  . LEU B 23  ? 0.2071 0.1909 0.2585 0.0352  -0.0332 -0.0605 41  LEU B CB  
5038 C CG  . LEU B 23  ? 0.2304 0.1980 0.2491 0.0257  -0.0486 -0.0401 41  LEU B CG  
5039 C CD1 . LEU B 23  ? 0.2469 0.2050 0.2764 0.0483  -0.0363 -0.0302 41  LEU B CD1 
5040 C CD2 . LEU B 23  ? 0.2187 0.2109 0.2538 0.0197  -0.0671 -0.0455 41  LEU B CD2 
5052 N N   . ASP B 24  ? 0.2286 0.2140 0.3074 0.0502  -0.0234 -0.0816 42  ASP B N   
5053 C CA  . ASP B 24  ? 0.2329 0.2312 0.3306 0.0303  -0.0184 -0.0665 42  ASP B CA  
5054 C C   . ASP B 24  ? 0.2244 0.2190 0.3313 0.0269  -0.0192 -0.0582 42  ASP B C   
5055 O O   . ASP B 24  ? 0.2454 0.2183 0.3289 0.0117  -0.0040 -0.0615 42  ASP B O   
5056 C CB  . ASP B 24  ? 0.2278 0.2614 0.3365 0.0339  -0.0205 -0.0665 42  ASP B CB  
5057 C CG  . ASP B 24  ? 0.2573 0.3159 0.3559 0.0153  -0.0126 -0.0586 42  ASP B CG  
5058 O OD1 . ASP B 24  ? 0.2629 0.3370 0.3541 0.0182  -0.0287 -0.0577 42  ASP B OD1 
5059 O OD2 . ASP B 24  ? 0.2705 0.3444 0.3746 0.0246  0.0121  -0.0625 42  ASP B OD2 
5064 N N   . ALA B 25  ? 0.2049 0.2301 0.3390 0.0324  -0.0418 -0.0626 43  ALA B N   
5065 C CA  . ALA B 25  ? 0.2171 0.2385 0.3452 0.0001  -0.0565 -0.0694 43  ALA B CA  
5066 C C   . ALA B 25  ? 0.2348 0.2276 0.3386 0.0239  -0.0551 -0.0560 43  ALA B C   
5067 O O   . ALA B 25  ? 0.2565 0.2472 0.3446 0.0455  -0.0641 -0.0469 43  ALA B O   
5068 C CB  . ALA B 25  ? 0.2411 0.2555 0.3678 -0.0118 -0.0326 -0.0642 43  ALA B CB  
5074 N N   . GLY B 26  ? 0.2203 0.1917 0.3148 0.0310  -0.0517 -0.0693 44  GLY B N   
5075 C CA  . GLY B 26  ? 0.2333 0.1880 0.3038 0.0417  -0.0558 -0.0657 44  GLY B CA  
5076 C C   . GLY B 26  ? 0.2158 0.1712 0.2836 0.0297  -0.0586 -0.0592 44  GLY B C   
5077 O O   . GLY B 26  ? 0.2455 0.1793 0.2707 -0.0101 -0.0491 -0.0620 44  GLY B O   
5081 N N   . LEU B 27  ? 0.2392 0.1787 0.2909 0.0214  -0.0497 -0.0688 45  LEU B N   
5082 C CA  . LEU B 27  ? 0.2198 0.1727 0.2850 0.0377  -0.0756 -0.0774 45  LEU B CA  
5083 C C   . LEU B 27  ? 0.2392 0.1703 0.3031 0.0633  -0.0797 -0.0665 45  LEU B C   
5084 O O   . LEU B 27  ? 0.2533 0.1938 0.3299 0.0652  -0.0629 -0.0991 45  LEU B O   
5085 C CB  . LEU B 27  ? 0.2442 0.1890 0.2976 0.0368  -0.0899 -0.0618 45  LEU B CB  
5086 C CG  . LEU B 27  ? 0.2582 0.1925 0.3033 0.0588  -0.1003 -0.0500 45  LEU B CG  
5087 C CD1 . LEU B 27  ? 0.2650 0.2048 0.3204 0.0624  -0.0893 -0.0441 45  LEU B CD1 
5088 C CD2 . LEU B 27  ? 0.2850 0.2191 0.3182 0.0299  -0.0976 -0.0573 45  LEU B CD2 
5100 N N   . THR B 28  ? 0.2631 0.1566 0.3088 0.0408  -0.0658 -0.0755 46  THR B N   
5101 C CA  . THR B 28  ? 0.2756 0.1650 0.3219 0.0513  -0.0764 -0.0789 46  THR B CA  
5102 C C   . THR B 28  ? 0.2581 0.1678 0.3263 0.0525  -0.0851 -0.0870 46  THR B C   
5103 O O   . THR B 28  ? 0.2667 0.1671 0.3347 0.0315  -0.0779 -0.1042 46  THR B O   
5104 C CB  . THR B 28  ? 0.2592 0.1674 0.3450 0.0709  -0.1051 -0.0676 46  THR B CB  
5105 O OG1 . THR B 28  ? 0.2700 0.2080 0.3583 0.0485  -0.1038 -0.0774 46  THR B OG1 
5106 C CG2 . THR B 28  ? 0.2863 0.1536 0.3583 0.0502  -0.0973 -0.0679 46  THR B CG2 
5114 N N   . CYS B 29  ? 0.2732 0.1779 0.3536 0.0221  -0.0735 -0.1062 47  CYS B N   
5115 C CA  . CYS B 29  ? 0.2966 0.1795 0.3628 0.0455  -0.0792 -0.1187 47  CYS B CA  
5116 C C   . CYS B 29  ? 0.3014 0.1957 0.3959 0.0684  -0.0904 -0.1212 47  CYS B C   
5117 O O   . CYS B 29  ? 0.3011 0.2142 0.4098 0.0728  -0.0594 -0.1428 47  CYS B O   
5118 C CB  . CYS B 29  ? 0.3299 0.1965 0.3560 0.0646  -0.0612 -0.1086 47  CYS B CB  
5119 S SG  . CYS B 29  ? 0.3373 0.2023 0.3300 0.0562  -0.0623 -0.1067 47  CYS B SG  
5124 N N   . GLN B 30  ? 0.3250 0.2171 0.4110 0.0780  -0.1092 -0.1066 48  GLN B N   
5125 C CA  . GLN B 30  ? 0.3575 0.2060 0.4278 0.0923  -0.0902 -0.1080 48  GLN B CA  
5126 C C   . GLN B 30  ? 0.3822 0.2361 0.4386 0.1129  -0.0944 -0.0991 48  GLN B C   
5127 O O   . GLN B 30  ? 0.3848 0.2457 0.4395 0.0965  -0.1230 -0.1013 48  GLN B O   
5128 C CB  . GLN B 30  ? 0.3770 0.1947 0.4432 0.1147  -0.0756 -0.0746 48  GLN B CB  
5129 C CG  . GLN B 30  ? 0.4125 0.1762 0.4705 0.0947  -0.0452 -0.0611 48  GLN B CG  
5130 C CD  . GLN B 30  ? 0.4708 0.1840 0.4818 0.0686  -0.0067 -0.0860 48  GLN B CD  
5131 O OE1 . GLN B 30  ? 0.4991 0.2050 0.5000 0.0356  0.0366  -0.0919 48  GLN B OE1 
5132 N NE2 . GLN B 30  ? 0.4980 0.1817 0.4877 0.0835  0.0218  -0.1023 48  GLN B NE2 
5141 N N   . GLY B 31  ? 0.3811 0.2515 0.4396 0.1483  -0.0631 -0.1053 49  GLY B N   
5142 C CA  . GLY B 31  ? 0.4014 0.2666 0.4328 0.1594  -0.0418 -0.1085 49  GLY B CA  
5143 C C   . GLY B 31  ? 0.4138 0.2774 0.4202 0.1573  -0.0497 -0.1155 49  GLY B C   
5144 O O   . GLY B 31  ? 0.4585 0.3022 0.4408 0.1472  -0.0135 -0.1159 49  GLY B O   
5148 N N   . ALA B 32  ? 0.3991 0.2834 0.4055 0.1270  -0.0809 -0.1227 50  ALA B N   
5149 C CA  . ALA B 32  ? 0.3735 0.2826 0.3737 0.0982  -0.0658 -0.1237 50  ALA B CA  
5150 C C   . ALA B 32  ? 0.3480 0.2990 0.3741 0.0788  -0.0640 -0.1053 50  ALA B C   
5151 O O   . ALA B 32  ? 0.3706 0.3111 0.3747 0.0550  -0.0670 -0.1049 50  ALA B O   
5152 C CB  . ALA B 32  ? 0.3870 0.2784 0.3649 0.0923  -0.0625 -0.1115 50  ALA B CB  
5158 N N   . SER B 33  ? 0.3053 0.2981 0.3680 0.0875  -0.0406 -0.0907 51  SER B N   
5159 C CA  . SER B 33  ? 0.3568 0.3159 0.3819 0.0686  -0.0170 -0.0918 51  SER B CA  
5160 C C   . SER B 33  ? 0.3569 0.2996 0.3543 0.0777  -0.0472 -0.1074 51  SER B C   
5161 O O   . SER B 33  ? 0.3829 0.2893 0.3352 0.0857  -0.0317 -0.1258 51  SER B O   
5162 C CB  . SER B 33  ? 0.4241 0.3459 0.4061 0.0539  0.0281  -0.0686 51  SER B CB  
5163 O OG  . SER B 33  ? 0.4726 0.3703 0.4220 0.0501  0.0342  -0.0556 51  SER B OG  
5169 N N   . PRO B 34  ? 0.3255 0.2952 0.3493 0.0718  -0.0652 -0.1151 52  PRO B N   
5170 C CA  . PRO B 34  ? 0.3202 0.2990 0.3626 0.0744  -0.0730 -0.1099 52  PRO B CA  
5171 C C   . PRO B 34  ? 0.3348 0.3143 0.3815 0.0706  -0.0449 -0.1130 52  PRO B C   
5172 O O   . PRO B 34  ? 0.3444 0.3252 0.3799 0.0655  -0.0543 -0.1062 52  PRO B O   
5173 C CB  . PRO B 34  ? 0.3193 0.2877 0.3517 0.0855  -0.0905 -0.1140 52  PRO B CB  
5174 C CG  . PRO B 34  ? 0.3339 0.2910 0.3635 0.0700  -0.0892 -0.1099 52  PRO B CG  
5175 C CD  . PRO B 34  ? 0.3074 0.2964 0.3454 0.0660  -0.0866 -0.1194 52  PRO B CD  
5183 N N   . SER B 35  ? 0.3486 0.3319 0.4103 0.0469  -0.0376 -0.1142 53  SER B N   
5184 C CA  . SER B 35  ? 0.3737 0.3397 0.3932 0.0324  -0.0320 -0.1139 53  SER B CA  
5185 C C   . SER B 35  ? 0.3444 0.3285 0.3671 0.0502  -0.0289 -0.1193 53  SER B C   
5186 O O   . SER B 35  ? 0.3159 0.3366 0.3499 0.0426  -0.0053 -0.1318 53  SER B O   
5187 C CB  . SER B 35  ? 0.4856 0.3615 0.4271 -0.0078 0.0078  -0.0996 53  SER B CB  
5188 O OG  . SER B 35  ? 0.5536 0.3906 0.4629 -0.0041 0.0297  -0.0700 53  SER B OG  
5194 N N   . SER B 36  ? 0.3454 0.3108 0.3373 0.0781  -0.0610 -0.1063 54  SER B N   
5195 C CA  . SER B 36  ? 0.3654 0.3011 0.3362 0.0889  -0.0576 -0.0944 54  SER B CA  
5196 C C   . SER B 36  ? 0.3711 0.2855 0.3318 0.0952  -0.0538 -0.1041 54  SER B C   
5197 O O   . SER B 36  ? 0.3719 0.2797 0.3577 0.1113  -0.0411 -0.1187 54  SER B O   
5198 C CB  . SER B 36  ? 0.4063 0.3151 0.3529 0.0906  -0.0527 -0.0787 54  SER B CB  
5199 O OG  . SER B 36  ? 0.4188 0.3320 0.3660 0.0797  -0.0465 -0.0544 54  SER B OG  
5205 N N   . VAL B 37  ? 0.3750 0.2715 0.3112 0.0895  -0.0435 -0.1043 55  VAL B N   
5206 C CA  . VAL B 37  ? 0.3953 0.2677 0.3426 0.0826  -0.0606 -0.1182 55  VAL B CA  
5207 C C   . VAL B 37  ? 0.4040 0.2544 0.3603 0.0770  -0.1025 -0.1171 55  VAL B C   
5208 O O   . VAL B 37  ? 0.4304 0.2600 0.3853 0.0719  -0.1047 -0.1107 55  VAL B O   
5209 C CB  . VAL B 37  ? 0.3946 0.2754 0.3169 0.0909  -0.0311 -0.1104 55  VAL B CB  
5210 C CG1 . VAL B 37  ? 0.4120 0.2692 0.3187 0.0758  -0.0141 -0.1244 55  VAL B CG1 
5211 C CG2 . VAL B 37  ? 0.4193 0.2832 0.2934 0.0903  -0.0547 -0.0970 55  VAL B CG2 
5221 N N   . SER B 38  ? 0.4212 0.2490 0.3638 0.0875  -0.1093 -0.1157 56  SER B N   
5222 C CA  . SER B 38  ? 0.4376 0.2455 0.3599 0.0700  -0.1159 -0.1164 56  SER B CA  
5223 C C   . SER B 38  ? 0.4024 0.2395 0.3399 0.0509  -0.1236 -0.0993 56  SER B C   
5224 O O   . SER B 38  ? 0.3887 0.2363 0.3490 0.0434  -0.1106 -0.0970 56  SER B O   
5225 C CB  . SER B 38  ? 0.4605 0.2407 0.3785 0.0329  -0.1302 -0.1378 56  SER B CB  
5226 O OG  . SER B 38  ? 0.5157 0.2666 0.4080 0.0418  -0.1009 -0.1239 56  SER B OG  
5232 N N   . LYS B 39  ? 0.3946 0.2235 0.3290 0.0388  -0.1279 -0.0983 57  LYS B N   
5233 C CA  . LYS B 39  ? 0.3978 0.2054 0.3270 -0.0067 -0.1157 -0.1088 57  LYS B CA  
5234 C C   . LYS B 39  ? 0.3639 0.1756 0.3142 0.0108  -0.0941 -0.0826 57  LYS B C   
5235 O O   . LYS B 39  ? 0.3371 0.1708 0.3329 -0.0043 -0.0897 -0.0759 57  LYS B O   
5236 C CB  . LYS B 39  ? 0.4369 0.2429 0.3378 -0.0568 -0.0839 -0.1316 57  LYS B CB  
5237 C CG  . LYS B 39  ? 0.5132 0.2534 0.3915 -0.0700 -0.0704 -0.1375 57  LYS B CG  
5238 C CD  . LYS B 39  ? 0.5245 0.3089 0.4434 -0.0715 -0.0547 -0.1013 57  LYS B CD  
5239 C CE  . LYS B 39  ? 0.5308 0.3456 0.4793 -0.0761 -0.0640 -0.0877 57  LYS B CE  
5240 N NZ  . LYS B 39  ? 0.5511 0.3770 0.5177 -0.0629 -0.0517 -0.0636 57  LYS B NZ  
5254 N N   . PRO B 40  ? 0.3315 0.1674 0.2921 0.0302  -0.1198 -0.0527 58  PRO B N   
5255 C CA  . PRO B 40  ? 0.3279 0.1570 0.2743 0.0293  -0.1288 -0.0612 58  PRO B CA  
5256 C C   . PRO B 40  ? 0.3174 0.1678 0.2898 0.0276  -0.1257 -0.0577 58  PRO B C   
5257 O O   . PRO B 40  ? 0.2968 0.1830 0.3134 0.0230  -0.1252 -0.0608 58  PRO B O   
5258 C CB  . PRO B 40  ? 0.3293 0.1456 0.2679 0.0161  -0.1237 -0.0598 58  PRO B CB  
5259 C CG  . PRO B 40  ? 0.3053 0.1715 0.2811 0.0180  -0.1097 -0.0470 58  PRO B CG  
5260 C CD  . PRO B 40  ? 0.3233 0.1630 0.2878 0.0201  -0.0938 -0.0566 58  PRO B CD  
5268 N N   . ILE B 41  ? 0.3094 0.1459 0.2941 0.0432  -0.1171 -0.0794 59  ILE B N   
5269 C CA  . ILE B 41  ? 0.2881 0.1262 0.2955 0.0329  -0.0995 -0.0677 59  ILE B CA  
5270 C C   . ILE B 41  ? 0.2757 0.1218 0.3004 0.0176  -0.1009 -0.0550 59  ILE B C   
5271 O O   . ILE B 41  ? 0.2694 0.1279 0.3357 0.0224  -0.1001 -0.0630 59  ILE B O   
5272 C CB  . ILE B 41  ? 0.2898 0.1233 0.2894 0.0350  -0.1234 -0.0551 59  ILE B CB  
5273 C CG1 . ILE B 41  ? 0.3292 0.1169 0.2946 0.0275  -0.1029 -0.0449 59  ILE B CG1 
5274 C CG2 . ILE B 41  ? 0.2921 0.1198 0.2931 0.0322  -0.1177 -0.0518 59  ILE B CG2 
5275 C CD1 . ILE B 41  ? 0.3455 0.1127 0.3002 0.0209  -0.0998 -0.0318 59  ILE B CD1 
5287 N N   . LEU B 42  ? 0.2562 0.1235 0.2786 0.0206  -0.1088 -0.0396 60  LEU B N   
5288 C CA  . LEU B 42  ? 0.2575 0.1154 0.2709 0.0093  -0.0942 -0.0497 60  LEU B CA  
5289 C C   . LEU B 42  ? 0.2508 0.1039 0.2594 0.0036  -0.1023 -0.0386 60  LEU B C   
5290 O O   . LEU B 42  ? 0.2672 0.1279 0.2280 -0.0031 -0.0966 -0.0260 60  LEU B O   
5291 C CB  . LEU B 42  ? 0.2436 0.1361 0.2740 -0.0003 -0.0748 -0.0506 60  LEU B CB  
5292 C CG  . LEU B 42  ? 0.2373 0.1437 0.2734 0.0015  -0.0825 -0.0396 60  LEU B CG  
5293 C CD1 . LEU B 42  ? 0.2533 0.1688 0.2286 0.0123  -0.0955 -0.0580 60  LEU B CD1 
5294 C CD2 . LEU B 42  ? 0.2454 0.1448 0.2811 0.0065  -0.0741 -0.0081 60  LEU B CD2 
5306 N N   . LEU B 43  ? 0.2496 0.1036 0.2603 0.0226  -0.1006 -0.0390 61  LEU B N   
5307 C CA  . LEU B 43  ? 0.2508 0.1102 0.2667 0.0568  -0.0851 -0.0334 61  LEU B CA  
5308 C C   . LEU B 43  ? 0.2626 0.1275 0.2589 0.0377  -0.1011 -0.0500 61  LEU B C   
5309 O O   . LEU B 43  ? 0.2645 0.1487 0.2763 0.0212  -0.1151 -0.0620 61  LEU B O   
5310 C CB  . LEU B 43  ? 0.2861 0.1060 0.2819 0.0413  -0.0861 -0.0326 61  LEU B CB  
5311 C CG  . LEU B 43  ? 0.2957 0.1049 0.2760 0.0418  -0.0917 -0.0166 61  LEU B CG  
5312 C CD1 . LEU B 43  ? 0.3515 0.1103 0.2961 0.0227  -0.1034 -0.0063 61  LEU B CD1 
5313 C CD2 . LEU B 43  ? 0.3534 0.1143 0.2759 0.0195  -0.0684 -0.0405 61  LEU B CD2 
5325 N N   . VAL B 44  ? 0.2409 0.1035 0.2475 0.0236  -0.0846 -0.0327 62  VAL B N   
5326 C CA  . VAL B 44  ? 0.2433 0.1036 0.2335 0.0147  -0.0758 -0.0118 62  VAL B CA  
5327 C C   . VAL B 44  ? 0.2190 0.1081 0.2265 0.0080  -0.0698 -0.0354 62  VAL B C   
5328 O O   . VAL B 44  ? 0.2310 0.1056 0.2324 0.0163  -0.0559 -0.0188 62  VAL B O   
5329 C CB  . VAL B 44  ? 0.2583 0.1021 0.2317 0.0346  -0.0713 0.0073  62  VAL B CB  
5330 C CG1 . VAL B 44  ? 0.2596 0.1136 0.2344 -0.0026 -0.0449 -0.0243 62  VAL B CG1 
5331 C CG2 . VAL B 44  ? 0.2530 0.1367 0.2391 0.0316  -0.0869 -0.0015 62  VAL B CG2 
5341 N N   . PRO B 45  ? 0.2395 0.1198 0.2197 0.0095  -0.0780 -0.0466 63  PRO B N   
5342 C CA  . PRO B 45  ? 0.2238 0.1230 0.2366 0.0160  -0.0933 -0.0280 63  PRO B CA  
5343 C C   . PRO B 45  ? 0.2323 0.1051 0.2446 0.0100  -0.0764 -0.0189 63  PRO B C   
5344 O O   . PRO B 45  ? 0.2333 0.0944 0.2504 0.0347  -0.0438 -0.0431 63  PRO B O   
5345 C CB  . PRO B 45  ? 0.2317 0.1412 0.2415 0.0049  -0.0643 -0.0356 63  PRO B CB  
5346 C CG  . PRO B 45  ? 0.2387 0.1528 0.2338 -0.0003 -0.0705 -0.0520 63  PRO B CG  
5347 C CD  . PRO B 45  ? 0.2431 0.1426 0.2347 0.0121  -0.0713 -0.0543 63  PRO B CD  
5355 N N   . GLY B 46  ? 0.2458 0.1052 0.2346 0.0014  -0.0572 -0.0144 64  GLY B N   
5356 C CA  . GLY B 46  ? 0.2310 0.1033 0.2386 -0.0070 -0.0503 -0.0025 64  GLY B CA  
5357 C C   . GLY B 46  ? 0.2153 0.1185 0.2286 0.0048  -0.0871 0.0076  64  GLY B C   
5358 O O   . GLY B 46  ? 0.2158 0.1234 0.2333 0.0129  -0.0890 -0.0080 64  GLY B O   
5362 N N   . THR B 47  ? 0.2386 0.1097 0.2172 0.0281  -0.0795 -0.0023 65  THR B N   
5363 C CA  . THR B 47  ? 0.2354 0.1142 0.1964 0.0176  -0.0732 -0.0085 65  THR B CA  
5364 C C   . THR B 47  ? 0.2572 0.1242 0.2132 0.0181  -0.0761 -0.0014 65  THR B C   
5365 O O   . THR B 47  ? 0.2704 0.1299 0.2094 0.0035  -0.0737 0.0183  65  THR B O   
5366 C CB  . THR B 47  ? 0.2527 0.1183 0.2210 0.0348  -0.0347 -0.0016 65  THR B CB  
5367 O OG1 . THR B 47  ? 0.2355 0.1188 0.2215 0.0517  -0.0282 0.0097  65  THR B OG1 
5368 C CG2 . THR B 47  ? 0.2496 0.1299 0.2229 0.0146  -0.0416 -0.0245 65  THR B CG2 
5376 N N   . GLY B 48  ? 0.2459 0.1181 0.2277 0.0050  -0.0782 0.0025  66  GLY B N   
5377 C CA  . GLY B 48  ? 0.2646 0.1099 0.2144 0.0207  -0.1020 0.0005  66  GLY B CA  
5378 C C   . GLY B 48  ? 0.2702 0.1195 0.2355 0.0141  -0.0962 0.0064  66  GLY B C   
5379 O O   . GLY B 48  ? 0.2975 0.1311 0.2405 0.0074  -0.0964 0.0180  66  GLY B O   
5383 N N   . THR B 49  ? 0.2651 0.1106 0.2299 0.0024  -0.0998 0.0055  67  THR B N   
5384 C CA  . THR B 49  ? 0.2741 0.0973 0.2482 0.0240  -0.1057 -0.0005 67  THR B CA  
5385 C C   . THR B 49  ? 0.2657 0.0956 0.2590 0.0421  -0.0733 -0.0087 67  THR B C   
5386 O O   . THR B 49  ? 0.2477 0.1028 0.2512 0.0146  -0.0694 -0.0083 67  THR B O   
5387 C CB  . THR B 49  ? 0.2813 0.1160 0.2657 0.0145  -0.1378 -0.0153 67  THR B CB  
5388 O OG1 . THR B 49  ? 0.2859 0.1081 0.2784 0.0209  -0.1133 -0.0370 67  THR B OG1 
5389 C CG2 . THR B 49  ? 0.3306 0.1357 0.2793 -0.0072 -0.1197 0.0079  67  THR B CG2 
5397 N N   . THR B 50  ? 0.2770 0.1144 0.2749 0.0368  -0.0784 -0.0132 68  THR B N   
5398 C CA  . THR B 50  ? 0.2510 0.1217 0.2683 0.0551  -0.0798 -0.0097 68  THR B CA  
5399 C C   . THR B 50  ? 0.2368 0.1253 0.2540 0.0159  -0.0582 -0.0303 68  THR B C   
5400 O O   . THR B 50  ? 0.2441 0.1361 0.2524 0.0342  -0.0559 -0.0439 68  THR B O   
5401 C CB  . THR B 50  ? 0.2735 0.1358 0.2701 0.0173  -0.1094 -0.0039 68  THR B CB  
5402 O OG1 . THR B 50  ? 0.2920 0.1214 0.2760 0.0217  -0.1036 0.0137  68  THR B OG1 
5403 C CG2 . THR B 50  ? 0.2851 0.1465 0.2689 0.0346  -0.1000 -0.0272 68  THR B CG2 
5411 N N   . GLY B 51  ? 0.2357 0.1129 0.2532 0.0365  -0.0784 -0.0365 69  GLY B N   
5412 C CA  . GLY B 51  ? 0.2539 0.1192 0.2640 0.0328  -0.0735 -0.0399 69  GLY B CA  
5413 C C   . GLY B 51  ? 0.2562 0.1399 0.2535 0.0349  -0.0770 -0.0210 69  GLY B C   
5414 O O   . GLY B 51  ? 0.2556 0.1626 0.2440 0.0220  -0.0621 -0.0386 69  GLY B O   
5418 N N   . PRO B 52  ? 0.2870 0.1409 0.2672 0.0444  -0.0870 -0.0223 70  PRO B N   
5419 C CA  . PRO B 52  ? 0.2768 0.1401 0.2835 0.0463  -0.1100 -0.0160 70  PRO B CA  
5420 C C   . PRO B 52  ? 0.3010 0.1263 0.2763 0.0395  -0.1284 -0.0332 70  PRO B C   
5421 O O   . PRO B 52  ? 0.3230 0.1340 0.2988 0.0285  -0.1317 -0.0374 70  PRO B O   
5422 C CB  . PRO B 52  ? 0.2823 0.1503 0.2961 0.0480  -0.0883 -0.0246 70  PRO B CB  
5423 C CG  . PRO B 52  ? 0.2877 0.1345 0.2912 0.0608  -0.0613 -0.0414 70  PRO B CG  
5424 C CD  . PRO B 52  ? 0.2777 0.1364 0.2691 0.0828  -0.0680 -0.0543 70  PRO B CD  
5432 N N   . GLN B 53  ? 0.3025 0.1203 0.2655 0.0526  -0.1257 -0.0368 71  GLN B N   
5433 C CA  . GLN B 53  ? 0.3180 0.1143 0.2667 0.0323  -0.1237 -0.0349 71  GLN B CA  
5434 C C   . GLN B 53  ? 0.2976 0.1170 0.2688 0.0202  -0.1297 -0.0156 71  GLN B C   
5435 O O   . GLN B 53  ? 0.2791 0.1392 0.2907 0.0179  -0.1159 0.0156  71  GLN B O   
5436 C CB  . GLN B 53  ? 0.3079 0.1236 0.2635 0.0359  -0.1302 -0.0289 71  GLN B CB  
5437 C CG  . GLN B 53  ? 0.3051 0.1318 0.2736 0.0218  -0.1265 -0.0203 71  GLN B CG  
5438 C CD  . GLN B 53  ? 0.3085 0.1289 0.2813 0.0267  -0.1384 -0.0113 71  GLN B CD  
5439 O OE1 . GLN B 53  ? 0.3565 0.1192 0.2910 0.0256  -0.1293 0.0006  71  GLN B OE1 
5440 N NE2 . GLN B 53  ? 0.3245 0.1655 0.2989 0.0319  -0.1339 0.0070  71  GLN B NE2 
5449 N N   . SER B 54  ? 0.2817 0.1161 0.2682 0.0320  -0.1254 -0.0144 72  SER B N   
5450 C CA  . SER B 54  ? 0.2796 0.1085 0.2635 0.0149  -0.1026 -0.0029 72  SER B CA  
5451 C C   . SER B 54  ? 0.2833 0.1185 0.2554 0.0162  -0.1025 -0.0066 72  SER B C   
5452 O O   . SER B 54  ? 0.2793 0.1321 0.2740 0.0027  -0.0706 -0.0023 72  SER B O   
5453 C CB  . SER B 54  ? 0.2582 0.0980 0.2635 0.0339  -0.0898 0.0018  72  SER B CB  
5454 O OG  . SER B 54  ? 0.2732 0.0856 0.2540 0.0194  -0.0685 -0.0074 72  SER B OG  
5460 N N   . PHE B 55  ? 0.3033 0.1285 0.2716 0.0253  -0.1202 -0.0029 73  PHE B N   
5461 C CA  . PHE B 55  ? 0.2885 0.1106 0.2696 0.0149  -0.1526 -0.0065 73  PHE B CA  
5462 C C   . PHE B 55  ? 0.3165 0.1126 0.3073 0.0065  -0.1340 -0.0133 73  PHE B C   
5463 O O   . PHE B 55  ? 0.3361 0.1129 0.3136 0.0001  -0.1235 -0.0093 73  PHE B O   
5464 C CB  . PHE B 55  ? 0.2986 0.0982 0.2512 0.0164  -0.1024 -0.0200 73  PHE B CB  
5465 C CG  . PHE B 55  ? 0.2798 0.0906 0.2442 0.0208  -0.0811 -0.0210 73  PHE B CG  
5466 C CD1 . PHE B 55  ? 0.2856 0.0895 0.2495 0.0177  -0.0671 -0.0258 73  PHE B CD1 
5467 C CD2 . PHE B 55  ? 0.2939 0.0931 0.2460 0.0275  -0.0790 -0.0162 73  PHE B CD2 
5468 C CE1 . PHE B 55  ? 0.2786 0.0892 0.2527 0.0231  -0.0700 -0.0217 73  PHE B CE1 
5469 C CE2 . PHE B 55  ? 0.2552 0.0927 0.2383 0.0172  -0.0991 -0.0279 73  PHE B CE2 
5470 C CZ  . PHE B 55  ? 0.2749 0.0929 0.2409 0.0214  -0.0906 -0.0247 73  PHE B CZ  
5480 N N   . ASP B 56  ? 0.3101 0.1248 0.3240 0.0269  -0.1238 -0.0265 74  ASP B N   
5481 C CA  . ASP B 56  ? 0.3365 0.1377 0.3342 0.0481  -0.1110 -0.0156 74  ASP B CA  
5482 C C   . ASP B 56  ? 0.3755 0.1263 0.3244 0.0529  -0.1002 -0.0110 74  ASP B C   
5483 O O   . ASP B 56  ? 0.3929 0.1254 0.3482 0.0439  -0.0950 -0.0127 74  ASP B O   
5484 C CB  . ASP B 56  ? 0.3137 0.1542 0.3220 0.0704  -0.1322 -0.0052 74  ASP B CB  
5485 C CG  . ASP B 56  ? 0.3216 0.1596 0.3438 0.0653  -0.1186 -0.0077 74  ASP B CG  
5486 O OD1 . ASP B 56  ? 0.3285 0.1862 0.3601 0.0451  -0.1102 -0.0075 74  ASP B OD1 
5487 O OD2 . ASP B 56  ? 0.3719 0.1701 0.3588 0.0762  -0.0953 -0.0141 74  ASP B OD2 
5492 N N   . SER B 57  ? 0.3608 0.1247 0.3054 0.0424  -0.1039 0.0145  75  SER B N   
5493 C CA  . SER B 57  ? 0.3825 0.1274 0.3006 0.0364  -0.1073 0.0196  75  SER B CA  
5494 C C   . SER B 57  ? 0.3987 0.1221 0.2900 0.0044  -0.1128 0.0225  75  SER B C   
5495 O O   . SER B 57  ? 0.4254 0.1440 0.2950 -0.0184 -0.1040 0.0355  75  SER B O   
5496 C CB  . SER B 57  ? 0.3927 0.1335 0.3056 0.0427  -0.0942 0.0320  75  SER B CB  
5497 O OG  . SER B 57  ? 0.4059 0.1409 0.3103 0.0164  -0.1039 0.0135  75  SER B OG  
5503 N N   . ASN B 58  ? 0.3627 0.1122 0.2698 0.0066  -0.1232 -0.0007 76  ASN B N   
5504 C CA  . ASN B 58  ? 0.3692 0.1145 0.2746 0.0157  -0.1057 -0.0118 76  ASN B CA  
5505 C C   . ASN B 58  ? 0.3409 0.1133 0.2794 0.0232  -0.1221 -0.0231 76  ASN B C   
5506 O O   . ASN B 58  ? 0.3508 0.1240 0.3107 0.0144  -0.1440 -0.0277 76  ASN B O   
5507 C CB  . ASN B 58  ? 0.3533 0.1021 0.2490 0.0012  -0.0929 -0.0054 76  ASN B CB  
5508 C CG  . ASN B 58  ? 0.3309 0.1012 0.2277 -0.0060 -0.1097 -0.0031 76  ASN B CG  
5509 O OD1 . ASN B 58  ? 0.3259 0.1055 0.2466 -0.0022 -0.0859 0.0184  76  ASN B OD1 
5510 N ND2 . ASN B 58  ? 0.3644 0.1103 0.2412 -0.0132 -0.0815 -0.0122 76  ASN B ND2 
5517 N N   . TRP B 59  ? 0.3235 0.1136 0.2750 0.0046  -0.1195 -0.0310 77  TRP B N   
5518 C CA  . TRP B 59  ? 0.3262 0.1195 0.2895 0.0154  -0.1063 -0.0066 77  TRP B CA  
5519 C C   . TRP B 59  ? 0.3108 0.1363 0.2976 0.0356  -0.1389 -0.0061 77  TRP B C   
5520 O O   . TRP B 59  ? 0.3379 0.1345 0.3109 0.0373  -0.1227 -0.0141 77  TRP B O   
5521 C CB  . TRP B 59  ? 0.3073 0.0953 0.2718 0.0183  -0.0811 -0.0115 77  TRP B CB  
5522 C CG  . TRP B 59  ? 0.3195 0.0931 0.2724 -0.0130 -0.0690 0.0003  77  TRP B CG  
5523 C CD1 . TRP B 59  ? 0.3111 0.0892 0.2664 -0.0069 -0.0635 0.0016  77  TRP B CD1 
5524 C CD2 . TRP B 59  ? 0.3112 0.1105 0.2526 -0.0190 -0.0777 -0.0068 77  TRP B CD2 
5525 N NE1 . TRP B 59  ? 0.3321 0.0916 0.2698 -0.0233 -0.0439 0.0082  77  TRP B NE1 
5526 C CE2 . TRP B 59  ? 0.3185 0.1068 0.2629 -0.0277 -0.0726 -0.0037 77  TRP B CE2 
5527 C CE3 . TRP B 59  ? 0.3173 0.1319 0.2600 -0.0002 -0.0781 0.0084  77  TRP B CE3 
5528 C CZ2 . TRP B 59  ? 0.3269 0.1260 0.2723 -0.0297 -0.0743 0.0037  77  TRP B CZ2 
5529 C CZ3 . TRP B 59  ? 0.3278 0.1169 0.2736 -0.0150 -0.0630 -0.0021 77  TRP B CZ3 
5530 C CH2 . TRP B 59  ? 0.3394 0.1253 0.2837 -0.0124 -0.0648 0.0111  77  TRP B CH2 
5541 N N   . ILE B 60  ? 0.3302 0.1327 0.3083 0.0126  -0.1161 -0.0275 78  ILE B N   
5542 C CA  . ILE B 60  ? 0.3293 0.1340 0.3035 0.0274  -0.1091 -0.0406 78  ILE B CA  
5543 C C   . ILE B 60  ? 0.3538 0.1385 0.2968 0.0375  -0.1073 -0.0407 78  ILE B C   
5544 O O   . ILE B 60  ? 0.3586 0.1382 0.2816 0.0461  -0.1083 -0.0646 78  ILE B O   
5545 C CB  . ILE B 60  ? 0.3162 0.1320 0.3257 0.0356  -0.0780 -0.0441 78  ILE B CB  
5546 C CG1 . ILE B 60  ? 0.2950 0.1484 0.3402 0.0279  -0.0929 -0.0479 78  ILE B CG1 
5547 C CG2 . ILE B 60  ? 0.3285 0.1657 0.3124 0.0342  -0.0494 -0.0376 78  ILE B CG2 
5548 C CD1 . ILE B 60  ? 0.2901 0.1488 0.3541 0.0153  -0.1085 -0.0536 78  ILE B CD1 
5560 N N   . PRO B 61  ? 0.3581 0.1270 0.2861 0.0331  -0.1225 -0.0460 79  PRO B N   
5561 C CA  . PRO B 61  ? 0.4172 0.1368 0.2923 0.0059  -0.1303 -0.0379 79  PRO B CA  
5562 C C   . PRO B 61  ? 0.4366 0.1413 0.3129 0.0238  -0.1300 -0.0313 79  PRO B C   
5563 O O   . PRO B 61  ? 0.4612 0.1536 0.3312 0.0026  -0.1209 -0.0556 79  PRO B O   
5564 C CB  . PRO B 61  ? 0.4266 0.1292 0.2962 0.0048  -0.1210 -0.0245 79  PRO B CB  
5565 C CG  . PRO B 61  ? 0.4157 0.1259 0.2902 0.0131  -0.1128 -0.0286 79  PRO B CG  
5566 C CD  . PRO B 61  ? 0.3949 0.1227 0.2916 0.0214  -0.1152 -0.0234 79  PRO B CD  
5574 N N   . LEU B 62  ? 0.4250 0.1376 0.3173 0.0147  -0.1412 -0.0258 80  LEU B N   
5575 C CA  . LEU B 62  ? 0.4338 0.1381 0.3178 0.0105  -0.1423 -0.0284 80  LEU B CA  
5576 C C   . LEU B 62  ? 0.4379 0.1503 0.3370 0.0095  -0.1583 -0.0392 80  LEU B C   
5577 O O   . LEU B 62  ? 0.4406 0.1632 0.3355 -0.0141 -0.1607 -0.0430 80  LEU B O   
5578 C CB  . LEU B 62  ? 0.4254 0.1385 0.3200 0.0107  -0.1299 -0.0290 80  LEU B CB  
5579 C CG  . LEU B 62  ? 0.4126 0.1365 0.3205 -0.0206 -0.1242 -0.0292 80  LEU B CG  
5580 C CD1 . LEU B 62  ? 0.4134 0.1601 0.3215 -0.0332 -0.1256 -0.0250 80  LEU B CD1 
5581 C CD2 . LEU B 62  ? 0.4260 0.1491 0.3335 -0.0237 -0.1286 -0.0416 80  LEU B CD2 
5593 N N   . SER B 63  ? 0.4049 0.1547 0.3400 0.0009  -0.1748 -0.0389 81  SER B N   
5594 C CA  . SER B 63  ? 0.4035 0.1590 0.3344 0.0107  -0.1797 -0.0353 81  SER B CA  
5595 C C   . SER B 63  ? 0.4261 0.1542 0.3469 0.0298  -0.1650 -0.0343 81  SER B C   
5596 O O   . SER B 63  ? 0.4201 0.1451 0.3437 0.0057  -0.1522 -0.0310 81  SER B O   
5597 C CB  . SER B 63  ? 0.4217 0.1687 0.3400 0.0172  -0.1726 -0.0074 81  SER B CB  
5598 O OG  . SER B 63  ? 0.4447 0.1685 0.3547 0.0025  -0.1625 -0.0318 81  SER B OG  
5604 N N   . THR B 64  ? 0.4578 0.1667 0.3633 0.0461  -0.1586 -0.0584 82  THR B N   
5605 C CA  . THR B 64  ? 0.4923 0.1783 0.3838 0.0434  -0.1365 -0.0607 82  THR B CA  
5606 C C   . THR B 64  ? 0.5196 0.1715 0.3902 0.0311  -0.1325 -0.0665 82  THR B C   
5607 O O   . THR B 64  ? 0.5337 0.1774 0.3993 0.0468  -0.1160 -0.0757 82  THR B O   
5608 C CB  . THR B 64  ? 0.4581 0.1762 0.3870 0.0580  -0.1325 -0.0574 82  THR B CB  
5609 O OG1 . THR B 64  ? 0.4517 0.1752 0.3770 0.0372  -0.1323 -0.0323 82  THR B OG1 
5610 C CG2 . THR B 64  ? 0.4563 0.1945 0.4014 0.0489  -0.1143 -0.0714 82  THR B CG2 
5618 N N   . GLN B 65  ? 0.5327 0.1759 0.3909 0.0133  -0.1510 -0.0598 83  GLN B N   
5619 C CA  . GLN B 65  ? 0.5481 0.1819 0.3866 -0.0125 -0.1588 -0.0514 83  GLN B CA  
5620 C C   . GLN B 65  ? 0.5173 0.1838 0.3827 -0.0392 -0.1559 -0.0459 83  GLN B C   
5621 O O   . GLN B 65  ? 0.5337 0.1780 0.4014 -0.0368 -0.1421 -0.0454 83  GLN B O   
5622 C CB  . GLN B 65  ? 0.6310 0.1937 0.4122 -0.0074 -0.1539 -0.0438 83  GLN B CB  
5623 C CG  . GLN B 65  ? 0.7041 0.2501 0.4189 -0.0201 -0.1449 -0.0211 83  GLN B CG  
5624 C CD  . GLN B 65  ? 0.7559 0.2966 0.4211 -0.0041 -0.1320 0.0148  83  GLN B CD  
5625 O OE1 . GLN B 65  ? 0.8070 0.3066 0.4359 0.0116  -0.0916 0.0352  83  GLN B OE1 
5626 N NE2 . GLN B 65  ? 0.7454 0.3178 0.4069 -0.0106 -0.1609 0.0245  83  GLN B NE2 
5635 N N   . LEU B 66  ? 0.4990 0.1729 0.3801 -0.0230 -0.1834 -0.0281 84  LEU B N   
5636 C CA  . LEU B 66  ? 0.5162 0.1876 0.3743 -0.0421 -0.1750 -0.0352 84  LEU B CA  
5637 C C   . LEU B 66  ? 0.5264 0.2041 0.3591 -0.0477 -0.1846 -0.0374 84  LEU B C   
5638 O O   . LEU B 66  ? 0.5570 0.2389 0.3654 -0.0619 -0.2062 -0.0279 84  LEU B O   
5639 C CB  . LEU B 66  ? 0.5074 0.1703 0.3879 -0.0274 -0.1764 -0.0230 84  LEU B CB  
5640 C CG  . LEU B 66  ? 0.5145 0.1674 0.3916 -0.0237 -0.1671 -0.0242 84  LEU B CG  
5641 C CD1 . LEU B 66  ? 0.5321 0.1688 0.3959 -0.0233 -0.1484 -0.0344 84  LEU B CD1 
5642 C CD2 . LEU B 66  ? 0.5195 0.1742 0.3945 -0.0285 -0.1733 -0.0280 84  LEU B CD2 
5654 N N   . GLY B 67  ? 0.5176 0.1896 0.3430 -0.0252 -0.1616 -0.0524 85  GLY B N   
5655 C CA  . GLY B 67  ? 0.5420 0.1835 0.3389 -0.0285 -0.1148 -0.0637 85  GLY B CA  
5656 C C   . GLY B 67  ? 0.5582 0.1862 0.3178 -0.0379 -0.1178 -0.0529 85  GLY B C   
5657 O O   . GLY B 67  ? 0.6358 0.2018 0.3076 -0.0611 -0.0952 -0.0342 85  GLY B O   
5661 N N   . TYR B 68  ? 0.4617 0.1737 0.3003 -0.0078 -0.1317 -0.0635 86  TYR B N   
5662 C CA  . TYR B 68  ? 0.4315 0.1554 0.3000 0.0041  -0.1235 -0.0603 86  TYR B CA  
5663 C C   . TYR B 68  ? 0.4218 0.1674 0.3185 0.0333  -0.1284 -0.0504 86  TYR B C   
5664 O O   . TYR B 68  ? 0.4353 0.1816 0.3321 0.0241  -0.1311 -0.0392 86  TYR B O   
5665 C CB  . TYR B 68  ? 0.3825 0.1590 0.2976 0.0015  -0.0857 -0.0878 86  TYR B CB  
5666 C CG  . TYR B 68  ? 0.3648 0.1527 0.3003 -0.0014 -0.0980 -0.0792 86  TYR B CG  
5667 C CD1 . TYR B 68  ? 0.3760 0.1330 0.3322 0.0150  -0.0842 -0.0662 86  TYR B CD1 
5668 C CD2 . TYR B 68  ? 0.3953 0.1675 0.3324 0.0038  -0.0864 -0.0726 86  TYR B CD2 
5669 C CE1 . TYR B 68  ? 0.3739 0.1539 0.3408 0.0097  -0.0864 -0.0631 86  TYR B CE1 
5670 C CE2 . TYR B 68  ? 0.3644 0.1707 0.3438 -0.0087 -0.0925 -0.0599 86  TYR B CE2 
5671 C CZ  . TYR B 68  ? 0.3462 0.1763 0.3450 0.0078  -0.1007 -0.0434 86  TYR B CZ  
5672 O OH  . TYR B 68  ? 0.3758 0.2170 0.3610 -0.0053 -0.0779 -0.0180 86  TYR B OH  
5682 N N   . THR B 69  ? 0.3966 0.1642 0.3081 0.0188  -0.1483 -0.0677 87  THR B N   
5683 C CA  . THR B 69  ? 0.3989 0.1661 0.3120 0.0396  -0.1304 -0.0751 87  THR B CA  
5684 C C   . THR B 69  ? 0.3465 0.1365 0.3098 0.0486  -0.1316 -0.0562 87  THR B C   
5685 O O   . THR B 69  ? 0.3398 0.1467 0.3208 0.0395  -0.1222 -0.0453 87  THR B O   
5686 C CB  . THR B 69  ? 0.4125 0.1690 0.3002 0.0536  -0.1235 -0.0827 87  THR B CB  
5687 O OG1 . THR B 69  ? 0.4396 0.1884 0.3025 0.0405  -0.1011 -0.1005 87  THR B OG1 
5688 C CG2 . THR B 69  ? 0.4083 0.1717 0.2960 0.0743  -0.0951 -0.0869 87  THR B CG2 
5696 N N   . PRO B 70  ? 0.3375 0.1427 0.2980 0.0384  -0.1186 -0.0719 88  PRO B N   
5697 C CA  . PRO B 70  ? 0.3394 0.1467 0.2838 0.0233  -0.1037 -0.0781 88  PRO B CA  
5698 C C   . PRO B 70  ? 0.3034 0.1372 0.2930 0.0516  -0.1077 -0.0726 88  PRO B C   
5699 O O   . PRO B 70  ? 0.3129 0.1484 0.2995 0.0763  -0.0986 -0.0726 88  PRO B O   
5700 C CB  . PRO B 70  ? 0.3730 0.1421 0.2927 0.0207  -0.1209 -0.0621 88  PRO B CB  
5701 C CG  . PRO B 70  ? 0.3921 0.1314 0.3054 0.0279  -0.0981 -0.0538 88  PRO B CG  
5702 C CD  . PRO B 70  ? 0.3479 0.1319 0.2945 0.0367  -0.1167 -0.0577 88  PRO B CD  
5710 N N   . CYS B 71  ? 0.2907 0.1402 0.2754 0.0556  -0.1162 -0.0714 89  CYS B N   
5711 C CA  . CYS B 71  ? 0.2752 0.1704 0.2926 0.0394  -0.0883 -0.0579 89  CYS B CA  
5712 C C   . CYS B 71  ? 0.2505 0.1567 0.2825 0.0423  -0.0896 -0.0701 89  CYS B C   
5713 O O   . CYS B 71  ? 0.2404 0.1801 0.2872 0.0433  -0.0858 -0.0688 89  CYS B O   
5714 C CB  . CYS B 71  ? 0.2690 0.1868 0.3029 0.0613  -0.0681 -0.0630 89  CYS B CB  
5715 S SG  . CYS B 71  ? 0.2802 0.1846 0.3099 0.0422  -0.0873 -0.0992 89  CYS B SG  
5720 N N   . TRP B 72  ? 0.2755 0.1499 0.2687 0.0247  -0.0812 -0.0761 90  TRP B N   
5721 C CA  . TRP B 72  ? 0.2817 0.1297 0.2475 0.0272  -0.0902 -0.0691 90  TRP B CA  
5722 C C   . TRP B 72  ? 0.2685 0.1372 0.2302 0.0132  -0.0956 -0.0622 90  TRP B C   
5723 O O   . TRP B 72  ? 0.2831 0.1372 0.2154 0.0222  -0.0559 -0.0420 90  TRP B O   
5724 C CB  . TRP B 72  ? 0.2661 0.1295 0.2674 0.0355  -0.1076 -0.0546 90  TRP B CB  
5725 C CG  . TRP B 72  ? 0.2775 0.1451 0.2908 0.0532  -0.1103 -0.0407 90  TRP B CG  
5726 C CD1 . TRP B 72  ? 0.2550 0.1410 0.3049 0.0527  -0.1164 -0.0551 90  TRP B CD1 
5727 C CD2 . TRP B 72  ? 0.2966 0.1435 0.3229 0.0513  -0.1151 -0.0358 90  TRP B CD2 
5728 N NE1 . TRP B 72  ? 0.2836 0.1573 0.3364 0.0573  -0.0974 -0.0476 90  TRP B NE1 
5729 C CE2 . TRP B 72  ? 0.2906 0.1470 0.3279 0.0638  -0.1259 -0.0435 90  TRP B CE2 
5730 C CE3 . TRP B 72  ? 0.3236 0.1420 0.3198 0.0664  -0.1210 -0.0332 90  TRP B CE3 
5731 C CZ2 . TRP B 72  ? 0.3363 0.1417 0.3360 0.0672  -0.1184 -0.0259 90  TRP B CZ2 
5732 C CZ3 . TRP B 72  ? 0.3398 0.1363 0.3279 0.0538  -0.1102 -0.0207 90  TRP B CZ3 
5733 C CH2 . TRP B 72  ? 0.3389 0.1451 0.3295 0.0638  -0.1218 -0.0269 90  TRP B CH2 
5744 N N   . ILE B 73  ? 0.2443 0.1324 0.2409 0.0116  -0.0720 -0.0608 91  ILE B N   
5745 C CA  . ILE B 73  ? 0.2592 0.1252 0.2370 0.0100  -0.0561 -0.0384 91  ILE B CA  
5746 C C   . ILE B 73  ? 0.2563 0.1159 0.2254 0.0197  -0.0584 -0.0188 91  ILE B C   
5747 O O   . ILE B 73  ? 0.2389 0.1229 0.2452 0.0136  -0.0790 -0.0234 91  ILE B O   
5748 C CB  . ILE B 73  ? 0.2301 0.1303 0.2421 0.0161  -0.0536 -0.0262 91  ILE B CB  
5749 C CG1 . ILE B 73  ? 0.2605 0.1197 0.2393 0.0010  -0.0479 -0.0080 91  ILE B CG1 
5750 C CG2 . ILE B 73  ? 0.2413 0.1663 0.2441 -0.0030 -0.0443 -0.0517 91  ILE B CG2 
5751 C CD1 . ILE B 73  ? 0.2491 0.1102 0.2391 -0.0043 -0.0642 -0.0112 91  ILE B CD1 
5763 N N   . SER B 74  ? 0.2672 0.1293 0.2165 0.0245  -0.0589 -0.0238 92  SER B N   
5764 C CA  . SER B 74  ? 0.2439 0.1291 0.2333 0.0356  -0.0846 -0.0316 92  SER B CA  
5765 C C   . SER B 74  ? 0.1993 0.1293 0.2302 0.0196  -0.0943 -0.0229 92  SER B C   
5766 O O   . SER B 74  ? 0.2158 0.1591 0.2416 0.0173  -0.0562 -0.0404 92  SER B O   
5767 C CB  . SER B 74  ? 0.2424 0.1255 0.2494 0.0459  -0.0886 -0.0233 92  SER B CB  
5768 O OG  . SER B 74  ? 0.2637 0.1206 0.2826 0.0450  -0.1010 -0.0379 92  SER B OG  
5774 N N   . PRO B 75  ? 0.1930 0.1236 0.2385 0.0238  -0.0764 -0.0385 93  PRO B N   
5775 C CA  . PRO B 75  ? 0.2310 0.1117 0.2201 0.0150  -0.0669 -0.0366 93  PRO B CA  
5776 C C   . PRO B 75  ? 0.2338 0.1243 0.2174 0.0170  -0.0696 -0.0310 93  PRO B C   
5777 O O   . PRO B 75  ? 0.2619 0.1531 0.2179 0.0014  -0.0660 -0.0307 93  PRO B O   
5778 C CB  . PRO B 75  ? 0.2479 0.1299 0.2122 0.0327  -0.0648 -0.0331 93  PRO B CB  
5779 C CG  . PRO B 75  ? 0.2158 0.1133 0.2341 0.0157  -0.0467 -0.0212 93  PRO B CG  
5780 C CD  . PRO B 75  ? 0.2173 0.1128 0.2471 0.0323  -0.0692 -0.0218 93  PRO B CD  
5788 N N   . PRO B 76  ? 0.2212 0.1466 0.2327 0.0222  -0.0555 -0.0389 94  PRO B N   
5789 C CA  . PRO B 76  ? 0.2082 0.1561 0.2422 0.0050  -0.0757 -0.0270 94  PRO B CA  
5790 C C   . PRO B 76  ? 0.1944 0.1434 0.2416 -0.0012 -0.0578 -0.0319 94  PRO B C   
5791 O O   . PRO B 76  ? 0.2012 0.1620 0.2291 -0.0136 -0.0478 -0.0100 94  PRO B O   
5792 C CB  . PRO B 76  ? 0.2180 0.1824 0.2450 0.0185  -0.0787 -0.0323 94  PRO B CB  
5793 C CG  . PRO B 76  ? 0.2222 0.1859 0.2547 0.0095  -0.0507 -0.0280 94  PRO B CG  
5794 C CD  . PRO B 76  ? 0.2295 0.1603 0.2342 -0.0002 -0.0592 -0.0341 94  PRO B CD  
5802 N N   . PRO B 77  ? 0.2123 0.1045 0.2416 0.0186  -0.0617 -0.0294 95  PRO B N   
5803 C CA  . PRO B 77  ? 0.2161 0.1093 0.2363 0.0088  -0.0959 -0.0349 95  PRO B CA  
5804 C C   . PRO B 77  ? 0.2188 0.1108 0.2502 0.0273  -0.0931 -0.0340 95  PRO B C   
5805 O O   . PRO B 77  ? 0.2262 0.1093 0.2622 0.0304  -0.0683 -0.0340 95  PRO B O   
5806 C CB  . PRO B 77  ? 0.2293 0.1301 0.2543 0.0170  -0.0806 -0.0283 95  PRO B CB  
5807 C CG  . PRO B 77  ? 0.2371 0.1149 0.2526 0.0107  -0.1042 -0.0205 95  PRO B CG  
5808 C CD  . PRO B 77  ? 0.2430 0.1102 0.2423 0.0108  -0.0744 -0.0395 95  PRO B CD  
5816 N N   . PHE B 78  ? 0.2257 0.1097 0.2586 0.0371  -0.0796 -0.0351 96  PHE B N   
5817 C CA  . PHE B 78  ? 0.2384 0.1072 0.2575 0.0243  -0.0839 -0.0257 96  PHE B CA  
5818 C C   . PHE B 78  ? 0.2386 0.1019 0.2340 0.0334  -0.0819 -0.0143 96  PHE B C   
5819 O O   . PHE B 78  ? 0.2534 0.1124 0.2163 0.0121  -0.0674 -0.0104 96  PHE B O   
5820 C CB  . PHE B 78  ? 0.2408 0.1395 0.2706 0.0256  -0.1097 -0.0222 96  PHE B CB  
5821 C CG  . PHE B 78  ? 0.2788 0.1886 0.3063 0.0493  -0.1365 -0.0415 96  PHE B CG  
5822 C CD1 . PHE B 78  ? 0.2369 0.2191 0.3413 0.0498  -0.1425 -0.0399 96  PHE B CD1 
5823 C CD2 . PHE B 78  ? 0.3282 0.2138 0.3333 0.0927  -0.1334 -0.0546 96  PHE B CD2 
5824 C CE1 . PHE B 78  ? 0.2860 0.2452 0.3666 0.0668  -0.1301 -0.0574 96  PHE B CE1 
5825 C CE2 . PHE B 78  ? 0.3516 0.2368 0.3678 0.1060  -0.1131 -0.0720 96  PHE B CE2 
5826 C CZ  . PHE B 78  ? 0.3167 0.2590 0.3771 0.0948  -0.1234 -0.0497 96  PHE B CZ  
5836 N N   . MET B 79  ? 0.1961 0.1006 0.2241 0.0359  -0.0750 -0.0145 97  MET B N   
5837 C CA  . MET B 79  ? 0.2127 0.0973 0.2289 0.0145  -0.0729 -0.0045 97  MET B CA  
5838 C C   . MET B 79  ? 0.1958 0.0979 0.2386 0.0200  -0.0746 -0.0104 97  MET B C   
5839 O O   . MET B 79  ? 0.1883 0.0998 0.2616 0.0138  -0.0670 -0.0286 97  MET B O   
5840 C CB  . MET B 79  ? 0.2241 0.1064 0.2200 -0.0070 -0.0629 -0.0127 97  MET B CB  
5841 C CG  . MET B 79  ? 0.2470 0.1188 0.2190 -0.0039 -0.0663 -0.0147 97  MET B CG  
5842 S SD  . MET B 79  ? 0.2448 0.1315 0.2132 0.0054  -0.0828 -0.0125 97  MET B SD  
5843 C CE  . MET B 79  ? 0.2756 0.1194 0.1979 0.0091  -0.0711 -0.0074 97  MET B CE  
5853 N N   . LEU B 80  ? 0.2171 0.0832 0.2149 0.0185  -0.0631 -0.0094 98  LEU B N   
5854 C CA  . LEU B 80  ? 0.2266 0.0935 0.2024 0.0031  -0.0485 -0.0027 98  LEU B CA  
5855 C C   . LEU B 80  ? 0.2322 0.1000 0.2082 -0.0122 -0.0640 -0.0031 98  LEU B C   
5856 O O   . LEU B 80  ? 0.2221 0.1161 0.2240 -0.0100 -0.0683 0.0042  98  LEU B O   
5857 C CB  . LEU B 80  ? 0.2224 0.1000 0.2097 0.0161  -0.0706 -0.0117 98  LEU B CB  
5858 C CG  . LEU B 80  ? 0.2526 0.1094 0.2239 0.0159  -0.0958 -0.0008 98  LEU B CG  
5859 C CD1 . LEU B 80  ? 0.2929 0.1111 0.2159 0.0181  -0.1194 0.0036  98  LEU B CD1 
5860 C CD2 . LEU B 80  ? 0.3110 0.1141 0.2516 -0.0122 -0.0394 0.0158  98  LEU B CD2 
5872 N N   . ASN B 81  ? 0.2185 0.1013 0.2069 0.0006  -0.0521 0.0216  99  ASN B N   
5873 C CA  . ASN B 81  ? 0.2188 0.1010 0.2194 0.0046  -0.0445 0.0104  99  ASN B CA  
5874 C C   . ASN B 81  ? 0.2005 0.1057 0.2135 0.0033  -0.0535 0.0058  99  ASN B C   
5875 O O   . ASN B 81  ? 0.2031 0.1115 0.2218 -0.0001 -0.0616 -0.0155 99  ASN B O   
5876 C CB  . ASN B 81  ? 0.2416 0.1356 0.2603 -0.0013 -0.0564 0.0334  99  ASN B CB  
5877 C CG  . ASN B 81  ? 0.2567 0.1873 0.3041 -0.0032 -0.0821 0.0237  99  ASN B CG  
5878 O OD1 . ASN B 81  ? 0.2798 0.2178 0.3425 -0.0549 -0.0570 0.0030  99  ASN B OD1 
5879 N ND2 . ASN B 81  ? 0.2831 0.2074 0.3457 0.0067  -0.1071 0.0349  99  ASN B ND2 
5886 N N   . ASP B 82  ? 0.2366 0.0962 0.2046 -0.0015 -0.0651 0.0015  100 ASP B N   
5887 C CA  . ASP B 82  ? 0.2164 0.1106 0.2007 0.0203  -0.0555 0.0004  100 ASP B CA  
5888 C C   . ASP B 82  ? 0.1915 0.0991 0.1950 0.0285  -0.0566 -0.0010 100 ASP B C   
5889 O O   . ASP B 82  ? 0.1927 0.0989 0.2198 0.0159  -0.0510 -0.0280 100 ASP B O   
5890 C CB  . ASP B 82  ? 0.1896 0.0771 0.2163 0.0131  -0.0689 0.0047  100 ASP B CB  
5891 C CG  . ASP B 82  ? 0.1913 0.1081 0.2472 0.0242  -0.0392 0.0102  100 ASP B CG  
5892 O OD1 . ASP B 82  ? 0.1869 0.1156 0.2333 0.0130  -0.0389 -0.0050 100 ASP B OD1 
5893 O OD2 . ASP B 82  ? 0.1879 0.1546 0.2920 0.0256  -0.0234 0.0341  100 ASP B OD2 
5898 N N   . THR B 83  ? 0.1926 0.1005 0.1915 0.0270  -0.0552 0.0040  101 THR B N   
5899 C CA  . THR B 83  ? 0.2050 0.1113 0.2015 0.0121  -0.0462 -0.0075 101 THR B CA  
5900 C C   . THR B 83  ? 0.1879 0.0860 0.1910 0.0136  -0.0442 -0.0037 101 THR B C   
5901 O O   . THR B 83  ? 0.1708 0.1212 0.1915 0.0190  -0.0401 -0.0066 101 THR B O   
5902 C CB  . THR B 83  ? 0.2269 0.1250 0.2145 -0.0136 -0.0361 -0.0135 101 THR B CB  
5903 O OG1 . THR B 83  ? 0.2179 0.1158 0.2263 0.0020  -0.0397 -0.0014 101 THR B OG1 
5904 C CG2 . THR B 83  ? 0.2429 0.1227 0.2479 -0.0047 -0.0235 -0.0165 101 THR B CG2 
5912 N N   . GLN B 84  ? 0.1851 0.0897 0.1789 0.0238  -0.0531 0.0050  102 GLN B N   
5913 C CA  . GLN B 84  ? 0.1887 0.1067 0.1935 -0.0058 -0.0482 0.0071  102 GLN B CA  
5914 C C   . GLN B 84  ? 0.1894 0.1117 0.1789 0.0140  -0.0298 -0.0053 102 GLN B C   
5915 O O   . GLN B 84  ? 0.1976 0.1276 0.1701 0.0054  -0.0231 -0.0319 102 GLN B O   
5916 C CB  . GLN B 84  ? 0.1624 0.1083 0.2105 -0.0011 -0.0494 0.0034  102 GLN B CB  
5917 C CG  . GLN B 84  ? 0.1999 0.1110 0.2098 0.0146  -0.0325 -0.0016 102 GLN B CG  
5918 C CD  . GLN B 84  ? 0.1837 0.1081 0.2159 -0.0037 -0.0405 0.0081  102 GLN B CD  
5919 O OE1 . GLN B 84  ? 0.1990 0.1305 0.2268 0.0217  -0.0520 0.0107  102 GLN B OE1 
5920 N NE2 . GLN B 84  ? 0.2027 0.1070 0.2286 0.0082  -0.0309 0.0017  102 GLN B NE2 
5929 N N   . VAL B 85  ? 0.1655 0.1334 0.2042 0.0115  -0.0318 0.0034  103 VAL B N   
5930 C CA  . VAL B 85  ? 0.1899 0.1565 0.2215 0.0058  -0.0390 0.0058  103 VAL B CA  
5931 C C   . VAL B 85  ? 0.1891 0.1422 0.2043 0.0252  -0.0332 -0.0120 103 VAL B C   
5932 O O   . VAL B 85  ? 0.1772 0.1366 0.2064 0.0216  -0.0266 -0.0275 103 VAL B O   
5933 C CB  . VAL B 85  ? 0.1922 0.1715 0.2519 0.0052  -0.0132 -0.0107 103 VAL B CB  
5934 C CG1 . VAL B 85  ? 0.1875 0.1856 0.2742 -0.0010 -0.0170 -0.0271 103 VAL B CG1 
5935 C CG2 . VAL B 85  ? 0.2035 0.1914 0.2633 -0.0248 -0.0283 0.0046  103 VAL B CG2 
5945 N N   . ASN B 86  ? 0.2080 0.1280 0.1976 0.0058  -0.0493 -0.0168 104 ASN B N   
5946 C CA  . ASN B 86  ? 0.1993 0.1288 0.2127 0.0089  -0.0391 -0.0185 104 ASN B CA  
5947 C C   . ASN B 86  ? 0.2007 0.1346 0.1990 0.0448  -0.0263 -0.0148 104 ASN B C   
5948 O O   . ASN B 86  ? 0.2105 0.1291 0.2057 0.0269  -0.0265 -0.0126 104 ASN B O   
5949 C CB  . ASN B 86  ? 0.2071 0.1110 0.2226 0.0336  -0.0252 -0.0157 104 ASN B CB  
5950 C CG  . ASN B 86  ? 0.2078 0.1268 0.2130 0.0157  -0.0350 0.0120  104 ASN B CG  
5951 O OD1 . ASN B 86  ? 0.2133 0.1656 0.2308 0.0091  -0.0520 -0.0010 104 ASN B OD1 
5952 N ND2 . ASN B 86  ? 0.1987 0.1167 0.2104 0.0177  -0.0174 0.0159  104 ASN B ND2 
5959 N N   . THR B 87  ? 0.1718 0.1304 0.1929 0.0313  -0.0544 -0.0151 105 THR B N   
5960 C CA  . THR B 87  ? 0.1796 0.1481 0.1888 0.0271  -0.0580 0.0065  105 THR B CA  
5961 C C   . THR B 87  ? 0.1837 0.1337 0.1754 0.0118  -0.0412 -0.0086 105 THR B C   
5962 O O   . THR B 87  ? 0.1915 0.1331 0.1921 0.0226  -0.0370 -0.0143 105 THR B O   
5963 C CB  . THR B 87  ? 0.1771 0.1645 0.1926 0.0342  -0.0545 -0.0126 105 THR B CB  
5964 O OG1 . THR B 87  ? 0.1970 0.1497 0.2082 0.0238  -0.0297 -0.0228 105 THR B OG1 
5965 C CG2 . THR B 87  ? 0.1978 0.1657 0.1915 0.0480  -0.0393 -0.0361 105 THR B CG2 
5973 N N   . GLU B 88  ? 0.1900 0.1306 0.1830 -0.0005 -0.0309 -0.0341 106 GLU B N   
5974 C CA  . GLU B 88  ? 0.1825 0.1392 0.1959 -0.0030 -0.0481 -0.0107 106 GLU B CA  
5975 C C   . GLU B 88  ? 0.2110 0.1487 0.1982 -0.0044 -0.0363 -0.0229 106 GLU B C   
5976 O O   . GLU B 88  ? 0.2109 0.1354 0.1870 -0.0079 -0.0301 -0.0034 106 GLU B O   
5977 C CB  . GLU B 88  ? 0.2064 0.1333 0.2280 -0.0233 -0.0561 -0.0334 106 GLU B CB  
5978 C CG  . GLU B 88  ? 0.2302 0.1186 0.2559 -0.0338 -0.0225 -0.0351 106 GLU B CG  
5979 C CD  . GLU B 88  ? 0.2736 0.1467 0.2901 -0.0377 0.0156  -0.0554 106 GLU B CD  
5980 O OE1 . GLU B 88  ? 0.3024 0.1658 0.2824 -0.0686 0.0013  -0.0498 106 GLU B OE1 
5981 O OE2 . GLU B 88  ? 0.3335 0.1660 0.3207 -0.0500 0.0259  -0.0447 106 GLU B OE2 
5988 N N   . TYR B 89  ? 0.1898 0.1524 0.1964 0.0130  -0.0362 -0.0433 107 TYR B N   
5989 C CA  . TYR B 89  ? 0.2150 0.1482 0.2048 0.0045  -0.0755 -0.0388 107 TYR B CA  
5990 C C   . TYR B 89  ? 0.2133 0.1458 0.2072 0.0098  -0.0677 -0.0246 107 TYR B C   
5991 O O   . TYR B 89  ? 0.2175 0.1563 0.1996 0.0066  -0.0429 -0.0350 107 TYR B O   
5992 C CB  . TYR B 89  ? 0.2355 0.1450 0.2139 0.0078  -0.0658 -0.0180 107 TYR B CB  
5993 C CG  . TYR B 89  ? 0.2056 0.1476 0.2103 0.0235  -0.0593 -0.0233 107 TYR B CG  
5994 C CD1 . TYR B 89  ? 0.2100 0.1438 0.2111 0.0309  -0.0682 -0.0219 107 TYR B CD1 
5995 C CD2 . TYR B 89  ? 0.2027 0.1415 0.2243 0.0249  -0.0620 -0.0302 107 TYR B CD2 
5996 C CE1 . TYR B 89  ? 0.2219 0.1552 0.2047 0.0228  -0.0784 -0.0208 107 TYR B CE1 
5997 C CE2 . TYR B 89  ? 0.1888 0.1342 0.2161 0.0103  -0.0653 -0.0415 107 TYR B CE2 
5998 C CZ  . TYR B 89  ? 0.2127 0.1524 0.2250 0.0048  -0.0622 -0.0368 107 TYR B CZ  
5999 O OH  . TYR B 89  ? 0.2417 0.1786 0.2450 -0.0030 -0.0520 -0.0243 107 TYR B OH  
6009 N N   . MET B 90  ? 0.2136 0.1500 0.2012 0.0083  -0.0704 -0.0345 108 MET B N   
6010 C CA  . MET B 90  ? 0.2080 0.1452 0.2172 0.0033  -0.0747 -0.0295 108 MET B CA  
6011 C C   . MET B 90  ? 0.2166 0.1568 0.2076 0.0173  -0.0692 -0.0420 108 MET B C   
6012 O O   . MET B 90  ? 0.2207 0.1676 0.2118 0.0184  -0.0632 -0.0598 108 MET B O   
6013 C CB  . MET B 90  ? 0.2314 0.1469 0.2339 0.0204  -0.0618 -0.0169 108 MET B CB  
6014 C CG  . MET B 90  ? 0.2113 0.1705 0.2651 -0.0061 -0.0614 -0.0150 108 MET B CG  
6015 S SD  . MET B 90  ? 0.3187 0.1872 0.2684 0.0005  -0.0558 -0.0084 108 MET B SD  
6016 C CE  . MET B 90  ? 0.1987 0.0956 0.1782 -0.0449 -0.1089 0.0411  108 MET B CE  
6026 N N   . VAL B 91  ? 0.2165 0.1459 0.1943 0.0190  -0.0778 -0.0128 109 VAL B N   
6027 C CA  . VAL B 91  ? 0.2253 0.1359 0.2079 -0.0005 -0.0649 -0.0138 109 VAL B CA  
6028 C C   . VAL B 91  ? 0.2255 0.1500 0.2066 -0.0107 -0.0679 -0.0247 109 VAL B C   
6029 O O   . VAL B 91  ? 0.2425 0.1785 0.2243 -0.0008 -0.0686 -0.0204 109 VAL B O   
6030 C CB  . VAL B 91  ? 0.2412 0.1299 0.2219 0.0068  -0.0594 -0.0024 109 VAL B CB  
6031 C CG1 . VAL B 91  ? 0.2348 0.1275 0.2288 -0.0003 -0.0524 0.0034  109 VAL B CG1 
6032 C CG2 . VAL B 91  ? 0.2190 0.1142 0.2145 -0.0022 -0.0486 0.0192  109 VAL B CG2 
6042 N N   . ASN B 92  ? 0.2076 0.1703 0.2120 0.0006  -0.0565 -0.0314 110 ASN B N   
6043 C CA  . ASN B 92  ? 0.2077 0.1870 0.2234 0.0021  -0.0371 -0.0379 110 ASN B CA  
6044 C C   . ASN B 92  ? 0.2019 0.1853 0.2149 0.0035  -0.0420 -0.0438 110 ASN B C   
6045 O O   . ASN B 92  ? 0.2222 0.1989 0.2164 -0.0071 -0.0168 -0.0613 110 ASN B O   
6046 C CB  . ASN B 92  ? 0.2065 0.1978 0.2377 -0.0141 -0.0285 -0.0360 110 ASN B CB  
6047 C CG  . ASN B 92  ? 0.2473 0.2254 0.2513 -0.0077 -0.0044 -0.0281 110 ASN B CG  
6048 O OD1 . ASN B 92  ? 0.2833 0.2497 0.2781 0.0062  0.0163  -0.0124 110 ASN B OD1 
6049 N ND2 . ASN B 92  ? 0.2202 0.2135 0.2289 0.0200  0.0031  -0.0401 110 ASN B ND2 
6056 N N   . ALA B 93  ? 0.2098 0.1756 0.2140 0.0079  -0.0622 -0.0559 111 ALA B N   
6057 C CA  . ALA B 93  ? 0.2195 0.1697 0.2187 0.0211  -0.0575 -0.0606 111 ALA B CA  
6058 C C   . ALA B 93  ? 0.2231 0.1769 0.2522 0.0348  -0.0678 -0.0587 111 ALA B C   
6059 O O   . ALA B 93  ? 0.2489 0.1680 0.2681 0.0330  -0.0559 -0.0792 111 ALA B O   
6060 C CB  . ALA B 93  ? 0.2235 0.1613 0.2120 0.0139  -0.0557 -0.0617 111 ALA B CB  
6066 N N   . ILE B 94  ? 0.1985 0.1822 0.2552 0.0091  -0.0785 -0.0760 112 ILE B N   
6067 C CA  . ILE B 94  ? 0.2061 0.1954 0.2388 0.0223  -0.0869 -0.0746 112 ILE B CA  
6068 C C   . ILE B 94  ? 0.2422 0.2045 0.2303 0.0490  -0.0641 -0.0578 112 ILE B C   
6069 O O   . ILE B 94  ? 0.2514 0.2157 0.2402 0.0619  -0.0445 -0.0719 112 ILE B O   
6070 C CB  . ILE B 94  ? 0.2273 0.1858 0.2517 0.0247  -0.0994 -0.0834 112 ILE B CB  
6071 C CG1 . ILE B 94  ? 0.2560 0.2162 0.2565 0.0221  -0.0753 -0.0685 112 ILE B CG1 
6072 C CG2 . ILE B 94  ? 0.2452 0.1834 0.2610 0.0226  -0.0913 -0.0698 112 ILE B CG2 
6073 C CD1 . ILE B 94  ? 0.2817 0.2274 0.2844 0.0356  -0.0682 -0.0391 112 ILE B CD1 
6085 N N   . THR B 95  ? 0.2524 0.2139 0.2141 0.0330  -0.0493 -0.0542 113 THR B N   
6086 C CA  . THR B 95  ? 0.2632 0.2259 0.2252 0.0396  -0.0312 -0.0594 113 THR B CA  
6087 C C   . THR B 95  ? 0.2642 0.2409 0.2179 0.0477  -0.0446 -0.0847 113 THR B C   
6088 O O   . THR B 95  ? 0.2555 0.2514 0.2295 0.0346  -0.0354 -0.0978 113 THR B O   
6089 C CB  . THR B 95  ? 0.2625 0.2308 0.2526 0.0328  -0.0359 -0.0467 113 THR B CB  
6090 O OG1 . THR B 95  ? 0.2621 0.2507 0.2613 0.0255  -0.0360 -0.0465 113 THR B OG1 
6091 C CG2 . THR B 95  ? 0.2900 0.2239 0.2607 0.0105  -0.0244 -0.0318 113 THR B CG2 
6099 N N   . ALA B 96  ? 0.2281 0.2335 0.2252 0.0596  -0.0448 -0.0906 114 ALA B N   
6100 C CA  . ALA B 96  ? 0.2364 0.2512 0.2564 0.0404  -0.0618 -0.0836 114 ALA B CA  
6101 C C   . ALA B 96  ? 0.2377 0.2546 0.2523 0.0431  -0.0673 -0.0934 114 ALA B C   
6102 O O   . ALA B 96  ? 0.2651 0.2575 0.2582 0.0430  -0.0374 -0.1060 114 ALA B O   
6103 C CB  . ALA B 96  ? 0.2267 0.2602 0.2607 0.0484  -0.0710 -0.0860 114 ALA B CB  
6109 N N   . LEU B 97  ? 0.2441 0.2512 0.2681 0.0298  -0.0724 -0.0904 115 LEU B N   
6110 C CA  . LEU B 97  ? 0.2417 0.2412 0.2542 0.0320  -0.0527 -0.0929 115 LEU B CA  
6111 C C   . LEU B 97  ? 0.2458 0.2250 0.2390 0.0577  -0.0511 -0.0967 115 LEU B C   
6112 O O   . LEU B 97  ? 0.2565 0.2317 0.2508 0.0232  -0.0460 -0.1176 115 LEU B O   
6113 C CB  . LEU B 97  ? 0.2466 0.2377 0.2496 0.0470  -0.0652 -0.0767 115 LEU B CB  
6114 C CG  . LEU B 97  ? 0.2353 0.2276 0.2612 0.0461  -0.0593 -0.0673 115 LEU B CG  
6115 C CD1 . LEU B 97  ? 0.2339 0.2344 0.2634 0.0465  -0.0764 -0.0660 115 LEU B CD1 
6116 C CD2 . LEU B 97  ? 0.2574 0.2345 0.2691 0.0535  -0.0145 -0.0547 115 LEU B CD2 
6128 N N   . TYR B 98  ? 0.2454 0.2263 0.2372 0.0464  -0.0517 -0.0780 116 TYR B N   
6129 C CA  . TYR B 98  ? 0.2466 0.2218 0.2258 0.0406  -0.0380 -0.0732 116 TYR B CA  
6130 C C   . TYR B 98  ? 0.2630 0.2384 0.2331 0.0394  -0.0483 -0.0827 116 TYR B C   
6131 O O   . TYR B 98  ? 0.2887 0.2460 0.2136 0.0256  -0.0514 -0.0934 116 TYR B O   
6132 C CB  . TYR B 98  ? 0.2290 0.2253 0.2122 0.0227  -0.0469 -0.0693 116 TYR B CB  
6133 C CG  . TYR B 98  ? 0.2603 0.2294 0.2086 0.0130  -0.0707 -0.0516 116 TYR B CG  
6134 C CD1 . TYR B 98  ? 0.2903 0.2293 0.1934 0.0004  -0.1031 -0.0500 116 TYR B CD1 
6135 C CD2 . TYR B 98  ? 0.2829 0.2584 0.2174 0.0135  -0.0554 -0.0507 116 TYR B CD2 
6136 C CE1 . TYR B 98  ? 0.3235 0.2432 0.2132 -0.0330 -0.1059 -0.0343 116 TYR B CE1 
6137 C CE2 . TYR B 98  ? 0.3233 0.2667 0.2095 0.0001  -0.0560 -0.0281 116 TYR B CE2 
6138 C CZ  . TYR B 98  ? 0.3367 0.2672 0.2115 -0.0216 -0.1041 -0.0310 116 TYR B CZ  
6139 O OH  . TYR B 98  ? 0.3924 0.2894 0.2398 -0.0261 -0.0971 -0.0227 116 TYR B OH  
6149 N N   . ALA B 99  ? 0.2437 0.2435 0.2560 0.0405  -0.0305 -0.0741 117 ALA B N   
6150 C CA  . ALA B 99  ? 0.2723 0.2751 0.2899 0.0055  -0.0222 -0.0988 117 ALA B CA  
6151 C C   . ALA B 99  ? 0.2784 0.2932 0.3068 0.0057  -0.0281 -0.1195 117 ALA B C   
6152 O O   . ALA B 99  ? 0.3009 0.3056 0.3103 0.0307  -0.0133 -0.1184 117 ALA B O   
6153 C CB  . ALA B 99  ? 0.2803 0.2800 0.3021 -0.0032 -0.0124 -0.0978 117 ALA B CB  
6159 N N   . GLY B 100 ? 0.2944 0.2943 0.3114 0.0157  -0.0164 -0.1163 118 GLY B N   
6160 C CA  . GLY B 100 ? 0.2941 0.2896 0.3205 0.0344  -0.0375 -0.1177 118 GLY B CA  
6161 C C   . GLY B 100 ? 0.3178 0.2901 0.3307 0.0591  -0.0332 -0.1290 118 GLY B C   
6162 O O   . GLY B 100 ? 0.3128 0.2882 0.3489 0.0891  -0.0537 -0.1232 118 GLY B O   
6166 N N   . SER B 101 ? 0.2989 0.2861 0.3084 0.0549  -0.0513 -0.1195 119 SER B N   
6167 C CA  . SER B 101 ? 0.3217 0.2864 0.2922 0.0473  -0.0355 -0.1145 119 SER B CA  
6168 C C   . SER B 101 ? 0.3391 0.3050 0.2678 0.0401  -0.0138 -0.1124 119 SER B C   
6169 O O   . SER B 101 ? 0.3758 0.3059 0.2629 0.0264  0.0144  -0.1250 119 SER B O   
6170 C CB  . SER B 101 ? 0.2997 0.2659 0.2901 0.0586  -0.0416 -0.1085 119 SER B CB  
6171 O OG  . SER B 101 ? 0.2856 0.2612 0.2889 0.0805  -0.0594 -0.1137 119 SER B OG  
6177 N N   . GLY B 102 ? 0.3188 0.3113 0.2592 0.0441  0.0058  -0.0980 120 GLY B N   
6178 C CA  . GLY B 102 ? 0.2971 0.3160 0.2625 0.0379  -0.0211 -0.0773 120 GLY B CA  
6179 C C   . GLY B 102 ? 0.3169 0.3155 0.2616 0.0274  -0.0137 -0.0622 120 GLY B C   
6180 O O   . GLY B 102 ? 0.3493 0.3316 0.2751 0.0283  0.0001  -0.0668 120 GLY B O   
6184 N N   . ASN B 103 ? 0.3126 0.3113 0.2505 0.0117  -0.0106 -0.0565 121 ASN B N   
6185 C CA  . ASN B 103 ? 0.2948 0.3096 0.2398 0.0255  -0.0480 -0.0393 121 ASN B CA  
6186 C C   . ASN B 103 ? 0.3035 0.2726 0.2340 0.0267  -0.0599 -0.0482 121 ASN B C   
6187 O O   . ASN B 103 ? 0.3270 0.2991 0.2472 0.0234  -0.0656 -0.0323 121 ASN B O   
6188 C CB  . ASN B 103 ? 0.3317 0.3596 0.2496 -0.0267 -0.0576 -0.0267 121 ASN B CB  
6189 C CG  . ASN B 103 ? 0.3630 0.4178 0.2759 -0.0383 -0.0403 -0.0110 121 ASN B CG  
6190 O OD1 . ASN B 103 ? 0.3549 0.4383 0.2821 -0.0508 -0.0680 0.0016  121 ASN B OD1 
6191 N ND2 . ASN B 103 ? 0.4009 0.4397 0.3021 -0.0156 -0.0128 -0.0158 121 ASN B ND2 
6198 N N   . ASN B 104 ? 0.2801 0.2507 0.2309 0.0252  -0.0395 -0.0479 122 ASN B N   
6199 C CA  . ASN B 104 ? 0.3173 0.2463 0.2488 0.0082  -0.0303 -0.0605 122 ASN B CA  
6200 C C   . ASN B 104 ? 0.2767 0.2118 0.2038 0.0035  -0.0415 -0.0438 122 ASN B C   
6201 O O   . ASN B 104 ? 0.2549 0.2162 0.2351 0.0035  -0.0490 -0.0363 122 ASN B O   
6202 C CB  . ASN B 104 ? 0.3504 0.2656 0.2742 0.0318  -0.0416 -0.0735 122 ASN B CB  
6203 C CG  . ASN B 104 ? 0.4104 0.2996 0.3053 0.0355  -0.0569 -0.0878 122 ASN B CG  
6204 O OD1 . ASN B 104 ? 0.4382 0.3223 0.3214 0.0207  -0.0881 -0.0864 122 ASN B OD1 
6205 N ND2 . ASN B 104 ? 0.4171 0.3189 0.3121 0.0660  -0.0230 -0.0848 122 ASN B ND2 
6212 N N   . LYS B 105 ? 0.2932 0.2027 0.2123 -0.0025 -0.0230 -0.0271 123 LYS B N   
6213 C CA  . LYS B 105 ? 0.2883 0.2164 0.2010 -0.0015 -0.0502 -0.0317 123 LYS B CA  
6214 C C   . LYS B 105 ? 0.2853 0.1902 0.2197 0.0039  -0.0532 -0.0424 123 LYS B C   
6215 O O   . LYS B 105 ? 0.3105 0.1993 0.2291 -0.0075 -0.0224 -0.0370 123 LYS B O   
6216 C CB  . LYS B 105 ? 0.3115 0.2544 0.2173 -0.0106 -0.0416 -0.0192 123 LYS B CB  
6217 C CG  . LYS B 105 ? 0.3638 0.3010 0.2409 0.0045  -0.0322 -0.0097 123 LYS B CG  
6218 C CD  . LYS B 105 ? 0.4224 0.3522 0.2780 0.0018  -0.0414 0.0060  123 LYS B CD  
6219 C CE  . LYS B 105 ? 0.4968 0.3975 0.3332 -0.0053 -0.0266 0.0107  123 LYS B CE  
6220 N NZ  . LYS B 105 ? 0.5448 0.4201 0.3708 -0.0057 -0.0180 0.0055  123 LYS B NZ  
6234 N N   . LEU B 106 ? 0.2771 0.1708 0.2272 0.0096  -0.0873 -0.0557 124 LEU B N   
6235 C CA  . LEU B 106 ? 0.2987 0.1586 0.2338 0.0111  -0.0789 -0.0473 124 LEU B CA  
6236 C C   . LEU B 106 ? 0.2919 0.1516 0.2321 0.0174  -0.1024 -0.0517 124 LEU B C   
6237 O O   . LEU B 106 ? 0.3137 0.1486 0.2226 0.0197  -0.1104 -0.0269 124 LEU B O   
6238 C CB  . LEU B 106 ? 0.2832 0.1725 0.2446 0.0013  -0.0757 -0.0660 124 LEU B CB  
6239 C CG  . LEU B 106 ? 0.3041 0.2040 0.2453 -0.0120 -0.0613 -0.0642 124 LEU B CG  
6240 C CD1 . LEU B 106 ? 0.2743 0.2242 0.2459 -0.0291 -0.0909 -0.0618 124 LEU B CD1 
6241 C CD2 . LEU B 106 ? 0.3272 0.2227 0.2301 0.0084  -0.0537 -0.0648 124 LEU B CD2 
6253 N N   . PRO B 107 ? 0.2783 0.1355 0.2586 0.0059  -0.0954 -0.0576 125 PRO B N   
6254 C CA  . PRO B 107 ? 0.2626 0.1370 0.2654 -0.0141 -0.0860 -0.0512 125 PRO B CA  
6255 C C   . PRO B 107 ? 0.2483 0.1561 0.2397 -0.0071 -0.0990 -0.0410 125 PRO B C   
6256 O O   . PRO B 107 ? 0.2477 0.1588 0.2447 -0.0270 -0.0833 -0.0448 125 PRO B O   
6257 C CB  . PRO B 107 ? 0.2801 0.1385 0.2878 -0.0224 -0.0817 -0.0523 125 PRO B CB  
6258 C CG  . PRO B 107 ? 0.2950 0.1473 0.2840 -0.0107 -0.0715 -0.0384 125 PRO B CG  
6259 C CD  . PRO B 107 ? 0.3255 0.1341 0.2742 -0.0141 -0.0643 -0.0509 125 PRO B CD  
6267 N N   . VAL B 108 ? 0.2210 0.1449 0.2445 0.0015  -0.0920 -0.0264 126 VAL B N   
6268 C CA  . VAL B 108 ? 0.2559 0.1349 0.2423 0.0207  -0.0676 -0.0280 126 VAL B CA  
6269 C C   . VAL B 108 ? 0.2571 0.1260 0.2360 0.0207  -0.0696 -0.0298 126 VAL B C   
6270 O O   . VAL B 108 ? 0.2721 0.1416 0.2330 0.0147  -0.0773 -0.0290 126 VAL B O   
6271 C CB  . VAL B 108 ? 0.2671 0.1252 0.2243 0.0252  -0.0866 -0.0383 126 VAL B CB  
6272 C CG1 . VAL B 108 ? 0.2675 0.1339 0.2277 0.0021  -0.1008 -0.0317 126 VAL B CG1 
6273 C CG2 . VAL B 108 ? 0.2752 0.1372 0.2469 0.0031  -0.0678 -0.0344 126 VAL B CG2 
6283 N N   . LEU B 109 ? 0.2587 0.1130 0.2558 0.0112  -0.0870 -0.0153 127 LEU B N   
6284 C CA  . LEU B 109 ? 0.2564 0.1004 0.2480 -0.0049 -0.0986 -0.0103 127 LEU B CA  
6285 C C   . LEU B 109 ? 0.2674 0.1148 0.2353 -0.0053 -0.0936 -0.0058 127 LEU B C   
6286 O O   . LEU B 109 ? 0.2628 0.1214 0.2323 0.0025  -0.0753 -0.0293 127 LEU B O   
6287 C CB  . LEU B 109 ? 0.2657 0.0966 0.2552 -0.0238 -0.0865 0.0071  127 LEU B CB  
6288 C CG  . LEU B 109 ? 0.2732 0.0917 0.2594 -0.0152 -0.0912 0.0161  127 LEU B CG  
6289 C CD1 . LEU B 109 ? 0.3323 0.1042 0.2762 -0.0395 -0.0734 0.0183  127 LEU B CD1 
6290 C CD2 . LEU B 109 ? 0.2667 0.0953 0.2677 -0.0095 -0.0999 0.0226  127 LEU B CD2 
6302 N N   . THR B 110 ? 0.2612 0.1062 0.2426 -0.0166 -0.0919 -0.0238 128 THR B N   
6303 C CA  . THR B 110 ? 0.2720 0.1051 0.2302 -0.0212 -0.0911 -0.0178 128 THR B CA  
6304 C C   . THR B 110 ? 0.2706 0.1102 0.2322 -0.0182 -0.0930 -0.0003 128 THR B C   
6305 O O   . THR B 110 ? 0.2909 0.0957 0.2307 -0.0395 -0.0707 0.0046  128 THR B O   
6306 C CB  . THR B 110 ? 0.2516 0.1063 0.2442 -0.0086 -0.1023 -0.0065 128 THR B CB  
6307 O OG1 . THR B 110 ? 0.2521 0.1189 0.2506 0.0014  -0.0746 0.0121  128 THR B OG1 
6308 C CG2 . THR B 110 ? 0.2533 0.1016 0.2533 -0.0305 -0.1112 0.0021  128 THR B CG2 
6316 N N   . TRP B 111 ? 0.2694 0.1011 0.2304 -0.0152 -0.1014 0.0036  129 TRP B N   
6317 C CA  . TRP B 111 ? 0.2446 0.1124 0.2388 -0.0076 -0.0898 0.0084  129 TRP B CA  
6318 C C   . TRP B 111 ? 0.2345 0.1205 0.2269 0.0020  -0.0779 0.0021  129 TRP B C   
6319 O O   . TRP B 111 ? 0.2384 0.1286 0.2093 0.0125  -0.0709 0.0083  129 TRP B O   
6320 C CB  . TRP B 111 ? 0.2481 0.1133 0.2610 0.0122  -0.0571 0.0020  129 TRP B CB  
6321 C CG  . TRP B 111 ? 0.2509 0.1209 0.2597 0.0041  -0.0639 0.0036  129 TRP B CG  
6322 C CD1 . TRP B 111 ? 0.2684 0.1407 0.2539 0.0236  -0.0625 0.0012  129 TRP B CD1 
6323 C CD2 . TRP B 111 ? 0.2938 0.1300 0.2497 -0.0053 -0.0570 0.0266  129 TRP B CD2 
6324 N NE1 . TRP B 111 ? 0.2646 0.1366 0.2426 0.0103  -0.0754 0.0022  129 TRP B NE1 
6325 C CE2 . TRP B 111 ? 0.2841 0.1437 0.2355 -0.0134 -0.0842 0.0115  129 TRP B CE2 
6326 C CE3 . TRP B 111 ? 0.3134 0.1314 0.2331 -0.0049 -0.0730 0.0296  129 TRP B CE3 
6327 C CZ2 . TRP B 111 ? 0.3095 0.1407 0.2408 -0.0399 -0.0837 0.0157  129 TRP B CZ2 
6328 C CZ3 . TRP B 111 ? 0.3288 0.1553 0.2342 -0.0168 -0.0699 0.0234  129 TRP B CZ3 
6329 C CH2 . TRP B 111 ? 0.3219 0.1671 0.2403 -0.0298 -0.0766 0.0242  129 TRP B CH2 
6340 N N   . SER B 112 ? 0.2517 0.1308 0.2508 -0.0262 -0.0572 0.0030  130 SER B N   
6341 C CA  . SER B 112 ? 0.2643 0.1199 0.2382 -0.0320 -0.0595 0.0136  130 SER B CA  
6342 C C   . SER B 112 ? 0.2500 0.1199 0.2303 -0.0130 -0.0716 0.0103  130 SER B C   
6343 O O   . SER B 112 ? 0.2594 0.1195 0.2319 -0.0020 -0.0892 0.0155  130 SER B O   
6344 C CB  . SER B 112 ? 0.3374 0.1255 0.2259 -0.0420 -0.0659 0.0053  130 SER B CB  
6345 O OG  . SER B 112 ? 0.3924 0.1590 0.2598 -0.0275 -0.0596 -0.0004 130 SER B OG  
6351 N N   . GLN B 113 ? 0.2351 0.1204 0.2437 -0.0098 -0.0736 0.0048  131 GLN B N   
6352 C CA  . GLN B 113 ? 0.2237 0.0999 0.2359 0.0023  -0.0682 0.0085  131 GLN B CA  
6353 C C   . GLN B 113 ? 0.2162 0.0884 0.2336 0.0242  -0.0873 -0.0148 131 GLN B C   
6354 O O   . GLN B 113 ? 0.1998 0.1097 0.2598 0.0079  -0.0761 0.0011  131 GLN B O   
6355 C CB  . GLN B 113 ? 0.2080 0.1112 0.2454 -0.0112 -0.0598 -0.0110 131 GLN B CB  
6356 C CG  . GLN B 113 ? 0.2004 0.1056 0.2303 -0.0066 -0.0619 -0.0082 131 GLN B CG  
6357 C CD  . GLN B 113 ? 0.2058 0.1225 0.2176 0.0075  -0.0666 -0.0113 131 GLN B CD  
6358 O OE1 . GLN B 113 ? 0.2258 0.1506 0.2136 -0.0172 -0.0554 -0.0166 131 GLN B OE1 
6359 N NE2 . GLN B 113 ? 0.2052 0.1231 0.2208 -0.0049 -0.0893 -0.0043 131 GLN B NE2 
6368 N N   . GLY B 114 ? 0.2410 0.0951 0.2351 0.0094  -0.0961 0.0012  132 GLY B N   
6369 C CA  . GLY B 114 ? 0.2201 0.1146 0.2303 0.0234  -0.0697 -0.0078 132 GLY B CA  
6370 C C   . GLY B 114 ? 0.2066 0.1151 0.2228 -0.0075 -0.0790 -0.0171 132 GLY B C   
6371 O O   . GLY B 114 ? 0.2316 0.1152 0.2494 -0.0040 -0.0800 -0.0032 132 GLY B O   
6375 N N   . GLY B 115 ? 0.2085 0.1340 0.2196 0.0004  -0.0619 -0.0012 133 GLY B N   
6376 C CA  . GLY B 115 ? 0.2050 0.1202 0.2196 -0.0177 -0.0624 0.0104  133 GLY B CA  
6377 C C   . GLY B 115 ? 0.2196 0.1120 0.1997 -0.0243 -0.0463 0.0008  133 GLY B C   
6378 O O   . GLY B 115 ? 0.2519 0.1277 0.1899 -0.0345 -0.0485 0.0053  133 GLY B O   
6382 N N   . LEU B 116 ? 0.2090 0.1116 0.1917 -0.0071 -0.0398 -0.0097 134 LEU B N   
6383 C CA  . LEU B 116 ? 0.1974 0.1257 0.2113 -0.0067 -0.0681 -0.0112 134 LEU B CA  
6384 C C   . LEU B 116 ? 0.2038 0.1169 0.2098 0.0037  -0.0502 -0.0010 134 LEU B C   
6385 O O   . LEU B 116 ? 0.2099 0.1144 0.1983 -0.0062 -0.0413 0.0167  134 LEU B O   
6386 C CB  . LEU B 116 ? 0.2151 0.1128 0.2120 0.0034  -0.0399 -0.0085 134 LEU B CB  
6387 C CG  . LEU B 116 ? 0.2137 0.1125 0.2152 -0.0184 -0.0475 0.0004  134 LEU B CG  
6388 C CD1 . LEU B 116 ? 0.2259 0.1197 0.2498 -0.0200 -0.0330 -0.0042 134 LEU B CD1 
6389 C CD2 . LEU B 116 ? 0.2719 0.1344 0.2254 -0.0407 -0.0368 0.0278  134 LEU B CD2 
6401 N N   . VAL B 117 ? 0.2017 0.1328 0.2344 -0.0096 -0.0634 0.0003  135 VAL B N   
6402 C CA  . VAL B 117 ? 0.2078 0.1383 0.2261 0.0041  -0.0729 0.0161  135 VAL B CA  
6403 C C   . VAL B 117 ? 0.2040 0.1269 0.2261 -0.0079 -0.0410 -0.0123 135 VAL B C   
6404 O O   . VAL B 117 ? 0.2228 0.1167 0.2376 0.0042  -0.0319 -0.0139 135 VAL B O   
6405 C CB  . VAL B 117 ? 0.2028 0.1278 0.2237 0.0139  -0.0687 0.0149  135 VAL B CB  
6406 C CG1 . VAL B 117 ? 0.2158 0.1208 0.2470 0.0010  -0.0745 0.0142  135 VAL B CG1 
6407 C CG2 . VAL B 117 ? 0.1953 0.1378 0.2147 0.0101  -0.0579 -0.0014 135 VAL B CG2 
6417 N N   . ALA B 118 ? 0.2169 0.1135 0.2073 -0.0174 -0.0536 -0.0244 136 ALA B N   
6418 C CA  . ALA B 118 ? 0.2358 0.1024 0.1932 -0.0191 -0.0901 -0.0198 136 ALA B CA  
6419 C C   . ALA B 118 ? 0.2254 0.1150 0.2064 -0.0125 -0.0692 -0.0100 136 ALA B C   
6420 O O   . ALA B 118 ? 0.2256 0.1197 0.2174 -0.0136 -0.0543 0.0174  136 ALA B O   
6421 C CB  . ALA B 118 ? 0.2545 0.0988 0.2265 -0.0115 -0.0733 -0.0082 136 ALA B CB  
6427 N N   . GLN B 119 ? 0.2217 0.1311 0.2221 -0.0019 -0.0577 -0.0075 137 GLN B N   
6428 C CA  . GLN B 119 ? 0.2073 0.1496 0.2262 0.0166  -0.0417 -0.0095 137 GLN B CA  
6429 C C   . GLN B 119 ? 0.1811 0.1222 0.2131 0.0188  -0.0678 0.0031  137 GLN B C   
6430 O O   . GLN B 119 ? 0.1945 0.1468 0.2046 0.0104  -0.0487 0.0240  137 GLN B O   
6431 C CB  . GLN B 119 ? 0.2215 0.1763 0.2353 0.0084  -0.0384 -0.0119 137 GLN B CB  
6432 C CG  . GLN B 119 ? 0.2297 0.1771 0.2344 0.0261  -0.0729 -0.0088 137 GLN B CG  
6433 C CD  . GLN B 119 ? 0.2519 0.1912 0.2496 -0.0119 -0.0476 0.0060  137 GLN B CD  
6434 O OE1 . GLN B 119 ? 0.2298 0.2003 0.2547 -0.0094 -0.0737 0.0140  137 GLN B OE1 
6435 N NE2 . GLN B 119 ? 0.2287 0.1827 0.2556 -0.0416 -0.0532 0.0000  137 GLN B NE2 
6444 N N   . TRP B 120 ? 0.1988 0.1026 0.2170 -0.0045 -0.0492 -0.0001 138 TRP B N   
6445 C CA  . TRP B 120 ? 0.1873 0.1109 0.2203 -0.0054 -0.0586 -0.0057 138 TRP B CA  
6446 C C   . TRP B 120 ? 0.1896 0.1156 0.2229 0.0075  -0.0625 -0.0012 138 TRP B C   
6447 O O   . TRP B 120 ? 0.2016 0.1331 0.2202 0.0055  -0.0665 0.0046  138 TRP B O   
6448 C CB  . TRP B 120 ? 0.1849 0.1079 0.2010 -0.0065 -0.0513 -0.0182 138 TRP B CB  
6449 C CG  . TRP B 120 ? 0.1811 0.1167 0.2117 0.0030  -0.0550 0.0120  138 TRP B CG  
6450 C CD1 . TRP B 120 ? 0.2016 0.1227 0.2230 0.0028  -0.0308 -0.0006 138 TRP B CD1 
6451 C CD2 . TRP B 120 ? 0.1826 0.1259 0.2143 -0.0063 -0.0519 0.0075  138 TRP B CD2 
6452 N NE1 . TRP B 120 ? 0.1978 0.1331 0.2144 0.0223  -0.0165 -0.0040 138 TRP B NE1 
6453 C CE2 . TRP B 120 ? 0.1736 0.1191 0.1965 0.0039  -0.0320 -0.0004 138 TRP B CE2 
6454 C CE3 . TRP B 120 ? 0.1755 0.1268 0.2142 -0.0290 -0.0442 0.0090  138 TRP B CE3 
6455 C CZ2 . TRP B 120 ? 0.1925 0.1211 0.2007 -0.0004 -0.0533 0.0070  138 TRP B CZ2 
6456 C CZ3 . TRP B 120 ? 0.1882 0.1394 0.2079 -0.0022 -0.0479 0.0117  138 TRP B CZ3 
6457 C CH2 . TRP B 120 ? 0.2120 0.1191 0.2094 -0.0035 -0.0463 0.0141  138 TRP B CH2 
6468 N N   . GLY B 121 ? 0.1866 0.1285 0.2157 -0.0052 -0.0550 -0.0002 139 GLY B N   
6469 C CA  . GLY B 121 ? 0.1737 0.1190 0.2101 0.0021  -0.0235 0.0243  139 GLY B CA  
6470 C C   . GLY B 121 ? 0.1898 0.1274 0.1952 -0.0084 -0.0241 -0.0081 139 GLY B C   
6471 O O   . GLY B 121 ? 0.2101 0.1343 0.1917 -0.0075 -0.0182 0.0119  139 GLY B O   
6475 N N   . LEU B 122 ? 0.1829 0.1317 0.1777 -0.0115 -0.0378 -0.0004 140 LEU B N   
6476 C CA  . LEU B 122 ? 0.1610 0.1396 0.1897 -0.0106 -0.0554 0.0171  140 LEU B CA  
6477 C C   . LEU B 122 ? 0.1997 0.1598 0.1948 -0.0168 -0.0506 0.0130  140 LEU B C   
6478 O O   . LEU B 122 ? 0.2120 0.1676 0.2022 -0.0050 -0.0678 0.0246  140 LEU B O   
6479 C CB  . LEU B 122 ? 0.2138 0.1314 0.2015 -0.0187 -0.0530 -0.0055 140 LEU B CB  
6480 C CG  . LEU B 122 ? 0.2273 0.1515 0.2081 -0.0010 -0.0654 0.0174  140 LEU B CG  
6481 C CD1 . LEU B 122 ? 0.2547 0.1630 0.2197 -0.0021 -0.0780 -0.0001 140 LEU B CD1 
6482 C CD2 . LEU B 122 ? 0.2499 0.1609 0.2182 -0.0171 -0.0636 0.0221  140 LEU B CD2 
6494 N N   . THR B 123 ? 0.1825 0.1449 0.1883 0.0119  -0.0179 0.0172  141 THR B N   
6495 C CA  . THR B 123 ? 0.1968 0.1462 0.2115 0.0118  -0.0273 0.0141  141 THR B CA  
6496 C C   . THR B 123 ? 0.1794 0.1530 0.2286 0.0199  -0.0503 0.0191  141 THR B C   
6497 O O   . THR B 123 ? 0.2141 0.1608 0.2356 0.0035  -0.0689 0.0351  141 THR B O   
6498 C CB  . THR B 123 ? 0.1949 0.1564 0.2172 0.0091  -0.0292 0.0099  141 THR B CB  
6499 O OG1 . THR B 123 ? 0.1948 0.1552 0.1976 0.0012  -0.0366 0.0194  141 THR B OG1 
6500 C CG2 . THR B 123 ? 0.2162 0.1790 0.2284 0.0243  -0.0348 0.0214  141 THR B CG2 
6508 N N   . PHE B 124 ? 0.1645 0.1449 0.2284 0.0199  -0.0448 -0.0006 142 PHE B N   
6509 C CA  . PHE B 124 ? 0.1985 0.1334 0.2160 0.0031  -0.0349 0.0027  142 PHE B CA  
6510 C C   . PHE B 124 ? 0.2166 0.1337 0.2159 0.0017  -0.0425 0.0145  142 PHE B C   
6511 O O   . PHE B 124 ? 0.2144 0.1238 0.2167 -0.0046 -0.0376 0.0037  142 PHE B O   
6512 C CB  . PHE B 124 ? 0.1921 0.1316 0.2203 -0.0186 -0.0491 0.0013  142 PHE B CB  
6513 C CG  . PHE B 124 ? 0.2031 0.1268 0.2095 -0.0020 -0.0599 -0.0079 142 PHE B CG  
6514 C CD1 . PHE B 124 ? 0.2274 0.1189 0.1970 0.0211  -0.0560 -0.0092 142 PHE B CD1 
6515 C CD2 . PHE B 124 ? 0.2036 0.1227 0.2136 -0.0095 -0.0571 0.0023  142 PHE B CD2 
6516 C CE1 . PHE B 124 ? 0.2230 0.1160 0.2110 0.0124  -0.0431 -0.0197 142 PHE B CE1 
6517 C CE2 . PHE B 124 ? 0.2071 0.1233 0.2267 0.0107  -0.0599 0.0018  142 PHE B CE2 
6518 C CZ  . PHE B 124 ? 0.2145 0.1279 0.2356 0.0185  -0.0403 -0.0036 142 PHE B CZ  
6528 N N   . PHE B 125 ? 0.2001 0.1393 0.1947 -0.0047 -0.0396 0.0015  143 PHE B N   
6529 C CA  . PHE B 125 ? 0.1993 0.1635 0.1984 0.0116  -0.0623 0.0015  143 PHE B CA  
6530 C C   . PHE B 125 ? 0.2057 0.1606 0.2047 0.0192  -0.0750 -0.0008 143 PHE B C   
6531 O O   . PHE B 125 ? 0.2189 0.1410 0.2173 0.0263  -0.0523 0.0158  143 PHE B O   
6532 C CB  . PHE B 125 ? 0.1805 0.1550 0.2000 0.0141  -0.0388 0.0049  143 PHE B CB  
6533 C CG  . PHE B 125 ? 0.1902 0.1394 0.2122 0.0095  -0.0384 -0.0009 143 PHE B CG  
6534 C CD1 . PHE B 125 ? 0.1812 0.1559 0.2309 -0.0015 -0.0410 0.0111  143 PHE B CD1 
6535 C CD2 . PHE B 125 ? 0.2345 0.1584 0.2159 -0.0014 -0.0027 -0.0187 143 PHE B CD2 
6536 C CE1 . PHE B 125 ? 0.1830 0.1787 0.2215 0.0094  -0.0269 0.0192  143 PHE B CE1 
6537 C CE2 . PHE B 125 ? 0.2149 0.1748 0.2410 0.0014  -0.0151 -0.0083 143 PHE B CE2 
6538 C CZ  . PHE B 125 ? 0.1963 0.1765 0.2306 -0.0106 -0.0168 0.0142  143 PHE B CZ  
6548 N N   . PRO B 126 ? 0.2211 0.1726 0.2124 0.0149  -0.0551 0.0040  144 PRO B N   
6549 C CA  . PRO B 126 ? 0.2140 0.1765 0.2095 0.0309  -0.0545 0.0056  144 PRO B CA  
6550 C C   . PRO B 126 ? 0.2018 0.1846 0.2197 0.0068  -0.0605 0.0050  144 PRO B C   
6551 O O   . PRO B 126 ? 0.2115 0.2043 0.2471 0.0026  -0.0498 -0.0021 144 PRO B O   
6552 C CB  . PRO B 126 ? 0.2520 0.1894 0.2104 0.0273  -0.0722 -0.0005 144 PRO B CB  
6553 C CG  . PRO B 126 ? 0.2620 0.1889 0.2236 0.0379  -0.0502 -0.0144 144 PRO B CG  
6554 C CD  . PRO B 126 ? 0.2381 0.1906 0.2108 0.0417  -0.0508 0.0021  144 PRO B CD  
6562 N N   . SER B 127 ? 0.2184 0.1813 0.2227 0.0152  -0.0246 0.0067  145 SER B N   
6563 C CA  . SER B 127 ? 0.2479 0.1887 0.2156 -0.0039 -0.0378 -0.0128 145 SER B CA  
6564 C C   . SER B 127 ? 0.2335 0.1718 0.2270 -0.0008 -0.0658 -0.0339 145 SER B C   
6565 O O   . SER B 127 ? 0.2764 0.1759 0.2469 0.0142  -0.0619 -0.0317 145 SER B O   
6566 C CB  . SER B 127 ? 0.2658 0.1967 0.2309 -0.0079 -0.0403 -0.0324 145 SER B CB  
6567 O OG  . SER B 127 ? 0.2670 0.2198 0.2655 -0.0043 -0.0524 -0.0439 145 SER B OG  
6573 N N   . ILE B 128 ? 0.2267 0.1683 0.2142 0.0118  -0.0610 -0.0360 146 ILE B N   
6574 C CA  . ILE B 128 ? 0.2279 0.1593 0.2268 0.0268  -0.0730 -0.0148 146 ILE B CA  
6575 C C   . ILE B 128 ? 0.2043 0.1658 0.2323 0.0354  -0.0866 -0.0121 146 ILE B C   
6576 O O   . ILE B 128 ? 0.2237 0.1725 0.2343 0.0328  -0.0857 -0.0160 146 ILE B O   
6577 C CB  . ILE B 128 ? 0.2330 0.1532 0.2240 0.0068  -0.0988 -0.0216 146 ILE B CB  
6578 C CG1 . ILE B 128 ? 0.2883 0.1414 0.2103 -0.0082 -0.0754 -0.0200 146 ILE B CG1 
6579 C CG2 . ILE B 128 ? 0.2725 0.1604 0.2212 0.0142  -0.1079 -0.0260 146 ILE B CG2 
6580 C CD1 . ILE B 128 ? 0.3121 0.1501 0.2344 0.0075  -0.0791 0.0098  146 ILE B CD1 
6592 N N   . ARG B 129 ? 0.1965 0.1828 0.2313 0.0189  -0.0700 -0.0102 147 ARG B N   
6593 C CA  . ARG B 129 ? 0.2121 0.1890 0.2221 0.0136  -0.0621 -0.0036 147 ARG B CA  
6594 C C   . ARG B 129 ? 0.2139 0.1831 0.2134 0.0032  -0.0868 0.0127  147 ARG B C   
6595 O O   . ARG B 129 ? 0.2601 0.1872 0.2452 -0.0348 -0.0527 0.0036  147 ARG B O   
6596 C CB  . ARG B 129 ? 0.2538 0.2014 0.2039 0.0167  -0.0867 -0.0115 147 ARG B CB  
6597 C CG  . ARG B 129 ? 0.2397 0.2157 0.2272 0.0270  -0.0792 -0.0116 147 ARG B CG  
6598 C CD  . ARG B 129 ? 0.2374 0.2176 0.2254 0.0736  -0.0813 -0.0011 147 ARG B CD  
6599 N NE  . ARG B 129 ? 0.2461 0.2162 0.2161 0.0941  -0.0747 -0.0094 147 ARG B NE  
6600 C CZ  . ARG B 129 ? 0.2515 0.2366 0.2213 0.1074  -0.0751 -0.0056 147 ARG B CZ  
6601 N NH1 . ARG B 129 ? 0.3021 0.2543 0.2197 0.1084  -0.0640 -0.0154 147 ARG B NH1 
6602 N NH2 . ARG B 129 ? 0.3058 0.2368 0.2508 0.0820  -0.0479 -0.0089 147 ARG B NH2 
6616 N N   . SER B 130 ? 0.2210 0.1975 0.2111 -0.0077 -0.0615 -0.0079 148 SER B N   
6617 C CA  . SER B 130 ? 0.2614 0.2000 0.2229 -0.0095 -0.0576 -0.0188 148 SER B CA  
6618 C C   . SER B 130 ? 0.2512 0.1847 0.2150 0.0172  -0.0751 -0.0395 148 SER B C   
6619 O O   . SER B 130 ? 0.2924 0.1958 0.2577 0.0462  -0.0797 -0.0468 148 SER B O   
6620 C CB  . SER B 130 ? 0.2805 0.2135 0.2310 -0.0218 -0.0672 -0.0251 148 SER B CB  
6621 O OG  . SER B 130 ? 0.3145 0.2192 0.2419 -0.0296 -0.0425 -0.0185 148 SER B OG  
6627 N N   . LYS B 131 ? 0.2353 0.1719 0.2085 0.0084  -0.0906 -0.0307 149 LYS B N   
6628 C CA  . LYS B 131 ? 0.2402 0.1834 0.2250 0.0120  -0.0664 -0.0453 149 LYS B CA  
6629 C C   . LYS B 131 ? 0.2533 0.1772 0.2179 0.0183  -0.0761 -0.0456 149 LYS B C   
6630 O O   . LYS B 131 ? 0.2698 0.1716 0.2168 0.0357  -0.0650 -0.0546 149 LYS B O   
6631 C CB  . LYS B 131 ? 0.2516 0.1967 0.2355 0.0106  -0.0504 -0.0523 149 LYS B CB  
6632 C CG  . LYS B 131 ? 0.2431 0.1899 0.2555 -0.0007 -0.0440 -0.0466 149 LYS B CG  
6633 C CD  . LYS B 131 ? 0.2708 0.2171 0.2537 0.0026  -0.0535 -0.0725 149 LYS B CD  
6634 C CE  . LYS B 131 ? 0.3208 0.2547 0.2698 -0.0161 -0.0349 -0.0720 149 LYS B CE  
6635 N NZ  . LYS B 131 ? 0.3851 0.2985 0.2892 0.0007  -0.0015 -0.0586 149 LYS B NZ  
6649 N N   . VAL B 132 ? 0.2583 0.1854 0.2252 0.0063  -0.0541 -0.0218 150 VAL B N   
6650 C CA  . VAL B 132 ? 0.2654 0.1674 0.2234 0.0023  -0.0768 -0.0181 150 VAL B CA  
6651 C C   . VAL B 132 ? 0.2990 0.1674 0.2300 0.0148  -0.0820 -0.0064 150 VAL B C   
6652 O O   . VAL B 132 ? 0.2850 0.1470 0.2458 -0.0026 -0.0806 -0.0173 150 VAL B O   
6653 C CB  . VAL B 132 ? 0.2693 0.1656 0.2285 -0.0305 -0.0607 -0.0319 150 VAL B CB  
6654 C CG1 . VAL B 132 ? 0.2537 0.1797 0.2404 -0.0270 -0.0527 -0.0218 150 VAL B CG1 
6655 C CG2 . VAL B 132 ? 0.3028 0.1888 0.2348 -0.0525 -0.0584 -0.0136 150 VAL B CG2 
6665 N N   . ASP B 133 ? 0.3138 0.1714 0.2268 0.0147  -0.1059 -0.0133 151 ASP B N   
6666 C CA  . ASP B 133 ? 0.3622 0.1891 0.2523 -0.0190 -0.1045 0.0099  151 ASP B CA  
6667 C C   . ASP B 133 ? 0.2909 0.1726 0.2428 -0.0293 -0.1354 0.0091  151 ASP B C   
6668 O O   . ASP B 133 ? 0.3581 0.1964 0.2589 -0.0140 -0.1167 0.0160  151 ASP B O   
6669 C CB  . ASP B 133 ? 0.4724 0.2490 0.2902 -0.0796 -0.0664 -0.0136 151 ASP B CB  
6670 C CG  . ASP B 133 ? 0.5409 0.2678 0.2993 -0.1374 -0.0874 0.0102  151 ASP B CG  
6671 O OD1 . ASP B 133 ? 0.5508 0.2909 0.3126 -0.1385 -0.1179 0.0323  151 ASP B OD1 
6672 O OD2 . ASP B 133 ? 0.6132 0.2374 0.2841 -0.1519 -0.0894 0.0128  151 ASP B OD2 
6677 N N   . ARG B 134 ? 0.2694 0.1702 0.2332 -0.0277 -0.1154 0.0033  152 ARG B N   
6678 C CA  . ARG B 134 ? 0.2661 0.1655 0.2488 -0.0366 -0.1018 0.0026  152 ARG B CA  
6679 C C   . ARG B 134 ? 0.2629 0.1409 0.2338 -0.0167 -0.1006 0.0060  152 ARG B C   
6680 O O   . ARG B 134 ? 0.2501 0.1381 0.2336 -0.0191 -0.0917 0.0033  152 ARG B O   
6681 C CB  . ARG B 134 ? 0.3218 0.1599 0.2408 -0.0506 -0.0891 0.0130  152 ARG B CB  
6682 C CG  . ARG B 134 ? 0.3732 0.1469 0.2574 -0.0551 -0.0813 0.0021  152 ARG B CG  
6683 C CD  . ARG B 134 ? 0.4182 0.1453 0.2569 -0.0654 -0.0910 -0.0203 152 ARG B CD  
6684 N NE  . ARG B 134 ? 0.4640 0.1487 0.2491 -0.0611 -0.0679 -0.0288 152 ARG B NE  
6685 C CZ  . ARG B 134 ? 0.4972 0.1483 0.2453 -0.0582 -0.0710 -0.0177 152 ARG B CZ  
6686 N NH1 . ARG B 134 ? 0.4883 0.1688 0.2628 -0.0933 -0.0896 -0.0075 152 ARG B NH1 
6687 N NH2 . ARG B 134 ? 0.5378 0.1517 0.2265 -0.0371 -0.0609 -0.0228 152 ARG B NH2 
6701 N N   . LEU B 135 ? 0.2584 0.1355 0.2437 -0.0207 -0.0965 0.0069  153 LEU B N   
6702 C CA  . LEU B 135 ? 0.2711 0.1257 0.2459 -0.0336 -0.0796 0.0049  153 LEU B CA  
6703 C C   . LEU B 135 ? 0.2521 0.1171 0.2526 -0.0054 -0.0831 0.0119  153 LEU B C   
6704 O O   . LEU B 135 ? 0.2550 0.1362 0.2671 0.0007  -0.0875 0.0195  153 LEU B O   
6705 C CB  . LEU B 135 ? 0.2782 0.1350 0.2272 -0.0172 -0.0776 0.0101  153 LEU B CB  
6706 C CG  . LEU B 135 ? 0.2619 0.1149 0.2256 -0.0180 -0.0844 0.0041  153 LEU B CG  
6707 C CD1 . LEU B 135 ? 0.2599 0.1390 0.2496 -0.0182 -0.0612 -0.0035 153 LEU B CD1 
6708 C CD2 . LEU B 135 ? 0.2843 0.1003 0.2312 -0.0292 -0.0577 0.0104  153 LEU B CD2 
6720 N N   . MET B 136 ? 0.2683 0.0940 0.2421 -0.0153 -0.0835 -0.0035 154 MET B N   
6721 C CA  . MET B 136 ? 0.2439 0.1304 0.2526 -0.0096 -0.0878 0.0135  154 MET B CA  
6722 C C   . MET B 136 ? 0.2661 0.1269 0.2334 -0.0117 -0.0806 0.0086  154 MET B C   
6723 O O   . MET B 136 ? 0.2664 0.1373 0.2424 -0.0312 -0.0814 -0.0068 154 MET B O   
6724 C CB  . MET B 136 ? 0.2673 0.1447 0.2548 -0.0347 -0.0834 0.0093  154 MET B CB  
6725 C CG  . MET B 136 ? 0.2918 0.1467 0.2582 -0.0254 -0.0867 0.0094  154 MET B CG  
6726 S SD  . MET B 136 ? 0.3199 0.1427 0.2757 -0.0466 -0.0963 0.0056  154 MET B SD  
6727 C CE  . MET B 136 ? 0.3293 0.1547 0.2835 -0.0316 -0.0628 -0.0059 154 MET B CE  
6737 N N   . ALA B 137 ? 0.2495 0.1343 0.2186 -0.0242 -0.0631 0.0006  155 ALA B N   
6738 C CA  . ALA B 137 ? 0.2401 0.1097 0.2314 -0.0226 -0.0578 -0.0073 155 ALA B CA  
6739 C C   . ALA B 137 ? 0.2364 0.1178 0.2559 -0.0272 -0.0752 -0.0019 155 ALA B C   
6740 O O   . ALA B 137 ? 0.2548 0.1344 0.2802 -0.0354 -0.0785 0.0104  155 ALA B O   
6741 C CB  . ALA B 137 ? 0.2726 0.0888 0.2286 -0.0098 -0.0176 -0.0083 155 ALA B CB  
6747 N N   . PHE B 138 ? 0.2674 0.1133 0.2443 -0.0373 -0.0926 -0.0033 156 PHE B N   
6748 C CA  . PHE B 138 ? 0.2491 0.1082 0.2567 -0.0150 -0.0810 0.0270  156 PHE B CA  
6749 C C   . PHE B 138 ? 0.2551 0.1221 0.2550 -0.0261 -0.0886 0.0273  156 PHE B C   
6750 O O   . PHE B 138 ? 0.2784 0.1219 0.2618 -0.0487 -0.0955 0.0163  156 PHE B O   
6751 C CB  . PHE B 138 ? 0.2833 0.1023 0.2768 -0.0196 -0.0805 0.0169  156 PHE B CB  
6752 C CG  . PHE B 138 ? 0.3141 0.1095 0.2779 -0.0050 -0.0945 0.0139  156 PHE B CG  
6753 C CD1 . PHE B 138 ? 0.3260 0.1244 0.2882 -0.0215 -0.0679 0.0051  156 PHE B CD1 
6754 C CD2 . PHE B 138 ? 0.3406 0.0987 0.2638 -0.0057 -0.0790 -0.0101 156 PHE B CD2 
6755 C CE1 . PHE B 138 ? 0.3258 0.1231 0.2854 -0.0271 -0.0799 0.0030  156 PHE B CE1 
6756 C CE2 . PHE B 138 ? 0.3452 0.1078 0.2573 -0.0136 -0.0898 -0.0239 156 PHE B CE2 
6757 C CZ  . PHE B 138 ? 0.3276 0.1110 0.2537 -0.0099 -0.0941 -0.0068 156 PHE B CZ  
6767 N N   . ALA B 139 ? 0.2637 0.1390 0.2548 -0.0362 -0.0616 0.0149  157 ALA B N   
6768 C CA  . ALA B 139 ? 0.2294 0.1396 0.2377 -0.0488 -0.0778 0.0211  157 ALA B CA  
6769 C C   . ALA B 139 ? 0.2079 0.1410 0.2412 -0.0273 -0.0769 0.0268  157 ALA B C   
6770 O O   . ALA B 139 ? 0.2574 0.1429 0.2600 -0.0336 -0.0569 0.0193  157 ALA B O   
6771 C CB  . ALA B 139 ? 0.2435 0.1414 0.2489 -0.0578 -0.0509 0.0256  157 ALA B CB  
6777 N N   . PRO B 140 ? 0.2023 0.1447 0.2377 -0.0425 -0.0868 0.0268  158 PRO B N   
6778 C CA  . PRO B 140 ? 0.2107 0.1246 0.2434 -0.0419 -0.0799 0.0269  158 PRO B CA  
6779 C C   . PRO B 140 ? 0.2113 0.1230 0.2383 -0.0421 -0.0625 0.0134  158 PRO B C   
6780 O O   . PRO B 140 ? 0.2426 0.1335 0.2633 -0.0236 -0.0525 0.0162  158 PRO B O   
6781 C CB  . PRO B 140 ? 0.2220 0.1454 0.2344 -0.0394 -0.0747 0.0137  158 PRO B CB  
6782 C CG  . PRO B 140 ? 0.2282 0.1568 0.2476 -0.0320 -0.0669 0.0204  158 PRO B CG  
6783 C CD  . PRO B 140 ? 0.2089 0.1570 0.2499 -0.0167 -0.0804 0.0406  158 PRO B CD  
6791 N N   . ASP B 141 ? 0.2025 0.1212 0.2438 -0.0473 -0.0578 0.0243  159 ASP B N   
6792 C CA  . ASP B 141 ? 0.1872 0.1024 0.2394 -0.0303 -0.0469 0.0221  159 ASP B CA  
6793 C C   . ASP B 141 ? 0.2065 0.1234 0.2279 -0.0182 -0.0408 0.0278  159 ASP B C   
6794 O O   . ASP B 141 ? 0.2146 0.1104 0.2350 -0.0323 -0.0543 0.0204  159 ASP B O   
6795 C CB  . ASP B 141 ? 0.2200 0.1047 0.2255 -0.0333 -0.0888 0.0099  159 ASP B CB  
6796 C CG  . ASP B 141 ? 0.2224 0.1201 0.2363 -0.0488 -0.0835 0.0014  159 ASP B CG  
6797 O OD1 . ASP B 141 ? 0.2222 0.1276 0.2600 -0.0403 -0.0510 0.0018  159 ASP B OD1 
6798 O OD2 . ASP B 141 ? 0.2383 0.1478 0.2518 -0.0561 -0.0684 -0.0148 159 ASP B OD2 
6803 N N   . TYR B 142 ? 0.2040 0.1248 0.2274 -0.0268 -0.0803 0.0113  160 TYR B N   
6804 C CA  . TYR B 142 ? 0.2254 0.1446 0.2267 -0.0303 -0.0690 0.0175  160 TYR B CA  
6805 C C   . TYR B 142 ? 0.2185 0.1424 0.2233 -0.0382 -0.0684 0.0190  160 TYR B C   
6806 O O   . TYR B 142 ? 0.2373 0.1395 0.2392 -0.0169 -0.0647 0.0186  160 TYR B O   
6807 C CB  . TYR B 142 ? 0.2295 0.1382 0.2158 -0.0164 -0.0729 0.0019  160 TYR B CB  
6808 C CG  . TYR B 142 ? 0.2092 0.1493 0.2334 -0.0280 -0.0634 -0.0103 160 TYR B CG  
6809 C CD1 . TYR B 142 ? 0.2027 0.1630 0.2483 -0.0416 -0.0755 0.0006  160 TYR B CD1 
6810 C CD2 . TYR B 142 ? 0.2039 0.1463 0.2608 -0.0310 -0.0649 -0.0003 160 TYR B CD2 
6811 C CE1 . TYR B 142 ? 0.2076 0.1385 0.2453 -0.0353 -0.0478 0.0270  160 TYR B CE1 
6812 C CE2 . TYR B 142 ? 0.2106 0.1383 0.2569 -0.0439 -0.0557 0.0168  160 TYR B CE2 
6813 C CZ  . TYR B 142 ? 0.2172 0.1408 0.2603 -0.0199 -0.0495 0.0176  160 TYR B CZ  
6814 O OH  . TYR B 142 ? 0.2316 0.1432 0.2564 -0.0292 -0.0550 0.0252  160 TYR B OH  
6824 N N   . LYS B 143 ? 0.2161 0.1508 0.2185 -0.0340 -0.0651 0.0185  161 LYS B N   
6825 C CA  . LYS B 143 ? 0.2306 0.1613 0.2326 -0.0073 -0.0563 0.0163  161 LYS B CA  
6826 C C   . LYS B 143 ? 0.2499 0.1498 0.2033 -0.0078 -0.0507 -0.0124 161 LYS B C   
6827 O O   . LYS B 143 ? 0.2723 0.1906 0.2204 -0.0256 -0.0294 -0.0259 161 LYS B O   
6828 C CB  . LYS B 143 ? 0.2306 0.1754 0.2422 0.0098  -0.0386 0.0187  161 LYS B CB  
6829 C CG  . LYS B 143 ? 0.2326 0.2185 0.2515 0.0037  -0.0342 -0.0049 161 LYS B CG  
6830 C CD  . LYS B 143 ? 0.2218 0.2593 0.2724 0.0001  -0.0629 0.0069  161 LYS B CD  
6831 C CE  . LYS B 143 ? 0.2436 0.2678 0.2921 -0.0132 -0.0289 -0.0080 161 LYS B CE  
6832 N NZ  . LYS B 143 ? 0.2386 0.2465 0.2976 -0.0301 -0.0139 -0.0228 161 LYS B NZ  
6846 N N   . GLY B 144 ? 0.2447 0.1455 0.1970 -0.0145 -0.0532 -0.0019 162 GLY B N   
6847 C CA  . GLY B 144 ? 0.2526 0.1416 0.2039 -0.0431 -0.0426 0.0124  162 GLY B CA  
6848 C C   . GLY B 144 ? 0.2440 0.1374 0.2100 -0.0578 -0.0471 0.0244  162 GLY B C   
6849 O O   . GLY B 144 ? 0.2692 0.1543 0.2174 -0.0692 -0.0578 0.0144  162 GLY B O   
6853 N N   . THR B 145 ? 0.2242 0.1421 0.1981 -0.0454 -0.0350 0.0437  163 THR B N   
6854 C CA  . THR B 145 ? 0.2251 0.1537 0.2046 0.0043  -0.0382 0.0527  163 THR B CA  
6855 C C   . THR B 145 ? 0.2450 0.1784 0.2269 -0.0057 -0.0342 0.0295  163 THR B C   
6856 O O   . THR B 145 ? 0.2284 0.1677 0.2335 -0.0146 -0.0337 -0.0065 163 THR B O   
6857 C CB  . THR B 145 ? 0.2332 0.1567 0.2346 -0.0001 -0.0436 0.0525  163 THR B CB  
6858 O OG1 . THR B 145 ? 0.2310 0.1476 0.2170 -0.0094 -0.0421 0.0449  163 THR B OG1 
6859 C CG2 . THR B 145 ? 0.2546 0.1844 0.2367 0.0103  -0.0407 0.0350  163 THR B CG2 
6867 N N   . VAL B 146 ? 0.2569 0.2114 0.2378 -0.0151 -0.0475 0.0278  164 VAL B N   
6868 C CA  . VAL B 146 ? 0.2777 0.2115 0.2667 -0.0066 -0.0316 0.0409  164 VAL B CA  
6869 C C   . VAL B 146 ? 0.2894 0.2258 0.2690 -0.0207 -0.0419 0.0463  164 VAL B C   
6870 O O   . VAL B 146 ? 0.2778 0.2349 0.2688 -0.0014 -0.0498 0.0423  164 VAL B O   
6871 C CB  . VAL B 146 ? 0.2955 0.2219 0.2910 0.0114  -0.0256 0.0435  164 VAL B CB  
6872 C CG1 . VAL B 146 ? 0.2825 0.2322 0.2883 0.0206  -0.0306 0.0353  164 VAL B CG1 
6873 C CG2 . VAL B 146 ? 0.3116 0.2227 0.3097 0.0265  -0.0148 0.0454  164 VAL B CG2 
6883 N N   . LEU B 147 ? 0.2812 0.2404 0.2847 -0.0058 -0.0780 0.0633  165 LEU B N   
6884 C CA  . LEU B 147 ? 0.2849 0.2260 0.3019 -0.0233 -0.1080 0.0766  165 LEU B CA  
6885 C C   . LEU B 147 ? 0.3173 0.2475 0.3540 -0.0122 -0.1269 0.0856  165 LEU B C   
6886 O O   . LEU B 147 ? 0.3869 0.2482 0.3638 -0.0383 -0.1180 0.0472  165 LEU B O   
6887 C CB  . LEU B 147 ? 0.2760 0.2346 0.3138 -0.0071 -0.0897 0.0787  165 LEU B CB  
6888 C CG  . LEU B 147 ? 0.2659 0.2322 0.3214 -0.0071 -0.1065 0.0566  165 LEU B CG  
6889 C CD1 . LEU B 147 ? 0.3084 0.2401 0.3324 0.0102  -0.0947 0.0618  165 LEU B CD1 
6890 C CD2 . LEU B 147 ? 0.3258 0.2419 0.3509 -0.0047 -0.0507 0.0448  165 LEU B CD2 
6902 N N   . ALA B 148 ? 0.3249 0.2663 0.3876 -0.0197 -0.1175 0.0758  166 ALA B N   
6903 C CA  . ALA B 148 ? 0.3428 0.2927 0.4194 -0.0065 -0.1153 0.0626  166 ALA B CA  
6904 C C   . ALA B 148 ? 0.3691 0.3184 0.4198 -0.0219 -0.0895 0.0432  166 ALA B C   
6905 O O   . ALA B 148 ? 0.3856 0.3414 0.4231 -0.0409 -0.1038 0.0619  166 ALA B O   
6906 C CB  . ALA B 148 ? 0.3540 0.2972 0.4411 0.0020  -0.1298 0.0627  166 ALA B CB  
6912 N N   . GLY B 149 ? 0.3746 0.3072 0.3975 -0.0226 -0.0558 0.0489  167 GLY B N   
6913 C CA  . GLY B 149 ? 0.3793 0.2869 0.3609 -0.0158 -0.0116 0.0459  167 GLY B CA  
6914 C C   . GLY B 149 ? 0.3663 0.2676 0.3502 -0.0170 0.0067  0.0165  167 GLY B C   
6915 O O   . GLY B 149 ? 0.3542 0.2406 0.2958 -0.0163 -0.0062 -0.0044 167 GLY B O   
6919 N N   . PRO B 150 ? 0.3842 0.2943 0.3798 0.0029  0.0613  -0.0034 168 PRO B N   
6920 C CA  . PRO B 150 ? 0.3661 0.2926 0.3930 0.0324  0.0493  -0.0158 168 PRO B CA  
6921 C C   . PRO B 150 ? 0.3303 0.2732 0.3892 0.0324  0.0347  -0.0296 168 PRO B C   
6922 O O   . PRO B 150 ? 0.3246 0.2727 0.3844 0.0068  0.0109  -0.0511 168 PRO B O   
6923 C CB  . PRO B 150 ? 0.3871 0.3130 0.3992 0.0373  0.0697  -0.0087 168 PRO B CB  
6924 C CG  . PRO B 150 ? 0.4235 0.3117 0.3976 0.0335  0.0609  0.0025  168 PRO B CG  
6925 C CD  . PRO B 150 ? 0.4084 0.3063 0.3916 0.0124  0.0777  -0.0021 168 PRO B CD  
6933 N N   . LEU B 151 ? 0.3252 0.2642 0.4061 0.0424  0.0125  -0.0157 169 LEU B N   
6934 C CA  . LEU B 151 ? 0.3543 0.2796 0.3981 0.0421  0.0065  0.0205  169 LEU B CA  
6935 C C   . LEU B 151 ? 0.3760 0.2881 0.3866 0.0284  0.0011  0.0008  169 LEU B C   
6936 O O   . LEU B 151 ? 0.3718 0.2686 0.3752 0.0335  0.0380  0.0074  169 LEU B O   
6937 C CB  . LEU B 151 ? 0.3789 0.2985 0.4166 0.0415  0.0005  0.0638  169 LEU B CB  
6938 C CG  . LEU B 151 ? 0.3707 0.3080 0.4331 0.0556  -0.0238 0.0856  169 LEU B CG  
6939 C CD1 . LEU B 151 ? 0.3974 0.3184 0.4508 0.0738  -0.0086 0.0966  169 LEU B CD1 
6940 C CD2 . LEU B 151 ? 0.3463 0.3232 0.4437 0.0631  -0.0469 0.0947  169 LEU B CD2 
6952 N N   . ASP B 152 ? 0.4246 0.3295 0.4141 0.0139  -0.0016 -0.0203 170 ASP B N   
6953 C CA  . ASP B 152 ? 0.4946 0.3764 0.4297 0.0272  -0.0079 -0.0351 170 ASP B CA  
6954 C C   . ASP B 152 ? 0.4815 0.3806 0.4214 0.0128  -0.0187 -0.0391 170 ASP B C   
6955 O O   . ASP B 152 ? 0.4841 0.3928 0.4249 0.0090  -0.0415 -0.0559 170 ASP B O   
6956 C CB  . ASP B 152 ? 0.5819 0.4096 0.4672 0.0453  0.0079  -0.0416 170 ASP B CB  
6957 C CG  . ASP B 152 ? 0.6735 0.4559 0.5117 0.0407  0.0338  -0.0505 170 ASP B CG  
6958 O OD1 . ASP B 152 ? 0.7168 0.4773 0.5337 0.0304  0.0415  -0.0456 170 ASP B OD1 
6959 O OD2 . ASP B 152 ? 0.7012 0.4750 0.5335 0.0417  0.0488  -0.0529 170 ASP B OD2 
6964 N N   . ALA B 153 ? 0.4781 0.3779 0.4003 0.0087  -0.0062 -0.0213 171 ALA B N   
6965 C CA  . ALA B 153 ? 0.4914 0.3740 0.3813 -0.0012 0.0098  -0.0102 171 ALA B CA  
6966 C C   . ALA B 153 ? 0.5000 0.3669 0.3516 -0.0291 0.0103  -0.0055 171 ALA B C   
6967 O O   . ALA B 153 ? 0.5211 0.3726 0.3548 -0.0486 0.0244  0.0068  171 ALA B O   
6968 C CB  . ALA B 153 ? 0.4916 0.3691 0.3996 -0.0087 0.0202  -0.0083 171 ALA B CB  
6974 N N   . LEU B 154 ? 0.4923 0.3520 0.3311 -0.0589 0.0009  -0.0064 172 LEU B N   
6975 C CA  . LEU B 154 ? 0.4856 0.3334 0.3082 -0.0775 0.0106  -0.0085 172 LEU B CA  
6976 C C   . LEU B 154 ? 0.4620 0.3171 0.3113 -0.0845 0.0001  -0.0073 172 LEU B C   
6977 O O   . LEU B 154 ? 0.4701 0.3134 0.3284 -0.0816 0.0061  -0.0401 172 LEU B O   
6978 C CB  . LEU B 154 ? 0.5141 0.3195 0.2993 -0.0805 0.0313  -0.0026 172 LEU B CB  
6979 C CG  . LEU B 154 ? 0.5286 0.3006 0.3069 -0.1072 0.0492  -0.0054 172 LEU B CG  
6980 C CD1 . LEU B 154 ? 0.5544 0.3020 0.3250 -0.1056 0.0632  0.0004  172 LEU B CD1 
6981 C CD2 . LEU B 154 ? 0.5258 0.2912 0.2982 -0.1089 0.0674  0.0042  172 LEU B CD2 
6993 N N   . ALA B 155 ? 0.4557 0.3031 0.2755 -0.1051 -0.0418 0.0238  173 ALA B N   
6994 C CA  . ALA B 155 ? 0.4663 0.3003 0.2928 -0.0781 -0.0359 0.0305  173 ALA B CA  
6995 C C   . ALA B 155 ? 0.4323 0.2520 0.2488 -0.0532 -0.0437 0.0208  173 ALA B C   
6996 O O   . ALA B 155 ? 0.4297 0.2531 0.2725 -0.0830 -0.0472 0.0248  173 ALA B O   
6997 C CB  . ALA B 155 ? 0.4965 0.3301 0.3112 -0.0706 -0.0550 0.0256  173 ALA B CB  
7003 N N   . VAL B 156 ? 0.4071 0.2146 0.2318 -0.0361 -0.0499 0.0164  174 VAL B N   
7004 C CA  . VAL B 156 ? 0.3908 0.1670 0.2229 -0.0006 -0.0617 0.0162  174 VAL B CA  
7005 C C   . VAL B 156 ? 0.3929 0.1306 0.1992 -0.0166 -0.0672 0.0335  174 VAL B C   
7006 O O   . VAL B 156 ? 0.4632 0.1484 0.1762 -0.0048 -0.0546 0.0323  174 VAL B O   
7007 C CB  . VAL B 156 ? 0.3956 0.1670 0.2400 0.0256  -0.0683 0.0124  174 VAL B CB  
7008 C CG1 . VAL B 156 ? 0.3673 0.1900 0.2722 0.0153  -0.0792 0.0017  174 VAL B CG1 
7009 C CG2 . VAL B 156 ? 0.4455 0.1712 0.2283 0.0441  -0.0806 0.0380  174 VAL B CG2 
7019 N N   . SER B 157 ? 0.3512 0.1234 0.2129 -0.0232 -0.0426 0.0063  175 SER B N   
7020 C CA  . SER B 157 ? 0.3060 0.1178 0.2177 -0.0233 -0.0536 0.0038  175 SER B CA  
7021 C C   . SER B 157 ? 0.2530 0.0997 0.2158 0.0034  -0.0522 0.0060  175 SER B C   
7022 O O   . SER B 157 ? 0.2642 0.1105 0.2033 -0.0031 -0.0654 -0.0015 175 SER B O   
7023 C CB  . SER B 157 ? 0.3426 0.1879 0.2469 -0.0345 -0.0348 0.0066  175 SER B CB  
7024 O OG  . SER B 157 ? 0.3776 0.2417 0.2547 -0.0652 -0.0341 0.0065  175 SER B OG  
7030 N N   . ALA B 158 ? 0.2567 0.1024 0.2227 -0.0023 -0.0885 -0.0123 176 ALA B N   
7031 C CA  . ALA B 158 ? 0.2584 0.1010 0.2333 -0.0026 -0.0706 -0.0236 176 ALA B CA  
7032 C C   . ALA B 158 ? 0.2182 0.0914 0.2217 0.0117  -0.0515 -0.0146 176 ALA B C   
7033 O O   . ALA B 158 ? 0.2539 0.1012 0.2104 0.0079  -0.0574 0.0065  176 ALA B O   
7034 C CB  . ALA B 158 ? 0.2683 0.1241 0.2366 0.0244  -0.0673 -0.0165 176 ALA B CB  
7040 N N   . PRO B 159 ? 0.1921 0.1090 0.2282 0.0034  -0.0378 -0.0103 177 PRO B N   
7041 C CA  . PRO B 159 ? 0.1900 0.1059 0.2292 -0.0070 -0.0302 -0.0127 177 PRO B CA  
7042 C C   . PRO B 159 ? 0.2073 0.1011 0.2000 0.0015  -0.0316 -0.0148 177 PRO B C   
7043 O O   . PRO B 159 ? 0.1978 0.1230 0.1967 0.0029  -0.0231 -0.0073 177 PRO B O   
7044 C CB  . PRO B 159 ? 0.1724 0.1263 0.2214 -0.0172 -0.0397 0.0091  177 PRO B CB  
7045 C CG  . PRO B 159 ? 0.1879 0.1273 0.2299 -0.0209 -0.0282 -0.0071 177 PRO B CG  
7046 C CD  . PRO B 159 ? 0.1713 0.1289 0.2213 0.0077  -0.0451 -0.0062 177 PRO B CD  
7054 N N   . SER B 160 ? 0.2157 0.0875 0.2000 -0.0174 -0.0325 -0.0144 178 SER B N   
7055 C CA  . SER B 160 ? 0.2179 0.0925 0.2020 -0.0173 -0.0291 -0.0030 178 SER B CA  
7056 C C   . SER B 160 ? 0.2083 0.1068 0.1981 -0.0284 -0.0590 0.0015  178 SER B C   
7057 O O   . SER B 160 ? 0.2237 0.1065 0.1982 -0.0187 -0.0504 -0.0145 178 SER B O   
7058 C CB  . SER B 160 ? 0.1953 0.0892 0.2151 0.0130  -0.0182 -0.0102 178 SER B CB  
7059 O OG  . SER B 160 ? 0.2233 0.0869 0.2210 0.0217  -0.0232 -0.0231 178 SER B OG  
7065 N N   . VAL B 161 ? 0.2164 0.1149 0.1942 -0.0124 -0.0396 0.0088  179 VAL B N   
7066 C CA  . VAL B 161 ? 0.2081 0.1238 0.1985 -0.0113 -0.0741 0.0151  179 VAL B CA  
7067 C C   . VAL B 161 ? 0.1946 0.1118 0.2062 -0.0282 -0.0578 0.0007  179 VAL B C   
7068 O O   . VAL B 161 ? 0.2209 0.1332 0.2220 -0.0263 -0.0468 0.0118  179 VAL B O   
7069 C CB  . VAL B 161 ? 0.2733 0.1388 0.2362 0.0006  -0.0566 0.0154  179 VAL B CB  
7070 C CG1 . VAL B 161 ? 0.3012 0.1402 0.2189 -0.0224 -0.0434 0.0322  179 VAL B CG1 
7071 C CG2 . VAL B 161 ? 0.3167 0.1311 0.2477 0.0065  -0.0659 0.0385  179 VAL B CG2 
7081 N N   . TRP B 162 ? 0.2134 0.0924 0.2055 -0.0166 -0.0334 0.0094  180 TRP B N   
7082 C CA  . TRP B 162 ? 0.2289 0.0948 0.1910 -0.0096 -0.0371 -0.0042 180 TRP B CA  
7083 C C   . TRP B 162 ? 0.2181 0.1041 0.2153 -0.0008 -0.0232 0.0000  180 TRP B C   
7084 O O   . TRP B 162 ? 0.2006 0.1023 0.2446 -0.0133 -0.0094 -0.0167 180 TRP B O   
7085 C CB  . TRP B 162 ? 0.2433 0.1071 0.2052 -0.0123 -0.0234 -0.0114 180 TRP B CB  
7086 C CG  . TRP B 162 ? 0.2410 0.1239 0.2106 -0.0006 -0.0394 0.0095  180 TRP B CG  
7087 C CD1 . TRP B 162 ? 0.2451 0.1213 0.2111 -0.0019 -0.0303 0.0147  180 TRP B CD1 
7088 C CD2 . TRP B 162 ? 0.2059 0.1560 0.2389 -0.0122 -0.0164 0.0079  180 TRP B CD2 
7089 N NE1 . TRP B 162 ? 0.2423 0.1560 0.1999 -0.0140 -0.0601 0.0064  180 TRP B NE1 
7090 C CE2 . TRP B 162 ? 0.2366 0.1714 0.2337 -0.0163 -0.0320 -0.0104 180 TRP B CE2 
7091 C CE3 . TRP B 162 ? 0.2055 0.1740 0.2506 -0.0132 -0.0052 -0.0209 180 TRP B CE3 
7092 C CZ2 . TRP B 162 ? 0.2620 0.2115 0.2651 -0.0251 -0.0047 -0.0292 180 TRP B CZ2 
7093 C CZ3 . TRP B 162 ? 0.2343 0.2068 0.2769 -0.0272 0.0185  -0.0343 180 TRP B CZ3 
7094 C CH2 . TRP B 162 ? 0.2535 0.2169 0.2651 -0.0082 0.0230  -0.0372 180 TRP B CH2 
7105 N N   . GLN B 163 ? 0.1946 0.1072 0.2135 0.0076  -0.0108 0.0046  181 GLN B N   
7106 C CA  . GLN B 163 ? 0.1909 0.1220 0.2113 0.0008  -0.0370 -0.0116 181 GLN B CA  
7107 C C   . GLN B 163 ? 0.1816 0.1270 0.2040 0.0079  -0.0506 0.0180  181 GLN B C   
7108 O O   . GLN B 163 ? 0.2071 0.1289 0.1875 -0.0026 -0.0391 -0.0027 181 GLN B O   
7109 C CB  . GLN B 163 ? 0.1815 0.1182 0.2354 0.0092  -0.0388 0.0004  181 GLN B CB  
7110 C CG  . GLN B 163 ? 0.1855 0.0920 0.2232 0.0161  -0.0519 0.0002  181 GLN B CG  
7111 C CD  . GLN B 163 ? 0.2045 0.0935 0.2062 0.0088  -0.0362 -0.0085 181 GLN B CD  
7112 O OE1 . GLN B 163 ? 0.2206 0.1108 0.1954 0.0316  -0.0435 0.0005  181 GLN B OE1 
7113 N NE2 . GLN B 163 ? 0.1962 0.1284 0.2073 0.0235  -0.0196 -0.0130 181 GLN B NE2 
7122 N N   . GLN B 164 ? 0.1846 0.1264 0.2012 0.0024  -0.0374 0.0211  182 GLN B N   
7123 C CA  . GLN B 164 ? 0.1964 0.1160 0.2059 -0.0026 -0.0473 0.0205  182 GLN B CA  
7124 C C   . GLN B 164 ? 0.2112 0.1241 0.2197 -0.0044 -0.0544 0.0037  182 GLN B C   
7125 O O   . GLN B 164 ? 0.2285 0.1335 0.2280 -0.0261 -0.0401 -0.0043 182 GLN B O   
7126 C CB  . GLN B 164 ? 0.1844 0.1245 0.2347 -0.0074 -0.0253 0.0162  182 GLN B CB  
7127 C CG  . GLN B 164 ? 0.2148 0.1435 0.2535 -0.0097 -0.0345 0.0093  182 GLN B CG  
7128 C CD  . GLN B 164 ? 0.2363 0.1340 0.2673 -0.0124 -0.0416 0.0011  182 GLN B CD  
7129 O OE1 . GLN B 164 ? 0.2647 0.1695 0.2956 -0.0178 -0.0687 0.0011  182 GLN B OE1 
7130 N NE2 . GLN B 164 ? 0.1912 0.1146 0.2666 -0.0182 -0.0688 0.0039  182 GLN B NE2 
7139 N N   . THR B 165 ? 0.2212 0.1299 0.2111 -0.0181 -0.0174 -0.0016 183 THR B N   
7140 C CA  . THR B 165 ? 0.2085 0.1372 0.2154 -0.0232 -0.0177 0.0084  183 THR B CA  
7141 C C   . THR B 165 ? 0.2072 0.1307 0.2358 -0.0120 -0.0183 0.0039  183 THR B C   
7142 O O   . THR B 165 ? 0.2197 0.1402 0.2446 0.0121  -0.0081 0.0084  183 THR B O   
7143 C CB  . THR B 165 ? 0.2184 0.1643 0.2247 -0.0218 -0.0187 0.0201  183 THR B CB  
7144 O OG1 . THR B 165 ? 0.2121 0.2063 0.2300 -0.0193 -0.0640 -0.0041 183 THR B OG1 
7145 C CG2 . THR B 165 ? 0.2488 0.1543 0.2174 -0.0280 -0.0310 0.0177  183 THR B CG2 
7153 N N   . THR B 166 ? 0.2211 0.1350 0.2442 -0.0079 -0.0461 0.0247  184 THR B N   
7154 C CA  . THR B 166 ? 0.2217 0.1565 0.2619 -0.0055 -0.0305 0.0320  184 THR B CA  
7155 C C   . THR B 166 ? 0.2175 0.1641 0.2669 0.0039  -0.0170 -0.0019 184 THR B C   
7156 O O   . THR B 166 ? 0.2364 0.1738 0.2770 0.0315  -0.0189 -0.0116 184 THR B O   
7157 C CB  . THR B 166 ? 0.2314 0.1946 0.2934 -0.0187 -0.0455 0.0471  184 THR B CB  
7158 O OG1 . THR B 166 ? 0.2705 0.2081 0.3051 -0.0269 -0.0254 0.0535  184 THR B OG1 
7159 C CG2 . THR B 166 ? 0.2083 0.1993 0.2979 -0.0126 -0.0301 0.0529  184 THR B CG2 
7167 N N   . GLY B 167 ? 0.2166 0.1442 0.2617 -0.0024 0.0470  0.0198  185 GLY B N   
7168 C CA  . GLY B 167 ? 0.2563 0.1420 0.2642 0.0155  0.0394  0.0318  185 GLY B CA  
7169 C C   . GLY B 167 ? 0.2306 0.1297 0.2571 0.0165  0.0139  0.0220  185 GLY B C   
7170 O O   . GLY B 167 ? 0.2803 0.1268 0.2564 0.0392  0.0497  0.0232  185 GLY B O   
7174 N N   . SER B 168 ? 0.2061 0.1310 0.2423 0.0197  -0.0091 0.0153  186 SER B N   
7175 C CA  . SER B 168 ? 0.2033 0.1122 0.2237 0.0162  -0.0163 0.0200  186 SER B CA  
7176 C C   . SER B 168 ? 0.1848 0.1244 0.2291 0.0134  -0.0194 0.0162  186 SER B C   
7177 O O   . SER B 168 ? 0.1946 0.1476 0.2292 0.0017  -0.0014 0.0171  186 SER B O   
7178 C CB  . SER B 168 ? 0.1960 0.1160 0.2262 0.0017  -0.0093 0.0032  186 SER B CB  
7179 O OG  . SER B 168 ? 0.1854 0.1214 0.2315 -0.0015 -0.0172 0.0016  186 SER B OG  
7185 N N   . ALA B 169 ? 0.1860 0.1219 0.2315 0.0131  -0.0250 -0.0003 187 ALA B N   
7186 C CA  . ALA B 169 ? 0.1764 0.1243 0.2369 -0.0004 -0.0306 0.0057  187 ALA B CA  
7187 C C   . ALA B 169 ? 0.1783 0.1216 0.2202 0.0036  -0.0299 0.0018  187 ALA B C   
7188 O O   . ALA B 169 ? 0.1962 0.1149 0.2231 0.0117  -0.0371 -0.0033 187 ALA B O   
7189 C CB  . ALA B 169 ? 0.1955 0.1230 0.2451 -0.0343 -0.0454 -0.0020 187 ALA B CB  
7195 N N   . LEU B 170 ? 0.1969 0.1101 0.2107 0.0086  -0.0133 -0.0084 188 LEU B N   
7196 C CA  . LEU B 170 ? 0.1709 0.1062 0.1940 0.0027  -0.0100 0.0023  188 LEU B CA  
7197 C C   . LEU B 170 ? 0.1551 0.1108 0.1877 0.0022  -0.0376 0.0123  188 LEU B C   
7198 O O   . LEU B 170 ? 0.1765 0.1240 0.2017 0.0051  -0.0483 0.0115  188 LEU B O   
7199 C CB  . LEU B 170 ? 0.1809 0.1175 0.1923 0.0276  -0.0255 0.0034  188 LEU B CB  
7200 C CG  . LEU B 170 ? 0.2155 0.1447 0.1916 0.0219  -0.0180 -0.0193 188 LEU B CG  
7201 C CD1 . LEU B 170 ? 0.2231 0.1560 0.1954 0.0001  0.0335  -0.0479 188 LEU B CD1 
7202 C CD2 . LEU B 170 ? 0.2980 0.1715 0.2230 -0.0007 0.0171  -0.0215 188 LEU B CD2 
7214 N N   . THR B 171 ? 0.1792 0.1190 0.1768 -0.0102 -0.0245 0.0137  189 THR B N   
7215 C CA  . THR B 171 ? 0.1776 0.1304 0.2049 0.0061  -0.0229 0.0200  189 THR B CA  
7216 C C   . THR B 171 ? 0.1818 0.1205 0.2055 -0.0119 -0.0227 0.0198  189 THR B C   
7217 O O   . THR B 171 ? 0.1940 0.1307 0.2007 0.0095  -0.0321 -0.0077 189 THR B O   
7218 C CB  . THR B 171 ? 0.1888 0.1303 0.2370 0.0163  -0.0160 0.0022  189 THR B CB  
7219 O OG1 . THR B 171 ? 0.2089 0.1507 0.2368 0.0215  -0.0004 -0.0096 189 THR B OG1 
7220 C CG2 . THR B 171 ? 0.1983 0.1350 0.2527 -0.0301 -0.0251 0.0194  189 THR B CG2 
7228 N N   . THR B 172 ? 0.1966 0.1147 0.2169 0.0124  -0.0164 0.0090  190 THR B N   
7229 C CA  . THR B 172 ? 0.1873 0.1280 0.2350 0.0118  -0.0347 -0.0035 190 THR B CA  
7230 C C   . THR B 172 ? 0.1959 0.1353 0.2289 0.0116  -0.0536 0.0104  190 THR B C   
7231 O O   . THR B 172 ? 0.1874 0.1357 0.2360 0.0204  -0.0376 0.0363  190 THR B O   
7232 C CB  . THR B 172 ? 0.2221 0.1401 0.2442 0.0269  -0.0210 -0.0034 190 THR B CB  
7233 O OG1 . THR B 172 ? 0.2244 0.1394 0.2682 0.0055  -0.0171 -0.0098 190 THR B OG1 
7234 C CG2 . THR B 172 ? 0.2086 0.1351 0.2515 0.0397  -0.0088 -0.0024 190 THR B CG2 
7242 N N   . ALA B 173 ? 0.1917 0.1245 0.2091 -0.0011 -0.0576 -0.0026 191 ALA B N   
7243 C CA  . ALA B 173 ? 0.1901 0.1337 0.2269 0.0013  -0.0584 0.0070  191 ALA B CA  
7244 C C   . ALA B 173 ? 0.1733 0.1243 0.2236 0.0031  -0.0707 0.0022  191 ALA B C   
7245 O O   . ALA B 173 ? 0.2158 0.1293 0.2141 0.0042  -0.0565 -0.0087 191 ALA B O   
7246 C CB  . ALA B 173 ? 0.1801 0.1141 0.2443 0.0056  -0.0508 0.0097  191 ALA B CB  
7252 N N   . LEU B 174 ? 0.2015 0.1330 0.2131 -0.0149 -0.0395 0.0247  192 LEU B N   
7253 C CA  . LEU B 174 ? 0.1832 0.1314 0.2207 -0.0117 -0.0660 0.0171  192 LEU B CA  
7254 C C   . LEU B 174 ? 0.1777 0.1400 0.2376 -0.0102 -0.0567 0.0054  192 LEU B C   
7255 O O   . LEU B 174 ? 0.1828 0.1738 0.2502 0.0058  -0.0644 -0.0099 192 LEU B O   
7256 C CB  . LEU B 174 ? 0.1816 0.1202 0.2278 -0.0151 -0.0430 0.0022  192 LEU B CB  
7257 C CG  . LEU B 174 ? 0.2236 0.1440 0.2029 -0.0337 -0.0262 0.0168  192 LEU B CG  
7258 C CD1 . LEU B 174 ? 0.2427 0.1571 0.2100 -0.0235 -0.0235 0.0052  192 LEU B CD1 
7259 C CD2 . LEU B 174 ? 0.2648 0.1524 0.2135 -0.0255 -0.0540 0.0275  192 LEU B CD2 
7271 N N   . ARG B 175 ? 0.1651 0.1379 0.2372 -0.0088 -0.0178 0.0017  193 ARG B N   
7272 C CA  . ARG B 175 ? 0.1799 0.1692 0.2427 -0.0120 -0.0282 0.0153  193 ARG B CA  
7273 C C   . ARG B 175 ? 0.1970 0.1792 0.2414 -0.0020 -0.0674 0.0256  193 ARG B C   
7274 O O   . ARG B 175 ? 0.2397 0.1906 0.2421 -0.0074 -0.0418 0.0235  193 ARG B O   
7275 C CB  . ARG B 175 ? 0.1955 0.2015 0.2450 0.0114  -0.0254 0.0261  193 ARG B CB  
7276 C CG  . ARG B 175 ? 0.2380 0.2543 0.2760 0.0083  0.0046  0.0127  193 ARG B CG  
7277 C CD  . ARG B 175 ? 0.2157 0.2613 0.3126 0.0340  0.0075  -0.0110 193 ARG B CD  
7278 N NE  . ARG B 175 ? 0.3010 0.2766 0.3374 0.0515  -0.0063 0.0206  193 ARG B NE  
7279 C CZ  . ARG B 175 ? 0.3380 0.2641 0.3528 0.0496  -0.0256 0.0267  193 ARG B CZ  
7280 N NH1 . ARG B 175 ? 0.3455 0.2592 0.3484 0.0391  0.0064  0.0426  193 ARG B NH1 
7281 N NH2 . ARG B 175 ? 0.3666 0.2717 0.3764 0.0616  -0.0259 0.0229  193 ARG B NH2 
7295 N N   . ASN B 176 ? 0.2079 0.1645 0.2295 0.0212  -0.0481 0.0255  194 ASN B N   
7296 C CA  . ASN B 176 ? 0.1892 0.1802 0.2376 0.0195  -0.0519 0.0171  194 ASN B CA  
7297 C C   . ASN B 176 ? 0.2103 0.1964 0.2500 0.0248  -0.0596 0.0184  194 ASN B C   
7298 O O   . ASN B 176 ? 0.2527 0.2323 0.2667 0.0287  -0.0534 0.0226  194 ASN B O   
7299 C CB  . ASN B 176 ? 0.1912 0.1697 0.2512 -0.0063 -0.0413 0.0070  194 ASN B CB  
7300 C CG  . ASN B 176 ? 0.1882 0.1794 0.2705 -0.0231 -0.0294 0.0007  194 ASN B CG  
7301 O OD1 . ASN B 176 ? 0.2196 0.1757 0.3017 -0.0277 -0.0223 -0.0235 194 ASN B OD1 
7302 N ND2 . ASN B 176 ? 0.1865 0.1833 0.2563 -0.0173 -0.0447 0.0009  194 ASN B ND2 
7309 N N   . ALA B 177 ? 0.2021 0.1662 0.2416 0.0170  -0.0726 -0.0025 195 ALA B N   
7310 C CA  . ALA B 177 ? 0.2014 0.1575 0.2292 -0.0040 -0.0777 0.0099  195 ALA B CA  
7311 C C   . ALA B 177 ? 0.2501 0.1863 0.2288 -0.0209 -0.0679 0.0120  195 ALA B C   
7312 O O   . ALA B 177 ? 0.2969 0.2333 0.2361 -0.0515 -0.0540 -0.0076 195 ALA B O   
7313 C CB  . ALA B 177 ? 0.2177 0.1447 0.2464 -0.0005 -0.0592 -0.0063 195 ALA B CB  
7319 N N   . GLY B 178 ? 0.2545 0.1815 0.2347 -0.0278 -0.0743 0.0285  196 GLY B N   
7320 C CA  . GLY B 178 ? 0.3011 0.2004 0.2448 -0.0271 -0.0674 0.0394  196 GLY B CA  
7321 C C   . GLY B 178 ? 0.2721 0.2068 0.2620 -0.0230 -0.0629 0.0332  196 GLY B C   
7322 O O   . GLY B 178 ? 0.2703 0.2046 0.2649 -0.0195 -0.0700 0.0158  196 GLY B O   
7326 N N   . GLY B 179 ? 0.2515 0.1948 0.2691 -0.0253 -0.0766 0.0501  197 GLY B N   
7327 C CA  . GLY B 179 ? 0.2360 0.1990 0.2863 -0.0436 -0.0910 0.0599  197 GLY B CA  
7328 C C   . GLY B 179 ? 0.2392 0.1953 0.2903 -0.0388 -0.0776 0.0468  197 GLY B C   
7329 O O   . GLY B 179 ? 0.2410 0.1792 0.3009 -0.0151 -0.0802 0.0405  197 GLY B O   
7333 N N   . LEU B 180 ? 0.2460 0.1927 0.2840 -0.0450 -0.0764 0.0366  198 LEU B N   
7334 C CA  . LEU B 180 ? 0.2661 0.2126 0.2901 -0.0353 -0.0729 0.0076  198 LEU B CA  
7335 C C   . LEU B 180 ? 0.2460 0.2106 0.2756 -0.0129 -0.0857 0.0161  198 LEU B C   
7336 O O   . LEU B 180 ? 0.2352 0.2188 0.2685 -0.0383 -0.0681 0.0189  198 LEU B O   
7337 C CB  . LEU B 180 ? 0.3015 0.2402 0.2847 -0.0400 -0.0707 0.0065  198 LEU B CB  
7338 C CG  . LEU B 180 ? 0.3154 0.2473 0.2871 -0.0342 -0.1012 0.0118  198 LEU B CG  
7339 C CD1 . LEU B 180 ? 0.3547 0.2851 0.3087 -0.0642 -0.1057 -0.0040 198 LEU B CD1 
7340 C CD2 . LEU B 180 ? 0.3429 0.2267 0.2776 -0.0194 -0.1040 0.0253  198 LEU B CD2 
7352 N N   . THR B 181 ? 0.2390 0.1913 0.2747 -0.0245 -0.0960 0.0293  199 THR B N   
7353 C CA  . THR B 181 ? 0.2347 0.1946 0.2729 -0.0468 -0.1003 0.0224  199 THR B CA  
7354 C C   . THR B 181 ? 0.2489 0.1804 0.2637 -0.0512 -0.0910 0.0181  199 THR B C   
7355 O O   . THR B 181 ? 0.2585 0.1899 0.2800 -0.0593 -0.1151 0.0175  199 THR B O   
7356 C CB  . THR B 181 ? 0.2522 0.2099 0.2727 -0.0295 -0.0888 0.0315  199 THR B CB  
7357 O OG1 . THR B 181 ? 0.2807 0.2201 0.2757 -0.0449 -0.0661 0.0134  199 THR B OG1 
7358 C CG2 . THR B 181 ? 0.2512 0.2220 0.2502 -0.0193 -0.0941 0.0529  199 THR B CG2 
7366 N N   . GLN B 182 ? 0.2379 0.1741 0.2613 -0.0387 -0.0952 0.0424  200 GLN B N   
7367 C CA  . GLN B 182 ? 0.2637 0.1776 0.2470 -0.0268 -0.1066 0.0417  200 GLN B CA  
7368 C C   . GLN B 182 ? 0.2402 0.1889 0.2458 -0.0481 -0.1177 0.0335  200 GLN B C   
7369 O O   . GLN B 182 ? 0.2215 0.2206 0.2863 -0.0328 -0.0965 0.0318  200 GLN B O   
7370 C CB  . GLN B 182 ? 0.2621 0.1883 0.2603 -0.0466 -0.0975 0.0341  200 GLN B CB  
7371 C CG  . GLN B 182 ? 0.2549 0.2093 0.2682 -0.0486 -0.1095 0.0105  200 GLN B CG  
7372 C CD  . GLN B 182 ? 0.2618 0.2180 0.2848 -0.0406 -0.1036 0.0202  200 GLN B CD  
7373 O OE1 . GLN B 182 ? 0.2602 0.2144 0.2965 -0.0761 -0.1030 0.0252  200 GLN B OE1 
7374 N NE2 . GLN B 182 ? 0.2402 0.2252 0.2892 -0.0400 -0.0919 -0.0049 200 GLN B NE2 
7383 N N   . ILE B 183 ? 0.2632 0.1764 0.2290 -0.0451 -0.0890 0.0343  201 ILE B N   
7384 C CA  . ILE B 183 ? 0.2407 0.1797 0.2248 -0.0265 -0.1059 0.0072  201 ILE B CA  
7385 C C   . ILE B 183 ? 0.2499 0.1905 0.2340 -0.0091 -0.1271 -0.0025 201 ILE B C   
7386 O O   . ILE B 183 ? 0.3510 0.2136 0.2415 0.0187  -0.1187 -0.0191 201 ILE B O   
7387 C CB  . ILE B 183 ? 0.2349 0.1843 0.2466 -0.0270 -0.0698 0.0157  201 ILE B CB  
7388 C CG1 . ILE B 183 ? 0.2036 0.1964 0.2564 -0.0301 -0.0706 -0.0067 201 ILE B CG1 
7389 C CG2 . ILE B 183 ? 0.2490 0.1972 0.2316 -0.0451 -0.0397 0.0321  201 ILE B CG2 
7390 C CD1 . ILE B 183 ? 0.2157 0.1986 0.2893 -0.0708 -0.0613 -0.0307 201 ILE B CD1 
7402 N N   . VAL B 184 ? 0.2318 0.1777 0.2511 -0.0199 -0.0944 0.0020  202 VAL B N   
7403 C CA  . VAL B 184 ? 0.2530 0.1646 0.2530 -0.0154 -0.0930 0.0026  202 VAL B CA  
7404 C C   . VAL B 184 ? 0.2649 0.1711 0.2424 -0.0361 -0.0994 0.0051  202 VAL B C   
7405 O O   . VAL B 184 ? 0.2549 0.1627 0.2369 -0.0358 -0.0874 0.0077  202 VAL B O   
7406 C CB  . VAL B 184 ? 0.2700 0.1551 0.2595 -0.0020 -0.0856 -0.0127 202 VAL B CB  
7407 C CG1 . VAL B 184 ? 0.3040 0.1506 0.2759 -0.0065 -0.0436 -0.0257 202 VAL B CG1 
7408 C CG2 . VAL B 184 ? 0.2775 0.1558 0.2752 0.0000  -0.0951 -0.0050 202 VAL B CG2 
7418 N N   . PRO B 185 ? 0.2568 0.1738 0.2454 -0.0468 -0.1105 0.0097  203 PRO B N   
7419 C CA  . PRO B 185 ? 0.2588 0.1756 0.2422 -0.0512 -0.0972 0.0185  203 PRO B CA  
7420 C C   . PRO B 185 ? 0.2522 0.1793 0.2382 -0.0627 -0.0897 0.0101  203 PRO B C   
7421 O O   . PRO B 185 ? 0.2403 0.1869 0.2240 -0.0358 -0.0868 0.0100  203 PRO B O   
7422 C CB  . PRO B 185 ? 0.2799 0.1704 0.2460 -0.0649 -0.0886 0.0271  203 PRO B CB  
7423 C CG  . PRO B 185 ? 0.2829 0.1764 0.2424 -0.0686 -0.1022 0.0200  203 PRO B CG  
7424 C CD  . PRO B 185 ? 0.2728 0.1827 0.2488 -0.0541 -0.0994 -0.0097 203 PRO B CD  
7432 N N   . THR B 186 ? 0.2241 0.1798 0.2428 -0.0685 -0.0942 0.0184  204 THR B N   
7433 C CA  . THR B 186 ? 0.2600 0.1609 0.2451 -0.0548 -0.0791 0.0129  204 THR B CA  
7434 C C   . THR B 186 ? 0.2502 0.1549 0.2619 -0.0413 -0.1020 0.0296  204 THR B C   
7435 O O   . THR B 186 ? 0.2599 0.1707 0.2834 -0.0464 -0.0982 0.0367  204 THR B O   
7436 C CB  . THR B 186 ? 0.2671 0.1511 0.2392 -0.0306 -0.0675 0.0138  204 THR B CB  
7437 O OG1 . THR B 186 ? 0.2710 0.1584 0.2424 -0.0309 -0.0927 0.0195  204 THR B OG1 
7438 C CG2 . THR B 186 ? 0.2591 0.1539 0.2347 -0.0411 -0.0626 0.0183  204 THR B CG2 
7446 N N   . THR B 187 ? 0.2603 0.1333 0.2533 -0.0541 -0.1023 0.0273  205 THR B N   
7447 C CA  . THR B 187 ? 0.2631 0.1396 0.2704 -0.0636 -0.0918 0.0263  205 THR B CA  
7448 C C   . THR B 187 ? 0.2699 0.1297 0.2696 -0.0634 -0.0780 0.0426  205 THR B C   
7449 O O   . THR B 187 ? 0.2762 0.1405 0.2672 -0.0452 -0.1011 0.0382  205 THR B O   
7450 C CB  . THR B 187 ? 0.2549 0.1529 0.2875 -0.0562 -0.0883 0.0339  205 THR B CB  
7451 O OG1 . THR B 187 ? 0.2551 0.1575 0.2826 -0.0791 -0.1066 0.0320  205 THR B OG1 
7452 C CG2 . THR B 187 ? 0.2609 0.1899 0.3014 -0.0455 -0.0960 0.0191  205 THR B CG2 
7460 N N   . ASN B 188 ? 0.2362 0.1454 0.2614 -0.0393 -0.0921 0.0296  206 ASN B N   
7461 C CA  . ASN B 188 ? 0.2156 0.1520 0.2397 -0.0323 -0.0771 0.0480  206 ASN B CA  
7462 C C   . ASN B 188 ? 0.2430 0.1580 0.2744 -0.0643 -0.0664 0.0515  206 ASN B C   
7463 O O   . ASN B 188 ? 0.2674 0.1907 0.3036 -0.0664 -0.0787 0.0542  206 ASN B O   
7464 C CB  . ASN B 188 ? 0.2364 0.1527 0.2304 -0.0424 -0.0628 0.0475  206 ASN B CB  
7465 C CG  . ASN B 188 ? 0.2421 0.1588 0.2399 -0.0400 -0.0607 0.0298  206 ASN B CG  
7466 O OD1 . ASN B 188 ? 0.2377 0.1718 0.2379 -0.0302 -0.0503 0.0372  206 ASN B OD1 
7467 N ND2 . ASN B 188 ? 0.2606 0.1800 0.2356 -0.0303 -0.0685 0.0322  206 ASN B ND2 
7474 N N   A LEU B 189 ? 0.2457 0.1340 0.2676 -0.0734 -0.0721 0.0537  207 LEU B N   
7475 N N   B LEU B 189 ? 0.2585 0.1591 0.2740 -0.0688 -0.0591 0.0502  207 LEU B N   
7476 C CA  A LEU B 189 ? 0.2576 0.1344 0.2515 -0.0620 -0.0716 0.0445  207 LEU B CA  
7477 C CA  B LEU B 189 ? 0.2734 0.1646 0.2700 -0.0698 -0.0547 0.0451  207 LEU B CA  
7478 C C   A LEU B 189 ? 0.2633 0.1452 0.2520 -0.0686 -0.0702 0.0193  207 LEU B C   
7479 C C   B LEU B 189 ? 0.2735 0.1612 0.2676 -0.0682 -0.0573 0.0340  207 LEU B C   
7480 O O   A LEU B 189 ? 0.2762 0.1521 0.2523 -0.0504 -0.0524 0.0257  207 LEU B O   
7481 O O   B LEU B 189 ? 0.2741 0.1637 0.2670 -0.0613 -0.0554 0.0364  207 LEU B O   
7482 C CB  A LEU B 189 ? 0.2791 0.1227 0.2868 -0.0504 -0.0530 0.0376  207 LEU B CB  
7483 C CB  B LEU B 189 ? 0.2912 0.1726 0.2791 -0.0741 -0.0448 0.0460  207 LEU B CB  
7484 C CG  A LEU B 189 ? 0.3044 0.1198 0.3292 -0.0365 -0.0450 0.0197  207 LEU B CG  
7485 C CG  B LEU B 189 ? 0.3102 0.1821 0.2896 -0.0775 -0.0382 0.0443  207 LEU B CG  
7486 C CD1 A LEU B 189 ? 0.2956 0.1047 0.3414 -0.0171 -0.0471 0.0154  207 LEU B CD1 
7487 C CD1 B LEU B 189 ? 0.3250 0.1821 0.2949 -0.0843 -0.0363 0.0453  207 LEU B CD1 
7488 C CD2 A LEU B 189 ? 0.3457 0.1166 0.3472 -0.0480 -0.0447 0.0164  207 LEU B CD2 
7489 C CD2 B LEU B 189 ? 0.3165 0.1873 0.2922 -0.0770 -0.0348 0.0427  207 LEU B CD2 
7512 N N   . TYR B 190 ? 0.2777 0.1566 0.2685 -0.0674 -0.0565 0.0298  208 TYR B N   
7513 C CA  . TYR B 190 ? 0.2633 0.1497 0.2655 -0.0559 -0.0622 0.0331  208 TYR B CA  
7514 C C   . TYR B 190 ? 0.2704 0.1679 0.2895 -0.0595 -0.0433 0.0392  208 TYR B C   
7515 O O   . TYR B 190 ? 0.2716 0.1866 0.2819 -0.0845 -0.0482 0.0311  208 TYR B O   
7516 C CB  . TYR B 190 ? 0.2642 0.1559 0.2769 -0.0553 -0.0505 0.0404  208 TYR B CB  
7517 C CG  . TYR B 190 ? 0.2816 0.1841 0.2695 -0.0473 -0.0669 0.0586  208 TYR B CG  
7518 C CD1 . TYR B 190 ? 0.2783 0.1922 0.2795 -0.0780 -0.0759 0.0660  208 TYR B CD1 
7519 C CD2 . TYR B 190 ? 0.2680 0.2094 0.2984 -0.0290 -0.0423 0.0614  208 TYR B CD2 
7520 C CE1 . TYR B 190 ? 0.2813 0.2070 0.2985 -0.0867 -0.0616 0.0629  208 TYR B CE1 
7521 C CE2 . TYR B 190 ? 0.2521 0.2211 0.3051 -0.0569 -0.0597 0.0524  208 TYR B CE2 
7522 C CZ  . TYR B 190 ? 0.2366 0.2265 0.3173 -0.0700 -0.0864 0.0574  208 TYR B CZ  
7523 O OH  . TYR B 190 ? 0.2755 0.2371 0.3428 -0.0441 -0.0873 0.0722  208 TYR B OH  
7533 N N   . SER B 191 ? 0.2617 0.1494 0.2830 -0.0564 -0.0630 0.0532  209 SER B N   
7534 C CA  . SER B 191 ? 0.2982 0.1634 0.3064 -0.0556 -0.0301 0.0586  209 SER B CA  
7535 C C   . SER B 191 ? 0.3104 0.1639 0.3100 -0.0658 -0.0052 0.0485  209 SER B C   
7536 O O   . SER B 191 ? 0.3360 0.1593 0.3134 -0.0538 0.0059  0.0586  209 SER B O   
7537 C CB  . SER B 191 ? 0.3146 0.1717 0.3206 -0.0559 -0.0339 0.0602  209 SER B CB  
7538 O OG  . SER B 191 ? 0.3445 0.1851 0.3196 -0.0695 -0.0422 0.0696  209 SER B OG  
7544 N N   . ALA B 192 ? 0.2998 0.1770 0.3143 -0.0602 0.0070  0.0186  210 ALA B N   
7545 C CA  . ALA B 192 ? 0.3075 0.1903 0.3001 -0.0590 0.0120  0.0205  210 ALA B CA  
7546 C C   . ALA B 192 ? 0.3265 0.1843 0.2805 -0.0827 0.0185  0.0367  210 ALA B C   
7547 O O   . ALA B 192 ? 0.3496 0.1848 0.2692 -0.0948 0.0208  0.0327  210 ALA B O   
7548 C CB  . ALA B 192 ? 0.3174 0.1906 0.3096 -0.0564 0.0290  0.0148  210 ALA B CB  
7554 N N   . THR B 193 ? 0.3416 0.1921 0.2820 -0.0790 -0.0055 0.0581  211 THR B N   
7555 C CA  . THR B 193 ? 0.3634 0.1978 0.2811 -0.0685 -0.0248 0.0640  211 THR B CA  
7556 C C   . THR B 193 ? 0.3232 0.2056 0.2817 -0.0809 -0.0391 0.0733  211 THR B C   
7557 O O   . THR B 193 ? 0.3444 0.2376 0.2961 -0.0876 -0.0770 0.0907  211 THR B O   
7558 C CB  . THR B 193 ? 0.4053 0.1752 0.2774 -0.0808 0.0099  0.0632  211 THR B CB  
7559 O OG1 . THR B 193 ? 0.4520 0.1682 0.2828 -0.0534 0.0234  0.0509  211 THR B OG1 
7560 C CG2 . THR B 193 ? 0.4117 0.1769 0.2912 -0.0887 0.0144  0.0807  211 THR B CG2 
7568 N N   . ASP B 194 ? 0.3022 0.1905 0.2761 -0.0775 -0.0313 0.0606  212 ASP B N   
7569 C CA  . ASP B 194 ? 0.3238 0.1653 0.2719 -0.0802 -0.0280 0.0490  212 ASP B CA  
7570 C C   . ASP B 194 ? 0.3394 0.1744 0.2574 -0.0413 -0.0255 0.0594  212 ASP B C   
7571 O O   . ASP B 194 ? 0.3467 0.1951 0.2543 -0.0300 -0.0331 0.0329  212 ASP B O   
7572 C CB  . ASP B 194 ? 0.3455 0.1430 0.2659 -0.0649 -0.0214 0.0388  212 ASP B CB  
7573 C CG  . ASP B 194 ? 0.3365 0.1317 0.2378 -0.0337 -0.0221 0.0287  212 ASP B CG  
7574 O OD1 . ASP B 194 ? 0.3310 0.1308 0.2301 -0.0383 -0.0231 0.0202  212 ASP B OD1 
7575 O OD2 . ASP B 194 ? 0.3736 0.1271 0.2442 -0.0357 -0.0071 -0.0007 212 ASP B OD2 
7580 N N   . GLU B 195 ? 0.3242 0.1711 0.2535 -0.0477 -0.0570 0.0522  213 GLU B N   
7581 C CA  . GLU B 195 ? 0.3433 0.1724 0.2547 -0.0285 -0.0770 0.0485  213 GLU B CA  
7582 C C   . GLU B 195 ? 0.3374 0.1665 0.2575 -0.0238 -0.0708 0.0491  213 GLU B C   
7583 O O   . GLU B 195 ? 0.3431 0.1686 0.2629 -0.0161 -0.0524 0.0449  213 GLU B O   
7584 C CB  . GLU B 195 ? 0.3606 0.1697 0.2320 -0.0263 -0.0885 0.0310  213 GLU B CB  
7585 C CG  . GLU B 195 ? 0.3949 0.1821 0.2400 0.0083  -0.0763 0.0353  213 GLU B CG  
7586 C CD  . GLU B 195 ? 0.4129 0.1973 0.2730 0.0073  -0.0698 0.0272  213 GLU B CD  
7587 O OE1 . GLU B 195 ? 0.4238 0.1872 0.2560 -0.0089 -0.0521 0.0267  213 GLU B OE1 
7588 O OE2 . GLU B 195 ? 0.4117 0.2335 0.3036 -0.0007 -0.0670 0.0095  213 GLU B OE2 
7595 N N   . ILE B 196 ? 0.3215 0.1651 0.2669 -0.0203 -0.0619 0.0424  214 ILE B N   
7596 C CA  . ILE B 196 ? 0.2833 0.1598 0.2692 -0.0191 -0.0837 0.0372  214 ILE B CA  
7597 C C   . ILE B 196 ? 0.2718 0.1452 0.2644 -0.0092 -0.0415 0.0499  214 ILE B C   
7598 O O   . ILE B 196 ? 0.2847 0.1288 0.2622 -0.0136 -0.0343 0.0507  214 ILE B O   
7599 C CB  . ILE B 196 ? 0.3339 0.1664 0.2706 -0.0343 -0.0801 0.0278  214 ILE B CB  
7600 C CG1 . ILE B 196 ? 0.3620 0.1767 0.2833 -0.0215 -0.0878 0.0503  214 ILE B CG1 
7601 C CG2 . ILE B 196 ? 0.3140 0.1803 0.2335 -0.0585 -0.0896 0.0277  214 ILE B CG2 
7602 C CD1 . ILE B 196 ? 0.3850 0.1945 0.3221 -0.0251 -0.0765 0.0543  214 ILE B CD1 
7614 N N   . VAL B 197 ? 0.2625 0.1515 0.2551 -0.0212 -0.0425 0.0459  215 VAL B N   
7615 C CA  . VAL B 197 ? 0.2397 0.1545 0.2305 -0.0094 -0.0421 0.0548  215 VAL B CA  
7616 C C   . VAL B 197 ? 0.2511 0.1694 0.2375 -0.0168 -0.0390 0.0365  215 VAL B C   
7617 O O   . VAL B 197 ? 0.2682 0.1739 0.2392 -0.0295 -0.0392 0.0222  215 VAL B O   
7618 C CB  . VAL B 197 ? 0.2205 0.1484 0.2297 -0.0098 -0.0469 0.0349  215 VAL B CB  
7619 C CG1 . VAL B 197 ? 0.2520 0.1666 0.2331 -0.0166 -0.0412 0.0150  215 VAL B CG1 
7620 C CG2 . VAL B 197 ? 0.2240 0.1557 0.2134 -0.0181 -0.0554 0.0228  215 VAL B CG2 
7630 N N   . GLN B 198 ? 0.2313 0.1754 0.2415 -0.0001 -0.0225 0.0291  216 GLN B N   
7631 C CA  . GLN B 198 ? 0.2276 0.1891 0.2544 -0.0079 -0.0125 0.0616  216 GLN B CA  
7632 C C   . GLN B 198 ? 0.2429 0.1869 0.2920 -0.0098 -0.0009 0.0558  216 GLN B C   
7633 O O   . GLN B 198 ? 0.2361 0.1687 0.2820 -0.0350 0.0055  0.0707  216 GLN B O   
7634 C CB  . GLN B 198 ? 0.2508 0.1944 0.2655 -0.0177 0.0031  0.0835  216 GLN B CB  
7635 C CG  . GLN B 198 ? 0.2835 0.1975 0.2672 -0.0395 -0.0121 0.0594  216 GLN B CG  
7636 C CD  . GLN B 198 ? 0.2695 0.2000 0.2712 -0.0505 -0.0066 0.0539  216 GLN B CD  
7637 O OE1 . GLN B 198 ? 0.2632 0.1971 0.2734 -0.0523 -0.0124 0.0524  216 GLN B OE1 
7638 N NE2 . GLN B 198 ? 0.2848 0.2010 0.2719 -0.0664 -0.0229 0.0426  216 GLN B NE2 
7647 N N   . PRO B 199 ? 0.2364 0.1953 0.3150 -0.0039 -0.0260 0.0526  217 PRO B N   
7648 C CA  . PRO B 199 ? 0.2342 0.2042 0.3122 -0.0006 -0.0243 0.0300  217 PRO B CA  
7649 C C   . PRO B 199 ? 0.2445 0.1865 0.2909 -0.0196 -0.0141 0.0296  217 PRO B C   
7650 O O   . PRO B 199 ? 0.2762 0.1630 0.2850 0.0104  -0.0231 0.0352  217 PRO B O   
7651 C CB  . PRO B 199 ? 0.2432 0.2191 0.3292 0.0042  -0.0243 0.0240  217 PRO B CB  
7652 C CG  . PRO B 199 ? 0.2325 0.2186 0.3347 0.0071  -0.0131 0.0406  217 PRO B CG  
7653 C CD  . PRO B 199 ? 0.2487 0.2045 0.3238 -0.0153 -0.0080 0.0426  217 PRO B CD  
7661 N N   . GLN B 200 ? 0.2760 0.2086 0.2995 -0.0262 0.0050  0.0444  218 GLN B N   
7662 C CA  . GLN B 200 ? 0.2534 0.2076 0.2821 -0.0485 0.0040  0.0548  218 GLN B CA  
7663 C C   . GLN B 200 ? 0.2479 0.2244 0.3165 -0.0511 0.0292  0.0532  218 GLN B C   
7664 O O   . GLN B 200 ? 0.2880 0.2280 0.3155 -0.0481 0.0231  0.0308  218 GLN B O   
7665 C CB  . GLN B 200 ? 0.2508 0.2067 0.2726 -0.0389 -0.0225 0.0558  218 GLN B CB  
7666 C CG  . GLN B 200 ? 0.2490 0.2019 0.2689 -0.0342 -0.0432 0.0361  218 GLN B CG  
7667 C CD  . GLN B 200 ? 0.2597 0.2006 0.2509 -0.0455 -0.0569 0.0370  218 GLN B CD  
7668 O OE1 . GLN B 200 ? 0.2487 0.2076 0.2658 -0.0237 -0.0656 0.0390  218 GLN B OE1 
7669 N NE2 . GLN B 200 ? 0.2808 0.1856 0.2218 -0.0607 -0.0572 0.0282  218 GLN B NE2 
7678 N N   . VAL B 201 ? 0.2579 0.2325 0.3303 -0.0567 0.0396  0.0538  219 VAL B N   
7679 C CA  . VAL B 201 ? 0.2781 0.2496 0.3440 -0.0639 0.0529  0.0679  219 VAL B CA  
7680 C C   . VAL B 201 ? 0.2837 0.2658 0.3702 -0.0752 0.0531  0.0765  219 VAL B C   
7681 O O   . VAL B 201 ? 0.3127 0.2766 0.3889 -0.0918 0.0528  0.0598  219 VAL B O   
7682 C CB  . VAL B 201 ? 0.3018 0.2655 0.3321 -0.0331 0.0479  0.0579  219 VAL B CB  
7683 C CG1 . VAL B 201 ? 0.3291 0.2728 0.3239 -0.0219 0.0550  0.0481  219 VAL B CG1 
7684 C CG2 . VAL B 201 ? 0.3342 0.2835 0.3527 -0.0516 0.0653  0.0418  219 VAL B CG2 
7694 N N   . SER B 202 ? 0.2529 0.2750 0.3887 -0.0543 0.0234  0.0897  220 SER B N   
7695 C CA  . SER B 202 ? 0.2313 0.2865 0.4104 -0.0707 0.0117  0.0823  220 SER B CA  
7696 C C   . SER B 202 ? 0.2316 0.2825 0.4185 -0.0743 0.0065  0.0666  220 SER B C   
7697 O O   . SER B 202 ? 0.2423 0.2904 0.4182 -0.0702 0.0108  0.0452  220 SER B O   
7698 C CB  . SER B 202 ? 0.2489 0.3030 0.4126 -0.0723 -0.0026 0.0991  220 SER B CB  
7699 O OG  . SER B 202 ? 0.2807 0.3240 0.4283 -0.0746 -0.0164 0.0920  220 SER B OG  
7705 N N   . ASN B 203 ? 0.2419 0.2710 0.4296 -0.0821 0.0004  0.0520  221 ASN B N   
7706 C CA  . ASN B 203 ? 0.2448 0.2774 0.4394 -0.0723 -0.0229 0.0556  221 ASN B CA  
7707 C C   . ASN B 203 ? 0.2551 0.2774 0.4375 -0.0659 -0.0234 0.0532  221 ASN B C   
7708 O O   . ASN B 203 ? 0.2782 0.2705 0.4404 -0.0919 -0.0416 0.0482  221 ASN B O   
7709 C CB  . ASN B 203 ? 0.2627 0.2782 0.4506 -0.0884 -0.0285 0.0532  221 ASN B CB  
7710 C CG  . ASN B 203 ? 0.2468 0.2803 0.4545 -0.1352 -0.0465 0.0368  221 ASN B CG  
7711 O OD1 . ASN B 203 ? 0.2964 0.2957 0.4647 -0.1237 -0.0379 0.0335  221 ASN B OD1 
7712 N ND2 . ASN B 203 ? 0.2665 0.2800 0.4642 -0.1297 -0.0305 0.0246  221 ASN B ND2 
7719 N N   . SER B 204 ? 0.2318 0.2687 0.4221 -0.0621 -0.0293 0.0525  222 SER B N   
7720 C CA  . SER B 204 ? 0.2065 0.2755 0.4112 -0.0382 -0.0412 0.0606  222 SER B CA  
7721 C C   . SER B 204 ? 0.1854 0.2612 0.3885 -0.0511 -0.0486 0.0617  222 SER B C   
7722 O O   . SER B 204 ? 0.1928 0.2593 0.3730 -0.0528 -0.0305 0.0809  222 SER B O   
7723 C CB  . SER B 204 ? 0.2339 0.2960 0.4233 -0.0383 -0.0404 0.0589  222 SER B CB  
7724 O OG  . SER B 204 ? 0.2767 0.3009 0.4357 -0.0532 -0.0215 0.0464  222 SER B OG  
7730 N N   . PRO B 205 ? 0.1958 0.2566 0.3880 -0.0559 -0.0442 0.0490  223 PRO B N   
7731 C CA  . PRO B 205 ? 0.2034 0.2604 0.3885 -0.0336 -0.0459 0.0461  223 PRO B CA  
7732 C C   . PRO B 205 ? 0.2289 0.2589 0.3781 -0.0505 -0.0373 0.0568  223 PRO B C   
7733 O O   . PRO B 205 ? 0.2357 0.2639 0.3708 -0.0566 -0.0252 0.0564  223 PRO B O   
7734 C CB  . PRO B 205 ? 0.2187 0.2652 0.3869 -0.0251 -0.0397 0.0423  223 PRO B CB  
7735 C CG  . PRO B 205 ? 0.2313 0.2698 0.3922 -0.0281 -0.0390 0.0474  223 PRO B CG  
7736 C CD  . PRO B 205 ? 0.2232 0.2599 0.3879 -0.0432 -0.0439 0.0549  223 PRO B CD  
7744 N N   . LEU B 206 ? 0.2445 0.2513 0.3781 -0.0609 -0.0330 0.0526  224 LEU B N   
7745 C CA  . LEU B 206 ? 0.2337 0.2420 0.3779 -0.0528 -0.0352 0.0531  224 LEU B CA  
7746 C C   . LEU B 206 ? 0.2223 0.2304 0.3599 -0.0390 -0.0287 0.0404  224 LEU B C   
7747 O O   . LEU B 206 ? 0.2450 0.2253 0.3649 -0.0430 -0.0442 0.0286  224 LEU B O   
7748 C CB  . LEU B 206 ? 0.2229 0.2245 0.3915 -0.0460 -0.0213 0.0765  224 LEU B CB  
7749 C CG  . LEU B 206 ? 0.2493 0.2450 0.4305 -0.0667 -0.0087 0.0702  224 LEU B CG  
7750 C CD1 . LEU B 206 ? 0.2297 0.2568 0.4368 -0.0587 -0.0063 0.0695  224 LEU B CD1 
7751 C CD2 . LEU B 206 ? 0.2963 0.2392 0.4544 -0.0817 0.0112  0.0653  224 LEU B CD2 
7763 N N   . ASP B 207 ? 0.2091 0.2391 0.3240 -0.0444 -0.0180 0.0113  225 ASP B N   
7764 C CA  . ASP B 207 ? 0.2073 0.2171 0.2939 -0.0329 -0.0273 0.0369  225 ASP B CA  
7765 C C   . ASP B 207 ? 0.2044 0.1990 0.2589 -0.0496 -0.0339 0.0364  225 ASP B C   
7766 O O   . ASP B 207 ? 0.2147 0.2051 0.2474 -0.0337 -0.0290 0.0329  225 ASP B O   
7767 C CB  . ASP B 207 ? 0.2254 0.2371 0.3028 -0.0550 -0.0318 0.0483  225 ASP B CB  
7768 C CG  . ASP B 207 ? 0.2467 0.2571 0.3140 -0.0558 -0.0224 0.0513  225 ASP B CG  
7769 O OD1 . ASP B 207 ? 0.2696 0.2794 0.3032 -0.0846 -0.0116 0.0541  225 ASP B OD1 
7770 O OD2 . ASP B 207 ? 0.2455 0.2534 0.3202 -0.0702 -0.0416 0.0471  225 ASP B OD2 
7775 N N   . SER B 208 ? 0.2106 0.1812 0.2442 -0.0569 -0.0398 0.0370  226 SER B N   
7776 C CA  . SER B 208 ? 0.2198 0.1682 0.2485 -0.0354 -0.0746 0.0259  226 SER B CA  
7777 C C   . SER B 208 ? 0.2139 0.1460 0.2566 -0.0416 -0.0613 0.0201  226 SER B C   
7778 O O   . SER B 208 ? 0.2178 0.1533 0.2546 -0.0130 -0.0476 0.0275  226 SER B O   
7779 C CB  . SER B 208 ? 0.2335 0.1627 0.2548 -0.0388 -0.0553 0.0183  226 SER B CB  
7780 O OG  . SER B 208 ? 0.2372 0.1544 0.2218 -0.0328 -0.0589 0.0288  226 SER B OG  
7786 N N   . SER B 209 ? 0.2333 0.1692 0.2759 -0.0655 -0.0542 0.0238  227 SER B N   
7787 C CA  . SER B 209 ? 0.2480 0.1674 0.2620 -0.0522 -0.0645 0.0359  227 SER B CA  
7788 C C   . SER B 209 ? 0.2319 0.1826 0.2446 -0.0551 -0.0893 0.0175  227 SER B C   
7789 O O   . SER B 209 ? 0.2559 0.1969 0.2315 -0.0654 -0.0546 0.0319  227 SER B O   
7790 C CB  . SER B 209 ? 0.2799 0.1463 0.2522 -0.0444 -0.0778 0.0121  227 SER B CB  
7791 O OG  . SER B 209 ? 0.2931 0.1483 0.2316 -0.0449 -0.0769 0.0204  227 SER B OG  
7797 N N   . TYR B 210 ? 0.2402 0.1692 0.2687 -0.0341 -0.0989 0.0174  228 TYR B N   
7798 C CA  . TYR B 210 ? 0.2246 0.2072 0.2870 -0.0078 -0.0884 0.0347  228 TYR B CA  
7799 C C   . TYR B 210 ? 0.2276 0.1862 0.2640 -0.0183 -0.0884 0.0404  228 TYR B C   
7800 O O   . TYR B 210 ? 0.2771 0.1948 0.2710 -0.0278 -0.0777 0.0336  228 TYR B O   
7801 C CB  . TYR B 210 ? 0.2438 0.2594 0.3180 -0.0284 -0.1135 0.0345  228 TYR B CB  
7802 C CG  . TYR B 210 ? 0.2628 0.3008 0.3428 -0.0344 -0.1101 0.0370  228 TYR B CG  
7803 C CD1 . TYR B 210 ? 0.2546 0.3270 0.3391 -0.0317 -0.1411 0.0172  228 TYR B CD1 
7804 C CD2 . TYR B 210 ? 0.2606 0.3252 0.3666 -0.0485 -0.1213 0.0365  228 TYR B CD2 
7805 C CE1 . TYR B 210 ? 0.2743 0.3454 0.3745 -0.0504 -0.1282 0.0165  228 TYR B CE1 
7806 C CE2 . TYR B 210 ? 0.2689 0.3500 0.3858 -0.0409 -0.1043 0.0367  228 TYR B CE2 
7807 C CZ  . TYR B 210 ? 0.2697 0.3599 0.3903 -0.0413 -0.1274 0.0246  228 TYR B CZ  
7808 O OH  . TYR B 210 ? 0.3079 0.3772 0.4092 -0.0676 -0.1181 -0.0084 228 TYR B OH  
7818 N N   . LEU B 211 ? 0.2272 0.1808 0.2560 -0.0239 -0.0687 0.0265  229 LEU B N   
7819 C CA  . LEU B 211 ? 0.2292 0.1812 0.2618 -0.0309 -0.0723 0.0295  229 LEU B CA  
7820 C C   . LEU B 211 ? 0.2211 0.1891 0.2715 -0.0480 -0.0809 0.0465  229 LEU B C   
7821 O O   . LEU B 211 ? 0.2545 0.1889 0.2616 -0.0518 -0.0545 0.0246  229 LEU B O   
7822 C CB  . LEU B 211 ? 0.2516 0.1840 0.2741 -0.0499 -0.0509 0.0139  229 LEU B CB  
7823 C CG  . LEU B 211 ? 0.2245 0.1775 0.2767 -0.0418 -0.0560 0.0081  229 LEU B CG  
7824 C CD1 . LEU B 211 ? 0.2368 0.1767 0.2664 -0.0282 -0.0512 0.0096  229 LEU B CD1 
7825 C CD2 . LEU B 211 ? 0.2008 0.1684 0.2801 -0.0169 -0.0646 -0.0013 229 LEU B CD2 
7837 N N   . PHE B 212 ? 0.2215 0.2211 0.2753 -0.0259 -0.0968 0.0532  230 PHE B N   
7838 C CA  . PHE B 212 ? 0.2153 0.2325 0.2794 -0.0343 -0.1099 0.0520  230 PHE B CA  
7839 C C   . PHE B 212 ? 0.2392 0.2471 0.2769 -0.0472 -0.0786 0.0407  230 PHE B C   
7840 O O   . PHE B 212 ? 0.2392 0.2533 0.2550 -0.0610 -0.0822 0.0342  230 PHE B O   
7841 C CB  . PHE B 212 ? 0.2520 0.2367 0.3032 -0.0315 -0.0806 0.0803  230 PHE B CB  
7842 C CG  . PHE B 212 ? 0.2767 0.2786 0.3528 -0.0283 -0.0493 0.0529  230 PHE B CG  
7843 C CD1 . PHE B 212 ? 0.2885 0.2946 0.3770 -0.0412 -0.0130 0.0414  230 PHE B CD1 
7844 C CD2 . PHE B 212 ? 0.2891 0.2983 0.3690 -0.0138 -0.0557 0.0347  230 PHE B CD2 
7845 C CE1 . PHE B 212 ? 0.3022 0.3030 0.3866 -0.0340 0.0065  0.0408  230 PHE B CE1 
7846 C CE2 . PHE B 212 ? 0.2975 0.3159 0.3793 -0.0065 -0.0392 0.0384  230 PHE B CE2 
7847 C CZ  . PHE B 212 ? 0.3057 0.3079 0.3760 -0.0314 -0.0105 0.0463  230 PHE B CZ  
7857 N N   . ASN B 213 ? 0.2227 0.2553 0.2857 -0.0574 -0.0908 0.0192  231 ASN B N   
7858 C CA  . ASN B 213 ? 0.2161 0.2599 0.2717 -0.0350 -0.1142 0.0349  231 ASN B CA  
7859 C C   . ASN B 213 ? 0.2238 0.2540 0.2846 -0.0495 -0.1138 0.0215  231 ASN B C   
7860 O O   . ASN B 213 ? 0.2674 0.2638 0.3085 -0.0759 -0.0696 0.0265  231 ASN B O   
7861 C CB  . ASN B 213 ? 0.2330 0.2614 0.2877 -0.0305 -0.1030 0.0369  231 ASN B CB  
7862 C CG  . ASN B 213 ? 0.2528 0.2809 0.2980 -0.0410 -0.0878 0.0202  231 ASN B CG  
7863 O OD1 . ASN B 213 ? 0.2617 0.3167 0.3234 -0.0374 -0.0613 0.0147  231 ASN B OD1 
7864 N ND2 . ASN B 213 ? 0.2863 0.2507 0.3031 -0.0389 -0.0709 0.0140  231 ASN B ND2 
7871 N N   . GLY B 214 ? 0.2159 0.2395 0.2824 -0.0485 -0.1137 0.0282  232 GLY B N   
7872 C CA  . GLY B 214 ? 0.2132 0.2238 0.2856 -0.0653 -0.1124 0.0263  232 GLY B CA  
7873 C C   . GLY B 214 ? 0.2538 0.2263 0.2923 -0.0853 -0.0925 0.0321  232 GLY B C   
7874 O O   . GLY B 214 ? 0.2802 0.2169 0.3138 -0.0793 -0.0839 0.0382  232 GLY B O   
7878 N N   . LYS B 215 ? 0.2828 0.2150 0.2830 -0.1009 -0.0745 0.0461  233 LYS B N   
7879 C CA  . LYS B 215 ? 0.2904 0.2300 0.2918 -0.0994 -0.0691 0.0538  233 LYS B CA  
7880 C C   . LYS B 215 ? 0.2658 0.2308 0.2833 -0.0797 -0.0706 0.0525  233 LYS B C   
7881 O O   . LYS B 215 ? 0.2583 0.2439 0.2852 -0.0833 -0.0788 0.0379  233 LYS B O   
7882 C CB  . LYS B 215 ? 0.2830 0.2253 0.3051 -0.1156 -0.0672 0.0383  233 LYS B CB  
7883 C CG  . LYS B 215 ? 0.2641 0.2336 0.3321 -0.1319 -0.0493 0.0352  233 LYS B CG  
7884 C CD  . LYS B 215 ? 0.3014 0.2488 0.3646 -0.1471 -0.0226 0.0345  233 LYS B CD  
7885 C CE  . LYS B 215 ? 0.3125 0.2639 0.3945 -0.1673 -0.0097 0.0364  233 LYS B CE  
7886 N NZ  . LYS B 215 ? 0.3606 0.2765 0.4350 -0.1467 -0.0074 0.0349  233 LYS B NZ  
7900 N N   . ASN B 216 ? 0.2532 0.2287 0.3057 -0.0688 -0.0549 0.0592  234 ASN B N   
7901 C CA  . ASN B 216 ? 0.2281 0.2197 0.2932 -0.0899 -0.0601 0.0582  234 ASN B CA  
7902 C C   . ASN B 216 ? 0.2747 0.2177 0.2993 -0.1026 -0.0439 0.0649  234 ASN B C   
7903 O O   . ASN B 216 ? 0.3153 0.2277 0.3107 -0.1106 -0.0341 0.0628  234 ASN B O   
7904 C CB  . ASN B 216 ? 0.2248 0.2303 0.3018 -0.0694 -0.0551 0.0552  234 ASN B CB  
7905 C CG  . ASN B 216 ? 0.2166 0.2225 0.2926 -0.0564 -0.0696 0.0444  234 ASN B CG  
7906 O OD1 . ASN B 216 ? 0.2117 0.2140 0.2933 -0.0505 -0.0833 0.0383  234 ASN B OD1 
7907 N ND2 . ASN B 216 ? 0.2513 0.2482 0.2971 -0.0518 -0.0693 0.0348  234 ASN B ND2 
7914 N N   . VAL B 217 ? 0.2827 0.2017 0.3121 -0.0817 -0.0511 0.0606  235 VAL B N   
7915 C CA  . VAL B 217 ? 0.2895 0.2019 0.3025 -0.0974 -0.0572 0.0434  235 VAL B CA  
7916 C C   . VAL B 217 ? 0.2952 0.2019 0.3010 -0.0759 -0.0722 0.0456  235 VAL B C   
7917 O O   . VAL B 217 ? 0.3008 0.2062 0.2996 -0.0863 -0.0723 0.0440  235 VAL B O   
7918 C CB  . VAL B 217 ? 0.3172 0.2008 0.3036 -0.0762 -0.0630 0.0426  235 VAL B CB  
7919 C CG1 . VAL B 217 ? 0.3269 0.1945 0.2985 -0.0849 -0.0609 0.0427  235 VAL B CG1 
7920 C CG2 . VAL B 217 ? 0.3255 0.1933 0.3036 -0.0594 -0.0758 0.0572  235 VAL B CG2 
7930 N N   . GLN B 218 ? 0.3051 0.1925 0.3115 -0.0586 -0.0742 0.0589  236 GLN B N   
7931 C CA  . GLN B 218 ? 0.3102 0.1917 0.3333 -0.0573 -0.0500 0.0606  236 GLN B CA  
7932 C C   . GLN B 218 ? 0.3350 0.1881 0.3320 -0.0752 -0.0495 0.0565  236 GLN B C   
7933 O O   . GLN B 218 ? 0.3494 0.1760 0.3454 -0.0687 -0.0572 0.0490  236 GLN B O   
7934 C CB  . GLN B 218 ? 0.3176 0.2008 0.3548 -0.0842 -0.0287 0.0650  236 GLN B CB  
7935 C CG  . GLN B 218 ? 0.3114 0.2101 0.3741 -0.0821 -0.0268 0.0643  236 GLN B CG  
7936 C CD  . GLN B 218 ? 0.3373 0.2239 0.3846 -0.0932 -0.0061 0.0530  236 GLN B CD  
7937 O OE1 . GLN B 218 ? 0.3415 0.2463 0.4046 -0.1236 0.0050  0.0317  236 GLN B OE1 
7938 N NE2 . GLN B 218 ? 0.3350 0.2292 0.3770 -0.0630 -0.0256 0.0519  236 GLN B NE2 
7947 N N   . ALA B 219 ? 0.3440 0.1871 0.3327 -0.0873 -0.0637 0.0441  237 ALA B N   
7948 C CA  . ALA B 219 ? 0.3609 0.1843 0.3345 -0.0760 -0.0589 0.0415  237 ALA B CA  
7949 C C   . ALA B 219 ? 0.3643 0.1914 0.3449 -0.0894 -0.0296 0.0379  237 ALA B C   
7950 O O   . ALA B 219 ? 0.3791 0.1865 0.3360 -0.0712 -0.0247 0.0391  237 ALA B O   
7951 C CB  . ALA B 219 ? 0.3245 0.2046 0.3597 -0.0601 -0.0593 0.0333  237 ALA B CB  
7957 N N   . GLN B 220 ? 0.3746 0.2162 0.3685 -0.1124 -0.0093 0.0544  238 GLN B N   
7958 C CA  . GLN B 220 ? 0.3836 0.2383 0.3798 -0.0975 -0.0057 0.0581  238 GLN B CA  
7959 C C   . GLN B 220 ? 0.3656 0.2526 0.3970 -0.0942 -0.0208 0.0519  238 GLN B C   
7960 O O   . GLN B 220 ? 0.3677 0.2679 0.4117 -0.0811 -0.0204 0.0602  238 GLN B O   
7961 C CB  . GLN B 220 ? 0.3816 0.2504 0.3688 -0.1054 -0.0065 0.0487  238 GLN B CB  
7962 C CG  . GLN B 220 ? 0.3691 0.2378 0.3583 -0.0861 -0.0143 0.0595  238 GLN B CG  
7963 C CD  . GLN B 220 ? 0.3484 0.2110 0.3350 -0.1081 -0.0214 0.0541  238 GLN B CD  
7964 O OE1 . GLN B 220 ? 0.3578 0.2094 0.3205 -0.1180 -0.0067 0.0678  238 GLN B OE1 
7965 N NE2 . GLN B 220 ? 0.3428 0.2074 0.3286 -0.0972 -0.0517 0.0614  238 GLN B NE2 
7974 N N   . ALA B 221 ? 0.3539 0.2605 0.3967 -0.1007 -0.0426 0.0478  239 ALA B N   
7975 C CA  . ALA B 221 ? 0.3607 0.2719 0.4191 -0.0993 -0.0427 0.0284  239 ALA B CA  
7976 C C   . ALA B 221 ? 0.3700 0.2730 0.4275 -0.0983 -0.0377 0.0259  239 ALA B C   
7977 O O   . ALA B 221 ? 0.3534 0.2761 0.4427 -0.1013 -0.0295 0.0204  239 ALA B O   
7978 C CB  . ALA B 221 ? 0.3445 0.2782 0.4115 -0.0858 -0.0769 0.0196  239 ALA B CB  
7984 N N   . VAL B 222 ? 0.3889 0.2672 0.4163 -0.0912 -0.0467 0.0382  240 VAL B N   
7985 C CA  . VAL B 222 ? 0.3995 0.2627 0.4190 -0.1239 -0.0544 0.0332  240 VAL B CA  
7986 C C   . VAL B 222 ? 0.4001 0.2509 0.4226 -0.1623 -0.0293 0.0221  240 VAL B C   
7987 O O   . VAL B 222 ? 0.4267 0.2625 0.4257 -0.1761 -0.0295 0.0027  240 VAL B O   
7988 C CB  . VAL B 222 ? 0.3878 0.2673 0.4278 -0.1075 -0.0548 0.0484  240 VAL B CB  
7989 C CG1 . VAL B 222 ? 0.3865 0.2700 0.4372 -0.0971 -0.0518 0.0493  240 VAL B CG1 
7990 C CG2 . VAL B 222 ? 0.4238 0.2755 0.4310 -0.0901 -0.0346 0.0654  240 VAL B CG2 
8000 N N   . CYS B 223 ? 0.4113 0.2419 0.4209 -0.1335 -0.0128 0.0301  241 CYS B N   
8001 C CA  . CYS B 223 ? 0.4277 0.2309 0.4273 -0.1392 0.0021  0.0435  241 CYS B CA  
8002 C C   . CYS B 223 ? 0.4373 0.2499 0.4425 -0.1449 0.0144  0.0508  241 CYS B C   
8003 O O   . CYS B 223 ? 0.4714 0.2562 0.4429 -0.1277 0.0326  0.0633  241 CYS B O   
8004 C CB  . CYS B 223 ? 0.4506 0.2128 0.4234 -0.1096 -0.0078 0.0381  241 CYS B CB  
8005 S SG  . CYS B 223 ? 0.4170 0.1874 0.4320 -0.0899 -0.0124 0.0423  241 CYS B SG  
8010 N N   . GLY B 224 ? 0.4241 0.2601 0.4558 -0.1611 0.0231  0.0450  242 GLY B N   
8011 C CA  . GLY B 224 ? 0.4593 0.2803 0.4664 -0.1362 0.0447  0.0511  242 GLY B CA  
8012 C C   . GLY B 224 ? 0.5002 0.2927 0.4793 -0.1173 0.0653  0.0481  242 GLY B C   
8013 O O   . GLY B 224 ? 0.4935 0.2733 0.4708 -0.1028 0.0430  0.0575  242 GLY B O   
8017 N N   . PRO B 225 ? 0.5508 0.3331 0.4934 -0.1078 0.0973  0.0268  243 PRO B N   
8018 C CA  . PRO B 225 ? 0.5805 0.3541 0.4906 -0.1035 0.1050  0.0199  243 PRO B CA  
8019 C C   . PRO B 225 ? 0.5841 0.3400 0.4698 -0.1295 0.0909  0.0206  243 PRO B C   
8020 O O   . PRO B 225 ? 0.6249 0.3410 0.4752 -0.1368 0.0995  -0.0016 243 PRO B O   
8021 C CB  . PRO B 225 ? 0.6104 0.3673 0.5044 -0.0801 0.1101  0.0117  243 PRO B CB  
8022 C CG  . PRO B 225 ? 0.6070 0.3665 0.5114 -0.0775 0.1124  0.0087  243 PRO B CG  
8023 C CD  . PRO B 225 ? 0.5818 0.3450 0.5084 -0.0912 0.1050  0.0178  243 PRO B CD  
8031 N N   . LEU B 226 ? 0.5585 0.3242 0.4458 -0.1582 0.0736  0.0332  244 LEU B N   
8032 C CA  . LEU B 226 ? 0.5541 0.3124 0.4453 -0.1467 0.0474  0.0448  244 LEU B CA  
8033 C C   . LEU B 226 ? 0.5357 0.2934 0.4183 -0.1486 0.0219  0.0608  244 LEU B C   
8034 O O   . LEU B 226 ? 0.5276 0.3025 0.4141 -0.1374 0.0112  0.0845  244 LEU B O   
8035 C CB  . LEU B 226 ? 0.5814 0.3250 0.4630 -0.1416 0.0462  0.0374  244 LEU B CB  
8036 C CG  . LEU B 226 ? 0.6023 0.3329 0.4723 -0.1332 0.0398  0.0259  244 LEU B CG  
8037 C CD1 . LEU B 226 ? 0.6090 0.3246 0.4752 -0.1513 0.0419  0.0185  244 LEU B CD1 
8038 C CD2 . LEU B 226 ? 0.6075 0.3378 0.4721 -0.1137 0.0287  0.0183  244 LEU B CD2 
8050 N N   . PHE B 227 ? 0.5053 0.2524 0.3954 -0.1651 -0.0035 0.0462  245 PHE B N   
8051 C CA  . PHE B 227 ? 0.4849 0.2220 0.3878 -0.1373 0.0035  0.0483  245 PHE B CA  
8052 C C   . PHE B 227 ? 0.4771 0.2242 0.3931 -0.1262 -0.0007 0.0467  245 PHE B C   
8053 O O   . PHE B 227 ? 0.4875 0.2444 0.4093 -0.1169 0.0139  0.0493  245 PHE B O   
8054 C CB  . PHE B 227 ? 0.4742 0.2009 0.3757 -0.1180 -0.0176 0.0516  245 PHE B CB  
8055 C CG  . PHE B 227 ? 0.4729 0.1923 0.3742 -0.0985 -0.0198 0.0549  245 PHE B CG  
8056 C CD1 . PHE B 227 ? 0.4801 0.2011 0.3874 -0.0815 -0.0236 0.0392  245 PHE B CD1 
8057 C CD2 . PHE B 227 ? 0.4623 0.2067 0.3652 -0.0965 -0.0338 0.0708  245 PHE B CD2 
8058 C CE1 . PHE B 227 ? 0.4741 0.2138 0.3899 -0.0743 -0.0257 0.0356  245 PHE B CE1 
8059 C CE2 . PHE B 227 ? 0.4486 0.2030 0.3665 -0.0846 -0.0599 0.0666  245 PHE B CE2 
8060 C CZ  . PHE B 227 ? 0.4680 0.2193 0.3795 -0.0619 -0.0535 0.0487  245 PHE B CZ  
8070 N N   . VAL B 228 ? 0.4809 0.2189 0.3893 -0.1087 -0.0191 0.0414  246 VAL B N   
8071 C CA  . VAL B 228 ? 0.4875 0.2011 0.3830 -0.1044 -0.0103 0.0380  246 VAL B CA  
8072 C C   . VAL B 228 ? 0.4849 0.1871 0.3831 -0.0729 -0.0140 0.0408  246 VAL B C   
8073 O O   . VAL B 228 ? 0.5053 0.1936 0.3971 -0.0454 0.0030  0.0536  246 VAL B O   
8074 C CB  . VAL B 228 ? 0.5055 0.2320 0.3807 -0.1154 -0.0108 0.0296  246 VAL B CB  
8075 C CG1 . VAL B 228 ? 0.5161 0.2335 0.3641 -0.1176 -0.0286 0.0375  246 VAL B CG1 
8076 C CG2 . VAL B 228 ? 0.5149 0.2440 0.3867 -0.1328 0.0194  0.0301  246 VAL B CG2 
8086 N N   . ILE B 229 ? 0.4379 0.1812 0.3641 -0.0671 -0.0389 0.0386  247 ILE B N   
8087 C CA  . ILE B 229 ? 0.4075 0.1669 0.3533 -0.0571 -0.0238 0.0258  247 ILE B CA  
8088 C C   . ILE B 229 ? 0.4065 0.1629 0.3271 -0.0603 -0.0241 0.0300  247 ILE B C   
8089 O O   . ILE B 229 ? 0.3948 0.1689 0.3261 -0.0706 -0.0142 0.0239  247 ILE B O   
8090 C CB  . ILE B 229 ? 0.3906 0.1667 0.3811 -0.0189 -0.0168 0.0251  247 ILE B CB  
8091 C CG1 . ILE B 229 ? 0.3815 0.1789 0.3879 -0.0256 -0.0090 0.0205  247 ILE B CG1 
8092 C CG2 . ILE B 229 ? 0.4015 0.1702 0.3927 -0.0217 -0.0166 0.0153  247 ILE B CG2 
8093 C CD1 . ILE B 229 ? 0.3575 0.1747 0.4052 -0.0536 -0.0145 0.0068  247 ILE B CD1 
8105 N N   . ASP B 230 ? 0.4044 0.1669 0.3082 -0.0592 -0.0407 0.0264  248 ASP B N   
8106 C CA  . ASP B 230 ? 0.3660 0.1595 0.2760 -0.0483 -0.0468 0.0401  248 ASP B CA  
8107 C C   . ASP B 230 ? 0.3359 0.1572 0.2538 -0.0395 -0.0402 0.0474  248 ASP B C   
8108 O O   . ASP B 230 ? 0.3593 0.1658 0.2538 -0.0613 -0.0294 0.0666  248 ASP B O   
8109 C CB  . ASP B 230 ? 0.3880 0.1661 0.2511 -0.0046 -0.0780 0.0477  248 ASP B CB  
8110 C CG  . ASP B 230 ? 0.4399 0.2040 0.2683 0.0011  -0.0700 0.0269  248 ASP B CG  
8111 O OD1 . ASP B 230 ? 0.4548 0.2336 0.2987 0.0145  -0.0463 0.0371  248 ASP B OD1 
8112 O OD2 . ASP B 230 ? 0.4806 0.2252 0.2841 0.0162  -0.0551 0.0056  248 ASP B OD2 
8117 N N   . HIS B 231 ? 0.3057 0.1366 0.2293 -0.0367 -0.0454 0.0314  249 HIS B N   
8118 C CA  . HIS B 231 ? 0.3149 0.1255 0.2080 -0.0378 -0.0591 0.0300  249 HIS B CA  
8119 C C   . HIS B 231 ? 0.3184 0.1296 0.2392 -0.0416 -0.0698 0.0146  249 HIS B C   
8120 O O   . HIS B 231 ? 0.3204 0.1386 0.2486 -0.0331 -0.0571 0.0250  249 HIS B O   
8121 C CB  . HIS B 231 ? 0.3346 0.1296 0.2320 -0.0449 -0.0336 0.0117  249 HIS B CB  
8122 C CG  . HIS B 231 ? 0.3508 0.1259 0.2436 -0.0248 -0.0243 -0.0087 249 HIS B CG  
8123 N ND1 . HIS B 231 ? 0.3387 0.1281 0.2445 -0.0419 -0.0313 0.0032  249 HIS B ND1 
8124 C CD2 . HIS B 231 ? 0.3285 0.1437 0.2490 -0.0053 -0.0364 -0.0159 249 HIS B CD2 
8125 C CE1 . HIS B 231 ? 0.3401 0.1285 0.2636 -0.0440 -0.0405 -0.0044 249 HIS B CE1 
8126 N NE2 . HIS B 231 ? 0.3598 0.1316 0.2659 -0.0376 -0.0344 -0.0231 249 HIS B NE2 
8134 N N   . ALA B 232 ? 0.3388 0.1279 0.2768 -0.0227 -0.0661 -0.0022 250 ALA B N   
8135 C CA  . ALA B 232 ? 0.3257 0.1400 0.2887 -0.0036 -0.0799 0.0069  250 ALA B CA  
8136 C C   . ALA B 232 ? 0.3450 0.1385 0.3064 0.0035  -0.0531 0.0146  250 ALA B C   
8137 O O   . ALA B 232 ? 0.3416 0.1174 0.3076 0.0032  -0.0833 0.0072  250 ALA B O   
8138 C CB  . ALA B 232 ? 0.3287 0.1420 0.3079 -0.0277 -0.0717 0.0209  250 ALA B CB  
8144 N N   . GLY B 233 ? 0.3647 0.1328 0.3117 0.0160  -0.0415 0.0339  251 GLY B N   
8145 C CA  . GLY B 233 ? 0.3610 0.1312 0.2849 -0.0005 -0.0421 0.0384  251 GLY B CA  
8146 C C   . GLY B 233 ? 0.3667 0.1228 0.2630 -0.0104 -0.0406 0.0377  251 GLY B C   
8147 O O   . GLY B 233 ? 0.3716 0.1332 0.2741 -0.0349 -0.0186 0.0519  251 GLY B O   
8151 N N   . SER B 234 ? 0.3721 0.1095 0.2550 -0.0111 -0.0432 0.0277  252 SER B N   
8152 C CA  . SER B 234 ? 0.3511 0.1347 0.2479 -0.0094 -0.0585 0.0192  252 SER B CA  
8153 C C   . SER B 234 ? 0.3332 0.1264 0.2508 -0.0272 -0.0749 0.0224  252 SER B C   
8154 O O   . SER B 234 ? 0.3323 0.1192 0.2595 -0.0407 -0.0790 0.0296  252 SER B O   
8155 C CB  . SER B 234 ? 0.3642 0.1387 0.2471 -0.0213 -0.0502 0.0183  252 SER B CB  
8156 O OG  . SER B 234 ? 0.3559 0.1454 0.2689 -0.0288 -0.0568 0.0118  252 SER B OG  
8162 N N   . LEU B 235 ? 0.3387 0.1181 0.2565 -0.0390 -0.0991 0.0281  253 LEU B N   
8163 C CA  . LEU B 235 ? 0.3323 0.1114 0.2610 -0.0203 -0.0871 0.0336  253 LEU B CA  
8164 C C   . LEU B 235 ? 0.3265 0.1127 0.2797 -0.0122 -0.0797 0.0321  253 LEU B C   
8165 O O   . LEU B 235 ? 0.3495 0.1214 0.2873 -0.0295 -0.0871 0.0229  253 LEU B O   
8166 C CB  . LEU B 235 ? 0.3364 0.1275 0.2632 -0.0280 -0.0921 0.0032  253 LEU B CB  
8167 C CG  . LEU B 235 ? 0.3393 0.1250 0.2435 -0.0316 -0.1237 0.0197  253 LEU B CG  
8168 C CD1 . LEU B 235 ? 0.3168 0.1336 0.2426 -0.0390 -0.1237 0.0342  253 LEU B CD1 
8169 C CD2 . LEU B 235 ? 0.3388 0.1188 0.2547 -0.0022 -0.1147 0.0367  253 LEU B CD2 
8181 N N   . THR B 236 ? 0.3224 0.1187 0.2938 -0.0240 -0.0768 0.0531  254 THR B N   
8182 C CA  . THR B 236 ? 0.3334 0.1182 0.2918 -0.0107 -0.1014 0.0388  254 THR B CA  
8183 C C   . THR B 236 ? 0.3263 0.1111 0.2933 -0.0302 -0.0939 0.0370  254 THR B C   
8184 O O   . THR B 236 ? 0.3610 0.1164 0.3029 -0.0145 -0.0741 0.0491  254 THR B O   
8185 C CB  . THR B 236 ? 0.3787 0.1324 0.2992 -0.0154 -0.0939 0.0273  254 THR B CB  
8186 O OG1 . THR B 236 ? 0.3821 0.1334 0.3224 -0.0085 -0.0830 0.0391  254 THR B OG1 
8187 C CG2 . THR B 236 ? 0.3790 0.1457 0.2932 -0.0167 -0.0986 0.0134  254 THR B CG2 
8195 N N   . SER B 237 ? 0.3448 0.1160 0.3116 -0.0432 -0.0849 0.0341  255 SER B N   
8196 C CA  . SER B 237 ? 0.3496 0.1190 0.3035 -0.0577 -0.0666 0.0362  255 SER B CA  
8197 C C   . SER B 237 ? 0.3542 0.1197 0.2934 -0.0532 -0.0779 0.0383  255 SER B C   
8198 O O   . SER B 237 ? 0.3771 0.1148 0.2774 -0.0317 -0.0872 0.0264  255 SER B O   
8199 C CB  . SER B 237 ? 0.3899 0.1328 0.3092 -0.0586 -0.0862 0.0469  255 SER B CB  
8200 O OG  . SER B 237 ? 0.3953 0.1361 0.3017 -0.0590 -0.0863 0.0525  255 SER B OG  
8206 N N   . GLN B 238 ? 0.3730 0.1218 0.2831 -0.0531 -0.0917 0.0282  256 GLN B N   
8207 C CA  . GLN B 238 ? 0.3588 0.1253 0.2905 -0.0669 -0.0830 0.0120  256 GLN B CA  
8208 C C   . GLN B 238 ? 0.3607 0.1270 0.2852 -0.0705 -0.0780 0.0288  256 GLN B C   
8209 O O   . GLN B 238 ? 0.3561 0.1255 0.2904 -0.0557 -0.0792 0.0348  256 GLN B O   
8210 C CB  . GLN B 238 ? 0.4033 0.1346 0.3078 -0.0640 -0.0687 0.0147  256 GLN B CB  
8211 C CG  . GLN B 238 ? 0.4011 0.1380 0.3111 -0.0840 -0.0548 0.0269  256 GLN B CG  
8212 C CD  . GLN B 238 ? 0.4083 0.1351 0.3340 -0.0684 -0.0834 0.0159  256 GLN B CD  
8213 O OE1 . GLN B 238 ? 0.3951 0.1251 0.3549 -0.0361 -0.0969 0.0235  256 GLN B OE1 
8214 N NE2 . GLN B 238 ? 0.4331 0.1392 0.3264 -0.0659 -0.0939 0.0205  256 GLN B NE2 
8223 N N   . PHE B 239 ? 0.3761 0.1306 0.2826 -0.0711 -0.0848 0.0296  257 PHE B N   
8224 C CA  . PHE B 239 ? 0.3652 0.1446 0.3065 -0.0692 -0.0757 0.0344  257 PHE B CA  
8225 C C   . PHE B 239 ? 0.3262 0.1289 0.3025 -0.0519 -0.1028 0.0436  257 PHE B C   
8226 O O   . PHE B 239 ? 0.3266 0.1550 0.2896 -0.0638 -0.0774 0.0200  257 PHE B O   
8227 C CB  . PHE B 239 ? 0.3758 0.1767 0.3294 -0.0546 -0.0850 0.0186  257 PHE B CB  
8228 C CG  . PHE B 239 ? 0.3799 0.1829 0.3542 -0.0403 -0.0644 0.0236  257 PHE B CG  
8229 C CD1 . PHE B 239 ? 0.3951 0.1858 0.3743 -0.0338 -0.0679 0.0190  257 PHE B CD1 
8230 C CD2 . PHE B 239 ? 0.3885 0.1831 0.3610 -0.0271 -0.0579 0.0292  257 PHE B CD2 
8231 C CE1 . PHE B 239 ? 0.3896 0.1905 0.3893 -0.0464 -0.0532 0.0222  257 PHE B CE1 
8232 C CE2 . PHE B 239 ? 0.3932 0.1718 0.3759 -0.0409 -0.0529 0.0290  257 PHE B CE2 
8233 C CZ  . PHE B 239 ? 0.3910 0.1825 0.3952 -0.0402 -0.0415 0.0325  257 PHE B CZ  
8243 N N   . SER B 240 ? 0.3119 0.1103 0.3221 -0.0486 -0.0672 0.0269  258 SER B N   
8244 C CA  . SER B 240 ? 0.3051 0.1078 0.3002 -0.0471 -0.0738 0.0266  258 SER B CA  
8245 C C   . SER B 240 ? 0.3114 0.1086 0.3021 -0.0426 -0.0801 0.0291  258 SER B C   
8246 O O   . SER B 240 ? 0.3298 0.1101 0.3079 -0.0358 -0.0918 0.0210  258 SER B O   
8247 C CB  . SER B 240 ? 0.3572 0.1204 0.2923 -0.0697 -0.0556 0.0144  258 SER B CB  
8248 O OG  . SER B 240 ? 0.3819 0.1225 0.2745 -0.0569 -0.0660 0.0372  258 SER B OG  
8254 N N   . TYR B 241 ? 0.3185 0.1142 0.3093 -0.0331 -0.0706 0.0362  259 TYR B N   
8255 C CA  . TYR B 241 ? 0.3442 0.1320 0.3300 -0.0323 -0.0559 0.0213  259 TYR B CA  
8256 C C   . TYR B 241 ? 0.3613 0.1374 0.3087 -0.0448 -0.0563 0.0189  259 TYR B C   
8257 O O   . TYR B 241 ? 0.3526 0.1239 0.2771 -0.0700 -0.0506 0.0006  259 TYR B O   
8258 C CB  . TYR B 241 ? 0.3359 0.1331 0.3158 -0.0397 -0.0912 0.0010  259 TYR B CB  
8259 C CG  . TYR B 241 ? 0.3579 0.1494 0.3116 -0.0145 -0.1357 -0.0148 259 TYR B CG  
8260 C CD1 . TYR B 241 ? 0.3765 0.1532 0.3357 -0.0026 -0.1217 -0.0259 259 TYR B CD1 
8261 C CD2 . TYR B 241 ? 0.4087 0.1557 0.3388 -0.0162 -0.0812 -0.0241 259 TYR B CD2 
8262 C CE1 . TYR B 241 ? 0.4342 0.1622 0.3536 0.0117  -0.0895 -0.0357 259 TYR B CE1 
8263 C CE2 . TYR B 241 ? 0.4321 0.1393 0.3499 0.0003  -0.0840 -0.0415 259 TYR B CE2 
8264 C CZ  . TYR B 241 ? 0.4421 0.1521 0.3526 0.0290  -0.0874 -0.0537 259 TYR B CZ  
8265 O OH  . TYR B 241 ? 0.4993 0.1779 0.3728 0.0652  -0.0696 -0.0631 259 TYR B OH  
8275 N N   . VAL B 242 ? 0.3668 0.1544 0.3075 -0.0594 -0.0918 0.0328  260 VAL B N   
8276 C CA  . VAL B 242 ? 0.3898 0.1604 0.3125 -0.0725 -0.0967 0.0228  260 VAL B CA  
8277 C C   . VAL B 242 ? 0.4019 0.1562 0.3026 -0.0841 -0.0864 0.0162  260 VAL B C   
8278 O O   . VAL B 242 ? 0.3917 0.1653 0.2935 -0.1086 -0.0750 0.0017  260 VAL B O   
8279 C CB  . VAL B 242 ? 0.4043 0.1791 0.3208 -0.0734 -0.0794 0.0416  260 VAL B CB  
8280 C CG1 . VAL B 242 ? 0.4410 0.1955 0.3352 -0.0791 -0.0558 0.0413  260 VAL B CG1 
8281 C CG2 . VAL B 242 ? 0.4052 0.1919 0.3277 -0.0747 -0.0859 0.0395  260 VAL B CG2 
8291 N N   . VAL B 243 ? 0.3682 0.1597 0.3014 -0.0720 -0.1054 0.0254  261 VAL B N   
8292 C CA  . VAL B 243 ? 0.3689 0.1487 0.3031 -0.0531 -0.0821 0.0415  261 VAL B CA  
8293 C C   . VAL B 243 ? 0.3640 0.1448 0.2753 -0.0540 -0.0888 0.0224  261 VAL B C   
8294 O O   . VAL B 243 ? 0.3894 0.1435 0.2753 -0.0638 -0.0949 0.0194  261 VAL B O   
8295 C CB  . VAL B 243 ? 0.3427 0.1345 0.3246 -0.0429 -0.0659 0.0507  261 VAL B CB  
8296 C CG1 . VAL B 243 ? 0.3501 0.1462 0.3398 -0.0259 -0.0572 0.0609  261 VAL B CG1 
8297 C CG2 . VAL B 243 ? 0.3433 0.1388 0.3368 -0.0446 -0.0544 0.0342  261 VAL B CG2 
8307 N N   . GLY B 244 ? 0.3225 0.1403 0.2753 -0.0403 -0.0759 0.0229  262 GLY B N   
8308 C CA  . GLY B 244 ? 0.3256 0.1417 0.2641 -0.0396 -0.0743 0.0128  262 GLY B CA  
8309 C C   . GLY B 244 ? 0.3463 0.1366 0.2660 -0.0528 -0.0581 0.0004  262 GLY B C   
8310 O O   . GLY B 244 ? 0.3331 0.1384 0.2561 -0.0598 -0.0476 0.0008  262 GLY B O   
8314 N N   . ARG B 245 ? 0.4210 0.1248 0.2737 -0.0469 -0.0591 -0.0095 263 ARG B N   
8315 C CA  . ARG B 245 ? 0.4133 0.1437 0.2928 -0.0618 -0.0757 -0.0155 263 ARG B CA  
8316 C C   . ARG B 245 ? 0.3938 0.1431 0.2849 -0.0622 -0.0860 -0.0087 263 ARG B C   
8317 O O   . ARG B 245 ? 0.4200 0.1517 0.3003 -0.0595 -0.1013 -0.0206 263 ARG B O   
8318 C CB  . ARG B 245 ? 0.4284 0.1530 0.3165 -0.0615 -0.0869 -0.0159 263 ARG B CB  
8319 C CG  . ARG B 245 ? 0.4729 0.1433 0.3230 -0.0571 -0.0781 -0.0193 263 ARG B CG  
8320 C CD  . ARG B 245 ? 0.5159 0.1494 0.3439 -0.0481 -0.0904 -0.0066 263 ARG B CD  
8321 N NE  . ARG B 245 ? 0.5509 0.1589 0.3824 -0.0485 -0.0873 0.0000  263 ARG B NE  
8322 C CZ  . ARG B 245 ? 0.5865 0.1690 0.4338 -0.0549 -0.0703 0.0032  263 ARG B CZ  
8323 N NH1 . ARG B 245 ? 0.6032 0.1699 0.4480 -0.0626 -0.0743 -0.0071 263 ARG B NH1 
8324 N NH2 . ARG B 245 ? 0.6100 0.1823 0.4551 -0.0373 -0.0642 0.0179  263 ARG B NH2 
8338 N N   . SER B 246 ? 0.4036 0.1549 0.2857 -0.0482 -0.0613 0.0106  264 SER B N   
8339 C CA  . SER B 246 ? 0.3771 0.1617 0.2894 -0.0763 -0.0744 0.0030  264 SER B CA  
8340 C C   . SER B 246 ? 0.3490 0.1591 0.2852 -0.0871 -0.0902 -0.0013 264 SER B C   
8341 O O   . SER B 246 ? 0.3668 0.1697 0.2979 -0.0750 -0.0627 0.0004  264 SER B O   
8342 C CB  . SER B 246 ? 0.3875 0.1845 0.3210 -0.0817 -0.0780 0.0099  264 SER B CB  
8343 O OG  . SER B 246 ? 0.3937 0.1942 0.3125 -0.1064 -0.0792 0.0016  264 SER B OG  
8349 N N   . ALA B 247 ? 0.3131 0.1688 0.2754 -0.0852 -0.1015 -0.0030 265 ALA B N   
8350 C CA  . ALA B 247 ? 0.3093 0.1596 0.2809 -0.0638 -0.1070 -0.0143 265 ALA B CA  
8351 C C   . ALA B 247 ? 0.3113 0.1699 0.2844 -0.0606 -0.1136 -0.0172 265 ALA B C   
8352 O O   . ALA B 247 ? 0.3290 0.2088 0.2980 -0.0610 -0.0854 0.0002  265 ALA B O   
8353 C CB  . ALA B 247 ? 0.2934 0.1439 0.2816 -0.0780 -0.0806 -0.0230 265 ALA B CB  
8359 N N   . LEU B 248 ? 0.3417 0.1678 0.2762 -0.0534 -0.1269 -0.0365 266 LEU B N   
8360 C CA  . LEU B 248 ? 0.3766 0.1837 0.2830 -0.0535 -0.1183 -0.0279 266 LEU B CA  
8361 C C   . LEU B 248 ? 0.4115 0.2103 0.2915 -0.0346 -0.1197 -0.0389 266 LEU B C   
8362 O O   . LEU B 248 ? 0.4208 0.2234 0.2697 -0.0178 -0.0976 -0.0355 266 LEU B O   
8363 C CB  . LEU B 248 ? 0.3736 0.1792 0.2814 -0.0470 -0.1143 -0.0242 266 LEU B CB  
8364 C CG  . LEU B 248 ? 0.3774 0.1706 0.2787 -0.0457 -0.1218 -0.0144 266 LEU B CG  
8365 C CD1 . LEU B 248 ? 0.4041 0.1679 0.2726 -0.0187 -0.1123 -0.0082 266 LEU B CD1 
8366 C CD2 . LEU B 248 ? 0.3993 0.1855 0.2916 -0.0526 -0.1104 -0.0125 266 LEU B CD2 
8378 N N   . ARG B 249 ? 0.4388 0.2082 0.3106 -0.0640 -0.1435 -0.0519 267 ARG B N   
8379 C CA  . ARG B 249 ? 0.5067 0.2344 0.3539 -0.0975 -0.1530 -0.0438 267 ARG B CA  
8380 C C   . ARG B 249 ? 0.4845 0.2595 0.3599 -0.1158 -0.1541 -0.0345 267 ARG B C   
8381 O O   . ARG B 249 ? 0.4970 0.3115 0.3592 -0.0751 -0.1651 -0.0183 267 ARG B O   
8382 C CB  . ARG B 249 ? 0.5861 0.2281 0.3858 -0.0885 -0.1592 -0.0437 267 ARG B CB  
8383 C CG  . ARG B 249 ? 0.6771 0.2379 0.4351 -0.1062 -0.1412 -0.0427 267 ARG B CG  
8384 C CD  . ARG B 249 ? 0.7629 0.2477 0.4685 -0.1073 -0.1324 -0.0355 267 ARG B CD  
8385 N NE  . ARG B 249 ? 0.8038 0.2543 0.4863 -0.1144 -0.1433 -0.0270 267 ARG B NE  
8386 C CZ  . ARG B 249 ? 0.8495 0.2940 0.5244 -0.1362 -0.1230 0.0076  267 ARG B CZ  
8387 N NH1 . ARG B 249 ? 0.8530 0.2985 0.5282 -0.1721 -0.1177 0.0132  267 ARG B NH1 
8388 N NH2 . ARG B 249 ? 0.8663 0.3141 0.5454 -0.1344 -0.1188 0.0210  267 ARG B NH2 
8402 N N   . SER B 250 ? 0.4358 0.2480 0.3523 -0.1263 -0.1451 -0.0210 268 SER B N   
8403 C CA  . SER B 250 ? 0.4422 0.2548 0.3323 -0.1151 -0.1662 -0.0119 268 SER B CA  
8404 C C   . SER B 250 ? 0.4713 0.2573 0.3386 -0.1248 -0.1631 -0.0124 268 SER B C   
8405 O O   . SER B 250 ? 0.4856 0.2435 0.3499 -0.1240 -0.1620 0.0133  268 SER B O   
8406 C CB  . SER B 250 ? 0.4399 0.2747 0.3523 -0.0932 -0.1559 -0.0001 268 SER B CB  
8407 O OG  . SER B 250 ? 0.4376 0.2958 0.3445 -0.0746 -0.1483 0.0004  268 SER B OG  
8413 N N   . THR B 251 ? 0.5273 0.2620 0.3414 -0.1271 -0.1837 0.0019  269 THR B N   
8414 C CA  . THR B 251 ? 0.5646 0.2695 0.3654 -0.1112 -0.1817 0.0197  269 THR B CA  
8415 C C   . THR B 251 ? 0.5639 0.2599 0.3809 -0.1264 -0.1465 0.0315  269 THR B C   
8416 O O   . THR B 251 ? 0.6157 0.2916 0.3910 -0.1158 -0.0992 0.0449  269 THR B O   
8417 C CB  . THR B 251 ? 0.6040 0.2886 0.3881 -0.1127 -0.1673 0.0088  269 THR B CB  
8418 O OG1 . THR B 251 ? 0.5961 0.3150 0.4060 -0.1216 -0.1752 0.0037  269 THR B OG1 
8419 C CG2 . THR B 251 ? 0.6358 0.3001 0.3995 -0.1052 -0.1555 0.0025  269 THR B CG2 
8427 N N   . THR B 252 ? 0.5071 0.2548 0.3918 -0.1259 -0.1577 0.0320  270 THR B N   
8428 C CA  . THR B 252 ? 0.4838 0.2732 0.4194 -0.1330 -0.1364 0.0068  270 THR B CA  
8429 C C   . THR B 252 ? 0.4684 0.2410 0.4079 -0.1119 -0.1322 0.0095  270 THR B C   
8430 O O   . THR B 252 ? 0.4497 0.2171 0.4126 -0.0999 -0.1400 0.0062  270 THR B O   
8431 C CB  . THR B 252 ? 0.4879 0.3119 0.4622 -0.1452 -0.1206 -0.0136 270 THR B CB  
8432 O OG1 . THR B 252 ? 0.4862 0.3143 0.4742 -0.1679 -0.1014 -0.0132 270 THR B OG1 
8433 C CG2 . THR B 252 ? 0.4767 0.3278 0.4713 -0.1635 -0.1467 -0.0368 270 THR B CG2 
8441 N N   . GLY B 253 ? 0.4282 0.2249 0.3789 -0.1069 -0.1495 0.0182  271 GLY B N   
8442 C CA  . GLY B 253 ? 0.4102 0.2011 0.3634 -0.1164 -0.1351 0.0118  271 GLY B CA  
8443 C C   . GLY B 253 ? 0.3715 0.1939 0.3543 -0.1100 -0.1359 0.0210  271 GLY B C   
8444 O O   . GLY B 253 ? 0.3759 0.1943 0.3514 -0.1034 -0.1463 0.0331  271 GLY B O   
8448 N N   . GLN B 254 ? 0.3671 0.1949 0.3687 -0.1008 -0.1209 0.0108  272 GLN B N   
8449 C CA  . GLN B 254 ? 0.3612 0.1949 0.3729 -0.1081 -0.1168 0.0145  272 GLN B CA  
8450 C C   . GLN B 254 ? 0.3585 0.1892 0.3880 -0.1168 -0.0977 0.0210  272 GLN B C   
8451 O O   . GLN B 254 ? 0.3891 0.1959 0.3911 -0.1283 -0.0900 0.0147  272 GLN B O   
8452 C CB  . GLN B 254 ? 0.3859 0.2247 0.3793 -0.1144 -0.1032 0.0089  272 GLN B CB  
8453 C CG  . GLN B 254 ? 0.3887 0.2302 0.3833 -0.1184 -0.1086 0.0111  272 GLN B CG  
8454 C CD  . GLN B 254 ? 0.3738 0.2506 0.4027 -0.1042 -0.1214 0.0033  272 GLN B CD  
8455 O OE1 . GLN B 254 ? 0.3714 0.2852 0.4495 -0.0618 -0.1259 -0.0143 272 GLN B OE1 
8456 N NE2 . GLN B 254 ? 0.3699 0.2461 0.3685 -0.1151 -0.1325 0.0071  272 GLN B NE2 
8465 N N   . ALA B 255 ? 0.3346 0.1862 0.3944 -0.1004 -0.1201 0.0172  273 ALA B N   
8466 C CA  . ALA B 255 ? 0.3339 0.1928 0.4163 -0.1037 -0.1081 0.0300  273 ALA B CA  
8467 C C   . ALA B 255 ? 0.3347 0.2132 0.4168 -0.1128 -0.1407 0.0372  273 ALA B C   
8468 O O   . ALA B 255 ? 0.3266 0.2279 0.4174 -0.0915 -0.1095 0.0391  273 ALA B O   
8469 C CB  . ALA B 255 ? 0.3568 0.1845 0.4263 -0.0986 -0.1020 0.0362  273 ALA B CB  
8475 N N   . ARG B 256 ? 0.3722 0.2356 0.4293 -0.1308 -0.1290 0.0502  274 ARG B N   
8476 C CA  . ARG B 256 ? 0.3895 0.2623 0.4405 -0.1430 -0.1619 0.0427  274 ARG B CA  
8477 C C   . ARG B 256 ? 0.3574 0.2595 0.4519 -0.1398 -0.1488 0.0526  274 ARG B C   
8478 O O   . ARG B 256 ? 0.3745 0.2276 0.4785 -0.1291 -0.1298 0.0613  274 ARG B O   
8479 C CB  . ARG B 256 ? 0.4570 0.3106 0.4441 -0.1554 -0.1770 0.0129  274 ARG B CB  
8480 C CG  . ARG B 256 ? 0.5175 0.3500 0.4556 -0.1563 -0.1828 0.0131  274 ARG B CG  
8481 C CD  . ARG B 256 ? 0.5528 0.4047 0.4766 -0.1388 -0.1962 0.0149  274 ARG B CD  
8482 N NE  . ARG B 256 ? 0.5976 0.4480 0.4940 -0.1453 -0.1947 0.0179  274 ARG B NE  
8483 C CZ  . ARG B 256 ? 0.6259 0.4760 0.5031 -0.1484 -0.1926 0.0178  274 ARG B CZ  
8484 N NH1 . ARG B 256 ? 0.6270 0.4807 0.5037 -0.1581 -0.1925 0.0305  274 ARG B NH1 
8485 N NH2 . ARG B 256 ? 0.6695 0.4990 0.5152 -0.1302 -0.1733 0.0236  274 ARG B NH2 
8499 N N   . SER B 257 ? 0.3533 0.2618 0.4731 -0.1463 -0.1270 0.0579  275 SER B N   
8500 C CA  . SER B 257 ? 0.3886 0.2611 0.4920 -0.1546 -0.1076 0.0726  275 SER B CA  
8501 C C   . SER B 257 ? 0.4168 0.2729 0.4900 -0.1481 -0.1251 0.0710  275 SER B C   
8502 O O   . SER B 257 ? 0.4221 0.2875 0.4899 -0.1475 -0.1258 0.0789  275 SER B O   
8503 C CB  . SER B 257 ? 0.4132 0.2626 0.5161 -0.1544 -0.0867 0.0632  275 SER B CB  
8504 O OG  . SER B 257 ? 0.4473 0.2617 0.5330 -0.1703 -0.0679 0.0508  275 SER B OG  
8510 N N   . ALA B 258 ? 0.4239 0.2607 0.4875 -0.1559 -0.1413 0.0498  276 ALA B N   
8511 C CA  . ALA B 258 ? 0.4493 0.2815 0.5033 -0.1501 -0.1376 0.0414  276 ALA B CA  
8512 C C   . ALA B 258 ? 0.4690 0.2684 0.5089 -0.1469 -0.1165 0.0400  276 ALA B C   
8513 O O   . ALA B 258 ? 0.4762 0.2457 0.5264 -0.1515 -0.0981 0.0523  276 ALA B O   
8514 C CB  . ALA B 258 ? 0.4839 0.3022 0.5105 -0.1514 -0.1278 0.0252  276 ALA B CB  
8520 N N   . ASP B 259 ? 0.4642 0.2791 0.4891 -0.1682 -0.1176 0.0271  277 ASP B N   
8521 C CA  . ASP B 259 ? 0.4831 0.2890 0.4652 -0.1588 -0.1029 0.0306  277 ASP B CA  
8522 C C   . ASP B 259 ? 0.4970 0.2970 0.4668 -0.1439 -0.0895 0.0510  277 ASP B C   
8523 O O   . ASP B 259 ? 0.5139 0.2994 0.4649 -0.1476 -0.0824 0.0491  277 ASP B O   
8524 C CB  . ASP B 259 ? 0.4848 0.2848 0.4394 -0.1757 -0.0873 0.0168  277 ASP B CB  
8525 C CG  . ASP B 259 ? 0.4969 0.2815 0.4179 -0.1838 -0.0822 -0.0211 277 ASP B CG  
8526 O OD1 . ASP B 259 ? 0.5069 0.2827 0.4309 -0.1806 -0.0606 -0.0240 277 ASP B OD1 
8527 O OD2 . ASP B 259 ? 0.5218 0.2834 0.4003 -0.1846 -0.0797 -0.0434 277 ASP B OD2 
8532 N N   . TYR B 260 ? 0.4764 0.2969 0.4661 -0.1424 -0.0887 0.0742  278 TYR B N   
8533 C CA  . TYR B 260 ? 0.4804 0.2961 0.4626 -0.1200 -0.0813 0.0968  278 TYR B CA  
8534 C C   . TYR B 260 ? 0.4897 0.2926 0.4663 -0.0953 -0.0627 0.1168  278 TYR B C   
8535 O O   . TYR B 260 ? 0.5013 0.3058 0.4771 -0.0821 -0.0628 0.1155  278 TYR B O   
8536 C CB  . TYR B 260 ? 0.4818 0.2977 0.4479 -0.1303 -0.1023 0.1051  278 TYR B CB  
8537 C CG  . TYR B 260 ? 0.4987 0.2968 0.4322 -0.1443 -0.1184 0.1205  278 TYR B CG  
8538 C CD1 . TYR B 260 ? 0.5309 0.2946 0.4277 -0.1507 -0.1175 0.1226  278 TYR B CD1 
8539 C CD2 . TYR B 260 ? 0.4851 0.2897 0.4399 -0.1718 -0.1342 0.1248  278 TYR B CD2 
8540 C CE1 . TYR B 260 ? 0.5410 0.2837 0.4221 -0.1698 -0.1283 0.1209  278 TYR B CE1 
8541 C CE2 . TYR B 260 ? 0.4886 0.2916 0.4301 -0.1846 -0.1446 0.1101  278 TYR B CE2 
8542 C CZ  . TYR B 260 ? 0.5347 0.2901 0.4294 -0.1834 -0.1534 0.1067  278 TYR B CZ  
8543 O OH  . TYR B 260 ? 0.5900 0.3002 0.4351 -0.1864 -0.1547 0.1132  278 TYR B OH  
8553 N N   . GLY B 261 ? 0.4769 0.2841 0.4611 -0.1148 -0.0271 0.1279  279 GLY B N   
8554 C CA  . GLY B 261 ? 0.4730 0.2804 0.4609 -0.0991 -0.0301 0.1169  279 GLY B CA  
8555 C C   . GLY B 261 ? 0.4594 0.2616 0.4484 -0.0836 -0.0505 0.1180  279 GLY B C   
8556 O O   . GLY B 261 ? 0.4396 0.2440 0.4455 -0.0726 -0.0635 0.1200  279 GLY B O   
8560 N N   . ILE B 262 ? 0.4645 0.2451 0.4429 -0.1039 -0.0469 0.1104  280 ILE B N   
8561 C CA  . ILE B 262 ? 0.4774 0.2308 0.4312 -0.1193 -0.0301 0.0764  280 ILE B CA  
8562 C C   . ILE B 262 ? 0.4827 0.2023 0.4155 -0.1330 -0.0260 0.0588  280 ILE B C   
8563 O O   . ILE B 262 ? 0.5009 0.1945 0.4153 -0.1246 -0.0381 0.0527  280 ILE B O   
8564 C CB  . ILE B 262 ? 0.5178 0.2358 0.4383 -0.1065 -0.0148 0.0579  280 ILE B CB  
8565 C CG1 . ILE B 262 ? 0.5421 0.2356 0.4417 -0.1175 0.0055  0.0493  280 ILE B CG1 
8566 C CG2 . ILE B 262 ? 0.5146 0.2460 0.4302 -0.1215 -0.0281 0.0482  280 ILE B CG2 
8567 C CD1 . ILE B 262 ? 0.5513 0.2469 0.4435 -0.1134 0.0178  0.0306  280 ILE B CD1 
8579 N N   . THR B 263 ? 0.4858 0.2068 0.3946 -0.1245 -0.0302 0.0392  281 THR B N   
8580 C CA  . THR B 263 ? 0.5055 0.2041 0.3844 -0.1210 -0.0493 0.0249  281 THR B CA  
8581 C C   . THR B 263 ? 0.5019 0.1876 0.3705 -0.1211 -0.0484 0.0185  281 THR B C   
8582 O O   . THR B 263 ? 0.5420 0.1903 0.3808 -0.1231 -0.0382 -0.0015 281 THR B O   
8583 C CB  . THR B 263 ? 0.5320 0.2207 0.3889 -0.1385 -0.0609 0.0114  281 THR B CB  
8584 O OG1 . THR B 263 ? 0.5698 0.2391 0.3998 -0.1285 -0.0593 -0.0087 281 THR B OG1 
8585 C CG2 . THR B 263 ? 0.5199 0.2387 0.3837 -0.1556 -0.0781 0.0068  281 THR B CG2 
8593 N N   . ASP B 264 ? 0.4743 0.1834 0.3727 -0.1239 -0.0457 0.0143  282 ASP B N   
8594 C CA  . ASP B 264 ? 0.4499 0.1914 0.3679 -0.0982 -0.0537 0.0202  282 ASP B CA  
8595 C C   . ASP B 264 ? 0.4097 0.1808 0.3808 -0.0766 -0.0478 0.0321  282 ASP B C   
8596 O O   . ASP B 264 ? 0.3747 0.1785 0.3858 -0.0469 -0.0785 0.0545  282 ASP B O   
8597 C CB  . ASP B 264 ? 0.4590 0.2024 0.3545 -0.1024 -0.0513 0.0227  282 ASP B CB  
8598 C CG  . ASP B 264 ? 0.4565 0.2375 0.3400 -0.0932 -0.0670 0.0258  282 ASP B CG  
8599 O OD1 . ASP B 264 ? 0.4450 0.2591 0.3356 -0.0569 -0.0691 0.0115  282 ASP B OD1 
8600 O OD2 . ASP B 264 ? 0.4751 0.2546 0.3408 -0.0985 -0.0622 0.0237  282 ASP B OD2 
8605 N N   . CYS B 265 ? 0.4092 0.1758 0.3730 -0.0928 -0.0266 0.0285  283 CYS B N   
8606 C CA  . CYS B 265 ? 0.4064 0.1813 0.3760 -0.1119 -0.0109 0.0228  283 CYS B CA  
8607 C C   . CYS B 265 ? 0.4185 0.1748 0.3740 -0.0940 0.0192  0.0389  283 CYS B C   
8608 O O   . CYS B 265 ? 0.4117 0.2221 0.3819 -0.0618 0.0470  0.0353  283 CYS B O   
8609 C CB  . CYS B 265 ? 0.4278 0.1895 0.3867 -0.0984 -0.0330 0.0224  283 CYS B CB  
8610 S SG  . CYS B 265 ? 0.4281 0.1972 0.4033 -0.0871 -0.0339 0.0273  283 CYS B SG  
8615 N N   . ASN B 266 ? 0.3879 0.1568 0.3573 -0.0642 -0.0151 0.0309  284 ASN B N   
8616 C CA  . ASN B 266 ? 0.4119 0.1477 0.3590 -0.0623 -0.0361 0.0239  284 ASN B CA  
8617 C C   . ASN B 266 ? 0.4206 0.1432 0.3463 -0.0599 -0.0422 0.0304  284 ASN B C   
8618 O O   . ASN B 266 ? 0.4057 0.1464 0.3487 -0.0447 -0.0401 0.0263  284 ASN B O   
8619 C CB  . ASN B 266 ? 0.4281 0.1512 0.3611 -0.0453 -0.0348 0.0194  284 ASN B CB  
8620 C CG  . ASN B 266 ? 0.4292 0.1559 0.3614 -0.0286 -0.0441 0.0257  284 ASN B CG  
8621 O OD1 . ASN B 266 ? 0.4212 0.1657 0.3415 -0.0151 -0.0478 0.0380  284 ASN B OD1 
8622 N ND2 . ASN B 266 ? 0.4505 0.1440 0.3796 -0.0377 -0.0141 0.0225  284 ASN B ND2 
8629 N N   . PRO B 267 ? 0.4545 0.1451 0.3280 -0.0563 -0.0516 0.0223  285 PRO B N   
8630 C CA  . PRO B 267 ? 0.4656 0.1515 0.3302 -0.0481 -0.0573 0.0309  285 PRO B CA  
8631 C C   . PRO B 267 ? 0.4278 0.1431 0.3324 -0.0681 -0.0943 0.0183  285 PRO B C   
8632 O O   . PRO B 267 ? 0.4461 0.1394 0.3461 -0.0570 -0.0903 0.0114  285 PRO B O   
8633 C CB  . PRO B 267 ? 0.4761 0.1523 0.3367 -0.0433 -0.0454 0.0367  285 PRO B CB  
8634 C CG  . PRO B 267 ? 0.4729 0.1399 0.3297 -0.0576 -0.0470 0.0227  285 PRO B CG  
8635 C CD  . PRO B 267 ? 0.4887 0.1342 0.3423 -0.0448 -0.0316 0.0301  285 PRO B CD  
8643 N N   . LEU B 268 ? 0.4510 0.1538 0.3210 -0.0523 -0.0780 0.0129  286 LEU B N   
8644 C CA  . LEU B 268 ? 0.4533 0.1518 0.3309 -0.0349 -0.0853 0.0310  286 LEU B CA  
8645 C C   . LEU B 268 ? 0.4306 0.1374 0.3162 -0.0291 -0.1081 0.0295  286 LEU B C   
8646 O O   . LEU B 268 ? 0.4159 0.1439 0.3225 -0.0343 -0.0999 0.0168  286 LEU B O   
8647 C CB  . LEU B 268 ? 0.5179 0.1865 0.3685 -0.0224 -0.0490 0.0775  286 LEU B CB  
8648 C CG  . LEU B 268 ? 0.5896 0.2258 0.4043 -0.0084 -0.0200 0.0907  286 LEU B CG  
8649 C CD1 . LEU B 268 ? 0.6029 0.2349 0.4256 0.0045  -0.0195 0.1044  286 LEU B CD1 
8650 C CD2 . LEU B 268 ? 0.6107 0.2481 0.4077 -0.0038 -0.0224 0.0898  286 LEU B CD2 
8662 N N   . PRO B 269 ? 0.4264 0.1303 0.3106 0.0001  -0.1069 0.0270  287 PRO B N   
8663 C CA  . PRO B 269 ? 0.4499 0.1368 0.3159 0.0099  -0.0904 0.0141  287 PRO B CA  
8664 C C   . PRO B 269 ? 0.4460 0.1231 0.3058 -0.0106 -0.0907 0.0006  287 PRO B C   
8665 O O   . PRO B 269 ? 0.4741 0.1294 0.3052 0.0011  -0.0934 -0.0087 287 PRO B O   
8666 C CB  . PRO B 269 ? 0.4299 0.1378 0.3134 0.0091  -0.1223 0.0067  287 PRO B CB  
8667 C CG  . PRO B 269 ? 0.4351 0.1498 0.3261 -0.0045 -0.1147 0.0212  287 PRO B CG  
8668 C CD  . PRO B 269 ? 0.4401 0.1437 0.3188 0.0095  -0.1029 0.0359  287 PRO B CD  
8676 N N   . ALA B 270 ? 0.4368 0.1176 0.2960 -0.0054 -0.0759 0.0029  288 ALA B N   
8677 C CA  . ALA B 270 ? 0.4202 0.1178 0.3166 0.0015  -0.0877 0.0062  288 ALA B CA  
8678 C C   . ALA B 270 ? 0.4120 0.1176 0.3274 -0.0023 -0.0913 0.0001  288 ALA B C   
8679 O O   . ALA B 270 ? 0.3937 0.1203 0.3299 -0.0185 -0.1085 0.0035  288 ALA B O   
8680 C CB  . ALA B 270 ? 0.4075 0.1198 0.3141 -0.0196 -0.1015 0.0079  288 ALA B CB  
8686 N N   . ASN B 271 ? 0.3719 0.1125 0.3260 -0.0198 -0.0889 -0.0048 289 ASN B N   
8687 C CA  . ASN B 271 ? 0.4152 0.1228 0.3285 -0.0030 -0.1011 -0.0188 289 ASN B CA  
8688 C C   . ASN B 271 ? 0.4221 0.1443 0.3237 0.0065  -0.0911 -0.0029 289 ASN B C   
8689 O O   . ASN B 271 ? 0.4369 0.1706 0.3183 0.0134  -0.1082 -0.0020 289 ASN B O   
8690 C CB  . ASN B 271 ? 0.4401 0.1388 0.3461 -0.0473 -0.0806 -0.0325 289 ASN B CB  
8691 C CG  . ASN B 271 ? 0.4803 0.1530 0.3683 -0.0635 -0.0542 -0.0489 289 ASN B CG  
8692 O OD1 . ASN B 271 ? 0.5041 0.1912 0.3902 -0.0886 -0.0358 -0.0773 289 ASN B OD1 
8693 N ND2 . ASN B 271 ? 0.4741 0.1362 0.3691 -0.0592 -0.0236 -0.0292 289 ASN B ND2 
8700 N N   . ASP B 272 ? 0.4321 0.1364 0.3385 -0.0191 -0.0729 -0.0127 290 ASP B N   
8701 C CA  . ASP B 272 ? 0.4131 0.1446 0.3315 -0.0128 -0.0937 -0.0010 290 ASP B CA  
8702 C C   . ASP B 272 ? 0.4028 0.1536 0.3263 -0.0075 -0.0814 0.0095  290 ASP B C   
8703 O O   . ASP B 272 ? 0.4285 0.1754 0.3362 -0.0178 -0.0706 0.0172  290 ASP B O   
8704 C CB  . ASP B 272 ? 0.4330 0.1655 0.3513 -0.0256 -0.0939 0.0067  290 ASP B CB  
8705 C CG  . ASP B 272 ? 0.4626 0.1884 0.3794 -0.0374 -0.0980 -0.0139 290 ASP B CG  
8706 O OD1 . ASP B 272 ? 0.4669 0.2090 0.4026 -0.0322 -0.1047 -0.0434 290 ASP B OD1 
8707 O OD2 . ASP B 272 ? 0.4750 0.2054 0.3924 -0.0253 -0.0905 -0.0155 290 ASP B OD2 
8712 N N   . LEU B 273 ? 0.3823 0.1489 0.3094 0.0069  -0.0851 0.0012  291 LEU B N   
8713 C CA  . LEU B 273 ? 0.3554 0.1521 0.3037 0.0220  -0.0983 0.0152  291 LEU B CA  
8714 C C   . LEU B 273 ? 0.3900 0.1512 0.3092 0.0259  -0.0747 0.0011  291 LEU B C   
8715 O O   . LEU B 273 ? 0.3924 0.1697 0.3242 0.0381  -0.0682 0.0155  291 LEU B O   
8716 C CB  . LEU B 273 ? 0.3529 0.1421 0.2882 0.0310  -0.1005 0.0267  291 LEU B CB  
8717 C CG  . LEU B 273 ? 0.3712 0.1501 0.2897 0.0061  -0.0689 0.0134  291 LEU B CG  
8718 C CD1 . LEU B 273 ? 0.3913 0.1631 0.2793 -0.0063 -0.0656 -0.0153 291 LEU B CD1 
8719 C CD2 . LEU B 273 ? 0.3409 0.1631 0.2842 -0.0020 -0.0619 0.0223  291 LEU B CD2 
8731 N N   . THR B 274 ? 0.3885 0.1428 0.3278 0.0478  -0.0664 -0.0073 292 THR B N   
8732 C CA  . THR B 274 ? 0.3780 0.1485 0.3473 0.0507  -0.0764 0.0074  292 THR B CA  
8733 C C   . THR B 274 ? 0.4000 0.1467 0.3523 0.0511  -0.0831 0.0091  292 THR B C   
8734 O O   . THR B 274 ? 0.3736 0.1504 0.3576 0.0363  -0.0912 0.0103  292 THR B O   
8735 C CB  . THR B 274 ? 0.3821 0.1642 0.3616 0.0585  -0.0770 0.0225  292 THR B CB  
8736 O OG1 . THR B 274 ? 0.4089 0.1753 0.3616 0.0749  -0.0753 0.0280  292 THR B OG1 
8737 C CG2 . THR B 274 ? 0.4147 0.1611 0.3638 0.0586  -0.0641 0.0517  292 THR B CG2 
8745 N N   . PRO B 275 ? 0.4308 0.1465 0.3487 0.0790  -0.0836 -0.0011 293 PRO B N   
8746 C CA  . PRO B 275 ? 0.4357 0.1512 0.3317 0.0777  -0.1075 -0.0077 293 PRO B CA  
8747 C C   . PRO B 275 ? 0.4427 0.1656 0.3261 0.0737  -0.0953 -0.0098 293 PRO B C   
8748 O O   . PRO B 275 ? 0.4450 0.1611 0.3180 0.0741  -0.0723 -0.0057 293 PRO B O   
8749 C CB  . PRO B 275 ? 0.4595 0.1603 0.3258 0.0854  -0.1145 -0.0118 293 PRO B CB  
8750 C CG  . PRO B 275 ? 0.4851 0.1531 0.3446 0.0748  -0.0945 -0.0093 293 PRO B CG  
8751 C CD  . PRO B 275 ? 0.4804 0.1500 0.3553 0.0741  -0.0841 -0.0168 293 PRO B CD  
8759 N N   A GLU B 276 ? 0.4134 0.1795 0.3271 0.0825  -0.1140 -0.0094 294 GLU B N   
8760 N N   B GLU B 276 ? 0.4438 0.1813 0.3291 0.0760  -0.1004 -0.0094 294 GLU B N   
8761 C CA  A GLU B 276 ? 0.4198 0.1925 0.3335 0.0944  -0.1061 0.0007  294 GLU B CA  
8762 C CA  B GLU B 276 ? 0.4651 0.1962 0.3342 0.0793  -0.0920 -0.0014 294 GLU B CA  
8763 C C   A GLU B 276 ? 0.4406 0.1840 0.3039 0.0830  -0.1051 0.0012  294 GLU B C   
8764 C C   B GLU B 276 ? 0.4531 0.1871 0.3100 0.0776  -0.0995 -0.0006 294 GLU B C   
8765 O O   A GLU B 276 ? 0.4599 0.1749 0.2765 0.0745  -0.1217 -0.0067 294 GLU B O   
8766 O O   B GLU B 276 ? 0.4616 0.1833 0.2991 0.0716  -0.1063 -0.0062 294 GLU B O   
8767 C CB  A GLU B 276 ? 0.3943 0.2233 0.3596 0.1077  -0.1221 -0.0042 294 GLU B CB  
8768 C CB  B GLU B 276 ? 0.4934 0.2259 0.3573 0.0783  -0.0895 -0.0036 294 GLU B CB  
8769 C CG  A GLU B 276 ? 0.3759 0.2480 0.3814 0.1145  -0.1129 -0.0292 294 GLU B CG  
8770 C CG  B GLU B 276 ? 0.5201 0.2505 0.3779 0.0753  -0.0802 -0.0165 294 GLU B CG  
8771 C CD  A GLU B 276 ? 0.3661 0.2669 0.4109 0.1136  -0.0731 -0.0794 294 GLU B CD  
8772 C CD  B GLU B 276 ? 0.5409 0.2763 0.3920 0.0748  -0.0737 -0.0274 294 GLU B CD  
8773 O OE1 A GLU B 276 ? 0.2821 0.2596 0.3798 0.1339  -0.1174 -0.0943 294 GLU B OE1 
8774 O OE1 B GLU B 276 ? 0.4915 0.2817 0.3885 0.1018  -0.1242 -0.0088 294 GLU B OE1 
8775 O OE2 A GLU B 276 ? 0.4341 0.2999 0.4465 0.0558  -0.0355 -0.0951 294 GLU B OE2 
8776 O OE2 B GLU B 276 ? 0.5706 0.2813 0.4039 0.0696  -0.0367 -0.0420 294 GLU B OE2 
8789 N N   . GLN B 277 ? 0.4242 0.1773 0.2894 0.0846  -0.1157 0.0028  295 GLN B N   
8790 C CA  . GLN B 277 ? 0.3639 0.1580 0.2725 0.0947  -0.1017 -0.0064 295 GLN B CA  
8791 C C   . GLN B 277 ? 0.3882 0.1556 0.2716 0.0444  -0.0954 -0.0053 295 GLN B C   
8792 O O   . GLN B 277 ? 0.3766 0.1372 0.2851 0.0297  -0.0831 0.0077  295 GLN B O   
8793 C CB  . GLN B 277 ? 0.3834 0.1637 0.2717 0.0761  -0.0691 -0.0054 295 GLN B CB  
8794 C CG  . GLN B 277 ? 0.3948 0.1689 0.2704 0.0410  -0.0583 -0.0177 295 GLN B CG  
8795 C CD  . GLN B 277 ? 0.3981 0.1896 0.2689 0.0340  -0.0665 -0.0116 295 GLN B CD  
8796 O OE1 . GLN B 277 ? 0.4069 0.1879 0.2896 0.0338  -0.0522 -0.0030 295 GLN B OE1 
8797 N NE2 . GLN B 277 ? 0.3956 0.2055 0.2663 0.0482  -0.0648 -0.0157 295 GLN B NE2 
8806 N N   . LYS B 278 ? 0.4022 0.1400 0.2879 0.0282  -0.0779 -0.0116 296 LYS B N   
8807 C CA  . LYS B 278 ? 0.4064 0.1387 0.3074 0.0119  -0.0754 -0.0030 296 LYS B CA  
8808 C C   . LYS B 278 ? 0.3887 0.1591 0.3068 0.0321  -0.0909 0.0072  296 LYS B C   
8809 O O   . LYS B 278 ? 0.3754 0.1695 0.3145 0.0496  -0.0870 -0.0044 296 LYS B O   
8810 C CB  . LYS B 278 ? 0.4294 0.1205 0.3210 -0.0068 -0.0885 -0.0043 296 LYS B CB  
8811 C CG  . LYS B 278 ? 0.4518 0.1271 0.3103 -0.0016 -0.0900 -0.0145 296 LYS B CG  
8812 C CD  . LYS B 278 ? 0.4726 0.1437 0.2949 -0.0073 -0.0921 -0.0116 296 LYS B CD  
8813 C CE  . LYS B 278 ? 0.4624 0.1586 0.3002 -0.0187 -0.0942 -0.0150 296 LYS B CE  
8814 N NZ  . LYS B 278 ? 0.5088 0.1850 0.3011 -0.0134 -0.0813 -0.0071 296 LYS B NZ  
8828 N N   . VAL B 279 ? 0.3717 0.1639 0.3159 0.0169  -0.0991 0.0024  297 VAL B N   
8829 C CA  . VAL B 279 ? 0.3724 0.1793 0.3220 0.0382  -0.1086 -0.0013 297 VAL B CA  
8830 C C   . VAL B 279 ? 0.3740 0.1761 0.3397 0.0319  -0.1020 -0.0066 297 VAL B C   
8831 O O   . VAL B 279 ? 0.3577 0.1828 0.3401 0.0391  -0.1132 -0.0122 297 VAL B O   
8832 C CB  . VAL B 279 ? 0.3791 0.1926 0.3223 0.0477  -0.1104 -0.0104 297 VAL B CB  
8833 C CG1 . VAL B 279 ? 0.3782 0.2119 0.3194 0.0444  -0.1124 -0.0251 297 VAL B CG1 
8834 C CG2 . VAL B 279 ? 0.3921 0.1913 0.3491 0.0425  -0.0753 -0.0189 297 VAL B CG2 
8844 N N   . ALA B 280 ? 0.3536 0.1637 0.3405 0.0152  -0.1063 -0.0055 298 ALA B N   
8845 C CA  . ALA B 280 ? 0.3608 0.1561 0.3432 -0.0034 -0.0978 0.0032  298 ALA B CA  
8846 C C   . ALA B 280 ? 0.3677 0.1262 0.3221 0.0101  -0.1145 0.0093  298 ALA B C   
8847 O O   . ALA B 280 ? 0.3778 0.1212 0.3063 -0.0052 -0.1201 0.0107  298 ALA B O   
8848 C CB  . ALA B 280 ? 0.3470 0.1678 0.3415 0.0002  -0.0935 0.0047  298 ALA B CB  
8854 N N   . ALA B 281 ? 0.3726 0.1196 0.3229 0.0134  -0.1085 -0.0109 299 ALA B N   
8855 C CA  . ALA B 281 ? 0.3952 0.1343 0.3043 0.0128  -0.1126 -0.0239 299 ALA B CA  
8856 C C   . ALA B 281 ? 0.4320 0.1514 0.3093 0.0128  -0.0903 0.0008  299 ALA B C   
8857 O O   . ALA B 281 ? 0.4067 0.1592 0.3095 0.0268  -0.0911 -0.0028 299 ALA B O   
8858 C CB  . ALA B 281 ? 0.3957 0.1290 0.2965 0.0458  -0.1168 -0.0307 299 ALA B CB  
8864 N N   . ALA B 282 ? 0.4820 0.1610 0.2987 -0.0074 -0.0793 0.0091  300 ALA B N   
8865 C CA  . ALA B 282 ? 0.4842 0.1722 0.3041 0.0028  -0.0878 0.0498  300 ALA B CA  
8866 C C   . ALA B 282 ? 0.4786 0.1841 0.2983 0.0175  -0.1032 0.0394  300 ALA B C   
8867 O O   . ALA B 282 ? 0.4984 0.2192 0.3248 0.0301  -0.0656 0.0099  300 ALA B O   
8868 C CB  . ALA B 282 ? 0.5041 0.1700 0.3184 0.0031  -0.0590 0.0756  300 ALA B CB  
8874 N N   . ALA B 283 ? 0.4543 0.1937 0.2952 0.0549  -0.1366 0.0490  301 ALA B N   
8875 C CA  . ALA B 283 ? 0.4314 0.1985 0.3006 0.0632  -0.1421 0.0216  301 ALA B CA  
8876 C C   . ALA B 283 ? 0.4295 0.2019 0.2878 0.0573  -0.1311 0.0200  301 ALA B C   
8877 O O   . ALA B 283 ? 0.4332 0.2192 0.3103 0.0552  -0.1366 0.0271  301 ALA B O   
8878 C CB  . ALA B 283 ? 0.4744 0.2102 0.3018 0.0802  -0.1446 0.0271  301 ALA B CB  
8884 N N   . LEU B 284 ? 0.4069 0.1870 0.2628 0.0528  -0.1400 0.0156  302 LEU B N   
8885 C CA  . LEU B 284 ? 0.4094 0.1686 0.2711 0.0357  -0.1170 0.0228  302 LEU B CA  
8886 C C   . LEU B 284 ? 0.4076 0.1760 0.2729 0.0352  -0.1103 0.0208  302 LEU B C   
8887 O O   . LEU B 284 ? 0.3917 0.2074 0.2841 0.0114  -0.1255 -0.0011 302 LEU B O   
8888 C CB  . LEU B 284 ? 0.4141 0.1644 0.2753 -0.0001 -0.1161 0.0171  302 LEU B CB  
8889 C CG  . LEU B 284 ? 0.4025 0.1601 0.2839 0.0079  -0.1177 0.0297  302 LEU B CG  
8890 C CD1 . LEU B 284 ? 0.4523 0.1725 0.2611 -0.0026 -0.0923 0.0031  302 LEU B CD1 
8891 C CD2 . LEU B 284 ? 0.4024 0.1578 0.2858 0.0088  -0.1436 0.0285  302 LEU B CD2 
8903 N N   . LEU B 285 ? 0.4404 0.1624 0.2606 0.0357  -0.0961 0.0284  303 LEU B N   
8904 C CA  . LEU B 285 ? 0.4614 0.1405 0.2692 0.0374  -0.0871 0.0275  303 LEU B CA  
8905 C C   . LEU B 285 ? 0.4488 0.1379 0.2790 0.0375  -0.1000 0.0225  303 LEU B C   
8906 O O   . LEU B 285 ? 0.4227 0.1255 0.3083 0.0267  -0.0478 0.0460  303 LEU B O   
8907 C CB  . LEU B 285 ? 0.4794 0.1572 0.2952 0.0428  -0.0835 0.0136  303 LEU B CB  
8908 C CG  . LEU B 285 ? 0.5125 0.1789 0.3147 0.0300  -0.0515 0.0017  303 LEU B CG  
8909 C CD1 . LEU B 285 ? 0.5134 0.1866 0.3080 0.0466  -0.0750 0.0157  303 LEU B CD1 
8910 C CD2 . LEU B 285 ? 0.5452 0.1988 0.3314 0.0186  -0.0275 -0.0051 303 LEU B CD2 
8922 N N   . ALA B 286 ? 0.4966 0.1570 0.2773 0.0082  -0.1361 0.0232  304 ALA B N   
8923 C CA  . ALA B 286 ? 0.4889 0.1498 0.2902 0.0061  -0.1497 0.0178  304 ALA B CA  
8924 C C   . ALA B 286 ? 0.4728 0.1432 0.3066 0.0216  -0.1536 -0.0154 304 ALA B C   
8925 O O   . ALA B 286 ? 0.4900 0.1541 0.3046 0.0368  -0.1744 -0.0239 304 ALA B O   
8926 C CB  . ALA B 286 ? 0.4770 0.1739 0.3064 0.0200  -0.1607 0.0404  304 ALA B CB  
8932 N N   . PRO B 287 ? 0.4412 0.1538 0.3047 0.0035  -0.1534 -0.0332 305 PRO B N   
8933 C CA  . PRO B 287 ? 0.4022 0.1711 0.3107 0.0101  -0.1453 -0.0537 305 PRO B CA  
8934 C C   . PRO B 287 ? 0.3340 0.1600 0.3022 0.0114  -0.1412 -0.0449 305 PRO B C   
8935 O O   . PRO B 287 ? 0.3032 0.1661 0.3044 0.0162  -0.1118 -0.0223 305 PRO B O   
8936 C CB  . PRO B 287 ? 0.4244 0.1891 0.3246 0.0061  -0.1392 -0.0605 305 PRO B CB  
8937 C CG  . PRO B 287 ? 0.4421 0.1876 0.3290 -0.0139 -0.1417 -0.0693 305 PRO B CG  
8938 C CD  . PRO B 287 ? 0.4455 0.1722 0.3000 0.0077  -0.1467 -0.0629 305 PRO B CD  
8946 N N   . ALA B 288 ? 0.3070 0.1607 0.2950 0.0063  -0.1433 -0.0236 306 ALA B N   
8947 C CA  . ALA B 288 ? 0.2902 0.1549 0.2695 0.0074  -0.1358 0.0287  306 ALA B CA  
8948 C C   . ALA B 288 ? 0.3013 0.1421 0.2664 -0.0072 -0.0942 0.0414  306 ALA B C   
8949 O O   . ALA B 288 ? 0.3105 0.1241 0.2595 -0.0282 -0.0755 0.0461  306 ALA B O   
8950 C CB  . ALA B 288 ? 0.2861 0.1561 0.2790 0.0039  -0.1149 0.0376  306 ALA B CB  
8956 N N   . ALA B 289 ? 0.2789 0.1571 0.2590 -0.0109 -0.0907 0.0327  307 ALA B N   
8957 C CA  . ALA B 289 ? 0.2902 0.1657 0.2474 -0.0065 -0.0991 0.0474  307 ALA B CA  
8958 C C   . ALA B 289 ? 0.2697 0.1281 0.2217 -0.0186 -0.1014 0.0392  307 ALA B C   
8959 O O   . ALA B 289 ? 0.3036 0.1130 0.2401 0.0007  -0.0669 0.0153  307 ALA B O   
8960 C CB  . ALA B 289 ? 0.3259 0.1753 0.2737 -0.0041 -0.0864 0.0806  307 ALA B CB  
8966 N N   . ALA B 290 ? 0.3024 0.1282 0.2224 -0.0281 -0.0765 0.0334  308 ALA B N   
8967 C CA  . ALA B 290 ? 0.2736 0.1178 0.2198 0.0059  -0.0768 0.0402  308 ALA B CA  
8968 C C   . ALA B 290 ? 0.2732 0.1129 0.2067 0.0045  -0.0947 0.0212  308 ALA B C   
8969 O O   . ALA B 290 ? 0.2795 0.1374 0.2120 -0.0038 -0.0815 0.0003  308 ALA B O   
8970 C CB  . ALA B 290 ? 0.2880 0.1234 0.2305 0.0068  -0.0701 0.0333  308 ALA B CB  
8976 N N   . ALA B 291 ? 0.3052 0.1089 0.2011 -0.0014 -0.0846 -0.0026 309 ALA B N   
8977 C CA  . ALA B 291 ? 0.3058 0.1206 0.2083 0.0173  -0.0836 -0.0062 309 ALA B CA  
8978 C C   . ALA B 291 ? 0.2982 0.1059 0.2094 0.0107  -0.0722 -0.0031 309 ALA B C   
8979 O O   . ALA B 291 ? 0.2642 0.1148 0.1953 -0.0148 -0.0617 0.0118  309 ALA B O   
8980 C CB  . ALA B 291 ? 0.3264 0.1329 0.2059 0.0093  -0.1074 -0.0011 309 ALA B CB  
8986 N N   . ILE B 292 ? 0.2912 0.0882 0.2042 0.0091  -0.0489 0.0212  310 ILE B N   
8987 C CA  . ILE B 292 ? 0.2856 0.1132 0.2000 0.0089  -0.0602 0.0090  310 ILE B CA  
8988 C C   . ILE B 292 ? 0.2652 0.1104 0.1891 0.0009  -0.0683 0.0204  310 ILE B C   
8989 O O   . ILE B 292 ? 0.2888 0.1142 0.1975 0.0002  -0.0476 0.0002  310 ILE B O   
8990 C CB  . ILE B 292 ? 0.3094 0.1418 0.1962 0.0082  -0.0663 0.0052  310 ILE B CB  
8991 C CG1 . ILE B 292 ? 0.3377 0.1830 0.2132 0.0066  -0.0831 0.0056  310 ILE B CG1 
8992 C CG2 . ILE B 292 ? 0.3307 0.1396 0.1989 0.0205  -0.0677 0.0065  310 ILE B CG2 
8993 C CD1 . ILE B 292 ? 0.3559 0.1972 0.2237 0.0012  -0.0911 0.0297  310 ILE B CD1 
9005 N N   . VAL B 293 ? 0.2795 0.1040 0.1970 -0.0197 -0.0681 0.0321  311 VAL B N   
9006 C CA  . VAL B 293 ? 0.2838 0.1284 0.2041 -0.0200 -0.0888 0.0381  311 VAL B CA  
9007 C C   . VAL B 293 ? 0.2903 0.1399 0.2090 -0.0108 -0.0911 0.0457  311 VAL B C   
9008 O O   . VAL B 293 ? 0.3188 0.1440 0.2421 -0.0343 -0.0881 0.0188  311 VAL B O   
9009 C CB  . VAL B 293 ? 0.2823 0.1563 0.2116 0.0039  -0.1149 0.0438  311 VAL B CB  
9010 C CG1 . VAL B 293 ? 0.2892 0.1852 0.2381 0.0035  -0.1293 0.0449  311 VAL B CG1 
9011 C CG2 . VAL B 293 ? 0.3143 0.1655 0.2282 0.0187  -0.0753 0.0466  311 VAL B CG2 
9021 N N   . ALA B 294 ? 0.2674 0.1625 0.2380 -0.0177 -0.0717 0.0439  312 ALA B N   
9022 C CA  . ALA B 294 ? 0.2483 0.1706 0.2458 0.0105  -0.0635 0.0246  312 ALA B CA  
9023 C C   . ALA B 294 ? 0.2571 0.1536 0.2504 -0.0001 -0.0520 0.0189  312 ALA B C   
9024 O O   . ALA B 294 ? 0.2827 0.1742 0.2589 -0.0154 -0.0501 0.0401  312 ALA B O   
9025 C CB  . ALA B 294 ? 0.2566 0.1821 0.2647 0.0362  -0.0540 0.0237  312 ALA B CB  
9031 N N   . GLY B 295 ? 0.2539 0.1151 0.2240 0.0281  -0.0673 0.0090  313 GLY B N   
9032 C CA  . GLY B 295 ? 0.2433 0.0897 0.2098 0.0092  -0.0862 -0.0100 313 GLY B CA  
9033 C C   . GLY B 295 ? 0.2494 0.0982 0.2139 -0.0015 -0.0694 -0.0022 313 GLY B C   
9034 O O   . GLY B 295 ? 0.2650 0.1050 0.2398 -0.0054 -0.0547 0.0153  313 GLY B O   
9038 N N   . PRO B 296 ? 0.2512 0.0934 0.1853 0.0106  -0.0448 0.0006  314 PRO B N   
9039 C CA  . PRO B 296 ? 0.2321 0.1068 0.1983 0.0076  -0.0582 0.0052  314 PRO B CA  
9040 C C   . PRO B 296 ? 0.2054 0.1181 0.1992 0.0027  -0.0549 0.0181  314 PRO B C   
9041 O O   . PRO B 296 ? 0.2095 0.1246 0.2170 0.0085  -0.0396 0.0078  314 PRO B O   
9042 C CB  . PRO B 296 ? 0.2732 0.1197 0.2105 0.0160  -0.0424 -0.0010 314 PRO B CB  
9043 C CG  . PRO B 296 ? 0.3171 0.1375 0.2187 0.0300  -0.0159 -0.0015 314 PRO B CG  
9044 C CD  . PRO B 296 ? 0.2519 0.1193 0.2045 0.0329  -0.0367 -0.0050 314 PRO B CD  
9052 N N   . LYS B 297 ? 0.2086 0.1189 0.2214 -0.0198 -0.0537 0.0193  315 LYS B N   
9053 C CA  . LYS B 297 ? 0.2233 0.1199 0.2180 -0.0375 -0.0579 0.0166  315 LYS B CA  
9054 C C   . LYS B 297 ? 0.2251 0.1082 0.2124 -0.0176 -0.0648 0.0077  315 LYS B C   
9055 O O   . LYS B 297 ? 0.2149 0.1155 0.2473 -0.0095 -0.0260 0.0272  315 LYS B O   
9056 C CB  . LYS B 297 ? 0.2454 0.1503 0.2212 -0.0069 -0.0370 0.0410  315 LYS B CB  
9057 C CG  . LYS B 297 ? 0.2937 0.1625 0.2353 -0.0091 -0.0477 0.0310  315 LYS B CG  
9058 C CD  . LYS B 297 ? 0.3840 0.1790 0.2491 -0.0416 -0.0432 0.0328  315 LYS B CD  
9059 C CE  . LYS B 297 ? 0.4440 0.1979 0.2883 -0.0642 -0.0850 0.0198  315 LYS B CE  
9060 N NZ  . LYS B 297 ? 0.4938 0.2196 0.3152 -0.0735 -0.0518 0.0077  315 LYS B NZ  
9074 N N   . GLN B 298 ? 0.2254 0.0965 0.1959 -0.0023 -0.0652 -0.0019 316 GLN B N   
9075 C CA  . GLN B 298 ? 0.2561 0.1032 0.1919 0.0022  -0.0412 0.0033  316 GLN B CA  
9076 C C   . GLN B 298 ? 0.2403 0.1135 0.1793 0.0144  -0.0391 0.0090  316 GLN B C   
9077 O O   . GLN B 298 ? 0.2462 0.1180 0.1998 -0.0082 -0.0287 0.0169  316 GLN B O   
9078 C CB  . GLN B 298 ? 0.2414 0.1004 0.1954 0.0151  -0.0516 -0.0037 316 GLN B CB  
9079 C CG  . GLN B 298 ? 0.2362 0.1049 0.2051 -0.0020 -0.0383 -0.0046 316 GLN B CG  
9080 C CD  . GLN B 298 ? 0.2009 0.1296 0.1906 0.0127  -0.0175 0.0050  316 GLN B CD  
9081 O OE1 . GLN B 298 ? 0.2026 0.1225 0.1967 -0.0040 -0.0258 0.0137  316 GLN B OE1 
9082 N NE2 . GLN B 298 ? 0.2063 0.1648 0.1812 0.0321  -0.0054 0.0092  316 GLN B NE2 
9091 N N   . ASN B 299 ? 0.2277 0.1233 0.1724 0.0255  -0.0266 0.0123  317 ASN B N   
9092 C CA  . ASN B 299 ? 0.2145 0.1306 0.1769 -0.0009 -0.0248 -0.0154 317 ASN B CA  
9093 C C   . ASN B 299 ? 0.2232 0.1201 0.1856 -0.0178 0.0057  0.0090  317 ASN B C   
9094 O O   . ASN B 299 ? 0.2424 0.1440 0.2166 -0.0207 -0.0108 0.0125  317 ASN B O   
9095 C CB  . ASN B 299 ? 0.2775 0.1220 0.1790 0.0013  -0.0222 -0.0112 317 ASN B CB  
9096 C CG  . ASN B 299 ? 0.2634 0.1270 0.1906 -0.0043 -0.0472 -0.0052 317 ASN B CG  
9097 O OD1 . ASN B 299 ? 0.2514 0.1326 0.2022 0.0026  -0.0531 -0.0138 317 ASN B OD1 
9098 N ND2 . ASN B 299 ? 0.3172 0.1324 0.2266 -0.0070 -0.0186 0.0004  317 ASN B ND2 
9105 N N   . CYS B 300 ? 0.2083 0.1200 0.1638 -0.0026 -0.0253 -0.0008 318 CYS B N   
9106 C CA  . CYS B 300 ? 0.1764 0.1088 0.1673 0.0013  -0.0238 -0.0002 318 CYS B CA  
9107 C C   . CYS B 300 ? 0.1907 0.1185 0.1873 0.0054  -0.0330 0.0016  318 CYS B C   
9108 O O   . CYS B 300 ? 0.1928 0.1124 0.2020 0.0207  -0.0336 0.0044  318 CYS B O   
9109 C CB  . CYS B 300 ? 0.2161 0.1383 0.2021 0.0100  -0.0256 0.0082  318 CYS B CB  
9110 S SG  . CYS B 300 ? 0.2295 0.1462 0.2338 0.0014  -0.0515 0.0167  318 CYS B SG  
9115 N N   . GLU B 301 ? 0.2097 0.1385 0.1907 0.0102  -0.0335 -0.0021 319 GLU B N   
9116 C CA  . GLU B 301 ? 0.2022 0.1242 0.1983 0.0035  -0.0344 -0.0145 319 GLU B CA  
9117 C C   . GLU B 301 ? 0.1894 0.1214 0.2047 -0.0055 -0.0394 -0.0071 319 GLU B C   
9118 O O   . GLU B 301 ? 0.2123 0.1021 0.1953 -0.0121 -0.0049 -0.0027 319 GLU B O   
9119 C CB  . GLU B 301 ? 0.1978 0.1264 0.2052 0.0050  -0.0183 -0.0038 319 GLU B CB  
9120 C CG  . GLU B 301 ? 0.2070 0.1169 0.2063 0.0046  -0.0293 0.0019  319 GLU B CG  
9121 C CD  . GLU B 301 ? 0.2039 0.1354 0.2059 0.0192  -0.0289 -0.0053 319 GLU B CD  
9122 O OE1 . GLU B 301 ? 0.1807 0.1664 0.2092 -0.0042 -0.0392 0.0075  319 GLU B OE1 
9123 O OE2 . GLU B 301 ? 0.2032 0.1395 0.2036 0.0269  -0.0192 -0.0161 319 GLU B OE2 
9130 N N   . PRO B 302 ? 0.1794 0.1122 0.2086 0.0065  -0.0505 0.0134  320 PRO B N   
9131 C CA  . PRO B 302 ? 0.1834 0.0988 0.2203 -0.0141 -0.0210 0.0116  320 PRO B CA  
9132 C C   . PRO B 302 ? 0.1927 0.0991 0.2098 0.0015  -0.0158 0.0026  320 PRO B C   
9133 O O   . PRO B 302 ? 0.2044 0.1156 0.2039 0.0124  -0.0328 0.0019  320 PRO B O   
9134 C CB  . PRO B 302 ? 0.2073 0.1322 0.2401 0.0207  -0.0172 0.0177  320 PRO B CB  
9135 C CG  . PRO B 302 ? 0.2158 0.1168 0.2373 -0.0110 -0.0138 0.0292  320 PRO B CG  
9136 C CD  . PRO B 302 ? 0.2049 0.1056 0.2172 0.0039  -0.0245 0.0138  320 PRO B CD  
9144 N N   . ASP B 303 ? 0.2121 0.0946 0.1903 -0.0105 -0.0129 0.0225  321 ASP B N   
9145 C CA  . ASP B 303 ? 0.2087 0.0907 0.2192 0.0004  -0.0170 0.0163  321 ASP B CA  
9146 C C   . ASP B 303 ? 0.1679 0.0928 0.2110 0.0067  -0.0396 0.0072  321 ASP B C   
9147 O O   . ASP B 303 ? 0.2269 0.1010 0.2335 0.0176  -0.0330 0.0117  321 ASP B O   
9148 C CB  . ASP B 303 ? 0.2273 0.1082 0.2295 -0.0078 -0.0040 0.0390  321 ASP B CB  
9149 C CG  . ASP B 303 ? 0.2544 0.1434 0.2833 -0.0289 0.0224  0.0025  321 ASP B CG  
9150 O OD1 . ASP B 303 ? 0.2196 0.1376 0.2609 -0.0193 -0.0141 -0.0077 321 ASP B OD1 
9151 O OD2 . ASP B 303 ? 0.3200 0.1914 0.3231 -0.0528 0.0718  -0.0398 321 ASP B OD2 
9156 N N   . LEU B 304 ? 0.1646 0.1314 0.2011 0.0093  -0.0171 0.0051  322 LEU B N   
9157 C CA  . LEU B 304 ? 0.1822 0.1405 0.2054 0.0200  -0.0265 -0.0065 322 LEU B CA  
9158 C C   . LEU B 304 ? 0.1770 0.1324 0.2204 0.0155  -0.0312 -0.0069 322 LEU B C   
9159 O O   . LEU B 304 ? 0.2104 0.1425 0.2407 0.0076  -0.0195 0.0157  322 LEU B O   
9160 C CB  . LEU B 304 ? 0.1918 0.1510 0.2125 0.0262  -0.0218 0.0120  322 LEU B CB  
9161 C CG  . LEU B 304 ? 0.1805 0.1510 0.2118 0.0014  -0.0131 0.0262  322 LEU B CG  
9162 C CD1 . LEU B 304 ? 0.2068 0.1740 0.2173 -0.0051 0.0033  0.0470  322 LEU B CD1 
9163 C CD2 . LEU B 304 ? 0.2224 0.1500 0.2303 -0.0064 -0.0079 0.0128  322 LEU B CD2 
9175 N N   . MET B 305 ? 0.1923 0.1308 0.2155 0.0412  -0.0396 -0.0035 323 MET B N   
9176 C CA  . MET B 305 ? 0.1979 0.1436 0.2309 0.0388  -0.0494 -0.0080 323 MET B CA  
9177 C C   . MET B 305 ? 0.2248 0.1399 0.2287 0.0233  -0.0257 -0.0060 323 MET B C   
9178 O O   . MET B 305 ? 0.2018 0.1433 0.2089 0.0079  -0.0336 0.0035  323 MET B O   
9179 C CB  . MET B 305 ? 0.2642 0.1619 0.2563 0.0671  -0.0665 -0.0089 323 MET B CB  
9180 C CG  . MET B 305 ? 0.3557 0.2162 0.3212 0.1107  -0.0469 -0.0069 323 MET B CG  
9181 S SD  . MET B 305 ? 0.3124 0.2659 0.3960 0.0989  -0.0648 -0.0534 323 MET B SD  
9182 C CE  . MET B 305 ? 0.2613 0.2475 0.4050 0.0870  -0.0552 -0.0314 323 MET B CE  
9192 N N   . PRO B 306 ? 0.2367 0.1450 0.2407 0.0334  -0.0201 0.0220  324 PRO B N   
9193 C CA  . PRO B 306 ? 0.2343 0.1424 0.2376 0.0437  -0.0039 0.0543  324 PRO B CA  
9194 C C   . PRO B 306 ? 0.2514 0.1579 0.2330 0.0496  -0.0161 0.0481  324 PRO B C   
9195 O O   . PRO B 306 ? 0.2588 0.1878 0.2379 0.0558  -0.0195 0.0426  324 PRO B O   
9196 C CB  . PRO B 306 ? 0.2498 0.1631 0.2612 0.0373  0.0048  0.0614  324 PRO B CB  
9197 C CG  . PRO B 306 ? 0.2925 0.1620 0.2772 0.0236  -0.0015 0.0540  324 PRO B CG  
9198 C CD  . PRO B 306 ? 0.2590 0.1540 0.2751 0.0376  -0.0033 0.0329  324 PRO B CD  
9206 N N   . TYR B 307 ? 0.2390 0.1821 0.2301 0.0482  -0.0253 0.0209  325 TYR B N   
9207 C CA  . TYR B 307 ? 0.2253 0.1670 0.2196 0.0219  -0.0443 -0.0020 325 TYR B CA  
9208 C C   . TYR B 307 ? 0.2127 0.1736 0.2134 0.0224  -0.0637 -0.0051 325 TYR B C   
9209 O O   . TYR B 307 ? 0.2339 0.2040 0.2269 0.0377  -0.0632 0.0087  325 TYR B O   
9210 C CB  . TYR B 307 ? 0.2422 0.1823 0.2208 0.0061  -0.0203 -0.0097 325 TYR B CB  
9211 C CG  . TYR B 307 ? 0.2266 0.1655 0.2253 -0.0053 -0.0321 -0.0159 325 TYR B CG  
9212 C CD1 . TYR B 307 ? 0.2291 0.1574 0.2364 -0.0042 -0.0444 -0.0131 325 TYR B CD1 
9213 C CD2 . TYR B 307 ? 0.2096 0.1708 0.2394 -0.0003 -0.0361 -0.0079 325 TYR B CD2 
9214 C CE1 . TYR B 307 ? 0.2099 0.1383 0.2485 0.0153  -0.0514 -0.0266 325 TYR B CE1 
9215 C CE2 . TYR B 307 ? 0.2066 0.1474 0.2423 0.0084  -0.0515 -0.0123 325 TYR B CE2 
9216 C CZ  . TYR B 307 ? 0.2174 0.1297 0.2381 0.0123  -0.0578 -0.0270 325 TYR B CZ  
9217 O OH  . TYR B 307 ? 0.2483 0.1276 0.2696 0.0144  -0.0559 -0.0105 325 TYR B OH  
9227 N N   . ALA B 308 ? 0.2233 0.1549 0.2249 0.0306  -0.0391 -0.0044 326 ALA B N   
9228 C CA  . ALA B 308 ? 0.2179 0.1349 0.2062 0.0201  -0.0406 0.0055  326 ALA B CA  
9229 C C   . ALA B 308 ? 0.2202 0.1319 0.2141 0.0085  -0.0169 0.0039  326 ALA B C   
9230 O O   . ALA B 308 ? 0.2086 0.1293 0.2328 0.0116  -0.0254 0.0039  326 ALA B O   
9231 C CB  . ALA B 308 ? 0.2270 0.1430 0.2122 0.0305  -0.0289 0.0096  326 ALA B CB  
9237 N N   . ARG B 309 ? 0.2265 0.1429 0.2356 -0.0093 -0.0044 0.0182  327 ARG B N   
9238 C CA  . ARG B 309 ? 0.2267 0.1640 0.2681 -0.0167 0.0215  0.0074  327 ARG B CA  
9239 C C   . ARG B 309 ? 0.2237 0.1597 0.2735 -0.0141 0.0110  0.0252  327 ARG B C   
9240 O O   . ARG B 309 ? 0.2551 0.1632 0.2839 0.0000  0.0038  0.0070  327 ARG B O   
9241 C CB  . ARG B 309 ? 0.2302 0.2015 0.3299 -0.0447 0.0286  0.0023  327 ARG B CB  
9242 C CG  . ARG B 309 ? 0.2580 0.2595 0.4047 -0.0601 0.0133  0.0178  327 ARG B CG  
9243 C CD  . ARG B 309 ? 0.3168 0.2835 0.4695 -0.0743 0.0152  -0.0039 327 ARG B CD  
9244 N NE  . ARG B 309 ? 0.3852 0.3313 0.5452 -0.0363 0.0345  0.0164  327 ARG B NE  
9245 C CZ  . ARG B 309 ? 0.4161 0.3660 0.5954 -0.0318 0.0474  0.0218  327 ARG B CZ  
9246 N NH1 . ARG B 309 ? 0.4593 0.3909 0.6124 -0.0440 0.0564  0.0344  327 ARG B NH1 
9247 N NH2 . ARG B 309 ? 0.3721 0.3594 0.6241 -0.0091 0.0621  0.0130  327 ARG B NH2 
9261 N N   . PRO B 310 ? 0.2441 0.1522 0.2727 0.0085  -0.0052 0.0573  328 PRO B N   
9262 C CA  . PRO B 310 ? 0.2637 0.1701 0.2861 0.0242  -0.0085 0.0619  328 PRO B CA  
9263 C C   . PRO B 310 ? 0.2209 0.1727 0.2999 0.0418  -0.0335 0.0399  328 PRO B C   
9264 O O   . PRO B 310 ? 0.2428 0.1811 0.3543 0.0225  0.0217  0.0290  328 PRO B O   
9265 C CB  . PRO B 310 ? 0.2942 0.2032 0.2958 0.0450  -0.0049 0.0590  328 PRO B CB  
9266 C CG  . PRO B 310 ? 0.3307 0.2061 0.3045 0.0361  0.0148  0.0555  328 PRO B CG  
9267 C CD  . PRO B 310 ? 0.2672 0.1838 0.2938 0.0347  -0.0003 0.0583  328 PRO B CD  
9275 N N   . PHE B 311 ? 0.2166 0.1454 0.2676 0.0453  -0.0396 0.0332  329 PHE B N   
9276 C CA  . PHE B 311 ? 0.2108 0.1419 0.2615 0.0376  -0.0560 0.0170  329 PHE B CA  
9277 C C   . PHE B 311 ? 0.2195 0.1326 0.2478 0.0203  -0.0458 0.0196  329 PHE B C   
9278 O O   . PHE B 311 ? 0.2176 0.1455 0.2576 0.0005  -0.0290 0.0191  329 PHE B O   
9279 C CB  . PHE B 311 ? 0.2068 0.1502 0.2460 0.0420  -0.0593 0.0320  329 PHE B CB  
9280 C CG  . PHE B 311 ? 0.2265 0.1653 0.2370 0.0238  -0.0544 0.0304  329 PHE B CG  
9281 C CD1 . PHE B 311 ? 0.2138 0.1822 0.2278 0.0129  -0.0555 0.0418  329 PHE B CD1 
9282 C CD2 . PHE B 311 ? 0.2370 0.1474 0.2340 0.0356  -0.0436 0.0226  329 PHE B CD2 
9283 C CE1 . PHE B 311 ? 0.2572 0.1966 0.2356 0.0263  -0.0542 0.0542  329 PHE B CE1 
9284 C CE2 . PHE B 311 ? 0.2393 0.1676 0.2337 0.0284  -0.0525 0.0433  329 PHE B CE2 
9285 C CZ  . PHE B 311 ? 0.2808 0.1990 0.2262 0.0421  -0.0376 0.0553  329 PHE B CZ  
9295 N N   . ALA B 312 ? 0.2160 0.1281 0.2262 0.0018  -0.0659 0.0096  330 ALA B N   
9296 C CA  . ALA B 312 ? 0.2172 0.1227 0.2205 0.0122  -0.0518 0.0129  330 ALA B CA  
9297 C C   . ALA B 312 ? 0.1844 0.1391 0.2407 -0.0005 -0.0355 -0.0025 330 ALA B C   
9298 O O   . ALA B 312 ? 0.1959 0.1581 0.2617 0.0034  -0.0359 -0.0147 330 ALA B O   
9299 C CB  . ALA B 312 ? 0.2074 0.1320 0.2301 0.0219  -0.0439 0.0153  330 ALA B CB  
9305 N N   . VAL B 313 ? 0.1771 0.1305 0.2578 -0.0037 -0.0210 0.0113  331 VAL B N   
9306 C CA  . VAL B 313 ? 0.1914 0.1365 0.2615 0.0217  -0.0264 0.0165  331 VAL B CA  
9307 C C   . VAL B 313 ? 0.1979 0.1254 0.2622 0.0333  -0.0246 0.0093  331 VAL B C   
9308 O O   . VAL B 313 ? 0.1995 0.1443 0.2837 0.0293  -0.0186 0.0152  331 VAL B O   
9309 C CB  . VAL B 313 ? 0.2109 0.1383 0.2712 0.0211  -0.0162 0.0269  331 VAL B CB  
9310 C CG1 . VAL B 313 ? 0.1947 0.1541 0.3000 0.0324  -0.0310 0.0228  331 VAL B CG1 
9311 C CG2 . VAL B 313 ? 0.2682 0.1466 0.2599 0.0375  0.0021  0.0146  331 VAL B CG2 
9321 N N   . GLY B 314 ? 0.2098 0.1169 0.2691 0.0136  -0.0295 0.0045  332 GLY B N   
9322 C CA  . GLY B 314 ? 0.2077 0.1138 0.2458 0.0242  -0.0363 0.0003  332 GLY B CA  
9323 C C   . GLY B 314 ? 0.2289 0.1442 0.2479 0.0411  -0.0195 0.0108  332 GLY B C   
9324 O O   . GLY B 314 ? 0.2608 0.1591 0.2508 0.0285  -0.0162 0.0089  332 GLY B O   
9328 N N   . LYS B 315 ? 0.2266 0.1372 0.2308 0.0249  -0.0287 0.0009  333 LYS B N   
9329 C CA  . LYS B 315 ? 0.2289 0.1311 0.2399 0.0311  -0.0469 -0.0046 333 LYS B CA  
9330 C C   . LYS B 315 ? 0.2337 0.1380 0.2521 0.0287  -0.0484 0.0117  333 LYS B C   
9331 O O   . LYS B 315 ? 0.2810 0.1414 0.2630 0.0039  -0.0515 0.0260  333 LYS B O   
9332 C CB  . LYS B 315 ? 0.2515 0.1439 0.2478 0.0086  -0.0511 -0.0230 333 LYS B CB  
9333 C CG  . LYS B 315 ? 0.3257 0.1352 0.2850 0.0169  -0.0302 -0.0204 333 LYS B CG  
9334 C CD  . LYS B 315 ? 0.4098 0.1890 0.3401 -0.0275 0.0298  -0.0526 333 LYS B CD  
9335 C CE  . LYS B 315 ? 0.4760 0.2333 0.3818 -0.0388 0.0722  -0.0617 333 LYS B CE  
9336 N NZ  . LYS B 315 ? 0.5129 0.2468 0.3974 -0.0341 0.1020  -0.0724 333 LYS B NZ  
9350 N N   . ARG B 316 ? 0.2465 0.1480 0.2618 0.0502  -0.0303 0.0313  334 ARG B N   
9351 C CA  . ARG B 316 ? 0.2223 0.1707 0.2742 0.0637  -0.0197 0.0253  334 ARG B CA  
9352 C C   . ARG B 316 ? 0.2247 0.1542 0.2636 0.0500  -0.0025 0.0304  334 ARG B C   
9353 O O   . ARG B 316 ? 0.2530 0.1720 0.2944 0.0574  0.0111  0.0635  334 ARG B O   
9354 C CB  . ARG B 316 ? 0.2693 0.2279 0.3114 0.0661  0.0066  -0.0086 334 ARG B CB  
9355 C CG  . ARG B 316 ? 0.3092 0.2868 0.3510 0.0752  0.0190  -0.0355 334 ARG B CG  
9356 C CD  . ARG B 316 ? 0.4113 0.3483 0.4069 0.0575  0.0022  -0.0406 334 ARG B CD  
9357 N NE  . ARG B 316 ? 0.5371 0.4066 0.4605 0.0313  0.0206  -0.0384 334 ARG B NE  
9358 C CZ  . ARG B 316 ? 0.5966 0.4313 0.4883 0.0416  0.0238  -0.0506 334 ARG B CZ  
9359 N NH1 . ARG B 316 ? 0.5947 0.4388 0.4792 0.0720  0.0297  -0.0625 334 ARG B NH1 
9360 N NH2 . ARG B 316 ? 0.6178 0.4351 0.5074 0.0464  0.0270  -0.0425 334 ARG B NH2 
9374 N N   . THR B 317 ? 0.2063 0.1249 0.2313 0.0130  -0.0262 0.0126  335 THR B N   
9375 C CA  . THR B 317 ? 0.1949 0.1140 0.2258 0.0091  -0.0264 0.0055  335 THR B CA  
9376 C C   . THR B 317 ? 0.1811 0.1111 0.2350 0.0111  -0.0219 0.0042  335 THR B C   
9377 O O   . THR B 317 ? 0.2043 0.1006 0.2589 0.0168  -0.0086 0.0090  335 THR B O   
9378 C CB  . THR B 317 ? 0.2166 0.1188 0.2175 -0.0004 -0.0205 -0.0130 335 THR B CB  
9379 O OG1 . THR B 317 ? 0.2512 0.1179 0.2039 0.0020  -0.0297 -0.0082 335 THR B OG1 
9380 C CG2 . THR B 317 ? 0.2267 0.1262 0.2219 0.0079  -0.0018 -0.0145 335 THR B CG2 
9388 N N   . CYS B 318 ? 0.2076 0.1060 0.2215 -0.0024 -0.0402 0.0206  336 CYS B N   
9389 C CA  . CYS B 318 ? 0.1958 0.1045 0.2269 -0.0092 -0.0372 0.0052  336 CYS B CA  
9390 C C   . CYS B 318 ? 0.2134 0.1040 0.2377 -0.0105 -0.0646 -0.0026 336 CYS B C   
9391 O O   . CYS B 318 ? 0.2602 0.1271 0.2692 -0.0197 -0.0892 0.0122  336 CYS B O   
9392 C CB  . CYS B 318 ? 0.2035 0.1238 0.2370 0.0112  -0.0400 0.0185  336 CYS B CB  
9393 S SG  . CYS B 318 ? 0.2184 0.1335 0.2431 -0.0012 -0.0318 0.0063  336 CYS B SG  
9398 N N   . SER B 319 ? 0.1860 0.0832 0.2534 -0.0140 -0.0471 -0.0189 337 SER B N   
9399 C CA  . SER B 319 ? 0.2246 0.0943 0.2867 -0.0130 -0.0276 -0.0124 337 SER B CA  
9400 C C   . SER B 319 ? 0.2243 0.0930 0.2742 0.0173  -0.0468 -0.0042 337 SER B C   
9401 O O   . SER B 319 ? 0.2667 0.1148 0.3113 0.0262  -0.0237 0.0072  337 SER B O   
9402 C CB  . SER B 319 ? 0.2952 0.1009 0.3287 0.0236  0.0474  0.0184  337 SER B CB  
9403 O OG  . SER B 319 ? 0.3475 0.1633 0.3623 -0.0004 0.0341  0.0062  337 SER B OG  
9409 N N   . GLY B 320 ? 0.1901 0.1032 0.2575 0.0100  -0.0314 -0.0064 338 GLY B N   
9410 C CA  . GLY B 320 ? 0.2099 0.1218 0.2838 -0.0001 -0.0212 -0.0109 338 GLY B CA  
9411 C C   . GLY B 320 ? 0.2333 0.1121 0.2700 0.0153  -0.0452 -0.0092 338 GLY B C   
9412 O O   . GLY B 320 ? 0.2091 0.0945 0.2680 0.0196  -0.0607 -0.0106 338 GLY B O   
9416 N N   . ILE B 321 ? 0.2131 0.1154 0.2731 0.0386  -0.0467 -0.0035 339 ILE B N   
9417 C CA  . ILE B 321 ? 0.2223 0.1448 0.2591 0.0355  -0.0631 -0.0026 339 ILE B CA  
9418 C C   . ILE B 321 ? 0.2183 0.1409 0.2480 0.0067  -0.0380 0.0227  339 ILE B C   
9419 O O   . ILE B 321 ? 0.2526 0.1649 0.2552 -0.0023 -0.0215 0.0442  339 ILE B O   
9420 C CB  . ILE B 321 ? 0.2648 0.1791 0.2830 0.0570  -0.0535 -0.0134 339 ILE B CB  
9421 C CG1 . ILE B 321 ? 0.2920 0.2021 0.3083 0.0846  -0.0534 -0.0162 339 ILE B CG1 
9422 C CG2 . ILE B 321 ? 0.2603 0.1873 0.2775 0.0516  -0.0752 -0.0227 339 ILE B CG2 
9423 C CD1 . ILE B 321 ? 0.3256 0.2286 0.3251 0.0789  -0.0610 0.0001  339 ILE B CD1 
9435 N N   . VAL B 322 ? 0.1987 0.1268 0.2551 0.0213  -0.0361 0.0167  340 VAL B N   
9436 C CA  . VAL B 322 ? 0.1890 0.1209 0.2652 0.0264  -0.0367 0.0071  340 VAL B CA  
9437 C C   . VAL B 322 ? 0.2019 0.1264 0.2699 0.0163  -0.0365 0.0103  340 VAL B C   
9438 O O   . VAL B 322 ? 0.1783 0.1273 0.2903 0.0233  -0.0352 0.0133  340 VAL B O   
9439 C CB  . VAL B 322 ? 0.1944 0.1064 0.2715 0.0166  -0.0403 -0.0215 340 VAL B CB  
9440 C CG1 . VAL B 322 ? 0.2085 0.1251 0.2718 -0.0058 -0.0406 -0.0364 340 VAL B CG1 
9441 C CG2 . VAL B 322 ? 0.1998 0.1275 0.2904 0.0238  -0.0274 -0.0258 340 VAL B CG2 
9451 N N   . THR B 323 ? 0.2165 0.1515 0.2620 0.0202  -0.0073 0.0452  341 THR B N   
9452 C CA  . THR B 323 ? 0.2361 0.1520 0.2757 -0.0015 -0.0140 0.0398  341 THR B CA  
9453 C C   . THR B 323 ? 0.2430 0.1625 0.2635 0.0172  -0.0060 0.0284  341 THR B C   
9454 O O   . THR B 323 ? 0.2661 0.1650 0.2768 0.0273  -0.0010 0.0432  341 THR B O   
9455 C CB  . THR B 323 ? 0.2386 0.1802 0.3282 -0.0113 -0.0164 0.0431  341 THR B CB  
9456 O OG1 . THR B 323 ? 0.2877 0.1966 0.3626 -0.0101 -0.0148 0.0639  341 THR B OG1 
9457 C CG2 . THR B 323 ? 0.2697 0.1933 0.3556 -0.0148 -0.0040 0.0406  341 THR B CG2 
9465 N N   . PRO B 324 ? 0.2594 0.1801 0.2381 0.0281  -0.0156 0.0247  342 PRO B N   
9466 C CA  . PRO B 324 ? 0.3055 0.2142 0.2151 0.0845  0.0197  0.0437  342 PRO B CA  
9467 C C   . PRO B 324 ? 0.3998 0.2731 0.2080 0.1154  0.0996  0.0871  342 PRO B C   
9468 O O   . PRO B 324 ? 0.4499 0.3110 0.2736 0.0827  0.1093  0.0688  342 PRO B O   
9469 C CB  . PRO B 324 ? 0.2927 0.2126 0.2323 0.0658  -0.0018 0.0270  342 PRO B CB  
9470 C CG  . PRO B 324 ? 0.2562 0.1926 0.2319 0.0418  -0.0130 0.0157  342 PRO B CG  
9471 C CD  . PRO B 324 ? 0.2636 0.1702 0.2377 0.0329  -0.0112 0.0230  342 PRO B CD  
# 
