data_8J4N
# 
_entry.id   8J4N 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.398 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8J4N         pdb_00008j4n 10.2210/pdb8j4n/pdb 
WWPDB D_1300037027 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2024-11-06 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8J4N 
_pdbx_database_status.recvd_initial_deposition_date   2023-04-20 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_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              jmma@ahu.edu.cn 
_pdbx_contact_author.name_first         Jinming 
_pdbx_contact_author.name_last          Ma 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3199-9860 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Ma, J.M.' 1 ? 
'Ge, H.H.' 2 ? 
# 
_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 Acinetobacter baumannii LysR family regulator AceR effector binding domain (apo)' 
_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 'Ma, J.M.' 1 ? 
primary 'Ge, H.H.' 2 ? 
# 
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 'Bacterial regulatory helix-turn-helix protein, lysR family protein' 34169.141 2  ? ? 'effector-binding domain' ? 
2 water   nat water                                                                18.015    79 ? ? ?                         ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'LysR family regulator AceR' 
# 
_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       
;MNINQEQLLMFQAVMETGSFSAAARKLGKVPSAVSMSIANLEIDLNLTLFERKGREPTPTAEARVLYEKTAQLLIEMNQW
KQHAHALSTGLEPNLTIVVVSELLHTNWTDYVCLLESRFPDLQINIVSAPQEDALQMLLDGSAQLALMFEREHLDNREQF
VELKREALIPVISKTHPLASQEHVSYEQILGTRQIVVASRDETLKPELLFSKHYWRTDNHHSACLMILRNLGWGVLPQEM
FKENPELNNKLKALDVFDFTPRFEYYVDLVWSRESELGAAARFLIDYIRNKRMQPAP
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MNINQEQLLMFQAVMETGSFSAAARKLGKVPSAVSMSIANLEIDLNLTLFERKGREPTPTAEARVLYEKTAQLLIEMNQW
KQHAHALSTGLEPNLTIVVVSELLHTNWTDYVCLLESRFPDLQINIVSAPQEDALQMLLDGSAQLALMFEREHLDNREQF
VELKREALIPVISKTHPLASQEHVSYEQILGTRQIVVASRDETLKPELLFSKHYWRTDNHHSACLMILRNLGWGVLPQEM
FKENPELNNKLKALDVFDFTPRFEYYVDLVWSRESELGAAARFLIDYIRNKRMQPAP
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ASN n 
1 3   ILE n 
1 4   ASN n 
1 5   GLN n 
1 6   GLU n 
1 7   GLN n 
1 8   LEU n 
1 9   LEU n 
1 10  MET n 
1 11  PHE n 
1 12  GLN n 
1 13  ALA n 
1 14  VAL n 
1 15  MET n 
1 16  GLU n 
1 17  THR n 
1 18  GLY n 
1 19  SER n 
1 20  PHE n 
1 21  SER n 
1 22  ALA n 
1 23  ALA n 
1 24  ALA n 
1 25  ARG n 
1 26  LYS n 
1 27  LEU n 
1 28  GLY n 
1 29  LYS n 
1 30  VAL n 
1 31  PRO n 
1 32  SER n 
1 33  ALA n 
1 34  VAL n 
1 35  SER n 
1 36  MET n 
1 37  SER n 
1 38  ILE n 
1 39  ALA n 
1 40  ASN n 
1 41  LEU n 
1 42  GLU n 
1 43  ILE n 
1 44  ASP n 
1 45  LEU n 
1 46  ASN n 
1 47  LEU n 
1 48  THR n 
1 49  LEU n 
1 50  PHE n 
1 51  GLU n 
1 52  ARG n 
1 53  LYS n 
1 54  GLY n 
1 55  ARG n 
1 56  GLU n 
1 57  PRO n 
1 58  THR n 
1 59  PRO n 
1 60  THR n 
1 61  ALA n 
1 62  GLU n 
1 63  ALA n 
1 64  ARG n 
1 65  VAL n 
1 66  LEU n 
1 67  TYR n 
1 68  GLU n 
1 69  LYS n 
1 70  THR n 
1 71  ALA n 
1 72  GLN n 
1 73  LEU n 
1 74  LEU n 
1 75  ILE n 
1 76  GLU n 
1 77  MET n 
1 78  ASN n 
1 79  GLN n 
1 80  TRP n 
1 81  LYS n 
1 82  GLN n 
1 83  HIS n 
1 84  ALA n 
1 85  HIS n 
1 86  ALA n 
1 87  LEU n 
1 88  SER n 
1 89  THR n 
1 90  GLY n 
1 91  LEU n 
1 92  GLU n 
1 93  PRO n 
1 94  ASN n 
1 95  LEU n 
1 96  THR n 
1 97  ILE n 
1 98  VAL n 
1 99  VAL n 
1 100 VAL n 
1 101 SER n 
1 102 GLU n 
1 103 LEU n 
1 104 LEU n 
1 105 HIS n 
1 106 THR n 
1 107 ASN n 
1 108 TRP n 
1 109 THR n 
1 110 ASP n 
1 111 TYR n 
1 112 VAL n 
1 113 CYS n 
1 114 LEU n 
1 115 LEU n 
1 116 GLU n 
1 117 SER n 
1 118 ARG n 
1 119 PHE n 
1 120 PRO n 
1 121 ASP n 
1 122 LEU n 
1 123 GLN n 
1 124 ILE n 
1 125 ASN n 
1 126 ILE n 
1 127 VAL n 
1 128 SER n 
1 129 ALA n 
1 130 PRO n 
1 131 GLN n 
1 132 GLU n 
1 133 ASP n 
1 134 ALA n 
1 135 LEU n 
1 136 GLN n 
1 137 MET n 
1 138 LEU n 
1 139 LEU n 
1 140 ASP n 
1 141 GLY n 
1 142 SER n 
1 143 ALA n 
1 144 GLN n 
1 145 LEU n 
1 146 ALA n 
1 147 LEU n 
1 148 MET n 
1 149 PHE n 
1 150 GLU n 
1 151 ARG n 
1 152 GLU n 
1 153 HIS n 
1 154 LEU n 
1 155 ASP n 
1 156 ASN n 
1 157 ARG n 
1 158 GLU n 
1 159 GLN n 
1 160 PHE n 
1 161 VAL n 
1 162 GLU n 
1 163 LEU n 
1 164 LYS n 
1 165 ARG n 
1 166 GLU n 
1 167 ALA n 
1 168 LEU n 
1 169 ILE n 
1 170 PRO n 
1 171 VAL n 
1 172 ILE n 
1 173 SER n 
1 174 LYS n 
1 175 THR n 
1 176 HIS n 
1 177 PRO n 
1 178 LEU n 
1 179 ALA n 
1 180 SER n 
1 181 GLN n 
1 182 GLU n 
1 183 HIS n 
1 184 VAL n 
1 185 SER n 
1 186 TYR n 
1 187 GLU n 
1 188 GLN n 
1 189 ILE n 
1 190 LEU n 
1 191 GLY n 
1 192 THR n 
1 193 ARG n 
1 194 GLN n 
1 195 ILE n 
1 196 VAL n 
1 197 VAL n 
1 198 ALA n 
1 199 SER n 
1 200 ARG n 
1 201 ASP n 
1 202 GLU n 
1 203 THR n 
1 204 LEU n 
1 205 LYS n 
1 206 PRO n 
1 207 GLU n 
1 208 LEU n 
1 209 LEU n 
1 210 PHE n 
1 211 SER n 
1 212 LYS n 
1 213 HIS n 
1 214 TYR n 
1 215 TRP n 
1 216 ARG n 
1 217 THR n 
1 218 ASP n 
1 219 ASN n 
1 220 HIS n 
1 221 HIS n 
1 222 SER n 
1 223 ALA n 
1 224 CYS n 
1 225 LEU n 
1 226 MET n 
1 227 ILE n 
1 228 LEU n 
1 229 ARG n 
1 230 ASN n 
1 231 LEU n 
1 232 GLY n 
1 233 TRP n 
1 234 GLY n 
1 235 VAL n 
1 236 LEU n 
1 237 PRO n 
1 238 GLN n 
1 239 GLU n 
1 240 MET n 
1 241 PHE n 
1 242 LYS n 
1 243 GLU n 
1 244 ASN n 
1 245 PRO n 
1 246 GLU n 
1 247 LEU n 
1 248 ASN n 
1 249 ASN n 
1 250 LYS n 
1 251 LEU n 
1 252 LYS n 
1 253 ALA n 
1 254 LEU n 
1 255 ASP n 
1 256 VAL n 
1 257 PHE n 
1 258 ASP n 
1 259 PHE n 
1 260 THR n 
1 261 PRO n 
1 262 ARG n 
1 263 PHE n 
1 264 GLU n 
1 265 TYR n 
1 266 TYR n 
1 267 VAL n 
1 268 ASP n 
1 269 LEU n 
1 270 VAL n 
1 271 TRP n 
1 272 SER n 
1 273 ARG n 
1 274 GLU n 
1 275 SER n 
1 276 GLU n 
1 277 LEU n 
1 278 GLY n 
1 279 ALA n 
1 280 ALA n 
1 281 ALA n 
1 282 ARG n 
1 283 PHE n 
1 284 LEU n 
1 285 ILE n 
1 286 ASP n 
1 287 TYR n 
1 288 ILE n 
1 289 ARG n 
1 290 ASN n 
1 291 LYS n 
1 292 ARG n 
1 293 MET n 
1 294 GLN n 
1 295 PRO n 
1 296 ALA n 
1 297 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                   297 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 cynR_1 
_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      'Acinetobacter baumannii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     470 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ASN 2   2   ?   ?   ?   A . n 
A 1 3   ILE 3   3   ?   ?   ?   A . n 
A 1 4   ASN 4   4   ?   ?   ?   A . n 
A 1 5   GLN 5   5   ?   ?   ?   A . n 
A 1 6   GLU 6   6   ?   ?   ?   A . n 
A 1 7   GLN 7   7   ?   ?   ?   A . n 
A 1 8   LEU 8   8   ?   ?   ?   A . n 
A 1 9   LEU 9   9   ?   ?   ?   A . n 
A 1 10  MET 10  10  ?   ?   ?   A . n 
A 1 11  PHE 11  11  ?   ?   ?   A . n 
A 1 12  GLN 12  12  ?   ?   ?   A . n 
A 1 13  ALA 13  13  ?   ?   ?   A . n 
A 1 14  VAL 14  14  ?   ?   ?   A . n 
A 1 15  MET 15  15  ?   ?   ?   A . n 
A 1 16  GLU 16  16  ?   ?   ?   A . n 
A 1 17  THR 17  17  ?   ?   ?   A . n 
A 1 18  GLY 18  18  ?   ?   ?   A . n 
A 1 19  SER 19  19  ?   ?   ?   A . n 
A 1 20  PHE 20  20  ?   ?   ?   A . n 
A 1 21  SER 21  21  ?   ?   ?   A . n 
A 1 22  ALA 22  22  ?   ?   ?   A . n 
A 1 23  ALA 23  23  ?   ?   ?   A . n 
A 1 24  ALA 24  24  ?   ?   ?   A . n 
A 1 25  ARG 25  25  ?   ?   ?   A . n 
A 1 26  LYS 26  26  ?   ?   ?   A . n 
A 1 27  LEU 27  27  ?   ?   ?   A . n 
A 1 28  GLY 28  28  ?   ?   ?   A . n 
A 1 29  LYS 29  29  ?   ?   ?   A . n 
A 1 30  VAL 30  30  ?   ?   ?   A . n 
A 1 31  PRO 31  31  ?   ?   ?   A . n 
A 1 32  SER 32  32  ?   ?   ?   A . n 
A 1 33  ALA 33  33  ?   ?   ?   A . n 
A 1 34  VAL 34  34  ?   ?   ?   A . n 
A 1 35  SER 35  35  ?   ?   ?   A . n 
A 1 36  MET 36  36  ?   ?   ?   A . n 
A 1 37  SER 37  37  ?   ?   ?   A . n 
A 1 38  ILE 38  38  ?   ?   ?   A . n 
A 1 39  ALA 39  39  ?   ?   ?   A . n 
A 1 40  ASN 40  40  ?   ?   ?   A . n 
A 1 41  LEU 41  41  ?   ?   ?   A . n 
A 1 42  GLU 42  42  ?   ?   ?   A . n 
A 1 43  ILE 43  43  ?   ?   ?   A . n 
A 1 44  ASP 44  44  ?   ?   ?   A . n 
A 1 45  LEU 45  45  ?   ?   ?   A . n 
A 1 46  ASN 46  46  ?   ?   ?   A . n 
A 1 47  LEU 47  47  ?   ?   ?   A . n 
A 1 48  THR 48  48  ?   ?   ?   A . n 
A 1 49  LEU 49  49  ?   ?   ?   A . n 
A 1 50  PHE 50  50  ?   ?   ?   A . n 
A 1 51  GLU 51  51  ?   ?   ?   A . n 
A 1 52  ARG 52  52  ?   ?   ?   A . n 
A 1 53  LYS 53  53  ?   ?   ?   A . n 
A 1 54  GLY 54  54  ?   ?   ?   A . n 
A 1 55  ARG 55  55  ?   ?   ?   A . n 
A 1 56  GLU 56  56  ?   ?   ?   A . n 
A 1 57  PRO 57  57  ?   ?   ?   A . n 
A 1 58  THR 58  58  ?   ?   ?   A . n 
A 1 59  PRO 59  59  ?   ?   ?   A . n 
A 1 60  THR 60  60  ?   ?   ?   A . n 
A 1 61  ALA 61  61  ?   ?   ?   A . n 
A 1 62  GLU 62  62  ?   ?   ?   A . n 
A 1 63  ALA 63  63  ?   ?   ?   A . n 
A 1 64  ARG 64  64  ?   ?   ?   A . n 
A 1 65  VAL 65  65  ?   ?   ?   A . n 
A 1 66  LEU 66  66  ?   ?   ?   A . n 
A 1 67  TYR 67  67  ?   ?   ?   A . n 
A 1 68  GLU 68  68  ?   ?   ?   A . n 
A 1 69  LYS 69  69  ?   ?   ?   A . n 
A 1 70  THR 70  70  ?   ?   ?   A . n 
A 1 71  ALA 71  71  ?   ?   ?   A . n 
A 1 72  GLN 72  72  ?   ?   ?   A . n 
A 1 73  LEU 73  73  ?   ?   ?   A . n 
A 1 74  LEU 74  74  ?   ?   ?   A . n 
A 1 75  ILE 75  75  ?   ?   ?   A . n 
A 1 76  GLU 76  76  ?   ?   ?   A . n 
A 1 77  MET 77  77  ?   ?   ?   A . n 
A 1 78  ASN 78  78  ?   ?   ?   A . n 
A 1 79  GLN 79  79  ?   ?   ?   A . n 
A 1 80  TRP 80  80  ?   ?   ?   A . n 
A 1 81  LYS 81  81  ?   ?   ?   A . n 
A 1 82  GLN 82  82  ?   ?   ?   A . n 
A 1 83  HIS 83  83  ?   ?   ?   A . n 
A 1 84  ALA 84  84  ?   ?   ?   A . n 
A 1 85  HIS 85  85  ?   ?   ?   A . n 
A 1 86  ALA 86  86  ?   ?   ?   A . n 
A 1 87  LEU 87  87  ?   ?   ?   A . n 
A 1 88  SER 88  88  ?   ?   ?   A . n 
A 1 89  THR 89  89  ?   ?   ?   A . n 
A 1 90  GLY 90  90  ?   ?   ?   A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  PRO 93  93  93  PRO PRO A . n 
A 1 94  ASN 94  94  94  ASN ASN A . n 
A 1 95  LEU 95  95  95  LEU LEU A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  ILE 97  97  97  ILE ILE A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  VAL 99  99  99  VAL VAL A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 LEU 103 103 103 LEU LEU A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 HIS 105 105 105 HIS HIS A . n 
A 1 106 THR 106 106 106 THR THR A . n 
A 1 107 ASN 107 107 107 ASN ASN A . n 
A 1 108 TRP 108 108 108 TRP TRP A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 TYR 111 111 111 TYR TYR A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 CYS 113 113 113 CYS CYS A . n 
A 1 114 LEU 114 114 114 LEU LEU A . n 
A 1 115 LEU 115 115 115 LEU LEU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 PRO 120 120 120 PRO PRO A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 GLN 123 123 123 GLN GLN A . n 
A 1 124 ILE 124 124 124 ILE ILE A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 ILE 126 126 126 ILE ILE A . n 
A 1 127 VAL 127 127 127 VAL VAL A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 PRO 130 130 130 PRO PRO A . n 
A 1 131 GLN 131 131 131 GLN GLN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 ASP 133 133 133 ASP ASP A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 GLN 136 136 136 GLN GLN A . n 
A 1 137 MET 137 137 137 MET MET A . n 
A 1 138 LEU 138 138 138 LEU LEU A . n 
A 1 139 LEU 139 139 139 LEU LEU A . n 
A 1 140 ASP 140 140 140 ASP ASP A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ALA 143 143 143 ALA ALA A . n 
A 1 144 GLN 144 144 144 GLN GLN A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 ALA 146 146 146 ALA ALA A . n 
A 1 147 LEU 147 147 147 LEU LEU A . n 
A 1 148 MET 148 148 148 MET MET A . n 
A 1 149 PHE 149 149 149 PHE PHE A . n 
A 1 150 GLU 150 150 150 GLU GLU A . n 
A 1 151 ARG 151 151 151 ARG ARG A . n 
A 1 152 GLU 152 152 ?   ?   ?   A . n 
A 1 153 HIS 153 153 ?   ?   ?   A . n 
A 1 154 LEU 154 154 ?   ?   ?   A . n 
A 1 155 ASP 155 155 155 ASP ASP A . n 
A 1 156 ASN 156 156 156 ASN ASN A . n 
A 1 157 ARG 157 157 157 ARG ARG A . n 
A 1 158 GLU 158 158 158 GLU GLU A . n 
A 1 159 GLN 159 159 159 GLN GLN A . n 
A 1 160 PHE 160 160 160 PHE PHE A . n 
A 1 161 VAL 161 161 161 VAL VAL A . n 
A 1 162 GLU 162 162 162 GLU GLU A . n 
A 1 163 LEU 163 163 163 LEU LEU A . n 
A 1 164 LYS 164 164 164 LYS LYS A . n 
A 1 165 ARG 165 165 165 ARG ARG A . n 
A 1 166 GLU 166 166 166 GLU GLU A . n 
A 1 167 ALA 167 167 167 ALA ALA A . n 
A 1 168 LEU 168 168 168 LEU LEU A . n 
A 1 169 ILE 169 169 169 ILE ILE A . n 
A 1 170 PRO 170 170 170 PRO PRO A . n 
A 1 171 VAL 171 171 171 VAL VAL A . n 
A 1 172 ILE 172 172 172 ILE ILE A . n 
A 1 173 SER 173 173 173 SER SER A . n 
A 1 174 LYS 174 174 174 LYS LYS A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 HIS 176 176 176 HIS HIS A . n 
A 1 177 PRO 177 177 177 PRO PRO A . n 
A 1 178 LEU 178 178 178 LEU LEU A . n 
A 1 179 ALA 179 179 179 ALA ALA A . n 
A 1 180 SER 180 180 180 SER SER A . n 
A 1 181 GLN 181 181 181 GLN GLN A . n 
A 1 182 GLU 182 182 ?   ?   ?   A . n 
A 1 183 HIS 183 183 ?   ?   ?   A . n 
A 1 184 VAL 184 184 184 VAL VAL A . n 
A 1 185 SER 185 185 185 SER SER A . n 
A 1 186 TYR 186 186 186 TYR TYR A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 GLN 188 188 188 GLN GLN A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 LEU 190 190 190 LEU LEU A . n 
A 1 191 GLY 191 191 191 GLY GLY A . n 
A 1 192 THR 192 192 192 THR THR A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 GLN 194 194 194 GLN GLN A . n 
A 1 195 ILE 195 195 195 ILE ILE A . n 
A 1 196 VAL 196 196 196 VAL VAL A . n 
A 1 197 VAL 197 197 197 VAL VAL A . n 
A 1 198 ALA 198 198 198 ALA ALA A . n 
A 1 199 SER 199 199 199 SER SER A . n 
A 1 200 ARG 200 200 200 ARG ARG A . n 
A 1 201 ASP 201 201 ?   ?   ?   A . n 
A 1 202 GLU 202 202 ?   ?   ?   A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 LEU 204 204 204 LEU LEU A . n 
A 1 205 LYS 205 205 205 LYS LYS A . n 
A 1 206 PRO 206 206 206 PRO PRO A . n 
A 1 207 GLU 207 207 207 GLU GLU A . n 
A 1 208 LEU 208 208 208 LEU LEU A . n 
A 1 209 LEU 209 209 209 LEU LEU A . n 
A 1 210 PHE 210 210 210 PHE PHE A . n 
A 1 211 SER 211 211 211 SER SER A . n 
A 1 212 LYS 212 212 212 LYS LYS A . n 
A 1 213 HIS 213 213 213 HIS HIS A . n 
A 1 214 TYR 214 214 214 TYR TYR A . n 
A 1 215 TRP 215 215 215 TRP TRP A . n 
A 1 216 ARG 216 216 216 ARG ARG A . n 
A 1 217 THR 217 217 217 THR THR A . n 
A 1 218 ASP 218 218 218 ASP ASP A . n 
A 1 219 ASN 219 219 219 ASN ASN A . n 
A 1 220 HIS 220 220 220 HIS HIS A . n 
A 1 221 HIS 221 221 221 HIS HIS A . n 
A 1 222 SER 222 222 222 SER SER A . n 
A 1 223 ALA 223 223 223 ALA ALA A . n 
A 1 224 CYS 224 224 224 CYS CYS A . n 
A 1 225 LEU 225 225 225 LEU LEU A . n 
A 1 226 MET 226 226 226 MET MET A . n 
A 1 227 ILE 227 227 227 ILE ILE A . n 
A 1 228 LEU 228 228 228 LEU LEU A . n 
A 1 229 ARG 229 229 229 ARG ARG A . n 
A 1 230 ASN 230 230 230 ASN ASN A . n 
A 1 231 LEU 231 231 231 LEU LEU A . n 
A 1 232 GLY 232 232 232 GLY GLY A . n 
A 1 233 TRP 233 233 233 TRP TRP A . n 
A 1 234 GLY 234 234 234 GLY GLY A . n 
A 1 235 VAL 235 235 235 VAL VAL A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 PRO 237 237 237 PRO PRO A . n 
A 1 238 GLN 238 238 238 GLN GLN A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 MET 240 240 240 MET MET A . n 
A 1 241 PHE 241 241 241 PHE PHE A . n 
A 1 242 LYS 242 242 242 LYS LYS A . n 
A 1 243 GLU 243 243 243 GLU GLU A . n 
A 1 244 ASN 244 244 244 ASN ASN A . n 
A 1 245 PRO 245 245 245 PRO PRO A . n 
A 1 246 GLU 246 246 246 GLU GLU A . n 
A 1 247 LEU 247 247 247 LEU LEU A . n 
A 1 248 ASN 248 248 248 ASN ASN A . n 
A 1 249 ASN 249 249 249 ASN ASN A . n 
A 1 250 LYS 250 250 250 LYS LYS A . n 
A 1 251 LEU 251 251 251 LEU LEU A . n 
A 1 252 LYS 252 252 252 LYS LYS A . n 
A 1 253 ALA 253 253 253 ALA ALA A . n 
A 1 254 LEU 254 254 254 LEU LEU A . n 
A 1 255 ASP 255 255 255 ASP ASP A . n 
A 1 256 VAL 256 256 256 VAL VAL A . n 
A 1 257 PHE 257 257 257 PHE PHE A . n 
A 1 258 ASP 258 258 258 ASP ASP A . n 
A 1 259 PHE 259 259 259 PHE PHE A . n 
A 1 260 THR 260 260 260 THR THR A . n 
A 1 261 PRO 261 261 261 PRO PRO A . n 
A 1 262 ARG 262 262 262 ARG ARG A . n 
A 1 263 PHE 263 263 263 PHE PHE A . n 
A 1 264 GLU 264 264 264 GLU GLU A . n 
A 1 265 TYR 265 265 265 TYR TYR A . n 
A 1 266 TYR 266 266 266 TYR TYR A . n 
A 1 267 VAL 267 267 267 VAL VAL A . n 
A 1 268 ASP 268 268 268 ASP ASP A . n 
A 1 269 LEU 269 269 269 LEU LEU A . n 
A 1 270 VAL 270 270 270 VAL VAL A . n 
A 1 271 TRP 271 271 271 TRP TRP A . n 
A 1 272 SER 272 272 272 SER SER A . n 
A 1 273 ARG 273 273 273 ARG ARG A . n 
A 1 274 GLU 274 274 274 GLU GLU A . n 
A 1 275 SER 275 275 275 SER SER A . n 
A 1 276 GLU 276 276 276 GLU GLU A . n 
A 1 277 LEU 277 277 277 LEU LEU A . n 
A 1 278 GLY 278 278 278 GLY GLY A . n 
A 1 279 ALA 279 279 279 ALA ALA A . n 
A 1 280 ALA 280 280 280 ALA ALA A . n 
A 1 281 ALA 281 281 281 ALA ALA A . n 
A 1 282 ARG 282 282 282 ARG ARG A . n 
A 1 283 PHE 283 283 283 PHE PHE A . n 
A 1 284 LEU 284 284 284 LEU LEU A . n 
A 1 285 ILE 285 285 285 ILE ILE A . n 
A 1 286 ASP 286 286 286 ASP ASP A . n 
A 1 287 TYR 287 287 287 TYR TYR A . n 
A 1 288 ILE 288 288 288 ILE ILE A . n 
A 1 289 ARG 289 289 289 ARG ARG A . n 
A 1 290 ASN 290 290 290 ASN ASN A . n 
A 1 291 LYS 291 291 291 LYS LYS A . n 
A 1 292 ARG 292 292 292 ARG ARG A . n 
A 1 293 MET 293 293 293 MET MET A . n 
A 1 294 GLN 294 294 294 GLN GLN A . n 
A 1 295 PRO 295 295 ?   ?   ?   A . n 
A 1 296 ALA 296 296 ?   ?   ?   A . n 
A 1 297 PRO 297 297 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ASN 2   2   ?   ?   ?   B . n 
B 1 3   ILE 3   3   ?   ?   ?   B . n 
B 1 4   ASN 4   4   ?   ?   ?   B . n 
B 1 5   GLN 5   5   ?   ?   ?   B . n 
B 1 6   GLU 6   6   ?   ?   ?   B . n 
B 1 7   GLN 7   7   ?   ?   ?   B . n 
B 1 8   LEU 8   8   ?   ?   ?   B . n 
B 1 9   LEU 9   9   ?   ?   ?   B . n 
B 1 10  MET 10  10  ?   ?   ?   B . n 
B 1 11  PHE 11  11  ?   ?   ?   B . n 
B 1 12  GLN 12  12  ?   ?   ?   B . n 
B 1 13  ALA 13  13  ?   ?   ?   B . n 
B 1 14  VAL 14  14  ?   ?   ?   B . n 
B 1 15  MET 15  15  ?   ?   ?   B . n 
B 1 16  GLU 16  16  ?   ?   ?   B . n 
B 1 17  THR 17  17  ?   ?   ?   B . n 
B 1 18  GLY 18  18  ?   ?   ?   B . n 
B 1 19  SER 19  19  ?   ?   ?   B . n 
B 1 20  PHE 20  20  ?   ?   ?   B . n 
B 1 21  SER 21  21  ?   ?   ?   B . n 
B 1 22  ALA 22  22  ?   ?   ?   B . n 
B 1 23  ALA 23  23  ?   ?   ?   B . n 
B 1 24  ALA 24  24  ?   ?   ?   B . n 
B 1 25  ARG 25  25  ?   ?   ?   B . n 
B 1 26  LYS 26  26  ?   ?   ?   B . n 
B 1 27  LEU 27  27  ?   ?   ?   B . n 
B 1 28  GLY 28  28  ?   ?   ?   B . n 
B 1 29  LYS 29  29  ?   ?   ?   B . n 
B 1 30  VAL 30  30  ?   ?   ?   B . n 
B 1 31  PRO 31  31  ?   ?   ?   B . n 
B 1 32  SER 32  32  ?   ?   ?   B . n 
B 1 33  ALA 33  33  ?   ?   ?   B . n 
B 1 34  VAL 34  34  ?   ?   ?   B . n 
B 1 35  SER 35  35  ?   ?   ?   B . n 
B 1 36  MET 36  36  ?   ?   ?   B . n 
B 1 37  SER 37  37  ?   ?   ?   B . n 
B 1 38  ILE 38  38  ?   ?   ?   B . n 
B 1 39  ALA 39  39  ?   ?   ?   B . n 
B 1 40  ASN 40  40  ?   ?   ?   B . n 
B 1 41  LEU 41  41  ?   ?   ?   B . n 
B 1 42  GLU 42  42  ?   ?   ?   B . n 
B 1 43  ILE 43  43  ?   ?   ?   B . n 
B 1 44  ASP 44  44  ?   ?   ?   B . n 
B 1 45  LEU 45  45  ?   ?   ?   B . n 
B 1 46  ASN 46  46  ?   ?   ?   B . n 
B 1 47  LEU 47  47  ?   ?   ?   B . n 
B 1 48  THR 48  48  ?   ?   ?   B . n 
B 1 49  LEU 49  49  ?   ?   ?   B . n 
B 1 50  PHE 50  50  ?   ?   ?   B . n 
B 1 51  GLU 51  51  ?   ?   ?   B . n 
B 1 52  ARG 52  52  ?   ?   ?   B . n 
B 1 53  LYS 53  53  ?   ?   ?   B . n 
B 1 54  GLY 54  54  ?   ?   ?   B . n 
B 1 55  ARG 55  55  ?   ?   ?   B . n 
B 1 56  GLU 56  56  ?   ?   ?   B . n 
B 1 57  PRO 57  57  ?   ?   ?   B . n 
B 1 58  THR 58  58  ?   ?   ?   B . n 
B 1 59  PRO 59  59  ?   ?   ?   B . n 
B 1 60  THR 60  60  ?   ?   ?   B . n 
B 1 61  ALA 61  61  ?   ?   ?   B . n 
B 1 62  GLU 62  62  ?   ?   ?   B . n 
B 1 63  ALA 63  63  ?   ?   ?   B . n 
B 1 64  ARG 64  64  ?   ?   ?   B . n 
B 1 65  VAL 65  65  ?   ?   ?   B . n 
B 1 66  LEU 66  66  ?   ?   ?   B . n 
B 1 67  TYR 67  67  ?   ?   ?   B . n 
B 1 68  GLU 68  68  ?   ?   ?   B . n 
B 1 69  LYS 69  69  ?   ?   ?   B . n 
B 1 70  THR 70  70  ?   ?   ?   B . n 
B 1 71  ALA 71  71  ?   ?   ?   B . n 
B 1 72  GLN 72  72  ?   ?   ?   B . n 
B 1 73  LEU 73  73  ?   ?   ?   B . n 
B 1 74  LEU 74  74  ?   ?   ?   B . n 
B 1 75  ILE 75  75  ?   ?   ?   B . n 
B 1 76  GLU 76  76  ?   ?   ?   B . n 
B 1 77  MET 77  77  ?   ?   ?   B . n 
B 1 78  ASN 78  78  ?   ?   ?   B . n 
B 1 79  GLN 79  79  ?   ?   ?   B . n 
B 1 80  TRP 80  80  ?   ?   ?   B . n 
B 1 81  LYS 81  81  ?   ?   ?   B . n 
B 1 82  GLN 82  82  ?   ?   ?   B . n 
B 1 83  HIS 83  83  ?   ?   ?   B . n 
B 1 84  ALA 84  84  ?   ?   ?   B . n 
B 1 85  HIS 85  85  ?   ?   ?   B . n 
B 1 86  ALA 86  86  ?   ?   ?   B . n 
B 1 87  LEU 87  87  ?   ?   ?   B . n 
B 1 88  SER 88  88  ?   ?   ?   B . n 
B 1 89  THR 89  89  ?   ?   ?   B . n 
B 1 90  GLY 90  90  ?   ?   ?   B . n 
B 1 91  LEU 91  91  ?   ?   ?   B . n 
B 1 92  GLU 92  92  ?   ?   ?   B . n 
B 1 93  PRO 93  93  93  PRO PRO B . n 
B 1 94  ASN 94  94  94  ASN ASN B . n 
B 1 95  LEU 95  95  95  LEU LEU B . n 
B 1 96  THR 96  96  96  THR THR B . n 
B 1 97  ILE 97  97  97  ILE ILE B . n 
B 1 98  VAL 98  98  98  VAL VAL B . n 
B 1 99  VAL 99  99  99  VAL VAL B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 GLU 102 102 102 GLU GLU B . n 
B 1 103 LEU 103 103 103 LEU LEU B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 HIS 105 105 105 HIS HIS B . n 
B 1 106 THR 106 106 106 THR THR B . n 
B 1 107 ASN 107 107 107 ASN ASN B . n 
B 1 108 TRP 108 108 108 TRP TRP B . n 
B 1 109 THR 109 109 109 THR THR B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 TYR 111 111 111 TYR TYR B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 CYS 113 113 113 CYS CYS B . n 
B 1 114 LEU 114 114 114 LEU LEU B . n 
B 1 115 LEU 115 115 115 LEU LEU B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 SER 117 117 117 SER SER B . n 
B 1 118 ARG 118 118 118 ARG ARG B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 PRO 120 120 120 PRO PRO B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 GLN 123 123 123 GLN GLN B . n 
B 1 124 ILE 124 124 124 ILE ILE B . n 
B 1 125 ASN 125 125 125 ASN ASN B . n 
B 1 126 ILE 126 126 126 ILE ILE B . n 
B 1 127 VAL 127 127 127 VAL VAL B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 PRO 130 130 130 PRO PRO B . n 
B 1 131 GLN 131 131 131 GLN GLN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 ASP 133 133 133 ASP ASP B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 GLN 136 136 136 GLN GLN B . n 
B 1 137 MET 137 137 137 MET MET B . n 
B 1 138 LEU 138 138 138 LEU LEU B . n 
B 1 139 LEU 139 139 139 LEU LEU B . n 
B 1 140 ASP 140 140 140 ASP ASP B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ALA 143 143 143 ALA ALA B . n 
B 1 144 GLN 144 144 144 GLN GLN B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 ALA 146 146 146 ALA ALA B . n 
B 1 147 LEU 147 147 147 LEU LEU B . n 
B 1 148 MET 148 148 148 MET MET B . n 
B 1 149 PHE 149 149 149 PHE PHE B . n 
B 1 150 GLU 150 150 150 GLU GLU B . n 
B 1 151 ARG 151 151 ?   ?   ?   B . n 
B 1 152 GLU 152 152 ?   ?   ?   B . n 
B 1 153 HIS 153 153 ?   ?   ?   B . n 
B 1 154 LEU 154 154 154 LEU LEU B . n 
B 1 155 ASP 155 155 155 ASP ASP B . n 
B 1 156 ASN 156 156 156 ASN ASN B . n 
B 1 157 ARG 157 157 157 ARG ARG B . n 
B 1 158 GLU 158 158 158 GLU GLU B . n 
B 1 159 GLN 159 159 159 GLN GLN B . n 
B 1 160 PHE 160 160 160 PHE PHE B . n 
B 1 161 VAL 161 161 161 VAL VAL B . n 
B 1 162 GLU 162 162 162 GLU GLU B . n 
B 1 163 LEU 163 163 163 LEU LEU B . n 
B 1 164 LYS 164 164 164 LYS LYS B . n 
B 1 165 ARG 165 165 165 ARG ARG B . n 
B 1 166 GLU 166 166 166 GLU GLU B . n 
B 1 167 ALA 167 167 167 ALA ALA B . n 
B 1 168 LEU 168 168 168 LEU LEU B . n 
B 1 169 ILE 169 169 169 ILE ILE B . n 
B 1 170 PRO 170 170 170 PRO PRO B . n 
B 1 171 VAL 171 171 171 VAL VAL B . n 
B 1 172 ILE 172 172 172 ILE ILE B . n 
B 1 173 SER 173 173 173 SER SER B . n 
B 1 174 LYS 174 174 174 LYS LYS B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 HIS 176 176 176 HIS HIS B . n 
B 1 177 PRO 177 177 177 PRO PRO B . n 
B 1 178 LEU 178 178 178 LEU LEU B . n 
B 1 179 ALA 179 179 179 ALA ALA B . n 
B 1 180 SER 180 180 180 SER SER B . n 
B 1 181 GLN 181 181 181 GLN GLN B . n 
B 1 182 GLU 182 182 182 GLU GLU B . n 
B 1 183 HIS 183 183 183 HIS HIS B . n 
B 1 184 VAL 184 184 184 VAL VAL B . n 
B 1 185 SER 185 185 185 SER SER B . n 
B 1 186 TYR 186 186 186 TYR TYR B . n 
B 1 187 GLU 187 187 187 GLU GLU B . n 
B 1 188 GLN 188 188 188 GLN GLN B . n 
B 1 189 ILE 189 189 189 ILE ILE B . n 
B 1 190 LEU 190 190 190 LEU LEU B . n 
B 1 191 GLY 191 191 191 GLY GLY B . n 
B 1 192 THR 192 192 192 THR THR B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 GLN 194 194 194 GLN GLN B . n 
B 1 195 ILE 195 195 195 ILE ILE B . n 
B 1 196 VAL 196 196 196 VAL VAL B . n 
B 1 197 VAL 197 197 197 VAL VAL B . n 
B 1 198 ALA 198 198 198 ALA ALA B . n 
B 1 199 SER 199 199 199 SER SER B . n 
B 1 200 ARG 200 200 ?   ?   ?   B . n 
B 1 201 ASP 201 201 ?   ?   ?   B . n 
B 1 202 GLU 202 202 ?   ?   ?   B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 LEU 204 204 204 LEU LEU B . n 
B 1 205 LYS 205 205 205 LYS LYS B . n 
B 1 206 PRO 206 206 206 PRO PRO B . n 
B 1 207 GLU 207 207 207 GLU GLU B . n 
B 1 208 LEU 208 208 208 LEU LEU B . n 
B 1 209 LEU 209 209 209 LEU LEU B . n 
B 1 210 PHE 210 210 210 PHE PHE B . n 
B 1 211 SER 211 211 211 SER SER B . n 
B 1 212 LYS 212 212 212 LYS LYS B . n 
B 1 213 HIS 213 213 213 HIS HIS B . n 
B 1 214 TYR 214 214 214 TYR TYR B . n 
B 1 215 TRP 215 215 215 TRP TRP B . n 
B 1 216 ARG 216 216 216 ARG ARG B . n 
B 1 217 THR 217 217 217 THR THR B . n 
B 1 218 ASP 218 218 218 ASP ASP B . n 
B 1 219 ASN 219 219 219 ASN ASN B . n 
B 1 220 HIS 220 220 220 HIS HIS B . n 
B 1 221 HIS 221 221 221 HIS HIS B . n 
B 1 222 SER 222 222 222 SER SER B . n 
B 1 223 ALA 223 223 223 ALA ALA B . n 
B 1 224 CYS 224 224 224 CYS CYS B . n 
B 1 225 LEU 225 225 225 LEU LEU B . n 
B 1 226 MET 226 226 226 MET MET B . n 
B 1 227 ILE 227 227 227 ILE ILE B . n 
B 1 228 LEU 228 228 228 LEU LEU B . n 
B 1 229 ARG 229 229 229 ARG ARG B . n 
B 1 230 ASN 230 230 230 ASN ASN B . n 
B 1 231 LEU 231 231 231 LEU LEU B . n 
B 1 232 GLY 232 232 232 GLY GLY B . n 
B 1 233 TRP 233 233 233 TRP TRP B . n 
B 1 234 GLY 234 234 234 GLY GLY B . n 
B 1 235 VAL 235 235 235 VAL VAL B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 PRO 237 237 237 PRO PRO B . n 
B 1 238 GLN 238 238 238 GLN GLN B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 MET 240 240 240 MET MET B . n 
B 1 241 PHE 241 241 241 PHE PHE B . n 
B 1 242 LYS 242 242 242 LYS LYS B . n 
B 1 243 GLU 243 243 243 GLU GLU B . n 
B 1 244 ASN 244 244 244 ASN ASN B . n 
B 1 245 PRO 245 245 245 PRO PRO B . n 
B 1 246 GLU 246 246 246 GLU GLU B . n 
B 1 247 LEU 247 247 247 LEU LEU B . n 
B 1 248 ASN 248 248 248 ASN ASN B . n 
B 1 249 ASN 249 249 249 ASN ASN B . n 
B 1 250 LYS 250 250 250 LYS LYS B . n 
B 1 251 LEU 251 251 251 LEU LEU B . n 
B 1 252 LYS 252 252 252 LYS LYS B . n 
B 1 253 ALA 253 253 253 ALA ALA B . n 
B 1 254 LEU 254 254 254 LEU LEU B . n 
B 1 255 ASP 255 255 255 ASP ASP B . n 
B 1 256 VAL 256 256 256 VAL VAL B . n 
B 1 257 PHE 257 257 257 PHE PHE B . n 
B 1 258 ASP 258 258 258 ASP ASP B . n 
B 1 259 PHE 259 259 259 PHE PHE B . n 
B 1 260 THR 260 260 260 THR THR B . n 
B 1 261 PRO 261 261 261 PRO PRO B . n 
B 1 262 ARG 262 262 262 ARG ARG B . n 
B 1 263 PHE 263 263 263 PHE PHE B . n 
B 1 264 GLU 264 264 264 GLU GLU B . n 
B 1 265 TYR 265 265 265 TYR TYR B . n 
B 1 266 TYR 266 266 266 TYR TYR B . n 
B 1 267 VAL 267 267 267 VAL VAL B . n 
B 1 268 ASP 268 268 268 ASP ASP B . n 
B 1 269 LEU 269 269 269 LEU LEU B . n 
B 1 270 VAL 270 270 270 VAL VAL B . n 
B 1 271 TRP 271 271 271 TRP TRP B . n 
B 1 272 SER 272 272 272 SER SER B . n 
B 1 273 ARG 273 273 273 ARG ARG B . n 
B 1 274 GLU 274 274 274 GLU GLU B . n 
B 1 275 SER 275 275 275 SER SER B . n 
B 1 276 GLU 276 276 276 GLU GLU B . n 
B 1 277 LEU 277 277 277 LEU LEU B . n 
B 1 278 GLY 278 278 278 GLY GLY B . n 
B 1 279 ALA 279 279 279 ALA ALA B . n 
B 1 280 ALA 280 280 280 ALA ALA B . n 
B 1 281 ALA 281 281 281 ALA ALA B . n 
B 1 282 ARG 282 282 282 ARG ARG B . n 
B 1 283 PHE 283 283 283 PHE PHE B . n 
B 1 284 LEU 284 284 284 LEU LEU B . n 
B 1 285 ILE 285 285 285 ILE ILE B . n 
B 1 286 ASP 286 286 286 ASP ASP B . n 
B 1 287 TYR 287 287 287 TYR TYR B . n 
B 1 288 ILE 288 288 288 ILE ILE B . n 
B 1 289 ARG 289 289 289 ARG ARG B . n 
B 1 290 ASN 290 290 290 ASN ASN B . n 
B 1 291 LYS 291 291 291 LYS LYS B . n 
B 1 292 ARG 292 292 292 ARG ARG B . n 
B 1 293 MET 293 293 293 MET MET B . n 
B 1 294 GLN 294 294 ?   ?   ?   B . n 
B 1 295 PRO 295 295 ?   ?   ?   B . n 
B 1 296 ALA 296 296 ?   ?   ?   B . n 
B 1 297 PRO 297 297 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 HOH 1  301 12 HOH HOH A . 
C 2 HOH 2  302 53 HOH HOH A . 
C 2 HOH 3  303 2  HOH HOH A . 
C 2 HOH 4  304 23 HOH HOH A . 
C 2 HOH 5  305 66 HOH HOH A . 
C 2 HOH 6  306 21 HOH HOH A . 
C 2 HOH 7  307 38 HOH HOH A . 
C 2 HOH 8  308 33 HOH HOH A . 
C 2 HOH 9  309 11 HOH HOH A . 
C 2 HOH 10 310 79 HOH HOH A . 
C 2 HOH 11 311 86 HOH HOH A . 
C 2 HOH 12 312 70 HOH HOH A . 
C 2 HOH 13 313 45 HOH HOH A . 
C 2 HOH 14 314 84 HOH HOH A . 
C 2 HOH 15 315 15 HOH HOH A . 
C 2 HOH 16 316 19 HOH HOH A . 
C 2 HOH 17 317 1  HOH HOH A . 
C 2 HOH 18 318 80 HOH HOH A . 
C 2 HOH 19 319 61 HOH HOH A . 
C 2 HOH 20 320 43 HOH HOH A . 
C 2 HOH 21 321 65 HOH HOH A . 
C 2 HOH 22 322 10 HOH HOH A . 
C 2 HOH 23 323 24 HOH HOH A . 
C 2 HOH 24 324 7  HOH HOH A . 
C 2 HOH 25 325 20 HOH HOH A . 
C 2 HOH 26 326 9  HOH HOH A . 
C 2 HOH 27 327 5  HOH HOH A . 
C 2 HOH 28 328 58 HOH HOH A . 
C 2 HOH 29 329 44 HOH HOH A . 
C 2 HOH 30 330 26 HOH HOH A . 
C 2 HOH 31 331 29 HOH HOH A . 
C 2 HOH 32 332 49 HOH HOH A . 
C 2 HOH 33 333 40 HOH HOH A . 
C 2 HOH 34 334 31 HOH HOH A . 
C 2 HOH 35 335 37 HOH HOH A . 
C 2 HOH 36 336 8  HOH HOH A . 
C 2 HOH 37 337 14 HOH HOH A . 
C 2 HOH 38 338 56 HOH HOH A . 
C 2 HOH 39 339 22 HOH HOH A . 
C 2 HOH 40 340 30 HOH HOH A . 
C 2 HOH 41 341 34 HOH HOH A . 
C 2 HOH 42 342 17 HOH HOH A . 
C 2 HOH 43 343 60 HOH HOH A . 
C 2 HOH 44 344 59 HOH HOH A . 
C 2 HOH 45 345 46 HOH HOH A . 
C 2 HOH 46 346 74 HOH HOH A . 
C 2 HOH 47 347 36 HOH HOH A . 
C 2 HOH 48 348 54 HOH HOH A . 
D 2 HOH 1  301 39 HOH HOH B . 
D 2 HOH 2  302 62 HOH HOH B . 
D 2 HOH 3  303 3  HOH HOH B . 
D 2 HOH 4  304 32 HOH HOH B . 
D 2 HOH 5  305 35 HOH HOH B . 
D 2 HOH 6  306 13 HOH HOH B . 
D 2 HOH 7  307 67 HOH HOH B . 
D 2 HOH 8  308 77 HOH HOH B . 
D 2 HOH 9  309 4  HOH HOH B . 
D 2 HOH 10 310 25 HOH HOH B . 
D 2 HOH 11 311 55 HOH HOH B . 
D 2 HOH 12 312 48 HOH HOH B . 
D 2 HOH 13 313 51 HOH HOH B . 
D 2 HOH 14 314 16 HOH HOH B . 
D 2 HOH 15 315 27 HOH HOH B . 
D 2 HOH 16 316 18 HOH HOH B . 
D 2 HOH 17 317 6  HOH HOH B . 
D 2 HOH 18 318 52 HOH HOH B . 
D 2 HOH 19 319 81 HOH HOH B . 
D 2 HOH 20 320 50 HOH HOH B . 
D 2 HOH 21 321 64 HOH HOH B . 
D 2 HOH 22 322 87 HOH HOH B . 
D 2 HOH 23 323 42 HOH HOH B . 
D 2 HOH 24 324 28 HOH HOH B . 
D 2 HOH 25 325 78 HOH HOH B . 
D 2 HOH 26 326 71 HOH HOH B . 
D 2 HOH 27 327 69 HOH HOH B . 
D 2 HOH 28 328 63 HOH HOH B . 
D 2 HOH 29 329 73 HOH HOH B . 
D 2 HOH 30 330 41 HOH HOH B . 
D 2 HOH 31 331 68 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.19.2_4158: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8J4N 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     77.520 
_cell.length_a_esd                 ? 
_cell.length_b                     101.219 
_cell.length_b_esd                 ? 
_cell.length_c                     57.970 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8J4N 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_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                   8J4N 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             1.66 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          26.08 
_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' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '1.5 M Ammonium sulfate, 0.1 M Tris-HCl pH8.5' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            290 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     80 
_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 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-09-10 
_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   0.9792 
_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                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9792 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8J4N 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.23 
_reflns.d_resolution_low                               61.54 
_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                                     22957 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.7 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.3 
_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                                0.094 
_reflns.pdbx_Rpim_I_all                                0.043 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.083 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.23 
_reflns_shell.d_res_low                                     2.35 
_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                             3285 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.794 
_reflns_shell.pdbx_Rpim_I_all                               0.364 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.787 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          99.9 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.703 
_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                                 8J4N 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.23 
_refine.ls_d_res_low                             42.38 
_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                     22912 
_refine.ls_number_reflns_R_free                  1095 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.55 
_refine.ls_percent_reflns_R_free                 4.78 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1995 
_refine.ls_R_factor_R_free                       0.2390 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1976 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      AlphaFold 
_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                 24.15 
_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                            0.26 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.23 
_refine_hist.d_res_low                        42.38 
_refine_hist.number_atoms_solvent             79 
_refine_hist.number_atoms_total               3296 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3217 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004 ? 3293 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.740 ? 4463 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 6.066 ? 422  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.048 ? 505  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007 ? 568  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.23 2.33  . . 144 2672 100.00 . . . . 0.2707 . . . . . . . . . . . 0.3552 
'X-RAY DIFFRACTION' 2.33 2.45  . . 139 2674 100.00 . . . . 0.2445 . . . . . . . . . . . 0.3068 
'X-RAY DIFFRACTION' 2.45 2.60  . . 145 2694 100.00 . . . . 0.2244 . . . . . . . . . . . 0.2279 
'X-RAY DIFFRACTION' 2.60 2.80  . . 124 2709 100.00 . . . . 0.2125 . . . . . . . . . . . 0.2462 
'X-RAY DIFFRACTION' 2.80 3.09  . . 127 2721 100.00 . . . . 0.2241 . . . . . . . . . . . 0.3006 
'X-RAY DIFFRACTION' 3.09 3.53  . . 142 2714 99.00  . . . . 0.2046 . . . . . . . . . . . 0.2739 
'X-RAY DIFFRACTION' 3.53 4.45  . . 143 2739 99.00  . . . . 0.1658 . . . . . . . . . . . 0.1840 
'X-RAY DIFFRACTION' 4.45 42.38 . . 131 2894 99.00  . . . . 0.1819 . . . . . . . . . . . 0.2183 
# 
_struct.entry_id                     8J4N 
_struct.title                        
'Crystal Structure of the Acinetobacter baumannii LysR family regulator AceR effector-binding domain (APO FORM)' 
_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        8J4N 
_struct_keywords.text            'LysR family regulator, effector-binding domain, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    V5VDR8_ACIBA 
_struct_ref.pdbx_db_accession          V5VDR8 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MNINQEQLLMFQAVMETGSFSAAARKLGKVPSAVSMSIANLEIDLNLTLFERKGREPTPTAEARVLYEKTAQLLIEMNQW
KQHAHALSTGLEPNLTIVVVSELLHTNWTDYVCLLESRFPDLQINIVSAPQEDALQMLLDGSAQLALMFEREHLDNREQF
VELKREALIPVISKTHPLASQEHVSYEQILGTRQIVVASRDETLKPELLFSKHYWRTDNHHSACLMILRNLGWGVLPQEM
FKENPELNNKLKALDVFDFTPRFEYYVDLVWSRESELGAAARFLIDYIRNKRMQPAP
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8J4N A 1 ? 297 ? V5VDR8 1 ? 297 ? 1 297 
2 1 8J4N B 1 ? 297 ? V5VDR8 1 ? 297 ? 1 297 
# 
_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)' 3200  ? 
1 MORE         -12   ? 
1 'SSA (A^2)'  18800 ? 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLU A 102 ? LEU A 104 ? GLU A 102 LEU A 104 5 ? 3  
HELX_P HELX_P2  AA2 TRP A 108 ? PHE A 119 ? TRP A 108 PHE A 119 1 ? 12 
HELX_P HELX_P3  AA3 PRO A 130 ? ASP A 140 ? PRO A 130 ASP A 140 1 ? 11 
HELX_P HELX_P4  AA4 HIS A 176 ? GLN A 181 ? HIS A 176 GLN A 181 5 ? 6  
HELX_P HELX_P5  AA5 SER A 185 ? GLY A 191 ? SER A 185 GLY A 191 1 ? 7  
HELX_P HELX_P6  AA6 LYS A 205 ? LEU A 209 ? LYS A 205 LEU A 209 5 ? 5  
HELX_P HELX_P7  AA7 ASN A 219 ? ARG A 229 ? ASN A 219 ARG A 229 1 ? 11 
HELX_P HELX_P8  AA8 GLN A 238 ? ASN A 244 ? GLN A 238 ASN A 244 1 ? 7  
HELX_P HELX_P9  AA9 PRO A 245 ? LYS A 250 ? PRO A 245 LYS A 250 1 ? 6  
HELX_P HELX_P10 AB1 GLY A 278 ? MET A 293 ? GLY A 278 MET A 293 1 ? 16 
HELX_P HELX_P11 AB2 GLU B 102 ? LEU B 104 ? GLU B 102 LEU B 104 5 ? 3  
HELX_P HELX_P12 AB3 TRP B 108 ? PHE B 119 ? TRP B 108 PHE B 119 1 ? 12 
HELX_P HELX_P13 AB4 PRO B 130 ? ASP B 140 ? PRO B 130 ASP B 140 1 ? 11 
HELX_P HELX_P14 AB5 HIS B 176 ? GLN B 181 ? HIS B 176 GLN B 181 5 ? 6  
HELX_P HELX_P15 AB6 SER B 185 ? GLY B 191 ? SER B 185 GLY B 191 1 ? 7  
HELX_P HELX_P16 AB7 LYS B 205 ? LEU B 209 ? LYS B 205 LEU B 209 5 ? 5  
HELX_P HELX_P17 AB8 ASN B 219 ? ARG B 229 ? ASN B 219 ARG B 229 1 ? 11 
HELX_P HELX_P18 AB9 GLN B 238 ? ASN B 244 ? GLN B 238 ASN B 244 1 ? 7  
HELX_P HELX_P19 AC1 GLU B 246 ? LYS B 250 ? GLU B 246 LYS B 250 1 ? 5  
HELX_P HELX_P20 AC2 VAL B 256 ? THR B 260 ? VAL B 256 THR B 260 5 ? 5  
HELX_P HELX_P21 AC3 GLY B 278 ? ARG B 292 ? GLY B 278 ARG B 292 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 6 ? 
AA3 ? 8 ? 
AA4 ? 6 ? 
# 
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 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? 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 GLN A 123 ? ALA A 129 ? GLN A 123 ALA A 129 
AA1 2 ASN A 94  ? VAL A 100 ? ASN A 94  VAL A 100 
AA1 3 LEU A 145 ? PHE A 149 ? LEU A 145 PHE A 149 
AA1 4 GLU A 264 ? SER A 272 ? GLU A 264 SER A 272 
AA1 5 GLU A 158 ? SER A 173 ? GLU A 158 SER A 173 
AA1 6 TRP A 233 ? PRO A 237 ? TRP A 233 PRO A 237 
AA1 7 GLN A 194 ? VAL A 197 ? GLN A 194 VAL A 197 
AA1 8 TYR A 214 ? THR A 217 ? TYR A 214 THR A 217 
AA2 1 GLN A 123 ? ALA A 129 ? GLN A 123 ALA A 129 
AA2 2 ASN A 94  ? VAL A 100 ? ASN A 94  VAL A 100 
AA2 3 LEU A 145 ? PHE A 149 ? LEU A 145 PHE A 149 
AA2 4 GLU A 264 ? SER A 272 ? GLU A 264 SER A 272 
AA2 5 GLU A 158 ? SER A 173 ? GLU A 158 SER A 173 
AA2 6 LEU A 251 ? ALA A 253 ? LEU A 251 ALA A 253 
AA3 1 GLN B 123 ? ALA B 129 ? GLN B 123 ALA B 129 
AA3 2 ASN B 94  ? VAL B 100 ? ASN B 94  VAL B 100 
AA3 3 LEU B 145 ? MET B 148 ? LEU B 145 MET B 148 
AA3 4 GLU B 264 ? SER B 272 ? GLU B 264 SER B 272 
AA3 5 GLU B 158 ? SER B 173 ? GLU B 158 SER B 173 
AA3 6 TRP B 233 ? PRO B 237 ? TRP B 233 PRO B 237 
AA3 7 GLN B 194 ? VAL B 197 ? GLN B 194 VAL B 197 
AA3 8 TYR B 214 ? THR B 217 ? TYR B 214 THR B 217 
AA4 1 GLN B 123 ? ALA B 129 ? GLN B 123 ALA B 129 
AA4 2 ASN B 94  ? VAL B 100 ? ASN B 94  VAL B 100 
AA4 3 LEU B 145 ? MET B 148 ? LEU B 145 MET B 148 
AA4 4 GLU B 264 ? SER B 272 ? GLU B 264 SER B 272 
AA4 5 GLU B 158 ? SER B 173 ? GLU B 158 SER B 173 
AA4 6 LEU B 251 ? ALA B 253 ? LEU B 251 ALA B 253 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O VAL A 127 ? O VAL A 127 N VAL A 99  ? N VAL A 99  
AA1 2 3 N VAL A 98  ? N VAL A 98  O LEU A 147 ? O LEU A 147 
AA1 3 4 N MET A 148 ? N MET A 148 O ASP A 268 ? O ASP A 268 
AA1 4 5 O VAL A 267 ? O VAL A 267 N LEU A 163 ? N LEU A 163 
AA1 5 6 N ILE A 169 ? N ILE A 169 O LEU A 236 ? O LEU A 236 
AA1 6 7 O TRP A 233 ? O TRP A 233 N ILE A 195 ? N ILE A 195 
AA1 7 8 N VAL A 196 ? N VAL A 196 O TRP A 215 ? O TRP A 215 
AA2 1 2 O VAL A 127 ? O VAL A 127 N VAL A 99  ? N VAL A 99  
AA2 2 3 N VAL A 98  ? N VAL A 98  O LEU A 147 ? O LEU A 147 
AA2 3 4 N MET A 148 ? N MET A 148 O ASP A 268 ? O ASP A 268 
AA2 4 5 O VAL A 267 ? O VAL A 267 N LEU A 163 ? N LEU A 163 
AA2 5 6 N ILE A 172 ? N ILE A 172 O LYS A 252 ? O LYS A 252 
AA3 1 2 O VAL B 127 ? O VAL B 127 N VAL B 99  ? N VAL B 99  
AA3 2 3 N VAL B 98  ? N VAL B 98  O LEU B 145 ? O LEU B 145 
AA3 3 4 N MET B 148 ? N MET B 148 O ASP B 268 ? O ASP B 268 
AA3 4 5 O LEU B 269 ? O LEU B 269 N VAL B 161 ? N VAL B 161 
AA3 5 6 N VAL B 171 ? N VAL B 171 O GLY B 234 ? O GLY B 234 
AA3 6 7 O TRP B 233 ? O TRP B 233 N ILE B 195 ? N ILE B 195 
AA3 7 8 N VAL B 196 ? N VAL B 196 O TRP B 215 ? O TRP B 215 
AA4 1 2 O VAL B 127 ? O VAL B 127 N VAL B 99  ? N VAL B 99  
AA4 2 3 N VAL B 98  ? N VAL B 98  O LEU B 145 ? O LEU B 145 
AA4 3 4 N MET B 148 ? N MET B 148 O ASP B 268 ? O ASP B 268 
AA4 4 5 O LEU B 269 ? O LEU B 269 N VAL B 161 ? N VAL B 161 
AA4 5 6 N ILE B 172 ? N ILE B 172 O LYS B 252 ? O LYS B 252 
# 
_pdbx_entry_details.entry_id                   8J4N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 92  ? ? 82.14   105.84  
2 1 GLU A 150 ? ? 63.38   -71.81  
3 1 THR B 106 ? ? -104.92 -168.35 
4 1 LEU B 163 ? ? -103.99 -67.18  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -21.6111 19.8937 -0.5325 0.1784 ? 0.0076 ? -0.0070 ? 0.2016 ? -0.0158 ? 0.2321 ? 0.6203 ? -0.0549 
? 0.2654  ? 0.9920 ? -0.2118 ? 2.3220 ? -0.0296 ? 0.0727  ? -0.1026 ? -0.0532 ? 0.0081 ? 0.0069 ? 0.1529  ? 0.0512  ? 0.0000 ? 
2 'X-RAY DIFFRACTION' ? refined -24.4583 40.3173 5.0465  0.1801 ? 0.0174 ? -0.0257 ? 0.1760 ? -0.0249 ? 0.2116 ? 0.7500 ? 0.5276  
? -0.8146 ? 1.2320 ? -0.6146 ? 1.9370 ? 0.0204  ? -0.0443 ? 0.1425  ? 0.1486  ? 0.0363 ? 0.1179 ? -0.1385 ? -0.0816 ? 0.0000 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? ? ? ? ? ? ? ? ? ? '(chain A and resseq 91:295)' 
2 'X-RAY DIFFRACTION' 2 ? ? ? ? ? ? ? ? ? ? ? '(chain B and resseq 93:293)' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1   1 Y 1 A MET 1   ? A MET 1   
2   1 Y 1 A ASN 2   ? A ASN 2   
3   1 Y 1 A ILE 3   ? A ILE 3   
4   1 Y 1 A ASN 4   ? A ASN 4   
5   1 Y 1 A GLN 5   ? A GLN 5   
6   1 Y 1 A GLU 6   ? A GLU 6   
7   1 Y 1 A GLN 7   ? A GLN 7   
8   1 Y 1 A LEU 8   ? A LEU 8   
9   1 Y 1 A LEU 9   ? A LEU 9   
10  1 Y 1 A MET 10  ? A MET 10  
11  1 Y 1 A PHE 11  ? A PHE 11  
12  1 Y 1 A GLN 12  ? A GLN 12  
13  1 Y 1 A ALA 13  ? A ALA 13  
14  1 Y 1 A VAL 14  ? A VAL 14  
15  1 Y 1 A MET 15  ? A MET 15  
16  1 Y 1 A GLU 16  ? A GLU 16  
17  1 Y 1 A THR 17  ? A THR 17  
18  1 Y 1 A GLY 18  ? A GLY 18  
19  1 Y 1 A SER 19  ? A SER 19  
20  1 Y 1 A PHE 20  ? A PHE 20  
21  1 Y 1 A SER 21  ? A SER 21  
22  1 Y 1 A ALA 22  ? A ALA 22  
23  1 Y 1 A ALA 23  ? A ALA 23  
24  1 Y 1 A ALA 24  ? A ALA 24  
25  1 Y 1 A ARG 25  ? A ARG 25  
26  1 Y 1 A LYS 26  ? A LYS 26  
27  1 Y 1 A LEU 27  ? A LEU 27  
28  1 Y 1 A GLY 28  ? A GLY 28  
29  1 Y 1 A LYS 29  ? A LYS 29  
30  1 Y 1 A VAL 30  ? A VAL 30  
31  1 Y 1 A PRO 31  ? A PRO 31  
32  1 Y 1 A SER 32  ? A SER 32  
33  1 Y 1 A ALA 33  ? A ALA 33  
34  1 Y 1 A VAL 34  ? A VAL 34  
35  1 Y 1 A SER 35  ? A SER 35  
36  1 Y 1 A MET 36  ? A MET 36  
37  1 Y 1 A SER 37  ? A SER 37  
38  1 Y 1 A ILE 38  ? A ILE 38  
39  1 Y 1 A ALA 39  ? A ALA 39  
40  1 Y 1 A ASN 40  ? A ASN 40  
41  1 Y 1 A LEU 41  ? A LEU 41  
42  1 Y 1 A GLU 42  ? A GLU 42  
43  1 Y 1 A ILE 43  ? A ILE 43  
44  1 Y 1 A ASP 44  ? A ASP 44  
45  1 Y 1 A LEU 45  ? A LEU 45  
46  1 Y 1 A ASN 46  ? A ASN 46  
47  1 Y 1 A LEU 47  ? A LEU 47  
48  1 Y 1 A THR 48  ? A THR 48  
49  1 Y 1 A LEU 49  ? A LEU 49  
50  1 Y 1 A PHE 50  ? A PHE 50  
51  1 Y 1 A GLU 51  ? A GLU 51  
52  1 Y 1 A ARG 52  ? A ARG 52  
53  1 Y 1 A LYS 53  ? A LYS 53  
54  1 Y 1 A GLY 54  ? A GLY 54  
55  1 Y 1 A ARG 55  ? A ARG 55  
56  1 Y 1 A GLU 56  ? A GLU 56  
57  1 Y 1 A PRO 57  ? A PRO 57  
58  1 Y 1 A THR 58  ? A THR 58  
59  1 Y 1 A PRO 59  ? A PRO 59  
60  1 Y 1 A THR 60  ? A THR 60  
61  1 Y 1 A ALA 61  ? A ALA 61  
62  1 Y 1 A GLU 62  ? A GLU 62  
63  1 Y 1 A ALA 63  ? A ALA 63  
64  1 Y 1 A ARG 64  ? A ARG 64  
65  1 Y 1 A VAL 65  ? A VAL 65  
66  1 Y 1 A LEU 66  ? A LEU 66  
67  1 Y 1 A TYR 67  ? A TYR 67  
68  1 Y 1 A GLU 68  ? A GLU 68  
69  1 Y 1 A LYS 69  ? A LYS 69  
70  1 Y 1 A THR 70  ? A THR 70  
71  1 Y 1 A ALA 71  ? A ALA 71  
72  1 Y 1 A GLN 72  ? A GLN 72  
73  1 Y 1 A LEU 73  ? A LEU 73  
74  1 Y 1 A LEU 74  ? A LEU 74  
75  1 Y 1 A ILE 75  ? A ILE 75  
76  1 Y 1 A GLU 76  ? A GLU 76  
77  1 Y 1 A MET 77  ? A MET 77  
78  1 Y 1 A ASN 78  ? A ASN 78  
79  1 Y 1 A GLN 79  ? A GLN 79  
80  1 Y 1 A TRP 80  ? A TRP 80  
81  1 Y 1 A LYS 81  ? A LYS 81  
82  1 Y 1 A GLN 82  ? A GLN 82  
83  1 Y 1 A HIS 83  ? A HIS 83  
84  1 Y 1 A ALA 84  ? A ALA 84  
85  1 Y 1 A HIS 85  ? A HIS 85  
86  1 Y 1 A ALA 86  ? A ALA 86  
87  1 Y 1 A LEU 87  ? A LEU 87  
88  1 Y 1 A SER 88  ? A SER 88  
89  1 Y 1 A THR 89  ? A THR 89  
90  1 Y 1 A GLY 90  ? A GLY 90  
91  1 Y 1 A GLU 152 ? A GLU 152 
92  1 Y 1 A HIS 153 ? A HIS 153 
93  1 Y 1 A LEU 154 ? A LEU 154 
94  1 Y 1 A GLU 182 ? A GLU 182 
95  1 Y 1 A HIS 183 ? A HIS 183 
96  1 Y 1 A ASP 201 ? A ASP 201 
97  1 Y 1 A GLU 202 ? A GLU 202 
98  1 Y 1 A PRO 295 ? A PRO 295 
99  1 Y 1 A ALA 296 ? A ALA 296 
100 1 Y 1 A PRO 297 ? A PRO 297 
101 1 Y 1 B MET 1   ? B MET 1   
102 1 Y 1 B ASN 2   ? B ASN 2   
103 1 Y 1 B ILE 3   ? B ILE 3   
104 1 Y 1 B ASN 4   ? B ASN 4   
105 1 Y 1 B GLN 5   ? B GLN 5   
106 1 Y 1 B GLU 6   ? B GLU 6   
107 1 Y 1 B GLN 7   ? B GLN 7   
108 1 Y 1 B LEU 8   ? B LEU 8   
109 1 Y 1 B LEU 9   ? B LEU 9   
110 1 Y 1 B MET 10  ? B MET 10  
111 1 Y 1 B PHE 11  ? B PHE 11  
112 1 Y 1 B GLN 12  ? B GLN 12  
113 1 Y 1 B ALA 13  ? B ALA 13  
114 1 Y 1 B VAL 14  ? B VAL 14  
115 1 Y 1 B MET 15  ? B MET 15  
116 1 Y 1 B GLU 16  ? B GLU 16  
117 1 Y 1 B THR 17  ? B THR 17  
118 1 Y 1 B GLY 18  ? B GLY 18  
119 1 Y 1 B SER 19  ? B SER 19  
120 1 Y 1 B PHE 20  ? B PHE 20  
121 1 Y 1 B SER 21  ? B SER 21  
122 1 Y 1 B ALA 22  ? B ALA 22  
123 1 Y 1 B ALA 23  ? B ALA 23  
124 1 Y 1 B ALA 24  ? B ALA 24  
125 1 Y 1 B ARG 25  ? B ARG 25  
126 1 Y 1 B LYS 26  ? B LYS 26  
127 1 Y 1 B LEU 27  ? B LEU 27  
128 1 Y 1 B GLY 28  ? B GLY 28  
129 1 Y 1 B LYS 29  ? B LYS 29  
130 1 Y 1 B VAL 30  ? B VAL 30  
131 1 Y 1 B PRO 31  ? B PRO 31  
132 1 Y 1 B SER 32  ? B SER 32  
133 1 Y 1 B ALA 33  ? B ALA 33  
134 1 Y 1 B VAL 34  ? B VAL 34  
135 1 Y 1 B SER 35  ? B SER 35  
136 1 Y 1 B MET 36  ? B MET 36  
137 1 Y 1 B SER 37  ? B SER 37  
138 1 Y 1 B ILE 38  ? B ILE 38  
139 1 Y 1 B ALA 39  ? B ALA 39  
140 1 Y 1 B ASN 40  ? B ASN 40  
141 1 Y 1 B LEU 41  ? B LEU 41  
142 1 Y 1 B GLU 42  ? B GLU 42  
143 1 Y 1 B ILE 43  ? B ILE 43  
144 1 Y 1 B ASP 44  ? B ASP 44  
145 1 Y 1 B LEU 45  ? B LEU 45  
146 1 Y 1 B ASN 46  ? B ASN 46  
147 1 Y 1 B LEU 47  ? B LEU 47  
148 1 Y 1 B THR 48  ? B THR 48  
149 1 Y 1 B LEU 49  ? B LEU 49  
150 1 Y 1 B PHE 50  ? B PHE 50  
151 1 Y 1 B GLU 51  ? B GLU 51  
152 1 Y 1 B ARG 52  ? B ARG 52  
153 1 Y 1 B LYS 53  ? B LYS 53  
154 1 Y 1 B GLY 54  ? B GLY 54  
155 1 Y 1 B ARG 55  ? B ARG 55  
156 1 Y 1 B GLU 56  ? B GLU 56  
157 1 Y 1 B PRO 57  ? B PRO 57  
158 1 Y 1 B THR 58  ? B THR 58  
159 1 Y 1 B PRO 59  ? B PRO 59  
160 1 Y 1 B THR 60  ? B THR 60  
161 1 Y 1 B ALA 61  ? B ALA 61  
162 1 Y 1 B GLU 62  ? B GLU 62  
163 1 Y 1 B ALA 63  ? B ALA 63  
164 1 Y 1 B ARG 64  ? B ARG 64  
165 1 Y 1 B VAL 65  ? B VAL 65  
166 1 Y 1 B LEU 66  ? B LEU 66  
167 1 Y 1 B TYR 67  ? B TYR 67  
168 1 Y 1 B GLU 68  ? B GLU 68  
169 1 Y 1 B LYS 69  ? B LYS 69  
170 1 Y 1 B THR 70  ? B THR 70  
171 1 Y 1 B ALA 71  ? B ALA 71  
172 1 Y 1 B GLN 72  ? B GLN 72  
173 1 Y 1 B LEU 73  ? B LEU 73  
174 1 Y 1 B LEU 74  ? B LEU 74  
175 1 Y 1 B ILE 75  ? B ILE 75  
176 1 Y 1 B GLU 76  ? B GLU 76  
177 1 Y 1 B MET 77  ? B MET 77  
178 1 Y 1 B ASN 78  ? B ASN 78  
179 1 Y 1 B GLN 79  ? B GLN 79  
180 1 Y 1 B TRP 80  ? B TRP 80  
181 1 Y 1 B LYS 81  ? B LYS 81  
182 1 Y 1 B GLN 82  ? B GLN 82  
183 1 Y 1 B HIS 83  ? B HIS 83  
184 1 Y 1 B ALA 84  ? B ALA 84  
185 1 Y 1 B HIS 85  ? B HIS 85  
186 1 Y 1 B ALA 86  ? B ALA 86  
187 1 Y 1 B LEU 87  ? B LEU 87  
188 1 Y 1 B SER 88  ? B SER 88  
189 1 Y 1 B THR 89  ? B THR 89  
190 1 Y 1 B GLY 90  ? B GLY 90  
191 1 Y 1 B LEU 91  ? B LEU 91  
192 1 Y 1 B GLU 92  ? B GLU 92  
193 1 Y 1 B ARG 151 ? B ARG 151 
194 1 Y 1 B GLU 152 ? B GLU 152 
195 1 Y 1 B HIS 153 ? B HIS 153 
196 1 Y 1 B ARG 200 ? B ARG 200 
197 1 Y 1 B ASP 201 ? B ASP 201 
198 1 Y 1 B GLU 202 ? B GLU 202 
199 1 Y 1 B GLN 294 ? B GLN 294 
200 1 Y 1 B PRO 295 ? B PRO 295 
201 1 Y 1 B ALA 296 ? B ALA 296 
202 1 Y 1 B PRO 297 ? B PRO 297 
# 
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 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TRP N    N N N 321 
TRP CA   C N S 322 
TRP C    C N N 323 
TRP O    O N N 324 
TRP CB   C N N 325 
TRP CG   C Y N 326 
TRP CD1  C Y N 327 
TRP CD2  C Y N 328 
TRP NE1  N Y N 329 
TRP CE2  C Y N 330 
TRP CE3  C Y N 331 
TRP CZ2  C Y N 332 
TRP CZ3  C Y N 333 
TRP CH2  C Y N 334 
TRP OXT  O N N 335 
TRP H    H N N 336 
TRP H2   H N N 337 
TRP HA   H N N 338 
TRP HB2  H N N 339 
TRP HB3  H N N 340 
TRP HD1  H N N 341 
TRP HE1  H N N 342 
TRP HE3  H N N 343 
TRP HZ2  H N N 344 
TRP HZ3  H N N 345 
TRP HH2  H N N 346 
TRP HXT  H N N 347 
TYR N    N N N 348 
TYR CA   C N S 349 
TYR C    C N N 350 
TYR O    O N N 351 
TYR CB   C N N 352 
TYR CG   C Y N 353 
TYR CD1  C Y N 354 
TYR CD2  C Y N 355 
TYR CE1  C Y N 356 
TYR CE2  C Y N 357 
TYR CZ   C Y N 358 
TYR OH   O N N 359 
TYR OXT  O N N 360 
TYR H    H N N 361 
TYR H2   H N N 362 
TYR HA   H N N 363 
TYR HB2  H N N 364 
TYR HB3  H N N 365 
TYR HD1  H N N 366 
TYR HD2  H N N 367 
TYR HE1  H N N 368 
TYR HE2  H N N 369 
TYR HH   H N N 370 
TYR HXT  H N N 371 
VAL N    N N N 372 
VAL CA   C N S 373 
VAL C    C N N 374 
VAL O    O N N 375 
VAL CB   C N N 376 
VAL CG1  C N N 377 
VAL CG2  C N N 378 
VAL OXT  O N N 379 
VAL H    H N N 380 
VAL H2   H N N 381 
VAL HA   H N N 382 
VAL HB   H N N 383 
VAL HG11 H N N 384 
VAL HG12 H N N 385 
VAL HG13 H N N 386 
VAL HG21 H N N 387 
VAL HG22 H N N 388 
VAL HG23 H N N 389 
VAL HXT  H N N 390 
# 
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 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TRP N   CA   sing N N 306 
TRP N   H    sing N N 307 
TRP N   H2   sing N N 308 
TRP CA  C    sing N N 309 
TRP CA  CB   sing N N 310 
TRP CA  HA   sing N N 311 
TRP C   O    doub N N 312 
TRP C   OXT  sing N N 313 
TRP CB  CG   sing N N 314 
TRP CB  HB2  sing N N 315 
TRP CB  HB3  sing N N 316 
TRP CG  CD1  doub Y N 317 
TRP CG  CD2  sing Y N 318 
TRP CD1 NE1  sing Y N 319 
TRP CD1 HD1  sing N N 320 
TRP CD2 CE2  doub Y N 321 
TRP CD2 CE3  sing Y N 322 
TRP NE1 CE2  sing Y N 323 
TRP NE1 HE1  sing N N 324 
TRP CE2 CZ2  sing Y N 325 
TRP CE3 CZ3  doub Y N 326 
TRP CE3 HE3  sing N N 327 
TRP CZ2 CH2  doub Y N 328 
TRP CZ2 HZ2  sing N N 329 
TRP CZ3 CH2  sing Y N 330 
TRP CZ3 HZ3  sing N N 331 
TRP CH2 HH2  sing N N 332 
TRP OXT HXT  sing N N 333 
TYR N   CA   sing N N 334 
TYR N   H    sing N N 335 
TYR N   H2   sing N N 336 
TYR CA  C    sing N N 337 
TYR CA  CB   sing N N 338 
TYR CA  HA   sing N N 339 
TYR C   O    doub N N 340 
TYR C   OXT  sing N N 341 
TYR CB  CG   sing N N 342 
TYR CB  HB2  sing N N 343 
TYR CB  HB3  sing N N 344 
TYR CG  CD1  doub Y N 345 
TYR CG  CD2  sing Y N 346 
TYR CD1 CE1  sing Y N 347 
TYR CD1 HD1  sing N N 348 
TYR CD2 CE2  doub Y N 349 
TYR CD2 HD2  sing N N 350 
TYR CE1 CZ   doub Y N 351 
TYR CE1 HE1  sing N N 352 
TYR CE2 CZ   sing Y N 353 
TYR CE2 HE2  sing N N 354 
TYR CZ  OH   sing N N 355 
TYR OH  HH   sing N N 356 
TYR OXT HXT  sing N N 357 
VAL N   CA   sing N N 358 
VAL N   H    sing N N 359 
VAL N   H2   sing N N 360 
VAL CA  C    sing N N 361 
VAL CA  CB   sing N N 362 
VAL CA  HA   sing N N 363 
VAL C   O    doub N N 364 
VAL C   OXT  sing N N 365 
VAL CB  CG1  sing N N 366 
VAL CB  CG2  sing N N 367 
VAL CB  HB   sing N N 368 
VAL CG1 HG11 sing N N 369 
VAL CG1 HG12 sing N N 370 
VAL CG1 HG13 sing N N 371 
VAL CG2 HG21 sing N N 372 
VAL CG2 HG22 sing N N 373 
VAL CG2 HG23 sing N N 374 
VAL OXT HXT  sing N N 375 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           32071215 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8J4N 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.012900 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.009880 
_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]   0.017250 
_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 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . LEU A 1 91  ? -31.809 38.200 -25.211 1.00 68.49  ? 91  LEU A N   1 
ATOM   2    C CA  . LEU A 1 91  ? -30.786 39.205 -25.472 1.00 72.11  ? 91  LEU A CA  1 
ATOM   3    C C   . LEU A 1 91  ? -29.918 39.336 -24.225 1.00 74.57  ? 91  LEU A C   1 
ATOM   4    O O   . LEU A 1 91  ? -30.427 39.722 -23.171 1.00 85.60  ? 91  LEU A O   1 
ATOM   5    C CB  . LEU A 1 91  ? -31.420 40.551 -25.844 1.00 70.80  ? 91  LEU A CB  1 
ATOM   6    C CG  . LEU A 1 91  ? -32.099 40.684 -27.210 1.00 70.94  ? 91  LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 91  ? -33.462 40.002 -27.218 1.00 69.70  ? 91  LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 91  ? -32.224 42.144 -27.620 1.00 71.31  ? 91  LEU A CD2 1 
ATOM   9    N N   . GLU A 1 92  ? -28.614 39.015 -24.371 1.00 67.09  ? 92  GLU A N   1 
ATOM   10   C CA  . GLU A 1 92  ? -27.629 38.795 -23.309 1.00 69.47  ? 92  GLU A CA  1 
ATOM   11   C C   . GLU A 1 92  ? -27.772 37.368 -22.786 1.00 64.06  ? 92  GLU A C   1 
ATOM   12   O O   . GLU A 1 92  ? -28.734 37.060 -22.067 1.00 60.71  ? 92  GLU A O   1 
ATOM   13   C CB  . GLU A 1 92  ? -27.777 39.825 -22.181 1.00 73.28  ? 92  GLU A CB  1 
ATOM   14   C CG  . GLU A 1 92  ? -27.032 39.540 -20.881 1.00 80.09  ? 92  GLU A CG  1 
ATOM   15   C CD  . GLU A 1 92  ? -25.515 39.545 -20.990 1.00 82.89  ? 92  GLU A CD  1 
ATOM   16   O OE1 . GLU A 1 92  ? -24.956 39.592 -22.105 1.00 83.68  ? 92  GLU A OE1 1 
ATOM   17   O OE2 . GLU A 1 92  ? -24.868 39.496 -19.927 1.00 75.83  ? 92  GLU A OE2 1 
ATOM   18   N N   . PRO A 1 93  ? -26.846 36.468 -23.127 1.00 56.05  ? 93  PRO A N   1 
ATOM   19   C CA  . PRO A 1 93  ? -27.008 35.060 -22.742 1.00 53.43  ? 93  PRO A CA  1 
ATOM   20   C C   . PRO A 1 93  ? -26.721 34.828 -21.266 1.00 45.56  ? 93  PRO A C   1 
ATOM   21   O O   . PRO A 1 93  ? -25.814 35.426 -20.681 1.00 48.15  ? 93  PRO A O   1 
ATOM   22   C CB  . PRO A 1 93  ? -26.000 34.326 -23.633 1.00 48.45  ? 93  PRO A CB  1 
ATOM   23   C CG  . PRO A 1 93  ? -24.981 35.339 -24.004 1.00 54.67  ? 93  PRO A CG  1 
ATOM   24   C CD  . PRO A 1 93  ? -25.589 36.714 -23.860 1.00 58.01  ? 93  PRO A CD  1 
ATOM   25   N N   . ASN A 1 94  ? -27.506 33.933 -20.675 1.00 38.90  ? 94  ASN A N   1 
ATOM   26   C CA  . ASN A 1 94  ? -27.474 33.674 -19.247 1.00 41.00  ? 94  ASN A CA  1 
ATOM   27   C C   . ASN A 1 94  ? -27.366 32.179 -18.989 1.00 42.17  ? 94  ASN A C   1 
ATOM   28   O O   . ASN A 1 94  ? -27.894 31.367 -19.754 1.00 51.55  ? 94  ASN A O   1 
ATOM   29   C CB  . ASN A 1 94  ? -28.730 34.223 -18.569 1.00 39.03  ? 94  ASN A CB  1 
ATOM   30   C CG  . ASN A 1 94  ? -28.839 33.792 -17.121 1.00 58.39  ? 94  ASN A CG  1 
ATOM   31   O OD1 . ASN A 1 94  ? -28.167 34.334 -16.243 1.00 60.07  ? 94  ASN A OD1 1 
ATOM   32   N ND2 . ASN A 1 94  ? -29.670 32.794 -16.869 1.00 50.18  ? 94  ASN A ND2 1 
ATOM   33   N N   . LEU A 1 95  ? -26.666 31.828 -17.912 1.00 40.53  ? 95  LEU A N   1 
ATOM   34   C CA  . LEU A 1 95  ? -26.601 30.458 -17.423 1.00 35.42  ? 95  LEU A CA  1 
ATOM   35   C C   . LEU A 1 95  ? -26.651 30.510 -15.906 1.00 39.85  ? 95  LEU A C   1 
ATOM   36   O O   . LEU A 1 95  ? -25.758 31.084 -15.278 1.00 35.89  ? 95  LEU A O   1 
ATOM   37   C CB  . LEU A 1 95  ? -25.329 29.754 -17.900 1.00 29.01  ? 95  LEU A CB  1 
ATOM   38   C CG  . LEU A 1 95  ? -25.039 28.390 -17.266 1.00 34.78  ? 95  LEU A CG  1 
ATOM   39   C CD1 . LEU A 1 95  ? -26.203 27.433 -17.445 1.00 36.12  ? 95  LEU A CD1 1 
ATOM   40   C CD2 . LEU A 1 95  ? -23.796 27.803 -17.877 1.00 31.10  ? 95  LEU A CD2 1 
ATOM   41   N N   . THR A 1 96  ? -27.701 29.937 -15.325 1.00 34.60  ? 96  THR A N   1 
ATOM   42   C CA  . THR A 1 96  ? -27.860 29.876 -13.878 1.00 31.11  ? 96  THR A CA  1 
ATOM   43   C C   . THR A 1 96  ? -27.622 28.452 -13.398 1.00 28.76  ? 96  THR A C   1 
ATOM   44   O O   . THR A 1 96  ? -28.264 27.510 -13.878 1.00 30.02  ? 96  THR A O   1 
ATOM   45   C CB  . THR A 1 96  ? -29.248 30.352 -13.441 1.00 35.94  ? 96  THR A CB  1 
ATOM   46   O OG1 . THR A 1 96  ? -29.417 31.728 -13.802 1.00 39.80  ? 96  THR A OG1 1 
ATOM   47   C CG2 . THR A 1 96  ? -29.412 30.210 -11.925 1.00 34.51  ? 96  THR A CG2 1 
ATOM   48   N N   . ILE A 1 97  ? -26.708 28.311 -12.442 1.00 34.93  ? 97  ILE A N   1 
ATOM   49   C CA  . ILE A 1 97  ? -26.338 27.031 -11.855 1.00 27.67  ? 97  ILE A CA  1 
ATOM   50   C C   . ILE A 1 97  ? -26.681 27.088 -10.374 1.00 33.85  ? 97  ILE A C   1 
ATOM   51   O O   . ILE A 1 97  ? -26.267 28.021 -9.678  1.00 31.02  ? 97  ILE A O   1 
ATOM   52   C CB  . ILE A 1 97  ? -24.840 26.746 -12.053 1.00 28.60  ? 97  ILE A CB  1 
ATOM   53   C CG1 . ILE A 1 97  ? -24.481 26.786 -13.540 1.00 31.71  ? 97  ILE A CG1 1 
ATOM   54   C CG2 . ILE A 1 97  ? -24.459 25.415 -11.422 1.00 30.46  ? 97  ILE A CG2 1 
ATOM   55   C CD1 . ILE A 1 97  ? -23.005 26.599 -13.815 1.00 31.67  ? 97  ILE A CD1 1 
ATOM   56   N N   . VAL A 1 98  ? -27.438 26.102 -9.896  1.00 26.32  ? 98  VAL A N   1 
ATOM   57   C CA  . VAL A 1 98  ? -27.789 26.028 -8.481  1.00 34.23  ? 98  VAL A CA  1 
ATOM   58   C C   . VAL A 1 98  ? -26.925 24.964 -7.816  1.00 26.42  ? 98  VAL A C   1 
ATOM   59   O O   . VAL A 1 98  ? -26.952 23.791 -8.202  1.00 33.85  ? 98  VAL A O   1 
ATOM   60   C CB  . VAL A 1 98  ? -29.289 25.752 -8.270  1.00 34.98  ? 98  VAL A CB  1 
ATOM   61   C CG1 . VAL A 1 98  ? -29.752 24.527 -9.044  1.00 27.20  ? 98  VAL A CG1 1 
ATOM   62   C CG2 . VAL A 1 98  ? -29.597 25.594 -6.786  1.00 30.21  ? 98  VAL A CG2 1 
ATOM   63   N N   . VAL A 1 99  ? -26.136 25.382 -6.833  1.00 26.45  ? 99  VAL A N   1 
ATOM   64   C CA  . VAL A 1 99  ? -25.336 24.480 -6.017  1.00 28.46  ? 99  VAL A CA  1 
ATOM   65   C C   . VAL A 1 99  ? -26.109 24.230 -4.733  1.00 30.99  ? 99  VAL A C   1 
ATOM   66   O O   . VAL A 1 99  ? -26.434 25.176 -4.008  1.00 35.50  ? 99  VAL A O   1 
ATOM   67   C CB  . VAL A 1 99  ? -23.952 25.076 -5.719  1.00 30.03  ? 99  VAL A CB  1 
ATOM   68   C CG1 . VAL A 1 99  ? -23.113 24.090 -4.920  1.00 32.61  ? 99  VAL A CG1 1 
ATOM   69   C CG2 . VAL A 1 99  ? -23.252 25.478 -7.009  1.00 33.40  ? 99  VAL A CG2 1 
ATOM   70   N N   . VAL A 1 100 ? -26.426 22.965 -4.451  1.00 30.15  ? 100 VAL A N   1 
ATOM   71   C CA  . VAL A 1 100 ? -27.170 22.676 -3.237  1.00 30.90  ? 100 VAL A CA  1 
ATOM   72   C C   . VAL A 1 100 ? -26.333 23.072 -2.027  1.00 32.32  ? 100 VAL A C   1 
ATOM   73   O O   . VAL A 1 100 ? -25.098 23.077 -2.063  1.00 31.25  ? 100 VAL A O   1 
ATOM   74   C CB  . VAL A 1 100 ? -27.597 21.201 -3.164  1.00 33.00  ? 100 VAL A CB  1 
ATOM   75   C CG1 . VAL A 1 100 ? -28.404 20.834 -4.400  1.00 33.25  ? 100 VAL A CG1 1 
ATOM   76   C CG2 . VAL A 1 100 ? -26.387 20.296 -3.013  1.00 31.45  ? 100 VAL A CG2 1 
ATOM   77   N N   . SER A 1 101 ? -27.023 23.420 -0.944  1.00 39.22  ? 101 SER A N   1 
ATOM   78   C CA  . SER A 1 101 ? -26.370 24.033 0.209   1.00 36.13  ? 101 SER A CA  1 
ATOM   79   C C   . SER A 1 101 ? -25.196 23.199 0.707   1.00 33.27  ? 101 SER A C   1 
ATOM   80   O O   . SER A 1 101 ? -24.117 23.731 0.990   1.00 35.57  ? 101 SER A O   1 
ATOM   81   C CB  . SER A 1 101 ? -27.396 24.245 1.324   1.00 36.77  ? 101 SER A CB  1 
ATOM   82   O OG  . SER A 1 101 ? -28.621 24.719 0.797   1.00 43.94  ? 101 SER A OG  1 
ATOM   83   N N   . GLU A 1 102 ? -25.379 21.881 0.792   1.00 35.16  ? 102 GLU A N   1 
ATOM   84   C CA  . GLU A 1 102 ? -24.335 21.018 1.335   1.00 35.07  ? 102 GLU A CA  1 
ATOM   85   C C   . GLU A 1 102 ? -23.054 21.044 0.507   1.00 35.31  ? 102 GLU A C   1 
ATOM   86   O O   . GLU A 1 102 ? -21.984 20.718 1.033   1.00 35.76  ? 102 GLU A O   1 
ATOM   87   C CB  . GLU A 1 102 ? -24.841 19.575 1.449   1.00 30.57  ? 102 GLU A CB  1 
ATOM   88   C CG  . GLU A 1 102 ? -25.896 19.341 2.529   1.00 47.32  ? 102 GLU A CG  1 
ATOM   89   C CD  . GLU A 1 102 ? -27.315 19.520 2.026   1.00 42.76  ? 102 GLU A CD  1 
ATOM   90   O OE1 . GLU A 1 102 ? -27.522 20.298 1.073   1.00 38.40  ? 102 GLU A OE1 1 
ATOM   91   O OE2 . GLU A 1 102 ? -28.230 18.874 2.578   1.00 51.71  ? 102 GLU A OE2 1 
ATOM   92   N N   . LEU A 1 103 ? -23.128 21.434 -0.765  1.00 32.31  ? 103 LEU A N   1 
ATOM   93   C CA  . LEU A 1 103 ? -21.969 21.426 -1.648  1.00 32.74  ? 103 LEU A CA  1 
ATOM   94   C C   . LEU A 1 103 ? -21.337 22.801 -1.817  1.00 29.64  ? 103 LEU A C   1 
ATOM   95   O O   . LEU A 1 103 ? -20.407 22.946 -2.615  1.00 29.80  ? 103 LEU A O   1 
ATOM   96   C CB  . LEU A 1 103 ? -22.364 20.872 -3.021  1.00 30.17  ? 103 LEU A CB  1 
ATOM   97   C CG  . LEU A 1 103 ? -22.885 19.431 -3.024  1.00 35.32  ? 103 LEU A CG  1 
ATOM   98   C CD1 . LEU A 1 103 ? -23.113 18.920 -4.441  1.00 34.71  ? 103 LEU A CD1 1 
ATOM   99   C CD2 . LEU A 1 103 ? -21.955 18.496 -2.261  1.00 31.34  ? 103 LEU A CD2 1 
ATOM   100  N N   . LEU A 1 104 ? -21.813 23.812 -1.086  1.00 34.42  ? 104 LEU A N   1 
ATOM   101  C CA  . LEU A 1 104 ? -21.329 25.176 -1.292  1.00 34.99  ? 104 LEU A CA  1 
ATOM   102  C C   . LEU A 1 104 ? -19.833 25.296 -1.016  1.00 36.92  ? 104 LEU A C   1 
ATOM   103  O O   . LEU A 1 104 ? -19.118 25.999 -1.740  1.00 33.26  ? 104 LEU A O   1 
ATOM   104  C CB  . LEU A 1 104 ? -22.122 26.146 -0.413  1.00 41.35  ? 104 LEU A CB  1 
ATOM   105  C CG  . LEU A 1 104 ? -22.340 27.559 -0.953  1.00 47.33  ? 104 LEU A CG  1 
ATOM   106  C CD1 . LEU A 1 104 ? -23.000 27.521 -2.322  1.00 50.24  ? 104 LEU A CD1 1 
ATOM   107  C CD2 . LEU A 1 104 ? -23.185 28.371 0.019   1.00 52.31  ? 104 LEU A CD2 1 
ATOM   108  N N   . HIS A 1 105 ? -19.341 24.619 0.024   1.00 30.53  ? 105 HIS A N   1 
ATOM   109  C CA  . HIS A 1 105 ? -17.943 24.711 0.430   1.00 35.15  ? 105 HIS A CA  1 
ATOM   110  C C   . HIS A 1 105 ? -17.122 23.521 -0.055  1.00 35.87  ? 105 HIS A C   1 
ATOM   111  O O   . HIS A 1 105 ? -16.187 23.079 0.624   1.00 43.85  ? 105 HIS A O   1 
ATOM   112  C CB  . HIS A 1 105 ? -17.859 24.878 1.945   1.00 27.13  ? 105 HIS A CB  1 
ATOM   113  C CG  . HIS A 1 105 ? -18.480 26.153 2.431   1.00 29.83  ? 105 HIS A CG  1 
ATOM   114  N ND1 . HIS A 1 105 ? -17.747 27.294 2.677   1.00 38.23  ? 105 HIS A ND1 1 
ATOM   115  C CD2 . HIS A 1 105 ? -19.773 26.477 2.676   1.00 36.64  ? 105 HIS A CD2 1 
ATOM   116  C CE1 . HIS A 1 105 ? -18.557 28.259 3.074   1.00 35.67  ? 105 HIS A CE1 1 
ATOM   117  N NE2 . HIS A 1 105 ? -19.792 27.790 3.081   1.00 36.87  ? 105 HIS A NE2 1 
ATOM   118  N N   . THR A 1 106 ? -17.483 22.986 -1.214  1.00 32.64  ? 106 THR A N   1 
ATOM   119  C CA  . THR A 1 106 ? -16.667 22.085 -2.009  1.00 41.74  ? 106 THR A CA  1 
ATOM   120  C C   . THR A 1 106 ? -16.143 22.854 -3.215  1.00 46.84  ? 106 THR A C   1 
ATOM   121  O O   . THR A 1 106 ? -16.470 24.025 -3.418  1.00 48.88  ? 106 THR A O   1 
ATOM   122  C CB  . THR A 1 106 ? -17.478 20.861 -2.449  1.00 39.74  ? 106 THR A CB  1 
ATOM   123  O OG1 . THR A 1 106 ? -18.468 21.259 -3.406  1.00 41.69  ? 106 THR A OG1 1 
ATOM   124  C CG2 . THR A 1 106 ? -18.171 20.219 -1.252  1.00 34.11  ? 106 THR A CG2 1 
ATOM   125  N N   . ASN A 1 107 ? -15.329 22.187 -4.028  1.00 46.34  ? 107 ASN A N   1 
ATOM   126  C CA  . ASN A 1 107 ? -14.682 22.845 -5.164  1.00 45.77  ? 107 ASN A CA  1 
ATOM   127  C C   . ASN A 1 107 ? -15.551 22.671 -6.403  1.00 47.67  ? 107 ASN A C   1 
ATOM   128  O O   . ASN A 1 107 ? -15.525 21.626 -7.055  1.00 55.31  ? 107 ASN A O   1 
ATOM   129  C CB  . ASN A 1 107 ? -13.276 22.296 -5.381  1.00 58.23  ? 107 ASN A CB  1 
ATOM   130  C CG  . ASN A 1 107 ? -12.493 23.085 -6.428  1.00 59.27  ? 107 ASN A CG  1 
ATOM   131  O OD1 . ASN A 1 107 ? -12.867 23.133 -7.600  1.00 62.09  ? 107 ASN A OD1 1 
ATOM   132  N ND2 . ASN A 1 107 ? -11.413 23.726 -5.999  1.00 61.53  ? 107 ASN A ND2 1 
ATOM   133  N N   . TRP A 1 108 ? -16.322 23.710 -6.728  1.00 44.35  ? 108 TRP A N   1 
ATOM   134  C CA  . TRP A 1 108 ? -17.104 23.774 -7.954  1.00 44.41  ? 108 TRP A CA  1 
ATOM   135  C C   . TRP A 1 108 ? -16.604 24.850 -8.904  1.00 33.57  ? 108 TRP A C   1 
ATOM   136  O O   . TRP A 1 108 ? -17.163 25.009 -9.994  1.00 47.90  ? 108 TRP A O   1 
ATOM   137  C CB  . TRP A 1 108 ? -18.581 24.025 -7.623  1.00 46.09  ? 108 TRP A CB  1 
ATOM   138  C CG  . TRP A 1 108 ? -18.785 25.123 -6.625  1.00 40.30  ? 108 TRP A CG  1 
ATOM   139  C CD1 . TRP A 1 108 ? -19.004 24.974 -5.287  1.00 40.07  ? 108 TRP A CD1 1 
ATOM   140  C CD2 . TRP A 1 108 ? -18.811 26.534 -6.880  1.00 34.10  ? 108 TRP A CD2 1 
ATOM   141  N NE1 . TRP A 1 108 ? -19.145 26.200 -4.690  1.00 32.01  ? 108 TRP A NE1 1 
ATOM   142  C CE2 . TRP A 1 108 ? -19.035 27.176 -5.646  1.00 36.98  ? 108 TRP A CE2 1 
ATOM   143  C CE3 . TRP A 1 108 ? -18.662 27.318 -8.029  1.00 41.21  ? 108 TRP A CE3 1 
ATOM   144  C CZ2 . TRP A 1 108 ? -19.113 28.561 -5.526  1.00 33.20  ? 108 TRP A CZ2 1 
ATOM   145  C CZ3 . TRP A 1 108 ? -18.739 28.692 -7.910  1.00 41.40  ? 108 TRP A CZ3 1 
ATOM   146  C CH2 . TRP A 1 108 ? -18.962 29.301 -6.668  1.00 44.22  ? 108 TRP A CH2 1 
ATOM   147  N N   . THR A 1 109 ? -15.553 25.574 -8.529  1.00 41.00  ? 109 THR A N   1 
ATOM   148  C CA  . THR A 1 109 ? -15.147 26.770 -9.253  1.00 42.29  ? 109 THR A CA  1 
ATOM   149  C C   . THR A 1 109 ? -14.378 26.467 -10.536 1.00 42.57  ? 109 THR A C   1 
ATOM   150  O O   . THR A 1 109 ? -14.302 27.336 -11.411 1.00 43.81  ? 109 THR A O   1 
ATOM   151  C CB  . THR A 1 109 ? -14.333 27.668 -8.314  1.00 42.94  ? 109 THR A CB  1 
ATOM   152  O OG1 . THR A 1 109 ? -14.552 29.047 -8.645  1.00 53.94  ? 109 THR A OG1 1 
ATOM   153  C CG2 . THR A 1 109 ? -12.853 27.316 -8.335  1.00 43.87  ? 109 THR A CG2 1 
ATOM   154  N N   . ASP A 1 110 ? -13.826 25.260 -10.683 1.00 37.01  ? 110 ASP A N   1 
ATOM   155  C CA  . ASP A 1 110 ? -13.133 24.917 -11.923 1.00 46.26  ? 110 ASP A CA  1 
ATOM   156  C C   . ASP A 1 110 ? -14.090 24.854 -13.102 1.00 40.07  ? 110 ASP A C   1 
ATOM   157  O O   . ASP A 1 110 ? -13.710 25.185 -14.231 1.00 41.40  ? 110 ASP A O   1 
ATOM   158  C CB  . ASP A 1 110 ? -12.405 23.582 -11.774 1.00 51.44  ? 110 ASP A CB  1 
ATOM   159  C CG  . ASP A 1 110 ? -11.231 23.663 -10.826 1.00 59.56  ? 110 ASP A CG  1 
ATOM   160  O OD1 . ASP A 1 110 ? -10.618 24.746 -10.729 1.00 66.40  ? 110 ASP A OD1 1 
ATOM   161  O OD2 . ASP A 1 110 ? -10.921 22.644 -10.175 1.00 63.67  ? 110 ASP A OD2 1 
ATOM   162  N N   . TYR A 1 111 ? -15.328 24.422 -12.862 1.00 37.30  ? 111 TYR A N   1 
ATOM   163  C CA  . TYR A 1 111 ? -16.304 24.344 -13.942 1.00 36.97  ? 111 TYR A CA  1 
ATOM   164  C C   . TYR A 1 111 ? -16.721 25.733 -14.401 1.00 38.71  ? 111 TYR A C   1 
ATOM   165  O O   . TYR A 1 111 ? -17.019 25.939 -15.584 1.00 36.50  ? 111 TYR A O   1 
ATOM   166  C CB  . TYR A 1 111 ? -17.515 23.533 -13.485 1.00 37.65  ? 111 TYR A CB  1 
ATOM   167  C CG  . TYR A 1 111 ? -17.145 22.193 -12.892 1.00 44.38  ? 111 TYR A CG  1 
ATOM   168  C CD1 . TYR A 1 111 ? -16.490 21.232 -13.652 1.00 47.90  ? 111 TYR A CD1 1 
ATOM   169  C CD2 . TYR A 1 111 ? -17.452 21.888 -11.572 1.00 50.35  ? 111 TYR A CD2 1 
ATOM   170  C CE1 . TYR A 1 111 ? -16.148 20.005 -13.112 1.00 50.29  ? 111 TYR A CE1 1 
ATOM   171  C CE2 . TYR A 1 111 ? -17.111 20.666 -11.023 1.00 52.44  ? 111 TYR A CE2 1 
ATOM   172  C CZ  . TYR A 1 111 ? -16.461 19.728 -11.798 1.00 53.34  ? 111 TYR A CZ  1 
ATOM   173  O OH  . TYR A 1 111 ? -16.122 18.510 -11.256 1.00 64.66  ? 111 TYR A OH  1 
ATOM   174  N N   . VAL A 1 112 ? -16.737 26.699 -13.481 1.00 32.24  ? 112 VAL A N   1 
ATOM   175  C CA  . VAL A 1 112 ? -17.077 28.070 -13.845 1.00 31.68  ? 112 VAL A CA  1 
ATOM   176  C C   . VAL A 1 112 ? -15.971 28.687 -14.694 1.00 35.33  ? 112 VAL A C   1 
ATOM   177  O O   . VAL A 1 112 ? -16.236 29.329 -15.715 1.00 37.94  ? 112 VAL A O   1 
ATOM   178  C CB  . VAL A 1 112 ? -17.357 28.903 -12.582 1.00 42.63  ? 112 VAL A CB  1 
ATOM   179  C CG1 . VAL A 1 112 ? -17.644 30.349 -12.949 1.00 33.95  ? 112 VAL A CG1 1 
ATOM   180  C CG2 . VAL A 1 112 ? -18.526 28.307 -11.813 1.00 39.00  ? 112 VAL A CG2 1 
ATOM   181  N N   . CYS A 1 113 ? -14.712 28.498 -14.286 1.00 37.09  ? 113 CYS A N   1 
ATOM   182  C CA  . CYS A 1 113 ? -13.594 29.026 -15.066 1.00 30.26  ? 113 CYS A CA  1 
ATOM   183  C C   . CYS A 1 113 ? -13.542 28.398 -16.455 1.00 39.51  ? 113 CYS A C   1 
ATOM   184  O O   . CYS A 1 113 ? -13.211 29.070 -17.440 1.00 40.69  ? 113 CYS A O   1 
ATOM   185  C CB  . CYS A 1 113 ? -12.278 28.794 -14.322 1.00 37.68  ? 113 CYS A CB  1 
ATOM   186  S SG  . CYS A 1 113 ? -12.153 29.669 -12.744 1.00 45.96  ? 113 CYS A SG  1 
ATOM   187  N N   . LEU A 1 114 ? -13.865 27.107 -16.554 1.00 33.27  ? 114 LEU A N   1 
ATOM   188  C CA  . LEU A 1 114 ? -13.924 26.448 -17.856 1.00 34.22  ? 114 LEU A CA  1 
ATOM   189  C C   . LEU A 1 114 ? -14.979 27.092 -18.747 1.00 39.12  ? 114 LEU A C   1 
ATOM   190  O O   . LEU A 1 114 ? -14.737 27.355 -19.932 1.00 39.33  ? 114 LEU A O   1 
ATOM   191  C CB  . LEU A 1 114 ? -14.218 24.959 -17.671 1.00 36.55  ? 114 LEU A CB  1 
ATOM   192  C CG  . LEU A 1 114 ? -14.399 24.132 -18.946 1.00 45.06  ? 114 LEU A CG  1 
ATOM   193  C CD1 . LEU A 1 114 ? -13.104 24.100 -19.751 1.00 42.21  ? 114 LEU A CD1 1 
ATOM   194  C CD2 . LEU A 1 114 ? -14.877 22.727 -18.610 1.00 37.66  ? 114 LEU A CD2 1 
ATOM   195  N N   . LEU A 1 115 ? -16.160 27.356 -18.184 1.00 35.75  ? 115 LEU A N   1 
ATOM   196  C CA  . LEU A 1 115 ? -17.235 27.971 -18.954 1.00 34.95  ? 115 LEU A CA  1 
ATOM   197  C C   . LEU A 1 115 ? -16.891 29.403 -19.340 1.00 40.86  ? 115 LEU A C   1 
ATOM   198  O O   . LEU A 1 115 ? -17.185 29.839 -20.460 1.00 40.34  ? 115 LEU A O   1 
ATOM   199  C CB  . LEU A 1 115 ? -18.532 27.930 -18.150 1.00 35.81  ? 115 LEU A CB  1 
ATOM   200  C CG  . LEU A 1 115 ? -19.231 26.570 -18.095 1.00 36.60  ? 115 LEU A CG  1 
ATOM   201  C CD1 . LEU A 1 115 ? -20.494 26.659 -17.277 1.00 39.36  ? 115 LEU A CD1 1 
ATOM   202  C CD2 . LEU A 1 115 ? -19.549 26.061 -19.491 1.00 39.06  ? 115 LEU A CD2 1 
ATOM   203  N N   . GLU A 1 116 ? -16.265 30.150 -18.428 1.00 34.77  ? 116 GLU A N   1 
ATOM   204  C CA  . GLU A 1 116 ? -15.955 31.550 -18.704 1.00 35.29  ? 116 GLU A CA  1 
ATOM   205  C C   . GLU A 1 116 ? -14.920 31.685 -19.813 1.00 43.16  ? 116 GLU A C   1 
ATOM   206  O O   . GLU A 1 116 ? -15.048 32.549 -20.688 1.00 45.00  ? 116 GLU A O   1 
ATOM   207  C CB  . GLU A 1 116 ? -15.468 32.243 -17.430 1.00 43.05  ? 116 GLU A CB  1 
ATOM   208  C CG  . GLU A 1 116 ? -15.364 33.761 -17.542 1.00 43.13  ? 116 GLU A CG  1 
ATOM   209  C CD  . GLU A 1 116 ? -14.037 34.225 -18.116 1.00 47.82  ? 116 GLU A CD  1 
ATOM   210  O OE1 . GLU A 1 116 ? -13.073 33.432 -18.112 1.00 47.06  ? 116 GLU A OE1 1 
ATOM   211  O OE2 . GLU A 1 116 ? -13.955 35.385 -18.571 1.00 55.69  ? 116 GLU A OE2 1 
ATOM   212  N N   . SER A 1 117 ? -13.885 30.845 -19.791 1.00 42.33  ? 117 SER A N   1 
ATOM   213  C CA  . SER A 1 117 ? -12.840 30.929 -20.808 1.00 49.34  ? 117 SER A CA  1 
ATOM   214  C C   . SER A 1 117 ? -13.355 30.536 -22.188 1.00 40.50  ? 117 SER A C   1 
ATOM   215  O O   . SER A 1 117 ? -12.828 31.006 -23.203 1.00 52.17  ? 117 SER A O   1 
ATOM   216  C CB  . SER A 1 117 ? -11.659 30.042 -20.416 1.00 41.69  ? 117 SER A CB  1 
ATOM   217  O OG  . SER A 1 117 ? -12.032 28.674 -20.437 1.00 51.11  ? 117 SER A OG  1 
ATOM   218  N N   . ARG A 1 118 ? -14.368 29.675 -22.246 1.00 39.99  ? 118 ARG A N   1 
ATOM   219  C CA  . ARG A 1 118 ? -14.947 29.233 -23.509 1.00 43.82  ? 118 ARG A CA  1 
ATOM   220  C C   . ARG A 1 118 ? -16.074 30.145 -23.980 1.00 49.16  ? 118 ARG A C   1 
ATOM   221  O O   . ARG A 1 118 ? -16.256 30.323 -25.190 1.00 47.87  ? 118 ARG A O   1 
ATOM   222  C CB  . ARG A 1 118 ? -15.466 27.798 -23.360 1.00 46.38  ? 118 ARG A CB  1 
ATOM   223  C CG  . ARG A 1 118 ? -16.193 27.211 -24.564 1.00 57.35  ? 118 ARG A CG  1 
ATOM   224  C CD  . ARG A 1 118 ? -15.278 26.858 -25.731 1.00 63.55  ? 118 ARG A CD  1 
ATOM   225  N NE  . ARG A 1 118 ? -16.050 26.260 -26.814 1.00 66.62  ? 118 ARG A NE  1 
ATOM   226  C CZ  . ARG A 1 118 ? -16.906 26.925 -27.578 1.00 66.53  ? 118 ARG A CZ  1 
ATOM   227  N NH1 . ARG A 1 118 ? -17.004 28.243 -27.520 1.00 68.99  ? 118 ARG A NH1 1 
ATOM   228  N NH2 . ARG A 1 118 ? -17.678 26.251 -28.426 1.00 77.31  ? 118 ARG A NH2 1 
ATOM   229  N N   . PHE A 1 119 ? -16.823 30.739 -23.055 1.00 47.51  ? 119 PHE A N   1 
ATOM   230  C CA  . PHE A 1 119 ? -17.953 31.613 -23.374 1.00 42.05  ? 119 PHE A CA  1 
ATOM   231  C C   . PHE A 1 119 ? -17.758 32.940 -22.673 1.00 45.36  ? 119 PHE A C   1 
ATOM   232  O O   . PHE A 1 119 ? -18.395 33.228 -21.646 1.00 45.87  ? 119 PHE A O   1 
ATOM   233  C CB  . PHE A 1 119 ? -19.267 30.965 -22.955 1.00 45.94  ? 119 PHE A CB  1 
ATOM   234  C CG  . PHE A 1 119 ? -19.539 29.646 -23.652 1.00 44.04  ? 119 PHE A CG  1 
ATOM   235  C CD1 . PHE A 1 119 ? -20.105 29.621 -24.914 1.00 45.05  ? 119 PHE A CD1 1 
ATOM   236  C CD2 . PHE A 1 119 ? -19.243 28.430 -23.040 1.00 43.91  ? 119 PHE A CD2 1 
ATOM   237  C CE1 . PHE A 1 119 ? -20.363 28.429 -25.560 1.00 42.85  ? 119 PHE A CE1 1 
ATOM   238  C CE2 . PHE A 1 119 ? -19.498 27.232 -23.677 1.00 45.91  ? 119 PHE A CE2 1 
ATOM   239  C CZ  . PHE A 1 119 ? -20.057 27.228 -24.940 1.00 41.95  ? 119 PHE A CZ  1 
ATOM   240  N N   . PRO A 1 120 ? -16.866 33.793 -23.184 1.00 49.78  ? 120 PRO A N   1 
ATOM   241  C CA  . PRO A 1 120 ? -16.468 34.984 -22.405 1.00 46.80  ? 120 PRO A CA  1 
ATOM   242  C C   . PRO A 1 120 ? -17.568 36.027 -22.245 1.00 48.69  ? 120 PRO A C   1 
ATOM   243  O O   . PRO A 1 120 ? -17.478 36.863 -21.335 1.00 58.63  ? 120 PRO A O   1 
ATOM   244  C CB  . PRO A 1 120 ? -15.271 35.573 -23.185 1.00 51.94  ? 120 PRO A CB  1 
ATOM   245  C CG  . PRO A 1 120 ? -15.274 34.911 -24.512 1.00 51.75  ? 120 PRO A CG  1 
ATOM   246  C CD  . PRO A 1 120 ? -16.250 33.772 -24.529 1.00 45.89  ? 120 PRO A CD  1 
ATOM   247  N N   . ASP A 1 121 ? -18.598 36.011 -23.084 1.00 51.15  ? 121 ASP A N   1 
ATOM   248  C CA  . ASP A 1 121 ? -19.693 36.965 -22.963 1.00 50.87  ? 121 ASP A CA  1 
ATOM   249  C C   . ASP A 1 121 ? -20.865 36.420 -22.160 1.00 46.03  ? 121 ASP A C   1 
ATOM   250  O O   . ASP A 1 121 ? -21.896 37.094 -22.059 1.00 51.65  ? 121 ASP A O   1 
ATOM   251  C CB  . ASP A 1 121 ? -20.173 37.386 -24.352 1.00 50.07  ? 121 ASP A CB  1 
ATOM   252  C CG  . ASP A 1 121 ? -19.064 37.968 -25.191 1.00 65.23  ? 121 ASP A CG  1 
ATOM   253  O OD1 . ASP A 1 121 ? -18.276 38.780 -24.662 1.00 63.37  ? 121 ASP A OD1 1 
ATOM   254  O OD2 . ASP A 1 121 ? -18.965 37.601 -26.380 1.00 71.54  ? 121 ASP A OD2 1 
ATOM   255  N N   . LEU A 1 122 ? -20.729 35.230 -21.587 1.00 43.69  ? 122 LEU A N   1 
ATOM   256  C CA  . LEU A 1 122 ? -21.832 34.576 -20.897 1.00 37.85  ? 122 LEU A CA  1 
ATOM   257  C C   . LEU A 1 122 ? -21.953 35.079 -19.464 1.00 33.44  ? 122 LEU A C   1 
ATOM   258  O O   . LEU A 1 122 ? -20.972 35.082 -18.714 1.00 39.79  ? 122 LEU A O   1 
ATOM   259  C CB  . LEU A 1 122 ? -21.623 33.063 -20.902 1.00 36.00  ? 122 LEU A CB  1 
ATOM   260  C CG  . LEU A 1 122 ? -22.718 32.201 -20.274 1.00 40.32  ? 122 LEU A CG  1 
ATOM   261  C CD1 . LEU A 1 122 ? -23.973 32.169 -21.132 1.00 38.96  ? 122 LEU A CD1 1 
ATOM   262  C CD2 . LEU A 1 122 ? -22.190 30.807 -20.006 1.00 39.11  ? 122 LEU A CD2 1 
ATOM   263  N N   . GLN A 1 123 ? -23.157 35.501 -19.079 1.00 37.96  ? 123 GLN A N   1 
ATOM   264  C CA  . GLN A 1 123 ? -23.436 35.768 -17.673 1.00 36.56  ? 123 GLN A CA  1 
ATOM   265  C C   . GLN A 1 123 ? -23.683 34.443 -16.966 1.00 38.34  ? 123 GLN A C   1 
ATOM   266  O O   . GLN A 1 123 ? -24.558 33.669 -17.372 1.00 37.52  ? 123 GLN A O   1 
ATOM   267  C CB  . GLN A 1 123 ? -24.635 36.696 -17.494 1.00 33.20  ? 123 GLN A CB  1 
ATOM   268  C CG  . GLN A 1 123 ? -24.930 36.957 -16.022 1.00 39.90  ? 123 GLN A CG  1 
ATOM   269  C CD  . GLN A 1 123 ? -26.145 37.831 -15.790 1.00 37.92  ? 123 GLN A CD  1 
ATOM   270  O OE1 . GLN A 1 123 ? -27.276 37.422 -16.036 1.00 43.19  ? 123 GLN A OE1 1 
ATOM   271  N NE2 . GLN A 1 123 ? -25.915 39.037 -15.288 1.00 39.17  ? 123 GLN A NE2 1 
ATOM   272  N N   . ILE A 1 124 ? -22.913 34.182 -15.916 1.00 29.56  ? 124 ILE A N   1 
ATOM   273  C CA  . ILE A 1 124 ? -22.990 32.937 -15.164 1.00 33.40  ? 124 ILE A CA  1 
ATOM   274  C C   . ILE A 1 124 ? -23.406 33.287 -13.743 1.00 30.68  ? 124 ILE A C   1 
ATOM   275  O O   . ILE A 1 124 ? -22.636 33.906 -12.999 1.00 36.37  ? 124 ILE A O   1 
ATOM   276  C CB  . ILE A 1 124 ? -21.658 32.181 -15.177 1.00 29.89  ? 124 ILE A CB  1 
ATOM   277  C CG1 . ILE A 1 124 ? -21.310 31.755 -16.604 1.00 32.24  ? 124 ILE A CG1 1 
ATOM   278  C CG2 . ILE A 1 124 ? -21.732 30.976 -14.257 1.00 35.49  ? 124 ILE A CG2 1 
ATOM   279  C CD1 . ILE A 1 124 ? -19.880 31.315 -16.771 1.00 30.97  ? 124 ILE A CD1 1 
ATOM   280  N N   . ASN A 1 125 ? -24.620 32.896 -13.365 1.00 35.07  ? 125 ASN A N   1 
ATOM   281  C CA  . ASN A 1 125 ? -25.141 33.147 -12.029 1.00 27.83  ? 125 ASN A CA  1 
ATOM   282  C C   . ASN A 1 125 ? -25.113 31.864 -11.211 1.00 36.28  ? 125 ASN A C   1 
ATOM   283  O O   . ASN A 1 125 ? -25.696 30.851 -11.610 1.00 35.95  ? 125 ASN A O   1 
ATOM   284  C CB  . ASN A 1 125 ? -26.561 33.712 -12.092 1.00 30.39  ? 125 ASN A CB  1 
ATOM   285  C CG  . ASN A 1 125 ? -26.669 34.902 -13.029 1.00 41.97  ? 125 ASN A CG  1 
ATOM   286  O OD1 . ASN A 1 125 ? -25.939 35.884 -12.887 1.00 39.27  ? 125 ASN A OD1 1 
ATOM   287  N ND2 . ASN A 1 125 ? -27.584 34.824 -13.987 1.00 41.68  ? 125 ASN A ND2 1 
ATOM   288  N N   . ILE A 1 126 ? -24.437 31.914 -10.069 1.00 33.70  ? 126 ILE A N   1 
ATOM   289  C CA  . ILE A 1 126 ? -24.307 30.777 -9.166  1.00 33.74  ? 126 ILE A CA  1 
ATOM   290  C C   . ILE A 1 126 ? -25.192 31.052 -7.956  1.00 35.07  ? 126 ILE A C   1 
ATOM   291  O O   . ILE A 1 126 ? -24.909 31.961 -7.168  1.00 38.53  ? 126 ILE A O   1 
ATOM   292  C CB  . ILE A 1 126 ? -22.848 30.545 -8.746  1.00 37.63  ? 126 ILE A CB  1 
ATOM   293  C CG1 . ILE A 1 126 ? -21.941 30.463 -9.976  1.00 37.65  ? 126 ILE A CG1 1 
ATOM   294  C CG2 . ILE A 1 126 ? -22.731 29.289 -7.904  1.00 38.15  ? 126 ILE A CG2 1 
ATOM   295  C CD1 . ILE A 1 126 ? -22.159 29.220 -10.800 1.00 34.98  ? 126 ILE A CD1 1 
ATOM   296  N N   . VAL A 1 127 ? -26.268 30.277 -7.813  1.00 33.62  ? 127 VAL A N   1 
ATOM   297  C CA  . VAL A 1 127 ? -27.156 30.379 -6.664  1.00 39.22  ? 127 VAL A CA  1 
ATOM   298  C C   . VAL A 1 127 ? -27.062 29.089 -5.851  1.00 36.55  ? 127 VAL A C   1 
ATOM   299  O O   . VAL A 1 127 ? -26.507 28.084 -6.295  1.00 30.91  ? 127 VAL A O   1 
ATOM   300  C CB  . VAL A 1 127 ? -28.613 30.673 -7.077  1.00 34.03  ? 127 VAL A CB  1 
ATOM   301  C CG1 . VAL A 1 127 ? -28.705 32.017 -7.780  1.00 34.84  ? 127 VAL A CG1 1 
ATOM   302  C CG2 . VAL A 1 127 ? -29.152 29.558 -7.960  1.00 31.59  ? 127 VAL A CG2 1 
ATOM   303  N N   . SER A 1 128 ? -27.613 29.130 -4.639  1.00 34.12  ? 128 SER A N   1 
ATOM   304  C CA  . SER A 1 128 ? -27.631 27.982 -3.747  1.00 32.24  ? 128 SER A CA  1 
ATOM   305  C C   . SER A 1 128 ? -29.036 27.791 -3.199  1.00 34.12  ? 128 SER A C   1 
ATOM   306  O O   . SER A 1 128 ? -29.805 28.748 -3.071  1.00 34.41  ? 128 SER A O   1 
ATOM   307  C CB  . SER A 1 128 ? -26.624 28.141 -2.596  1.00 40.30  ? 128 SER A CB  1 
ATOM   308  O OG  . SER A 1 128 ? -26.843 29.338 -1.872  1.00 59.14  ? 128 SER A OG  1 
ATOM   309  N N   . ALA A 1 129 ? -29.370 26.546 -2.879  1.00 31.53  ? 129 ALA A N   1 
ATOM   310  C CA  . ALA A 1 129 ? -30.711 26.197 -2.456  1.00 33.26  ? 129 ALA A CA  1 
ATOM   311  C C   . ALA A 1 129 ? -30.688 24.825 -1.825  1.00 29.52  ? 129 ALA A C   1 
ATOM   312  O O   . ALA A 1 129 ? -29.712 24.070 -2.010  1.00 31.45  ? 129 ALA A O   1 
ATOM   313  C CB  . ALA A 1 129 ? -31.698 26.233 -3.640  1.00 29.26  ? 129 ALA A CB  1 
ATOM   314  N N   . PRO A 1 130 ? -31.702 24.446 -1.065  1.00 39.26  ? 130 PRO A N   1 
ATOM   315  C CA  . PRO A 1 130 ? -31.819 23.063 -0.628  1.00 42.18  ? 130 PRO A CA  1 
ATOM   316  C C   . PRO A 1 130 ? -32.043 22.128 -1.809  1.00 35.36  ? 130 PRO A C   1 
ATOM   317  O O   . PRO A 1 130 ? -32.494 22.537 -2.882  1.00 44.48  ? 130 PRO A O   1 
ATOM   318  C CB  . PRO A 1 130 ? -33.020 23.068 0.320   1.00 41.86  ? 130 PRO A CB  1 
ATOM   319  C CG  . PRO A 1 130 ? -33.216 24.487 0.698   1.00 42.39  ? 130 PRO A CG  1 
ATOM   320  C CD  . PRO A 1 130 ? -32.722 25.318 -0.437  1.00 39.87  ? 130 PRO A CD  1 
ATOM   321  N N   . GLN A 1 131 ? -31.704 20.860 -1.584  1.00 35.33  ? 131 GLN A N   1 
ATOM   322  C CA  . GLN A 1 131 ? -31.880 19.811 -2.581  1.00 40.66  ? 131 GLN A CA  1 
ATOM   323  C C   . GLN A 1 131 ? -33.244 19.875 -3.251  1.00 44.30  ? 131 GLN A C   1 
ATOM   324  O O   . GLN A 1 131 ? -33.347 19.882 -4.480  1.00 46.94  ? 131 GLN A O   1 
ATOM   325  C CB  . GLN A 1 131 ? -31.672 18.454 -1.907  1.00 48.00  ? 131 GLN A CB  1 
ATOM   326  C CG  . GLN A 1 131 ? -30.215 18.045 -1.762  1.00 45.85  ? 131 GLN A CG  1 
ATOM   327  C CD  . GLN A 1 131 ? -29.673 17.369 -3.005  1.00 55.34  ? 131 GLN A CD  1 
ATOM   328  O OE1 . GLN A 1 131 ? -28.492 17.023 -3.078  1.00 46.48  ? 131 GLN A OE1 1 
ATOM   329  N NE2 . GLN A 1 131 ? -30.543 17.157 -3.987  1.00 57.35  ? 131 GLN A NE2 1 
ATOM   330  N N   . GLU A 1 132 ? -34.304 19.938 -2.447  1.00 46.15  ? 132 GLU A N   1 
ATOM   331  C CA  . GLU A 1 132 ? -35.661 19.914 -2.983  1.00 48.47  ? 132 GLU A CA  1 
ATOM   332  C C   . GLU A 1 132 ? -35.953 21.141 -3.841  1.00 45.78  ? 132 GLU A C   1 
ATOM   333  O O   . GLU A 1 132 ? -36.606 21.032 -4.886  1.00 46.14  ? 132 GLU A O   1 
ATOM   334  C CB  . GLU A 1 132 ? -36.673 19.808 -1.837  1.00 52.86  ? 132 GLU A CB  1 
ATOM   335  C CG  . GLU A 1 132 ? -36.234 18.924 -0.663  1.00 63.87  ? 132 GLU A CG  1 
ATOM   336  C CD  . GLU A 1 132 ? -35.244 19.612 0.259   1.00 67.00  ? 132 GLU A CD  1 
ATOM   337  O OE1 . GLU A 1 132 ? -35.687 20.235 1.245   1.00 73.58  ? 132 GLU A OE1 1 
ATOM   338  O OE2 . GLU A 1 132 ? -34.023 19.525 0.007   1.00 62.84  ? 132 GLU A OE2 1 
ATOM   339  N N   . ASP A 1 133 ? -35.488 22.319 -3.418  1.00 44.45  ? 133 ASP A N   1 
ATOM   340  C CA  . ASP A 1 133 ? -35.755 23.527 -4.193  1.00 44.45  ? 133 ASP A CA  1 
ATOM   341  C C   . ASP A 1 133 ? -34.906 23.572 -5.457  1.00 37.87  ? 133 ASP A C   1 
ATOM   342  O O   . ASP A 1 133 ? -35.356 24.065 -6.498  1.00 44.21  ? 133 ASP A O   1 
ATOM   343  C CB  . ASP A 1 133 ? -35.505 24.766 -3.336  1.00 47.99  ? 133 ASP A CB  1 
ATOM   344  C CG  . ASP A 1 133 ? -36.497 24.892 -2.197  1.00 60.84  ? 133 ASP A CG  1 
ATOM   345  O OD1 . ASP A 1 133 ? -37.127 23.870 -1.853  1.00 57.25  ? 133 ASP A OD1 1 
ATOM   346  O OD2 . ASP A 1 133 ? -36.629 26.000 -1.636  1.00 66.60  ? 133 ASP A OD2 1 
ATOM   347  N N   . ALA A 1 134 ? -33.670 23.073 -5.382  1.00 32.25  ? 134 ALA A N   1 
ATOM   348  C CA  . ALA A 1 134 ? -32.807 23.037 -6.559  1.00 37.59  ? 134 ALA A CA  1 
ATOM   349  C C   . ALA A 1 134 ? -33.432 22.212 -7.677  1.00 38.46  ? 134 ALA A C   1 
ATOM   350  O O   . ALA A 1 134 ? -33.383 22.602 -8.849  1.00 34.27  ? 134 ALA A O   1 
ATOM   351  C CB  . ALA A 1 134 ? -31.433 22.480 -6.183  1.00 33.74  ? 134 ALA A CB  1 
ATOM   352  N N   . LEU A 1 135 ? -34.033 21.072 -7.328  1.00 31.72  ? 135 LEU A N   1 
ATOM   353  C CA  . LEU A 1 135 ? -34.699 20.239 -8.325  1.00 43.23  ? 135 LEU A CA  1 
ATOM   354  C C   . LEU A 1 135 ? -35.860 20.983 -8.975  1.00 43.17  ? 135 LEU A C   1 
ATOM   355  O O   . LEU A 1 135 ? -36.023 20.949 -10.201 1.00 38.97  ? 135 LEU A O   1 
ATOM   356  C CB  . LEU A 1 135 ? -35.156 18.926 -7.673  1.00 45.04  ? 135 LEU A CB  1 
ATOM   357  C CG  . LEU A 1 135 ? -36.003 17.853 -8.379  1.00 45.25  ? 135 LEU A CG  1 
ATOM   358  C CD1 . LEU A 1 135 ? -37.481 18.180 -8.424  1.00 50.54  ? 135 LEU A CD1 1 
ATOM   359  C CD2 . LEU A 1 135 ? -35.489 17.634 -9.797  1.00 49.23  ? 135 LEU A CD2 1 
ATOM   360  N N   . GLN A 1 136 ? -36.673 21.669 -8.167  1.00 37.51  ? 136 GLN A N   1 
ATOM   361  C CA  . GLN A 1 136 ? -37.781 22.450 -8.711  1.00 40.72  ? 136 GLN A CA  1 
ATOM   362  C C   . GLN A 1 136 ? -37.293 23.587 -9.600  1.00 37.61  ? 136 GLN A C   1 
ATOM   363  O O   . GLN A 1 136 ? -37.991 23.980 -10.540 1.00 35.77  ? 136 GLN A O   1 
ATOM   364  C CB  . GLN A 1 136 ? -38.641 22.998 -7.573  1.00 42.20  ? 136 GLN A CB  1 
ATOM   365  C CG  . GLN A 1 136 ? -39.420 21.928 -6.820  1.00 43.95  ? 136 GLN A CG  1 
ATOM   366  C CD  . GLN A 1 136 ? -40.320 21.099 -7.727  1.00 52.61  ? 136 GLN A CD  1 
ATOM   367  O OE1 . GLN A 1 136 ? -40.972 21.627 -8.632  1.00 46.88  ? 136 GLN A OE1 1 
ATOM   368  N NE2 . GLN A 1 136 ? -40.366 19.794 -7.480  1.00 50.71  ? 136 GLN A NE2 1 
ATOM   369  N N   . MET A 1 137 ? -36.107 24.131 -9.318  1.00 34.54  ? 137 MET A N   1 
ATOM   370  C CA  . MET A 1 137 ? -35.550 25.180 -10.167 1.00 32.27  ? 137 MET A CA  1 
ATOM   371  C C   . MET A 1 137 ? -35.211 24.648 -11.553 1.00 36.66  ? 137 MET A C   1 
ATOM   372  O O   . MET A 1 137 ? -35.393 25.348 -12.556 1.00 34.42  ? 137 MET A O   1 
ATOM   373  C CB  . MET A 1 137 ? -34.311 25.782 -9.508  1.00 29.91  ? 137 MET A CB  1 
ATOM   374  C CG  . MET A 1 137 ? -34.616 26.611 -8.278  1.00 34.91  ? 137 MET A CG  1 
ATOM   375  S SD  . MET A 1 137 ? -33.116 27.277 -7.533  1.00 43.97  ? 137 MET A SD  1 
ATOM   376  C CE  . MET A 1 137 ? -32.810 28.690 -8.585  1.00 35.33  ? 137 MET A CE  1 
ATOM   377  N N   . LEU A 1 138 ? -34.709 23.415 -11.629 1.00 33.52  ? 138 LEU A N   1 
ATOM   378  C CA  . LEU A 1 138 ? -34.492 22.780 -12.923 1.00 42.68  ? 138 LEU A CA  1 
ATOM   379  C C   . LEU A 1 138 ? -35.809 22.590 -13.666 1.00 40.09  ? 138 LEU A C   1 
ATOM   380  O O   . LEU A 1 138 ? -35.897 22.834 -14.872 1.00 37.09  ? 138 LEU A O   1 
ATOM   381  C CB  . LEU A 1 138 ? -33.790 21.434 -12.736 1.00 33.15  ? 138 LEU A CB  1 
ATOM   382  C CG  . LEU A 1 138 ? -32.371 21.426 -12.155 1.00 37.46  ? 138 LEU A CG  1 
ATOM   383  C CD1 . LEU A 1 138 ? -31.900 19.994 -11.978 1.00 24.89  ? 138 LEU A CD1 1 
ATOM   384  C CD2 . LEU A 1 138 ? -31.394 22.208 -13.023 1.00 28.18  ? 138 LEU A CD2 1 
ATOM   385  N N   . LEU A 1 139 ? -36.852 22.161 -12.954 1.00 42.71  ? 139 LEU A N   1 
ATOM   386  C CA  . LEU A 1 139 ? -38.099 21.810 -13.627 1.00 41.58  ? 139 LEU A CA  1 
ATOM   387  C C   . LEU A 1 139 ? -38.862 23.044 -14.095 1.00 41.42  ? 139 LEU A C   1 
ATOM   388  O O   . LEU A 1 139 ? -39.513 23.007 -15.145 1.00 41.69  ? 139 LEU A O   1 
ATOM   389  C CB  . LEU A 1 139 ? -38.978 20.958 -12.712 1.00 42.98  ? 139 LEU A CB  1 
ATOM   390  C CG  . LEU A 1 139 ? -38.447 19.577 -12.334 1.00 47.06  ? 139 LEU A CG  1 
ATOM   391  C CD1 . LEU A 1 139 ? -39.390 18.942 -11.331 1.00 46.59  ? 139 LEU A CD1 1 
ATOM   392  C CD2 . LEU A 1 139 ? -38.270 18.688 -13.564 1.00 37.57  ? 139 LEU A CD2 1 
ATOM   393  N N   . ASP A 1 140 ? -38.814 24.140 -13.341 1.00 40.74  ? 140 ASP A N   1 
ATOM   394  C CA  . ASP A 1 140 ? -39.524 25.344 -13.758 1.00 39.63  ? 140 ASP A CA  1 
ATOM   395  C C   . ASP A 1 140 ? -38.648 26.318 -14.538 1.00 44.41  ? 140 ASP A C   1 
ATOM   396  O O   . ASP A 1 140 ? -39.128 27.390 -14.921 1.00 45.79  ? 140 ASP A O   1 
ATOM   397  C CB  . ASP A 1 140 ? -40.174 26.038 -12.545 1.00 44.85  ? 140 ASP A CB  1 
ATOM   398  C CG  . ASP A 1 140 ? -39.174 26.718 -11.620 1.00 50.39  ? 140 ASP A CG  1 
ATOM   399  O OD1 . ASP A 1 140 ? -37.981 26.873 -11.956 1.00 51.47  ? 140 ASP A OD1 1 
ATOM   400  O OD2 . ASP A 1 140 ? -39.601 27.129 -10.521 1.00 60.75  ? 140 ASP A OD2 1 
ATOM   401  N N   . GLY A 1 141 ? -37.381 25.978 -14.767 1.00 45.25  ? 141 GLY A N   1 
ATOM   402  C CA  . GLY A 1 141 ? -36.521 26.746 -15.639 1.00 38.64  ? 141 GLY A CA  1 
ATOM   403  C C   . GLY A 1 141 ? -35.689 27.821 -14.979 1.00 44.90  ? 141 GLY A C   1 
ATOM   404  O O   . GLY A 1 141 ? -34.964 28.533 -15.684 1.00 42.77  ? 141 GLY A O   1 
ATOM   405  N N   . SER A 1 142 ? -35.764 27.971 -13.659 1.00 39.35  ? 142 SER A N   1 
ATOM   406  C CA  . SER A 1 142 ? -34.973 29.006 -13.006 1.00 40.80  ? 142 SER A CA  1 
ATOM   407  C C   . SER A 1 142 ? -33.481 28.703 -13.094 1.00 32.20  ? 142 SER A C   1 
ATOM   408  O O   . SER A 1 142 ? -32.657 29.624 -13.086 1.00 39.09  ? 142 SER A O   1 
ATOM   409  C CB  . SER A 1 142 ? -35.423 29.153 -11.555 1.00 32.03  ? 142 SER A CB  1 
ATOM   410  O OG  . SER A 1 142 ? -36.839 29.134 -11.501 1.00 49.01  ? 142 SER A OG  1 
ATOM   411  N N   . ALA A 1 143 ? -33.120 27.426 -13.216 1.00 36.73  ? 143 ALA A N   1 
ATOM   412  C CA  . ALA A 1 143 ? -31.737 26.996 -13.354 1.00 32.64  ? 143 ALA A CA  1 
ATOM   413  C C   . ALA A 1 143 ? -31.629 25.975 -14.479 1.00 30.66  ? 143 ALA A C   1 
ATOM   414  O O   . ALA A 1 143 ? -32.541 25.174 -14.700 1.00 36.80  ? 143 ALA A O   1 
ATOM   415  C CB  . ALA A 1 143 ? -31.200 26.388 -12.048 1.00 28.92  ? 143 ALA A CB  1 
ATOM   416  N N   . GLN A 1 144 ? -30.502 26.013 -15.191 1.00 35.08  ? 144 GLN A N   1 
ATOM   417  C CA  . GLN A 1 144 ? -30.224 25.038 -16.239 1.00 27.98  ? 144 GLN A CA  1 
ATOM   418  C C   . GLN A 1 144 ? -29.459 23.834 -15.715 1.00 32.18  ? 144 GLN A C   1 
ATOM   419  O O   . GLN A 1 144 ? -29.616 22.725 -16.241 1.00 32.33  ? 144 GLN A O   1 
ATOM   420  C CB  . GLN A 1 144 ? -29.416 25.686 -17.367 1.00 35.83  ? 144 GLN A CB  1 
ATOM   421  C CG  . GLN A 1 144 ? -30.203 26.676 -18.216 1.00 30.51  ? 144 GLN A CG  1 
ATOM   422  C CD  . GLN A 1 144 ? -29.397 27.200 -19.384 1.00 50.65  ? 144 GLN A CD  1 
ATOM   423  O OE1 . GLN A 1 144 ? -28.993 26.438 -20.266 1.00 50.86  ? 144 GLN A OE1 1 
ATOM   424  N NE2 . GLN A 1 144 ? -29.137 28.506 -19.386 1.00 49.66  ? 144 GLN A NE2 1 
ATOM   425  N N   . LEU A 1 145 ? -28.632 24.034 -14.693 1.00 27.15  ? 145 LEU A N   1 
ATOM   426  C CA  . LEU A 1 145 ? -27.774 22.990 -14.162 1.00 30.42  ? 145 LEU A CA  1 
ATOM   427  C C   . LEU A 1 145 ? -27.814 23.044 -12.644 1.00 27.26  ? 145 LEU A C   1 
ATOM   428  O O   . LEU A 1 145 ? -28.061 24.097 -12.051 1.00 31.58  ? 145 LEU A O   1 
ATOM   429  C CB  . LEU A 1 145 ? -26.327 23.150 -14.656 1.00 26.99  ? 145 LEU A CB  1 
ATOM   430  C CG  . LEU A 1 145 ? -26.056 22.994 -16.152 1.00 36.09  ? 145 LEU A CG  1 
ATOM   431  C CD1 . LEU A 1 145 ? -24.602 23.316 -16.472 1.00 28.49  ? 145 LEU A CD1 1 
ATOM   432  C CD2 . LEU A 1 145 ? -26.417 21.599 -16.647 1.00 34.26  ? 145 LEU A CD2 1 
ATOM   433  N N   . ALA A 1 146 ? -27.566 21.897 -12.023 1.00 31.16  ? 146 ALA A N   1 
ATOM   434  C CA  . ALA A 1 146 ? -27.538 21.785 -10.574 1.00 27.95  ? 146 ALA A CA  1 
ATOM   435  C C   . ALA A 1 146 ? -26.375 20.903 -10.149 1.00 29.74  ? 146 ALA A C   1 
ATOM   436  O O   . ALA A 1 146 ? -26.081 19.893 -10.796 1.00 25.48  ? 146 ALA A O   1 
ATOM   437  C CB  . ALA A 1 146 ? -28.855 21.208 -10.033 1.00 29.32  ? 146 ALA A CB  1 
ATOM   438  N N   . LEU A 1 147 ? -25.706 21.296 -9.066  1.00 33.61  ? 147 LEU A N   1 
ATOM   439  C CA  . LEU A 1 147 ? -24.737 20.441 -8.392  1.00 29.66  ? 147 LEU A CA  1 
ATOM   440  C C   . LEU A 1 147 ? -25.433 19.818 -7.189  1.00 35.37  ? 147 LEU A C   1 
ATOM   441  O O   . LEU A 1 147 ? -25.763 20.514 -6.223  1.00 34.34  ? 147 LEU A O   1 
ATOM   442  C CB  . LEU A 1 147 ? -23.494 21.218 -7.970  1.00 34.85  ? 147 LEU A CB  1 
ATOM   443  C CG  . LEU A 1 147 ? -22.547 21.695 -9.068  1.00 39.48  ? 147 LEU A CG  1 
ATOM   444  C CD1 . LEU A 1 147 ? -21.168 21.881 -8.487  1.00 42.58  ? 147 LEU A CD1 1 
ATOM   445  C CD2 . LEU A 1 147 ? -22.503 20.712 -10.220 1.00 37.51  ? 147 LEU A CD2 1 
ATOM   446  N N   . MET A 1 148 ? -25.657 18.508 -7.260  1.00 35.90  ? 148 MET A N   1 
ATOM   447  C CA  . MET A 1 148 ? -26.395 17.737 -6.272  1.00 38.39  ? 148 MET A CA  1 
ATOM   448  C C   . MET A 1 148 ? -25.499 16.600 -5.797  1.00 37.97  ? 148 MET A C   1 
ATOM   449  O O   . MET A 1 148 ? -24.487 16.279 -6.424  1.00 35.09  ? 148 MET A O   1 
ATOM   450  C CB  . MET A 1 148 ? -27.706 17.204 -6.878  1.00 33.92  ? 148 MET A CB  1 
ATOM   451  C CG  . MET A 1 148 ? -28.571 18.309 -7.516  1.00 35.24  ? 148 MET A CG  1 
ATOM   452  S SD  . MET A 1 148 ? -30.101 17.835 -8.379  1.00 52.39  ? 148 MET A SD  1 
ATOM   453  C CE  . MET A 1 148 ? -31.249 17.365 -7.099  1.00 51.58  ? 148 MET A CE  1 
ATOM   454  N N   . PHE A 1 149 ? -25.855 15.994 -4.671  1.00 35.68  ? 149 PHE A N   1 
ATOM   455  C CA  . PHE A 1 149 ? -25.107 14.854 -4.166  1.00 52.92  ? 149 PHE A CA  1 
ATOM   456  C C   . PHE A 1 149 ? -26.015 13.640 -4.023  1.00 51.91  ? 149 PHE A C   1 
ATOM   457  O O   . PHE A 1 149 ? -27.245 13.754 -3.981  1.00 54.14  ? 149 PHE A O   1 
ATOM   458  C CB  . PHE A 1 149 ? -24.414 15.162 -2.820  1.00 38.69  ? 149 PHE A CB  1 
ATOM   459  C CG  . PHE A 1 149 ? -25.356 15.383 -1.664  1.00 43.83  ? 149 PHE A CG  1 
ATOM   460  C CD1 . PHE A 1 149 ? -25.998 16.597 -1.503  1.00 50.45  ? 149 PHE A CD1 1 
ATOM   461  C CD2 . PHE A 1 149 ? -25.574 14.385 -0.721  1.00 52.97  ? 149 PHE A CD2 1 
ATOM   462  C CE1 . PHE A 1 149 ? -26.857 16.812 -0.443  1.00 45.59  ? 149 PHE A CE1 1 
ATOM   463  C CE2 . PHE A 1 149 ? -26.435 14.596 0.346   1.00 49.42  ? 149 PHE A CE2 1 
ATOM   464  C CZ  . PHE A 1 149 ? -27.075 15.811 0.482   1.00 47.00  ? 149 PHE A CZ  1 
ATOM   465  N N   . GLU A 1 150 ? -25.374 12.470 -3.975  1.00 54.02  ? 150 GLU A N   1 
ATOM   466  C CA  . GLU A 1 150 ? -26.021 11.185 -3.728  1.00 67.78  ? 150 GLU A CA  1 
ATOM   467  C C   . GLU A 1 150 ? -27.006 10.856 -4.846  1.00 80.32  ? 150 GLU A C   1 
ATOM   468  O O   . GLU A 1 150 ? -26.731 9.971  -5.660  1.00 90.53  ? 150 GLU A O   1 
ATOM   469  C CB  . GLU A 1 150 ? -26.677 11.185 -2.339  1.00 66.34  ? 150 GLU A CB  1 
ATOM   470  C CG  . GLU A 1 150 ? -27.416 9.915  -1.958  1.00 78.64  ? 150 GLU A CG  1 
ATOM   471  C CD  . GLU A 1 150 ? -28.890 9.967  -2.270  1.00 80.98  ? 150 GLU A CD  1 
ATOM   472  O OE1 . GLU A 1 150 ? -29.542 10.963 -1.892  1.00 78.39  ? 150 GLU A OE1 1 
ATOM   473  O OE2 . GLU A 1 150 ? -29.405 9.010  -2.882  1.00 77.50  ? 150 GLU A OE2 1 
ATOM   474  N N   . ARG A 1 151 ? -28.138 11.546 -4.917  1.00 95.23  ? 151 ARG A N   1 
ATOM   475  C CA  . ARG A 1 151 ? -28.967 11.443 -6.116  1.00 95.38  ? 151 ARG A CA  1 
ATOM   476  C C   . ARG A 1 151 ? -28.379 12.297 -7.236  1.00 93.10  ? 151 ARG A C   1 
ATOM   477  O O   . ARG A 1 151 ? -28.427 11.920 -8.404  1.00 85.50  ? 151 ARG A O   1 
ATOM   478  C CB  . ARG A 1 151 ? -30.419 11.862 -5.850  1.00 97.87  ? 151 ARG A CB  1 
ATOM   479  C CG  . ARG A 1 151 ? -31.000 11.292 -4.576  1.00 95.05  ? 151 ARG A CG  1 
ATOM   480  C CD  . ARG A 1 151 ? -32.524 11.339 -4.556  1.00 99.87  ? 151 ARG A CD  1 
ATOM   481  N NE  . ARG A 1 151 ? -33.114 10.276 -5.362  1.00 100.42 ? 151 ARG A NE  1 
ATOM   482  C CZ  . ARG A 1 151 ? -33.724 10.469 -6.523  1.00 101.11 ? 151 ARG A CZ  1 
ATOM   483  N NH1 . ARG A 1 151 ? -33.918 11.684 -7.009  1.00 98.78  ? 151 ARG A NH1 1 
ATOM   484  N NH2 . ARG A 1 151 ? -34.165 9.417  -7.207  1.00 98.81  ? 151 ARG A NH2 1 
ATOM   485  N N   . ASP A 1 155 ? -35.574 10.545 -9.573  1.00 72.13  ? 155 ASP A N   1 
ATOM   486  C CA  . ASP A 1 155 ? -36.723 11.035 -10.324 1.00 73.43  ? 155 ASP A CA  1 
ATOM   487  C C   . ASP A 1 155 ? -36.429 10.857 -11.811 1.00 68.58  ? 155 ASP A C   1 
ATOM   488  O O   . ASP A 1 155 ? -35.338 11.171 -12.274 1.00 68.54  ? 155 ASP A O   1 
ATOM   489  C CB  . ASP A 1 155 ? -37.009 12.503 -9.977  1.00 74.67  ? 155 ASP A CB  1 
ATOM   490  C CG  . ASP A 1 155 ? -38.288 13.024 -10.615 1.00 76.13  ? 155 ASP A CG  1 
ATOM   491  O OD1 . ASP A 1 155 ? -38.872 12.331 -11.475 1.00 75.13  ? 155 ASP A OD1 1 
ATOM   492  O OD2 . ASP A 1 155 ? -38.726 14.128 -10.235 1.00 63.98  ? 155 ASP A OD2 1 
ATOM   493  N N   . ASN A 1 156 ? -37.395 10.337 -12.561 1.00 67.84  ? 156 ASN A N   1 
ATOM   494  C CA  . ASN A 1 156 ? -37.138 10.000 -13.954 1.00 66.81  ? 156 ASN A CA  1 
ATOM   495  C C   . ASN A 1 156 ? -37.112 11.215 -14.877 1.00 63.59  ? 156 ASN A C   1 
ATOM   496  O O   . ASN A 1 156 ? -36.841 11.056 -16.071 1.00 58.42  ? 156 ASN A O   1 
ATOM   497  C CB  . ASN A 1 156 ? -38.182 8.995  -14.437 1.00 78.84  ? 156 ASN A CB  1 
ATOM   498  C CG  . ASN A 1 156 ? -39.544 9.618  -14.608 1.00 76.03  ? 156 ASN A CG  1 
ATOM   499  O OD1 . ASN A 1 156 ? -39.922 10.524 -13.867 1.00 79.03  ? 156 ASN A OD1 1 
ATOM   500  N ND2 . ASN A 1 156 ? -40.300 9.125  -15.579 1.00 71.77  ? 156 ASN A ND2 1 
ATOM   501  N N   . ARG A 1 157 ? -37.378 12.415 -14.362 1.00 65.28  ? 157 ARG A N   1 
ATOM   502  C CA  . ARG A 1 157 ? -37.317 13.624 -15.174 1.00 59.41  ? 157 ARG A CA  1 
ATOM   503  C C   . ARG A 1 157 ? -35.955 14.303 -15.138 1.00 51.61  ? 157 ARG A C   1 
ATOM   504  O O   . ARG A 1 157 ? -35.687 15.165 -15.983 1.00 47.29  ? 157 ARG A O   1 
ATOM   505  C CB  . ARG A 1 157 ? -38.399 14.615 -14.728 1.00 58.13  ? 157 ARG A CB  1 
ATOM   506  C CG  . ARG A 1 157 ? -39.811 14.199 -15.113 1.00 65.19  ? 157 ARG A CG  1 
ATOM   507  C CD  . ARG A 1 157 ? -40.839 15.207 -14.634 1.00 64.59  ? 157 ARG A CD  1 
ATOM   508  N NE  . ARG A 1 157 ? -40.828 15.327 -13.181 1.00 63.94  ? 157 ARG A NE  1 
ATOM   509  C CZ  . ARG A 1 157 ? -41.612 16.143 -12.489 1.00 65.85  ? 157 ARG A CZ  1 
ATOM   510  N NH1 . ARG A 1 157 ? -42.472 16.949 -13.090 1.00 52.84  ? 157 ARG A NH1 1 
ATOM   511  N NH2 . ARG A 1 157 ? -41.533 16.146 -11.162 1.00 60.38  ? 157 ARG A NH2 1 
ATOM   512  N N   . GLU A 1 158 ? -35.092 13.937 -14.199 1.00 46.33  ? 158 GLU A N   1 
ATOM   513  C CA  . GLU A 1 158 ? -33.737 14.461 -14.179 1.00 48.22  ? 158 GLU A CA  1 
ATOM   514  C C   . GLU A 1 158 ? -32.785 13.484 -14.855 1.00 52.99  ? 158 GLU A C   1 
ATOM   515  O O   . GLU A 1 158 ? -32.958 12.264 -14.781 1.00 49.68  ? 158 GLU A O   1 
ATOM   516  C CB  . GLU A 1 158 ? -33.267 14.739 -12.748 1.00 51.53  ? 158 GLU A CB  1 
ATOM   517  C CG  . GLU A 1 158 ? -33.736 13.742 -11.704 1.00 62.05  ? 158 GLU A CG  1 
ATOM   518  C CD  . GLU A 1 158 ? -32.885 13.783 -10.450 1.00 77.09  ? 158 GLU A CD  1 
ATOM   519  O OE1 . GLU A 1 158 ? -32.865 14.840 -9.783  1.00 70.68  ? 158 GLU A OE1 1 
ATOM   520  O OE2 . GLU A 1 158 ? -32.253 12.758 -10.113 1.00 75.71  ? 158 GLU A OE2 1 
ATOM   521  N N   . GLN A 1 159 ? -31.800 14.040 -15.552 1.00 46.85  ? 159 GLN A N   1 
ATOM   522  C CA  . GLN A 1 159 ? -30.625 13.313 -15.999 1.00 47.63  ? 159 GLN A CA  1 
ATOM   523  C C   . GLN A 1 159 ? -29.401 13.874 -15.290 1.00 40.10  ? 159 GLN A C   1 
ATOM   524  O O   . GLN A 1 159 ? -29.411 14.997 -14.785 1.00 40.76  ? 159 GLN A O   1 
ATOM   525  C CB  . GLN A 1 159 ? -30.445 13.391 -17.520 1.00 46.51  ? 159 GLN A CB  1 
ATOM   526  C CG  . GLN A 1 159 ? -30.887 12.132 -18.257 1.00 64.18  ? 159 GLN A CG  1 
ATOM   527  C CD  . GLN A 1 159 ? -29.869 10.993 -18.178 1.00 71.79  ? 159 GLN A CD  1 
ATOM   528  O OE1 . GLN A 1 159 ? -29.480 10.553 -17.090 1.00 62.88  ? 159 GLN A OE1 1 
ATOM   529  N NE2 . GLN A 1 159 ? -29.444 10.503 -19.339 1.00 64.24  ? 159 GLN A NE2 1 
ATOM   530  N N   . PHE A 1 160 ? -28.346 13.071 -15.236 1.00 39.92  ? 160 PHE A N   1 
ATOM   531  C CA  . PHE A 1 160 ? -27.178 13.460 -14.464 1.00 41.50  ? 160 PHE A CA  1 
ATOM   532  C C   . PHE A 1 160 ? -25.947 12.724 -14.963 1.00 42.29  ? 160 PHE A C   1 
ATOM   533  O O   . PHE A 1 160 ? -26.040 11.714 -15.666 1.00 46.76  ? 160 PHE A O   1 
ATOM   534  C CB  . PHE A 1 160 ? -27.397 13.204 -12.965 1.00 37.21  ? 160 PHE A CB  1 
ATOM   535  C CG  . PHE A 1 160 ? -27.265 11.760 -12.565 1.00 45.99  ? 160 PHE A CG  1 
ATOM   536  C CD1 . PHE A 1 160 ? -26.036 11.232 -12.195 1.00 46.84  ? 160 PHE A CD1 1 
ATOM   537  C CD2 . PHE A 1 160 ? -28.369 10.924 -12.584 1.00 52.39  ? 160 PHE A CD2 1 
ATOM   538  C CE1 . PHE A 1 160 ? -25.918 9.902  -11.841 1.00 49.81  ? 160 PHE A CE1 1 
ATOM   539  C CE2 . PHE A 1 160 ? -28.256 9.593  -12.231 1.00 54.87  ? 160 PHE A CE2 1 
ATOM   540  C CZ  . PHE A 1 160 ? -27.028 9.081  -11.859 1.00 57.01  ? 160 PHE A CZ  1 
ATOM   541  N N   . VAL A 1 161 ? -24.791 13.261 -14.584 1.00 41.13  ? 161 VAL A N   1 
ATOM   542  C CA  . VAL A 1 161 ? -23.502 12.608 -14.762 1.00 43.44  ? 161 VAL A CA  1 
ATOM   543  C C   . VAL A 1 161 ? -22.691 12.853 -13.498 1.00 42.51  ? 161 VAL A C   1 
ATOM   544  O O   . VAL A 1 161 ? -22.686 13.966 -12.960 1.00 39.16  ? 161 VAL A O   1 
ATOM   545  C CB  . VAL A 1 161 ? -22.759 13.129 -16.012 1.00 36.76  ? 161 VAL A CB  1 
ATOM   546  C CG1 . VAL A 1 161 ? -22.611 14.643 -15.961 1.00 32.63  ? 161 VAL A CG1 1 
ATOM   547  C CG2 . VAL A 1 161 ? -21.411 12.448 -16.151 1.00 45.30  ? 161 VAL A CG2 1 
ATOM   548  N N   . GLU A 1 162 ? -22.032 11.807 -13.004 1.00 42.56  ? 162 GLU A N   1 
ATOM   549  C CA  . GLU A 1 162 ? -21.268 11.929 -11.772 1.00 44.68  ? 162 GLU A CA  1 
ATOM   550  C C   . GLU A 1 162 ? -20.004 12.741 -12.013 1.00 45.02  ? 162 GLU A C   1 
ATOM   551  O O   . GLU A 1 162 ? -19.347 12.600 -13.048 1.00 43.86  ? 162 GLU A O   1 
ATOM   552  C CB  . GLU A 1 162 ? -20.915 10.550 -11.219 1.00 39.40  ? 162 GLU A CB  1 
ATOM   553  C CG  . GLU A 1 162 ? -20.328 10.590 -9.822  1.00 46.57  ? 162 GLU A CG  1 
ATOM   554  C CD  . GLU A 1 162 ? -20.139 9.210  -9.241  1.00 54.63  ? 162 GLU A CD  1 
ATOM   555  O OE1 . GLU A 1 162 ? -21.122 8.660  -8.701  1.00 58.99  ? 162 GLU A OE1 1 
ATOM   556  O OE2 . GLU A 1 162 ? -19.012 8.677  -9.318  1.00 50.52  ? 162 GLU A OE2 1 
ATOM   557  N N   . LEU A 1 163 ? -19.672 13.604 -11.051 1.00 32.82  ? 163 LEU A N   1 
ATOM   558  C CA  . LEU A 1 163 ? -18.526 14.498 -11.173 1.00 37.58  ? 163 LEU A CA  1 
ATOM   559  C C   . LEU A 1 163 ? -17.324 14.007 -10.374 1.00 45.38  ? 163 LEU A C   1 
ATOM   560  O O   . LEU A 1 163 ? -16.249 13.783 -10.938 1.00 51.26  ? 163 LEU A O   1 
ATOM   561  C CB  . LEU A 1 163 ? -18.911 15.913 -10.728 1.00 38.42  ? 163 LEU A CB  1 
ATOM   562  C CG  . LEU A 1 163 ? -19.873 16.680 -11.637 1.00 40.85  ? 163 LEU A CG  1 
ATOM   563  C CD1 . LEU A 1 163 ? -20.024 18.115 -11.172 1.00 40.06  ? 163 LEU A CD1 1 
ATOM   564  C CD2 . LEU A 1 163 ? -19.387 16.639 -13.072 1.00 37.88  ? 163 LEU A CD2 1 
ATOM   565  N N   . LYS A 1 164 ? -17.492 13.825 -9.068  1.00 40.80  ? 164 LYS A N   1 
ATOM   566  C CA  . LYS A 1 164 ? -16.351 13.611 -8.189  1.00 42.61  ? 164 LYS A CA  1 
ATOM   567  C C   . LYS A 1 164 ? -16.850 13.201 -6.811  1.00 39.60  ? 164 LYS A C   1 
ATOM   568  O O   . LYS A 1 164 ? -18.025 13.364 -6.472  1.00 37.30  ? 164 LYS A O   1 
ATOM   569  C CB  . LYS A 1 164 ? -15.497 14.876 -8.087  1.00 44.91  ? 164 LYS A CB  1 
ATOM   570  C CG  . LYS A 1 164 ? -16.266 16.052 -7.505  1.00 53.58  ? 164 LYS A CG  1 
ATOM   571  C CD  . LYS A 1 164 ? -15.351 17.191 -7.116  1.00 56.53  ? 164 LYS A CD  1 
ATOM   572  C CE  . LYS A 1 164 ? -14.513 17.643 -8.291  1.00 69.05  ? 164 LYS A CE  1 
ATOM   573  N NZ  . LYS A 1 164 ? -14.531 19.125 -8.411  1.00 70.50  ? 164 LYS A NZ  1 
ATOM   574  N N   . ARG A 1 165 ? -15.926 12.663 -6.023  1.00 38.30  ? 165 ARG A N   1 
ATOM   575  C CA  . ARG A 1 165 ? -16.125 12.451 -4.599  1.00 38.77  ? 165 ARG A CA  1 
ATOM   576  C C   . ARG A 1 165 ? -15.524 13.622 -3.834  1.00 41.88  ? 165 ARG A C   1 
ATOM   577  O O   . ARG A 1 165 ? -14.444 14.112 -4.175  1.00 47.53  ? 165 ARG A O   1 
ATOM   578  C CB  . ARG A 1 165 ? -15.467 11.139 -4.170  1.00 35.17  ? 165 ARG A CB  1 
ATOM   579  C CG  . ARG A 1 165 ? -15.781 10.660 -2.767  1.00 41.26  ? 165 ARG A CG  1 
ATOM   580  C CD  . ARG A 1 165 ? -14.931 9.431  -2.458  1.00 42.44  ? 165 ARG A CD  1 
ATOM   581  N NE  . ARG A 1 165 ? -13.562 9.779  -2.089  1.00 48.80  ? 165 ARG A NE  1 
ATOM   582  C CZ  . ARG A 1 165 ? -13.195 10.205 -0.888  1.00 52.50  ? 165 ARG A CZ  1 
ATOM   583  N NH1 . ARG A 1 165 ? -14.059 10.284 0.112   1.00 46.46  ? 165 ARG A NH1 1 
ATOM   584  N NH2 . ARG A 1 165 ? -11.927 10.548 -0.679  1.00 47.64  ? 165 ARG A NH2 1 
ATOM   585  N N   . GLU A 1 166 ? -16.236 14.084 -2.812  1.00 36.10  ? 166 GLU A N   1 
ATOM   586  C CA  . GLU A 1 166 ? -15.754 15.142 -1.931  1.00 36.27  ? 166 GLU A CA  1 
ATOM   587  C C   . GLU A 1 166 ? -15.663 14.572 -0.522  1.00 37.39  ? 166 GLU A C   1 
ATOM   588  O O   . GLU A 1 166 ? -16.668 14.113 0.029   1.00 34.98  ? 166 GLU A O   1 
ATOM   589  C CB  . GLU A 1 166 ? -16.680 16.362 -1.969  1.00 34.52  ? 166 GLU A CB  1 
ATOM   590  C CG  . GLU A 1 166 ? -16.515 17.242 -3.207  1.00 47.85  ? 166 GLU A CG  1 
ATOM   591  C CD  . GLU A 1 166 ? -15.334 18.182 -3.110  1.00 52.67  ? 166 GLU A CD  1 
ATOM   592  O OE1 . GLU A 1 166 ? -14.760 18.308 -2.010  1.00 54.34  ? 166 GLU A OE1 1 
ATOM   593  O OE2 . GLU A 1 166 ? -14.983 18.808 -4.131  1.00 66.06  ? 166 GLU A OE2 1 
ATOM   594  N N   . ALA A 1 167 ? -14.459 14.576 0.045   1.00 30.99  ? 167 ALA A N   1 
ATOM   595  C CA  . ALA A 1 167 ? -14.248 14.002 1.366   1.00 37.86  ? 167 ALA A CA  1 
ATOM   596  C C   . ALA A 1 167 ? -14.639 14.996 2.451   1.00 32.77  ? 167 ALA A C   1 
ATOM   597  O O   . ALA A 1 167 ? -14.457 16.207 2.300   1.00 30.20  ? 167 ALA A O   1 
ATOM   598  C CB  . ALA A 1 167 ? -12.788 13.582 1.542   1.00 38.13  ? 167 ALA A CB  1 
ATOM   599  N N   . LEU A 1 168 ? -15.193 14.476 3.542   1.00 32.29  ? 168 LEU A N   1 
ATOM   600  C CA  . LEU A 1 168 ? -15.543 15.272 4.708   1.00 31.45  ? 168 LEU A CA  1 
ATOM   601  C C   . LEU A 1 168 ? -14.869 14.694 5.945   1.00 39.12  ? 168 LEU A C   1 
ATOM   602  O O   . LEU A 1 168 ? -14.525 13.509 5.995   1.00 36.19  ? 168 LEU A O   1 
ATOM   603  C CB  . LEU A 1 168 ? -17.062 15.339 4.913   1.00 30.49  ? 168 LEU A CB  1 
ATOM   604  C CG  . LEU A 1 168 ? -17.865 16.021 3.806   1.00 36.71  ? 168 LEU A CG  1 
ATOM   605  C CD1 . LEU A 1 168 ? -18.612 15.006 2.980   1.00 35.02  ? 168 LEU A CD1 1 
ATOM   606  C CD2 . LEU A 1 168 ? -18.822 17.030 4.397   1.00 38.47  ? 168 LEU A CD2 1 
ATOM   607  N N   . ILE A 1 169 ? -14.670 15.553 6.941   1.00 33.94  ? 169 ILE A N   1 
ATOM   608  C CA  . ILE A 1 169 ? -13.896 15.207 8.133   1.00 34.42  ? 169 ILE A CA  1 
ATOM   609  C C   . ILE A 1 169 ? -14.663 15.579 9.397   1.00 32.72  ? 169 ILE A C   1 
ATOM   610  O O   . ILE A 1 169 ? -15.132 16.721 9.519   1.00 28.60  ? 169 ILE A O   1 
ATOM   611  C CB  . ILE A 1 169 ? -12.527 15.908 8.124   1.00 39.31  ? 169 ILE A CB  1 
ATOM   612  C CG1 . ILE A 1 169 ? -11.823 15.776 6.771   1.00 50.01  ? 169 ILE A CG1 1 
ATOM   613  C CG2 . ILE A 1 169 ? -11.637 15.350 9.218   1.00 40.90  ? 169 ILE A CG2 1 
ATOM   614  C CD1 . ILE A 1 169 ? -11.480 14.352 6.384   1.00 55.22  ? 169 ILE A CD1 1 
ATOM   615  N N   . PRO A 1 170 ? -14.811 14.671 10.364  1.00 32.05  ? 170 PRO A N   1 
ATOM   616  C CA  . PRO A 1 170 ? -15.330 15.082 11.675  1.00 32.28  ? 170 PRO A CA  1 
ATOM   617  C C   . PRO A 1 170 ? -14.267 15.862 12.431  1.00 33.27  ? 170 PRO A C   1 
ATOM   618  O O   . PRO A 1 170 ? -13.129 15.409 12.575  1.00 39.66  ? 170 PRO A O   1 
ATOM   619  C CB  . PRO A 1 170 ? -15.657 13.755 12.367  1.00 29.21  ? 170 PRO A CB  1 
ATOM   620  C CG  . PRO A 1 170 ? -14.776 12.751 11.710  1.00 33.57  ? 170 PRO A CG  1 
ATOM   621  C CD  . PRO A 1 170 ? -14.523 13.227 10.302  1.00 30.75  ? 170 PRO A CD  1 
ATOM   622  N N   . VAL A 1 171 ? -14.638 17.057 12.897  1.00 30.24  ? 171 VAL A N   1 
ATOM   623  C CA  . VAL A 1 171 ? -13.683 17.965 13.515  1.00 33.75  ? 171 VAL A CA  1 
ATOM   624  C C   . VAL A 1 171 ? -14.271 18.570 14.782  1.00 32.58  ? 171 VAL A C   1 
ATOM   625  O O   . VAL A 1 171 ? -15.487 18.598 14.987  1.00 26.83  ? 171 VAL A O   1 
ATOM   626  C CB  . VAL A 1 171 ? -13.234 19.095 12.560  1.00 30.89  ? 171 VAL A CB  1 
ATOM   627  C CG1 . VAL A 1 171 ? -12.527 18.522 11.346  1.00 35.78  ? 171 VAL A CG1 1 
ATOM   628  C CG2 . VAL A 1 171 ? -14.423 19.939 12.148  1.00 27.32  ? 171 VAL A CG2 1 
ATOM   629  N N   . ILE A 1 172 ? -13.363 19.075 15.624  1.00 34.05  ? 172 ILE A N   1 
ATOM   630  C CA  . ILE A 1 172 ? -13.702 19.722 16.885  1.00 34.12  ? 172 ILE A CA  1 
ATOM   631  C C   . ILE A 1 172 ? -12.655 20.797 17.141  1.00 34.71  ? 172 ILE A C   1 
ATOM   632  O O   . ILE A 1 172 ? -11.530 20.730 16.643  1.00 36.08  ? 172 ILE A O   1 
ATOM   633  C CB  . ILE A 1 172 ? -13.758 18.714 18.057  1.00 35.29  ? 172 ILE A CB  1 
ATOM   634  C CG1 . ILE A 1 172 ? -14.407 19.339 19.295  1.00 32.46  ? 172 ILE A CG1 1 
ATOM   635  C CG2 . ILE A 1 172 ? -12.365 18.212 18.394  1.00 32.47  ? 172 ILE A CG2 1 
ATOM   636  C CD1 . ILE A 1 172 ? -15.029 18.329 20.225  1.00 38.97  ? 172 ILE A CD1 1 
ATOM   637  N N   . SER A 1 173 ? -13.036 21.803 17.923  1.00 28.75  ? 173 SER A N   1 
ATOM   638  C CA  . SER A 1 173 ? -12.097 22.870 18.235  1.00 35.67  ? 173 SER A CA  1 
ATOM   639  C C   . SER A 1 173 ? -10.992 22.362 19.154  1.00 37.69  ? 173 SER A C   1 
ATOM   640  O O   . SER A 1 173 ? -11.230 21.543 20.046  1.00 36.65  ? 173 SER A O   1 
ATOM   641  C CB  . SER A 1 173 ? -12.828 24.041 18.880  1.00 30.03  ? 173 SER A CB  1 
ATOM   642  O OG  . SER A 1 173 ? -11.911 24.956 19.461  1.00 32.96  ? 173 SER A OG  1 
ATOM   643  N N   . LYS A 1 174 ? -9.772  22.862 18.933  1.00 35.25  ? 174 LYS A N   1 
ATOM   644  C CA  . LYS A 1 174 ? -8.638  22.456 19.758  1.00 33.75  ? 174 LYS A CA  1 
ATOM   645  C C   . LYS A 1 174 ? -8.773  22.920 21.203  1.00 34.58  ? 174 LYS A C   1 
ATOM   646  O O   . LYS A 1 174 ? -8.125  22.352 22.089  1.00 43.16  ? 174 LYS A O   1 
ATOM   647  C CB  . LYS A 1 174 ? -7.335  22.989 19.161  1.00 37.12  ? 174 LYS A CB  1 
ATOM   648  C CG  . LYS A 1 174 ? -6.936  22.333 17.843  1.00 38.08  ? 174 LYS A CG  1 
ATOM   649  C CD  . LYS A 1 174 ? -5.570  22.815 17.384  1.00 45.04  ? 174 LYS A CD  1 
ATOM   650  C CE  . LYS A 1 174 ? -5.273  22.379 15.956  1.00 36.11  ? 174 LYS A CE  1 
ATOM   651  N NZ  . LYS A 1 174 ? -3.842  22.580 15.590  1.00 39.82  ? 174 LYS A NZ  1 
ATOM   652  N N   . THR A 1 175 ? -9.602  23.928 21.464  1.00 36.90  ? 175 THR A N   1 
ATOM   653  C CA  . THR A 1 175 ? -9.824  24.427 22.813  1.00 39.43  ? 175 THR A CA  1 
ATOM   654  C C   . THR A 1 175 ? -11.115 23.900 23.430  1.00 41.27  ? 175 THR A C   1 
ATOM   655  O O   . THR A 1 175 ? -11.472 24.306 24.537  1.00 46.82  ? 175 THR A O   1 
ATOM   656  C CB  . THR A 1 175 ? -9.822  25.956 22.815  1.00 34.79  ? 175 THR A CB  1 
ATOM   657  O OG1 . THR A 1 175 ? -10.899 26.440 22.007  1.00 45.31  ? 175 THR A OG1 1 
ATOM   658  C CG2 . THR A 1 175 ? -8.501  26.488 22.271  1.00 36.55  ? 175 THR A CG2 1 
ATOM   659  N N   . HIS A 1 176 ? -11.821 23.015 22.738  1.00 43.44  ? 176 HIS A N   1 
ATOM   660  C CA  . HIS A 1 176 ? -12.982 22.360 23.322  1.00 37.05  ? 176 HIS A CA  1 
ATOM   661  C C   . HIS A 1 176 ? -12.534 21.503 24.507  1.00 41.87  ? 176 HIS A C   1 
ATOM   662  O O   . HIS A 1 176 ? -11.466 20.885 24.449  1.00 49.67  ? 176 HIS A O   1 
ATOM   663  C CB  . HIS A 1 176 ? -13.689 21.500 22.268  1.00 36.28  ? 176 HIS A CB  1 
ATOM   664  C CG  . HIS A 1 176 ? -15.039 21.003 22.687  1.00 40.56  ? 176 HIS A CG  1 
ATOM   665  N ND1 . HIS A 1 176 ? -15.211 19.973 23.587  1.00 41.90  ? 176 HIS A ND1 1 
ATOM   666  C CD2 . HIS A 1 176 ? -16.284 21.391 22.319  1.00 32.29  ? 176 HIS A CD2 1 
ATOM   667  C CE1 . HIS A 1 176 ? -16.502 19.751 23.759  1.00 40.98  ? 176 HIS A CE1 1 
ATOM   668  N NE2 . HIS A 1 176 ? -17.175 20.598 23.001  1.00 39.85  ? 176 HIS A NE2 1 
ATOM   669  N N   . PRO A 1 177 ? -13.308 21.467 25.601  1.00 47.57  ? 177 PRO A N   1 
ATOM   670  C CA  . PRO A 1 177 ? -12.894 20.655 26.763  1.00 46.97  ? 177 PRO A CA  1 
ATOM   671  C C   . PRO A 1 177 ? -12.529 19.224 26.402  1.00 49.06  ? 177 PRO A C   1 
ATOM   672  O O   . PRO A 1 177 ? -11.593 18.657 26.974  1.00 57.21  ? 177 PRO A O   1 
ATOM   673  C CB  . PRO A 1 177 ? -14.126 20.711 27.672  1.00 47.01  ? 177 PRO A CB  1 
ATOM   674  C CG  . PRO A 1 177 ? -14.793 21.994 27.329  1.00 43.52  ? 177 PRO A CG  1 
ATOM   675  C CD  . PRO A 1 177 ? -14.549 22.221 25.858  1.00 43.09  ? 177 PRO A CD  1 
ATOM   676  N N   . LEU A 1 178 ? -13.239 18.634 25.440  1.00 50.46  ? 178 LEU A N   1 
ATOM   677  C CA  . LEU A 1 178 ? -12.947 17.269 25.018  1.00 49.81  ? 178 LEU A CA  1 
ATOM   678  C C   . LEU A 1 178 ? -11.563 17.155 24.389  1.00 53.32  ? 178 LEU A C   1 
ATOM   679  O O   . LEU A 1 178 ? -10.950 16.084 24.433  1.00 53.82  ? 178 LEU A O   1 
ATOM   680  C CB  . LEU A 1 178 ? -14.024 16.800 24.037  1.00 49.53  ? 178 LEU A CB  1 
ATOM   681  C CG  . LEU A 1 178 ? -14.429 15.331 23.993  1.00 54.87  ? 178 LEU A CG  1 
ATOM   682  C CD1 . LEU A 1 178 ? -14.966 14.881 25.341  1.00 55.02  ? 178 LEU A CD1 1 
ATOM   683  C CD2 . LEU A 1 178 ? -15.475 15.117 22.909  1.00 48.57  ? 178 LEU A CD2 1 
ATOM   684  N N   . ALA A 1 179 ? -11.046 18.245 23.819  1.00 51.95  ? 179 ALA A N   1 
ATOM   685  C CA  . ALA A 1 179 ? -9.813  18.172 23.046  1.00 48.80  ? 179 ALA A CA  1 
ATOM   686  C C   . ALA A 1 179 ? -8.559  18.116 23.909  1.00 59.76  ? 179 ALA A C   1 
ATOM   687  O O   . ALA A 1 179 ? -7.485  17.791 23.391  1.00 68.12  ? 179 ALA A O   1 
ATOM   688  C CB  . ALA A 1 179 ? -9.727  19.361 22.086  1.00 54.78  ? 179 ALA A CB  1 
ATOM   689  N N   . SER A 1 180 ? -8.663  18.418 25.203  1.00 59.23  ? 180 SER A N   1 
ATOM   690  C CA  . SER A 1 180 ? -7.500  18.378 26.081  1.00 64.88  ? 180 SER A CA  1 
ATOM   691  C C   . SER A 1 180 ? -7.068  16.960 26.435  1.00 78.88  ? 180 SER A C   1 
ATOM   692  O O   . SER A 1 180 ? -5.985  16.786 27.005  1.00 86.29  ? 180 SER A O   1 
ATOM   693  C CB  . SER A 1 180 ? -7.784  19.159 27.368  1.00 61.10  ? 180 SER A CB  1 
ATOM   694  O OG  . SER A 1 180 ? -8.774  18.512 28.150  1.00 65.11  ? 180 SER A OG  1 
ATOM   695  N N   . GLN A 1 181 ? -7.873  15.953 26.118  1.00 78.03  ? 181 GLN A N   1 
ATOM   696  C CA  . GLN A 1 181 ? -7.538  14.574 26.454  1.00 70.98  ? 181 GLN A CA  1 
ATOM   697  C C   . GLN A 1 181 ? -6.789  13.893 25.308  1.00 78.23  ? 181 GLN A C   1 
ATOM   698  O O   . GLN A 1 181 ? -6.579  12.681 25.325  1.00 85.65  ? 181 GLN A O   1 
ATOM   699  C CB  . GLN A 1 181 ? -8.803  13.793 26.802  1.00 72.25  ? 181 GLN A CB  1 
ATOM   700  C CG  . GLN A 1 181 ? -9.778  14.580 27.666  1.00 66.07  ? 181 GLN A CG  1 
ATOM   701  C CD  . GLN A 1 181 ? -11.143 13.928 27.759  1.00 68.58  ? 181 GLN A CD  1 
ATOM   702  O OE1 . GLN A 1 181 ? -11.297 12.739 27.483  1.00 73.85  ? 181 GLN A OE1 1 
ATOM   703  N NE2 . GLN A 1 181 ? -12.145 14.707 28.152  1.00 64.67  ? 181 GLN A NE2 1 
ATOM   704  N N   . VAL A 1 184 ? -10.294 10.198 23.638  1.00 65.63  ? 184 VAL A N   1 
ATOM   705  C CA  . VAL A 1 184 ? -11.719 10.320 23.925  1.00 58.07  ? 184 VAL A CA  1 
ATOM   706  C C   . VAL A 1 184 ? -12.476 9.084  23.446  1.00 57.27  ? 184 VAL A C   1 
ATOM   707  O O   . VAL A 1 184 ? -12.097 8.454  22.461  1.00 56.83  ? 184 VAL A O   1 
ATOM   708  C CB  . VAL A 1 184 ? -12.290 11.609 23.309  1.00 55.22  ? 184 VAL A CB  1 
ATOM   709  C CG1 . VAL A 1 184 ? -11.400 12.785 23.656  1.00 59.98  ? 184 VAL A CG1 1 
ATOM   710  C CG2 . VAL A 1 184 ? -12.398 11.476 21.798  1.00 62.13  ? 184 VAL A CG2 1 
ATOM   711  N N   . SER A 1 185 ? -13.542 8.736  24.160  1.00 50.79  ? 185 SER A N   1 
ATOM   712  C CA  . SER A 1 185 ? -14.291 7.528  23.858  1.00 48.65  ? 185 SER A CA  1 
ATOM   713  C C   . SER A 1 185 ? -15.474 7.837  22.944  1.00 52.94  ? 185 SER A C   1 
ATOM   714  O O   . SER A 1 185 ? -15.856 8.992  22.738  1.00 52.41  ? 185 SER A O   1 
ATOM   715  C CB  . SER A 1 185 ? -14.778 6.858  25.143  1.00 62.46  ? 185 SER A CB  1 
ATOM   716  O OG  . SER A 1 185 ? -15.645 7.710  25.872  1.00 54.94  ? 185 SER A OG  1 
ATOM   717  N N   . TYR A 1 186 ? -16.049 6.772  22.379  1.00 51.62  ? 186 TYR A N   1 
ATOM   718  C CA  . TYR A 1 186 ? -17.272 6.920  21.599  1.00 46.06  ? 186 TYR A CA  1 
ATOM   719  C C   . TYR A 1 186 ? -18.420 7.390  22.481  1.00 48.25  ? 186 TYR A C   1 
ATOM   720  O O   . TYR A 1 186 ? -19.284 8.155  22.039  1.00 45.30  ? 186 TYR A O   1 
ATOM   721  C CB  . TYR A 1 186 ? -17.623 5.596  20.922  1.00 49.37  ? 186 TYR A CB  1 
ATOM   722  C CG  . TYR A 1 186 ? -18.973 5.589  20.242  1.00 54.46  ? 186 TYR A CG  1 
ATOM   723  C CD1 . TYR A 1 186 ? -19.184 6.292  19.063  1.00 45.80  ? 186 TYR A CD1 1 
ATOM   724  C CD2 . TYR A 1 186 ? -20.041 4.886  20.787  1.00 53.63  ? 186 TYR A CD2 1 
ATOM   725  C CE1 . TYR A 1 186 ? -20.418 6.288  18.441  1.00 50.04  ? 186 TYR A CE1 1 
ATOM   726  C CE2 . TYR A 1 186 ? -21.279 4.879  20.173  1.00 49.35  ? 186 TYR A CE2 1 
ATOM   727  C CZ  . TYR A 1 186 ? -21.462 5.581  19.000  1.00 41.66  ? 186 TYR A CZ  1 
ATOM   728  O OH  . TYR A 1 186 ? -22.692 5.575  18.384  1.00 47.66  ? 186 TYR A OH  1 
ATOM   729  N N   . GLU A 1 187 ? -18.441 6.934  23.735  1.00 44.18  ? 187 GLU A N   1 
ATOM   730  C CA  . GLU A 1 187 ? -19.456 7.373  24.688  1.00 48.18  ? 187 GLU A CA  1 
ATOM   731  C C   . GLU A 1 187 ? -19.448 8.887  24.855  1.00 43.91  ? 187 GLU A C   1 
ATOM   732  O O   . GLU A 1 187 ? -20.503 9.507  25.010  1.00 49.82  ? 187 GLU A O   1 
ATOM   733  C CB  . GLU A 1 187 ? -19.229 6.684  26.038  1.00 53.51  ? 187 GLU A CB  1 
ATOM   734  C CG  . GLU A 1 187 ? -20.343 6.886  27.059  1.00 68.75  ? 187 GLU A CG  1 
ATOM   735  C CD  . GLU A 1 187 ? -21.664 6.267  26.642  1.00 79.27  ? 187 GLU A CD  1 
ATOM   736  O OE1 . GLU A 1 187 ? -21.651 5.190  26.011  1.00 81.00  ? 187 GLU A OE1 1 
ATOM   737  O OE2 . GLU A 1 187 ? -22.722 6.848  26.961  1.00 83.68  ? 187 GLU A OE2 1 
ATOM   738  N N   . GLN A 1 188 ? -18.266 9.503  24.820  1.00 44.40  ? 188 GLN A N   1 
ATOM   739  C CA  . GLN A 1 188 ? -18.176 10.951 24.993  1.00 37.67  ? 188 GLN A CA  1 
ATOM   740  C C   . GLN A 1 188 ? -18.664 11.692 23.754  1.00 39.50  ? 188 GLN A C   1 
ATOM   741  O O   . GLN A 1 188 ? -19.293 12.751 23.868  1.00 35.12  ? 188 GLN A O   1 
ATOM   742  C CB  . GLN A 1 188 ? -16.739 11.356 25.334  1.00 52.57  ? 188 GLN A CB  1 
ATOM   743  C CG  . GLN A 1 188 ? -16.231 10.753 26.631  1.00 51.05  ? 188 GLN A CG  1 
ATOM   744  C CD  . GLN A 1 188 ? -14.773 11.066 26.888  1.00 53.31  ? 188 GLN A CD  1 
ATOM   745  O OE1 . GLN A 1 188 ? -13.901 10.221 26.695  1.00 61.33  ? 188 GLN A OE1 1 
ATOM   746  N NE2 . GLN A 1 188 ? -14.500 12.288 27.330  1.00 62.08  ? 188 GLN A NE2 1 
ATOM   747  N N   . ILE A 1 189 ? -18.383 11.159 22.562  1.00 33.52  ? 189 ILE A N   1 
ATOM   748  C CA  . ILE A 1 189 ? -18.943 11.728 21.338  1.00 39.22  ? 189 ILE A CA  1 
ATOM   749  C C   . ILE A 1 189 ? -20.465 11.651 21.367  1.00 38.30  ? 189 ILE A C   1 
ATOM   750  O O   . ILE A 1 189 ? -21.160 12.596 20.980  1.00 39.93  ? 189 ILE A O   1 
ATOM   751  C CB  . ILE A 1 189 ? -18.366 11.020 20.099  1.00 39.41  ? 189 ILE A CB  1 
ATOM   752  C CG1 . ILE A 1 189 ? -16.871 11.313 19.968  1.00 50.09  ? 189 ILE A CG1 1 
ATOM   753  C CG2 . ILE A 1 189 ? -19.092 11.459 18.844  1.00 46.99  ? 189 ILE A CG2 1 
ATOM   754  C CD1 . ILE A 1 189 ? -16.564 12.792 19.766  1.00 48.29  ? 189 ILE A CD1 1 
ATOM   755  N N   . LEU A 1 190 ? -21.002 10.517 21.826  1.00 36.66  ? 190 LEU A N   1 
ATOM   756  C CA  . LEU A 1 190 ? -22.449 10.387 21.993  1.00 38.46  ? 190 LEU A CA  1 
ATOM   757  C C   . LEU A 1 190 ? -23.013 11.506 22.860  1.00 38.21  ? 190 LEU A C   1 
ATOM   758  O O   . LEU A 1 190 ? -24.086 12.051 22.571  1.00 38.34  ? 190 LEU A O   1 
ATOM   759  C CB  . LEU A 1 190 ? -22.785 9.029  22.613  1.00 43.55  ? 190 LEU A CB  1 
ATOM   760  C CG  . LEU A 1 190 ? -23.021 7.832  21.689  1.00 48.21  ? 190 LEU A CG  1 
ATOM   761  C CD1 . LEU A 1 190 ? -23.341 6.598  22.515  1.00 44.80  ? 190 LEU A CD1 1 
ATOM   762  C CD2 . LEU A 1 190 ? -24.142 8.118  20.708  1.00 41.29  ? 190 LEU A CD2 1 
ATOM   763  N N   . GLY A 1 191 ? -22.302 11.867 23.923  1.00 35.59  ? 191 GLY A N   1 
ATOM   764  C CA  . GLY A 1 191 ? -22.716 12.900 24.847  1.00 32.85  ? 191 GLY A CA  1 
ATOM   765  C C   . GLY A 1 191 ? -22.247 14.300 24.519  1.00 34.79  ? 191 GLY A C   1 
ATOM   766  O O   . GLY A 1 191 ? -22.409 15.201 25.348  1.00 43.17  ? 191 GLY A O   1 
ATOM   767  N N   . THR A 1 192 ? -21.662 14.517 23.345  1.00 33.32  ? 192 THR A N   1 
ATOM   768  C CA  . THR A 1 192 ? -21.227 15.837 22.914  1.00 29.84  ? 192 THR A CA  1 
ATOM   769  C C   . THR A 1 192 ? -22.110 16.308 21.767  1.00 34.57  ? 192 THR A C   1 
ATOM   770  O O   . THR A 1 192 ? -22.438 15.529 20.868  1.00 36.14  ? 192 THR A O   1 
ATOM   771  C CB  . THR A 1 192 ? -19.757 15.826 22.478  1.00 34.87  ? 192 THR A CB  1 
ATOM   772  O OG1 . THR A 1 192 ? -18.953 15.231 23.505  1.00 38.40  ? 192 THR A OG1 1 
ATOM   773  C CG2 . THR A 1 192 ? -19.265 17.246 22.224  1.00 30.07  ? 192 THR A CG2 1 
ATOM   774  N N   . ARG A 1 193 ? -22.496 17.583 21.809  1.00 32.54  ? 193 ARG A N   1 
ATOM   775  C CA  . ARG A 1 193 ? -23.412 18.129 20.815  1.00 29.96  ? 193 ARG A CA  1 
ATOM   776  C C   . ARG A 1 193 ? -22.810 18.071 19.416  1.00 31.19  ? 193 ARG A C   1 
ATOM   777  O O   . ARG A 1 193 ? -21.675 18.503 19.193  1.00 26.57  ? 193 ARG A O   1 
ATOM   778  C CB  . ARG A 1 193 ? -23.771 19.572 21.168  1.00 29.20  ? 193 ARG A CB  1 
ATOM   779  C CG  . ARG A 1 193 ? -24.843 20.174 20.273  1.00 27.92  ? 193 ARG A CG  1 
ATOM   780  C CD  . ARG A 1 193 ? -24.963 21.665 20.504  1.00 32.47  ? 193 ARG A CD  1 
ATOM   781  N NE  . ARG A 1 193 ? -25.588 21.954 21.788  1.00 39.22  ? 193 ARG A NE  1 
ATOM   782  C CZ  . ARG A 1 193 ? -25.022 22.654 22.760  1.00 30.33  ? 193 ARG A CZ  1 
ATOM   783  N NH1 . ARG A 1 193 ? -23.805 23.153 22.632  1.00 35.56  ? 193 ARG A NH1 1 
ATOM   784  N NH2 . ARG A 1 193 ? -25.693 22.852 23.892  1.00 36.40  ? 193 ARG A NH2 1 
ATOM   785  N N   . GLN A 1 194 ? -23.578 17.530 18.474  1.00 26.54  ? 194 GLN A N   1 
ATOM   786  C CA  . GLN A 1 194 ? -23.198 17.509 17.069  1.00 26.22  ? 194 GLN A CA  1 
ATOM   787  C C   . GLN A 1 194 ? -23.864 18.668 16.346  1.00 24.53  ? 194 GLN A C   1 
ATOM   788  O O   . GLN A 1 194 ? -25.064 18.902 16.512  1.00 29.59  ? 194 GLN A O   1 
ATOM   789  C CB  . GLN A 1 194 ? -23.597 16.192 16.405  1.00 26.49  ? 194 GLN A CB  1 
ATOM   790  C CG  . GLN A 1 194 ? -23.183 16.108 14.941  1.00 31.44  ? 194 GLN A CG  1 
ATOM   791  C CD  . GLN A 1 194 ? -23.729 14.881 14.238  1.00 38.00  ? 194 GLN A CD  1 
ATOM   792  O OE1 . GLN A 1 194 ? -24.373 14.032 14.853  1.00 32.82  ? 194 GLN A OE1 1 
ATOM   793  N NE2 . GLN A 1 194 ? -23.467 14.780 12.940  1.00 31.06  ? 194 GLN A NE2 1 
ATOM   794  N N   . ILE A 1 195 ? -23.084 19.398 15.555  1.00 27.96  ? 195 ILE A N   1 
ATOM   795  C CA  . ILE A 1 195 ? -23.626 20.419 14.666  1.00 31.59  ? 195 ILE A CA  1 
ATOM   796  C C   . ILE A 1 195 ? -23.854 19.757 13.314  1.00 28.42  ? 195 ILE A C   1 
ATOM   797  O O   . ILE A 1 195 ? -22.899 19.439 12.600  1.00 28.70  ? 195 ILE A O   1 
ATOM   798  C CB  . ILE A 1 195 ? -22.691 21.627 14.546  1.00 34.75  ? 195 ILE A CB  1 
ATOM   799  C CG1 . ILE A 1 195 ? -22.271 22.114 15.933  1.00 29.92  ? 195 ILE A CG1 1 
ATOM   800  C CG2 . ILE A 1 195 ? -23.365 22.745 13.777  1.00 25.06  ? 195 ILE A CG2 1 
ATOM   801  C CD1 . ILE A 1 195 ? -23.437 22.505 16.802  1.00 25.25  ? 195 ILE A CD1 1 
ATOM   802  N N   . VAL A 1 196 ? -25.117 19.534 12.969  1.00 24.59  ? 196 VAL A N   1 
ATOM   803  C CA  . VAL A 1 196 ? -25.485 18.775 11.780  1.00 28.57  ? 196 VAL A CA  1 
ATOM   804  C C   . VAL A 1 196 ? -25.788 19.747 10.649  1.00 28.02  ? 196 VAL A C   1 
ATOM   805  O O   . VAL A 1 196 ? -26.480 20.753 10.854  1.00 33.66  ? 196 VAL A O   1 
ATOM   806  C CB  . VAL A 1 196 ? -26.688 17.859 12.063  1.00 32.73  ? 196 VAL A CB  1 
ATOM   807  C CG1 . VAL A 1 196 ? -27.041 17.039 10.835  1.00 29.59  ? 196 VAL A CG1 1 
ATOM   808  C CG2 . VAL A 1 196 ? -26.393 16.955 13.249  1.00 32.70  ? 196 VAL A CG2 1 
ATOM   809  N N   . VAL A 1 197 ? -25.265 19.455 9.461   1.00 35.54  ? 197 VAL A N   1 
ATOM   810  C CA  . VAL A 1 197 ? -25.530 20.244 8.263   1.00 31.24  ? 197 VAL A CA  1 
ATOM   811  C C   . VAL A 1 197 ? -26.521 19.474 7.402   1.00 30.89  ? 197 VAL A C   1 
ATOM   812  O O   . VAL A 1 197 ? -26.225 18.366 6.940   1.00 35.52  ? 197 VAL A O   1 
ATOM   813  C CB  . VAL A 1 197 ? -24.240 20.544 7.485   1.00 32.81  ? 197 VAL A CB  1 
ATOM   814  C CG1 . VAL A 1 197 ? -24.557 21.351 6.233   1.00 32.79  ? 197 VAL A CG1 1 
ATOM   815  C CG2 . VAL A 1 197 ? -23.256 21.291 8.360   1.00 28.17  ? 197 VAL A CG2 1 
ATOM   816  N N   . ALA A 1 198 ? -27.699 20.052 7.188   1.00 31.34  ? 198 ALA A N   1 
ATOM   817  C CA  . ALA A 1 198 ? -28.708 19.432 6.339   1.00 35.87  ? 198 ALA A CA  1 
ATOM   818  C C   . ALA A 1 198 ? -29.631 20.508 5.792   1.00 47.01  ? 198 ALA A C   1 
ATOM   819  O O   . ALA A 1 198 ? -30.077 21.381 6.545   1.00 55.99  ? 198 ALA A O   1 
ATOM   820  C CB  . ALA A 1 198 ? -29.520 18.383 7.106   1.00 34.10  ? 198 ALA A CB  1 
ATOM   821  N N   . SER A 1 199 ? -29.898 20.443 4.485   1.00 54.24  ? 199 SER A N   1 
ATOM   822  C CA  . SER A 1 199 ? -30.826 21.349 3.820   1.00 54.32  ? 199 SER A CA  1 
ATOM   823  C C   . SER A 1 199 ? -32.124 21.476 4.608   1.00 49.65  ? 199 SER A C   1 
ATOM   824  O O   . SER A 1 199 ? -32.604 20.498 5.191   1.00 55.44  ? 199 SER A O   1 
ATOM   825  C CB  . SER A 1 199 ? -31.108 20.860 2.399   1.00 57.54  ? 199 SER A CB  1 
ATOM   826  O OG  . SER A 1 199 ? -30.048 21.200 1.521   1.00 55.59  ? 199 SER A OG  1 
ATOM   827  N N   . ARG A 1 200 ? -32.682 22.679 4.650   1.00 60.00  ? 200 ARG A N   1 
ATOM   828  C CA  . ARG A 1 200 ? -33.890 22.942 5.417   1.00 66.97  ? 200 ARG A CA  1 
ATOM   829  C C   . ARG A 1 200 ? -35.130 22.534 4.630   1.00 65.17  ? 200 ARG A C   1 
ATOM   830  O O   . ARG A 1 200 ? -35.831 21.597 5.008   1.00 74.88  ? 200 ARG A O   1 
ATOM   831  C CB  . ARG A 1 200 ? -33.960 24.421 5.797   1.00 73.33  ? 200 ARG A CB  1 
ATOM   832  C CG  . ARG A 1 200 ? -33.653 25.336 4.626   1.00 71.42  ? 200 ARG A CG  1 
ATOM   833  C CD  . ARG A 1 200 ? -34.268 26.708 4.793   1.00 79.40  ? 200 ARG A CD  1 
ATOM   834  N NE  . ARG A 1 200 ? -34.204 27.461 3.547   1.00 75.84  ? 200 ARG A NE  1 
ATOM   835  C CZ  . ARG A 1 200 ? -35.229 28.105 3.007   1.00 82.87  ? 200 ARG A CZ  1 
ATOM   836  N NH1 . ARG A 1 200 ? -36.402 28.173 3.616   1.00 82.96  ? 200 ARG A NH1 1 
ATOM   837  N NH2 . ARG A 1 200 ? -35.072 28.704 1.830   1.00 74.48  ? 200 ARG A NH2 1 
ATOM   838  N N   . THR A 1 203 ? -35.635 16.603 6.283   1.00 65.54  ? 203 THR A N   1 
ATOM   839  C CA  . THR A 1 203 ? -35.624 16.132 7.664   1.00 80.72  ? 203 THR A CA  1 
ATOM   840  C C   . THR A 1 203 ? -34.604 15.002 7.848   1.00 79.48  ? 203 THR A C   1 
ATOM   841  O O   . THR A 1 203 ? -34.109 14.435 6.873   1.00 71.95  ? 203 THR A O   1 
ATOM   842  C CB  . THR A 1 203 ? -37.025 15.693 8.101   1.00 80.04  ? 203 THR A CB  1 
ATOM   843  O OG1 . THR A 1 203 ? -37.602 14.866 7.089   1.00 68.56  ? 203 THR A OG1 1 
ATOM   844  C CG2 . THR A 1 203 ? -37.912 16.918 8.330   1.00 72.39  ? 203 THR A CG2 1 
ATOM   845  N N   . LEU A 1 204 ? -34.312 14.675 9.106   1.00 74.44  ? 204 LEU A N   1 
ATOM   846  C CA  . LEU A 1 204 ? -33.044 14.061 9.487   1.00 62.64  ? 204 LEU A CA  1 
ATOM   847  C C   . LEU A 1 204 ? -33.205 12.567 9.748   1.00 58.29  ? 204 LEU A C   1 
ATOM   848  O O   . LEU A 1 204 ? -33.825 12.162 10.735  1.00 51.36  ? 204 LEU A O   1 
ATOM   849  C CB  . LEU A 1 204 ? -32.482 14.768 10.716  1.00 57.84  ? 204 LEU A CB  1 
ATOM   850  C CG  . LEU A 1 204 ? -31.719 16.057 10.404  1.00 58.55  ? 204 LEU A CG  1 
ATOM   851  C CD1 . LEU A 1 204 ? -31.532 16.865 11.663  1.00 57.83  ? 204 LEU A CD1 1 
ATOM   852  C CD2 . LEU A 1 204 ? -30.372 15.744 9.779   1.00 61.17  ? 204 LEU A CD2 1 
ATOM   853  N N   . LYS A 1 205 ? -32.616 11.756 8.874   1.00 54.32  ? 205 LYS A N   1 
ATOM   854  C CA  . LYS A 1 205 ? -32.597 10.316 9.057   1.00 45.35  ? 205 LYS A CA  1 
ATOM   855  C C   . LYS A 1 205 ? -31.539 9.932  10.089  1.00 35.29  ? 205 LYS A C   1 
ATOM   856  O O   . LYS A 1 205 ? -30.557 10.658 10.284  1.00 37.07  ? 205 LYS A O   1 
ATOM   857  C CB  . LYS A 1 205 ? -32.316 9.628  7.721   1.00 46.95  ? 205 LYS A CB  1 
ATOM   858  C CG  . LYS A 1 205 ? -30.972 10.009 7.113   1.00 48.89  ? 205 LYS A CG  1 
ATOM   859  C CD  . LYS A 1 205 ? -30.976 9.929  5.590   1.00 57.48  ? 205 LYS A CD  1 
ATOM   860  C CE  . LYS A 1 205 ? -30.807 8.505  5.093   1.00 63.31  ? 205 LYS A CE  1 
ATOM   861  N NZ  . LYS A 1 205 ? -31.198 8.364  3.663   1.00 69.01  ? 205 LYS A NZ  1 
ATOM   862  N N   . PRO A 1 206 ? -31.710 8.790  10.773  1.00 39.14  ? 206 PRO A N   1 
ATOM   863  C CA  . PRO A 1 206 ? -30.744 8.392  11.809  1.00 40.23  ? 206 PRO A CA  1 
ATOM   864  C C   . PRO A 1 206 ? -29.321 8.221  11.294  1.00 41.55  ? 206 PRO A C   1 
ATOM   865  O O   . PRO A 1 206 ? -28.373 8.213  12.084  1.00 31.06  ? 206 PRO A O   1 
ATOM   866  C CB  . PRO A 1 206 ? -31.300 7.058  12.330  1.00 33.69  ? 206 PRO A CB  1 
ATOM   867  C CG  . PRO A 1 206 ? -32.724 7.025  11.922  1.00 39.54  ? 206 PRO A CG  1 
ATOM   868  C CD  . PRO A 1 206 ? -32.876 7.888  10.709  1.00 36.66  ? 206 PRO A CD  1 
ATOM   869  N N   . GLU A 1 207 ? -29.154 8.078  9.978   1.00 34.17  ? 207 GLU A N   1 
ATOM   870  C CA  . GLU A 1 207 ? -27.818 7.897  9.420   1.00 30.29  ? 207 GLU A CA  1 
ATOM   871  C C   . GLU A 1 207 ? -26.985 9.173  9.445   1.00 33.93  ? 207 GLU A C   1 
ATOM   872  O O   . GLU A 1 207 ? -25.762 9.101  9.279   1.00 34.45  ? 207 GLU A O   1 
ATOM   873  C CB  . GLU A 1 207 ? -27.907 7.361  7.990   1.00 36.63  ? 207 GLU A CB  1 
ATOM   874  C CG  . GLU A 1 207 ? -28.355 5.914  7.901   1.00 37.53  ? 207 GLU A CG  1 
ATOM   875  C CD  . GLU A 1 207 ? -29.857 5.758  7.851   1.00 43.95  ? 207 GLU A CD  1 
ATOM   876  O OE1 . GLU A 1 207 ? -30.572 6.768  8.009   1.00 42.43  ? 207 GLU A OE1 1 
ATOM   877  O OE2 . GLU A 1 207 ? -30.330 4.621  7.652   1.00 44.54  ? 207 GLU A OE2 1 
ATOM   878  N N   . LEU A 1 208 ? -27.605 10.333 9.649   1.00 30.10  ? 208 LEU A N   1 
ATOM   879  C CA  . LEU A 1 208 ? -26.873 11.590 9.729   1.00 35.10  ? 208 LEU A CA  1 
ATOM   880  C C   . LEU A 1 208 ? -26.601 12.034 11.158  1.00 36.21  ? 208 LEU A C   1 
ATOM   881  O O   . LEU A 1 208 ? -25.926 13.049 11.356  1.00 38.89  ? 208 LEU A O   1 
ATOM   882  C CB  . LEU A 1 208 ? -27.640 12.702 8.999   1.00 41.93  ? 208 LEU A CB  1 
ATOM   883  C CG  . LEU A 1 208 ? -28.143 12.373 7.591   1.00 46.39  ? 208 LEU A CG  1 
ATOM   884  C CD1 . LEU A 1 208 ? -29.113 13.437 7.101   1.00 36.18  ? 208 LEU A CD1 1 
ATOM   885  C CD2 . LEU A 1 208 ? -26.984 12.213 6.622   1.00 29.59  ? 208 LEU A CD2 1 
ATOM   886  N N   . LEU A 1 209 ? -27.098 11.303 12.149  1.00 32.03  ? 209 LEU A N   1 
ATOM   887  C CA  . LEU A 1 209 ? -27.050 11.718 13.544  1.00 33.40  ? 209 LEU A CA  1 
ATOM   888  C C   . LEU A 1 209 ? -26.190 10.739 14.329  1.00 31.99  ? 209 LEU A C   1 
ATOM   889  O O   . LEU A 1 209 ? -26.461 9.534  14.333  1.00 35.96  ? 209 LEU A O   1 
ATOM   890  C CB  . LEU A 1 209 ? -28.459 11.787 14.129  1.00 36.46  ? 209 LEU A CB  1 
ATOM   891  C CG  . LEU A 1 209 ? -29.412 12.702 13.354  1.00 39.20  ? 209 LEU A CG  1 
ATOM   892  C CD1 . LEU A 1 209 ? -30.836 12.521 13.838  1.00 41.15  ? 209 LEU A CD1 1 
ATOM   893  C CD2 . LEU A 1 209 ? -28.981 14.153 13.483  1.00 40.43  ? 209 LEU A CD2 1 
ATOM   894  N N   . PHE A 1 210 ? -25.163 11.257 14.994  1.00 36.21  ? 210 PHE A N   1 
ATOM   895  C CA  . PHE A 1 210 ? -24.208 10.427 15.713  1.00 31.86  ? 210 PHE A CA  1 
ATOM   896  C C   . PHE A 1 210 ? -24.099 10.771 17.190  1.00 34.31  ? 210 PHE A C   1 
ATOM   897  O O   . PHE A 1 210 ? -23.351 10.099 17.909  1.00 35.35  ? 210 PHE A O   1 
ATOM   898  C CB  . PHE A 1 210 ? -22.821 10.532 15.058  1.00 28.08  ? 210 PHE A CB  1 
ATOM   899  C CG  . PHE A 1 210 ? -22.793 10.073 13.626  1.00 33.58  ? 210 PHE A CG  1 
ATOM   900  C CD1 . PHE A 1 210 ? -23.162 10.929 12.598  1.00 29.84  ? 210 PHE A CD1 1 
ATOM   901  C CD2 . PHE A 1 210 ? -22.392 8.787  13.308  1.00 29.80  ? 210 PHE A CD2 1 
ATOM   902  C CE1 . PHE A 1 210 ? -23.136 10.507 11.277  1.00 36.56  ? 210 PHE A CE1 1 
ATOM   903  C CE2 . PHE A 1 210 ? -22.360 8.359  11.990  1.00 35.31  ? 210 PHE A CE2 1 
ATOM   904  C CZ  . PHE A 1 210 ? -22.734 9.220  10.975  1.00 30.12  ? 210 PHE A CZ  1 
ATOM   905  N N   . SER A 1 211 ? -24.818 11.783 17.660  1.00 34.97  ? 211 SER A N   1 
ATOM   906  C CA  . SER A 1 211 ? -24.831 12.156 19.062  1.00 37.98  ? 211 SER A CA  1 
ATOM   907  C C   . SER A 1 211 ? -26.271 12.217 19.547  1.00 34.94  ? 211 SER A C   1 
ATOM   908  O O   . SER A 1 211 ? -27.211 12.340 18.760  1.00 37.99  ? 211 SER A O   1 
ATOM   909  C CB  . SER A 1 211 ? -24.137 13.503 19.284  1.00 35.37  ? 211 SER A CB  1 
ATOM   910  O OG  . SER A 1 211 ? -22.771 13.444 18.904  1.00 35.14  ? 211 SER A OG  1 
ATOM   911  N N   . LYS A 1 212 ? -26.437 12.123 20.865  1.00 40.34  ? 212 LYS A N   1 
ATOM   912  C CA  . LYS A 1 212 ? -27.775 12.181 21.444  1.00 37.57  ? 212 LYS A CA  1 
ATOM   913  C C   . LYS A 1 212 ? -28.424 13.541 21.215  1.00 34.27  ? 212 LYS A C   1 
ATOM   914  O O   . LYS A 1 212 ? -29.635 13.628 20.988  1.00 35.90  ? 212 LYS A O   1 
ATOM   915  C CB  . LYS A 1 212 ? -27.719 11.858 22.938  1.00 39.72  ? 212 LYS A CB  1 
ATOM   916  C CG  . LYS A 1 212 ? -27.771 10.374 23.244  1.00 46.42  ? 212 LYS A CG  1 
ATOM   917  C CD  . LYS A 1 212 ? -27.215 10.086 24.627  1.00 53.34  ? 212 LYS A CD  1 
ATOM   918  C CE  . LYS A 1 212 ? -26.439 8.779  24.667  1.00 58.98  ? 212 LYS A CE  1 
ATOM   919  N NZ  . LYS A 1 212 ? -27.350 7.603  24.702  1.00 61.87  ? 212 LYS A NZ  1 
ATOM   920  N N   . HIS A 1 213 ? -27.638 14.611 21.271  1.00 32.52  ? 213 HIS A N   1 
ATOM   921  C CA  . HIS A 1 213 ? -28.140 15.967 21.103  1.00 40.58  ? 213 HIS A CA  1 
ATOM   922  C C   . HIS A 1 213 ? -27.441 16.630 19.925  1.00 34.72  ? 213 HIS A C   1 
ATOM   923  O O   . HIS A 1 213 ? -26.256 16.386 19.675  1.00 34.01  ? 213 HIS A O   1 
ATOM   924  C CB  . HIS A 1 213 ? -27.937 16.796 22.378  1.00 32.55  ? 213 HIS A CB  1 
ATOM   925  C CG  . HIS A 1 213 ? -28.720 16.296 23.553  1.00 41.59  ? 213 HIS A CG  1 
ATOM   926  N ND1 . HIS A 1 213 ? -30.098 16.329 23.597  1.00 53.72  ? 213 HIS A ND1 1 
ATOM   927  C CD2 . HIS A 1 213 ? -28.323 15.734 24.719  1.00 42.29  ? 213 HIS A CD2 1 
ATOM   928  C CE1 . HIS A 1 213 ? -30.515 15.820 24.742  1.00 49.41  ? 213 HIS A CE1 1 
ATOM   929  N NE2 . HIS A 1 213 ? -29.458 15.450 25.441  1.00 56.92  ? 213 HIS A NE2 1 
ATOM   930  N N   . TYR A 1 214 ? -28.177 17.470 19.202  1.00 30.67  ? 214 TYR A N   1 
ATOM   931  C CA  . TYR A 1 214 ? -27.638 18.068 17.992  1.00 29.55  ? 214 TYR A CA  1 
ATOM   932  C C   . TYR A 1 214 ? -28.345 19.381 17.696  1.00 30.95  ? 214 TYR A C   1 
ATOM   933  O O   . TYR A 1 214 ? -29.498 19.596 18.083  1.00 29.73  ? 214 TYR A O   1 
ATOM   934  C CB  . TYR A 1 214 ? -27.764 17.117 16.792  1.00 26.46  ? 214 TYR A CB  1 
ATOM   935  C CG  . TYR A 1 214 ? -29.191 16.851 16.362  1.00 37.18  ? 214 TYR A CG  1 
ATOM   936  C CD1 . TYR A 1 214 ? -29.817 17.661 15.422  1.00 37.93  ? 214 TYR A CD1 1 
ATOM   937  C CD2 . TYR A 1 214 ? -29.912 15.791 16.896  1.00 32.76  ? 214 TYR A CD2 1 
ATOM   938  C CE1 . TYR A 1 214 ? -31.120 17.425 15.031  1.00 41.51  ? 214 TYR A CE1 1 
ATOM   939  C CE2 . TYR A 1 214 ? -31.218 15.544 16.504  1.00 36.23  ? 214 TYR A CE2 1 
ATOM   940  C CZ  . TYR A 1 214 ? -31.816 16.365 15.572  1.00 46.50  ? 214 TYR A CZ  1 
ATOM   941  O OH  . TYR A 1 214 ? -33.113 16.127 15.179  1.00 58.23  ? 214 TYR A OH  1 
ATOM   942  N N   . TRP A 1 215 ? -27.625 20.259 17.005  1.00 27.06  ? 215 TRP A N   1 
ATOM   943  C CA  . TRP A 1 215 ? -28.195 21.427 16.357  1.00 26.95  ? 215 TRP A CA  1 
ATOM   944  C C   . TRP A 1 215 ? -28.158 21.225 14.850  1.00 34.37  ? 215 TRP A C   1 
ATOM   945  O O   . TRP A 1 215 ? -27.305 20.504 14.324  1.00 30.12  ? 215 TRP A O   1 
ATOM   946  C CB  . TRP A 1 215 ? -27.430 22.699 16.708  1.00 27.54  ? 215 TRP A CB  1 
ATOM   947  C CG  . TRP A 1 215 ? -27.597 23.174 18.103  1.00 33.09  ? 215 TRP A CG  1 
ATOM   948  C CD1 . TRP A 1 215 ? -28.348 22.607 19.090  1.00 30.92  ? 215 TRP A CD1 1 
ATOM   949  C CD2 . TRP A 1 215 ? -26.969 24.318 18.680  1.00 33.23  ? 215 TRP A CD2 1 
ATOM   950  N NE1 . TRP A 1 215 ? -28.235 23.339 20.247  1.00 30.41  ? 215 TRP A NE1 1 
ATOM   951  C CE2 . TRP A 1 215 ? -27.391 24.395 20.021  1.00 35.76  ? 215 TRP A CE2 1 
ATOM   952  C CE3 . TRP A 1 215 ? -26.092 25.290 18.190  1.00 33.57  ? 215 TRP A CE3 1 
ATOM   953  C CZ2 . TRP A 1 215 ? -26.963 25.406 20.878  1.00 33.36  ? 215 TRP A CZ2 1 
ATOM   954  C CZ3 . TRP A 1 215 ? -25.671 26.287 19.039  1.00 39.25  ? 215 TRP A CZ3 1 
ATOM   955  C CH2 . TRP A 1 215 ? -26.106 26.341 20.366  1.00 37.73  ? 215 TRP A CH2 1 
ATOM   956  N N   . ARG A 1 216 ? -29.080 21.881 14.157  1.00 30.45  ? 216 ARG A N   1 
ATOM   957  C CA  . ARG A 1 216 ? -29.198 21.783 12.710  1.00 36.60  ? 216 ARG A CA  1 
ATOM   958  C C   . ARG A 1 216 ? -28.887 23.127 12.072  1.00 33.50  ? 216 ARG A C   1 
ATOM   959  O O   . ARG A 1 216 ? -29.386 24.163 12.519  1.00 38.65  ? 216 ARG A O   1 
ATOM   960  C CB  . ARG A 1 216 ? -30.600 21.311 12.318  1.00 38.12  ? 216 ARG A CB  1 
ATOM   961  C CG  . ARG A 1 216 ? -30.830 21.050 10.836  1.00 41.63  ? 216 ARG A CG  1 
ATOM   962  C CD  . ARG A 1 216 ? -32.313 20.776 10.607  1.00 40.72  ? 216 ARG A CD  1 
ATOM   963  N NE  . ARG A 1 216 ? -32.614 20.338 9.251   1.00 58.92  ? 216 ARG A NE  1 
ATOM   964  C CZ  . ARG A 1 216 ? -33.701 19.659 8.909   1.00 63.96  ? 216 ARG A CZ  1 
ATOM   965  N NH1 . ARG A 1 216 ? -34.562 19.225 9.817   1.00 63.14  ? 216 ARG A NH1 1 
ATOM   966  N NH2 . ARG A 1 216 ? -33.922 19.393 7.625   1.00 64.60  ? 216 ARG A NH2 1 
ATOM   967  N N   . THR A 1 217 ? -28.051 23.103 11.041  1.00 28.21  ? 217 THR A N   1 
ATOM   968  C CA  . THR A 1 217 ? -27.765 24.260 10.210  1.00 33.09  ? 217 THR A CA  1 
ATOM   969  C C   . THR A 1 217 ? -27.755 23.798 8.761   1.00 32.73  ? 217 THR A C   1 
ATOM   970  O O   . THR A 1 217 ? -27.640 22.604 8.479   1.00 30.65  ? 217 THR A O   1 
ATOM   971  C CB  . THR A 1 217 ? -26.428 24.915 10.570  1.00 28.26  ? 217 THR A CB  1 
ATOM   972  O OG1 . THR A 1 217 ? -26.312 26.167 9.883   1.00 44.59  ? 217 THR A OG1 1 
ATOM   973  C CG2 . THR A 1 217 ? -25.281 24.021 10.169  1.00 31.93  ? 217 THR A CG2 1 
ATOM   974  N N   . ASP A 1 218 ? -27.891 24.742 7.832   1.00 32.50  ? 218 ASP A N   1 
ATOM   975  C CA  . ASP A 1 218 ? -28.039 24.373 6.432   1.00 40.20  ? 218 ASP A CA  1 
ATOM   976  C C   . ASP A 1 218 ? -26.810 24.657 5.577   1.00 38.49  ? 218 ASP A C   1 
ATOM   977  O O   . ASP A 1 218 ? -26.894 24.527 4.356   1.00 36.01  ? 218 ASP A O   1 
ATOM   978  C CB  . ASP A 1 218 ? -29.274 25.053 5.820   1.00 36.10  ? 218 ASP A CB  1 
ATOM   979  C CG  . ASP A 1 218 ? -29.177 26.564 5.802   1.00 41.92  ? 218 ASP A CG  1 
ATOM   980  O OD1 . ASP A 1 218 ? -28.154 27.132 6.238   1.00 42.70  ? 218 ASP A OD1 1 
ATOM   981  O OD2 . ASP A 1 218 ? -30.145 27.199 5.331   1.00 40.69  ? 218 ASP A OD2 1 
ATOM   982  N N   . ASN A 1 219 ? -25.675 25.025 6.168   1.00 30.14  ? 219 ASN A N   1 
ATOM   983  C CA  . ASN A 1 219 ? -24.443 25.135 5.399   1.00 35.38  ? 219 ASN A CA  1 
ATOM   984  C C   . ASN A 1 219 ? -23.239 25.030 6.326   1.00 34.36  ? 219 ASN A C   1 
ATOM   985  O O   . ASN A 1 219 ? -23.336 25.233 7.538   1.00 34.62  ? 219 ASN A O   1 
ATOM   986  C CB  . ASN A 1 219 ? -24.393 26.430 4.577   1.00 39.00  ? 219 ASN A CB  1 
ATOM   987  C CG  . ASN A 1 219 ? -24.006 27.639 5.397   1.00 35.52  ? 219 ASN A CG  1 
ATOM   988  O OD1 . ASN A 1 219 ? -22.850 28.063 5.380   1.00 38.72  ? 219 ASN A OD1 1 
ATOM   989  N ND2 . ASN A 1 219 ? -24.971 28.214 6.103   1.00 42.82  ? 219 ASN A ND2 1 
ATOM   990  N N   . HIS A 1 220 ? -22.091 24.705 5.725   1.00 35.88  ? 220 HIS A N   1 
ATOM   991  C CA  . HIS A 1 220 ? -20.915 24.313 6.499   1.00 32.35  ? 220 HIS A CA  1 
ATOM   992  C C   . HIS A 1 220 ? -20.196 25.511 7.106   1.00 31.38  ? 220 HIS A C   1 
ATOM   993  O O   . HIS A 1 220 ? -19.492 25.361 8.110   1.00 31.14  ? 220 HIS A O   1 
ATOM   994  C CB  . HIS A 1 220 ? -19.959 23.509 5.618   1.00 27.86  ? 220 HIS A CB  1 
ATOM   995  C CG  . HIS A 1 220 ? -20.491 22.165 5.226   1.00 34.44  ? 220 HIS A CG  1 
ATOM   996  N ND1 . HIS A 1 220 ? -20.603 21.114 6.111   1.00 30.46  ? 220 HIS A ND1 1 
ATOM   997  C CD2 . HIS A 1 220 ? -20.972 21.712 4.044   1.00 24.89  ? 220 HIS A CD2 1 
ATOM   998  C CE1 . HIS A 1 220 ? -21.113 20.066 5.487   1.00 24.77  ? 220 HIS A CE1 1 
ATOM   999  N NE2 . HIS A 1 220 ? -21.347 20.404 4.233   1.00 36.90  ? 220 HIS A NE2 1 
ATOM   1000 N N   . HIS A 1 221 ? -20.344 26.697 6.514   1.00 33.18  ? 221 HIS A N   1 
ATOM   1001 C CA  . HIS A 1 221 ? -19.768 27.894 7.119   1.00 32.03  ? 221 HIS A CA  1 
ATOM   1002 C C   . HIS A 1 221 ? -20.418 28.180 8.465   1.00 27.86  ? 221 HIS A C   1 
ATOM   1003 O O   . HIS A 1 221 ? -19.731 28.428 9.461   1.00 30.34  ? 221 HIS A O   1 
ATOM   1004 C CB  . HIS A 1 221 ? -19.921 29.094 6.183   1.00 36.25  ? 221 HIS A CB  1 
ATOM   1005 C CG  . HIS A 1 221 ? -19.628 30.410 6.840   1.00 33.57  ? 221 HIS A CG  1 
ATOM   1006 N ND1 . HIS A 1 221 ? -18.354 30.806 7.188   1.00 28.44  ? 221 HIS A ND1 1 
ATOM   1007 C CD2 . HIS A 1 221 ? -20.451 31.415 7.222   1.00 34.66  ? 221 HIS A CD2 1 
ATOM   1008 C CE1 . HIS A 1 221 ? -18.404 31.999 7.752   1.00 29.08  ? 221 HIS A CE1 1 
ATOM   1009 N NE2 . HIS A 1 221 ? -19.664 32.391 7.785   1.00 35.73  ? 221 HIS A NE2 1 
ATOM   1010 N N   . SER A 1 222 ? -21.751 28.150 8.508   1.00 29.00  ? 222 SER A N   1 
ATOM   1011 C CA  . SER A 1 222 ? -22.457 28.330 9.771   1.00 35.74  ? 222 SER A CA  1 
ATOM   1012 C C   . SER A 1 222 ? -22.055 27.264 10.782  1.00 32.50  ? 222 SER A C   1 
ATOM   1013 O O   . SER A 1 222 ? -21.827 27.570 11.960  1.00 32.08  ? 222 SER A O   1 
ATOM   1014 C CB  . SER A 1 222 ? -23.964 28.305 9.527   1.00 34.82  ? 222 SER A CB  1 
ATOM   1015 O OG  . SER A 1 222 ? -24.363 29.407 8.735   1.00 43.44  ? 222 SER A OG  1 
ATOM   1016 N N   . ALA A 1 223 ? -21.957 26.006 10.342  1.00 27.98  ? 223 ALA A N   1 
ATOM   1017 C CA  . ALA A 1 223 ? -21.538 24.939 11.245  1.00 27.06  ? 223 ALA A CA  1 
ATOM   1018 C C   . ALA A 1 223 ? -20.118 25.172 11.745  1.00 34.08  ? 223 ALA A C   1 
ATOM   1019 O O   . ALA A 1 223 ? -19.832 25.004 12.937  1.00 29.56  ? 223 ALA A O   1 
ATOM   1020 C CB  . ALA A 1 223 ? -21.641 23.585 10.547  1.00 26.38  ? 223 ALA A CB  1 
ATOM   1021 N N   . CYS A 1 224 ? -19.213 25.565 10.841  1.00 27.06  ? 224 CYS A N   1 
ATOM   1022 C CA  . CYS A 1 224 ? -17.824 25.792 11.231  1.00 27.80  ? 224 CYS A CA  1 
ATOM   1023 C C   . CYS A 1 224 ? -17.708 26.912 12.258  1.00 29.02  ? 224 CYS A C   1 
ATOM   1024 O O   . CYS A 1 224 ? -16.941 26.800 13.222  1.00 30.88  ? 224 CYS A O   1 
ATOM   1025 C CB  . CYS A 1 224 ? -16.970 26.102 10.000  1.00 27.78  ? 224 CYS A CB  1 
ATOM   1026 S SG  . CYS A 1 224 ? -15.198 26.268 10.345  1.00 37.15  ? 224 CYS A SG  1 
ATOM   1027 N N   . LEU A 1 225 ? -18.468 27.997 12.075  1.00 30.08  ? 225 LEU A N   1 
ATOM   1028 C CA  . LEU A 1 225 ? -18.444 29.094 13.041  1.00 28.38  ? 225 LEU A CA  1 
ATOM   1029 C C   . LEU A 1 225 ? -18.820 28.618 14.441  1.00 28.72  ? 225 LEU A C   1 
ATOM   1030 O O   . LEU A 1 225 ? -18.204 29.028 15.432  1.00 37.69  ? 225 LEU A O   1 
ATOM   1031 C CB  . LEU A 1 225 ? -19.388 30.211 12.596  1.00 25.82  ? 225 LEU A CB  1 
ATOM   1032 C CG  . LEU A 1 225 ? -18.918 31.151 11.487  1.00 37.42  ? 225 LEU A CG  1 
ATOM   1033 C CD1 . LEU A 1 225 ? -20.009 32.154 11.160  1.00 33.66  ? 225 LEU A CD1 1 
ATOM   1034 C CD2 . LEU A 1 225 ? -17.641 31.876 11.887  1.00 32.80  ? 225 LEU A CD2 1 
ATOM   1035 N N   . MET A 1 226 ? -19.827 27.747 14.541  1.00 30.56  ? 226 MET A N   1 
ATOM   1036 C CA  . MET A 1 226 ? -20.293 27.292 15.847  1.00 36.54  ? 226 MET A CA  1 
ATOM   1037 C C   . MET A 1 226 ? -19.369 26.233 16.437  1.00 37.02  ? 226 MET A C   1 
ATOM   1038 O O   . MET A 1 226 ? -19.220 26.161 17.663  1.00 32.25  ? 226 MET A O   1 
ATOM   1039 C CB  . MET A 1 226 ? -21.727 26.776 15.727  1.00 30.50  ? 226 MET A CB  1 
ATOM   1040 C CG  . MET A 1 226 ? -22.745 27.901 15.597  1.00 38.06  ? 226 MET A CG  1 
ATOM   1041 S SD  . MET A 1 226 ? -24.460 27.351 15.573  1.00 47.56  ? 226 MET A SD  1 
ATOM   1042 C CE  . MET A 1 226 ? -24.467 26.333 14.101  1.00 45.81  ? 226 MET A CE  1 
ATOM   1043 N N   . ILE A 1 227 ? -18.729 25.419 15.592  1.00 28.05  ? 227 ILE A N   1 
ATOM   1044 C CA  . ILE A 1 227 ? -17.678 24.529 16.079  1.00 33.24  ? 227 ILE A CA  1 
ATOM   1045 C C   . ILE A 1 227 ? -16.498 25.341 16.607  1.00 34.53  ? 227 ILE A C   1 
ATOM   1046 O O   . ILE A 1 227 ? -15.874 24.978 17.610  1.00 35.32  ? 227 ILE A O   1 
ATOM   1047 C CB  . ILE A 1 227 ? -17.242 23.556 14.968  1.00 30.79  ? 227 ILE A CB  1 
ATOM   1048 C CG1 . ILE A 1 227 ? -18.413 22.663 14.553  1.00 33.70  ? 227 ILE A CG1 1 
ATOM   1049 C CG2 . ILE A 1 227 ? -16.074 22.697 15.429  1.00 28.20  ? 227 ILE A CG2 1 
ATOM   1050 C CD1 . ILE A 1 227 ? -18.207 21.963 13.245  1.00 29.58  ? 227 ILE A CD1 1 
ATOM   1051 N N   . LEU A 1 228 ? -16.179 26.455 15.941  1.00 30.83  ? 228 LEU A N   1 
ATOM   1052 C CA  . LEU A 1 228 ? -15.083 27.302 16.407  1.00 34.19  ? 228 LEU A CA  1 
ATOM   1053 C C   . LEU A 1 228 ? -15.391 27.946 17.754  1.00 29.69  ? 228 LEU A C   1 
ATOM   1054 O O   . LEU A 1 228 ? -14.466 28.261 18.513  1.00 32.72  ? 228 LEU A O   1 
ATOM   1055 C CB  . LEU A 1 228 ? -14.765 28.376 15.366  1.00 27.84  ? 228 LEU A CB  1 
ATOM   1056 C CG  . LEU A 1 228 ? -14.104 27.936 14.061  1.00 31.50  ? 228 LEU A CG  1 
ATOM   1057 C CD1 . LEU A 1 228 ? -14.196 29.047 13.038  1.00 27.31  ? 228 LEU A CD1 1 
ATOM   1058 C CD2 . LEU A 1 228 ? -12.657 27.570 14.293  1.00 25.41  ? 228 LEU A CD2 1 
ATOM   1059 N N   . ARG A 1 229 ? -16.668 28.153 18.073  1.00 29.72  ? 229 ARG A N   1 
ATOM   1060 C CA  . ARG A 1 229 ? -17.068 28.688 19.369  1.00 33.09  ? 229 ARG A CA  1 
ATOM   1061 C C   . ARG A 1 229 ? -17.210 27.606 20.440  1.00 29.15  ? 229 ARG A C   1 
ATOM   1062 O O   . ARG A 1 229 ? -17.756 27.886 21.513  1.00 31.82  ? 229 ARG A O   1 
ATOM   1063 C CB  . ARG A 1 229 ? -18.383 29.465 19.244  1.00 27.78  ? 229 ARG A CB  1 
ATOM   1064 C CG  . ARG A 1 229 ? -18.383 30.599 18.225  1.00 39.75  ? 229 ARG A CG  1 
ATOM   1065 C CD  . ARG A 1 229 ? -17.357 31.676 18.536  1.00 35.52  ? 229 ARG A CD  1 
ATOM   1066 N NE  . ARG A 1 229 ? -17.524 32.229 19.875  1.00 42.61  ? 229 ARG A NE  1 
ATOM   1067 C CZ  . ARG A 1 229 ? -18.082 33.402 20.147  1.00 44.24  ? 229 ARG A CZ  1 
ATOM   1068 N NH1 . ARG A 1 229 ? -18.637 34.144 19.201  1.00 40.39  ? 229 ARG A NH1 1 
ATOM   1069 N NH2 . ARG A 1 229 ? -18.095 33.836 21.404  1.00 37.27  ? 229 ARG A NH2 1 
ATOM   1070 N N   . ASN A 1 230 ? -16.735 26.386 20.170  1.00 28.43  ? 230 ASN A N   1 
ATOM   1071 C CA  . ASN A 1 230 ? -16.775 25.268 21.116  1.00 32.37  ? 230 ASN A CA  1 
ATOM   1072 C C   . ASN A 1 230 ? -18.200 24.827 21.429  1.00 35.47  ? 230 ASN A C   1 
ATOM   1073 O O   . ASN A 1 230 ? -18.466 24.283 22.502  1.00 34.10  ? 230 ASN A O   1 
ATOM   1074 C CB  . ASN A 1 230 ? -16.040 25.599 22.419  1.00 28.89  ? 230 ASN A CB  1 
ATOM   1075 C CG  . ASN A 1 230 ? -14.563 25.818 22.209  1.00 37.83  ? 230 ASN A CG  1 
ATOM   1076 O OD1 . ASN A 1 230 ? -14.038 25.541 21.141  1.00 41.24  ? 230 ASN A OD1 1 
ATOM   1077 N ND2 . ASN A 1 230 ? -13.885 26.323 23.228  1.00 42.72  ? 230 ASN A ND2 1 
ATOM   1078 N N   . LEU A 1 231 ? -19.129 25.063 20.507  1.00 27.80  ? 231 LEU A N   1 
ATOM   1079 C CA  . LEU A 1 231 ? -20.511 24.666 20.729  1.00 31.17  ? 231 LEU A CA  1 
ATOM   1080 C C   . LEU A 1 231 ? -20.768 23.207 20.375  1.00 28.87  ? 231 LEU A C   1 
ATOM   1081 O O   . LEU A 1 231 ? -21.874 22.716 20.622  1.00 33.10  ? 231 LEU A O   1 
ATOM   1082 C CB  . LEU A 1 231 ? -21.454 25.575 19.935  1.00 31.33  ? 231 LEU A CB  1 
ATOM   1083 C CG  . LEU A 1 231 ? -21.470 27.044 20.373  1.00 35.14  ? 231 LEU A CG  1 
ATOM   1084 C CD1 . LEU A 1 231 ? -22.265 27.901 19.403  1.00 31.30  ? 231 LEU A CD1 1 
ATOM   1085 C CD2 . LEU A 1 231 ? -22.022 27.171 21.779  1.00 30.95  ? 231 LEU A CD2 1 
ATOM   1086 N N   . GLY A 1 232 ? -19.786 22.510 19.820  1.00 32.35  ? 232 GLY A N   1 
ATOM   1087 C CA  . GLY A 1 232 ? -19.942 21.103 19.512  1.00 27.91  ? 232 GLY A CA  1 
ATOM   1088 C C   . GLY A 1 232 ? -18.944 20.656 18.463  1.00 34.37  ? 232 GLY A C   1 
ATOM   1089 O O   . GLY A 1 232 ? -18.026 21.387 18.092  1.00 30.69  ? 232 GLY A O   1 
ATOM   1090 N N   . TRP A 1 233 ? -19.141 19.422 18.005  1.00 23.89  ? 233 TRP A N   1 
ATOM   1091 C CA  . TRP A 1 233 ? -18.374 18.850 16.911  1.00 30.13  ? 233 TRP A CA  1 
ATOM   1092 C C   . TRP A 1 233 ? -19.260 18.724 15.680  1.00 26.30  ? 233 TRP A C   1 
ATOM   1093 O O   . TRP A 1 233 ? -20.488 18.806 15.752  1.00 32.18  ? 233 TRP A O   1 
ATOM   1094 C CB  . TRP A 1 233 ? -17.793 17.485 17.295  1.00 25.59  ? 233 TRP A CB  1 
ATOM   1095 C CG  . TRP A 1 233 ? -18.818 16.395 17.372  1.00 32.92  ? 233 TRP A CG  1 
ATOM   1096 C CD1 . TRP A 1 233 ? -19.642 16.114 18.422  1.00 30.77  ? 233 TRP A CD1 1 
ATOM   1097 C CD2 . TRP A 1 233 ? -19.151 15.457 16.340  1.00 28.81  ? 233 TRP A CD2 1 
ATOM   1098 N NE1 . TRP A 1 233 ? -20.453 15.047 18.116  1.00 27.04  ? 233 TRP A NE1 1 
ATOM   1099 C CE2 . TRP A 1 233 ? -20.173 14.627 16.843  1.00 31.82  ? 233 TRP A CE2 1 
ATOM   1100 C CE3 . TRP A 1 233 ? -18.678 15.235 15.043  1.00 26.98  ? 233 TRP A CE3 1 
ATOM   1101 C CZ2 . TRP A 1 233 ? -20.730 13.593 16.095  1.00 34.60  ? 233 TRP A CZ2 1 
ATOM   1102 C CZ3 . TRP A 1 233 ? -19.234 14.205 14.300  1.00 34.52  ? 233 TRP A CZ3 1 
ATOM   1103 C CH2 . TRP A 1 233 ? -20.248 13.398 14.828  1.00 34.78  ? 233 TRP A CH2 1 
ATOM   1104 N N   . GLY A 1 234 ? -18.619 18.520 14.537  1.00 30.37  ? 234 GLY A N   1 
ATOM   1105 C CA  . GLY A 1 234 ? -19.356 18.435 13.291  1.00 26.09  ? 234 GLY A CA  1 
ATOM   1106 C C   . GLY A 1 234 ? -18.474 17.949 12.165  1.00 30.51  ? 234 GLY A C   1 
ATOM   1107 O O   . GLY A 1 234 ? -17.262 17.781 12.323  1.00 35.56  ? 234 GLY A O   1 
ATOM   1108 N N   . VAL A 1 235 ? -19.112 17.741 11.014  1.00 30.17  ? 235 VAL A N   1 
ATOM   1109 C CA  . VAL A 1 235 ? -18.469 17.166 9.840   1.00 28.49  ? 235 VAL A CA  1 
ATOM   1110 C C   . VAL A 1 235 ? -18.366 18.247 8.774   1.00 29.32  ? 235 VAL A C   1 
ATOM   1111 O O   . VAL A 1 235 ? -19.384 18.799 8.341   1.00 29.34  ? 235 VAL A O   1 
ATOM   1112 C CB  . VAL A 1 235 ? -19.243 15.945 9.327   1.00 35.17  ? 235 VAL A CB  1 
ATOM   1113 C CG1 . VAL A 1 235 ? -18.597 15.405 8.064   1.00 33.58  ? 235 VAL A CG1 1 
ATOM   1114 C CG2 . VAL A 1 235 ? -19.317 14.880 10.404  1.00 32.61  ? 235 VAL A CG2 1 
ATOM   1115 N N   . LEU A 1 236 ? -17.141 18.532 8.341   1.00 30.67  ? 236 LEU A N   1 
ATOM   1116 C CA  . LEU A 1 236 ? -16.836 19.612 7.413   1.00 29.18  ? 236 LEU A CA  1 
ATOM   1117 C C   . LEU A 1 236 ? -16.096 19.084 6.223   1.00 29.55  ? 236 LEU A C   1 
ATOM   1118 O O   . LEU A 1 236 ? -15.317 18.117 6.325   1.00 30.06  ? 236 LEU A O   1 
ATOM   1119 C CB  . LEU A 1 236 ? -15.993 20.696 8.105   1.00 29.94  ? 236 LEU A CB  1 
ATOM   1120 C CG  . LEU A 1 236 ? -16.584 21.406 9.325   1.00 31.85  ? 236 LEU A CG  1 
ATOM   1121 C CD1 . LEU A 1 236 ? -15.656 22.519 9.784   1.00 26.40  ? 236 LEU A CD1 1 
ATOM   1122 C CD2 . LEU A 1 236 ? -17.969 21.948 9.022   1.00 28.96  ? 236 LEU A CD2 1 
ATOM   1123 N N   . PRO A 1 237 ? -16.286 19.668 5.036   1.00 32.78  ? 237 PRO A N   1 
ATOM   1124 C CA  . PRO A 1 237 ? -15.507 19.272 3.870   1.00 30.36  ? 237 PRO A CA  1 
ATOM   1125 C C   . PRO A 1 237 ? -14.023 19.561 4.069   1.00 31.01  ? 237 PRO A C   1 
ATOM   1126 O O   . PRO A 1 237 ? -13.643 20.611 4.594   1.00 29.53  ? 237 PRO A O   1 
ATOM   1127 C CB  . PRO A 1 237 ? -16.093 20.109 2.730   1.00 29.20  ? 237 PRO A CB  1 
ATOM   1128 C CG  . PRO A 1 237 ? -17.442 20.547 3.230   1.00 36.14  ? 237 PRO A CG  1 
ATOM   1129 C CD  . PRO A 1 237 ? -17.267 20.724 4.706   1.00 27.68  ? 237 PRO A CD  1 
ATOM   1130 N N   . GLN A 1 238 ? -13.189 18.606 3.649   1.00 30.19  ? 238 GLN A N   1 
ATOM   1131 C CA  . GLN A 1 238 ? -11.743 18.817 3.618   1.00 37.85  ? 238 GLN A CA  1 
ATOM   1132 C C   . GLN A 1 238 ? -11.390 20.068 2.822   1.00 35.68  ? 238 GLN A C   1 
ATOM   1133 O O   . GLN A 1 238 ? -10.389 20.736 3.107   1.00 36.02  ? 238 GLN A O   1 
ATOM   1134 C CB  . GLN A 1 238 ? -11.061 17.584 3.017   1.00 34.97  ? 238 GLN A CB  1 
ATOM   1135 C CG  . GLN A 1 238 ? -9.534  17.616 2.935   1.00 44.13  ? 238 GLN A CG  1 
ATOM   1136 C CD  . GLN A 1 238 ? -8.867  18.004 4.241   1.00 59.98  ? 238 GLN A CD  1 
ATOM   1137 O OE1 . GLN A 1 238 ? -9.148  17.423 5.290   1.00 57.85  ? 238 GLN A OE1 1 
ATOM   1138 N NE2 . GLN A 1 238 ? -7.941  18.952 4.173   1.00 57.44  ? 238 GLN A NE2 1 
ATOM   1139 N N   . GLU A 1 239 ? -12.214 20.394 1.819   1.00 37.40  ? 239 GLU A N   1 
ATOM   1140 C CA  . GLU A 1 239 ? -12.010 21.583 0.993   1.00 36.87  ? 239 GLU A CA  1 
ATOM   1141 C C   . GLU A 1 239 ? -11.925 22.862 1.818   1.00 42.04  ? 239 GLU A C   1 
ATOM   1142 O O   . GLU A 1 239 ? -11.187 23.788 1.461   1.00 36.51  ? 239 GLU A O   1 
ATOM   1143 C CB  . GLU A 1 239 ? -13.141 21.689 -0.032  1.00 40.89  ? 239 GLU A CB  1 
ATOM   1144 C CG  . GLU A 1 239 ? -13.083 22.898 -0.966  1.00 42.34  ? 239 GLU A CG  1 
ATOM   1145 C CD  . GLU A 1 239 ? -11.841 22.948 -1.835  1.00 50.02  ? 239 GLU A CD  1 
ATOM   1146 O OE1 . GLU A 1 239 ? -11.231 21.889 -2.087  1.00 53.70  ? 239 GLU A OE1 1 
ATOM   1147 O OE2 . GLU A 1 239 ? -11.484 24.054 -2.292  1.00 52.30  ? 239 GLU A OE2 1 
ATOM   1148 N N   . MET A 1 240 ? -12.682 22.944 2.913   1.00 31.62  ? 240 MET A N   1 
ATOM   1149 C CA  . MET A 1 240 ? -12.659 24.152 3.734   1.00 34.78  ? 240 MET A CA  1 
ATOM   1150 C C   . MET A 1 240 ? -11.278 24.418 4.316   1.00 33.84  ? 240 MET A C   1 
ATOM   1151 O O   . MET A 1 240 ? -10.900 25.579 4.511   1.00 34.51  ? 240 MET A O   1 
ATOM   1152 C CB  . MET A 1 240 ? -13.686 24.054 4.863   1.00 33.25  ? 240 MET A CB  1 
ATOM   1153 C CG  . MET A 1 240 ? -15.124 24.205 4.409   1.00 29.57  ? 240 MET A CG  1 
ATOM   1154 S SD  . MET A 1 240 ? -16.275 24.233 5.798   1.00 40.10  ? 240 MET A SD  1 
ATOM   1155 C CE  . MET A 1 240 ? -16.127 25.937 6.329   1.00 35.21  ? 240 MET A CE  1 
ATOM   1156 N N   . PHE A 1 241 ? -10.513 23.367 4.597   1.00 32.91  ? 241 PHE A N   1 
ATOM   1157 C CA  . PHE A 1 241 ? -9.179  23.557 5.151   1.00 35.90  ? 241 PHE A CA  1 
ATOM   1158 C C   . PHE A 1 241 ? -8.174  23.949 4.077   1.00 41.70  ? 241 PHE A C   1 
ATOM   1159 O O   . PHE A 1 241 ? -7.174  24.608 4.379   1.00 41.09  ? 241 PHE A O   1 
ATOM   1160 C CB  . PHE A 1 241 ? -8.736  22.289 5.881   1.00 37.85  ? 241 PHE A CB  1 
ATOM   1161 C CG  . PHE A 1 241 ? -9.560  21.983 7.102   1.00 36.46  ? 241 PHE A CG  1 
ATOM   1162 C CD1 . PHE A 1 241 ? -10.778 21.331 6.984   1.00 38.02  ? 241 PHE A CD1 1 
ATOM   1163 C CD2 . PHE A 1 241 ? -9.125  22.354 8.364   1.00 39.56  ? 241 PHE A CD2 1 
ATOM   1164 C CE1 . PHE A 1 241 ? -11.544 21.050 8.100   1.00 33.18  ? 241 PHE A CE1 1 
ATOM   1165 C CE2 . PHE A 1 241 ? -9.887  22.075 9.486   1.00 32.67  ? 241 PHE A CE2 1 
ATOM   1166 C CZ  . PHE A 1 241 ? -11.098 21.422 9.352   1.00 37.21  ? 241 PHE A CZ  1 
ATOM   1167 N N   . LYS A 1 242 ? -8.420  23.565 2.824   1.00 32.47  ? 242 LYS A N   1 
ATOM   1168 C CA  . LYS A 1 242 ? -7.625  24.102 1.726   1.00 42.43  ? 242 LYS A CA  1 
ATOM   1169 C C   . LYS A 1 242 ? -7.912  25.584 1.529   1.00 38.63  ? 242 LYS A C   1 
ATOM   1170 O O   . LYS A 1 242 ? -6.990  26.397 1.402   1.00 43.74  ? 242 LYS A O   1 
ATOM   1171 C CB  . LYS A 1 242 ? -7.901  23.329 0.432   1.00 43.37  ? 242 LYS A CB  1 
ATOM   1172 C CG  . LYS A 1 242 ? -7.313  21.925 0.387   1.00 56.18  ? 242 LYS A CG  1 
ATOM   1173 C CD  . LYS A 1 242 ? -8.020  21.077 -0.664  1.00 70.00  ? 242 LYS A CD  1 
ATOM   1174 C CE  . LYS A 1 242 ? -8.590  19.795 -0.075  1.00 71.16  ? 242 LYS A CE  1 
ATOM   1175 N NZ  . LYS A 1 242 ? -9.426  19.055 -1.067  1.00 71.23  ? 242 LYS A NZ  1 
ATOM   1176 N N   . GLU A 1 243 ? -9.192  25.954 1.509   1.00 35.83  ? 243 GLU A N   1 
ATOM   1177 C CA  . GLU A 1 243 ? -9.553  27.344 1.256   1.00 43.35  ? 243 GLU A CA  1 
ATOM   1178 C C   . GLU A 1 243 ? -9.184  28.256 2.418   1.00 45.00  ? 243 GLU A C   1 
ATOM   1179 O O   . GLU A 1 243 ? -8.862  29.429 2.197   1.00 38.59  ? 243 GLU A O   1 
ATOM   1180 C CB  . GLU A 1 243 ? -11.047 27.457 0.954   1.00 40.54  ? 243 GLU A CB  1 
ATOM   1181 C CG  . GLU A 1 243 ? -11.480 26.780 -0.327  1.00 42.26  ? 243 GLU A CG  1 
ATOM   1182 C CD  . GLU A 1 243 ? -12.985 26.755 -0.475  1.00 47.94  ? 243 GLU A CD  1 
ATOM   1183 O OE1 . GLU A 1 243 ? -13.680 27.245 0.440   1.00 60.45  ? 243 GLU A OE1 1 
ATOM   1184 O OE2 . GLU A 1 243 ? -13.473 26.250 -1.507  1.00 52.91  ? 243 GLU A OE2 1 
ATOM   1185 N N   . ASN A 1 244 ? -9.223  27.757 3.651   1.00 36.17  ? 244 ASN A N   1 
ATOM   1186 C CA  . ASN A 1 244 ? -8.928  28.582 4.819   1.00 34.42  ? 244 ASN A CA  1 
ATOM   1187 C C   . ASN A 1 244 ? -7.910  27.882 5.699   1.00 40.76  ? 244 ASN A C   1 
ATOM   1188 O O   . ASN A 1 244 ? -8.260  27.063 6.568   1.00 32.61  ? 244 ASN A O   1 
ATOM   1189 C CB  . ASN A 1 244 ? -10.195 28.903 5.593   1.00 33.42  ? 244 ASN A CB  1 
ATOM   1190 C CG  . ASN A 1 244 ? -9.991  29.992 6.621   1.00 39.56  ? 244 ASN A CG  1 
ATOM   1191 O OD1 . ASN A 1 244 ? -8.889  30.483 6.805   1.00 35.62  ? 244 ASN A OD1 1 
ATOM   1192 N ND2 . ASN A 1 244 ? -11.077 30.399 7.279   1.00 40.82  ? 244 ASN A ND2 1 
ATOM   1193 N N   . PRO A 1 245 ? -6.622  28.178 5.519   1.00 41.62  ? 245 PRO A N   1 
ATOM   1194 C CA  . PRO A 1 245 ? -5.604  27.507 6.346   1.00 34.83  ? 245 PRO A CA  1 
ATOM   1195 C C   . PRO A 1 245 ? -5.749  27.815 7.833   1.00 39.00  ? 245 PRO A C   1 
ATOM   1196 O O   . PRO A 1 245 ? -5.317  27.017 8.678   1.00 41.42  ? 245 PRO A O   1 
ATOM   1197 C CB  . PRO A 1 245 ? -4.255  28.031 5.801   1.00 51.28  ? 245 PRO A CB  1 
ATOM   1198 C CG  . PRO A 1 245 ? -4.579  28.855 4.611   1.00 48.13  ? 245 PRO A CG  1 
ATOM   1199 C CD  . PRO A 1 245 ? -6.028  29.205 4.646   1.00 38.75  ? 245 PRO A CD  1 
ATOM   1200 N N   . GLU A 1 246 ? -6.384  28.945 8.172   1.00 38.22  ? 246 GLU A N   1 
ATOM   1201 C CA  . GLU A 1 246 ? -6.641  29.306 9.564   1.00 42.34  ? 246 GLU A CA  1 
ATOM   1202 C C   . GLU A 1 246 ? -7.348  28.193 10.326  1.00 40.22  ? 246 GLU A C   1 
ATOM   1203 O O   . GLU A 1 246 ? -7.121  28.029 11.528  1.00 40.86  ? 246 GLU A O   1 
ATOM   1204 C CB  . GLU A 1 246 ? -7.477  30.588 9.612   1.00 40.78  ? 246 GLU A CB  1 
ATOM   1205 C CG  . GLU A 1 246 ? -7.696  31.169 11.002  1.00 53.71  ? 246 GLU A CG  1 
ATOM   1206 C CD  . GLU A 1 246 ? -6.415  31.638 11.665  1.00 61.31  ? 246 GLU A CD  1 
ATOM   1207 O OE1 . GLU A 1 246 ? -5.438  31.960 10.956  1.00 59.48  ? 246 GLU A OE1 1 
ATOM   1208 O OE2 . GLU A 1 246 ? -6.390  31.694 12.910  1.00 64.49  ? 246 GLU A OE2 1 
ATOM   1209 N N   . LEU A 1 247 ? -8.196  27.415 9.647   1.00 35.76  ? 247 LEU A N   1 
ATOM   1210 C CA  . LEU A 1 247 ? -8.983  26.389 10.328  1.00 40.27  ? 247 LEU A CA  1 
ATOM   1211 C C   . LEU A 1 247 ? -8.103  25.307 10.942  1.00 38.82  ? 247 LEU A C   1 
ATOM   1212 O O   . LEU A 1 247 ? -8.472  24.719 11.964  1.00 36.44  ? 247 LEU A O   1 
ATOM   1213 C CB  . LEU A 1 247 ? -9.987  25.780 9.350   1.00 34.76  ? 247 LEU A CB  1 
ATOM   1214 C CG  . LEU A 1 247 ? -11.075 26.729 8.837   1.00 33.50  ? 247 LEU A CG  1 
ATOM   1215 C CD1 . LEU A 1 247 ? -12.057 26.012 7.921   1.00 37.22  ? 247 LEU A CD1 1 
ATOM   1216 C CD2 . LEU A 1 247 ? -11.807 27.401 9.990   1.00 35.50  ? 247 LEU A CD2 1 
ATOM   1217 N N   . ASN A 1 248 ? -6.942  25.028 10.343  1.00 36.82  ? 248 ASN A N   1 
ATOM   1218 C CA  . ASN A 1 248 ? -6.017  24.074 10.944  1.00 38.28  ? 248 ASN A CA  1 
ATOM   1219 C C   . ASN A 1 248 ? -5.414  24.594 12.246  1.00 42.01  ? 248 ASN A C   1 
ATOM   1220 O O   . ASN A 1 248 ? -5.027  23.787 13.097  1.00 42.87  ? 248 ASN A O   1 
ATOM   1221 C CB  . ASN A 1 248 ? -4.904  23.708 9.954   1.00 46.00  ? 248 ASN A CB  1 
ATOM   1222 C CG  . ASN A 1 248 ? -5.380  22.764 8.853   1.00 48.75  ? 248 ASN A CG  1 
ATOM   1223 O OD1 . ASN A 1 248 ? -5.435  23.135 7.678   1.00 53.90  ? 248 ASN A OD1 1 
ATOM   1224 N ND2 . ASN A 1 248 ? -5.720  21.536 9.232   1.00 56.53  ? 248 ASN A ND2 1 
ATOM   1225 N N   . ASN A 1 249 ? -5.332  25.915 12.429  1.00 38.89  ? 249 ASN A N   1 
ATOM   1226 C CA  . ASN A 1 249 ? -4.847  26.457 13.694  1.00 42.50  ? 249 ASN A CA  1 
ATOM   1227 C C   . ASN A 1 249 ? -5.864  26.304 14.810  1.00 39.12  ? 249 ASN A C   1 
ATOM   1228 O O   . ASN A 1 249 ? -5.486  26.294 15.987  1.00 40.81  ? 249 ASN A O   1 
ATOM   1229 C CB  . ASN A 1 249 ? -4.486  27.936 13.534  1.00 39.48  ? 249 ASN A CB  1 
ATOM   1230 C CG  . ASN A 1 249 ? -3.677  28.194 12.287  1.00 46.82  ? 249 ASN A CG  1 
ATOM   1231 O OD1 . ASN A 1 249 ? -2.969  27.306 11.813  1.00 45.83  ? 249 ASN A OD1 1 
ATOM   1232 N ND2 . ASN A 1 249 ? -3.766  29.403 11.748  1.00 41.68  ? 249 ASN A ND2 1 
ATOM   1233 N N   . LYS A 1 250 ? -7.140  26.177 14.463  1.00 41.79  ? 250 LYS A N   1 
ATOM   1234 C CA  . LYS A 1 250 ? -8.220  26.201 15.435  1.00 35.93  ? 250 LYS A CA  1 
ATOM   1235 C C   . LYS A 1 250 ? -8.902  24.859 15.625  1.00 37.45  ? 250 LYS A C   1 
ATOM   1236 O O   . LYS A 1 250 ? -9.346  24.561 16.735  1.00 32.79  ? 250 LYS A O   1 
ATOM   1237 C CB  . LYS A 1 250 ? -9.282  27.220 15.010  1.00 36.41  ? 250 LYS A CB  1 
ATOM   1238 C CG  . LYS A 1 250 ? -8.815  28.661 14.948  1.00 37.00  ? 250 LYS A CG  1 
ATOM   1239 C CD  . LYS A 1 250 ? -8.098  29.091 16.210  1.00 54.45  ? 250 LYS A CD  1 
ATOM   1240 C CE  . LYS A 1 250 ? -8.077  30.607 16.321  1.00 65.71  ? 250 LYS A CE  1 
ATOM   1241 N NZ  . LYS A 1 250 ? -6.700  31.137 16.518  1.00 59.16  ? 250 LYS A NZ  1 
ATOM   1242 N N   . LEU A 1 251 ? -9.018  24.055 14.573  1.00 35.83  ? 251 LEU A N   1 
ATOM   1243 C CA  . LEU A 1 251 ? -9.773  22.812 14.610  1.00 28.43  ? 251 LEU A CA  1 
ATOM   1244 C C   . LEU A 1 251 ? -8.842  21.616 14.456  1.00 31.68  ? 251 LEU A C   1 
ATOM   1245 O O   . LEU A 1 251 ? -7.792  21.703 13.814  1.00 33.04  ? 251 LEU A O   1 
ATOM   1246 C CB  . LEU A 1 251 ? -10.837 22.790 13.507  1.00 33.90  ? 251 LEU A CB  1 
ATOM   1247 C CG  . LEU A 1 251 ? -11.860 23.925 13.475  1.00 38.48  ? 251 LEU A CG  1 
ATOM   1248 C CD1 . LEU A 1 251 ? -12.828 23.740 12.316  1.00 29.01  ? 251 LEU A CD1 1 
ATOM   1249 C CD2 . LEU A 1 251 ? -12.619 24.016 14.793  1.00 36.17  ? 251 LEU A CD2 1 
ATOM   1250 N N   . LYS A 1 252 ? -9.231  20.499 15.065  1.00 34.60  ? 252 LYS A N   1 
ATOM   1251 C CA  . LYS A 1 252 ? -8.525  19.238 14.901  1.00 32.43  ? 252 LYS A CA  1 
ATOM   1252 C C   . LYS A 1 252 ? -9.504  18.171 14.433  1.00 35.04  ? 252 LYS A C   1 
ATOM   1253 O O   . LYS A 1 252 ? -10.696 18.215 14.752  1.00 35.33  ? 252 LYS A O   1 
ATOM   1254 C CB  . LYS A 1 252 ? -7.854  18.771 16.201  1.00 42.06  ? 252 LYS A CB  1 
ATOM   1255 C CG  . LYS A 1 252 ? -8.827  18.473 17.333  1.00 43.21  ? 252 LYS A CG  1 
ATOM   1256 C CD  . LYS A 1 252 ? -8.224  17.496 18.333  1.00 43.76  ? 252 LYS A CD  1 
ATOM   1257 C CE  . LYS A 1 252 ? -6.900  17.990 18.875  1.00 54.04  ? 252 LYS A CE  1 
ATOM   1258 N NZ  . LYS A 1 252 ? -6.820  17.850 20.357  1.00 64.16  ? 252 LYS A NZ  1 
ATOM   1259 N N   . ALA A 1 253 ? -8.998  17.212 13.664  1.00 36.59  ? 253 ALA A N   1 
ATOM   1260 C CA  . ALA A 1 253 ? -9.814  16.061 13.308  1.00 40.96  ? 253 ALA A CA  1 
ATOM   1261 C C   . ALA A 1 253 ? -10.041 15.201 14.544  1.00 38.26  ? 253 ALA A C   1 
ATOM   1262 O O   . ALA A 1 253 ? -9.145  15.031 15.375  1.00 42.47  ? 253 ALA A O   1 
ATOM   1263 C CB  . ALA A 1 253 ? -9.141  15.246 12.201  1.00 32.41  ? 253 ALA A CB  1 
ATOM   1264 N N   . LEU A 1 254 ? -11.256 14.680 14.681  1.00 42.60  ? 254 LEU A N   1 
ATOM   1265 C CA  . LEU A 1 254 ? -11.557 13.793 15.795  1.00 39.66  ? 254 LEU A CA  1 
ATOM   1266 C C   . LEU A 1 254 ? -10.842 12.460 15.615  1.00 45.86  ? 254 LEU A C   1 
ATOM   1267 O O   . LEU A 1 254 ? -10.889 11.858 14.538  1.00 46.30  ? 254 LEU A O   1 
ATOM   1268 C CB  . LEU A 1 254 ? -13.065 13.565 15.905  1.00 38.57  ? 254 LEU A CB  1 
ATOM   1269 C CG  . LEU A 1 254 ? -13.938 14.605 16.611  1.00 39.75  ? 254 LEU A CG  1 
ATOM   1270 C CD1 . LEU A 1 254 ? -15.405 14.254 16.454  1.00 40.35  ? 254 LEU A CD1 1 
ATOM   1271 C CD2 . LEU A 1 254 ? -13.591 14.698 18.085  1.00 46.03  ? 254 LEU A CD2 1 
ATOM   1272 N N   . ASP A 1 255 ? -10.164 12.008 16.667  1.00 52.71  ? 255 ASP A N   1 
ATOM   1273 C CA  . ASP A 1 255 ? -9.632  10.651 16.737  1.00 56.73  ? 255 ASP A CA  1 
ATOM   1274 C C   . ASP A 1 255 ? -10.279 9.985  17.943  1.00 67.26  ? 255 ASP A C   1 
ATOM   1275 O O   . ASP A 1 255 ? -9.939  10.300 19.091  1.00 66.72  ? 255 ASP A O   1 
ATOM   1276 C CB  . ASP A 1 255 ? -8.107  10.634 16.837  1.00 57.71  ? 255 ASP A CB  1 
ATOM   1277 C CG  . ASP A 1 255 ? -7.545  9.226  16.805  1.00 67.77  ? 255 ASP A CG  1 
ATOM   1278 O OD1 . ASP A 1 255 ? -7.807  8.512  15.813  1.00 69.77  ? 255 ASP A OD1 1 
ATOM   1279 O OD2 . ASP A 1 255 ? -6.845  8.829  17.760  1.00 80.31  ? 255 ASP A OD2 1 
ATOM   1280 N N   . VAL A 1 256 ? -11.215 9.075  17.676  1.00 55.89  ? 256 VAL A N   1 
ATOM   1281 C CA  . VAL A 1 256 ? -12.082 8.499  18.696  1.00 50.26  ? 256 VAL A CA  1 
ATOM   1282 C C   . VAL A 1 256 ? -12.106 6.993  18.484  1.00 56.91  ? 256 VAL A C   1 
ATOM   1283 O O   . VAL A 1 256 ? -12.321 6.529  17.362  1.00 55.37  ? 256 VAL A O   1 
ATOM   1284 C CB  . VAL A 1 256 ? -13.514 9.065  18.608  1.00 57.84  ? 256 VAL A CB  1 
ATOM   1285 C CG1 . VAL A 1 256 ? -14.399 8.479  19.707  1.00 51.72  ? 256 VAL A CG1 1 
ATOM   1286 C CG2 . VAL A 1 256 ? -13.520 10.589 18.585  1.00 51.58  ? 256 VAL A CG2 1 
ATOM   1287 N N   . PHE A 1 257 ? -11.904 6.230  19.556  1.00 58.68  ? 257 PHE A N   1 
ATOM   1288 C CA  . PHE A 1 257 ? -11.895 4.778  19.445  1.00 60.90  ? 257 PHE A CA  1 
ATOM   1289 C C   . PHE A 1 257 ? -13.320 4.265  19.265  1.00 57.67  ? 257 PHE A C   1 
ATOM   1290 O O   . PHE A 1 257 ? -14.248 4.737  19.931  1.00 57.04  ? 257 PHE A O   1 
ATOM   1291 C CB  . PHE A 1 257 ? -11.238 4.147  20.675  1.00 63.25  ? 257 PHE A CB  1 
ATOM   1292 C CG  . PHE A 1 257 ? -10.982 2.672  20.529  1.00 71.82  ? 257 PHE A CG  1 
ATOM   1293 C CD1 . PHE A 1 257 ? -10.244 2.193  19.458  1.00 74.94  ? 257 PHE A CD1 1 
ATOM   1294 C CD2 . PHE A 1 257 ? -11.474 1.766  21.453  1.00 69.87  ? 257 PHE A CD2 1 
ATOM   1295 C CE1 . PHE A 1 257 ? -10.004 0.842  19.307  1.00 75.40  ? 257 PHE A CE1 1 
ATOM   1296 C CE2 . PHE A 1 257 ? -11.237 0.408  21.309  1.00 77.55  ? 257 PHE A CE2 1 
ATOM   1297 C CZ  . PHE A 1 257 ? -10.499 -0.053 20.232  1.00 79.61  ? 257 PHE A CZ  1 
ATOM   1298 N N   . ASP A 1 258 ? -13.483 3.301  18.353  1.00 56.85  ? 258 ASP A N   1 
ATOM   1299 C CA  . ASP A 1 258 ? -14.765 2.724  17.944  1.00 54.35  ? 258 ASP A CA  1 
ATOM   1300 C C   . ASP A 1 258 ? -15.631 3.701  17.160  1.00 50.42  ? 258 ASP A C   1 
ATOM   1301 O O   . ASP A 1 258 ? -16.834 3.469  16.995  1.00 48.68  ? 258 ASP A O   1 
ATOM   1302 C CB  . ASP A 1 258 ? -15.562 2.178  19.135  1.00 53.88  ? 258 ASP A CB  1 
ATOM   1303 C CG  . ASP A 1 258 ? -14.866 1.026  19.820  1.00 67.53  ? 258 ASP A CG  1 
ATOM   1304 O OD1 . ASP A 1 258 ? -14.437 0.088  19.120  1.00 64.81  ? 258 ASP A OD1 1 
ATOM   1305 O OD2 . ASP A 1 258 ? -14.763 1.052  21.063  1.00 74.50  ? 258 ASP A OD2 1 
ATOM   1306 N N   . PHE A 1 259 ? -15.044 4.790  16.665  1.00 44.70  ? 259 PHE A N   1 
ATOM   1307 C CA  . PHE A 1 259 ? -15.766 5.806  15.899  1.00 51.72  ? 259 PHE A CA  1 
ATOM   1308 C C   . PHE A 1 259 ? -15.034 5.992  14.574  1.00 45.32  ? 259 PHE A C   1 
ATOM   1309 O O   . PHE A 1 259 ? -14.176 6.870  14.440  1.00 47.96  ? 259 PHE A O   1 
ATOM   1310 C CB  . PHE A 1 259 ? -15.874 7.110  16.680  1.00 47.78  ? 259 PHE A CB  1 
ATOM   1311 C CG  . PHE A 1 259 ? -16.812 8.107  16.063  1.00 42.21  ? 259 PHE A CG  1 
ATOM   1312 C CD1 . PHE A 1 259 ? -18.161 7.817  15.934  1.00 43.01  ? 259 PHE A CD1 1 
ATOM   1313 C CD2 . PHE A 1 259 ? -16.353 9.342  15.635  1.00 46.31  ? 259 PHE A CD2 1 
ATOM   1314 C CE1 . PHE A 1 259 ? -19.033 8.734  15.374  1.00 39.66  ? 259 PHE A CE1 1 
ATOM   1315 C CE2 . PHE A 1 259 ? -17.218 10.265 15.077  1.00 42.48  ? 259 PHE A CE2 1 
ATOM   1316 C CZ  . PHE A 1 259 ? -18.560 9.961  14.947  1.00 37.60  ? 259 PHE A CZ  1 
ATOM   1317 N N   . THR A 1 260 ? -15.385 5.167  13.590  1.00 42.11  ? 260 THR A N   1 
ATOM   1318 C CA  . THR A 1 260 ? -14.697 5.191  12.306  1.00 46.92  ? 260 THR A CA  1 
ATOM   1319 C C   . THR A 1 260 ? -15.607 5.320  11.078  1.00 37.67  ? 260 THR A C   1 
ATOM   1320 O O   . THR A 1 260 ? -15.312 4.714  10.038  1.00 37.87  ? 260 THR A O   1 
ATOM   1321 C CB  . THR A 1 260 ? -13.811 3.934  12.221  1.00 43.83  ? 260 THR A CB  1 
ATOM   1322 O OG1 . THR A 1 260 ? -12.766 4.119  11.253  1.00 67.88  ? 260 THR A OG1 1 
ATOM   1323 C CG2 . THR A 1 260 ? -14.623 2.643  11.969  1.00 45.94  ? 260 THR A CG2 1 
ATOM   1324 N N   . PRO A 1 261 ? -16.669 6.131  11.101  1.00 42.17  ? 261 PRO A N   1 
ATOM   1325 C CA  . PRO A 1 261 ? -17.527 6.222  9.917   1.00 41.57  ? 261 PRO A CA  1 
ATOM   1326 C C   . PRO A 1 261 ? -16.841 6.990  8.796   1.00 41.37  ? 261 PRO A C   1 
ATOM   1327 O O   . PRO A 1 261 ? -15.895 7.753  9.006   1.00 42.91  ? 261 PRO A O   1 
ATOM   1328 C CB  . PRO A 1 261 ? -18.761 6.970  10.425  1.00 34.41  ? 261 PRO A CB  1 
ATOM   1329 C CG  . PRO A 1 261 ? -18.217 7.845  11.483  1.00 46.81  ? 261 PRO A CG  1 
ATOM   1330 C CD  . PRO A 1 261 ? -17.148 7.036  12.168  1.00 40.84  ? 261 PRO A CD  1 
ATOM   1331 N N   . ARG A 1 262 ? -17.337 6.771  7.582   1.00 37.41  ? 262 ARG A N   1 
ATOM   1332 C CA  . ARG A 1 262 ? -16.822 7.436  6.393   1.00 34.53  ? 262 ARG A CA  1 
ATOM   1333 C C   . ARG A 1 262 ? -17.818 8.497  5.943   1.00 38.77  ? 262 ARG A C   1 
ATOM   1334 O O   . ARG A 1 262 ? -18.985 8.187  5.681   1.00 38.23  ? 262 ARG A O   1 
ATOM   1335 C CB  . ARG A 1 262 ? -16.573 6.438  5.263   1.00 36.40  ? 262 ARG A CB  1 
ATOM   1336 C CG  . ARG A 1 262 ? -16.380 7.096  3.905   1.00 36.67  ? 262 ARG A CG  1 
ATOM   1337 C CD  . ARG A 1 262 ? -15.021 7.773  3.854   1.00 40.88  ? 262 ARG A CD  1 
ATOM   1338 N NE  . ARG A 1 262 ? -13.947 6.804  3.669   1.00 48.10  ? 262 ARG A NE  1 
ATOM   1339 C CZ  . ARG A 1 262 ? -13.632 6.249  2.506   1.00 48.40  ? 262 ARG A CZ  1 
ATOM   1340 N NH1 . ARG A 1 262 ? -14.236 6.604  1.383   1.00 44.72  ? 262 ARG A NH1 1 
ATOM   1341 N NH2 . ARG A 1 262 ? -12.679 5.321  2.467   1.00 47.33  ? 262 ARG A NH2 1 
ATOM   1342 N N   . PHE A 1 263 ? -17.357 9.740  5.839   1.00 34.48  ? 263 PHE A N   1 
ATOM   1343 C CA  . PHE A 1 263 ? -18.180 10.850 5.376   1.00 29.08  ? 263 PHE A CA  1 
ATOM   1344 C C   . PHE A 1 263 ? -17.668 11.316 4.021   1.00 32.36  ? 263 PHE A C   1 
ATOM   1345 O O   . PHE A 1 263 ? -16.482 11.624 3.875   1.00 34.91  ? 263 PHE A O   1 
ATOM   1346 C CB  . PHE A 1 263 ? -18.168 11.999 6.383   1.00 30.00  ? 263 PHE A CB  1 
ATOM   1347 C CG  . PHE A 1 263 ? -18.606 11.599 7.761   1.00 36.34  ? 263 PHE A CG  1 
ATOM   1348 C CD1 . PHE A 1 263 ? -19.949 11.398 8.040   1.00 39.21  ? 263 PHE A CD1 1 
ATOM   1349 C CD2 . PHE A 1 263 ? -17.680 11.431 8.779   1.00 32.89  ? 263 PHE A CD2 1 
ATOM   1350 C CE1 . PHE A 1 263 ? -20.360 11.031 9.305   1.00 35.93  ? 263 PHE A CE1 1 
ATOM   1351 C CE2 . PHE A 1 263 ? -18.086 11.064 10.047  1.00 33.11  ? 263 PHE A CE2 1 
ATOM   1352 C CZ  . PHE A 1 263 ? -19.428 10.865 10.308  1.00 32.78  ? 263 PHE A CZ  1 
ATOM   1353 N N   . GLU A 1 264 ? -18.565 11.381 3.043   1.00 34.88  ? 264 GLU A N   1 
ATOM   1354 C CA  . GLU A 1 264 ? -18.205 11.769 1.687   1.00 34.69  ? 264 GLU A CA  1 
ATOM   1355 C C   . GLU A 1 264 ? -19.474 12.127 0.930   1.00 37.72  ? 264 GLU A C   1 
ATOM   1356 O O   . GLU A 1 264 ? -20.567 11.647 1.246   1.00 33.51  ? 264 GLU A O   1 
ATOM   1357 C CB  . GLU A 1 264 ? -17.443 10.650 0.970   1.00 33.31  ? 264 GLU A CB  1 
ATOM   1358 C CG  . GLU A 1 264 ? -18.314 9.466  0.585   1.00 34.05  ? 264 GLU A CG  1 
ATOM   1359 C CD  . GLU A 1 264 ? -17.509 8.210  0.340   1.00 37.73  ? 264 GLU A CD  1 
ATOM   1360 O OE1 . GLU A 1 264 ? -16.278 8.239  0.556   1.00 35.73  ? 264 GLU A OE1 1 
ATOM   1361 O OE2 . GLU A 1 264 ? -18.104 7.185  -0.057  1.00 44.74  ? 264 GLU A OE2 1 
ATOM   1362 N N   . TYR A 1 265 ? -19.319 13.002 -0.058  1.00 39.26  ? 265 TYR A N   1 
ATOM   1363 C CA  . TYR A 1 265 ? -20.363 13.276 -1.033  1.00 37.22  ? 265 TYR A CA  1 
ATOM   1364 C C   . TYR A 1 265 ? -19.911 12.781 -2.396  1.00 40.26  ? 265 TYR A C   1 
ATOM   1365 O O   . TYR A 1 265 ? -18.760 12.992 -2.793  1.00 40.86  ? 265 TYR A O   1 
ATOM   1366 C CB  . TYR A 1 265 ? -20.692 14.768 -1.160  1.00 32.52  ? 265 TYR A CB  1 
ATOM   1367 C CG  . TYR A 1 265 ? -21.202 15.465 0.079   1.00 35.71  ? 265 TYR A CG  1 
ATOM   1368 C CD1 . TYR A 1 265 ? -22.290 14.976 0.790   1.00 41.40  ? 265 TYR A CD1 1 
ATOM   1369 C CD2 . TYR A 1 265 ? -20.625 16.655 0.501   1.00 33.90  ? 265 TYR A CD2 1 
ATOM   1370 C CE1 . TYR A 1 265 ? -22.761 15.639 1.916   1.00 37.67  ? 265 TYR A CE1 1 
ATOM   1371 C CE2 . TYR A 1 265 ? -21.087 17.320 1.615   1.00 37.75  ? 265 TYR A CE2 1 
ATOM   1372 C CZ  . TYR A 1 265 ? -22.154 16.813 2.321   1.00 34.11  ? 265 TYR A CZ  1 
ATOM   1373 O OH  . TYR A 1 265 ? -22.606 17.484 3.434   1.00 47.53  ? 265 TYR A OH  1 
ATOM   1374 N N   . TYR A 1 266 ? -20.823 12.145 -3.121  1.00 36.27  ? 266 TYR A N   1 
ATOM   1375 C CA  . TYR A 1 266 ? -20.646 11.940 -4.552  1.00 38.43  ? 266 TYR A CA  1 
ATOM   1376 C C   . TYR A 1 266 ? -21.456 13.007 -5.273  1.00 37.09  ? 266 TYR A C   1 
ATOM   1377 O O   . TYR A 1 266 ? -22.691 13.008 -5.217  1.00 45.09  ? 266 TYR A O   1 
ATOM   1378 C CB  . TYR A 1 266 ? -21.049 10.528 -4.963  1.00 33.23  ? 266 TYR A CB  1 
ATOM   1379 C CG  . TYR A 1 266 ? -19.944 9.542  -4.694  1.00 38.94  ? 266 TYR A CG  1 
ATOM   1380 C CD1 . TYR A 1 266 ? -18.940 9.329  -5.629  1.00 32.49  ? 266 TYR A CD1 1 
ATOM   1381 C CD2 . TYR A 1 266 ? -19.878 8.853  -3.491  1.00 41.36  ? 266 TYR A CD2 1 
ATOM   1382 C CE1 . TYR A 1 266 ? -17.912 8.442  -5.381  1.00 42.44  ? 266 TYR A CE1 1 
ATOM   1383 C CE2 . TYR A 1 266 ? -18.852 7.962  -3.235  1.00 37.06  ? 266 TYR A CE2 1 
ATOM   1384 C CZ  . TYR A 1 266 ? -17.872 7.760  -4.182  1.00 33.33  ? 266 TYR A CZ  1 
ATOM   1385 O OH  . TYR A 1 266 ? -16.850 6.876  -3.931  1.00 38.34  ? 266 TYR A OH  1 
ATOM   1386 N N   . VAL A 1 267 ? -20.754 13.923 -5.931  1.00 31.72  ? 267 VAL A N   1 
ATOM   1387 C CA  . VAL A 1 267 ? -21.363 15.099 -6.537  1.00 32.00  ? 267 VAL A CA  1 
ATOM   1388 C C   . VAL A 1 267 ? -21.780 14.766 -7.961  1.00 37.00  ? 267 VAL A C   1 
ATOM   1389 O O   . VAL A 1 267 ? -20.973 14.261 -8.753  1.00 32.67  ? 267 VAL A O   1 
ATOM   1390 C CB  . VAL A 1 267 ? -20.391 16.290 -6.510  1.00 30.50  ? 267 VAL A CB  1 
ATOM   1391 C CG1 . VAL A 1 267 ? -21.044 17.524 -7.116  1.00 30.36  ? 267 VAL A CG1 1 
ATOM   1392 C CG2 . VAL A 1 267 ? -19.921 16.559 -5.083  1.00 35.10  ? 267 VAL A CG2 1 
ATOM   1393 N N   . ASP A 1 268 ? -23.040 15.043 -8.287  1.00 36.48  ? 268 ASP A N   1 
ATOM   1394 C CA  . ASP A 1 268 ? -23.568 14.838 -9.624  1.00 34.44  ? 268 ASP A CA  1 
ATOM   1395 C C   . ASP A 1 268 ? -23.900 16.182 -10.255 1.00 38.78  ? 268 ASP A C   1 
ATOM   1396 O O   . ASP A 1 268 ? -24.264 17.140 -9.566  1.00 30.38  ? 268 ASP A O   1 
ATOM   1397 C CB  . ASP A 1 268 ? -24.823 13.964 -9.602  1.00 37.69  ? 268 ASP A CB  1 
ATOM   1398 C CG  . ASP A 1 268 ? -24.587 12.619 -8.960  1.00 48.64  ? 268 ASP A CG  1 
ATOM   1399 O OD1 . ASP A 1 268 ? -23.525 12.015 -9.209  1.00 47.41  ? 268 ASP A OD1 1 
ATOM   1400 O OD2 . ASP A 1 268 ? -25.471 12.159 -8.207  1.00 63.65  ? 268 ASP A OD2 1 
ATOM   1401 N N   . LEU A 1 269 ? -23.755 16.248 -11.574 1.00 30.08  ? 269 LEU A N   1 
ATOM   1402 C CA  . LEU A 1 269 ? -24.243 17.369 -12.366 1.00 33.75  ? 269 LEU A CA  1 
ATOM   1403 C C   . LEU A 1 269 ? -25.603 16.983 -12.934 1.00 33.57  ? 269 LEU A C   1 
ATOM   1404 O O   . LEU A 1 269 ? -25.702 16.024 -13.706 1.00 33.16  ? 269 LEU A O   1 
ATOM   1405 C CB  . LEU A 1 269 ? -23.269 17.722 -13.490 1.00 29.49  ? 269 LEU A CB  1 
ATOM   1406 C CG  . LEU A 1 269 ? -23.695 18.881 -14.394 1.00 37.54  ? 269 LEU A CG  1 
ATOM   1407 C CD1 . LEU A 1 269 ? -23.614 20.215 -13.665 1.00 29.27  ? 269 LEU A CD1 1 
ATOM   1408 C CD2 . LEU A 1 269 ? -22.850 18.907 -15.656 1.00 32.97  ? 269 LEU A CD2 1 
ATOM   1409 N N   . VAL A 1 270 ? -26.641 17.729 -12.562 1.00 29.37  ? 270 VAL A N   1 
ATOM   1410 C CA  . VAL A 1 270 ? -28.019 17.330 -12.817 1.00 29.23  ? 270 VAL A CA  1 
ATOM   1411 C C   . VAL A 1 270 ? -28.706 18.394 -13.663 1.00 27.04  ? 270 VAL A C   1 
ATOM   1412 O O   . VAL A 1 270 ? -28.443 19.589 -13.508 1.00 29.75  ? 270 VAL A O   1 
ATOM   1413 C CB  . VAL A 1 270 ? -28.776 17.103 -11.492 1.00 32.41  ? 270 VAL A CB  1 
ATOM   1414 C CG1 . VAL A 1 270 ? -30.188 16.573 -11.745 1.00 32.23  ? 270 VAL A CG1 1 
ATOM   1415 C CG2 . VAL A 1 270 ? -27.991 16.162 -10.587 1.00 28.18  ? 270 VAL A CG2 1 
ATOM   1416 N N   . TRP A 1 271 ? -29.580 17.948 -14.565 1.00 31.89  ? 271 TRP A N   1 
ATOM   1417 C CA  . TRP A 1 271 ? -30.393 18.833 -15.388 1.00 33.36  ? 271 TRP A CA  1 
ATOM   1418 C C   . TRP A 1 271 ? -31.730 18.159 -15.674 1.00 35.79  ? 271 TRP A C   1 
ATOM   1419 O O   . TRP A 1 271 ? -31.927 16.971 -15.397 1.00 35.02  ? 271 TRP A O   1 
ATOM   1420 C CB  . TRP A 1 271 ? -29.685 19.194 -16.701 1.00 34.34  ? 271 TRP A CB  1 
ATOM   1421 C CG  . TRP A 1 271 ? -29.444 18.031 -17.626 1.00 36.87  ? 271 TRP A CG  1 
ATOM   1422 C CD1 . TRP A 1 271 ? -30.239 17.624 -18.661 1.00 37.21  ? 271 TRP A CD1 1 
ATOM   1423 C CD2 . TRP A 1 271 ? -28.326 17.135 -17.605 1.00 29.92  ? 271 TRP A CD2 1 
ATOM   1424 N NE1 . TRP A 1 271 ? -29.685 16.528 -19.281 1.00 38.12  ? 271 TRP A NE1 1 
ATOM   1425 C CE2 . TRP A 1 271 ? -28.511 16.208 -18.651 1.00 39.40  ? 271 TRP A CE2 1 
ATOM   1426 C CE3 . TRP A 1 271 ? -27.187 17.024 -16.800 1.00 33.53  ? 271 TRP A CE3 1 
ATOM   1427 C CZ2 . TRP A 1 271 ? -27.601 15.186 -18.914 1.00 34.31  ? 271 TRP A CZ2 1 
ATOM   1428 C CZ3 . TRP A 1 271 ? -26.285 16.008 -17.063 1.00 37.23  ? 271 TRP A CZ3 1 
ATOM   1429 C CH2 . TRP A 1 271 ? -26.497 15.103 -18.112 1.00 37.24  ? 271 TRP A CH2 1 
ATOM   1430 N N   . SER A 1 272 ? -32.655 18.934 -16.234 1.00 35.10  ? 272 SER A N   1 
ATOM   1431 C CA  . SER A 1 272 ? -33.986 18.443 -16.564 1.00 38.49  ? 272 SER A CA  1 
ATOM   1432 C C   . SER A 1 272 ? -34.007 17.934 -18.000 1.00 44.93  ? 272 SER A C   1 
ATOM   1433 O O   . SER A 1 272 ? -33.603 18.647 -18.922 1.00 48.14  ? 272 SER A O   1 
ATOM   1434 C CB  . SER A 1 272 ? -35.023 19.550 -16.370 1.00 42.40  ? 272 SER A CB  1 
ATOM   1435 O OG  . SER A 1 272 ? -36.283 19.179 -16.907 1.00 51.69  ? 272 SER A OG  1 
ATOM   1436 N N   . ARG A 1 273 ? -34.481 16.701 -18.187 1.00 49.47  ? 273 ARG A N   1 
ATOM   1437 C CA  . ARG A 1 273 ? -34.515 16.129 -19.529 1.00 59.68  ? 273 ARG A CA  1 
ATOM   1438 C C   . ARG A 1 273 ? -35.545 16.803 -20.426 1.00 64.50  ? 273 ARG A C   1 
ATOM   1439 O O   . ARG A 1 273 ? -35.444 16.697 -21.653 1.00 68.84  ? 273 ARG A O   1 
ATOM   1440 C CB  . ARG A 1 273 ? -34.791 14.624 -19.458 1.00 64.82  ? 273 ARG A CB  1 
ATOM   1441 C CG  . ARG A 1 273 ? -36.225 14.261 -19.113 1.00 74.33  ? 273 ARG A CG  1 
ATOM   1442 C CD  . ARG A 1 273 ? -36.477 12.772 -19.313 1.00 78.07  ? 273 ARG A CD  1 
ATOM   1443 N NE  . ARG A 1 273 ? -35.522 11.959 -18.569 1.00 84.98  ? 273 ARG A NE  1 
ATOM   1444 C CZ  . ARG A 1 273 ? -34.568 11.222 -19.122 1.00 88.96  ? 273 ARG A CZ  1 
ATOM   1445 N NH1 . ARG A 1 273 ? -34.442 11.125 -20.436 1.00 90.84  ? 273 ARG A NH1 1 
ATOM   1446 N NH2 . ARG A 1 273 ? -33.724 10.559 -18.337 1.00 89.46  ? 273 ARG A NH2 1 
ATOM   1447 N N   . GLU A 1 274 ? -36.521 17.502 -19.850 1.00 62.35  ? 274 GLU A N   1 
ATOM   1448 C CA  . GLU A 1 274 ? -37.561 18.151 -20.634 1.00 67.03  ? 274 GLU A CA  1 
ATOM   1449 C C   . GLU A 1 274 ? -37.302 19.633 -20.873 1.00 69.59  ? 274 GLU A C   1 
ATOM   1450 O O   . GLU A 1 274 ? -38.026 20.250 -21.661 1.00 76.64  ? 274 GLU A O   1 
ATOM   1451 C CB  . GLU A 1 274 ? -38.920 17.966 -19.955 1.00 78.32  ? 274 GLU A CB  1 
ATOM   1452 C CG  . GLU A 1 274 ? -39.369 16.516 -19.895 1.00 83.65  ? 274 GLU A CG  1 
ATOM   1453 C CD  . GLU A 1 274 ? -40.475 16.296 -18.889 1.00 91.68  ? 274 GLU A CD  1 
ATOM   1454 O OE1 . GLU A 1 274 ? -40.209 16.436 -17.676 1.00 90.07  ? 274 GLU A OE1 1 
ATOM   1455 O OE2 . GLU A 1 274 ? -41.610 15.980 -19.305 1.00 97.24  ? 274 GLU A OE2 1 
ATOM   1456 N N   . SER A 1 275 ? -36.304 20.216 -20.219 1.00 67.52  ? 275 SER A N   1 
ATOM   1457 C CA  . SER A 1 275 ? -35.887 21.579 -20.503 1.00 68.11  ? 275 SER A CA  1 
ATOM   1458 C C   . SER A 1 275 ? -34.906 21.591 -21.670 1.00 67.96  ? 275 SER A C   1 
ATOM   1459 O O   . SER A 1 275 ? -34.302 20.572 -22.015 1.00 71.86  ? 275 SER A O   1 
ATOM   1460 C CB  . SER A 1 275 ? -35.236 22.215 -19.275 1.00 66.94  ? 275 SER A CB  1 
ATOM   1461 O OG  . SER A 1 275 ? -33.871 21.842 -19.190 1.00 65.22  ? 275 SER A OG  1 
ATOM   1462 N N   . GLU A 1 276 ? -34.756 22.759 -22.285 1.00 66.54  ? 276 GLU A N   1 
ATOM   1463 C CA  . GLU A 1 276 ? -33.772 22.941 -23.342 1.00 76.06  ? 276 GLU A CA  1 
ATOM   1464 C C   . GLU A 1 276 ? -32.526 23.602 -22.773 1.00 66.20  ? 276 GLU A C   1 
ATOM   1465 O O   . GLU A 1 276 ? -32.602 24.663 -22.145 1.00 65.85  ? 276 GLU A O   1 
ATOM   1466 C CB  . GLU A 1 276 ? -34.330 23.755 -24.508 1.00 81.23  ? 276 GLU A CB  1 
ATOM   1467 C CG  . GLU A 1 276 ? -35.016 22.878 -25.538 1.00 88.61  ? 276 GLU A CG  1 
ATOM   1468 C CD  . GLU A 1 276 ? -35.328 23.601 -26.830 1.00 98.32  ? 276 GLU A CD  1 
ATOM   1469 O OE1 . GLU A 1 276 ? -35.721 24.785 -26.784 1.00 100.66 ? 276 GLU A OE1 1 
ATOM   1470 O OE2 . GLU A 1 276 ? -35.163 22.979 -27.901 1.00 91.81  ? 276 GLU A OE2 1 
ATOM   1471 N N   . LEU A 1 277 ? -31.388 22.958 -22.991 1.00 60.60  ? 277 LEU A N   1 
ATOM   1472 C CA  . LEU A 1 277 ? -30.117 23.431 -22.472 1.00 54.28  ? 277 LEU A CA  1 
ATOM   1473 C C   . LEU A 1 277 ? -29.475 24.379 -23.474 1.00 47.01  ? 277 LEU A C   1 
ATOM   1474 O O   . LEU A 1 277 ? -29.446 24.098 -24.678 1.00 54.75  ? 277 LEU A O   1 
ATOM   1475 C CB  . LEU A 1 277 ? -29.200 22.241 -22.198 1.00 52.29  ? 277 LEU A CB  1 
ATOM   1476 C CG  . LEU A 1 277 ? -29.616 21.269 -21.093 1.00 52.59  ? 277 LEU A CG  1 
ATOM   1477 C CD1 . LEU A 1 277 ? -28.756 20.026 -21.176 1.00 49.81  ? 277 LEU A CD1 1 
ATOM   1478 C CD2 . LEU A 1 277 ? -29.485 21.914 -19.721 1.00 52.65  ? 277 LEU A CD2 1 
ATOM   1479 N N   . GLY A 1 278 ? -28.978 25.508 -22.983 1.00 43.25  ? 278 GLY A N   1 
ATOM   1480 C CA  . GLY A 1 278 ? -28.179 26.384 -23.814 1.00 42.48  ? 278 GLY A CA  1 
ATOM   1481 C C   . GLY A 1 278 ? -26.879 25.719 -24.230 1.00 40.58  ? 278 GLY A C   1 
ATOM   1482 O O   . GLY A 1 278 ? -26.531 24.617 -23.803 1.00 40.09  ? 278 GLY A O   1 
ATOM   1483 N N   . ALA A 1 279 ? -26.141 26.420 -25.093 1.00 43.70  ? 279 ALA A N   1 
ATOM   1484 C CA  . ALA A 1 279 ? -24.895 25.860 -25.606 1.00 36.84  ? 279 ALA A CA  1 
ATOM   1485 C C   . ALA A 1 279 ? -23.865 25.683 -24.495 1.00 36.21  ? 279 ALA A C   1 
ATOM   1486 O O   . ALA A 1 279 ? -23.106 24.708 -24.489 1.00 35.78  ? 279 ALA A O   1 
ATOM   1487 C CB  . ALA A 1 279 ? -24.338 26.745 -26.720 1.00 38.33  ? 279 ALA A CB  1 
ATOM   1488 N N   . ALA A 1 280 ? -23.835 26.608 -23.534 1.00 36.53  ? 280 ALA A N   1 
ATOM   1489 C CA  . ALA A 1 280 ? -22.866 26.517 -22.445 1.00 36.52  ? 280 ALA A CA  1 
ATOM   1490 C C   . ALA A 1 280 ? -23.086 25.262 -21.608 1.00 32.05  ? 280 ALA A C   1 
ATOM   1491 O O   . ALA A 1 280 ? -22.136 24.533 -21.301 1.00 38.06  ? 280 ALA A O   1 
ATOM   1492 C CB  . ALA A 1 280 ? -22.947 27.765 -21.568 1.00 32.67  ? 280 ALA A CB  1 
ATOM   1493 N N   . ALA A 1 281 ? -24.338 24.996 -21.226 1.00 39.15  ? 281 ALA A N   1 
ATOM   1494 C CA  . ALA A 1 281 ? -24.623 23.806 -20.430 1.00 39.89  ? 281 ALA A CA  1 
ATOM   1495 C C   . ALA A 1 281 ? -24.282 22.534 -21.198 1.00 37.07  ? 281 ALA A C   1 
ATOM   1496 O O   . ALA A 1 281 ? -23.725 21.587 -20.632 1.00 35.88  ? 281 ALA A O   1 
ATOM   1497 C CB  . ALA A 1 281 ? -26.088 23.800 -19.999 1.00 34.27  ? 281 ALA A CB  1 
ATOM   1498 N N   . ARG A 1 282 ? -24.601 22.499 -22.492 1.00 31.77  ? 282 ARG A N   1 
ATOM   1499 C CA  . ARG A 1 282 ? -24.297 21.328 -23.310 1.00 38.77  ? 282 ARG A CA  1 
ATOM   1500 C C   . ARG A 1 282 ? -22.796 21.110 -23.435 1.00 37.74  ? 282 ARG A C   1 
ATOM   1501 O O   . ARG A 1 282 ? -22.329 19.965 -23.441 1.00 40.64  ? 282 ARG A O   1 
ATOM   1502 C CB  . ARG A 1 282 ? -24.934 21.480 -24.691 1.00 34.25  ? 282 ARG A CB  1 
ATOM   1503 C CG  . ARG A 1 282 ? -26.436 21.344 -24.655 1.00 39.35  ? 282 ARG A CG  1 
ATOM   1504 C CD  . ARG A 1 282 ? -27.055 21.534 -26.021 1.00 43.13  ? 282 ARG A CD  1 
ATOM   1505 N NE  . ARG A 1 282 ? -28.480 21.817 -25.907 1.00 47.06  ? 282 ARG A NE  1 
ATOM   1506 C CZ  . ARG A 1 282 ? -29.409 21.304 -26.701 1.00 51.59  ? 282 ARG A CZ  1 
ATOM   1507 N NH1 . ARG A 1 282 ? -29.092 20.507 -27.707 1.00 51.90  ? 282 ARG A NH1 1 
ATOM   1508 N NH2 . ARG A 1 282 ? -30.686 21.602 -26.482 1.00 56.05  ? 282 ARG A NH2 1 
ATOM   1509 N N   . PHE A 1 283 ? -22.028 22.195 -23.542 1.00 38.01  ? 283 PHE A N   1 
ATOM   1510 C CA  . PHE A 1 283 ? -20.575 22.076 -23.595 1.00 33.78  ? 283 PHE A CA  1 
ATOM   1511 C C   . PHE A 1 283 ? -20.036 21.418 -22.331 1.00 36.89  ? 283 PHE A C   1 
ATOM   1512 O O   . PHE A 1 283 ? -19.214 20.496 -22.398 1.00 42.01  ? 283 PHE A O   1 
ATOM   1513 C CB  . PHE A 1 283 ? -19.943 23.454 -23.792 1.00 39.43  ? 283 PHE A CB  1 
ATOM   1514 C CG  . PHE A 1 283 ? -18.448 23.458 -23.646 1.00 43.29  ? 283 PHE A CG  1 
ATOM   1515 C CD1 . PHE A 1 283 ? -17.635 23.111 -24.713 1.00 47.47  ? 283 PHE A CD1 1 
ATOM   1516 C CD2 . PHE A 1 283 ? -17.855 23.792 -22.437 1.00 37.90  ? 283 PHE A CD2 1 
ATOM   1517 C CE1 . PHE A 1 283 ? -16.260 23.106 -24.582 1.00 41.80  ? 283 PHE A CE1 1 
ATOM   1518 C CE2 . PHE A 1 283 ? -16.481 23.785 -22.298 1.00 44.53  ? 283 PHE A CE2 1 
ATOM   1519 C CZ  . PHE A 1 283 ? -15.684 23.443 -23.372 1.00 44.84  ? 283 PHE A CZ  1 
ATOM   1520 N N   . LEU A 1 284 ? -20.494 21.885 -21.165 1.00 34.36  ? 284 LEU A N   1 
ATOM   1521 C CA  . LEU A 1 284 ? -20.021 21.332 -19.901 1.00 30.64  ? 284 LEU A CA  1 
ATOM   1522 C C   . LEU A 1 284 ? -20.372 19.855 -19.777 1.00 36.50  ? 284 LEU A C   1 
ATOM   1523 O O   . LEU A 1 284 ? -19.552 19.052 -19.318 1.00 36.96  ? 284 LEU A O   1 
ATOM   1524 C CB  . LEU A 1 284 ? -20.613 22.118 -18.732 1.00 29.40  ? 284 LEU A CB  1 
ATOM   1525 C CG  . LEU A 1 284 ? -20.177 21.677 -17.332 1.00 36.13  ? 284 LEU A CG  1 
ATOM   1526 C CD1 . LEU A 1 284 ? -18.658 21.701 -17.203 1.00 29.53  ? 284 LEU A CD1 1 
ATOM   1527 C CD2 . LEU A 1 284 ? -20.828 22.554 -16.276 1.00 30.54  ? 284 LEU A CD2 1 
ATOM   1528 N N   . ILE A 1 285 ? -21.588 19.478 -20.177 1.00 39.58  ? 285 ILE A N   1 
ATOM   1529 C CA  . ILE A 1 285 ? -22.008 18.082 -20.070 1.00 37.28  ? 285 ILE A CA  1 
ATOM   1530 C C   . ILE A 1 285 ? -21.149 17.195 -20.963 1.00 40.36  ? 285 ILE A C   1 
ATOM   1531 O O   . ILE A 1 285 ? -20.706 16.115 -20.555 1.00 40.06  ? 285 ILE A O   1 
ATOM   1532 C CB  . ILE A 1 285 ? -23.503 17.944 -20.406 1.00 38.97  ? 285 ILE A CB  1 
ATOM   1533 C CG1 . ILE A 1 285 ? -24.344 18.579 -19.298 1.00 35.58  ? 285 ILE A CG1 1 
ATOM   1534 C CG2 . ILE A 1 285 ? -23.874 16.479 -20.630 1.00 33.95  ? 285 ILE A CG2 1 
ATOM   1535 C CD1 . ILE A 1 285 ? -25.782 18.782 -19.662 1.00 33.44  ? 285 ILE A CD1 1 
ATOM   1536 N N   . ASP A 1 286 ? -20.901 17.639 -22.196 1.00 42.94  ? 286 ASP A N   1 
ATOM   1537 C CA  . ASP A 1 286 ? -20.053 16.870 -23.101 1.00 39.36  ? 286 ASP A CA  1 
ATOM   1538 C C   . ASP A 1 286 ? -18.619 16.799 -22.590 1.00 41.25  ? 286 ASP A C   1 
ATOM   1539 O O   . ASP A 1 286 ? -17.969 15.753 -22.691 1.00 45.16  ? 286 ASP A O   1 
ATOM   1540 C CB  . ASP A 1 286 ? -20.098 17.477 -24.505 1.00 43.92  ? 286 ASP A CB  1 
ATOM   1541 C CG  . ASP A 1 286 ? -21.379 17.144 -25.245 1.00 56.13  ? 286 ASP A CG  1 
ATOM   1542 O OD1 . ASP A 1 286 ? -21.742 15.949 -25.284 1.00 64.81  ? 286 ASP A OD1 1 
ATOM   1543 O OD2 . ASP A 1 286 ? -22.020 18.069 -25.791 1.00 64.38  ? 286 ASP A OD2 1 
ATOM   1544 N N   . TYR A 1 287 ? -18.111 17.900 -22.035 1.00 42.03  ? 287 TYR A N   1 
ATOM   1545 C CA  . TYR A 1 287 ? -16.760 17.906 -21.483 1.00 41.72  ? 287 TYR A CA  1 
ATOM   1546 C C   . TYR A 1 287 ? -16.618 16.874 -20.368 1.00 47.09  ? 287 TYR A C   1 
ATOM   1547 O O   . TYR A 1 287 ? -15.638 16.122 -20.320 1.00 47.05  ? 287 TYR A O   1 
ATOM   1548 C CB  . TYR A 1 287 ? -16.419 19.315 -20.988 1.00 36.28  ? 287 TYR A CB  1 
ATOM   1549 C CG  . TYR A 1 287 ? -15.007 19.496 -20.484 1.00 39.64  ? 287 TYR A CG  1 
ATOM   1550 C CD1 . TYR A 1 287 ? -13.975 19.829 -21.353 1.00 43.51  ? 287 TYR A CD1 1 
ATOM   1551 C CD2 . TYR A 1 287 ? -14.702 19.316 -19.146 1.00 48.12  ? 287 TYR A CD2 1 
ATOM   1552 C CE1 . TYR A 1 287 ? -12.679 19.992 -20.896 1.00 40.00  ? 287 TYR A CE1 1 
ATOM   1553 C CE2 . TYR A 1 287 ? -13.425 19.500 -18.684 1.00 46.12  ? 287 TYR A CE2 1 
ATOM   1554 C CZ  . TYR A 1 287 ? -12.410 19.816 -19.557 1.00 55.63  ? 287 TYR A CZ  1 
ATOM   1555 O OH  . TYR A 1 287 ? -11.129 19.973 -19.078 1.00 68.94  ? 287 TYR A OH  1 
ATOM   1556 N N   . ILE A 1 288 ? -17.607 16.810 -19.474 1.00 42.51  ? 288 ILE A N   1 
ATOM   1557 C CA  . ILE A 1 288 ? -17.545 15.880 -18.348 1.00 42.69  ? 288 ILE A CA  1 
ATOM   1558 C C   . ILE A 1 288 ? -17.647 14.441 -18.836 1.00 46.30  ? 288 ILE A C   1 
ATOM   1559 O O   . ILE A 1 288 ? -16.816 13.591 -18.497 1.00 49.28  ? 288 ILE A O   1 
ATOM   1560 C CB  . ILE A 1 288 ? -18.648 16.204 -17.327 1.00 33.06  ? 288 ILE A CB  1 
ATOM   1561 C CG1 . ILE A 1 288 ? -18.341 17.530 -16.627 1.00 38.56  ? 288 ILE A CG1 1 
ATOM   1562 C CG2 . ILE A 1 288 ? -18.778 15.083 -16.319 1.00 40.59  ? 288 ILE A CG2 1 
ATOM   1563 C CD1 . ILE A 1 288 ? -16.980 17.554 -15.954 1.00 42.32  ? 288 ILE A CD1 1 
ATOM   1564 N N   . ARG A 1 289 ? -18.680 14.144 -19.625 1.00 38.43  ? 289 ARG A N   1 
ATOM   1565 C CA  . ARG A 1 289 ? -18.829 12.810 -20.199 1.00 44.71  ? 289 ARG A CA  1 
ATOM   1566 C C   . ARG A 1 289 ? -17.575 12.376 -20.952 1.00 46.66  ? 289 ARG A C   1 
ATOM   1567 O O   . ARG A 1 289 ? -17.181 11.207 -20.889 1.00 55.07  ? 289 ARG A O   1 
ATOM   1568 C CB  . ARG A 1 289 ? -20.045 12.776 -21.125 1.00 43.64  ? 289 ARG A CB  1 
ATOM   1569 C CG  . ARG A 1 289 ? -21.384 12.734 -20.417 1.00 45.52  ? 289 ARG A CG  1 
ATOM   1570 C CD  . ARG A 1 289 ? -22.494 12.903 -21.432 1.00 45.31  ? 289 ARG A CD  1 
ATOM   1571 N NE  . ARG A 1 289 ? -23.817 12.708 -20.857 1.00 52.29  ? 289 ARG A NE  1 
ATOM   1572 C CZ  . ARG A 1 289 ? -24.948 12.946 -21.506 1.00 54.69  ? 289 ARG A CZ  1 
ATOM   1573 N NH1 . ARG A 1 289 ? -24.948 13.442 -22.734 1.00 51.40  ? 289 ARG A NH1 1 
ATOM   1574 N NH2 . ARG A 1 289 ? -26.107 12.681 -20.911 1.00 50.81  ? 289 ARG A NH2 1 
ATOM   1575 N N   . ASN A 1 290 ? -16.929 13.302 -21.666 1.00 49.12  ? 290 ASN A N   1 
ATOM   1576 C CA  . ASN A 1 290 ? -15.755 12.948 -22.463 1.00 56.50  ? 290 ASN A CA  1 
ATOM   1577 C C   . ASN A 1 290 ? -14.581 12.588 -21.564 1.00 53.57  ? 290 ASN A C   1 
ATOM   1578 O O   . ASN A 1 290 ? -13.775 11.709 -21.887 1.00 62.59  ? 290 ASN A O   1 
ATOM   1579 C CB  . ASN A 1 290 ? -15.400 14.115 -23.391 1.00 54.47  ? 290 ASN A CB  1 
ATOM   1580 C CG  . ASN A 1 290 ? -14.681 13.673 -24.656 1.00 63.62  ? 290 ASN A CG  1 
ATOM   1581 O OD1 . ASN A 1 290 ? -13.925 12.702 -24.651 1.00 72.64  ? 290 ASN A OD1 1 
ATOM   1582 N ND2 . ASN A 1 290 ? -14.933 14.382 -25.757 1.00 70.12  ? 290 ASN A ND2 1 
ATOM   1583 N N   . LYS A 1 291 ? -14.539 13.182 -20.393 1.00 45.39  ? 291 LYS A N   1 
ATOM   1584 C CA  . LYS A 1 291 ? -13.490 12.895 -19.459 1.00 56.27  ? 291 LYS A CA  1 
ATOM   1585 C C   . LYS A 1 291 ? -13.728 11.557 -18.829 1.00 57.13  ? 291 LYS A C   1 
ATOM   1586 O O   . LYS A 1 291 ? -12.817 10.801 -18.620 1.00 61.19  ? 291 LYS A O   1 
ATOM   1587 C CB  . LYS A 1 291 ? -13.429 13.944 -18.358 1.00 60.66  ? 291 LYS A CB  1 
ATOM   1588 C CG  . LYS A 1 291 ? -12.485 15.101 -18.603 1.00 63.07  ? 291 LYS A CG  1 
ATOM   1589 C CD  . LYS A 1 291 ? -12.520 16.072 -17.437 1.00 66.40  ? 291 LYS A CD  1 
ATOM   1590 C CE  . LYS A 1 291 ? -11.142 16.611 -17.106 1.00 74.88  ? 291 LYS A CE  1 
ATOM   1591 N NZ  . LYS A 1 291 ? -11.061 17.178 -15.738 1.00 74.70  ? 291 LYS A NZ  1 
ATOM   1592 N N   . ARG A 1 292 ? -14.963 11.291 -18.482 1.00 54.36  ? 292 ARG A N   1 
ATOM   1593 C CA  . ARG A 1 292 ? -15.328 10.016 -17.865 1.00 57.30  ? 292 ARG A CA  1 
ATOM   1594 C C   . ARG A 1 292 ? -15.136 8.817  -18.788 1.00 58.45  ? 292 ARG A C   1 
ATOM   1595 O O   . ARG A 1 292 ? -15.200 7.677  -18.311 1.00 67.75  ? 292 ARG A O   1 
ATOM   1596 C CB  . ARG A 1 292 ? -16.777 10.071 -17.375 1.00 55.80  ? 292 ARG A CB  1 
ATOM   1597 C CG  . ARG A 1 292 ? -17.006 11.167 -16.350 1.00 55.61  ? 292 ARG A CG  1 
ATOM   1598 C CD  . ARG A 1 292 ? -18.261 10.941 -15.524 1.00 54.59  ? 292 ARG A CD  1 
ATOM   1599 N NE  . ARG A 1 292 ? -18.074 9.962  -14.459 1.00 58.45  ? 292 ARG A NE  1 
ATOM   1600 C CZ  . ARG A 1 292 ? -17.321 10.150 -13.382 1.00 63.20  ? 292 ARG A CZ  1 
ATOM   1601 N NH1 . ARG A 1 292 ? -16.637 11.268 -13.199 1.00 64.56  ? 292 ARG A NH1 1 
ATOM   1602 N NH2 . ARG A 1 292 ? -17.254 9.191  -12.463 1.00 55.59  ? 292 ARG A NH2 1 
ATOM   1603 N N   . MET A 1 293 ? -14.848 9.102  -20.034 1.00 53.49  ? 293 MET A N   1 
ATOM   1604 C CA  . MET A 1 293 ? -14.487 8.089  -20.974 1.00 63.30  ? 293 MET A CA  1 
ATOM   1605 C C   . MET A 1 293 ? -13.261 7.367  -20.425 1.00 67.13  ? 293 MET A C   1 
ATOM   1606 O O   . MET A 1 293 ? -12.842 6.405  -20.995 1.00 74.49  ? 293 MET A O   1 
ATOM   1607 C CB  . MET A 1 293 ? -14.066 8.745  -22.273 1.00 69.85  ? 293 MET A CB  1 
ATOM   1608 C CG  . MET A 1 293 ? -14.907 8.428  -23.472 1.00 75.87  ? 293 MET A CG  1 
ATOM   1609 S SD  . MET A 1 293 ? -16.626 8.324  -23.028 1.00 91.77  ? 293 MET A SD  1 
ATOM   1610 C CE  . MET A 1 293 ? -17.343 9.124  -24.433 1.00 82.79  ? 293 MET A CE  1 
ATOM   1611 N N   . GLN A 1 294 ? -12.629 7.881  -19.369 1.00 73.37  ? 294 GLN A N   1 
ATOM   1612 C CA  . GLN A 1 294 ? -11.476 7.247  -18.727 1.00 73.00  ? 294 GLN A CA  1 
ATOM   1613 C C   . GLN A 1 294 ? -11.622 7.216  -17.213 1.00 69.79  ? 294 GLN A C   1 
ATOM   1614 O O   . GLN A 1 294 ? -12.066 6.247  -16.623 1.00 85.34  ? 294 GLN A O   1 
ATOM   1615 C CB  . GLN A 1 294 ? -10.209 7.987  -19.074 1.00 71.67  ? 294 GLN A CB  1 
ATOM   1616 C CG  . GLN A 1 294 ? -9.968  8.146  -20.557 1.00 77.85  ? 294 GLN A CG  1 
ATOM   1617 C CD  . GLN A 1 294 ? -10.143 9.560  -21.062 1.00 72.99  ? 294 GLN A CD  1 
ATOM   1618 O OE1 . GLN A 1 294 ? -10.094 10.503 -20.318 1.00 75.02  ? 294 GLN A OE1 1 
ATOM   1619 N NE2 . GLN A 1 294 ? -10.326 9.694  -22.351 1.00 77.44  ? 294 GLN A NE2 1 
ATOM   1620 N N   . PRO B 1 93  ? -37.746 21.560 23.193  1.00 68.70  ? 93  PRO B N   1 
ATOM   1621 C CA  . PRO B 1 93  ? -37.815 22.988 22.868  1.00 66.07  ? 93  PRO B CA  1 
ATOM   1622 C C   . PRO B 1 93  ? -36.777 23.363 21.820  1.00 56.10  ? 93  PRO B C   1 
ATOM   1623 O O   . PRO B 1 93  ? -35.633 22.914 21.915  1.00 50.75  ? 93  PRO B O   1 
ATOM   1624 C CB  . PRO B 1 93  ? -37.500 23.667 24.200  1.00 62.90  ? 93  PRO B CB  1 
ATOM   1625 C CG  . PRO B 1 93  ? -36.662 22.670 24.945  1.00 62.35  ? 93  PRO B CG  1 
ATOM   1626 C CD  . PRO B 1 93  ? -36.941 21.297 24.399  1.00 63.76  ? 93  PRO B CD  1 
ATOM   1627 N N   . ASN B 1 94  ? -37.155 24.172 20.834  1.00 54.53  ? 94  ASN B N   1 
ATOM   1628 C CA  . ASN B 1 94  ? -36.194 24.554 19.814  1.00 50.95  ? 94  ASN B CA  1 
ATOM   1629 C C   . ASN B 1 94  ? -36.524 25.929 19.252  1.00 48.16  ? 94  ASN B C   1 
ATOM   1630 O O   . ASN B 1 94  ? -37.651 26.420 19.347  1.00 47.24  ? 94  ASN B O   1 
ATOM   1631 C CB  . ASN B 1 94  ? -36.118 23.506 18.699  1.00 55.83  ? 94  ASN B CB  1 
ATOM   1632 C CG  . ASN B 1 94  ? -37.324 23.524 17.794  1.00 56.38  ? 94  ASN B CG  1 
ATOM   1633 O OD1 . ASN B 1 94  ? -38.455 23.311 18.234  1.00 63.50  ? 94  ASN B OD1 1 
ATOM   1634 N ND2 . ASN B 1 94  ? -37.090 23.771 16.511  1.00 61.13  ? 94  ASN B ND2 1 
ATOM   1635 N N   . LEU B 1 95  ? -35.501 26.534 18.655  1.00 38.05  ? 95  LEU B N   1 
ATOM   1636 C CA  . LEU B 1 95  ? -35.533 27.909 18.174  1.00 38.36  ? 95  LEU B CA  1 
ATOM   1637 C C   . LEU B 1 95  ? -34.867 27.954 16.810  1.00 37.03  ? 95  LEU B C   1 
ATOM   1638 O O   . LEU B 1 95  ? -33.705 27.558 16.679  1.00 31.56  ? 95  LEU B O   1 
ATOM   1639 C CB  . LEU B 1 95  ? -34.803 28.832 19.153  1.00 35.09  ? 95  LEU B CB  1 
ATOM   1640 C CG  . LEU B 1 95  ? -34.461 30.251 18.697  1.00 35.27  ? 95  LEU B CG  1 
ATOM   1641 C CD1 . LEU B 1 95  ? -35.707 31.063 18.416  1.00 35.58  ? 95  LEU B CD1 1 
ATOM   1642 C CD2 . LEU B 1 95  ? -33.594 30.934 19.731  1.00 45.81  ? 95  LEU B CD2 1 
ATOM   1643 N N   . THR B 1 96  ? -35.584 28.438 15.800  1.00 33.22  ? 96  THR B N   1 
ATOM   1644 C CA  . THR B 1 96  ? -35.042 28.553 14.451  1.00 32.05  ? 96  THR B CA  1 
ATOM   1645 C C   . THR B 1 96  ? -34.780 30.015 14.128  1.00 30.36  ? 96  THR B C   1 
ATOM   1646 O O   . THR B 1 96  ? -35.698 30.841 14.169  1.00 32.59  ? 96  THR B O   1 
ATOM   1647 C CB  . THR B 1 96  ? -35.981 27.935 13.416  1.00 37.21  ? 96  THR B CB  1 
ATOM   1648 O OG1 . THR B 1 96  ? -36.103 26.529 13.670  1.00 37.26  ? 96  THR B OG1 1 
ATOM   1649 C CG2 . THR B 1 96  ? -35.439 28.147 11.995  1.00 31.09  ? 96  THR B CG2 1 
ATOM   1650 N N   . ILE B 1 97  ? -33.530 30.320 13.791  1.00 28.12  ? 97  ILE B N   1 
ATOM   1651 C CA  . ILE B 1 97  ? -33.104 31.658 13.406  1.00 27.29  ? 97  ILE B CA  1 
ATOM   1652 C C   . ILE B 1 97  ? -32.722 31.614 11.933  1.00 31.59  ? 97  ILE B C   1 
ATOM   1653 O O   . ILE B 1 97  ? -31.924 30.762 11.526  1.00 29.87  ? 97  ILE B O   1 
ATOM   1654 C CB  . ILE B 1 97  ? -31.914 32.129 14.259  1.00 31.77  ? 97  ILE B CB  1 
ATOM   1655 C CG1 . ILE B 1 97  ? -32.302 32.189 15.740  1.00 31.65  ? 97  ILE B CG1 1 
ATOM   1656 C CG2 . ILE B 1 97  ? -31.409 33.483 13.774  1.00 33.94  ? 97  ILE B CG2 1 
ATOM   1657 C CD1 . ILE B 1 97  ? -31.118 32.230 16.672  1.00 41.58  ? 97  ILE B CD1 1 
ATOM   1658 N N   . VAL B 1 98  ? -33.289 32.515 11.135  1.00 26.52  ? 98  VAL B N   1 
ATOM   1659 C CA  . VAL B 1 98  ? -32.921 32.619 9.726   1.00 30.06  ? 98  VAL B CA  1 
ATOM   1660 C C   . VAL B 1 98  ? -32.005 33.822 9.546   1.00 32.24  ? 98  VAL B C   1 
ATOM   1661 O O   . VAL B 1 98  ? -32.399 34.966 9.802   1.00 30.58  ? 98  VAL B O   1 
ATOM   1662 C CB  . VAL B 1 98  ? -34.153 32.702 8.808   1.00 29.87  ? 98  VAL B CB  1 
ATOM   1663 C CG1 . VAL B 1 98  ? -35.104 33.812 9.233   1.00 28.29  ? 98  VAL B CG1 1 
ATOM   1664 C CG2 . VAL B 1 98  ? -33.715 32.894 7.366   1.00 39.37  ? 98  VAL B CG2 1 
ATOM   1665 N N   . VAL B 1 99  ? -30.772 33.559 9.131   1.00 36.49  ? 99  VAL B N   1 
ATOM   1666 C CA  . VAL B 1 99  ? -29.812 34.601 8.800   1.00 30.71  ? 99  VAL B CA  1 
ATOM   1667 C C   . VAL B 1 99  ? -29.885 34.825 7.300   1.00 36.24  ? 99  VAL B C   1 
ATOM   1668 O O   . VAL B 1 99  ? -29.659 33.896 6.519   1.00 34.70  ? 99  VAL B O   1 
ATOM   1669 C CB  . VAL B 1 99  ? -28.391 34.210 9.229   1.00 41.80  ? 99  VAL B CB  1 
ATOM   1670 C CG1 . VAL B 1 99  ? -27.415 35.326 8.884   1.00 36.53  ? 99  VAL B CG1 1 
ATOM   1671 C CG2 . VAL B 1 99  ? -28.355 33.877 10.713  1.00 33.13  ? 99  VAL B CG2 1 
ATOM   1672 N N   . VAL B 1 100 ? -30.216 36.051 6.891   1.00 32.78  ? 100 VAL B N   1 
ATOM   1673 C CA  . VAL B 1 100 ? -30.296 36.344 5.469   1.00 37.66  ? 100 VAL B CA  1 
ATOM   1674 C C   . VAL B 1 100 ? -28.930 36.094 4.836   1.00 31.73  ? 100 VAL B C   1 
ATOM   1675 O O   . VAL B 1 100 ? -27.882 36.313 5.453   1.00 36.59  ? 100 VAL B O   1 
ATOM   1676 C CB  . VAL B 1 100 ? -30.781 37.785 5.237   1.00 38.39  ? 100 VAL B CB  1 
ATOM   1677 C CG1 . VAL B 1 100 ? -30.649 38.177 3.771   1.00 44.76  ? 100 VAL B CG1 1 
ATOM   1678 C CG2 . VAL B 1 100 ? -32.222 37.931 5.708   1.00 36.45  ? 100 VAL B CG2 1 
ATOM   1679 N N   . SER B 1 101 ? -28.949 35.601 3.595   1.00 38.74  ? 101 SER B N   1 
ATOM   1680 C CA  . SER B 1 101 ? -27.733 35.137 2.931   1.00 40.30  ? 101 SER B CA  1 
ATOM   1681 C C   . SER B 1 101 ? -26.599 36.154 3.020   1.00 37.38  ? 101 SER B C   1 
ATOM   1682 O O   . SER B 1 101 ? -25.458 35.800 3.341   1.00 39.68  ? 101 SER B O   1 
ATOM   1683 C CB  . SER B 1 101 ? -28.039 34.805 1.470   1.00 41.03  ? 101 SER B CB  1 
ATOM   1684 O OG  . SER B 1 101 ? -29.295 34.163 1.355   1.00 50.10  ? 101 SER B OG  1 
ATOM   1685 N N   . GLU B 1 102 ? -26.897 37.428 2.759   1.00 31.72  ? 102 GLU B N   1 
ATOM   1686 C CA  . GLU B 1 102 ? -25.843 38.438 2.726   1.00 34.50  ? 102 GLU B CA  1 
ATOM   1687 C C   . GLU B 1 102 ? -25.171 38.649 4.081   1.00 36.52  ? 102 GLU B C   1 
ATOM   1688 O O   . GLU B 1 102 ? -24.089 39.243 4.133   1.00 37.10  ? 102 GLU B O   1 
ATOM   1689 C CB  . GLU B 1 102 ? -26.404 39.763 2.206   1.00 39.10  ? 102 GLU B CB  1 
ATOM   1690 C CG  . GLU B 1 102 ? -26.723 39.780 0.714   1.00 45.13  ? 102 GLU B CG  1 
ATOM   1691 C CD  . GLU B 1 102 ? -28.168 39.447 0.409   1.00 46.70  ? 102 GLU B CD  1 
ATOM   1692 O OE1 . GLU B 1 102 ? -28.763 38.632 1.141   1.00 49.94  ? 102 GLU B OE1 1 
ATOM   1693 O OE2 . GLU B 1 102 ? -28.717 40.001 -0.565  1.00 51.14  ? 102 GLU B OE2 1 
ATOM   1694 N N   . LEU B 1 103 ? -25.771 38.171 5.170   1.00 35.67  ? 103 LEU B N   1 
ATOM   1695 C CA  . LEU B 1 103 ? -25.220 38.355 6.507   1.00 36.89  ? 103 LEU B CA  1 
ATOM   1696 C C   . LEU B 1 103 ? -24.532 37.108 7.046   1.00 41.92  ? 103 LEU B C   1 
ATOM   1697 O O   . LEU B 1 103 ? -24.118 37.100 8.209   1.00 40.56  ? 103 LEU B O   1 
ATOM   1698 C CB  . LEU B 1 103 ? -26.325 38.782 7.477   1.00 35.27  ? 103 LEU B CB  1 
ATOM   1699 C CG  . LEU B 1 103 ? -27.062 40.079 7.116   1.00 38.97  ? 103 LEU B CG  1 
ATOM   1700 C CD1 . LEU B 1 103 ? -28.047 40.469 8.207   1.00 33.98  ? 103 LEU B CD1 1 
ATOM   1701 C CD2 . LEU B 1 103 ? -26.089 41.219 6.837   1.00 28.76  ? 103 LEU B CD2 1 
ATOM   1702 N N   . LEU B 1 104 ? -24.400 36.058 6.235   1.00 38.66  ? 104 LEU B N   1 
ATOM   1703 C CA  . LEU B 1 104 ? -23.832 34.806 6.726   1.00 41.55  ? 104 LEU B CA  1 
ATOM   1704 C C   . LEU B 1 104 ? -22.375 34.977 7.133   1.00 49.96  ? 104 LEU B C   1 
ATOM   1705 O O   . LEU B 1 104 ? -21.949 34.457 8.169   1.00 44.86  ? 104 LEU B O   1 
ATOM   1706 C CB  . LEU B 1 104 ? -23.959 33.716 5.661   1.00 48.33  ? 104 LEU B CB  1 
ATOM   1707 C CG  . LEU B 1 104 ? -25.339 33.095 5.482   1.00 52.91  ? 104 LEU B CG  1 
ATOM   1708 C CD1 . LEU B 1 104 ? -25.489 32.488 4.087   1.00 52.77  ? 104 LEU B CD1 1 
ATOM   1709 C CD2 . LEU B 1 104 ? -25.596 32.058 6.569   1.00 49.49  ? 104 LEU B CD2 1 
ATOM   1710 N N   . HIS B 1 105 ? -21.598 35.701 6.331   1.00 51.53  ? 105 HIS B N   1 
ATOM   1711 C CA  . HIS B 1 105 ? -20.176 35.886 6.584   1.00 51.89  ? 105 HIS B CA  1 
ATOM   1712 C C   . HIS B 1 105 ? -19.903 37.166 7.366   1.00 44.11  ? 105 HIS B C   1 
ATOM   1713 O O   . HIS B 1 105 ? -18.835 37.775 7.228   1.00 45.78  ? 105 HIS B O   1 
ATOM   1714 C CB  . HIS B 1 105 ? -19.426 35.849 5.257   1.00 36.11  ? 105 HIS B CB  1 
ATOM   1715 C CG  . HIS B 1 105 ? -19.562 34.533 4.554   1.00 42.21  ? 105 HIS B CG  1 
ATOM   1716 N ND1 . HIS B 1 105 ? -20.564 34.279 3.641   1.00 51.26  ? 105 HIS B ND1 1 
ATOM   1717 C CD2 . HIS B 1 105 ? -18.857 33.383 4.666   1.00 48.12  ? 105 HIS B CD2 1 
ATOM   1718 C CE1 . HIS B 1 105 ? -20.457 33.037 3.206   1.00 51.97  ? 105 HIS B CE1 1 
ATOM   1719 N NE2 . HIS B 1 105 ? -19.429 32.471 3.811   1.00 55.91  ? 105 HIS B NE2 1 
ATOM   1720 N N   . THR B 1 106 ? -20.871 37.584 8.182   1.00 49.96  ? 106 THR B N   1 
ATOM   1721 C CA  . THR B 1 106 ? -20.704 38.573 9.234   1.00 48.04  ? 106 THR B CA  1 
ATOM   1722 C C   . THR B 1 106 ? -20.684 37.857 10.586  1.00 47.85  ? 106 THR B C   1 
ATOM   1723 O O   . THR B 1 106 ? -20.610 36.627 10.659  1.00 61.05  ? 106 THR B O   1 
ATOM   1724 C CB  . THR B 1 106 ? -21.805 39.636 9.154   1.00 56.11  ? 106 THR B CB  1 
ATOM   1725 O OG1 . THR B 1 106 ? -23.047 39.085 9.616   1.00 49.88  ? 106 THR B OG1 1 
ATOM   1726 C CG2 . THR B 1 106 ? -21.960 40.139 7.724   1.00 55.34  ? 106 THR B CG2 1 
ATOM   1727 N N   . ASN B 1 107 ? -20.779 38.632 11.662  1.00 50.89  ? 107 ASN B N   1 
ATOM   1728 C CA  . ASN B 1 107 ? -20.455 38.176 13.013  1.00 54.56  ? 107 ASN B CA  1 
ATOM   1729 C C   . ASN B 1 107 ? -21.738 38.022 13.827  1.00 49.77  ? 107 ASN B C   1 
ATOM   1730 O O   . ASN B 1 107 ? -22.194 38.975 14.457  1.00 56.89  ? 107 ASN B O   1 
ATOM   1731 C CB  . ASN B 1 107 ? -19.489 39.175 13.651  1.00 60.51  ? 107 ASN B CB  1 
ATOM   1732 C CG  . ASN B 1 107 ? -19.029 38.769 15.038  1.00 52.10  ? 107 ASN B CG  1 
ATOM   1733 O OD1 . ASN B 1 107 ? -19.610 37.900 15.693  1.00 65.17  ? 107 ASN B OD1 1 
ATOM   1734 N ND2 . ASN B 1 107 ? -17.939 39.381 15.477  1.00 63.77  ? 107 ASN B ND2 1 
ATOM   1735 N N   . TRP B 1 108 ? -22.293 36.810 13.860  1.00 49.85  ? 108 TRP B N   1 
ATOM   1736 C CA  . TRP B 1 108 ? -23.569 36.592 14.529  1.00 37.27  ? 108 TRP B CA  1 
ATOM   1737 C C   . TRP B 1 108 ? -23.532 35.548 15.636  1.00 43.73  ? 108 TRP B C   1 
ATOM   1738 O O   . TRP B 1 108 ? -24.554 35.336 16.294  1.00 42.27  ? 108 TRP B O   1 
ATOM   1739 C CB  . TRP B 1 108 ? -24.644 36.195 13.507  1.00 40.11  ? 108 TRP B CB  1 
ATOM   1740 C CG  . TRP B 1 108 ? -24.201 35.119 12.584  1.00 42.55  ? 108 TRP B CG  1 
ATOM   1741 C CD1 . TRP B 1 108 ? -23.684 35.281 11.335  1.00 43.68  ? 108 TRP B CD1 1 
ATOM   1742 C CD2 . TRP B 1 108 ? -24.229 33.707 12.828  1.00 42.88  ? 108 TRP B CD2 1 
ATOM   1743 N NE1 . TRP B 1 108 ? -23.384 34.062 10.786  1.00 43.21  ? 108 TRP B NE1 1 
ATOM   1744 C CE2 . TRP B 1 108 ? -23.710 33.077 11.682  1.00 36.04  ? 108 TRP B CE2 1 
ATOM   1745 C CE3 . TRP B 1 108 ? -24.642 32.915 13.905  1.00 39.03  ? 108 TRP B CE3 1 
ATOM   1746 C CZ2 . TRP B 1 108 ? -23.592 31.696 11.577  1.00 30.44  ? 108 TRP B CZ2 1 
ATOM   1747 C CZ3 . TRP B 1 108 ? -24.524 31.543 13.801  1.00 37.06  ? 108 TRP B CZ3 1 
ATOM   1748 C CH2 . TRP B 1 108 ? -24.003 30.946 12.644  1.00 38.81  ? 108 TRP B CH2 1 
ATOM   1749 N N   . THR B 1 109 ? -22.395 34.901 15.871  1.00 38.43  ? 109 THR B N   1 
ATOM   1750 C CA  . THR B 1 109 ? -22.360 33.780 16.801  1.00 40.80  ? 109 THR B CA  1 
ATOM   1751 C C   . THR B 1 109 ? -22.384 34.202 18.263  1.00 37.27  ? 109 THR B C   1 
ATOM   1752 O O   . THR B 1 109 ? -22.641 33.356 19.126  1.00 41.62  ? 109 THR B O   1 
ATOM   1753 C CB  . THR B 1 109 ? -21.128 32.918 16.532  1.00 37.59  ? 109 THR B CB  1 
ATOM   1754 O OG1 . THR B 1 109 ? -19.945 33.679 16.788  1.00 47.48  ? 109 THR B OG1 1 
ATOM   1755 C CG2 . THR B 1 109 ? -21.126 32.458 15.093  1.00 37.82  ? 109 THR B CG2 1 
ATOM   1756 N N   . ASP B 1 110 ? -22.114 35.475 18.566  1.00 33.26  ? 110 ASP B N   1 
ATOM   1757 C CA  . ASP B 1 110 ? -22.215 35.930 19.950  1.00 38.78  ? 110 ASP B CA  1 
ATOM   1758 C C   . ASP B 1 110 ? -23.619 35.732 20.499  1.00 36.43  ? 110 ASP B C   1 
ATOM   1759 O O   . ASP B 1 110 ? -23.786 35.377 21.671  1.00 49.30  ? 110 ASP B O   1 
ATOM   1760 C CB  . ASP B 1 110 ? -21.817 37.401 20.065  1.00 39.00  ? 110 ASP B CB  1 
ATOM   1761 C CG  . ASP B 1 110 ? -20.336 37.612 19.881  1.00 49.68  ? 110 ASP B CG  1 
ATOM   1762 O OD1 . ASP B 1 110 ? -19.600 36.604 19.864  1.00 61.74  ? 110 ASP B OD1 1 
ATOM   1763 O OD2 . ASP B 1 110 ? -19.900 38.777 19.776  1.00 55.68  ? 110 ASP B OD2 1 
ATOM   1764 N N   . TYR B 1 111 ? -24.637 35.954 19.667  1.00 38.74  ? 111 TYR B N   1 
ATOM   1765 C CA  . TYR B 1 111 ? -26.015 35.802 20.116  1.00 38.14  ? 111 TYR B CA  1 
ATOM   1766 C C   . TYR B 1 111 ? -26.351 34.338 20.358  1.00 34.18  ? 111 TYR B C   1 
ATOM   1767 O O   . TYR B 1 111 ? -27.146 34.015 21.249  1.00 39.08  ? 111 TYR B O   1 
ATOM   1768 C CB  . TYR B 1 111 ? -26.953 36.418 19.080  1.00 47.48  ? 111 TYR B CB  1 
ATOM   1769 C CG  . TYR B 1 111 ? -26.557 37.830 18.714  1.00 48.03  ? 111 TYR B CG  1 
ATOM   1770 C CD1 . TYR B 1 111 ? -26.680 38.866 19.629  1.00 47.10  ? 111 TYR B CD1 1 
ATOM   1771 C CD2 . TYR B 1 111 ? -26.016 38.117 17.466  1.00 43.26  ? 111 TYR B CD2 1 
ATOM   1772 C CE1 . TYR B 1 111 ? -26.306 40.157 19.301  1.00 48.56  ? 111 TYR B CE1 1 
ATOM   1773 C CE2 . TYR B 1 111 ? -25.636 39.402 17.130  1.00 49.96  ? 111 TYR B CE2 1 
ATOM   1774 C CZ  . TYR B 1 111 ? -25.784 40.419 18.052  1.00 53.51  ? 111 TYR B CZ  1 
ATOM   1775 O OH  . TYR B 1 111 ? -25.405 41.700 17.720  1.00 62.27  ? 111 TYR B OH  1 
ATOM   1776 N N   . VAL B 1 112 ? -25.740 33.437 19.587  1.00 33.90  ? 112 VAL B N   1 
ATOM   1777 C CA  . VAL B 1 112 ? -25.983 32.011 19.772  1.00 37.66  ? 112 VAL B CA  1 
ATOM   1778 C C   . VAL B 1 112 ? -25.323 31.519 21.056  1.00 35.50  ? 112 VAL B C   1 
ATOM   1779 O O   . VAL B 1 112 ? -25.921 30.764 21.830  1.00 38.28  ? 112 VAL B O   1 
ATOM   1780 C CB  . VAL B 1 112 ? -25.494 31.224 18.545  1.00 32.53  ? 112 VAL B CB  1 
ATOM   1781 C CG1 . VAL B 1 112 ? -25.718 29.739 18.746  1.00 34.10  ? 112 VAL B CG1 1 
ATOM   1782 C CG2 . VAL B 1 112 ? -26.212 31.708 17.293  1.00 34.95  ? 112 VAL B CG2 1 
ATOM   1783 N N   . CYS B 1 113 ? -24.077 31.938 21.300  1.00 37.74  ? 113 CYS B N   1 
ATOM   1784 C CA  . CYS B 1 113 ? -23.397 31.558 22.538  1.00 40.79  ? 113 CYS B CA  1 
ATOM   1785 C C   . CYS B 1 113 ? -24.150 32.070 23.761  1.00 38.84  ? 113 CYS B C   1 
ATOM   1786 O O   . CYS B 1 113 ? -24.237 31.378 24.784  1.00 38.62  ? 113 CYS B O   1 
ATOM   1787 C CB  . CYS B 1 113 ? -21.961 32.084 22.530  1.00 36.94  ? 113 CYS B CB  1 
ATOM   1788 S SG  . CYS B 1 113 ? -20.916 31.385 21.227  1.00 45.80  ? 113 CYS B SG  1 
ATOM   1789 N N   . LEU B 1 114 ? -24.706 33.281 23.670  1.00 34.49  ? 114 LEU B N   1 
ATOM   1790 C CA  . LEU B 1 114 ? -25.507 33.825 24.764  1.00 40.37  ? 114 LEU B CA  1 
ATOM   1791 C C   . LEU B 1 114 ? -26.725 32.952 25.037  1.00 41.05  ? 114 LEU B C   1 
ATOM   1792 O O   . LEU B 1 114 ? -27.036 32.634 26.192  1.00 41.58  ? 114 LEU B O   1 
ATOM   1793 C CB  . LEU B 1 114 ? -25.938 35.253 24.431  1.00 38.70  ? 114 LEU B CB  1 
ATOM   1794 C CG  . LEU B 1 114 ? -26.825 35.963 25.457  1.00 47.17  ? 114 LEU B CG  1 
ATOM   1795 C CD1 . LEU B 1 114 ? -26.101 36.102 26.793  1.00 40.87  ? 114 LEU B CD1 1 
ATOM   1796 C CD2 . LEU B 1 114 ? -27.270 37.321 24.934  1.00 41.29  ? 114 LEU B CD2 1 
ATOM   1797 N N   . LEU B 1 115 ? -27.426 32.552 23.974  1.00 37.84  ? 115 LEU B N   1 
ATOM   1798 C CA  . LEU B 1 115 ? -28.617 31.724 24.126  1.00 34.32  ? 115 LEU B CA  1 
ATOM   1799 C C   . LEU B 1 115 ? -28.265 30.337 24.645  1.00 39.33  ? 115 LEU B C   1 
ATOM   1800 O O   . LEU B 1 115 ? -28.995 29.771 25.469  1.00 35.67  ? 115 LEU B O   1 
ATOM   1801 C CB  . LEU B 1 115 ? -29.348 31.628 22.789  1.00 35.07  ? 115 LEU B CB  1 
ATOM   1802 C CG  . LEU B 1 115 ? -30.172 32.862 22.422  1.00 36.56  ? 115 LEU B CG  1 
ATOM   1803 C CD1 . LEU B 1 115 ? -30.839 32.670 21.086  1.00 38.44  ? 115 LEU B CD1 1 
ATOM   1804 C CD2 . LEU B 1 115 ? -31.215 33.149 23.487  1.00 43.47  ? 115 LEU B CD2 1 
ATOM   1805 N N   . GLU B 1 116 ? -27.150 29.773 24.178  1.00 30.37  ? 116 GLU B N   1 
ATOM   1806 C CA  . GLU B 1 116 ? -26.767 28.430 24.604  1.00 32.72  ? 116 GLU B CA  1 
ATOM   1807 C C   . GLU B 1 116 ? -26.415 28.396 26.085  1.00 34.42  ? 116 GLU B C   1 
ATOM   1808 O O   . GLU B 1 116 ? -26.781 27.453 26.796  1.00 43.31  ? 116 GLU B O   1 
ATOM   1809 C CB  . GLU B 1 116 ? -25.596 27.927 23.760  1.00 44.66  ? 116 GLU B CB  1 
ATOM   1810 C CG  . GLU B 1 116 ? -25.295 26.441 23.914  1.00 42.58  ? 116 GLU B CG  1 
ATOM   1811 C CD  . GLU B 1 116 ? -24.373 26.139 25.078  1.00 46.58  ? 116 GLU B CD  1 
ATOM   1812 O OE1 . GLU B 1 116 ? -23.675 27.065 25.538  1.00 50.84  ? 116 GLU B OE1 1 
ATOM   1813 O OE2 . GLU B 1 116 ? -24.337 24.975 25.531  1.00 49.23  ? 116 GLU B OE2 1 
ATOM   1814 N N   . SER B 1 117 ? -25.709 29.419 26.569  1.00 34.22  ? 117 SER B N   1 
ATOM   1815 C CA  . SER B 1 117 ? -25.302 29.433 27.971  1.00 50.02  ? 117 SER B CA  1 
ATOM   1816 C C   . SER B 1 117 ? -26.486 29.644 28.908  1.00 41.78  ? 117 SER B C   1 
ATOM   1817 O O   . SER B 1 117 ? -26.475 29.146 30.040  1.00 51.20  ? 117 SER B O   1 
ATOM   1818 C CB  . SER B 1 117 ? -24.248 30.517 28.197  1.00 46.66  ? 117 SER B CB  1 
ATOM   1819 O OG  . SER B 1 117 ? -24.803 31.808 28.011  1.00 50.56  ? 117 SER B OG  1 
ATOM   1820 N N   . ARG B 1 118 ? -27.507 30.375 28.464  1.00 41.51  ? 118 ARG B N   1 
ATOM   1821 C CA  . ARG B 1 118 ? -28.683 30.614 29.290  1.00 43.94  ? 118 ARG B CA  1 
ATOM   1822 C C   . ARG B 1 118 ? -29.722 29.507 29.168  1.00 42.25  ? 118 ARG B C   1 
ATOM   1823 O O   . ARG B 1 118 ? -30.480 29.272 30.117  1.00 47.41  ? 118 ARG B O   1 
ATOM   1824 C CB  . ARG B 1 118 ? -29.337 31.945 28.913  1.00 46.30  ? 118 ARG B CB  1 
ATOM   1825 C CG  . ARG B 1 118 ? -28.458 33.175 29.087  1.00 52.17  ? 118 ARG B CG  1 
ATOM   1826 C CD  . ARG B 1 118 ? -27.899 33.323 30.490  1.00 56.76  ? 118 ARG B CD  1 
ATOM   1827 N NE  . ARG B 1 118 ? -28.583 34.376 31.232  1.00 71.09  ? 118 ARG B NE  1 
ATOM   1828 C CZ  . ARG B 1 118 ? -28.138 35.619 31.360  1.00 70.29  ? 118 ARG B CZ  1 
ATOM   1829 N NH1 . ARG B 1 118 ? -27.027 36.025 30.762  1.00 72.37  ? 118 ARG B NH1 1 
ATOM   1830 N NH2 . ARG B 1 118 ? -28.834 36.484 32.092  1.00 76.72  ? 118 ARG B NH2 1 
ATOM   1831 N N   . PHE B 1 119 ? -29.783 28.828 28.024  1.00 36.91  ? 119 PHE B N   1 
ATOM   1832 C CA  . PHE B 1 119 ? -30.780 27.790 27.756  1.00 39.86  ? 119 PHE B CA  1 
ATOM   1833 C C   . PHE B 1 119 ? -30.069 26.546 27.238  1.00 38.64  ? 119 PHE B C   1 
ATOM   1834 O O   . PHE B 1 119 ? -30.114 26.243 26.040  1.00 38.89  ? 119 PHE B O   1 
ATOM   1835 C CB  . PHE B 1 119 ? -31.819 28.277 26.744  1.00 43.32  ? 119 PHE B CB  1 
ATOM   1836 C CG  . PHE B 1 119 ? -32.583 29.497 27.185  1.00 44.82  ? 119 PHE B CG  1 
ATOM   1837 C CD1 . PHE B 1 119 ? -32.073 30.766 26.959  1.00 41.71  ? 119 PHE B CD1 1 
ATOM   1838 C CD2 . PHE B 1 119 ? -33.821 29.377 27.798  1.00 39.94  ? 119 PHE B CD2 1 
ATOM   1839 C CE1 . PHE B 1 119 ? -32.771 31.890 27.350  1.00 40.22  ? 119 PHE B CE1 1 
ATOM   1840 C CE2 . PHE B 1 119 ? -34.526 30.499 28.191  1.00 45.42  ? 119 PHE B CE2 1 
ATOM   1841 C CZ  . PHE B 1 119 ? -33.999 31.757 27.966  1.00 39.48  ? 119 PHE B CZ  1 
ATOM   1842 N N   . PRO B 1 120 ? -29.405 25.790 28.122  1.00 40.96  ? 120 PRO B N   1 
ATOM   1843 C CA  . PRO B 1 120 ? -28.566 24.673 27.650  1.00 43.10  ? 120 PRO B CA  1 
ATOM   1844 C C   . PRO B 1 120 ? -29.348 23.500 27.074  1.00 37.05  ? 120 PRO B C   1 
ATOM   1845 O O   . PRO B 1 120 ? -28.734 22.617 26.460  1.00 31.81  ? 120 PRO B O   1 
ATOM   1846 C CB  . PRO B 1 120 ? -27.783 24.251 28.903  1.00 51.20  ? 120 PRO B CB  1 
ATOM   1847 C CG  . PRO B 1 120 ? -28.373 24.998 30.060  1.00 46.29  ? 120 PRO B CG  1 
ATOM   1848 C CD  . PRO B 1 120 ? -29.486 25.875 29.590  1.00 46.42  ? 120 PRO B CD  1 
ATOM   1849 N N   . ASP B 1 121 ? -30.664 23.449 27.260  1.00 41.57  ? 121 ASP B N   1 
ATOM   1850 C CA  . ASP B 1 121 ? -31.486 22.404 26.664  1.00 42.60  ? 121 ASP B CA  1 
ATOM   1851 C C   . ASP B 1 121 ? -31.999 22.768 25.278  1.00 42.51  ? 121 ASP B C   1 
ATOM   1852 O O   . ASP B 1 121 ? -32.592 21.915 24.610  1.00 44.40  ? 121 ASP B O   1 
ATOM   1853 C CB  . ASP B 1 121 ? -32.684 22.086 27.569  1.00 54.44  ? 121 ASP B CB  1 
ATOM   1854 C CG  . ASP B 1 121 ? -32.337 21.122 28.684  1.00 60.50  ? 121 ASP B CG  1 
ATOM   1855 O OD1 . ASP B 1 121 ? -31.254 20.499 28.625  1.00 54.65  ? 121 ASP B OD1 1 
ATOM   1856 O OD2 . ASP B 1 121 ? -33.152 20.978 29.619  1.00 72.51  ? 121 ASP B OD2 1 
ATOM   1857 N N   . LEU B 1 122 ? -31.771 23.996 24.826  1.00 32.34  ? 122 LEU B N   1 
ATOM   1858 C CA  . LEU B 1 122 ? -32.445 24.514 23.644  1.00 41.72  ? 122 LEU B CA  1 
ATOM   1859 C C   . LEU B 1 122 ? -31.750 24.057 22.366  1.00 33.67  ? 122 LEU B C   1 
ATOM   1860 O O   . LEU B 1 122 ? -30.541 24.251 22.201  1.00 34.05  ? 122 LEU B O   1 
ATOM   1861 C CB  . LEU B 1 122 ? -32.490 26.040 23.698  1.00 35.61  ? 122 LEU B CB  1 
ATOM   1862 C CG  . LEU B 1 122 ? -33.262 26.754 22.590  1.00 42.28  ? 122 LEU B CG  1 
ATOM   1863 C CD1 . LEU B 1 122 ? -34.759 26.547 22.755  1.00 45.25  ? 122 LEU B CD1 1 
ATOM   1864 C CD2 . LEU B 1 122 ? -32.911 28.226 22.583  1.00 36.21  ? 122 LEU B CD2 1 
ATOM   1865 N N   . GLN B 1 123 ? -32.518 23.458 21.456  1.00 39.73  ? 123 GLN B N   1 
ATOM   1866 C CA  . GLN B 1 123 ? -32.021 23.201 20.110  1.00 30.23  ? 123 GLN B CA  1 
ATOM   1867 C C   . GLN B 1 123 ? -32.113 24.492 19.310  1.00 33.77  ? 123 GLN B C   1 
ATOM   1868 O O   . GLN B 1 123 ? -33.196 25.073 19.185  1.00 41.08  ? 123 GLN B O   1 
ATOM   1869 C CB  . GLN B 1 123 ? -32.807 22.086 19.426  1.00 29.50  ? 123 GLN B CB  1 
ATOM   1870 C CG  . GLN B 1 123 ? -32.255 21.738 18.050  1.00 37.69  ? 123 GLN B CG  1 
ATOM   1871 C CD  . GLN B 1 123 ? -33.086 20.710 17.310  1.00 38.21  ? 123 GLN B CD  1 
ATOM   1872 O OE1 . GLN B 1 123 ? -34.232 20.966 16.940  1.00 43.63  ? 123 GLN B OE1 1 
ATOM   1873 N NE2 . GLN B 1 123 ? -32.502 19.545 17.071  1.00 44.81  ? 123 GLN B NE2 1 
ATOM   1874 N N   . ILE B 1 124 ? -30.985 24.953 18.787  1.00 31.85  ? 124 ILE B N   1 
ATOM   1875 C CA  . ILE B 1 124 ? -30.928 26.197 18.033  1.00 30.23  ? 124 ILE B CA  1 
ATOM   1876 C C   . ILE B 1 124 ? -30.557 25.852 16.599  1.00 34.83  ? 124 ILE B C   1 
ATOM   1877 O O   . ILE B 1 124 ? -29.444 25.385 16.329  1.00 39.77  ? 124 ILE B O   1 
ATOM   1878 C CB  . ILE B 1 124 ? -29.938 27.192 18.649  1.00 35.72  ? 124 ILE B CB  1 
ATOM   1879 C CG1 . ILE B 1 124 ? -30.316 27.467 20.106  1.00 33.60  ? 124 ILE B CG1 1 
ATOM   1880 C CG2 . ILE B 1 124 ? -29.907 28.477 17.840  1.00 40.44  ? 124 ILE B CG2 1 
ATOM   1881 C CD1 . ILE B 1 124 ? -29.199 28.063 20.930  1.00 37.97  ? 124 ILE B CD1 1 
ATOM   1882 N N   . ASN B 1 125 ? -31.492 26.072 15.678  1.00 33.19  ? 125 ASN B N   1 
ATOM   1883 C CA  . ASN B 1 125 ? -31.298 25.766 14.268  1.00 31.18  ? 125 ASN B CA  1 
ATOM   1884 C C   . ASN B 1 125 ? -31.074 27.057 13.493  1.00 33.02  ? 125 ASN B C   1 
ATOM   1885 O O   . ASN B 1 125 ? -31.939 27.938 13.481  1.00 32.85  ? 125 ASN B O   1 
ATOM   1886 C CB  . ASN B 1 125 ? -32.492 24.993 13.709  1.00 31.56  ? 125 ASN B CB  1 
ATOM   1887 C CG  . ASN B 1 125 ? -32.820 23.764 14.536  1.00 44.42  ? 125 ASN B CG  1 
ATOM   1888 O OD1 . ASN B 1 125 ? -31.964 22.906 14.759  1.00 37.37  ? 125 ASN B OD1 1 
ATOM   1889 N ND2 . ASN B 1 125 ? -34.062 23.673 14.997  1.00 43.98  ? 125 ASN B ND2 1 
ATOM   1890 N N   . ILE B 1 126 ? -29.917 27.162 12.848  1.00 37.38  ? 126 ILE B N   1 
ATOM   1891 C CA  . ILE B 1 126 ? -29.526 28.345 12.093  1.00 35.04  ? 126 ILE B CA  1 
ATOM   1892 C C   . ILE B 1 126 ? -29.691 28.020 10.612  1.00 36.58  ? 126 ILE B C   1 
ATOM   1893 O O   . ILE B 1 126 ? -28.936 27.209 10.064  1.00 40.69  ? 126 ILE B O   1 
ATOM   1894 C CB  . ILE B 1 126 ? -28.083 28.768 12.409  1.00 34.16  ? 126 ILE B CB  1 
ATOM   1895 C CG1 . ILE B 1 126 ? -27.849 28.841 13.918  1.00 33.24  ? 126 ILE B CG1 1 
ATOM   1896 C CG2 . ILE B 1 126 ? -27.763 30.095 11.741  1.00 37.84  ? 126 ILE B CG2 1 
ATOM   1897 C CD1 . ILE B 1 126 ? -28.479 30.044 14.573  1.00 36.09  ? 126 ILE B CD1 1 
ATOM   1898 N N   . VAL B 1 127 ? -30.674 28.642 9.963   1.00 31.12  ? 127 VAL B N   1 
ATOM   1899 C CA  . VAL B 1 127 ? -30.870 28.501 8.526   1.00 39.41  ? 127 VAL B CA  1 
ATOM   1900 C C   . VAL B 1 127 ? -30.563 29.837 7.851   1.00 39.15  ? 127 VAL B C   1 
ATOM   1901 O O   . VAL B 1 127 ? -30.464 30.880 8.496   1.00 33.24  ? 127 VAL B O   1 
ATOM   1902 C CB  . VAL B 1 127 ? -32.290 28.012 8.173   1.00 32.06  ? 127 VAL B CB  1 
ATOM   1903 C CG1 . VAL B 1 127 ? -32.517 26.610 8.705   1.00 42.61  ? 127 VAL B CG1 1 
ATOM   1904 C CG2 . VAL B 1 127 ? -33.335 28.968 8.721   1.00 31.98  ? 127 VAL B CG2 1 
ATOM   1905 N N   . SER B 1 128 ? -30.411 29.791 6.528   1.00 35.35  ? 128 SER B N   1 
ATOM   1906 C CA  . SER B 1 128 ? -30.158 30.976 5.724   1.00 34.24  ? 128 SER B CA  1 
ATOM   1907 C C   . SER B 1 128 ? -31.117 30.996 4.543   1.00 41.65  ? 128 SER B C   1 
ATOM   1908 O O   . SER B 1 128 ? -31.539 29.947 4.048   1.00 44.45  ? 128 SER B O   1 
ATOM   1909 C CB  . SER B 1 128 ? -28.708 31.030 5.226   1.00 43.90  ? 128 SER B CB  1 
ATOM   1910 O OG  . SER B 1 128 ? -28.377 29.887 4.457   1.00 51.07  ? 128 SER B OG  1 
ATOM   1911 N N   . ALA B 1 129 ? -31.458 32.200 4.096   1.00 35.42  ? 129 ALA B N   1 
ATOM   1912 C CA  . ALA B 1 129 ? -32.433 32.383 3.033   1.00 41.46  ? 129 ALA B CA  1 
ATOM   1913 C C   . ALA B 1 129 ? -32.305 33.799 2.503   1.00 39.80  ? 129 ALA B C   1 
ATOM   1914 O O   . ALA B 1 129 ? -31.698 34.658 3.159   1.00 44.50  ? 129 ALA B O   1 
ATOM   1915 C CB  . ALA B 1 129 ? -33.863 32.117 3.539   1.00 35.49  ? 129 ALA B CB  1 
ATOM   1916 N N   . PRO B 1 130 ? -32.837 34.082 1.317   1.00 51.42  ? 130 PRO B N   1 
ATOM   1917 C CA  . PRO B 1 130 ? -32.940 35.474 0.877   1.00 46.04  ? 130 PRO B CA  1 
ATOM   1918 C C   . PRO B 1 130 ? -33.907 36.257 1.755   1.00 46.76  ? 130 PRO B C   1 
ATOM   1919 O O   . PRO B 1 130 ? -34.763 35.687 2.435   1.00 44.91  ? 130 PRO B O   1 
ATOM   1920 C CB  . PRO B 1 130 ? -33.449 35.364 -0.565  1.00 42.87  ? 130 PRO B CB  1 
ATOM   1921 C CG  . PRO B 1 130 ? -33.194 33.952 -0.972  1.00 52.64  ? 130 PRO B CG  1 
ATOM   1922 C CD  . PRO B 1 130 ? -33.264 33.130 0.272   1.00 41.91  ? 130 PRO B CD  1 
ATOM   1923 N N   . GLN B 1 131 ? -33.748 37.584 1.729   1.00 51.82  ? 131 GLN B N   1 
ATOM   1924 C CA  . GLN B 1 131 ? -34.582 38.486 2.520   1.00 46.16  ? 131 GLN B CA  1 
ATOM   1925 C C   . GLN B 1 131 ? -36.063 38.139 2.429   1.00 45.43  ? 131 GLN B C   1 
ATOM   1926 O O   . GLN B 1 131 ? -36.753 38.026 3.447   1.00 55.37  ? 131 GLN B O   1 
ATOM   1927 C CB  . GLN B 1 131 ? -34.353 39.933 2.062   1.00 56.11  ? 131 GLN B CB  1 
ATOM   1928 C CG  . GLN B 1 131 ? -33.102 40.616 2.608   1.00 62.07  ? 131 GLN B CG  1 
ATOM   1929 C CD  . GLN B 1 131 ? -33.294 41.135 4.020   1.00 60.38  ? 131 GLN B CD  1 
ATOM   1930 O OE1 . GLN B 1 131 ? -32.346 41.576 4.670   1.00 44.12  ? 131 GLN B OE1 1 
ATOM   1931 N NE2 . GLN B 1 131 ? -34.530 41.082 4.504   1.00 58.90  ? 131 GLN B NE2 1 
ATOM   1932 N N   . GLU B 1 132 ? -36.560 37.947 1.208   1.00 44.29  ? 132 GLU B N   1 
ATOM   1933 C CA  . GLU B 1 132 ? -37.994 37.763 1.005   1.00 53.54  ? 132 GLU B CA  1 
ATOM   1934 C C   . GLU B 1 132 ? -38.468 36.431 1.573   1.00 52.56  ? 132 GLU B C   1 
ATOM   1935 O O   . GLU B 1 132 ? -39.565 36.348 2.137   1.00 49.96  ? 132 GLU B O   1 
ATOM   1936 C CB  . GLU B 1 132 ? -38.337 37.864 -0.485  1.00 57.50  ? 132 GLU B CB  1 
ATOM   1937 C CG  . GLU B 1 132 ? -37.401 37.109 -1.430  1.00 64.74  ? 132 GLU B CG  1 
ATOM   1938 C CD  . GLU B 1 132 ? -36.092 37.823 -1.715  1.00 63.73  ? 132 GLU B CD  1 
ATOM   1939 O OE1 . GLU B 1 132 ? -35.607 38.582 -0.850  1.00 60.01  ? 132 GLU B OE1 1 
ATOM   1940 O OE2 . GLU B 1 132 ? -35.539 37.611 -2.813  1.00 62.62  ? 132 GLU B OE2 1 
ATOM   1941 N N   . ASP B 1 133 ? -37.660 35.378 1.434   1.00 48.87  ? 133 ASP B N   1 
ATOM   1942 C CA  . ASP B 1 133 ? -38.041 34.091 2.003   1.00 48.49  ? 133 ASP B CA  1 
ATOM   1943 C C   . ASP B 1 133 ? -37.947 34.116 3.522   1.00 44.57  ? 133 ASP B C   1 
ATOM   1944 O O   . ASP B 1 133 ? -38.779 33.512 4.210   1.00 47.70  ? 133 ASP B O   1 
ATOM   1945 C CB  . ASP B 1 133 ? -37.165 32.983 1.429   1.00 47.14  ? 133 ASP B CB  1 
ATOM   1946 C CG  . ASP B 1 133 ? -37.323 32.840 -0.066  1.00 59.16  ? 133 ASP B CG  1 
ATOM   1947 O OD1 . ASP B 1 133 ? -38.373 32.328 -0.511  1.00 69.71  ? 133 ASP B OD1 1 
ATOM   1948 O OD2 . ASP B 1 133 ? -36.403 33.254 -0.800  1.00 67.24  ? 133 ASP B OD2 1 
ATOM   1949 N N   . ALA B 1 134 ? -36.939 34.808 4.061   1.00 43.62  ? 134 ALA B N   1 
ATOM   1950 C CA  . ALA B 1 134 ? -36.803 34.909 5.510   1.00 44.43  ? 134 ALA B CA  1 
ATOM   1951 C C   . ALA B 1 134 ? -38.013 35.594 6.130   1.00 44.05  ? 134 ALA B C   1 
ATOM   1952 O O   . ALA B 1 134 ? -38.494 35.180 7.191   1.00 41.02  ? 134 ALA B O   1 
ATOM   1953 C CB  . ALA B 1 134 ? -35.521 35.661 5.860   1.00 33.37  ? 134 ALA B CB  1 
ATOM   1954 N N   . LEU B 1 135 ? -38.521 36.642 5.478   1.00 42.33  ? 135 LEU B N   1 
ATOM   1955 C CA  . LEU B 1 135 ? -39.715 37.327 5.965   1.00 42.06  ? 135 LEU B CA  1 
ATOM   1956 C C   . LEU B 1 135 ? -40.902 36.376 6.043   1.00 48.01  ? 135 LEU B C   1 
ATOM   1957 O O   . LEU B 1 135 ? -41.617 36.336 7.051   1.00 48.17  ? 135 LEU B O   1 
ATOM   1958 C CB  . LEU B 1 135 ? -40.037 38.516 5.058   1.00 47.71  ? 135 LEU B CB  1 
ATOM   1959 C CG  . LEU B 1 135 ? -41.056 39.530 5.581   1.00 55.95  ? 135 LEU B CG  1 
ATOM   1960 C CD1 . LEU B 1 135 ? -40.882 39.739 7.073   1.00 52.36  ? 135 LEU B CD1 1 
ATOM   1961 C CD2 . LEU B 1 135 ? -40.914 40.847 4.837   1.00 57.51  ? 135 LEU B CD2 1 
ATOM   1962 N N   . GLN B 1 136 ? -41.124 35.599 4.979   1.00 42.42  ? 136 GLN B N   1 
ATOM   1963 C CA  . GLN B 1 136 ? -42.226 34.644 4.968   1.00 46.30  ? 136 GLN B CA  1 
ATOM   1964 C C   . GLN B 1 136 ? -42.057 33.573 6.039   1.00 42.45  ? 136 GLN B C   1 
ATOM   1965 O O   . GLN B 1 136 ? -43.052 33.072 6.578   1.00 50.95  ? 136 GLN B O   1 
ATOM   1966 C CB  . GLN B 1 136 ? -42.339 33.997 3.587   1.00 48.41  ? 136 GLN B CB  1 
ATOM   1967 C CG  . GLN B 1 136 ? -42.715 34.961 2.466   1.00 55.15  ? 136 GLN B CG  1 
ATOM   1968 C CD  . GLN B 1 136 ? -43.976 35.749 2.764   1.00 57.86  ? 136 GLN B CD  1 
ATOM   1969 O OE1 . GLN B 1 136 ? -43.954 36.978 2.814   1.00 64.77  ? 136 GLN B OE1 1 
ATOM   1970 N NE2 . GLN B 1 136 ? -45.084 35.044 2.968   1.00 56.01  ? 136 GLN B NE2 1 
ATOM   1971 N N   . MET B 1 137 ? -40.813 33.208 6.358   1.00 42.10  ? 137 MET B N   1 
ATOM   1972 C CA  . MET B 1 137 ? -40.576 32.218 7.404   1.00 47.17  ? 137 MET B CA  1 
ATOM   1973 C C   . MET B 1 137 ? -41.002 32.741 8.768   1.00 40.48  ? 137 MET B C   1 
ATOM   1974 O O   . MET B 1 137 ? -41.534 31.986 9.590   1.00 41.72  ? 137 MET B O   1 
ATOM   1975 C CB  . MET B 1 137 ? -39.103 31.822 7.421   1.00 42.15  ? 137 MET B CB  1 
ATOM   1976 C CG  . MET B 1 137 ? -38.701 30.889 6.298   1.00 45.03  ? 137 MET B CG  1 
ATOM   1977 S SD  . MET B 1 137 ? -36.934 30.524 6.347   1.00 48.82  ? 137 MET B SD  1 
ATOM   1978 C CE  . MET B 1 137 ? -36.870 29.356 7.707   1.00 44.03  ? 137 MET B CE  1 
ATOM   1979 N N   . LEU B 1 138 ? -40.771 34.030 9.030   1.00 43.81  ? 138 LEU B N   1 
ATOM   1980 C CA  . LEU B 1 138 ? -41.261 34.638 10.262  1.00 40.93  ? 138 LEU B CA  1 
ATOM   1981 C C   . LEU B 1 138 ? -42.782 34.634 10.305  1.00 44.25  ? 138 LEU B C   1 
ATOM   1982 O O   . LEU B 1 138 ? -43.381 34.345 11.347  1.00 42.83  ? 138 LEU B O   1 
ATOM   1983 C CB  . LEU B 1 138 ? -40.737 36.069 10.385  1.00 36.83  ? 138 LEU B CB  1 
ATOM   1984 C CG  . LEU B 1 138 ? -39.246 36.311 10.618  1.00 29.79  ? 138 LEU B CG  1 
ATOM   1985 C CD1 . LEU B 1 138 ? -38.987 37.800 10.738  1.00 30.20  ? 138 LEU B CD1 1 
ATOM   1986 C CD2 . LEU B 1 138 ? -38.753 35.590 11.860  1.00 29.44  ? 138 LEU B CD2 1 
ATOM   1987 N N   . LEU B 1 139 ? -43.425 34.938 9.177   1.00 42.19  ? 139 LEU B N   1 
ATOM   1988 C CA  . LEU B 1 139 ? -44.872 35.124 9.173   1.00 48.06  ? 139 LEU B CA  1 
ATOM   1989 C C   . LEU B 1 139 ? -45.622 33.798 9.218   1.00 51.62  ? 139 LEU B C   1 
ATOM   1990 O O   . LEU B 1 139 ? -46.711 33.729 9.798   1.00 50.11  ? 139 LEU B O   1 
ATOM   1991 C CB  . LEU B 1 139 ? -45.289 35.936 7.947   1.00 47.63  ? 139 LEU B CB  1 
ATOM   1992 C CG  . LEU B 1 139 ? -44.718 37.357 7.908   1.00 55.59  ? 139 LEU B CG  1 
ATOM   1993 C CD1 . LEU B 1 139 ? -45.046 38.026 6.585   1.00 53.86  ? 139 LEU B CD1 1 
ATOM   1994 C CD2 . LEU B 1 139 ? -45.232 38.187 9.080   1.00 52.65  ? 139 LEU B CD2 1 
ATOM   1995 N N   . ASP B 1 140 ? -45.071 32.739 8.626   1.00 47.17  ? 140 ASP B N   1 
ATOM   1996 C CA  . ASP B 1 140 ? -45.713 31.432 8.703   1.00 52.07  ? 140 ASP B CA  1 
ATOM   1997 C C   . ASP B 1 140 ? -45.197 30.585 9.863   1.00 50.72  ? 140 ASP B C   1 
ATOM   1998 O O   . ASP B 1 140 ? -45.661 29.454 10.040  1.00 58.64  ? 140 ASP B O   1 
ATOM   1999 C CB  . ASP B 1 140 ? -45.574 30.680 7.363   1.00 53.65  ? 140 ASP B CB  1 
ATOM   2000 C CG  . ASP B 1 140 ? -44.173 30.120 7.115   1.00 59.41  ? 140 ASP B CG  1 
ATOM   2001 O OD1 . ASP B 1 140 ? -43.282 30.201 7.987   1.00 69.50  ? 140 ASP B OD1 1 
ATOM   2002 O OD2 . ASP B 1 140 ? -43.961 29.592 6.006   1.00 69.24  ? 140 ASP B OD2 1 
ATOM   2003 N N   . GLY B 1 141 ? -44.237 31.093 10.635  1.00 48.26  ? 141 GLY B N   1 
ATOM   2004 C CA  . GLY B 1 141 ? -43.849 30.488 11.890  1.00 43.68  ? 141 GLY B CA  1 
ATOM   2005 C C   . GLY B 1 141 ? -42.707 29.497 11.837  1.00 45.14  ? 141 GLY B C   1 
ATOM   2006 O O   . GLY B 1 141 ? -42.344 28.949 12.886  1.00 42.59  ? 141 GLY B O   1 
ATOM   2007 N N   . SER B 1 142 ? -42.129 29.240 10.662  1.00 38.59  ? 142 SER B N   1 
ATOM   2008 C CA  . SER B 1 142 ? -41.036 28.277 10.584  1.00 37.97  ? 142 SER B CA  1 
ATOM   2009 C C   . SER B 1 142 ? -39.727 28.843 11.118  1.00 45.45  ? 142 SER B C   1 
ATOM   2010 O O   . SER B 1 142 ? -38.773 28.084 11.317  1.00 47.06  ? 142 SER B O   1 
ATOM   2011 C CB  . SER B 1 142 ? -40.861 27.798 9.143   1.00 39.21  ? 142 SER B CB  1 
ATOM   2012 O OG  . SER B 1 142 ? -41.049 28.865 8.233   1.00 53.08  ? 142 SER B OG  1 
ATOM   2013 N N   . ALA B 1 143 ? -39.659 30.152 11.348  1.00 41.54  ? 143 ALA B N   1 
ATOM   2014 C CA  . ALA B 1 143 ? -38.544 30.782 12.038  1.00 32.32  ? 143 ALA B CA  1 
ATOM   2015 C C   . ALA B 1 143 ? -39.092 31.773 13.054  1.00 38.23  ? 143 ALA B C   1 
ATOM   2016 O O   . ALA B 1 143 ? -40.085 32.459 12.800  1.00 44.00  ? 143 ALA B O   1 
ATOM   2017 C CB  . ALA B 1 143 ? -37.592 31.498 11.066  1.00 32.31  ? 143 ALA B CB  1 
ATOM   2018 N N   . GLN B 1 144 ? -38.438 31.840 14.212  1.00 29.59  ? 144 GLN B N   1 
ATOM   2019 C CA  . GLN B 1 144 ? -38.865 32.751 15.267  1.00 34.46  ? 144 GLN B CA  1 
ATOM   2020 C C   . GLN B 1 144 ? -38.131 34.082 15.212  1.00 33.10  ? 144 GLN B C   1 
ATOM   2021 O O   . GLN B 1 144 ? -38.691 35.113 15.605  1.00 39.11  ? 144 GLN B O   1 
ATOM   2022 C CB  . GLN B 1 144 ? -38.650 32.113 16.644  1.00 38.30  ? 144 GLN B CB  1 
ATOM   2023 C CG  . GLN B 1 144 ? -39.579 30.946 16.970  1.00 38.73  ? 144 GLN B CG  1 
ATOM   2024 C CD  . GLN B 1 144 ? -39.353 29.737 16.078  1.00 47.87  ? 144 GLN B CD  1 
ATOM   2025 O OE1 . GLN B 1 144 ? -38.280 29.132 16.089  1.00 43.23  ? 144 GLN B OE1 1 
ATOM   2026 N NE2 . GLN B 1 144 ? -40.367 29.382 15.297  1.00 47.66  ? 144 GLN B NE2 1 
ATOM   2027 N N   . LEU B 1 145 ? -36.892 34.081 14.728  1.00 35.25  ? 145 LEU B N   1 
ATOM   2028 C CA  . LEU B 1 145 ? -36.076 35.281 14.658  1.00 31.48  ? 145 LEU B CA  1 
ATOM   2029 C C   . LEU B 1 145 ? -35.368 35.321 13.314  1.00 32.82  ? 145 LEU B C   1 
ATOM   2030 O O   . LEU B 1 145 ? -35.121 34.283 12.694  1.00 25.11  ? 145 LEU B O   1 
ATOM   2031 C CB  . LEU B 1 145 ? -35.045 35.327 15.796  1.00 27.05  ? 145 LEU B CB  1 
ATOM   2032 C CG  . LEU B 1 145 ? -35.572 35.494 17.221  1.00 29.19  ? 145 LEU B CG  1 
ATOM   2033 C CD1 . LEU B 1 145 ? -34.442 35.404 18.228  1.00 28.22  ? 145 LEU B CD1 1 
ATOM   2034 C CD2 . LEU B 1 145 ? -36.303 36.813 17.371  1.00 33.56  ? 145 LEU B CD2 1 
ATOM   2035 N N   . ALA B 1 146 ? -35.043 36.530 12.871  1.00 30.60  ? 146 ALA B N   1 
ATOM   2036 C CA  . ALA B 1 146 ? -34.337 36.734 11.617  1.00 32.27  ? 146 ALA B CA  1 
ATOM   2037 C C   . ALA B 1 146 ? -33.282 37.815 11.791  1.00 28.75  ? 146 ALA B C   1 
ATOM   2038 O O   . ALA B 1 146 ? -33.498 38.796 12.509  1.00 32.33  ? 146 ALA B O   1 
ATOM   2039 C CB  . ALA B 1 146 ? -35.302 37.119 10.488  1.00 26.36  ? 146 ALA B CB  1 
ATOM   2040 N N   . LEU B 1 147 ? -32.134 37.622 11.151  1.00 30.93  ? 147 LEU B N   1 
ATOM   2041 C CA  . LEU B 1 147 ? -31.123 38.664 11.039  1.00 32.51  ? 147 LEU B CA  1 
ATOM   2042 C C   . LEU B 1 147 ? -31.228 39.267 9.648   1.00 33.09  ? 147 LEU B C   1 
ATOM   2043 O O   . LEU B 1 147 ? -31.011 38.574 8.649   1.00 30.89  ? 147 LEU B O   1 
ATOM   2044 C CB  . LEU B 1 147 ? -29.716 38.127 11.298  1.00 30.64  ? 147 LEU B CB  1 
ATOM   2045 C CG  . LEU B 1 147 ? -29.256 38.112 12.760  1.00 41.23  ? 147 LEU B CG  1 
ATOM   2046 C CD1 . LEU B 1 147 ? -30.125 37.220 13.649  1.00 40.27  ? 147 LEU B CD1 1 
ATOM   2047 C CD2 . LEU B 1 147 ? -27.791 37.720 12.845  1.00 37.01  ? 147 LEU B CD2 1 
ATOM   2048 N N   . MET B 1 148 ? -31.584 40.544 9.584   1.00 31.72  ? 148 MET B N   1 
ATOM   2049 C CA  . MET B 1 148 ? -31.837 41.200 8.316   1.00 34.01  ? 148 MET B CA  1 
ATOM   2050 C C   . MET B 1 148 ? -31.076 42.515 8.250   1.00 37.03  ? 148 MET B C   1 
ATOM   2051 O O   . MET B 1 148 ? -30.726 43.112 9.271   1.00 39.08  ? 148 MET B O   1 
ATOM   2052 C CB  . MET B 1 148 ? -33.340 41.455 8.114   1.00 30.76  ? 148 MET B CB  1 
ATOM   2053 C CG  . MET B 1 148 ? -34.186 40.191 8.054   1.00 32.64  ? 148 MET B CG  1 
ATOM   2054 S SD  . MET B 1 148 ? -35.965 40.506 8.002   1.00 48.61  ? 148 MET B SD  1 
ATOM   2055 C CE  . MET B 1 148 ? -36.554 39.186 6.939   1.00 51.78  ? 148 MET B CE  1 
ATOM   2056 N N   . PHE B 1 149 ? -30.809 42.944 7.022   1.00 36.29  ? 149 PHE B N   1 
ATOM   2057 C CA  . PHE B 1 149 ? -30.391 44.299 6.699   1.00 40.69  ? 149 PHE B CA  1 
ATOM   2058 C C   . PHE B 1 149 ? -31.520 44.934 5.899   1.00 42.89  ? 149 PHE B C   1 
ATOM   2059 O O   . PHE B 1 149 ? -32.459 44.247 5.497   1.00 60.22  ? 149 PHE B O   1 
ATOM   2060 C CB  . PHE B 1 149 ? -29.067 44.301 5.927   1.00 37.59  ? 149 PHE B CB  1 
ATOM   2061 C CG  . PHE B 1 149 ? -29.184 43.798 4.525   1.00 38.97  ? 149 PHE B CG  1 
ATOM   2062 C CD1 . PHE B 1 149 ? -29.333 42.446 4.278   1.00 39.79  ? 149 PHE B CD1 1 
ATOM   2063 C CD2 . PHE B 1 149 ? -29.092 44.666 3.453   1.00 42.02  ? 149 PHE B CD2 1 
ATOM   2064 C CE1 . PHE B 1 149 ? -29.429 41.969 2.990   1.00 40.00  ? 149 PHE B CE1 1 
ATOM   2065 C CE2 . PHE B 1 149 ? -29.178 44.197 2.158   1.00 45.07  ? 149 PHE B CE2 1 
ATOM   2066 C CZ  . PHE B 1 149 ? -29.347 42.844 1.926   1.00 46.02  ? 149 PHE B CZ  1 
ATOM   2067 N N   . GLU B 1 150 ? -31.418 46.245 5.664   1.00 46.23  ? 150 GLU B N   1 
ATOM   2068 C CA  . GLU B 1 150 ? -32.555 47.084 5.224   1.00 70.71  ? 150 GLU B CA  1 
ATOM   2069 C C   . GLU B 1 150 ? -33.652 46.333 4.466   1.00 68.63  ? 150 GLU B C   1 
ATOM   2070 O O   . GLU B 1 150 ? -34.717 46.049 5.021   1.00 60.80  ? 150 GLU B O   1 
ATOM   2071 C CB  . GLU B 1 150 ? -32.087 48.237 4.335   1.00 75.86  ? 150 GLU B CB  1 
ATOM   2072 C CG  . GLU B 1 150 ? -33.069 49.418 4.281   1.00 81.89  ? 150 GLU B CG  1 
ATOM   2073 C CD  . GLU B 1 150 ? -34.257 49.147 3.374   1.00 89.63  ? 150 GLU B CD  1 
ATOM   2074 O OE1 . GLU B 1 150 ? -34.060 49.012 2.150   1.00 86.69  ? 150 GLU B OE1 1 
ATOM   2075 O OE2 . GLU B 1 150 ? -35.391 49.034 3.888   1.00 90.78  ? 150 GLU B OE2 1 
ATOM   2076 N N   . LEU B 1 154 ? -39.620 45.624 4.950   1.00 61.59  ? 154 LEU B N   1 
ATOM   2077 C CA  . LEU B 1 154 ? -40.414 45.345 6.141   1.00 58.91  ? 154 LEU B CA  1 
ATOM   2078 C C   . LEU B 1 154 ? -41.742 46.094 6.117   1.00 65.61  ? 154 LEU B C   1 
ATOM   2079 O O   . LEU B 1 154 ? -41.891 47.064 5.377   1.00 74.70  ? 154 LEU B O   1 
ATOM   2080 C CB  . LEU B 1 154 ? -39.637 45.718 7.403   1.00 56.69  ? 154 LEU B CB  1 
ATOM   2081 C CG  . LEU B 1 154 ? -38.915 44.573 8.108   1.00 56.23  ? 154 LEU B CG  1 
ATOM   2082 C CD1 . LEU B 1 154 ? -37.919 43.872 7.204   1.00 57.72  ? 154 LEU B CD1 1 
ATOM   2083 C CD2 . LEU B 1 154 ? -38.240 45.085 9.363   1.00 52.30  ? 154 LEU B CD2 1 
ATOM   2084 N N   . ASP B 1 155 ? -42.699 45.655 6.931   1.00 62.78  ? 155 ASP B N   1 
ATOM   2085 C CA  . ASP B 1 155 ? -44.021 46.275 6.958   1.00 65.40  ? 155 ASP B CA  1 
ATOM   2086 C C   . ASP B 1 155 ? -44.524 46.333 8.398   1.00 61.87  ? 155 ASP B C   1 
ATOM   2087 O O   . ASP B 1 155 ? -43.761 46.205 9.360   1.00 60.25  ? 155 ASP B O   1 
ATOM   2088 C CB  . ASP B 1 155 ? -44.979 45.532 6.009   1.00 69.11  ? 155 ASP B CB  1 
ATOM   2089 C CG  . ASP B 1 155 ? -45.553 44.254 6.609   1.00 74.12  ? 155 ASP B CG  1 
ATOM   2090 O OD1 . ASP B 1 155 ? -46.283 44.317 7.619   1.00 73.44  ? 155 ASP B OD1 1 
ATOM   2091 O OD2 . ASP B 1 155 ? -45.273 43.168 6.059   1.00 75.54  ? 155 ASP B OD2 1 
ATOM   2092 N N   . ASN B 1 156 ? -45.839 46.523 8.534   1.00 61.64  ? 156 ASN B N   1 
ATOM   2093 C CA  . ASN B 1 156 ? -46.500 46.683 9.824   1.00 61.53  ? 156 ASN B CA  1 
ATOM   2094 C C   . ASN B 1 156 ? -46.365 45.468 10.736  1.00 56.43  ? 156 ASN B C   1 
ATOM   2095 O O   . ASN B 1 156 ? -46.470 45.620 11.956  1.00 47.63  ? 156 ASN B O   1 
ATOM   2096 C CB  . ASN B 1 156 ? -47.985 46.983 9.587   1.00 56.63  ? 156 ASN B CB  1 
ATOM   2097 C CG  . ASN B 1 156 ? -48.681 47.533 10.809  1.00 65.01  ? 156 ASN B CG  1 
ATOM   2098 O OD1 . ASN B 1 156 ? -49.684 46.978 11.254  1.00 80.34  ? 156 ASN B OD1 1 
ATOM   2099 N ND2 . ASN B 1 156 ? -48.162 48.629 11.355  1.00 76.23  ? 156 ASN B ND2 1 
ATOM   2100 N N   . ARG B 1 157 ? -46.131 44.277 10.187  1.00 47.66  ? 157 ARG B N   1 
ATOM   2101 C CA  . ARG B 1 157 ? -46.291 43.039 10.943  1.00 54.08  ? 157 ARG B CA  1 
ATOM   2102 C C   . ARG B 1 157 ? -45.020 42.558 11.637  1.00 56.66  ? 157 ARG B C   1 
ATOM   2103 O O   . ARG B 1 157 ? -45.090 41.610 12.429  1.00 47.42  ? 157 ARG B O   1 
ATOM   2104 C CB  . ARG B 1 157 ? -46.818 41.943 10.017  1.00 55.91  ? 157 ARG B CB  1 
ATOM   2105 C CG  . ARG B 1 157 ? -48.327 41.970 9.857   1.00 64.18  ? 157 ARG B CG  1 
ATOM   2106 C CD  . ARG B 1 157 ? -48.757 41.108 8.694   1.00 61.64  ? 157 ARG B CD  1 
ATOM   2107 N NE  . ARG B 1 157 ? -48.051 41.493 7.479   1.00 69.49  ? 157 ARG B NE  1 
ATOM   2108 C CZ  . ARG B 1 157 ? -47.921 40.722 6.409   1.00 68.93  ? 157 ARG B CZ  1 
ATOM   2109 N NH1 . ARG B 1 157 ? -48.392 39.486 6.387   1.00 71.72  ? 157 ARG B NH1 1 
ATOM   2110 N NH2 . ARG B 1 157 ? -47.302 41.203 5.335   1.00 59.04  ? 157 ARG B NH2 1 
ATOM   2111 N N   . GLU B 1 158 ? -43.873 43.177 11.375  1.00 48.63  ? 158 GLU B N   1 
ATOM   2112 C CA  . GLU B 1 158 ? -42.631 42.825 12.045  1.00 46.66  ? 158 GLU B CA  1 
ATOM   2113 C C   . GLU B 1 158 ? -42.239 43.897 13.053  1.00 50.93  ? 158 GLU B C   1 
ATOM   2114 O O   . GLU B 1 158 ? -42.552 45.078 12.888  1.00 52.01  ? 158 GLU B O   1 
ATOM   2115 C CB  . GLU B 1 158 ? -41.489 42.635 11.041  1.00 49.73  ? 158 GLU B CB  1 
ATOM   2116 C CG  . GLU B 1 158 ? -41.771 41.639 9.928   1.00 53.89  ? 158 GLU B CG  1 
ATOM   2117 C CD  . GLU B 1 158 ? -42.513 42.250 8.755   1.00 57.55  ? 158 GLU B CD  1 
ATOM   2118 O OE1 . GLU B 1 158 ? -41.977 43.187 8.127   1.00 58.70  ? 158 GLU B OE1 1 
ATOM   2119 O OE2 . GLU B 1 158 ? -43.634 41.789 8.459   1.00 56.02  ? 158 GLU B OE2 1 
ATOM   2120 N N   . GLN B 1 159 ? -41.563 43.469 14.110  1.00 47.90  ? 159 GLN B N   1 
ATOM   2121 C CA  . GLN B 1 159 ? -40.805 44.363 14.967  1.00 38.88  ? 159 GLN B CA  1 
ATOM   2122 C C   . GLN B 1 159 ? -39.330 44.042 14.802  1.00 43.49  ? 159 GLN B C   1 
ATOM   2123 O O   . GLN B 1 159 ? -38.954 43.008 14.248  1.00 37.58  ? 159 GLN B O   1 
ATOM   2124 C CB  . GLN B 1 159 ? -41.207 44.236 16.441  1.00 43.32  ? 159 GLN B CB  1 
ATOM   2125 C CG  . GLN B 1 159 ? -42.668 44.431 16.719  1.00 49.78  ? 159 GLN B CG  1 
ATOM   2126 C CD  . GLN B 1 159 ? -42.927 45.352 17.885  1.00 63.03  ? 159 GLN B CD  1 
ATOM   2127 O OE1 . GLN B 1 159 ? -43.010 46.569 17.730  1.00 74.73  ? 159 GLN B OE1 1 
ATOM   2128 N NE2 . GLN B 1 159 ? -43.044 44.773 19.071  1.00 62.15  ? 159 GLN B NE2 1 
ATOM   2129 N N   . PHE B 1 160 ? -38.486 44.937 15.299  1.00 41.04  ? 160 PHE B N   1 
ATOM   2130 C CA  . PHE B 1 160 ? -37.053 44.730 15.191  1.00 36.70  ? 160 PHE B CA  1 
ATOM   2131 C C   . PHE B 1 160 ? -36.337 45.559 16.241  1.00 36.75  ? 160 PHE B C   1 
ATOM   2132 O O   . PHE B 1 160 ? -36.894 46.506 16.801  1.00 39.53  ? 160 PHE B O   1 
ATOM   2133 C CB  . PHE B 1 160 ? -36.549 45.066 13.781  1.00 40.12  ? 160 PHE B CB  1 
ATOM   2134 C CG  . PHE B 1 160 ? -36.535 46.535 13.465  1.00 43.74  ? 160 PHE B CG  1 
ATOM   2135 C CD1 . PHE B 1 160 ? -35.446 47.328 13.802  1.00 45.71  ? 160 PHE B CD1 1 
ATOM   2136 C CD2 . PHE B 1 160 ? -37.618 47.124 12.839  1.00 47.16  ? 160 PHE B CD2 1 
ATOM   2137 C CE1 . PHE B 1 160 ? -35.442 48.676 13.516  1.00 49.65  ? 160 PHE B CE1 1 
ATOM   2138 C CE2 . PHE B 1 160 ? -37.619 48.472 12.550  1.00 52.57  ? 160 PHE B CE2 1 
ATOM   2139 C CZ  . PHE B 1 160 ? -36.529 49.249 12.889  1.00 49.31  ? 160 PHE B CZ  1 
ATOM   2140 N N   . VAL B 1 161 ? -35.094 45.166 16.509  1.00 36.88  ? 161 VAL B N   1 
ATOM   2141 C CA  . VAL B 1 161 ? -34.148 45.962 17.276  1.00 41.53  ? 161 VAL B CA  1 
ATOM   2142 C C   . VAL B 1 161 ? -32.821 45.963 16.532  1.00 36.67  ? 161 VAL B C   1 
ATOM   2143 O O   . VAL B 1 161 ? -32.435 44.973 15.901  1.00 34.17  ? 161 VAL B O   1 
ATOM   2144 C CB  . VAL B 1 161 ? -33.961 45.454 18.725  1.00 34.46  ? 161 VAL B CB  1 
ATOM   2145 C CG1 . VAL B 1 161 ? -35.274 45.509 19.481  1.00 47.20  ? 161 VAL B CG1 1 
ATOM   2146 C CG2 . VAL B 1 161 ? -33.410 44.043 18.726  1.00 34.84  ? 161 VAL B CG2 1 
ATOM   2147 N N   . GLU B 1 162 ? -32.127 47.094 16.604  1.00 32.03  ? 162 GLU B N   1 
ATOM   2148 C CA  . GLU B 1 162 ? -30.881 47.264 15.877  1.00 44.07  ? 162 GLU B CA  1 
ATOM   2149 C C   . GLU B 1 162 ? -29.759 46.497 16.562  1.00 42.05  ? 162 GLU B C   1 
ATOM   2150 O O   . GLU B 1 162 ? -29.662 46.478 17.793  1.00 47.97  ? 162 GLU B O   1 
ATOM   2151 C CB  . GLU B 1 162 ? -30.538 48.748 15.780  1.00 42.94  ? 162 GLU B CB  1 
ATOM   2152 C CG  . GLU B 1 162 ? -31.555 49.547 14.982  1.00 50.84  ? 162 GLU B CG  1 
ATOM   2153 C CD  . GLU B 1 162 ? -31.279 51.032 15.018  1.00 62.75  ? 162 GLU B CD  1 
ATOM   2154 O OE1 . GLU B 1 162 ? -30.627 51.486 15.980  1.00 65.48  ? 162 GLU B OE1 1 
ATOM   2155 O OE2 . GLU B 1 162 ? -31.728 51.746 14.097  1.00 69.61  ? 162 GLU B OE2 1 
ATOM   2156 N N   . LEU B 1 163 ? -28.919 45.847 15.755  1.00 40.38  ? 163 LEU B N   1 
ATOM   2157 C CA  . LEU B 1 163 ? -27.801 45.069 16.273  1.00 45.84  ? 163 LEU B CA  1 
ATOM   2158 C C   . LEU B 1 163 ? -26.472 45.793 16.096  1.00 49.81  ? 163 LEU B C   1 
ATOM   2159 O O   . LEU B 1 163 ? -25.849 46.197 17.081  1.00 60.12  ? 163 LEU B O   1 
ATOM   2160 C CB  . LEU B 1 163 ? -27.746 43.693 15.601  1.00 42.21  ? 163 LEU B CB  1 
ATOM   2161 C CG  . LEU B 1 163 ? -28.853 42.711 15.979  1.00 44.91  ? 163 LEU B CG  1 
ATOM   2162 C CD1 . LEU B 1 163 ? -28.606 41.351 15.350  1.00 40.73  ? 163 LEU B CD1 1 
ATOM   2163 C CD2 . LEU B 1 163 ? -28.958 42.596 17.487  1.00 45.42  ? 163 LEU B CD2 1 
ATOM   2164 N N   . LYS B 1 164 ? -26.030 45.967 14.855  1.00 40.30  ? 164 LYS B N   1 
ATOM   2165 C CA  . LYS B 1 164 ? -24.690 46.486 14.620  1.00 49.61  ? 164 LYS B CA  1 
ATOM   2166 C C   . LYS B 1 164 ? -24.523 46.821 13.143  1.00 43.29  ? 164 LYS B C   1 
ATOM   2167 O O   . LYS B 1 164 ? -25.330 46.440 12.292  1.00 45.83  ? 164 LYS B O   1 
ATOM   2168 C CB  . LYS B 1 164 ? -23.628 45.476 15.038  1.00 50.12  ? 164 LYS B CB  1 
ATOM   2169 C CG  . LYS B 1 164 ? -23.662 44.226 14.194  1.00 57.55  ? 164 LYS B CG  1 
ATOM   2170 C CD  . LYS B 1 164 ? -22.767 43.156 14.764  1.00 69.67  ? 164 LYS B CD  1 
ATOM   2171 C CE  . LYS B 1 164 ? -23.257 41.785 14.363  1.00 74.47  ? 164 LYS B CE  1 
ATOM   2172 N NZ  . LYS B 1 164 ? -24.733 41.653 14.489  1.00 78.42  ? 164 LYS B NZ  1 
ATOM   2173 N N   . ARG B 1 165 ? -23.439 47.529 12.864  1.00 42.82  ? 165 ARG B N   1 
ATOM   2174 C CA  . ARG B 1 165 ? -23.015 47.845 11.512  1.00 40.66  ? 165 ARG B CA  1 
ATOM   2175 C C   . ARG B 1 165 ? -21.951 46.845 11.075  1.00 48.41  ? 165 ARG B C   1 
ATOM   2176 O O   . ARG B 1 165 ? -21.095 46.446 11.871  1.00 49.83  ? 165 ARG B O   1 
ATOM   2177 C CB  . ARG B 1 165 ? -22.473 49.276 11.467  1.00 40.44  ? 165 ARG B CB  1 
ATOM   2178 C CG  . ARG B 1 165 ? -22.099 49.804 10.100  1.00 53.55  ? 165 ARG B CG  1 
ATOM   2179 C CD  . ARG B 1 165 ? -21.500 51.202 10.216  1.00 58.56  ? 165 ARG B CD  1 
ATOM   2180 N NE  . ARG B 1 165 ? -20.781 51.595 9.011   1.00 68.46  ? 165 ARG B NE  1 
ATOM   2181 C CZ  . ARG B 1 165 ? -19.612 51.095 8.632   1.00 66.17  ? 165 ARG B CZ  1 
ATOM   2182 N NH1 . ARG B 1 165 ? -18.942 50.245 9.394   1.00 62.18  ? 165 ARG B NH1 1 
ATOM   2183 N NH2 . ARG B 1 165 ? -19.098 51.466 7.464   1.00 66.37  ? 165 ARG B NH2 1 
ATOM   2184 N N   . GLU B 1 166 ? -22.028 46.417 9.818   1.00 38.08  ? 166 GLU B N   1 
ATOM   2185 C CA  . GLU B 1 166 ? -21.033 45.528 9.229   1.00 42.09  ? 166 GLU B CA  1 
ATOM   2186 C C   . GLU B 1 166 ? -20.425 46.223 8.019   1.00 40.85  ? 166 GLU B C   1 
ATOM   2187 O O   . GLU B 1 166 ? -21.139 46.550 7.066   1.00 37.71  ? 166 GLU B O   1 
ATOM   2188 C CB  . GLU B 1 166 ? -21.650 44.186 8.826   1.00 39.19  ? 166 GLU B CB  1 
ATOM   2189 C CG  . GLU B 1 166 ? -22.010 43.270 9.991   1.00 53.91  ? 166 GLU B CG  1 
ATOM   2190 C CD  . GLU B 1 166 ? -20.800 42.621 10.637  1.00 61.53  ? 166 GLU B CD  1 
ATOM   2191 O OE1 . GLU B 1 166 ? -19.713 42.626 10.025  1.00 60.00  ? 166 GLU B OE1 1 
ATOM   2192 O OE2 . GLU B 1 166 ? -20.939 42.087 11.756  1.00 59.01  ? 166 GLU B OE2 1 
ATOM   2193 N N   . ALA B 1 167 ? -19.117 46.457 8.063   1.00 34.32  ? 167 ALA B N   1 
ATOM   2194 C CA  . ALA B 1 167 ? -18.436 47.115 6.960   1.00 40.12  ? 167 ALA B CA  1 
ATOM   2195 C C   . ALA B 1 167 ? -18.121 46.114 5.858   1.00 36.10  ? 167 ALA B C   1 
ATOM   2196 O O   . ALA B 1 167 ? -17.853 44.939 6.122   1.00 32.50  ? 167 ALA B O   1 
ATOM   2197 C CB  . ALA B 1 167 ? -17.149 47.783 7.444   1.00 35.07  ? 167 ALA B CB  1 
ATOM   2198 N N   . LEU B 1 168 ? -18.171 46.582 4.616   1.00 37.01  ? 168 LEU B N   1 
ATOM   2199 C CA  . LEU B 1 168 ? -17.781 45.787 3.465   1.00 32.20  ? 168 LEU B CA  1 
ATOM   2200 C C   . LEU B 1 168 ? -16.694 46.520 2.693   1.00 40.68  ? 168 LEU B C   1 
ATOM   2201 O O   . LEU B 1 168 ? -16.520 47.734 2.831   1.00 33.71  ? 168 LEU B O   1 
ATOM   2202 C CB  . LEU B 1 168 ? -18.980 45.482 2.558   1.00 27.28  ? 168 LEU B CB  1 
ATOM   2203 C CG  . LEU B 1 168 ? -20.088 44.625 3.175   1.00 32.87  ? 168 LEU B CG  1 
ATOM   2204 C CD1 . LEU B 1 168 ? -21.290 45.471 3.529   1.00 33.61  ? 168 LEU B CD1 1 
ATOM   2205 C CD2 . LEU B 1 168 ? -20.484 43.501 2.231   1.00 33.78  ? 168 LEU B CD2 1 
ATOM   2206 N N   . ILE B 1 169 ? -15.944 45.766 1.896   1.00 36.28  ? 169 ILE B N   1 
ATOM   2207 C CA  . ILE B 1 169 ? -14.769 46.305 1.212   1.00 31.57  ? 169 ILE B CA  1 
ATOM   2208 C C   . ILE B 1 169 ? -14.772 45.907 -0.259  1.00 36.00  ? 169 ILE B C   1 
ATOM   2209 O O   . ILE B 1 169 ? -14.881 44.714 -0.578  1.00 33.02  ? 169 ILE B O   1 
ATOM   2210 C CB  . ILE B 1 169 ? -13.471 45.827 1.883   1.00 40.25  ? 169 ILE B CB  1 
ATOM   2211 C CG1 . ILE B 1 169 ? -13.464 46.165 3.372   1.00 47.65  ? 169 ILE B CG1 1 
ATOM   2212 C CG2 . ILE B 1 169 ? -12.253 46.435 1.196   1.00 43.17  ? 169 ILE B CG2 1 
ATOM   2213 C CD1 . ILE B 1 169 ? -12.365 45.459 4.136   1.00 48.32  ? 169 ILE B CD1 1 
ATOM   2214 N N   . PRO B 1 170 ? -14.638 46.856 -1.187  1.00 37.70  ? 170 PRO B N   1 
ATOM   2215 C CA  . PRO B 1 170 ? -14.438 46.478 -2.594  1.00 31.30  ? 170 PRO B CA  1 
ATOM   2216 C C   . PRO B 1 170 ? -13.038 45.919 -2.785  1.00 34.61  ? 170 PRO B C   1 
ATOM   2217 O O   . PRO B 1 170 ? -12.051 46.530 -2.365  1.00 31.26  ? 170 PRO B O   1 
ATOM   2218 C CB  . PRO B 1 170 ? -14.630 47.794 -3.358  1.00 25.97  ? 170 PRO B CB  1 
ATOM   2219 C CG  . PRO B 1 170 ? -14.465 48.880 -2.356  1.00 38.79  ? 170 PRO B CG  1 
ATOM   2220 C CD  . PRO B 1 170 ? -14.633 48.314 -0.976  1.00 34.71  ? 170 PRO B CD  1 
ATOM   2221 N N   . VAL B 1 171 ? -12.956 44.736 -3.402  1.00 27.68  ? 171 VAL B N   1 
ATOM   2222 C CA  . VAL B 1 171 ? -11.696 44.013 -3.517  1.00 33.17  ? 171 VAL B CA  1 
ATOM   2223 C C   . VAL B 1 171 ? -11.543 43.418 -4.911  1.00 26.59  ? 171 VAL B C   1 
ATOM   2224 O O   . VAL B 1 171 ? -12.510 43.253 -5.659  1.00 29.45  ? 171 VAL B O   1 
ATOM   2225 C CB  . VAL B 1 171 ? -11.563 42.893 -2.460  1.00 26.96  ? 171 VAL B CB  1 
ATOM   2226 C CG1 . VAL B 1 171 ? -11.562 43.471 -1.052  1.00 30.81  ? 171 VAL B CG1 1 
ATOM   2227 C CG2 . VAL B 1 171 ? -12.682 41.878 -2.623  1.00 24.13  ? 171 VAL B CG2 1 
ATOM   2228 N N   . ILE B 1 172 ? -10.293 43.081 -5.233  1.00 27.66  ? 172 ILE B N   1 
ATOM   2229 C CA  . ILE B 1 172 ? -9.934  42.423 -6.484  1.00 31.69  ? 172 ILE B CA  1 
ATOM   2230 C C   . ILE B 1 172 ? -8.710  41.561 -6.209  1.00 27.16  ? 172 ILE B C   1 
ATOM   2231 O O   . ILE B 1 172 ? -7.954  41.813 -5.268  1.00 35.92  ? 172 ILE B O   1 
ATOM   2232 C CB  . ILE B 1 172 ? -9.663  43.442 -7.618  1.00 28.00  ? 172 ILE B CB  1 
ATOM   2233 C CG1 . ILE B 1 172 ? -9.817  42.784 -8.987  1.00 31.87  ? 172 ILE B CG1 1 
ATOM   2234 C CG2 . ILE B 1 172 ? -8.281  44.053 -7.467  1.00 25.47  ? 172 ILE B CG2 1 
ATOM   2235 C CD1 . ILE B 1 172 ? -10.002 43.767 -10.126 1.00 32.82  ? 172 ILE B CD1 1 
ATOM   2236 N N   . SER B 1 173 ? -8.520  40.530 -7.028  1.00 31.85  ? 173 SER B N   1 
ATOM   2237 C CA  . SER B 1 173 ? -7.354  39.672 -6.865  1.00 29.46  ? 173 SER B CA  1 
ATOM   2238 C C   . SER B 1 173 ? -6.077  40.455 -7.148  1.00 31.13  ? 173 SER B C   1 
ATOM   2239 O O   . SER B 1 173 ? -6.030  41.281 -8.063  1.00 34.74  ? 173 SER B O   1 
ATOM   2240 C CB  . SER B 1 173 ? -7.451  38.467 -7.798  1.00 30.31  ? 173 SER B CB  1 
ATOM   2241 O OG  . SER B 1 173 ? -6.223  37.760 -7.857  1.00 32.21  ? 173 SER B OG  1 
ATOM   2242 N N   . LYS B 1 174 ? -5.032  40.187 -6.353  1.00 31.37  ? 174 LYS B N   1 
ATOM   2243 C CA  . LYS B 1 174 ? -3.757  40.876 -6.539  1.00 33.57  ? 174 LYS B CA  1 
ATOM   2244 C C   . LYS B 1 174 ? -3.127  40.590 -7.896  1.00 34.76  ? 174 LYS B C   1 
ATOM   2245 O O   . LYS B 1 174 ? -2.309  41.387 -8.368  1.00 39.86  ? 174 LYS B O   1 
ATOM   2246 C CB  . LYS B 1 174 ? -2.767  40.491 -5.438  1.00 38.91  ? 174 LYS B CB  1 
ATOM   2247 C CG  . LYS B 1 174 ? -3.006  41.161 -4.091  1.00 38.89  ? 174 LYS B CG  1 
ATOM   2248 C CD  . LYS B 1 174 ? -1.716  41.201 -3.282  1.00 48.28  ? 174 LYS B CD  1 
ATOM   2249 C CE  . LYS B 1 174 ? -1.975  41.061 -1.795  1.00 50.96  ? 174 LYS B CE  1 
ATOM   2250 N NZ  . LYS B 1 174 ? -2.203  42.378 -1.142  1.00 54.18  ? 174 LYS B NZ  1 
ATOM   2251 N N   . THR B 1 175 ? -3.477  39.477 -8.532  1.00 35.56  ? 175 THR B N   1 
ATOM   2252 C CA  . THR B 1 175 ? -2.928  39.117 -9.830  1.00 41.06  ? 175 THR B CA  1 
ATOM   2253 C C   . THR B 1 175 ? -3.824  39.530 -10.992 1.00 34.95  ? 175 THR B C   1 
ATOM   2254 O O   . THR B 1 175 ? -3.487  39.250 -12.142 1.00 41.71  ? 175 THR B O   1 
ATOM   2255 C CB  . THR B 1 175 ? -2.657  37.610 -9.889  1.00 33.94  ? 175 THR B CB  1 
ATOM   2256 O OG1 . THR B 1 175 ? -3.882  36.895 -9.724  1.00 34.40  ? 175 THR B OG1 1 
ATOM   2257 C CG2 . THR B 1 175 ? -1.675  37.195 -8.797  1.00 33.90  ? 175 THR B CG2 1 
ATOM   2258 N N   . HIS B 1 176 ? -4.952  40.171 -10.720 1.00 35.61  ? 176 HIS B N   1 
ATOM   2259 C CA  . HIS B 1 176 ? -5.777  40.721 -11.784 1.00 36.05  ? 176 HIS B CA  1 
ATOM   2260 C C   . HIS B 1 176 ? -5.036  41.877 -12.458 1.00 40.92  ? 176 HIS B C   1 
ATOM   2261 O O   . HIS B 1 176 ? -4.369  42.659 -11.776 1.00 38.83  ? 176 HIS B O   1 
ATOM   2262 C CB  . HIS B 1 176 ? -7.119  41.198 -11.220 1.00 29.22  ? 176 HIS B CB  1 
ATOM   2263 C CG  . HIS B 1 176 ? -8.158  41.475 -12.264 1.00 31.86  ? 176 HIS B CG  1 
ATOM   2264 N ND1 . HIS B 1 176 ? -8.131  42.597 -13.066 1.00 33.43  ? 176 HIS B ND1 1 
ATOM   2265 C CD2 . HIS B 1 176 ? -9.263  40.783 -12.627 1.00 33.27  ? 176 HIS B CD2 1 
ATOM   2266 C CE1 . HIS B 1 176 ? -9.169  42.580 -13.881 1.00 36.67  ? 176 HIS B CE1 1 
ATOM   2267 N NE2 . HIS B 1 176 ? -9.872  41.489 -13.637 1.00 38.43  ? 176 HIS B NE2 1 
ATOM   2268 N N   . PRO B 1 177 ? -5.120  42.000 -13.789 1.00 38.24  ? 177 PRO B N   1 
ATOM   2269 C CA  . PRO B 1 177 ? -4.422  43.112 -14.467 1.00 34.53  ? 177 PRO B CA  1 
ATOM   2270 C C   . PRO B 1 177 ? -4.740  44.478 -13.875 1.00 38.09  ? 177 PRO B C   1 
ATOM   2271 O O   . PRO B 1 177 ? -3.861  45.345 -13.807 1.00 48.13  ? 177 PRO B O   1 
ATOM   2272 C CB  . PRO B 1 177 ? -4.908  42.998 -15.917 1.00 35.02  ? 177 PRO B CB  1 
ATOM   2273 C CG  . PRO B 1 177 ? -5.349  41.583 -16.080 1.00 36.12  ? 177 PRO B CG  1 
ATOM   2274 C CD  . PRO B 1 177 ? -5.781  41.080 -14.734 1.00 36.09  ? 177 PRO B CD  1 
ATOM   2275 N N   . LEU B 1 178 ? -5.978  44.685 -13.424 1.00 39.89  ? 178 LEU B N   1 
ATOM   2276 C CA  . LEU B 1 178 ? -6.360  45.956 -12.822 1.00 40.60  ? 178 LEU B CA  1 
ATOM   2277 C C   . LEU B 1 178 ? -5.651  46.206 -11.498 1.00 39.34  ? 178 LEU B C   1 
ATOM   2278 O O   . LEU B 1 178 ? -5.523  47.363 -11.083 1.00 41.55  ? 178 LEU B O   1 
ATOM   2279 C CB  . LEU B 1 178 ? -7.878  45.991 -12.627 1.00 39.32  ? 178 LEU B CB  1 
ATOM   2280 C CG  . LEU B 1 178 ? -8.586  47.338 -12.526 1.00 50.66  ? 178 LEU B CG  1 
ATOM   2281 C CD1 . LEU B 1 178 ? -8.334  48.163 -13.776 1.00 47.77  ? 178 LEU B CD1 1 
ATOM   2282 C CD2 . LEU B 1 178 ? -10.081 47.137 -12.308 1.00 42.03  ? 178 LEU B CD2 1 
ATOM   2283 N N   . ALA B 1 179 ? -5.179  45.154 -10.831 1.00 37.52  ? 179 ALA B N   1 
ATOM   2284 C CA  . ALA B 1 179 ? -4.576  45.309 -9.514  1.00 42.71  ? 179 ALA B CA  1 
ATOM   2285 C C   . ALA B 1 179 ? -3.169  45.886 -9.560  1.00 41.98  ? 179 ALA B C   1 
ATOM   2286 O O   . ALA B 1 179 ? -2.653  46.287 -8.511  1.00 43.63  ? 179 ALA B O   1 
ATOM   2287 C CB  . ALA B 1 179 ? -4.552  43.964 -8.791  1.00 39.62  ? 179 ALA B CB  1 
ATOM   2288 N N   . SER B 1 180 ? -2.539  45.939 -10.734 1.00 40.44  ? 180 SER B N   1 
ATOM   2289 C CA  . SER B 1 180 ? -1.176  46.443 -10.838 1.00 46.30  ? 180 SER B CA  1 
ATOM   2290 C C   . SER B 1 180 ? -1.085  47.952 -10.655 1.00 47.52  ? 180 SER B C   1 
ATOM   2291 O O   . SER B 1 180 ? 0.026   48.473 -10.515 1.00 51.40  ? 180 SER B O   1 
ATOM   2292 C CB  . SER B 1 180 ? -0.577  46.056 -12.192 1.00 45.23  ? 180 SER B CB  1 
ATOM   2293 O OG  . SER B 1 180 ? -1.234  46.736 -13.248 1.00 45.01  ? 180 SER B OG  1 
ATOM   2294 N N   . GLN B 1 181 ? -2.210  48.659 -10.645 1.00 42.18  ? 181 GLN B N   1 
ATOM   2295 C CA  . GLN B 1 181 ? -2.223  50.110 -10.564 1.00 43.80  ? 181 GLN B CA  1 
ATOM   2296 C C   . GLN B 1 181 ? -2.533  50.576 -9.146  1.00 40.28  ? 181 GLN B C   1 
ATOM   2297 O O   . GLN B 1 181 ? -3.308  49.950 -8.417  1.00 42.84  ? 181 GLN B O   1 
ATOM   2298 C CB  . GLN B 1 181 ? -3.249  50.684 -11.541 1.00 51.49  ? 181 GLN B CB  1 
ATOM   2299 C CG  . GLN B 1 181 ? -3.073  50.207 -12.978 1.00 58.97  ? 181 GLN B CG  1 
ATOM   2300 C CD  . GLN B 1 181 ? -4.381  50.180 -13.745 1.00 62.51  ? 181 GLN B CD  1 
ATOM   2301 O OE1 . GLN B 1 181 ? -5.394  50.708 -13.285 1.00 73.29  ? 181 GLN B OE1 1 
ATOM   2302 N NE2 . GLN B 1 181 ? -4.368  49.560 -14.920 1.00 64.73  ? 181 GLN B NE2 1 
ATOM   2303 N N   . GLU B 1 182 ? -1.901  51.686 -8.756  1.00 42.91  ? 182 GLU B N   1 
ATOM   2304 C CA  . GLU B 1 182 ? -2.255  52.346 -7.503  1.00 46.27  ? 182 GLU B CA  1 
ATOM   2305 C C   . GLU B 1 182 ? -3.721  52.753 -7.501  1.00 50.82  ? 182 GLU B C   1 
ATOM   2306 O O   . GLU B 1 182 ? -4.446  52.501 -6.531  1.00 48.90  ? 182 GLU B O   1 
ATOM   2307 C CB  . GLU B 1 182 ? -1.367  53.577 -7.291  1.00 48.85  ? 182 GLU B CB  1 
ATOM   2308 C CG  . GLU B 1 182 ? 0.108   53.284 -7.082  1.00 57.70  ? 182 GLU B CG  1 
ATOM   2309 C CD  . GLU B 1 182 ? 0.453   53.037 -5.630  1.00 60.81  ? 182 GLU B CD  1 
ATOM   2310 O OE1 . GLU B 1 182 ? 0.212   51.921 -5.130  1.00 64.54  ? 182 GLU B OE1 1 
ATOM   2311 O OE2 . GLU B 1 182 ? 0.959   53.970 -4.974  1.00 64.92  ? 182 GLU B OE2 1 
ATOM   2312 N N   . HIS B 1 183 ? -4.175  53.365 -8.593  1.00 40.99  ? 183 HIS B N   1 
ATOM   2313 C CA  . HIS B 1 183 ? -5.504  53.943 -8.690  1.00 45.60  ? 183 HIS B CA  1 
ATOM   2314 C C   . HIS B 1 183 ? -6.213  53.385 -9.915  1.00 41.60  ? 183 HIS B C   1 
ATOM   2315 O O   . HIS B 1 183 ? -5.582  52.908 -10.862 1.00 42.93  ? 183 HIS B O   1 
ATOM   2316 C CB  . HIS B 1 183 ? -5.426  55.472 -8.783  1.00 38.20  ? 183 HIS B CB  1 
ATOM   2317 C CG  . HIS B 1 183 ? -4.760  56.112 -7.606  1.00 45.22  ? 183 HIS B CG  1 
ATOM   2318 N ND1 . HIS B 1 183 ? -5.288  56.060 -6.334  1.00 48.68  ? 183 HIS B ND1 1 
ATOM   2319 C CD2 . HIS B 1 183 ? -3.591  56.787 -7.502  1.00 47.74  ? 183 HIS B CD2 1 
ATOM   2320 C CE1 . HIS B 1 183 ? -4.483  56.694 -5.501  1.00 45.27  ? 183 HIS B CE1 1 
ATOM   2321 N NE2 . HIS B 1 183 ? -3.445  57.143 -6.184  1.00 44.02  ? 183 HIS B NE2 1 
ATOM   2322 N N   . VAL B 1 184 ? -7.543  53.453 -9.893  1.00 32.62  ? 184 VAL B N   1 
ATOM   2323 C CA  . VAL B 1 184 ? -8.364  53.026 -11.019 1.00 39.49  ? 184 VAL B CA  1 
ATOM   2324 C C   . VAL B 1 184 ? -9.420  54.088 -11.291 1.00 40.13  ? 184 VAL B C   1 
ATOM   2325 O O   . VAL B 1 184 ? -9.859  54.803 -10.387 1.00 35.96  ? 184 VAL B O   1 
ATOM   2326 C CB  . VAL B 1 184 ? -9.024  51.649 -10.773 1.00 39.58  ? 184 VAL B CB  1 
ATOM   2327 C CG1 . VAL B 1 184 ? -7.968  50.593 -10.481 1.00 44.17  ? 184 VAL B CG1 1 
ATOM   2328 C CG2 . VAL B 1 184 ? -10.029 51.733 -9.634  1.00 34.20  ? 184 VAL B CG2 1 
ATOM   2329 N N   . SER B 1 185 ? -9.817  54.197 -12.553 1.00 29.76  ? 185 SER B N   1 
ATOM   2330 C CA  . SER B 1 185 ? -10.857 55.140 -12.922 1.00 29.67  ? 185 SER B CA  1 
ATOM   2331 C C   . SER B 1 185 ? -12.211 54.442 -12.957 1.00 34.27  ? 185 SER B C   1 
ATOM   2332 O O   . SER B 1 185 ? -12.313 53.214 -12.914 1.00 31.84  ? 185 SER B O   1 
ATOM   2333 C CB  . SER B 1 185 ? -10.551 55.779 -14.276 1.00 33.88  ? 185 SER B CB  1 
ATOM   2334 O OG  . SER B 1 185 ? -10.512 54.804 -15.307 1.00 34.16  ? 185 SER B OG  1 
ATOM   2335 N N   . TYR B 1 186 ? -13.269 55.251 -13.027 1.00 31.20  ? 186 TYR B N   1 
ATOM   2336 C CA  . TYR B 1 186 ? -14.603 54.690 -13.198 1.00 27.16  ? 186 TYR B CA  1 
ATOM   2337 C C   . TYR B 1 186 ? -14.729 53.993 -14.546 1.00 34.76  ? 186 TYR B C   1 
ATOM   2338 O O   . TYR B 1 186 ? -15.419 52.975 -14.663 1.00 37.52  ? 186 TYR B O   1 
ATOM   2339 C CB  . TYR B 1 186 ? -15.659 55.786 -13.059 1.00 36.05  ? 186 TYR B CB  1 
ATOM   2340 C CG  . TYR B 1 186 ? -17.066 55.332 -13.382 1.00 38.44  ? 186 TYR B CG  1 
ATOM   2341 C CD1 . TYR B 1 186 ? -17.803 54.578 -12.476 1.00 32.76  ? 186 TYR B CD1 1 
ATOM   2342 C CD2 . TYR B 1 186 ? -17.653 55.650 -14.600 1.00 36.44  ? 186 TYR B CD2 1 
ATOM   2343 C CE1 . TYR B 1 186 ? -19.091 54.163 -12.772 1.00 37.93  ? 186 TYR B CE1 1 
ATOM   2344 C CE2 . TYR B 1 186 ? -18.935 55.238 -14.905 1.00 39.32  ? 186 TYR B CE2 1 
ATOM   2345 C CZ  . TYR B 1 186 ? -19.651 54.495 -13.988 1.00 38.91  ? 186 TYR B CZ  1 
ATOM   2346 O OH  . TYR B 1 186 ? -20.928 54.085 -14.289 1.00 42.41  ? 186 TYR B OH  1 
ATOM   2347 N N   . GLU B 1 187 ? -14.074 54.532 -15.578 1.00 33.66  ? 187 GLU B N   1 
ATOM   2348 C CA  . GLU B 1 187 ? -14.105 53.895 -16.890 1.00 38.59  ? 187 GLU B CA  1 
ATOM   2349 C C   . GLU B 1 187 ? -13.566 52.474 -16.829 1.00 33.67  ? 187 GLU B C   1 
ATOM   2350 O O   . GLU B 1 187 ? -14.085 51.577 -17.499 1.00 39.84  ? 187 GLU B O   1 
ATOM   2351 C CB  . GLU B 1 187 ? -13.308 54.719 -17.904 1.00 33.58  ? 187 GLU B CB  1 
ATOM   2352 C CG  . GLU B 1 187 ? -13.359 54.152 -19.316 1.00 37.06  ? 187 GLU B CG  1 
ATOM   2353 C CD  . GLU B 1 187 ? -12.676 55.046 -20.328 1.00 47.41  ? 187 GLU B CD  1 
ATOM   2354 O OE1 . GLU B 1 187 ? -11.969 55.987 -19.907 1.00 52.82  ? 187 GLU B OE1 1 
ATOM   2355 O OE2 . GLU B 1 187 ? -12.829 54.803 -21.544 1.00 54.27  ? 187 GLU B OE2 1 
ATOM   2356 N N   . GLN B 1 188 ? -12.520 52.248 -16.031 1.00 38.48  ? 188 GLN B N   1 
ATOM   2357 C CA  . GLN B 1 188 ? -11.952 50.908 -15.924 1.00 37.80  ? 188 GLN B CA  1 
ATOM   2358 C C   . GLN B 1 188 ? -12.879 49.973 -15.158 1.00 35.60  ? 188 GLN B C   1 
ATOM   2359 O O   . GLN B 1 188 ? -13.057 48.813 -15.551 1.00 33.75  ? 188 GLN B O   1 
ATOM   2360 C CB  . GLN B 1 188 ? -10.574 50.967 -15.264 1.00 31.80  ? 188 GLN B CB  1 
ATOM   2361 C CG  . GLN B 1 188 ? -9.563  51.797 -16.036 1.00 37.38  ? 188 GLN B CG  1 
ATOM   2362 C CD  . GLN B 1 188 ? -8.261  51.973 -15.279 1.00 39.92  ? 188 GLN B CD  1 
ATOM   2363 O OE1 . GLN B 1 188 ? -8.209  52.676 -14.271 1.00 41.78  ? 188 GLN B OE1 1 
ATOM   2364 N NE2 . GLN B 1 188 ? -7.203  51.328 -15.757 1.00 47.55  ? 188 GLN B NE2 1 
ATOM   2365 N N   . ILE B 1 189 ? -13.476 50.453 -14.062 1.00 33.25  ? 189 ILE B N   1 
ATOM   2366 C CA  . ILE B 1 189 ? -14.473 49.658 -13.348 1.00 32.81  ? 189 ILE B CA  1 
ATOM   2367 C C   . ILE B 1 189 ? -15.639 49.319 -14.271 1.00 29.53  ? 189 ILE B C   1 
ATOM   2368 O O   . ILE B 1 189 ? -16.148 48.194 -14.275 1.00 31.77  ? 189 ILE B O   1 
ATOM   2369 C CB  . ILE B 1 189 ? -14.952 50.398 -12.086 1.00 30.49  ? 189 ILE B CB  1 
ATOM   2370 C CG1 . ILE B 1 189 ? -13.788 50.629 -11.124 1.00 35.65  ? 189 ILE B CG1 1 
ATOM   2371 C CG2 . ILE B 1 189 ? -16.056 49.613 -11.396 1.00 33.66  ? 189 ILE B CG2 1 
ATOM   2372 C CD1 . ILE B 1 189 ? -13.022 49.356 -10.779 1.00 41.69  ? 189 ILE B CD1 1 
ATOM   2373 N N   . LEU B 1 190 ? -16.078 50.299 -15.063 1.00 36.03  ? 190 LEU B N   1 
ATOM   2374 C CA  . LEU B 1 190 ? -17.158 50.074 -16.022 1.00 36.44  ? 190 LEU B CA  1 
ATOM   2375 C C   . LEU B 1 190 ? -16.854 48.904 -16.948 1.00 35.55  ? 190 LEU B C   1 
ATOM   2376 O O   . LEU B 1 190 ? -17.748 48.115 -17.280 1.00 36.67  ? 190 LEU B O   1 
ATOM   2377 C CB  . LEU B 1 190 ? -17.400 51.348 -16.836 1.00 37.59  ? 190 LEU B CB  1 
ATOM   2378 C CG  . LEU B 1 190 ? -18.699 51.448 -17.636 1.00 42.18  ? 190 LEU B CG  1 
ATOM   2379 C CD1 . LEU B 1 190 ? -19.901 51.456 -16.713 1.00 43.95  ? 190 LEU B CD1 1 
ATOM   2380 C CD2 . LEU B 1 190 ? -18.695 52.687 -18.507 1.00 41.82  ? 190 LEU B CD2 1 
ATOM   2381 N N   . GLY B 1 191 ? -15.601 48.770 -17.366 1.00 35.11  ? 191 GLY B N   1 
ATOM   2382 C CA  . GLY B 1 191 ? -15.175 47.719 -18.262 1.00 31.99  ? 191 GLY B CA  1 
ATOM   2383 C C   . GLY B 1 191 ? -14.677 46.454 -17.598 1.00 35.65  ? 191 GLY B C   1 
ATOM   2384 O O   . GLY B 1 191 ? -14.154 45.571 -18.287 1.00 41.43  ? 191 GLY B O   1 
ATOM   2385 N N   . THR B 1 192 ? -14.811 46.334 -16.283 1.00 37.84  ? 192 THR B N   1 
ATOM   2386 C CA  . THR B 1 192 ? -14.400 45.141 -15.557 1.00 31.49  ? 192 THR B CA  1 
ATOM   2387 C C   . THR B 1 192 ? -15.637 44.417 -15.047 1.00 33.43  ? 192 THR B C   1 
ATOM   2388 O O   . THR B 1 192 ? -16.608 45.056 -14.637 1.00 42.72  ? 192 THR B O   1 
ATOM   2389 C CB  . THR B 1 192 ? -13.474 45.496 -14.387 1.00 36.50  ? 192 THR B CB  1 
ATOM   2390 O OG1 . THR B 1 192 ? -12.449 46.392 -14.839 1.00 38.08  ? 192 THR B OG1 1 
ATOM   2391 C CG2 . THR B 1 192 ? -12.828 44.244 -13.818 1.00 31.31  ? 192 THR B CG2 1 
ATOM   2392 N N   . ARG B 1 193 ? -15.610 43.087 -15.090 1.00 31.53  ? 193 ARG B N   1 
ATOM   2393 C CA  . ARG B 1 193 ? -16.744 42.307 -14.610 1.00 26.59  ? 193 ARG B CA  1 
ATOM   2394 C C   . ARG B 1 193 ? -16.891 42.445 -13.098 1.00 34.51  ? 193 ARG B C   1 
ATOM   2395 O O   . ARG B 1 193 ? -15.920 42.291 -12.351 1.00 28.08  ? 193 ARG B O   1 
ATOM   2396 C CB  . ARG B 1 193 ? -16.583 40.835 -14.982 1.00 22.71  ? 193 ARG B CB  1 
ATOM   2397 C CG  . ARG B 1 193 ? -17.781 39.990 -14.574 1.00 26.99  ? 193 ARG B CG  1 
ATOM   2398 C CD  . ARG B 1 193 ? -17.532 38.507 -14.760 1.00 26.23  ? 193 ARG B CD  1 
ATOM   2399 N NE  . ARG B 1 193 ? -17.418 38.138 -16.165 1.00 34.72  ? 193 ARG B NE  1 
ATOM   2400 C CZ  . ARG B 1 193 ? -16.335 37.602 -16.710 1.00 38.60  ? 193 ARG B CZ  1 
ATOM   2401 N NH1 . ARG B 1 193 ? -15.238 37.384 -16.001 1.00 30.48  ? 193 ARG B NH1 1 
ATOM   2402 N NH2 . ARG B 1 193 ? -16.349 37.280 -18.000 1.00 29.50  ? 193 ARG B NH2 1 
ATOM   2403 N N   . GLN B 1 194 ? -18.110 42.738 -12.650 1.00 31.10  ? 194 GLN B N   1 
ATOM   2404 C CA  . GLN B 1 194 ? -18.427 42.819 -11.231 1.00 26.85  ? 194 GLN B CA  1 
ATOM   2405 C C   . GLN B 1 194 ? -19.123 41.540 -10.787 1.00 27.74  ? 194 GLN B C   1 
ATOM   2406 O O   . GLN B 1 194 ? -20.031 41.055 -11.468 1.00 29.19  ? 194 GLN B O   1 
ATOM   2407 C CB  . GLN B 1 194 ? -19.318 44.026 -10.935 1.00 28.87  ? 194 GLN B CB  1 
ATOM   2408 C CG  . GLN B 1 194 ? -19.633 44.208 -9.456  1.00 31.17  ? 194 GLN B CG  1 
ATOM   2409 C CD  . GLN B 1 194 ? -20.498 45.419 -9.183  1.00 41.54  ? 194 GLN B CD  1 
ATOM   2410 O OE1 . GLN B 1 194 ? -20.805 46.196 -10.089 1.00 31.42  ? 194 GLN B OE1 1 
ATOM   2411 N NE2 . GLN B 1 194 ? -20.903 45.584 -7.927  1.00 39.73  ? 194 GLN B NE2 1 
ATOM   2412 N N   . ILE B 1 195 ? -18.694 40.995 -9.654  1.00 30.12  ? 195 ILE B N   1 
ATOM   2413 C CA  . ILE B 1 195 ? -19.365 39.859 -9.034  1.00 28.13  ? 195 ILE B CA  1 
ATOM   2414 C C   . ILE B 1 195 ? -20.292 40.416 -7.962  1.00 32.11  ? 195 ILE B C   1 
ATOM   2415 O O   . ILE B 1 195 ? -19.834 40.977 -6.962  1.00 29.71  ? 195 ILE B O   1 
ATOM   2416 C CB  . ILE B 1 195 ? -18.363 38.862 -8.445  1.00 33.50  ? 195 ILE B CB  1 
ATOM   2417 C CG1 . ILE B 1 195 ? -17.293 38.511 -9.480  1.00 29.72  ? 195 ILE B CG1 1 
ATOM   2418 C CG2 . ILE B 1 195 ? -19.076 37.608 -7.985  1.00 27.23  ? 195 ILE B CG2 1 
ATOM   2419 C CD1 . ILE B 1 195 ? -17.856 37.921 -10.752 1.00 32.25  ? 195 ILE B CD1 1 
ATOM   2420 N N   . VAL B 1 196 ? -21.597 40.273 -8.173  1.00 33.40  ? 196 VAL B N   1 
ATOM   2421 C CA  . VAL B 1 196 ? -22.601 40.933 -7.347  1.00 32.95  ? 196 VAL B CA  1 
ATOM   2422 C C   . VAL B 1 196 ? -23.305 39.884 -6.496  1.00 37.00  ? 196 VAL B C   1 
ATOM   2423 O O   . VAL B 1 196 ? -23.615 38.789 -6.980  1.00 37.99  ? 196 VAL B O   1 
ATOM   2424 C CB  . VAL B 1 196 ? -23.603 41.719 -8.210  1.00 35.04  ? 196 VAL B CB  1 
ATOM   2425 C CG1 . VAL B 1 196 ? -24.592 42.466 -7.336  1.00 43.10  ? 196 VAL B CG1 1 
ATOM   2426 C CG2 . VAL B 1 196 ? -22.865 42.678 -9.126  1.00 33.66  ? 196 VAL B CG2 1 
ATOM   2427 N N   . VAL B 1 197 ? -23.549 40.225 -5.232  1.00 35.36  ? 197 VAL B N   1 
ATOM   2428 C CA  . VAL B 1 197 ? -24.274 39.373 -4.299  1.00 37.33  ? 197 VAL B CA  1 
ATOM   2429 C C   . VAL B 1 197 ? -25.673 39.945 -4.129  1.00 42.66  ? 197 VAL B C   1 
ATOM   2430 O O   . VAL B 1 197 ? -25.835 41.058 -3.617  1.00 41.98  ? 197 VAL B O   1 
ATOM   2431 C CB  . VAL B 1 197 ? -23.555 39.286 -2.947  1.00 39.61  ? 197 VAL B CB  1 
ATOM   2432 C CG1 . VAL B 1 197 ? -24.397 38.494 -1.956  1.00 34.48  ? 197 VAL B CG1 1 
ATOM   2433 C CG2 . VAL B 1 197 ? -22.187 38.664 -3.122  1.00 29.97  ? 197 VAL B CG2 1 
ATOM   2434 N N   . ALA B 1 198 ? -26.685 39.187 -4.541  1.00 36.18  ? 198 ALA B N   1 
ATOM   2435 C CA  . ALA B 1 198 ? -28.065 39.646 -4.429  1.00 47.07  ? 198 ALA B CA  1 
ATOM   2436 C C   . ALA B 1 198 ? -28.999 38.477 -4.724  1.00 47.96  ? 198 ALA B C   1 
ATOM   2437 O O   . ALA B 1 198 ? -28.559 37.387 -5.099  1.00 47.22  ? 198 ALA B O   1 
ATOM   2438 C CB  . ALA B 1 198 ? -28.344 40.825 -5.367  1.00 43.47  ? 198 ALA B CB  1 
ATOM   2439 N N   . SER B 1 199 ? -30.296 38.726 -4.541  1.00 63.64  ? 199 SER B N   1 
ATOM   2440 C CA  . SER B 1 199 ? -31.355 37.743 -4.762  1.00 57.07  ? 199 SER B CA  1 
ATOM   2441 C C   . SER B 1 199 ? -31.161 36.516 -3.892  1.00 59.36  ? 199 SER B C   1 
ATOM   2442 O O   . SER B 1 199 ? -31.482 36.543 -2.707  1.00 68.71  ? 199 SER B O   1 
ATOM   2443 C CB  . SER B 1 199 ? -31.429 37.330 -6.236  1.00 56.59  ? 199 SER B CB  1 
ATOM   2444 O OG  . SER B 1 199 ? -32.309 38.174 -6.950  1.00 60.02  ? 199 SER B OG  1 
ATOM   2445 N N   . THR B 1 203 ? -34.616 41.776 -6.445  1.00 75.06  ? 203 THR B N   1 
ATOM   2446 C CA  . THR B 1 203 ? -33.526 41.659 -7.406  1.00 75.81  ? 203 THR B CA  1 
ATOM   2447 C C   . THR B 1 203 ? -32.514 42.808 -7.253  1.00 81.49  ? 203 THR B C   1 
ATOM   2448 O O   . THR B 1 203 ? -32.163 43.174 -6.133  1.00 75.62  ? 203 THR B O   1 
ATOM   2449 C CB  . THR B 1 203 ? -34.071 41.582 -8.838  1.00 73.52  ? 203 THR B CB  1 
ATOM   2450 O OG1 . THR B 1 203 ? -35.136 42.519 -8.992  1.00 74.36  ? 203 THR B OG1 1 
ATOM   2451 C CG2 . THR B 1 203 ? -34.596 40.182 -9.125  1.00 65.87  ? 203 THR B CG2 1 
ATOM   2452 N N   . LEU B 1 204 ? -32.062 43.387 -8.362  1.00 82.59  ? 204 LEU B N   1 
ATOM   2453 C CA  . LEU B 1 204 ? -30.812 44.145 -8.392  1.00 82.82  ? 204 LEU B CA  1 
ATOM   2454 C C   . LEU B 1 204 ? -31.058 45.652 -8.336  1.00 84.46  ? 204 LEU B C   1 
ATOM   2455 O O   . LEU B 1 204 ? -31.656 46.227 -9.251  1.00 83.69  ? 204 LEU B O   1 
ATOM   2456 C CB  . LEU B 1 204 ? -30.007 43.778 -9.635  1.00 78.35  ? 204 LEU B CB  1 
ATOM   2457 C CG  . LEU B 1 204 ? -29.124 42.546 -9.454  1.00 73.83  ? 204 LEU B CG  1 
ATOM   2458 C CD1 . LEU B 1 204 ? -28.690 42.027 -10.799 1.00 73.46  ? 204 LEU B CD1 1 
ATOM   2459 C CD2 . LEU B 1 204 ? -27.918 42.880 -8.596  1.00 67.20  ? 204 LEU B CD2 1 
ATOM   2460 N N   . LYS B 1 205 ? -30.565 46.285 -7.279  1.00 82.27  ? 205 LYS B N   1 
ATOM   2461 C CA  . LYS B 1 205 ? -30.592 47.738 -7.135  1.00 84.00  ? 205 LYS B CA  1 
ATOM   2462 C C   . LYS B 1 205 ? -29.529 48.384 -8.017  1.00 77.82  ? 205 LYS B C   1 
ATOM   2463 O O   . LYS B 1 205 ? -28.335 48.149 -7.801  1.00 69.63  ? 205 LYS B O   1 
ATOM   2464 C CB  . LYS B 1 205 ? -30.380 48.123 -5.668  1.00 86.98  ? 205 LYS B CB  1 
ATOM   2465 C CG  . LYS B 1 205 ? -31.526 47.718 -4.755  1.00 89.95  ? 205 LYS B CG  1 
ATOM   2466 C CD  . LYS B 1 205 ? -31.212 47.937 -3.279  1.00 91.08  ? 205 LYS B CD  1 
ATOM   2467 C CE  . LYS B 1 205 ? -30.010 47.126 -2.830  1.00 87.87  ? 205 LYS B CE  1 
ATOM   2468 N NZ  . LYS B 1 205 ? -30.050 46.891 -1.358  1.00 86.16  ? 205 LYS B NZ  1 
ATOM   2469 N N   . PRO B 1 206 ? -29.910 49.214 -8.997  1.00 82.16  ? 206 PRO B N   1 
ATOM   2470 C CA  . PRO B 1 206 ? -28.913 49.714 -9.962  1.00 81.18  ? 206 PRO B CA  1 
ATOM   2471 C C   . PRO B 1 206 ? -27.849 50.616 -9.358  1.00 71.28  ? 206 PRO B C   1 
ATOM   2472 O O   . PRO B 1 206 ? -26.808 50.818 -9.996  1.00 71.99  ? 206 PRO B O   1 
ATOM   2473 C CB  . PRO B 1 206 ? -29.767 50.474 -10.992 1.00 80.93  ? 206 PRO B CB  1 
ATOM   2474 C CG  . PRO B 1 206 ? -31.064 50.750 -10.304 1.00 77.85  ? 206 PRO B CG  1 
ATOM   2475 C CD  . PRO B 1 206 ? -31.278 49.642 -9.324  1.00 83.81  ? 206 PRO B CD  1 
ATOM   2476 N N   . GLU B 1 207 ? -28.064 51.171 -8.164  1.00 73.15  ? 207 GLU B N   1 
ATOM   2477 C CA  . GLU B 1 207 ? -27.062 52.065 -7.596  1.00 71.73  ? 207 GLU B CA  1 
ATOM   2478 C C   . GLU B 1 207 ? -25.919 51.329 -6.909  1.00 65.97  ? 207 GLU B C   1 
ATOM   2479 O O   . GLU B 1 207 ? -24.929 51.969 -6.541  1.00 62.57  ? 207 GLU B O   1 
ATOM   2480 C CB  . GLU B 1 207 ? -27.702 53.052 -6.611  1.00 81.04  ? 207 GLU B CB  1 
ATOM   2481 C CG  . GLU B 1 207 ? -28.308 52.436 -5.370  1.00 83.55  ? 207 GLU B CG  1 
ATOM   2482 C CD  . GLU B 1 207 ? -29.720 51.948 -5.592  1.00 91.11  ? 207 GLU B CD  1 
ATOM   2483 O OE1 . GLU B 1 207 ? -30.226 52.089 -6.724  1.00 91.70  ? 207 GLU B OE1 1 
ATOM   2484 O OE2 . GLU B 1 207 ? -30.335 51.445 -4.630  1.00 89.76  ? 207 GLU B OE2 1 
ATOM   2485 N N   . LEU B 1 208 ? -26.034 50.016 -6.719  1.00 73.25  ? 208 LEU B N   1 
ATOM   2486 C CA  . LEU B 1 208 ? -24.931 49.189 -6.255  1.00 63.34  ? 208 LEU B CA  1 
ATOM   2487 C C   . LEU B 1 208 ? -24.274 48.433 -7.400  1.00 57.67  ? 208 LEU B C   1 
ATOM   2488 O O   . LEU B 1 208 ? -23.473 47.525 -7.161  1.00 52.10  ? 208 LEU B O   1 
ATOM   2489 C CB  . LEU B 1 208 ? -25.409 48.209 -5.180  1.00 59.71  ? 208 LEU B CB  1 
ATOM   2490 C CG  . LEU B 1 208 ? -25.655 48.790 -3.781  1.00 76.72  ? 208 LEU B CG  1 
ATOM   2491 C CD1 . LEU B 1 208 ? -24.474 49.656 -3.346  1.00 66.54  ? 208 LEU B CD1 1 
ATOM   2492 C CD2 . LEU B 1 208 ? -26.967 49.563 -3.686  1.00 76.24  ? 208 LEU B CD2 1 
ATOM   2493 N N   . LEU B 1 209 ? -24.605 48.787 -8.637  1.00 59.75  ? 209 LEU B N   1 
ATOM   2494 C CA  . LEU B 1 209 ? -24.020 48.197 -9.833  1.00 49.36  ? 209 LEU B CA  1 
ATOM   2495 C C   . LEU B 1 209 ? -23.174 49.260 -10.518 1.00 41.17  ? 209 LEU B C   1 
ATOM   2496 O O   . LEU B 1 209 ? -23.686 50.327 -10.867 1.00 46.31  ? 209 LEU B O   1 
ATOM   2497 C CB  . LEU B 1 209 ? -25.107 47.688 -10.779 1.00 59.05  ? 209 LEU B CB  1 
ATOM   2498 C CG  . LEU B 1 209 ? -25.520 46.219 -10.716 1.00 61.92  ? 209 LEU B CG  1 
ATOM   2499 C CD1 . LEU B 1 209 ? -24.557 45.405 -11.559 1.00 59.78  ? 209 LEU B CD1 1 
ATOM   2500 C CD2 . LEU B 1 209 ? -25.591 45.689 -9.283  1.00 61.48  ? 209 LEU B CD2 1 
ATOM   2501 N N   . PHE B 1 210 ? -21.890 48.975 -10.713 1.00 36.51  ? 210 PHE B N   1 
ATOM   2502 C CA  . PHE B 1 210 ? -20.972 49.961 -11.267 1.00 38.16  ? 210 PHE B CA  1 
ATOM   2503 C C   . PHE B 1 210 ? -20.256 49.483 -12.519 1.00 37.16  ? 210 PHE B C   1 
ATOM   2504 O O   . PHE B 1 210 ? -19.467 50.241 -13.092 1.00 44.16  ? 210 PHE B O   1 
ATOM   2505 C CB  . PHE B 1 210 ? -19.943 50.380 -10.211 1.00 36.05  ? 210 PHE B CB  1 
ATOM   2506 C CG  . PHE B 1 210 ? -20.558 50.942 -8.959  1.00 42.32  ? 210 PHE B CG  1 
ATOM   2507 C CD1 . PHE B 1 210 ? -20.953 50.107 -7.923  1.00 38.25  ? 210 PHE B CD1 1 
ATOM   2508 C CD2 . PHE B 1 210 ? -20.781 52.304 -8.836  1.00 37.71  ? 210 PHE B CD2 1 
ATOM   2509 C CE1 . PHE B 1 210 ? -21.526 50.627 -6.777  1.00 45.15  ? 210 PHE B CE1 1 
ATOM   2510 C CE2 . PHE B 1 210 ? -21.358 52.826 -7.697  1.00 47.79  ? 210 PHE B CE2 1 
ATOM   2511 C CZ  . PHE B 1 210 ? -21.732 51.986 -6.670  1.00 42.26  ? 210 PHE B CZ  1 
ATOM   2512 N N   . SER B 1 211 ? -20.514 48.262 -12.962 1.00 34.64  ? 211 SER B N   1 
ATOM   2513 C CA  . SER B 1 211 ? -19.888 47.709 -14.147 1.00 35.07  ? 211 SER B CA  1 
ATOM   2514 C C   . SER B 1 211 ? -20.961 47.381 -15.173 1.00 31.49  ? 211 SER B C   1 
ATOM   2515 O O   . SER B 1 211 ? -22.095 47.040 -14.824 1.00 31.49  ? 211 SER B O   1 
ATOM   2516 C CB  . SER B 1 211 ? -19.085 46.458 -13.807 1.00 33.14  ? 211 SER B CB  1 
ATOM   2517 O OG  . SER B 1 211 ? -18.060 46.752 -12.873 1.00 32.09  ? 211 SER B OG  1 
ATOM   2518 N N   . LYS B 1 212 ? -20.594 47.496 -16.448 1.00 35.65  ? 212 LYS B N   1 
ATOM   2519 C CA  . LYS B 1 212 ? -21.545 47.173 -17.505 1.00 32.54  ? 212 LYS B CA  1 
ATOM   2520 C C   . LYS B 1 212 ? -21.892 45.689 -17.498 1.00 36.32  ? 212 LYS B C   1 
ATOM   2521 O O   . LYS B 1 212 ? -23.055 45.318 -17.686 1.00 39.35  ? 212 LYS B O   1 
ATOM   2522 C CB  . LYS B 1 212 ? -20.987 47.597 -18.866 1.00 38.10  ? 212 LYS B CB  1 
ATOM   2523 C CG  . LYS B 1 212 ? -21.946 47.361 -20.023 1.00 53.27  ? 212 LYS B CG  1 
ATOM   2524 C CD  . LYS B 1 212 ? -23.381 47.730 -19.641 1.00 64.73  ? 212 LYS B CD  1 
ATOM   2525 C CE  . LYS B 1 212 ? -24.314 47.745 -20.842 1.00 68.29  ? 212 LYS B CE  1 
ATOM   2526 N NZ  . LYS B 1 212 ? -23.905 48.742 -21.869 1.00 64.97  ? 212 LYS B NZ  1 
ATOM   2527 N N   . HIS B 1 213 ? -20.907 44.826 -17.272 1.00 35.15  ? 213 HIS B N   1 
ATOM   2528 C CA  . HIS B 1 213 ? -21.110 43.385 -17.271 1.00 40.05  ? 213 HIS B CA  1 
ATOM   2529 C C   . HIS B 1 213 ? -20.865 42.833 -15.874 1.00 31.76  ? 213 HIS B C   1 
ATOM   2530 O O   . HIS B 1 213 ? -19.915 43.234 -15.194 1.00 34.15  ? 213 HIS B O   1 
ATOM   2531 C CB  . HIS B 1 213 ? -20.189 42.707 -18.286 1.00 33.74  ? 213 HIS B CB  1 
ATOM   2532 C CG  . HIS B 1 213 ? -20.466 43.108 -19.701 1.00 49.00  ? 213 HIS B CG  1 
ATOM   2533 N ND1 . HIS B 1 213 ? -21.689 42.905 -20.307 1.00 54.37  ? 213 HIS B ND1 1 
ATOM   2534 C CD2 . HIS B 1 213 ? -19.687 43.718 -20.625 1.00 46.41  ? 213 HIS B CD2 1 
ATOM   2535 C CE1 . HIS B 1 213 ? -21.647 43.363 -21.545 1.00 55.69  ? 213 HIS B CE1 1 
ATOM   2536 N NE2 . HIS B 1 213 ? -20.444 43.862 -21.763 1.00 59.39  ? 213 HIS B NE2 1 
ATOM   2537 N N   . TYR B 1 214 ? -21.723 41.908 -15.451 1.00 35.90  ? 214 TYR B N   1 
ATOM   2538 C CA  . TYR B 1 214 ? -21.703 41.444 -14.074 1.00 32.99  ? 214 TYR B CA  1 
ATOM   2539 C C   . TYR B 1 214 ? -22.275 40.038 -13.990 1.00 30.91  ? 214 TYR B C   1 
ATOM   2540 O O   . TYR B 1 214 ? -23.082 39.624 -14.828 1.00 30.27  ? 214 TYR B O   1 
ATOM   2541 C CB  . TYR B 1 214 ? -22.487 42.398 -13.159 1.00 25.88  ? 214 TYR B CB  1 
ATOM   2542 C CG  . TYR B 1 214 ? -23.987 42.406 -13.391 1.00 34.48  ? 214 TYR B CG  1 
ATOM   2543 C CD1 . TYR B 1 214 ? -24.812 41.462 -12.789 1.00 37.89  ? 214 TYR B CD1 1 
ATOM   2544 C CD2 . TYR B 1 214 ? -24.577 43.355 -14.217 1.00 38.63  ? 214 TYR B CD2 1 
ATOM   2545 C CE1 . TYR B 1 214 ? -26.175 41.462 -13.004 1.00 37.89  ? 214 TYR B CE1 1 
ATOM   2546 C CE2 . TYR B 1 214 ? -25.945 43.368 -14.429 1.00 34.73  ? 214 TYR B CE2 1 
ATOM   2547 C CZ  . TYR B 1 214 ? -26.738 42.419 -13.821 1.00 46.51  ? 214 TYR B CZ  1 
ATOM   2548 O OH  . TYR B 1 214 ? -28.098 42.428 -14.035 1.00 57.08  ? 214 TYR B OH  1 
ATOM   2549 N N   . TRP B 1 215 ? -21.842 39.316 -12.961 1.00 27.64  ? 215 TRP B N   1 
ATOM   2550 C CA  . TRP B 1 215 ? -22.426 38.048 -12.557 1.00 28.05  ? 215 TRP B CA  1 
ATOM   2551 C C   . TRP B 1 215 ? -23.124 38.223 -11.217 1.00 38.29  ? 215 TRP B C   1 
ATOM   2552 O O   . TRP B 1 215 ? -22.689 39.008 -10.369 1.00 29.50  ? 215 TRP B O   1 
ATOM   2553 C CB  . TRP B 1 215 ? -21.362 36.958 -12.425 1.00 24.25  ? 215 TRP B CB  1 
ATOM   2554 C CG  . TRP B 1 215 ? -20.753 36.504 -13.703 1.00 36.24  ? 215 TRP B CG  1 
ATOM   2555 C CD1 . TRP B 1 215 ? -21.039 36.948 -14.960 1.00 31.12  ? 215 TRP B CD1 1 
ATOM   2556 C CD2 . TRP B 1 215 ? -19.734 35.513 -13.847 1.00 28.84  ? 215 TRP B CD2 1 
ATOM   2557 N NE1 . TRP B 1 215 ? -20.262 36.288 -15.880 1.00 29.91  ? 215 TRP B NE1 1 
ATOM   2558 C CE2 . TRP B 1 215 ? -19.451 35.401 -15.221 1.00 31.46  ? 215 TRP B CE2 1 
ATOM   2559 C CE3 . TRP B 1 215 ? -19.035 34.707 -12.945 1.00 28.41  ? 215 TRP B CE3 1 
ATOM   2560 C CZ2 . TRP B 1 215 ? -18.497 34.515 -15.715 1.00 27.30  ? 215 TRP B CZ2 1 
ATOM   2561 C CZ3 . TRP B 1 215 ? -18.091 33.830 -13.436 1.00 34.90  ? 215 TRP B CZ3 1 
ATOM   2562 C CH2 . TRP B 1 215 ? -17.830 33.739 -14.807 1.00 33.24  ? 215 TRP B CH2 1 
ATOM   2563 N N   . ARG B 1 216 ? -24.204 37.476 -11.021 1.00 38.65  ? 216 ARG B N   1 
ATOM   2564 C CA  . ARG B 1 216 ? -24.939 37.497 -9.766  1.00 32.38  ? 216 ARG B CA  1 
ATOM   2565 C C   . ARG B 1 216 ? -24.740 36.180 -9.032  1.00 35.73  ? 216 ARG B C   1 
ATOM   2566 O O   . ARG B 1 216 ? -24.871 35.106 -9.626  1.00 30.60  ? 216 ARG B O   1 
ATOM   2567 C CB  . ARG B 1 216 ? -26.428 37.748 -9.997  1.00 38.22  ? 216 ARG B CB  1 
ATOM   2568 C CG  . ARG B 1 216 ? -27.173 38.165 -8.744  1.00 43.59  ? 216 ARG B CG  1 
ATOM   2569 C CD  . ARG B 1 216 ? -28.649 38.341 -9.039  1.00 42.13  ? 216 ARG B CD  1 
ATOM   2570 N NE  . ARG B 1 216 ? -29.284 37.129 -9.550  1.00 55.85  ? 216 ARG B NE  1 
ATOM   2571 C CZ  . ARG B 1 216 ? -29.375 35.977 -8.895  1.00 54.02  ? 216 ARG B CZ  1 
ATOM   2572 N NH1 . ARG B 1 216 ? -28.904 35.835 -7.667  1.00 50.50  ? 216 ARG B NH1 1 
ATOM   2573 N NH2 . ARG B 1 216 ? -29.971 34.943 -9.483  1.00 44.10  ? 216 ARG B NH2 1 
ATOM   2574 N N   . THR B 1 217 ? -24.408 36.271 -7.748  1.00 27.77  ? 217 THR B N   1 
ATOM   2575 C CA  . THR B 1 217 ? -24.381 35.139 -6.836  1.00 30.08  ? 217 THR B CA  1 
ATOM   2576 C C   . THR B 1 217 ? -25.133 35.544 -5.577  1.00 37.08  ? 217 THR B C   1 
ATOM   2577 O O   . THR B 1 217 ? -25.396 36.725 -5.349  1.00 35.52  ? 217 THR B O   1 
ATOM   2578 C CB  . THR B 1 217 ? -22.949 34.703 -6.507  1.00 29.87  ? 217 THR B CB  1 
ATOM   2579 O OG1 . THR B 1 217 ? -22.988 33.513 -5.713  1.00 41.04  ? 217 THR B OG1 1 
ATOM   2580 C CG2 . THR B 1 217 ? -22.232 35.790 -5.740  1.00 33.63  ? 217 THR B CG2 1 
ATOM   2581 N N   . ASP B 1 218 ? -25.507 34.565 -4.756  1.00 31.43  ? 218 ASP B N   1 
ATOM   2582 C CA  . ASP B 1 218 ? -26.377 34.853 -3.622  1.00 39.59  ? 218 ASP B CA  1 
ATOM   2583 C C   . ASP B 1 218 ? -25.665 34.806 -2.274  1.00 33.90  ? 218 ASP B C   1 
ATOM   2584 O O   . ASP B 1 218 ? -26.331 34.878 -1.240  1.00 38.79  ? 218 ASP B O   1 
ATOM   2585 C CB  . ASP B 1 218 ? -27.587 33.910 -3.616  1.00 40.37  ? 218 ASP B CB  1 
ATOM   2586 C CG  . ASP B 1 218 ? -27.206 32.453 -3.437  1.00 39.63  ? 218 ASP B CG  1 
ATOM   2587 O OD1 . ASP B 1 218 ? -26.000 32.130 -3.417  1.00 37.32  ? 218 ASP B OD1 1 
ATOM   2588 O OD2 . ASP B 1 218 ? -28.129 31.627 -3.313  1.00 45.28  ? 218 ASP B OD2 1 
ATOM   2589 N N   . ASN B 1 219 ? -24.339 34.698 -2.252  1.00 35.67  ? 219 ASN B N   1 
ATOM   2590 C CA  . ASN B 1 219 ? -23.616 34.769 -0.990  1.00 31.44  ? 219 ASN B CA  1 
ATOM   2591 C C   . ASN B 1 219 ? -22.157 35.119 -1.252  1.00 32.07  ? 219 ASN B C   1 
ATOM   2592 O O   . ASN B 1 219 ? -21.650 34.978 -2.367  1.00 31.68  ? 219 ASN B O   1 
ATOM   2593 C CB  . ASN B 1 219 ? -23.736 33.466 -0.192  1.00 35.24  ? 219 ASN B CB  1 
ATOM   2594 C CG  . ASN B 1 219 ? -22.835 32.371 -0.712  1.00 33.08  ? 219 ASN B CG  1 
ATOM   2595 O OD1 . ASN B 1 219 ? -21.759 32.130 -0.164  1.00 42.16  ? 219 ASN B OD1 1 
ATOM   2596 N ND2 . ASN B 1 219 ? -23.272 31.691 -1.762  1.00 48.87  ? 219 ASN B ND2 1 
ATOM   2597 N N   . HIS B 1 220 ? -21.491 35.579 -0.193  1.00 26.79  ? 220 HIS B N   1 
ATOM   2598 C CA  . HIS B 1 220 ? -20.167 36.180 -0.326  1.00 27.14  ? 220 HIS B CA  1 
ATOM   2599 C C   . HIS B 1 220 ? -19.063 35.143 -0.475  1.00 28.77  ? 220 HIS B C   1 
ATOM   2600 O O   . HIS B 1 220 ? -18.003 35.454 -1.027  1.00 34.89  ? 220 HIS B O   1 
ATOM   2601 C CB  . HIS B 1 220 ? -19.883 37.080 0.879   1.00 29.43  ? 220 HIS B CB  1 
ATOM   2602 C CG  . HIS B 1 220 ? -20.793 38.268 0.966   1.00 34.46  ? 220 HIS B CG  1 
ATOM   2603 N ND1 . HIS B 1 220 ? -20.771 39.298 0.049   1.00 39.45  ? 220 HIS B ND1 1 
ATOM   2604 C CD2 . HIS B 1 220 ? -21.771 38.575 1.850   1.00 28.56  ? 220 HIS B CD2 1 
ATOM   2605 C CE1 . HIS B 1 220 ? -21.686 40.195 0.372   1.00 28.39  ? 220 HIS B CE1 1 
ATOM   2606 N NE2 . HIS B 1 220 ? -22.309 39.779 1.460   1.00 33.74  ? 220 HIS B NE2 1 
ATOM   2607 N N   . HIS B 1 221 ? -19.277 33.924 0.024   1.00 27.70  ? 221 HIS B N   1 
ATOM   2608 C CA  . HIS B 1 221 ? -18.299 32.863 -0.189  1.00 34.49  ? 221 HIS B CA  1 
ATOM   2609 C C   . HIS B 1 221 ? -18.170 32.544 -1.672  1.00 33.41  ? 221 HIS B C   1 
ATOM   2610 O O   . HIS B 1 221 ? -17.061 32.459 -2.208  1.00 33.79  ? 221 HIS B O   1 
ATOM   2611 C CB  . HIS B 1 221 ? -18.689 31.610 0.595   1.00 29.83  ? 221 HIS B CB  1 
ATOM   2612 C CG  . HIS B 1 221 ? -17.941 30.383 0.172   1.00 32.97  ? 221 HIS B CG  1 
ATOM   2613 N ND1 . HIS B 1 221 ? -18.529 29.373 -0.557  1.00 33.76  ? 221 HIS B ND1 1 
ATOM   2614 C CD2 . HIS B 1 221 ? -16.657 30.004 0.374   1.00 30.71  ? 221 HIS B CD2 1 
ATOM   2615 C CE1 . HIS B 1 221 ? -17.639 28.425 -0.790  1.00 36.43  ? 221 HIS B CE1 1 
ATOM   2616 N NE2 . HIS B 1 221 ? -16.495 28.782 -0.235  1.00 33.66  ? 221 HIS B NE2 1 
ATOM   2617 N N   . SER B 1 222 ? -19.305 32.356 -2.348  1.00 25.07  ? 222 SER B N   1 
ATOM   2618 C CA  . SER B 1 222 ? -19.284 32.127 -3.789  1.00 35.15  ? 222 SER B CA  1 
ATOM   2619 C C   . SER B 1 222 ? -18.652 33.302 -4.523  1.00 32.42  ? 222 SER B C   1 
ATOM   2620 O O   . SER B 1 222 ? -17.858 33.110 -5.452  1.00 35.35  ? 222 SER B O   1 
ATOM   2621 C CB  . SER B 1 222 ? -20.705 31.876 -4.292  1.00 27.80  ? 222 SER B CB  1 
ATOM   2622 O OG  . SER B 1 222 ? -21.228 30.669 -3.766  1.00 42.49  ? 222 SER B OG  1 
ATOM   2623 N N   . ALA B 1 223 ? -18.988 34.529 -4.116  1.00 31.08  ? 223 ALA B N   1 
ATOM   2624 C CA  . ALA B 1 223 ? -18.393 35.704 -4.744  1.00 29.90  ? 223 ALA B CA  1 
ATOM   2625 C C   . ALA B 1 223 ? -16.887 35.740 -4.518  1.00 36.95  ? 223 ALA B C   1 
ATOM   2626 O O   . ALA B 1 223 ? -16.115 36.022 -5.442  1.00 30.97  ? 223 ALA B O   1 
ATOM   2627 C CB  . ALA B 1 223 ? -19.050 36.976 -4.210  1.00 27.29  ? 223 ALA B CB  1 
ATOM   2628 N N   . CYS B 1 224 ? -16.451 35.446 -3.288  1.00 27.05  ? 224 CYS B N   1 
ATOM   2629 C CA  . CYS B 1 224 ? -15.023 35.485 -2.977  1.00 26.97  ? 224 CYS B CA  1 
ATOM   2630 C C   . CYS B 1 224 ? -14.242 34.470 -3.801  1.00 27.90  ? 224 CYS B C   1 
ATOM   2631 O O   . CYS B 1 224 ? -13.148 34.772 -4.293  1.00 29.40  ? 224 CYS B O   1 
ATOM   2632 C CB  . CYS B 1 224 ? -14.801 35.248 -1.482  1.00 30.12  ? 224 CYS B CB  1 
ATOM   2633 S SG  . CYS B 1 224 ? -13.073 35.360 -0.952  1.00 36.78  ? 224 CYS B SG  1 
ATOM   2634 N N   . LEU B 1 225 ? -14.787 33.262 -3.966  1.00 25.50  ? 225 LEU B N   1 
ATOM   2635 C CA  . LEU B 1 225 ? -14.104 32.241 -4.757  1.00 30.28  ? 225 LEU B CA  1 
ATOM   2636 C C   . LEU B 1 225 ? -13.884 32.700 -6.194  1.00 28.02  ? 225 LEU B C   1 
ATOM   2637 O O   . LEU B 1 225 ? -12.820 32.457 -6.778  1.00 37.15  ? 225 LEU B O   1 
ATOM   2638 C CB  . LEU B 1 225 ? -14.900 30.936 -4.740  1.00 28.10  ? 225 LEU B CB  1 
ATOM   2639 C CG  . LEU B 1 225 ? -14.880 30.085 -3.470  1.00 40.88  ? 225 LEU B CG  1 
ATOM   2640 C CD1 . LEU B 1 225 ? -15.770 28.867 -3.652  1.00 36.07  ? 225 LEU B CD1 1 
ATOM   2641 C CD2 . LEU B 1 225 ? -13.464 29.657 -3.101  1.00 32.97  ? 225 LEU B CD2 1 
ATOM   2642 N N   . MET B 1 226 ? -14.878 33.367 -6.782  1.00 28.42  ? 226 MET B N   1 
ATOM   2643 C CA  . MET B 1 226 ? -14.762 33.793 -8.171  1.00 33.82  ? 226 MET B CA  1 
ATOM   2644 C C   . MET B 1 226 ? -13.866 35.018 -8.311  1.00 31.86  ? 226 MET B C   1 
ATOM   2645 O O   . MET B 1 226 ? -13.186 35.167 -9.333  1.00 34.05  ? 226 MET B O   1 
ATOM   2646 C CB  . MET B 1 226 ? -16.157 34.048 -8.748  1.00 26.07  ? 226 MET B CB  1 
ATOM   2647 C CG  . MET B 1 226 ? -16.912 32.760 -9.075  1.00 34.73  ? 226 MET B CG  1 
ATOM   2648 S SD  . MET B 1 226 ? -18.573 32.996 -9.731  1.00 46.85  ? 226 MET B SD  1 
ATOM   2649 C CE  . MET B 1 226 ? -19.369 33.840 -8.378  1.00 42.86  ? 226 MET B CE  1 
ATOM   2650 N N   . ILE B 1 227 ? -13.834 35.890 -7.298  1.00 28.15  ? 227 ILE B N   1 
ATOM   2651 C CA  . ILE B 1 227 ? -12.864 36.982 -7.294  1.00 29.44  ? 227 ILE B CA  1 
ATOM   2652 C C   . ILE B 1 227 ? -11.447 36.430 -7.188  1.00 27.91  ? 227 ILE B C   1 
ATOM   2653 O O   . ILE B 1 227 ? -10.511 36.954 -7.806  1.00 28.95  ? 227 ILE B O   1 
ATOM   2654 C CB  . ILE B 1 227 ? -13.169 37.971 -6.154  1.00 26.62  ? 227 ILE B CB  1 
ATOM   2655 C CG1 . ILE B 1 227 ? -14.532 38.626 -6.370  1.00 27.77  ? 227 ILE B CG1 1 
ATOM   2656 C CG2 . ILE B 1 227 ? -12.089 39.043 -6.066  1.00 27.09  ? 227 ILE B CG2 1 
ATOM   2657 C CD1 . ILE B 1 227 ? -15.086 39.295 -5.149  1.00 28.01  ? 227 ILE B CD1 1 
ATOM   2658 N N   . LEU B 1 228 ? -11.268 35.357 -6.407  1.00 28.48  ? 228 LEU B N   1 
ATOM   2659 C CA  . LEU B 1 228 ? -9.940  34.761 -6.270  1.00 31.63  ? 228 LEU B CA  1 
ATOM   2660 C C   . LEU B 1 228 ? -9.471  34.098 -7.562  1.00 32.50  ? 228 LEU B C   1 
ATOM   2661 O O   . LEU B 1 228 ? -8.261  33.979 -7.788  1.00 32.61  ? 228 LEU B O   1 
ATOM   2662 C CB  . LEU B 1 228 ? -9.928  33.755 -5.123  1.00 30.46  ? 228 LEU B CB  1 
ATOM   2663 C CG  . LEU B 1 228 ? -10.012 34.324 -3.703  1.00 39.16  ? 228 LEU B CG  1 
ATOM   2664 C CD1 . LEU B 1 228 ? -10.313 33.218 -2.714  1.00 31.63  ? 228 LEU B CD1 1 
ATOM   2665 C CD2 . LEU B 1 228 ? -8.709  35.007 -3.336  1.00 34.72  ? 228 LEU B CD2 1 
ATOM   2666 N N   . ARG B 1 229 ? -10.395 33.660 -8.415  1.00 30.28  ? 229 ARG B N   1 
ATOM   2667 C CA  . ARG B 1 229 ? -10.047 33.107 -9.721  1.00 31.60  ? 229 ARG B CA  1 
ATOM   2668 C C   . ARG B 1 229 ? -9.895  34.181 -10.798 1.00 31.99  ? 229 ARG B C   1 
ATOM   2669 O O   . ARG B 1 229 ? -9.877  33.849 -11.989 1.00 33.67  ? 229 ARG B O   1 
ATOM   2670 C CB  . ARG B 1 229 ? -11.093 32.075 -10.165 1.00 32.79  ? 229 ARG B CB  1 
ATOM   2671 C CG  . ARG B 1 229 ? -11.321 30.910 -9.199  1.00 40.26  ? 229 ARG B CG  1 
ATOM   2672 C CD  . ARG B 1 229 ? -10.057 30.083 -8.972  1.00 36.35  ? 229 ARG B CD  1 
ATOM   2673 N NE  . ARG B 1 229 ? -9.454  29.608 -10.214 1.00 48.87  ? 229 ARG B NE  1 
ATOM   2674 C CZ  . ARG B 1 229 ? -9.577  28.381 -10.707 1.00 47.66  ? 229 ARG B CZ  1 
ATOM   2675 N NH1 . ARG B 1 229 ? -10.306 27.458 -10.103 1.00 44.86  ? 229 ARG B NH1 1 
ATOM   2676 N NH2 . ARG B 1 229 ? -8.947  28.070 -11.835 1.00 42.68  ? 229 ARG B NH2 1 
ATOM   2677 N N   . ASN B 1 230 ? -9.791  35.455 -10.401 1.00 33.24  ? 230 ASN B N   1 
ATOM   2678 C CA  . ASN B 1 230 ? -9.603  36.587 -11.312 1.00 33.73  ? 230 ASN B CA  1 
ATOM   2679 C C   . ASN B 1 230 ? -10.788 36.779 -12.253 1.00 34.44  ? 230 ASN B C   1 
ATOM   2680 O O   . ASN B 1 230 ? -10.635 37.329 -13.345 1.00 33.85  ? 230 ASN B O   1 
ATOM   2681 C CB  . ASN B 1 230 ? -8.312  36.455 -12.128 1.00 29.02  ? 230 ASN B CB  1 
ATOM   2682 C CG  . ASN B 1 230 ? -7.070  36.590 -11.276 1.00 36.79  ? 230 ASN B CG  1 
ATOM   2683 O OD1 . ASN B 1 230 ? -7.136  36.501 -10.054 1.00 40.36  ? 230 ASN B OD1 1 
ATOM   2684 N ND2 . ASN B 1 230 ? -5.931  36.822 -11.917 1.00 36.16  ? 230 ASN B ND2 1 
ATOM   2685 N N   . LEU B 1 231 ? -11.974 36.329 -11.856 1.00 31.70  ? 231 LEU B N   1 
ATOM   2686 C CA  . LEU B 1 231 ? -13.137 36.488 -12.718 1.00 35.61  ? 231 LEU B CA  1 
ATOM   2687 C C   . LEU B 1 231 ? -13.775 37.868 -12.603 1.00 34.09  ? 231 LEU B C   1 
ATOM   2688 O O   . LEU B 1 231 ? -14.667 38.184 -13.400 1.00 34.07  ? 231 LEU B O   1 
ATOM   2689 C CB  . LEU B 1 231 ? -14.168 35.398 -12.412 1.00 29.18  ? 231 LEU B CB  1 
ATOM   2690 C CG  . LEU B 1 231 ? -13.693 33.987 -12.764 1.00 38.91  ? 231 LEU B CG  1 
ATOM   2691 C CD1 . LEU B 1 231 ? -14.621 32.925 -12.185 1.00 34.80  ? 231 LEU B CD1 1 
ATOM   2692 C CD2 . LEU B 1 231 ? -13.545 33.826 -14.273 1.00 34.57  ? 231 LEU B CD2 1 
ATOM   2693 N N   . GLY B 1 232 ? -13.341 38.690 -11.656 1.00 28.83  ? 232 GLY B N   1 
ATOM   2694 C CA  . GLY B 1 232 ? -13.857 40.038 -11.544 1.00 29.43  ? 232 GLY B CA  1 
ATOM   2695 C C   . GLY B 1 232 ? -13.567 40.628 -10.180 1.00 30.98  ? 232 GLY B C   1 
ATOM   2696 O O   . GLY B 1 232 ? -12.777 40.094 -9.400  1.00 30.54  ? 232 GLY B O   1 
ATOM   2697 N N   . TRP B 1 233 ? -14.224 41.754 -9.918  1.00 26.04  ? 233 TRP B N   1 
ATOM   2698 C CA  . TRP B 1 233 ? -14.140 42.444 -8.643  1.00 29.85  ? 233 TRP B CA  1 
ATOM   2699 C C   . TRP B 1 233 ? -15.488 42.389 -7.940  1.00 27.33  ? 233 TRP B C   1 
ATOM   2700 O O   . TRP B 1 233 ? -16.521 42.094 -8.548  1.00 28.93  ? 233 TRP B O   1 
ATOM   2701 C CB  . TRP B 1 233 ? -13.705 43.901 -8.825  1.00 23.91  ? 233 TRP B CB  1 
ATOM   2702 C CG  . TRP B 1 233 ? -14.788 44.787 -9.365  1.00 30.08  ? 233 TRP B CG  1 
ATOM   2703 C CD1 . TRP B 1 233 ? -15.179 44.908 -10.667 1.00 25.57  ? 233 TRP B CD1 1 
ATOM   2704 C CD2 . TRP B 1 233 ? -15.627 45.672 -8.611  1.00 28.71  ? 233 TRP B CD2 1 
ATOM   2705 N NE1 . TRP B 1 233 ? -16.203 45.818 -10.771 1.00 28.00  ? 233 TRP B NE1 1 
ATOM   2706 C CE2 . TRP B 1 233 ? -16.498 46.300 -9.523  1.00 25.78  ? 233 TRP B CE2 1 
ATOM   2707 C CE3 . TRP B 1 233 ? -15.725 45.995 -7.254  1.00 30.41  ? 233 TRP B CE3 1 
ATOM   2708 C CZ2 . TRP B 1 233 ? -17.453 47.232 -9.124  1.00 31.17  ? 233 TRP B CZ2 1 
ATOM   2709 C CZ3 . TRP B 1 233 ? -16.676 46.922 -6.860  1.00 31.50  ? 233 TRP B CZ3 1 
ATOM   2710 C CH2 . TRP B 1 233 ? -17.525 47.529 -7.791  1.00 30.09  ? 233 TRP B CH2 1 
ATOM   2711 N N   . GLY B 1 234 ? -15.466 42.685 -6.646  1.00 25.30  ? 234 GLY B N   1 
ATOM   2712 C CA  . GLY B 1 234 ? -16.684 42.617 -5.862  1.00 24.87  ? 234 GLY B CA  1 
ATOM   2713 C C   . GLY B 1 234 ? -16.484 43.210 -4.487  1.00 33.81  ? 234 GLY B C   1 
ATOM   2714 O O   . GLY B 1 234 ? -15.398 43.682 -4.138  1.00 34.88  ? 234 GLY B O   1 
ATOM   2715 N N   . VAL B 1 235 ? -17.561 43.167 -3.706  1.00 33.64  ? 235 VAL B N   1 
ATOM   2716 C CA  . VAL B 1 235 ? -17.612 43.776 -2.384  1.00 28.80  ? 235 VAL B CA  1 
ATOM   2717 C C   . VAL B 1 235 ? -17.816 42.667 -1.361  1.00 31.55  ? 235 VAL B C   1 
ATOM   2718 O O   . VAL B 1 235 ? -18.796 41.917 -1.436  1.00 29.46  ? 235 VAL B O   1 
ATOM   2719 C CB  . VAL B 1 235 ? -18.726 44.828 -2.299  1.00 39.78  ? 235 VAL B CB  1 
ATOM   2720 C CG1 . VAL B 1 235 ? -18.798 45.392 -0.898  1.00 29.09  ? 235 VAL B CG1 1 
ATOM   2721 C CG2 . VAL B 1 235 ? -18.488 45.926 -3.322  1.00 26.64  ? 235 VAL B CG2 1 
ATOM   2722 N N   . LEU B 1 236 ? -16.899 42.572 -0.397  1.00 26.14  ? 236 LEU B N   1 
ATOM   2723 C CA  . LEU B 1 236 ? -16.891 41.494 0.576   1.00 29.22  ? 236 LEU B CA  1 
ATOM   2724 C C   . LEU B 1 236 ? -16.905 42.042 1.999   1.00 31.32  ? 236 LEU B C   1 
ATOM   2725 O O   . LEU B 1 236 ? -16.360 43.118 2.264   1.00 29.39  ? 236 LEU B O   1 
ATOM   2726 C CB  . LEU B 1 236 ? -15.657 40.599 0.400   1.00 27.04  ? 236 LEU B CB  1 
ATOM   2727 C CG  . LEU B 1 236 ? -15.459 39.885 -0.938  1.00 37.96  ? 236 LEU B CG  1 
ATOM   2728 C CD1 . LEU B 1 236 ? -14.238 38.981 -0.869  1.00 29.36  ? 236 LEU B CD1 1 
ATOM   2729 C CD2 . LEU B 1 236 ? -16.700 39.094 -1.306  1.00 32.55  ? 236 LEU B CD2 1 
ATOM   2730 N N   . PRO B 1 237 ? -17.520 41.323 2.934   1.00 31.62  ? 237 PRO B N   1 
ATOM   2731 C CA  . PRO B 1 237 ? -17.478 41.757 4.335   1.00 33.54  ? 237 PRO B CA  1 
ATOM   2732 C C   . PRO B 1 237 ? -16.058 41.759 4.881   1.00 26.94  ? 237 PRO B C   1 
ATOM   2733 O O   . PRO B 1 237 ? -15.262 40.854 4.622   1.00 30.82  ? 237 PRO B O   1 
ATOM   2734 C CB  . PRO B 1 237 ? -18.357 40.730 5.060   1.00 25.89  ? 237 PRO B CB  1 
ATOM   2735 C CG  . PRO B 1 237 ? -19.195 40.108 3.992   1.00 32.79  ? 237 PRO B CG  1 
ATOM   2736 C CD  . PRO B 1 237 ? -18.371 40.139 2.743   1.00 27.31  ? 237 PRO B CD  1 
ATOM   2737 N N   . GLN B 1 238 ? -15.751 42.812 5.636   1.00 33.94  ? 238 GLN B N   1 
ATOM   2738 C CA  . GLN B 1 238 ? -14.483 42.911 6.351   1.00 28.42  ? 238 GLN B CA  1 
ATOM   2739 C C   . GLN B 1 238 ? -14.253 41.698 7.247   1.00 34.65  ? 238 GLN B C   1 
ATOM   2740 O O   . GLN B 1 238 ? -13.109 41.266 7.430   1.00 36.84  ? 238 GLN B O   1 
ATOM   2741 C CB  . GLN B 1 238 ? -14.492 44.211 7.161   1.00 37.49  ? 238 GLN B CB  1 
ATOM   2742 C CG  . GLN B 1 238 ? -13.152 44.812 7.498   1.00 48.40  ? 238 GLN B CG  1 
ATOM   2743 C CD  . GLN B 1 238 ? -13.290 46.054 8.358   1.00 67.24  ? 238 GLN B CD  1 
ATOM   2744 O OE1 . GLN B 1 238 ? -13.300 47.178 7.849   1.00 66.33  ? 238 GLN B OE1 1 
ATOM   2745 N NE2 . GLN B 1 238 ? -13.403 45.859 9.662   1.00 67.32  ? 238 GLN B NE2 1 
ATOM   2746 N N   . GLU B 1 239 ? -15.336 41.125 7.783   1.00 28.87  ? 239 GLU B N   1 
ATOM   2747 C CA  . GLU B 1 239 ? -15.271 39.942 8.638   1.00 33.28  ? 239 GLU B CA  1 
ATOM   2748 C C   . GLU B 1 239 ? -14.572 38.765 7.966   1.00 39.21  ? 239 GLU B C   1 
ATOM   2749 O O   . GLU B 1 239 ? -13.930 37.959 8.647   1.00 36.18  ? 239 GLU B O   1 
ATOM   2750 C CB  . GLU B 1 239 ? -16.695 39.557 9.050   1.00 37.92  ? 239 GLU B CB  1 
ATOM   2751 C CG  . GLU B 1 239 ? -16.868 38.225 9.769   1.00 48.80  ? 239 GLU B CG  1 
ATOM   2752 C CD  . GLU B 1 239 ? -16.144 38.153 11.097  1.00 60.84  ? 239 GLU B CD  1 
ATOM   2753 O OE1 . GLU B 1 239 ? -16.175 39.144 11.852  1.00 57.54  ? 239 GLU B OE1 1 
ATOM   2754 O OE2 . GLU B 1 239 ? -15.581 37.088 11.414  1.00 60.35  ? 239 GLU B OE2 1 
ATOM   2755 N N   . MET B 1 240 ? -14.681 38.640 6.639   1.00 31.43  ? 240 MET B N   1 
ATOM   2756 C CA  . MET B 1 240 ? -14.035 37.525 5.947   1.00 29.02  ? 240 MET B CA  1 
ATOM   2757 C C   . MET B 1 240 ? -12.519 37.584 6.067   1.00 34.14  ? 240 MET B C   1 
ATOM   2758 O O   . MET B 1 240 ? -11.854 36.544 6.035   1.00 35.17  ? 240 MET B O   1 
ATOM   2759 C CB  . MET B 1 240 ? -14.436 37.502 4.471   1.00 29.61  ? 240 MET B CB  1 
ATOM   2760 C CG  . MET B 1 240 ? -15.901 37.188 4.232   1.00 27.63  ? 240 MET B CG  1 
ATOM   2761 S SD  . MET B 1 240 ? -16.288 36.995 2.479   1.00 38.30  ? 240 MET B SD  1 
ATOM   2762 C CE  . MET B 1 240 ? -15.693 35.333 2.184   1.00 29.38  ? 240 MET B CE  1 
ATOM   2763 N N   . PHE B 1 241 ? -11.953 38.783 6.201   1.00 31.86  ? 241 PHE B N   1 
ATOM   2764 C CA  . PHE B 1 241 ? -10.510 38.906 6.371   1.00 30.92  ? 241 PHE B CA  1 
ATOM   2765 C C   . PHE B 1 241 ? -10.093 38.637 7.810   1.00 35.63  ? 241 PHE B C   1 
ATOM   2766 O O   . PHE B 1 241 ? -8.946  38.252 8.058   1.00 38.13  ? 241 PHE B O   1 
ATOM   2767 C CB  . PHE B 1 241 ? -10.053 40.290 5.907   1.00 36.07  ? 241 PHE B CB  1 
ATOM   2768 C CG  . PHE B 1 241 ? -10.302 40.542 4.443   1.00 33.36  ? 241 PHE B CG  1 
ATOM   2769 C CD1 . PHE B 1 241 ? -9.353  40.197 3.495   1.00 35.60  ? 241 PHE B CD1 1 
ATOM   2770 C CD2 . PHE B 1 241 ? -11.498 41.098 4.013   1.00 34.33  ? 241 PHE B CD2 1 
ATOM   2771 C CE1 . PHE B 1 241 ? -9.580  40.419 2.146   1.00 36.02  ? 241 PHE B CE1 1 
ATOM   2772 C CE2 . PHE B 1 241 ? -11.734 41.321 2.666   1.00 39.23  ? 241 PHE B CE2 1 
ATOM   2773 C CZ  . PHE B 1 241 ? -10.774 40.981 1.732   1.00 41.67  ? 241 PHE B CZ  1 
ATOM   2774 N N   . LYS B 1 242 ? -11.002 38.826 8.765   1.00 33.56  ? 242 LYS B N   1 
ATOM   2775 C CA  . LYS B 1 242 ? -10.760 38.333 10.116  1.00 40.26  ? 242 LYS B CA  1 
ATOM   2776 C C   . LYS B 1 242 ? -10.753 36.810 10.140  1.00 35.73  ? 242 LYS B C   1 
ATOM   2777 O O   . LYS B 1 242 ? -9.839  36.188 10.689  1.00 36.22  ? 242 LYS B O   1 
ATOM   2778 C CB  . LYS B 1 242 ? -11.821 38.865 11.083  1.00 43.53  ? 242 LYS B CB  1 
ATOM   2779 C CG  . LYS B 1 242 ? -11.464 40.154 11.806  1.00 60.78  ? 242 LYS B CG  1 
ATOM   2780 C CD  . LYS B 1 242 ? -12.724 40.797 12.373  1.00 68.86  ? 242 LYS B CD  1 
ATOM   2781 C CE  . LYS B 1 242 ? -12.711 42.309 12.269  1.00 76.34  ? 242 LYS B CE  1 
ATOM   2782 N NZ  . LYS B 1 242 ? -14.017 42.818 11.747  1.00 73.83  ? 242 LYS B NZ  1 
ATOM   2783 N N   . GLU B 1 243 ? -11.777 36.192 9.549   1.00 37.79  ? 243 GLU B N   1 
ATOM   2784 C CA  . GLU B 1 243 ? -11.893 34.737 9.582   1.00 43.18  ? 243 GLU B CA  1 
ATOM   2785 C C   . GLU B 1 243 ? -10.784 34.060 8.793   1.00 42.75  ? 243 GLU B C   1 
ATOM   2786 O O   . GLU B 1 243 ? -10.338 32.970 9.169   1.00 40.71  ? 243 GLU B O   1 
ATOM   2787 C CB  . GLU B 1 243 ? -13.255 34.300 9.040   1.00 36.30  ? 243 GLU B CB  1 
ATOM   2788 C CG  . GLU B 1 243 ? -14.422 34.686 9.916   1.00 42.14  ? 243 GLU B CG  1 
ATOM   2789 C CD  . GLU B 1 243 ? -15.755 34.524 9.217   1.00 59.13  ? 243 GLU B CD  1 
ATOM   2790 O OE1 . GLU B 1 243 ? -15.765 34.106 8.039   1.00 60.84  ? 243 GLU B OE1 1 
ATOM   2791 O OE2 . GLU B 1 243 ? -16.795 34.804 9.848   1.00 59.87  ? 243 GLU B OE2 1 
ATOM   2792 N N   . ASN B 1 244 ? -10.327 34.678 7.707   1.00 36.61  ? 244 ASN B N   1 
ATOM   2793 C CA  . ASN B 1 244 ? -9.312  34.092 6.833   1.00 37.39  ? 244 ASN B CA  1 
ATOM   2794 C C   . ASN B 1 244 ? -8.258  35.157 6.556   1.00 40.08  ? 244 ASN B C   1 
ATOM   2795 O O   . ASN B 1 244 ? -8.322  35.860 5.539   1.00 41.96  ? 244 ASN B O   1 
ATOM   2796 C CB  . ASN B 1 244 ? -9.949  33.561 5.548   1.00 32.52  ? 244 ASN B CB  1 
ATOM   2797 C CG  . ASN B 1 244 ? -8.971  32.802 4.668   1.00 33.96  ? 244 ASN B CG  1 
ATOM   2798 O OD1 . ASN B 1 244 ? -7.757  32.880 4.843   1.00 38.48  ? 244 ASN B OD1 1 
ATOM   2799 N ND2 . ASN B 1 244 ? -9.507  32.044 3.722   1.00 37.82  ? 244 ASN B ND2 1 
ATOM   2800 N N   . PRO B 1 245 ? -7.269  35.299 7.443   1.00 39.27  ? 245 PRO B N   1 
ATOM   2801 C CA  . PRO B 1 245 ? -6.253  36.347 7.246   1.00 39.01  ? 245 PRO B CA  1 
ATOM   2802 C C   . PRO B 1 245 ? -5.488  36.225 5.942   1.00 45.35  ? 245 PRO B C   1 
ATOM   2803 O O   . PRO B 1 245 ? -4.995  37.236 5.427   1.00 47.65  ? 245 PRO B O   1 
ATOM   2804 C CB  . PRO B 1 245 ? -5.324  36.167 8.456   1.00 49.79  ? 245 PRO B CB  1 
ATOM   2805 C CG  . PRO B 1 245 ? -6.128  35.443 9.473   1.00 41.46  ? 245 PRO B CG  1 
ATOM   2806 C CD  . PRO B 1 245 ? -7.106  34.588 8.723   1.00 41.93  ? 245 PRO B CD  1 
ATOM   2807 N N   . GLU B 1 246 ? -5.378  35.019 5.382   1.00 44.61  ? 246 GLU B N   1 
ATOM   2808 C CA  . GLU B 1 246 ? -4.618  34.846 4.150   1.00 47.14  ? 246 GLU B CA  1 
ATOM   2809 C C   . GLU B 1 246 ? -5.291  35.506 2.954   1.00 43.69  ? 246 GLU B C   1 
ATOM   2810 O O   . GLU B 1 246 ? -4.658  35.641 1.903   1.00 46.09  ? 246 GLU B O   1 
ATOM   2811 C CB  . GLU B 1 246 ? -4.392  33.357 3.869   1.00 50.54  ? 246 GLU B CB  1 
ATOM   2812 C CG  . GLU B 1 246 ? -3.765  32.553 5.013   1.00 65.94  ? 246 GLU B CG  1 
ATOM   2813 C CD  . GLU B 1 246 ? -2.942  33.388 5.983   1.00 74.21  ? 246 GLU B CD  1 
ATOM   2814 O OE1 . GLU B 1 246 ? -1.984  34.063 5.547   1.00 82.46  ? 246 GLU B OE1 1 
ATOM   2815 O OE2 . GLU B 1 246 ? -3.253  33.374 7.191   1.00 71.26  ? 246 GLU B OE2 1 
ATOM   2816 N N   . LEU B 1 247 ? -6.554  35.915 3.086   1.00 37.95  ? 247 LEU B N   1 
ATOM   2817 C CA  . LEU B 1 247 ? -7.197  36.682 2.023   1.00 40.07  ? 247 LEU B CA  1 
ATOM   2818 C C   . LEU B 1 247 ? -6.477  38.002 1.771   1.00 40.71  ? 247 LEU B C   1 
ATOM   2819 O O   . LEU B 1 247 ? -6.520  38.526 0.651   1.00 42.35  ? 247 LEU B O   1 
ATOM   2820 C CB  . LEU B 1 247 ? -8.667  36.930 2.371   1.00 34.04  ? 247 LEU B CB  1 
ATOM   2821 C CG  . LEU B 1 247 ? -9.654  35.772 2.232   1.00 40.30  ? 247 LEU B CG  1 
ATOM   2822 C CD1 . LEU B 1 247 ? -11.080 36.236 2.522   1.00 38.81  ? 247 LEU B CD1 1 
ATOM   2823 C CD2 . LEU B 1 247 ? -9.572  35.130 0.848   1.00 32.39  ? 247 LEU B CD2 1 
ATOM   2824 N N   . ASN B 1 248 ? -5.814  38.555 2.792   1.00 39.44  ? 248 ASN B N   1 
ATOM   2825 C CA  . ASN B 1 248 ? -5.031  39.767 2.583   1.00 40.97  ? 248 ASN B CA  1 
ATOM   2826 C C   . ASN B 1 248 ? -3.865  39.529 1.629   1.00 43.30  ? 248 ASN B C   1 
ATOM   2827 O O   . ASN B 1 248 ? -3.454  40.450 0.915   1.00 44.95  ? 248 ASN B O   1 
ATOM   2828 C CB  . ASN B 1 248 ? -4.528  40.310 3.921   1.00 43.88  ? 248 ASN B CB  1 
ATOM   2829 C CG  . ASN B 1 248 ? -5.658  40.720 4.843   1.00 49.13  ? 248 ASN B CG  1 
ATOM   2830 O OD1 . ASN B 1 248 ? -6.512  41.519 4.471   1.00 48.17  ? 248 ASN B OD1 1 
ATOM   2831 N ND2 . ASN B 1 248 ? -5.668  40.173 6.054   1.00 48.10  ? 248 ASN B ND2 1 
ATOM   2832 N N   . ASN B 1 249 ? -3.329  38.308 1.589   1.00 41.16  ? 249 ASN B N   1 
ATOM   2833 C CA  . ASN B 1 249 ? -2.248  37.989 0.662   1.00 38.91  ? 249 ASN B CA  1 
ATOM   2834 C C   . ASN B 1 249 ? -2.737  37.798 -0.763  1.00 44.75  ? 249 ASN B C   1 
ATOM   2835 O O   . ASN B 1 249 ? -1.933  37.874 -1.700  1.00 46.54  ? 249 ASN B O   1 
ATOM   2836 C CB  . ASN B 1 249 ? -1.522  36.721 1.111   1.00 43.77  ? 249 ASN B CB  1 
ATOM   2837 C CG  . ASN B 1 249 ? -0.862  36.881 2.458   1.00 56.32  ? 249 ASN B CG  1 
ATOM   2838 O OD1 . ASN B 1 249 ? -0.615  35.902 3.159   1.00 65.58  ? 249 ASN B OD1 1 
ATOM   2839 N ND2 . ASN B 1 249 ? -0.575  38.122 2.833   1.00 60.63  ? 249 ASN B ND2 1 
ATOM   2840 N N   . LYS B 1 250 ? -4.028  37.536 -0.943  1.00 37.50  ? 250 LYS B N   1 
ATOM   2841 C CA  . LYS B 1 250 ? -4.590  37.229 -2.248  1.00 42.43  ? 250 LYS B CA  1 
ATOM   2842 C C   . LYS B 1 250 ? -5.403  38.366 -2.839  1.00 34.13  ? 250 LYS B C   1 
ATOM   2843 O O   . LYS B 1 250 ? -5.395  38.547 -4.058  1.00 44.91  ? 250 LYS B O   1 
ATOM   2844 C CB  . LYS B 1 250 ? -5.485  35.987 -2.158  1.00 42.37  ? 250 LYS B CB  1 
ATOM   2845 C CG  . LYS B 1 250 ? -4.731  34.674 -2.121  1.00 42.39  ? 250 LYS B CG  1 
ATOM   2846 C CD  . LYS B 1 250 ? -3.721  34.589 -3.247  1.00 51.98  ? 250 LYS B CD  1 
ATOM   2847 C CE  . LYS B 1 250 ? -2.763  33.428 -3.043  1.00 67.42  ? 250 LYS B CE  1 
ATOM   2848 N NZ  . LYS B 1 250 ? -1.373  33.781 -3.441  1.00 73.60  ? 250 LYS B NZ  1 
ATOM   2849 N N   . LEU B 1 251 ? -6.104  39.128 -2.006  1.00 31.89  ? 251 LEU B N   1 
ATOM   2850 C CA  . LEU B 1 251 ? -6.993  40.189 -2.452  1.00 36.23  ? 251 LEU B CA  1 
ATOM   2851 C C   . LEU B 1 251 ? -6.437  41.541 -2.028  1.00 41.39  ? 251 LEU B C   1 
ATOM   2852 O O   . LEU B 1 251 ? -5.797  41.658 -0.978  1.00 43.98  ? 251 LEU B O   1 
ATOM   2853 C CB  . LEU B 1 251 ? -8.397  39.995 -1.871  1.00 31.00  ? 251 LEU B CB  1 
ATOM   2854 C CG  . LEU B 1 251 ? -9.089  38.678 -2.219  1.00 33.54  ? 251 LEU B CG  1 
ATOM   2855 C CD1 . LEU B 1 251 ? -10.462 38.609 -1.586  1.00 28.28  ? 251 LEU B CD1 1 
ATOM   2856 C CD2 . LEU B 1 251 ? -9.195  38.518 -3.723  1.00 32.19  ? 251 LEU B CD2 1 
ATOM   2857 N N   . LYS B 1 252 ? -6.671  42.558 -2.851  1.00 40.66  ? 252 LYS B N   1 
ATOM   2858 C CA  . LYS B 1 252 ? -6.324  43.925 -2.497  1.00 33.08  ? 252 LYS B CA  1 
ATOM   2859 C C   . LYS B 1 252 ? -7.567  44.798 -2.572  1.00 34.35  ? 252 LYS B C   1 
ATOM   2860 O O   . LYS B 1 252 ? -8.473  44.549 -3.374  1.00 33.81  ? 252 LYS B O   1 
ATOM   2861 C CB  . LYS B 1 252 ? -5.234  44.505 -3.412  1.00 33.29  ? 252 LYS B CB  1 
ATOM   2862 C CG  . LYS B 1 252 ? -5.630  44.635 -4.867  1.00 38.81  ? 252 LYS B CG  1 
ATOM   2863 C CD  . LYS B 1 252 ? -4.626  45.499 -5.616  1.00 49.37  ? 252 LYS B CD  1 
ATOM   2864 C CE  . LYS B 1 252 ? -4.784  46.972 -5.269  1.00 48.01  ? 252 LYS B CE  1 
ATOM   2865 N NZ  . LYS B 1 252 ? -3.813  47.832 -6.008  1.00 48.69  ? 252 LYS B NZ  1 
ATOM   2866 N N   . ALA B 1 253 ? -7.610  45.814 -1.715  1.00 38.66  ? 253 ALA B N   1 
ATOM   2867 C CA  . ALA B 1 253 ? -8.720  46.751 -1.747  1.00 35.93  ? 253 ALA B CA  1 
ATOM   2868 C C   . ALA B 1 253 ? -8.635  47.594 -3.010  1.00 39.53  ? 253 ALA B C   1 
ATOM   2869 O O   . ALA B 1 253 ? -7.562  48.087 -3.370  1.00 44.36  ? 253 ALA B O   1 
ATOM   2870 C CB  . ALA B 1 253 ? -8.709  47.640 -0.506  1.00 35.08  ? 253 ALA B CB  1 
ATOM   2871 N N   . LEU B 1 254 ? -9.755  47.716 -3.709  1.00 34.33  ? 254 LEU B N   1 
ATOM   2872 C CA  . LEU B 1 254 ? -9.864  48.669 -4.801  1.00 36.28  ? 254 LEU B CA  1 
ATOM   2873 C C   . LEU B 1 254 ? -10.136 50.052 -4.220  1.00 44.21  ? 254 LEU B C   1 
ATOM   2874 O O   . LEU B 1 254 ? -10.976 50.208 -3.330  1.00 46.81  ? 254 LEU B O   1 
ATOM   2875 C CB  . LEU B 1 254 ? -10.990 48.257 -5.755  1.00 43.43  ? 254 LEU B CB  1 
ATOM   2876 C CG  . LEU B 1 254 ? -10.746 47.338 -6.963  1.00 37.59  ? 254 LEU B CG  1 
ATOM   2877 C CD1 . LEU B 1 254 ? -12.052 47.142 -7.723  1.00 37.89  ? 254 LEU B CD1 1 
ATOM   2878 C CD2 . LEU B 1 254 ? -9.650  47.829 -7.913  1.00 39.74  ? 254 LEU B CD2 1 
ATOM   2879 N N   . ASP B 1 255 ? -9.402  51.057 -4.700  1.00 47.84  ? 255 ASP B N   1 
ATOM   2880 C CA  . ASP B 1 255 ? -9.585  52.435 -4.241  1.00 55.60  ? 255 ASP B CA  1 
ATOM   2881 C C   . ASP B 1 255 ? -10.545 53.068 -5.247  1.00 52.35  ? 255 ASP B C   1 
ATOM   2882 O O   . ASP B 1 255 ? -10.162 53.453 -6.357  1.00 47.48  ? 255 ASP B O   1 
ATOM   2883 C CB  . ASP B 1 255 ? -8.248  53.165 -4.094  1.00 56.38  ? 255 ASP B CB  1 
ATOM   2884 C CG  . ASP B 1 255 ? -8.389  54.671 -4.107  1.00 68.72  ? 255 ASP B CG  1 
ATOM   2885 O OD1 . ASP B 1 255 ? -9.377  55.164 -3.520  1.00 95.10  ? 255 ASP B OD1 1 
ATOM   2886 O OD2 . ASP B 1 255 ? -7.482  55.380 -4.607  1.00 65.42  ? 255 ASP B OD2 1 
ATOM   2887 N N   . VAL B 1 256 ? -11.800 53.176 -4.822  1.00 46.59  ? 256 VAL B N   1 
ATOM   2888 C CA  . VAL B 1 256 ? -12.970 53.245 -5.684  1.00 36.94  ? 256 VAL B CA  1 
ATOM   2889 C C   . VAL B 1 256 ? -13.983 54.112 -4.944  1.00 41.46  ? 256 VAL B C   1 
ATOM   2890 O O   . VAL B 1 256 ? -15.108 54.356 -5.398  1.00 42.75  ? 256 VAL B O   1 
ATOM   2891 C CB  . VAL B 1 256 ? -13.461 51.813 -5.979  1.00 37.35  ? 256 VAL B CB  1 
ATOM   2892 C CG1 . VAL B 1 256 ? -14.751 51.484 -5.249  1.00 37.06  ? 256 VAL B CG1 1 
ATOM   2893 C CG2 . VAL B 1 256 ? -13.589 51.590 -7.460  1.00 47.55  ? 256 VAL B CG2 1 
ATOM   2894 N N   . PHE B 1 257 ? -13.527 54.651 -3.817  1.00 36.71  ? 257 PHE B N   1 
ATOM   2895 C CA  . PHE B 1 257 ? -14.406 55.283 -2.843  1.00 41.54  ? 257 PHE B CA  1 
ATOM   2896 C C   . PHE B 1 257 ? -14.860 56.657 -3.304  1.00 34.87  ? 257 PHE B C   1 
ATOM   2897 O O   . PHE B 1 257 ? -15.942 57.113 -2.917  1.00 40.33  ? 257 PHE B O   1 
ATOM   2898 C CB  . PHE B 1 257 ? -13.666 55.366 -1.507  1.00 46.09  ? 257 PHE B CB  1 
ATOM   2899 C CG  . PHE B 1 257 ? -13.130 54.037 -1.040  1.00 65.30  ? 257 PHE B CG  1 
ATOM   2900 C CD1 . PHE B 1 257 ? -13.926 53.155 -0.329  1.00 64.46  ? 257 PHE B CD1 1 
ATOM   2901 C CD2 . PHE B 1 257 ? -11.840 53.642 -1.381  1.00 65.84  ? 257 PHE B CD2 1 
ATOM   2902 C CE1 . PHE B 1 257 ? -13.431 51.927 0.081   1.00 67.80  ? 257 PHE B CE1 1 
ATOM   2903 C CE2 . PHE B 1 257 ? -11.346 52.412 -0.981  1.00 70.68  ? 257 PHE B CE2 1 
ATOM   2904 C CZ  . PHE B 1 257 ? -12.141 51.556 -0.251  1.00 72.57  ? 257 PHE B CZ  1 
ATOM   2905 N N   . ASP B 1 258 ? -14.055 57.331 -4.124  1.00 41.25  ? 258 ASP B N   1 
ATOM   2906 C CA  . ASP B 1 258 ? -14.440 58.648 -4.605  1.00 42.12  ? 258 ASP B CA  1 
ATOM   2907 C C   . ASP B 1 258 ? -15.586 58.611 -5.602  1.00 34.52  ? 258 ASP B C   1 
ATOM   2908 O O   . ASP B 1 258 ? -16.124 59.672 -5.927  1.00 36.27  ? 258 ASP B O   1 
ATOM   2909 C CB  . ASP B 1 258 ? -13.235 59.354 -5.222  1.00 41.14  ? 258 ASP B CB  1 
ATOM   2910 C CG  . ASP B 1 258 ? -12.203 59.739 -4.190  1.00 50.42  ? 258 ASP B CG  1 
ATOM   2911 O OD1 . ASP B 1 258 ? -12.561 60.407 -3.203  1.00 55.40  ? 258 ASP B OD1 1 
ATOM   2912 O OD2 . ASP B 1 258 ? -11.030 59.347 -4.358  1.00 58.62  ? 258 ASP B OD2 1 
ATOM   2913 N N   . PHE B 1 259 ? -15.972 57.435 -6.096  1.00 30.75  ? 259 PHE B N   1 
ATOM   2914 C CA  . PHE B 1 259 ? -17.158 57.340 -6.939  1.00 37.29  ? 259 PHE B CA  1 
ATOM   2915 C C   . PHE B 1 259 ? -18.073 56.178 -6.564  1.00 36.90  ? 259 PHE B C   1 
ATOM   2916 O O   . PHE B 1 259 ? -18.869 55.738 -7.396  1.00 33.16  ? 259 PHE B O   1 
ATOM   2917 C CB  . PHE B 1 259 ? -16.781 57.275 -8.427  1.00 37.74  ? 259 PHE B CB  1 
ATOM   2918 C CG  . PHE B 1 259 ? -15.872 56.134 -8.817  1.00 33.65  ? 259 PHE B CG  1 
ATOM   2919 C CD1 . PHE B 1 259 ? -16.357 54.842 -8.957  1.00 30.84  ? 259 PHE B CD1 1 
ATOM   2920 C CD2 . PHE B 1 259 ? -14.540 56.377 -9.109  1.00 38.77  ? 259 PHE B CD2 1 
ATOM   2921 C CE1 . PHE B 1 259 ? -15.517 53.811 -9.340  1.00 37.84  ? 259 PHE B CE1 1 
ATOM   2922 C CE2 . PHE B 1 259 ? -13.699 55.355 -9.493  1.00 33.17  ? 259 PHE B CE2 1 
ATOM   2923 C CZ  . PHE B 1 259 ? -14.188 54.073 -9.612  1.00 39.99  ? 259 PHE B CZ  1 
ATOM   2924 N N   . THR B 1 260 ? -18.016 55.696 -5.330  1.00 28.26  ? 260 THR B N   1 
ATOM   2925 C CA  . THR B 1 260 ? -18.918 54.677 -4.839  1.00 33.07  ? 260 THR B CA  1 
ATOM   2926 C C   . THR B 1 260 ? -19.443 55.063 -3.462  1.00 34.39  ? 260 THR B C   1 
ATOM   2927 O O   . THR B 1 260 ? -18.794 55.830 -2.739  1.00 28.50  ? 260 THR B O   1 
ATOM   2928 C CB  . THR B 1 260 ? -18.235 53.302 -4.750  1.00 36.27  ? 260 THR B CB  1 
ATOM   2929 O OG1 . THR B 1 260 ? -16.998 53.428 -4.041  1.00 40.92  ? 260 THR B OG1 1 
ATOM   2930 C CG2 . THR B 1 260 ? -17.986 52.723 -6.143  1.00 39.52  ? 260 THR B CG2 1 
ATOM   2931 N N   . PRO B 1 261 ? -20.610 54.563 -3.076  1.00 33.55  ? 261 PRO B N   1 
ATOM   2932 C CA  . PRO B 1 261 ? -21.071 54.768 -1.703  1.00 38.34  ? 261 PRO B CA  1 
ATOM   2933 C C   . PRO B 1 261 ? -20.295 53.892 -0.734  1.00 37.98  ? 261 PRO B C   1 
ATOM   2934 O O   . PRO B 1 261 ? -19.685 52.885 -1.103  1.00 39.21  ? 261 PRO B O   1 
ATOM   2935 C CB  . PRO B 1 261 ? -22.547 54.363 -1.760  1.00 39.47  ? 261 PRO B CB  1 
ATOM   2936 C CG  . PRO B 1 261 ? -22.583 53.315 -2.821  1.00 39.93  ? 261 PRO B CG  1 
ATOM   2937 C CD  . PRO B 1 261 ? -21.574 53.765 -3.856  1.00 38.91  ? 261 PRO B CD  1 
ATOM   2938 N N   . ARG B 1 262 ? -20.295 54.327 0.522   1.00 30.51  ? 262 ARG B N   1 
ATOM   2939 C CA  . ARG B 1 262 ? -19.822 53.491 1.615   1.00 32.00  ? 262 ARG B CA  1 
ATOM   2940 C C   . ARG B 1 262 ? -20.614 52.192 1.654   1.00 34.27  ? 262 ARG B C   1 
ATOM   2941 O O   . ARG B 1 262 ? -21.841 52.204 1.796   1.00 42.17  ? 262 ARG B O   1 
ATOM   2942 C CB  . ARG B 1 262 ? -19.967 54.250 2.931   1.00 34.38  ? 262 ARG B CB  1 
ATOM   2943 C CG  . ARG B 1 262 ? -19.330 53.607 4.150   1.00 49.01  ? 262 ARG B CG  1 
ATOM   2944 C CD  . ARG B 1 262 ? -19.567 54.509 5.349   1.00 46.92  ? 262 ARG B CD  1 
ATOM   2945 N NE  . ARG B 1 262 ? -18.601 55.600 5.415   1.00 46.94  ? 262 ARG B NE  1 
ATOM   2946 C CZ  . ARG B 1 262 ? -18.531 56.473 6.411   1.00 45.73  ? 262 ARG B CZ  1 
ATOM   2947 N NH1 . ARG B 1 262 ? -19.446 56.505 7.367   1.00 43.89  ? 262 ARG B NH1 1 
ATOM   2948 N NH2 . ARG B 1 262 ? -17.542 57.362 6.427   1.00 45.03  ? 262 ARG B NH2 1 
ATOM   2949 N N   . PHE B 1 263 ? -19.913 51.071 1.520   1.00 28.98  ? 263 PHE B N   1 
ATOM   2950 C CA  . PHE B 1 263 ? -20.546 49.759 1.539   1.00 36.22  ? 263 PHE B CA  1 
ATOM   2951 C C   . PHE B 1 263 ? -20.646 49.268 2.979   1.00 39.11  ? 263 PHE B C   1 
ATOM   2952 O O   . PHE B 1 263 ? -19.625 49.104 3.656   1.00 38.32  ? 263 PHE B O   1 
ATOM   2953 C CB  . PHE B 1 263 ? -19.763 48.770 0.677   1.00 34.43  ? 263 PHE B CB  1 
ATOM   2954 C CG  . PHE B 1 263 ? -19.657 49.173 -0.767  1.00 42.26  ? 263 PHE B CG  1 
ATOM   2955 C CD1 . PHE B 1 263 ? -20.743 49.023 -1.616  1.00 44.00  ? 263 PHE B CD1 1 
ATOM   2956 C CD2 . PHE B 1 263 ? -18.474 49.686 -1.281  1.00 37.39  ? 263 PHE B CD2 1 
ATOM   2957 C CE1 . PHE B 1 263 ? -20.658 49.385 -2.945  1.00 38.61  ? 263 PHE B CE1 1 
ATOM   2958 C CE2 . PHE B 1 263 ? -18.382 50.049 -2.617  1.00 39.01  ? 263 PHE B CE2 1 
ATOM   2959 C CZ  . PHE B 1 263 ? -19.477 49.898 -3.446  1.00 34.95  ? 263 PHE B CZ  1 
ATOM   2960 N N   . GLU B 1 264 ? -21.872 49.027 3.437   1.00 38.96  ? 264 GLU B N   1 
ATOM   2961 C CA  . GLU B 1 264 ? -22.116 48.654 4.822   1.00 37.24  ? 264 GLU B CA  1 
ATOM   2962 C C   . GLU B 1 264 ? -23.506 48.046 4.932   1.00 38.20  ? 264 GLU B C   1 
ATOM   2963 O O   . GLU B 1 264 ? -24.392 48.340 4.125   1.00 33.06  ? 264 GLU B O   1 
ATOM   2964 C CB  . GLU B 1 264 ? -21.983 49.865 5.754   1.00 34.68  ? 264 GLU B CB  1 
ATOM   2965 C CG  . GLU B 1 264 ? -23.060 50.922 5.553   1.00 44.96  ? 264 GLU B CG  1 
ATOM   2966 C CD  . GLU B 1 264 ? -22.701 52.249 6.190   1.00 59.14  ? 264 GLU B CD  1 
ATOM   2967 O OE1 . GLU B 1 264 ? -21.684 52.308 6.911   1.00 57.91  ? 264 GLU B OE1 1 
ATOM   2968 O OE2 . GLU B 1 264 ? -23.435 53.236 5.971   1.00 55.13  ? 264 GLU B OE2 1 
ATOM   2969 N N   . TYR B 1 265 ? -23.675 47.178 5.925   1.00 36.02  ? 265 TYR B N   1 
ATOM   2970 C CA  . TYR B 1 265 ? -24.979 46.657 6.310   1.00 39.27  ? 265 TYR B CA  1 
ATOM   2971 C C   . TYR B 1 265 ? -25.324 47.153 7.704   1.00 40.14  ? 265 TYR B C   1 
ATOM   2972 O O   . TYR B 1 265 ? -24.470 47.166 8.597   1.00 41.73  ? 265 TYR B O   1 
ATOM   2973 C CB  . TYR B 1 265 ? -25.025 45.124 6.332   1.00 38.11  ? 265 TYR B CB  1 
ATOM   2974 C CG  . TYR B 1 265 ? -24.763 44.418 5.026   1.00 28.03  ? 265 TYR B CG  1 
ATOM   2975 C CD1 . TYR B 1 265 ? -25.443 44.764 3.864   1.00 32.26  ? 265 TYR B CD1 1 
ATOM   2976 C CD2 . TYR B 1 265 ? -23.870 43.357 4.971   1.00 27.61  ? 265 TYR B CD2 1 
ATOM   2977 C CE1 . TYR B 1 265 ? -25.207 44.091 2.673   1.00 35.61  ? 265 TYR B CE1 1 
ATOM   2978 C CE2 . TYR B 1 265 ? -23.630 42.681 3.793   1.00 40.71  ? 265 TYR B CE2 1 
ATOM   2979 C CZ  . TYR B 1 265 ? -24.298 43.048 2.645   1.00 31.82  ? 265 TYR B CZ  1 
ATOM   2980 O OH  . TYR B 1 265 ? -24.053 42.369 1.472   1.00 44.52  ? 265 TYR B OH  1 
ATOM   2981 N N   . TYR B 1 266 ? -26.578 47.549 7.889   1.00 34.30  ? 266 TYR B N   1 
ATOM   2982 C CA  . TYR B 1 266 ? -27.134 47.792 9.214   1.00 38.24  ? 266 TYR B CA  1 
ATOM   2983 C C   . TYR B 1 266 ? -28.005 46.592 9.561   1.00 35.54  ? 266 TYR B C   1 
ATOM   2984 O O   . TYR B 1 266 ? -29.059 46.383 8.952   1.00 38.18  ? 266 TYR B O   1 
ATOM   2985 C CB  . TYR B 1 266 ? -27.917 49.101 9.250   1.00 35.92  ? 266 TYR B CB  1 
ATOM   2986 C CG  . TYR B 1 266 ? -27.015 50.304 9.149   1.00 50.23  ? 266 TYR B CG  1 
ATOM   2987 C CD1 . TYR B 1 266 ? -26.388 50.822 10.275  1.00 53.87  ? 266 TYR B CD1 1 
ATOM   2988 C CD2 . TYR B 1 266 ? -26.757 50.898 7.923   1.00 46.09  ? 266 TYR B CD2 1 
ATOM   2989 C CE1 . TYR B 1 266 ? -25.549 51.916 10.184  1.00 53.72  ? 266 TYR B CE1 1 
ATOM   2990 C CE2 . TYR B 1 266 ? -25.918 51.991 7.822   1.00 55.61  ? 266 TYR B CE2 1 
ATOM   2991 C CZ  . TYR B 1 266 ? -25.316 52.497 8.955   1.00 62.92  ? 266 TYR B CZ  1 
ATOM   2992 O OH  . TYR B 1 266 ? -24.479 53.584 8.860   1.00 66.76  ? 266 TYR B OH  1 
ATOM   2993 N N   . VAL B 1 267 ? -27.548 45.794 10.521  1.00 31.85  ? 267 VAL B N   1 
ATOM   2994 C CA  . VAL B 1 267 ? -28.169 44.514 10.841  1.00 31.26  ? 267 VAL B CA  1 
ATOM   2995 C C   . VAL B 1 267 ? -29.225 44.722 11.917  1.00 39.32  ? 267 VAL B C   1 
ATOM   2996 O O   . VAL B 1 267 ? -28.955 45.330 12.960  1.00 37.20  ? 267 VAL B O   1 
ATOM   2997 C CB  . VAL B 1 267 ? -27.112 43.495 11.296  1.00 34.53  ? 267 VAL B CB  1 
ATOM   2998 C CG1 . VAL B 1 267 ? -27.754 42.139 11.550  1.00 37.30  ? 267 VAL B CG1 1 
ATOM   2999 C CG2 . VAL B 1 267 ? -26.003 43.382 10.256  1.00 35.62  ? 267 VAL B CG2 1 
ATOM   3000 N N   . ASP B 1 268 ? -30.431 44.216 11.661  1.00 40.17  ? 268 ASP B N   1 
ATOM   3001 C CA  . ASP B 1 268 ? -31.521 44.240 12.620  1.00 34.98  ? 268 ASP B CA  1 
ATOM   3002 C C   . ASP B 1 268 ? -31.905 42.817 12.997  1.00 38.77  ? 268 ASP B C   1 
ATOM   3003 O O   . ASP B 1 268 ? -31.793 41.892 12.187  1.00 37.71  ? 268 ASP B O   1 
ATOM   3004 C CB  . ASP B 1 268 ? -32.751 44.965 12.053  1.00 37.22  ? 268 ASP B CB  1 
ATOM   3005 C CG  . ASP B 1 268 ? -32.478 46.421 11.729  1.00 47.87  ? 268 ASP B CG  1 
ATOM   3006 O OD1 . ASP B 1 268 ? -31.699 47.060 12.466  1.00 56.31  ? 268 ASP B OD1 1 
ATOM   3007 O OD2 . ASP B 1 268 ? -33.042 46.922 10.734  1.00 55.15  ? 268 ASP B OD2 1 
ATOM   3008 N N   . LEU B 1 269 ? -32.346 42.647 14.240  1.00 30.90  ? 269 LEU B N   1 
ATOM   3009 C CA  . LEU B 1 269 ? -32.975 41.412 14.686  1.00 34.71  ? 269 LEU B CA  1 
ATOM   3010 C C   . LEU B 1 269 ? -34.481 41.585 14.555  1.00 32.73  ? 269 LEU B C   1 
ATOM   3011 O O   . LEU B 1 269 ? -35.061 42.457 15.206  1.00 36.18  ? 269 LEU B O   1 
ATOM   3012 C CB  . LEU B 1 269 ? -32.588 41.091 16.127  1.00 35.57  ? 269 LEU B CB  1 
ATOM   3013 C CG  . LEU B 1 269 ? -33.195 39.809 16.707  1.00 41.58  ? 269 LEU B CG  1 
ATOM   3014 C CD1 . LEU B 1 269 ? -32.515 38.568 16.146  1.00 27.37  ? 269 LEU B CD1 1 
ATOM   3015 C CD2 . LEU B 1 269 ? -33.122 39.834 18.223  1.00 31.30  ? 269 LEU B CD2 1 
ATOM   3016 N N   . VAL B 1 270 ? -35.108 40.755 13.724  1.00 32.71  ? 270 VAL B N   1 
ATOM   3017 C CA  . VAL B 1 270 ? -36.486 40.960 13.296  1.00 28.57  ? 270 VAL B CA  1 
ATOM   3018 C C   . VAL B 1 270 ? -37.327 39.770 13.737  1.00 34.12  ? 270 VAL B C   1 
ATOM   3019 O O   . VAL B 1 270 ? -36.838 38.635 13.787  1.00 35.66  ? 270 VAL B O   1 
ATOM   3020 C CB  . VAL B 1 270 ? -36.561 41.162 11.767  1.00 33.91  ? 270 VAL B CB  1 
ATOM   3021 C CG1 . VAL B 1 270 ? -37.986 41.445 11.313  1.00 35.61  ? 270 VAL B CG1 1 
ATOM   3022 C CG2 . VAL B 1 270 ? -35.621 42.279 11.335  1.00 33.51  ? 270 VAL B CG2 1 
ATOM   3023 N N   . TRP B 1 271 ? -38.589 40.035 14.078  1.00 37.30  ? 271 TRP B N   1 
ATOM   3024 C CA  . TRP B 1 271 ? -39.533 38.980 14.423  1.00 41.04  ? 271 TRP B CA  1 
ATOM   3025 C C   . TRP B 1 271 ? -40.935 39.417 14.026  1.00 38.51  ? 271 TRP B C   1 
ATOM   3026 O O   . TRP B 1 271 ? -41.177 40.580 13.705  1.00 39.39  ? 271 TRP B O   1 
ATOM   3027 C CB  . TRP B 1 271 ? -39.484 38.636 15.916  1.00 32.34  ? 271 TRP B CB  1 
ATOM   3028 C CG  . TRP B 1 271 ? -39.909 39.746 16.837  1.00 37.30  ? 271 TRP B CG  1 
ATOM   3029 C CD1 . TRP B 1 271 ? -41.156 39.950 17.362  1.00 41.91  ? 271 TRP B CD1 1 
ATOM   3030 C CD2 . TRP B 1 271 ? -39.075 40.779 17.372  1.00 29.86  ? 271 TRP B CD2 1 
ATOM   3031 N NE1 . TRP B 1 271 ? -41.147 41.055 18.180  1.00 39.06  ? 271 TRP B NE1 1 
ATOM   3032 C CE2 . TRP B 1 271 ? -39.883 41.581 18.204  1.00 36.20  ? 271 TRP B CE2 1 
ATOM   3033 C CE3 . TRP B 1 271 ? -37.725 41.108 17.223  1.00 32.96  ? 271 TRP B CE3 1 
ATOM   3034 C CZ2 . TRP B 1 271 ? -39.384 42.690 18.884  1.00 38.88  ? 271 TRP B CZ2 1 
ATOM   3035 C CZ3 . TRP B 1 271 ? -37.232 42.211 17.900  1.00 38.80  ? 271 TRP B CZ3 1 
ATOM   3036 C CH2 . TRP B 1 271 ? -38.060 42.989 18.718  1.00 38.85  ? 271 TRP B CH2 1 
ATOM   3037 N N   . SER B 1 272 ? -41.865 38.466 14.058  1.00 38.02  ? 272 SER B N   1 
ATOM   3038 C CA  . SER B 1 272 ? -43.257 38.731 13.731  1.00 39.72  ? 272 SER B CA  1 
ATOM   3039 C C   . SER B 1 272 ? -44.000 39.160 14.984  1.00 41.82  ? 272 SER B C   1 
ATOM   3040 O O   . SER B 1 272 ? -44.018 38.436 15.982  1.00 42.15  ? 272 SER B O   1 
ATOM   3041 C CB  . SER B 1 272 ? -43.908 37.487 13.133  1.00 45.95  ? 272 SER B CB  1 
ATOM   3042 O OG  . SER B 1 272 ? -45.320 37.596 13.105  1.00 47.04  ? 272 SER B OG  1 
ATOM   3043 N N   . ARG B 1 273 ? -44.608 40.342 14.930  1.00 47.86  ? 273 ARG B N   1 
ATOM   3044 C CA  . ARG B 1 273 ? -45.403 40.818 16.058  1.00 52.98  ? 273 ARG B CA  1 
ATOM   3045 C C   . ARG B 1 273 ? -46.446 39.801 16.498  1.00 51.97  ? 273 ARG B C   1 
ATOM   3046 O O   . ARG B 1 273 ? -46.661 39.619 17.701  1.00 55.92  ? 273 ARG B O   1 
ATOM   3047 C CB  . ARG B 1 273 ? -46.135 42.106 15.705  1.00 54.63  ? 273 ARG B CB  1 
ATOM   3048 C CG  . ARG B 1 273 ? -45.300 43.222 15.221  1.00 58.58  ? 273 ARG B CG  1 
ATOM   3049 C CD  . ARG B 1 273 ? -46.206 44.204 14.593  1.00 57.27  ? 273 ARG B CD  1 
ATOM   3050 N NE  . ARG B 1 273 ? -46.829 45.036 15.609  1.00 64.14  ? 273 ARG B NE  1 
ATOM   3051 C CZ  . ARG B 1 273 ? -46.862 46.356 15.539  1.00 63.39  ? 273 ARG B CZ  1 
ATOM   3052 N NH1 . ARG B 1 273 ? -46.339 46.998 14.509  1.00 61.44  ? 273 ARG B NH1 1 
ATOM   3053 N NH2 . ARG B 1 273 ? -47.428 47.046 16.523  1.00 61.66  ? 273 ARG B NH2 1 
ATOM   3054 N N   . GLU B 1 274 ? -47.118 39.156 15.552  1.00 53.47  ? 274 GLU B N   1 
ATOM   3055 C CA  . GLU B 1 274 ? -48.229 38.275 15.861  1.00 64.81  ? 274 GLU B CA  1 
ATOM   3056 C C   . GLU B 1 274 ? -47.817 36.820 16.004  1.00 61.95  ? 274 GLU B C   1 
ATOM   3057 O O   . GLU B 1 274 ? -48.699 35.947 15.982  1.00 65.66  ? 274 GLU B O   1 
ATOM   3058 C CB  . GLU B 1 274 ? -49.311 38.368 14.781  1.00 61.35  ? 274 GLU B CB  1 
ATOM   3059 C CG  . GLU B 1 274 ? -48.923 37.736 13.445  1.00 69.57  ? 274 GLU B CG  1 
ATOM   3060 C CD  . GLU B 1 274 ? -48.622 38.783 12.381  1.00 74.62  ? 274 GLU B CD  1 
ATOM   3061 O OE1 . GLU B 1 274 ? -49.485 39.001 11.501  1.00 68.21  ? 274 GLU B OE1 1 
ATOM   3062 O OE2 . GLU B 1 274 ? -47.536 39.404 12.423  1.00 67.35  ? 274 GLU B OE2 1 
ATOM   3063 N N   . SER B 1 275 ? -46.517 36.528 16.104  1.00 51.59  ? 275 SER B N   1 
ATOM   3064 C CA  . SER B 1 275 ? -46.134 35.165 16.410  1.00 59.90  ? 275 SER B CA  1 
ATOM   3065 C C   . SER B 1 275 ? -45.964 34.979 17.910  1.00 62.98  ? 275 SER B C   1 
ATOM   3066 O O   . SER B 1 275 ? -45.888 35.943 18.681  1.00 60.02  ? 275 SER B O   1 
ATOM   3067 C CB  . SER B 1 275 ? -44.864 34.793 15.665  1.00 55.46  ? 275 SER B CB  1 
ATOM   3068 O OG  . SER B 1 275 ? -45.185 34.227 14.408  1.00 56.86  ? 275 SER B OG  1 
ATOM   3069 N N   . GLU B 1 276 ? -45.926 33.711 18.315  1.00 64.41  ? 276 GLU B N   1 
ATOM   3070 C CA  . GLU B 1 276 ? -45.629 33.353 19.690  1.00 70.43  ? 276 GLU B CA  1 
ATOM   3071 C C   . GLU B 1 276 ? -44.130 33.151 19.798  1.00 70.59  ? 276 GLU B C   1 
ATOM   3072 O O   . GLU B 1 276 ? -43.574 32.239 19.174  1.00 67.58  ? 276 GLU B O   1 
ATOM   3073 C CB  . GLU B 1 276 ? -46.374 32.092 20.117  1.00 75.62  ? 276 GLU B CB  1 
ATOM   3074 C CG  . GLU B 1 276 ? -46.407 31.875 21.641  1.00 87.67  ? 276 GLU B CG  1 
ATOM   3075 C CD  . GLU B 1 276 ? -45.406 30.845 22.140  1.00 93.26  ? 276 GLU B CD  1 
ATOM   3076 O OE1 . GLU B 1 276 ? -44.395 31.233 22.756  1.00 89.52  ? 276 GLU B OE1 1 
ATOM   3077 O OE2 . GLU B 1 276 ? -45.649 29.633 21.960  1.00 103.15 ? 276 GLU B OE2 1 
ATOM   3078 N N   . LEU B 1 277 ? -43.479 34.017 20.562  1.00 67.80  ? 277 LEU B N   1 
ATOM   3079 C CA  . LEU B 1 277 ? -42.050 33.920 20.812  1.00 70.05  ? 277 LEU B CA  1 
ATOM   3080 C C   . LEU B 1 277 ? -41.824 33.083 22.063  1.00 67.42  ? 277 LEU B C   1 
ATOM   3081 O O   . LEU B 1 277 ? -42.466 33.318 23.092  1.00 72.69  ? 277 LEU B O   1 
ATOM   3082 C CB  . LEU B 1 277 ? -41.431 35.309 20.988  1.00 67.77  ? 277 LEU B CB  1 
ATOM   3083 C CG  . LEU B 1 277 ? -41.326 36.177 19.734  1.00 61.90  ? 277 LEU B CG  1 
ATOM   3084 C CD1 . LEU B 1 277 ? -40.638 37.494 20.062  1.00 57.94  ? 277 LEU B CD1 1 
ATOM   3085 C CD2 . LEU B 1 277 ? -40.585 35.435 18.632  1.00 59.61  ? 277 LEU B CD2 1 
ATOM   3086 N N   . GLY B 1 278 ? -40.934 32.098 21.968  1.00 63.57  ? 278 GLY B N   1 
ATOM   3087 C CA  . GLY B 1 278 ? -40.533 31.346 23.142  1.00 55.84  ? 278 GLY B CA  1 
ATOM   3088 C C   . GLY B 1 278 ? -39.780 32.219 24.127  1.00 49.66  ? 278 GLY B C   1 
ATOM   3089 O O   . GLY B 1 278 ? -39.444 33.373 23.867  1.00 44.58  ? 278 GLY B O   1 
ATOM   3090 N N   . ALA B 1 279 ? -39.513 31.644 25.301  1.00 52.77  ? 279 ALA B N   1 
ATOM   3091 C CA  . ALA B 1 279 ? -38.768 32.386 26.314  1.00 50.75  ? 279 ALA B CA  1 
ATOM   3092 C C   . ALA B 1 279 ? -37.367 32.731 25.824  1.00 43.37  ? 279 ALA B C   1 
ATOM   3093 O O   . ALA B 1 279 ? -36.823 33.787 26.162  1.00 45.75  ? 279 ALA B O   1 
ATOM   3094 C CB  . ALA B 1 279 ? -38.698 31.585 27.613  1.00 47.02  ? 279 ALA B CB  1 
ATOM   3095 N N   . ALA B 1 280 ? -36.773 31.855 25.012  1.00 37.13  ? 280 ALA B N   1 
ATOM   3096 C CA  . ALA B 1 280 ? -35.426 32.098 24.505  1.00 39.20  ? 280 ALA B CA  1 
ATOM   3097 C C   . ALA B 1 280 ? -35.381 33.340 23.624  1.00 42.84  ? 280 ALA B C   1 
ATOM   3098 O O   . ALA B 1 280 ? -34.539 34.223 23.819  1.00 38.61  ? 280 ALA B O   1 
ATOM   3099 C CB  . ALA B 1 280 ? -34.932 30.875 23.734  1.00 37.60  ? 280 ALA B CB  1 
ATOM   3100 N N   . ALA B 1 281 ? -36.274 33.419 22.635  1.00 41.56  ? 281 ALA B N   1 
ATOM   3101 C CA  . ALA B 1 281 ? -36.302 34.588 21.762  1.00 41.63  ? 281 ALA B CA  1 
ATOM   3102 C C   . ALA B 1 281 ? -36.598 35.857 22.550  1.00 36.81  ? 281 ALA B C   1 
ATOM   3103 O O   . ALA B 1 281 ? -35.980 36.902 22.311  1.00 38.33  ? 281 ALA B O   1 
ATOM   3104 C CB  . ALA B 1 281 ? -37.335 34.392 20.653  1.00 44.11  ? 281 ALA B CB  1 
ATOM   3105 N N   . ARG B 1 282 ? -37.502 35.771 23.498  1.00 38.86  ? 282 ARG B N   1 
ATOM   3106 C CA  . ARG B 1 282 ? -37.842 36.917 24.297  1.00 44.43  ? 282 ARG B CA  1 
ATOM   3107 C C   . ARG B 1 282 ? -36.678 37.382 25.115  1.00 43.75  ? 282 ARG B C   1 
ATOM   3108 O O   . ARG B 1 282 ? -36.451 38.545 25.226  1.00 49.84  ? 282 ARG B O   1 
ATOM   3109 C CB  . ARG B 1 282 ? -39.042 36.629 25.172  1.00 53.17  ? 282 ARG B CB  1 
ATOM   3110 C CG  . ARG B 1 282 ? -40.344 36.622 24.412  1.00 57.87  ? 282 ARG B CG  1 
ATOM   3111 C CD  . ARG B 1 282 ? -41.550 36.673 25.314  1.00 59.67  ? 282 ARG B CD  1 
ATOM   3112 N NE  . ARG B 1 282 ? -42.027 35.351 25.652  1.00 72.30  ? 282 ARG B NE  1 
ATOM   3113 C CZ  . ARG B 1 282 ? -41.961 34.843 26.871  1.00 76.54  ? 282 ARG B CZ  1 
ATOM   3114 N NH1 . ARG B 1 282 ? -41.420 35.553 27.854  1.00 76.96  ? 282 ARG B NH1 1 
ATOM   3115 N NH2 . ARG B 1 282 ? -42.424 33.635 27.114  1.00 83.60  ? 282 ARG B NH2 1 
ATOM   3116 N N   . PHE B 1 283 ? -35.937 36.463 25.687  1.00 41.61  ? 283 PHE B N   1 
ATOM   3117 C CA  . PHE B 1 283 ? -34.752 36.811 26.468  1.00 40.85  ? 283 PHE B CA  1 
ATOM   3118 C C   . PHE B 1 283 ? -33.750 37.587 25.623  1.00 43.13  ? 283 PHE B C   1 
ATOM   3119 O O   . PHE B 1 283 ? -33.220 38.619 26.053  1.00 46.86  ? 283 PHE B O   1 
ATOM   3120 C CB  . PHE B 1 283 ? -34.100 35.546 27.035  1.00 36.92  ? 283 PHE B CB  1 
ATOM   3121 C CG  . PHE B 1 283 ? -32.713 35.772 27.578  1.00 43.77  ? 283 PHE B CG  1 
ATOM   3122 C CD1 . PHE B 1 283 ? -32.532 36.258 28.863  1.00 46.55  ? 283 PHE B CD1 1 
ATOM   3123 C CD2 . PHE B 1 283 ? -31.593 35.513 26.801  1.00 36.92  ? 283 PHE B CD2 1 
ATOM   3124 C CE1 . PHE B 1 283 ? -31.261 36.477 29.366  1.00 52.22  ? 283 PHE B CE1 1 
ATOM   3125 C CE2 . PHE B 1 283 ? -30.321 35.732 27.297  1.00 44.25  ? 283 PHE B CE2 1 
ATOM   3126 C CZ  . PHE B 1 283 ? -30.155 36.215 28.582  1.00 55.13  ? 283 PHE B CZ  1 
ATOM   3127 N N   . LEU B 1 284 ? -33.475 37.095 24.412  1.00 41.59  ? 284 LEU B N   1 
ATOM   3128 C CA  . LEU B 1 284 ? -32.503 37.746 23.542  1.00 41.04  ? 284 LEU B CA  1 
ATOM   3129 C C   . LEU B 1 284 ? -32.926 39.173 23.224  1.00 42.94  ? 284 LEU B C   1 
ATOM   3130 O O   . LEU B 1 284 ? -32.101 40.094 23.226  1.00 42.17  ? 284 LEU B O   1 
ATOM   3131 C CB  . LEU B 1 284 ? -32.328 36.935 22.258  1.00 32.28  ? 284 LEU B CB  1 
ATOM   3132 C CG  . LEU B 1 284 ? -31.310 37.461 21.244  1.00 41.81  ? 284 LEU B CG  1 
ATOM   3133 C CD1 . LEU B 1 284 ? -29.936 37.594 21.886  1.00 41.97  ? 284 LEU B CD1 1 
ATOM   3134 C CD2 . LEU B 1 284 ? -31.259 36.548 20.026  1.00 31.57  ? 284 LEU B CD2 1 
ATOM   3135 N N   . ILE B 1 285 ? -34.218 39.377 22.957  1.00 43.56  ? 285 ILE B N   1 
ATOM   3136 C CA  . ILE B 1 285 ? -34.706 40.714 22.628  1.00 43.02  ? 285 ILE B CA  1 
ATOM   3137 C C   . ILE B 1 285 ? -34.558 41.643 23.828  1.00 46.03  ? 285 ILE B C   1 
ATOM   3138 O O   . ILE B 1 285 ? -34.099 42.785 23.700  1.00 48.74  ? 285 ILE B O   1 
ATOM   3139 C CB  . ILE B 1 285 ? -36.163 40.647 22.142  1.00 43.56  ? 285 ILE B CB  1 
ATOM   3140 C CG1 . ILE B 1 285 ? -36.213 40.046 20.740  1.00 46.94  ? 285 ILE B CG1 1 
ATOM   3141 C CG2 . ILE B 1 285 ? -36.805 42.031 22.169  1.00 40.33  ? 285 ILE B CG2 1 
ATOM   3142 C CD1 . ILE B 1 285 ? -37.568 39.543 20.339  1.00 42.44  ? 285 ILE B CD1 1 
ATOM   3143 N N   . ASP B 1 286 ? -34.948 41.166 25.013  1.00 43.32  ? 286 ASP B N   1 
ATOM   3144 C CA  . ASP B 1 286 ? -34.769 41.967 26.220  1.00 49.96  ? 286 ASP B CA  1 
ATOM   3145 C C   . ASP B 1 286 ? -33.297 42.268 26.463  1.00 51.02  ? 286 ASP B C   1 
ATOM   3146 O O   . ASP B 1 286 ? -32.937 43.401 26.798  1.00 56.16  ? 286 ASP B O   1 
ATOM   3147 C CB  . ASP B 1 286 ? -35.372 41.251 27.430  1.00 54.11  ? 286 ASP B CB  1 
ATOM   3148 C CG  . ASP B 1 286 ? -36.884 41.215 27.391  1.00 65.21  ? 286 ASP B CG  1 
ATOM   3149 O OD1 . ASP B 1 286 ? -37.467 41.699 26.398  1.00 68.19  ? 286 ASP B OD1 1 
ATOM   3150 O OD2 . ASP B 1 286 ? -37.497 40.707 28.356  1.00 73.53  ? 286 ASP B OD2 1 
ATOM   3151 N N   . TYR B 1 287 ? -32.433 41.265 26.295  1.00 49.09  ? 287 TYR B N   1 
ATOM   3152 C CA  . TYR B 1 287 ? -31.006 41.457 26.532  1.00 45.13  ? 287 TYR B CA  1 
ATOM   3153 C C   . TYR B 1 287 ? -30.445 42.561 25.646  1.00 52.16  ? 287 TYR B C   1 
ATOM   3154 O O   . TYR B 1 287 ? -29.685 43.420 26.108  1.00 54.49  ? 287 TYR B O   1 
ATOM   3155 C CB  . TYR B 1 287 ? -30.264 40.143 26.290  1.00 42.46  ? 287 TYR B CB  1 
ATOM   3156 C CG  . TYR B 1 287 ? -28.814 40.149 26.719  1.00 49.39  ? 287 TYR B CG  1 
ATOM   3157 C CD1 . TYR B 1 287 ? -27.816 40.614 25.871  1.00 47.17  ? 287 TYR B CD1 1 
ATOM   3158 C CD2 . TYR B 1 287 ? -28.441 39.664 27.965  1.00 56.32  ? 287 TYR B CD2 1 
ATOM   3159 C CE1 . TYR B 1 287 ? -26.489 40.611 26.260  1.00 47.85  ? 287 TYR B CE1 1 
ATOM   3160 C CE2 . TYR B 1 287 ? -27.120 39.656 28.362  1.00 53.17  ? 287 TYR B CE2 1 
ATOM   3161 C CZ  . TYR B 1 287 ? -26.147 40.130 27.506  1.00 57.04  ? 287 TYR B CZ  1 
ATOM   3162 O OH  . TYR B 1 287 ? -24.828 40.124 27.897  1.00 70.07  ? 287 TYR B OH  1 
ATOM   3163 N N   . ILE B 1 288 ? -30.811 42.554 24.363  1.00 52.97  ? 288 ILE B N   1 
ATOM   3164 C CA  . ILE B 1 288 ? -30.282 43.550 23.434  1.00 47.64  ? 288 ILE B CA  1 
ATOM   3165 C C   . ILE B 1 288 ? -30.815 44.935 23.778  1.00 53.01  ? 288 ILE B C   1 
ATOM   3166 O O   . ILE B 1 288 ? -30.045 45.882 23.970  1.00 54.27  ? 288 ILE B O   1 
ATOM   3167 C CB  . ILE B 1 288 ? -30.609 43.157 21.982  1.00 47.58  ? 288 ILE B CB  1 
ATOM   3168 C CG1 . ILE B 1 288 ? -29.602 42.110 21.485  1.00 43.72  ? 288 ILE B CG1 1 
ATOM   3169 C CG2 . ILE B 1 288 ? -30.591 44.375 21.074  1.00 48.65  ? 288 ILE B CG2 1 
ATOM   3170 C CD1 . ILE B 1 288 ? -30.219 41.013 20.648  1.00 44.08  ? 288 ILE B CD1 1 
ATOM   3171 N N   . ARG B 1 289 ? -32.142 45.069 23.868  1.00 51.17  ? 289 ARG B N   1 
ATOM   3172 C CA  . ARG B 1 289 ? -32.750 46.335 24.275  1.00 56.76  ? 289 ARG B CA  1 
ATOM   3173 C C   . ARG B 1 289 ? -32.109 46.884 25.546  1.00 62.04  ? 289 ARG B C   1 
ATOM   3174 O O   . ARG B 1 289 ? -31.820 48.085 25.638  1.00 64.78  ? 289 ARG B O   1 
ATOM   3175 C CB  . ARG B 1 289 ? -34.251 46.146 24.490  1.00 49.16  ? 289 ARG B CB  1 
ATOM   3176 C CG  . ARG B 1 289 ? -35.068 46.058 23.223  1.00 47.39  ? 289 ARG B CG  1 
ATOM   3177 C CD  . ARG B 1 289 ? -36.491 45.666 23.556  1.00 48.21  ? 289 ARG B CD  1 
ATOM   3178 N NE  . ARG B 1 289 ? -37.378 45.759 22.406  1.00 53.28  ? 289 ARG B NE  1 
ATOM   3179 C CZ  . ARG B 1 289 ? -38.618 45.294 22.389  1.00 56.74  ? 289 ARG B CZ  1 
ATOM   3180 N NH1 . ARG B 1 289 ? -39.135 44.672 23.436  1.00 59.23  ? 289 ARG B NH1 1 
ATOM   3181 N NH2 . ARG B 1 289 ? -39.358 45.455 21.296  1.00 64.07  ? 289 ARG B NH2 1 
ATOM   3182 N N   . ASN B 1 290 ? -31.878 46.015 26.535  1.00 63.50  ? 290 ASN B N   1 
ATOM   3183 C CA  . ASN B 1 290 ? -31.280 46.448 27.795  1.00 63.69  ? 290 ASN B CA  1 
ATOM   3184 C C   . ASN B 1 290 ? -29.858 46.958 27.578  1.00 64.39  ? 290 ASN B C   1 
ATOM   3185 O O   . ASN B 1 290 ? -29.433 47.929 28.213  1.00 72.30  ? 290 ASN B O   1 
ATOM   3186 C CB  . ASN B 1 290 ? -31.325 45.282 28.791  1.00 61.99  ? 290 ASN B CB  1 
ATOM   3187 C CG  . ASN B 1 290 ? -30.791 45.638 30.179  1.00 72.25  ? 290 ASN B CG  1 
ATOM   3188 O OD1 . ASN B 1 290 ? -29.676 46.135 30.336  1.00 71.39  ? 290 ASN B OD1 1 
ATOM   3189 N ND2 . ASN B 1 290 ? -31.609 45.380 31.200  1.00 76.16  ? 290 ASN B ND2 1 
ATOM   3190 N N   . LYS B 1 291 ? -29.112 46.323 26.673  1.00 69.12  ? 291 LYS B N   1 
ATOM   3191 C CA  . LYS B 1 291 ? -27.764 46.785 26.349  1.00 68.75  ? 291 LYS B CA  1 
ATOM   3192 C C   . LYS B 1 291 ? -27.781 48.156 25.684  1.00 77.79  ? 291 LYS B C   1 
ATOM   3193 O O   . LYS B 1 291 ? -26.968 49.024 26.024  1.00 86.76  ? 291 LYS B O   1 
ATOM   3194 C CB  . LYS B 1 291 ? -27.059 45.772 25.441  1.00 71.10  ? 291 LYS B CB  1 
ATOM   3195 C CG  . LYS B 1 291 ? -26.610 44.495 26.130  1.00 75.05  ? 291 LYS B CG  1 
ATOM   3196 C CD  . LYS B 1 291 ? -25.723 44.767 27.340  1.00 73.28  ? 291 LYS B CD  1 
ATOM   3197 C CE  . LYS B 1 291 ? -25.964 43.743 28.446  1.00 74.07  ? 291 LYS B CE  1 
ATOM   3198 N NZ  . LYS B 1 291 ? -25.486 44.206 29.783  1.00 75.72  ? 291 LYS B NZ  1 
ATOM   3199 N N   . ARG B 1 292 ? -28.698 48.376 24.739  1.00 75.89  ? 292 ARG B N   1 
ATOM   3200 C CA  . ARG B 1 292 ? -28.725 49.613 23.963  1.00 79.74  ? 292 ARG B CA  1 
ATOM   3201 C C   . ARG B 1 292 ? -29.004 50.831 24.838  1.00 88.11  ? 292 ARG B C   1 
ATOM   3202 O O   . ARG B 1 292 ? -28.965 51.968 24.358  1.00 95.87  ? 292 ARG B O   1 
ATOM   3203 C CB  . ARG B 1 292 ? -29.764 49.515 22.842  1.00 77.37  ? 292 ARG B CB  1 
ATOM   3204 C CG  . ARG B 1 292 ? -29.673 48.229 22.035  1.00 80.98  ? 292 ARG B CG  1 
ATOM   3205 C CD  . ARG B 1 292 ? -30.062 48.430 20.580  1.00 79.91  ? 292 ARG B CD  1 
ATOM   3206 N NE  . ARG B 1 292 ? -28.982 49.019 19.796  1.00 87.31  ? 292 ARG B NE  1 
ATOM   3207 C CZ  . ARG B 1 292 ? -27.852 48.399 19.479  1.00 85.32  ? 292 ARG B CZ  1 
ATOM   3208 N NH1 . ARG B 1 292 ? -27.622 47.147 19.841  1.00 81.77  ? 292 ARG B NH1 1 
ATOM   3209 N NH2 . ARG B 1 292 ? -26.933 49.049 18.771  1.00 80.22  ? 292 ARG B NH2 1 
ATOM   3210 N N   . MET B 1 293 ? -29.293 50.606 26.114  1.00 88.14  ? 293 MET B N   1 
ATOM   3211 C CA  . MET B 1 293 ? -29.405 51.690 27.077  1.00 89.02  ? 293 MET B CA  1 
ATOM   3212 C C   . MET B 1 293 ? -28.704 51.323 28.380  1.00 88.28  ? 293 MET B C   1 
ATOM   3213 O O   . MET B 1 293 ? -27.475 51.321 28.454  1.00 81.18  ? 293 MET B O   1 
ATOM   3214 C CB  . MET B 1 293 ? -30.869 52.027 27.342  1.00 93.67  ? 293 MET B CB  1 
ATOM   3215 C CG  . MET B 1 293 ? -31.778 50.820 27.366  1.00 98.70  ? 293 MET B CG  1 
ATOM   3216 S SD  . MET B 1 293 ? -33.516 51.289 27.358  1.00 116.66 ? 293 MET B SD  1 
ATOM   3217 C CE  . MET B 1 293 ? -34.266 49.754 27.907  1.00 100.03 ? 293 MET B CE  1 
HETATM 3218 O O   . HOH C 2 .   ? -20.085 22.139 1.222   1.00 43.84  ? 301 HOH A O   1 
HETATM 3219 O O   . HOH C 2 .   ? -34.198 17.801 4.802   1.00 62.95  ? 302 HOH A O   1 
HETATM 3220 O O   . HOH C 2 .   ? -15.866 26.132 -1.615  1.00 46.76  ? 303 HOH A O   1 
HETATM 3221 O O   . HOH C 2 .   ? -22.881 7.473  16.881  1.00 40.72  ? 304 HOH A O   1 
HETATM 3222 O O   . HOH C 2 .   ? -23.139 9.798  -7.774  1.00 52.29  ? 305 HOH A O   1 
HETATM 3223 O O   . HOH C 2 .   ? -16.468 5.939  -1.517  1.00 39.21  ? 306 HOH A O   1 
HETATM 3224 O O   . HOH C 2 .   ? -14.082 11.012 3.372   1.00 51.26  ? 307 HOH A O   1 
HETATM 3225 O O   . HOH C 2 .   ? -16.939 10.154 -9.297  1.00 59.11  ? 308 HOH A O   1 
HETATM 3226 O O   . HOH C 2 .   ? -33.980 23.618 -16.412 1.00 35.46  ? 309 HOH A O   1 
HETATM 3227 O O   . HOH C 2 .   ? -18.335 16.756 25.520  1.00 49.04  ? 310 HOH A O   1 
HETATM 3228 O O   . HOH C 2 .   ? -8.574  10.061 21.647  1.00 57.37  ? 311 HOH A O   1 
HETATM 3229 O O   . HOH C 2 .   ? -27.341 29.557 -21.587 1.00 53.99  ? 312 HOH A O   1 
HETATM 3230 O O   . HOH C 2 .   ? -16.879 31.321 15.263  1.00 49.61  ? 313 HOH A O   1 
HETATM 3231 O O   . HOH C 2 .   ? -22.292 9.461  -14.233 1.00 54.19  ? 314 HOH A O   1 
HETATM 3232 O O   . HOH C 2 .   ? -25.790 7.673  12.479  1.00 34.36  ? 315 HOH A O   1 
HETATM 3233 O O   . HOH C 2 .   ? -20.670 7.084  0.688   1.00 36.71  ? 316 HOH A O   1 
HETATM 3234 O O   . HOH C 2 .   ? -22.168 24.163 2.769   1.00 33.05  ? 317 HOH A O   1 
HETATM 3235 O O   . HOH C 2 .   ? -6.626  14.107 15.301  1.00 51.49  ? 318 HOH A O   1 
HETATM 3236 O O   . HOH C 2 .   ? -23.756 10.415 8.050   1.00 42.32  ? 319 HOH A O   1 
HETATM 3237 O O   . HOH C 2 .   ? -12.350 8.721  15.222  1.00 47.63  ? 320 HOH A O   1 
HETATM 3238 O O   . HOH C 2 .   ? -26.504 27.009 -21.229 1.00 48.34  ? 321 HOH A O   1 
HETATM 3239 O O   . HOH C 2 .   ? -20.407 8.152  3.333   1.00 35.41  ? 322 HOH A O   1 
HETATM 3240 O O   . HOH C 2 .   ? -22.216 17.021 11.490  1.00 34.13  ? 323 HOH A O   1 
HETATM 3241 O O   . HOH C 2 .   ? -13.945 18.433 0.611   1.00 34.44  ? 324 HOH A O   1 
HETATM 3242 O O   . HOH C 2 .   ? -15.824 22.676 19.126  1.00 36.92  ? 325 HOH A O   1 
HETATM 3243 O O   . HOH C 2 .   ? -23.546 17.262 9.071   1.00 27.60  ? 326 HOH A O   1 
HETATM 3244 O O   . HOH C 2 .   ? -32.168 21.646 -16.834 1.00 36.23  ? 327 HOH A O   1 
HETATM 3245 O O   . HOH C 2 .   ? -21.409 30.103 3.041   1.00 41.16  ? 328 HOH A O   1 
HETATM 3246 O O   . HOH C 2 .   ? -13.659 29.355 6.573   1.00 51.52  ? 329 HOH A O   1 
HETATM 3247 O O   . HOH C 2 .   ? -30.176 29.496 -16.751 1.00 41.36  ? 330 HOH A O   1 
HETATM 3248 O O   . HOH C 2 .   ? -29.990 20.143 20.890  1.00 39.16  ? 331 HOH A O   1 
HETATM 3249 O O   . HOH C 2 .   ? -20.075 20.773 22.984  1.00 47.86  ? 332 HOH A O   1 
HETATM 3250 O O   . HOH C 2 .   ? -14.731 10.602 6.772   1.00 42.39  ? 333 HOH A O   1 
HETATM 3251 O O   . HOH C 2 .   ? -23.420 11.692 -1.838  1.00 39.97  ? 334 HOH A O   1 
HETATM 3252 O O   . HOH C 2 .   ? -9.805  13.510 19.165  1.00 47.65  ? 335 HOH A O   1 
HETATM 3253 O O   . HOH C 2 .   ? -21.791 17.575 7.126   1.00 38.91  ? 336 HOH A O   1 
HETATM 3254 O O   . HOH C 2 .   ? -25.406 7.001  15.445  1.00 32.32  ? 337 HOH A O   1 
HETATM 3255 O O   . HOH C 2 .   ? -11.228 2.811  16.478  1.00 64.89  ? 338 HOH A O   1 
HETATM 3256 O O   . HOH C 2 .   ? -13.019 27.692 4.479   1.00 49.50  ? 339 HOH A O   1 
HETATM 3257 O O   . HOH C 2 .   ? -21.993 19.353 24.246  1.00 41.73  ? 340 HOH A O   1 
HETATM 3258 O O   . HOH C 2 .   ? -29.382 8.394  14.986  1.00 43.07  ? 341 HOH A O   1 
HETATM 3259 O O   . HOH C 2 .   ? -28.412 20.743 22.344  1.00 43.97  ? 342 HOH A O   1 
HETATM 3260 O O   . HOH C 2 .   ? -24.362 41.467 -17.458 1.00 52.31  ? 343 HOH A O   1 
HETATM 3261 O O   . HOH C 2 .   ? -25.411 29.376 -23.087 1.00 46.17  ? 344 HOH A O   1 
HETATM 3262 O O   . HOH C 2 .   ? -13.244 11.495 -7.431  1.00 53.99  ? 345 HOH A O   1 
HETATM 3263 O O   . HOH C 2 .   ? -28.100 9.164  18.229  1.00 55.82  ? 346 HOH A O   1 
HETATM 3264 O O   . HOH C 2 .   ? -27.134 7.588  17.000  1.00 40.95  ? 347 HOH A O   1 
HETATM 3265 O O   . HOH C 2 .   ? -31.492 9.612  15.373  1.00 55.84  ? 348 HOH A O   1 
HETATM 3266 O O   . HOH D 2 .   ? -31.580 39.267 -8.796  1.00 63.17  ? 301 HOH B O   1 
HETATM 3267 O O   . HOH D 2 .   ? -21.982 38.451 5.018   1.00 50.98  ? 302 HOH B O   1 
HETATM 3268 O O   . HOH D 2 .   ? -10.375 39.387 -9.208  1.00 29.12  ? 303 HOH B O   1 
HETATM 3269 O O   . HOH D 2 .   ? -42.303 33.582 13.488  1.00 43.11  ? 304 HOH B O   1 
HETATM 3270 O O   . HOH D 2 .   ? -20.147 43.235 -5.887  1.00 47.64  ? 305 HOH B O   1 
HETATM 3271 O O   . HOH D 2 .   ? -37.231 48.038 5.402   1.00 53.76  ? 306 HOH B O   1 
HETATM 3272 O O   . HOH D 2 .   ? -34.428 36.673 -7.197  1.00 62.03  ? 307 HOH B O   1 
HETATM 3273 O O   . HOH D 2 .   ? -38.099 26.141 15.987  1.00 55.16  ? 308 HOH B O   1 
HETATM 3274 O O   . HOH D 2 .   ? -11.190 56.714 -4.784  1.00 42.41  ? 309 HOH B O   1 
HETATM 3275 O O   . HOH D 2 .   ? -5.643  48.601 -8.522  1.00 41.52  ? 310 HOH B O   1 
HETATM 3276 O O   . HOH D 2 .   ? -17.884 42.683 8.012   1.00 37.44  ? 311 HOH B O   1 
HETATM 3277 O O   . HOH D 2 .   ? -1.739  42.583 -11.079 1.00 49.29  ? 312 HOH B O   1 
HETATM 3278 O O   . HOH D 2 .   ? -28.676 25.375 23.842  1.00 45.56  ? 313 HOH B O   1 
HETATM 3279 O O   . HOH D 2 .   ? -18.074 45.383 -17.166 1.00 40.12  ? 314 HOH B O   1 
HETATM 3280 O O   . HOH D 2 .   ? -17.449 61.162 -4.000  1.00 44.09  ? 315 HOH B O   1 
HETATM 3281 O O   . HOH D 2 .   ? -41.308 35.709 14.879  1.00 36.68  ? 316 HOH B O   1 
HETATM 3282 O O   . HOH D 2 .   ? -22.836 35.708 2.394   1.00 37.43  ? 317 HOH B O   1 
HETATM 3283 O O   . HOH D 2 .   ? -39.416 40.347 24.815  1.00 54.38  ? 318 HOH B O   1 
HETATM 3284 O O   . HOH D 2 .   ? -23.949 30.443 -4.655  1.00 53.80  ? 319 HOH B O   1 
HETATM 3285 O O   . HOH D 2 .   ? 2.467   46.916 -10.860 1.00 50.83  ? 320 HOH B O   1 
HETATM 3286 O O   . HOH D 2 .   ? -21.642 42.561 -1.490  1.00 45.53  ? 321 HOH B O   1 
HETATM 3287 O O   . HOH D 2 .   ? -17.509 50.414 5.237   1.00 53.74  ? 322 HOH B O   1 
HETATM 3288 O O   . HOH D 2 .   ? -28.456 47.824 5.628   1.00 46.51  ? 323 HOH B O   1 
HETATM 3289 O O   . HOH D 2 .   ? -22.270 42.601 -4.018  1.00 30.32  ? 324 HOH B O   1 
HETATM 3290 O O   . HOH D 2 .   ? -0.809  43.797 -7.528  1.00 58.19  ? 325 HOH B O   1 
HETATM 3291 O O   . HOH D 2 .   ? -12.364 40.409 -14.842 1.00 49.67  ? 326 HOH B O   1 
HETATM 3292 O O   . HOH D 2 .   ? -13.289 41.736 -16.543 1.00 45.71  ? 327 HOH B O   1 
HETATM 3293 O O   . HOH D 2 .   ? -22.082 39.093 -17.668 1.00 39.50  ? 328 HOH B O   1 
HETATM 3294 O O   . HOH D 2 .   ? -11.626 31.324 11.484  1.00 52.60  ? 329 HOH B O   1 
HETATM 3295 O O   . HOH D 2 .   ? -7.018  50.438 -6.812  1.00 41.49  ? 330 HOH B O   1 
HETATM 3296 O O   . HOH D 2 .   ? -15.518 63.656 -7.467  1.00 51.56  ? 331 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LEU A 91  ? 0.9765 0.8811 0.7447 0.0372  -0.1193 0.0336  91  LEU A N   
2    C CA  . LEU A 91  ? 1.0396 0.9169 0.7834 0.0314  -0.1156 0.0402  91  LEU A CA  
3    C C   . LEU A 91  ? 1.0682 0.9419 0.8233 0.0261  -0.1068 0.0396  91  LEU A C   
4    O O   . LEU A 91  ? 1.2046 1.0777 0.9700 0.0345  -0.1089 0.0391  91  LEU A O   
5    C CB  . LEU A 91  ? 1.0386 0.8927 0.7588 0.0420  -0.1253 0.0472  91  LEU A CB  
6    C CG  . LEU A 91  ? 1.0475 0.8988 0.7490 0.0467  -0.1347 0.0499  91  LEU A CG  
7    C CD1 . LEU A 91  ? 1.0163 0.8946 0.7375 0.0571  -0.1431 0.0451  91  LEU A CD1 
8    C CD2 . LEU A 91  ? 1.0733 0.8923 0.7438 0.0535  -0.1416 0.0587  91  LEU A CD2 
9    N N   . GLU A 92  ? 0.9748 0.8472 0.7273 0.0127  -0.0972 0.0398  92  GLU A N   
10   C CA  . GLU A 92  ? 0.9989 0.8752 0.7656 0.0051  -0.0880 0.0382  92  GLU A CA  
11   C C   . GLU A 92  ? 0.9120 0.8154 0.7066 0.0050  -0.0837 0.0300  92  GLU A C   
12   O O   . GLU A 92  ? 0.8602 0.7748 0.6718 0.0135  -0.0877 0.0264  92  GLU A O   
13   C CB  . GLU A 92  ? 1.0530 0.9131 0.8184 0.0103  -0.0904 0.0411  92  GLU A CB  
14   C CG  . GLU A 92  ? 1.1310 0.9978 0.9143 0.0050  -0.0830 0.0384  92  GLU A CG  
15   C CD  . GLU A 92  ? 1.1689 1.0331 0.9473 -0.0103 -0.0743 0.0410  92  GLU A CD  
16   O OE1 . GLU A 92  ? 1.1851 1.0461 0.9484 -0.0178 -0.0721 0.0442  92  GLU A OE1 
17   O OE2 . GLU A 92  ? 1.0747 0.9418 0.8648 -0.0148 -0.0695 0.0399  92  GLU A OE2 
18   N N   . PRO A 93  ? 0.8055 0.7196 0.6045 -0.0041 -0.0755 0.0271  93  PRO A N   
19   C CA  . PRO A 93  ? 0.7577 0.6934 0.5792 -0.0038 -0.0721 0.0193  93  PRO A CA  
20   C C   . PRO A 93  ? 0.6486 0.5913 0.4910 -0.0038 -0.0675 0.0171  93  PRO A C   
21   O O   . PRO A 93  ? 0.6848 0.6196 0.5251 -0.0086 -0.0629 0.0204  93  PRO A O   
22   C CB  . PRO A 93  ? 0.6952 0.6358 0.5099 -0.0120 -0.0646 0.0175  93  PRO A CB  
23   C CG  . PRO A 93  ? 0.7849 0.7113 0.5812 -0.0191 -0.0605 0.0247  93  PRO A CG  
24   C CD  . PRO A 93  ? 0.8381 0.7449 0.6210 -0.0147 -0.0686 0.0310  93  PRO A CD  
25   N N   . ASN A 94  ? 0.5528 0.5106 0.4145 0.0008  -0.0692 0.0115  94  ASN A N   
26   C CA  . ASN A 94  ? 0.5706 0.5355 0.4518 0.0024  -0.0660 0.0094  94  ASN A CA  
27   C C   . ASN A 94  ? 0.5743 0.5555 0.4724 -0.0004 -0.0615 0.0029  94  ASN A C   
28   O O   . ASN A 94  ? 0.6909 0.6791 0.5886 -0.0006 -0.0642 -0.0008 94  ASN A O   
29   C CB  . ASN A 94  ? 0.5432 0.5088 0.4308 0.0123  -0.0731 0.0101  94  ASN A CB  
30   C CG  . ASN A 94  ? 0.7785 0.7537 0.6863 0.0142  -0.0697 0.0072  94  ASN A CG  
31   O OD1 . ASN A 94  ? 0.8026 0.7694 0.7104 0.0129  -0.0660 0.0091  94  ASN A OD1 
32   N ND2 . ASN A 94  ? 0.6632 0.6558 0.5875 0.0162  -0.0710 0.0028  94  ASN A ND2 
33   N N   . LEU A 95  ? 0.5479 0.5332 0.4587 -0.0027 -0.0552 0.0015  95  LEU A N   
34   C CA  . LEU A 95  ? 0.4738 0.4717 0.4005 -0.0041 -0.0512 -0.0042 95  LEU A CA  
35   C C   . LEU A 95  ? 0.5236 0.5249 0.4656 -0.0019 -0.0494 -0.0042 95  LEU A C   
36   O O   . LEU A 95  ? 0.4755 0.4714 0.4167 -0.0040 -0.0455 -0.0015 95  LEU A O   
37   C CB  . LEU A 95  ? 0.3933 0.3928 0.3164 -0.0096 -0.0435 -0.0061 95  LEU A CB  
38   C CG  . LEU A 95  ? 0.4586 0.4670 0.3958 -0.0101 -0.0387 -0.0115 95  LEU A CG  
39   C CD1 . LEU A 95  ? 0.4723 0.4853 0.4147 -0.0086 -0.0438 -0.0163 95  LEU A CD1 
40   C CD2 . LEU A 95  ? 0.4136 0.4235 0.3446 -0.0130 -0.0313 -0.0132 95  LEU A CD2 
41   N N   . THR A 96  ? 0.4496 0.4603 0.4048 0.0017  -0.0524 -0.0070 96  THR A N   
42   C CA  . THR A 96  ? 0.3993 0.4143 0.3686 0.0041  -0.0504 -0.0073 96  THR A CA  
43   C C   . THR A 96  ? 0.3626 0.3861 0.3442 0.0007  -0.0459 -0.0117 96  THR A C   
44   O O   . THR A 96  ? 0.3753 0.4052 0.3600 -0.0009 -0.0482 -0.0151 96  THR A O   
45   C CB  . THR A 96  ? 0.4566 0.4773 0.4318 0.0114  -0.0562 -0.0063 96  THR A CB  
46   O OG1 . THR A 96  ? 0.5140 0.5230 0.4754 0.0163  -0.0605 -0.0020 96  THR A OG1 
47   C CG2 . THR A 96  ? 0.4321 0.4581 0.4211 0.0139  -0.0532 -0.0068 96  THR A CG2 
48   N N   . ILE A 97  ? 0.4392 0.4616 0.4265 -0.0007 -0.0403 -0.0115 97  ILE A N   
49   C CA  . ILE A 97  ? 0.3423 0.3698 0.3394 -0.0028 -0.0359 -0.0151 97  ILE A CA  
50   C C   . ILE A 97  ? 0.4154 0.4463 0.4242 -0.0004 -0.0351 -0.0142 97  ILE A C   
51   O O   . ILE A 97  ? 0.3816 0.4079 0.3890 0.0013  -0.0342 -0.0113 97  ILE A O   
52   C CB  . ILE A 97  ? 0.3561 0.3812 0.3493 -0.0057 -0.0298 -0.0153 97  ILE A CB  
53   C CG1 . ILE A 97  ? 0.4008 0.4231 0.3807 -0.0076 -0.0298 -0.0158 97  ILE A CG1 
54   C CG2 . ILE A 97  ? 0.3757 0.4042 0.3776 -0.0059 -0.0257 -0.0189 97  ILE A CG2 
55   C CD1 . ILE A 97  ? 0.4012 0.4248 0.3774 -0.0097 -0.0231 -0.0155 97  ILE A CD1 
56   N N   . VAL A 98  ? 0.3146 0.3524 0.3332 -0.0009 -0.0354 -0.0167 98  VAL A N   
57   C CA  . VAL A 98  ? 0.4099 0.4518 0.4390 0.0011  -0.0338 -0.0159 98  VAL A CA  
58   C C   . VAL A 98  ? 0.3102 0.3502 0.3435 -0.0015 -0.0288 -0.0177 98  VAL A C   
59   O O   . VAL A 98  ? 0.4043 0.4440 0.4379 -0.0046 -0.0282 -0.0207 98  VAL A O   
60   C CB  . VAL A 98  ? 0.4129 0.4657 0.4505 0.0021  -0.0374 -0.0163 98  VAL A CB  
61   C CG1 . VAL A 98  ? 0.3127 0.3692 0.3515 -0.0037 -0.0393 -0.0196 98  VAL A CG1 
62   C CG2 . VAL A 98  ? 0.3474 0.4052 0.3950 0.0038  -0.0345 -0.0153 98  VAL A CG2 
63   N N   . VAL A 99  ? 0.3110 0.3482 0.3459 0.0000  -0.0258 -0.0158 99  VAL A N   
64   C CA  . VAL A 99  ? 0.3353 0.3716 0.3746 -0.0008 -0.0216 -0.0168 99  VAL A CA  
65   C C   . VAL A 99  ? 0.3636 0.4031 0.4109 0.0003  -0.0213 -0.0160 99  VAL A C   
66   O O   . VAL A 99  ? 0.4202 0.4603 0.4682 0.0034  -0.0220 -0.0138 99  VAL A O   
67   C CB  . VAL A 99  ? 0.3570 0.3905 0.3933 -0.0006 -0.0191 -0.0148 99  VAL A CB  
68   C CG1 . VAL A 99  ? 0.3879 0.4220 0.4290 -0.0002 -0.0154 -0.0157 99  VAL A CG1 
69   C CG2 . VAL A 99  ? 0.4027 0.4353 0.4309 -0.0025 -0.0189 -0.0146 99  VAL A CG2 
70   N N   . VAL A 100 ? 0.3514 0.3915 0.4028 -0.0021 -0.0200 -0.0178 100 VAL A N   
71   C CA  . VAL A 100 ? 0.3573 0.4013 0.4157 -0.0020 -0.0191 -0.0165 100 VAL A CA  
72   C C   . VAL A 100 ? 0.3763 0.4169 0.4348 0.0010  -0.0163 -0.0146 100 VAL A C   
73   O O   . VAL A 100 ? 0.3654 0.4013 0.4206 0.0016  -0.0149 -0.0146 100 VAL A O   
74   C CB  . VAL A 100 ? 0.3836 0.4261 0.4441 -0.0069 -0.0184 -0.0182 100 VAL A CB  
75   C CG1 . VAL A 100 ? 0.3863 0.4316 0.4453 -0.0112 -0.0222 -0.0204 100 VAL A CG1 
76   C CG2 . VAL A 100 ? 0.3691 0.4011 0.4250 -0.0065 -0.0156 -0.0196 100 VAL A CG2 
77   N N   . SER A 101 ? 0.4611 0.5055 0.5234 0.0030  -0.0157 -0.0128 101 SER A N   
78   C CA  . SER A 101 ? 0.4241 0.4644 0.4843 0.0061  -0.0142 -0.0110 101 SER A CA  
79   C C   . SER A 101 ? 0.3899 0.4249 0.4494 0.0049  -0.0120 -0.0111 101 SER A C   
80   O O   . SER A 101 ? 0.4212 0.4530 0.4775 0.0060  -0.0121 -0.0102 101 SER A O   
81   C CB  . SER A 101 ? 0.4294 0.4748 0.4929 0.0087  -0.0129 -0.0095 101 SER A CB  
82   O OG  . SER A 101 ? 0.5162 0.5705 0.5828 0.0105  -0.0147 -0.0096 101 SER A OG  
83   N N   . GLU A 102 ? 0.4135 0.4472 0.4751 0.0025  -0.0105 -0.0119 102 GLU A N   
84   C CA  . GLU A 102 ? 0.4150 0.4426 0.4749 0.0033  -0.0088 -0.0118 102 GLU A CA  
85   C C   . GLU A 102 ? 0.4193 0.4458 0.4766 0.0048  -0.0089 -0.0130 102 GLU A C   
86   O O   . GLU A 102 ? 0.4256 0.4508 0.4825 0.0073  -0.0078 -0.0123 102 GLU A O   
87   C CB  . GLU A 102 ? 0.3598 0.3822 0.4194 0.0002  -0.0077 -0.0124 102 GLU A CB  
88   C CG  . GLU A 102 ? 0.5704 0.5950 0.6327 -0.0022 -0.0064 -0.0101 102 GLU A CG  
89   C CD  . GLU A 102 ? 0.5079 0.5418 0.5750 -0.0062 -0.0074 -0.0103 102 GLU A CD  
90   O OE1 . GLU A 102 ? 0.4504 0.4898 0.5187 -0.0051 -0.0097 -0.0117 102 GLU A OE1 
91   O OE2 . GLU A 102 ? 0.6195 0.6562 0.6891 -0.0107 -0.0062 -0.0088 102 GLU A OE2 
92   N N   . LEU A 103 ? 0.3811 0.4098 0.4367 0.0036  -0.0100 -0.0146 103 LEU A N   
93   C CA  . LEU A 103 ? 0.3870 0.4170 0.4400 0.0048  -0.0091 -0.0157 103 LEU A CA  
94   C C   . LEU A 103 ? 0.3466 0.3811 0.3986 0.0041  -0.0101 -0.0136 103 LEU A C   
95   O O   . LEU A 103 ? 0.3480 0.3862 0.3981 0.0038  -0.0090 -0.0138 103 LEU A O   
96   C CB  . LEU A 103 ? 0.3565 0.3843 0.4055 0.0034  -0.0095 -0.0188 103 LEU A CB  
97   C CG  . LEU A 103 ? 0.4252 0.4449 0.4720 0.0025  -0.0092 -0.0213 103 LEU A CG  
98   C CD1 . LEU A 103 ? 0.4210 0.4367 0.4611 0.0010  -0.0101 -0.0250 103 LEU A CD1 
99   C CD2 . LEU A 103 ? 0.3769 0.3911 0.4228 0.0066  -0.0067 -0.0212 103 LEU A CD2 
100  N N   . LEU A 104 ? 0.4075 0.4410 0.4593 0.0036  -0.0120 -0.0115 104 LEU A N   
101  C CA  . LEU A 104 ? 0.4163 0.4495 0.4636 0.0018  -0.0138 -0.0095 104 LEU A CA  
102  C C   . LEU A 104 ? 0.4390 0.4766 0.4872 0.0002  -0.0129 -0.0079 104 LEU A C   
103  O O   . LEU A 104 ? 0.3927 0.4331 0.4378 -0.0032 -0.0133 -0.0066 104 LEU A O   
104  C CB  . LEU A 104 ? 0.4995 0.5275 0.5441 0.0030  -0.0160 -0.0082 104 LEU A CB  
105  C CG  . LEU A 104 ? 0.5799 0.6021 0.6162 0.0022  -0.0190 -0.0068 104 LEU A CG  
106  C CD1 . LEU A 104 ? 0.6167 0.6406 0.6516 0.0022  -0.0199 -0.0079 104 LEU A CD1 
107  C CD2 . LEU A 104 ? 0.6465 0.6622 0.6788 0.0060  -0.0208 -0.0062 104 LEU A CD2 
108  N N   . HIS A 105 ? 0.3561 0.3955 0.4084 0.0023  -0.0120 -0.0076 105 HIS A N   
109  C CA  . HIS A 105 ? 0.4114 0.4580 0.4661 0.0014  -0.0120 -0.0058 105 HIS A CA  
110  C C   . HIS A 105 ? 0.4163 0.4709 0.4756 0.0051  -0.0088 -0.0071 105 HIS A C   
111  O O   . HIS A 105 ? 0.5139 0.5750 0.5773 0.0077  -0.0086 -0.0060 105 HIS A O   
112  C CB  . HIS A 105 ? 0.3109 0.3543 0.3655 0.0020  -0.0139 -0.0043 105 HIS A CB  
113  C CG  . HIS A 105 ? 0.3504 0.3849 0.3980 -0.0005 -0.0169 -0.0033 105 HIS A CG  
114  N ND1 . HIS A 105 ? 0.4590 0.4920 0.5015 -0.0055 -0.0201 -0.0012 105 HIS A ND1 
115  C CD2 . HIS A 105 ? 0.4407 0.4670 0.4845 0.0017  -0.0172 -0.0042 105 HIS A CD2 
116  C CE1 . HIS A 105 ? 0.4335 0.4543 0.4674 -0.0055 -0.0224 -0.0013 105 HIS A CE1 
117  N NE2 . HIS A 105 ? 0.4491 0.4673 0.4844 -0.0003 -0.0204 -0.0030 105 HIS A NE2 
118  N N   . THR A 106 ? 0.3764 0.4299 0.4340 0.0064  -0.0068 -0.0096 106 THR A N   
119  C CA  . THR A 106 ? 0.4891 0.5491 0.5477 0.0104  -0.0034 -0.0114 106 THR A CA  
120  C C   . THR A 106 ? 0.5517 0.6198 0.6081 0.0067  -0.0021 -0.0106 106 THR A C   
121  O O   . THR A 106 ? 0.5793 0.6454 0.6325 0.0008  -0.0044 -0.0086 106 THR A O   
122  C CB  . THR A 106 ? 0.4685 0.5181 0.5232 0.0141  -0.0022 -0.0152 106 THR A CB  
123  O OG1 . THR A 106 ? 0.4964 0.5412 0.5466 0.0102  -0.0033 -0.0166 106 THR A OG1 
124  C CG2 . THR A 106 ? 0.4001 0.4403 0.4555 0.0154  -0.0036 -0.0150 106 THR A CG2 
125  N N   . ASN A 107 ? 0.5425 0.6189 0.5992 0.0108  0.0017  -0.0121 107 ASN A N   
126  C CA  . ASN A 107 ? 0.5326 0.6194 0.5871 0.0072  0.0041  -0.0109 107 ASN A CA  
127  C C   . ASN A 107 ? 0.5629 0.6402 0.6083 0.0071  0.0047  -0.0140 107 ASN A C   
128  O O   . ASN A 107 ? 0.6617 0.7366 0.7033 0.0129  0.0075  -0.0179 107 ASN A O   
129  C CB  . ASN A 107 ? 0.6826 0.7872 0.7425 0.0124  0.0086  -0.0105 107 ASN A CB  
130  C CG  . ASN A 107 ? 0.6913 0.8106 0.7501 0.0071  0.0117  -0.0080 107 ASN A CG  
131  O OD1 . ASN A 107 ? 0.7312 0.8461 0.7818 0.0063  0.0137  -0.0098 107 ASN A OD1 
132  N ND2 . ASN A 107 ? 0.7114 0.8485 0.7779 0.0025  0.0118  -0.0036 107 ASN A ND2 
133  N N   . TRP A 108 ? 0.5246 0.5953 0.5652 0.0008  0.0015  -0.0124 108 TRP A N   
134  C CA  . TRP A 108 ? 0.5307 0.5944 0.5623 -0.0004 0.0010  -0.0144 108 TRP A CA  
135  C C   . TRP A 108 ? 0.3937 0.4626 0.4192 -0.0060 0.0020  -0.0112 108 TRP A C   
136  O O   . TRP A 108 ? 0.5801 0.6434 0.5965 -0.0071 0.0013  -0.0123 108 TRP A O   
137  C CB  . TRP A 108 ? 0.5566 0.6081 0.5865 -0.0017 -0.0040 -0.0151 108 TRP A CB  
138  C CG  . TRP A 108 ? 0.4832 0.5325 0.5157 -0.0049 -0.0072 -0.0114 108 TRP A CG  
139  C CD1 . TRP A 108 ? 0.4789 0.5262 0.5174 -0.0033 -0.0085 -0.0110 108 TRP A CD1 
140  C CD2 . TRP A 108 ? 0.4078 0.4538 0.4340 -0.0098 -0.0098 -0.0078 108 TRP A CD2 
141  N NE1 . TRP A 108 ? 0.3789 0.4222 0.4152 -0.0064 -0.0116 -0.0079 108 TRP A NE1 
142  C CE2 . TRP A 108 ? 0.4452 0.4865 0.4735 -0.0104 -0.0127 -0.0059 108 TRP A CE2 
143  C CE3 . TRP A 108 ? 0.5013 0.5461 0.5184 -0.0137 -0.0101 -0.0059 108 TRP A CE3 
144  C CZ2 . TRP A 108 ? 0.4025 0.4359 0.4232 -0.0144 -0.0160 -0.0027 108 TRP A CZ2 
145  C CZ3 . TRP A 108 ? 0.5088 0.5458 0.5186 -0.0183 -0.0135 -0.0020 108 TRP A CZ3 
146  C CH2 . TRP A 108 ? 0.5462 0.5766 0.5574 -0.0184 -0.0166 -0.0006 108 TRP A CH2 
147  N N   . THR A 109 ? 0.4830 0.5624 0.5123 -0.0104 0.0031  -0.0070 109 THR A N   
148  C CA  . THR A 109 ? 0.5010 0.5827 0.5233 -0.0184 0.0031  -0.0027 109 THR A CA  
149  C C   . THR A 109 ? 0.5020 0.5953 0.5201 -0.0182 0.0090  -0.0029 109 THR A C   
150  O O   . THR A 109 ? 0.5213 0.6132 0.5300 -0.0246 0.0092  0.0003  109 THR A O   
151  C CB  . THR A 109 ? 0.5056 0.5934 0.5327 -0.0253 0.0014  0.0022  109 THR A CB  
152  O OG1 . THR A 109 ? 0.6518 0.7294 0.6682 -0.0340 -0.0020 0.0063  109 THR A OG1 
153  C CG2 . THR A 109 ? 0.5068 0.6175 0.5427 -0.0261 0.0065  0.0039  109 THR A CG2 
154  N N   . ASP A 110 ? 0.4266 0.5299 0.4496 -0.0103 0.0139  -0.0065 110 ASP A N   
155  C CA  . ASP A 110 ? 0.5420 0.6562 0.5595 -0.0081 0.0203  -0.0074 110 ASP A CA  
156  C C   . ASP A 110 ? 0.4733 0.5730 0.4764 -0.0077 0.0192  -0.0103 110 ASP A C   
157  O O   . ASP A 110 ? 0.4914 0.5962 0.4854 -0.0104 0.0229  -0.0089 110 ASP A O   
158  C CB  . ASP A 110 ? 0.6019 0.7270 0.6257 0.0029  0.0255  -0.0114 110 ASP A CB  
159  C CG  . ASP A 110 ? 0.6932 0.8384 0.7313 0.0030  0.0273  -0.0078 110 ASP A CG  
160  O OD1 . ASP A 110 ? 0.7746 0.9319 0.8163 -0.0069 0.0270  -0.0020 110 ASP A OD1 
161  O OD2 . ASP A 110 ? 0.7419 0.8905 0.7868 0.0126  0.0284  -0.0106 110 ASP A OD2 
162  N N   . TYR A 111 ? 0.4445 0.5274 0.4452 -0.0049 0.0141  -0.0140 111 TYR A N   
163  C CA  . TYR A 111 ? 0.4489 0.5192 0.4366 -0.0050 0.0117  -0.0168 111 TYR A CA  
164  C C   . TYR A 111 ? 0.4754 0.5404 0.4552 -0.0129 0.0079  -0.0118 111 TYR A C   
165  O O   . TYR A 111 ? 0.4532 0.5135 0.4201 -0.0142 0.0077  -0.0121 111 TYR A O   
166  C CB  . TYR A 111 ? 0.4616 0.5185 0.4506 -0.0014 0.0067  -0.0214 111 TYR A CB  
167  C CG  . TYR A 111 ? 0.5447 0.6022 0.5394 0.0059  0.0096  -0.0256 111 TYR A CG  
168  C CD1 . TYR A 111 ? 0.5909 0.6502 0.5788 0.0124  0.0149  -0.0297 111 TYR A CD1 
169  C CD2 . TYR A 111 ? 0.6177 0.6724 0.6228 0.0070  0.0071  -0.0254 111 TYR A CD2 
170  C CE1 . TYR A 111 ? 0.6212 0.6778 0.6118 0.0203  0.0172  -0.0335 111 TYR A CE1 
171  C CE2 . TYR A 111 ? 0.6439 0.6965 0.6520 0.0138  0.0093  -0.0287 111 TYR A CE2 
172  C CZ  . TYR A 111 ? 0.6579 0.7105 0.6584 0.0207  0.0141  -0.0328 111 TYR A CZ  
173  O OH  . TYR A 111 ? 0.8027 0.8501 0.8039 0.0287  0.0159  -0.0360 111 TYR A OH  
174  N N   . VAL A 112 ? 0.3920 0.4556 0.3773 -0.0177 0.0045  -0.0073 112 VAL A N   
175  C CA  . VAL A 112 ? 0.3911 0.4461 0.3666 -0.0246 0.0005  -0.0023 112 VAL A CA  
176  C C   . VAL A 112 ? 0.4369 0.5008 0.4049 -0.0312 0.0054  0.0022  112 VAL A C   
177  O O   . VAL A 112 ? 0.4770 0.5335 0.4308 -0.0348 0.0043  0.0046  112 VAL A O   
178  C CB  . VAL A 112 ? 0.5302 0.5785 0.5110 -0.0272 -0.0043 0.0006  112 VAL A CB  
179  C CG1 . VAL A 112 ? 0.4289 0.4645 0.3966 -0.0334 -0.0086 0.0058  112 VAL A CG1 
180  C CG2 . VAL A 112 ? 0.4843 0.5257 0.4718 -0.0208 -0.0083 -0.0034 112 VAL A CG2 
181  N N   . CYS A 113 ? 0.4501 0.5313 0.4277 -0.0330 0.0109  0.0039  113 CYS A N   
182  C CA  . CYS A 113 ? 0.3608 0.4555 0.3335 -0.0402 0.0165  0.0087  113 CYS A CA  
183  C C   . CYS A 113 ? 0.4802 0.5784 0.4425 -0.0359 0.0218  0.0058  113 CYS A C   
184  O O   . CYS A 113 ? 0.4988 0.5984 0.4490 -0.0425 0.0243  0.0100  113 CYS A O   
185  C CB  . CYS A 113 ? 0.4422 0.5596 0.4300 -0.0417 0.0212  0.0106  113 CYS A CB  
186  S SG  . CYS A 113 ? 0.5454 0.6589 0.5422 -0.0491 0.0148  0.0146  113 CYS A SG  
187  N N   . LEU A 114 ? 0.4003 0.4983 0.3654 -0.0253 0.0234  -0.0013 114 LEU A N   
188  C CA  . LEU A 114 ? 0.4169 0.5142 0.3692 -0.0204 0.0276  -0.0052 114 LEU A CA  
189  C C   . LEU A 114 ? 0.4906 0.5697 0.4261 -0.0242 0.0219  -0.0043 114 LEU A C   
190  O O   . LEU A 114 ? 0.4977 0.5779 0.4188 -0.0266 0.0253  -0.0027 114 LEU A O   
191  C CB  . LEU A 114 ? 0.4463 0.5403 0.4021 -0.0089 0.0285  -0.0133 114 LEU A CB  
192  C CG  . LEU A 114 ? 0.5612 0.6496 0.5013 -0.0028 0.0317  -0.0190 114 LEU A CG  
193  C CD1 . LEU A 114 ? 0.5201 0.6277 0.4560 -0.0012 0.0418  -0.0174 114 LEU A CD1 
194  C CD2 . LEU A 114 ? 0.4704 0.5487 0.4118 0.0068  0.0303  -0.0269 114 LEU A CD2 
195  N N   . LEU A 115 ? 0.4525 0.5162 0.3895 -0.0242 0.0134  -0.0050 115 LEU A N   
196  C CA  . LEU A 115 ? 0.4526 0.5005 0.3750 -0.0262 0.0069  -0.0040 115 LEU A CA  
197  C C   . LEU A 115 ? 0.5321 0.5765 0.4439 -0.0353 0.0062  0.0040  115 LEU A C   
198  O O   . LEU A 115 ? 0.5338 0.5703 0.4285 -0.0374 0.0049  0.0059  115 LEU A O   
199  C CB  . LEU A 115 ? 0.4650 0.5015 0.3940 -0.0232 -0.0015 -0.0062 115 LEU A CB  
200  C CG  . LEU A 115 ? 0.4743 0.5087 0.4075 -0.0165 -0.0029 -0.0138 115 LEU A CG  
201  C CD1 . LEU A 115 ? 0.5092 0.5363 0.4502 -0.0151 -0.0107 -0.0146 115 LEU A CD1 
202  C CD2 . LEU A 115 ? 0.5125 0.5420 0.4297 -0.0148 -0.0030 -0.0174 115 LEU A CD2 
203  N N   . GLU A 116 ? 0.4509 0.4993 0.3709 -0.0412 0.0066  0.0089  116 GLU A N   
204  C CA  . GLU A 116 ? 0.4639 0.5049 0.3719 -0.0513 0.0050  0.0169  116 GLU A CA  
205  C C   . GLU A 116 ? 0.5632 0.6157 0.4612 -0.0574 0.0128  0.0205  116 GLU A C   
206  O O   . GLU A 116 ? 0.5962 0.6378 0.4759 -0.0635 0.0113  0.0256  116 GLU A O   
207  C CB  . GLU A 116 ? 0.5587 0.6005 0.4767 -0.0572 0.0033  0.0207  116 GLU A CB  
208  C CG  . GLU A 116 ? 0.5698 0.5962 0.4727 -0.0680 -0.0007 0.0286  116 GLU A CG  
209  C CD  . GLU A 116 ? 0.6265 0.6660 0.5244 -0.0800 0.0060  0.0349  116 GLU A CD  
210  O OE1 . GLU A 116 ? 0.6042 0.6687 0.5151 -0.0795 0.0138  0.0334  116 GLU A OE1 
211  O OE2 . GLU A 116 ? 0.7368 0.7619 0.6173 -0.0898 0.0034  0.0418  116 GLU A OE2 
212  N N   . SER A 117 ? 0.5414 0.6166 0.4504 -0.0554 0.0214  0.0184  117 SER A N   
213  C CA  . SER A 117 ? 0.6275 0.7184 0.5287 -0.0604 0.0302  0.0219  117 SER A CA  
214  C C   . SER A 117 ? 0.5242 0.6073 0.4072 -0.0556 0.0316  0.0188  117 SER A C   
215  O O   . SER A 117 ? 0.6754 0.7627 0.5440 -0.0618 0.0366  0.0235  117 SER A O   
216  C CB  . SER A 117 ? 0.5155 0.6346 0.4341 -0.0564 0.0391  0.0197  117 SER A CB  
217  O OG  . SER A 117 ? 0.6330 0.7526 0.5562 -0.0425 0.0405  0.0108  117 SER A OG  
218  N N   . ARG A 118 ? 0.5217 0.5937 0.4040 -0.0454 0.0271  0.0113  118 ARG A N   
219  C CA  . ARG A 118 ? 0.5793 0.6422 0.4434 -0.0408 0.0268  0.0074  118 ARG A CA  
220  C C   . ARG A 118 ? 0.6596 0.7004 0.5079 -0.0443 0.0172  0.0106  118 ARG A C   
221  O O   . ARG A 118 ? 0.6521 0.6863 0.4805 -0.0453 0.0175  0.0117  118 ARG A O   
222  C CB  . ARG A 118 ? 0.6102 0.6716 0.4803 -0.0293 0.0261  -0.0024 118 ARG A CB  
223  C CG  . ARG A 118 ? 0.7595 0.8090 0.6107 -0.0245 0.0240  -0.0078 118 ARG A CG  
224  C CD  . ARG A 118 ? 0.8395 0.8989 0.6762 -0.0228 0.0340  -0.0087 118 ARG A CD  
225  N NE  . ARG A 118 ? 0.8896 0.9348 0.7067 -0.0182 0.0307  -0.0146 118 ARG A NE  
226  C CZ  . ARG A 118 ? 0.8990 0.9295 0.6993 -0.0223 0.0233  -0.0121 118 ARG A CZ  
227  N NH1 . ARG A 118 ? 0.9324 0.9591 0.7300 -0.0306 0.0198  -0.0034 118 ARG A NH1 
228  N NH2 . ARG A 118 ? 1.0451 1.0630 0.8294 -0.0179 0.0188  -0.0184 118 ARG A NH2 
229  N N   . PHE A 119 ? 0.6400 0.6694 0.4956 -0.0452 0.0088  0.0123  119 PHE A N   
230  C CA  . PHE A 119 ? 0.5822 0.5913 0.4242 -0.0460 -0.0010 0.0153  119 PHE A CA  
231  C C   . PHE A 119 ? 0.6272 0.6276 0.4687 -0.0536 -0.0041 0.0230  119 PHE A C   
232  O O   . PHE A 119 ? 0.6329 0.6258 0.4840 -0.0509 -0.0104 0.0225  119 PHE A O   
233  C CB  . PHE A 119 ? 0.6310 0.6335 0.4809 -0.0375 -0.0090 0.0088  119 PHE A CB  
234  C CG  . PHE A 119 ? 0.6064 0.6131 0.4539 -0.0313 -0.0073 0.0009  119 PHE A CG  
235  C CD1 . PHE A 119 ? 0.6284 0.6266 0.4565 -0.0304 -0.0108 0.0000  119 PHE A CD1 
236  C CD2 . PHE A 119 ? 0.5964 0.6131 0.4589 -0.0265 -0.0030 -0.0056 119 PHE A CD2 
237  C CE1 . PHE A 119 ? 0.6019 0.6011 0.4250 -0.0255 -0.0101 -0.0077 119 PHE A CE1 
238  C CE2 . PHE A 119 ? 0.6238 0.6398 0.4808 -0.0212 -0.0021 -0.0130 119 PHE A CE2 
239  C CZ  . PHE A 119 ? 0.5833 0.5904 0.4204 -0.0210 -0.0057 -0.0143 119 PHE A CZ  
240  N N   . PRO A 120 ? 0.6872 0.6876 0.5165 -0.0637 0.0001  0.0304  120 PRO A N   
241  C CA  . PRO A 120 ? 0.6525 0.6445 0.4813 -0.0729 -0.0022 0.0376  120 PRO A CA  
242  C C   . PRO A 120 ? 0.6899 0.6546 0.5054 -0.0713 -0.0131 0.0407  120 PRO A C   
243  O O   . PRO A 120 ? 0.8189 0.7730 0.6357 -0.0756 -0.0168 0.0443  120 PRO A O   
244  C CB  . PRO A 120 ? 0.7193 0.7184 0.5357 -0.0856 0.0052  0.0451  120 PRO A CB  
245  C CG  . PRO A 120 ? 0.7184 0.7242 0.5235 -0.0817 0.0101  0.0426  120 PRO A CG  
246  C CD  . PRO A 120 ? 0.6418 0.6476 0.4543 -0.0679 0.0068  0.0330  120 PRO A CD  
247  N N   . ASP A 121 ? 0.7295 0.6823 0.5317 -0.0645 -0.0188 0.0393  121 ASP A N   
248  C CA  . ASP A 121 ? 0.7380 0.6669 0.5280 -0.0603 -0.0294 0.0421  121 ASP A CA  
249  C C   . ASP A 121 ? 0.6709 0.6013 0.4769 -0.0482 -0.0357 0.0354  121 ASP A C   
250  O O   . ASP A 121 ? 0.7500 0.6642 0.5481 -0.0418 -0.0445 0.0368  121 ASP A O   
251  C CB  . ASP A 121 ? 0.7407 0.6561 0.5056 -0.0597 -0.0332 0.0455  121 ASP A CB  
252  C CG  . ASP A 121 ? 0.9394 0.8527 0.6863 -0.0724 -0.0267 0.0529  121 ASP A CG  
253  O OD1 . ASP A 121 ? 0.9185 0.8263 0.6631 -0.0828 -0.0246 0.0590  121 ASP A OD1 
254  O OD2 . ASP A 121 ? 1.0221 0.9397 0.7565 -0.0728 -0.0235 0.0528  121 ASP A OD2 
255  N N   . LEU A 122 ? 0.6276 0.5772 0.4553 -0.0447 -0.0313 0.0286  122 LEU A N   
256  C CA  . LEU A 122 ? 0.5472 0.5006 0.3902 -0.0348 -0.0364 0.0224  122 LEU A CA  
257  C C   . LEU A 122 ? 0.4892 0.4381 0.3435 -0.0334 -0.0386 0.0233  122 LEU A C   
258  O O   . LEU A 122 ? 0.5647 0.5196 0.4277 -0.0392 -0.0333 0.0242  122 LEU A O   
259  C CB  . LEU A 122 ? 0.5125 0.4847 0.3708 -0.0323 -0.0308 0.0151  122 LEU A CB  
260  C CG  . LEU A 122 ? 0.5601 0.5378 0.4339 -0.0243 -0.0353 0.0087  122 LEU A CG  
261  C CD1 . LEU A 122 ? 0.5478 0.5204 0.4123 -0.0192 -0.0434 0.0073  122 LEU A CD1 
262  C CD2 . LEU A 122 ? 0.5354 0.5277 0.4231 -0.0236 -0.0287 0.0025  122 LEU A CD2 
263  N N   . GLN A 123 ? 0.5496 0.4891 0.4037 -0.0251 -0.0466 0.0228  123 GLN A N   
264  C CA  . GLN A 123 ? 0.5287 0.4659 0.3945 -0.0214 -0.0483 0.0220  123 GLN A CA  
265  C C   . GLN A 123 ? 0.5371 0.4935 0.4261 -0.0175 -0.0454 0.0152  123 GLN A C   
266  O O   . GLN A 123 ? 0.5223 0.4869 0.4167 -0.0122 -0.0479 0.0111  123 GLN A O   
267  C CB  . GLN A 123 ? 0.4943 0.4160 0.3512 -0.0123 -0.0571 0.0239  123 GLN A CB  
268  C CG  . GLN A 123 ? 0.5764 0.4957 0.4441 -0.0073 -0.0582 0.0225  123 GLN A CG  
269  C CD  . GLN A 123 ? 0.5584 0.4644 0.4180 0.0042  -0.0662 0.0239  123 GLN A CD  
270  O OE1 . GLN A 123 ? 0.6194 0.5356 0.4859 0.0132  -0.0702 0.0213  123 GLN A OE1 
271  N NE2 . GLN A 123 ? 0.5869 0.4700 0.4313 0.0042  -0.0686 0.0279  123 GLN A NE2 
272  N N   . ILE A 124 ? 0.4196 0.3823 0.3210 -0.0207 -0.0405 0.0143  124 ILE A N   
273  C CA  . ILE A 124 ? 0.4564 0.4348 0.3778 -0.0178 -0.0372 0.0086  124 ILE A CA  
274  C C   . ILE A 124 ? 0.4201 0.3952 0.3504 -0.0138 -0.0394 0.0084  124 ILE A C   
275  O O   . ILE A 124 ? 0.4945 0.4638 0.4234 -0.0181 -0.0379 0.0111  124 ILE A O   
276  C CB  . ILE A 124 ? 0.4057 0.3963 0.3338 -0.0238 -0.0292 0.0075  124 ILE A CB  
277  C CG1 . ILE A 124 ? 0.4374 0.4320 0.3557 -0.0261 -0.0262 0.0069  124 ILE A CG1 
278  C CG2 . ILE A 124 ? 0.4663 0.4690 0.4130 -0.0200 -0.0265 0.0022  124 ILE A CG2 
279  C CD1 . ILE A 124 ? 0.4163 0.4230 0.3376 -0.0315 -0.0178 0.0073  124 ILE A CD1 
280  N N   . ASN A 125 ? 0.4715 0.4508 0.4104 -0.0061 -0.0430 0.0053  125 ASN A N   
281  C CA  . ASN A 125 ? 0.3774 0.3555 0.3246 -0.0009 -0.0444 0.0047  125 ASN A CA  
282  C C   . ASN A 125 ? 0.4733 0.4662 0.4390 -0.0007 -0.0403 0.0004  125 ASN A C   
283  O O   . ASN A 125 ? 0.4632 0.4665 0.4364 0.0006  -0.0404 -0.0031 125 ASN A O   
284  C CB  . ASN A 125 ? 0.4121 0.3865 0.3561 0.0084  -0.0510 0.0051  125 ASN A CB  
285  C CG  . ASN A 125 ? 0.5712 0.5290 0.4946 0.0095  -0.0559 0.0096  125 ASN A CG  
286  O OD1 . ASN A 125 ? 0.5470 0.4882 0.4570 0.0057  -0.0559 0.0134  125 ASN A OD1 
287  N ND2 . ASN A 125 ? 0.5675 0.5289 0.4873 0.0141  -0.0607 0.0093  125 ASN A ND2 
288  N N   . ILE A 126 ? 0.4389 0.4313 0.4103 -0.0024 -0.0372 0.0007  126 ILE A N   
289  C CA  . ILE A 126 ? 0.4305 0.4341 0.4173 -0.0021 -0.0334 -0.0026 126 ILE A CA  
290  C C   . ILE A 126 ? 0.4458 0.4484 0.4382 0.0039  -0.0353 -0.0030 126 ILE A C   
291  O O   . ILE A 126 ? 0.4948 0.4875 0.4816 0.0046  -0.0361 -0.0009 126 ILE A O   
292  C CB  . ILE A 126 ? 0.4780 0.4842 0.4674 -0.0079 -0.0286 -0.0019 126 ILE A CB  
293  C CG1 . ILE A 126 ? 0.4797 0.4884 0.4623 -0.0133 -0.0260 -0.0009 126 ILE A CG1 
294  C CG2 . ILE A 126 ? 0.4766 0.4928 0.4801 -0.0064 -0.0251 -0.0052 126 ILE A CG2 
295  C CD1 . ILE A 126 ? 0.4418 0.4590 0.4282 -0.0117 -0.0239 -0.0049 126 ILE A CD1 
296  N N   . VAL A 127 ? 0.4209 0.4335 0.4231 0.0079  -0.0361 -0.0056 127 VAL A N   
297  C CA  . VAL A 127 ? 0.4884 0.5043 0.4976 0.0137  -0.0366 -0.0059 127 VAL A CA  
298  C C   . VAL A 127 ? 0.4469 0.4726 0.4693 0.0114  -0.0325 -0.0083 127 VAL A C   
299  O O   . VAL A 127 ? 0.3732 0.4025 0.3988 0.0067  -0.0302 -0.0101 127 VAL A O   
300  C CB  . VAL A 127 ? 0.4202 0.4422 0.4306 0.0204  -0.0411 -0.0059 127 VAL A CB  
301  C CG1 . VAL A 127 ? 0.4400 0.4488 0.4348 0.0243  -0.0457 -0.0030 127 VAL A CG1 
302  C CG2 . VAL A 127 ? 0.3827 0.4172 0.4003 0.0170  -0.0421 -0.0082 127 VAL A CG2 
303  N N   . SER A 128 ? 0.4132 0.4419 0.4415 0.0154  -0.0315 -0.0083 128 SER A N   
304  C CA  . SER A 128 ? 0.3833 0.4195 0.4222 0.0134  -0.0278 -0.0097 128 SER A CA  
305  C C   . SER A 128 ? 0.4006 0.4481 0.4479 0.0176  -0.0282 -0.0098 128 SER A C   
306  O O   . SER A 128 ? 0.4048 0.4532 0.4495 0.0244  -0.0304 -0.0087 128 SER A O   
307  C CB  . SER A 128 ? 0.4881 0.5175 0.5255 0.0127  -0.0250 -0.0089 128 SER A CB  
308  O OG  . SER A 128 ? 0.7317 0.7534 0.7621 0.0178  -0.0264 -0.0074 128 SER A OG  
309  N N   . ALA A 129 ? 0.3617 0.4178 0.4184 0.0135  -0.0260 -0.0110 129 ALA A N   
310  C CA  . ALA A 129 ? 0.3756 0.4463 0.4419 0.0149  -0.0259 -0.0107 129 ALA A CA  
311  C C   . ALA A 129 ? 0.3248 0.3988 0.3980 0.0085  -0.0225 -0.0113 129 ALA A C   
312  O O   . ALA A 129 ? 0.3535 0.4182 0.4234 0.0040  -0.0212 -0.0126 129 ALA A O   
313  C CB  . ALA A 129 ? 0.3206 0.4017 0.3895 0.0147  -0.0307 -0.0111 129 ALA A CB  
314  N N   . PRO A 130 ? 0.4411 0.5277 0.5229 0.0082  -0.0208 -0.0101 130 PRO A N   
315  C CA  . PRO A 130 ? 0.4758 0.5642 0.5625 0.0002  -0.0184 -0.0102 130 PRO A CA  
316  C C   . PRO A 130 ? 0.3892 0.4780 0.4763 -0.0077 -0.0218 -0.0122 130 PRO A C   
317  O O   . PRO A 130 ? 0.5029 0.5973 0.5898 -0.0071 -0.0261 -0.0131 130 PRO A O   
318  C CB  . PRO A 130 ? 0.4631 0.5684 0.5590 0.0013  -0.0160 -0.0078 130 PRO A CB  
319  C CG  . PRO A 130 ? 0.4697 0.5775 0.5632 0.0124  -0.0158 -0.0069 130 PRO A CG  
320  C CD  . PRO A 130 ? 0.4434 0.5422 0.5293 0.0159  -0.0204 -0.0083 130 PRO A CD  
321  N N   . GLN A 131 ? 0.3920 0.4727 0.4776 -0.0148 -0.0200 -0.0130 131 GLN A N   
322  C CA  . GLN A 131 ? 0.4619 0.5384 0.5446 -0.0230 -0.0232 -0.0155 131 GLN A CA  
323  C C   . GLN A 131 ? 0.4997 0.5937 0.5897 -0.0273 -0.0277 -0.0152 131 GLN A C   
324  O O   . GLN A 131 ? 0.5349 0.6279 0.6209 -0.0292 -0.0324 -0.0175 131 GLN A O   
325  C CB  . GLN A 131 ? 0.5592 0.6251 0.6393 -0.0298 -0.0206 -0.0153 131 GLN A CB  
326  C CG  . GLN A 131 ? 0.5417 0.5882 0.6122 -0.0263 -0.0181 -0.0169 131 GLN A CG  
327  C CD  . GLN A 131 ? 0.6693 0.7030 0.7302 -0.0284 -0.0205 -0.0210 131 GLN A CD  
328  O OE1 . GLN A 131 ? 0.5641 0.5846 0.6174 -0.0243 -0.0185 -0.0226 131 GLN A OE1 
329  N NE2 . GLN A 131 ? 0.6932 0.7318 0.7540 -0.0344 -0.0250 -0.0227 131 GLN A NE2 
330  N N   . GLU A 132 ? 0.5137 0.6254 0.6145 -0.0287 -0.0264 -0.0122 132 GLU A N   
331  C CA  . GLU A 132 ? 0.5327 0.6660 0.6431 -0.0335 -0.0308 -0.0113 132 GLU A CA  
332  C C   . GLU A 132 ? 0.4952 0.6377 0.6063 -0.0245 -0.0351 -0.0117 132 GLU A C   
333  O O   . GLU A 132 ? 0.4963 0.6478 0.6090 -0.0285 -0.0412 -0.0127 132 GLU A O   
334  C CB  . GLU A 132 ? 0.5773 0.7311 0.7001 -0.0355 -0.0271 -0.0074 132 GLU A CB  
335  C CG  . GLU A 132 ? 0.7216 0.8638 0.8414 -0.0408 -0.0214 -0.0058 132 GLU A CG  
336  C CD  . GLU A 132 ? 0.7673 0.8972 0.8813 -0.0301 -0.0164 -0.0054 132 GLU A CD  
337  O OE1 . GLU A 132 ? 0.8446 0.9869 0.9641 -0.0240 -0.0124 -0.0028 132 GLU A OE1 
338  O OE2 . GLU A 132 ? 0.7252 0.8338 0.8287 -0.0277 -0.0165 -0.0077 132 GLU A OE2 
339  N N   . ASP A 133 ? 0.4806 0.6195 0.5889 -0.0127 -0.0327 -0.0108 133 ASP A N   
340  C CA  . ASP A 133 ? 0.4797 0.6235 0.5859 -0.0037 -0.0370 -0.0107 133 ASP A CA  
341  C C   . ASP A 133 ? 0.4060 0.5328 0.4999 -0.0051 -0.0407 -0.0133 133 ASP A C   
342  O O   . ASP A 133 ? 0.4852 0.6174 0.5770 -0.0029 -0.0463 -0.0135 133 ASP A O   
343  C CB  . ASP A 133 ? 0.5264 0.6670 0.6299 0.0087  -0.0337 -0.0090 133 ASP A CB  
344  C CG  . ASP A 133 ? 0.6789 0.8391 0.7936 0.0127  -0.0301 -0.0065 133 ASP A CG  
345  O OD1 . ASP A 133 ? 0.6256 0.7994 0.7501 0.0037  -0.0286 -0.0056 133 ASP A OD1 
346  O OD2 . ASP A 133 ? 0.7524 0.9133 0.8646 0.0246  -0.0286 -0.0054 133 ASP A OD2 
347  N N   . ALA A 134 ? 0.3441 0.4516 0.4295 -0.0081 -0.0374 -0.0151 134 ALA A N   
348  C CA  . ALA A 134 ? 0.4204 0.5136 0.4941 -0.0095 -0.0396 -0.0175 134 ALA A CA  
349  C C   . ALA A 134 ? 0.4306 0.5276 0.5031 -0.0173 -0.0449 -0.0199 134 ALA A C   
350  O O   . ALA A 134 ? 0.3810 0.4753 0.4458 -0.0162 -0.0491 -0.0210 134 ALA A O   
351  C CB  . ALA A 134 ? 0.3797 0.4557 0.4468 -0.0109 -0.0346 -0.0189 134 ALA A CB  
352  N N   . LEU A 135 ? 0.3415 0.4437 0.4200 -0.0261 -0.0450 -0.0205 135 LEU A N   
353  C CA  . LEU A 135 ? 0.4870 0.5920 0.5634 -0.0354 -0.0509 -0.0229 135 LEU A CA  
354  C C   . LEU A 135 ? 0.4772 0.6029 0.5603 -0.0333 -0.0576 -0.0213 135 LEU A C   
355  O O   . LEU A 135 ? 0.4271 0.5510 0.5028 -0.0357 -0.0636 -0.0234 135 LEU A O   
356  C CB  . LEU A 135 ? 0.5082 0.6137 0.5892 -0.0465 -0.0499 -0.0230 135 LEU A CB  
357  C CG  . LEU A 135 ? 0.5105 0.6186 0.5901 -0.0599 -0.0562 -0.0250 135 LEU A CG  
358  C CD1 . LEU A 135 ? 0.5625 0.7005 0.6572 -0.0636 -0.0613 -0.0220 135 LEU A CD1 
359  C CD2 . LEU A 135 ? 0.5715 0.6636 0.6353 -0.0609 -0.0607 -0.0296 135 LEU A CD2 
360  N N   . GLN A 136 ? 0.3944 0.5401 0.4908 -0.0279 -0.0566 -0.0176 136 GLN A N   
361  C CA  . GLN A 136 ? 0.4253 0.5929 0.5289 -0.0231 -0.0628 -0.0157 136 GLN A CA  
362  C C   . GLN A 136 ? 0.3933 0.5507 0.4852 -0.0131 -0.0658 -0.0159 136 GLN A C   
363  O O   . GLN A 136 ? 0.3666 0.5345 0.4580 -0.0112 -0.0730 -0.0155 136 GLN A O   
364  C CB  . GLN A 136 ? 0.4315 0.6217 0.5503 -0.0166 -0.0597 -0.0119 136 GLN A CB  
365  C CG  . GLN A 136 ? 0.4437 0.6506 0.5756 -0.0279 -0.0578 -0.0106 136 GLN A CG  
366  C CD  . GLN A 136 ? 0.5471 0.7682 0.6837 -0.0407 -0.0656 -0.0114 136 GLN A CD  
367  O OE1 . GLN A 136 ? 0.4690 0.7043 0.6078 -0.0374 -0.0728 -0.0111 136 GLN A OE1 
368  N NE2 . GLN A 136 ? 0.5246 0.7407 0.6614 -0.0558 -0.0647 -0.0122 136 GLN A NE2 
369  N N   . MET A 137 ? 0.3645 0.5017 0.4463 -0.0072 -0.0607 -0.0160 137 MET A N   
370  C CA  . MET A 137 ? 0.3441 0.4692 0.4128 0.0002  -0.0631 -0.0156 137 MET A CA  
371  C C   . MET A 137 ? 0.4069 0.5223 0.4638 -0.0064 -0.0673 -0.0186 137 MET A C   
372  O O   . MET A 137 ? 0.3817 0.4961 0.4301 -0.0024 -0.0727 -0.0178 137 MET A O   
373  C CB  . MET A 137 ? 0.3228 0.4297 0.3839 0.0051  -0.0567 -0.0149 137 MET A CB  
374  C CG  . MET A 137 ? 0.3821 0.4945 0.4497 0.0139  -0.0536 -0.0122 137 MET A CG  
375  S SD  . MET A 137 ? 0.5079 0.5978 0.5650 0.0172  -0.0476 -0.0116 137 MET A SD  
376  C CE  . MET A 137 ? 0.4082 0.4850 0.4491 0.0237  -0.0522 -0.0097 137 MET A CE  
377  N N   . LEU A 138 ? 0.3711 0.4774 0.4251 -0.0157 -0.0650 -0.0220 138 LEU A N   
378  C CA  . LEU A 138 ? 0.4944 0.5913 0.5360 -0.0219 -0.0690 -0.0256 138 LEU A CA  
379  C C   . LEU A 138 ? 0.4547 0.5681 0.5004 -0.0263 -0.0781 -0.0257 138 LEU A C   
380  O O   . LEU A 138 ? 0.4214 0.5318 0.4561 -0.0261 -0.0839 -0.0268 138 LEU A O   
381  C CB  . LEU A 138 ? 0.3800 0.4627 0.4170 -0.0297 -0.0648 -0.0294 138 LEU A CB  
382  C CG  . LEU A 138 ? 0.4414 0.5085 0.4734 -0.0258 -0.0564 -0.0298 138 LEU A CG  
383  C CD1 . LEU A 138 ? 0.2880 0.3423 0.3156 -0.0323 -0.0536 -0.0336 138 LEU A CD1 
384  C CD2 . LEU A 138 ? 0.3317 0.3885 0.3505 -0.0204 -0.0551 -0.0298 138 LEU A CD2 
385  N N   . LEU A 139 ? 0.4761 0.6088 0.5377 -0.0308 -0.0796 -0.0244 139 LEU A N   
386  C CA  . LEU A 139 ? 0.4538 0.6052 0.5210 -0.0375 -0.0887 -0.0245 139 LEU A CA  
387  C C   . LEU A 139 ? 0.4447 0.6134 0.5157 -0.0272 -0.0948 -0.0211 139 LEU A C   
388  O O   . LEU A 139 ? 0.4465 0.6235 0.5141 -0.0302 -0.1037 -0.0218 139 LEU A O   
389  C CB  . LEU A 139 ? 0.4600 0.6293 0.5438 -0.0469 -0.0882 -0.0234 139 LEU A CB  
390  C CG  . LEU A 139 ? 0.5194 0.6709 0.5978 -0.0588 -0.0843 -0.0266 139 LEU A CG  
391  C CD1 . LEU A 139 ? 0.5013 0.6723 0.5965 -0.0677 -0.0834 -0.0239 139 LEU A CD1 
392  C CD2 . LEU A 139 ? 0.4104 0.5451 0.4721 -0.0685 -0.0903 -0.0316 139 LEU A CD2 
393  N N   . ASP A 140 ? 0.4328 0.6060 0.5093 -0.0148 -0.0908 -0.0176 140 ASP A N   
394  C CA  . ASP A 140 ? 0.4139 0.6003 0.4916 -0.0029 -0.0966 -0.0143 140 ASP A CA  
395  C C   . ASP A 140 ? 0.4887 0.6521 0.5467 0.0052  -0.0972 -0.0138 140 ASP A C   
396  O O   . ASP A 140 ? 0.5054 0.6741 0.5602 0.0160  -0.1022 -0.0108 140 ASP A O   
397  C CB  . ASP A 140 ? 0.4685 0.6737 0.5618 0.0074  -0.0931 -0.0106 140 ASP A CB  
398  C CG  . ASP A 140 ? 0.5474 0.7328 0.6343 0.0155  -0.0844 -0.0098 140 ASP A CG  
399  O OD1 . ASP A 140 ? 0.5750 0.7344 0.6464 0.0146  -0.0816 -0.0112 140 ASP A OD1 
400  O OD2 . ASP A 140 ? 0.6711 0.8684 0.7687 0.0228  -0.0803 -0.0077 140 ASP A OD2 
401  N N   . GLY A 141 ? 0.5121 0.6509 0.5564 0.0005  -0.0920 -0.0164 141 GLY A N   
402  C CA  . GLY A 141 ? 0.4416 0.5601 0.4666 0.0049  -0.0924 -0.0158 141 GLY A CA  
403  C C   . GLY A 141 ? 0.5275 0.6316 0.5469 0.0135  -0.0864 -0.0129 141 GLY A C   
404  O O   . GLY A 141 ? 0.5117 0.5990 0.5145 0.0160  -0.0865 -0.0116 141 GLY A O   
405  N N   . SER A 142 ? 0.4514 0.5610 0.4827 0.0171  -0.0812 -0.0118 142 SER A N   
406  C CA  . SER A 142 ? 0.4774 0.5715 0.5016 0.0243  -0.0764 -0.0093 142 SER A CA  
407  C C   . SER A 142 ? 0.3782 0.4528 0.3923 0.0178  -0.0702 -0.0108 142 SER A C   
408  O O   . SER A 142 ? 0.4747 0.5334 0.4771 0.0210  -0.0681 -0.0086 142 SER A O   
409  C CB  . SER A 142 ? 0.3582 0.4627 0.3963 0.0296  -0.0724 -0.0083 142 SER A CB  
410  O OG  . SER A 142 ? 0.5607 0.6895 0.6117 0.0340  -0.0773 -0.0073 142 SER A OG  
411  N N   . ALA A 143 ? 0.4342 0.5097 0.4517 0.0086  -0.0675 -0.0145 143 ALA A N   
412  C CA  . ALA A 143 ? 0.3901 0.4507 0.3993 0.0036  -0.0615 -0.0163 143 ALA A CA  
413  C C   . ALA A 143 ? 0.3682 0.4265 0.3703 -0.0033 -0.0633 -0.0202 143 ALA A C   
414  O O   . ALA A 143 ? 0.4407 0.5088 0.4486 -0.0075 -0.0677 -0.0224 143 ALA A O   
415  C CB  . ALA A 143 ? 0.3396 0.4002 0.3590 0.0017  -0.0546 -0.0172 143 ALA A CB  
416  N N   . GLN A 144 ? 0.4329 0.4784 0.4215 -0.0049 -0.0599 -0.0209 144 GLN A N   
417  C CA  . GLN A 144 ? 0.3481 0.3884 0.3267 -0.0101 -0.0603 -0.0252 144 GLN A CA  
418  C C   . GLN A 144 ? 0.4018 0.4373 0.3836 -0.0137 -0.0539 -0.0290 144 GLN A C   
419  O O   . GLN A 144 ? 0.4065 0.4383 0.3835 -0.0182 -0.0553 -0.0336 144 GLN A O   
420  C CB  . GLN A 144 ? 0.4568 0.4870 0.4177 -0.0092 -0.0594 -0.0239 144 GLN A CB  
421  C CG  . GLN A 144 ? 0.3919 0.4231 0.3442 -0.0061 -0.0671 -0.0207 144 GLN A CG  
422  C CD  . GLN A 144 ? 0.6573 0.6773 0.5898 -0.0066 -0.0658 -0.0192 144 GLN A CD  
423  O OE1 . GLN A 144 ? 0.6650 0.6806 0.5869 -0.0101 -0.0643 -0.0230 144 GLN A OE1 
424  N NE2 . GLN A 144 ? 0.6491 0.6630 0.5747 -0.0031 -0.0660 -0.0137 144 GLN A NE2 
425  N N   . LEU A 145 ? 0.3365 0.3704 0.3248 -0.0114 -0.0475 -0.0273 145 LEU A N   
426  C CA  . LEU A 145 ? 0.3789 0.4077 0.3693 -0.0128 -0.0414 -0.0303 145 LEU A CA  
427  C C   . LEU A 145 ? 0.3325 0.3660 0.3371 -0.0114 -0.0387 -0.0281 145 LEU A C   
428  O O   . LEU A 145 ? 0.3840 0.4220 0.3938 -0.0083 -0.0395 -0.0242 145 LEU A O   
429  C CB  . LEU A 145 ? 0.3407 0.3633 0.3213 -0.0110 -0.0353 -0.0303 145 LEU A CB  
430  C CG  . LEU A 145 ? 0.4633 0.4803 0.4275 -0.0119 -0.0359 -0.0327 145 LEU A CG  
431  C CD1 . LEU A 145 ? 0.3698 0.3854 0.3271 -0.0100 -0.0286 -0.0315 145 LEU A CD1 
432  C CD2 . LEU A 145 ? 0.4443 0.4548 0.4024 -0.0145 -0.0376 -0.0389 145 LEU A CD2 
433  N N   . ALA A 146 ? 0.3818 0.4120 0.3903 -0.0133 -0.0356 -0.0307 146 ALA A N   
434  C CA  . ALA A 146 ? 0.3362 0.3694 0.3563 -0.0123 -0.0327 -0.0288 146 ALA A CA  
435  C C   . ALA A 146 ? 0.3622 0.3875 0.3804 -0.0112 -0.0270 -0.0307 146 ALA A C   
436  O O   . ALA A 146 ? 0.3138 0.3307 0.3236 -0.0123 -0.0263 -0.0347 146 ALA A O   
437  C CB  . ALA A 146 ? 0.3484 0.3883 0.3774 -0.0164 -0.0362 -0.0290 146 ALA A CB  
438  N N   . LEU A 147 ? 0.4084 0.4356 0.4330 -0.0082 -0.0233 -0.0280 147 LEU A N   
439  C CA  . LEU A 147 ? 0.3598 0.3820 0.3852 -0.0061 -0.0187 -0.0290 147 LEU A CA  
440  C C   . LEU A 147 ? 0.4298 0.4514 0.4628 -0.0080 -0.0190 -0.0283 147 LEU A C   
441  O O   . LEU A 147 ? 0.4120 0.4399 0.4528 -0.0072 -0.0191 -0.0250 147 LEU A O   
442  C CB  . LEU A 147 ? 0.4237 0.4497 0.4509 -0.0025 -0.0149 -0.0262 147 LEU A CB  
443  C CG  . LEU A 147 ? 0.4842 0.5119 0.5039 -0.0015 -0.0129 -0.0263 147 LEU A CG  
444  C CD1 . LEU A 147 ? 0.5207 0.5535 0.5439 0.0011  -0.0084 -0.0243 147 LEU A CD1 
445  C CD2 . LEU A 147 ? 0.4646 0.4862 0.4744 -0.0010 -0.0123 -0.0310 147 LEU A CD2 
446  N N   . MET A 148 ? 0.4408 0.4535 0.4698 -0.0106 -0.0193 -0.0313 148 MET A N   
447  C CA  . MET A 148 ? 0.4717 0.4818 0.5053 -0.0146 -0.0198 -0.0304 148 MET A CA  
448  C C   . MET A 148 ? 0.4728 0.4693 0.5005 -0.0118 -0.0165 -0.0319 148 MET A C   
449  O O   . MET A 148 ? 0.4412 0.4311 0.4610 -0.0069 -0.0144 -0.0346 148 MET A O   
450  C CB  . MET A 148 ? 0.4154 0.4257 0.4476 -0.0225 -0.0247 -0.0322 148 MET A CB  
451  C CG  . MET A 148 ? 0.4257 0.4504 0.4627 -0.0234 -0.0287 -0.0308 148 MET A CG  
452  S SD  . MET A 148 ? 0.6410 0.6715 0.6780 -0.0327 -0.0359 -0.0326 148 MET A SD  
453  C CE  . MET A 148 ? 0.6231 0.6639 0.6728 -0.0395 -0.0360 -0.0293 148 MET A CE  
454  N N   . PHE A 149 ? 0.4440 0.4367 0.4749 -0.0142 -0.0159 -0.0300 149 PHE A N   
455  C CA  . PHE A 149 ? 0.6699 0.6472 0.6936 -0.0112 -0.0136 -0.0310 149 PHE A CA  
456  C C   . PHE A 149 ? 0.6638 0.6275 0.6810 -0.0194 -0.0159 -0.0319 149 PHE A C   
457  O O   . PHE A 149 ? 0.6877 0.6589 0.7104 -0.0280 -0.0187 -0.0306 149 PHE A O   
458  C CB  . PHE A 149 ? 0.4863 0.4675 0.5163 -0.0060 -0.0105 -0.0271 149 PHE A CB  
459  C CG  . PHE A 149 ? 0.5468 0.5340 0.5845 -0.0109 -0.0107 -0.0232 149 PHE A CG  
460  C CD1 . PHE A 149 ? 0.6222 0.6253 0.6692 -0.0121 -0.0115 -0.0210 149 PHE A CD1 
461  C CD2 . PHE A 149 ? 0.6675 0.6437 0.7016 -0.0136 -0.0100 -0.0215 149 PHE A CD2 
462  C CE1 . PHE A 149 ? 0.5562 0.5663 0.6098 -0.0150 -0.0108 -0.0176 149 PHE A CE1 
463  C CE2 . PHE A 149 ? 0.6178 0.6013 0.6586 -0.0181 -0.0093 -0.0176 149 PHE A CE2 
464  C CZ  . PHE A 149 ? 0.5777 0.5793 0.6287 -0.0184 -0.0094 -0.0158 149 PHE A CZ  
465  N N   . GLU A 150 ? 0.7014 0.6449 0.7063 -0.0164 -0.0149 -0.0341 150 GLU A N   
466  C CA  . GLU A 150 ? 0.8855 0.8096 0.8801 -0.0242 -0.0171 -0.0347 150 GLU A CA  
467  C C   . GLU A 150 ? 1.0477 0.9679 1.0362 -0.0341 -0.0220 -0.0382 150 GLU A C   
468  O O   . GLU A 150 ? 1.1894 1.0890 1.1613 -0.0337 -0.0236 -0.0430 150 GLU A O   
469  C CB  . GLU A 150 ? 0.8626 0.7921 0.8657 -0.0298 -0.0162 -0.0292 150 GLU A CB  
470  C CG  . GLU A 150 ? 1.0281 0.9387 1.0210 -0.0403 -0.0183 -0.0283 150 GLU A CG  
471  C CD  . GLU A 150 ? 1.0521 0.9736 1.0510 -0.0546 -0.0219 -0.0274 150 GLU A CD  
472  O OE1 . GLU A 150 ? 1.0055 0.9523 1.0207 -0.0563 -0.0211 -0.0241 150 GLU A OE1 
473  O OE2 . GLU A 150 ? 1.0176 0.9226 1.0044 -0.0641 -0.0259 -0.0300 150 GLU A OE2 
474  N N   . ARG A 151 ? 1.2262 1.1654 1.2266 -0.0424 -0.0246 -0.0360 151 ARG A N   
475  C CA  . ARG A 151 ? 1.2292 1.1694 1.2253 -0.0505 -0.0300 -0.0393 151 ARG A CA  
476  C C   . ARG A 151 ? 1.1982 1.1459 1.1932 -0.0425 -0.0299 -0.0423 151 ARG A C   
477  O O   . ARG A 151 ? 1.1094 1.0473 1.0921 -0.0445 -0.0331 -0.0470 151 ARG A O   
478  C CB  . ARG A 151 ? 1.2491 1.2103 1.2592 -0.0614 -0.0334 -0.0357 151 ARG A CB  
479  C CG  . ARG A 151 ? 1.2120 1.1728 1.2268 -0.0689 -0.0318 -0.0311 151 ARG A CG  
480  C CD  . ARG A 151 ? 1.2631 1.2429 1.2887 -0.0824 -0.0358 -0.0284 151 ARG A CD  
481  N NE  . ARG A 151 ? 1.2790 1.2441 1.2922 -0.0954 -0.0419 -0.0316 151 ARG A NE  
482  C CZ  . ARG A 151 ? 1.2852 1.2584 1.2981 -0.1005 -0.0481 -0.0345 151 ARG A CZ  
483  N NH1 . ARG A 151 ? 1.2439 1.2406 1.2687 -0.0938 -0.0489 -0.0341 151 ARG A NH1 
484  N NH2 . ARG A 151 ? 1.2668 1.2224 1.2653 -0.1130 -0.0540 -0.0378 151 ARG A NH2 
485  N N   . ASP A 155 ? 0.9148 0.9048 0.9209 -0.1196 -0.0678 -0.0421 155 ASP A N   
486  C CA  . ASP A 155 ? 0.9194 0.9350 0.9355 -0.1269 -0.0755 -0.0414 155 ASP A CA  
487  C C   . ASP A 155 ? 0.8698 0.8688 0.8670 -0.1264 -0.0816 -0.0480 155 ASP A C   
488  O O   . ASP A 155 ? 0.8777 0.8623 0.8641 -0.1135 -0.0777 -0.0513 155 ASP A O   
489  C CB  . ASP A 155 ? 0.9166 0.9657 0.9546 -0.1159 -0.0728 -0.0368 155 ASP A CB  
490  C CG  . ASP A 155 ? 0.9209 1.0002 0.9715 -0.1220 -0.0808 -0.0351 155 ASP A CG  
491  O OD1 . ASP A 155 ? 0.9126 0.9875 0.9547 -0.1348 -0.0892 -0.0380 155 ASP A OD1 
492  O OD2 . ASP A 155 ? 0.7517 0.8591 0.8202 -0.1137 -0.0792 -0.0310 155 ASP A OD2 
493  N N   . ASN A 156 ? 0.8611 0.8629 0.8538 -0.1411 -0.0911 -0.0498 156 ASN A N   
494  C CA  . ASN A 156 ? 0.8620 0.8438 0.8327 -0.1422 -0.0973 -0.0566 156 ASN A CA  
495  C C   . ASN A 156 ? 0.8136 0.8138 0.7888 -0.1315 -0.0995 -0.0570 156 ASN A C   
496  O O   . ASN A 156 ? 0.7596 0.7444 0.7159 -0.1307 -0.1040 -0.0624 156 ASN A O   
497  C CB  . ASN A 156 ? 1.0190 0.9953 0.9811 -0.1632 -0.1078 -0.0586 156 ASN A CB  
498  C CG  . ASN A 156 ? 0.9627 0.9794 0.9465 -0.1720 -0.1154 -0.0541 156 ASN A CG  
499  O OD1 . ASN A 156 ? 0.9818 1.0307 0.9903 -0.1657 -0.1114 -0.0480 156 ASN A OD1 
500  N ND2 . ASN A 156 ? 0.9124 0.9280 0.8865 -0.1862 -0.1267 -0.0573 156 ASN A ND2 
501  N N   . ARG A 157 ? 0.8174 0.8479 0.8150 -0.1228 -0.0965 -0.0513 157 ARG A N   
502  C CA  . ARG A 157 ? 0.7375 0.7825 0.7375 -0.1119 -0.0984 -0.0509 157 ARG A CA  
503  C C   . ARG A 157 ? 0.6448 0.6773 0.6386 -0.0954 -0.0895 -0.0516 157 ARG A C   
504  O O   . ARG A 157 ? 0.5906 0.6265 0.5795 -0.0871 -0.0908 -0.0520 157 ARG A O   
505  C CB  . ARG A 157 ? 0.7001 0.7833 0.7252 -0.1105 -0.1009 -0.0446 157 ARG A CB  
506  C CG  . ARG A 157 ? 0.7801 0.8839 0.8128 -0.1257 -0.1115 -0.0438 157 ARG A CG  
507  C CD  . ARG A 157 ? 0.7503 0.8948 0.8089 -0.1214 -0.1131 -0.0374 157 ARG A CD  
508  N NE  . ARG A 157 ? 0.7334 0.8880 0.8080 -0.1184 -0.1041 -0.0328 157 ARG A NE  
509  C CZ  . ARG A 157 ? 0.7391 0.9270 0.8358 -0.1128 -0.1027 -0.0272 157 ARG A CZ  
510  N NH1 . ARG A 157 ? 0.5619 0.7773 0.6686 -0.1085 -0.1098 -0.0252 157 ARG A NH1 
511  N NH2 . ARG A 157 ? 0.6643 0.8577 0.7722 -0.1106 -0.0941 -0.0237 157 ARG A NH2 
512  N N   . GLU A 158 ? 0.5828 0.6014 0.5761 -0.0911 -0.0810 -0.0512 158 GLU A N   
513  C CA  . GLU A 158 ? 0.6125 0.6200 0.5997 -0.0771 -0.0730 -0.0519 158 GLU A CA  
514  C C   . GLU A 158 ? 0.6910 0.6680 0.6545 -0.0761 -0.0713 -0.0584 158 GLU A C   
515  O O   . GLU A 158 ? 0.6587 0.6173 0.6114 -0.0848 -0.0735 -0.0616 158 GLU A O   
516  C CB  . GLU A 158 ? 0.6482 0.6606 0.6490 -0.0711 -0.0649 -0.0476 158 GLU A CB  
517  C CG  . GLU A 158 ? 0.7811 0.7897 0.7868 -0.0805 -0.0641 -0.0462 158 GLU A CG  
518  C CD  . GLU A 158 ? 0.9716 0.9752 0.9825 -0.0730 -0.0555 -0.0435 158 GLU A CD  
519  O OE1 . GLU A 158 ? 0.8796 0.9010 0.9050 -0.0658 -0.0521 -0.0392 158 GLU A OE1 
520  O OE2 . GLU A 158 ? 0.9653 0.9463 0.9650 -0.0740 -0.0527 -0.0457 158 GLU A OE2 
521  N N   . GLN A 159 ? 0.6182 0.5897 0.5722 -0.0655 -0.0674 -0.0602 159 GLN A N   
522  C CA  . GLN A 159 ? 0.6430 0.5895 0.5771 -0.0595 -0.0626 -0.0655 159 GLN A CA  
523  C C   . GLN A 159 ? 0.5442 0.4939 0.4856 -0.0473 -0.0529 -0.0627 159 GLN A C   
524  O O   . GLN A 159 ? 0.5408 0.5097 0.4981 -0.0434 -0.0508 -0.0574 159 GLN A O   
525  C CB  . GLN A 159 ? 0.6380 0.5763 0.5529 -0.0579 -0.0658 -0.0702 159 GLN A CB  
526  C CG  . GLN A 159 ? 0.8765 0.7920 0.7702 -0.0671 -0.0724 -0.0769 159 GLN A CG  
527  C CD  . GLN A 159 ? 0.9890 0.8750 0.8638 -0.0616 -0.0667 -0.0824 159 GLN A CD  
528  O OE1 . GLN A 159 ? 0.8757 0.7562 0.7572 -0.0593 -0.0618 -0.0806 159 GLN A OE1 
529  N NE2 . GLN A 159 ? 0.9083 0.7745 0.7580 -0.0587 -0.0676 -0.0892 159 GLN A NE2 
530  N N   . PHE A 160 ? 0.5525 0.4829 0.4813 -0.0411 -0.0473 -0.0663 160 PHE A N   
531  C CA  . PHE A 160 ? 0.5684 0.5034 0.5051 -0.0305 -0.0388 -0.0636 160 PHE A CA  
532  C C   . PHE A 160 ? 0.5903 0.5072 0.5094 -0.0213 -0.0332 -0.0686 160 PHE A C   
533  O O   . PHE A 160 ? 0.6605 0.5562 0.5600 -0.0230 -0.0358 -0.0746 160 PHE A O   
534  C CB  . PHE A 160 ? 0.5083 0.4461 0.4593 -0.0328 -0.0372 -0.0595 160 PHE A CB  
535  C CG  . PHE A 160 ? 0.6316 0.5453 0.5705 -0.0348 -0.0370 -0.0628 160 PHE A CG  
536  C CD1 . PHE A 160 ? 0.6489 0.5498 0.5809 -0.0242 -0.0307 -0.0643 160 PHE A CD1 
537  C CD2 . PHE A 160 ? 0.7180 0.6212 0.6513 -0.0473 -0.0436 -0.0643 160 PHE A CD2 
538  C CE1 . PHE A 160 ? 0.6997 0.5751 0.6178 -0.0247 -0.0310 -0.0672 160 PHE A CE1 
539  C CE2 . PHE A 160 ? 0.7630 0.6398 0.6821 -0.0501 -0.0440 -0.0671 160 PHE A CE2 
540  C CZ  . PHE A 160 ? 0.7981 0.6594 0.7087 -0.0380 -0.0376 -0.0686 160 PHE A CZ  
541  N N   . VAL A 161 ? 0.5703 0.4963 0.4962 -0.0112 -0.0258 -0.0661 161 VAL A N   
542  C CA  . VAL A 161 ? 0.6071 0.5220 0.5214 0.0000  -0.0191 -0.0697 161 VAL A CA  
543  C C   . VAL A 161 ? 0.5868 0.5120 0.5166 0.0064  -0.0136 -0.0650 161 VAL A C   
544  O O   . VAL A 161 ? 0.5321 0.4770 0.4787 0.0050  -0.0128 -0.0594 161 VAL A O   
545  C CB  . VAL A 161 ? 0.5240 0.4446 0.4283 0.0062  -0.0153 -0.0718 161 VAL A CB  
546  C CG1 . VAL A 161 ? 0.4582 0.4034 0.3780 0.0053  -0.0137 -0.0654 161 VAL A CG1 
547  C CG2 . VAL A 161 ? 0.6380 0.5511 0.5320 0.0192  -0.0075 -0.0752 161 VAL A CG2 
548  N N   . GLU A 162 ? 0.5948 0.5050 0.5174 0.0135  -0.0105 -0.0674 162 GLU A N   
549  C CA  . GLU A 162 ? 0.6143 0.5332 0.5503 0.0197  -0.0063 -0.0630 162 GLU A CA  
550  C C   . GLU A 162 ? 0.6097 0.5485 0.5525 0.0289  0.0002  -0.0610 162 GLU A C   
551  O O   . GLU A 162 ? 0.5991 0.5369 0.5304 0.0354  0.0038  -0.0647 162 GLU A O   
552  C CB  . GLU A 162 ? 0.5589 0.4547 0.4834 0.0258  -0.0054 -0.0659 162 GLU A CB  
553  C CG  . GLU A 162 ? 0.6429 0.5459 0.5806 0.0308  -0.0028 -0.0609 162 GLU A CG  
554  C CD  . GLU A 162 ? 0.7582 0.6352 0.6825 0.0361  -0.0031 -0.0631 162 GLU A CD  
555  O OE1 . GLU A 162 ? 0.8195 0.6813 0.7406 0.0262  -0.0078 -0.0623 162 GLU A OE1 
556  O OE2 . GLU A 162 ? 0.7103 0.5822 0.6270 0.0501  0.0013  -0.0653 162 GLU A OE2 
557  N N   . LEU A 163 ? 0.4431 0.4002 0.4039 0.0286  0.0017  -0.0551 163 LEU A N   
558  C CA  . LEU A 163 ? 0.4934 0.4717 0.4626 0.0341  0.0070  -0.0520 163 LEU A CA  
559  C C   . LEU A 163 ? 0.5891 0.5721 0.5631 0.0447  0.0116  -0.0510 163 LEU A C   
560  O O   . LEU A 163 ? 0.6628 0.6525 0.6324 0.0542  0.0170  -0.0528 163 LEU A O   
561  C CB  . LEU A 163 ? 0.4936 0.4887 0.4776 0.0260  0.0048  -0.0461 163 LEU A CB  
562  C CG  . LEU A 163 ? 0.5252 0.5213 0.5057 0.0179  0.0008  -0.0461 163 LEU A CG  
563  C CD1 . LEU A 163 ? 0.5062 0.5170 0.4990 0.0129  -0.0006 -0.0401 163 LEU A CD1 
564  C CD2 . LEU A 163 ? 0.4921 0.4879 0.4592 0.0210  0.0038  -0.0494 163 LEU A CD2 
565  N N   . LYS A 164 ? 0.5290 0.5097 0.5116 0.0437  0.0095  -0.0480 164 LYS A N   
566  C CA  . LYS A 164 ? 0.5464 0.5360 0.5364 0.0530  0.0128  -0.0456 164 LYS A CA  
567  C C   . LYS A 164 ? 0.5102 0.4898 0.5045 0.0507  0.0093  -0.0430 164 LYS A C   
568  O O   . LYS A 164 ? 0.4831 0.4553 0.4787 0.0407  0.0052  -0.0419 164 LYS A O   
569  C CB  . LYS A 164 ? 0.5616 0.5788 0.5660 0.0521  0.0155  -0.0408 164 LYS A CB  
570  C CG  . LYS A 164 ? 0.6657 0.6895 0.6805 0.0406  0.0114  -0.0362 164 LYS A CG  
571  C CD  . LYS A 164 ? 0.6915 0.7379 0.7187 0.0392  0.0130  -0.0311 164 LYS A CD  
572  C CE  . LYS A 164 ? 0.8458 0.9068 0.8710 0.0407  0.0176  -0.0313 164 LYS A CE  
573  N NZ  . LYS A 164 ? 0.8582 0.9315 0.8892 0.0310  0.0163  -0.0267 164 LYS A NZ  
574  N N   . ARG A 165 ? 0.4927 0.4736 0.4891 0.0604  0.0112  -0.0417 165 ARG A N   
575  C CA  . ARG A 165 ? 0.4984 0.4744 0.5002 0.0592  0.0086  -0.0380 165 ARG A CA  
576  C C   . ARG A 165 ? 0.5240 0.5246 0.5426 0.0574  0.0088  -0.0325 165 ARG A C   
577  O O   . ARG A 165 ? 0.5869 0.6072 0.6119 0.0624  0.0118  -0.0316 165 ARG A O   
578  C CB  . ARG A 165 ? 0.4613 0.4217 0.4531 0.0717  0.0095  -0.0396 165 ARG A CB  
579  C CG  . ARG A 165 ? 0.5424 0.4909 0.5344 0.0706  0.0065  -0.0360 165 ARG A CG  
580  C CD  . ARG A 165 ? 0.5660 0.4998 0.5468 0.0854  0.0074  -0.0373 165 ARG A CD  
581  N NE  . ARG A 165 ? 0.6347 0.5926 0.6268 0.0968  0.0098  -0.0347 165 ARG A NE  
582  C CZ  . ARG A 165 ? 0.6736 0.6441 0.6771 0.0966  0.0079  -0.0294 165 ARG A CZ  
583  N NH1 . ARG A 165 ? 0.6005 0.5605 0.6043 0.0873  0.0045  -0.0262 165 ARG A NH1 
584  N NH2 . ARG A 165 ? 0.6001 0.5954 0.6146 0.1059  0.0094  -0.0272 165 ARG A NH2 
585  N N   . GLU A 166 ? 0.4491 0.4487 0.4739 0.0497  0.0056  -0.0290 166 GLU A N   
586  C CA  . GLU A 166 ? 0.4409 0.4586 0.4784 0.0473  0.0048  -0.0241 166 GLU A CA  
587  C C   . GLU A 166 ? 0.4575 0.4679 0.4953 0.0506  0.0030  -0.0214 166 GLU A C   
588  O O   . GLU A 166 ? 0.4340 0.4284 0.4667 0.0461  0.0011  -0.0212 166 GLU A O   
589  C CB  . GLU A 166 ? 0.4154 0.4381 0.4580 0.0362  0.0027  -0.0224 166 GLU A CB  
590  C CG  . GLU A 166 ? 0.5803 0.6141 0.6237 0.0329  0.0040  -0.0233 166 GLU A CG  
591  C CD  . GLU A 166 ? 0.6317 0.6859 0.6835 0.0333  0.0053  -0.0200 166 GLU A CD  
592  O OE1 . GLU A 166 ? 0.6487 0.7092 0.7067 0.0349  0.0041  -0.0170 166 GLU A OE1 
593  O OE2 . GLU A 166 ? 0.7983 0.8621 0.8497 0.0310  0.0072  -0.0202 166 GLU A OE2 
594  N N   . ALA A 167 ? 0.3703 0.3934 0.4137 0.0582  0.0034  -0.0191 167 ALA A N   
595  C CA  . ALA A 167 ? 0.4599 0.4761 0.5023 0.0627  0.0012  -0.0163 167 ALA A CA  
596  C C   . ALA A 167 ? 0.3912 0.4136 0.4404 0.0543  -0.0016 -0.0123 167 ALA A C   
597  O O   . ALA A 167 ? 0.3507 0.3889 0.4079 0.0485  -0.0021 -0.0110 167 ALA A O   
598  C CB  . ALA A 167 ? 0.4580 0.4870 0.5037 0.0754  0.0021  -0.0154 167 ALA A CB  
599  N N   . LEU A 168 ? 0.3916 0.3997 0.4356 0.0536  -0.0034 -0.0103 168 LEU A N   
600  C CA  . LEU A 168 ? 0.3785 0.3901 0.4262 0.0476  -0.0058 -0.0067 168 LEU A CA  
601  C C   . LEU A 168 ? 0.4776 0.4862 0.5227 0.0544  -0.0079 -0.0035 168 LEU A C   
602  O O   . LEU A 168 ? 0.4467 0.4439 0.4846 0.0629  -0.0077 -0.0039 168 LEU A O   
603  C CB  . LEU A 168 ? 0.3719 0.3710 0.4156 0.0389  -0.0055 -0.0069 168 LEU A CB  
604  C CG  . LEU A 168 ? 0.4485 0.4515 0.4950 0.0321  -0.0045 -0.0095 168 LEU A CG  
605  C CD1 . LEU A 168 ? 0.4343 0.4230 0.4735 0.0308  -0.0034 -0.0126 168 LEU A CD1 
606  C CD2 . LEU A 168 ? 0.4687 0.4748 0.5181 0.0249  -0.0054 -0.0077 168 LEU A CD2 
607  N N   . ILE A 169 ? 0.4075 0.4251 0.4568 0.0512  -0.0105 -0.0004 169 ILE A N   
608  C CA  . ILE A 169 ? 0.4139 0.4325 0.4615 0.0573  -0.0136 0.0030  169 ILE A CA  
609  C C   . ILE A 169 ? 0.3969 0.4069 0.4394 0.0515  -0.0153 0.0057  169 ILE A C   
610  O O   . ILE A 169 ? 0.3418 0.3575 0.3873 0.0438  -0.0156 0.0056  169 ILE A O   
611  C CB  . ILE A 169 ? 0.4644 0.5070 0.5222 0.0601  -0.0162 0.0043  169 ILE A CB  
612  C CG1 . ILE A 169 ? 0.5933 0.6491 0.6575 0.0645  -0.0133 0.0017  169 ILE A CG1 
613  C CG2 . ILE A 169 ? 0.4842 0.5294 0.5404 0.0685  -0.0200 0.0077  169 ILE A CG2 
614  C CD1 . ILE A 169 ? 0.6646 0.7107 0.7226 0.0770  -0.0113 0.0000  169 ILE A CD1 
615  N N   . PRO A 170 ? 0.3964 0.3919 0.4296 0.0553  -0.0161 0.0083  170 PRO A N   
616  C CA  . PRO A 170 ? 0.4028 0.3931 0.4306 0.0509  -0.0176 0.0113  170 PRO A CA  
617  C C   . PRO A 170 ? 0.4092 0.4141 0.4409 0.0527  -0.0224 0.0134  170 PRO A C   
618  O O   . PRO A 170 ? 0.4869 0.4992 0.5206 0.0607  -0.0254 0.0147  170 PRO A O   
619  C CB  . PRO A 170 ? 0.3750 0.3447 0.3903 0.0547  -0.0171 0.0139  170 PRO A CB  
620  C CG  . PRO A 170 ? 0.4315 0.3982 0.4457 0.0648  -0.0177 0.0128  170 PRO A CG  
621  C CD  . PRO A 170 ? 0.3876 0.3682 0.4124 0.0642  -0.0158 0.0086  170 PRO A CD  
622  N N   . VAL A 171 ? 0.3691 0.3785 0.4013 0.0455  -0.0235 0.0134  171 VAL A N   
623  C CA  . VAL A 171 ? 0.4083 0.4308 0.4431 0.0445  -0.0288 0.0148  171 VAL A CA  
624  C C   . VAL A 171 ? 0.3998 0.4134 0.4246 0.0403  -0.0304 0.0163  171 VAL A C   
625  O O   . VAL A 171 ? 0.3329 0.3349 0.3517 0.0372  -0.0263 0.0157  171 VAL A O   
626  C CB  . VAL A 171 ? 0.3635 0.4019 0.4082 0.0389  -0.0296 0.0127  171 VAL A CB  
627  C CG1 . VAL A 171 ? 0.4185 0.4682 0.4726 0.0438  -0.0276 0.0114  171 VAL A CG1 
628  C CG2 . VAL A 171 ? 0.3215 0.3527 0.3640 0.0317  -0.0265 0.0103  171 VAL A CG2 
629  N N   . ILE A 172 ? 0.4167 0.4375 0.4397 0.0404  -0.0364 0.0181  172 ILE A N   
630  C CA  . ILE A 172 ? 0.4241 0.4367 0.4355 0.0372  -0.0389 0.0192  172 ILE A CA  
631  C C   . ILE A 172 ? 0.4266 0.4518 0.4402 0.0329  -0.0461 0.0192  172 ILE A C   
632  O O   . ILE A 172 ? 0.4349 0.4770 0.4591 0.0340  -0.0495 0.0200  172 ILE A O   
633  C CB  . ILE A 172 ? 0.4465 0.4476 0.4468 0.0430  -0.0397 0.0227  172 ILE A CB  
634  C CG1 . ILE A 172 ? 0.4192 0.4092 0.4050 0.0396  -0.0402 0.0234  172 ILE A CG1 
635  C CG2 . ILE A 172 ? 0.4063 0.4179 0.4096 0.0493  -0.0463 0.0254  172 ILE A CG2 
636  C CD1 . ILE A 172 ? 0.5109 0.4856 0.4842 0.0433  -0.0373 0.0267  172 ILE A CD1 
637  N N   . SER A 173 ? 0.3576 0.3745 0.3602 0.0277  -0.0483 0.0184  173 SER A N   
638  C CA  . SER A 173 ? 0.4429 0.4681 0.4444 0.0215  -0.0560 0.0184  173 SER A CA  
639  C C   . SER A 173 ? 0.4661 0.4996 0.4665 0.0251  -0.0632 0.0217  173 SER A C   
640  O O   . SER A 173 ? 0.4589 0.4829 0.4505 0.0313  -0.0628 0.0239  173 SER A O   
641  C CB  . SER A 173 ? 0.3817 0.3913 0.3679 0.0161  -0.0569 0.0161  173 SER A CB  
642  O OG  . SER A 173 ? 0.4198 0.4325 0.4001 0.0097  -0.0657 0.0163  173 SER A OG  
643  N N   . LYS A 174 ? 0.4260 0.4783 0.4351 0.0206  -0.0699 0.0227  174 LYS A N   
644  C CA  . LYS A 174 ? 0.4025 0.4673 0.4126 0.0239  -0.0779 0.0261  174 LYS A CA  
645  C C   . LYS A 174 ? 0.4240 0.4745 0.4153 0.0212  -0.0839 0.0266  174 LYS A C   
646  O O   . LYS A 174 ? 0.5324 0.5874 0.5202 0.0262  -0.0897 0.0297  174 LYS A O   
647  C CB  . LYS A 174 ? 0.4310 0.5231 0.4563 0.0179  -0.0838 0.0272  174 LYS A CB  
648  C CG  . LYS A 174 ? 0.4308 0.5413 0.4747 0.0232  -0.0784 0.0274  174 LYS A CG  
649  C CD  . LYS A 174 ? 0.5035 0.6452 0.5628 0.0175  -0.0840 0.0294  174 LYS A CD  
650  C CE  . LYS A 174 ? 0.3789 0.5382 0.4550 0.0216  -0.0773 0.0289  174 LYS A CE  
651  N NZ  . LYS A 174 ? 0.4082 0.6034 0.5013 0.0188  -0.0820 0.0318  174 LYS A NZ  
652  N N   . THR A 175 ? 0.4639 0.4967 0.4416 0.0145  -0.0826 0.0235  175 THR A N   
653  C CA  . THR A 175 ? 0.5083 0.5248 0.4652 0.0125  -0.0874 0.0232  175 THR A CA  
654  C C   . THR A 175 ? 0.5432 0.5388 0.4863 0.0192  -0.0796 0.0228  175 THR A C   
655  O O   . THR A 175 ? 0.6250 0.6053 0.5488 0.0186  -0.0817 0.0221  175 THR A O   
656  C CB  . THR A 175 ? 0.4553 0.4639 0.4025 0.0012  -0.0918 0.0198  175 THR A CB  
657  O OG1 . THR A 175 ? 0.5926 0.5898 0.5393 0.0004  -0.0836 0.0165  175 THR A OG1 
658  C CG2 . THR A 175 ? 0.4660 0.4965 0.4261 -0.0079 -0.0999 0.0211  175 THR A CG2 
659  N N   . HIS A 176 ? 0.5679 0.5629 0.5198 0.0248  -0.0707 0.0232  176 HIS A N   
660  C CA  . HIS A 176 ? 0.4961 0.4747 0.4368 0.0300  -0.0634 0.0240  176 HIS A CA  
661  C C   . HIS A 176 ? 0.5621 0.5366 0.4923 0.0356  -0.0675 0.0282  176 HIS A C   
662  O O   . HIS A 176 ? 0.6539 0.6409 0.5924 0.0392  -0.0732 0.0311  176 HIS A O   
663  C CB  . HIS A 176 ? 0.4817 0.4620 0.4348 0.0333  -0.0546 0.0240  176 HIS A CB  
664  C CG  . HIS A 176 ? 0.5439 0.5097 0.4875 0.0355  -0.0462 0.0246  176 HIS A CG  
665  N ND1 . HIS A 176 ? 0.5674 0.5240 0.5008 0.0400  -0.0450 0.0287  176 HIS A ND1 
666  C CD2 . HIS A 176 ? 0.4412 0.4017 0.3841 0.0335  -0.0387 0.0222  176 HIS A CD2 
667  C CE1 . HIS A 176 ? 0.5609 0.5080 0.4882 0.0394  -0.0367 0.0289  176 HIS A CE1 
668  N NE2 . HIS A 176 ? 0.5432 0.4939 0.4770 0.0359  -0.0328 0.0249  176 HIS A NE2 
669  N N   . PRO A 177 ? 0.6460 0.6040 0.5573 0.0370  -0.0649 0.0290  177 PRO A N   
670  C CA  . PRO A 177 ? 0.6446 0.5967 0.5432 0.0422  -0.0691 0.0336  177 PRO A CA  
671  C C   . PRO A 177 ? 0.6667 0.6229 0.5746 0.0493  -0.0680 0.0378  177 PRO A C   
672  O O   . PRO A 177 ? 0.7696 0.7296 0.6747 0.0544  -0.0754 0.0415  177 PRO A O   
673  C CB  . PRO A 177 ? 0.6578 0.5916 0.5369 0.0426  -0.0621 0.0337  177 PRO A CB  
674  C CG  . PRO A 177 ? 0.6149 0.5462 0.4924 0.0376  -0.0589 0.0282  177 PRO A CG  
675  C CD  . PRO A 177 ? 0.5977 0.5425 0.4971 0.0347  -0.0582 0.0258  177 PRO A CD  
676  N N   . LEU A 178 ? 0.6814 0.6364 0.5994 0.0502  -0.0596 0.0372  178 LEU A N   
677  C CA  . LEU A 178 ? 0.6713 0.6258 0.5955 0.0572  -0.0585 0.0406  178 LEU A CA  
678  C C   . LEU A 178 ? 0.7042 0.6779 0.6437 0.0614  -0.0656 0.0407  178 LEU A C   
679  O O   . LEU A 178 ? 0.7104 0.6842 0.6505 0.0702  -0.0681 0.0441  178 LEU A O   
680  C CB  . LEU A 178 ? 0.6674 0.6162 0.5984 0.0553  -0.0486 0.0391  178 LEU A CB  
681  C CG  . LEU A 178 ? 0.7415 0.6762 0.6673 0.0598  -0.0443 0.0429  178 LEU A CG  
682  C CD1 . LEU A 178 ? 0.7560 0.6734 0.6610 0.0600  -0.0430 0.0475  178 LEU A CD1 
683  C CD2 . LEU A 178 ? 0.6596 0.5918 0.5939 0.0552  -0.0358 0.0403  178 LEU A CD2 
684  N N   . ALA A 179 ? 0.6775 0.6677 0.6286 0.0557  -0.0690 0.0372  179 ALA A N   
685  C CA  . ALA A 179 ? 0.6243 0.6371 0.5930 0.0586  -0.0740 0.0373  179 ALA A CA  
686  C C   . ALA A 179 ? 0.7596 0.7847 0.7265 0.0624  -0.0848 0.0407  179 ALA A C   
687  O O   . ALA A 179 ? 0.8536 0.8997 0.8351 0.0676  -0.0889 0.0420  179 ALA A O   
688  C CB  . ALA A 179 ? 0.6913 0.7175 0.6725 0.0494  -0.0735 0.0331  179 ALA A CB  
689  N N   . SER A 180 ? 0.7623 0.7764 0.7117 0.0604  -0.0896 0.0423  180 SER A N   
690  C CA  . SER A 180 ? 0.8310 0.8567 0.7774 0.0636  -0.1010 0.0456  180 SER A CA  
691  C C   . SER A 180 ? 1.0101 1.0333 0.9537 0.0774  -0.1028 0.0507  180 SER A C   
692  O O   . SER A 180 ? 1.0989 1.1363 1.0435 0.0825  -0.1127 0.0540  180 SER A O   
693  C CB  . SER A 180 ? 0.7946 0.8067 0.7200 0.0572  -0.1058 0.0454  180 SER A CB  
694  O OG  . SER A 180 ? 0.8602 0.8472 0.7663 0.0613  -0.1001 0.0473  180 SER A OG  
695  N N   . GLN A 181 ? 1.0069 1.0120 0.9459 0.0834  -0.0942 0.0516  181 GLN A N   
696  C CA  . GLN A 181 ? 0.9228 0.9192 0.8550 0.0967  -0.0958 0.0565  181 GLN A CA  
697  C C   . GLN A 181 ? 1.0031 1.0157 0.9537 0.1063  -0.0951 0.0562  181 GLN A C   
698  O O   . GLN A 181 ? 1.1023 1.1048 1.0474 0.1189  -0.0951 0.0594  181 GLN A O   
699  C CB  . GLN A 181 ? 0.9554 0.9204 0.8694 0.0969  -0.0874 0.0583  181 GLN A CB  
700  C CG  . GLN A 181 ? 0.8869 0.8382 0.7853 0.0866  -0.0845 0.0574  181 GLN A CG  
701  C CD  . GLN A 181 ? 0.9312 0.8577 0.8169 0.0843  -0.0741 0.0587  181 GLN A CD  
702  O OE1 . GLN A 181 ? 1.0032 0.9170 0.8857 0.0904  -0.0711 0.0616  181 GLN A OE1 
703  N NE2 . GLN A 181 ? 0.8867 0.8062 0.7643 0.0753  -0.0688 0.0565  181 GLN A NE2 
704  N N   . VAL A 184 ? 0.8853 0.8045 0.8040 0.1131  -0.0643 0.0569  184 VAL A N   
705  C CA  . VAL A 184 ? 0.7991 0.7001 0.7073 0.1011  -0.0569 0.0570  184 VAL A CA  
706  C C   . VAL A 184 ? 0.8010 0.6758 0.6990 0.1018  -0.0510 0.0582  184 VAL A C   
707  O O   . VAL A 184 ? 0.7939 0.6676 0.6979 0.1088  -0.0505 0.0561  184 VAL A O   
708  C CB  . VAL A 184 ? 0.7525 0.6700 0.6754 0.0894  -0.0526 0.0515  184 VAL A CB  
709  C CG1 . VAL A 184 ? 0.8019 0.7431 0.7338 0.0884  -0.0595 0.0501  184 VAL A CG1 
710  C CG2 . VAL A 184 ? 0.8329 0.7570 0.7709 0.0891  -0.0481 0.0469  184 VAL A CG2 
711  N N   . SER A 185 ? 0.7316 0.5852 0.6130 0.0941  -0.0465 0.0618  185 SER A N   
712  C CA  . SER A 185 ? 0.7179 0.5441 0.5864 0.0923  -0.0417 0.0640  185 SER A CA  
713  C C   . SER A 185 ? 0.7683 0.5968 0.6464 0.0796  -0.0336 0.0599  185 SER A C   
714  O O   . SER A 185 ? 0.7503 0.5990 0.6421 0.0723  -0.0310 0.0561  185 SER A O   
715  C CB  . SER A 185 ? 0.9093 0.7108 0.7532 0.0900  -0.0414 0.0713  185 SER A CB  
716  O OG  . SER A 185 ? 0.8125 0.6207 0.6545 0.0787  -0.0370 0.0720  185 SER A OG  
717  N N   . TYR A 186 ? 0.7618 0.5682 0.6314 0.0771  -0.0301 0.0606  186 TYR A N   
718  C CA  . TYR A 186 ? 0.6889 0.4959 0.5654 0.0639  -0.0230 0.0577  186 TYR A CA  
719  C C   . TYR A 186 ? 0.7179 0.5263 0.5893 0.0515  -0.0176 0.0609  186 TYR A C   
720  O O   . TYR A 186 ? 0.6712 0.4950 0.5551 0.0422  -0.0125 0.0576  186 TYR A O   
721  C CB  . TYR A 186 ? 0.7438 0.5235 0.6086 0.0628  -0.0216 0.0583  186 TYR A CB  
722  C CG  . TYR A 186 ? 0.8073 0.5855 0.6764 0.0474  -0.0151 0.0565  186 TYR A CG  
723  C CD1 . TYR A 186 ? 0.6845 0.4826 0.5731 0.0443  -0.0131 0.0499  186 TYR A CD1 
724  C CD2 . TYR A 186 ? 0.8086 0.5669 0.6622 0.0355  -0.0111 0.0618  186 TYR A CD2 
725  C CE1 . TYR A 186 ? 0.7365 0.5352 0.6296 0.0306  -0.0080 0.0484  186 TYR A CE1 
726  C CE2 . TYR A 186 ? 0.7517 0.5124 0.6109 0.0206  -0.0057 0.0605  186 TYR A CE2 
727  C CZ  . TYR A 186 ? 0.6408 0.4221 0.5200 0.0187  -0.0044 0.0536  186 TYR A CZ  
728  O OH  . TYR A 186 ? 0.7133 0.4989 0.5986 0.0044  0.0001  0.0525  186 TYR A OH  
729  N N   . GLU A 187 ? 0.6777 0.4708 0.5302 0.0521  -0.0186 0.0674  187 GLU A N   
730  C CA  . GLU A 187 ? 0.7298 0.5253 0.5756 0.0418  -0.0129 0.0708  187 GLU A CA  
731  C C   . GLU A 187 ? 0.6618 0.4847 0.5218 0.0414  -0.0124 0.0664  187 GLU A C   
732  O O   . GLU A 187 ? 0.7321 0.5649 0.5959 0.0324  -0.0058 0.0658  187 GLU A O   
733  C CB  . GLU A 187 ? 0.8124 0.5871 0.6338 0.0448  -0.0152 0.0786  187 GLU A CB  
734  C CG  . GLU A 187 ? 1.0095 0.7828 0.8198 0.0339  -0.0082 0.0834  187 GLU A CG  
735  C CD  . GLU A 187 ? 1.1461 0.9111 0.9547 0.0195  -0.0001 0.0856  187 GLU A CD  
736  O OE1 . GLU A 187 ? 1.1769 0.9213 0.9794 0.0180  -0.0015 0.0869  187 GLU A OE1 
737  O OE2 . GLU A 187 ? 1.1959 0.9750 1.0085 0.0097  0.0074  0.0861  187 GLU A OE2 
738  N N   . GLN A 188 ? 0.6613 0.4969 0.5290 0.0510  -0.0194 0.0634  188 GLN A N   
739  C CA  . GLN A 188 ? 0.5651 0.4227 0.4433 0.0501  -0.0200 0.0593  188 GLN A CA  
740  C C   . GLN A 188 ? 0.5762 0.4503 0.4742 0.0450  -0.0163 0.0530  188 GLN A C   
741  O O   . GLN A 188 ? 0.5150 0.4013 0.4180 0.0401  -0.0128 0.0503  188 GLN A O   
742  C CB  . GLN A 188 ? 0.7504 0.6168 0.6302 0.0599  -0.0294 0.0586  188 GLN A CB  
743  C CG  . GLN A 188 ? 0.7428 0.5946 0.6024 0.0656  -0.0342 0.0648  188 GLN A CG  
744  C CD  . GLN A 188 ? 0.7663 0.6298 0.6295 0.0754  -0.0446 0.0644  188 GLN A CD  
745  O OE1 . GLN A 188 ? 0.8697 0.7286 0.7320 0.0850  -0.0498 0.0665  188 GLN A OE1 
746  N NE2 . GLN A 188 ? 0.8712 0.7499 0.7378 0.0730  -0.0478 0.0617  188 GLN A NE2 
747  N N   . ILE A 189 ? 0.4973 0.3710 0.4052 0.0469  -0.0170 0.0505  189 ILE A N   
748  C CA  . ILE A 189 ? 0.5596 0.4465 0.4842 0.0416  -0.0133 0.0451  189 ILE A CA  
749  C C   . ILE A 189 ? 0.5494 0.4336 0.4722 0.0309  -0.0055 0.0462  189 ILE A C   
750  O O   . ILE A 189 ? 0.5615 0.4607 0.4949 0.0262  -0.0019 0.0428  189 ILE A O   
751  C CB  . ILE A 189 ? 0.5605 0.4445 0.4924 0.0461  -0.0153 0.0425  189 ILE A CB  
752  C CG1 . ILE A 189 ? 0.6899 0.5851 0.6284 0.0567  -0.0223 0.0409  189 ILE A CG1 
753  C CG2 . ILE A 189 ? 0.6483 0.5427 0.5945 0.0395  -0.0113 0.0375  189 ILE A CG2 
754  C CD1 . ILE A 189 ? 0.6548 0.5731 0.6069 0.0547  -0.0239 0.0370  189 ILE A CD1 
755  N N   . LEU A 190 ? 0.5396 0.4050 0.4485 0.0269  -0.0028 0.0514  190 LEU A N   
756  C CA  . LEU A 190 ? 0.5630 0.4285 0.4699 0.0154  0.0048  0.0537  190 LEU A CA  
757  C C   . LEU A 190 ? 0.5547 0.4351 0.4619 0.0138  0.0087  0.0538  190 LEU A C   
758  O O   . LEU A 190 ? 0.5488 0.4430 0.4649 0.0074  0.0145  0.0522  190 LEU A O   
759  C CB  . LEU A 190 ? 0.6419 0.4829 0.5299 0.0108  0.0064  0.0607  190 LEU A CB  
760  C CG  . LEU A 190 ? 0.7077 0.5312 0.5929 0.0058  0.0061  0.0610  190 LEU A CG  
761  C CD1 . LEU A 190 ? 0.6811 0.4775 0.5437 0.0004  0.0074  0.0688  190 LEU A CD1 
762  C CD2 . LEU A 190 ? 0.6103 0.4481 0.5103 -0.0050 0.0109  0.0577  190 LEU A CD2 
763  N N   . GLY A 191 ? 0.5259 0.4036 0.4226 0.0203  0.0052  0.0555  191 GLY A N   
764  C CA  . GLY A 191 ? 0.4895 0.3769 0.3818 0.0204  0.0082  0.0552  191 GLY A CA  
765  C C   . GLY A 191 ? 0.5053 0.4083 0.4083 0.0250  0.0048  0.0489  191 GLY A C   
766  O O   . GLY A 191 ? 0.6124 0.5196 0.5082 0.0267  0.0058  0.0480  191 GLY A O   
767  N N   . THR A 192 ? 0.4794 0.3893 0.3972 0.0270  0.0007  0.0444  192 THR A N   
768  C CA  . THR A 192 ? 0.4276 0.3510 0.3552 0.0297  -0.0026 0.0388  192 THR A CA  
769  C C   . THR A 192 ? 0.4787 0.4137 0.4211 0.0254  0.0019  0.0349  192 THR A C   
770  O O   . THR A 192 ? 0.4964 0.4304 0.4465 0.0221  0.0038  0.0351  192 THR A O   
771  C CB  . THR A 192 ? 0.4889 0.4141 0.4220 0.0352  -0.0111 0.0372  192 THR A CB  
772  O OG1 . THR A 192 ? 0.5413 0.4564 0.4611 0.0399  -0.0159 0.0415  192 THR A OG1 
773  C CG2 . THR A 192 ? 0.4218 0.3590 0.3616 0.0359  -0.0151 0.0325  192 THR A CG2 
774  N N   . ARG A 193 ? 0.4491 0.3934 0.3938 0.0260  0.0032  0.0314  193 ARG A N   
775  C CA  . ARG A 193 ? 0.4084 0.3641 0.3657 0.0232  0.0072  0.0280  193 ARG A CA  
776  C C   . ARG A 193 ? 0.4181 0.3781 0.3891 0.0229  0.0033  0.0248  193 ARG A C   
777  O O   . ARG A 193 ? 0.3587 0.3193 0.3315 0.0259  -0.0028 0.0229  193 ARG A O   
778  C CB  . ARG A 193 ? 0.3981 0.3594 0.3520 0.0262  0.0081  0.0246  193 ARG A CB  
779  C CG  . ARG A 193 ? 0.3742 0.3474 0.3392 0.0251  0.0125  0.0217  193 ARG A CG  
780  C CD  . ARG A 193 ? 0.4331 0.4077 0.3928 0.0301  0.0116  0.0177  193 ARG A CD  
781  N NE  . ARG A 193 ? 0.5242 0.4964 0.4697 0.0334  0.0164  0.0190  193 ARG A NE  
782  C CZ  . ARG A 193 ? 0.4203 0.3823 0.3499 0.0374  0.0131  0.0178  193 ARG A CZ  
783  N NH1 . ARG A 193 ? 0.4899 0.4445 0.4166 0.0375  0.0045  0.0156  193 ARG A NH1 
784  N NH2 . ARG A 193 ? 0.5024 0.4624 0.4181 0.0409  0.0185  0.0188  193 ARG A NH2 
785  N N   . GLN A 194 ? 0.3548 0.3187 0.3351 0.0185  0.0068  0.0245  194 GLN A N   
786  C CA  . GLN A 194 ? 0.3453 0.3136 0.3375 0.0180  0.0042  0.0212  194 GLN A CA  
787  C C   . GLN A 194 ? 0.3170 0.2973 0.3178 0.0174  0.0055  0.0174  194 GLN A C   
788  O O   . GLN A 194 ? 0.3785 0.3653 0.3805 0.0153  0.0104  0.0179  194 GLN A O   
789  C CB  . GLN A 194 ? 0.3497 0.3123 0.3445 0.0134  0.0061  0.0226  194 GLN A CB  
790  C CG  . GLN A 194 ? 0.4081 0.3737 0.4129 0.0136  0.0035  0.0188  194 GLN A CG  
791  C CD  . GLN A 194 ? 0.4936 0.4516 0.4987 0.0083  0.0052  0.0194  194 GLN A CD  
792  O OE1 . GLN A 194 ? 0.4333 0.3827 0.4310 0.0035  0.0080  0.0232  194 GLN A OE1 
793  N NE2 . GLN A 194 ? 0.4028 0.3625 0.4147 0.0084  0.0034  0.0158  194 GLN A NE2 
794  N N   . ILE A 195 ? 0.3574 0.3413 0.3638 0.0194  0.0012  0.0141  195 ILE A N   
795  C CA  . ILE A 195 ? 0.3981 0.3907 0.4116 0.0190  0.0016  0.0108  195 ILE A CA  
796  C C   . ILE A 195 ? 0.3534 0.3495 0.3769 0.0157  0.0020  0.0095  195 ILE A C   
797  O O   . ILE A 195 ? 0.3564 0.3510 0.3830 0.0163  -0.0011 0.0084  195 ILE A O   
798  C CB  . ILE A 195 ? 0.4388 0.4313 0.4504 0.0214  -0.0034 0.0084  195 ILE A CB  
799  C CG1 . ILE A 195 ? 0.3839 0.3698 0.3831 0.0239  -0.0053 0.0095  195 ILE A CG1 
800  C CG2 . ILE A 195 ? 0.3131 0.3108 0.3282 0.0217  -0.0029 0.0055  195 ILE A CG2 
801  C CD1 . ILE A 195 ? 0.3276 0.3126 0.3192 0.0259  -0.0004 0.0099  195 ILE A CD1 
802  N N   . VAL A 196 ? 0.3013 0.3034 0.3295 0.0122  0.0059  0.0097  196 VAL A N   
803  C CA  . VAL A 196 ? 0.3487 0.3527 0.3841 0.0078  0.0061  0.0086  196 VAL A CA  
804  C C   . VAL A 196 ? 0.3361 0.3494 0.3790 0.0085  0.0046  0.0053  196 VAL A C   
805  O O   . VAL A 196 ? 0.4049 0.4256 0.4486 0.0108  0.0058  0.0048  196 VAL A O   
806  C CB  . VAL A 196 ? 0.4007 0.4064 0.4367 0.0015  0.0103  0.0114  196 VAL A CB  
807  C CG1 . VAL A 196 ? 0.3592 0.3644 0.4006 -0.0043 0.0094  0.0100  196 VAL A CG1 
808  C CG2 . VAL A 196 ? 0.4074 0.4015 0.4334 0.0007  0.0118  0.0154  196 VAL A CG2 
809  N N   . VAL A 197 ? 0.4306 0.4426 0.4773 0.0073  0.0021  0.0031  197 VAL A N   
810  C CA  . VAL A 197 ? 0.3718 0.3911 0.4241 0.0073  0.0005  0.0003  197 VAL A CA  
811  C C   . VAL A 197 ? 0.3643 0.3877 0.4218 0.0019  0.0014  -0.0003 197 VAL A C   
812  O O   . VAL A 197 ? 0.4259 0.4418 0.4819 -0.0012 0.0009  -0.0008 197 VAL A O   
813  C CB  . VAL A 197 ? 0.3927 0.4093 0.4447 0.0093  -0.0027 -0.0016 197 VAL A CB  
814  C CG1 . VAL A 197 ? 0.3891 0.4117 0.4449 0.0088  -0.0043 -0.0039 197 VAL A CG1 
815  C CG2 . VAL A 197 ? 0.3364 0.3504 0.3836 0.0127  -0.0045 -0.0006 197 VAL A CG2 
816  N N   . ALA A 198 ? 0.3644 0.3993 0.4271 0.0011  0.0023  -0.0003 198 ALA A N   
817  C CA  . ALA A 198 ? 0.4175 0.4593 0.4862 -0.0051 0.0022  -0.0008 198 ALA A CA  
818  C C   . ALA A 198 ? 0.5517 0.6080 0.6266 -0.0025 0.0013  -0.0017 198 ALA A C   
819  O O   . ALA A 198 ? 0.6632 0.7262 0.7382 0.0028  0.0032  -0.0006 198 ALA A O   
820  C CB  . ALA A 198 ? 0.3945 0.4376 0.4636 -0.0117 0.0054  0.0023  198 ALA A CB  
821  N N   . SER A 199 ? 0.6409 0.7007 0.7193 -0.0052 -0.0018 -0.0038 199 SER A N   
822  C CA  . SER A 199 ? 0.6354 0.7090 0.7195 -0.0025 -0.0037 -0.0045 199 SER A CA  
823  C C   . SER A 199 ? 0.5684 0.6588 0.6594 -0.0022 -0.0005 -0.0019 199 SER A C   
824  O O   . SER A 199 ? 0.6395 0.7336 0.7332 -0.0089 0.0022  0.0003  199 SER A O   
825  C CB  . SER A 199 ? 0.6747 0.7504 0.7613 -0.0080 -0.0075 -0.0065 199 SER A CB  
826  O OG  . SER A 199 ? 0.6556 0.7204 0.7360 -0.0056 -0.0100 -0.0090 199 SER A OG  
827  N N   . ARG A 200 ? 0.6956 0.7959 0.7884 0.0061  -0.0007 -0.0019 200 ARG A N   
828  C CA  . ARG A 200 ? 0.7754 0.8944 0.8748 0.0093  0.0030  0.0003  200 ARG A CA  
829  C C   . ARG A 200 ? 0.7414 0.8819 0.8531 0.0038  0.0013  0.0011  200 ARG A C   
830  O O   . ARG A 200 ? 0.8581 1.0102 0.9767 -0.0048 0.0039  0.0036  200 ARG A O   
831  C CB  . ARG A 200 ? 0.8577 0.9765 0.9518 0.0223  0.0033  -0.0004 200 ARG A CB  
832  C CG  . ARG A 200 ? 0.8370 0.9492 0.9273 0.0271  -0.0023 -0.0027 200 ARG A CG  
833  C CD  . ARG A 200 ? 0.9378 1.0546 1.0246 0.0400  -0.0027 -0.0030 200 ARG A CD  
834  N NE  . ARG A 200 ? 0.8952 1.0076 0.9788 0.0434  -0.0085 -0.0043 200 ARG A NE  
835  C CZ  . ARG A 200 ? 0.9781 1.1045 1.0659 0.0510  -0.0107 -0.0040 200 ARG A CZ  
836  N NH1 . ARG A 200 ? 0.9694 1.1173 1.0656 0.0571  -0.0073 -0.0026 200 ARG A NH1 
837  N NH2 . ARG A 200 ? 0.8758 0.9954 0.9587 0.0530  -0.0165 -0.0048 200 ARG A NH2 
838  N N   . THR A 203 ? 0.7538 0.8743 0.8619 -0.0499 0.0091  0.0112  203 THR A N   
839  C CA  . THR A 203 ? 0.9493 1.0656 1.0523 -0.0523 0.0149  0.0155  203 THR A CA  
840  C C   . THR A 203 ? 0.9486 1.0342 1.0371 -0.0573 0.0138  0.0156  203 THR A C   
841  O O   . THR A 203 ? 0.8601 0.9302 0.9436 -0.0607 0.0089  0.0124  203 THR A O   
842  C CB  . THR A 203 ? 0.9292 1.0699 1.0422 -0.0630 0.0186  0.0204  203 THR A CB  
843  O OG1 . THR A 203 ? 0.7813 0.9250 0.8984 -0.0767 0.0137  0.0200  203 THR A OG1 
844  C CG2 . THR A 203 ? 0.8177 0.9894 0.9435 -0.0532 0.0218  0.0210  203 THR A CG2 
845  N N   . LEU A 204 ? 0.8903 0.9670 0.9710 -0.0568 0.0183  0.0192  204 LEU A N   
846  C CA  . LEU A 204 ? 0.7553 0.8033 0.8214 -0.0539 0.0173  0.0189  204 LEU A CA  
847  C C   . LEU A 204 ? 0.7094 0.7399 0.7654 -0.0668 0.0174  0.0224  204 LEU A C   
848  O O   . LEU A 204 ? 0.6209 0.6557 0.6749 -0.0735 0.0220  0.0277  204 LEU A O   
849  C CB  . LEU A 204 ? 0.6966 0.7432 0.7579 -0.0435 0.0210  0.0204  204 LEU A CB  
850  C CG  . LEU A 204 ? 0.7041 0.7530 0.7676 -0.0305 0.0187  0.0161  204 LEU A CG  
851  C CD1 . LEU A 204 ? 0.6955 0.7471 0.7546 -0.0221 0.0224  0.0177  204 LEU A CD1 
852  C CD2 . LEU A 204 ? 0.7464 0.7750 0.8029 -0.0269 0.0140  0.0128  204 LEU A CD2 
853  N N   . LYS A 205 ? 0.6690 0.6781 0.7169 -0.0697 0.0125  0.0194  205 LYS A N   
854  C CA  . LYS A 205 ? 0.5681 0.5530 0.6019 -0.0804 0.0116  0.0221  205 LYS A CA  
855  C C   . LYS A 205 ? 0.4529 0.4154 0.4724 -0.0728 0.0131  0.0244  205 LYS A C   
856  O O   . LYS A 205 ? 0.4755 0.4377 0.4954 -0.0592 0.0128  0.0221  205 LYS A O   
857  C CB  . LYS A 205 ? 0.5962 0.5639 0.6237 -0.0841 0.0056  0.0172  205 LYS A CB  
858  C CG  . LYS A 205 ? 0.6259 0.5820 0.6496 -0.0695 0.0030  0.0118  205 LYS A CG  
859  C CD  . LYS A 205 ? 0.7352 0.6890 0.7597 -0.0711 -0.0018 0.0060  205 LYS A CD  
860  C CE  . LYS A 205 ? 0.8251 0.7484 0.8320 -0.0785 -0.0053 0.0046  205 LYS A CE  
861  N NZ  . LYS A 205 ? 0.8973 0.8207 0.9042 -0.0841 -0.0101 -0.0005 205 LYS A NZ  
862  N N   . PRO A 206 ? 0.5126 0.4559 0.5184 -0.0820 0.0142  0.0293  206 PRO A N   
863  C CA  . PRO A 206 ? 0.5386 0.4605 0.5296 -0.0743 0.0152  0.0322  206 PRO A CA  
864  C C   . PRO A 206 ? 0.5648 0.4663 0.5477 -0.0614 0.0106  0.0275  206 PRO A C   
865  O O   . PRO A 206 ? 0.4381 0.3290 0.4130 -0.0513 0.0107  0.0290  206 PRO A O   
866  C CB  . PRO A 206 ? 0.4676 0.3689 0.4434 -0.0888 0.0160  0.0381  206 PRO A CB  
867  C CG  . PRO A 206 ? 0.5312 0.4531 0.5181 -0.1050 0.0175  0.0397  206 PRO A CG  
868  C CD  . PRO A 206 ? 0.4822 0.4249 0.4857 -0.1006 0.0147  0.0332  206 PRO A CD  
869  N N   . GLU A 207 ? 0.4721 0.3694 0.4567 -0.0612 0.0067  0.0219  207 GLU A N   
870  C CA  . GLU A 207 ? 0.4308 0.3118 0.4084 -0.0484 0.0033  0.0174  207 GLU A CA  
871  C C   . GLU A 207 ? 0.4666 0.3665 0.4560 -0.0349 0.0037  0.0148  207 GLU A C   
872  O O   . GLU A 207 ? 0.4778 0.3685 0.4626 -0.0234 0.0017  0.0125  207 GLU A O   
873  C CB  . GLU A 207 ? 0.5158 0.3862 0.4898 -0.0522 -0.0005 0.0121  207 GLU A CB  
874  C CG  . GLU A 207 ? 0.5431 0.3841 0.4987 -0.0637 -0.0026 0.0138  207 GLU A CG  
875  C CD  . GLU A 207 ? 0.6187 0.4713 0.5800 -0.0827 -0.0019 0.0167  207 GLU A CD  
876  O OE1 . GLU A 207 ? 0.5825 0.4673 0.5624 -0.0851 0.0008  0.0179  207 GLU A OE1 
877  O OE2 . GLU A 207 ? 0.6387 0.4682 0.5853 -0.0952 -0.0044 0.0179  207 GLU A OE2 
878  N N   . LEU A 208 ? 0.4047 0.3307 0.4085 -0.0359 0.0061  0.0153  208 LEU A N   
879  C CA  . LEU A 208 ? 0.4600 0.4011 0.4726 -0.0248 0.0060  0.0131  208 LEU A CA  
880  C C   . LEU A 208 ? 0.4739 0.4180 0.4840 -0.0201 0.0084  0.0171  208 LEU A C   
881  O O   . LEU A 208 ? 0.5031 0.4568 0.5179 -0.0118 0.0076  0.0156  208 LEU A O   
882  C CB  . LEU A 208 ? 0.5338 0.4984 0.5610 -0.0268 0.0064  0.0105  208 LEU A CB  
883  C CG  . LEU A 208 ? 0.5891 0.5542 0.6194 -0.0329 0.0039  0.0068  208 LEU A CG  
884  C CD1 . LEU A 208 ? 0.4470 0.4365 0.4911 -0.0352 0.0043  0.0057  208 LEU A CD1 
885  C CD2 . LEU A 208 ? 0.3815 0.3355 0.4074 -0.0255 0.0008  0.0022  208 LEU A CD2 
886  N N   . LEU A 209 ? 0.4269 0.3620 0.4282 -0.0260 0.0109  0.0222  209 LEU A N   
887  C CA  . LEU A 209 ? 0.4443 0.3831 0.4418 -0.0229 0.0137  0.0263  209 LEU A CA  
888  C C   . LEU A 209 ? 0.4396 0.3548 0.4210 -0.0192 0.0120  0.0297  209 LEU A C   
889  O O   . LEU A 209 ? 0.4998 0.3962 0.4703 -0.0260 0.0119  0.0324  209 LEU A O   
890  C CB  . LEU A 209 ? 0.4776 0.4293 0.4782 -0.0326 0.0190  0.0302  209 LEU A CB  
891  C CG  . LEU A 209 ? 0.4987 0.4752 0.5154 -0.0352 0.0204  0.0273  209 LEU A CG  
892  C CD1 . LEU A 209 ? 0.5172 0.5083 0.5379 -0.0457 0.0257  0.0316  209 LEU A CD1 
893  C CD2 . LEU A 209 ? 0.5077 0.4975 0.5308 -0.0242 0.0201  0.0241  209 LEU A CD2 
894  N N   . PHE A 210 ? 0.4939 0.4092 0.4727 -0.0089 0.0101  0.0298  210 PHE A N   
895  C CA  . PHE A 210 ? 0.4503 0.3455 0.4146 -0.0029 0.0074  0.0328  210 PHE A CA  
896  C C   . PHE A 210 ? 0.4837 0.3797 0.4403 -0.0003 0.0087  0.0373  210 PHE A C   
897  O O   . PHE A 210 ? 0.5068 0.3863 0.4502 0.0049  0.0061  0.0406  210 PHE A O   
898  C CB  . PHE A 210 ? 0.4019 0.2958 0.3691 0.0084  0.0024  0.0288  210 PHE A CB  
899  C CG  . PHE A 210 ? 0.4717 0.3615 0.4428 0.0075  0.0011  0.0244  210 PHE A CG  
900  C CD1 . PHE A 210 ? 0.4137 0.3212 0.3989 0.0049  0.0018  0.0198  210 PHE A CD1 
901  C CD2 . PHE A 210 ? 0.4359 0.3021 0.3944 0.0099  -0.0009 0.0247  210 PHE A CD2 
902  C CE1 . PHE A 210 ? 0.4996 0.4027 0.4867 0.0041  0.0006  0.0156  210 PHE A CE1 
903  C CE2 . PHE A 210 ? 0.5072 0.3677 0.4668 0.0096  -0.0020 0.0200  210 PHE A CE2 
904  C CZ  . PHE A 210 ? 0.4302 0.3098 0.4043 0.0063  -0.0012 0.0155  210 PHE A CZ  
905  N N   . SER A 211 ? 0.4841 0.3976 0.4469 -0.0028 0.0125  0.0373  211 SER A N   
906  C CA  . SER A 211 ? 0.5250 0.4392 0.4787 -0.0006 0.0144  0.0411  211 SER A CA  
907  C C   . SER A 211 ? 0.4834 0.4068 0.4373 -0.0098 0.0217  0.0443  211 SER A C   
908  O O   . SER A 211 ? 0.5141 0.4499 0.4793 -0.0164 0.0245  0.0426  211 SER A O   
909  C CB  . SER A 211 ? 0.4861 0.4128 0.4449 0.0077  0.0116  0.0375  211 SER A CB  
910  O OG  . SER A 211 ? 0.4844 0.4065 0.4442 0.0154  0.0050  0.0353  211 SER A OG  
911  N N   . LYS A 212 ? 0.5576 0.4763 0.4986 -0.0099 0.0246  0.0492  212 LYS A N   
912  C CA  . LYS A 212 ? 0.5190 0.4490 0.4595 -0.0180 0.0326  0.0529  212 LYS A CA  
913  C C   . LYS A 212 ? 0.4645 0.4193 0.4184 -0.0149 0.0359  0.0486  212 LYS A C   
914  O O   . LYS A 212 ? 0.4766 0.4481 0.4394 -0.0216 0.0417  0.0495  212 LYS A O   
915  C CB  . LYS A 212 ? 0.5560 0.4753 0.4779 -0.0176 0.0353  0.0590  212 LYS A CB  
916  C CG  . LYS A 212 ? 0.6532 0.5501 0.5606 -0.0256 0.0355  0.0657  212 LYS A CG  
917  C CD  . LYS A 212 ? 0.7531 0.6340 0.6396 -0.0212 0.0349  0.0709  212 LYS A CD  
918  C CE  . LYS A 212 ? 0.8395 0.6907 0.7106 -0.0209 0.0294  0.0749  212 LYS A CE  
919  N NZ  . LYS A 212 ? 0.8836 0.7216 0.7455 -0.0351 0.0338  0.0813  212 LYS A NZ  
920  N N   . HIS A 213 ? 0.4410 0.3987 0.3961 -0.0048 0.0320  0.0440  213 HIS A N   
921  C CA  . HIS A 213 ? 0.5340 0.5100 0.4978 -0.0002 0.0342  0.0397  213 HIS A CA  
922  C C   . HIS A 213 ? 0.4552 0.4338 0.4301 0.0042  0.0280  0.0337  213 HIS A C   
923  O O   . HIS A 213 ? 0.4508 0.4179 0.4234 0.0073  0.0217  0.0325  213 HIS A O   
924  C CB  . HIS A 213 ? 0.4372 0.4117 0.3878 0.0071  0.0355  0.0398  213 HIS A CB  
925  C CG  . HIS A 213 ? 0.5555 0.5302 0.4946 0.0033  0.0429  0.0457  213 HIS A CG  
926  N ND1 . HIS A 213 ? 0.7008 0.6937 0.6464 -0.0014 0.0515  0.0477  213 HIS A ND1 
927  C CD2 . HIS A 213 ? 0.5751 0.5353 0.4964 0.0034  0.0432  0.0504  213 HIS A CD2 
928  C CE1 . HIS A 213 ? 0.6516 0.6417 0.5840 -0.0047 0.0574  0.0535  213 HIS A CE1 
929  N NE2 . HIS A 213 ? 0.7591 0.7279 0.6756 -0.0019 0.0524  0.0552  213 HIS A NE2 
930  N N   . TYR A 214 ? 0.3947 0.3892 0.3813 0.0050  0.0298  0.0302  214 TYR A N   
931  C CA  . TYR A 214 ? 0.3764 0.3734 0.3730 0.0077  0.0245  0.0251  214 TYR A CA  
932  C C   . TYR A 214 ? 0.3872 0.3986 0.3899 0.0123  0.0264  0.0216  214 TYR A C   
933  O O   . TYR A 214 ? 0.3671 0.3911 0.3715 0.0122  0.0324  0.0230  214 TYR A O   
934  C CB  . TYR A 214 ? 0.3343 0.3308 0.3403 0.0010  0.0231  0.0249  214 TYR A CB  
935  C CG  . TYR A 214 ? 0.4621 0.4731 0.4773 -0.0062 0.0280  0.0262  214 TYR A CG  
936  C CD1 . TYR A 214 ? 0.4623 0.4892 0.4897 -0.0050 0.0278  0.0228  214 TYR A CD1 
937  C CD2 . TYR A 214 ? 0.4078 0.4175 0.4193 -0.0149 0.0323  0.0314  214 TYR A CD2 
938  C CE1 . TYR A 214 ? 0.4989 0.5424 0.5361 -0.0115 0.0315  0.0242  214 TYR A CE1 
939  C CE2 . TYR A 214 ? 0.4431 0.4694 0.4643 -0.0231 0.0364  0.0330  214 TYR A CE2 
940  C CZ  . TYR A 214 ? 0.5624 0.6070 0.5974 -0.0210 0.0358  0.0293  214 TYR A CZ  
941  O OH  . TYR A 214 ? 0.7007 0.7651 0.7468 -0.0291 0.0392  0.0311  214 TYR A OH  
942  N N   . TRP A 215 ? 0.3378 0.3472 0.3431 0.0168  0.0210  0.0174  215 TRP A N   
943  C CA  . TRP A 215 ? 0.3310 0.3505 0.3423 0.0209  0.0211  0.0138  215 TRP A CA  
944  C C   . TRP A 215 ? 0.4194 0.4435 0.4431 0.0173  0.0180  0.0118  215 TRP A C   
945  O O   . TRP A 215 ? 0.3675 0.3839 0.3928 0.0140  0.0145  0.0117  215 TRP A O   
946  C CB  . TRP A 215 ? 0.3447 0.3555 0.3462 0.0278  0.0170  0.0107  215 TRP A CB  
947  C CG  . TRP A 215 ? 0.4214 0.4273 0.4086 0.0328  0.0198  0.0114  215 TRP A CG  
948  C CD1 . TRP A 215 ? 0.3940 0.4042 0.3766 0.0323  0.0263  0.0148  215 TRP A CD1 
949  C CD2 . TRP A 215 ? 0.4314 0.4260 0.4050 0.0384  0.0160  0.0085  215 TRP A CD2 
950  N NE1 . TRP A 215 ? 0.3955 0.3979 0.3620 0.0385  0.0271  0.0140  215 TRP A NE1 
951  C CE2 . TRP A 215 ? 0.4690 0.4607 0.4292 0.0423  0.0204  0.0099  215 TRP A CE2 
952  C CE3 . TRP A 215 ? 0.4398 0.4256 0.4100 0.0397  0.0091  0.0052  215 TRP A CE3 
953  C CZ2 . TRP A 215 ? 0.4488 0.4275 0.3913 0.0479  0.0177  0.0073  215 TRP A CZ2 
954  C CZ3 . TRP A 215 ? 0.5217 0.4946 0.4749 0.0439  0.0061  0.0030  215 TRP A CZ3 
955  C CH2 . TRP A 215 ? 0.5085 0.4772 0.4476 0.0483  0.0102  0.0038  215 TRP A CH2 
956  N N   . ARG A 216 ? 0.3629 0.3996 0.3944 0.0191  0.0193  0.0100  216 ARG A N   
957  C CA  . ARG A 216 ? 0.4354 0.4775 0.4776 0.0159  0.0164  0.0080  216 ARG A CA  
958  C C   . ARG A 216 ? 0.3972 0.4377 0.4382 0.0221  0.0125  0.0045  216 ARG A C   
959  O O   . ARG A 216 ? 0.4631 0.5061 0.4994 0.0290  0.0139  0.0035  216 ARG A O   
960  C CB  . ARG A 216 ? 0.4454 0.5047 0.4982 0.0115  0.0201  0.0096  216 ARG A CB  
961  C CG  . ARG A 216 ? 0.4846 0.5496 0.5475 0.0070  0.0168  0.0078  216 ARG A CG  
962  C CD  . ARG A 216 ? 0.4626 0.5483 0.5362 0.0028  0.0200  0.0095  216 ARG A CD  
963  N NE  . ARG A 216 ? 0.6886 0.7794 0.7707 -0.0034 0.0163  0.0081  216 ARG A NE  
964  C CZ  . ARG A 216 ? 0.7444 0.8503 0.8356 -0.0116 0.0174  0.0100  216 ARG A CZ  
965  N NH1 . ARG A 216 ? 0.7290 0.8472 0.8230 -0.0158 0.0228  0.0139  216 ARG A NH1 
966  N NH2 . ARG A 216 ? 0.7493 0.8586 0.8465 -0.0166 0.0129  0.0080  216 ARG A NH2 
967  N N   . THR A 217 ? 0.3311 0.3662 0.3746 0.0198  0.0079  0.0027  217 THR A N   
968  C CA  . THR A 217 ? 0.3938 0.4269 0.4363 0.0233  0.0040  0.0000  217 THR A CA  
969  C C   . THR A 217 ? 0.3850 0.4224 0.4361 0.0188  0.0018  -0.0011 217 THR A C   
970  O O   . THR A 217 ? 0.3572 0.3949 0.4127 0.0134  0.0025  -0.0003 217 THR A O   
971  C CB  . THR A 217 ? 0.3403 0.3603 0.3733 0.0247  0.0001  -0.0008 217 THR A CB  
972  O OG1 . THR A 217 ? 0.5495 0.5658 0.5788 0.0274  -0.0033 -0.0028 217 THR A OG1 
973  C CG2 . THR A 217 ? 0.3868 0.4034 0.4229 0.0199  -0.0021 -0.0003 217 THR A CG2 
974  N N   . ASP A 218 ? 0.3816 0.4203 0.4331 0.0214  -0.0009 -0.0029 218 ASP A N   
975  C CA  . ASP A 218 ? 0.4751 0.5187 0.5335 0.0176  -0.0029 -0.0040 218 ASP A CA  
976  C C   . ASP A 218 ? 0.4573 0.4927 0.5125 0.0160  -0.0065 -0.0053 218 ASP A C   
977  O O   . ASP A 218 ? 0.4239 0.4622 0.4823 0.0138  -0.0082 -0.0064 218 ASP A O   
978  C CB  . ASP A 218 ? 0.4182 0.4727 0.4807 0.0211  -0.0034 -0.0045 218 ASP A CB  
979  C CG  . ASP A 218 ? 0.4970 0.5448 0.5509 0.0285  -0.0058 -0.0053 218 ASP A CG  
980  O OD1 . ASP A 218 ? 0.5145 0.5489 0.5590 0.0292  -0.0074 -0.0056 218 ASP A OD1 
981  O OD2 . ASP A 218 ? 0.4783 0.5337 0.5340 0.0335  -0.0067 -0.0056 218 ASP A OD2 
982  N N   . ASN A 219 ? 0.3566 0.3833 0.4053 0.0166  -0.0077 -0.0049 219 ASN A N   
983  C CA  . ASN A 219 ? 0.4246 0.4476 0.4722 0.0139  -0.0103 -0.0055 219 ASN A CA  
984  C C   . ASN A 219 ? 0.4145 0.4327 0.4584 0.0134  -0.0111 -0.0044 219 ASN A C   
985  O O   . ASN A 219 ? 0.4207 0.4351 0.4597 0.0155  -0.0107 -0.0035 219 ASN A O   
986  C CB  . ASN A 219 ? 0.4730 0.4930 0.5157 0.0146  -0.0134 -0.0061 219 ASN A CB  
987  C CG  . ASN A 219 ? 0.4357 0.4460 0.4680 0.0165  -0.0156 -0.0055 219 ASN A CG  
988  O OD1 . ASN A 219 ? 0.4793 0.4847 0.5073 0.0130  -0.0181 -0.0049 219 ASN A OD1 
989  N ND2 . ASN A 219 ? 0.5305 0.5382 0.5581 0.0220  -0.0148 -0.0058 219 ASN A ND2 
990  N N   . HIS A 220 ? 0.4324 0.4522 0.4785 0.0110  -0.0123 -0.0044 220 HIS A N   
991  C CA  . HIS A 220 ? 0.3881 0.4075 0.4336 0.0110  -0.0133 -0.0031 220 HIS A CA  
992  C C   . HIS A 220 ? 0.3793 0.3950 0.4179 0.0095  -0.0169 -0.0022 220 HIS A C   
993  O O   . HIS A 220 ? 0.3774 0.3922 0.4137 0.0097  -0.0184 -0.0009 220 HIS A O   
994  C CB  . HIS A 220 ? 0.3274 0.3526 0.3784 0.0104  -0.0129 -0.0036 220 HIS A CB  
995  C CG  . HIS A 220 ? 0.4101 0.4343 0.4642 0.0117  -0.0101 -0.0047 220 HIS A CG  
996  N ND1 . HIS A 220 ? 0.3616 0.3811 0.4146 0.0136  -0.0088 -0.0036 220 HIS A ND1 
997  C CD2 . HIS A 220 ? 0.2882 0.3131 0.3444 0.0107  -0.0089 -0.0067 220 HIS A CD2 
998  C CE1 . HIS A 220 ? 0.2903 0.3067 0.3443 0.0132  -0.0069 -0.0049 220 HIS A CE1 
999  N NE2 . HIS A 220 ? 0.4420 0.4619 0.4980 0.0114  -0.0071 -0.0070 220 HIS A NE2 
1000 N N   . HIS A 221 ? 0.4048 0.4170 0.4388 0.0076  -0.0189 -0.0027 221 HIS A N   
1001 C CA  . HIS A 221 ? 0.3962 0.4005 0.4204 0.0050  -0.0229 -0.0019 221 HIS A CA  
1002 C C   . HIS A 221 ? 0.3491 0.3445 0.3648 0.0090  -0.0229 -0.0023 221 HIS A C   
1003 O O   . HIS A 221 ? 0.3841 0.3751 0.3935 0.0076  -0.0257 -0.0016 221 HIS A O   
1004 C CB  . HIS A 221 ? 0.4539 0.4519 0.4716 0.0023  -0.0252 -0.0022 221 HIS A CB  
1005 C CG  . HIS A 221 ? 0.4294 0.4133 0.4328 -0.0002 -0.0297 -0.0018 221 HIS A CG  
1006 N ND1 . HIS A 221 ? 0.3656 0.3492 0.3657 -0.0074 -0.0337 -0.0002 221 HIS A ND1 
1007 C CD2 . HIS A 221 ? 0.4527 0.4214 0.4430 0.0037  -0.0311 -0.0029 221 HIS A CD2 
1008 C CE1 . HIS A 221 ? 0.3847 0.3512 0.3690 -0.0091 -0.0379 -0.0005 221 HIS A CE1 
1009 N NE2 . HIS A 221 ? 0.4748 0.4309 0.4520 -0.0016 -0.0362 -0.0023 221 HIS A NE2 
1010 N N   . SER A 222 ? 0.3642 0.3582 0.3794 0.0141  -0.0197 -0.0034 222 SER A N   
1011 C CA  . SER A 222 ? 0.4542 0.4422 0.4617 0.0190  -0.0182 -0.0037 222 SER A CA  
1012 C C   . SER A 222 ? 0.4112 0.4026 0.4213 0.0188  -0.0167 -0.0022 222 SER A C   
1013 O O   . SER A 222 ? 0.4115 0.3956 0.4117 0.0201  -0.0180 -0.0020 222 SER A O   
1014 C CB  . SER A 222 ? 0.4400 0.4324 0.4505 0.0245  -0.0142 -0.0045 222 SER A CB  
1015 O OG  . SER A 222 ? 0.5527 0.5399 0.5581 0.0266  -0.0164 -0.0057 222 SER A OG  
1016 N N   . ALA A 223 ? 0.3473 0.3474 0.3682 0.0174  -0.0144 -0.0013 223 ALA A N   
1017 C CA  . ALA A 223 ? 0.3353 0.3360 0.3569 0.0178  -0.0134 0.0005  223 ALA A CA  
1018 C C   . ALA A 223 ? 0.4259 0.4251 0.4438 0.0159  -0.0183 0.0014  223 ALA A C   
1019 O O   . ALA A 223 ? 0.3724 0.3674 0.3836 0.0173  -0.0194 0.0027  223 ALA A O   
1020 C CB  . ALA A 223 ? 0.3215 0.3281 0.3528 0.0170  -0.0107 0.0010  223 ALA A CB  
1021 N N   . CYS A 224 ? 0.3340 0.3380 0.3562 0.0124  -0.0213 0.0011  224 CYS A N   
1022 C CA  . CYS A 224 ? 0.3426 0.3498 0.3638 0.0094  -0.0262 0.0025  224 CYS A CA  
1023 C C   . CYS A 224 ? 0.3660 0.3627 0.3737 0.0075  -0.0305 0.0023  224 CYS A C   
1024 O O   . CYS A 224 ? 0.3910 0.3877 0.3947 0.0068  -0.0341 0.0036  224 CYS A O   
1025 C CB  . CYS A 224 ? 0.3368 0.3533 0.3653 0.0050  -0.0278 0.0025  224 CYS A CB  
1026 S SG  . CYS A 224 ? 0.4506 0.4787 0.4822 0.0003  -0.0336 0.0049  224 CYS A SG  
1027 N N   . LEU A 225 ? 0.3858 0.3723 0.3849 0.0074  -0.0305 0.0005  225 LEU A N   
1028 C CA  . LEU A 225 ? 0.3745 0.3466 0.3571 0.0065  -0.0345 -0.0004 225 LEU A CA  
1029 C C   . LEU A 225 ? 0.3830 0.3502 0.3582 0.0115  -0.0330 -0.0002 225 LEU A C   
1030 O O   . LEU A 225 ? 0.5027 0.4627 0.4667 0.0095  -0.0377 -0.0001 225 LEU A O   
1031 C CB  . LEU A 225 ? 0.3493 0.3092 0.3225 0.0087  -0.0338 -0.0026 225 LEU A CB  
1032 C CG  . LEU A 225 ? 0.4980 0.4544 0.4694 0.0024  -0.0374 -0.0026 225 LEU A CG  
1033 C CD1 . LEU A 225 ? 0.4589 0.4009 0.4191 0.0074  -0.0365 -0.0046 225 LEU A CD1 
1034 C CD2 . LEU A 225 ? 0.4442 0.3950 0.4071 -0.0066 -0.0446 -0.0015 225 LEU A CD2 
1035 N N   . MET A 226 ? 0.4031 0.3744 0.3836 0.0170  -0.0266 0.0001  226 MET A N   
1036 C CA  . MET A 226 ? 0.4830 0.4500 0.4555 0.0213  -0.0240 0.0008  226 MET A CA  
1037 C C   . MET A 226 ? 0.4862 0.4582 0.4622 0.0201  -0.0260 0.0036  226 MET A C   
1038 O O   . MET A 226 ? 0.4316 0.3972 0.3966 0.0217  -0.0274 0.0046  226 MET A O   
1039 C CB  . MET A 226 ? 0.4036 0.3748 0.3807 0.0260  -0.0164 0.0008  226 MET A CB  
1040 C CG  . MET A 226 ? 0.5037 0.4691 0.4732 0.0304  -0.0145 -0.0018 226 MET A CG  
1041 S SD  . MET A 226 ? 0.6182 0.5942 0.5946 0.0360  -0.0057 -0.0013 226 MET A SD  
1042 C CE  . MET A 226 ? 0.5849 0.5743 0.5812 0.0307  -0.0048 -0.0002 226 MET A CE  
1043 N N   . ILE A 227 ? 0.3645 0.3472 0.3542 0.0182  -0.0264 0.0049  227 ILE A N   
1044 C CA  . ILE A 227 ? 0.4276 0.4153 0.4201 0.0186  -0.0295 0.0075  227 ILE A CA  
1045 C C   . ILE A 227 ? 0.4459 0.4338 0.4324 0.0147  -0.0373 0.0078  227 ILE A C   
1046 O O   . ILE A 227 ? 0.4580 0.4452 0.4390 0.0159  -0.0410 0.0098  227 ILE A O   
1047 C CB  . ILE A 227 ? 0.3880 0.3865 0.3952 0.0191  -0.0279 0.0083  227 ILE A CB  
1048 C CG1 . ILE A 227 ? 0.4244 0.4208 0.4354 0.0214  -0.0212 0.0081  227 ILE A CG1 
1049 C CG2 . ILE A 227 ? 0.3524 0.3568 0.3622 0.0216  -0.0316 0.0109  227 ILE A CG2 
1050 C CD1 . ILE A 227 ? 0.3659 0.3693 0.3885 0.0214  -0.0195 0.0074  227 ILE A CD1 
1051 N N   . LEU A 228 ? 0.3991 0.3871 0.3853 0.0094  -0.0405 0.0061  228 LEU A N   
1052 C CA  . LEU A 228 ? 0.4439 0.4316 0.4236 0.0031  -0.0486 0.0065  228 LEU A CA  
1053 C C   . LEU A 228 ? 0.3989 0.3701 0.3589 0.0038  -0.0515 0.0054  228 LEU A C   
1054 O O   . LEU A 228 ? 0.4399 0.4105 0.3928 -0.0004 -0.0589 0.0063  228 LEU A O   
1055 C CB  . LEU A 228 ? 0.3626 0.3512 0.3441 -0.0042 -0.0510 0.0054  228 LEU A CB  
1056 C CG  . LEU A 228 ? 0.3970 0.4037 0.3960 -0.0067 -0.0497 0.0068  228 LEU A CG  
1057 C CD1 . LEU A 228 ? 0.3460 0.3486 0.3429 -0.0133 -0.0503 0.0057  228 LEU A CD1 
1058 C CD2 . LEU A 228 ? 0.3114 0.3355 0.3187 -0.0099 -0.0550 0.0095  228 LEU A CD2 
1059 N N   . ARG A 229 ? 0.4067 0.3653 0.3572 0.0090  -0.0461 0.0034  229 ARG A N   
1060 C CA  . ARG A 229 ? 0.4615 0.4041 0.3917 0.0116  -0.0473 0.0020  229 ARG A CA  
1061 C C   . ARG A 229 ? 0.4121 0.3561 0.3395 0.0167  -0.0449 0.0044  229 ARG A C   
1062 O O   . ARG A 229 ? 0.4557 0.3873 0.3662 0.0203  -0.0437 0.0034  229 ARG A O   
1063 C CB  . ARG A 229 ? 0.4016 0.3318 0.3221 0.0165  -0.0420 -0.0012 229 ARG A CB  
1064 C CG  . ARG A 229 ? 0.5557 0.4799 0.4749 0.0127  -0.0445 -0.0034 229 ARG A CG  
1065 C CD  . ARG A 229 ? 0.5108 0.4229 0.4158 0.0045  -0.0540 -0.0043 229 ARG A CD  
1066 N NE  . ARG A 229 ? 0.6145 0.5081 0.4963 0.0072  -0.0567 -0.0065 229 ARG A NE  
1067 C CZ  . ARG A 229 ? 0.6498 0.5209 0.5102 0.0098  -0.0579 -0.0102 229 ARG A CZ  
1068 N NH1 . ARG A 229 ? 0.6037 0.4677 0.4632 0.0113  -0.0562 -0.0118 229 ARG A NH1 
1069 N NH2 . ARG A 229 ? 0.5748 0.4287 0.4126 0.0121  -0.0609 -0.0124 229 ARG A NH2 
1070 N N   . ASN A 230 ? 0.3936 0.3509 0.3355 0.0175  -0.0440 0.0076  230 ASN A N   
1071 C CA  . ASN A 230 ? 0.4449 0.4018 0.3833 0.0220  -0.0423 0.0108  230 ASN A CA  
1072 C C   . ASN A 230 ? 0.4875 0.4386 0.4215 0.0268  -0.0331 0.0109  230 ASN A C   
1073 O O   . ASN A 230 ? 0.4757 0.4208 0.3991 0.0298  -0.0313 0.0132  230 ASN A O   
1074 C CB  . ASN A 230 ? 0.4085 0.3583 0.3309 0.0211  -0.0497 0.0115  230 ASN A CB  
1075 C CG  . ASN A 230 ? 0.5159 0.4763 0.4450 0.0157  -0.0593 0.0125  230 ASN A CG  
1076 O OD1 . ASN A 230 ? 0.5486 0.5233 0.4951 0.0139  -0.0594 0.0132  230 ASN A OD1 
1077 N ND2 . ASN A 230 ? 0.5844 0.5393 0.4996 0.0129  -0.0673 0.0126  230 ASN A ND2 
1078 N N   . LEU A 231 ? 0.3868 0.3406 0.3287 0.0272  -0.0274 0.0090  231 LEU A N   
1079 C CA  . LEU A 231 ? 0.4304 0.3833 0.3706 0.0308  -0.0187 0.0095  231 LEU A CA  
1080 C C   . LEU A 231 ? 0.3952 0.3549 0.3469 0.0304  -0.0143 0.0129  231 LEU A C   
1081 O O   . LEU A 231 ? 0.4488 0.4092 0.3997 0.0315  -0.0072 0.0143  231 LEU A O   
1082 C CB  . LEU A 231 ? 0.4310 0.3852 0.3743 0.0320  -0.0151 0.0061  231 LEU A CB  
1083 C CG  . LEU A 231 ? 0.4886 0.4307 0.4158 0.0338  -0.0184 0.0025  231 LEU A CG  
1084 C CD1 . LEU A 231 ? 0.4386 0.3813 0.3695 0.0359  -0.0160 -0.0005 231 LEU A CD1 
1085 C CD2 . LEU A 231 ? 0.4447 0.3777 0.3537 0.0388  -0.0153 0.0025  231 LEU A CD2 
1086 N N   . GLY A 232 ? 0.4345 0.3989 0.3957 0.0290  -0.0182 0.0143  232 GLY A N   
1087 C CA  . GLY A 232 ? 0.3755 0.3414 0.3436 0.0292  -0.0149 0.0172  232 GLY A CA  
1088 C C   . GLY A 232 ? 0.4508 0.4237 0.4314 0.0290  -0.0187 0.0168  232 GLY A C   
1089 O O   . GLY A 232 ? 0.4010 0.3798 0.3855 0.0280  -0.0240 0.0151  232 GLY A O   
1090 N N   . TRP A 233 ? 0.3169 0.2884 0.3025 0.0297  -0.0157 0.0185  233 TRP A N   
1091 C CA  . TRP A 233 ? 0.3906 0.3676 0.3869 0.0310  -0.0176 0.0177  233 TRP A CA  
1092 C C   . TRP A 233 ? 0.3382 0.3179 0.3432 0.0279  -0.0130 0.0154  233 TRP A C   
1093 O O   . TRP A 233 ? 0.4138 0.3915 0.4174 0.0250  -0.0083 0.0152  233 TRP A O   
1094 C CB  . TRP A 233 ? 0.3367 0.3066 0.3289 0.0356  -0.0189 0.0211  233 TRP A CB  
1095 C CG  . TRP A 233 ? 0.4352 0.3932 0.4222 0.0339  -0.0136 0.0232  233 TRP A CG  
1096 C CD1 . TRP A 233 ? 0.4147 0.3636 0.3907 0.0318  -0.0103 0.0263  233 TRP A CD1 
1097 C CD2 . TRP A 233 ? 0.3833 0.3368 0.3747 0.0330  -0.0110 0.0223  233 TRP A CD2 
1098 N NE1 . TRP A 233 ? 0.3711 0.3110 0.3452 0.0284  -0.0060 0.0280  233 TRP A NE1 
1099 C CE2 . TRP A 233 ? 0.4282 0.3695 0.4111 0.0290  -0.0067 0.0253  233 TRP A CE2 
1100 C CE3 . TRP A 233 ? 0.3554 0.3137 0.3561 0.0347  -0.0118 0.0192  233 TRP A CE3 
1101 C CZ2 . TRP A 233 ? 0.4666 0.3987 0.4493 0.0256  -0.0041 0.0253  233 TRP A CZ2 
1102 C CZ3 . TRP A 233 ? 0.4545 0.4029 0.4540 0.0329  -0.0090 0.0187  233 TRP A CZ3 
1103 C CH2 . TRP A 233 ? 0.4654 0.4002 0.4558 0.0279  -0.0056 0.0217  233 TRP A CH2 
1104 N N   . GLY A 234 ? 0.3847 0.3703 0.3988 0.0288  -0.0144 0.0135  234 GLY A N   
1105 C CA  . GLY A 234 ? 0.3273 0.3154 0.3487 0.0259  -0.0110 0.0110  234 GLY A CA  
1106 C C   . GLY A 234 ? 0.3794 0.3720 0.4077 0.0285  -0.0124 0.0093  234 GLY A C   
1107 O O   . GLY A 234 ? 0.4415 0.4385 0.4709 0.0330  -0.0158 0.0102  234 GLY A O   
1108 N N   . VAL A 235 ? 0.3735 0.3664 0.4064 0.0259  -0.0098 0.0069  235 VAL A N   
1109 C CA  . VAL A 235 ? 0.3500 0.3452 0.3874 0.0287  -0.0099 0.0048  235 VAL A CA  
1110 C C   . VAL A 235 ? 0.3542 0.3610 0.3989 0.0259  -0.0102 0.0021  235 VAL A C   
1111 O O   . VAL A 235 ? 0.3539 0.3610 0.3998 0.0213  -0.0087 0.0008  235 VAL A O   
1112 C CB  . VAL A 235 ? 0.4400 0.4229 0.4734 0.0275  -0.0072 0.0039  235 VAL A CB  
1113 C CG1 . VAL A 235 ? 0.4190 0.4024 0.4545 0.0313  -0.0072 0.0009  235 VAL A CG1 
1114 C CG2 . VAL A 235 ? 0.4156 0.3841 0.4393 0.0295  -0.0071 0.0073  235 VAL A CG2 
1115 N N   . LEU A 236 ? 0.3663 0.3833 0.4156 0.0287  -0.0122 0.0018  236 LEU A N   
1116 C CA  . LEU A 236 ? 0.3421 0.3700 0.3968 0.0252  -0.0128 0.0003  236 LEU A CA  
1117 C C   . LEU A 236 ? 0.3429 0.3777 0.4020 0.0285  -0.0113 -0.0015 236 LEU A C   
1118 O O   . LEU A 236 ? 0.3492 0.3846 0.4083 0.0354  -0.0112 -0.0011 236 LEU A O   
1119 C CB  . LEU A 236 ? 0.3486 0.3849 0.4042 0.0230  -0.0166 0.0022  236 LEU A CB  
1120 C CG  . LEU A 236 ? 0.3775 0.4064 0.4263 0.0204  -0.0184 0.0035  236 LEU A CG  
1121 C CD1 . LEU A 236 ? 0.3065 0.3421 0.3545 0.0169  -0.0232 0.0048  236 LEU A CD1 
1122 C CD2 . LEU A 236 ? 0.3440 0.3661 0.3901 0.0173  -0.0160 0.0019  236 LEU A CD2 
1123 N N   . PRO A 237 ? 0.3814 0.4211 0.4430 0.0250  -0.0101 -0.0034 237 PRO A N   
1124 C CA  . PRO A 237 ? 0.3471 0.3948 0.4117 0.0284  -0.0082 -0.0051 237 PRO A CA  
1125 C C   . PRO A 237 ? 0.3476 0.4123 0.4184 0.0309  -0.0095 -0.0030 237 PRO A C   
1126 O O   . PRO A 237 ? 0.3255 0.3978 0.3987 0.0256  -0.0125 -0.0007 237 PRO A O   
1127 C CB  . PRO A 237 ? 0.3318 0.3811 0.3964 0.0225  -0.0073 -0.0068 237 PRO A CB  
1128 C CG  . PRO A 237 ? 0.4242 0.4633 0.4855 0.0181  -0.0083 -0.0067 237 PRO A CG  
1129 C CD  . PRO A 237 ? 0.3180 0.3553 0.3784 0.0187  -0.0104 -0.0041 237 PRO A CD  
1130 N N   . GLN A 238 ? 0.3346 0.4052 0.4074 0.0392  -0.0076 -0.0039 238 GLN A N   
1131 C CA  . GLN A 238 ? 0.4217 0.5140 0.5026 0.0424  -0.0081 -0.0019 238 GLN A CA  
1132 C C   . GLN A 238 ? 0.3876 0.4947 0.4735 0.0337  -0.0078 -0.0010 238 GLN A C   
1133 O O   . GLN A 238 ? 0.3835 0.5088 0.4762 0.0303  -0.0100 0.0020  238 GLN A O   
1134 C CB  . GLN A 238 ? 0.3840 0.4798 0.4649 0.0545  -0.0048 -0.0038 238 GLN A CB  
1135 C CG  . GLN A 238 ? 0.4877 0.6104 0.5787 0.0604  -0.0046 -0.0017 238 GLN A CG  
1136 C CD  . GLN A 238 ? 0.6828 0.8165 0.7796 0.0592  -0.0099 0.0025  238 GLN A CD  
1137 O OE1 . GLN A 238 ? 0.6622 0.7823 0.7536 0.0634  -0.0128 0.0034  238 GLN A OE1 
1138 N NE2 . GLN A 238 ? 0.6390 0.7976 0.7459 0.0530  -0.0116 0.0054  238 GLN A NE2 
1139 N N   . GLU A 239 ? 0.4135 0.5125 0.4950 0.0292  -0.0055 -0.0033 239 GLU A N   
1140 C CA  . GLU A 239 ? 0.4031 0.5117 0.4861 0.0205  -0.0052 -0.0022 239 GLU A CA  
1141 C C   . GLU A 239 ? 0.4682 0.5779 0.5512 0.0112  -0.0100 0.0011  239 GLU A C   
1142 O O   . GLU A 239 ? 0.3930 0.5156 0.4788 0.0039  -0.0108 0.0036  239 GLU A O   
1143 C CB  . GLU A 239 ? 0.4608 0.5560 0.5367 0.0180  -0.0033 -0.0051 239 GLU A CB  
1144 C CG  . GLU A 239 ? 0.4780 0.5786 0.5523 0.0094  -0.0031 -0.0037 239 GLU A CG  
1145 C CD  . GLU A 239 ? 0.5667 0.6879 0.6460 0.0095  0.0004  -0.0025 239 GLU A CD  
1146 O OE1 . GLU A 239 ? 0.6094 0.7390 0.6920 0.0187  0.0039  -0.0042 239 GLU A OE1 
1147 O OE2 . GLU A 239 ? 0.5933 0.7218 0.6720 0.0005  -0.0002 0.0004  239 GLU A OE2 
1148 N N   . MET A 240 ? 0.3425 0.4378 0.4210 0.0108  -0.0130 0.0011  240 MET A N   
1149 C CA  . MET A 240 ? 0.3847 0.4771 0.4599 0.0028  -0.0178 0.0035  240 MET A CA  
1150 C C   . MET A 240 ? 0.3648 0.4748 0.4462 0.0002  -0.0211 0.0067  240 MET A C   
1151 O O   . MET A 240 ? 0.3733 0.4856 0.4523 -0.0094 -0.0249 0.0089  240 MET A O   
1152 C CB  . MET A 240 ? 0.3733 0.4483 0.4418 0.0048  -0.0196 0.0027  240 MET A CB  
1153 C CG  . MET A 240 ? 0.3334 0.3938 0.3961 0.0046  -0.0176 0.0004  240 MET A CG  
1154 S SD  . MET A 240 ? 0.4743 0.5192 0.5300 0.0064  -0.0189 0.0002  240 MET A SD  
1155 C CE  . MET A 240 ? 0.4171 0.4564 0.4644 -0.0004 -0.0237 0.0016  240 MET A CE  
1156 N N   . PHE A 241 ? 0.3465 0.4687 0.4351 0.0084  -0.0202 0.0071  241 PHE A N   
1157 C CA  . PHE A 241 ? 0.3748 0.5180 0.4713 0.0067  -0.0238 0.0104  241 PHE A CA  
1158 C C   . PHE A 241 ? 0.4374 0.6044 0.5425 0.0022  -0.0215 0.0122  241 PHE A C   
1159 O O   . PHE A 241 ? 0.4216 0.6070 0.5327 -0.0053 -0.0252 0.0157  241 PHE A O   
1160 C CB  . PHE A 241 ? 0.3966 0.5445 0.4970 0.0188  -0.0241 0.0106  241 PHE A CB  
1161 C CG  . PHE A 241 ? 0.3890 0.5158 0.4804 0.0214  -0.0268 0.0101  241 PHE A CG  
1162 C CD1 . PHE A 241 ? 0.4183 0.5240 0.5022 0.0257  -0.0233 0.0074  241 PHE A CD1 
1163 C CD2 . PHE A 241 ? 0.4282 0.5571 0.5179 0.0188  -0.0330 0.0127  241 PHE A CD2 
1164 C CE1 . PHE A 241 ? 0.3654 0.4539 0.4412 0.0273  -0.0250 0.0076  241 PHE A CE1 
1165 C CE2 . PHE A 241 ? 0.3505 0.4602 0.4305 0.0213  -0.0348 0.0124  241 PHE A CE2 
1166 C CZ  . PHE A 241 ? 0.4167 0.5069 0.4901 0.0256  -0.0303 0.0101  241 PHE A CZ  
1167 N N   . LYS A 242 ? 0.3203 0.4879 0.4257 0.0058  -0.0155 0.0100  242 LYS A N   
1168 C CA  . LYS A 242 ? 0.4377 0.6258 0.5487 -0.0002 -0.0125 0.0119  242 LYS A CA  
1169 C C   . LYS A 242 ? 0.3946 0.5746 0.4985 -0.0155 -0.0155 0.0140  242 LYS A C   
1170 O O   . LYS A 242 ? 0.4521 0.6495 0.5604 -0.0259 -0.0173 0.0179  242 LYS A O   
1171 C CB  . LYS A 242 ? 0.4503 0.6376 0.5600 0.0079  -0.0053 0.0085  242 LYS A CB  
1172 C CG  . LYS A 242 ? 0.6069 0.8051 0.7225 0.0233  -0.0017 0.0067  242 LYS A CG  
1173 C CD  . LYS A 242 ? 0.7893 0.9732 0.8972 0.0314  0.0039  0.0019  242 LYS A CD  
1174 C CE  . LYS A 242 ? 0.8123 0.9769 0.9146 0.0432  0.0035  -0.0014 242 LYS A CE  
1175 N NZ  . LYS A 242 ? 0.8226 0.9690 0.9149 0.0482  0.0075  -0.0062 242 LYS A NZ  
1176 N N   . GLU A 243 ? 0.3720 0.5253 0.4643 -0.0171 -0.0164 0.0117  243 GLU A N   
1177 C CA  . GLU A 243 ? 0.4744 0.6157 0.5570 -0.0295 -0.0193 0.0134  243 GLU A CA  
1178 C C   . GLU A 243 ? 0.4977 0.6354 0.5766 -0.0385 -0.0264 0.0160  243 GLU A C   
1179 O O   . GLU A 243 ? 0.4192 0.5550 0.4920 -0.0511 -0.0295 0.0189  243 GLU A O   
1180 C CB  . GLU A 243 ? 0.4510 0.5666 0.5227 -0.0266 -0.0185 0.0102  243 GLU A CB  
1181 C CG  . GLU A 243 ? 0.4723 0.5888 0.5445 -0.0208 -0.0127 0.0076  243 GLU A CG  
1182 C CD  . GLU A 243 ? 0.5544 0.6488 0.6182 -0.0174 -0.0129 0.0045  243 GLU A CD  
1183 O OE1 . GLU A 243 ? 0.7195 0.7995 0.7777 -0.0183 -0.0167 0.0044  243 GLU A OE1 
1184 O OE2 . GLU A 243 ? 0.6184 0.7110 0.6808 -0.0136 -0.0094 0.0021  243 GLU A OE2 
1185 N N   . ASN A 244 ? 0.3865 0.5212 0.4667 -0.0329 -0.0295 0.0152  244 ASN A N   
1186 C CA  . ASN A 244 ? 0.3682 0.4970 0.4425 -0.0409 -0.0369 0.0171  244 ASN A CA  
1187 C C   . ASN A 244 ? 0.4382 0.5873 0.5232 -0.0371 -0.0395 0.0188  244 ASN A C   
1188 O O   . ASN A 244 ? 0.3372 0.4799 0.4220 -0.0274 -0.0400 0.0171  244 ASN A O   
1189 C CB  . ASN A 244 ? 0.3700 0.4696 0.4303 -0.0381 -0.0390 0.0143  244 ASN A CB  
1190 C CG  . ASN A 244 ? 0.4555 0.5433 0.5044 -0.0474 -0.0465 0.0156  244 ASN A CG  
1191 O OD1 . ASN A 244 ? 0.4001 0.5015 0.4519 -0.0572 -0.0510 0.0188  244 ASN A OD1 
1192 N ND2 . ASN A 244 ? 0.4845 0.5469 0.5195 -0.0445 -0.0480 0.0132  244 ASN A ND2 
1193 N N   . PRO A 245 ? 0.4371 0.6123 0.5318 -0.0449 -0.0416 0.0225  245 PRO A N   
1194 C CA  . PRO A 245 ? 0.3397 0.5378 0.4460 -0.0403 -0.0448 0.0245  245 PRO A CA  
1195 C C   . PRO A 245 ? 0.4002 0.5840 0.4975 -0.0426 -0.0527 0.0245  245 PRO A C   
1196 O O   . PRO A 245 ? 0.4258 0.6194 0.5288 -0.0343 -0.0552 0.0251  245 PRO A O   
1197 C CB  . PRO A 245 ? 0.5333 0.7639 0.6514 -0.0513 -0.0460 0.0291  245 PRO A CB  
1198 C CG  . PRO A 245 ? 0.4979 0.7211 0.6099 -0.0610 -0.0422 0.0296  245 PRO A CG  
1199 C CD  . PRO A 245 ? 0.3974 0.5827 0.4922 -0.0592 -0.0418 0.0258  245 PRO A CD  
1200 N N   . GLU A 246 ? 0.4042 0.5629 0.4853 -0.0525 -0.0568 0.0238  246 GLU A N   
1201 C CA  . GLU A 246 ? 0.4663 0.6073 0.5351 -0.0543 -0.0638 0.0230  246 GLU A CA  
1202 C C   . GLU A 246 ? 0.4433 0.5741 0.5107 -0.0391 -0.0614 0.0205  246 GLU A C   
1203 O O   . GLU A 246 ? 0.4535 0.5822 0.5168 -0.0374 -0.0668 0.0211  246 GLU A O   
1204 C CB  . GLU A 246 ? 0.4635 0.5737 0.5123 -0.0632 -0.0664 0.0214  246 GLU A CB  
1205 C CG  . GLU A 246 ? 0.6396 0.7293 0.6720 -0.0664 -0.0738 0.0203  246 GLU A CG  
1206 C CD  . GLU A 246 ? 0.7301 0.8354 0.7642 -0.0785 -0.0830 0.0236  246 GLU A CD  
1207 O OE1 . GLU A 246 ? 0.6959 0.8237 0.7404 -0.0891 -0.0842 0.0272  246 GLU A OE1 
1208 O OE2 . GLU A 246 ? 0.7767 0.8723 0.8011 -0.0779 -0.0891 0.0228  246 GLU A OE2 
1209 N N   . LEU A 247 ? 0.3884 0.5124 0.4581 -0.0289 -0.0537 0.0181  247 LEU A N   
1210 C CA  . LEU A 247 ? 0.4507 0.5621 0.5172 -0.0166 -0.0511 0.0161  247 LEU A CA  
1211 C C   . LEU A 247 ? 0.4234 0.5522 0.4992 -0.0081 -0.0529 0.0181  247 LEU A C   
1212 O O   . LEU A 247 ? 0.3992 0.5168 0.4686 -0.0014 -0.0542 0.0178  247 LEU A O   
1213 C CB  . LEU A 247 ? 0.3835 0.4861 0.4512 -0.0096 -0.0432 0.0134  247 LEU A CB  
1214 C CG  . LEU A 247 ? 0.3773 0.4608 0.4348 -0.0149 -0.0415 0.0113  247 LEU A CG  
1215 C CD1 . LEU A 247 ? 0.4257 0.5032 0.4853 -0.0080 -0.0347 0.0088  247 LEU A CD1 
1216 C CD2 . LEU A 247 ? 0.4146 0.4770 0.4572 -0.0165 -0.0452 0.0103  247 LEU A CD2 
1217 N N   . ASN A 248 ? 0.3840 0.5406 0.4743 -0.0078 -0.0528 0.0203  248 ASN A N   
1218 C CA  . ASN A 248 ? 0.3934 0.5686 0.4925 0.0014  -0.0554 0.0226  248 ASN A CA  
1219 C C   . ASN A 248 ? 0.4408 0.6196 0.5358 -0.0046 -0.0649 0.0251  248 ASN A C   
1220 O O   . ASN A 248 ? 0.4496 0.6334 0.5458 0.0045  -0.0681 0.0265  248 ASN A O   
1221 C CB  . ASN A 248 ? 0.4746 0.6821 0.5909 0.0044  -0.0526 0.0243  248 ASN A CB  
1222 C CG  . ASN A 248 ? 0.5099 0.7135 0.6289 0.0154  -0.0436 0.0215  248 ASN A CG  
1223 O OD1 . ASN A 248 ? 0.5723 0.7812 0.6945 0.0109  -0.0387 0.0206  248 ASN A OD1 
1224 N ND2 . ASN A 248 ? 0.6132 0.8057 0.7289 0.0294  -0.0416 0.0202  248 ASN A ND2 
1225 N N   . ASN A 249 ? 0.4050 0.5793 0.4931 -0.0196 -0.0701 0.0255  249 ASN A N   
1226 C CA  . ASN A 249 ? 0.4536 0.6270 0.5343 -0.0265 -0.0798 0.0273  249 ASN A CA  
1227 C C   . ASN A 249 ? 0.4268 0.5699 0.4896 -0.0211 -0.0808 0.0250  249 ASN A C   
1228 O O   . ASN A 249 ? 0.4506 0.5929 0.5070 -0.0213 -0.0880 0.0263  249 ASN A O   
1229 C CB  . ASN A 249 ? 0.4174 0.5903 0.4925 -0.0451 -0.0854 0.0282  249 ASN A CB  
1230 C CG  . ASN A 249 ? 0.4961 0.6962 0.5868 -0.0523 -0.0827 0.0307  249 ASN A CG  
1231 O OD1 . ASN A 249 ? 0.4682 0.6965 0.5766 -0.0438 -0.0793 0.0325  249 ASN A OD1 
1232 N ND2 . ASN A 249 ? 0.4364 0.6277 0.5197 -0.0674 -0.0839 0.0309  249 ASN A ND2 
1233 N N   . LYS A 250 ? 0.4711 0.5910 0.5259 -0.0165 -0.0736 0.0218  250 LYS A N   
1234 C CA  . LYS A 250 ? 0.4118 0.5041 0.4493 -0.0129 -0.0733 0.0197  250 LYS A CA  
1235 C C   . LYS A 250 ? 0.4332 0.5183 0.4714 0.0007  -0.0672 0.0193  250 LYS A C   
1236 O O   . LYS A 250 ? 0.3828 0.4537 0.4094 0.0049  -0.0685 0.0194  250 LYS A O   
1237 C CB  . LYS A 250 ? 0.4291 0.4994 0.4549 -0.0188 -0.0702 0.0165  250 LYS A CB  
1238 C CG  . LYS A 250 ? 0.4402 0.5074 0.4584 -0.0331 -0.0767 0.0167  250 LYS A CG  
1239 C CD  . LYS A 250 ? 0.6646 0.7309 0.6732 -0.0389 -0.0865 0.0179  250 LYS A CD  
1240 C CE  . LYS A 250 ? 0.8185 0.8677 0.8106 -0.0527 -0.0926 0.0167  250 LYS A CE  
1241 N NZ  . LYS A 250 ? 0.7280 0.7954 0.7242 -0.0661 -0.1022 0.0198  250 LYS A NZ  
1242 N N   . LEU A 251 ? 0.4062 0.4991 0.4558 0.0070  -0.0606 0.0188  251 LEU A N   
1243 C CA  . LEU A 251 ? 0.3167 0.3988 0.3648 0.0179  -0.0547 0.0182  251 LEU A CA  
1244 C C   . LEU A 251 ? 0.3488 0.4474 0.4075 0.0279  -0.0548 0.0204  251 LEU A C   
1245 O O   . LEU A 251 ? 0.3540 0.4759 0.4254 0.0274  -0.0563 0.0215  251 LEU A O   
1246 C CB  . LEU A 251 ? 0.3888 0.4613 0.4380 0.0177  -0.0470 0.0153  251 LEU A CB  
1247 C CG  . LEU A 251 ? 0.4553 0.5121 0.4947 0.0105  -0.0460 0.0130  251 LEU A CG  
1248 C CD1 . LEU A 251 ? 0.3360 0.3875 0.3787 0.0116  -0.0391 0.0106  251 LEU A CD1 
1249 C CD2 . LEU A 251 ? 0.4368 0.4758 0.4617 0.0119  -0.0470 0.0129  251 LEU A CD2 
1250 N N   . LYS A 252 ? 0.3921 0.4782 0.4444 0.0374  -0.0532 0.0212  252 LYS A N   
1251 C CA  . LYS A 252 ? 0.3595 0.4546 0.4181 0.0495  -0.0528 0.0229  252 LYS A CA  
1252 C C   . LYS A 252 ? 0.4009 0.4766 0.4540 0.0560  -0.0457 0.0212  252 LYS A C   
1253 O O   . LYS A 252 ? 0.4146 0.4701 0.4576 0.0523  -0.0426 0.0202  252 LYS A O   
1254 C CB  . LYS A 252 ? 0.4826 0.5795 0.5358 0.0556  -0.0596 0.0266  252 LYS A CB  
1255 C CG  . LYS A 252 ? 0.5117 0.5825 0.5475 0.0561  -0.0593 0.0274  252 LYS A CG  
1256 C CD  . LYS A 252 ? 0.5214 0.5903 0.5510 0.0666  -0.0642 0.0313  252 LYS A CD  
1257 C CE  . LYS A 252 ? 0.6414 0.7341 0.6778 0.0660  -0.0735 0.0338  252 LYS A CE  
1258 N NZ  . LYS A 252 ? 0.7779 0.8604 0.7997 0.0679  -0.0800 0.0370  252 LYS A NZ  
1259 N N   . ALA A 253 ? 0.4161 0.4985 0.4756 0.0656  -0.0431 0.0209  253 ALA A N   
1260 C CA  . ALA A 253 ? 0.4811 0.5423 0.5327 0.0720  -0.0377 0.0195  253 ALA A CA  
1261 C C   . ALA A 253 ? 0.4575 0.5004 0.4958 0.0778  -0.0401 0.0226  253 ALA A C   
1262 O O   . ALA A 253 ? 0.5082 0.5594 0.5460 0.0837  -0.0459 0.0258  253 ALA A O   
1263 C CB  . ALA A 253 ? 0.3675 0.4378 0.4261 0.0821  -0.0348 0.0179  253 ALA A CB  
1264 N N   . LEU A 254 ? 0.5242 0.5430 0.5513 0.0754  -0.0360 0.0221  254 LEU A N   
1265 C CA  . LEU A 254 ? 0.4986 0.4974 0.5109 0.0798  -0.0373 0.0257  254 LEU A CA  
1266 C C   . LEU A 254 ? 0.5805 0.5731 0.5889 0.0937  -0.0383 0.0270  254 LEU A C   
1267 O O   . LEU A 254 ? 0.5867 0.5754 0.5970 0.0978  -0.0346 0.0241  254 LEU A O   
1268 C CB  . LEU A 254 ? 0.4955 0.4725 0.4977 0.0722  -0.0320 0.0252  254 LEU A CB  
1269 C CG  . LEU A 254 ? 0.5117 0.4878 0.5109 0.0619  -0.0310 0.0254  254 LEU A CG  
1270 C CD1 . LEU A 254 ? 0.5267 0.4868 0.5197 0.0554  -0.0248 0.0249  254 LEU A CD1 
1271 C CD2 . LEU A 254 ? 0.5957 0.5684 0.5847 0.0637  -0.0357 0.0294  254 LEU A CD2 
1272 N N   . ASP A 255 ? 0.6702 0.6610 0.6716 0.1016  -0.0438 0.0311  255 ASP A N   
1273 C CA  . ASP A 255 ? 0.7283 0.7064 0.7208 0.1162  -0.0452 0.0332  255 ASP A CA  
1274 C C   . ASP A 255 ? 0.8775 0.8281 0.8500 0.1157  -0.0464 0.0376  255 ASP A C   
1275 O O   . ASP A 255 ? 0.8709 0.8254 0.8390 0.1159  -0.0516 0.0413  255 ASP A O   
1276 C CB  . ASP A 255 ? 0.7290 0.7322 0.7315 0.1287  -0.0512 0.0348  255 ASP A CB  
1277 C CG  . ASP A 255 ? 0.8643 0.8538 0.8568 0.1465  -0.0525 0.0365  255 ASP A CG  
1278 O OD1 . ASP A 255 ? 0.8951 0.8715 0.8842 0.1514  -0.0475 0.0332  255 ASP A OD1 
1279 O OD2 . ASP A 255 ? 1.0249 1.0152 1.0115 0.1563  -0.0589 0.0409  255 ASP A OD2 
1280 N N   . VAL A 256 ? 0.7471 0.6698 0.7065 0.1139  -0.0417 0.0374  256 VAL A N   
1281 C CA  . VAL A 256 ? 0.6913 0.5868 0.6314 0.1093  -0.0409 0.0418  256 VAL A CA  
1282 C C   . VAL A 256 ? 0.7910 0.6571 0.7143 0.1183  -0.0405 0.0433  256 VAL A C   
1283 O O   . VAL A 256 ? 0.7735 0.6323 0.6981 0.1192  -0.0370 0.0394  256 VAL A O   
1284 C CB  . VAL A 256 ? 0.7889 0.6794 0.7292 0.0929  -0.0348 0.0403  256 VAL A CB  
1285 C CG1 . VAL A 256 ? 0.7261 0.5920 0.6470 0.0873  -0.0332 0.0455  256 VAL A CG1 
1286 C CG2 . VAL A 256 ? 0.6958 0.6125 0.6516 0.0851  -0.0349 0.0377  256 VAL A CG2 
1287 N N   . PHE A 257 ? 0.8258 0.6726 0.7312 0.1247  -0.0443 0.0490  257 PHE A N   
1288 C CA  . PHE A 257 ? 0.8715 0.6854 0.7569 0.1338  -0.0448 0.0511  257 PHE A CA  
1289 C C   . PHE A 257 ? 0.8443 0.6303 0.7166 0.1193  -0.0389 0.0514  257 PHE A C   
1290 O O   . PHE A 257 ? 0.8371 0.6228 0.7074 0.1054  -0.0360 0.0539  257 PHE A O   
1291 C CB  . PHE A 257 ? 0.9114 0.7120 0.7799 0.1452  -0.0512 0.0578  257 PHE A CB  
1292 C CG  . PHE A 257 ? 1.0384 0.8049 0.8854 0.1583  -0.0531 0.0598  257 PHE A CG  
1293 C CD1 . PHE A 257 ? 1.0755 0.8445 0.9273 0.1726  -0.0534 0.0553  257 PHE A CD1 
1294 C CD2 . PHE A 257 ? 1.0346 0.7652 0.8548 0.1568  -0.0542 0.0663  257 PHE A CD2 
1295 C CE1 . PHE A 257 ? 1.1004 0.8348 0.9297 0.1862  -0.0553 0.0566  257 PHE A CE1 
1296 C CE2 . PHE A 257 ? 1.1515 0.8463 0.9487 0.1690  -0.0564 0.0682  257 PHE A CE2 
1297 C CZ  . PHE A 257 ? 1.1759 0.8716 0.9772 0.1843  -0.0571 0.0631  257 PHE A CZ  
1298 N N   . ASP A 258 ? 0.8445 0.6081 0.7075 0.1226  -0.0372 0.0488  258 ASP A N   
1299 C CA  . ASP A 258 ? 0.8253 0.5631 0.6767 0.1084  -0.0323 0.0484  258 ASP A CA  
1300 C C   . ASP A 258 ? 0.7617 0.5215 0.6324 0.0934  -0.0271 0.0436  258 ASP A C   
1301 O O   . ASP A 258 ? 0.7462 0.4925 0.6111 0.0785  -0.0231 0.0440  258 ASP A O   
1302 C CB  . ASP A 258 ? 0.8350 0.5469 0.6654 0.0989  -0.0319 0.0559  258 ASP A CB  
1303 C CG  . ASP A 258 ? 1.0260 0.7076 0.8321 0.1129  -0.0372 0.0612  258 ASP A CG  
1304 O OD1 . ASP A 258 ? 1.0027 0.6623 0.7973 0.1238  -0.0390 0.0589  258 ASP A OD1 
1305 O OD2 . ASP A 258 ? 1.1187 0.7968 0.9151 0.1135  -0.0396 0.0676  258 ASP A OD2 
1306 N N   . PHE A 259 ? 0.6705 0.4641 0.5636 0.0967  -0.0273 0.0393  259 PHE A N   
1307 C CA  . PHE A 259 ? 0.7465 0.5613 0.6574 0.0844  -0.0230 0.0348  259 PHE A CA  
1308 C C   . PHE A 259 ? 0.6562 0.4858 0.5799 0.0926  -0.0230 0.0285  259 PHE A C   
1309 O O   . PHE A 259 ? 0.6749 0.5327 0.6147 0.0982  -0.0246 0.0269  259 PHE A O   
1310 C CB  . PHE A 259 ? 0.6840 0.5241 0.6074 0.0783  -0.0229 0.0362  259 PHE A CB  
1311 C CG  . PHE A 259 ? 0.6031 0.4600 0.5408 0.0655  -0.0185 0.0326  259 PHE A CG  
1312 C CD1 . PHE A 259 ? 0.6190 0.4638 0.5515 0.0527  -0.0141 0.0332  259 PHE A CD1 
1313 C CD2 . PHE A 259 ? 0.6397 0.5245 0.5954 0.0660  -0.0191 0.0291  259 PHE A CD2 
1314 C CE1 . PHE A 259 ? 0.5664 0.4281 0.5123 0.0425  -0.0104 0.0301  259 PHE A CE1 
1315 C CE2 . PHE A 259 ? 0.5832 0.4810 0.5500 0.0556  -0.0155 0.0260  259 PHE A CE2 
1316 C CZ  . PHE A 259 ? 0.5264 0.4134 0.4887 0.0448  -0.0112 0.0264  259 PHE A CZ  
1317 N N   . THR A 260 ? 0.6248 0.4350 0.5401 0.0924  -0.0212 0.0252  260 THR A N   
1318 C CA  . THR A 260 ? 0.6795 0.5001 0.6030 0.1013  -0.0206 0.0192  260 THR A CA  
1319 C C   . THR A 260 ? 0.5618 0.3806 0.4889 0.0902  -0.0169 0.0139  260 THR A C   
1320 O O   . THR A 260 ? 0.5696 0.3783 0.4910 0.0972  -0.0163 0.0094  260 THR A O   
1321 C CB  . THR A 260 ? 0.6536 0.4516 0.5603 0.1190  -0.0233 0.0192  260 THR A CB  
1322 O OG1 . THR A 260 ? 0.9480 0.7656 0.8657 0.1323  -0.0229 0.0145  260 THR A OG1 
1323 C CG2 . THR A 260 ? 0.7028 0.4580 0.5847 0.1147  -0.0228 0.0190  260 THR A CG2 
1324 N N   . PRO A 261 ? 0.6119 0.4419 0.5485 0.0745  -0.0144 0.0141  261 PRO A N   
1325 C CA  . PRO A 261 ? 0.6035 0.4327 0.5433 0.0646  -0.0118 0.0093  261 PRO A CA  
1326 C C   . PRO A 261 ? 0.5878 0.4412 0.5427 0.0704  -0.0109 0.0041  261 PRO A C   
1327 O O   . PRO A 261 ? 0.5954 0.4722 0.5627 0.0777  -0.0118 0.0047  261 PRO A O   
1328 C CB  . PRO A 261 ? 0.5070 0.3461 0.4542 0.0485  -0.0098 0.0119  261 PRO A CB  
1329 C CG  . PRO A 261 ? 0.6549 0.5129 0.6108 0.0523  -0.0107 0.0153  261 PRO A CG  
1330 C CD  . PRO A 261 ? 0.5876 0.4323 0.5319 0.0658  -0.0140 0.0182  261 PRO A CD  
1331 N N   . ARG A 262 ? 0.5405 0.3876 0.4934 0.0660  -0.0094 -0.0008 262 ARG A N   
1332 C CA  . ARG A 262 ? 0.4934 0.3607 0.4580 0.0699  -0.0080 -0.0057 262 ARG A CA  
1333 C C   . ARG A 262 ? 0.5374 0.4213 0.5145 0.0559  -0.0065 -0.0068 262 ARG A C   
1334 O O   . ARG A 262 ? 0.5364 0.4079 0.5081 0.0446  -0.0062 -0.0075 262 ARG A O   
1335 C CB  . ARG A 262 ? 0.5280 0.3759 0.4790 0.0772  -0.0075 -0.0109 262 ARG A CB  
1336 C CG  . ARG A 262 ? 0.5221 0.3882 0.4828 0.0775  -0.0052 -0.0162 262 ARG A CG  
1337 C CD  . ARG A 262 ? 0.5616 0.4557 0.5358 0.0895  -0.0042 -0.0159 262 ARG A CD  
1338 N NE  . ARG A 262 ? 0.6597 0.5441 0.6236 0.1072  -0.0040 -0.0176 262 ARG A NE  
1339 C CZ  . ARG A 262 ? 0.6692 0.5455 0.6242 0.1153  -0.0018 -0.0231 262 ARG A CZ  
1340 N NH1 . ARG A 262 ? 0.6217 0.5000 0.5775 0.1068  0.0001  -0.0274 262 ARG A NH1 
1341 N NH2 . ARG A 262 ? 0.6628 0.5287 0.6069 0.1334  -0.0016 -0.0244 262 ARG A NH2 
1342 N N   . PHE A 263 ? 0.4684 0.3800 0.4617 0.0565  -0.0059 -0.0069 263 PHE A N   
1343 C CA  . PHE A 263 ? 0.3911 0.3183 0.3954 0.0456  -0.0049 -0.0079 263 PHE A CA  
1344 C C   . PHE A 263 ? 0.4263 0.3664 0.4366 0.0487  -0.0037 -0.0123 263 PHE A C   
1345 O O   . PHE A 263 ? 0.4520 0.4063 0.4680 0.0575  -0.0034 -0.0124 263 PHE A O   
1346 C CB  . PHE A 263 ? 0.3935 0.3381 0.4082 0.0424  -0.0056 -0.0042 263 PHE A CB  
1347 C CG  . PHE A 263 ? 0.4797 0.4131 0.4878 0.0401  -0.0062 0.0004  263 PHE A CG  
1348 C CD1 . PHE A 263 ? 0.5203 0.4450 0.5247 0.0297  -0.0049 0.0017  263 PHE A CD1 
1349 C CD2 . PHE A 263 ? 0.4369 0.3703 0.4424 0.0480  -0.0081 0.0036  263 PHE A CD2 
1350 C CE1 . PHE A 263 ? 0.4841 0.3995 0.4816 0.0269  -0.0047 0.0063  263 PHE A CE1 
1351 C CE2 . PHE A 263 ? 0.4461 0.3683 0.4436 0.0458  -0.0086 0.0081  263 PHE A CE2 
1352 C CZ  . PHE A 263 ? 0.4465 0.3593 0.4395 0.0351  -0.0065 0.0095  263 PHE A CZ  
1353 N N   . GLU A 264 ? 0.4598 0.3966 0.4688 0.0411  -0.0032 -0.0154 264 GLU A N   
1354 C CA  . GLU A 264 ? 0.4532 0.3997 0.4651 0.0431  -0.0019 -0.0196 264 GLU A CA  
1355 C C   . GLU A 264 ? 0.4916 0.4374 0.5041 0.0318  -0.0025 -0.0215 264 GLU A C   
1356 O O   . GLU A 264 ? 0.4438 0.3775 0.4517 0.0237  -0.0038 -0.0207 264 GLU A O   
1357 C CB  . GLU A 264 ? 0.4443 0.3770 0.4443 0.0537  -0.0008 -0.0234 264 GLU A CB  
1358 C CG  . GLU A 264 ? 0.4687 0.3729 0.4521 0.0496  -0.0021 -0.0262 264 GLU A CG  
1359 C CD  . GLU A 264 ? 0.5275 0.4111 0.4951 0.0624  -0.0016 -0.0290 264 GLU A CD  
1360 O OE1 . GLU A 264 ? 0.4973 0.3917 0.4686 0.0755  -0.0001 -0.0283 264 GLU A OE1 
1361 O OE2 . GLU A 264 ? 0.6310 0.4873 0.5816 0.0595  -0.0030 -0.0320 264 GLU A OE2 
1362 N N   . TYR A 265 ? 0.5042 0.4647 0.5228 0.0310  -0.0018 -0.0235 265 TYR A N   
1363 C CA  . TYR A 265 ? 0.4787 0.4390 0.4965 0.0227  -0.0029 -0.0260 265 TYR A CA  
1364 C C   . TYR A 265 ? 0.5222 0.4764 0.5310 0.0271  -0.0019 -0.0310 265 TYR A C   
1365 O O   . TYR A 265 ? 0.5262 0.4897 0.5364 0.0356  0.0006  -0.0319 265 TYR A O   
1366 C CB  . TYR A 265 ? 0.4089 0.3885 0.4381 0.0178  -0.0034 -0.0242 265 TYR A CB  
1367 C CG  . TYR A 265 ? 0.4445 0.4309 0.4815 0.0141  -0.0042 -0.0199 265 TYR A CG  
1368 C CD1 . TYR A 265 ? 0.5195 0.4984 0.5552 0.0082  -0.0049 -0.0183 265 TYR A CD1 
1369 C CD2 . TYR A 265 ? 0.4144 0.4148 0.4589 0.0157  -0.0040 -0.0174 265 TYR A CD2 
1370 C CE1 . TYR A 265 ? 0.4678 0.4538 0.5095 0.0059  -0.0048 -0.0146 265 TYR A CE1 
1371 C CE2 . TYR A 265 ? 0.4603 0.4648 0.5092 0.0132  -0.0047 -0.0142 265 TYR A CE2 
1372 C CZ  . TYR A 265 ? 0.4169 0.4147 0.4644 0.0091  -0.0047 -0.0129 265 TYR A CZ  
1373 O OH  . TYR A 265 ? 0.5841 0.5867 0.6350 0.0077  -0.0046 -0.0099 265 TYR A OH  
1374 N N   . TYR A 266 ? 0.4796 0.4196 0.4789 0.0211  -0.0039 -0.0343 266 TYR A N   
1375 C CA  . TYR A 266 ? 0.5114 0.4472 0.5016 0.0232  -0.0035 -0.0394 266 TYR A CA  
1376 C C   . TYR A 266 ? 0.4874 0.4372 0.4845 0.0148  -0.0054 -0.0392 266 TYR A C   
1377 O O   . TYR A 266 ? 0.5891 0.5366 0.5875 0.0052  -0.0089 -0.0387 266 TYR A O   
1378 C CB  . TYR A 266 ? 0.4608 0.3690 0.4328 0.0221  -0.0054 -0.0437 266 TYR A CB  
1379 C CG  . TYR A 266 ? 0.5416 0.4351 0.5028 0.0350  -0.0030 -0.0453 266 TYR A CG  
1380 C CD1 . TYR A 266 ? 0.4626 0.3560 0.4161 0.0464  0.0002  -0.0495 266 TYR A CD1 
1381 C CD2 . TYR A 266 ? 0.5774 0.4583 0.5359 0.0368  -0.0036 -0.0422 266 TYR A CD2 
1382 C CE1 . TYR A 266 ? 0.5956 0.4775 0.5396 0.0605  0.0026  -0.0509 266 TYR A CE1 
1383 C CE2 . TYR A 266 ? 0.5310 0.3982 0.4790 0.0503  -0.0019 -0.0433 266 TYR A CE2 
1384 C CZ  . TYR A 266 ? 0.4856 0.3540 0.4269 0.0628  0.0012  -0.0478 266 TYR A CZ  
1385 O OH  . TYR A 266 ? 0.5564 0.4127 0.4875 0.0783  0.0030  -0.0489 266 TYR A OH  
1386 N N   . VAL A 267 ? 0.4128 0.3779 0.4143 0.0187  -0.0033 -0.0392 267 VAL A N   
1387 C CA  . VAL A 267 ? 0.4100 0.3883 0.4174 0.0124  -0.0051 -0.0381 267 VAL A CA  
1388 C C   . VAL A 267 ? 0.4798 0.4504 0.4755 0.0101  -0.0067 -0.0428 267 VAL A C   
1389 O O   . VAL A 267 ? 0.4303 0.3952 0.4158 0.0167  -0.0040 -0.0465 267 VAL A O   
1390 C CB  . VAL A 267 ? 0.3822 0.3786 0.3981 0.0160  -0.0023 -0.0350 267 VAL A CB  
1391 C CG1 . VAL A 267 ? 0.3762 0.3821 0.3953 0.0101  -0.0047 -0.0335 267 VAL A CG1 
1392 C CG2 . VAL A 267 ? 0.4352 0.4378 0.4608 0.0181  -0.0015 -0.0308 267 VAL A CG2 
1393 N N   . ASP A 268 ? 0.4727 0.4440 0.4693 0.0014  -0.0113 -0.0428 268 ASP A N   
1394 C CA  . ASP A 268 ? 0.4525 0.4178 0.4381 -0.0022 -0.0143 -0.0469 268 ASP A CA  
1395 C C   . ASP A 268 ? 0.5005 0.4813 0.4915 -0.0046 -0.0160 -0.0446 268 ASP A C   
1396 O O   . ASP A 268 ? 0.3860 0.3792 0.3892 -0.0063 -0.0169 -0.0402 268 ASP A O   
1397 C CB  . ASP A 268 ? 0.4992 0.4527 0.4801 -0.0113 -0.0196 -0.0488 268 ASP A CB  
1398 C CG  . ASP A 268 ? 0.6474 0.5810 0.6199 -0.0102 -0.0186 -0.0505 268 ASP A CG  
1399 O OD1 . ASP A 268 ? 0.6391 0.5613 0.6011 -0.0011 -0.0150 -0.0535 268 ASP A OD1 
1400 O OD2 . ASP A 268 ? 0.8377 0.7671 0.8135 -0.0181 -0.0214 -0.0486 268 ASP A OD2 
1401 N N   . LEU A 269 ? 0.3949 0.3733 0.3748 -0.0039 -0.0165 -0.0478 269 LEU A N   
1402 C CA  . LEU A 269 ? 0.4377 0.4264 0.4184 -0.0069 -0.0195 -0.0460 269 LEU A CA  
1403 C C   . LEU A 269 ? 0.4385 0.4226 0.4146 -0.0146 -0.0267 -0.0483 269 LEU A C   
1404 O O   . LEU A 269 ? 0.4424 0.4128 0.4045 -0.0162 -0.0284 -0.0534 269 LEU A O   
1405 C CB  . LEU A 269 ? 0.3867 0.3767 0.3570 -0.0023 -0.0158 -0.0474 269 LEU A CB  
1406 C CG  . LEU A 269 ? 0.4870 0.4846 0.4546 -0.0052 -0.0189 -0.0451 269 LEU A CG  
1407 C CD1 . LEU A 269 ? 0.3742 0.3840 0.3541 -0.0054 -0.0186 -0.0388 269 LEU A CD1 
1408 C CD2 . LEU A 269 ? 0.4347 0.4302 0.3877 -0.0018 -0.0152 -0.0474 269 LEU A CD2 
1409 N N   . VAL A 270 ? 0.3776 0.3735 0.3648 -0.0189 -0.0310 -0.0447 270 VAL A N   
1410 C CA  . VAL A 270 ? 0.3753 0.3722 0.3630 -0.0270 -0.0381 -0.0458 270 VAL A CA  
1411 C C   . VAL A 270 ? 0.3436 0.3520 0.3317 -0.0277 -0.0432 -0.0441 270 VAL A C   
1412 O O   . VAL A 270 ? 0.3732 0.3904 0.3666 -0.0230 -0.0417 -0.0401 270 VAL A O   
1413 C CB  . VAL A 270 ? 0.4087 0.4121 0.4106 -0.0310 -0.0387 -0.0428 270 VAL A CB  
1414 C CG1 . VAL A 270 ? 0.4046 0.4119 0.4082 -0.0410 -0.0458 -0.0437 270 VAL A CG1 
1415 C CG2 . VAL A 270 ? 0.3598 0.3508 0.3602 -0.0290 -0.0335 -0.0437 270 VAL A CG2 
1416 N N   . TRP A 271 ? 0.4082 0.4146 0.3889 -0.0339 -0.0500 -0.0469 271 TRP A N   
1417 C CA  . TRP A 271 ? 0.4231 0.4406 0.4037 -0.0347 -0.0564 -0.0452 271 TRP A CA  
1418 C C   . TRP A 271 ? 0.4518 0.4741 0.4340 -0.0442 -0.0648 -0.0470 271 TRP A C   
1419 O O   . TRP A 271 ? 0.4459 0.4589 0.4256 -0.0511 -0.0655 -0.0500 271 TRP A O   
1420 C CB  . TRP A 271 ? 0.4439 0.4535 0.4073 -0.0311 -0.0559 -0.0472 271 TRP A CB  
1421 C CG  . TRP A 271 ? 0.4875 0.4805 0.4328 -0.0344 -0.0569 -0.0537 271 TRP A CG  
1422 C CD1 . TRP A 271 ? 0.4969 0.4861 0.4308 -0.0405 -0.0649 -0.0572 271 TRP A CD1 
1423 C CD2 . TRP A 271 ? 0.4083 0.3853 0.3432 -0.0309 -0.0501 -0.0579 271 TRP A CD2 
1424 N NE1 . TRP A 271 ? 0.5214 0.4906 0.4366 -0.0413 -0.0633 -0.0636 271 TRP A NE1 
1425 C CE2 . TRP A 271 ? 0.5400 0.5015 0.4555 -0.0346 -0.0540 -0.0641 271 TRP A CE2 
1426 C CE3 . TRP A 271 ? 0.4534 0.4278 0.3928 -0.0244 -0.0415 -0.0569 271 TRP A CE3 
1427 C CZ2 . TRP A 271 ? 0.4872 0.4295 0.3868 -0.0307 -0.0490 -0.0697 271 TRP A CZ2 
1428 C CZ3 . TRP A 271 ? 0.5102 0.4686 0.4359 -0.0204 -0.0367 -0.0620 271 TRP A CZ3 
1429 C CH2 . TRP A 271 ? 0.5226 0.4643 0.4282 -0.0229 -0.0402 -0.0684 271 TRP A CH2 
1430 N N   . SER A 272 ? 0.4371 0.4738 0.4228 -0.0447 -0.0718 -0.0447 272 SER A N   
1431 C CA  . SER A 272 ? 0.4754 0.5223 0.4648 -0.0540 -0.0809 -0.0456 272 SER A CA  
1432 C C   . SER A 272 ? 0.5678 0.6022 0.5371 -0.0585 -0.0868 -0.0507 272 SER A C   
1433 O O   . SER A 272 ? 0.6132 0.6445 0.5713 -0.0527 -0.0874 -0.0506 272 SER A O   
1434 C CB  . SER A 272 ? 0.5115 0.5833 0.5162 -0.0507 -0.0857 -0.0403 272 SER A CB  
1435 O OG  . SER A 272 ? 0.6235 0.7090 0.6316 -0.0592 -0.0955 -0.0409 272 SER A OG  
1436 N N   . ARG A 273 ? 0.6303 0.6561 0.5933 -0.0695 -0.0914 -0.0549 273 ARG A N   
1437 C CA  . ARG A 273 ? 0.7719 0.7828 0.7130 -0.0744 -0.0975 -0.0605 273 ARG A CA  
1438 C C   . ARG A 273 ? 0.8267 0.8550 0.7689 -0.0767 -0.1080 -0.0588 273 ARG A C   
1439 O O   . ARG A 273 ? 0.8919 0.9093 0.8145 -0.0776 -0.1127 -0.0626 273 ARG A O   
1440 C CB  . ARG A 273 ? 0.8458 0.8396 0.7775 -0.0865 -0.1006 -0.0656 273 ARG A CB  
1441 C CG  . ARG A 273 ? 0.9556 0.9673 0.9013 -0.1001 -0.1095 -0.0635 273 ARG A CG  
1442 C CD  . ARG A 273 ? 1.0157 1.0051 0.9457 -0.1143 -0.1143 -0.0691 273 ARG A CD  
1443 N NE  . ARG A 273 ? 1.1140 1.0787 1.0363 -0.1116 -0.1055 -0.0712 273 ARG A NE  
1444 C CZ  . ARG A 273 ? 1.1832 1.1163 1.0805 -0.1077 -0.1024 -0.0777 273 ARG A CZ  
1445 N NH1 . ARG A 273 ? 1.2184 1.1388 1.0942 -0.1073 -0.1071 -0.0831 273 ARG A NH1 
1446 N NH2 . ARG A 273 ? 1.1975 1.1112 1.0903 -0.1033 -0.0944 -0.0788 273 ARG A NH2 
1447 N N   . GLU A 274 ? 0.7833 0.8386 0.7471 -0.0766 -0.1117 -0.0532 274 GLU A N   
1448 C CA  . GLU A 274 ? 0.8352 0.9099 0.8018 -0.0774 -0.1222 -0.0510 274 GLU A CA  
1449 C C   . GLU A 274 ? 0.8645 0.9470 0.8325 -0.0636 -0.1206 -0.0463 274 GLU A C   
1450 O O   . GLU A 274 ? 0.9502 1.0452 0.9164 -0.0618 -0.1295 -0.0445 274 GLU A O   
1451 C CB  . GLU A 274 ? 0.9614 1.0639 0.9506 -0.0856 -0.1284 -0.0477 274 GLU A CB  
1452 C CG  . GLU A 274 ? 1.0325 1.1276 1.0182 -0.1026 -0.1327 -0.0518 274 GLU A CG  
1453 C CD  . GLU A 274 ? 1.1168 1.2394 1.1273 -0.1110 -0.1347 -0.0475 274 GLU A CD  
1454 O OE1 . GLU A 274 ? 1.0904 1.2172 1.1146 -0.1066 -0.1258 -0.0442 274 GLU A OE1 
1455 O OE2 . GLU A 274 ? 1.1790 1.3203 1.1953 -0.1224 -0.1454 -0.0471 274 GLU A OE2 
1456 N N   . SER A 275 ? 0.8402 0.9150 0.8101 -0.0542 -0.1104 -0.0442 275 SER A N   
1457 C CA  . SER A 275 ? 0.8488 0.9242 0.8148 -0.0426 -0.1085 -0.0400 275 SER A CA  
1458 C C   . SER A 275 ? 0.8622 0.9166 0.8035 -0.0409 -0.1066 -0.0429 275 SER A C   
1459 O O   . SER A 275 ? 0.9214 0.9592 0.8499 -0.0460 -0.1037 -0.0485 275 SER A O   
1460 C CB  . SER A 275 ? 0.8298 0.9058 0.8077 -0.0350 -0.0989 -0.0362 275 SER A CB  
1461 O OG  . SER A 275 ? 0.8181 0.8743 0.7856 -0.0342 -0.0897 -0.0388 275 SER A OG  
1462 N N   . GLU A 276 ? 0.8469 0.9013 0.7801 -0.0333 -0.1080 -0.0391 276 GLU A N   
1463 C CA  . GLU A 276 ? 0.9811 1.0176 0.8911 -0.0312 -0.1048 -0.0406 276 GLU A CA  
1464 C C   . GLU A 276 ? 0.8589 0.8873 0.7690 -0.0249 -0.0936 -0.0375 276 GLU A C   
1465 O O   . GLU A 276 ? 0.8491 0.8842 0.7687 -0.0190 -0.0926 -0.0320 276 GLU A O   
1466 C CB  . GLU A 276 ? 1.0503 1.0891 0.9470 -0.0284 -0.1138 -0.0379 276 GLU A CB  
1467 C CG  . GLU A 276 ? 1.1482 1.1857 1.0328 -0.0362 -0.1234 -0.0431 276 GLU A CG  
1468 C CD  . GLU A 276 ? 1.2780 1.3136 1.1442 -0.0333 -0.1315 -0.0410 276 GLU A CD  
1469 O OE1 . GLU A 276 ? 1.3032 1.3476 1.1738 -0.0257 -0.1349 -0.0346 276 GLU A OE1 
1470 O OE2 . GLU A 276 ? 1.2066 1.2299 1.0518 -0.0380 -0.1344 -0.0458 276 GLU A OE2 
1471 N N   . LEU A 277 ? 0.7963 0.8108 0.6954 -0.0261 -0.0856 -0.0413 277 LEU A N   
1472 C CA  . LEU A 277 ? 0.7177 0.7271 0.6177 -0.0217 -0.0749 -0.0388 277 LEU A CA  
1473 C C   . LEU A 277 ? 0.6338 0.6364 0.5159 -0.0187 -0.0733 -0.0355 277 LEU A C   
1474 O O   . LEU A 277 ? 0.7406 0.7360 0.6038 -0.0204 -0.0758 -0.0382 277 LEU A O   
1475 C CB  . LEU A 277 ? 0.6961 0.6966 0.5941 -0.0233 -0.0669 -0.0443 277 LEU A CB  
1476 C CG  . LEU A 277 ? 0.6937 0.6970 0.6074 -0.0266 -0.0669 -0.0469 277 LEU A CG  
1477 C CD1 . LEU A 277 ? 0.6664 0.6558 0.5705 -0.0271 -0.0608 -0.0530 277 LEU A CD1 
1478 C CD2 . LEU A 277 ? 0.6848 0.6976 0.6181 -0.0233 -0.0628 -0.0419 277 LEU A CD2 
1479 N N   . GLY A 278 ? 0.5844 0.5882 0.4706 -0.0151 -0.0694 -0.0294 278 GLY A N   
1480 C CA  . GLY A 278 ? 0.5830 0.5790 0.4518 -0.0139 -0.0661 -0.0255 278 GLY A CA  
1481 C C   . GLY A 278 ? 0.5640 0.5546 0.4230 -0.0154 -0.0562 -0.0288 278 GLY A C   
1482 O O   . GLY A 278 ? 0.5556 0.5467 0.4210 -0.0159 -0.0517 -0.0341 278 GLY A O   
1483 N N   . ALA A 279 ? 0.6110 0.5964 0.4531 -0.0157 -0.0525 -0.0252 279 ALA A N   
1484 C CA  . ALA A 279 ? 0.5282 0.5116 0.3600 -0.0161 -0.0424 -0.0279 279 ALA A CA  
1485 C C   . ALA A 279 ? 0.5125 0.5028 0.3604 -0.0153 -0.0331 -0.0273 279 ALA A C   
1486 O O   . ALA A 279 ? 0.5066 0.4984 0.3544 -0.0134 -0.0259 -0.0322 279 ALA A O   
1487 C CB  . ALA A 279 ? 0.5556 0.5342 0.3664 -0.0175 -0.0400 -0.0230 279 ALA A CB  
1488 N N   . ALA A 280 ? 0.5110 0.5050 0.3719 -0.0159 -0.0334 -0.0216 280 ALA A N   
1489 C CA  . ALA A 280 ? 0.5035 0.5046 0.3794 -0.0157 -0.0256 -0.0206 280 ALA A CA  
1490 C C   . ALA A 280 ? 0.4413 0.4452 0.3313 -0.0132 -0.0251 -0.0267 280 ALA A C   
1491 O O   . ALA A 280 ? 0.5146 0.5225 0.4088 -0.0112 -0.0174 -0.0294 280 ALA A O   
1492 C CB  . ALA A 280 ? 0.4518 0.4531 0.3362 -0.0172 -0.0279 -0.0137 280 ALA A CB  
1493 N N   . ALA A 281 ? 0.5293 0.5318 0.4266 -0.0131 -0.0331 -0.0287 281 ALA A N   
1494 C CA  . ALA A 281 ? 0.5344 0.5377 0.4435 -0.0123 -0.0330 -0.0339 281 ALA A CA  
1495 C C   . ALA A 281 ? 0.5051 0.5015 0.4019 -0.0114 -0.0302 -0.0408 281 ALA A C   
1496 O O   . ALA A 281 ? 0.4888 0.4838 0.3906 -0.0090 -0.0252 -0.0444 281 ALA A O   
1497 C CB  . ALA A 281 ? 0.4595 0.4649 0.3777 -0.0137 -0.0422 -0.0340 281 ALA A CB  
1498 N N   . ARG A 282 ? 0.4461 0.4364 0.3248 -0.0125 -0.0337 -0.0429 282 ARG A N   
1499 C CA  . ARG A 282 ? 0.5431 0.5239 0.4060 -0.0111 -0.0314 -0.0501 282 ARG A CA  
1500 C C   . ARG A 282 ? 0.5309 0.5138 0.3891 -0.0060 -0.0198 -0.0508 282 ARG A C   
1501 O O   . ARG A 282 ? 0.5716 0.5479 0.4247 -0.0019 -0.0155 -0.0569 282 ARG A O   
1502 C CB  . ARG A 282 ? 0.4948 0.4688 0.3376 -0.0134 -0.0379 -0.0517 282 ARG A CB  
1503 C CG  . ARG A 282 ? 0.5582 0.5317 0.4051 -0.0181 -0.0500 -0.0527 282 ARG A CG  
1504 C CD  . ARG A 282 ? 0.6146 0.5826 0.4414 -0.0204 -0.0575 -0.0539 282 ARG A CD  
1505 N NE  . ARG A 282 ? 0.6595 0.6339 0.4947 -0.0243 -0.0695 -0.0521 282 ARG A NE  
1506 C CZ  . ARG A 282 ? 0.7219 0.6922 0.5460 -0.0286 -0.0792 -0.0561 282 ARG A CZ  
1507 N NH1 . ARG A 282 ? 0.7379 0.6944 0.5395 -0.0297 -0.0787 -0.0624 282 ARG A NH1 
1508 N NH2 . ARG A 282 ? 0.7709 0.7522 0.6066 -0.0318 -0.0898 -0.0537 282 ARG A NH2 
1509 N N   . PHE A 283 ? 0.5310 0.5231 0.3902 -0.0061 -0.0146 -0.0444 283 PHE A N   
1510 C CA  . PHE A 283 ? 0.4752 0.4750 0.3332 -0.0020 -0.0033 -0.0439 283 PHE A CA  
1511 C C   . PHE A 283 ? 0.5070 0.5120 0.3827 0.0018  0.0010  -0.0454 283 PHE A C   
1512 O O   . PHE A 283 ? 0.5728 0.5782 0.4451 0.0083  0.0079  -0.0498 283 PHE A O   
1513 C CB  . PHE A 283 ? 0.5435 0.5532 0.4014 -0.0058 0.0002  -0.0356 283 PHE A CB  
1514 C CG  . PHE A 283 ? 0.5863 0.6099 0.4485 -0.0034 0.0116  -0.0336 283 PHE A CG  
1515 C CD1 . PHE A 283 ? 0.6433 0.6704 0.4899 0.0000  0.0196  -0.0358 283 PHE A CD1 
1516 C CD2 . PHE A 283 ? 0.5078 0.5426 0.3896 -0.0042 0.0144  -0.0296 283 PHE A CD2 
1517 C CE1 . PHE A 283 ? 0.5638 0.6083 0.4162 0.0027  0.0304  -0.0336 283 PHE A CE1 
1518 C CE2 . PHE A 283 ? 0.5844 0.6356 0.4718 -0.0024 0.0243  -0.0275 283 PHE A CE2 
1519 C CZ  . PHE A 283 ? 0.5909 0.6484 0.4646 0.0012  0.0324  -0.0293 283 PHE A CZ  
1520 N N   . LEU A 284 ? 0.4677 0.4764 0.3613 -0.0011 -0.0031 -0.0416 284 LEU A N   
1521 C CA  . LEU A 284 ? 0.4137 0.4269 0.3235 0.0022  0.0003  -0.0422 284 LEU A CA  
1522 C C   . LEU A 284 ? 0.4932 0.4944 0.3992 0.0061  -0.0010 -0.0497 284 LEU A C   
1523 O O   . LEU A 284 ? 0.4978 0.4997 0.4067 0.0124  0.0048  -0.0523 284 LEU A O   
1524 C CB  . LEU A 284 ? 0.3912 0.4083 0.3176 -0.0019 -0.0047 -0.0372 284 LEU A CB  
1525 C CG  . LEU A 284 ? 0.4695 0.4912 0.4123 0.0008  -0.0020 -0.0369 284 LEU A CG  
1526 C CD1 . LEU A 284 ? 0.3807 0.4144 0.3269 0.0045  0.0069  -0.0352 284 LEU A CD1 
1527 C CD2 . LEU A 284 ? 0.3934 0.4176 0.3493 -0.0030 -0.0069 -0.0321 284 LEU A CD2 
1528 N N   . ILE A 285 ? 0.5386 0.5282 0.4373 0.0022  -0.0090 -0.0531 285 ILE A N   
1529 C CA  . ILE A 285 ? 0.5164 0.4912 0.4090 0.0035  -0.0114 -0.0599 285 ILE A CA  
1530 C C   . ILE A 285 ? 0.5647 0.5303 0.4385 0.0107  -0.0053 -0.0661 285 ILE A C   
1531 O O   . ILE A 285 ? 0.5647 0.5212 0.4361 0.0166  -0.0020 -0.0705 285 ILE A O   
1532 C CB  . ILE A 285 ? 0.5417 0.5086 0.4303 -0.0041 -0.0220 -0.0617 285 ILE A CB  
1533 C CG1 . ILE A 285 ? 0.4887 0.4655 0.3977 -0.0089 -0.0270 -0.0565 285 ILE A CG1 
1534 C CG2 . ILE A 285 ? 0.4888 0.4368 0.3645 -0.0047 -0.0249 -0.0694 285 ILE A CG2 
1535 C CD1 . ILE A 285 ? 0.4616 0.4388 0.3702 -0.0157 -0.0371 -0.0563 285 ILE A CD1 
1536 N N   . ASP A 286 ? 0.6021 0.5690 0.4606 0.0111  -0.0035 -0.0664 286 ASP A N   
1537 C CA  . ASP A 286 ? 0.5655 0.5251 0.4047 0.0192  0.0034  -0.0722 286 ASP A CA  
1538 C C   . ASP A 286 ? 0.5820 0.5553 0.4301 0.0283  0.0145  -0.0705 286 ASP A C   
1539 O O   . ASP A 286 ? 0.6372 0.6027 0.4759 0.0379  0.0198  -0.0763 286 ASP A O   
1540 C CB  . ASP A 286 ? 0.6292 0.5893 0.4501 0.0172  0.0034  -0.0719 286 ASP A CB  
1541 C CG  . ASP A 286 ? 0.7946 0.7379 0.6001 0.0109  -0.0073 -0.0763 286 ASP A CG  
1542 O OD1 . ASP A 286 ? 0.9141 0.8393 0.7091 0.0120  -0.0105 -0.0836 286 ASP A OD1 
1543 O OD2 . ASP A 286 ? 0.8983 0.8461 0.7015 0.0047  -0.0131 -0.0723 286 ASP A OD2 
1544 N N   . TYR A 287 ? 0.5793 0.5728 0.4448 0.0255  0.0175  -0.0627 287 TYR A N   
1545 C CA  . TYR A 287 ? 0.5659 0.5765 0.4426 0.0326  0.0270  -0.0602 287 TYR A CA  
1546 C C   . TYR A 287 ? 0.6329 0.6373 0.5189 0.0390  0.0270  -0.0633 287 TYR A C   
1547 O O   . TYR A 287 ? 0.6322 0.6397 0.5157 0.0500  0.0342  -0.0663 287 TYR A O   
1548 C CB  . TYR A 287 ? 0.4850 0.5153 0.3782 0.0254  0.0279  -0.0509 287 TYR A CB  
1549 C CG  . TYR A 287 ? 0.5160 0.5683 0.4220 0.0301  0.0369  -0.0472 287 TYR A CG  
1550 C CD1 . TYR A 287 ? 0.5618 0.6302 0.4613 0.0323  0.0457  -0.0453 287 TYR A CD1 
1551 C CD2 . TYR A 287 ? 0.6151 0.6739 0.5395 0.0321  0.0366  -0.0454 287 TYR A CD2 
1552 C CE1 . TYR A 287 ? 0.5047 0.5973 0.4176 0.0358  0.0536  -0.0415 287 TYR A CE1 
1553 C CE2 . TYR A 287 ? 0.5782 0.6593 0.5150 0.0358  0.0437  -0.0417 287 TYR A CE2 
1554 C CZ  . TYR A 287 ? 0.6943 0.7934 0.6262 0.0376  0.0522  -0.0398 287 TYR A CZ  
1555 O OH  . TYR A 287 ? 0.8492 0.9746 0.7955 0.0409  0.0591  -0.0358 287 TYR A OH  
1556 N N   . ILE A 288 ? 0.5747 0.5701 0.4703 0.0329  0.0191  -0.0625 288 ILE A N   
1557 C CA  . ILE A 288 ? 0.5769 0.5648 0.4803 0.0376  0.0186  -0.0644 288 ILE A CA  
1558 C C   . ILE A 288 ? 0.6370 0.6015 0.5205 0.0446  0.0185  -0.0730 288 ILE A C   
1559 O O   . ILE A 288 ? 0.6766 0.6379 0.5579 0.0557  0.0237  -0.0758 288 ILE A O   
1560 C CB  . ILE A 288 ? 0.4514 0.4363 0.3686 0.0284  0.0106  -0.0611 288 ILE A CB  
1561 C CG1 . ILE A 288 ? 0.5081 0.5133 0.4438 0.0241  0.0115  -0.0531 288 ILE A CG1 
1562 C CG2 . ILE A 288 ? 0.5501 0.5219 0.4702 0.0319  0.0092  -0.0637 288 ILE A CG2 
1563 C CD1 . ILE A 288 ? 0.5469 0.5676 0.4934 0.0310  0.0187  -0.0504 288 ILE A CD1 
1564 N N   . ARG A 289 ? 0.5484 0.4954 0.4163 0.0385  0.0120  -0.0772 289 ARG A N   
1565 C CA  . ARG A 289 ? 0.6444 0.5651 0.4892 0.0436  0.0109  -0.0859 289 ARG A CA  
1566 C C   . ARG A 289 ? 0.6736 0.5955 0.5039 0.0578  0.0207  -0.0900 289 ARG A C   
1567 O O   . ARG A 289 ? 0.7905 0.6944 0.6075 0.0680  0.0230  -0.0960 289 ARG A O   
1568 C CB  . ARG A 289 ? 0.6408 0.5469 0.4703 0.0335  0.0022  -0.0893 289 ARG A CB  
1569 C CG  . ARG A 289 ? 0.6633 0.5635 0.5029 0.0211  -0.0079 -0.0874 289 ARG A CG  
1570 C CD  . ARG A 289 ? 0.6671 0.5603 0.4941 0.0113  -0.0165 -0.0897 289 ARG A CD  
1571 N NE  . ARG A 289 ? 0.7542 0.6429 0.5895 -0.0007 -0.0263 -0.0886 289 ARG A NE  
1572 C CZ  . ARG A 289 ? 0.7864 0.6746 0.6171 -0.0107 -0.0355 -0.0891 289 ARG A CZ  
1573 N NH1 . ARG A 289 ? 0.7487 0.6387 0.5656 -0.0104 -0.0366 -0.0904 289 ARG A NH1 
1574 N NH2 . ARG A 289 ? 0.7345 0.6217 0.5745 -0.0214 -0.0437 -0.0879 289 ARG A NH2 
1575 N N   . ASN A 290 ? 0.6972 0.6401 0.5289 0.0590  0.0267  -0.0867 290 ASN A N   
1576 C CA  . ASN A 290 ? 0.7934 0.7417 0.6117 0.0724  0.0369  -0.0903 290 ASN A CA  
1577 C C   . ASN A 290 ? 0.7471 0.7093 0.5792 0.0847  0.0446  -0.0886 290 ASN A C   
1578 O O   . ASN A 290 ? 0.8674 0.8243 0.6864 0.0997  0.0513  -0.0941 290 ASN A O   
1579 C CB  . ASN A 290 ? 0.7609 0.7302 0.5786 0.0682  0.0414  -0.0856 290 ASN A CB  
1580 C CG  . ASN A 290 ? 0.8854 0.8525 0.6794 0.0789  0.0497  -0.0912 290 ASN A CG  
1581 O OD1 . ASN A 290 ? 1.0042 0.9661 0.7896 0.0934  0.0561  -0.0967 290 ASN A OD1 
1582 N ND2 . ASN A 290 ? 0.9708 0.9409 0.7525 0.0725  0.0495  -0.0900 290 ASN A ND2 
1583 N N   . LYS A 291 ? 0.6291 0.6089 0.4867 0.0793  0.0432  -0.0813 291 LYS A N   
1584 C CA  . LYS A 291 ? 0.7570 0.7512 0.6296 0.0896  0.0486  -0.0791 291 LYS A CA  
1585 C C   . LYS A 291 ? 0.7798 0.7470 0.6437 0.0976  0.0453  -0.0847 291 LYS A C   
1586 O O   . LYS A 291 ? 0.8327 0.7998 0.6924 0.1134  0.0512  -0.0876 291 LYS A O   
1587 C CB  . LYS A 291 ? 0.7964 0.8128 0.6956 0.0794  0.0463  -0.0700 291 LYS A CB  
1588 C CG  . LYS A 291 ? 0.8133 0.8605 0.7225 0.0762  0.0526  -0.0637 291 LYS A CG  
1589 C CD  . LYS A 291 ? 0.8450 0.9038 0.7742 0.0632  0.0475  -0.0558 291 LYS A CD  
1590 C CE  . LYS A 291 ? 0.9355 1.0249 0.8848 0.0630  0.0524  -0.0488 291 LYS A CE  
1591 N NZ  . LYS A 291 ? 0.9267 1.0263 0.8854 0.0754  0.0565  -0.0496 291 LYS A NZ  
1592 N N   . ARG A 292 ? 0.7543 0.6975 0.6137 0.0872  0.0358  -0.0863 292 ARG A N   
1593 C CA  . ARG A 292 ? 0.8048 0.7187 0.6538 0.0916  0.0317  -0.0909 292 ARG A CA  
1594 C C   . ARG A 292 ? 0.8388 0.7249 0.6573 0.1030  0.0337  -0.1004 292 ARG A C   
1595 O O   . ARG A 292 ? 0.9694 0.8290 0.7759 0.1095  0.0314  -0.1045 292 ARG A O   
1596 C CB  . ARG A 292 ? 0.7897 0.6885 0.6420 0.0751  0.0213  -0.0895 292 ARG A CB  
1597 C CG  . ARG A 292 ? 0.7702 0.6926 0.6502 0.0657  0.0192  -0.0809 292 ARG A CG  
1598 C CD  . ARG A 292 ? 0.7604 0.6686 0.6453 0.0537  0.0106  -0.0795 292 ARG A CD  
1599 N NE  . ARG A 292 ? 0.8144 0.7076 0.6989 0.0592  0.0103  -0.0799 292 ARG A NE  
1600 C CZ  . ARG A 292 ? 0.8644 0.7719 0.7649 0.0653  0.0137  -0.0751 292 ARG A CZ  
1601 N NH1 . ARG A 292 ? 0.8656 0.8031 0.7843 0.0662  0.0177  -0.0698 292 ARG A NH1 
1602 N NH2 . ARG A 292 ? 0.7750 0.6651 0.6719 0.0700  0.0124  -0.0756 292 ARG A NH2 
1603 N N   . MET A 293 ? 0.7797 0.6694 0.5835 0.1059  0.0378  -0.1039 293 MET A N   
1604 C CA  . MET A 293 ? 0.9221 0.7875 0.6956 0.1197  0.0414  -0.1133 293 MET A CA  
1605 C C   . MET A 293 ? 0.9690 0.8392 0.7425 0.1409  0.0499  -0.1147 293 MET A C   
1606 O O   . MET A 293 ? 1.0790 0.9253 0.8260 0.1554  0.0529  -0.1229 293 MET A O   
1607 C CB  . MET A 293 ? 1.0063 0.8812 0.7664 0.1198  0.0459  -0.1155 293 MET A CB  
1608 C CG  . MET A 293 ? 1.0827 0.9570 0.8429 0.1006  0.0378  -0.1134 293 MET A CG  
1609 S SD  . MET A 293 ? 1.3092 1.1390 1.0386 0.0915  0.0261  -0.1223 293 MET A SD  
1610 C CE  . MET A 293 ? 1.1882 1.0335 0.9242 0.0729  0.0193  -0.1174 293 MET A CE  
1611 N N   . GLN A 294 ? 1.0285 0.9290 0.8300 0.1435  0.0536  -0.1072 294 GLN A N   
1612 C CA  . GLN A 294 ? 1.0191 0.9291 0.8254 0.1631  0.0604  -0.1072 294 GLN A CA  
1613 C C   . GLN A 294 ? 0.9717 0.8823 0.7979 0.1585  0.0549  -0.1014 294 GLN A C   
1614 O O   . GLN A 294 ? 1.1486 1.0914 1.0023 0.1515  0.0556  -0.0933 294 GLN A O   
1615 C CB  . GLN A 294 ? 0.9821 0.9365 0.8046 0.1709  0.0712  -0.1027 294 GLN A CB  
1616 C CG  . GLN A 294 ? 1.0644 1.0241 0.8696 0.1734  0.0776  -0.1068 294 GLN A CG  
1617 C CD  . GLN A 294 ? 0.9882 0.9756 0.8093 0.1556  0.0777  -0.0996 294 GLN A CD  
1618 O OE1 . GLN A 294 ? 0.9987 1.0063 0.8456 0.1442  0.0746  -0.0915 294 GLN A OE1 
1619 N NE2 . GLN A 294 ? 1.0507 1.0372 0.8545 0.1535  0.0810  -0.1025 294 GLN A NE2 
1620 N N   . PRO B 93  ? 0.9479 0.8623 0.8002 -0.0426 0.0973  -0.0238 93  PRO B N   
1621 C CA  . PRO B 93  ? 0.9022 0.8340 0.7742 -0.0365 0.0932  -0.0259 93  PRO B CA  
1622 C C   . PRO B 93  ? 0.7725 0.7069 0.6521 -0.0315 0.0820  -0.0252 93  PRO B C   
1623 O O   . PRO B 93  ? 0.7142 0.6342 0.5797 -0.0281 0.0769  -0.0234 93  PRO B O   
1624 C CB  . PRO B 93  ? 0.8696 0.7918 0.7286 -0.0307 0.0957  -0.0278 93  PRO B CB  
1625 C CG  . PRO B 93  ? 0.8785 0.7790 0.7115 -0.0309 0.0948  -0.0253 93  PRO B CG  
1626 C CD  . PRO B 93  ? 0.8999 0.7943 0.7283 -0.0379 0.0977  -0.0226 93  PRO B CD  
1627 N N   . ASN B 94  ? 0.7389 0.6922 0.6407 -0.0308 0.0785  -0.0258 94  ASN B N   
1628 C CA  . ASN B 94  ? 0.6905 0.6461 0.5992 -0.0266 0.0685  -0.0252 94  ASN B CA  
1629 C C   . ASN B 94  ? 0.6419 0.6156 0.5722 -0.0221 0.0658  -0.0262 94  ASN B C   
1630 O O   . ASN B 94  ? 0.6210 0.6091 0.5649 -0.0230 0.0717  -0.0262 94  ASN B O   
1631 C CB  . ASN B 94  ? 0.7532 0.7069 0.6613 -0.0335 0.0663  -0.0233 94  ASN B CB  
1632 C CG  . ASN B 94  ? 0.7476 0.7211 0.6734 -0.0417 0.0680  -0.0228 94  ASN B CG  
1633 O OD1 . ASN B 94  ? 0.8338 0.8155 0.7632 -0.0475 0.0753  -0.0227 94  ASN B OD1 
1634 N ND2 . ASN B 94  ? 0.8010 0.7836 0.7381 -0.0427 0.0610  -0.0221 94  ASN B ND2 
1635 N N   . LEU B 95  ? 0.5132 0.4859 0.4465 -0.0167 0.0573  -0.0264 95  LEU B N   
1636 C CA  . LEU B 95  ? 0.5076 0.4923 0.4574 -0.0110 0.0542  -0.0273 95  LEU B CA  
1637 C C   . LEU B 95  ? 0.4865 0.4761 0.4446 -0.0110 0.0453  -0.0258 95  LEU B C   
1638 O O   . LEU B 95  ? 0.4245 0.4028 0.3720 -0.0096 0.0398  -0.0256 95  LEU B O   
1639 C CB  . LEU B 95  ? 0.4733 0.4472 0.4129 -0.0046 0.0539  -0.0302 95  LEU B CB  
1640 C CG  . LEU B 95  ? 0.4703 0.4492 0.4208 0.0013  0.0502  -0.0317 95  LEU B CG  
1641 C CD1 . LEU B 95  ? 0.4629 0.4565 0.4324 0.0038  0.0568  -0.0308 95  LEU B CD1 
1642 C CD2 . LEU B 95  ? 0.6140 0.5784 0.5482 0.0042  0.0496  -0.0351 95  LEU B CD2 
1643 N N   . THR B 96  ? 0.4260 0.4331 0.4032 -0.0121 0.0439  -0.0241 96  THR B N   
1644 C CA  . THR B 96  ? 0.4069 0.4190 0.3917 -0.0128 0.0359  -0.0227 96  THR B CA  
1645 C C   . THR B 96  ? 0.3793 0.3980 0.3762 -0.0051 0.0324  -0.0229 96  THR B C   
1646 O O   . THR B 96  ? 0.3987 0.4301 0.4097 -0.0020 0.0364  -0.0216 96  THR B O   
1647 C CB  . THR B 96  ? 0.4641 0.4907 0.4589 -0.0218 0.0356  -0.0198 96  THR B CB  
1648 O OG1 . THR B 96  ? 0.4733 0.4893 0.4532 -0.0301 0.0394  -0.0202 96  THR B OG1 
1649 C CG2 . THR B 96  ? 0.3830 0.4141 0.3842 -0.0228 0.0275  -0.0185 96  THR B CG2 
1650 N N   . ILE B 97  ? 0.3556 0.3656 0.3473 -0.0018 0.0259  -0.0241 97  ILE B N   
1651 C CA  . ILE B 97  ? 0.3413 0.3541 0.3416 0.0044  0.0223  -0.0247 97  ILE B CA  
1652 C C   . ILE B 97  ? 0.3909 0.4101 0.3992 0.0023  0.0152  -0.0224 97  ILE B C   
1653 O O   . ILE B 97  ? 0.3745 0.3863 0.3741 -0.0008 0.0116  -0.0224 97  ILE B O   
1654 C CB  . ILE B 97  ? 0.4075 0.4056 0.3941 0.0082  0.0204  -0.0280 97  ILE B CB  
1655 C CG1 . ILE B 97  ? 0.4123 0.4024 0.3878 0.0090  0.0277  -0.0304 97  ILE B CG1 
1656 C CG2 . ILE B 97  ? 0.4324 0.4313 0.4260 0.0128  0.0170  -0.0289 97  ILE B CG2 
1657 C CD1 . ILE B 97  ? 0.5487 0.5248 0.5063 0.0095  0.0247  -0.0328 97  ILE B CD1 
1658 N N   . VAL B 98  ? 0.3171 0.3494 0.3412 0.0045  0.0140  -0.0200 98  VAL B N   
1659 C CA  . VAL B 98  ? 0.3577 0.3958 0.3885 0.0026  0.0071  -0.0178 98  VAL B CA  
1660 C C   . VAL B 98  ? 0.3869 0.4191 0.4189 0.0091  0.0037  -0.0191 98  VAL B C   
1661 O O   . VAL B 98  ? 0.3625 0.3974 0.4020 0.0149  0.0067  -0.0187 98  VAL B O   
1662 C CB  . VAL B 98  ? 0.3433 0.4017 0.3901 -0.0009 0.0066  -0.0127 98  VAL B CB  
1663 C CG1 . VAL B 98  ? 0.3146 0.3844 0.3758 0.0064  0.0116  -0.0099 98  VAL B CG1 
1664 C CG2 . VAL B 98  ? 0.4607 0.5234 0.5117 -0.0033 -0.0008 -0.0105 98  VAL B CG2 
1665 N N   . VAL B 99  ? 0.4464 0.4697 0.4705 0.0080  -0.0014 -0.0206 99  VAL B N   
1666 C CA  . VAL B 99  ? 0.3744 0.3931 0.3995 0.0120  -0.0053 -0.0217 99  VAL B CA  
1667 C C   . VAL B 99  ? 0.4383 0.4654 0.4730 0.0103  -0.0099 -0.0185 99  VAL B C   
1668 O O   . VAL B 99  ? 0.4198 0.4473 0.4514 0.0049  -0.0125 -0.0175 99  VAL B O   
1669 C CB  . VAL B 99  ? 0.5228 0.5301 0.5355 0.0118  -0.0083 -0.0241 99  VAL B CB  
1670 C CG1 . VAL B 99  ? 0.4565 0.4609 0.4708 0.0143  -0.0123 -0.0253 99  VAL B CG1 
1671 C CG2 . VAL B 99  ? 0.4191 0.4191 0.4206 0.0124  -0.0046 -0.0263 99  VAL B CG2 
1672 N N   . VAL B 100 ? 0.3895 0.4217 0.4342 0.0146  -0.0101 -0.0167 100 VAL B N   
1673 C CA  . VAL B 100 ? 0.4458 0.4862 0.4988 0.0131  -0.0148 -0.0128 100 VAL B CA  
1674 C C   . VAL B 100 ? 0.3764 0.4076 0.4214 0.0106  -0.0196 -0.0149 100 VAL B C   
1675 O O   . VAL B 100 ? 0.4439 0.4648 0.4815 0.0126  -0.0197 -0.0184 100 VAL B O   
1676 C CB  . VAL B 100 ? 0.4500 0.4948 0.5138 0.0200  -0.0134 -0.0098 100 VAL B CB  
1677 C CG1 . VAL B 100 ? 0.5265 0.5776 0.5966 0.0187  -0.0190 -0.0055 100 VAL B CG1 
1678 C CG2 . VAL B 100 ? 0.4177 0.4750 0.4924 0.0233  -0.0078 -0.0059 100 VAL B CG2 
1679 N N   . SER B 101 ? 0.4633 0.4992 0.5095 0.0054  -0.0232 -0.0124 101 SER B N   
1680 C CA  . SER B 101 ? 0.4886 0.5157 0.5269 0.0026  -0.0259 -0.0139 101 SER B CA  
1681 C C   . SER B 101 ? 0.4539 0.4743 0.4920 0.0072  -0.0276 -0.0158 101 SER B C   
1682 O O   . SER B 101 ? 0.4878 0.5007 0.5192 0.0075  -0.0279 -0.0180 101 SER B O   
1683 C CB  . SER B 101 ? 0.4957 0.5282 0.5350 -0.0038 -0.0290 -0.0109 101 SER B CB  
1684 O OG  . SER B 101 ? 0.6064 0.6491 0.6480 -0.0094 -0.0283 -0.0085 101 SER B OG  
1685 N N   . GLU B 102 ? 0.3788 0.4021 0.4243 0.0109  -0.0283 -0.0143 102 GLU B N   
1686 C CA  . GLU B 102 ? 0.4171 0.4327 0.4610 0.0133  -0.0295 -0.0162 102 GLU B CA  
1687 C C   . GLU B 102 ? 0.4476 0.4554 0.4847 0.0151  -0.0276 -0.0205 102 GLU B C   
1688 O O   . GLU B 102 ? 0.4579 0.4601 0.4916 0.0146  -0.0293 -0.0226 102 GLU B O   
1689 C CB  . GLU B 102 ? 0.4722 0.4896 0.5237 0.0172  -0.0292 -0.0133 102 GLU B CB  
1690 C CG  . GLU B 102 ? 0.5444 0.5692 0.6011 0.0148  -0.0329 -0.0084 102 GLU B CG  
1691 C CD  . GLU B 102 ? 0.5568 0.5959 0.6217 0.0142  -0.0330 -0.0031 102 GLU B CD  
1692 O OE1 . GLU B 102 ? 0.5965 0.6399 0.6612 0.0128  -0.0308 -0.0041 102 GLU B OE1 
1693 O OE2 . GLU B 102 ? 0.6080 0.6552 0.6799 0.0149  -0.0355 0.0027  102 GLU B OE2 
1694 N N   . LEU B 103 ? 0.4378 0.4457 0.4719 0.0160  -0.0243 -0.0218 103 LEU B N   
1695 C CA  . LEU B 103 ? 0.4586 0.4591 0.4840 0.0165  -0.0227 -0.0256 103 LEU B CA  
1696 C C   . LEU B 103 ? 0.5248 0.5249 0.5429 0.0144  -0.0242 -0.0259 103 LEU B C   
1697 O O   . LEU B 103 ? 0.5118 0.5076 0.5218 0.0142  -0.0237 -0.0281 103 LEU B O   
1698 C CB  . LEU B 103 ? 0.4387 0.4374 0.4638 0.0195  -0.0168 -0.0267 103 LEU B CB  
1699 C CG  . LEU B 103 ? 0.4836 0.4814 0.5159 0.0240  -0.0132 -0.0253 103 LEU B CG  
1700 C CD1 . LEU B 103 ? 0.4220 0.4162 0.4530 0.0279  -0.0053 -0.0265 103 LEU B CD1 
1701 C CD2 . LEU B 103 ? 0.3587 0.3469 0.3871 0.0236  -0.0147 -0.0274 103 LEU B CD2 
1702 N N   . LEU B 104 ? 0.4821 0.4852 0.5015 0.0127  -0.0254 -0.0235 104 LEU B N   
1703 C CA  . LEU B 104 ? 0.5221 0.5226 0.5342 0.0122  -0.0250 -0.0227 104 LEU B CA  
1704 C C   . LEU B 104 ? 0.6299 0.6295 0.6387 0.0131  -0.0283 -0.0226 104 LEU B C   
1705 O O   . LEU B 104 ? 0.5680 0.5665 0.5700 0.0140  -0.0283 -0.0220 104 LEU B O   
1706 C CB  . LEU B 104 ? 0.6080 0.6082 0.6201 0.0098  -0.0240 -0.0203 104 LEU B CB  
1707 C CG  . LEU B 104 ? 0.6652 0.6676 0.6776 0.0064  -0.0209 -0.0198 104 LEU B CG  
1708 C CD1 . LEU B 104 ? 0.6636 0.6658 0.6757 0.0015  -0.0210 -0.0182 104 LEU B CD1 
1709 C CD2 . LEU B 104 ? 0.6264 0.6239 0.6301 0.0063  -0.0170 -0.0200 104 LEU B CD2 
1710 N N   . HIS B 105 ? 0.6476 0.6490 0.6612 0.0126  -0.0313 -0.0225 105 HIS B N   
1711 C CA  . HIS B 105 ? 0.6515 0.6557 0.6643 0.0124  -0.0348 -0.0215 105 HIS B CA  
1712 C C   . HIS B 105 ? 0.5543 0.5576 0.5641 0.0100  -0.0370 -0.0248 105 HIS B C   
1713 O O   . HIS B 105 ? 0.5740 0.5805 0.5851 0.0075  -0.0404 -0.0248 105 HIS B O   
1714 C CB  . HIS B 105 ? 0.4489 0.4554 0.4678 0.0122  -0.0357 -0.0195 105 HIS B CB  
1715 C CG  . HIS B 105 ? 0.5274 0.5312 0.5453 0.0136  -0.0322 -0.0167 105 HIS B CG  
1716 N ND1 . HIS B 105 ? 0.6431 0.6435 0.6612 0.0115  -0.0300 -0.0172 105 HIS B ND1 
1717 C CD2 . HIS B 105 ? 0.6034 0.6063 0.6187 0.0165  -0.0299 -0.0132 105 HIS B CD2 
1718 C CE1 . HIS B 105 ? 0.6552 0.6506 0.6687 0.0115  -0.0262 -0.0152 105 HIS B CE1 
1719 N NE2 . HIS B 105 ? 0.7056 0.7013 0.7174 0.0155  -0.0253 -0.0126 105 HIS B NE2 
1720 N N   . THR B 106 ? 0.6318 0.6298 0.6366 0.0099  -0.0342 -0.0278 106 THR B N   
1721 C CA  . THR B 106 ? 0.6119 0.6048 0.6085 0.0069  -0.0343 -0.0316 106 THR B CA  
1722 C C   . THR B 106 ? 0.6129 0.6056 0.5995 0.0063  -0.0342 -0.0315 106 THR B C   
1723 O O   . THR B 106 ? 0.7785 0.7754 0.7657 0.0088  -0.0345 -0.0278 106 THR B O   
1724 C CB  . THR B 106 ? 0.7168 0.7014 0.7138 0.0081  -0.0291 -0.0348 106 THR B CB  
1725 O OG1 . THR B 106 ? 0.6383 0.6220 0.6351 0.0113  -0.0242 -0.0345 106 THR B OG1 
1726 C CG2 . THR B 106 ? 0.7032 0.6892 0.7104 0.0098  -0.0294 -0.0331 106 THR B CG2 
1727 N N   . ASN B 107 ? 0.6575 0.6431 0.6331 0.0028  -0.0330 -0.0355 107 ASN B N   
1728 C CA  . ASN B 107 ? 0.7081 0.6936 0.6712 0.0000  -0.0346 -0.0354 107 ASN B CA  
1729 C C   . ASN B 107 ? 0.6529 0.6295 0.6088 0.0018  -0.0275 -0.0380 107 ASN B C   
1730 O O   . ASN B 107 ? 0.7495 0.7155 0.6964 -0.0007 -0.0230 -0.0430 107 ASN B O   
1731 C CB  . ASN B 107 ? 0.7875 0.7713 0.7403 -0.0080 -0.0387 -0.0384 107 ASN B CB  
1732 C CG  . ASN B 107 ? 0.6852 0.6708 0.6236 -0.0126 -0.0420 -0.0375 107 ASN B CG  
1733 O OD1 . ASN B 107 ? 0.8528 0.8369 0.7864 -0.0094 -0.0395 -0.0359 107 ASN B OD1 
1734 N ND2 . ASN B 107 ? 0.8341 0.8239 0.7649 -0.0210 -0.0481 -0.0381 107 ASN B ND2 
1735 N N   . TRP B 108 ? 0.6519 0.6317 0.6105 0.0057  -0.0256 -0.0348 108 TRP B N   
1736 C CA  . TRP B 108 ? 0.4963 0.4697 0.4503 0.0072  -0.0183 -0.0367 108 TRP B CA  
1737 C C   . TRP B 108 ? 0.5823 0.5545 0.5247 0.0066  -0.0181 -0.0347 108 TRP B C   
1738 O O   . TRP B 108 ? 0.5674 0.5340 0.5047 0.0071  -0.0116 -0.0364 108 TRP B O   
1739 C CB  . TRP B 108 ? 0.5264 0.5037 0.4940 0.0113  -0.0143 -0.0350 108 TRP B CB  
1740 C CG  . TRP B 108 ? 0.5526 0.5368 0.5272 0.0125  -0.0179 -0.0305 108 TRP B CG  
1741 C CD1 . TRP B 108 ? 0.5621 0.5511 0.5464 0.0130  -0.0215 -0.0288 108 TRP B CD1 
1742 C CD2 . TRP B 108 ? 0.5581 0.5425 0.5286 0.0132  -0.0170 -0.0271 108 TRP B CD2 
1743 N NE1 . TRP B 108 ? 0.5548 0.5463 0.5408 0.0139  -0.0222 -0.0250 108 TRP B NE1 
1744 C CE2 . TRP B 108 ? 0.4680 0.4560 0.4454 0.0142  -0.0193 -0.0238 108 TRP B CE2 
1745 C CE3 . TRP B 108 ? 0.5143 0.4941 0.4744 0.0129  -0.0136 -0.0266 108 TRP B CE3 
1746 C CZ2 . TRP B 108 ? 0.3990 0.3846 0.3728 0.0153  -0.0175 -0.0201 108 TRP B CZ2 
1747 C CZ3 . TRP B 108 ? 0.4909 0.4693 0.4480 0.0140  -0.0125 -0.0225 108 TRP B CZ3 
1748 C CH2 . TRP B 108 ? 0.5102 0.4907 0.4738 0.0153  -0.0140 -0.0194 108 TRP B CH2 
1749 N N   . THR B 109 ? 0.5146 0.4924 0.4532 0.0058  -0.0245 -0.0305 109 THR B N   
1750 C CA  . THR B 109 ? 0.5484 0.5252 0.4769 0.0066  -0.0242 -0.0268 109 THR B CA  
1751 C C   . THR B 109 ? 0.5118 0.4819 0.4222 0.0016  -0.0238 -0.0296 109 THR B C   
1752 O O   . THR B 109 ? 0.5716 0.5383 0.4717 0.0021  -0.0218 -0.0273 109 THR B O   
1753 C CB  . THR B 109 ? 0.5035 0.4896 0.4353 0.0092  -0.0305 -0.0194 109 THR B CB  
1754 O OG1 . THR B 109 ? 0.6268 0.6204 0.5566 0.0052  -0.0381 -0.0188 109 THR B OG1 
1755 C CG2 . THR B 109 ? 0.5004 0.4897 0.4469 0.0135  -0.0293 -0.0173 109 THR B CG2 
1756 N N   . ASP B 110 ? 0.4644 0.4306 0.3686 -0.0038 -0.0250 -0.0347 110 ASP B N   
1757 C CA  . ASP B 110 ? 0.5444 0.5010 0.4280 -0.0101 -0.0232 -0.0386 110 ASP B CA  
1758 C C   . ASP B 110 ? 0.5203 0.4657 0.3984 -0.0079 -0.0126 -0.0418 110 ASP B C   
1759 O O   . ASP B 110 ? 0.6910 0.6299 0.5522 -0.0109 -0.0106 -0.0421 110 ASP B O   
1760 C CB  . ASP B 110 ? 0.5520 0.5019 0.4281 -0.0173 -0.0240 -0.0447 110 ASP B CB  
1761 C CG  . ASP B 110 ? 0.6829 0.6449 0.5598 -0.0226 -0.0350 -0.0415 110 ASP B CG  
1762 O OD1 . ASP B 110 ? 0.8293 0.8053 0.7113 -0.0200 -0.0419 -0.0338 110 ASP B OD1 
1763 O OD2 . ASP B 110 ? 0.7619 0.7194 0.6342 -0.0294 -0.0362 -0.0462 110 ASP B OD2 
1764 N N   . TYR B 111 ? 0.5451 0.4894 0.4374 -0.0029 -0.0057 -0.0437 111 TYR B N   
1765 C CA  . TYR B 111 ? 0.5405 0.4777 0.4311 -0.0005 0.0049  -0.0459 111 TYR B CA  
1766 C C   . TYR B 111 ? 0.4892 0.4301 0.3793 0.0015  0.0056  -0.0412 111 TYR B C   
1767 O O   . TYR B 111 ? 0.5569 0.4909 0.4372 0.0007  0.0127  -0.0425 111 TYR B O   
1768 C CB  . TYR B 111 ? 0.6518 0.5915 0.5606 0.0045  0.0107  -0.0471 111 TYR B CB  
1769 C CG  . TYR B 111 ? 0.6605 0.5946 0.5697 0.0034  0.0104  -0.0509 111 TYR B CG  
1770 C CD1 . TYR B 111 ? 0.6594 0.5778 0.5523 0.0000  0.0168  -0.0567 111 TYR B CD1 
1771 C CD2 . TYR B 111 ? 0.5926 0.5349 0.5161 0.0050  0.0044  -0.0489 111 TYR B CD2 
1772 C CE1 . TYR B 111 ? 0.6814 0.5914 0.5723 -0.0018 0.0177  -0.0604 111 TYR B CE1 
1773 C CE2 . TYR B 111 ? 0.6800 0.6156 0.6027 0.0036  0.0045  -0.0521 111 TYR B CE2 
1774 C CZ  . TYR B 111 ? 0.7359 0.6549 0.6422 0.0001  0.0113  -0.0579 111 TYR B CZ  
1775 O OH  . TYR B 111 ? 0.8513 0.7604 0.7544 -0.0020 0.0127  -0.0614 111 TYR B OH  
1776 N N   . VAL B 112 ? 0.4796 0.4297 0.3787 0.0038  -0.0007 -0.0357 112 VAL B N   
1777 C CA  . VAL B 112 ? 0.5280 0.4783 0.4245 0.0055  0.0009  -0.0310 112 VAL B CA  
1778 C C   . VAL B 112 ? 0.5086 0.4543 0.3858 0.0032  -0.0020 -0.0283 112 VAL B C   
1779 O O   . VAL B 112 ? 0.5495 0.4886 0.4163 0.0028  0.0032  -0.0273 112 VAL B O   
1780 C CB  . VAL B 112 ? 0.4563 0.4140 0.3658 0.0089  -0.0032 -0.0261 112 VAL B CB  
1781 C CG1 . VAL B 112 ? 0.4794 0.4332 0.3832 0.0103  0.0000  -0.0215 112 VAL B CG1 
1782 C CG2 . VAL B 112 ? 0.4795 0.4423 0.4061 0.0099  -0.0009 -0.0284 112 VAL B CG2 
1783 N N   . CYS B 113 ? 0.5373 0.4874 0.4093 0.0011  -0.0107 -0.0266 113 CYS B N   
1784 C CA  . CYS B 113 ? 0.5826 0.5313 0.4360 -0.0020 -0.0151 -0.0229 113 CYS B CA  
1785 C C   . CYS B 113 ? 0.5685 0.5044 0.4031 -0.0075 -0.0087 -0.0288 113 CYS B C   
1786 O O   . CYS B 113 ? 0.5727 0.5033 0.3913 -0.0089 -0.0075 -0.0260 113 CYS B O   
1787 C CB  . CYS B 113 ? 0.5304 0.4897 0.3834 -0.0050 -0.0261 -0.0199 113 CYS B CB  
1788 S SG  . CYS B 113 ? 0.6307 0.6052 0.5043 0.0023  -0.0326 -0.0116 113 CYS B SG  
1789 N N   . LEU B 114 ? 0.5152 0.4447 0.3505 -0.0103 -0.0036 -0.0366 114 LEU B N   
1790 C CA  . LEU B 114 ? 0.6005 0.5154 0.4181 -0.0147 0.0052  -0.0428 114 LEU B CA  
1791 C C   . LEU B 114 ? 0.6104 0.5206 0.4286 -0.0112 0.0151  -0.0421 114 LEU B C   
1792 O O   . LEU B 114 ? 0.6267 0.5273 0.4258 -0.0145 0.0194  -0.0427 114 LEU B O   
1793 C CB  . LEU B 114 ? 0.5806 0.4881 0.4018 -0.0160 0.0111  -0.0505 114 LEU B CB  
1794 C CG  . LEU B 114 ? 0.6996 0.5893 0.5033 -0.0194 0.0232  -0.0575 114 LEU B CG  
1795 C CD1 . LEU B 114 ? 0.6330 0.5130 0.4070 -0.0293 0.0194  -0.0591 114 LEU B CD1 
1796 C CD2 . LEU B 114 ? 0.6255 0.5074 0.4359 -0.0179 0.0305  -0.0635 114 LEU B CD2 
1797 N N   . LEU B 115 ? 0.5605 0.4777 0.3997 -0.0055 0.0186  -0.0407 115 LEU B N   
1798 C CA  . LEU B 115 ? 0.5159 0.4309 0.3574 -0.0036 0.0278  -0.0399 115 LEU B CA  
1799 C C   . LEU B 115 ? 0.5836 0.4969 0.4140 -0.0039 0.0252  -0.0338 115 LEU B C   
1800 O O   . LEU B 115 ? 0.5436 0.4491 0.3627 -0.0055 0.0327  -0.0339 115 LEU B O   
1801 C CB  . LEU B 115 ? 0.5138 0.4391 0.3798 0.0006  0.0303  -0.0392 115 LEU B CB  
1802 C CG  . LEU B 115 ? 0.5284 0.4547 0.4059 0.0025  0.0371  -0.0439 115 LEU B CG  
1803 C CD1 . LEU B 115 ? 0.5399 0.4794 0.4412 0.0058  0.0376  -0.0415 115 LEU B CD1 
1804 C CD2 . LEU B 115 ? 0.6224 0.5394 0.4899 0.0015  0.0493  -0.0476 115 LEU B CD2 
1805 N N   . GLU B 116 ? 0.4669 0.3867 0.3003 -0.0017 0.0156  -0.0279 116 GLU B N   
1806 C CA  . GLU B 116 ? 0.5009 0.4179 0.3244 -0.0001 0.0140  -0.0206 116 GLU B CA  
1807 C C   . GLU B 116 ? 0.5331 0.4425 0.3322 -0.0040 0.0126  -0.0192 116 GLU B C   
1808 O O   . GLU B 116 ? 0.6527 0.5540 0.4390 -0.0041 0.0172  -0.0159 116 GLU B O   
1809 C CB  . GLU B 116 ? 0.6459 0.5718 0.4791 0.0046  0.0052  -0.0137 116 GLU B CB  
1810 C CG  . GLU B 116 ? 0.6233 0.5447 0.4498 0.0087  0.0061  -0.0052 116 GLU B CG  
1811 C CD  . GLU B 116 ? 0.6801 0.6010 0.4888 0.0089  0.0000  0.0015  116 GLU B CD  
1812 O OE1 . GLU B 116 ? 0.7332 0.6610 0.5374 0.0053  -0.0076 0.0004  116 GLU B OE1 
1813 O OE2 . GLU B 116 ? 0.7196 0.6332 0.5179 0.0121  0.0028  0.0085  116 GLU B OE2 
1814 N N   . SER B 117 ? 0.5328 0.4440 0.3236 -0.0084 0.0065  -0.0218 117 SER B N   
1815 C CA  . SER B 117 ? 0.7435 0.6482 0.5087 -0.0141 0.0038  -0.0204 117 SER B CA  
1816 C C   . SER B 117 ? 0.6495 0.5389 0.3991 -0.0183 0.0157  -0.0269 117 SER B C   
1817 O O   . SER B 117 ? 0.7787 0.6599 0.5066 -0.0217 0.0167  -0.0243 117 SER B O   
1818 C CB  . SER B 117 ? 0.7012 0.6116 0.4601 -0.0202 -0.0059 -0.0221 117 SER B CB  
1819 O OG  . SER B 117 ? 0.7522 0.6558 0.5129 -0.0241 0.0000  -0.0322 117 SER B OG  
1820 N N   . ARG B 118 ? 0.6436 0.5294 0.4041 -0.0178 0.0252  -0.0346 118 ARG B N   
1821 C CA  . ARG B 118 ? 0.6827 0.5552 0.4314 -0.0206 0.0384  -0.0404 118 ARG B CA  
1822 C C   . ARG B 118 ? 0.6592 0.5311 0.4149 -0.0172 0.0471  -0.0378 118 ARG B C   
1823 O O   . ARG B 118 ? 0.7333 0.5944 0.4739 -0.0201 0.0566  -0.0397 118 ARG B O   
1824 C CB  . ARG B 118 ? 0.7105 0.5800 0.4686 -0.0204 0.0461  -0.0486 118 ARG B CB  
1825 C CG  . ARG B 118 ? 0.7896 0.6550 0.5377 -0.0256 0.0403  -0.0530 118 ARG B CG  
1826 C CD  . ARG B 118 ? 0.8627 0.7158 0.5781 -0.0349 0.0380  -0.0544 118 ARG B CD  
1827 N NE  . ARG B 118 ? 1.0562 0.8904 0.7547 -0.0397 0.0506  -0.0635 118 ARG B NE  
1828 C CZ  . ARG B 118 ? 1.0528 0.8777 0.7403 -0.0458 0.0504  -0.0698 118 ARG B CZ  
1829 N NH1 . ARG B 118 ? 1.0738 0.9087 0.7673 -0.0484 0.0376  -0.0683 118 ARG B NH1 
1830 N NH2 . ARG B 118 ? 1.1472 0.9510 0.8167 -0.0496 0.0644  -0.0780 118 ARG B NH2 
1831 N N   . PHE B 119 ? 0.5812 0.4636 0.3577 -0.0123 0.0447  -0.0338 119 PHE B N   
1832 C CA  . PHE B 119 ? 0.6161 0.4985 0.3999 -0.0110 0.0528  -0.0317 119 PHE B CA  
1833 C C   . PHE B 119 ? 0.5993 0.4840 0.3849 -0.0081 0.0462  -0.0238 119 PHE B C   
1834 O O   . PHE B 119 ? 0.5937 0.4863 0.3976 -0.0054 0.0445  -0.0224 119 PHE B O   
1835 C CB  . PHE B 119 ? 0.6486 0.5406 0.4568 -0.0092 0.0591  -0.0355 119 PHE B CB  
1836 C CG  . PHE B 119 ? 0.6685 0.5576 0.4770 -0.0098 0.0679  -0.0421 119 PHE B CG  
1837 C CD1 . PHE B 119 ? 0.6279 0.5174 0.4393 -0.0087 0.0643  -0.0459 119 PHE B CD1 
1838 C CD2 . PHE B 119 ? 0.6087 0.4939 0.4148 -0.0113 0.0811  -0.0442 119 PHE B CD2 
1839 C CE1 . PHE B 119 ? 0.6115 0.4949 0.4218 -0.0083 0.0743  -0.0517 119 PHE B CE1 
1840 C CE2 . PHE B 119 ? 0.6790 0.5605 0.4860 -0.0103 0.0911  -0.0496 119 PHE B CE2 
1841 C CZ  . PHE B 119 ? 0.6041 0.4834 0.4125 -0.0084 0.0881  -0.0534 119 PHE B CZ  
1842 N N   . PRO B 120 ? 0.6379 0.5147 0.4035 -0.0084 0.0429  -0.0181 120 PRO B N   
1843 C CA  . PRO B 120 ? 0.6644 0.5422 0.4312 -0.0036 0.0371  -0.0093 120 PRO B CA  
1844 C C   . PRO B 120 ? 0.5879 0.4601 0.3598 -0.0031 0.0453  -0.0074 120 PRO B C   
1845 O O   . PRO B 120 ? 0.5211 0.3918 0.2957 0.0013  0.0426  -0.0010 120 PRO B O   
1846 C CB  . PRO B 120 ? 0.7772 0.6482 0.5199 -0.0039 0.0326  -0.0028 120 PRO B CB  
1847 C CG  . PRO B 120 ? 0.7231 0.5867 0.4491 -0.0106 0.0375  -0.0091 120 PRO B CG  
1848 C CD  . PRO B 120 ? 0.7194 0.5849 0.4596 -0.0128 0.0459  -0.0188 120 PRO B CD  
1849 N N   . ASP B 121 ? 0.6462 0.5147 0.4187 -0.0078 0.0559  -0.0124 121 ASP B N   
1850 C CA  . ASP B 121 ? 0.6588 0.5234 0.4362 -0.0100 0.0637  -0.0114 121 ASP B CA  
1851 C C   . ASP B 121 ? 0.6452 0.5228 0.4472 -0.0110 0.0637  -0.0150 121 ASP B C   
1852 O O   . ASP B 121 ? 0.6683 0.5440 0.4747 -0.0145 0.0687  -0.0142 121 ASP B O   
1853 C CB  . ASP B 121 ? 0.8151 0.6717 0.5815 -0.0159 0.0754  -0.0140 121 ASP B CB  
1854 C CG  . ASP B 121 ? 0.9063 0.7460 0.6466 -0.0159 0.0776  -0.0083 121 ASP B CG  
1855 O OD1 . ASP B 121 ? 0.8364 0.6709 0.5691 -0.0108 0.0710  -0.0010 121 ASP B OD1 
1856 O OD2 . ASP B 121 ? 1.0652 0.8971 0.7927 -0.0207 0.0865  -0.0103 121 ASP B OD2 
1857 N N   . LEU B 122 ? 0.5076 0.3973 0.3238 -0.0088 0.0581  -0.0187 122 LEU B N   
1858 C CA  . LEU B 122 ? 0.6143 0.5174 0.4533 -0.0100 0.0588  -0.0221 122 LEU B CA  
1859 C C   . LEU B 122 ? 0.5081 0.4145 0.3567 -0.0080 0.0525  -0.0190 122 LEU B C   
1860 O O   . LEU B 122 ? 0.5134 0.4196 0.3606 -0.0031 0.0444  -0.0164 122 LEU B O   
1861 C CB  . LEU B 122 ? 0.5308 0.4428 0.3794 -0.0078 0.0568  -0.0269 122 LEU B CB  
1862 C CG  . LEU B 122 ? 0.6022 0.5293 0.4748 -0.0078 0.0580  -0.0294 122 LEU B CG  
1863 C CD1 . LEU B 122 ? 0.6357 0.5685 0.5151 -0.0119 0.0687  -0.0305 122 LEU B CD1 
1864 C CD2 . LEU B 122 ? 0.5220 0.4531 0.4007 -0.0039 0.0547  -0.0328 122 LEU B CD2 
1865 N N   . GLN B 123 ? 0.5808 0.4905 0.4384 -0.0126 0.0565  -0.0192 123 GLN B N   
1866 C CA  . GLN B 123 ? 0.4560 0.3690 0.3234 -0.0121 0.0516  -0.0177 123 GLN B CA  
1867 C C   . GLN B 123 ? 0.4887 0.4183 0.3762 -0.0104 0.0463  -0.0208 123 GLN B C   
1868 O O   . GLN B 123 ? 0.5734 0.5144 0.4729 -0.0134 0.0500  -0.0235 123 GLN B O   
1869 C CB  . GLN B 123 ? 0.4486 0.3574 0.3150 -0.0199 0.0579  -0.0172 123 GLN B CB  
1870 C CG  . GLN B 123 ? 0.5506 0.4588 0.4226 -0.0204 0.0540  -0.0159 123 GLN B CG  
1871 C CD  . GLN B 123 ? 0.5600 0.4632 0.4288 -0.0308 0.0603  -0.0164 123 GLN B CD  
1872 O OE1 . GLN B 123 ? 0.6202 0.5374 0.5003 -0.0387 0.0622  -0.0188 123 GLN B OE1 
1873 N NE2 . GLN B 123 ? 0.6553 0.5386 0.5085 -0.0312 0.0639  -0.0135 123 GLN B NE2 
1874 N N   . ILE B 124 ? 0.4624 0.3938 0.3539 -0.0053 0.0383  -0.0197 124 ILE B N   
1875 C CA  . ILE B 124 ? 0.4318 0.3764 0.3402 -0.0033 0.0332  -0.0223 124 ILE B CA  
1876 C C   . ILE B 124 ? 0.4862 0.4338 0.4032 -0.0041 0.0294  -0.0207 124 ILE B C   
1877 O O   . ILE B 124 ? 0.5529 0.4937 0.4644 -0.0008 0.0258  -0.0177 124 ILE B O   
1878 C CB  . ILE B 124 ? 0.5026 0.4469 0.4076 0.0018  0.0274  -0.0231 124 ILE B CB  
1879 C CG1 . ILE B 124 ? 0.4822 0.4203 0.3743 0.0011  0.0321  -0.0252 124 ILE B CG1 
1880 C CG2 . ILE B 124 ? 0.5536 0.5085 0.4745 0.0035  0.0233  -0.0258 124 ILE B CG2 
1881 C CD1 . ILE B 124 ? 0.5427 0.4767 0.4233 0.0034  0.0261  -0.0251 124 ILE B CD1 
1882 N N   . ASN B 125 ? 0.4573 0.4159 0.3879 -0.0087 0.0305  -0.0220 125 ASN B N   
1883 C CA  . ASN B 125 ? 0.4288 0.3901 0.3659 -0.0115 0.0274  -0.0209 125 ASN B CA  
1884 C C   . ASN B 125 ? 0.4426 0.4165 0.3955 -0.0081 0.0211  -0.0219 125 ASN B C   
1885 O O   . ASN B 125 ? 0.4322 0.4185 0.3972 -0.0082 0.0220  -0.0230 125 ASN B O   
1886 C CB  . ASN B 125 ? 0.4317 0.3967 0.3705 -0.0214 0.0323  -0.0209 125 ASN B CB  
1887 C CG  . ASN B 125 ? 0.6049 0.5559 0.5270 -0.0257 0.0398  -0.0203 125 ASN B CG  
1888 O OD1 . ASN B 125 ? 0.5264 0.4601 0.4334 -0.0232 0.0412  -0.0184 125 ASN B OD1 
1889 N ND2 . ASN B 125 ? 0.5959 0.5544 0.5209 -0.0316 0.0453  -0.0211 125 ASN B ND2 
1890 N N   . ILE B 126 ? 0.4991 0.4695 0.4518 -0.0047 0.0158  -0.0209 126 ILE B N   
1891 C CA  . ILE B 126 ? 0.4621 0.4419 0.4275 -0.0016 0.0099  -0.0217 126 ILE B CA  
1892 C C   . ILE B 126 ? 0.4783 0.4619 0.4497 -0.0064 0.0082  -0.0207 126 ILE B C   
1893 O O   . ILE B 126 ? 0.5361 0.5101 0.4999 -0.0072 0.0081  -0.0194 126 ILE B O   
1894 C CB  . ILE B 126 ? 0.4539 0.4288 0.4152 0.0044  0.0049  -0.0212 126 ILE B CB  
1895 C CG1 . ILE B 126 ? 0.4476 0.4171 0.3982 0.0070  0.0062  -0.0217 126 ILE B CG1 
1896 C CG2 . ILE B 126 ? 0.4937 0.4769 0.4669 0.0067  -0.0002 -0.0226 126 ILE B CG2 
1897 C CD1 . ILE B 126 ? 0.4810 0.4549 0.4354 0.0076  0.0076  -0.0252 126 ILE B CD1 
1898 N N   . VAL B 127 ? 0.4003 0.3976 0.3846 -0.0096 0.0073  -0.0206 127 VAL B N   
1899 C CA  . VAL B 127 ? 0.5015 0.5046 0.4912 -0.0152 0.0044  -0.0193 127 VAL B CA  
1900 C C   . VAL B 127 ? 0.4909 0.5032 0.4933 -0.0105 -0.0012 -0.0188 127 VAL B C   
1901 O O   . VAL B 127 ? 0.4134 0.4284 0.4213 -0.0040 -0.0017 -0.0197 127 VAL B O   
1902 C CB  . VAL B 127 ? 0.4034 0.4174 0.3972 -0.0246 0.0070  -0.0181 127 VAL B CB  
1903 C CG1 . VAL B 127 ? 0.5463 0.5478 0.5248 -0.0310 0.0132  -0.0189 127 VAL B CG1 
1904 C CG2 . VAL B 127 ? 0.3920 0.4226 0.4005 -0.0215 0.0082  -0.0169 127 VAL B CG2 
1905 N N   . SER B 128 ? 0.4410 0.4561 0.4460 -0.0146 -0.0048 -0.0176 128 SER B N   
1906 C CA  . SER B 128 ? 0.4208 0.4437 0.4366 -0.0111 -0.0100 -0.0165 128 SER B CA  
1907 C C   . SER B 128 ? 0.5074 0.5439 0.5310 -0.0184 -0.0126 -0.0133 128 SER B C   
1908 O O   . SER B 128 ? 0.5457 0.5811 0.5621 -0.0279 -0.0114 -0.0130 128 SER B O   
1909 C CB  . SER B 128 ? 0.5485 0.5608 0.5588 -0.0083 -0.0128 -0.0175 128 SER B CB  
1910 O OG  . SER B 128 ? 0.6456 0.6489 0.6457 -0.0143 -0.0113 -0.0173 128 SER B OG  
1911 N N   . ALA B 129 ? 0.4200 0.4688 0.4571 -0.0143 -0.0160 -0.0106 129 ALA B N   
1912 C CA  . ALA B 129 ? 0.4875 0.5536 0.5344 -0.0201 -0.0195 -0.0057 129 ALA B CA  
1913 C C   . ALA B 129 ? 0.4601 0.5331 0.5188 -0.0127 -0.0232 -0.0026 129 ALA B C   
1914 O O   . ALA B 129 ? 0.5219 0.5870 0.5818 -0.0037 -0.0216 -0.0047 129 ALA B O   
1915 C CB  . ALA B 129 ? 0.4035 0.4859 0.4590 -0.0236 -0.0165 -0.0027 129 ALA B CB  
1916 N N   . PRO B 130 ? 0.6004 0.6871 0.6664 -0.0170 -0.0282 0.0026  130 PRO B N   
1917 C CA  . PRO B 130 ? 0.5253 0.6200 0.6039 -0.0088 -0.0307 0.0073  130 PRO B CA  
1918 C C   . PRO B 130 ? 0.5258 0.6320 0.6188 0.0000  -0.0261 0.0109  130 PRO B C   
1919 O O   . PRO B 130 ? 0.4983 0.6133 0.5948 -0.0023 -0.0224 0.0115  130 PRO B O   
1920 C CB  . PRO B 130 ? 0.4793 0.5884 0.5611 -0.0172 -0.0373 0.0133  130 PRO B CB  
1921 C CG  . PRO B 130 ? 0.6110 0.7120 0.6769 -0.0302 -0.0379 0.0093  130 PRO B CG  
1922 C CD  . PRO B 130 ? 0.4797 0.5728 0.5399 -0.0303 -0.0317 0.0045  130 PRO B CD  
1923 N N   . GLN B 131 ? 0.5880 0.6925 0.6886 0.0103  -0.0251 0.0132  131 GLN B N   
1924 C CA  . GLN B 131 ? 0.5098 0.6212 0.6230 0.0207  -0.0186 0.0168  131 GLN B CA  
1925 C C   . GLN B 131 ? 0.4866 0.6242 0.6151 0.0185  -0.0180 0.0246  131 GLN B C   
1926 O O   . GLN B 131 ? 0.6094 0.7514 0.7430 0.0218  -0.0110 0.0244  131 GLN B O   
1927 C CB  . GLN B 131 ? 0.6350 0.7425 0.7544 0.0304  -0.0183 0.0207  131 GLN B CB  
1928 C CG  . GLN B 131 ? 0.7234 0.8052 0.8300 0.0348  -0.0154 0.0131  131 GLN B CG  
1929 C CD  . GLN B 131 ? 0.7061 0.7773 0.8107 0.0422  -0.0058 0.0094  131 GLN B CD  
1930 O OE1 . GLN B 131 ? 0.5111 0.5621 0.6032 0.0435  -0.0033 0.0025  131 GLN B OE1 
1931 N NE2 . GLN B 131 ? 0.6789 0.7641 0.7951 0.0463  -0.0002 0.0140  131 GLN B NE2 
1932 N N   . GLU B 132 ? 0.4636 0.6200 0.5993 0.0120  -0.0254 0.0318  132 GLU B N   
1933 C CA  . GLU B 132 ? 0.5649 0.7515 0.7179 0.0095  -0.0261 0.0412  132 GLU B CA  
1934 C C   . GLU B 132 ? 0.5526 0.7440 0.7003 -0.0018 -0.0243 0.0374  132 GLU B C   
1935 O O   . GLU B 132 ? 0.5088 0.7191 0.6702 -0.0004 -0.0198 0.0422  132 GLU B O   
1936 C CB  . GLU B 132 ? 0.6064 0.8125 0.7660 0.0032  -0.0359 0.0501  132 GLU B CB  
1937 C CG  . GLU B 132 ? 0.7091 0.9014 0.8493 -0.0098 -0.0431 0.0444  132 GLU B CG  
1938 C CD  . GLU B 132 ? 0.7079 0.8758 0.8378 -0.0033 -0.0435 0.0396  132 GLU B CD  
1939 O OE1 . GLU B 132 ? 0.6657 0.8184 0.7958 0.0084  -0.0372 0.0359  132 GLU B OE1 
1940 O OE2 . GLU B 132 ? 0.6986 0.8620 0.8187 -0.0111 -0.0498 0.0394  132 GLU B OE2 
1941 N N   . ASP B 133 ? 0.5183 0.6924 0.6462 -0.0127 -0.0267 0.0293  133 ASP B N   
1942 C CA  . ASP B 133 ? 0.5162 0.6901 0.6360 -0.0233 -0.0238 0.0254  133 ASP B CA  
1943 C C   . ASP B 133 ? 0.4718 0.6326 0.5889 -0.0152 -0.0145 0.0200  133 ASP B C   
1944 O O   . ASP B 133 ? 0.5074 0.6774 0.6277 -0.0192 -0.0098 0.0205  133 ASP B O   
1945 C CB  . ASP B 133 ? 0.5127 0.6679 0.6105 -0.0356 -0.0272 0.0188  133 ASP B CB  
1946 C CG  . ASP B 133 ? 0.6616 0.8280 0.7583 -0.0463 -0.0356 0.0234  133 ASP B CG  
1947 O OD1 . ASP B 133 ? 0.7861 0.9743 0.8882 -0.0579 -0.0387 0.0286  133 ASP B OD1 
1948 O OD2 . ASP B 133 ? 0.7702 0.9245 0.8603 -0.0440 -0.0393 0.0220  133 ASP B OD2 
1949 N N   . ALA B 134 ? 0.4692 0.6088 0.5794 -0.0049 -0.0119 0.0149  134 ALA B N   
1950 C CA  . ALA B 134 ? 0.4855 0.6118 0.5907 0.0019  -0.0035 0.0097  134 ALA B CA  
1951 C C   . ALA B 134 ? 0.4692 0.6123 0.5920 0.0098  0.0036  0.0153  134 ALA B C   
1952 O O   . ALA B 134 ? 0.4318 0.5739 0.5529 0.0097  0.0108  0.0132  134 ALA B O   
1953 C CB  . ALA B 134 ? 0.3566 0.4598 0.4514 0.0098  -0.0031 0.0041  134 ALA B CB  
1954 N N   . LEU B 135 ? 0.4367 0.5951 0.5766 0.0173  0.0024  0.0232  135 LEU B N   
1955 C CA  . LEU B 135 ? 0.4207 0.5972 0.5800 0.0265  0.0102  0.0305  135 LEU B CA  
1956 C C   . LEU B 135 ? 0.4843 0.6860 0.6538 0.0174  0.0109  0.0351  135 LEU B C   
1957 O O   . LEU B 135 ? 0.4828 0.6892 0.6582 0.0212  0.0203  0.0355  135 LEU B O   
1958 C CB  . LEU B 135 ? 0.4822 0.6723 0.6584 0.0360  0.0079  0.0402  135 LEU B CB  
1959 C CG  . LEU B 135 ? 0.5757 0.7786 0.7716 0.0505  0.0183  0.0483  135 LEU B CG  
1960 C CD1 . LEU B 135 ? 0.5411 0.7215 0.7266 0.0571  0.0309  0.0402  135 LEU B CD1 
1961 C CD2 . LEU B 135 ? 0.5927 0.7950 0.7974 0.0624  0.0176  0.0553  135 LEU B CD2 
1962 N N   . GLN B 136 ? 0.4079 0.6255 0.5784 0.0043  0.0015  0.0385  136 GLN B N   
1963 C CA  . GLN B 136 ? 0.4463 0.6883 0.6247 -0.0076 0.0012  0.0427  136 GLN B CA  
1964 C C   . GLN B 136 ? 0.4088 0.6335 0.5705 -0.0147 0.0074  0.0336  136 GLN B C   
1965 O O   . GLN B 136 ? 0.5083 0.7494 0.6781 -0.0193 0.0126  0.0363  136 GLN B O   
1966 C CB  . GLN B 136 ? 0.4686 0.7255 0.6453 -0.0230 -0.0104 0.0465  136 GLN B CB  
1967 C CG  . GLN B 136 ? 0.5401 0.8203 0.7350 -0.0178 -0.0175 0.0578  136 GLN B CG  
1968 C CD  . GLN B 136 ? 0.5543 0.8661 0.7782 -0.0069 -0.0125 0.0699  136 GLN B CD  
1969 O OE1 . GLN B 136 ? 0.6379 0.9493 0.8737 0.0099  -0.0088 0.0751  136 GLN B OE1 
1970 N NE2 . GLN B 136 ? 0.5180 0.8569 0.7533 -0.0164 -0.0114 0.0748  136 GLN B NE2 
1971 N N   . MET B 137 ? 0.4228 0.6155 0.5614 -0.0154 0.0072  0.0238  137 MET B N   
1972 C CA  . MET B 137 ? 0.4988 0.6732 0.6201 -0.0206 0.0131  0.0161  137 MET B CA  
1973 C C   . MET B 137 ? 0.4134 0.5851 0.5396 -0.0100 0.0240  0.0152  137 MET B C   
1974 O O   . MET B 137 ? 0.4304 0.6023 0.5524 -0.0153 0.0303  0.0134  137 MET B O   
1975 C CB  . MET B 137 ? 0.4533 0.5968 0.5514 -0.0215 0.0101  0.0078  137 MET B CB  
1976 C CG  . MET B 137 ? 0.4947 0.6348 0.5816 -0.0345 0.0028  0.0068  137 MET B CG  
1977 S SD  . MET B 137 ? 0.5620 0.6677 0.6253 -0.0322 0.0011  -0.0012 137 MET B SD  
1978 C CE  . MET B 137 ? 0.5129 0.6009 0.5590 -0.0355 0.0092  -0.0065 137 MET B CE  
1979 N N   . LEU B 138 ? 0.4549 0.6217 0.5880 0.0043  0.0273  0.0161  138 LEU B N   
1980 C CA  . LEU B 138 ? 0.4182 0.5815 0.5554 0.0144  0.0392  0.0156  138 LEU B CA  
1981 C C   . LEU B 138 ? 0.4420 0.6368 0.6025 0.0146  0.0449  0.0245  138 LEU B C   
1982 O O   . LEU B 138 ? 0.4240 0.6191 0.5843 0.0150  0.0547  0.0232  138 LEU B O   
1983 C CB  . LEU B 138 ? 0.3702 0.5204 0.5089 0.0287  0.0423  0.0152  138 LEU B CB  
1984 C CG  . LEU B 138 ? 0.2985 0.4181 0.4153 0.0300  0.0389  0.0064  138 LEU B CG  
1985 C CD1 . LEU B 138 ? 0.3062 0.4153 0.4260 0.0427  0.0438  0.0069  138 LEU B CD1 
1986 C CD2 . LEU B 138 ? 0.3080 0.4069 0.4038 0.0260  0.0433  -0.0018 138 LEU B CD2 
1987 N N   . LEU B 139 ? 0.3997 0.6227 0.5807 0.0140  0.0386  0.0343  139 LEU B N   
1988 C CA  . LEU B 139 ? 0.4535 0.7113 0.6611 0.0163  0.0437  0.0450  139 LEU B CA  
1989 C C   . LEU B 139 ? 0.4926 0.7681 0.7007 -0.0005 0.0425  0.0457  139 LEU B C   
1990 O O   . LEU B 139 ? 0.4612 0.7576 0.6850 0.0005  0.0509  0.0509  139 LEU B O   
1991 C CB  . LEU B 139 ? 0.4320 0.7161 0.6617 0.0216  0.0367  0.0568  139 LEU B CB  
1992 C CG  . LEU B 139 ? 0.5378 0.8055 0.7691 0.0392  0.0401  0.0577  139 LEU B CG  
1993 C CD1 . LEU B 139 ? 0.5012 0.7935 0.7516 0.0429  0.0316  0.0698  139 LEU B CD1 
1994 C CD2 . LEU B 139 ? 0.4998 0.7617 0.7388 0.0548  0.0565  0.0587  139 LEU B CD2 
1995 N N   . ASP B 140 ? 0.4450 0.7117 0.6355 -0.0163 0.0333  0.0406  140 ASP B N   
1996 C CA  . ASP B 140 ? 0.5048 0.7825 0.6910 -0.0338 0.0332  0.0400  140 ASP B CA  
1997 C C   . ASP B 140 ? 0.5062 0.7532 0.6678 -0.0375 0.0406  0.0294  140 ASP B C   
1998 O O   . ASP B 140 ? 0.6078 0.8582 0.7621 -0.0521 0.0421  0.0278  140 ASP B O   
1999 C CB  . ASP B 140 ? 0.5243 0.8101 0.7040 -0.0509 0.0206  0.0412  140 ASP B CB  
2000 C CG  . ASP B 140 ? 0.6193 0.8682 0.7698 -0.0554 0.0160  0.0309  140 ASP B CG  
2001 O OD1 . ASP B 140 ? 0.7623 0.9811 0.8973 -0.0467 0.0213  0.0231  140 ASP B OD1 
2002 O OD2 . ASP B 140 ? 0.7458 0.9966 0.8885 -0.0680 0.0072  0.0313  140 ASP B OD2 
2003 N N   . GLY B 141 ? 0.4897 0.7066 0.6373 -0.0256 0.0448  0.0224  141 GLY B N   
2004 C CA  . GLY B 141 ? 0.4472 0.6383 0.5742 -0.0263 0.0527  0.0143  141 GLY B CA  
2005 C C   . GLY B 141 ? 0.4846 0.6467 0.5839 -0.0345 0.0478  0.0064  141 GLY B C   
2006 O O   . GLY B 141 ? 0.4655 0.6060 0.5466 -0.0349 0.0538  0.0006  141 GLY B O   
2007 N N   . SER B 142 ? 0.4036 0.5642 0.4985 -0.0407 0.0378  0.0065  142 SER B N   
2008 C CA  . SER B 142 ? 0.4136 0.5463 0.4829 -0.0471 0.0348  -0.0001 142 SER B CA  
2009 C C   . SER B 142 ? 0.5208 0.6281 0.5778 -0.0350 0.0344  -0.0052 142 SER B C   
2010 O O   . SER B 142 ? 0.5558 0.6398 0.5925 -0.0375 0.0336  -0.0098 142 SER B O   
2011 C CB  . SER B 142 ? 0.4282 0.5661 0.4954 -0.0582 0.0258  0.0015  142 SER B CB  
2012 O OG  . SER B 142 ? 0.5909 0.7488 0.6772 -0.0527 0.0194  0.0071  142 SER B OG  
2013 N N   . ALA B 143 ? 0.4660 0.5774 0.5348 -0.0223 0.0354  -0.0039 143 ALA B N   
2014 C CA  . ALA B 143 ? 0.3607 0.4497 0.4176 -0.0123 0.0360  -0.0089 143 ALA B CA  
2015 C C   . ALA B 143 ? 0.4324 0.5234 0.4967 -0.0024 0.0449  -0.0086 143 ALA B C   
2016 O O   . ALA B 143 ? 0.4919 0.6036 0.5764 0.0018  0.0482  -0.0031 143 ALA B O   
2017 C CB  . ALA B 143 ? 0.3612 0.4464 0.4199 -0.0080 0.0276  -0.0088 143 ALA B CB  
2018 N N   . GLN B 144 ? 0.3359 0.4053 0.3830 0.0015  0.0492  -0.0141 144 GLN B N   
2019 C CA  . GLN B 144 ? 0.3984 0.4639 0.4470 0.0099  0.0591  -0.0153 144 GLN B CA  
2020 C C   . GLN B 144 ? 0.3850 0.4399 0.4328 0.0192  0.0579  -0.0172 144 GLN B C   
2021 O O   . GLN B 144 ? 0.4579 0.5143 0.5137 0.0274  0.0663  -0.0161 144 GLN B O   
2022 C CB  . GLN B 144 ? 0.4602 0.5073 0.4877 0.0073  0.0653  -0.0203 144 GLN B CB  
2023 C CG  . GLN B 144 ? 0.4628 0.5182 0.4903 -0.0011 0.0704  -0.0186 144 GLN B CG  
2024 C CD  . GLN B 144 ? 0.5787 0.6372 0.6030 -0.0114 0.0626  -0.0173 144 GLN B CD  
2025 O OE1 . GLN B 144 ? 0.5317 0.5724 0.5385 -0.0137 0.0573  -0.0202 144 GLN B OE1 
2026 N NE2 . GLN B 144 ? 0.5631 0.6442 0.6037 -0.0181 0.0622  -0.0125 144 GLN B NE2 
2027 N N   . LEU B 145 ? 0.4192 0.4628 0.4572 0.0179  0.0487  -0.0199 145 LEU B N   
2028 C CA  . LEU B 145 ? 0.3764 0.4086 0.4113 0.0245  0.0469  -0.0222 145 LEU B CA  
2029 C C   . LEU B 145 ? 0.3897 0.4269 0.4304 0.0229  0.0361  -0.0202 145 LEU B C   
2030 O O   . LEU B 145 ? 0.2912 0.3326 0.3302 0.0160  0.0297  -0.0192 145 LEU B O   
2031 C CB  . LEU B 145 ? 0.3357 0.3449 0.3471 0.0237  0.0475  -0.0288 145 LEU B CB  
2032 C CG  . LEU B 145 ? 0.3699 0.3687 0.3704 0.0252  0.0588  -0.0320 145 LEU B CG  
2033 C CD1 . LEU B 145 ? 0.3729 0.3510 0.3484 0.0220  0.0565  -0.0376 145 LEU B CD1 
2034 C CD2 . LEU B 145 ? 0.4221 0.4208 0.4320 0.0336  0.0688  -0.0313 145 LEU B CD2 
2035 N N   . ALA B 146 ? 0.3607 0.3953 0.4068 0.0291  0.0351  -0.0198 146 ALA B N   
2036 C CA  . ALA B 146 ? 0.3792 0.4169 0.4300 0.0281  0.0257  -0.0180 146 ALA B CA  
2037 C C   . ALA B 146 ? 0.3433 0.3642 0.3849 0.0320  0.0247  -0.0221 146 ALA B C   
2038 O O   . ALA B 146 ? 0.3929 0.4042 0.4314 0.0375  0.0325  -0.0240 146 ALA B O   
2039 C CB  . ALA B 146 ? 0.2903 0.3489 0.3624 0.0307  0.0247  -0.0105 146 ALA B CB  
2040 N N   . LEU B 147 ? 0.3742 0.3907 0.4103 0.0284  0.0160  -0.0235 147 LEU B N   
2041 C CA  . LEU B 147 ? 0.4003 0.4046 0.4303 0.0305  0.0137  -0.0263 147 LEU B CA  
2042 C C   . LEU B 147 ? 0.4001 0.4133 0.4438 0.0330  0.0098  -0.0217 147 LEU B C   
2043 O O   . LEU B 147 ? 0.3678 0.3899 0.4161 0.0289  0.0028  -0.0191 147 LEU B O   
2044 C CB  . LEU B 147 ? 0.3844 0.3797 0.4002 0.0252  0.0070  -0.0301 147 LEU B CB  
2045 C CG  . LEU B 147 ? 0.5287 0.5108 0.5271 0.0233  0.0100  -0.0350 147 LEU B CG  
2046 C CD1 . LEU B 147 ? 0.5171 0.5010 0.5120 0.0225  0.0156  -0.0348 147 LEU B CD1 
2047 C CD2 . LEU B 147 ? 0.4800 0.4579 0.4681 0.0189  0.0020  -0.0365 147 LEU B CD2 
2048 N N   . MET B 148 ? 0.3824 0.3915 0.4312 0.0396  0.0150  -0.0204 148 MET B N   
2049 C CA  . MET B 148 ? 0.4041 0.4219 0.4663 0.0433  0.0123  -0.0145 148 MET B CA  
2050 C C   . MET B 148 ? 0.4503 0.4511 0.5056 0.0466  0.0140  -0.0171 148 MET B C   
2051 O O   . MET B 148 ? 0.4864 0.4697 0.5286 0.0472  0.0201  -0.0227 148 MET B O   
2052 C CB  . MET B 148 ? 0.3516 0.3857 0.4314 0.0500  0.0182  -0.0069 148 MET B CB  
2053 C CG  . MET B 148 ? 0.3663 0.4197 0.4541 0.0449  0.0162  -0.0037 148 MET B CG  
2054 S SD  . MET B 148 ? 0.5533 0.6300 0.6637 0.0524  0.0237  0.0060  148 MET B SD  
2055 C CE  . MET B 148 ? 0.5811 0.6845 0.7019 0.0417  0.0140  0.0117  148 MET B CE  
2056 N N   . PHE B 149 ? 0.4371 0.4422 0.4994 0.0473  0.0087  -0.0131 149 PHE B N   
2057 C CA  . PHE B 149 ? 0.4985 0.4897 0.5580 0.0516  0.0115  -0.0131 149 PHE B CA  
2058 C C   . PHE B 149 ? 0.5168 0.5197 0.5933 0.0605  0.0149  -0.0036 149 PHE B C   
2059 O O   . PHE B 149 ? 0.7244 0.7487 0.8149 0.0612  0.0126  0.0027  149 PHE B O   
2060 C CB  . PHE B 149 ? 0.4630 0.4493 0.5160 0.0450  0.0029  -0.0157 149 PHE B CB  
2061 C CG  . PHE B 149 ? 0.4715 0.4738 0.5355 0.0433  -0.0050 -0.0096 149 PHE B CG  
2062 C CD1 . PHE B 149 ? 0.4763 0.4923 0.5431 0.0377  -0.0104 -0.0088 149 PHE B CD1 
2063 C CD2 . PHE B 149 ? 0.5089 0.5102 0.5777 0.0462  -0.0065 -0.0050 149 PHE B CD2 
2064 C CE1 . PHE B 149 ? 0.4727 0.5010 0.5462 0.0343  -0.0170 -0.0040 149 PHE B CE1 
2065 C CE2 . PHE B 149 ? 0.5404 0.5555 0.6167 0.0432  -0.0139 0.0004  149 PHE B CE2 
2066 C CZ  . PHE B 149 ? 0.5473 0.5757 0.6254 0.0368  -0.0191 0.0006  149 PHE B CZ  
2067 N N   . GLU B 150 ? 0.5642 0.5533 0.6391 0.0670  0.0202  -0.0020 150 GLU B N   
2068 C CA  . GLU B 150 ? 0.8669 0.8629 0.9569 0.0789  0.0271  0.0079  150 GLU B CA  
2069 C C   . GLU B 150 ? 0.8232 0.8507 0.9339 0.0805  0.0218  0.0180  150 GLU B C   
2070 O O   . GLU B 150 ? 0.7162 0.7566 0.8374 0.0850  0.0276  0.0217  150 GLU B O   
2071 C CB  . GLU B 150 ? 0.9368 0.9208 1.0249 0.0829  0.0272  0.0111  150 GLU B CB  
2072 C CG  . GLU B 150 ? 1.0113 0.9912 1.1089 0.0976  0.0389  0.0199  150 GLU B CG  
2073 C CD  . GLU B 150 ? 1.0908 1.1019 1.2126 0.1044  0.0352  0.0337  150 GLU B CD  
2074 O OE1 . GLU B 150 ? 1.0476 1.0711 1.1752 0.1011  0.0249  0.0393  150 GLU B OE1 
2075 O OE2 . GLU B 150 ? 1.0965 1.1212 1.2315 0.1121  0.0423  0.0393  150 GLU B OE2 
2076 N N   . LEU B 154 ? 0.6697 0.8034 0.8670 0.1089  0.0420  0.0592  154 LEU B N   
2077 C CA  . LEU B 154 ? 0.6331 0.7705 0.8349 0.1125  0.0534  0.0579  154 LEU B CA  
2078 C C   . LEU B 154 ? 0.7024 0.8606 0.9297 0.1283  0.0640  0.0723  154 LEU B C   
2079 O O   . LEU B 154 ? 0.8136 0.9741 1.0506 0.1391  0.0651  0.0820  154 LEU B O   
2080 C CB  . LEU B 154 ? 0.6255 0.7253 0.8034 0.1134  0.0638  0.0445  154 LEU B CB  
2081 C CG  . LEU B 154 ? 0.6293 0.7190 0.7882 0.0991  0.0585  0.0319  154 LEU B CG  
2082 C CD1 . LEU B 154 ? 0.6507 0.7414 0.8010 0.0866  0.0427  0.0282  154 LEU B CD1 
2083 C CD2 . LEU B 154 ? 0.5987 0.6538 0.7347 0.1005  0.0689  0.0206  154 LEU B CD2 
2084 N N   . ASP B 155 ? 0.6579 0.8313 0.8962 0.1304  0.0725  0.0745  155 ASP B N   
2085 C CA  . ASP B 155 ? 0.6740 0.8714 0.9396 0.1460  0.0835  0.0894  155 ASP B CA  
2086 C C   . ASP B 155 ? 0.6343 0.8197 0.8969 0.1524  0.1014  0.0846  155 ASP B C   
2087 O O   . ASP B 155 ? 0.6333 0.7858 0.8700 0.1470  0.1064  0.0699  155 ASP B O   
2088 C CB  . ASP B 155 ? 0.6958 0.9421 0.9879 0.1401  0.0715  0.1030  155 ASP B CB  
2089 C CG  . ASP B 155 ? 0.7517 1.0174 1.0473 0.1277  0.0703  0.0996  155 ASP B CG  
2090 O OD1 . ASP B 155 ? 0.7396 1.0079 1.0428 0.1349  0.0846  0.1005  155 ASP B OD1 
2091 O OD2 . ASP B 155 ? 0.7679 1.0448 1.0575 0.1101  0.0557  0.0959  155 ASP B OD2 
2092 N N   . ASN B 156 ? 0.6167 0.8257 0.8995 0.1598  0.1085  0.0956  156 ASN B N   
2093 C CA  . ASN B 156 ? 0.6198 0.8182 0.8999 0.1659  0.1258  0.0926  156 ASN B CA  
2094 C C   . ASN B 156 ? 0.5560 0.7573 0.8307 0.1556  0.1281  0.0831  156 ASN B C   
2095 O O   . ASN B 156 ? 0.4561 0.6354 0.7183 0.1592  0.1433  0.0757  156 ASN B O   
2096 C CB  . ASN B 156 ? 0.5399 0.7681 0.8435 0.1727  0.1288  0.1074  156 ASN B CB  
2097 C CG  . ASN B 156 ? 0.6525 0.8647 0.9528 0.1827  0.1487  0.1063  156 ASN B CG  
2098 O OD1 . ASN B 156 ? 0.8339 1.0698 1.1487 0.1812  0.1527  0.1107  156 ASN B OD1 
2099 N ND2 . ASN B 156 ? 0.8150 0.9862 1.0953 0.1918  0.1615  0.1003  156 ASN B ND2 
2100 N N   . ARG B 157 ? 0.4383 0.6592 0.7135 0.1390  0.1115  0.0811  157 ARG B N   
2101 C CA  . ARG B 157 ? 0.5207 0.7460 0.7881 0.1253  0.1106  0.0733  157 ARG B CA  
2102 C C   . ARG B 157 ? 0.5779 0.7649 0.8100 0.1140  0.1073  0.0557  157 ARG B C   
2103 O O   . ARG B 157 ? 0.4651 0.6497 0.6871 0.1043  0.1088  0.0488  157 ARG B O   
2104 C CB  . ARG B 157 ? 0.5251 0.7903 0.8091 0.1114  0.0952  0.0806  157 ARG B CB  
2105 C CG  . ARG B 157 ? 0.6034 0.9130 0.9222 0.1179  0.1008  0.0967  157 ARG B CG  
2106 C CD  . ARG B 157 ? 0.5533 0.9018 0.8870 0.1032  0.0832  0.1051  157 ARG B CD  
2107 N NE  . ARG B 157 ? 0.6548 1.0005 0.9849 0.1022  0.0696  0.1076  157 ARG B NE  
2108 C CZ  . ARG B 157 ? 0.6417 1.0059 0.9714 0.0862  0.0524  0.1096  157 ARG B CZ  
2109 N NH1 . ARG B 157 ? 0.6697 1.0547 1.0006 0.0687  0.0463  0.1086  157 ARG B NH1 
2110 N NH2 . ARG B 157 ? 0.5191 0.8788 0.8452 0.0870  0.0418  0.1123  157 ARG B NH2 
2111 N N   . GLU B 158 ? 0.4920 0.6502 0.7055 0.1150  0.1030  0.0491  158 GLU B N   
2112 C CA  . GLU B 158 ? 0.4889 0.6133 0.6706 0.1053  0.0998  0.0339  158 GLU B CA  
2113 C C   . GLU B 158 ? 0.5612 0.6495 0.7245 0.1145  0.1148  0.0268  158 GLU B C   
2114 O O   . GLU B 158 ? 0.5743 0.6565 0.7455 0.1283  0.1248  0.0326  158 GLU B O   
2115 C CB  . GLU B 158 ? 0.5332 0.6514 0.7049 0.0967  0.0832  0.0305  158 GLU B CB  
2116 C CG  . GLU B 158 ? 0.5710 0.7200 0.7564 0.0864  0.0685  0.0367  158 GLU B CG  
2117 C CD  . GLU B 158 ? 0.5996 0.7763 0.8108 0.0939  0.0651  0.0509  158 GLU B CD  
2118 O OE1 . GLU B 158 ? 0.6185 0.7839 0.8279 0.1007  0.0631  0.0529  158 GLU B OE1 
2119 O OE2 . GLU B 158 ? 0.5616 0.7722 0.7946 0.0926  0.0642  0.0607  158 GLU B OE2 
2120 N N   . GLN B 159 ? 0.5397 0.6031 0.6770 0.1063  0.1169  0.0146  159 GLN B N   
2121 C CA  . GLN B 159 ? 0.4470 0.4719 0.5585 0.1090  0.1263  0.0050  159 GLN B CA  
2122 C C   . GLN B 159 ? 0.5186 0.5261 0.6077 0.0969  0.1121  -0.0044 159 GLN B C   
2123 O O   . GLN B 159 ? 0.4379 0.4604 0.5294 0.0870  0.0976  -0.0045 159 GLN B O   
2124 C CB  . GLN B 159 ? 0.5132 0.5223 0.6104 0.1091  0.1414  -0.0012 159 GLN B CB  
2125 C CG  . GLN B 159 ? 0.5813 0.6089 0.7011 0.1207  0.1568  0.0079  159 GLN B CG  
2126 C CD  . GLN B 159 ? 0.7644 0.7620 0.8686 0.1295  0.1785  0.0033  159 GLN B CD  
2127 O OE1 . GLN B 159 ? 0.9173 0.8995 1.0224 0.1416  0.1894  0.0061  159 GLN B OE1 
2128 N NE2 . GLN B 159 ? 0.7623 0.7491 0.8500 0.1231  0.1856  -0.0040 159 GLN B NE2 
2129 N N   . PHE B 160 ? 0.5059 0.4810 0.5723 0.0972  0.1170  -0.0123 160 PHE B N   
2130 C CA  . PHE B 160 ? 0.4626 0.4229 0.5089 0.0860  0.1042  -0.0204 160 PHE B CA  
2131 C C   . PHE B 160 ? 0.4849 0.4093 0.5020 0.0836  0.1130  -0.0305 160 PHE B C   
2132 O O   . PHE B 160 ? 0.5275 0.4347 0.5399 0.0920  0.1295  -0.0308 160 PHE B O   
2133 C CB  . PHE B 160 ? 0.4991 0.4685 0.5567 0.0869  0.0927  -0.0155 160 PHE B CB  
2134 C CG  . PHE B 160 ? 0.5508 0.5032 0.6079 0.0967  0.1015  -0.0134 160 PHE B CG  
2135 C CD1 . PHE B 160 ? 0.5941 0.5158 0.6269 0.0923  0.1028  -0.0221 160 PHE B CD1 
2136 C CD2 . PHE B 160 ? 0.5813 0.5486 0.6619 0.1102  0.1089  -0.0022 160 PHE B CD2 
2137 C CE1 . PHE B 160 ? 0.6513 0.5540 0.6813 0.1007  0.1123  -0.0204 160 PHE B CE1 
2138 C CE2 . PHE B 160 ? 0.6563 0.6057 0.7356 0.1205  0.1183  0.0007  160 PHE B CE2 
2139 C CZ  . PHE B 160 ? 0.6352 0.5504 0.6881 0.1155  0.1205  -0.0089 160 PHE B CZ  
2140 N N   . VAL B 161 ? 0.4970 0.4103 0.4939 0.0715  0.1022  -0.0382 161 VAL B N   
2141 C CA  . VAL B 161 ? 0.5761 0.4577 0.5441 0.0655  0.1059  -0.0477 161 VAL B CA  
2142 C C   . VAL B 161 ? 0.5161 0.3978 0.4793 0.0574  0.0904  -0.0497 161 VAL B C   
2143 O O   . VAL B 161 ? 0.4743 0.3764 0.4478 0.0529  0.0765  -0.0469 161 VAL B O   
2144 C CB  . VAL B 161 ? 0.4993 0.3671 0.4432 0.0571  0.1098  -0.0554 161 VAL B CB  
2145 C CG1 . VAL B 161 ? 0.6598 0.5259 0.6077 0.0652  0.1269  -0.0537 161 VAL B CG1 
2146 C CG2 . VAL B 161 ? 0.4980 0.3834 0.4424 0.0480  0.0945  -0.0554 161 VAL B CG2 
2147 N N   . GLU B 162 ? 0.4709 0.3285 0.4177 0.0551  0.0941  -0.0547 162 GLU B N   
2148 C CA  . GLU B 162 ? 0.6248 0.4819 0.5677 0.0476  0.0811  -0.0564 162 GLU B CA  
2149 C C   . GLU B 162 ? 0.6052 0.4621 0.5305 0.0340  0.0700  -0.0624 162 GLU B C   
2150 O O   . GLU B 162 ? 0.6922 0.5342 0.5963 0.0280  0.0752  -0.0685 162 GLU B O   
2151 C CB  . GLU B 162 ? 0.6240 0.4541 0.5536 0.0485  0.0898  -0.0598 162 GLU B CB  
2152 C CG  . GLU B 162 ? 0.7175 0.5485 0.6657 0.0637  0.1002  -0.0519 162 GLU B CG  
2153 C CD  . GLU B 162 ? 0.8847 0.6833 0.8161 0.0653  0.1118  -0.0554 162 GLU B CD  
2154 O OE1 . GLU B 162 ? 0.9379 0.7096 0.8403 0.0550  0.1166  -0.0653 162 GLU B OE1 
2155 O OE2 . GLU B 162 ? 0.9667 0.7658 0.9126 0.0762  0.1164  -0.0482 162 GLU B OE2 
2156 N N   . LEU B 163 ? 0.5754 0.4492 0.5096 0.0294  0.0550  -0.0600 163 LEU B N   
2157 C CA  . LEU B 163 ? 0.6475 0.5252 0.5690 0.0182  0.0437  -0.0633 163 LEU B CA  
2158 C C   . LEU B 163 ? 0.7052 0.5732 0.6142 0.0091  0.0372  -0.0673 163 LEU B C   
2159 O O   . LEU B 163 ? 0.8488 0.7011 0.7344 -0.0004 0.0383  -0.0736 163 LEU B O   
2160 C CB  . LEU B 163 ? 0.5872 0.4905 0.5263 0.0194  0.0327  -0.0574 163 LEU B CB  
2161 C CG  . LEU B 163 ? 0.6152 0.5290 0.5623 0.0239  0.0370  -0.0543 163 LEU B CG  
2162 C CD1 . LEU B 163 ? 0.5515 0.4855 0.5104 0.0226  0.0265  -0.0496 163 LEU B CD1 
2163 C CD2 . LEU B 163 ? 0.6331 0.5333 0.5593 0.0196  0.0434  -0.0595 163 LEU B CD2 
2164 N N   . LYS B 164 ? 0.5768 0.4543 0.5000 0.0109  0.0304  -0.0636 164 LYS B N   
2165 C CA  . LYS B 164 ? 0.6995 0.5723 0.6133 0.0013  0.0229  -0.0666 164 LYS B CA  
2166 C C   . LYS B 164 ? 0.6111 0.4917 0.5423 0.0058  0.0191  -0.0620 164 LYS B C   
2167 O O   . LYS B 164 ? 0.6325 0.5258 0.5830 0.0151  0.0195  -0.0560 164 LYS B O   
2168 C CB  . LYS B 164 ? 0.7026 0.5897 0.6121 -0.0074 0.0106  -0.0665 164 LYS B CB  
2169 C CG  . LYS B 164 ? 0.7819 0.6927 0.7122 -0.0020 0.0025  -0.0597 164 LYS B CG  
2170 C CD  . LYS B 164 ? 0.9329 0.8558 0.8583 -0.0079 -0.0069 -0.0584 164 LYS B CD  
2171 C CE  . LYS B 164 ? 0.9836 0.9224 0.9236 -0.0013 -0.0095 -0.0527 164 LYS B CE  
2172 N NZ  . LYS B 164 ? 1.0329 0.9687 0.9781 0.0058  -0.0003 -0.0522 164 LYS B NZ  
2173 N N   . ARG B 165 ? 0.6102 0.4837 0.5332 -0.0023 0.0150  -0.0648 165 ARG B N   
2174 C CA  . ARG B 165 ? 0.5764 0.4563 0.5123 -0.0005 0.0103  -0.0611 165 ARG B CA  
2175 C C   . ARG B 165 ? 0.6646 0.5659 0.6087 -0.0058 -0.0029 -0.0585 165 ARG B C   
2176 O O   . ARG B 165 ? 0.6847 0.5899 0.6187 -0.0145 -0.0086 -0.0610 165 ARG B O   
2177 C CB  . ARG B 165 ? 0.5860 0.4433 0.5070 -0.0067 0.0155  -0.0658 165 ARG B CB  
2178 C CG  . ARG B 165 ? 0.7479 0.6072 0.6796 -0.0048 0.0127  -0.0622 165 ARG B CG  
2179 C CD  . ARG B 165 ? 0.8260 0.6599 0.7390 -0.0130 0.0186  -0.0678 165 ARG B CD  
2180 N NE  . ARG B 165 ? 0.9477 0.7853 0.8682 -0.0152 0.0136  -0.0651 165 ARG B NE  
2181 C CZ  . ARG B 165 ? 0.9115 0.7660 0.8367 -0.0237 0.0024  -0.0647 165 ARG B CZ  
2182 N NH1 . ARG B 165 ? 0.8569 0.7260 0.7794 -0.0312 -0.0056 -0.0663 165 ARG B NH1 
2183 N NH2 . ARG B 165 ? 0.9106 0.7676 0.8434 -0.0243 -0.0005 -0.0618 165 ARG B NH2 
2184 N N   . GLU B 166 ? 0.5232 0.4384 0.4853 -0.0003 -0.0072 -0.0528 166 GLU B N   
2185 C CA  . GLU B 166 ? 0.5652 0.4982 0.5358 -0.0037 -0.0174 -0.0498 166 GLU B CA  
2186 C C   . GLU B 166 ? 0.5479 0.4800 0.5241 -0.0052 -0.0196 -0.0484 166 GLU B C   
2187 O O   . GLU B 166 ? 0.5056 0.4361 0.4910 0.0016  -0.0165 -0.0450 166 GLU B O   
2188 C CB  . GLU B 166 ? 0.5186 0.4676 0.5027 0.0028  -0.0200 -0.0447 166 GLU B CB  
2189 C CG  . GLU B 166 ? 0.7060 0.6580 0.6843 0.0030  -0.0193 -0.0456 166 GLU B CG  
2190 C CD  . GLU B 166 ? 0.8022 0.7617 0.7738 -0.0037 -0.0265 -0.0458 166 GLU B CD  
2191 O OE1 . GLU B 166 ? 0.7789 0.7459 0.7547 -0.0071 -0.0324 -0.0441 166 GLU B OE1 
2192 O OE2 . GLU B 166 ? 0.7734 0.7324 0.7361 -0.0050 -0.0260 -0.0468 166 GLU B OE2 
2193 N N   . ALA B 167 ? 0.4662 0.4006 0.4371 -0.0144 -0.0249 -0.0503 167 ALA B N   
2194 C CA  . ALA B 167 ? 0.5385 0.4719 0.5138 -0.0171 -0.0267 -0.0492 167 ALA B CA  
2195 C C   . ALA B 167 ? 0.4764 0.4278 0.4675 -0.0134 -0.0324 -0.0436 167 ALA B C   
2196 O O   . ALA B 167 ? 0.4245 0.3900 0.4205 -0.0125 -0.0367 -0.0413 167 ALA B O   
2197 C CB  . ALA B 167 ? 0.4797 0.4097 0.4432 -0.0298 -0.0298 -0.0534 167 ALA B CB  
2198 N N   . LEU B 168 ? 0.4865 0.4356 0.4842 -0.0111 -0.0315 -0.0411 168 LEU B N   
2199 C CA  . LEU B 168 ? 0.4171 0.3796 0.4266 -0.0092 -0.0358 -0.0365 168 LEU B CA  
2200 C C   . LEU B 168 ? 0.5252 0.4860 0.5344 -0.0155 -0.0373 -0.0368 168 LEU B C   
2201 O O   . LEU B 168 ? 0.4445 0.3914 0.4449 -0.0200 -0.0343 -0.0399 168 LEU B O   
2202 C CB  . LEU B 168 ? 0.3519 0.3154 0.3694 -0.0011 -0.0337 -0.0323 168 LEU B CB  
2203 C CG  . LEU B 168 ? 0.4202 0.3885 0.4402 0.0043  -0.0322 -0.0313 168 LEU B CG  
2204 C CD1 . LEU B 168 ? 0.4337 0.3917 0.4518 0.0095  -0.0260 -0.0315 168 LEU B CD1 
2205 C CD2 . LEU B 168 ? 0.4251 0.4045 0.4539 0.0071  -0.0346 -0.0268 168 LEU B CD2 
2206 N N   . ILE B 169 ? 0.4624 0.4361 0.4802 -0.0160 -0.0409 -0.0335 169 ILE B N   
2207 C CA  . ILE B 169 ? 0.4017 0.3772 0.4207 -0.0225 -0.0424 -0.0333 169 ILE B CA  
2208 C C   . ILE B 169 ? 0.4540 0.4330 0.4810 -0.0190 -0.0421 -0.0291 169 ILE B C   
2209 O O   . ILE B 169 ? 0.4110 0.3995 0.4442 -0.0148 -0.0430 -0.0262 169 ILE B O   
2210 C CB  . ILE B 169 ? 0.5059 0.4965 0.5270 -0.0287 -0.0468 -0.0332 169 ILE B CB  
2211 C CG1 . ILE B 169 ? 0.6040 0.5917 0.6147 -0.0338 -0.0480 -0.0372 169 ILE B CG1 
2212 C CG2 . ILE B 169 ? 0.5406 0.5353 0.5643 -0.0363 -0.0479 -0.0327 169 ILE B CG2 
2213 C CD1 . ILE B 169 ? 0.6051 0.6119 0.6191 -0.0384 -0.0537 -0.0350 169 ILE B CD1 
2214 N N   . PRO B 170 ? 0.4792 0.4490 0.5043 -0.0213 -0.0402 -0.0288 170 PRO B N   
2215 C CA  . PRO B 170 ? 0.3952 0.3685 0.4258 -0.0200 -0.0401 -0.0250 170 PRO B CA  
2216 C C   . PRO B 170 ? 0.4309 0.4171 0.4672 -0.0244 -0.0416 -0.0241 170 PRO B C   
2217 O O   . PRO B 170 ? 0.3878 0.3769 0.4232 -0.0315 -0.0425 -0.0260 170 PRO B O   
2218 C CB  . PRO B 170 ? 0.3344 0.2929 0.3595 -0.0217 -0.0374 -0.0248 170 PRO B CB  
2219 C CG  . PRO B 170 ? 0.5033 0.4509 0.5199 -0.0263 -0.0356 -0.0293 170 PRO B CG  
2220 C CD  . PRO B 170 ? 0.4498 0.4036 0.4655 -0.0258 -0.0372 -0.0320 170 PRO B CD  
2221 N N   . VAL B 171 ? 0.3384 0.3328 0.3805 -0.0205 -0.0412 -0.0209 171 VAL B N   
2222 C CA  . VAL B 171 ? 0.4012 0.4089 0.4504 -0.0219 -0.0410 -0.0188 171 VAL B CA  
2223 C C   . VAL B 171 ? 0.3176 0.3239 0.3687 -0.0200 -0.0373 -0.0159 171 VAL B C   
2224 O O   . VAL B 171 ? 0.3585 0.3557 0.4047 -0.0176 -0.0362 -0.0153 171 VAL B O   
2225 C CB  . VAL B 171 ? 0.3174 0.3365 0.3705 -0.0179 -0.0425 -0.0174 171 VAL B CB  
2226 C CG1 . VAL B 171 ? 0.3667 0.3878 0.4162 -0.0215 -0.0462 -0.0203 171 VAL B CG1 
2227 C CG2 . VAL B 171 ? 0.2840 0.2982 0.3347 -0.0114 -0.0408 -0.0166 171 VAL B CG2 
2228 N N   . ILE B 172 ? 0.3255 0.3419 0.3834 -0.0215 -0.0352 -0.0136 172 ILE B N   
2229 C CA  . ILE B 172 ? 0.3769 0.3916 0.4357 -0.0199 -0.0299 -0.0109 172 ILE B CA  
2230 C C   . ILE B 172 ? 0.3109 0.3410 0.3801 -0.0173 -0.0270 -0.0072 172 ILE B C   
2231 O O   . ILE B 172 ? 0.4147 0.4590 0.4913 -0.0192 -0.0304 -0.0062 172 ILE B O   
2232 C CB  . ILE B 172 ? 0.3341 0.3406 0.3892 -0.0256 -0.0282 -0.0114 172 ILE B CB  
2233 C CG1 . ILE B 172 ? 0.3875 0.3858 0.4376 -0.0243 -0.0229 -0.0097 172 ILE B CG1 
2234 C CG2 . ILE B 172 ? 0.2957 0.3133 0.3586 -0.0312 -0.0278 -0.0108 172 ILE B CG2 
2235 C CD1 . ILE B 172 ? 0.4061 0.3926 0.4485 -0.0292 -0.0223 -0.0099 172 ILE B CD1 
2236 N N   . SER B 173 ? 0.3713 0.3986 0.4403 -0.0129 -0.0204 -0.0046 173 SER B N   
2237 C CA  . SER B 173 ? 0.3328 0.3740 0.4126 -0.0082 -0.0156 0.0004  173 SER B CA  
2238 C C   . SER B 173 ? 0.3462 0.4004 0.4362 -0.0132 -0.0149 0.0024  173 SER B C   
2239 O O   . SER B 173 ? 0.3962 0.4421 0.4816 -0.0191 -0.0136 0.0002  173 SER B O   
2240 C CB  . SER B 173 ? 0.3489 0.3792 0.4234 -0.0029 -0.0062 0.0023  173 SER B CB  
2241 O OG  . SER B 173 ? 0.3654 0.4075 0.4510 0.0027  0.0010  0.0080  173 SER B OG  
2242 N N   . LYS B 174 ? 0.3375 0.4133 0.4413 -0.0112 -0.0159 0.0073  174 LYS B N   
2243 C CA  . LYS B 174 ? 0.3558 0.4485 0.4713 -0.0170 -0.0156 0.0101  174 LYS B CA  
2244 C C   . LYS B 174 ? 0.3711 0.4602 0.4894 -0.0152 -0.0053 0.0126  174 LYS B C   
2245 O O   . LYS B 174 ? 0.4312 0.5280 0.5552 -0.0221 -0.0043 0.0131  174 LYS B O   
2246 C CB  . LYS B 174 ? 0.4087 0.5295 0.5402 -0.0146 -0.0189 0.0168  174 LYS B CB  
2247 C CG  . LYS B 174 ? 0.4068 0.5352 0.5357 -0.0213 -0.0299 0.0142  174 LYS B CG  
2248 C CD  . LYS B 174 ? 0.5095 0.6700 0.6549 -0.0244 -0.0343 0.0213  174 LYS B CD  
2249 C CE  . LYS B 174 ? 0.5411 0.7109 0.6842 -0.0251 -0.0432 0.0219  174 LYS B CE  
2250 N NZ  . LYS B 174 ? 0.5869 0.7525 0.7192 -0.0395 -0.0513 0.0149  174 LYS B NZ  
2251 N N   . THR B 175 ? 0.3875 0.4637 0.5001 -0.0070 0.0030  0.0138  175 THR B N   
2252 C CA  . THR B 175 ? 0.4597 0.5288 0.5716 -0.0053 0.0145  0.0157  175 THR B CA  
2253 C C   . THR B 175 ? 0.3971 0.4405 0.4903 -0.0110 0.0161  0.0097  175 THR B C   
2254 O O   . THR B 175 ? 0.4876 0.5212 0.5759 -0.0109 0.0258  0.0104  175 THR B O   
2255 C CB  . THR B 175 ? 0.3690 0.4369 0.4838 0.0066  0.0249  0.0210  175 THR B CB  
2256 O OG1 . THR B 175 ? 0.3862 0.4350 0.4857 0.0095  0.0242  0.0174  175 THR B OG1 
2257 C CG2 . THR B 175 ? 0.3522 0.4484 0.4874 0.0135  0.0236  0.0292  175 THR B CG2 
2258 N N   . HIS B 176 ? 0.4125 0.4455 0.4951 -0.0156 0.0074  0.0047  176 HIS B N   
2259 C CA  . HIS B 176 ? 0.4301 0.4429 0.4968 -0.0213 0.0073  0.0008  176 HIS B CA  
2260 C C   . HIS B 176 ? 0.4905 0.5049 0.5592 -0.0289 0.0081  0.0006  176 HIS B C   
2261 O O   . HIS B 176 ? 0.4556 0.4846 0.5349 -0.0327 0.0038  0.0010  176 HIS B O   
2262 C CB  . HIS B 176 ? 0.3490 0.3540 0.4074 -0.0229 -0.0021 -0.0029 176 HIS B CB  
2263 C CG  . HIS B 176 ? 0.3939 0.3803 0.4365 -0.0266 -0.0026 -0.0050 176 HIS B CG  
2264 N ND1 . HIS B 176 ? 0.4180 0.3970 0.4551 -0.0329 -0.0036 -0.0056 176 HIS B ND1 
2265 C CD2 . HIS B 176 ? 0.4195 0.3943 0.4504 -0.0256 -0.0027 -0.0058 176 HIS B CD2 
2266 C CE1 . HIS B 176 ? 0.4683 0.4334 0.4917 -0.0348 -0.0047 -0.0060 176 HIS B CE1 
2267 N NE2 . HIS B 176 ? 0.4925 0.4556 0.5121 -0.0311 -0.0045 -0.0063 176 HIS B NE2 
2268 N N   . PRO B 177 ? 0.4654 0.4647 0.5229 -0.0323 0.0139  -0.0002 177 PRO B N   
2269 C CA  . PRO B 177 ? 0.4183 0.4174 0.4764 -0.0400 0.0154  -0.0002 177 PRO B CA  
2270 C C   . PRO B 177 ? 0.4634 0.4629 0.5209 -0.0461 0.0061  -0.0027 177 PRO B C   
2271 O O   . PRO B 177 ? 0.5857 0.5932 0.6498 -0.0525 0.0062  -0.0024 177 PRO B O   
2272 C CB  . PRO B 177 ? 0.4375 0.4155 0.4778 -0.0427 0.0208  -0.0011 177 PRO B CB  
2273 C CG  . PRO B 177 ? 0.4559 0.4268 0.4897 -0.0366 0.0261  -0.0008 177 PRO B CG  
2274 C CD  . PRO B 177 ? 0.4492 0.4305 0.4915 -0.0305 0.0199  -0.0008 177 PRO B CD  
2275 N N   . LEU B 178 ? 0.4920 0.4824 0.5414 -0.0447 -0.0010 -0.0049 178 LEU B N   
2276 C CA  . LEU B 178 ? 0.5029 0.4899 0.5499 -0.0493 -0.0079 -0.0072 178 LEU B CA  
2277 C C   . LEU B 178 ? 0.4772 0.4814 0.5363 -0.0512 -0.0116 -0.0079 178 LEU B C   
2278 O O   . LEU B 178 ? 0.5068 0.5084 0.5636 -0.0580 -0.0148 -0.0101 178 LEU B O   
2279 C CB  . LEU B 178 ? 0.4939 0.4689 0.5312 -0.0455 -0.0132 -0.0084 178 LEU B CB  
2280 C CG  . LEU B 178 ? 0.6443 0.6070 0.6738 -0.0484 -0.0174 -0.0096 178 LEU B CG  
2281 C CD1 . LEU B 178 ? 0.6146 0.5649 0.6355 -0.0537 -0.0139 -0.0081 178 LEU B CD1 
2282 C CD2 . LEU B 178 ? 0.5390 0.4950 0.5628 -0.0426 -0.0217 -0.0091 178 LEU B CD2 
2283 N N   . ALA B 179 ? 0.4448 0.4655 0.5152 -0.0459 -0.0110 -0.0057 179 ALA B N   
2284 C CA  . ALA B 179 ? 0.5009 0.5400 0.5819 -0.0480 -0.0159 -0.0054 179 ALA B CA  
2285 C C   . ALA B 179 ? 0.4826 0.5381 0.5742 -0.0560 -0.0143 -0.0034 179 ALA B C   
2286 O O   . ALA B 179 ? 0.4965 0.5669 0.5944 -0.0615 -0.0197 -0.0035 179 ALA B O   
2287 C CB  . ALA B 179 ? 0.4547 0.5067 0.5442 -0.0389 -0.0159 -0.0022 179 ALA B CB  
2288 N N   . SER B 180 ? 0.4633 0.5169 0.5563 -0.0579 -0.0071 -0.0016 180 SER B N   
2289 C CA  . SER B 180 ? 0.5277 0.5991 0.6324 -0.0659 -0.0048 0.0009  180 SER B CA  
2290 C C   . SER B 180 ? 0.5483 0.6124 0.6450 -0.0790 -0.0088 -0.0033 180 SER B C   
2291 O O   . SER B 180 ? 0.5887 0.6695 0.6947 -0.0884 -0.0085 -0.0019 180 SER B O   
2292 C CB  . SER B 180 ? 0.5142 0.5832 0.6212 -0.0639 0.0057  0.0039  180 SER B CB  
2293 O OG  . SER B 180 ? 0.5258 0.5690 0.6155 -0.0677 0.0080  0.0004  180 SER B OG  
2294 N N   . GLN B 181 ? 0.4942 0.5341 0.5742 -0.0801 -0.0119 -0.0081 181 GLN B N   
2295 C CA  . GLN B 181 ? 0.5229 0.5493 0.5919 -0.0915 -0.0136 -0.0121 181 GLN B CA  
2296 C C   . GLN B 181 ? 0.4793 0.5068 0.5445 -0.0956 -0.0206 -0.0157 181 GLN B C   
2297 O O   . GLN B 181 ? 0.5116 0.5395 0.5766 -0.0876 -0.0244 -0.0162 181 GLN B O   
2298 C CB  . GLN B 181 ? 0.6357 0.6328 0.6878 -0.0891 -0.0110 -0.0137 181 GLN B CB  
2299 C CG  . GLN B 181 ? 0.7321 0.7248 0.7836 -0.0858 -0.0042 -0.0106 181 GLN B CG  
2300 C CD  . GLN B 181 ? 0.7893 0.7594 0.8263 -0.0793 -0.0043 -0.0104 181 GLN B CD  
2301 O OE1 . GLN B 181 ? 0.9330 0.8904 0.9615 -0.0772 -0.0086 -0.0121 181 GLN B OE1 
2302 N NE2 . GLN B 181 ? 0.8198 0.7857 0.8539 -0.0763 0.0009  -0.0079 181 GLN B NE2 
2303 N N   . GLU B 182 ? 0.5141 0.5413 0.5750 -0.1095 -0.0216 -0.0186 182 GLU B N   
2304 C CA  . GLU B 182 ? 0.5620 0.5828 0.6132 -0.1159 -0.0267 -0.0233 182 GLU B CA  
2305 C C   . GLU B 182 ? 0.6351 0.6261 0.6699 -0.1085 -0.0259 -0.0267 182 GLU B C   
2306 O O   . GLU B 182 ? 0.6124 0.6014 0.6441 -0.1039 -0.0295 -0.0286 182 GLU B O   
2307 C CB  . GLU B 182 ? 0.5974 0.6168 0.6420 -0.1342 -0.0262 -0.0266 182 GLU B CB  
2308 C CG  . GLU B 182 ? 0.6922 0.7459 0.7543 -0.1437 -0.0283 -0.0227 182 GLU B CG  
2309 C CD  . GLU B 182 ? 0.7229 0.7980 0.7896 -0.1495 -0.0363 -0.0228 182 GLU B CD  
2310 O OE1 . GLU B 182 ? 0.7614 0.8520 0.8388 -0.1378 -0.0399 -0.0191 182 GLU B OE1 
2311 O OE2 . GLU B 182 ? 0.7779 0.8532 0.8357 -0.1666 -0.0390 -0.0267 182 GLU B OE2 
2312 N N   . HIS B 183 ? 0.5211 0.4901 0.5463 -0.1069 -0.0209 -0.0265 183 HIS B N   
2313 C CA  . HIS B 183 ? 0.5934 0.5351 0.6040 -0.1004 -0.0194 -0.0280 183 HIS B CA  
2314 C C   . HIS B 183 ? 0.5444 0.4801 0.5560 -0.0893 -0.0174 -0.0235 183 HIS B C   
2315 O O   . HIS B 183 ? 0.5561 0.5007 0.5742 -0.0897 -0.0151 -0.0205 183 HIS B O   
2316 C CB  . HIS B 183 ? 0.5136 0.4304 0.5075 -0.1105 -0.0150 -0.0313 183 HIS B CB  
2317 C CG  . HIS B 183 ? 0.6036 0.5225 0.5920 -0.1243 -0.0165 -0.0366 183 HIS B CG  
2318 N ND1 . HIS B 183 ? 0.6497 0.5667 0.6333 -0.1233 -0.0196 -0.0402 183 HIS B ND1 
2319 C CD2 . HIS B 183 ? 0.6346 0.5583 0.6208 -0.1409 -0.0154 -0.0390 183 HIS B CD2 
2320 C CE1 . HIS B 183 ? 0.6080 0.5272 0.5848 -0.1391 -0.0205 -0.0447 183 HIS B CE1 
2321 N NE2 . HIS B 183 ? 0.5899 0.5141 0.5686 -0.1504 -0.0184 -0.0440 183 HIS B NE2 
2322 N N   . VAL B 184 ? 0.4380 0.3589 0.4424 -0.0799 -0.0181 -0.0227 184 VAL B N   
2323 C CA  . VAL B 184 ? 0.5276 0.4424 0.5306 -0.0710 -0.0174 -0.0181 184 VAL B CA  
2324 C C   . VAL B 184 ? 0.5480 0.4386 0.5380 -0.0671 -0.0154 -0.0165 184 VAL B C   
2325 O O   . VAL B 184 ? 0.5011 0.3804 0.4850 -0.0669 -0.0147 -0.0192 184 VAL B O   
2326 C CB  . VAL B 184 ? 0.5211 0.4499 0.5327 -0.0614 -0.0211 -0.0165 184 VAL B CB  
2327 C CG1 . VAL B 184 ? 0.5676 0.5188 0.5919 -0.0633 -0.0217 -0.0169 184 VAL B CG1 
2328 C CG2 . VAL B 184 ? 0.4549 0.3799 0.4647 -0.0559 -0.0239 -0.0183 184 VAL B CG2 
2329 N N   . SER B 185 ? 0.4212 0.3033 0.4064 -0.0639 -0.0140 -0.0116 185 SER B N   
2330 C CA  . SER B 185 ? 0.4305 0.2920 0.4050 -0.0584 -0.0123 -0.0076 185 SER B CA  
2331 C C   . SER B 185 ? 0.4854 0.3526 0.4640 -0.0469 -0.0165 -0.0032 185 SER B C   
2332 O O   . SER B 185 ? 0.4462 0.3305 0.4332 -0.0445 -0.0202 -0.0033 185 SER B O   
2333 C CB  . SER B 185 ? 0.4911 0.3397 0.4565 -0.0620 -0.0088 -0.0035 185 SER B CB  
2334 O OG  . SER B 185 ? 0.4898 0.3496 0.4585 -0.0608 -0.0108 -0.0001 185 SER B OG  
2335 N N   . TYR B 186 ? 0.4534 0.3061 0.4258 -0.0396 -0.0152 0.0014  186 TYR B N   
2336 C CA  . TYR B 186 ? 0.3982 0.2585 0.3753 -0.0294 -0.0194 0.0074  186 TYR B CA  
2337 C C   . TYR B 186 ? 0.4920 0.3603 0.4684 -0.0301 -0.0229 0.0127  186 TYR B C   
2338 O O   . TYR B 186 ? 0.5204 0.4028 0.5023 -0.0266 -0.0275 0.0149  186 TYR B O   
2339 C CB  . TYR B 186 ? 0.5179 0.3620 0.4899 -0.0205 -0.0163 0.0129  186 TYR B CB  
2340 C CG  . TYR B 186 ? 0.5425 0.3972 0.5207 -0.0101 -0.0208 0.0213  186 TYR B CG  
2341 C CD1 . TYR B 186 ? 0.4628 0.3313 0.4507 -0.0047 -0.0235 0.0199  186 TYR B CD1 
2342 C CD2 . TYR B 186 ? 0.5194 0.3716 0.4937 -0.0065 -0.0226 0.0311  186 TYR B CD2 
2343 C CE1 . TYR B 186 ? 0.5220 0.4027 0.5166 0.0035  -0.0277 0.0279  186 TYR B CE1 
2344 C CE2 . TYR B 186 ? 0.5492 0.4148 0.5300 0.0017  -0.0277 0.0397  186 TYR B CE2 
2345 C CZ  . TYR B 186 ? 0.5355 0.4159 0.5270 0.0063  -0.0302 0.0380  186 TYR B CZ  
2346 O OH  . TYR B 186 ? 0.5721 0.4682 0.5712 0.0132  -0.0353 0.0469  186 TYR B OH  
2347 N N   . GLU B 187 ? 0.4844 0.3425 0.4522 -0.0358 -0.0202 0.0146  187 GLU B N   
2348 C CA  . GLU B 187 ? 0.5463 0.4096 0.5102 -0.0382 -0.0226 0.0190  187 GLU B CA  
2349 C C   . GLU B 187 ? 0.4765 0.3561 0.4468 -0.0421 -0.0240 0.0142  187 GLU B C   
2350 O O   . GLU B 187 ? 0.5527 0.4398 0.5213 -0.0417 -0.0273 0.0172  187 GLU B O   
2351 C CB  . GLU B 187 ? 0.4915 0.3400 0.4443 -0.0449 -0.0181 0.0207  187 GLU B CB  
2352 C CG  . GLU B 187 ? 0.5375 0.3881 0.4827 -0.0482 -0.0199 0.0254  187 GLU B CG  
2353 C CD  . GLU B 187 ? 0.6780 0.5125 0.6109 -0.0543 -0.0152 0.0279  187 GLU B CD  
2354 O OE1 . GLU B 187 ? 0.7509 0.5738 0.6822 -0.0576 -0.0099 0.0246  187 GLU B OE1 
2355 O OE2 . GLU B 187 ? 0.7688 0.6013 0.6920 -0.0570 -0.0164 0.0329  187 GLU B OE2 
2356 N N   . GLN B 188 ? 0.5333 0.4184 0.5103 -0.0462 -0.0213 0.0072  188 GLN B N   
2357 C CA  . GLN B 188 ? 0.5174 0.4174 0.5014 -0.0482 -0.0213 0.0037  188 GLN B CA  
2358 C C   . GLN B 188 ? 0.4838 0.3946 0.4743 -0.0418 -0.0257 0.0034  188 GLN B C   
2359 O O   . GLN B 188 ? 0.4580 0.3761 0.4484 -0.0417 -0.0264 0.0037  188 GLN B O   
2360 C CB  . GLN B 188 ? 0.4370 0.3431 0.4281 -0.0537 -0.0176 -0.0017 188 GLN B CB  
2361 C CG  . GLN B 188 ? 0.5124 0.4097 0.4980 -0.0616 -0.0126 -0.0016 188 GLN B CG  
2362 C CD  . GLN B 188 ? 0.5386 0.4453 0.5328 -0.0682 -0.0100 -0.0062 188 GLN B CD  
2363 O OE1 . GLN B 188 ? 0.5625 0.4672 0.5577 -0.0701 -0.0112 -0.0091 188 GLN B OE1 
2364 N NE2 . GLN B 188 ? 0.6297 0.5472 0.6298 -0.0720 -0.0060 -0.0065 188 GLN B NE2 
2365 N N   . ILE B 189 ? 0.4528 0.3632 0.4474 -0.0370 -0.0276 0.0024  189 ILE B N   
2366 C CA  . ILE B 189 ? 0.4421 0.3622 0.4425 -0.0309 -0.0314 0.0026  189 ILE B CA  
2367 C C   . ILE B 189 ? 0.4015 0.3229 0.3976 -0.0282 -0.0350 0.0090  189 ILE B C   
2368 O O   . ILE B 189 ? 0.4260 0.3571 0.4239 -0.0276 -0.0375 0.0092  189 ILE B O   
2369 C CB  . ILE B 189 ? 0.4127 0.3293 0.4163 -0.0263 -0.0314 0.0009  189 ILE B CB  
2370 C CG1 . ILE B 189 ? 0.4771 0.3944 0.4832 -0.0315 -0.0290 -0.0056 189 ILE B CG1 
2371 C CG2 . ILE B 189 ? 0.4477 0.3742 0.4571 -0.0200 -0.0347 0.0017  189 ILE B CG2 
2372 C CD1 . ILE B 189 ? 0.5457 0.4788 0.5593 -0.0336 -0.0299 -0.0087 189 ILE B CD1 
2373 N N   . LEU B 190 ? 0.4893 0.4011 0.4788 -0.0272 -0.0353 0.0149  190 LEU B N   
2374 C CA  . LEU B 190 ? 0.4947 0.4101 0.4799 -0.0257 -0.0399 0.0226  190 LEU B CA  
2375 C C   . LEU B 190 ? 0.4840 0.4041 0.4627 -0.0329 -0.0406 0.0217  190 LEU B C   
2376 O O   . LEU B 190 ? 0.4958 0.4245 0.4728 -0.0336 -0.0450 0.0248  190 LEU B O   
2377 C CB  . LEU B 190 ? 0.5157 0.4189 0.4936 -0.0241 -0.0394 0.0298  190 LEU B CB  
2378 C CG  . LEU B 190 ? 0.5727 0.4816 0.5482 -0.0204 -0.0451 0.0405  190 LEU B CG  
2379 C CD1 . LEU B 190 ? 0.5879 0.5072 0.5747 -0.0111 -0.0477 0.0439  190 LEU B CD1 
2380 C CD2 . LEU B 190 ? 0.5758 0.4708 0.5426 -0.0189 -0.0437 0.0480  190 LEU B CD2 
2381 N N   . GLY B 191 ? 0.4818 0.3960 0.4563 -0.0389 -0.0356 0.0174  191 GLY B N   
2382 C CA  . GLY B 191 ? 0.4449 0.3594 0.4112 -0.0455 -0.0336 0.0160  191 GLY B CA  
2383 C C   . GLY B 191 ? 0.4868 0.4087 0.4589 -0.0457 -0.0305 0.0099  191 GLY B C   
2384 O O   . GLY B 191 ? 0.5634 0.4825 0.5283 -0.0505 -0.0261 0.0081  191 GLY B O   
2385 N N   . THR B 192 ? 0.5081 0.4378 0.4919 -0.0403 -0.0318 0.0071  192 THR B N   
2386 C CA  . THR B 192 ? 0.4233 0.3603 0.4128 -0.0391 -0.0292 0.0025  192 THR B CA  
2387 C C   . THR B 192 ? 0.4453 0.3890 0.4361 -0.0363 -0.0337 0.0035  192 THR B C   
2388 O O   . THR B 192 ? 0.5606 0.5074 0.5551 -0.0324 -0.0386 0.0064  192 THR B O   
2389 C CB  . THR B 192 ? 0.4813 0.4233 0.4824 -0.0365 -0.0273 -0.0013 192 THR B CB  
2390 O OG1 . THR B 192 ? 0.5034 0.4401 0.5036 -0.0404 -0.0239 -0.0016 192 THR B OG1 
2391 C CG2 . THR B 192 ? 0.4111 0.3609 0.4178 -0.0350 -0.0237 -0.0043 192 THR B CG2 
2392 N N   . ARG B 193 ? 0.4218 0.3670 0.4091 -0.0381 -0.0311 0.0013  193 ARG B N   
2393 C CA  . ARG B 193 ? 0.3571 0.3084 0.3447 -0.0369 -0.0347 0.0018  193 ARG B CA  
2394 C C   . ARG B 193 ? 0.4505 0.4097 0.4509 -0.0300 -0.0364 -0.0003 193 ARG B C   
2395 O O   . ARG B 193 ? 0.3664 0.3272 0.3731 -0.0275 -0.0329 -0.0036 193 ARG B O   
2396 C CB  . ARG B 193 ? 0.3125 0.2595 0.2907 -0.0412 -0.0298 -0.0007 193 ARG B CB  
2397 C CG  . ARG B 193 ? 0.3657 0.3179 0.3420 -0.0423 -0.0332 -0.0004 193 ARG B CG  
2398 C CD  . ARG B 193 ? 0.3622 0.3065 0.3278 -0.0463 -0.0265 -0.0037 193 ARG B CD  
2399 N NE  . ARG B 193 ? 0.4796 0.4122 0.4275 -0.0554 -0.0230 -0.0034 193 ARG B NE  
2400 C CZ  . ARG B 193 ? 0.5354 0.4557 0.4754 -0.0568 -0.0134 -0.0060 193 ARG B CZ  
2401 N NH1 . ARG B 193 ? 0.4289 0.3499 0.3793 -0.0491 -0.0069 -0.0080 193 ARG B NH1 
2402 N NH2 . ARG B 193 ? 0.4308 0.3385 0.3517 -0.0661 -0.0100 -0.0060 193 ARG B NH2 
2403 N N   . GLN B 194 ? 0.4042 0.3694 0.4083 -0.0271 -0.0415 0.0024  194 GLN B N   
2404 C CA  . GLN B 194 ? 0.3450 0.3163 0.3588 -0.0211 -0.0424 0.0004  194 GLN B CA  
2405 C C   . GLN B 194 ? 0.3548 0.3316 0.3678 -0.0217 -0.0427 -0.0006 194 GLN B C   
2406 O O   . GLN B 194 ? 0.3741 0.3534 0.3814 -0.0259 -0.0452 0.0023  194 GLN B O   
2407 C CB  . GLN B 194 ? 0.3684 0.3413 0.3873 -0.0164 -0.0458 0.0041  194 GLN B CB  
2408 C CG  . GLN B 194 ? 0.3937 0.3702 0.4205 -0.0105 -0.0454 0.0016  194 GLN B CG  
2409 C CD  . GLN B 194 ? 0.5241 0.4993 0.5550 -0.0048 -0.0462 0.0055  194 GLN B CD  
2410 O OE1 . GLN B 194 ? 0.3977 0.3696 0.4264 -0.0043 -0.0474 0.0108  194 GLN B OE1 
2411 N NE2 . GLN B 194 ? 0.4989 0.4756 0.5349 0.0002  -0.0448 0.0034  194 GLN B NE2 
2412 N N   . ILE B 195 ? 0.3826 0.3616 0.4004 -0.0183 -0.0404 -0.0044 195 ILE B N   
2413 C CA  . ILE B 195 ? 0.3563 0.3392 0.3734 -0.0181 -0.0401 -0.0054 195 ILE B CA  
2414 C C   . ILE B 195 ? 0.4017 0.3915 0.4269 -0.0131 -0.0431 -0.0047 195 ILE B C   
2415 O O   . ILE B 195 ? 0.3695 0.3593 0.4000 -0.0088 -0.0424 -0.0070 195 ILE B O   
2416 C CB  . ILE B 195 ? 0.4253 0.4057 0.4418 -0.0166 -0.0350 -0.0087 195 ILE B CB  
2417 C CG1 . ILE B 195 ? 0.3819 0.3549 0.3922 -0.0198 -0.0301 -0.0089 195 ILE B CG1 
2418 C CG2 . ILE B 195 ? 0.3471 0.3280 0.3596 -0.0174 -0.0336 -0.0095 195 ILE B CG2 
2419 C CD1 . ILE B 195 ? 0.4206 0.3866 0.4181 -0.0270 -0.0289 -0.0078 195 ILE B CD1 
2420 N N   . VAL B 196 ? 0.4157 0.4120 0.4413 -0.0143 -0.0461 -0.0013 196 VAL B N   
2421 C CA  . VAL B 196 ? 0.4047 0.4082 0.4389 -0.0088 -0.0479 0.0008  196 VAL B CA  
2422 C C   . VAL B 196 ? 0.4537 0.4631 0.4890 -0.0091 -0.0471 -0.0007 196 VAL B C   
2423 O O   . VAL B 196 ? 0.4681 0.4786 0.4969 -0.0153 -0.0471 -0.0006 196 VAL B O   
2424 C CB  . VAL B 196 ? 0.4281 0.4379 0.4652 -0.0086 -0.0518 0.0078  196 VAL B CB  
2425 C CG1 . VAL B 196 ? 0.5246 0.5411 0.5720 -0.0008 -0.0516 0.0108  196 VAL B CG1 
2426 C CG2 . VAL B 196 ? 0.4146 0.4161 0.4482 -0.0090 -0.0520 0.0095  196 VAL B CG2 
2427 N N   . VAL B 197 ? 0.4303 0.4415 0.4717 -0.0032 -0.0457 -0.0023 197 VAL B N   
2428 C CA  . VAL B 197 ? 0.4530 0.4695 0.4957 -0.0028 -0.0444 -0.0035 197 VAL B CA  
2429 C C   . VAL B 197 ? 0.5140 0.5412 0.5655 0.0005  -0.0456 0.0013  197 VAL B C   
2430 O O   . VAL B 197 ? 0.5040 0.5299 0.5613 0.0073  -0.0441 0.0023  197 VAL B O   
2431 C CB  . VAL B 197 ? 0.4839 0.4951 0.5261 0.0011  -0.0414 -0.0084 197 VAL B CB  
2432 C CG1 . VAL B 197 ? 0.4170 0.4329 0.4600 0.0018  -0.0397 -0.0092 197 VAL B CG1 
2433 C CG2 . VAL B 197 ? 0.3660 0.3705 0.4024 -0.0011 -0.0401 -0.0112 197 VAL B CG2 
2434 N N   . ALA B 198 ? 0.4282 0.4661 0.4805 -0.0044 -0.0476 0.0047  198 ALA B N   
2435 C CA  . ALA B 198 ? 0.5576 0.6103 0.6208 -0.0013 -0.0489 0.0109  198 ALA B CA  
2436 C C   . ALA B 198 ? 0.5653 0.6300 0.6271 -0.0100 -0.0510 0.0130  198 ALA B C   
2437 O O   . ALA B 198 ? 0.5621 0.6200 0.6122 -0.0185 -0.0508 0.0093  198 ALA B O   
2438 C CB  . ALA B 198 ? 0.5084 0.5657 0.5774 0.0021  -0.0520 0.0179  198 ALA B CB  
2439 N N   . SER B 199 ? 0.7540 0.8363 0.8277 -0.0079 -0.0521 0.0192  199 SER B N   
2440 C CA  . SER B 199 ? 0.6653 0.7631 0.7399 -0.0172 -0.0545 0.0222  199 SER B CA  
2441 C C   . SER B 199 ? 0.7002 0.7894 0.7658 -0.0218 -0.0500 0.0151  199 SER B C   
2442 O O   . SER B 199 ? 0.8163 0.9066 0.8877 -0.0159 -0.0457 0.0134  199 SER B O   
2443 C CB  . SER B 199 ? 0.6605 0.7629 0.7267 -0.0290 -0.0606 0.0256  199 SER B CB  
2444 O OG  . SER B 199 ? 0.6935 0.8154 0.7716 -0.0271 -0.0661 0.0359  199 SER B OG  
2445 N N   . THR B 203 ? 0.8517 1.0158 0.9843 0.0107  -0.0642 0.0646  203 THR B N   
2446 C CA  . THR B 203 ? 0.8724 1.0200 0.9882 0.0030  -0.0683 0.0601  203 THR B CA  
2447 C C   . THR B 203 ? 0.9532 1.0778 1.0652 0.0136  -0.0636 0.0569  203 THR B C   
2448 O O   . THR B 203 ? 0.8829 0.9942 0.9960 0.0217  -0.0562 0.0509  203 THR B O   
2449 C CB  . THR B 203 ? 0.8374 1.0032 0.9528 -0.0058 -0.0779 0.0700  203 THR B CB  
2450 O OG1 . THR B 203 ? 0.8342 1.0224 0.9689 0.0043  -0.0796 0.0839  203 THR B OG1 
2451 C CG2 . THR B 203 ? 0.7385 0.9172 0.8472 -0.0227 -0.0826 0.0684  203 THR B CG2 
2452 N N   . LEU B 204 ? 0.9707 1.0904 1.0772 0.0124  -0.0676 0.0608  204 LEU B N   
2453 C CA  . LEU B 204 ? 0.9851 1.0797 1.0821 0.0166  -0.0638 0.0549  204 LEU B CA  
2454 C C   . LEU B 204 ? 1.0042 1.0950 1.1099 0.0304  -0.0599 0.0623  204 LEU B C   
2455 O O   . LEU B 204 ? 0.9886 1.0911 1.1001 0.0332  -0.0641 0.0738  204 LEU B O   
2456 C CB  . LEU B 204 ? 0.9358 1.0231 1.0182 0.0057  -0.0690 0.0531  204 LEU B CB  
2457 C CG  . LEU B 204 ? 0.8868 0.9627 0.9559 -0.0045 -0.0678 0.0419  204 LEU B CG  
2458 C CD1 . LEU B 204 ? 0.8877 0.9605 0.9429 -0.0162 -0.0725 0.0421  204 LEU B CD1 
2459 C CD2 . LEU B 204 ? 0.8109 0.8663 0.8759 0.0008  -0.0614 0.0326  204 LEU B CD2 
2460 N N   . LYS B 205 ? 0.9828 1.0556 1.0875 0.0385  -0.0516 0.0559  205 LYS B N   
2461 C CA  . LYS B 205 ? 1.0077 1.0684 1.1156 0.0509  -0.0453 0.0606  205 LYS B CA  
2462 C C   . LYS B 205 ? 0.9393 0.9822 1.0352 0.0480  -0.0466 0.0592  205 LYS B C   
2463 O O   . LYS B 205 ? 0.8449 0.8716 0.9290 0.0414  -0.0455 0.0486  205 LYS B O   
2464 C CB  . LYS B 205 ? 1.0511 1.0958 1.1578 0.0576  -0.0354 0.0526  205 LYS B CB  
2465 C CG  . LYS B 205 ? 1.0793 1.1398 1.1986 0.0628  -0.0318 0.0552  205 LYS B CG  
2466 C CD  . LYS B 205 ? 1.1013 1.1440 1.2152 0.0667  -0.0223 0.0457  205 LYS B CD  
2467 C CE  . LYS B 205 ? 1.0693 1.1003 1.1692 0.0558  -0.0248 0.0328  205 LYS B CE  
2468 N NZ  . LYS B 205 ? 1.0510 1.0749 1.1480 0.0573  -0.0181 0.0253  205 LYS B NZ  
2469 N N   . PRO B 206 ? 0.9922 1.0384 1.0911 0.0529  -0.0486 0.0704  206 PRO B N   
2470 C CA  . PRO B 206 ? 0.9893 1.0196 1.0755 0.0484  -0.0504 0.0694  206 PRO B CA  
2471 C C   . PRO B 206 ? 0.8768 0.8785 0.9532 0.0512  -0.0420 0.0610  206 PRO B C   
2472 O O   . PRO B 206 ? 0.8940 0.8822 0.9590 0.0446  -0.0431 0.0571  206 PRO B O   
2473 C CB  . PRO B 206 ? 0.9801 1.0217 1.0731 0.0552  -0.0537 0.0853  206 PRO B CB  
2474 C CG  . PRO B 206 ? 0.9300 0.9874 1.0405 0.0675  -0.0500 0.0940  206 PRO B CG  
2475 C CD  . PRO B 206 ? 1.0009 1.0680 1.1154 0.0624  -0.0499 0.0855  206 PRO B CD  
2476 N N   . GLU B 207 ? 0.9028 0.8944 0.9822 0.0596  -0.0333 0.0579  207 GLU B N   
2477 C CA  . GLU B 207 ? 0.8981 0.8616 0.9656 0.0600  -0.0254 0.0497  207 GLU B CA  
2478 C C   . GLU B 207 ? 0.8303 0.7873 0.8891 0.0492  -0.0263 0.0359  207 GLU B C   
2479 O O   . GLU B 207 ? 0.7975 0.7342 0.8456 0.0461  -0.0217 0.0288  207 GLU B O   
2480 C CB  . GLU B 207 ? 1.0194 0.9703 1.0896 0.0724  -0.0142 0.0517  207 GLU B CB  
2481 C CG  . GLU B 207 ? 1.0460 1.0055 1.1230 0.0750  -0.0110 0.0475  207 GLU B CG  
2482 C CD  . GLU B 207 ? 1.1265 1.1139 1.2215 0.0819  -0.0141 0.0587  207 GLU B CD  
2483 O OE1 . GLU B 207 ? 1.1269 1.1283 1.2289 0.0843  -0.0198 0.0702  207 GLU B OE1 
2484 O OE2 . GLU B 207 ? 1.1041 1.1003 1.2059 0.0844  -0.0111 0.0565  207 GLU B OE2 
2485 N N   . LEU B 208 ? 0.9154 0.8893 0.9784 0.0434  -0.0319 0.0327  208 LEU B N   
2486 C CA  . LEU B 208 ? 0.7933 0.7640 0.8492 0.0339  -0.0336 0.0219  208 LEU B CA  
2487 C C   . LEU B 208 ? 0.7209 0.6974 0.7727 0.0248  -0.0402 0.0218  208 LEU B C   
2488 O O   . LEU B 208 ? 0.6512 0.6289 0.6993 0.0178  -0.0417 0.0148  208 LEU B O   
2489 C CB  . LEU B 208 ? 0.7422 0.7234 0.8030 0.0339  -0.0334 0.0180  208 LEU B CB  
2490 C CG  . LEU B 208 ? 0.9614 0.9322 1.0214 0.0399  -0.0256 0.0140  208 LEU B CG  
2491 C CD1 . LEU B 208 ? 0.8438 0.7927 0.8916 0.0366  -0.0213 0.0067  208 LEU B CD1 
2492 C CD2 . LEU B 208 ? 0.9515 0.9248 1.0204 0.0516  -0.0204 0.0226  208 LEU B CD2 
2493 N N   . LEU B 209 ? 0.7462 0.7260 0.7981 0.0250  -0.0434 0.0299  209 LEU B N   
2494 C CA  . LEU B 209 ? 0.6159 0.5983 0.6612 0.0161  -0.0485 0.0302  209 LEU B CA  
2495 C C   . LEU B 209 ? 0.5202 0.4863 0.5576 0.0153  -0.0462 0.0308  209 LEU B C   
2496 O O   . LEU B 209 ? 0.5869 0.5477 0.6252 0.0219  -0.0445 0.0383  209 LEU B O   
2497 C CB  . LEU B 209 ? 0.7316 0.7315 0.7806 0.0147  -0.0549 0.0393  209 LEU B CB  
2498 C CG  . LEU B 209 ? 0.7627 0.7772 0.8126 0.0077  -0.0589 0.0371  209 LEU B CG  
2499 C CD1 . LEU B 209 ? 0.7417 0.7504 0.7794 -0.0031 -0.0604 0.0323  209 LEU B CD1 
2500 C CD2 . LEU B 209 ? 0.7551 0.7708 0.8100 0.0105  -0.0552 0.0303  209 LEU B CD2 
2501 N N   . PHE B 210 ? 0.4663 0.4246 0.4963 0.0076  -0.0454 0.0238  210 PHE B N   
2502 C CA  . PHE B 210 ? 0.4950 0.4377 0.5173 0.0053  -0.0425 0.0233  210 PHE B CA  
2503 C C   . PHE B 210 ? 0.4847 0.4275 0.4997 -0.0031 -0.0449 0.0235  210 PHE B C   
2504 O O   . PHE B 210 ? 0.5797 0.5102 0.5878 -0.0060 -0.0424 0.0233  210 PHE B O   
2505 C CB  . PHE B 210 ? 0.4728 0.4041 0.4928 0.0034  -0.0375 0.0144  210 PHE B CB  
2506 C CG  . PHE B 210 ? 0.5527 0.4793 0.5759 0.0104  -0.0335 0.0131  210 PHE B CG  
2507 C CD1 . PHE B 210 ? 0.4959 0.4326 0.5249 0.0120  -0.0343 0.0095  210 PHE B CD1 
2508 C CD2 . PHE B 210 ? 0.5014 0.4112 0.5203 0.0156  -0.0278 0.0158  210 PHE B CD2 
2509 C CE1 . PHE B 210 ? 0.5847 0.5158 0.6152 0.0181  -0.0296 0.0081  210 PHE B CE1 
2510 C CE2 . PHE B 210 ? 0.6312 0.5337 0.6510 0.0222  -0.0223 0.0143  210 PHE B CE2 
2511 C CZ  . PHE B 210 ? 0.5554 0.4690 0.5811 0.0232  -0.0233 0.0103  210 PHE B CZ  
2512 N N   . SER B 211 ? 0.4491 0.4035 0.4637 -0.0076 -0.0488 0.0237  211 SER B N   
2513 C CA  . SER B 211 ? 0.4582 0.4108 0.4636 -0.0159 -0.0497 0.0235  211 SER B CA  
2514 C C   . SER B 211 ? 0.4111 0.3727 0.4127 -0.0182 -0.0555 0.0316  211 SER B C   
2515 O O   . SER B 211 ? 0.4046 0.3789 0.4128 -0.0151 -0.0593 0.0355  211 SER B O   
2516 C CB  . SER B 211 ? 0.4331 0.3883 0.4377 -0.0210 -0.0476 0.0159  211 SER B CB  
2517 O OG  . SER B 211 ? 0.4199 0.3706 0.4288 -0.0197 -0.0434 0.0096  211 SER B OG  
2518 N N   . LYS B 212 ? 0.4694 0.4250 0.4600 -0.0245 -0.0563 0.0345  212 LYS B N   
2519 C CA  . LYS B 212 ? 0.4292 0.3937 0.4135 -0.0290 -0.0627 0.0425  212 LYS B CA  
2520 C C   . LYS B 212 ? 0.4752 0.4487 0.4560 -0.0363 -0.0647 0.0390  212 LYS B C   
2521 O O   . LYS B 212 ? 0.5084 0.4961 0.4907 -0.0382 -0.0708 0.0449  212 LYS B O   
2522 C CB  . LYS B 212 ? 0.5079 0.4617 0.4780 -0.0353 -0.0625 0.0457  212 LYS B CB  
2523 C CG  . LYS B 212 ? 0.6999 0.6629 0.6611 -0.0414 -0.0701 0.0549  212 LYS B CG  
2524 C CD  . LYS B 212 ? 0.8349 0.8159 0.8088 -0.0338 -0.0766 0.0647  212 LYS B CD  
2525 C CE  . LYS B 212 ? 0.8784 0.8714 0.8448 -0.0395 -0.0854 0.0765  212 LYS B CE  
2526 N NZ  . LYS B 212 ? 0.8439 0.8249 0.7999 -0.0395 -0.0853 0.0829  212 LYS B NZ  
2527 N N   . HIS B 213 ? 0.4645 0.4304 0.4407 -0.0406 -0.0591 0.0300  213 HIS B N   
2528 C CA  . HIS B 213 ? 0.5275 0.4967 0.4976 -0.0476 -0.0587 0.0259  213 HIS B CA  
2529 C C   . HIS B 213 ? 0.4181 0.3898 0.3988 -0.0420 -0.0551 0.0194  213 HIS B C   
2530 O O   . HIS B 213 ? 0.4481 0.4141 0.4351 -0.0368 -0.0506 0.0151  213 HIS B O   
2531 C CB  . HIS B 213 ? 0.4576 0.4136 0.4109 -0.0570 -0.0536 0.0219  213 HIS B CB  
2532 C CG  . HIS B 213 ? 0.6565 0.6093 0.5959 -0.0645 -0.0574 0.0281  213 HIS B CG  
2533 N ND1 . HIS B 213 ? 0.7229 0.6866 0.6563 -0.0707 -0.0654 0.0350  213 HIS B ND1 
2534 C CD2 . HIS B 213 ? 0.6307 0.5718 0.5607 -0.0673 -0.0546 0.0290  213 HIS B CD2 
2535 C CE1 . HIS B 213 ? 0.7457 0.7043 0.6658 -0.0770 -0.0679 0.0401  213 HIS B CE1 
2536 N NE2 . HIS B 213 ? 0.7985 0.7422 0.7158 -0.0749 -0.0609 0.0364  213 HIS B NE2 
2537 N N   . TYR B 214 ? 0.4672 0.4479 0.4490 -0.0441 -0.0572 0.0191  214 TYR B N   
2538 C CA  . TYR B 214 ? 0.4259 0.4101 0.4176 -0.0383 -0.0546 0.0144  214 TYR B CA  
2539 C C   . TYR B 214 ? 0.4006 0.3879 0.3858 -0.0450 -0.0543 0.0122  214 TYR B C   
2540 O O   . TYR B 214 ? 0.3940 0.3858 0.3703 -0.0536 -0.0583 0.0158  214 TYR B O   
2541 C CB  . TYR B 214 ? 0.3277 0.3216 0.3341 -0.0290 -0.0578 0.0181  214 TYR B CB  
2542 C CG  . TYR B 214 ? 0.4300 0.4393 0.4405 -0.0299 -0.0641 0.0257  214 TYR B CG  
2543 C CD1 . TYR B 214 ? 0.4688 0.4884 0.4823 -0.0321 -0.0652 0.0249  214 TYR B CD1 
2544 C CD2 . TYR B 214 ? 0.4804 0.4952 0.4921 -0.0287 -0.0688 0.0346  214 TYR B CD2 
2545 C CE1 . TYR B 214 ? 0.4611 0.4983 0.4802 -0.0337 -0.0711 0.0326  214 TYR B CE1 
2546 C CE2 . TYR B 214 ? 0.4229 0.4559 0.4407 -0.0290 -0.0751 0.0433  214 TYR B CE2 
2547 C CZ  . TYR B 214 ? 0.5665 0.6118 0.5887 -0.0319 -0.0763 0.0422  214 TYR B CZ  
2548 O OH  . TYR B 214 ? 0.6906 0.7574 0.7206 -0.0331 -0.0827 0.0515  214 TYR B OH  
2549 N N   . TRP B 215 ? 0.3591 0.3436 0.3477 -0.0416 -0.0496 0.0066  215 TRP B N   
2550 C CA  . TRP B 215 ? 0.3652 0.3515 0.3492 -0.0459 -0.0483 0.0043  215 TRP B CA  
2551 C C   . TRP B 215 ? 0.4865 0.4840 0.4845 -0.0386 -0.0502 0.0047  215 TRP B C   
2552 O O   . TRP B 215 ? 0.3714 0.3695 0.3799 -0.0297 -0.0494 0.0037  215 TRP B O   
2553 C CB  . TRP B 215 ? 0.3246 0.2968 0.2998 -0.0471 -0.0397 -0.0016 215 TRP B CB  
2554 C CG  . TRP B 215 ? 0.4866 0.4453 0.4453 -0.0551 -0.0352 -0.0028 215 TRP B CG  
2555 C CD1 . TRP B 215 ? 0.4252 0.3827 0.3745 -0.0627 -0.0388 0.0005  215 TRP B CD1 
2556 C CD2 . TRP B 215 ? 0.4013 0.3446 0.3500 -0.0559 -0.0252 -0.0072 215 TRP B CD2 
2557 N NE1 . TRP B 215 ? 0.4210 0.3619 0.3534 -0.0692 -0.0314 -0.0025 215 TRP B NE1 
2558 C CE2 . TRP B 215 ? 0.4438 0.3755 0.3762 -0.0645 -0.0223 -0.0071 215 TRP B CE2 
2559 C CE3 . TRP B 215 ? 0.3965 0.3346 0.3484 -0.0495 -0.0180 -0.0103 215 TRP B CE3 
2560 C CZ2 . TRP B 215 ? 0.4014 0.3152 0.3206 -0.0666 -0.0111 -0.0107 215 TRP B CZ2 
2561 C CZ3 . TRP B 215 ? 0.4879 0.4099 0.4283 -0.0506 -0.0074 -0.0128 215 TRP B CZ3 
2562 C CH2 . TRP B 215 ? 0.4765 0.3859 0.4008 -0.0589 -0.0033 -0.0132 215 TRP B CH2 
2563 N N   . ARG B 216 ? 0.4888 0.4944 0.4855 -0.0433 -0.0522 0.0059  216 ARG B N   
2564 C CA  . ARG B 216 ? 0.4019 0.4178 0.4106 -0.0373 -0.0530 0.0062  216 ARG B CA  
2565 C C   . ARG B 216 ? 0.4488 0.4578 0.4512 -0.0395 -0.0476 0.0008  216 ARG B C   
2566 O O   . ARG B 216 ? 0.3905 0.3930 0.3792 -0.0491 -0.0455 -0.0007 216 ARG B O   
2567 C CB  . ARG B 216 ? 0.4676 0.5016 0.4829 -0.0402 -0.0592 0.0131  216 ARG B CB  
2568 C CG  . ARG B 216 ? 0.5267 0.5721 0.5574 -0.0313 -0.0592 0.0146  216 ARG B CG  
2569 C CD  . ARG B 216 ? 0.4983 0.5648 0.5375 -0.0339 -0.0647 0.0228  216 ARG B CD  
2570 N NE  . ARG B 216 ? 0.6735 0.7457 0.7028 -0.0476 -0.0668 0.0229  216 ARG B NE  
2571 C CZ  . ARG B 216 ? 0.6539 0.7216 0.6772 -0.0524 -0.0628 0.0175  216 ARG B CZ  
2572 N NH1 . ARG B 216 ? 0.6109 0.6702 0.6377 -0.0442 -0.0572 0.0122  216 ARG B NH1 
2573 N NH2 . ARG B 216 ? 0.5310 0.6019 0.5428 -0.0667 -0.0644 0.0177  216 ARG B NH2 
2574 N N   . THR B 217 ? 0.3454 0.3539 0.3558 -0.0309 -0.0449 -0.0020 217 THR B N   
2575 C CA  . THR B 217 ? 0.3775 0.3814 0.3840 -0.0310 -0.0404 -0.0056 217 THR B CA  
2576 C C   . THR B 217 ? 0.4587 0.4731 0.4770 -0.0247 -0.0417 -0.0049 217 THR B C   
2577 O O   . THR B 217 ? 0.4330 0.4547 0.4618 -0.0188 -0.0446 -0.0024 217 THR B O   
2578 C CB  . THR B 217 ? 0.3806 0.3716 0.3828 -0.0267 -0.0346 -0.0094 217 THR B CB  
2579 O OG1 . THR B 217 ? 0.5257 0.5112 0.5224 -0.0267 -0.0298 -0.0117 217 THR B OG1 
2580 C CG2 . THR B 217 ? 0.4234 0.4176 0.4368 -0.0178 -0.0359 -0.0098 217 THR B CG2 
2581 N N   . ASP B 218 ? 0.3886 0.4020 0.4038 -0.0259 -0.0386 -0.0069 218 ASP B N   
2582 C CA  . ASP B 218 ? 0.4853 0.5087 0.5102 -0.0213 -0.0391 -0.0061 218 ASP B CA  
2583 C C   . ASP B 218 ? 0.4150 0.4320 0.4409 -0.0138 -0.0356 -0.0097 218 ASP B C   
2584 O O   . ASP B 218 ? 0.4736 0.4959 0.5044 -0.0106 -0.0346 -0.0099 218 ASP B O   
2585 C CB  . ASP B 218 ? 0.4938 0.5243 0.5157 -0.0293 -0.0389 -0.0048 218 ASP B CB  
2586 C CG  . ASP B 218 ? 0.4940 0.5106 0.5012 -0.0348 -0.0334 -0.0087 218 ASP B CG  
2587 O OD1 . ASP B 218 ? 0.4717 0.4743 0.4721 -0.0315 -0.0296 -0.0115 218 ASP B OD1 
2588 O OD2 . ASP B 218 ? 0.5659 0.5858 0.5687 -0.0423 -0.0322 -0.0085 218 ASP B OD2 
2589 N N   . ASN B 219 ? 0.4422 0.4493 0.4638 -0.0111 -0.0337 -0.0120 219 ASN B N   
2590 C CA  . ASN B 219 ? 0.3891 0.3932 0.4121 -0.0047 -0.0320 -0.0142 219 ASN B CA  
2591 C C   . ASN B 219 ? 0.3988 0.3981 0.4217 -0.0021 -0.0320 -0.0148 219 ASN B C   
2592 O O   . ASN B 219 ? 0.3962 0.3915 0.4158 -0.0050 -0.0314 -0.0141 219 ASN B O   
2593 C CB  . ASN B 219 ? 0.4413 0.4406 0.4572 -0.0053 -0.0278 -0.0153 219 ASN B CB  
2594 C CG  . ASN B 219 ? 0.4207 0.4090 0.4270 -0.0068 -0.0235 -0.0154 219 ASN B CG  
2595 O OD1 . ASN B 219 ? 0.5372 0.5218 0.5429 -0.0015 -0.0215 -0.0152 219 ASN B OD1 
2596 N ND2 . ASN B 219 ? 0.6251 0.6083 0.6234 -0.0141 -0.0216 -0.0152 219 ASN B ND2 
2597 N N   . HIS B 220 ? 0.3306 0.3309 0.3565 0.0027  -0.0325 -0.0161 220 HIS B N   
2598 C CA  . HIS B 220 ? 0.3343 0.3343 0.3627 0.0043  -0.0337 -0.0163 220 HIS B CA  
2599 C C   . HIS B 220 ? 0.3569 0.3539 0.3822 0.0055  -0.0304 -0.0149 220 HIS B C   
2600 O O   . HIS B 220 ? 0.4332 0.4310 0.4612 0.0058  -0.0303 -0.0140 220 HIS B O   
2601 C CB  . HIS B 220 ? 0.3615 0.3643 0.3926 0.0067  -0.0358 -0.0180 220 HIS B CB  
2602 C CG  . HIS B 220 ? 0.4242 0.4269 0.4581 0.0070  -0.0370 -0.0191 220 HIS B CG  
2603 N ND1 . HIS B 220 ? 0.4869 0.4881 0.5237 0.0060  -0.0382 -0.0184 220 HIS B ND1 
2604 C CD2 . HIS B 220 ? 0.3495 0.3524 0.3834 0.0089  -0.0359 -0.0201 220 HIS B CD2 
2605 C CE1 . HIS B 220 ? 0.3465 0.3468 0.3854 0.0082  -0.0377 -0.0184 220 HIS B CE1 
2606 N NE2 . HIS B 220 ? 0.4143 0.4159 0.4519 0.0100  -0.0359 -0.0196 220 HIS B NE2 
2607 N N   . HIS B 221 ? 0.3464 0.3398 0.3662 0.0068  -0.0268 -0.0142 221 HIS B N   
2608 C CA  . HIS B 221 ? 0.4353 0.4237 0.4516 0.0095  -0.0217 -0.0118 221 HIS B CA  
2609 C C   . HIS B 221 ? 0.4257 0.4063 0.4373 0.0058  -0.0179 -0.0116 221 HIS B C   
2610 O O   . HIS B 221 ? 0.4304 0.4098 0.4438 0.0080  -0.0149 -0.0098 221 HIS B O   
2611 C CB  . HIS B 221 ? 0.3806 0.3631 0.3895 0.0115  -0.0175 -0.0108 221 HIS B CB  
2612 C CG  . HIS B 221 ? 0.4259 0.3984 0.4285 0.0144  -0.0097 -0.0079 221 HIS B CG  
2613 N ND1 . HIS B 221 ? 0.4446 0.4029 0.4352 0.0102  -0.0032 -0.0088 221 HIS B ND1 
2614 C CD2 . HIS B 221 ? 0.3954 0.3698 0.4016 0.0214  -0.0066 -0.0035 221 HIS B CD2 
2615 C CE1 . HIS B 221 ? 0.4833 0.4318 0.4690 0.0150  0.0049  -0.0057 221 HIS B CE1 
2616 N NE2 . HIS B 221 ? 0.4411 0.4004 0.4375 0.0227  0.0030  -0.0018 221 HIS B NE2 
2617 N N   . SER B 222 ? 0.3239 0.2998 0.3291 -0.0005 -0.0178 -0.0132 222 SER B N   
2618 C CA  . SER B 222 ? 0.4566 0.4245 0.4545 -0.0062 -0.0150 -0.0134 222 SER B CA  
2619 C C   . SER B 222 ? 0.4181 0.3909 0.4228 -0.0062 -0.0184 -0.0130 222 SER B C   
2620 O O   . SER B 222 ? 0.4587 0.4250 0.4596 -0.0072 -0.0142 -0.0124 222 SER B O   
2621 C CB  . SER B 222 ? 0.3663 0.3329 0.3571 -0.0146 -0.0166 -0.0144 222 SER B CB  
2622 O OG  . SER B 222 ? 0.5578 0.5171 0.5396 -0.0165 -0.0119 -0.0151 222 SER B OG  
2623 N N   . ALA B 223 ? 0.3949 0.3774 0.4085 -0.0052 -0.0250 -0.0133 223 ALA B N   
2624 C CA  . ALA B 223 ? 0.3773 0.3625 0.3962 -0.0055 -0.0277 -0.0129 223 ALA B CA  
2625 C C   . ALA B 223 ? 0.4645 0.4514 0.4881 -0.0016 -0.0253 -0.0122 223 ALA B C   
2626 O O   . ALA B 223 ? 0.3894 0.3742 0.4132 -0.0031 -0.0233 -0.0115 223 ALA B O   
2627 C CB  . ALA B 223 ? 0.3397 0.3317 0.3655 -0.0044 -0.0334 -0.0133 223 ALA B CB  
2628 N N   . CYS B 224 ? 0.3359 0.3282 0.3638 0.0031  -0.0254 -0.0118 224 CYS B N   
2629 C CA  . CYS B 224 ? 0.3304 0.3292 0.3650 0.0066  -0.0242 -0.0096 224 CYS B CA  
2630 C C   . CYS B 224 ? 0.3451 0.3381 0.3769 0.0087  -0.0164 -0.0070 224 CYS B C   
2631 O O   . CYS B 224 ? 0.3608 0.3580 0.3983 0.0095  -0.0144 -0.0051 224 CYS B O   
2632 C CB  . CYS B 224 ? 0.3667 0.3733 0.4046 0.0106  -0.0265 -0.0085 224 CYS B CB  
2633 S SG  . CYS B 224 ? 0.4427 0.4636 0.4910 0.0141  -0.0272 -0.0042 224 CYS B SG  
2634 N N   . LEU B 225 ? 0.3215 0.3036 0.3437 0.0092  -0.0108 -0.0069 225 LEU B N   
2635 C CA  . LEU B 225 ? 0.3874 0.3592 0.4039 0.0114  -0.0010 -0.0047 225 LEU B CA  
2636 C C   . LEU B 225 ? 0.3621 0.3278 0.3747 0.0061  0.0013  -0.0060 225 LEU B C   
2637 O O   . LEU B 225 ? 0.4778 0.4414 0.4922 0.0090  0.0082  -0.0036 225 LEU B O   
2638 C CB  . LEU B 225 ? 0.3694 0.3262 0.3720 0.0105  0.0052  -0.0055 225 LEU B CB  
2639 C CG  . LEU B 225 ? 0.5308 0.4885 0.5339 0.0171  0.0071  -0.0029 225 LEU B CG  
2640 C CD1 . LEU B 225 ? 0.4815 0.4210 0.4680 0.0136  0.0140  -0.0046 225 LEU B CD1 
2641 C CD2 . LEU B 225 ? 0.4260 0.3893 0.4375 0.0271  0.0124  0.0032  225 LEU B CD2 
2642 N N   . MET B 226 ? 0.3697 0.3330 0.3772 -0.0013 -0.0041 -0.0090 226 MET B N   
2643 C CA  . MET B 226 ? 0.4422 0.3990 0.4438 -0.0072 -0.0025 -0.0098 226 MET B CA  
2644 C C   . MET B 226 ? 0.4103 0.3770 0.4233 -0.0061 -0.0058 -0.0088 226 MET B C   
2645 O O   . MET B 226 ? 0.4405 0.4024 0.4509 -0.0082 -0.0013 -0.0083 226 MET B O   
2646 C CB  . MET B 226 ? 0.3482 0.3013 0.3408 -0.0153 -0.0077 -0.0116 226 MET B CB  
2647 C CG  . MET B 226 ? 0.4675 0.4076 0.4444 -0.0205 -0.0025 -0.0129 226 MET B CG  
2648 S SD  . MET B 226 ? 0.6235 0.5649 0.5915 -0.0316 -0.0098 -0.0136 226 MET B SD  
2649 C CE  . MET B 226 ? 0.5617 0.5208 0.5459 -0.0262 -0.0191 -0.0126 226 MET B CE  
2650 N N   . ILE B 227 ? 0.3555 0.3346 0.3794 -0.0038 -0.0129 -0.0088 227 ILE B N   
2651 C CA  . ILE B 227 ? 0.3657 0.3535 0.3993 -0.0039 -0.0153 -0.0081 227 ILE B CA  
2652 C C   . ILE B 227 ? 0.3416 0.3360 0.3828 0.0008  -0.0093 -0.0048 227 ILE B C   
2653 O O   . ILE B 227 ? 0.3520 0.3499 0.3981 -0.0007 -0.0070 -0.0036 227 ILE B O   
2654 C CB  . ILE B 227 ? 0.3248 0.3216 0.3650 -0.0037 -0.0232 -0.0095 227 ILE B CB  
2655 C CG1 . ILE B 227 ? 0.3431 0.3343 0.3779 -0.0068 -0.0277 -0.0114 227 ILE B CG1 
2656 C CG2 . ILE B 227 ? 0.3254 0.3303 0.3737 -0.0057 -0.0252 -0.0092 227 ILE B CG2 
2657 C CD1 . ILE B 227 ? 0.3434 0.3393 0.3818 -0.0053 -0.0328 -0.0129 227 ILE B CD1 
2658 N N   . LEU B 228 ? 0.3475 0.3441 0.3903 0.0070  -0.0060 -0.0025 228 LEU B N   
2659 C CA  . LEU B 228 ? 0.3817 0.3866 0.4336 0.0134  0.0004  0.0026  228 LEU B CA  
2660 C C   . LEU B 228 ? 0.3989 0.3913 0.4445 0.0142  0.0117  0.0038  228 LEU B C   
2661 O O   . LEU B 228 ? 0.3945 0.3949 0.4497 0.0185  0.0176  0.0082  228 LEU B O   
2662 C CB  . LEU B 228 ? 0.3648 0.3737 0.4188 0.0209  0.0016  0.0060  228 LEU B CB  
2663 C CG  . LEU B 228 ? 0.4676 0.4915 0.5290 0.0209  -0.0083 0.0063  228 LEU B CG  
2664 C CD1 . LEU B 228 ? 0.3736 0.3962 0.4321 0.0274  -0.0066 0.0090  228 LEU B CD1 
2665 C CD2 . LEU B 228 ? 0.3996 0.4440 0.4757 0.0212  -0.0116 0.0103  228 LEU B CD2 
2666 N N   . ARG B 229 ? 0.3826 0.3560 0.4118 0.0095  0.0151  0.0002  229 ARG B N   
2667 C CA  . ARG B 229 ? 0.4080 0.3659 0.4267 0.0079  0.0262  0.0001  229 ARG B CA  
2668 C C   . ARG B 229 ? 0.4139 0.3708 0.4309 0.0005  0.0240  -0.0018 229 ARG B C   
2669 O O   . ARG B 229 ? 0.4447 0.3860 0.4485 -0.0036 0.0317  -0.0031 229 ARG B O   
2670 C CB  . ARG B 229 ? 0.4370 0.3736 0.4354 0.0039  0.0312  -0.0030 229 ARG B CB  
2671 C CG  . ARG B 229 ? 0.5336 0.4662 0.5298 0.0104  0.0351  -0.0013 229 ARG B CG  
2672 C CD  . ARG B 229 ? 0.4815 0.4147 0.4849 0.0217  0.0467  0.0046  229 ARG B CD  
2673 N NE  . ARG B 229 ? 0.6489 0.5655 0.6424 0.0213  0.0603  0.0048  229 ARG B NE  
2674 C CZ  . ARG B 229 ? 0.6478 0.5398 0.6232 0.0222  0.0740  0.0042  229 ARG B CZ  
2675 N NH1 . ARG B 229 ? 0.6197 0.5002 0.5846 0.0230  0.0760  0.0034  229 ARG B NH1 
2676 N NH2 . ARG B 229 ? 0.5930 0.4696 0.5593 0.0218  0.0871  0.0042  229 ARG B NH2 
2677 N N   . ASN B 230 ? 0.4212 0.3925 0.4493 -0.0018 0.0142  -0.0022 230 ASN B N   
2678 C CA  . ASN B 230 ? 0.4281 0.3985 0.4551 -0.0083 0.0119  -0.0034 230 ASN B CA  
2679 C C   . ASN B 230 ? 0.4475 0.4031 0.4578 -0.0160 0.0092  -0.0064 230 ASN B C   
2680 O O   . ASN B 230 ? 0.4445 0.3934 0.4483 -0.0214 0.0108  -0.0067 230 ASN B O   
2681 C CB  . ASN B 230 ? 0.3673 0.3376 0.3978 -0.0070 0.0220  -0.0009 230 ASN B CB  
2682 C CG  . ASN B 230 ? 0.4520 0.4432 0.5026 -0.0010 0.0225  0.0035  230 ASN B CG  
2683 O OD1 . ASN B 230 ? 0.4902 0.4938 0.5497 0.0029  0.0166  0.0048  230 ASN B OD1 
2684 N ND2 . ASN B 230 ? 0.4398 0.4364 0.4975 -0.0010 0.0293  0.0062  230 ASN B ND2 
2685 N N   . LEU B 231 ? 0.4164 0.3682 0.4199 -0.0169 0.0051  -0.0079 231 LEU B N   
2686 C CA  . LEU B 231 ? 0.4739 0.4161 0.4632 -0.0247 0.0014  -0.0093 231 LEU B CA  
2687 C C   . LEU B 231 ? 0.4503 0.4001 0.4450 -0.0269 -0.0089 -0.0088 231 LEU B C   
2688 O O   . LEU B 231 ? 0.4547 0.3998 0.4399 -0.0327 -0.0128 -0.0082 231 LEU B O   
2689 C CB  . LEU B 231 ? 0.3976 0.3336 0.3773 -0.0261 0.0018  -0.0105 231 LEU B CB  
2690 C CG  . LEU B 231 ? 0.5296 0.4510 0.4979 -0.0254 0.0140  -0.0112 231 LEU B CG  
2691 C CD1 . LEU B 231 ? 0.4820 0.3978 0.4422 -0.0264 0.0146  -0.0125 231 LEU B CD1 
2692 C CD2 . LEU B 231 ? 0.4857 0.3912 0.4367 -0.0334 0.0205  -0.0122 231 LEU B CD2 
2693 N N   . GLY B 232 ? 0.3753 0.3362 0.3838 -0.0226 -0.0130 -0.0086 232 GLY B N   
2694 C CA  . GLY B 232 ? 0.3806 0.3449 0.3926 -0.0239 -0.0204 -0.0082 232 GLY B CA  
2695 C C   . GLY B 232 ? 0.3930 0.3672 0.4169 -0.0197 -0.0240 -0.0092 232 GLY B C   
2696 O O   . GLY B 232 ? 0.3828 0.3640 0.4137 -0.0164 -0.0217 -0.0095 232 GLY B O   
2697 N N   . TRP B 233 ? 0.3301 0.3041 0.3551 -0.0201 -0.0293 -0.0092 233 TRP B N   
2698 C CA  . TRP B 233 ? 0.3742 0.3537 0.4064 -0.0177 -0.0324 -0.0109 233 TRP B CA  
2699 C C   . TRP B 233 ? 0.3423 0.3223 0.3739 -0.0145 -0.0359 -0.0109 233 TRP B C   
2700 O O   . TRP B 233 ? 0.3647 0.3425 0.3919 -0.0149 -0.0371 -0.0089 233 TRP B O   
2701 C CB  . TRP B 233 ? 0.3002 0.2757 0.3327 -0.0207 -0.0333 -0.0112 233 TRP B CB  
2702 C CG  . TRP B 233 ? 0.3829 0.3499 0.4101 -0.0204 -0.0356 -0.0092 233 TRP B CG  
2703 C CD1 . TRP B 233 ? 0.3298 0.2911 0.3506 -0.0225 -0.0355 -0.0059 233 TRP B CD1 
2704 C CD2 . TRP B 233 ? 0.3664 0.3302 0.3943 -0.0173 -0.0377 -0.0093 233 TRP B CD2 
2705 N NE1 . TRP B 233 ? 0.3627 0.3194 0.3817 -0.0201 -0.0382 -0.0029 233 TRP B NE1 
2706 C CE2 . TRP B 233 ? 0.3328 0.2903 0.3564 -0.0162 -0.0388 -0.0049 233 TRP B CE2 
2707 C CE3 . TRP B 233 ? 0.3866 0.3515 0.4171 -0.0152 -0.0382 -0.0122 233 TRP B CE3 
2708 C CZ2 . TRP B 233 ? 0.4025 0.3553 0.4265 -0.0116 -0.0394 -0.0028 233 TRP B CZ2 
2709 C CZ3 . TRP B 233 ? 0.4035 0.3612 0.4323 -0.0116 -0.0382 -0.0114 233 TRP B CZ3 
2710 C CH2 . TRP B 233 ? 0.3883 0.3403 0.4148 -0.0090 -0.0383 -0.0064 233 TRP B CH2 
2711 N N   . GLY B 234 ? 0.3138 0.2977 0.3498 -0.0122 -0.0375 -0.0130 234 GLY B N   
2712 C CA  . GLY B 234 ? 0.3080 0.2928 0.3442 -0.0087 -0.0395 -0.0132 234 GLY B CA  
2713 C C   . GLY B 234 ? 0.4203 0.4060 0.4585 -0.0075 -0.0403 -0.0161 234 GLY B C   
2714 O O   . GLY B 234 ? 0.4331 0.4200 0.4722 -0.0106 -0.0402 -0.0179 234 GLY B O   
2715 N N   . VAL B 235 ? 0.4181 0.4039 0.4562 -0.0041 -0.0408 -0.0165 235 VAL B N   
2716 C CA  . VAL B 235 ? 0.3579 0.3415 0.3948 -0.0032 -0.0406 -0.0197 235 VAL B CA  
2717 C C   . VAL B 235 ? 0.3904 0.3806 0.4279 -0.0012 -0.0410 -0.0206 235 VAL B C   
2718 O O   . VAL B 235 ? 0.3628 0.3554 0.4012 0.0015  -0.0405 -0.0190 235 VAL B O   
2719 C CB  . VAL B 235 ? 0.5002 0.4757 0.5357 0.0001  -0.0389 -0.0189 235 VAL B CB  
2720 C CG1 . VAL B 235 ? 0.3681 0.3380 0.3993 0.0004  -0.0370 -0.0229 235 VAL B CG1 
2721 C CG2 . VAL B 235 ? 0.3371 0.3043 0.3707 -0.0014 -0.0381 -0.0171 235 VAL B CG2 
2722 N N   . LEU B 236 ? 0.3209 0.3147 0.3574 -0.0033 -0.0419 -0.0228 236 LEU B N   
2723 C CA  . LEU B 236 ? 0.3579 0.3581 0.3942 -0.0013 -0.0424 -0.0227 236 LEU B CA  
2724 C C   . LEU B 236 ? 0.3869 0.3852 0.4180 -0.0028 -0.0432 -0.0260 236 LEU B C   
2725 O O   . LEU B 236 ? 0.3651 0.3592 0.3926 -0.0074 -0.0438 -0.0285 236 LEU B O   
2726 C CB  . LEU B 236 ? 0.3261 0.3352 0.3662 -0.0017 -0.0430 -0.0203 236 LEU B CB  
2727 C CG  . LEU B 236 ? 0.4636 0.4724 0.5062 -0.0007 -0.0405 -0.0174 236 LEU B CG  
2728 C CD1 . LEU B 236 ? 0.3505 0.3678 0.3973 0.0009  -0.0392 -0.0144 236 LEU B CD1 
2729 C CD2 . LEU B 236 ? 0.3978 0.4020 0.4372 0.0015  -0.0387 -0.0169 236 LEU B CD2 
2730 N N   . PRO B 237 ? 0.3910 0.3907 0.4197 -0.0001 -0.0426 -0.0263 237 PRO B N   
2731 C CA  . PRO B 237 ? 0.4187 0.4158 0.4399 -0.0025 -0.0430 -0.0295 237 PRO B CA  
2732 C C   . PRO B 237 ? 0.3328 0.3382 0.3527 -0.0077 -0.0472 -0.0292 237 PRO B C   
2733 O O   . PRO B 237 ? 0.3762 0.3927 0.4022 -0.0064 -0.0491 -0.0252 237 PRO B O   
2734 C CB  . PRO B 237 ? 0.3219 0.3203 0.3414 0.0017  -0.0414 -0.0288 237 PRO B CB  
2735 C CG  . PRO B 237 ? 0.4071 0.4062 0.4326 0.0055  -0.0395 -0.0262 237 PRO B CG  
2736 C CD  . PRO B 237 ? 0.3352 0.3369 0.3656 0.0041  -0.0409 -0.0241 237 PRO B CD  
2737 N N   . GLN B 238 ? 0.4260 0.4259 0.4375 -0.0141 -0.0479 -0.0332 238 GLN B N   
2738 C CA  . GLN B 238 ? 0.3537 0.3636 0.3625 -0.0215 -0.0529 -0.0329 238 GLN B CA  
2739 C C   . GLN B 238 ? 0.4286 0.4504 0.4378 -0.0188 -0.0559 -0.0291 238 GLN B C   
2740 O O   . GLN B 238 ? 0.4494 0.4869 0.4635 -0.0209 -0.0605 -0.0247 238 GLN B O   
2741 C CB  . GLN B 238 ? 0.4775 0.4749 0.4721 -0.0302 -0.0520 -0.0389 238 GLN B CB  
2742 C CG  . GLN B 238 ? 0.6143 0.6196 0.6051 -0.0417 -0.0571 -0.0396 238 GLN B CG  
2743 C CD  . GLN B 238 ? 0.8648 0.8529 0.8371 -0.0517 -0.0548 -0.0467 238 GLN B CD  
2744 O OE1 . GLN B 238 ? 0.8599 0.8335 0.8268 -0.0561 -0.0509 -0.0504 238 GLN B OE1 
2745 N NE2 . GLN B 238 ? 0.8701 0.8575 0.8304 -0.0556 -0.0563 -0.0486 238 GLN B NE2 
2746 N N   . GLU B 239 ? 0.3589 0.3741 0.3638 -0.0135 -0.0529 -0.0299 239 GLU B N   
2747 C CA  . GLU B 239 ? 0.4127 0.4359 0.4161 -0.0102 -0.0546 -0.0262 239 GLU B CA  
2748 C C   . GLU B 239 ? 0.4798 0.5154 0.4945 -0.0045 -0.0555 -0.0193 239 GLU B C   
2749 O O   . GLU B 239 ? 0.4377 0.4842 0.4528 -0.0029 -0.0583 -0.0142 239 GLU B O   
2750 C CB  . GLU B 239 ? 0.4768 0.4891 0.4749 -0.0055 -0.0495 -0.0285 239 GLU B CB  
2751 C CG  . GLU B 239 ? 0.6138 0.6306 0.6097 -0.0011 -0.0495 -0.0246 239 GLU B CG  
2752 C CD  . GLU B 239 ? 0.7673 0.7904 0.7541 -0.0056 -0.0542 -0.0233 239 GLU B CD  
2753 O OE1 . GLU B 239 ? 0.7311 0.7481 0.7070 -0.0127 -0.0550 -0.0283 239 GLU B OE1 
2754 O OE2 . GLU B 239 ? 0.7570 0.7902 0.7459 -0.0020 -0.0565 -0.0170 239 GLU B OE2 
2755 N N   . MET B 240 ? 0.3792 0.4127 0.4021 -0.0012 -0.0526 -0.0184 240 MET B N   
2756 C CA  . MET B 240 ? 0.3432 0.3846 0.3747 0.0044  -0.0512 -0.0123 240 MET B CA  
2757 C C   . MET B 240 ? 0.4001 0.4581 0.4387 0.0024  -0.0553 -0.0074 240 MET B C   
2758 O O   . MET B 240 ? 0.4080 0.4754 0.4528 0.0083  -0.0543 -0.0005 240 MET B O   
2759 C CB  . MET B 240 ? 0.3517 0.3858 0.3877 0.0063  -0.0470 -0.0131 240 MET B CB  
2760 C CG  . MET B 240 ? 0.3320 0.3545 0.3634 0.0084  -0.0433 -0.0157 240 MET B CG  
2761 S SD  . MET B 240 ? 0.4680 0.4844 0.5029 0.0090  -0.0396 -0.0153 240 MET B SD  
2762 C CE  . MET B 240 ? 0.3547 0.3719 0.3898 0.0139  -0.0350 -0.0103 240 MET B CE  
2763 N N   . PHE B 241 ? 0.3702 0.4322 0.4082 -0.0059 -0.0594 -0.0102 241 PHE B N   
2764 C CA  . PHE B 241 ? 0.3492 0.4306 0.3949 -0.0096 -0.0641 -0.0051 241 PHE B CA  
2765 C C   . PHE B 241 ? 0.4065 0.5000 0.4474 -0.0122 -0.0700 -0.0018 241 PHE B C   
2766 O O   . PHE B 241 ? 0.4282 0.5426 0.4780 -0.0120 -0.0740 0.0059  241 PHE B O   
2767 C CB  . PHE B 241 ? 0.4149 0.4953 0.4604 -0.0194 -0.0659 -0.0095 241 PHE B CB  
2768 C CG  . PHE B 241 ? 0.3822 0.4528 0.4326 -0.0170 -0.0608 -0.0112 241 PHE B CG  
2769 C CD1 . PHE B 241 ? 0.4028 0.4845 0.4654 -0.0147 -0.0591 -0.0061 241 PHE B CD1 
2770 C CD2 . PHE B 241 ? 0.4033 0.4546 0.4464 -0.0166 -0.0572 -0.0170 241 PHE B CD2 
2771 C CE1 . PHE B 241 ? 0.4107 0.4824 0.4756 -0.0133 -0.0543 -0.0078 241 PHE B CE1 
2772 C CE2 . PHE B 241 ? 0.4668 0.5103 0.5135 -0.0148 -0.0534 -0.0176 241 PHE B CE2 
2773 C CZ  . PHE B 241 ? 0.4914 0.5441 0.5477 -0.0138 -0.0520 -0.0134 241 PHE B CZ  
2774 N N   . LYS B 242 ? 0.3888 0.4705 0.4159 -0.0146 -0.0703 -0.0067 242 LYS B N   
2775 C CA  . LYS B 242 ? 0.4728 0.5637 0.4932 -0.0158 -0.0751 -0.0029 242 LYS B CA  
2776 C C   . LYS B 242 ? 0.4115 0.5078 0.4381 -0.0038 -0.0725 0.0053  242 LYS B C   
2777 O O   . LYS B 242 ? 0.4099 0.5247 0.4416 -0.0014 -0.0767 0.0141  242 LYS B O   
2778 C CB  . LYS B 242 ? 0.5258 0.5996 0.5285 -0.0207 -0.0741 -0.0106 242 LYS B CB  
2779 C CG  . LYS B 242 ? 0.7491 0.8210 0.7393 -0.0346 -0.0785 -0.0162 242 LYS B CG  
2780 C CD  . LYS B 242 ? 0.8648 0.9129 0.8384 -0.0372 -0.0731 -0.0252 242 LYS B CD  
2781 C CE  . LYS B 242 ? 0.9673 1.0020 0.9312 -0.0478 -0.0716 -0.0331 242 LYS B CE  
2782 N NZ  . LYS B 242 ? 0.9439 0.9561 0.9052 -0.0423 -0.0625 -0.0391 242 LYS B NZ  
2783 N N   . GLU B 243 ? 0.4432 0.5236 0.4689 0.0036  -0.0653 0.0030  243 GLU B N   
2784 C CA  . GLU B 243 ? 0.5109 0.5910 0.5387 0.0140  -0.0611 0.0096  243 GLU B CA  
2785 C C   . GLU B 243 ? 0.4965 0.5895 0.5385 0.0209  -0.0591 0.0182  243 GLU B C   
2786 O O   . GLU B 243 ? 0.4675 0.5672 0.5121 0.0290  -0.0576 0.0269  243 GLU B O   
2787 C CB  . GLU B 243 ? 0.4323 0.4924 0.4548 0.0176  -0.0537 0.0045  243 GLU B CB  
2788 C CG  . GLU B 243 ? 0.5142 0.5627 0.5242 0.0136  -0.0536 -0.0020 243 GLU B CG  
2789 C CD  . GLU B 243 ? 0.7350 0.7683 0.7433 0.0154  -0.0472 -0.0069 243 GLU B CD  
2790 O OE1 . GLU B 243 ? 0.7555 0.7861 0.7702 0.0185  -0.0435 -0.0057 243 GLU B OE1 
2791 O OE2 . GLU B 243 ? 0.7500 0.7747 0.7502 0.0132  -0.0457 -0.0116 243 GLU B OE2 
2792 N N   . ASN B 244 ? 0.4148 0.5104 0.4656 0.0185  -0.0582 0.0165  244 ASN B N   
2793 C CA  . ASN B 244 ? 0.4167 0.5227 0.4811 0.0252  -0.0544 0.0241  244 ASN B CA  
2794 C C   . ASN B 244 ? 0.4419 0.5650 0.5160 0.0176  -0.0597 0.0246  244 ASN B C   
2795 O O   . ASN B 244 ? 0.4672 0.5835 0.5435 0.0136  -0.0575 0.0195  244 ASN B O   
2796 C CB  . ASN B 244 ? 0.3616 0.4491 0.4250 0.0301  -0.0450 0.0212  244 ASN B CB  
2797 C CG  . ASN B 244 ? 0.3740 0.4677 0.4486 0.0382  -0.0383 0.0289  244 ASN B CG  
2798 O OD1 . ASN B 244 ? 0.4201 0.5348 0.5069 0.0399  -0.0410 0.0364  244 ASN B OD1 
2799 N ND2 . ASN B 244 ? 0.4305 0.5060 0.5003 0.0428  -0.0290 0.0273  244 ASN B ND2 
2800 N N   . PRO B 245 ? 0.4222 0.5683 0.5017 0.0146  -0.0671 0.0312  245 PRO B N   
2801 C CA  . PRO B 245 ? 0.4102 0.5741 0.4981 0.0049  -0.0727 0.0315  245 PRO B CA  
2802 C C   . PRO B 245 ? 0.4831 0.6536 0.5863 0.0094  -0.0669 0.0354  245 PRO B C   
2803 O O   . PRO B 245 ? 0.5091 0.6851 0.6165 0.0003  -0.0689 0.0322  245 PRO B O   
2804 C CB  . PRO B 245 ? 0.5362 0.7271 0.6283 0.0025  -0.0815 0.0407  245 PRO B CB  
2805 C CG  . PRO B 245 ? 0.4384 0.6193 0.5178 0.0071  -0.0820 0.0411  245 PRO B CG  
2806 C CD  . PRO B 245 ? 0.4535 0.6101 0.5296 0.0181  -0.0714 0.0383  245 PRO B CD  
2807 N N   . GLU B 246 ? 0.4723 0.6404 0.5824 0.0227  -0.0584 0.0420  246 GLU B N   
2808 C CA  . GLU B 246 ? 0.4983 0.6712 0.6217 0.0274  -0.0512 0.0460  246 GLU B CA  
2809 C C   . GLU B 246 ? 0.4642 0.6152 0.5807 0.0223  -0.0465 0.0358  246 GLU B C   
2810 O O   . GLU B 246 ? 0.4905 0.6446 0.6160 0.0230  -0.0413 0.0374  246 GLU B O   
2811 C CB  . GLU B 246 ? 0.5402 0.7109 0.6692 0.0432  -0.0412 0.0552  246 GLU B CB  
2812 C CG  . GLU B 246 ? 0.7260 0.9173 0.8619 0.0512  -0.0446 0.0674  246 GLU B CG  
2813 C CD  . GLU B 246 ? 0.8181 1.0399 0.9616 0.0414  -0.0577 0.0716  246 GLU B CD  
2814 O OE1 . GLU B 246 ? 0.9113 1.1533 1.0685 0.0359  -0.0601 0.0741  246 GLU B OE1 
2815 O OE2 . GLU B 246 ? 0.7824 1.0080 0.9171 0.0381  -0.0656 0.0721  246 GLU B OE2 
2816 N N   . LEU B 247 ? 0.4036 0.5335 0.5050 0.0176  -0.0480 0.0262  247 LEU B N   
2817 C CA  . LEU B 247 ? 0.4384 0.5503 0.5337 0.0122  -0.0452 0.0178  247 LEU B CA  
2818 C C   . LEU B 247 ? 0.4417 0.5634 0.5418 0.0017  -0.0498 0.0155  247 LEU B C   
2819 O O   . LEU B 247 ? 0.4656 0.5781 0.5655 -0.0011 -0.0460 0.0120  247 LEU B O   
2820 C CB  . LEU B 247 ? 0.3736 0.4656 0.4541 0.0097  -0.0466 0.0098  247 LEU B CB  
2821 C CG  . LEU B 247 ? 0.4605 0.5369 0.5337 0.0174  -0.0406 0.0097  247 LEU B CG  
2822 C CD1 . LEU B 247 ? 0.4507 0.5117 0.5121 0.0135  -0.0424 0.0021  247 LEU B CD1 
2823 C CD2 . LEU B 247 ? 0.3630 0.4300 0.4378 0.0219  -0.0318 0.0110  247 LEU B CD2 
2824 N N   . ASN B 248 ? 0.4187 0.5584 0.5214 -0.0054 -0.0577 0.0173  248 ASN B N   
2825 C CA  . ASN B 248 ? 0.4335 0.5831 0.5399 -0.0171 -0.0616 0.0154  248 ASN B CA  
2826 C C   . ASN B 248 ? 0.4522 0.6179 0.5753 -0.0143 -0.0572 0.0222  248 ASN B C   
2827 O O   . ASN B 248 ? 0.4724 0.6379 0.5974 -0.0223 -0.0565 0.0192  248 ASN B O   
2828 C CB  . ASN B 248 ? 0.4657 0.6320 0.5696 -0.0270 -0.0713 0.0163  248 ASN B CB  
2829 C CG  . ASN B 248 ? 0.5445 0.6922 0.6299 -0.0313 -0.0743 0.0084  248 ASN B CG  
2830 O OD1 . ASN B 248 ? 0.5436 0.6689 0.6179 -0.0351 -0.0717 -0.0001 248 ASN B OD1 
2831 N ND2 . ASN B 248 ? 0.5295 0.6866 0.6115 -0.0300 -0.0792 0.0120  248 ASN B ND2 
2832 N N   . ASN B 249 ? 0.4169 0.5954 0.5518 -0.0024 -0.0528 0.0317  249 ASN B N   
2833 C CA  . ASN B 249 ? 0.3782 0.5709 0.5295 0.0023  -0.0463 0.0389  249 ASN B CA  
2834 C C   . ASN B 249 ? 0.4618 0.6307 0.6079 0.0065  -0.0359 0.0345  249 ASN B C   
2835 O O   . ASN B 249 ? 0.4788 0.6545 0.6349 0.0071  -0.0298 0.0376  249 ASN B O   
2836 C CB  . ASN B 249 ? 0.4284 0.6411 0.5936 0.0153  -0.0433 0.0516  249 ASN B CB  
2837 C CG  . ASN B 249 ? 0.5753 0.8170 0.7476 0.0107  -0.0544 0.0584  249 ASN B CG  
2838 O OD1 . ASN B 249 ? 0.6864 0.9406 0.8646 0.0208  -0.0546 0.0679  249 ASN B OD1 
2839 N ND2 . ASN B 249 ? 0.6274 0.8789 0.7974 -0.0052 -0.0635 0.0537  249 ASN B ND2 
2840 N N   . LYS B 250 ? 0.3839 0.5264 0.5145 0.0089  -0.0336 0.0277  250 LYS B N   
2841 C CA  . LYS B 250 ? 0.4564 0.5763 0.5796 0.0121  -0.0245 0.0240  250 LYS B CA  
2842 C C   . LYS B 250 ? 0.3611 0.4634 0.4725 0.0026  -0.0272 0.0148  250 LYS B C   
2843 O O   . LYS B 250 ? 0.5019 0.5935 0.6109 0.0013  -0.0214 0.0130  250 LYS B O   
2844 C CB  . LYS B 250 ? 0.4643 0.5675 0.5780 0.0213  -0.0192 0.0242  250 LYS B CB  
2845 C CG  . LYS B 250 ? 0.4590 0.5701 0.5816 0.0335  -0.0109 0.0337  250 LYS B CG  
2846 C CD  . LYS B 250 ? 0.5756 0.6914 0.7080 0.0363  -0.0017 0.0379  250 LYS B CD  
2847 C CE  . LYS B 250 ? 0.7625 0.8915 0.9078 0.0496  0.0067  0.0496  250 LYS B CE  
2848 N NZ  . LYS B 250 ? 0.8261 0.9794 0.9910 0.0503  0.0095  0.0568  250 LYS B NZ  
2849 N N   . LEU B 251 ? 0.3366 0.4349 0.4401 -0.0036 -0.0351 0.0095  251 LEU B N   
2850 C CA  . LEU B 251 ? 0.4013 0.4818 0.4936 -0.0105 -0.0369 0.0019  251 LEU B CA  
2851 C C   . LEU B 251 ? 0.4639 0.5517 0.5568 -0.0214 -0.0427 -0.0007 251 LEU B C   
2852 O O   . LEU B 251 ? 0.4897 0.5942 0.5873 -0.0250 -0.0480 0.0015  251 LEU B O   
2853 C CB  . LEU B 251 ? 0.3437 0.4097 0.4246 -0.0082 -0.0390 -0.0023 251 LEU B CB  
2854 C CG  . LEU B 251 ? 0.3801 0.4368 0.4573 0.0002  -0.0335 -0.0007 251 LEU B CG  
2855 C CD1 . LEU B 251 ? 0.3205 0.3661 0.3880 0.0009  -0.0361 -0.0047 251 LEU B CD1 
2856 C CD2 . LEU B 251 ? 0.3680 0.4130 0.4422 0.0005  -0.0270 -0.0012 251 LEU B CD2 
2857 N N   . LYS B 252 ? 0.4611 0.5358 0.5480 -0.0275 -0.0414 -0.0051 252 LYS B N   
2858 C CA  . LYS B 252 ? 0.3664 0.4409 0.4494 -0.0388 -0.0455 -0.0088 252 LYS B CA  
2859 C C   . LYS B 252 ? 0.3953 0.4461 0.4639 -0.0406 -0.0455 -0.0151 252 LYS B C   
2860 O O   . LYS B 252 ? 0.3945 0.4314 0.4589 -0.0348 -0.0422 -0.0157 252 LYS B O   
2861 C CB  . LYS B 252 ? 0.3646 0.4460 0.4543 -0.0452 -0.0427 -0.0072 252 LYS B CB  
2862 C CG  . LYS B 252 ? 0.4416 0.5062 0.5269 -0.0429 -0.0365 -0.0082 252 LYS B CG  
2863 C CD  . LYS B 252 ? 0.5728 0.6413 0.6616 -0.0517 -0.0342 -0.0079 252 LYS B CD  
2864 C CE  . LYS B 252 ? 0.5632 0.6200 0.6411 -0.0629 -0.0374 -0.0133 252 LYS B CE  
2865 N NZ  . LYS B 252 ? 0.5703 0.6294 0.6501 -0.0727 -0.0346 -0.0132 252 LYS B NZ  
2866 N N   . ALA B 253 ? 0.4540 0.5002 0.5146 -0.0488 -0.0490 -0.0194 253 ALA B N   
2867 C CA  . ALA B 253 ? 0.4317 0.4546 0.4790 -0.0497 -0.0474 -0.0245 253 ALA B CA  
2868 C C   . ALA B 253 ? 0.4822 0.4929 0.5268 -0.0527 -0.0435 -0.0250 253 ALA B C   
2869 O O   . ALA B 253 ? 0.5402 0.5573 0.5879 -0.0607 -0.0431 -0.0245 253 ALA B O   
2870 C CB  . ALA B 253 ? 0.4261 0.4440 0.4629 -0.0583 -0.0501 -0.0293 253 ALA B CB  
2871 N N   . LEU B 254 ? 0.4235 0.4180 0.4628 -0.0464 -0.0408 -0.0252 254 LEU B N   
2872 C CA  . LEU B 254 ? 0.4551 0.4346 0.4887 -0.0489 -0.0374 -0.0253 254 LEU B CA  
2873 C C   . LEU B 254 ? 0.5654 0.5276 0.5868 -0.0548 -0.0361 -0.0296 254 LEU B C   
2874 O O   . LEU B 254 ? 0.6029 0.5573 0.6184 -0.0517 -0.0362 -0.0319 254 LEU B O   
2875 C CB  . LEU B 254 ? 0.5489 0.5200 0.5813 -0.0402 -0.0357 -0.0224 254 LEU B CB  
2876 C CG  . LEU B 254 ? 0.4712 0.4483 0.5087 -0.0373 -0.0341 -0.0187 254 LEU B CG  
2877 C CD1 . LEU B 254 ? 0.4798 0.4472 0.5126 -0.0313 -0.0338 -0.0163 254 LEU B CD1 
2878 C CD2 . LEU B 254 ? 0.4981 0.4753 0.5365 -0.0438 -0.0311 -0.0177 254 LEU B CD2 
2879 N N   . ASP B 255 ? 0.6155 0.5702 0.6320 -0.0636 -0.0337 -0.0308 255 ASP B N   
2880 C CA  . ASP B 255 ? 0.7257 0.6593 0.7276 -0.0703 -0.0306 -0.0352 255 ASP B CA  
2881 C C   . ASP B 255 ? 0.6935 0.6064 0.6891 -0.0633 -0.0260 -0.0326 255 ASP B C   
2882 O O   . ASP B 255 ? 0.6337 0.5418 0.6286 -0.0656 -0.0238 -0.0303 255 ASP B O   
2883 C CB  . ASP B 255 ? 0.7357 0.6724 0.7343 -0.0855 -0.0305 -0.0379 255 ASP B CB  
2884 C CG  . ASP B 255 ? 0.9072 0.8159 0.8881 -0.0930 -0.0249 -0.0419 255 ASP B CG  
2885 O OD1 . ASP B 255 ? 1.2515 1.1407 1.2212 -0.0885 -0.0216 -0.0443 255 ASP B OD1 
2886 O OD2 . ASP B 255 ? 0.8677 0.7732 0.8449 -0.1040 -0.0227 -0.0428 255 ASP B OD2 
2887 N N   . VAL B 256 ? 0.6257 0.5275 0.6171 -0.0544 -0.0245 -0.0324 256 VAL B N   
2888 C CA  . VAL B 256 ? 0.5063 0.3991 0.4980 -0.0436 -0.0225 -0.0272 256 VAL B CA  
2889 C C   . VAL B 256 ? 0.5733 0.4465 0.5555 -0.0386 -0.0176 -0.0284 256 VAL B C   
2890 O O   . VAL B 256 ? 0.5922 0.4573 0.5747 -0.0284 -0.0151 -0.0234 256 VAL B O   
2891 C CB  . VAL B 256 ? 0.5011 0.4131 0.5050 -0.0359 -0.0272 -0.0235 256 VAL B CB  
2892 C CG1 . VAL B 256 ? 0.4971 0.4088 0.5023 -0.0268 -0.0273 -0.0228 256 VAL B CG1 
2893 C CG2 . VAL B 256 ? 0.6291 0.5421 0.6354 -0.0333 -0.0275 -0.0181 256 VAL B CG2 
2894 N N   . PHE B 257 ? 0.5191 0.3840 0.4918 -0.0465 -0.0154 -0.0348 257 PHE B N   
2895 C CA  . PHE B 257 ? 0.5896 0.4365 0.5522 -0.0424 -0.0097 -0.0374 257 PHE B CA  
2896 C C   . PHE B 257 ? 0.5190 0.3369 0.4692 -0.0397 -0.0007 -0.0358 257 PHE B C   
2897 O O   . PHE B 257 ? 0.5947 0.3976 0.5403 -0.0302 0.0056  -0.0342 257 PHE B O   
2898 C CB  . PHE B 257 ? 0.6502 0.4971 0.6038 -0.0541 -0.0104 -0.0451 257 PHE B CB  
2899 C CG  . PHE B 257 ? 0.8798 0.7555 0.8457 -0.0562 -0.0191 -0.0453 257 PHE B CG  
2900 C CD1 . PHE B 257 ? 0.8642 0.7493 0.8356 -0.0480 -0.0211 -0.0447 257 PHE B CD1 
2901 C CD2 . PHE B 257 ? 0.8783 0.7722 0.8512 -0.0653 -0.0245 -0.0451 257 PHE B CD2 
2902 C CE1 . PHE B 257 ? 0.8950 0.8044 0.8766 -0.0491 -0.0281 -0.0441 257 PHE B CE1 
2903 C CE2 . PHE B 257 ? 0.9269 0.8468 0.9117 -0.0653 -0.0313 -0.0438 257 PHE B CE2 
2904 C CZ  . PHE B 257 ? 0.9475 0.8740 0.9358 -0.0570 -0.0331 -0.0433 257 PHE B CZ  
2905 N N   . ASP B 258 ? 0.6045 0.4137 0.5490 -0.0474 0.0008  -0.0355 258 ASP B N   
2906 C CA  . ASP B 258 ? 0.6298 0.4092 0.5611 -0.0447 0.0100  -0.0333 258 ASP B CA  
2907 C C   . ASP B 258 ? 0.5309 0.3103 0.4704 -0.0289 0.0108  -0.0232 258 ASP B C   
2908 O O   . ASP B 258 ? 0.5644 0.3193 0.4943 -0.0229 0.0191  -0.0193 258 ASP B O   
2909 C CB  . ASP B 258 ? 0.6235 0.3938 0.5459 -0.0584 0.0115  -0.0356 258 ASP B CB  
2910 C CG  . ASP B 258 ? 0.7468 0.5120 0.6571 -0.0756 0.0124  -0.0450 258 ASP B CG  
2911 O OD1 . ASP B 258 ? 0.8221 0.5657 0.7170 -0.0775 0.0191  -0.0500 258 ASP B OD1 
2912 O OD2 . ASP B 258 ? 0.8424 0.6264 0.7585 -0.0875 0.0064  -0.0471 258 ASP B OD2 
2913 N N   . PHE B 259 ? 0.4690 0.2744 0.4249 -0.0225 0.0028  -0.0184 259 PHE B N   
2914 C CA  . PHE B 259 ? 0.5481 0.3569 0.5119 -0.0087 0.0023  -0.0085 259 PHE B CA  
2915 C C   . PHE B 259 ? 0.5310 0.3623 0.5088 -0.0005 -0.0031 -0.0060 259 PHE B C   
2916 O O   . PHE B 259 ? 0.4766 0.3200 0.4635 0.0073  -0.0069 0.0021  259 PHE B O   
2917 C CB  . PHE B 259 ? 0.5514 0.3651 0.5172 -0.0107 -0.0014 -0.0027 259 PHE B CB  
2918 C CG  . PHE B 259 ? 0.4895 0.3256 0.4633 -0.0190 -0.0091 -0.0056 259 PHE B CG  
2919 C CD1 . PHE B 259 ? 0.4423 0.3012 0.4282 -0.0146 -0.0158 -0.0032 259 PHE B CD1 
2920 C CD2 . PHE B 259 ? 0.5570 0.3904 0.5257 -0.0311 -0.0086 -0.0100 259 PHE B CD2 
2921 C CE1 . PHE B 259 ? 0.5235 0.3993 0.5151 -0.0212 -0.0206 -0.0054 259 PHE B CE1 
2922 C CE2 . PHE B 259 ? 0.4766 0.3301 0.4535 -0.0371 -0.0139 -0.0115 259 PHE B CE2 
2923 C CZ  . PHE B 259 ? 0.5528 0.4261 0.5406 -0.0316 -0.0194 -0.0092 259 PHE B CZ  
2924 N N   . THR B 260 ? 0.4195 0.2561 0.3980 -0.0028 -0.0035 -0.0126 260 THR B N   
2925 C CA  . THR B 260 ? 0.4706 0.3254 0.4604 0.0045  -0.0071 -0.0108 260 THR B CA  
2926 C C   . THR B 260 ? 0.4933 0.3363 0.4772 0.0078  -0.0004 -0.0152 260 THR B C   
2927 O O   . THR B 260 ? 0.4295 0.2540 0.3995 0.0003  0.0049  -0.0221 260 THR B O   
2928 C CB  . THR B 260 ? 0.5008 0.3785 0.4985 -0.0020 -0.0154 -0.0143 260 THR B CB  
2929 O OG1 . THR B 260 ? 0.5631 0.4377 0.5538 -0.0132 -0.0155 -0.0221 260 THR B OG1 
2930 C CG2 . THR B 260 ? 0.5360 0.4258 0.5399 -0.0032 -0.0208 -0.0092 260 THR B CG2 
2931 N N   . PRO B 261 ? 0.4764 0.3291 0.4693 0.0177  0.0000  -0.0114 261 PRO B N   
2932 C CA  . PRO B 261 ? 0.5422 0.3852 0.5293 0.0202  0.0066  -0.0162 261 PRO B CA  
2933 C C   . PRO B 261 ? 0.5350 0.3885 0.5198 0.0103  0.0015  -0.0245 261 PRO B C   
2934 O O   . PRO B 261 ? 0.5414 0.4144 0.5338 0.0052  -0.0073 -0.0248 261 PRO B O   
2935 C CB  . PRO B 261 ? 0.5478 0.4034 0.5485 0.0338  0.0077  -0.0082 261 PRO B CB  
2936 C CG  . PRO B 261 ? 0.5409 0.4215 0.5548 0.0330  -0.0028 -0.0029 261 PRO B CG  
2937 C CD  . PRO B 261 ? 0.5322 0.4060 0.5403 0.0260  -0.0054 -0.0027 261 PRO B CD  
2938 N N   . ARG B 262 ? 0.4494 0.2880 0.4220 0.0076  0.0077  -0.0311 262 ARG B N   
2939 C CA  . ARG B 262 ? 0.4655 0.3146 0.4358 0.0003  0.0033  -0.0375 262 ARG B CA  
2940 C C   . ARG B 262 ? 0.4814 0.3537 0.4670 0.0077  -0.0018 -0.0334 262 ARG B C   
2941 O O   . ARG B 262 ? 0.5797 0.4519 0.5709 0.0182  0.0030  -0.0293 262 ARG B O   
2942 C CB  . ARG B 262 ? 0.5091 0.3356 0.4616 -0.0028 0.0123  -0.0443 262 ARG B CB  
2943 C CG  . ARG B 262 ? 0.6944 0.5281 0.6395 -0.0129 0.0079  -0.0513 262 ARG B CG  
2944 C CD  . ARG B 262 ? 0.6840 0.4906 0.6080 -0.0165 0.0185  -0.0581 262 ARG B CD  
2945 N NE  . ARG B 262 ? 0.6977 0.4830 0.6028 -0.0295 0.0217  -0.0639 262 ARG B NE  
2946 C CZ  . ARG B 262 ? 0.6993 0.4575 0.5807 -0.0373 0.0308  -0.0714 262 ARG B CZ  
2947 N NH1 . ARG B 262 ? 0.6827 0.4287 0.5563 -0.0313 0.0394  -0.0735 262 ARG B NH1 
2948 N NH2 . ARG B 262 ? 0.7020 0.4432 0.5657 -0.0522 0.0324  -0.0769 262 ARG B NH2 
2949 N N   . PHE B 263 ? 0.4055 0.2977 0.3979 0.0023  -0.0108 -0.0340 263 PHE B N   
2950 C CA  . PHE B 263 ? 0.4866 0.3987 0.4909 0.0074  -0.0153 -0.0308 263 PHE B CA  
2951 C C   . PHE B 263 ? 0.5249 0.4378 0.5235 0.0056  -0.0143 -0.0357 263 PHE B C   
2952 O O   . PHE B 263 ? 0.5170 0.4309 0.5081 -0.0032 -0.0175 -0.0406 263 PHE B O   
2953 C CB  . PHE B 263 ? 0.4555 0.3848 0.4679 0.0034  -0.0234 -0.0288 263 PHE B CB  
2954 C CG  . PHE B 263 ? 0.5537 0.4820 0.5700 0.0043  -0.0245 -0.0241 263 PHE B CG  
2955 C CD1 . PHE B 263 ? 0.5712 0.5050 0.5956 0.0118  -0.0246 -0.0173 263 PHE B CD1 
2956 C CD2 . PHE B 263 ? 0.4952 0.4186 0.5070 -0.0032 -0.0257 -0.0259 263 PHE B CD2 
2957 C CE1 . PHE B 263 ? 0.5025 0.4355 0.5288 0.0120  -0.0261 -0.0124 263 PHE B CE1 
2958 C CE2 . PHE B 263 ? 0.5156 0.4371 0.5297 -0.0027 -0.0262 -0.0215 263 PHE B CE2 
2959 C CZ  . PHE B 263 ? 0.4605 0.3862 0.4811 0.0050  -0.0266 -0.0147 263 PHE B CZ  
2960 N N   . GLU B 264 ? 0.5212 0.4354 0.5237 0.0136  -0.0101 -0.0337 264 GLU B N   
2961 C CA  . GLU B 264 ? 0.5024 0.4148 0.4979 0.0126  -0.0075 -0.0381 264 GLU B CA  
2962 C C   . GLU B 264 ? 0.5079 0.4297 0.5139 0.0220  -0.0047 -0.0336 264 GLU B C   
2963 O O   . GLU B 264 ? 0.4384 0.3633 0.4545 0.0298  -0.0023 -0.0274 264 GLU B O   
2964 C CB  . GLU B 264 ? 0.4839 0.3721 0.4619 0.0092  0.0008  -0.0441 264 GLU B CB  
2965 C CG  . GLU B 264 ? 0.6195 0.4914 0.5973 0.0190  0.0117  -0.0411 264 GLU B CG  
2966 C CD  . GLU B 264 ? 0.8157 0.6582 0.7730 0.0141  0.0210  -0.0473 264 GLU B CD  
2967 O OE1 . GLU B 264 ? 0.8070 0.6437 0.7496 0.0016  0.0182  -0.0544 264 GLU B OE1 
2968 O OE2 . GLU B 264 ? 0.7715 0.5966 0.7267 0.0225  0.0314  -0.0446 264 GLU B OE2 
2969 N N   . TYR B 265 ? 0.4790 0.4069 0.4826 0.0206  -0.0053 -0.0362 265 TYR B N   
2970 C CA  . TYR B 265 ? 0.5154 0.4504 0.5264 0.0278  -0.0011 -0.0332 265 TYR B CA  
2971 C C   . TYR B 265 ? 0.5359 0.4554 0.5339 0.0282  0.0077  -0.0383 265 TYR B C   
2972 O O   . TYR B 265 ? 0.5636 0.4749 0.5469 0.0201  0.0064  -0.0446 265 TYR B O   
2973 C CB  . TYR B 265 ? 0.4924 0.4456 0.5099 0.0259  -0.0076 -0.0317 265 TYR B CB  
2974 C CG  . TYR B 265 ? 0.3566 0.3238 0.3844 0.0247  -0.0150 -0.0272 265 TYR B CG  
2975 C CD1 . TYR B 265 ? 0.4049 0.3777 0.4433 0.0292  -0.0152 -0.0212 265 TYR B CD1 
2976 C CD2 . TYR B 265 ? 0.3494 0.3240 0.3756 0.0193  -0.0214 -0.0284 265 TYR B CD2 
2977 C CE1 . TYR B 265 ? 0.4416 0.4253 0.4862 0.0266  -0.0216 -0.0176 265 TYR B CE1 
2978 C CE2 . TYR B 265 ? 0.5099 0.4940 0.5429 0.0179  -0.0263 -0.0248 265 TYR B CE2 
2979 C CZ  . TYR B 265 ? 0.3933 0.3813 0.4344 0.0207  -0.0265 -0.0200 265 TYR B CZ  
2980 O OH  . TYR B 265 ? 0.5503 0.5459 0.5952 0.0179  -0.0311 -0.0170 265 TYR B OH  
2981 N N   . TYR B 266 ? 0.4611 0.3776 0.4645 0.0374  0.0168  -0.0352 266 TYR B N   
2982 C CA  . TYR B 266 ? 0.5188 0.4225 0.5115 0.0390  0.0267  -0.0393 266 TYR B CA  
2983 C C   . TYR B 266 ? 0.4752 0.3971 0.4781 0.0420  0.0257  -0.0364 266 TYR B C   
2984 O O   . TYR B 266 ? 0.4981 0.4343 0.5181 0.0497  0.0273  -0.0293 266 TYR B O   
2985 C CB  . TYR B 266 ? 0.4959 0.3818 0.4870 0.0481  0.0400  -0.0376 266 TYR B CB  
2986 C CG  . TYR B 266 ? 0.6906 0.5525 0.6656 0.0431  0.0429  -0.0422 266 TYR B CG  
2987 C CD1 . TYR B 266 ? 0.7523 0.5913 0.7032 0.0343  0.0480  -0.0514 266 TYR B CD1 
2988 C CD2 . TYR B 266 ? 0.6357 0.4976 0.6180 0.0455  0.0401  -0.0375 266 TYR B CD2 
2989 C CE1 . TYR B 266 ? 0.7633 0.5798 0.6978 0.0274  0.0507  -0.0561 266 TYR B CE1 
2990 C CE2 . TYR B 266 ? 0.7690 0.6081 0.7357 0.0398  0.0432  -0.0419 266 TYR B CE2 
2991 C CZ  . TYR B 266 ? 0.8772 0.6936 0.8200 0.0304  0.0486  -0.0514 266 TYR B CZ  
2992 O OH  . TYR B 266 ? 0.9393 0.7323 0.8650 0.0227  0.0519  -0.0562 266 TYR B OH  
2993 N N   . VAL B 267 ? 0.4318 0.3540 0.4241 0.0351  0.0227  -0.0414 267 VAL B N   
2994 C CA  . VAL B 267 ? 0.4168 0.3549 0.4162 0.0357  0.0208  -0.0391 267 VAL B CA  
2995 C C   . VAL B 267 ? 0.5226 0.4533 0.5179 0.0405  0.0326  -0.0404 267 VAL B C   
2996 O O   . VAL B 267 ? 0.5084 0.4195 0.4855 0.0376  0.0392  -0.0466 267 VAL B O   
2997 C CB  . VAL B 267 ? 0.4600 0.4021 0.4500 0.0269  0.0118  -0.0424 267 VAL B CB  
2998 C CG1 . VAL B 267 ? 0.4883 0.4443 0.4844 0.0276  0.0106  -0.0398 267 VAL B CG1 
2999 C CG2 . VAL B 267 ? 0.4703 0.4188 0.4644 0.0229  0.0019  -0.0411 267 VAL B CG2 
3000 N N   . ASP B 268 ? 0.5227 0.4691 0.5343 0.0469  0.0357  -0.0345 268 ASP B N   
3001 C CA  . ASP B 268 ? 0.4581 0.4018 0.4693 0.0519  0.0473  -0.0345 268 ASP B CA  
3002 C C   . ASP B 268 ? 0.4998 0.4588 0.5144 0.0481  0.0438  -0.0336 268 ASP B C   
3003 O O   . ASP B 268 ? 0.4775 0.4533 0.5021 0.0450  0.0344  -0.0301 268 ASP B O   
3004 C CB  . ASP B 268 ? 0.4778 0.4290 0.5075 0.0636  0.0561  -0.0268 268 ASP B CB  
3005 C CG  . ASP B 268 ? 0.6204 0.5529 0.6455 0.0689  0.0621  -0.0270 268 ASP B CG  
3006 O OD1 . ASP B 268 ? 0.7429 0.6505 0.7462 0.0642  0.0660  -0.0350 268 ASP B OD1 
3007 O OD2 . ASP B 268 ? 0.7037 0.6461 0.7458 0.0772  0.0630  -0.0188 268 ASP B OD2 
3008 N N   . LEU B 269 ? 0.4064 0.3572 0.4106 0.0478  0.0522  -0.0371 269 LEU B N   
3009 C CA  . LEU B 269 ? 0.4492 0.4127 0.4569 0.0455  0.0522  -0.0356 269 LEU B CA  
3010 C C   . LEU B 269 ? 0.4134 0.3904 0.4397 0.0539  0.0620  -0.0294 269 LEU B C   
3011 O O   . LEU B 269 ? 0.4618 0.4274 0.4854 0.0604  0.0749  -0.0302 269 LEU B O   
3012 C CB  . LEU B 269 ? 0.4729 0.4206 0.4578 0.0399  0.0557  -0.0424 269 LEU B CB  
3013 C CG  . LEU B 269 ? 0.5457 0.5031 0.5309 0.0371  0.0568  -0.0412 269 LEU B CG  
3014 C CD1 . LEU B 269 ? 0.3617 0.3299 0.3483 0.0309  0.0442  -0.0394 269 LEU B CD1 
3015 C CD2 . LEU B 269 ? 0.4291 0.3684 0.3918 0.0339  0.0643  -0.0471 269 LEU B CD2 
3016 N N   . VAL B 270 ? 0.3990 0.4000 0.4437 0.0532  0.0566  -0.0229 270 VAL B N   
3017 C CA  . VAL B 270 ? 0.3324 0.3533 0.3998 0.0605  0.0630  -0.0146 270 VAL B CA  
3018 C C   . VAL B 270 ? 0.3959 0.4322 0.4684 0.0559  0.0648  -0.0129 270 VAL B C   
3019 O O   . VAL B 270 ? 0.4182 0.4550 0.4817 0.0467  0.0572  -0.0158 270 VAL B O   
3020 C CB  . VAL B 270 ? 0.3880 0.4268 0.4735 0.0623  0.0542  -0.0071 270 VAL B CB  
3021 C CG1 . VAL B 270 ? 0.3932 0.4561 0.5038 0.0702  0.0599  0.0034  270 VAL B CG1 
3022 C CG2 . VAL B 270 ? 0.3913 0.4126 0.4693 0.0655  0.0522  -0.0093 270 VAL B CG2 
3023 N N   . TRP B 271 ? 0.4275 0.4756 0.5142 0.0627  0.0759  -0.0078 271 TRP B N   
3024 C CA  . TRP B 271 ? 0.4663 0.5321 0.5609 0.0581  0.0786  -0.0051 271 TRP B CA  
3025 C C   . TRP B 271 ? 0.4163 0.5083 0.5385 0.0664  0.0859  0.0054  271 TRP B C   
3026 O O   . TRP B 271 ? 0.4241 0.5160 0.5568 0.0777  0.0914  0.0101  271 TRP B O   
3027 C CB  . TRP B 271 ? 0.3689 0.4161 0.4437 0.0555  0.0877  -0.0124 271 TRP B CB  
3028 C CG  . TRP B 271 ? 0.4381 0.4702 0.5089 0.0654  0.1036  -0.0140 271 TRP B CG  
3029 C CD1 . TRP B 271 ? 0.4889 0.5311 0.5726 0.0723  0.1178  -0.0095 271 TRP B CD1 
3030 C CD2 . TRP B 271 ? 0.3603 0.3629 0.4112 0.0687  0.1080  -0.0208 271 TRP B CD2 
3031 N NE1 . TRP B 271 ? 0.4646 0.4830 0.5367 0.0806  0.1318  -0.0133 271 TRP B NE1 
3032 C CE2 . TRP B 271 ? 0.4439 0.4368 0.4946 0.0777  0.1260  -0.0206 271 TRP B CE2 
3033 C CE3 . TRP B 271 ? 0.4120 0.3955 0.4450 0.0642  0.0991  -0.0269 271 TRP B CE3 
3034 C CZ2 . TRP B 271 ? 0.4951 0.4569 0.5254 0.0813  0.1355  -0.0272 271 TRP B CZ2 
3035 C CZ3 . TRP B 271 ? 0.5014 0.4571 0.5157 0.0669  0.1074  -0.0330 271 TRP B CZ3 
3036 C CH2 . TRP B 271 ? 0.5069 0.4504 0.5186 0.0750  0.1255  -0.0335 271 TRP B CH2 
3037 N N   . SER B 272 ? 0.3986 0.5135 0.5326 0.0608  0.0865  0.0097  272 SER B N   
3038 C CA  . SER B 272 ? 0.4004 0.5459 0.5629 0.0672  0.0929  0.0209  272 SER B CA  
3039 C C   . SER B 272 ? 0.4290 0.5679 0.5920 0.0757  0.1110  0.0203  272 SER B C   
3040 O O   . SER B 272 ? 0.4415 0.5701 0.5898 0.0692  0.1159  0.0139  272 SER B O   
3041 C CB  . SER B 272 ? 0.4654 0.6404 0.6401 0.0547  0.0846  0.0258  272 SER B CB  
3042 O OG  . SER B 272 ? 0.4597 0.6665 0.6611 0.0591  0.0921  0.0364  272 SER B OG  
3043 N N   . ARG B 273 ? 0.4987 0.6421 0.6776 0.0907  0.1218  0.0272  273 ARG B N   
3044 C CA  . ARG B 273 ? 0.5648 0.7023 0.7458 0.1003  0.1414  0.0277  273 ARG B CA  
3045 C C   . ARG B 273 ? 0.5396 0.7020 0.7328 0.0938  0.1457  0.0312  273 ARG B C   
3046 O O   . ARG B 273 ? 0.5990 0.7464 0.7792 0.0935  0.1582  0.0255  273 ARG B O   
3047 C CB  . ARG B 273 ? 0.5750 0.7221 0.7786 0.1184  0.1527  0.0385  273 ARG B CB  
3048 C CG  . ARG B 273 ? 0.6358 0.7598 0.8302 0.1262  0.1510  0.0369  273 ARG B CG  
3049 C CD  . ARG B 273 ? 0.6029 0.7470 0.8260 0.1430  0.1590  0.0513  273 ARG B CD  
3050 N NE  . ARG B 273 ? 0.6958 0.8236 0.9177 0.1568  0.1818  0.0518  273 ARG B NE  
3051 C CZ  . ARG B 273 ? 0.6953 0.8018 0.9116 0.1678  0.1886  0.0544  273 ARG B CZ  
3052 N NH1 . ARG B 273 ? 0.6705 0.7746 0.8893 0.1713  0.1796  0.0583  273 ARG B NH1 
3053 N NH2 . ARG B 273 ? 0.6832 0.7695 0.8902 0.1748  0.2054  0.0531  273 ARG B NH2 
3054 N N   . GLU B 274 ? 0.5381 0.7383 0.7551 0.0877  0.1359  0.0407  274 GLU B N   
3055 C CA  . GLU B 274 ? 0.6672 0.8958 0.8995 0.0811  0.1403  0.0458  274 GLU B CA  
3056 C C   . GLU B 274 ? 0.6388 0.8627 0.8525 0.0618  0.1303  0.0379  274 GLU B C   
3057 O O   . GLU B 274 ? 0.6726 0.9231 0.8991 0.0525  0.1305  0.0426  274 GLU B O   
3058 C CB  . GLU B 274 ? 0.5952 0.8712 0.8646 0.0836  0.1358  0.0618  274 GLU B CB  
3059 C CG  . GLU B 274 ? 0.6931 0.9856 0.9649 0.0704  0.1150  0.0642  274 GLU B CG  
3060 C CD  . GLU B 274 ? 0.7517 1.0486 1.0348 0.0811  0.1083  0.0714  274 GLU B CD  
3061 O OE1 . GLU B 274 ? 0.6480 0.9835 0.9602 0.0840  0.1042  0.0857  274 GLU B OE1 
3062 O OE2 . GLU B 274 ? 0.6777 0.9407 0.9406 0.0863  0.1072  0.0635  274 GLU B OE2 
3063 N N   . SER B 275 ? 0.5277 0.7198 0.7125 0.0555  0.1219  0.0270  275 SER B N   
3064 C CA  . SER B 275 ? 0.6424 0.8259 0.8077 0.0396  0.1157  0.0200  275 SER B CA  
3065 C C   . SER B 275 ? 0.6980 0.8544 0.8405 0.0398  0.1277  0.0114  275 SER B C   
3066 O O   . SER B 275 ? 0.6687 0.8068 0.8049 0.0510  0.1393  0.0087  275 SER B O   
3067 C CB  . SER B 275 ? 0.5972 0.7648 0.7454 0.0323  0.1000  0.0146  275 SER B CB  
3068 O OG  . SER B 275 ? 0.6011 0.7952 0.7642 0.0233  0.0883  0.0211  275 SER B OG  
3069 N N   . GLU B 276 ? 0.7222 0.8746 0.8506 0.0266  0.1255  0.0074  276 GLU B N   
3070 C CA  . GLU B 276 ? 0.8160 0.9413 0.9187 0.0246  0.1343  -0.0008 276 GLU B CA  
3071 C C   . GLU B 276 ? 0.8378 0.9324 0.9120 0.0212  0.1243  -0.0092 276 GLU B C   
3072 O O   . GLU B 276 ? 0.8019 0.8964 0.8694 0.0117  0.1124  -0.0100 276 GLU B O   
3073 C CB  . GLU B 276 ? 0.8786 1.0145 0.9800 0.0125  0.1381  -0.0001 276 GLU B CB  
3074 C CG  . GLU B 276 ? 1.0466 1.1589 1.1257 0.0124  0.1512  -0.0064 276 GLU B CG  
3075 C CD  . GLU B 276 ? 1.1370 1.2222 1.1842 0.0024  0.1445  -0.0138 276 GLU B CD  
3076 O OE1 . GLU B 276 ? 1.1068 1.1637 1.1309 0.0063  0.1434  -0.0201 276 GLU B OE1 
3077 O OE2 . GLU B 276 ? 1.2611 1.3528 1.3053 -0.0096 0.1411  -0.0128 276 GLU B OE2 
3078 N N   . LEU B 277 ? 0.8166 0.8855 0.8741 0.0288  0.1295  -0.0149 277 LEU B N   
3079 C CA  . LEU B 277 ? 0.8630 0.9047 0.8939 0.0258  0.1207  -0.0222 277 LEU B CA  
3080 C C   . LEU B 277 ? 0.8448 0.8671 0.8497 0.0190  0.1252  -0.0276 277 LEU B C   
3081 O O   . LEU B 277 ? 0.9155 0.9315 0.9151 0.0214  0.1389  -0.0291 277 LEU B O   
3082 C CB  . LEU B 277 ? 0.8423 0.8662 0.8665 0.0352  0.1234  -0.0256 277 LEU B CB  
3083 C CG  . LEU B 277 ? 0.7571 0.7935 0.8012 0.0419  0.1171  -0.0209 277 LEU B CG  
3084 C CD1 . LEU B 277 ? 0.7189 0.7318 0.7506 0.0494  0.1211  -0.0255 277 LEU B CD1 
3085 C CD2 . LEU B 277 ? 0.7248 0.7692 0.7708 0.0345  0.1002  -0.0197 277 LEU B CD2 
3086 N N   . GLY B 278 ? 0.8045 0.8174 0.7934 0.0110  0.1145  -0.0297 278 GLY B N   
3087 C CA  . GLY B 278 ? 0.7224 0.7149 0.6843 0.0055  0.1172  -0.0340 278 GLY B CA  
3088 C C   . GLY B 278 ? 0.6595 0.6278 0.5996 0.0095  0.1203  -0.0398 278 GLY B C   
3089 O O   . GLY B 278 ? 0.5950 0.5597 0.5390 0.0158  0.1199  -0.0413 278 GLY B O   
3090 N N   . ALA B 279 ? 0.7132 0.6637 0.6280 0.0047  0.1238  -0.0430 279 ALA B N   
3091 C CA  . ALA B 279 ? 0.7037 0.6307 0.5937 0.0057  0.1260  -0.0487 279 ALA B CA  
3092 C C   . ALA B 279 ? 0.6147 0.5353 0.4977 0.0057  0.1116  -0.0500 279 ALA B C   
3093 O O   . ALA B 279 ? 0.6529 0.5604 0.5252 0.0076  0.1123  -0.0542 279 ALA B O   
3094 C CB  . ALA B 279 ? 0.6710 0.5817 0.5340 -0.0005 0.1305  -0.0507 279 ALA B CB  
3095 N N   . ALA B 280 ? 0.5309 0.4601 0.4196 0.0030  0.0993  -0.0464 280 ALA B N   
3096 C CA  . ALA B 280 ? 0.5600 0.4855 0.4440 0.0032  0.0860  -0.0468 280 ALA B CA  
3097 C C   . ALA B 280 ? 0.5983 0.5303 0.4991 0.0087  0.0846  -0.0476 280 ALA B C   
3098 O O   . ALA B 280 ? 0.5520 0.4729 0.4423 0.0092  0.0812  -0.0510 280 ALA B O   
3099 C CB  . ALA B 280 ? 0.5357 0.4689 0.4242 0.0004  0.0759  -0.0423 280 ALA B CB  
3100 N N   . ALA B 281 ? 0.5676 0.5176 0.4938 0.0122  0.0869  -0.0439 281 ALA B N   
3101 C CA  . ALA B 281 ? 0.5609 0.5174 0.5036 0.0184  0.0860  -0.0434 281 ALA B CA  
3102 C C   . ALA B 281 ? 0.5070 0.4494 0.4420 0.0232  0.0978  -0.0475 281 ALA B C   
3103 O O   . ALA B 281 ? 0.5303 0.4637 0.4623 0.0259  0.0958  -0.0499 281 ALA B O   
3104 C CB  . ALA B 281 ? 0.5748 0.5554 0.5457 0.0208  0.0868  -0.0373 281 ALA B CB  
3105 N N   . ARG B 282 ? 0.5360 0.4742 0.4661 0.0239  0.1112  -0.0485 282 ARG B N   
3106 C CA  . ARG B 282 ? 0.6153 0.5368 0.5359 0.0286  0.1251  -0.0526 282 ARG B CA  
3107 C C   . ARG B 282 ? 0.6258 0.5214 0.5151 0.0231  0.1220  -0.0598 282 ARG B C   
3108 O O   . ARG B 282 ? 0.7110 0.5907 0.5919 0.0257  0.1279  -0.0638 282 ARG B O   
3109 C CB  . ARG B 282 ? 0.7256 0.6482 0.6466 0.0299  0.1408  -0.0521 282 ARG B CB  
3110 C CG  . ARG B 282 ? 0.7647 0.7161 0.7182 0.0346  0.1449  -0.0443 282 ARG B CG  
3111 C CD  . ARG B 282 ? 0.7857 0.7381 0.7435 0.0392  0.1641  -0.0434 282 ARG B CD  
3112 N NE  . ARG B 282 ? 0.9552 0.8984 0.8934 0.0313  0.1684  -0.0464 282 ARG B NE  
3113 C CZ  . ARG B 282 ? 1.0001 0.9606 0.9477 0.0258  0.1673  -0.0424 282 ARG B CZ  
3114 N NH1 . ARG B 282 ? 0.9864 0.9754 0.9624 0.0260  0.1613  -0.0354 282 ARG B NH1 
3115 N NH2 . ARG B 282 ? 1.1006 1.0486 1.0270 0.0189  0.1723  -0.0454 282 ARG B NH2 
3116 N N   . PHE B 283 ? 0.6064 0.4971 0.4773 0.0149  0.1129  -0.0609 283 PHE B N   
3117 C CA  . PHE B 283 ? 0.6132 0.4840 0.4551 0.0081  0.1073  -0.0662 283 PHE B CA  
3118 C C   . PHE B 283 ? 0.6405 0.5117 0.4868 0.0084  0.0969  -0.0669 283 PHE B C   
3119 O O   . PHE B 283 ? 0.6993 0.5527 0.5284 0.0056  0.0992  -0.0724 283 PHE B O   
3120 C CB  . PHE B 283 ? 0.5686 0.4395 0.3947 0.0008  0.0979  -0.0644 283 PHE B CB  
3121 C CG  . PHE B 283 ? 0.6675 0.5264 0.4693 -0.0064 0.0874  -0.0671 283 PHE B CG  
3122 C CD1 . PHE B 283 ? 0.7196 0.5577 0.4915 -0.0128 0.0933  -0.0727 283 PHE B CD1 
3123 C CD2 . PHE B 283 ? 0.5750 0.4443 0.3836 -0.0075 0.0719  -0.0638 283 PHE B CD2 
3124 C CE1 . PHE B 283 ? 0.8016 0.6315 0.5510 -0.0212 0.0827  -0.0745 283 PHE B CE1 
3125 C CE2 . PHE B 283 ? 0.6767 0.5391 0.4653 -0.0145 0.0618  -0.0651 283 PHE B CE2 
3126 C CZ  . PHE B 283 ? 0.8305 0.6743 0.5897 -0.0219 0.0666  -0.0703 283 PHE B CZ  
3127 N N   . LEU B 284 ? 0.6075 0.4976 0.4752 0.0107  0.0858  -0.0618 284 LEU B N   
3128 C CA  . LEU B 284 ? 0.5981 0.4900 0.4711 0.0108  0.0757  -0.0620 284 LEU B CA  
3129 C C   . LEU B 284 ? 0.6229 0.5067 0.5019 0.0164  0.0851  -0.0645 284 LEU B C   
3130 O O   . LEU B 284 ? 0.6212 0.4923 0.4887 0.0135  0.0824  -0.0685 284 LEU B O   
3131 C CB  . LEU B 284 ? 0.4728 0.3857 0.3681 0.0128  0.0649  -0.0558 284 LEU B CB  
3132 C CG  . LEU B 284 ? 0.5897 0.5066 0.4922 0.0129  0.0541  -0.0552 284 LEU B CG  
3133 C CD1 . LEU B 284 ? 0.6025 0.5089 0.4833 0.0057  0.0458  -0.0583 284 LEU B CD1 
3134 C CD2 . LEU B 284 ? 0.4473 0.3828 0.3695 0.0145  0.0456  -0.0494 284 LEU B CD2 
3135 N N   . ILE B 285 ? 0.6222 0.5134 0.5193 0.0245  0.0966  -0.0616 285 ILE B N   
3136 C CA  . ILE B 285 ? 0.6154 0.4991 0.5200 0.0323  0.1071  -0.0622 285 ILE B CA  
3137 C C   . ILE B 285 ? 0.6730 0.5268 0.5491 0.0294  0.1190  -0.0700 285 ILE B C   
3138 O O   . ILE B 285 ? 0.7158 0.5530 0.5831 0.0297  0.1219  -0.0737 285 ILE B O   
3139 C CB  . ILE B 285 ? 0.6072 0.5090 0.5390 0.0422  0.1170  -0.0556 285 ILE B CB  
3140 C CG1 . ILE B 285 ? 0.6321 0.5610 0.5905 0.0439  0.1047  -0.0483 285 ILE B CG1 
3141 C CG2 . ILE B 285 ? 0.5690 0.4587 0.5047 0.0521  0.1326  -0.0557 285 ILE B CG2 
3142 C CD1 . ILE B 285 ? 0.5586 0.5116 0.5423 0.0491  0.1103  -0.0410 285 ILE B CD1 
3143 N N   . ASP B 286 ? 0.6473 0.4920 0.5065 0.0257  0.1269  -0.0729 286 ASP B N   
3144 C CA  . ASP B 286 ? 0.7523 0.5664 0.5797 0.0207  0.1382  -0.0811 286 ASP B CA  
3145 C C   . ASP B 286 ? 0.7784 0.5790 0.5811 0.0090  0.1258  -0.0864 286 ASP B C   
3146 O O   . ASP B 286 ? 0.8580 0.6346 0.6412 0.0056  0.1324  -0.0927 286 ASP B O   
3147 C CB  . ASP B 286 ? 0.8119 0.6200 0.6241 0.0173  0.1471  -0.0828 286 ASP B CB  
3148 C CG  . ASP B 286 ? 0.9423 0.7599 0.7755 0.0282  0.1634  -0.0786 286 ASP B CG  
3149 O OD1 . ASP B 286 ? 0.9661 0.7976 0.8271 0.0387  0.1666  -0.0732 286 ASP B OD1 
3150 O OD2 . ASP B 286 ? 1.0530 0.8655 0.8754 0.0262  0.1731  -0.0799 286 ASP B OD2 
3151 N N   . TYR B 287 ? 0.7487 0.5645 0.5519 0.0025  0.1084  -0.0836 287 TYR B N   
3152 C CA  . TYR B 287 ? 0.7078 0.5164 0.4905 -0.0088 0.0955  -0.0869 287 TYR B CA  
3153 C C   . TYR B 287 ? 0.7962 0.6006 0.5851 -0.0079 0.0927  -0.0885 287 TYR B C   
3154 O O   . TYR B 287 ? 0.8399 0.6252 0.6051 -0.0171 0.0926  -0.0947 287 TYR B O   
3155 C CB  . TYR B 287 ? 0.6647 0.4944 0.4542 -0.0121 0.0783  -0.0811 287 TYR B CB  
3156 C CG  . TYR B 287 ? 0.7603 0.5872 0.5292 -0.0237 0.0647  -0.0826 287 TYR B CG  
3157 C CD1 . TYR B 287 ? 0.7271 0.5612 0.5039 -0.0259 0.0537  -0.0818 287 TYR B CD1 
3158 C CD2 . TYR B 287 ? 0.8594 0.6787 0.6017 -0.0327 0.0624  -0.0839 287 TYR B CD2 
3159 C CE1 . TYR B 287 ? 0.7407 0.5764 0.5011 -0.0369 0.0409  -0.0821 287 TYR B CE1 
3160 C CE2 . TYR B 287 ? 0.8247 0.6456 0.5498 -0.0436 0.0489  -0.0837 287 TYR B CE2 
3161 C CZ  . TYR B 287 ? 0.8673 0.6975 0.6024 -0.0457 0.0381  -0.0826 287 TYR B CZ  
3162 O OH  . TYR B 287 ? 1.0355 0.8711 0.7557 -0.0570 0.0245  -0.0814 287 TYR B OH  
3163 N N   . ILE B 288 ? 0.7904 0.6123 0.6098 0.0019  0.0904  -0.0829 288 ILE B N   
3164 C CA  . ILE B 288 ? 0.7216 0.5403 0.5480 0.0032  0.0874  -0.0835 288 ILE B CA  
3165 C C   . ILE B 288 ? 0.8028 0.5945 0.6167 0.0063  0.1049  -0.0888 288 ILE B C   
3166 O O   . ILE B 288 ? 0.8322 0.6039 0.6260 -0.0015 0.1053  -0.0947 288 ILE B O   
3167 C CB  . ILE B 288 ? 0.7012 0.5450 0.5618 0.0128  0.0810  -0.0756 288 ILE B CB  
3168 C CG1 . ILE B 288 ? 0.6437 0.5068 0.5107 0.0074  0.0629  -0.0719 288 ILE B CG1 
3169 C CG2 . ILE B 288 ? 0.7140 0.5510 0.5835 0.0181  0.0847  -0.0754 288 ILE B CG2 
3170 C CD1 . ILE B 288 ? 0.6317 0.5188 0.5243 0.0140  0.0586  -0.0646 288 ILE B CD1 
3171 N N   . ARG B 289 ? 0.7760 0.5666 0.6015 0.0174  0.1204  -0.0865 289 ARG B N   
3172 C CA  . ARG B 289 ? 0.8601 0.6230 0.6735 0.0225  0.1402  -0.0908 289 ARG B CA  
3173 C C   . ARG B 289 ? 0.9516 0.6821 0.7236 0.0090  0.1458  -0.1011 289 ARG B C   
3174 O O   . ARG B 289 ? 1.0014 0.7047 0.7553 0.0062  0.1545  -0.1068 289 ARG B O   
3175 C CB  . ARG B 289 ? 0.7565 0.5254 0.5860 0.0352  0.1563  -0.0863 289 ARG B CB  
3176 C CG  . ARG B 289 ? 0.7121 0.5080 0.5806 0.0493  0.1557  -0.0760 289 ARG B CG  
3177 C CD  . ARG B 289 ? 0.7131 0.5207 0.5979 0.0592  0.1694  -0.0709 289 ARG B CD  
3178 N NE  . ARG B 289 ? 0.7565 0.5898 0.6780 0.0728  0.1707  -0.0603 289 ARG B NE  
3179 C CZ  . ARG B 289 ? 0.7857 0.6401 0.7300 0.0813  0.1788  -0.0531 289 ARG B CZ  
3180 N NH1 . ARG B 289 ? 0.8212 0.6732 0.7559 0.0782  0.1869  -0.0557 289 ARG B NH1 
3181 N NH2 . ARG B 289 ? 0.8592 0.7388 0.8365 0.0926  0.1785  -0.0426 289 ARG B NH2 
3182 N N   . ASN B 290 ? 0.9753 0.7072 0.7301 -0.0004 0.1409  -0.1035 290 ASN B N   
3183 C CA  . ASN B 290 ? 1.0012 0.7041 0.7145 -0.0152 0.1449  -0.1129 290 ASN B CA  
3184 C C   . ASN B 290 ? 1.0171 0.7145 0.7149 -0.0287 0.1310  -0.1167 290 ASN B C   
3185 O O   . ASN B 290 ? 1.1328 0.8076 0.8066 -0.0389 0.1351  -0.1215 290 ASN B O   
3186 C CB  . ASN B 290 ? 0.9812 0.6917 0.6825 -0.0216 0.1403  -0.1125 290 ASN B CB  
3187 C CG  . ASN B 290 ? 1.1316 0.8191 0.7946 -0.0374 0.1416  -0.1187 290 ASN B CG  
3188 O OD1 . ASN B 290 ? 1.1285 0.8096 0.7744 -0.0504 0.1313  -0.1216 290 ASN B OD1 
3189 N ND2 . ASN B 290 ? 1.1867 0.8664 0.8408 -0.0367 0.1528  -0.1186 290 ASN B ND2 
3190 N N   . LYS B 291 ? 1.0604 0.7861 0.7796 -0.0289 0.1118  -0.1107 291 LYS B N   
3191 C CA  . LYS B 291 ? 1.0593 0.7844 0.7687 -0.0408 0.0984  -0.1130 291 LYS B CA  
3192 C C   . LYS B 291 ? 1.1803 0.8858 0.8894 -0.0381 0.1078  -0.1164 291 LYS B C   
3193 O O   . LYS B 291 ? 1.3095 0.9945 0.9927 -0.0516 0.1075  -0.1231 291 LYS B O   
3194 C CB  . LYS B 291 ? 1.0686 0.8287 0.8043 -0.0391 0.0782  -0.1048 291 LYS B CB  
3195 C CG  . LYS B 291 ? 1.1149 0.8916 0.8449 -0.0451 0.0661  -0.1014 291 LYS B CG  
3196 C CD  . LYS B 291 ? 1.1097 0.8717 0.8030 -0.0629 0.0619  -0.1073 291 LYS B CD  
3197 C CE  . LYS B 291 ? 1.1233 0.8883 0.8028 -0.0659 0.0609  -0.1056 291 LYS B CE  
3198 N NZ  . LYS B 291 ? 1.1651 0.9083 0.8036 -0.0828 0.0626  -0.1127 291 LYS B NZ  
3199 N N   . ARG B 292 ? 1.1448 0.8566 0.8820 -0.0214 0.1160  -0.1111 292 ARG B N   
3200 C CA  . ARG B 292 ? 1.1979 0.8935 0.9383 -0.0165 0.1242  -0.1121 292 ARG B CA  
3201 C C   . ARG B 292 ? 1.3245 0.9851 1.0383 -0.0206 0.1415  -0.1178 292 ARG B C   
3202 O O   . ARG B 292 ? 1.4275 1.0734 1.1416 -0.0183 0.1482  -0.1172 292 ARG B O   
3203 C CB  . ARG B 292 ? 1.1494 0.8632 0.9272 0.0032  0.1289  -0.1029 292 ARG B CB  
3204 C CG  . ARG B 292 ? 1.1719 0.9250 0.9800 0.0071  0.1115  -0.0945 292 ARG B CG  
3205 C CD  . ARG B 292 ? 1.1420 0.9120 0.9820 0.0198  0.1095  -0.0864 292 ARG B CD  
3206 N NE  . ARG B 292 ? 1.2373 1.0046 1.0754 0.0137  0.0999  -0.0875 292 ARG B NE  
3207 C CZ  . ARG B 292 ? 1.2062 0.9899 1.0456 0.0040  0.0821  -0.0871 292 ARG B CZ  
3208 N NH1 . ARG B 292 ? 1.1537 0.9569 0.9963 0.0001  0.0716  -0.0852 292 ARG B NH1 
3209 N NH2 . ARG B 292 ? 1.1433 0.9234 0.9812 -0.0013 0.0757  -0.0881 292 ARG B NH2 
3210 N N   . MET B 293 ? 1.3340 0.9859 1.0290 -0.0268 0.1470  -0.1202 293 MET B N   
3211 C CA  . MET B 293 ? 1.3629 0.9862 1.0332 -0.0341 0.1598  -0.1233 293 MET B CA  
3212 C C   . MET B 293 ? 1.3652 0.9833 1.0059 -0.0528 0.1525  -0.1280 293 MET B C   
3213 O O   . MET B 293 ? 1.2782 0.9005 0.9057 -0.0682 0.1378  -0.1305 293 MET B O   
3214 C CB  . MET B 293 ? 1.4219 1.0354 1.1017 -0.0187 0.1804  -0.1195 293 MET B CB  
3215 C CG  . MET B 293 ? 1.4716 1.1070 1.1715 -0.0074 0.1814  -0.1156 293 MET B CG  
3216 S SD  . MET B 293 ? 1.6935 1.3251 1.4140 0.0131  0.2045  -0.1086 293 MET B SD  
3217 C CE  . MET B 293 ? 1.4718 1.1259 1.2027 0.0168  0.2035  -0.1068 293 MET B CE  
# 
