data_8ZC7
# 
_entry.id   8ZC7 
# 
_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   8ZC7         pdb_00008zc7 10.2210/pdb8zc7/pdb 
WWPDB D_1300047417 ?            ?                   
# 
_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       2024-11-27 
# 
_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                        8ZC7 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-28 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              fangpengfei@sioc.ac.cn 
_pdbx_contact_author.name_first         pengfei 
_pdbx_contact_author.name_last          fang 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3448-5494 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Xia, M.'  1 ? 
'Dong, D.' 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                     
'Crystallographic analysis of MitM, which catalyzes the post-mitosane modification in mitomycin biosynthesis' 
_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 'Xia, M.'  1 ? 
primary 'Dong, D.' 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 MitM  31914.092 2  ? ? ? 
'The sequence of organism Streptomyces caespitosus is not available, replaced by Q9X5Q9 temporarily.' 
2 water   nat water 18.015    35 ? ? ? ? 
# 
_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       
;MPHSELSELPMPSPASEEVGALYDRFTALGAASLGENLHFGYWDSPDSQVPLAEATDRLTDMMAERLRIGAGSRVLDLGC
GVGTPGVRIARLSGAHVTGISVSHEQVVRANALAEEAGLADRARFQRADAMDLPFEDESFDAVIALESIIHMPDRAQVLA
QVGRVLRPGGRLVLTDFFERAPLAPEGRAAVQRYLHDFMMTMVSAEAYPPLLRGAGLWLEEFLDISDQTLEKTFRLLSER
INSSKQRLETQFGEEMVNQFDPGDLVGVKEFGYLLLVAQRPGKHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MPHSELSELPMPSPASEEVGALYDRFTALGAASLGENLHFGYWDSPDSQVPLAEATDRLTDMMAERLRIGAGSRVLDLGC
GVGTPGVRIARLSGAHVTGISVSHEQVVRANALAEEAGLADRARFQRADAMDLPFEDESFDAVIALESIIHMPDRAQVLA
QVGRVLRPGGRLVLTDFFERAPLAPEGRAAVQRYLHDFMMTMVSAEAYPPLLRGAGLWLEEFLDISDQTLEKTFRLLSER
INSSKQRLETQFGEEMVNQFDPGDLVGVKEFGYLLLVAQRPGKHHHHHH
;
_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   PRO n 
1 3   HIS n 
1 4   SER n 
1 5   GLU n 
1 6   LEU n 
1 7   SER n 
1 8   GLU n 
1 9   LEU n 
1 10  PRO n 
1 11  MET n 
1 12  PRO n 
1 13  SER n 
1 14  PRO n 
1 15  ALA n 
1 16  SER n 
1 17  GLU n 
1 18  GLU n 
1 19  VAL n 
1 20  GLY n 
1 21  ALA n 
1 22  LEU n 
1 23  TYR n 
1 24  ASP n 
1 25  ARG n 
1 26  PHE n 
1 27  THR n 
1 28  ALA n 
1 29  LEU n 
1 30  GLY n 
1 31  ALA n 
1 32  ALA n 
1 33  SER n 
1 34  LEU n 
1 35  GLY n 
1 36  GLU n 
1 37  ASN n 
1 38  LEU n 
1 39  HIS n 
1 40  PHE n 
1 41  GLY n 
1 42  TYR n 
1 43  TRP n 
1 44  ASP n 
1 45  SER n 
1 46  PRO n 
1 47  ASP n 
1 48  SER n 
1 49  GLN n 
1 50  VAL n 
1 51  PRO n 
1 52  LEU n 
1 53  ALA n 
1 54  GLU n 
1 55  ALA n 
1 56  THR n 
1 57  ASP n 
1 58  ARG n 
1 59  LEU n 
1 60  THR n 
1 61  ASP n 
1 62  MET n 
1 63  MET n 
1 64  ALA n 
1 65  GLU n 
1 66  ARG n 
1 67  LEU n 
1 68  ARG n 
1 69  ILE n 
1 70  GLY n 
1 71  ALA n 
1 72  GLY n 
1 73  SER n 
1 74  ARG n 
1 75  VAL n 
1 76  LEU n 
1 77  ASP n 
1 78  LEU n 
1 79  GLY n 
1 80  CYS n 
1 81  GLY n 
1 82  VAL n 
1 83  GLY n 
1 84  THR n 
1 85  PRO n 
1 86  GLY n 
1 87  VAL n 
1 88  ARG n 
1 89  ILE n 
1 90  ALA n 
1 91  ARG n 
1 92  LEU n 
1 93  SER n 
1 94  GLY n 
1 95  ALA n 
1 96  HIS n 
1 97  VAL n 
1 98  THR n 
1 99  GLY n 
1 100 ILE n 
1 101 SER n 
1 102 VAL n 
1 103 SER n 
1 104 HIS n 
1 105 GLU n 
1 106 GLN n 
1 107 VAL n 
1 108 VAL n 
1 109 ARG n 
1 110 ALA n 
1 111 ASN n 
1 112 ALA n 
1 113 LEU n 
1 114 ALA n 
1 115 GLU n 
1 116 GLU n 
1 117 ALA n 
1 118 GLY n 
1 119 LEU n 
1 120 ALA n 
1 121 ASP n 
1 122 ARG n 
1 123 ALA n 
1 124 ARG n 
1 125 PHE n 
1 126 GLN n 
1 127 ARG n 
1 128 ALA n 
1 129 ASP n 
1 130 ALA n 
1 131 MET n 
1 132 ASP n 
1 133 LEU n 
1 134 PRO n 
1 135 PHE n 
1 136 GLU n 
1 137 ASP n 
1 138 GLU n 
1 139 SER n 
1 140 PHE n 
1 141 ASP n 
1 142 ALA n 
1 143 VAL n 
1 144 ILE n 
1 145 ALA n 
1 146 LEU n 
1 147 GLU n 
1 148 SER n 
1 149 ILE n 
1 150 ILE n 
1 151 HIS n 
1 152 MET n 
1 153 PRO n 
1 154 ASP n 
1 155 ARG n 
1 156 ALA n 
1 157 GLN n 
1 158 VAL n 
1 159 LEU n 
1 160 ALA n 
1 161 GLN n 
1 162 VAL n 
1 163 GLY n 
1 164 ARG n 
1 165 VAL n 
1 166 LEU n 
1 167 ARG n 
1 168 PRO n 
1 169 GLY n 
1 170 GLY n 
1 171 ARG n 
1 172 LEU n 
1 173 VAL n 
1 174 LEU n 
1 175 THR n 
1 176 ASP n 
1 177 PHE n 
1 178 PHE n 
1 179 GLU n 
1 180 ARG n 
1 181 ALA n 
1 182 PRO n 
1 183 LEU n 
1 184 ALA n 
1 185 PRO n 
1 186 GLU n 
1 187 GLY n 
1 188 ARG n 
1 189 ALA n 
1 190 ALA n 
1 191 VAL n 
1 192 GLN n 
1 193 ARG n 
1 194 TYR n 
1 195 LEU n 
1 196 HIS n 
1 197 ASP n 
1 198 PHE n 
1 199 MET n 
1 200 MET n 
1 201 THR n 
1 202 MET n 
1 203 VAL n 
1 204 SER n 
1 205 ALA n 
1 206 GLU n 
1 207 ALA n 
1 208 TYR n 
1 209 PRO n 
1 210 PRO n 
1 211 LEU n 
1 212 LEU n 
1 213 ARG n 
1 214 GLY n 
1 215 ALA n 
1 216 GLY n 
1 217 LEU n 
1 218 TRP n 
1 219 LEU n 
1 220 GLU n 
1 221 GLU n 
1 222 PHE n 
1 223 LEU n 
1 224 ASP n 
1 225 ILE n 
1 226 SER n 
1 227 ASP n 
1 228 GLN n 
1 229 THR n 
1 230 LEU n 
1 231 GLU n 
1 232 LYS n 
1 233 THR n 
1 234 PHE n 
1 235 ARG n 
1 236 LEU n 
1 237 LEU n 
1 238 SER n 
1 239 GLU n 
1 240 ARG n 
1 241 ILE n 
1 242 ASN n 
1 243 SER n 
1 244 SER n 
1 245 LYS n 
1 246 GLN n 
1 247 ARG n 
1 248 LEU n 
1 249 GLU n 
1 250 THR n 
1 251 GLN n 
1 252 PHE n 
1 253 GLY n 
1 254 GLU n 
1 255 GLU n 
1 256 MET n 
1 257 VAL n 
1 258 ASN n 
1 259 GLN n 
1 260 PHE n 
1 261 ASP n 
1 262 PRO n 
1 263 GLY n 
1 264 ASP n 
1 265 LEU n 
1 266 VAL n 
1 267 GLY n 
1 268 VAL n 
1 269 LYS n 
1 270 GLU n 
1 271 PHE n 
1 272 GLY n 
1 273 TYR n 
1 274 LEU n 
1 275 LEU n 
1 276 LEU n 
1 277 VAL n 
1 278 ALA n 
1 279 GLN n 
1 280 ARG n 
1 281 PRO n 
1 282 GLY n 
1 283 LYS n 
1 284 HIS n 
1 285 HIS n 
1 286 HIS n 
1 287 HIS n 
1 288 HIS n 
1 289 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   289 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 mitM 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    'ATCC 27422' 
_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      'Streptomyces caespitosus' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     53502 
_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     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
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   PRO 2   2   ?   ?   ?   A . n 
A 1 3   HIS 3   3   ?   ?   ?   A . n 
A 1 4   SER 4   4   ?   ?   ?   A . n 
A 1 5   GLU 5   5   ?   ?   ?   A . n 
A 1 6   LEU 6   6   6   LEU LEU A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLU 8   8   8   GLU GLU A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  PRO 10  10  10  PRO PRO A . n 
A 1 11  MET 11  11  11  MET MET A . n 
A 1 12  PRO 12  12  12  PRO PRO A . n 
A 1 13  SER 13  13  13  SER SER A . n 
A 1 14  PRO 14  14  14  PRO PRO A . n 
A 1 15  ALA 15  15  15  ALA ALA A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  GLU 17  17  17  GLU GLU A . n 
A 1 18  GLU 18  18  18  GLU GLU A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  GLY 20  20  20  GLY GLY A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  LEU 22  22  22  LEU LEU A . n 
A 1 23  TYR 23  23  23  TYR TYR A . n 
A 1 24  ASP 24  24  24  ASP ASP A . n 
A 1 25  ARG 25  25  25  ARG ARG A . n 
A 1 26  PHE 26  26  26  PHE PHE A . n 
A 1 27  THR 27  27  27  THR THR A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLY 30  30  30  GLY GLY A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  ALA 32  32  32  ALA ALA A . n 
A 1 33  SER 33  33  33  SER SER A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  GLY 35  35  35  GLY GLY A . n 
A 1 36  GLU 36  36  36  GLU GLU A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  HIS 39  39  39  HIS HIS A . n 
A 1 40  PHE 40  40  40  PHE PHE A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  TRP 43  43  43  TRP TRP A . n 
A 1 44  ASP 44  44  44  ASP ASP A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  PRO 46  46  46  PRO PRO A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  SER 48  48  48  SER SER A . n 
A 1 49  GLN 49  49  49  GLN GLN A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  PRO 51  51  51  PRO PRO A . n 
A 1 52  LEU 52  52  52  LEU LEU A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  THR 56  56  56  THR THR A . n 
A 1 57  ASP 57  57  57  ASP ASP A . n 
A 1 58  ARG 58  58  58  ARG ARG A . n 
A 1 59  LEU 59  59  59  LEU LEU A . n 
A 1 60  THR 60  60  60  THR THR A . n 
A 1 61  ASP 61  61  61  ASP ASP A . n 
A 1 62  MET 62  62  62  MET MET A . n 
A 1 63  MET 63  63  63  MET MET A . n 
A 1 64  ALA 64  64  64  ALA ALA A . n 
A 1 65  GLU 65  65  65  GLU GLU A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  GLY 70  70  70  GLY GLY A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  SER 73  73  73  SER SER A . n 
A 1 74  ARG 74  74  74  ARG ARG A . n 
A 1 75  VAL 75  75  75  VAL VAL A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  ASP 77  77  77  ASP ASP A . n 
A 1 78  LEU 78  78  78  LEU LEU A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  CYS 80  80  80  CYS CYS A . n 
A 1 81  GLY 81  81  81  GLY GLY A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  GLY 83  83  83  GLY GLY A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  PRO 85  85  85  PRO PRO A . n 
A 1 86  GLY 86  86  86  GLY GLY A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  ARG 88  88  88  ARG ARG A . n 
A 1 89  ILE 89  89  89  ILE ILE A . n 
A 1 90  ALA 90  90  90  ALA ALA A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  LEU 92  92  92  LEU LEU A . n 
A 1 93  SER 93  93  93  SER SER A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  HIS 96  96  96  HIS HIS A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  THR 98  98  98  THR THR A . n 
A 1 99  GLY 99  99  99  GLY GLY A . n 
A 1 100 ILE 100 100 100 ILE ILE A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 VAL 102 102 102 VAL VAL A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 HIS 104 104 104 HIS HIS A . n 
A 1 105 GLU 105 105 105 GLU GLU A . n 
A 1 106 GLN 106 106 106 GLN GLN A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 VAL 108 108 108 VAL VAL A . n 
A 1 109 ARG 109 109 109 ARG ARG A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ASN 111 111 111 ASN ASN A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 LEU 119 119 119 LEU LEU A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 ASP 121 121 121 ASP ASP A . n 
A 1 122 ARG 122 122 122 ARG ARG A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ARG 124 124 124 ARG ARG A . n 
A 1 125 PHE 125 125 125 PHE PHE A . n 
A 1 126 GLN 126 126 126 GLN GLN A . n 
A 1 127 ARG 127 127 127 ARG ARG A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 ASP 129 129 129 ASP ASP A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 MET 131 131 131 MET MET A . n 
A 1 132 ASP 132 132 132 ASP ASP A . n 
A 1 133 LEU 133 133 133 LEU LEU A . n 
A 1 134 PRO 134 134 134 PRO PRO A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 GLU 136 136 136 GLU GLU A . n 
A 1 137 ASP 137 137 137 ASP ASP A . n 
A 1 138 GLU 138 138 138 GLU GLU A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 PHE 140 140 140 PHE PHE A . n 
A 1 141 ASP 141 141 141 ASP ASP A . n 
A 1 142 ALA 142 142 142 ALA ALA A . n 
A 1 143 VAL 143 143 143 VAL VAL A . n 
A 1 144 ILE 144 144 144 ILE ILE A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 LEU 146 146 146 LEU LEU A . n 
A 1 147 GLU 147 147 147 GLU GLU A . n 
A 1 148 SER 148 148 148 SER SER A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 ILE 150 150 150 ILE ILE A . n 
A 1 151 HIS 151 151 151 HIS HIS A . n 
A 1 152 MET 152 152 152 MET MET A . n 
A 1 153 PRO 153 153 153 PRO PRO A . n 
A 1 154 ASP 154 154 154 ASP ASP A . n 
A 1 155 ARG 155 155 155 ARG ARG A . n 
A 1 156 ALA 156 156 156 ALA ALA A . n 
A 1 157 GLN 157 157 157 GLN GLN A . n 
A 1 158 VAL 158 158 158 VAL VAL A . n 
A 1 159 LEU 159 159 159 LEU LEU A . n 
A 1 160 ALA 160 160 160 ALA ALA A . n 
A 1 161 GLN 161 161 161 GLN GLN A . n 
A 1 162 VAL 162 162 162 VAL VAL A . n 
A 1 163 GLY 163 163 163 GLY GLY A . n 
A 1 164 ARG 164 164 164 ARG ARG A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 LEU 166 166 166 LEU LEU A . n 
A 1 167 ARG 167 167 167 ARG ARG A . n 
A 1 168 PRO 168 168 168 PRO PRO A . n 
A 1 169 GLY 169 169 169 GLY GLY A . n 
A 1 170 GLY 170 170 170 GLY GLY A . n 
A 1 171 ARG 171 171 171 ARG ARG A . n 
A 1 172 LEU 172 172 172 LEU LEU A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 LEU 174 174 174 LEU LEU A . n 
A 1 175 THR 175 175 175 THR THR A . n 
A 1 176 ASP 176 176 176 ASP ASP A . n 
A 1 177 PHE 177 177 177 PHE PHE A . n 
A 1 178 PHE 178 178 178 PHE PHE A . n 
A 1 179 GLU 179 179 179 GLU GLU A . n 
A 1 180 ARG 180 180 180 ARG ARG A . n 
A 1 181 ALA 181 181 181 ALA ALA A . n 
A 1 182 PRO 182 182 182 PRO PRO A . n 
A 1 183 LEU 183 183 183 LEU LEU A . n 
A 1 184 ALA 184 184 184 ALA ALA A . n 
A 1 185 PRO 185 185 185 PRO PRO A . n 
A 1 186 GLU 186 186 186 GLU GLU A . n 
A 1 187 GLY 187 187 187 GLY GLY A . n 
A 1 188 ARG 188 188 188 ARG ARG A . n 
A 1 189 ALA 189 189 189 ALA ALA A . n 
A 1 190 ALA 190 190 190 ALA ALA A . n 
A 1 191 VAL 191 191 191 VAL VAL A . n 
A 1 192 GLN 192 192 192 GLN GLN A . n 
A 1 193 ARG 193 193 193 ARG ARG A . n 
A 1 194 TYR 194 194 194 TYR TYR A . n 
A 1 195 LEU 195 195 195 LEU LEU A . n 
A 1 196 HIS 196 196 196 HIS HIS A . n 
A 1 197 ASP 197 197 197 ASP ASP A . n 
A 1 198 PHE 198 198 198 PHE PHE A . n 
A 1 199 MET 199 199 199 MET MET A . n 
A 1 200 MET 200 200 200 MET MET A . n 
A 1 201 THR 201 201 201 THR THR A . n 
A 1 202 MET 202 202 202 MET MET A . n 
A 1 203 VAL 203 203 203 VAL VAL A . n 
A 1 204 SER 204 204 204 SER SER A . n 
A 1 205 ALA 205 205 205 ALA ALA A . n 
A 1 206 GLU 206 206 206 GLU GLU A . n 
A 1 207 ALA 207 207 207 ALA ALA A . n 
A 1 208 TYR 208 208 208 TYR TYR A . n 
A 1 209 PRO 209 209 209 PRO PRO A . n 
A 1 210 PRO 210 210 210 PRO PRO A . n 
A 1 211 LEU 211 211 211 LEU LEU A . n 
A 1 212 LEU 212 212 212 LEU LEU A . n 
A 1 213 ARG 213 213 213 ARG ARG A . n 
A 1 214 GLY 214 214 214 GLY GLY A . n 
A 1 215 ALA 215 215 215 ALA ALA A . n 
A 1 216 GLY 216 216 216 GLY GLY A . n 
A 1 217 LEU 217 217 217 LEU LEU A . n 
A 1 218 TRP 218 218 218 TRP TRP A . n 
A 1 219 LEU 219 219 219 LEU LEU A . n 
A 1 220 GLU 220 220 220 GLU GLU A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 PHE 222 222 222 PHE PHE A . n 
A 1 223 LEU 223 223 223 LEU LEU A . n 
A 1 224 ASP 224 224 224 ASP ASP A . n 
A 1 225 ILE 225 225 225 ILE ILE A . n 
A 1 226 SER 226 226 226 SER SER A . n 
A 1 227 ASP 227 227 227 ASP ASP A . n 
A 1 228 GLN 228 228 228 GLN GLN A . n 
A 1 229 THR 229 229 229 THR THR A . n 
A 1 230 LEU 230 230 230 LEU LEU A . n 
A 1 231 GLU 231 231 231 GLU GLU A . n 
A 1 232 LYS 232 232 232 LYS LYS A . n 
A 1 233 THR 233 233 233 THR THR A . n 
A 1 234 PHE 234 234 234 PHE PHE A . n 
A 1 235 ARG 235 235 235 ARG ARG A . n 
A 1 236 LEU 236 236 236 LEU LEU A . n 
A 1 237 LEU 237 237 237 LEU LEU A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 GLU 239 239 239 GLU GLU A . n 
A 1 240 ARG 240 240 240 ARG ARG A . n 
A 1 241 ILE 241 241 241 ILE ILE A . n 
A 1 242 ASN 242 242 242 ASN ASN A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 SER 244 244 244 SER SER A . n 
A 1 245 LYS 245 245 245 LYS LYS A . n 
A 1 246 GLN 246 246 ?   ?   ?   A . n 
A 1 247 ARG 247 247 ?   ?   ?   A . n 
A 1 248 LEU 248 248 ?   ?   ?   A . n 
A 1 249 GLU 249 249 ?   ?   ?   A . n 
A 1 250 THR 250 250 ?   ?   ?   A . n 
A 1 251 GLN 251 251 ?   ?   ?   A . n 
A 1 252 PHE 252 252 ?   ?   ?   A . n 
A 1 253 GLY 253 253 ?   ?   ?   A . n 
A 1 254 GLU 254 254 ?   ?   ?   A . n 
A 1 255 GLU 255 255 ?   ?   ?   A . n 
A 1 256 MET 256 256 ?   ?   ?   A . n 
A 1 257 VAL 257 257 257 VAL VAL A . n 
A 1 258 ASN 258 258 258 ASN ASN A . n 
A 1 259 GLN 259 259 259 GLN GLN A . n 
A 1 260 PHE 260 260 260 PHE PHE A . n 
A 1 261 ASP 261 261 261 ASP ASP A . n 
A 1 262 PRO 262 262 262 PRO PRO A . n 
A 1 263 GLY 263 263 263 GLY GLY A . n 
A 1 264 ASP 264 264 264 ASP ASP A . n 
A 1 265 LEU 265 265 265 LEU LEU A . n 
A 1 266 VAL 266 266 266 VAL VAL A . n 
A 1 267 GLY 267 267 267 GLY GLY A . n 
A 1 268 VAL 268 268 268 VAL VAL A . n 
A 1 269 LYS 269 269 269 LYS LYS A . n 
A 1 270 GLU 270 270 270 GLU GLU A . n 
A 1 271 PHE 271 271 271 PHE PHE A . n 
A 1 272 GLY 272 272 272 GLY GLY A . n 
A 1 273 TYR 273 273 273 TYR TYR A . n 
A 1 274 LEU 274 274 274 LEU LEU A . n 
A 1 275 LEU 275 275 275 LEU LEU A . n 
A 1 276 LEU 276 276 276 LEU LEU A . n 
A 1 277 VAL 277 277 277 VAL VAL A . n 
A 1 278 ALA 278 278 278 ALA ALA A . n 
A 1 279 GLN 279 279 279 GLN GLN A . n 
A 1 280 ARG 280 280 280 ARG ARG A . n 
A 1 281 PRO 281 281 281 PRO PRO A . n 
A 1 282 GLY 282 282 282 GLY GLY A . n 
A 1 283 LYS 283 283 ?   ?   ?   A . n 
A 1 284 HIS 284 284 ?   ?   ?   A . n 
A 1 285 HIS 285 285 ?   ?   ?   A . n 
A 1 286 HIS 286 286 ?   ?   ?   A . n 
A 1 287 HIS 287 287 ?   ?   ?   A . n 
A 1 288 HIS 288 288 ?   ?   ?   A . n 
A 1 289 HIS 289 289 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   PRO 2   2   ?   ?   ?   B . n 
B 1 3   HIS 3   3   ?   ?   ?   B . n 
B 1 4   SER 4   4   ?   ?   ?   B . n 
B 1 5   GLU 5   5   ?   ?   ?   B . n 
B 1 6   LEU 6   6   6   LEU LEU B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLU 8   8   8   GLU GLU B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  PRO 10  10  10  PRO PRO B . n 
B 1 11  MET 11  11  11  MET MET B . n 
B 1 12  PRO 12  12  12  PRO PRO B . n 
B 1 13  SER 13  13  13  SER SER B . n 
B 1 14  PRO 14  14  14  PRO PRO B . n 
B 1 15  ALA 15  15  15  ALA ALA B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  GLU 17  17  17  GLU GLU B . n 
B 1 18  GLU 18  18  18  GLU GLU B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  GLY 20  20  20  GLY GLY B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  LEU 22  22  22  LEU LEU B . n 
B 1 23  TYR 23  23  23  TYR TYR B . n 
B 1 24  ASP 24  24  24  ASP ASP B . n 
B 1 25  ARG 25  25  25  ARG ARG B . n 
B 1 26  PHE 26  26  26  PHE PHE B . n 
B 1 27  THR 27  27  27  THR THR B . n 
B 1 28  ALA 28  28  28  ALA ALA B . n 
B 1 29  LEU 29  29  29  LEU LEU B . n 
B 1 30  GLY 30  30  30  GLY GLY B . n 
B 1 31  ALA 31  31  31  ALA ALA B . n 
B 1 32  ALA 32  32  32  ALA ALA B . n 
B 1 33  SER 33  33  33  SER SER B . n 
B 1 34  LEU 34  34  34  LEU LEU B . n 
B 1 35  GLY 35  35  35  GLY GLY B . n 
B 1 36  GLU 36  36  36  GLU GLU B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  HIS 39  39  39  HIS HIS B . n 
B 1 40  PHE 40  40  40  PHE PHE B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  TRP 43  43  43  TRP TRP B . n 
B 1 44  ASP 44  44  44  ASP ASP B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  PRO 46  46  46  PRO PRO B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  SER 48  48  48  SER SER B . n 
B 1 49  GLN 49  49  49  GLN GLN B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  PRO 51  51  51  PRO PRO B . n 
B 1 52  LEU 52  52  52  LEU LEU B . n 
B 1 53  ALA 53  53  53  ALA ALA B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  THR 56  56  56  THR THR B . n 
B 1 57  ASP 57  57  57  ASP ASP B . n 
B 1 58  ARG 58  58  58  ARG ARG B . n 
B 1 59  LEU 59  59  59  LEU LEU B . n 
B 1 60  THR 60  60  60  THR THR B . n 
B 1 61  ASP 61  61  61  ASP ASP B . n 
B 1 62  MET 62  62  62  MET MET B . n 
B 1 63  MET 63  63  63  MET MET B . n 
B 1 64  ALA 64  64  64  ALA ALA B . n 
B 1 65  GLU 65  65  65  GLU GLU B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  GLY 70  70  70  GLY GLY B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  SER 73  73  73  SER SER B . n 
B 1 74  ARG 74  74  74  ARG ARG B . n 
B 1 75  VAL 75  75  75  VAL VAL B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  ASP 77  77  77  ASP ASP B . n 
B 1 78  LEU 78  78  78  LEU LEU B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  CYS 80  80  80  CYS CYS B . n 
B 1 81  GLY 81  81  81  GLY GLY B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  GLY 83  83  83  GLY GLY B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  PRO 85  85  85  PRO PRO B . n 
B 1 86  GLY 86  86  86  GLY GLY B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  ARG 88  88  88  ARG ARG B . n 
B 1 89  ILE 89  89  89  ILE ILE B . n 
B 1 90  ALA 90  90  90  ALA ALA B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  LEU 92  92  92  LEU LEU B . n 
B 1 93  SER 93  93  93  SER SER B . n 
B 1 94  GLY 94  94  94  GLY GLY B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  HIS 96  96  96  HIS HIS B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  THR 98  98  98  THR THR B . n 
B 1 99  GLY 99  99  99  GLY GLY B . n 
B 1 100 ILE 100 100 100 ILE ILE B . n 
B 1 101 SER 101 101 101 SER SER B . n 
B 1 102 VAL 102 102 102 VAL VAL B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 HIS 104 104 104 HIS HIS B . n 
B 1 105 GLU 105 105 105 GLU GLU B . n 
B 1 106 GLN 106 106 106 GLN GLN B . n 
B 1 107 VAL 107 107 107 VAL VAL B . n 
B 1 108 VAL 108 108 108 VAL VAL B . n 
B 1 109 ARG 109 109 109 ARG ARG B . n 
B 1 110 ALA 110 110 110 ALA ALA B . n 
B 1 111 ASN 111 111 111 ASN ASN B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 LEU 113 113 113 LEU LEU B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 GLU 116 116 116 GLU GLU B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 LEU 119 119 119 LEU LEU B . n 
B 1 120 ALA 120 120 120 ALA ALA B . n 
B 1 121 ASP 121 121 121 ASP ASP B . n 
B 1 122 ARG 122 122 122 ARG ARG B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ARG 124 124 124 ARG ARG B . n 
B 1 125 PHE 125 125 125 PHE PHE B . n 
B 1 126 GLN 126 126 126 GLN GLN B . n 
B 1 127 ARG 127 127 127 ARG ARG B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 ASP 129 129 129 ASP ASP B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 MET 131 131 131 MET MET B . n 
B 1 132 ASP 132 132 132 ASP ASP B . n 
B 1 133 LEU 133 133 133 LEU LEU B . n 
B 1 134 PRO 134 134 134 PRO PRO B . n 
B 1 135 PHE 135 135 135 PHE PHE B . n 
B 1 136 GLU 136 136 136 GLU GLU B . n 
B 1 137 ASP 137 137 137 ASP ASP B . n 
B 1 138 GLU 138 138 138 GLU GLU B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 PHE 140 140 140 PHE PHE B . n 
B 1 141 ASP 141 141 141 ASP ASP B . n 
B 1 142 ALA 142 142 142 ALA ALA B . n 
B 1 143 VAL 143 143 143 VAL VAL B . n 
B 1 144 ILE 144 144 144 ILE ILE B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 LEU 146 146 146 LEU LEU B . n 
B 1 147 GLU 147 147 147 GLU GLU B . n 
B 1 148 SER 148 148 148 SER SER B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 ILE 150 150 150 ILE ILE B . n 
B 1 151 HIS 151 151 151 HIS HIS B . n 
B 1 152 MET 152 152 152 MET MET B . n 
B 1 153 PRO 153 153 153 PRO PRO B . n 
B 1 154 ASP 154 154 154 ASP ASP B . n 
B 1 155 ARG 155 155 155 ARG ARG B . n 
B 1 156 ALA 156 156 156 ALA ALA B . n 
B 1 157 GLN 157 157 157 GLN GLN B . n 
B 1 158 VAL 158 158 158 VAL VAL B . n 
B 1 159 LEU 159 159 159 LEU LEU B . n 
B 1 160 ALA 160 160 160 ALA ALA B . n 
B 1 161 GLN 161 161 161 GLN GLN B . n 
B 1 162 VAL 162 162 162 VAL VAL B . n 
B 1 163 GLY 163 163 163 GLY GLY B . n 
B 1 164 ARG 164 164 164 ARG ARG B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 LEU 166 166 166 LEU LEU B . n 
B 1 167 ARG 167 167 167 ARG ARG B . n 
B 1 168 PRO 168 168 168 PRO PRO B . n 
B 1 169 GLY 169 169 169 GLY GLY B . n 
B 1 170 GLY 170 170 170 GLY GLY B . n 
B 1 171 ARG 171 171 171 ARG ARG B . n 
B 1 172 LEU 172 172 172 LEU LEU B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 LEU 174 174 174 LEU LEU B . n 
B 1 175 THR 175 175 175 THR THR B . n 
B 1 176 ASP 176 176 176 ASP ASP B . n 
B 1 177 PHE 177 177 177 PHE PHE B . n 
B 1 178 PHE 178 178 178 PHE PHE B . n 
B 1 179 GLU 179 179 179 GLU GLU B . n 
B 1 180 ARG 180 180 180 ARG ARG B . n 
B 1 181 ALA 181 181 181 ALA ALA B . n 
B 1 182 PRO 182 182 182 PRO PRO B . n 
B 1 183 LEU 183 183 183 LEU LEU B . n 
B 1 184 ALA 184 184 184 ALA ALA B . n 
B 1 185 PRO 185 185 185 PRO PRO B . n 
B 1 186 GLU 186 186 186 GLU GLU B . n 
B 1 187 GLY 187 187 187 GLY GLY B . n 
B 1 188 ARG 188 188 188 ARG ARG B . n 
B 1 189 ALA 189 189 189 ALA ALA B . n 
B 1 190 ALA 190 190 190 ALA ALA B . n 
B 1 191 VAL 191 191 191 VAL VAL B . n 
B 1 192 GLN 192 192 192 GLN GLN B . n 
B 1 193 ARG 193 193 193 ARG ARG B . n 
B 1 194 TYR 194 194 194 TYR TYR B . n 
B 1 195 LEU 195 195 195 LEU LEU B . n 
B 1 196 HIS 196 196 196 HIS HIS B . n 
B 1 197 ASP 197 197 197 ASP ASP B . n 
B 1 198 PHE 198 198 198 PHE PHE B . n 
B 1 199 MET 199 199 199 MET MET B . n 
B 1 200 MET 200 200 200 MET MET B . n 
B 1 201 THR 201 201 201 THR THR B . n 
B 1 202 MET 202 202 202 MET MET B . n 
B 1 203 VAL 203 203 203 VAL VAL B . n 
B 1 204 SER 204 204 204 SER SER B . n 
B 1 205 ALA 205 205 205 ALA ALA B . n 
B 1 206 GLU 206 206 206 GLU GLU B . n 
B 1 207 ALA 207 207 207 ALA ALA B . n 
B 1 208 TYR 208 208 208 TYR TYR B . n 
B 1 209 PRO 209 209 209 PRO PRO B . n 
B 1 210 PRO 210 210 210 PRO PRO B . n 
B 1 211 LEU 211 211 211 LEU LEU B . n 
B 1 212 LEU 212 212 212 LEU LEU B . n 
B 1 213 ARG 213 213 213 ARG ARG B . n 
B 1 214 GLY 214 214 214 GLY GLY B . n 
B 1 215 ALA 215 215 215 ALA ALA B . n 
B 1 216 GLY 216 216 216 GLY GLY B . n 
B 1 217 LEU 217 217 217 LEU LEU B . n 
B 1 218 TRP 218 218 218 TRP TRP B . n 
B 1 219 LEU 219 219 219 LEU LEU B . n 
B 1 220 GLU 220 220 220 GLU GLU B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 PHE 222 222 222 PHE PHE B . n 
B 1 223 LEU 223 223 223 LEU LEU B . n 
B 1 224 ASP 224 224 224 ASP ASP B . n 
B 1 225 ILE 225 225 225 ILE ILE B . n 
B 1 226 SER 226 226 226 SER SER B . n 
B 1 227 ASP 227 227 227 ASP ASP B . n 
B 1 228 GLN 228 228 228 GLN GLN B . n 
B 1 229 THR 229 229 229 THR THR B . n 
B 1 230 LEU 230 230 230 LEU LEU B . n 
B 1 231 GLU 231 231 231 GLU GLU B . n 
B 1 232 LYS 232 232 232 LYS LYS B . n 
B 1 233 THR 233 233 233 THR THR B . n 
B 1 234 PHE 234 234 234 PHE PHE B . n 
B 1 235 ARG 235 235 235 ARG ARG B . n 
B 1 236 LEU 236 236 236 LEU LEU B . n 
B 1 237 LEU 237 237 237 LEU LEU B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 GLU 239 239 239 GLU GLU B . n 
B 1 240 ARG 240 240 240 ARG ARG B . n 
B 1 241 ILE 241 241 241 ILE ILE B . n 
B 1 242 ASN 242 242 242 ASN ASN B . n 
B 1 243 SER 243 243 243 SER SER B . n 
B 1 244 SER 244 244 244 SER SER B . n 
B 1 245 LYS 245 245 245 LYS LYS B . n 
B 1 246 GLN 246 246 ?   ?   ?   B . n 
B 1 247 ARG 247 247 ?   ?   ?   B . n 
B 1 248 LEU 248 248 ?   ?   ?   B . n 
B 1 249 GLU 249 249 ?   ?   ?   B . n 
B 1 250 THR 250 250 ?   ?   ?   B . n 
B 1 251 GLN 251 251 ?   ?   ?   B . n 
B 1 252 PHE 252 252 ?   ?   ?   B . n 
B 1 253 GLY 253 253 ?   ?   ?   B . n 
B 1 254 GLU 254 254 ?   ?   ?   B . n 
B 1 255 GLU 255 255 ?   ?   ?   B . n 
B 1 256 MET 256 256 ?   ?   ?   B . n 
B 1 257 VAL 257 257 257 VAL VAL B . n 
B 1 258 ASN 258 258 258 ASN ASN B . n 
B 1 259 GLN 259 259 259 GLN GLN B . n 
B 1 260 PHE 260 260 260 PHE PHE B . n 
B 1 261 ASP 261 261 261 ASP ASP B . n 
B 1 262 PRO 262 262 262 PRO PRO B . n 
B 1 263 GLY 263 263 263 GLY GLY B . n 
B 1 264 ASP 264 264 264 ASP ASP B . n 
B 1 265 LEU 265 265 265 LEU LEU B . n 
B 1 266 VAL 266 266 266 VAL VAL B . n 
B 1 267 GLY 267 267 267 GLY GLY B . n 
B 1 268 VAL 268 268 268 VAL VAL B . n 
B 1 269 LYS 269 269 269 LYS LYS B . n 
B 1 270 GLU 270 270 270 GLU GLU B . n 
B 1 271 PHE 271 271 271 PHE PHE B . n 
B 1 272 GLY 272 272 272 GLY GLY B . n 
B 1 273 TYR 273 273 273 TYR TYR B . n 
B 1 274 LEU 274 274 274 LEU LEU B . n 
B 1 275 LEU 275 275 275 LEU LEU B . n 
B 1 276 LEU 276 276 276 LEU LEU B . n 
B 1 277 VAL 277 277 277 VAL VAL B . n 
B 1 278 ALA 278 278 278 ALA ALA B . n 
B 1 279 GLN 279 279 279 GLN GLN B . n 
B 1 280 ARG 280 280 280 ARG ARG B . n 
B 1 281 PRO 281 281 281 PRO PRO B . n 
B 1 282 GLY 282 282 282 GLY GLY B . n 
B 1 283 LYS 283 283 283 LYS LYS B . n 
B 1 284 HIS 284 284 284 HIS HIS B . n 
B 1 285 HIS 285 285 285 HIS HIS B . n 
B 1 286 HIS 286 286 ?   ?   ?   B . n 
B 1 287 HIS 287 287 ?   ?   ?   B . n 
B 1 288 HIS 288 288 ?   ?   ?   B . n 
B 1 289 HIS 289 289 ?   ?   ?   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 24 HOH HOH A . 
C 2 HOH 2  302 15 HOH HOH A . 
C 2 HOH 3  303 4  HOH HOH A . 
C 2 HOH 4  304 2  HOH HOH A . 
C 2 HOH 5  305 33 HOH HOH A . 
C 2 HOH 6  306 18 HOH HOH A . 
C 2 HOH 7  307 9  HOH HOH A . 
C 2 HOH 8  308 31 HOH HOH A . 
C 2 HOH 9  309 17 HOH HOH A . 
C 2 HOH 10 310 1  HOH HOH A . 
C 2 HOH 11 311 29 HOH HOH A . 
C 2 HOH 12 312 35 HOH HOH A . 
C 2 HOH 13 313 34 HOH HOH A . 
C 2 HOH 14 314 28 HOH HOH A . 
C 2 HOH 15 315 14 HOH HOH A . 
C 2 HOH 16 316 23 HOH HOH A . 
C 2 HOH 17 317 3  HOH HOH A . 
C 2 HOH 18 318 22 HOH HOH A . 
C 2 HOH 19 319 16 HOH HOH A . 
C 2 HOH 20 320 21 HOH HOH A . 
C 2 HOH 21 321 13 HOH HOH A . 
C 2 HOH 22 322 10 HOH HOH A . 
C 2 HOH 23 323 30 HOH HOH A . 
C 2 HOH 24 324 25 HOH HOH A . 
D 2 HOH 1  301 8  HOH HOH B . 
D 2 HOH 2  302 20 HOH HOH B . 
D 2 HOH 3  303 32 HOH HOH B . 
D 2 HOH 4  304 5  HOH HOH B . 
D 2 HOH 5  305 26 HOH HOH B . 
D 2 HOH 6  306 7  HOH HOH B . 
D 2 HOH 7  307 12 HOH HOH B . 
D 2 HOH 8  308 19 HOH HOH B . 
D 2 HOH 9  309 27 HOH HOH B . 
D 2 HOH 10 310 6  HOH HOH B . 
D 2 HOH 11 311 11 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 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? SCALA       ? ? ? .        1 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .        2 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .        3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? MOSFLM      ? ? ? .        4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     5 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0049 6 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8ZC7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     113.357 
_cell.length_a_esd                 ? 
_cell.length_b                     113.357 
_cell.length_b_esd                 ? 
_cell.length_c                     110.044 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        12 
_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                         8ZC7 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                152 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 31 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8ZC7 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.34 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          63.18 
_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    '0.2 M Sodium nitrate, 0.1 M Bis-Tris propane, PH 6.5, 20 % w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     110 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-12-08 
_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   0.97891 
_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 BL17U' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97891 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL17U 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8ZC7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.23 
_reflns.d_resolution_low                               49.36 
_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                                     23376 
_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                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                10.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                     2.29 
_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                             23376 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.664 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_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                                 8ZC7 
_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                            2.660 
_refine.ls_d_res_low                             31.366 
_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                     23376 
_refine.ls_number_reflns_R_free                  1992 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.83 
_refine.ls_percent_reflns_R_free                 8.52 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2042 
_refine.ls_R_factor_R_free                       0.2538 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1997 
_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                          1.34 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.83 
_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                            0.36 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4107 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             35 
_refine_hist.number_atoms_total               4142 
_refine_hist.d_res_high                       2.660 
_refine_hist.d_res_low                        31.366 
# 
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' ? 0.012  ? 4187 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.497  ? 5673 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 23.229 ? 1551 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.297  ? 631  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 757  ? 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' 2.6601 2.7266 . . 145 1532 99.00  . . . . 0.3394 . . . . . . . . . . . 0.3866 
'X-RAY DIFFRACTION' 2.7266 2.8003 . . 144 1518 100.00 . . . . 0.2604 . . . . . . . . . . . 0.2950 
'X-RAY DIFFRACTION' 2.8003 2.8826 . . 148 1558 100.00 . . . . 0.2393 . . . . . . . . . . . 0.3294 
'X-RAY DIFFRACTION' 2.8826 2.9756 . . 146 1547 100.00 . . . . 0.2323 . . . . . . . . . . . 0.2917 
'X-RAY DIFFRACTION' 2.9756 3.0819 . . 145 1516 100.00 . . . . 0.2249 . . . . . . . . . . . 0.3065 
'X-RAY DIFFRACTION' 3.0819 3.2051 . . 146 1559 100.00 . . . . 0.2147 . . . . . . . . . . . 0.2611 
'X-RAY DIFFRACTION' 3.2051 3.3508 . . 144 1542 100.00 . . . . 0.2186 . . . . . . . . . . . 0.3397 
'X-RAY DIFFRACTION' 3.3508 3.5273 . . 142 1554 100.00 . . . . 0.2344 . . . . . . . . . . . 0.2714 
'X-RAY DIFFRACTION' 3.5273 3.7479 . . 119 1314 84.00  . . . . 0.2135 . . . . . . . . . . . 0.2850 
'X-RAY DIFFRACTION' 3.7479 4.0368 . . 126 1342 87.00  . . . . 0.1989 . . . . . . . . . . . 0.2286 
'X-RAY DIFFRACTION' 4.0368 4.4420 . . 145 1556 100.00 . . . . 0.1741 . . . . . . . . . . . 0.2553 
'X-RAY DIFFRACTION' 4.4420 5.0824 . . 145 1589 100.00 . . . . 0.1601 . . . . . . . . . . . 0.2165 
'X-RAY DIFFRACTION' 5.0824 6.3944 . . 149 1593 100.00 . . . . 0.2040 . . . . . . . . . . . 0.2569 
'X-RAY DIFFRACTION' 6.3944 31.36  . . 148 1664 99.00  . . . . 0.1722 . . . . . . . . . . . 0.1902 
# 
_struct.entry_id                     8ZC7 
_struct.title                        
'Crystallographic analysis of MitM, which catalyzes the post-mitosane modification in mitomycin biosynthesis' 
_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        8ZC7 
_struct_keywords.text            'SAM-dependent methyltransferase, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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                    Q9X5Q9_STRLA 
_struct_ref.pdbx_db_accession          Q9X5Q9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MPHSELSELPMPSPASEEVGALYDRFTALGAASLGENLHFGYWDSPDSQVPLAEATDRLTDMMAERLRIGAGSRVLDLGC
GVGTPGVRIARLSGAHVTGISVSHEQVVRANALAEEAGLADRARFQRADAMDLPFEDESFDAVIALESIIHMPDRAQVLA
QVGRVLRPGGRLVLTDFFERAPLAPEGRAAVQRYLHDFMMTMVSAEAYPPLLRGAGLWLEEFLDISDQTLEKTFRLLSER
INSSKQRLETQFGEEMVNQFDPGDLVGVKEFGYLLLVAQRPGK
;
_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 8ZC7 A 1 ? 283 ? Q9X5Q9 1 ? 283 ? 1 283 
2 1 8ZC7 B 1 ? 283 ? Q9X5Q9 1 ? 283 ? 1 283 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8ZC7 HIS A 284 ? UNP Q9X5Q9 ? ? 'expression tag' 284 1  
1 8ZC7 HIS A 285 ? UNP Q9X5Q9 ? ? 'expression tag' 285 2  
1 8ZC7 HIS A 286 ? UNP Q9X5Q9 ? ? 'expression tag' 286 3  
1 8ZC7 HIS A 287 ? UNP Q9X5Q9 ? ? 'expression tag' 287 4  
1 8ZC7 HIS A 288 ? UNP Q9X5Q9 ? ? 'expression tag' 288 5  
1 8ZC7 HIS A 289 ? UNP Q9X5Q9 ? ? 'expression tag' 289 6  
2 8ZC7 HIS B 284 ? UNP Q9X5Q9 ? ? 'expression tag' 284 7  
2 8ZC7 HIS B 285 ? UNP Q9X5Q9 ? ? 'expression tag' 285 8  
2 8ZC7 HIS B 286 ? UNP Q9X5Q9 ? ? 'expression tag' 286 9  
2 8ZC7 HIS B 287 ? UNP Q9X5Q9 ? ? 'expression tag' 287 10 
2 8ZC7 HIS B 288 ? UNP Q9X5Q9 ? ? 'expression tag' 288 11 
2 8ZC7 HIS B 289 ? UNP Q9X5Q9 ? ? 'expression tag' 289 12 
# 
_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)' 1710  ? 
1 MORE         -8    ? 
1 'SSA (A^2)'  22760 ? 
# 
_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 ALA A 15  ? GLY A 30  ? ALA A 15  GLY A 30  1 ? 16 
HELX_P HELX_P2  AA2 PRO A 51  ? ARG A 68  ? PRO A 51  ARG A 68  1 ? 18 
HELX_P HELX_P3  AA3 GLY A 83  ? GLY A 94  ? GLY A 83  GLY A 94  1 ? 12 
HELX_P HELX_P4  AA4 SER A 103 ? GLY A 118 ? SER A 103 GLY A 118 1 ? 16 
HELX_P HELX_P5  AA5 SER A 148 ? MET A 152 ? SER A 148 MET A 152 5 ? 5  
HELX_P HELX_P6  AA6 ASP A 154 ? VAL A 165 ? ASP A 154 VAL A 165 1 ? 12 
HELX_P HELX_P7  AA7 ALA A 184 ? PHE A 198 ? ALA A 184 PHE A 198 1 ? 15 
HELX_P HELX_P8  AA8 ALA A 207 ? ALA A 215 ? ALA A 207 ALA A 215 1 ? 9  
HELX_P HELX_P9  AA9 ILE A 225 ? SER A 243 ? ILE A 225 SER A 243 1 ? 19 
HELX_P HELX_P10 AB1 PRO A 262 ? VAL A 266 ? PRO A 262 VAL A 266 5 ? 5  
HELX_P HELX_P11 AB2 ALA B 15  ? THR B 27  ? ALA B 15  THR B 27  1 ? 13 
HELX_P HELX_P12 AB3 PRO B 51  ? ARG B 68  ? PRO B 51  ARG B 68  1 ? 18 
HELX_P HELX_P13 AB4 GLY B 83  ? GLY B 94  ? GLY B 83  GLY B 94  1 ? 12 
HELX_P HELX_P14 AB5 SER B 103 ? ALA B 117 ? SER B 103 ALA B 117 1 ? 15 
HELX_P HELX_P15 AB6 SER B 148 ? MET B 152 ? SER B 148 MET B 152 5 ? 5  
HELX_P HELX_P16 AB7 ASP B 154 ? VAL B 165 ? ASP B 154 VAL B 165 1 ? 12 
HELX_P HELX_P17 AB8 ALA B 184 ? PHE B 198 ? ALA B 184 PHE B 198 1 ? 15 
HELX_P HELX_P18 AB9 SER B 204 ? GLU B 206 ? SER B 204 GLU B 206 5 ? 3  
HELX_P HELX_P19 AC1 ALA B 207 ? ALA B 215 ? ALA B 207 ALA B 215 1 ? 9  
HELX_P HELX_P20 AC2 ILE B 225 ? SER B 243 ? ILE B 225 SER B 243 1 ? 19 
# 
_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 ? 6  ? 
AA2 ? 14 ? 
# 
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  ? parallel      
AA1 4  5  ? parallel      
AA1 5  6  ? parallel      
AA2 1  2  ? parallel      
AA2 2  3  ? parallel      
AA2 3  4  ? parallel      
AA2 4  5  ? parallel      
AA2 5  6  ? anti-parallel 
AA2 6  7  ? anti-parallel 
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? parallel      
AA2 11 12 ? parallel      
AA2 12 13 ? parallel      
AA2 13 14 ? 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  ALA A 123 ? ARG A 127 ? ALA A 123 ARG A 127 
AA1 2  HIS A 96  ? SER A 101 ? HIS A 96  SER A 101 
AA1 3  ARG A 74  ? LEU A 78  ? ARG A 74  LEU A 78  
AA1 4  PHE A 140 ? ALA A 145 ? PHE A 140 ALA A 145 
AA1 5  LEU A 166 ? GLU A 179 ? LEU A 166 GLU A 179 
AA1 6  VAL A 203 ? SER A 204 ? VAL A 203 SER A 204 
AA2 1  ALA A 123 ? ARG A 127 ? ALA A 123 ARG A 127 
AA2 2  HIS A 96  ? SER A 101 ? HIS A 96  SER A 101 
AA2 3  ARG A 74  ? LEU A 78  ? ARG A 74  LEU A 78  
AA2 4  PHE A 140 ? ALA A 145 ? PHE A 140 ALA A 145 
AA2 5  LEU A 166 ? GLU A 179 ? LEU A 166 GLU A 179 
AA2 6  PHE A 271 ? GLN A 279 ? PHE A 271 GLN A 279 
AA2 7  TRP A 218 ? ASP A 224 ? TRP A 218 ASP A 224 
AA2 8  TRP B 218 ? ASP B 224 ? TRP B 218 ASP B 224 
AA2 9  PHE B 271 ? GLN B 279 ? PHE B 271 GLN B 279 
AA2 10 LEU B 166 ? GLU B 179 ? LEU B 166 GLU B 179 
AA2 11 PHE B 140 ? ALA B 145 ? PHE B 140 ALA B 145 
AA2 12 ARG B 74  ? LEU B 78  ? ARG B 74  LEU B 78  
AA2 13 HIS B 96  ? SER B 101 ? HIS B 96  SER B 101 
AA2 14 ALA B 123 ? ARG B 127 ? ALA B 123 ARG B 127 
# 
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 ARG A 124 ? O ARG A 124 N GLY A 99  ? N GLY A 99  
AA1 2  3  O THR A 98  ? O THR A 98  N ASP A 77  ? N ASP A 77  
AA1 3  4  N LEU A 76  ? N LEU A 76  O ILE A 144 ? O ILE A 144 
AA1 4  5  N ALA A 145 ? N ALA A 145 O VAL A 173 ? O VAL A 173 
AA1 5  6  N GLU A 179 ? N GLU A 179 O VAL A 203 ? O VAL A 203 
AA2 1  2  O ARG A 124 ? O ARG A 124 N GLY A 99  ? N GLY A 99  
AA2 2  3  O THR A 98  ? O THR A 98  N ASP A 77  ? N ASP A 77  
AA2 3  4  N LEU A 76  ? N LEU A 76  O ILE A 144 ? O ILE A 144 
AA2 4  5  N ALA A 145 ? N ALA A 145 O VAL A 173 ? O VAL A 173 
AA2 5  6  N ASP A 176 ? N ASP A 176 O LEU A 274 ? O LEU A 274 
AA2 6  7  O VAL A 277 ? O VAL A 277 N GLU A 220 ? N GLU A 220 
AA2 7  8  N PHE A 222 ? N PHE A 222 O PHE B 222 ? O PHE B 222 
AA2 8  9  N GLU B 220 ? N GLU B 220 O VAL B 277 ? O VAL B 277 
AA2 9  10 O ALA B 278 ? O ALA B 278 N LEU B 172 ? N LEU B 172 
AA2 10 11 O ARG B 167 ? O ARG B 167 N PHE B 140 ? N PHE B 140 
AA2 11 12 O ASP B 141 ? O ASP B 141 N ARG B 74  ? N ARG B 74  
AA2 12 13 N VAL B 75  ? N VAL B 75  O HIS B 96  ? O HIS B 96  
AA2 13 14 N VAL B 97  ? N VAL B 97  O ARG B 124 ? O ARG B 124 
# 
_pdbx_entry_details.entry_id                   8ZC7 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 NE  A ARG 109 ? ? O   A HOH 301 ? ? 1.80 
2  1 O   A ASP 47  ? ? OE1 A GLN 49  ? ? 1.90 
3  1 O   A LEU 6   ? ? O   A HOH 302 ? ? 1.94 
4  1 O   A HOH 315 ? ? O   A HOH 318 ? ? 2.06 
5  1 OG  A SER 33  ? ? O   A HOH 303 ? ? 2.07 
6  1 ND1 A HIS 104 ? ? O   A HOH 304 ? ? 2.09 
7  1 OD2 A ASP 176 ? ? OH  A TYR 208 ? ? 2.11 
8  1 O   A PRO 185 ? ? O   A HOH 305 ? ? 2.11 
9  1 N   A LEU 6   ? ? OE2 A GLU 8   ? ? 2.13 
10 1 NH1 A ARG 109 ? ? O   A HOH 306 ? ? 2.14 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OD2 B ASP 121 ? ? 1_555 OD2 B ASP 121 ? ? 5_554 1.41 
2 1 CG  B ASP 121 ? ? 1_555 OD2 B ASP 121 ? ? 5_554 1.91 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N A ASN 258 ? ? CA A ASN 258 ? ? C  A ASN 258 ? ? 93.71  111.00 -17.29 2.70 N 
2 1 N A ASP 261 ? ? CA A ASP 261 ? ? C  A ASP 261 ? ? 88.66  111.00 -22.34 2.70 N 
3 1 C A ASP 261 ? ? N  A PRO 262 ? ? CA A PRO 262 ? ? 107.63 119.30 -11.67 1.50 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 LEU A 38  ? ? -100.99 61.87   
2  1 GLU A 147 ? ? 39.05   40.59   
3  1 THR A 201 ? ? -128.98 -166.11 
4  1 THR A 229 ? ? -124.63 -55.61  
5  1 PHE A 260 ? ? 177.19  156.84  
6  1 PRO B 10  ? ? -64.77  -178.26 
7  1 THR B 27  ? ? -84.36  46.44   
8  1 ALA B 28  ? ? -177.21 142.47  
9  1 ALA B 32  ? ? -171.96 111.63  
10 1 SER B 33  ? ? -109.91 -65.70  
11 1 THR B 229 ? ? -122.76 -55.93  
12 1 ASN B 258 ? ? -172.55 -175.42 
13 1 GLN B 259 ? ? -91.97  44.62   
14 1 ASP B 264 ? ? -63.78  0.08    
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         52.5281 
_pdbx_refine_tls.origin_y         -6.2020 
_pdbx_refine_tls.origin_z         9.6761 
_pdbx_refine_tls.T[1][1]          0.4476 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0645 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0466 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.2936 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0699 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.3282 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          1.5198 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.6646 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.7349 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.7162 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          -0.6017 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          0.8119 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.1510 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.1999 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.1339 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.1861 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0569 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.1141 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1674 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.1252 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.0001 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
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 PRO 2   ? A PRO 2   
3  1 Y 1 A HIS 3   ? A HIS 3   
4  1 Y 1 A SER 4   ? A SER 4   
5  1 Y 1 A GLU 5   ? A GLU 5   
6  1 Y 1 A GLN 246 ? A GLN 246 
7  1 Y 1 A ARG 247 ? A ARG 247 
8  1 Y 1 A LEU 248 ? A LEU 248 
9  1 Y 1 A GLU 249 ? A GLU 249 
10 1 Y 1 A THR 250 ? A THR 250 
11 1 Y 1 A GLN 251 ? A GLN 251 
12 1 Y 1 A PHE 252 ? A PHE 252 
13 1 Y 1 A GLY 253 ? A GLY 253 
14 1 Y 1 A GLU 254 ? A GLU 254 
15 1 Y 1 A GLU 255 ? A GLU 255 
16 1 Y 1 A MET 256 ? A MET 256 
17 1 Y 1 A LYS 283 ? A LYS 283 
18 1 Y 1 A HIS 284 ? A HIS 284 
19 1 Y 1 A HIS 285 ? A HIS 285 
20 1 Y 1 A HIS 286 ? A HIS 286 
21 1 Y 1 A HIS 287 ? A HIS 287 
22 1 Y 1 A HIS 288 ? A HIS 288 
23 1 Y 1 A HIS 289 ? A HIS 289 
24 1 Y 1 B MET 1   ? B MET 1   
25 1 Y 1 B PRO 2   ? B PRO 2   
26 1 Y 1 B HIS 3   ? B HIS 3   
27 1 Y 1 B SER 4   ? B SER 4   
28 1 Y 1 B GLU 5   ? B GLU 5   
29 1 Y 1 B GLN 246 ? B GLN 246 
30 1 Y 1 B ARG 247 ? B ARG 247 
31 1 Y 1 B LEU 248 ? B LEU 248 
32 1 Y 1 B GLU 249 ? B GLU 249 
33 1 Y 1 B THR 250 ? B THR 250 
34 1 Y 1 B GLN 251 ? B GLN 251 
35 1 Y 1 B PHE 252 ? B PHE 252 
36 1 Y 1 B GLY 253 ? B GLY 253 
37 1 Y 1 B GLU 254 ? B GLU 254 
38 1 Y 1 B GLU 255 ? B GLU 255 
39 1 Y 1 B MET 256 ? B MET 256 
40 1 Y 1 B HIS 286 ? B HIS 286 
41 1 Y 1 B HIS 287 ? B HIS 287 
42 1 Y 1 B HIS 288 ? B HIS 288 
43 1 Y 1 B HIS 289 ? B HIS 289 
# 
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           ? 
_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                    8ZC7 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.008822 
_atom_sites.fract_transf_matrix[1][2]   0.005093 
_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]   0.010186 
_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]   0.009087 
_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 6   ? 40.218 9.659   10.892  1.00 75.85  ?  6   LEU A N   1 
ATOM   2    C CA  . LEU A 1 6   ? 39.846 8.734   11.967  1.00 87.83  ?  6   LEU A CA  1 
ATOM   3    C C   . LEU A 1 6   ? 38.421 8.986   12.460  1.00 99.19  ?  6   LEU A C   1 
ATOM   4    O O   . LEU A 1 6   ? 37.687 8.057   12.838  1.00 98.17  ?  6   LEU A O   1 
ATOM   5    C CB  . LEU A 1 6   ? 40.825 8.848   13.152  1.00 87.91  ?  6   LEU A CB  1 
ATOM   6    C CG  . LEU A 1 6   ? 40.860 7.705   14.187  1.00 80.48  ?  6   LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 6   ? 42.263 7.509   14.813  1.00 74.95  ?  6   LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 6   ? 39.803 7.895   15.271  1.00 72.00  ?  6   LEU A CD2 1 
ATOM   9    N N   . SER A 1 7   ? 38.049 10.267  12.439  1.00 118.01 ?  7   SER A N   1 
ATOM   10   C CA  . SER A 1 7   ? 36.861 10.808  13.105  1.00 120.09 ?  7   SER A CA  1 
ATOM   11   C C   . SER A 1 7   ? 35.963 11.521  12.094  1.00 123.70 ?  7   SER A C   1 
ATOM   12   O O   . SER A 1 7   ? 35.450 12.622  12.337  1.00 123.35 ?  7   SER A O   1 
ATOM   13   C CB  . SER A 1 7   ? 37.259 11.750  14.251  1.00 108.54 ?  7   SER A CB  1 
ATOM   14   O OG  . SER A 1 7   ? 37.622 11.042  15.436  1.00 94.72  ?  7   SER A OG  1 
ATOM   15   N N   . GLU A 1 8   ? 35.765 10.902  10.935  1.00 118.74 ?  8   GLU A N   1 
ATOM   16   C CA  . GLU A 1 8   ? 34.936 11.484  9.894   1.00 105.31 ?  8   GLU A CA  1 
ATOM   17   C C   . GLU A 1 8   ? 33.599 10.768  9.777   1.00 103.30 ?  8   GLU A C   1 
ATOM   18   O O   . GLU A 1 8   ? 32.548 11.415  9.756   1.00 101.93 ?  8   GLU A O   1 
ATOM   19   C CB  . GLU A 1 8   ? 35.689 11.461  8.557   1.00 86.42  ?  8   GLU A CB  1 
ATOM   20   C CG  . GLU A 1 8   ? 37.121 11.970  8.654   1.00 98.12  ?  8   GLU A CG  1 
ATOM   21   C CD  . GLU A 1 8   ? 38.108 10.862  8.951   1.00 94.87  ?  8   GLU A CD  1 
ATOM   22   O OE1 . GLU A 1 8   ? 37.987 9.811   8.289   1.00 82.06  ?  8   GLU A OE1 1 
ATOM   23   O OE2 . GLU A 1 8   ? 38.994 11.039  9.825   1.00 98.98  -1 8   GLU A OE2 1 
ATOM   24   N N   . LEU A 1 9   ? 33.619 9.424   9.744   1.00 97.67  ?  9   LEU A N   1 
ATOM   25   C CA  . LEU A 1 9   ? 32.317 8.820   9.561   1.00 95.38  ?  9   LEU A CA  1 
ATOM   26   C C   . LEU A 1 9   ? 31.644 8.534   10.895  1.00 92.44  ?  9   LEU A C   1 
ATOM   27   O O   . LEU A 1 9   ? 32.314 8.208   11.884  1.00 88.67  ?  9   LEU A O   1 
ATOM   28   C CB  . LEU A 1 9   ? 32.440 7.530   8.759   1.00 93.53  ?  9   LEU A CB  1 
ATOM   29   C CG  . LEU A 1 9   ? 31.359 7.449   7.682   1.00 93.16  ?  9   LEU A CG  1 
ATOM   30   C CD1 . LEU A 1 9   ? 31.191 8.760   6.936   1.00 93.39  ?  9   LEU A CD1 1 
ATOM   31   C CD2 . LEU A 1 9   ? 31.659 6.328   6.713   1.00 91.05  ?  9   LEU A CD2 1 
ATOM   32   N N   . PRO A 1 10  ? 30.322 8.709   10.915  1.00 91.37  ?  10  PRO A N   1 
ATOM   33   C CA  . PRO A 1 10  ? 29.524 8.200   12.034  1.00 96.19  ?  10  PRO A CA  1 
ATOM   34   C C   . PRO A 1 10  ? 29.505 6.676   12.049  1.00 97.57  ?  10  PRO A C   1 
ATOM   35   O O   . PRO A 1 10  ? 29.194 6.021   11.046  1.00 88.32  ?  10  PRO A O   1 
ATOM   36   C CB  . PRO A 1 10  ? 28.126 8.777   11.773  1.00 98.07  ?  10  PRO A CB  1 
ATOM   37   C CG  . PRO A 1 10  ? 28.325 9.872   10.787  1.00 95.80  ?  10  PRO A CG  1 
ATOM   38   C CD  . PRO A 1 10  ? 29.516 9.513   9.982   1.00 93.40  ?  10  PRO A CD  1 
ATOM   39   N N   . MET A 1 11  ? 29.831 6.124   13.214  1.00 101.67 ?  11  MET A N   1 
ATOM   40   C CA  . MET A 1 11  ? 29.819 4.710   13.519  1.00 99.79  ?  11  MET A CA  1 
ATOM   41   C C   . MET A 1 11  ? 28.848 4.447   14.670  1.00 103.29 ?  11  MET A C   1 
ATOM   42   O O   . MET A 1 11  ? 28.794 5.230   15.629  1.00 100.52 ?  11  MET A O   1 
ATOM   43   C CB  . MET A 1 11  ? 31.251 4.214   13.894  1.00 88.67  ?  11  MET A CB  1 
ATOM   44   C CG  . MET A 1 11  ? 32.379 4.757   12.964  1.00 86.27  ?  11  MET A CG  1 
ATOM   45   S SD  . MET A 1 11  ? 34.074 4.075   13.082  1.00 77.04  ?  11  MET A SD  1 
ATOM   46   C CE  . MET A 1 11  ? 34.496 4.372   14.800  1.00 69.79  ?  11  MET A CE  1 
ATOM   47   N N   . PRO A 1 12  ? 28.058 3.379   14.607  1.00 103.80 ?  12  PRO A N   1 
ATOM   48   C CA  . PRO A 1 12  ? 27.310 2.970   15.798  1.00 93.67  ?  12  PRO A CA  1 
ATOM   49   C C   . PRO A 1 12  ? 28.291 2.503   16.851  1.00 90.09  ?  12  PRO A C   1 
ATOM   50   O O   . PRO A 1 12  ? 29.440 2.166   16.557  1.00 92.21  ?  12  PRO A O   1 
ATOM   51   C CB  . PRO A 1 12  ? 26.439 1.811   15.299  1.00 90.80  ?  12  PRO A CB  1 
ATOM   52   C CG  . PRO A 1 12  ? 27.256 1.197   14.202  1.00 93.23  ?  12  PRO A CG  1 
ATOM   53   C CD  . PRO A 1 12  ? 27.988 2.362   13.540  1.00 101.88 ?  12  PRO A CD  1 
ATOM   54   N N   . SER A 1 13  ? 27.839 2.486   18.099  1.00 90.86  ?  13  SER A N   1 
ATOM   55   C CA  . SER A 1 13  ? 28.632 1.829   19.129  1.00 95.94  ?  13  SER A CA  1 
ATOM   56   C C   . SER A 1 13  ? 27.860 0.577   19.553  1.00 90.49  ?  13  SER A C   1 
ATOM   57   O O   . SER A 1 13  ? 26.950 0.650   20.384  1.00 92.37  ?  13  SER A O   1 
ATOM   58   C CB  . SER A 1 13  ? 28.902 2.759   20.312  1.00 101.58 ?  13  SER A CB  1 
ATOM   59   O OG  . SER A 1 13  ? 30.050 2.315   21.020  1.00 108.32 ?  13  SER A OG  1 
ATOM   60   N N   . PRO A 1 14  ? 28.160 -0.585  18.962  1.00 87.83  ?  14  PRO A N   1 
ATOM   61   C CA  . PRO A 1 14  ? 27.250 -1.741  19.117  1.00 87.72  ?  14  PRO A CA  1 
ATOM   62   C C   . PRO A 1 14  ? 27.187 -2.270  20.544  1.00 81.65  ?  14  PRO A C   1 
ATOM   63   O O   . PRO A 1 14  ? 28.185 -2.309  21.274  1.00 83.64  ?  14  PRO A O   1 
ATOM   64   C CB  . PRO A 1 14  ? 27.852 -2.789  18.163  1.00 90.61  ?  14  PRO A CB  1 
ATOM   65   C CG  . PRO A 1 14  ? 29.317 -2.366  18.005  1.00 88.60  ?  14  PRO A CG  1 
ATOM   66   C CD  . PRO A 1 14  ? 29.332 -0.884  18.116  1.00 88.79  ?  14  PRO A CD  1 
ATOM   67   N N   . ALA A 1 15  ? 25.986 -2.690  20.935  1.00 76.84  ?  15  ALA A N   1 
ATOM   68   C CA  . ALA A 1 15  ? 25.760 -3.354  22.210  1.00 71.64  ?  15  ALA A CA  1 
ATOM   69   C C   . ALA A 1 15  ? 25.685 -4.856  21.983  1.00 72.82  ?  15  ALA A C   1 
ATOM   70   O O   . ALA A 1 15  ? 25.073 -5.306  21.006  1.00 80.77  ?  15  ALA A O   1 
ATOM   71   C CB  . ALA A 1 15  ? 24.469 -2.859  22.868  1.00 74.53  ?  15  ALA A CB  1 
ATOM   72   N N   . SER A 1 16  ? 26.306 -5.626  22.887  1.00 62.47  ?  16  SER A N   1 
ATOM   73   C CA  . SER A 1 16  ? 26.336 -7.082  22.750  1.00 67.81  ?  16  SER A CA  1 
ATOM   74   C C   . SER A 1 16  ? 24.941 -7.669  22.539  1.00 82.79  ?  16  SER A C   1 
ATOM   75   O O   . SER A 1 16  ? 24.707 -8.399  21.564  1.00 90.67  ?  16  SER A O   1 
ATOM   76   C CB  . SER A 1 16  ? 27.002 -7.719  23.968  1.00 65.84  ?  16  SER A CB  1 
ATOM   77   O OG  . SER A 1 16  ? 28.413 -7.538  23.936  1.00 71.25  ?  16  SER A OG  1 
ATOM   78   N N   . GLU A 1 17  ? 23.988 -7.350  23.423  1.00 82.30  ?  17  GLU A N   1 
ATOM   79   C CA  . GLU A 1 17  ? 22.699 -8.027  23.306  1.00 86.94  ?  17  GLU A CA  1 
ATOM   80   C C   . GLU A 1 17  ? 21.953 -7.585  22.052  1.00 82.84  ?  17  GLU A C   1 
ATOM   81   O O   . GLU A 1 17  ? 21.208 -8.384  21.465  1.00 82.13  ?  17  GLU A O   1 
ATOM   82   C CB  . GLU A 1 17  ? 21.836 -7.807  24.553  1.00 98.10  ?  17  GLU A CB  1 
ATOM   83   C CG  . GLU A 1 17  ? 20.461 -8.480  24.437  1.00 106.65 ?  17  GLU A CG  1 
ATOM   84   C CD  . GLU A 1 17  ? 19.344 -7.650  25.030  1.00 121.76 ?  17  GLU A CD  1 
ATOM   85   O OE1 . GLU A 1 17  ? 19.581 -7.021  26.087  1.00 128.43 ?  17  GLU A OE1 1 
ATOM   86   O OE2 . GLU A 1 17  ? 18.243 -7.608  24.429  1.00 129.81 -1 17  GLU A OE2 1 
ATOM   87   N N   . GLU A 1 18  ? 22.168 -6.346  21.592  1.00 81.47  ?  18  GLU A N   1 
ATOM   88   C CA  . GLU A 1 18  ? 21.526 -5.922  20.344  1.00 85.14  ?  18  GLU A CA  1 
ATOM   89   C C   . GLU A 1 18  ? 22.170 -6.573  19.116  1.00 78.20  ?  18  GLU A C   1 
ATOM   90   O O   . GLU A 1 18  ? 21.468 -6.863  18.134  1.00 77.28  ?  18  GLU A O   1 
ATOM   91   C CB  . GLU A 1 18  ? 21.556 -4.401  20.236  1.00 83.07  ?  18  GLU A CB  1 
ATOM   92   C CG  . GLU A 1 18  ? 20.548 -3.727  21.151  1.00 84.83  ?  18  GLU A CG  1 
ATOM   93   C CD  . GLU A 1 18  ? 20.368 -2.241  20.858  1.00 93.33  ?  18  GLU A CD  1 
ATOM   94   O OE1 . GLU A 1 18  ? 21.342 -1.563  20.464  1.00 89.68  ?  18  GLU A OE1 1 
ATOM   95   O OE2 . GLU A 1 18  ? 19.220 -1.762  20.984  1.00 101.48 -1 18  GLU A OE2 1 
ATOM   96   N N   . VAL A 1 19  ? 23.489 -6.815  19.149  1.00 67.90  ?  19  VAL A N   1 
ATOM   97   C CA  . VAL A 1 19  ? 24.126 -7.566  18.067  1.00 74.79  ?  19  VAL A CA  1 
ATOM   98   C C   . VAL A 1 19  ? 23.662 -9.016  18.092  1.00 73.43  ?  19  VAL A C   1 
ATOM   99   O O   . VAL A 1 19  ? 23.386 -9.613  17.043  1.00 74.35  ?  19  VAL A O   1 
ATOM   100  C CB  . VAL A 1 19  ? 25.664 -7.454  18.147  1.00 77.97  ?  19  VAL A CB  1 
ATOM   101  C CG1 . VAL A 1 19  ? 26.338 -8.396  17.124  1.00 71.50  ?  19  VAL A CG1 1 
ATOM   102  C CG2 . VAL A 1 19  ? 26.115 -6.017  17.911  1.00 62.83  ?  19  VAL A CG2 1 
ATOM   103  N N   . GLY A 1 20  ? 23.554 -9.597  19.296  1.00 71.55  ?  20  GLY A N   1 
ATOM   104  C CA  . GLY A 1 20  ? 22.960 -10.918 19.443  1.00 68.26  ?  20  GLY A CA  1 
ATOM   105  C C   . GLY A 1 20  ? 21.580 -11.044 18.825  1.00 66.81  ?  20  GLY A C   1 
ATOM   106  O O   . GLY A 1 20  ? 21.278 -12.044 18.161  1.00 64.81  ?  20  GLY A O   1 
ATOM   107  N N   . ALA A 1 21  ? 20.725 -10.030 19.022  1.00 65.40  ?  21  ALA A N   1 
ATOM   108  C CA  . ALA A 1 21  ? 19.392 -10.064 18.422  1.00 65.83  ?  21  ALA A CA  1 
ATOM   109  C C   . ALA A 1 21  ? 19.447 -9.935  16.898  1.00 73.14  ?  21  ALA A C   1 
ATOM   110  O O   . ALA A 1 21  ? 18.703 -10.624 16.182  1.00 72.59  ?  21  ALA A O   1 
ATOM   111  C CB  . ALA A 1 21  ? 18.522 -8.965  19.024  1.00 68.21  ?  21  ALA A CB  1 
ATOM   112  N N   . LEU A 1 22  ? 20.306 -9.053  16.377  1.00 71.76  ?  22  LEU A N   1 
ATOM   113  C CA  . LEU A 1 22  ? 20.438 -8.940  14.928  1.00 73.97  ?  22  LEU A CA  1 
ATOM   114  C C   . LEU A 1 22  ? 20.811 -10.284 14.316  1.00 77.97  ?  22  LEU A C   1 
ATOM   115  O O   . LEU A 1 22  ? 20.238 -10.713 13.307  1.00 62.85  ?  22  LEU A O   1 
ATOM   116  C CB  . LEU A 1 22  ? 21.485 -7.882  14.565  1.00 68.79  ?  22  LEU A CB  1 
ATOM   117  C CG  . LEU A 1 22  ? 21.869 -7.853  13.076  1.00 68.95  ?  22  LEU A CG  1 
ATOM   118  C CD1 . LEU A 1 22  ? 20.703 -7.404  12.218  1.00 65.75  ?  22  LEU A CD1 1 
ATOM   119  C CD2 . LEU A 1 22  ? 23.097 -7.000  12.806  1.00 68.03  ?  22  LEU A CD2 1 
ATOM   120  N N   . TYR A 1 23  ? 21.775 -10.971 14.932  1.00 85.11  ?  23  TYR A N   1 
ATOM   121  C CA  . TYR A 1 23  ? 22.330 -12.164 14.310  1.00 76.53  ?  23  TYR A CA  1 
ATOM   122  C C   . TYR A 1 23  ? 21.482 -13.405 14.566  1.00 73.37  ?  23  TYR A C   1 
ATOM   123  O O   . TYR A 1 23  ? 21.428 -14.287 13.698  1.00 61.86  ?  23  TYR A O   1 
ATOM   124  C CB  . TYR A 1 23  ? 23.778 -12.334 14.768  1.00 70.90  ?  23  TYR A CB  1 
ATOM   125  C CG  . TYR A 1 23  ? 24.672 -11.477 13.907  1.00 69.12  ?  23  TYR A CG  1 
ATOM   126  C CD1 . TYR A 1 23  ? 25.081 -11.930 12.649  1.00 67.83  ?  23  TYR A CD1 1 
ATOM   127  C CD2 . TYR A 1 23  ? 25.054 -10.190 14.313  1.00 60.85  ?  23  TYR A CD2 1 
ATOM   128  C CE1 . TYR A 1 23  ? 25.876 -11.145 11.825  1.00 69.95  ?  23  TYR A CE1 1 
ATOM   129  C CE2 . TYR A 1 23  ? 25.860 -9.400  13.502  1.00 66.26  ?  23  TYR A CE2 1 
ATOM   130  C CZ  . TYR A 1 23  ? 26.264 -9.883  12.251  1.00 71.78  ?  23  TYR A CZ  1 
ATOM   131  O OH  . TYR A 1 23  ? 27.047 -9.126  11.410  1.00 78.14  ?  23  TYR A OH  1 
ATOM   132  N N   . ASP A 1 24  ? 20.800 -13.475 15.723  1.00 68.29  ?  24  ASP A N   1 
ATOM   133  C CA  . ASP A 1 24  ? 19.757 -14.481 15.911  1.00 61.06  ?  24  ASP A CA  1 
ATOM   134  C C   . ASP A 1 24  ? 18.815 -14.491 14.724  1.00 67.65  ?  24  ASP A C   1 
ATOM   135  O O   . ASP A 1 24  ? 18.480 -15.555 14.191  1.00 62.01  ?  24  ASP A O   1 
ATOM   136  C CB  . ASP A 1 24  ? 18.970 -14.210 17.195  1.00 58.45  ?  24  ASP A CB  1 
ATOM   137  C CG  . ASP A 1 24  ? 19.696 -14.686 18.433  1.00 67.33  ?  24  ASP A CG  1 
ATOM   138  O OD1 . ASP A 1 24  ? 20.610 -15.522 18.286  1.00 68.24  ?  24  ASP A OD1 1 
ATOM   139  O OD2 . ASP A 1 24  ? 19.372 -14.225 19.554  1.00 71.71  -1 24  ASP A OD2 1 
ATOM   140  N N   . ARG A 1 25  ? 18.413 -13.304 14.268  1.00 69.70  ?  25  ARG A N   1 
ATOM   141  C CA  . ARG A 1 25  ? 17.502 -13.207 13.133  1.00 63.39  ?  25  ARG A CA  1 
ATOM   142  C C   . ARG A 1 25  ? 18.193 -13.625 11.842  1.00 72.08  ?  25  ARG A C   1 
ATOM   143  O O   . ARG A 1 25  ? 17.590 -14.321 11.015  1.00 80.44  ?  25  ARG A O   1 
ATOM   144  C CB  . ARG A 1 25  ? 16.970 -11.778 13.048  1.00 70.54  ?  25  ARG A CB  1 
ATOM   145  C CG  . ARG A 1 25  ? 15.797 -11.535 12.131  1.00 79.28  ?  25  ARG A CG  1 
ATOM   146  C CD  . ARG A 1 25  ? 14.998 -10.306 12.609  1.00 90.34  ?  25  ARG A CD  1 
ATOM   147  N NE  . ARG A 1 25  ? 15.643 -9.565  13.707  1.00 97.57  ?  25  ARG A NE  1 
ATOM   148  C CZ  . ARG A 1 25  ? 16.389 -8.461  13.565  1.00 99.04  ?  25  ARG A CZ  1 
ATOM   149  N NH1 . ARG A 1 25  ? 16.600 -7.945  12.354  1.00 99.30  ?  25  ARG A NH1 1 
ATOM   150  N NH2 . ARG A 1 25  ? 16.929 -7.870  14.640  1.00 93.42  ?  25  ARG A NH2 1 
ATOM   151  N N   . PHE A 1 26  ? 19.460 -13.217 11.652  1.00 68.46  ?  26  PHE A N   1 
ATOM   152  C CA  . PHE A 1 26  ? 20.232 -13.679 10.496  1.00 65.56  ?  26  PHE A CA  1 
ATOM   153  C C   . PHE A 1 26  ? 20.305 -15.193 10.485  1.00 67.53  ?  26  PHE A C   1 
ATOM   154  O O   . PHE A 1 26  ? 19.993 -15.844 9.479   1.00 68.84  ?  26  PHE A O   1 
ATOM   155  C CB  . PHE A 1 26  ? 21.659 -13.115 10.524  1.00 63.79  ?  26  PHE A CB  1 
ATOM   156  C CG  . PHE A 1 26  ? 21.777 -11.664 10.112  1.00 69.84  ?  26  PHE A CG  1 
ATOM   157  C CD1 . PHE A 1 26  ? 20.807 -11.047 9.336   1.00 76.07  ?  26  PHE A CD1 1 
ATOM   158  C CD2 . PHE A 1 26  ? 22.870 -10.916 10.513  1.00 70.04  ?  26  PHE A CD2 1 
ATOM   159  C CE1 . PHE A 1 26  ? 20.936 -9.713  8.976   1.00 73.50  ?  26  PHE A CE1 1 
ATOM   160  C CE2 . PHE A 1 26  ? 23.000 -9.586  10.157  1.00 74.85  ?  26  PHE A CE2 1 
ATOM   161  C CZ  . PHE A 1 26  ? 22.034 -8.986  9.388   1.00 71.94  ?  26  PHE A CZ  1 
ATOM   162  N N   . THR A 1 27  ? 20.729 -15.763 11.614  1.00 62.84  ?  27  THR A N   1 
ATOM   163  C CA  . THR A 1 27  ? 20.908 -17.202 11.717  1.00 54.34  ?  27  THR A CA  1 
ATOM   164  C C   . THR A 1 27  ? 19.595 -17.938 11.545  1.00 66.31  ?  27  THR A C   1 
ATOM   165  O O   . THR A 1 27  ? 19.532 -18.941 10.829  1.00 72.53  ?  27  THR A O   1 
ATOM   166  C CB  . THR A 1 27  ? 21.509 -17.543 13.072  1.00 50.85  ?  27  THR A CB  1 
ATOM   167  O OG1 . THR A 1 27  ? 22.690 -16.763 13.278  1.00 64.41  ?  27  THR A OG1 1 
ATOM   168  C CG2 . THR A 1 27  ? 21.837 -19.006 13.150  1.00 54.73  ?  27  THR A CG2 1 
ATOM   169  N N   . ALA A 1 28  ? 18.537 -17.466 12.212  1.00 73.55  ?  28  ALA A N   1 
ATOM   170  C CA  . ALA A 1 28  ? 17.280 -18.203 12.269  1.00 71.73  ?  28  ALA A CA  1 
ATOM   171  C C   . ALA A 1 28  ? 16.539 -18.224 10.939  1.00 73.89  ?  28  ALA A C   1 
ATOM   172  O O   . ALA A 1 28  ? 15.591 -19.005 10.797  1.00 73.08  ?  28  ALA A O   1 
ATOM   173  C CB  . ALA A 1 28  ? 16.372 -17.630 13.354  1.00 68.75  ?  28  ALA A CB  1 
ATOM   174  N N   . LEU A 1 29  ? 16.946 -17.401 9.965   1.00 71.93  ?  29  LEU A N   1 
ATOM   175  C CA  . LEU A 1 29  ? 16.416 -17.567 8.615   1.00 74.16  ?  29  LEU A CA  1 
ATOM   176  C C   . LEU A 1 29  ? 17.228 -18.574 7.803   1.00 79.57  ?  29  LEU A C   1 
ATOM   177  O O   . LEU A 1 29  ? 16.682 -19.237 6.919   1.00 94.39  ?  29  LEU A O   1 
ATOM   178  C CB  . LEU A 1 29  ? 16.379 -16.230 7.885   1.00 76.09  ?  29  LEU A CB  1 
ATOM   179  C CG  . LEU A 1 29  ? 15.683 -15.059 8.575   1.00 77.94  ?  29  LEU A CG  1 
ATOM   180  C CD1 . LEU A 1 29  ? 15.399 -13.983 7.533   1.00 79.78  ?  29  LEU A CD1 1 
ATOM   181  C CD2 . LEU A 1 29  ? 14.402 -15.506 9.263   1.00 72.44  ?  29  LEU A CD2 1 
ATOM   182  N N   . GLY A 1 30  ? 18.525 -18.693 8.069   1.00 74.91  ?  30  GLY A N   1 
ATOM   183  C CA  . GLY A 1 30  ? 19.420 -19.459 7.220   1.00 66.47  ?  30  GLY A CA  1 
ATOM   184  C C   . GLY A 1 30  ? 20.409 -18.599 6.463   1.00 67.15  ?  30  GLY A C   1 
ATOM   185  O O   . GLY A 1 30  ? 21.292 -19.146 5.783   1.00 74.87  ?  30  GLY A O   1 
ATOM   186  N N   . ALA A 1 31  ? 20.267 -17.271 6.535   1.00 61.32  ?  31  ALA A N   1 
ATOM   187  C CA  . ALA A 1 31  ? 21.267 -16.367 5.988   1.00 61.88  ?  31  ALA A CA  1 
ATOM   188  C C   . ALA A 1 31  ? 22.665 -16.853 6.342   1.00 68.67  ?  31  ALA A C   1 
ATOM   189  O O   . ALA A 1 31  ? 23.520 -16.981 5.458   1.00 79.61  ?  31  ALA A O   1 
ATOM   190  C CB  . ALA A 1 31  ? 21.024 -14.949 6.499   1.00 53.69  ?  31  ALA A CB  1 
ATOM   191  N N   . ALA A 1 32  ? 22.907 -17.178 7.630   1.00 65.14  ?  32  ALA A N   1 
ATOM   192  C CA  . ALA A 1 32  ? 24.088 -17.951 8.043   1.00 58.25  ?  32  ALA A CA  1 
ATOM   193  C C   . ALA A 1 32  ? 23.641 -19.375 8.377   1.00 65.29  ?  32  ALA A C   1 
ATOM   194  O O   . ALA A 1 32  ? 23.054 -19.627 9.435   1.00 70.38  ?  32  ALA A O   1 
ATOM   195  C CB  . ALA A 1 32  ? 24.801 -17.309 9.219   1.00 44.93  ?  32  ALA A CB  1 
ATOM   196  N N   . SER A 1 33  ? 23.950 -20.307 7.487   1.00 51.77  ?  33  SER A N   1 
ATOM   197  C CA  . SER A 1 33  ? 23.517 -21.688 7.602   1.00 55.14  ?  33  SER A CA  1 
ATOM   198  C C   . SER A 1 33  ? 24.693 -22.608 8.023   1.00 51.58  ?  33  SER A C   1 
ATOM   199  O O   . SER A 1 33  ? 25.876 -22.251 7.927   1.00 44.46  ?  33  SER A O   1 
ATOM   200  C CB  . SER A 1 33  ? 22.905 -22.095 6.253   1.00 53.85  ?  33  SER A CB  1 
ATOM   201  O OG  . SER A 1 33  ? 21.889 -23.073 6.377   1.00 84.49  ?  33  SER A OG  1 
ATOM   202  N N   . LEU A 1 34  ? 24.357 -23.820 8.483   1.00 51.77  ?  34  LEU A N   1 
ATOM   203  C CA  . LEU A 1 34  ? 25.370 -24.775 8.944   1.00 46.33  ?  34  LEU A CA  1 
ATOM   204  C C   . LEU A 1 34  ? 26.524 -24.965 7.954   1.00 53.62  ?  34  LEU A C   1 
ATOM   205  O O   . LEU A 1 34  ? 26.327 -25.231 6.762   1.00 53.72  ?  34  LEU A O   1 
ATOM   206  C CB  . LEU A 1 34  ? 24.731 -26.132 9.224   1.00 44.76  ?  34  LEU A CB  1 
ATOM   207  C CG  . LEU A 1 34  ? 24.164 -26.352 10.619  1.00 46.40  ?  34  LEU A CG  1 
ATOM   208  C CD1 . LEU A 1 34  ? 23.381 -27.652 10.655  1.00 45.63  ?  34  LEU A CD1 1 
ATOM   209  C CD2 . LEU A 1 34  ? 25.269 -26.321 11.693  1.00 54.85  ?  34  LEU A CD2 1 
ATOM   210  N N   . GLY A 1 35  ? 27.738 -24.891 8.483   1.00 59.32  ?  35  GLY A N   1 
ATOM   211  C CA  . GLY A 1 35  ? 28.923 -25.078 7.680   1.00 46.04  ?  35  GLY A CA  1 
ATOM   212  C C   . GLY A 1 35  ? 29.316 -23.872 6.871   1.00 44.98  ?  35  GLY A C   1 
ATOM   213  O O   . GLY A 1 35  ? 30.197 -23.981 6.018   1.00 51.14  ?  35  GLY A O   1 
ATOM   214  N N   . GLU A 1 36  ? 28.704 -22.726 7.106   1.00 40.94  ?  36  GLU A N   1 
ATOM   215  C CA  . GLU A 1 36  ? 29.076 -21.537 6.366   1.00 48.01  ?  36  GLU A CA  1 
ATOM   216  C C   . GLU A 1 36  ? 30.027 -20.663 7.177   1.00 44.73  ?  36  GLU A C   1 
ATOM   217  O O   . GLU A 1 36  ? 29.969 -20.615 8.404   1.00 48.17  ?  36  GLU A O   1 
ATOM   218  C CB  . GLU A 1 36  ? 27.823 -20.770 5.940   1.00 45.88  ?  36  GLU A CB  1 
ATOM   219  C CG  . GLU A 1 36  ? 27.063 -21.609 4.927   1.00 52.82  ?  36  GLU A CG  1 
ATOM   220  C CD  . GLU A 1 36  ? 25.865 -20.945 4.320   1.00 60.18  ?  36  GLU A CD  1 
ATOM   221  O OE1 . GLU A 1 36  ? 25.225 -20.085 4.965   1.00 68.22  ?  36  GLU A OE1 1 
ATOM   222  O OE2 . GLU A 1 36  ? 25.573 -21.290 3.162   1.00 64.07  -1 36  GLU A OE2 1 
ATOM   223  N N   . ASN A 1 37  ? 30.942 -20.020 6.465   1.00 46.13  ?  37  ASN A N   1 
ATOM   224  C CA  . ASN A 1 37  ? 31.875 -19.057 7.035   1.00 48.80  ?  37  ASN A CA  1 
ATOM   225  C C   . ASN A 1 37  ? 31.297 -17.645 6.963   1.00 53.16  ?  37  ASN A C   1 
ATOM   226  O O   . ASN A 1 37  ? 30.784 -17.234 5.921   1.00 53.99  ?  37  ASN A O   1 
ATOM   227  C CB  . ASN A 1 37  ? 33.188 -19.112 6.269   1.00 41.30  ?  37  ASN A CB  1 
ATOM   228  C CG  . ASN A 1 37  ? 34.035 -20.251 6.688   1.00 50.49  ?  37  ASN A CG  1 
ATOM   229  O OD1 . ASN A 1 37  ? 34.080 -20.593 7.873   1.00 56.88  ?  37  ASN A OD1 1 
ATOM   230  N ND2 . ASN A 1 37  ? 34.742 -20.846 5.737   1.00 44.05  ?  37  ASN A ND2 1 
ATOM   231  N N   . LEU A 1 38  ? 31.363 -16.908 8.068   1.00 55.98  ?  38  LEU A N   1 
ATOM   232  C CA  . LEU A 1 38  ? 30.921 -15.512 8.070   1.00 49.25  ?  38  LEU A CA  1 
ATOM   233  C C   . LEU A 1 38  ? 32.125 -14.566 7.983   1.00 45.92  ?  38  LEU A C   1 
ATOM   234  O O   . LEU A 1 38  ? 32.395 -13.734 8.860   1.00 47.11  ?  38  LEU A O   1 
ATOM   235  C CB  . LEU A 1 38  ? 30.056 -15.239 9.305   1.00 47.66  ?  38  LEU A CB  1 
ATOM   236  C CG  . LEU A 1 38  ? 28.952 -16.296 9.411   1.00 48.15  ?  38  LEU A CG  1 
ATOM   237  C CD1 . LEU A 1 38  ? 28.209 -16.259 10.727  1.00 39.03  ?  38  LEU A CD1 1 
ATOM   238  C CD2 . LEU A 1 38  ? 28.005 -16.144 8.271   1.00 45.19  ?  38  LEU A CD2 1 
ATOM   239  N N   . HIS A 1 39  ? 32.861 -14.670 6.891   1.00 39.51  ?  39  HIS A N   1 
ATOM   240  C CA  . HIS A 1 39  ? 34.031 -13.811 6.779   1.00 46.29  ?  39  HIS A CA  1 
ATOM   241  C C   . HIS A 1 39  ? 34.477 -13.789 5.325   1.00 45.45  ?  39  HIS A C   1 
ATOM   242  O O   . HIS A 1 39  ? 33.936 -14.509 4.488   1.00 50.24  ?  39  HIS A O   1 
ATOM   243  C CB  . HIS A 1 39  ? 35.153 -14.237 7.739   1.00 55.42  ?  39  HIS A CB  1 
ATOM   244  C CG  . HIS A 1 39  ? 35.636 -15.649 7.579   1.00 57.11  ?  39  HIS A CG  1 
ATOM   245  N ND1 . HIS A 1 39  ? 35.537 -16.588 8.583   1.00 62.32  ?  39  HIS A ND1 1 
ATOM   246  C CD2 . HIS A 1 39  ? 36.291 -16.260 6.566   1.00 55.56  ?  39  HIS A CD2 1 
ATOM   247  C CE1 . HIS A 1 39  ? 36.078 -17.726 8.180   1.00 53.27  ?  39  HIS A CE1 1 
ATOM   248  N NE2 . HIS A 1 39  ? 36.532 -17.557 6.956   1.00 48.45  ?  39  HIS A NE2 1 
ATOM   249  N N   . PHE A 1 40  ? 35.415 -12.896 5.019   1.00 47.33  ?  40  PHE A N   1 
ATOM   250  C CA  . PHE A 1 40  ? 35.815 -12.670 3.630   1.00 44.89  ?  40  PHE A CA  1 
ATOM   251  C C   . PHE A 1 40  ? 36.599 -13.849 3.102   1.00 47.79  ?  40  PHE A C   1 
ATOM   252  O O   . PHE A 1 40  ? 37.254 -14.574 3.855   1.00 56.27  ?  40  PHE A O   1 
ATOM   253  C CB  . PHE A 1 40  ? 36.688 -11.407 3.494   1.00 53.37  ?  40  PHE A CB  1 
ATOM   254  C CG  . PHE A 1 40  ? 35.920 -10.133 3.630   1.00 54.87  ?  40  PHE A CG  1 
ATOM   255  C CD1 . PHE A 1 40  ? 35.311 -9.563  2.525   1.00 50.69  ?  40  PHE A CD1 1 
ATOM   256  C CD2 . PHE A 1 40  ? 35.768 -9.535  4.863   1.00 43.49  ?  40  PHE A CD2 1 
ATOM   257  C CE1 . PHE A 1 40  ? 34.551 -8.416  2.649   1.00 49.26  ?  40  PHE A CE1 1 
ATOM   258  C CE2 . PHE A 1 40  ? 35.028 -8.406  4.992   1.00 53.43  ?  40  PHE A CE2 1 
ATOM   259  C CZ  . PHE A 1 40  ? 34.415 -7.831  3.884   1.00 50.93  ?  40  PHE A CZ  1 
ATOM   260  N N   . GLY A 1 41  ? 36.551 -14.028 1.790   1.00 49.67  ?  41  GLY A N   1 
ATOM   261  C CA  . GLY A 1 41  ? 37.512 -14.888 1.140   1.00 40.12  ?  41  GLY A CA  1 
ATOM   262  C C   . GLY A 1 41  ? 38.859 -14.200 1.049   1.00 45.23  ?  41  GLY A C   1 
ATOM   263  O O   . GLY A 1 41  ? 38.951 -12.976 1.040   1.00 54.59  ?  41  GLY A O   1 
ATOM   264  N N   . TYR A 1 42  ? 39.919 -14.999 0.995   1.00 45.08  ?  42  TYR A N   1 
ATOM   265  C CA  . TYR A 1 42  ? 41.262 -14.505 0.707   1.00 52.48  ?  42  TYR A CA  1 
ATOM   266  C C   . TYR A 1 42  ? 41.781 -15.136 -0.582  1.00 53.11  ?  42  TYR A C   1 
ATOM   267  O O   . TYR A 1 42  ? 41.808 -16.367 -0.704  1.00 61.61  ?  42  TYR A O   1 
ATOM   268  C CB  . TYR A 1 42  ? 42.221 -14.810 1.863   1.00 47.06  ?  42  TYR A CB  1 
ATOM   269  C CG  . TYR A 1 42  ? 43.601 -14.266 1.659   1.00 46.84  ?  42  TYR A CG  1 
ATOM   270  C CD1 . TYR A 1 42  ? 44.515 -14.936 0.864   1.00 49.31  ?  42  TYR A CD1 1 
ATOM   271  C CD2 . TYR A 1 42  ? 43.990 -13.079 2.252   1.00 49.66  ?  42  TYR A CD2 1 
ATOM   272  C CE1 . TYR A 1 42  ? 45.771 -14.443 0.657   1.00 47.84  ?  42  TYR A CE1 1 
ATOM   273  C CE2 . TYR A 1 42  ? 45.251 -12.581 2.065   1.00 55.99  ?  42  TYR A CE2 1 
ATOM   274  C CZ  . TYR A 1 42  ? 46.140 -13.267 1.255   1.00 54.61  ?  42  TYR A CZ  1 
ATOM   275  O OH  . TYR A 1 42  ? 47.407 -12.787 1.045   1.00 65.06  ?  42  TYR A OH  1 
ATOM   276  N N   . TRP A 1 43  ? 42.243 -14.302 -1.516  1.00 57.04  ?  43  TRP A N   1 
ATOM   277  C CA  . TRP A 1 43  ? 42.797 -14.767 -2.788  1.00 53.48  ?  43  TRP A CA  1 
ATOM   278  C C   . TRP A 1 43  ? 44.174 -14.164 -3.034  1.00 60.41  ?  43  TRP A C   1 
ATOM   279  O O   . TRP A 1 43  ? 44.364 -12.948 -2.901  1.00 61.61  ?  43  TRP A O   1 
ATOM   280  C CB  . TRP A 1 43  ? 41.927 -14.390 -3.948  1.00 42.28  ?  43  TRP A CB  1 
ATOM   281  C CG  . TRP A 1 43  ? 40.546 -14.989 -4.020  1.00 53.80  ?  43  TRP A CG  1 
ATOM   282  C CD1 . TRP A 1 43  ? 40.170 -16.113 -4.713  1.00 50.82  ?  43  TRP A CD1 1 
ATOM   283  C CD2 . TRP A 1 43  ? 39.339 -14.447 -3.453  1.00 52.89  ?  43  TRP A CD2 1 
ATOM   284  N NE1 . TRP A 1 43  ? 38.818 -16.315 -4.583  1.00 52.74  ?  43  TRP A NE1 1 
ATOM   285  C CE2 . TRP A 1 43  ? 38.282 -15.304 -3.825  1.00 49.57  ?  43  TRP A CE2 1 
ATOM   286  C CE3 . TRP A 1 43  ? 39.055 -13.331 -2.660  1.00 51.23  ?  43  TRP A CE3 1 
ATOM   287  C CZ2 . TRP A 1 43  ? 36.965 -15.074 -3.434  1.00 51.28  ?  43  TRP A CZ2 1 
ATOM   288  C CZ3 . TRP A 1 43  ? 37.744 -13.107 -2.263  1.00 54.14  ?  43  TRP A CZ3 1 
ATOM   289  C CH2 . TRP A 1 43  ? 36.716 -13.975 -2.652  1.00 55.64  ?  43  TRP A CH2 1 
ATOM   290  N N   . ASP A 1 44  ? 45.109 -15.016 -3.477  1.00 65.11  ?  44  ASP A N   1 
ATOM   291  C CA  . ASP A 1 44  ? 46.488 -14.603 -3.737  1.00 57.71  ?  44  ASP A CA  1 
ATOM   292  C C   . ASP A 1 44  ? 46.615 -13.640 -4.919  1.00 64.11  ?  44  ASP A C   1 
ATOM   293  O O   . ASP A 1 44  ? 47.544 -12.828 -4.947  1.00 75.38  ?  44  ASP A O   1 
ATOM   294  C CB  . ASP A 1 44  ? 47.342 -15.836 -3.973  1.00 58.98  ?  44  ASP A CB  1 
ATOM   295  C CG  . ASP A 1 44  ? 47.256 -16.819 -2.832  1.00 72.44  ?  44  ASP A CG  1 
ATOM   296  O OD1 . ASP A 1 44  ? 47.786 -16.516 -1.744  1.00 77.73  ?  44  ASP A OD1 1 
ATOM   297  O OD2 . ASP A 1 44  ? 46.611 -17.881 -3.009  1.00 78.07  -1 44  ASP A OD2 1 
ATOM   298  N N   . SER A 1 45  ? 45.721 -13.683 -5.896  1.00 68.88  ?  45  SER A N   1 
ATOM   299  C CA  . SER A 1 45  ? 45.809 -12.726 -6.985  1.00 70.91  ?  45  SER A CA  1 
ATOM   300  C C   . SER A 1 45  ? 44.400 -12.348 -7.423  1.00 70.88  ?  45  SER A C   1 
ATOM   301  O O   . SER A 1 45  ? 43.465 -13.127 -7.224  1.00 70.38  ?  45  SER A O   1 
ATOM   302  C CB  . SER A 1 45  ? 46.590 -13.283 -8.179  1.00 72.27  ?  45  SER A CB  1 
ATOM   303  O OG  . SER A 1 45  ? 45.722 -13.990 -9.034  1.00 78.54  ?  45  SER A OG  1 
ATOM   304  N N   . PRO A 1 46  ? 44.235 -11.172 -8.041  1.00 64.71  ?  46  PRO A N   1 
ATOM   305  C CA  . PRO A 1 46  ? 42.874 -10.641 -8.262  1.00 65.00  ?  46  PRO A CA  1 
ATOM   306  C C   . PRO A 1 46  ? 42.045 -11.451 -9.227  1.00 73.33  ?  46  PRO A C   1 
ATOM   307  O O   . PRO A 1 46  ? 40.807 -11.365 -9.191  1.00 75.48  ?  46  PRO A O   1 
ATOM   308  C CB  . PRO A 1 46  ? 43.130 -9.238  -8.828  1.00 62.66  ?  46  PRO A CB  1 
ATOM   309  C CG  . PRO A 1 46  ? 44.540 -8.933  -8.504  1.00 62.53  ?  46  PRO A CG  1 
ATOM   310  C CD  . PRO A 1 46  ? 45.268 -10.230 -8.492  1.00 61.24  ?  46  PRO A CD  1 
ATOM   311  N N   . ASP A 1 47  ? 42.679 -12.220 -10.103 1.00 75.44  ?  47  ASP A N   1 
ATOM   312  C CA  . ASP A 1 47  ? 41.936 -12.901 -11.149 1.00 88.14  ?  47  ASP A CA  1 
ATOM   313  C C   . ASP A 1 47  ? 41.726 -14.386 -10.878 1.00 95.83  ?  47  ASP A C   1 
ATOM   314  O O   . ASP A 1 47  ? 40.844 -14.979 -11.512 1.00 112.81 ?  47  ASP A O   1 
ATOM   315  C CB  . ASP A 1 47  ? 42.627 -12.700 -12.512 1.00 89.14  ?  47  ASP A CB  1 
ATOM   316  C CG  . ASP A 1 47  ? 44.113 -13.017 -12.472 1.00 89.70  ?  47  ASP A CG  1 
ATOM   317  O OD1 . ASP A 1 47  ? 44.552 -13.762 -11.564 1.00 88.62  ?  47  ASP A OD1 1 
ATOM   318  O OD2 . ASP A 1 47  ? 44.847 -12.500 -13.341 1.00 90.63  -1 47  ASP A OD2 1 
ATOM   319  N N   . SER A 1 48  ? 42.485 -14.994 -9.955  1.00 87.35  ?  48  SER A N   1 
ATOM   320  C CA  . SER A 1 48  ? 42.283 -16.403 -9.627  1.00 80.89  ?  48  SER A CA  1 
ATOM   321  C C   . SER A 1 48  ? 40.805 -16.647 -9.392  1.00 70.94  ?  48  SER A C   1 
ATOM   322  O O   . SER A 1 48  ? 40.127 -15.818 -8.784  1.00 68.35  ?  48  SER A O   1 
ATOM   323  C CB  . SER A 1 48  ? 43.074 -16.809 -8.382  1.00 77.55  ?  48  SER A CB  1 
ATOM   324  O OG  . SER A 1 48  ? 42.256 -16.765 -7.213  1.00 68.63  ?  48  SER A OG  1 
ATOM   325  N N   . GLN A 1 49  ? 40.295 -17.765 -9.913  1.00 73.19  ?  49  GLN A N   1 
ATOM   326  C CA  . GLN A 1 49  ? 38.861 -18.037 -9.860  1.00 81.54  ?  49  GLN A CA  1 
ATOM   327  C C   . GLN A 1 49  ? 38.492 -19.070 -8.807  1.00 71.70  ?  49  GLN A C   1 
ATOM   328  O O   . GLN A 1 49  ? 37.431 -19.695 -8.915  1.00 71.59  ?  49  GLN A O   1 
ATOM   329  C CB  . GLN A 1 49  ? 38.328 -18.478 -11.232 1.00 87.96  ?  49  GLN A CB  1 
ATOM   330  C CG  . GLN A 1 49  ? 37.774 -17.331 -12.086 1.00 91.14  ?  49  GLN A CG  1 
ATOM   331  C CD  . GLN A 1 49  ? 38.769 -16.192 -12.245 1.00 102.19 ?  49  GLN A CD  1 
ATOM   332  O OE1 . GLN A 1 49  ? 39.970 -16.431 -12.361 1.00 116.56 ?  49  GLN A OE1 1 
ATOM   333  N NE2 . GLN A 1 49  ? 38.282 -14.950 -12.213 1.00 95.09  ?  49  GLN A NE2 1 
ATOM   334  N N   . VAL A 1 50  ? 39.361 -19.292 -7.827  1.00 69.78  ?  50  VAL A N   1 
ATOM   335  C CA  . VAL A 1 50  ? 39.059 -20.103 -6.650  1.00 58.63  ?  50  VAL A CA  1 
ATOM   336  C C   . VAL A 1 50  ? 37.729 -19.626 -6.076  1.00 59.06  ?  50  VAL A C   1 
ATOM   337  O O   . VAL A 1 50  ? 37.536 -18.421 -5.852  1.00 60.98  ?  50  VAL A O   1 
ATOM   338  C CB  . VAL A 1 50  ? 40.196 -20.021 -5.623  1.00 55.82  ?  50  VAL A CB  1 
ATOM   339  C CG1 . VAL A 1 50  ? 39.801 -20.694 -4.349  1.00 53.68  ?  50  VAL A CG1 1 
ATOM   340  C CG2 . VAL A 1 50  ? 41.462 -20.648 -6.177  1.00 46.69  ?  50  VAL A CG2 1 
ATOM   341  N N   . PRO A 1 51  ? 36.773 -20.517 -5.865  1.00 58.04  ?  51  PRO A N   1 
ATOM   342  C CA  . PRO A 1 51  ? 35.426 -20.079 -5.468  1.00 57.62  ?  51  PRO A CA  1 
ATOM   343  C C   . PRO A 1 51  ? 35.403 -19.538 -4.043  1.00 56.17  ?  51  PRO A C   1 
ATOM   344  O O   . PRO A 1 51  ? 36.335 -19.708 -3.250  1.00 50.46  ?  51  PRO A O   1 
ATOM   345  C CB  . PRO A 1 51  ? 34.575 -21.350 -5.600  1.00 51.65  ?  51  PRO A CB  1 
ATOM   346  C CG  . PRO A 1 51  ? 35.416 -22.283 -6.418  1.00 53.44  ?  51  PRO A CG  1 
ATOM   347  C CD  . PRO A 1 51  ? 36.838 -21.967 -6.091  1.00 51.76  ?  51  PRO A CD  1 
ATOM   348  N N   . LEU A 1 52  ? 34.274 -18.898 -3.732  1.00 58.35  ?  52  LEU A N   1 
ATOM   349  C CA  . LEU A 1 52  ? 34.117 -18.183 -2.472  1.00 52.62  ?  52  LEU A CA  1 
ATOM   350  C C   . LEU A 1 52  ? 34.349 -19.099 -1.276  1.00 53.31  ?  52  LEU A C   1 
ATOM   351  O O   . LEU A 1 52  ? 35.108 -18.760 -0.368  1.00 53.15  ?  52  LEU A O   1 
ATOM   352  C CB  . LEU A 1 52  ? 32.730 -17.542 -2.409  1.00 50.73  ?  52  LEU A CB  1 
ATOM   353  C CG  . LEU A 1 52  ? 32.508 -16.743 -1.133  1.00 49.81  ?  52  LEU A CG  1 
ATOM   354  C CD1 . LEU A 1 52  ? 33.575 -15.639 -0.972  1.00 46.98  ?  52  LEU A CD1 1 
ATOM   355  C CD2 . LEU A 1 52  ? 31.088 -16.205 -1.072  1.00 39.01  ?  52  LEU A CD2 1 
ATOM   356  N N   . ALA A 1 53  ? 33.748 -20.283 -1.278  1.00 54.38  ?  53  ALA A N   1 
ATOM   357  C CA  . ALA A 1 53  ? 33.840 -21.153 -0.104  1.00 57.85  ?  53  ALA A CA  1 
ATOM   358  C C   . ALA A 1 53  ? 35.289 -21.528 0.225   1.00 58.71  ?  53  ALA A C   1 
ATOM   359  O O   . ALA A 1 53  ? 35.695 -21.489 1.392   1.00 67.20  ?  53  ALA A O   1 
ATOM   360  C CB  . ALA A 1 53  ? 32.980 -22.409 -0.305  1.00 50.16  ?  53  ALA A CB  1 
ATOM   361  N N   . GLU A 1 54  ? 36.088 -21.887 -0.781  1.00 52.30  ?  54  GLU A N   1 
ATOM   362  C CA  . GLU A 1 54  ? 37.462 -22.279 -0.490  1.00 50.09  ?  54  GLU A CA  1 
ATOM   363  C C   . GLU A 1 54  ? 38.321 -21.077 -0.159  1.00 54.74  ?  54  GLU A C   1 
ATOM   364  O O   . GLU A 1 54  ? 39.312 -21.208 0.573   1.00 53.94  ?  54  GLU A O   1 
ATOM   365  C CB  . GLU A 1 54  ? 38.064 -23.040 -1.669  1.00 56.61  ?  54  GLU A CB  1 
ATOM   366  C CG  . GLU A 1 54  ? 37.055 -23.989 -2.290  1.00 70.53  ?  54  GLU A CG  1 
ATOM   367  C CD  . GLU A 1 54  ? 37.539 -24.636 -3.573  1.00 83.18  ?  54  GLU A CD  1 
ATOM   368  O OE1 . GLU A 1 54  ? 38.765 -24.558 -3.893  1.00 81.92  ?  54  GLU A OE1 1 
ATOM   369  O OE2 . GLU A 1 54  ? 36.662 -25.208 -4.266  1.00 82.35  -1 54  GLU A OE2 1 
ATOM   370  N N   . ALA A 1 55  ? 37.956 -19.906 -0.686  1.00 48.06  ?  55  ALA A N   1 
ATOM   371  C CA  . ALA A 1 55  ? 38.672 -18.697 -0.329  1.00 46.61  ?  55  ALA A CA  1 
ATOM   372  C C   . ALA A 1 55  ? 38.414 -18.346 1.128   1.00 48.29  ?  55  ALA A C   1 
ATOM   373  O O   . ALA A 1 55  ? 39.317 -17.894 1.847   1.00 49.58  ?  55  ALA A O   1 
ATOM   374  C CB  . ALA A 1 55  ? 38.245 -17.564 -1.260  1.00 52.22  ?  55  ALA A CB  1 
ATOM   375  N N   . THR A 1 56  ? 37.187 -18.579 1.579   1.00 49.63  ?  56  THR A N   1 
ATOM   376  C CA  . THR A 1 56  ? 36.821 -18.318 2.960   1.00 50.46  ?  56  THR A CA  1 
ATOM   377  C C   . THR A 1 56  ? 37.560 -19.257 3.894   1.00 46.32  ?  56  THR A C   1 
ATOM   378  O O   . THR A 1 56  ? 38.011 -18.849 4.973   1.00 49.25  ?  56  THR A O   1 
ATOM   379  C CB  . THR A 1 56  ? 35.310 -18.485 3.154   1.00 60.82  ?  56  THR A CB  1 
ATOM   380  O OG1 . THR A 1 56  ? 34.620 -18.039 2.001   1.00 71.29  ?  56  THR A OG1 1 
ATOM   381  C CG2 . THR A 1 56  ? 34.860 -17.551 4.217   1.00 79.60  ?  56  THR A CG2 1 
ATOM   382  N N   . ASP A 1 57  ? 37.677 -20.529 3.512   1.00 45.41  ?  57  ASP A N   1 
ATOM   383  C CA  . ASP A 1 57  ? 38.470 -21.426 4.339   1.00 46.13  ?  57  ASP A CA  1 
ATOM   384  C C   . ASP A 1 57  ? 39.937 -21.041 4.277   1.00 45.06  ?  57  ASP A C   1 
ATOM   385  O O   . ASP A 1 57  ? 40.660 -21.203 5.262   1.00 47.38  ?  57  ASP A O   1 
ATOM   386  C CB  . ASP A 1 57  ? 38.237 -22.881 3.919   1.00 51.52  ?  57  ASP A CB  1 
ATOM   387  C CG  . ASP A 1 57  ? 36.911 -23.436 4.444   1.00 64.87  ?  57  ASP A CG  1 
ATOM   388  O OD1 . ASP A 1 57  ? 36.431 -22.982 5.512   1.00 66.59  ?  57  ASP A OD1 1 
ATOM   389  O OD2 . ASP A 1 57  ? 36.329 -24.318 3.783   1.00 66.99  -1 57  ASP A OD2 1 
ATOM   390  N N   . ARG A 1 58  ? 40.373 -20.479 3.148   1.00 46.15  ?  58  ARG A N   1 
ATOM   391  C CA  . ARG A 1 58  ? 41.746 -20.009 3.010   1.00 46.71  ?  58  ARG A CA  1 
ATOM   392  C C   . ARG A 1 58  ? 42.114 -18.999 4.100   1.00 49.02  ?  58  ARG A C   1 
ATOM   393  O O   . ARG A 1 58  ? 43.184 -19.089 4.714   1.00 50.33  ?  58  ARG A O   1 
ATOM   394  C CB  . ARG A 1 58  ? 41.922 -19.406 1.619   1.00 45.63  ?  58  ARG A CB  1 
ATOM   395  C CG  . ARG A 1 58  ? 43.261 -18.756 1.396   1.00 51.17  ?  58  ARG A CG  1 
ATOM   396  C CD  . ARG A 1 58  ? 44.382 -19.764 1.420   1.00 45.17  ?  58  ARG A CD  1 
ATOM   397  N NE  . ARG A 1 58  ? 45.679 -19.101 1.567   1.00 62.62  ?  58  ARG A NE  1 
ATOM   398  C CZ  . ARG A 1 58  ? 46.399 -18.587 0.566   1.00 72.31  ?  58  ARG A CZ  1 
ATOM   399  N NH1 . ARG A 1 58  ? 45.959 -18.646 -0.691  1.00 74.34  ?  58  ARG A NH1 1 
ATOM   400  N NH2 . ARG A 1 58  ? 47.568 -17.999 0.821   1.00 75.82  ?  58  ARG A NH2 1 
ATOM   401  N N   . LEU A 1 59  ? 41.238 -18.025 4.355   1.00 45.62  ?  59  LEU A N   1 
ATOM   402  C CA  . LEU A 1 59  ? 41.500 -17.084 5.434   1.00 48.74  ?  59  LEU A CA  1 
ATOM   403  C C   . LEU A 1 59  ? 41.582 -17.801 6.781   1.00 51.88  ?  59  LEU A C   1 
ATOM   404  O O   . LEU A 1 59  ? 42.482 -17.521 7.595   1.00 46.52  ?  59  LEU A O   1 
ATOM   405  C CB  . LEU A 1 59  ? 40.422 -16.003 5.450   1.00 43.45  ?  59  LEU A CB  1 
ATOM   406  C CG  . LEU A 1 59  ? 40.644 -14.846 6.423   1.00 48.13  ?  59  LEU A CG  1 
ATOM   407  C CD1 . LEU A 1 59  ? 41.933 -14.142 6.100   1.00 44.31  ?  59  LEU A CD1 1 
ATOM   408  C CD2 . LEU A 1 59  ? 39.461 -13.881 6.390   1.00 46.38  ?  59  LEU A CD2 1 
ATOM   409  N N   . THR A 1 60  ? 40.659 -18.737 7.035   1.00 44.40  ?  60  THR A N   1 
ATOM   410  C CA  . THR A 1 60  ? 40.688 -19.477 8.297   1.00 46.55  ?  60  THR A CA  1 
ATOM   411  C C   . THR A 1 60  ? 42.038 -20.162 8.502   1.00 54.64  ?  60  THR A C   1 
ATOM   412  O O   . THR A 1 60  ? 42.632 -20.082 9.591   1.00 49.88  ?  60  THR A O   1 
ATOM   413  C CB  . THR A 1 60  ? 39.574 -20.520 8.337   1.00 42.25  ?  60  THR A CB  1 
ATOM   414  O OG1 . THR A 1 60  ? 38.292 -19.913 8.121   1.00 42.25  ?  60  THR A OG1 1 
ATOM   415  C CG2 . THR A 1 60  ? 39.593 -21.227 9.651   1.00 45.36  ?  60  THR A CG2 1 
ATOM   416  N N   . ASP A 1 61  ? 42.551 -20.834 7.454   1.00 50.06  ?  61  ASP A N   1 
ATOM   417  C CA  . ASP A 1 61  ? 43.773 -21.624 7.620   1.00 47.31  ?  61  ASP A CA  1 
ATOM   418  C C   . ASP A 1 61  ? 44.988 -20.735 7.823   1.00 47.33  ?  61  ASP A C   1 
ATOM   419  O O   . ASP A 1 61  ? 45.870 -21.063 8.628   1.00 43.96  ?  61  ASP A O   1 
ATOM   420  C CB  . ASP A 1 61  ? 44.010 -22.552 6.432   1.00 40.57  ?  61  ASP A CB  1 
ATOM   421  C CG  . ASP A 1 61  ? 42.946 -23.601 6.296   1.00 46.08  ?  61  ASP A CG  1 
ATOM   422  O OD1 . ASP A 1 61  ? 42.164 -23.757 7.238   1.00 49.39  ?  61  ASP A OD1 1 
ATOM   423  O OD2 . ASP A 1 61  ? 42.908 -24.302 5.268   1.00 51.03  -1 61  ASP A OD2 1 
ATOM   424  N N   . MET A 1 62  ? 45.039 -19.604 7.106   1.00 46.34  ?  62  MET A N   1 
ATOM   425  C CA  . MET A 1 62  ? 46.118 -18.633 7.274   1.00 44.20  ?  62  MET A CA  1 
ATOM   426  C C   . MET A 1 62  ? 46.126 -18.035 8.675   1.00 44.18  ?  62  MET A C   1 
ATOM   427  O O   . MET A 1 62  ? 47.190 -17.901 9.282   1.00 50.74  ?  62  MET A O   1 
ATOM   428  C CB  . MET A 1 62  ? 45.998 -17.551 6.208   1.00 40.21  ?  62  MET A CB  1 
ATOM   429  C CG  . MET A 1 62  ? 46.511 -16.186 6.593   1.00 58.84  ?  62  MET A CG  1 
ATOM   430  S SD  . MET A 1 62  ? 46.414 -15.065 5.160   1.00 75.78  ?  62  MET A SD  1 
ATOM   431  C CE  . MET A 1 62  ? 45.024 -15.791 4.319   1.00 57.50  ?  62  MET A CE  1 
ATOM   432  N N   . MET A 1 63  ? 44.955 -17.714 9.232   1.00 44.64  ?  63  MET A N   1 
ATOM   433  C CA  . MET A 1 63  ? 44.937 -17.213 10.607  1.00 49.86  ?  63  MET A CA  1 
ATOM   434  C C   . MET A 1 63  ? 45.241 -18.326 11.613  1.00 50.51  ?  63  MET A C   1 
ATOM   435  O O   . MET A 1 63  ? 45.960 -18.104 12.593  1.00 43.04  ?  63  MET A O   1 
ATOM   436  C CB  . MET A 1 63  ? 43.597 -16.549 10.907  1.00 46.58  ?  63  MET A CB  1 
ATOM   437  C CG  . MET A 1 63  ? 43.279 -15.395 9.965   1.00 47.06  ?  63  MET A CG  1 
ATOM   438  S SD  . MET A 1 63  ? 41.687 -14.621 10.269  1.00 57.94  ?  63  MET A SD  1 
ATOM   439  C CE  . MET A 1 63  ? 41.931 -14.067 11.979  1.00 38.38  ?  63  MET A CE  1 
ATOM   440  N N   . ALA A 1 64  ? 44.742 -19.540 11.368  1.00 49.85  ?  64  ALA A N   1 
ATOM   441  C CA  . ALA A 1 64  ? 44.971 -20.615 12.328  1.00 52.04  ?  64  ALA A CA  1 
ATOM   442  C C   . ALA A 1 64  ? 46.451 -20.975 12.431  1.00 52.80  ?  64  ALA A C   1 
ATOM   443  O O   . ALA A 1 64  ? 46.941 -21.294 13.523  1.00 56.66  ?  64  ALA A O   1 
ATOM   444  C CB  . ALA A 1 64  ? 44.142 -21.846 11.963  1.00 31.51  ?  64  ALA A CB  1 
ATOM   445  N N   . GLU A 1 65  ? 47.187 -20.918 11.318  1.00 41.58  ?  65  GLU A N   1 
ATOM   446  C CA  . GLU A 1 65  ? 48.607 -21.249 11.416  1.00 48.25  ?  65  GLU A CA  1 
ATOM   447  C C   . GLU A 1 65  ? 49.371 -20.199 12.221  1.00 52.97  ?  65  GLU A C   1 
ATOM   448  O O   . GLU A 1 65  ? 50.305 -20.540 12.955  1.00 54.45  ?  65  GLU A O   1 
ATOM   449  C CB  . GLU A 1 65  ? 49.215 -21.417 10.025  1.00 49.97  ?  65  GLU A CB  1 
ATOM   450  C CG  . GLU A 1 65  ? 49.687 -20.137 9.397   1.00 70.57  ?  65  GLU A CG  1 
ATOM   451  C CD  . GLU A 1 65  ? 50.622 -20.389 8.230   1.00 84.12  ?  65  GLU A CD  1 
ATOM   452  O OE1 . GLU A 1 65  ? 50.612 -21.530 7.718   1.00 79.06  ?  65  GLU A OE1 1 
ATOM   453  O OE2 . GLU A 1 65  ? 51.368 -19.450 7.843   1.00 91.28  -1 65  GLU A OE2 1 
ATOM   454  N N   . ARG A 1 66  ? 48.951 -18.933 12.150  1.00 51.87  ?  66  ARG A N   1 
ATOM   455  C CA  . ARG A 1 66  ? 49.575 -17.908 12.967  1.00 48.18  ?  66  ARG A CA  1 
ATOM   456  C C   . ARG A 1 66  ? 49.350 -18.134 14.460  1.00 51.10  ?  66  ARG A C   1 
ATOM   457  O O   . ARG A 1 66  ? 50.162 -17.674 15.265  1.00 59.34  ?  66  ARG A O   1 
ATOM   458  C CB  . ARG A 1 66  ? 49.067 -16.538 12.523  1.00 45.69  ?  66  ARG A CB  1 
ATOM   459  C CG  . ARG A 1 66  ? 49.613 -16.155 11.161  1.00 45.54  ?  66  ARG A CG  1 
ATOM   460  C CD  . ARG A 1 66  ? 48.918 -14.976 10.586  1.00 41.90  ?  66  ARG A CD  1 
ATOM   461  N NE  . ARG A 1 66  ? 49.788 -14.302 9.648   1.00 49.66  ?  66  ARG A NE  1 
ATOM   462  C CZ  . ARG A 1 66  ? 49.885 -14.600 8.353   1.00 51.67  ?  66  ARG A CZ  1 
ATOM   463  N NH1 . ARG A 1 66  ? 49.136 -15.572 7.828   1.00 41.69  ?  66  ARG A NH1 1 
ATOM   464  N NH2 . ARG A 1 66  ? 50.709 -13.897 7.572   1.00 42.33  ?  66  ARG A NH2 1 
ATOM   465  N N   . LEU A 1 67  ? 48.282 -18.839 14.856  1.00 55.10  ?  67  LEU A N   1 
ATOM   466  C CA  . LEU A 1 67  ? 48.134 -19.220 16.266  1.00 59.56  ?  67  LEU A CA  1 
ATOM   467  C C   . LEU A 1 67  ? 49.297 -20.083 16.753  1.00 56.63  ?  67  LEU A C   1 
ATOM   468  O O   . LEU A 1 67  ? 49.592 -20.100 17.946  1.00 56.22  ?  67  LEU A O   1 
ATOM   469  C CB  . LEU A 1 67  ? 46.822 -19.980 16.493  1.00 53.49  ?  67  LEU A CB  1 
ATOM   470  C CG  . LEU A 1 67  ? 45.471 -19.323 16.181  1.00 54.96  ?  67  LEU A CG  1 
ATOM   471  C CD1 . LEU A 1 67  ? 44.326 -20.326 16.292  1.00 45.06  ?  67  LEU A CD1 1 
ATOM   472  C CD2 . LEU A 1 67  ? 45.225 -18.116 17.078  1.00 49.19  ?  67  LEU A CD2 1 
ATOM   473  N N   . ARG A 1 68  ? 49.959 -20.804 15.861  1.00 53.41  ?  68  ARG A N   1 
ATOM   474  C CA  . ARG A 1 68  ? 51.055 -21.676 16.242  1.00 52.93  ?  68  ARG A CA  1 
ATOM   475  C C   . ARG A 1 68  ? 50.596 -22.675 17.297  1.00 63.63  ?  68  ARG A C   1 
ATOM   476  O O   . ARG A 1 68  ? 51.076 -22.678 18.429  1.00 72.64  ?  68  ARG A O   1 
ATOM   477  C CB  . ARG A 1 68  ? 52.257 -20.855 16.716  1.00 54.14  ?  68  ARG A CB  1 
ATOM   478  C CG  . ARG A 1 68  ? 52.777 -19.941 15.588  1.00 60.30  ?  68  ARG A CG  1 
ATOM   479  C CD  . ARG A 1 68  ? 54.153 -19.366 15.825  1.00 65.68  ?  68  ARG A CD  1 
ATOM   480  N NE  . ARG A 1 68  ? 54.423 -18.292 14.863  1.00 87.60  ?  68  ARG A NE  1 
ATOM   481  C CZ  . ARG A 1 68  ? 55.523 -17.539 14.871  1.00 88.94  ?  68  ARG A CZ  1 
ATOM   482  N NH1 . ARG A 1 68  ? 56.447 -17.754 15.796  1.00 91.46  ?  68  ARG A NH1 1 
ATOM   483  N NH2 . ARG A 1 68  ? 55.697 -16.577 13.967  1.00 79.84  ?  68  ARG A NH2 1 
ATOM   484  N N   . ILE A 1 69  ? 49.645 -23.537 16.896  1.00 60.22  ?  69  ILE A N   1 
ATOM   485  C CA  . ILE A 1 69  ? 49.002 -24.490 17.794  1.00 52.10  ?  69  ILE A CA  1 
ATOM   486  C C   . ILE A 1 69  ? 48.991 -25.882 17.176  1.00 53.23  ?  69  ILE A C   1 
ATOM   487  O O   . ILE A 1 69  ? 49.315 -26.071 16.000  1.00 53.04  ?  69  ILE A O   1 
ATOM   488  C CB  . ILE A 1 69  ? 47.566 -24.084 18.145  1.00 49.24  ?  69  ILE A CB  1 
ATOM   489  C CG1 . ILE A 1 69  ? 46.788 -23.913 16.850  1.00 49.37  ?  69  ILE A CG1 1 
ATOM   490  C CG2 . ILE A 1 69  ? 47.596 -22.870 19.049  1.00 47.14  ?  69  ILE A CG2 1 
ATOM   491  C CD1 . ILE A 1 69  ? 45.359 -24.249 16.943  1.00 58.84  ?  69  ILE A CD1 1 
ATOM   492  N N   . GLY A 1 70  ? 48.568 -26.848 17.988  1.00 43.56  ?  70  GLY A N   1 
ATOM   493  C CA  . GLY A 1 70  ? 48.599 -28.246 17.618  1.00 45.95  ?  70  GLY A CA  1 
ATOM   494  C C   . GLY A 1 70  ? 47.697 -29.097 18.508  1.00 60.51  ?  70  GLY A C   1 
ATOM   495  O O   . GLY A 1 70  ? 46.820 -28.591 19.214  1.00 61.23  ?  70  GLY A O   1 
ATOM   496  N N   . ALA A 1 71  ? 47.934 -30.410 18.483  1.00 61.85  ?  71  ALA A N   1 
ATOM   497  C CA  . ALA A 1 71  ? 47.078 -31.329 19.229  1.00 54.14  ?  71  ALA A CA  1 
ATOM   498  C C   . ALA A 1 71  ? 47.116 -31.017 20.714  1.00 58.49  ?  71  ALA A C   1 
ATOM   499  O O   . ALA A 1 71  ? 48.167 -31.099 21.346  1.00 76.08  ?  71  ALA A O   1 
ATOM   500  C CB  . ALA A 1 71  ? 47.518 -32.757 18.986  1.00 41.54  ?  71  ALA A CB  1 
ATOM   501  N N   . GLY A 1 72  ? 45.985 -30.641 21.277  1.00 54.43  ?  72  GLY A N   1 
ATOM   502  C CA  . GLY A 1 72  ? 45.964 -30.354 22.689  1.00 55.09  ?  72  GLY A CA  1 
ATOM   503  C C   . GLY A 1 72  ? 46.188 -28.906 23.055  1.00 61.97  ?  72  GLY A C   1 
ATOM   504  O O   . GLY A 1 72  ? 46.245 -28.588 24.246  1.00 62.00  ?  72  GLY A O   1 
ATOM   505  N N   . SER A 1 73  ? 46.331 -28.017 22.084  1.00 58.36  ?  73  SER A N   1 
ATOM   506  C CA  . SER A 1 73  ? 46.263 -26.606 22.400  1.00 50.42  ?  73  SER A CA  1 
ATOM   507  C C   . SER A 1 73  ? 44.839 -26.258 22.801  1.00 57.04  ?  73  SER A C   1 
ATOM   508  O O   . SER A 1 73  ? 43.879 -26.837 22.288  1.00 60.49  ?  73  SER A O   1 
ATOM   509  C CB  . SER A 1 73  ? 46.701 -25.783 21.200  1.00 50.01  ?  73  SER A CB  1 
ATOM   510  O OG  . SER A 1 73  ? 47.818 -26.401 20.586  1.00 53.87  ?  73  SER A OG  1 
ATOM   511  N N   . ARG A 1 74  ? 44.687 -25.314 23.727  1.00 50.58  ?  74  ARG A N   1 
ATOM   512  C CA  . ARG A 1 74  ? 43.360 -24.792 24.017  1.00 51.46  ?  74  ARG A CA  1 
ATOM   513  C C   . ARG A 1 74  ? 43.209 -23.443 23.336  1.00 52.38  ?  74  ARG A C   1 
ATOM   514  O O   . ARG A 1 74  ? 43.988 -22.517 23.598  1.00 58.23  ?  74  ARG A O   1 
ATOM   515  C CB  . ARG A 1 74  ? 43.087 -24.693 25.519  1.00 57.94  ?  74  ARG A CB  1 
ATOM   516  C CG  . ARG A 1 74  ? 43.341 -25.992 26.291  1.00 72.77  ?  74  ARG A CG  1 
ATOM   517  C CD  . ARG A 1 74  ? 42.105 -26.364 27.171  1.00 94.10  ?  74  ARG A CD  1 
ATOM   518  N NE  . ARG A 1 74  ? 42.226 -25.825 28.532  1.00 104.65 ?  74  ARG A NE  1 
ATOM   519  C CZ  . ARG A 1 74  ? 41.303 -25.095 29.182  1.00 101.92 ?  74  ARG A CZ  1 
ATOM   520  N NH1 . ARG A 1 74  ? 40.123 -24.816 28.616  1.00 96.05  ?  74  ARG A NH1 1 
ATOM   521  N NH2 . ARG A 1 74  ? 41.555 -24.637 30.421  1.00 90.25  ?  74  ARG A NH2 1 
ATOM   522  N N   . VAL A 1 75  ? 42.209 -23.346 22.463  1.00 48.73  ?  75  VAL A N   1 
ATOM   523  C CA  . VAL A 1 75  ? 42.011 -22.204 21.584  1.00 52.60  ?  75  VAL A CA  1 
ATOM   524  C C   . VAL A 1 75  ? 40.673 -21.569 21.929  1.00 53.99  ?  75  VAL A C   1 
ATOM   525  O O   . VAL A 1 75  ? 39.656 -22.267 22.011  1.00 54.86  ?  75  VAL A O   1 
ATOM   526  C CB  . VAL A 1 75  ? 42.041 -22.619 20.094  1.00 49.65  ?  75  VAL A CB  1 
ATOM   527  C CG1 . VAL A 1 75  ? 41.628 -21.448 19.196  1.00 42.92  ?  75  VAL A CG1 1 
ATOM   528  C CG2 . VAL A 1 75  ? 43.404 -23.139 19.701  1.00 38.56  ?  75  VAL A CG2 1 
ATOM   529  N N   . LEU A 1 76  ? 40.664 -20.254 22.084  1.00 51.60  ?  76  LEU A N   1 
ATOM   530  C CA  . LEU A 1 76  ? 39.442 -19.510 22.324  1.00 53.08  ?  76  LEU A CA  1 
ATOM   531  C C   . LEU A 1 76  ? 38.982 -18.922 21.002  1.00 50.82  ?  76  LEU A C   1 
ATOM   532  O O   . LEU A 1 76  ? 39.711 -18.142 20.386  1.00 54.98  ?  76  LEU A O   1 
ATOM   533  C CB  . LEU A 1 76  ? 39.673 -18.415 23.368  1.00 54.08  ?  76  LEU A CB  1 
ATOM   534  C CG  . LEU A 1 76  ? 38.570 -17.357 23.502  1.00 52.41  ?  76  LEU A CG  1 
ATOM   535  C CD1 . LEU A 1 76  ? 37.191 -17.980 23.725  1.00 43.08  ?  76  LEU A CD1 1 
ATOM   536  C CD2 . LEU A 1 76  ? 38.923 -16.365 24.616  1.00 43.89  ?  76  LEU A CD2 1 
ATOM   537  N N   . ASP A 1 77  ? 37.780 -19.305 20.570  1.00 47.07  ?  77  ASP A N   1 
ATOM   538  C CA  . ASP A 1 77  ? 37.175 -18.830 19.322  1.00 48.57  ?  77  ASP A CA  1 
ATOM   539  C C   . ASP A 1 77  ? 36.320 -17.636 19.720  1.00 51.98  ?  77  ASP A C   1 
ATOM   540  O O   . ASP A 1 77  ? 35.128 -17.752 20.010  1.00 54.62  ?  77  ASP A O   1 
ATOM   541  C CB  . ASP A 1 77  ? 36.392 -19.956 18.642  1.00 46.54  ?  77  ASP A CB  1 
ATOM   542  C CG  . ASP A 1 77  ? 35.733 -19.545 17.312  1.00 42.97  ?  77  ASP A CG  1 
ATOM   543  O OD1 . ASP A 1 77  ? 35.972 -18.426 16.824  1.00 47.79  ?  77  ASP A OD1 1 
ATOM   544  O OD2 . ASP A 1 77  ? 34.952 -20.357 16.750  1.00 48.53  -1 77  ASP A OD2 1 
ATOM   545  N N   . LEU A 1 78  ? 36.965 -16.471 19.764  1.00 52.53  ?  78  LEU A N   1 
ATOM   546  C CA  . LEU A 1 78  ? 36.385 -15.250 20.318  1.00 47.83  ?  78  LEU A CA  1 
ATOM   547  C C   . LEU A 1 78  ? 35.397 -14.655 19.338  1.00 48.54  ?  78  LEU A C   1 
ATOM   548  O O   . LEU A 1 78  ? 35.707 -13.736 18.587  1.00 60.09  ?  78  LEU A O   1 
ATOM   549  C CB  . LEU A 1 78  ? 37.476 -14.242 20.627  1.00 45.42  ?  78  LEU A CB  1 
ATOM   550  C CG  . LEU A 1 78  ? 37.055 -13.040 21.452  1.00 47.72  ?  78  LEU A CG  1 
ATOM   551  C CD1 . LEU A 1 78  ? 37.164 -13.443 22.936  1.00 45.12  ?  78  LEU A CD1 1 
ATOM   552  C CD2 . LEU A 1 78  ? 37.948 -11.851 21.093  1.00 38.92  ?  78  LEU A CD2 1 
ATOM   553  N N   . GLY A 1 79  ? 34.183 -15.180 19.347  1.00 50.17  ?  79  GLY A N   1 
ATOM   554  C CA  . GLY A 1 79  ? 33.156 -14.661 18.464  1.00 46.83  ?  79  GLY A CA  1 
ATOM   555  C C   . GLY A 1 79  ? 33.114 -15.589 17.271  1.00 56.09  ?  79  GLY A C   1 
ATOM   556  O O   . GLY A 1 79  ? 33.836 -15.368 16.284  1.00 48.41  ?  79  GLY A O   1 
ATOM   557  N N   . CYS A 1 80  ? 32.212 -16.578 17.324  1.00 49.44  ?  80  CYS A N   1 
ATOM   558  C CA  . CYS A 1 80  ? 32.379 -17.837 16.624  1.00 33.61  ?  80  CYS A CA  1 
ATOM   559  C C   . CYS A 1 80  ? 31.420 -18.032 15.463  1.00 49.85  ?  80  CYS A C   1 
ATOM   560  O O   . CYS A 1 80  ? 31.473 -19.082 14.807  1.00 51.11  ?  80  CYS A O   1 
ATOM   561  C CB  . CYS A 1 80  ? 32.205 -18.988 17.611  1.00 46.48  ?  80  CYS A CB  1 
ATOM   562  S SG  . CYS A 1 80  ? 30.515 -19.278 18.212  1.00 51.88  ?  80  CYS A SG  1 
ATOM   563  N N   . GLY A 1 81  ? 30.440 -17.224 15.323  1.00 51.12  ?  81  GLY A N   1 
ATOM   564  C CA  . GLY A 1 81  ? 29.486 -17.487 14.297  1.00 50.18  ?  81  GLY A CA  1 
ATOM   565  C C   . GLY A 1 81  ? 28.670 -18.723 14.390  1.00 55.46  ?  81  GLY A C   1 
ATOM   566  O O   . GLY A 1 81  ? 28.149 -19.039 15.409  1.00 54.27  ?  81  GLY A O   1 
ATOM   567  N N   . VAL A 1 82  ? 28.515 -19.401 13.280  1.00 55.36  ?  82  VAL A N   1 
ATOM   568  C CA  . VAL A 1 82  ? 27.768 -20.621 13.233  1.00 49.16  ?  82  VAL A CA  1 
ATOM   569  C C   . VAL A 1 82  ? 28.721 -21.730 13.443  1.00 46.86  ?  82  VAL A C   1 
ATOM   570  O O   . VAL A 1 82  ? 28.401 -22.859 13.228  1.00 50.49  ?  82  VAL A O   1 
ATOM   571  C CB  . VAL A 1 82  ? 27.055 -20.722 11.907  1.00 52.88  ?  82  VAL A CB  1 
ATOM   572  C CG1 . VAL A 1 82  ? 25.780 -19.912 11.947  1.00 50.61  ?  82  VAL A CG1 1 
ATOM   573  C CG2 . VAL A 1 82  ? 27.939 -20.255 10.780  1.00 62.17  ?  82  VAL A CG2 1 
ATOM   574  N N   . GLY A 1 83  ? 29.905 -21.391 13.869  1.00 39.78  ?  83  GLY A N   1 
ATOM   575  C CA  . GLY A 1 83  ? 30.884 -22.372 14.191  1.00 41.58  ?  83  GLY A CA  1 
ATOM   576  C C   . GLY A 1 83  ? 31.775 -22.962 13.198  1.00 41.28  ?  83  GLY A C   1 
ATOM   577  O O   . GLY A 1 83  ? 32.635 -23.728 13.491  1.00 44.97  ?  83  GLY A O   1 
ATOM   578  N N   . THR A 1 84  ? 31.605 -22.545 12.001  1.00 41.11  ?  84  THR A N   1 
ATOM   579  C CA  . THR A 1 84  ? 32.386 -23.250 10.987  1.00 46.42  ?  84  THR A CA  1 
ATOM   580  C C   . THR A 1 84  ? 33.905 -23.142 11.148  1.00 52.04  ?  84  THR A C   1 
ATOM   581  O O   . THR A 1 84  ? 34.589 -24.175 11.027  1.00 56.01  ?  84  THR A O   1 
ATOM   582  C CB  . THR A 1 84  ? 31.931 -22.791 9.605   1.00 53.16  ?  84  THR A CB  1 
ATOM   583  O OG1 . THR A 1 84  ? 30.506 -22.963 9.519   1.00 47.84  ?  84  THR A OG1 1 
ATOM   584  C CG2 . THR A 1 84  ? 32.649 -23.610 8.531   1.00 33.00  ?  84  THR A CG2 1 
ATOM   585  N N   . PRO A 1 85  ? 34.510 -21.974 11.374  1.00 45.67  ?  85  PRO A N   1 
ATOM   586  C CA  . PRO A 1 85  ? 35.977 -21.985 11.525  1.00 42.84  ?  85  PRO A CA  1 
ATOM   587  C C   . PRO A 1 85  ? 36.430 -22.581 12.841  1.00 41.35  ?  85  PRO A C   1 
ATOM   588  O O   . PRO A 1 85  ? 37.489 -23.217 12.889  1.00 44.48  ?  85  PRO A O   1 
ATOM   589  C CB  . PRO A 1 85  ? 36.365 -20.502 11.388  1.00 44.48  ?  85  PRO A CB  1 
ATOM   590  C CG  . PRO A 1 85  ? 35.135 -19.841 10.688  1.00 33.26  ?  85  PRO A CG  1 
ATOM   591  C CD  . PRO A 1 85  ? 33.975 -20.603 11.257  1.00 33.92  ?  85  PRO A CD  1 
ATOM   592  N N   . GLY A 1 86  ? 35.656 -22.433 13.913  1.00 47.84  ?  86  GLY A N   1 
ATOM   593  C CA  . GLY A 1 86  ? 36.020 -23.119 15.142  1.00 40.79  ?  86  GLY A CA  1 
ATOM   594  C C   . GLY A 1 86  ? 36.101 -24.631 14.973  1.00 46.18  ?  86  GLY A C   1 
ATOM   595  O O   . GLY A 1 86  ? 37.051 -25.270 15.435  1.00 43.74  ?  86  GLY A O   1 
ATOM   596  N N   . VAL A 1 87  ? 35.101 -25.237 14.312  1.00 43.87  ?  87  VAL A N   1 
ATOM   597  C CA  . VAL A 1 87  ? 35.151 -26.697 14.232  1.00 50.37  ?  87  VAL A CA  1 
ATOM   598  C C   . VAL A 1 87  ? 36.207 -27.136 13.227  1.00 51.76  ?  87  VAL A C   1 
ATOM   599  O O   . VAL A 1 87  ? 36.848 -28.187 13.400  1.00 48.15  ?  87  VAL A O   1 
ATOM   600  C CB  . VAL A 1 87  ? 33.778 -27.324 13.902  1.00 47.05  ?  87  VAL A CB  1 
ATOM   601  C CG1 . VAL A 1 87  ? 32.705 -26.945 14.936  1.00 39.11  ?  87  VAL A CG1 1 
ATOM   602  C CG2 . VAL A 1 87  ? 33.380 -26.937 12.545  1.00 63.04  ?  87  VAL A CG2 1 
ATOM   603  N N   . ARG A 1 88  ? 36.407 -26.347 12.166  1.00 50.74  ?  88  ARG A N   1 
ATOM   604  C CA  . ARG A 1 88  ? 37.465 -26.649 11.206  1.00 44.08  ?  88  ARG A CA  1 
ATOM   605  C C   . ARG A 1 88  ? 38.832 -26.674 11.883  1.00 51.82  ?  88  ARG A C   1 
ATOM   606  O O   . ARG A 1 88  ? 39.658 -27.557 11.604  1.00 55.40  ?  88  ARG A O   1 
ATOM   607  C CB  . ARG A 1 88  ? 37.440 -25.636 10.062  1.00 36.57  ?  88  ARG A CB  1 
ATOM   608  C CG  . ARG A 1 88  ? 38.582 -25.791 9.117   1.00 39.95  ?  88  ARG A CG  1 
ATOM   609  C CD  . ARG A 1 88  ? 38.448 -24.857 7.953   1.00 47.29  ?  88  ARG A CD  1 
ATOM   610  N NE  . ARG A 1 88  ? 39.602 -24.955 7.071   1.00 43.53  ?  88  ARG A NE  1 
ATOM   611  C CZ  . ARG A 1 88  ? 39.669 -25.735 5.997   1.00 44.33  ?  88  ARG A CZ  1 
ATOM   612  N NH1 . ARG A 1 88  ? 38.642 -26.495 5.656   1.00 36.90  ?  88  ARG A NH1 1 
ATOM   613  N NH2 . ARG A 1 88  ? 40.769 -25.743 5.254   1.00 49.06  ?  88  ARG A NH2 1 
ATOM   614  N N   . ILE A 1 89  ? 39.090 -25.719 12.777  1.00 48.10  ?  89  ILE A N   1 
ATOM   615  C CA  . ILE A 1 89  ? 40.387 -25.693 13.449  1.00 46.08  ?  89  ILE A CA  1 
ATOM   616  C C   . ILE A 1 89  ? 40.540 -26.908 14.341  1.00 48.74  ?  89  ILE A C   1 
ATOM   617  O O   . ILE A 1 89  ? 41.638 -27.472 14.454  1.00 58.94  ?  89  ILE A O   1 
ATOM   618  C CB  . ILE A 1 89  ? 40.577 -24.378 14.228  1.00 42.15  ?  89  ILE A CB  1 
ATOM   619  C CG1 . ILE A 1 89  ? 40.734 -23.234 13.229  1.00 34.74  ?  89  ILE A CG1 1 
ATOM   620  C CG2 . ILE A 1 89  ? 41.750 -24.473 15.196  1.00 42.89  ?  89  ILE A CG2 1 
ATOM   621  C CD1 . ILE A 1 89  ? 40.694 -21.867 13.805  1.00 35.23  ?  89  ILE A CD1 1 
ATOM   622  N N   . ALA A 1 90  ? 39.445 -27.350 14.974  1.00 42.19  ?  90  ALA A N   1 
ATOM   623  C CA  . ALA A 1 90  ? 39.569 -28.521 15.841  1.00 52.32  ?  90  ALA A CA  1 
ATOM   624  C C   . ALA A 1 90  ? 39.810 -29.771 15.008  1.00 50.86  ?  90  ALA A C   1 
ATOM   625  O O   . ALA A 1 90  ? 40.652 -30.602 15.360  1.00 52.19  ?  90  ALA A O   1 
ATOM   626  C CB  . ALA A 1 90  ? 38.335 -28.693 16.720  1.00 42.85  ?  90  ALA A CB  1 
ATOM   627  N N   . ARG A 1 91  ? 39.112 -29.879 13.875  1.00 42.61  ?  91  ARG A N   1 
ATOM   628  C CA  . ARG A 1 91  ? 39.232 -31.039 13.001  1.00 47.09  ?  91  ARG A CA  1 
ATOM   629  C C   . ARG A 1 91  ? 40.627 -31.156 12.394  1.00 50.12  ?  91  ARG A C   1 
ATOM   630  O O   . ARG A 1 91  ? 41.216 -32.244 12.371  1.00 50.78  ?  91  ARG A O   1 
ATOM   631  C CB  . ARG A 1 91  ? 38.187 -30.937 11.894  1.00 47.17  ?  91  ARG A CB  1 
ATOM   632  C CG  . ARG A 1 91  ? 38.188 -32.079 10.946  1.00 43.90  ?  91  ARG A CG  1 
ATOM   633  C CD  . ARG A 1 91  ? 36.933 -32.048 10.126  1.00 50.61  ?  91  ARG A CD  1 
ATOM   634  N NE  . ARG A 1 91  ? 36.932 -30.935 9.183   1.00 54.44  ?  91  ARG A NE  1 
ATOM   635  C CZ  . ARG A 1 91  ? 37.646 -30.911 8.061   1.00 43.37  ?  91  ARG A CZ  1 
ATOM   636  N NH1 . ARG A 1 91  ? 38.420 -31.934 7.760   1.00 57.58  ?  91  ARG A NH1 1 
ATOM   637  N NH2 . ARG A 1 91  ? 37.599 -29.868 7.251   1.00 44.42  ?  91  ARG A NH2 1 
ATOM   638  N N   . LEU A 1 92  ? 41.164 -30.051 11.867  1.00 48.38  ?  92  LEU A N   1 
ATOM   639  C CA  . LEU A 1 92  ? 42.433 -30.111 11.152  1.00 43.78  ?  92  LEU A CA  1 
ATOM   640  C C   . LEU A 1 92  ? 43.653 -30.037 12.052  1.00 50.41  ?  92  LEU A C   1 
ATOM   641  O O   . LEU A 1 92  ? 44.711 -30.525 11.654  1.00 50.10  ?  92  LEU A O   1 
ATOM   642  C CB  . LEU A 1 92  ? 42.520 -28.988 10.126  1.00 33.23  ?  92  LEU A CB  1 
ATOM   643  C CG  . LEU A 1 92  ? 41.610 -29.208 8.919   1.00 43.90  ?  92  LEU A CG  1 
ATOM   644  C CD1 . LEU A 1 92  ? 41.820 -28.093 7.918   1.00 32.85  ?  92  LEU A CD1 1 
ATOM   645  C CD2 . LEU A 1 92  ? 41.779 -30.596 8.277   1.00 34.06  ?  92  LEU A CD2 1 
ATOM   646  N N   . SER A 1 93  ? 43.549 -29.459 13.249  1.00 48.99  ?  93  SER A N   1 
ATOM   647  C CA  . SER A 1 93  ? 44.726 -29.276 14.088  1.00 48.31  ?  93  SER A CA  1 
ATOM   648  C C   . SER A 1 93  ? 44.740 -30.146 15.340  1.00 56.35  ?  93  SER A C   1 
ATOM   649  O O   . SER A 1 93  ? 45.785 -30.229 16.003  1.00 51.83  ?  93  SER A O   1 
ATOM   650  C CB  . SER A 1 93  ? 44.851 -27.810 14.539  1.00 45.90  ?  93  SER A CB  1 
ATOM   651  O OG  . SER A 1 93  ? 43.944 -27.528 15.609  1.00 55.74  ?  93  SER A OG  1 
ATOM   652  N N   . GLY A 1 94  ? 43.608 -30.750 15.713  1.00 50.32  ?  94  GLY A N   1 
ATOM   653  C CA  . GLY A 1 94  ? 43.532 -31.479 16.964  1.00 50.42  ?  94  GLY A CA  1 
ATOM   654  C C   . GLY A 1 94  ? 43.481 -30.636 18.228  1.00 61.15  ?  94  GLY A C   1 
ATOM   655  O O   . GLY A 1 94  ? 43.738 -31.167 19.313  1.00 61.90  ?  94  GLY A O   1 
ATOM   656  N N   . ALA A 1 95  ? 43.170 -29.341 18.136  1.00 52.50  ?  95  ALA A N   1 
ATOM   657  C CA  . ALA A 1 95  ? 43.151 -28.541 19.350  1.00 47.85  ?  95  ALA A CA  1 
ATOM   658  C C   . ALA A 1 95  ? 41.789 -28.617 20.037  1.00 49.54  ?  95  ALA A C   1 
ATOM   659  O O   . ALA A 1 95  ? 40.834 -29.204 19.536  1.00 55.82  ?  95  ALA A O   1 
ATOM   660  C CB  . ALA A 1 95  ? 43.519 -27.090 19.050  1.00 43.85  ?  95  ALA A CB  1 
ATOM   661  N N   . HIS A 1 96  ? 41.706 -28.021 21.216  1.00 55.42  ?  96  HIS A N   1 
ATOM   662  C CA  . HIS A 1 96  ? 40.447 -27.901 21.947  1.00 53.66  ?  96  HIS A CA  1 
ATOM   663  C C   . HIS A 1 96  ? 39.917 -26.493 21.738  1.00 52.76  ?  96  HIS A C   1 
ATOM   664  O O   . HIS A 1 96  ? 40.453 -25.529 22.297  1.00 61.24  ?  96  HIS A O   1 
ATOM   665  C CB  . HIS A 1 96  ? 40.638 -28.208 23.430  1.00 50.76  ?  96  HIS A CB  1 
ATOM   666  C CG  . HIS A 1 96  ? 41.008 -29.630 23.688  1.00 65.93  ?  96  HIS A CG  1 
ATOM   667  N ND1 . HIS A 1 96  ? 40.079 -30.646 23.700  1.00 71.77  ?  96  HIS A ND1 1 
ATOM   668  C CD2 . HIS A 1 96  ? 42.213 -30.216 23.885  1.00 71.58  ?  96  HIS A CD2 1 
ATOM   669  C CE1 . HIS A 1 96  ? 40.694 -31.795 23.912  1.00 70.99  ?  96  HIS A CE1 1 
ATOM   670  N NE2 . HIS A 1 96  ? 41.988 -31.562 24.031  1.00 70.37  ?  96  HIS A NE2 1 
ATOM   671  N N   . VAL A 1 97  ? 38.869 -26.374 20.951  1.00 39.29  ?  97  VAL A N   1 
ATOM   672  C CA  . VAL A 1 97  ? 38.325 -25.070 20.625  1.00 51.19  ?  97  VAL A CA  1 
ATOM   673  C C   . VAL A 1 97  ? 37.149 -24.805 21.547  1.00 53.12  ?  97  VAL A C   1 
ATOM   674  O O   . VAL A 1 97  ? 36.217 -25.616 21.626  1.00 59.20  ?  97  VAL A O   1 
ATOM   675  C CB  . VAL A 1 97  ? 37.918 -24.996 19.136  1.00 49.05  ?  97  VAL A CB  1 
ATOM   676  C CG1 . VAL A 1 97  ? 37.072 -23.773 18.877  1.00 38.65  ?  97  VAL A CG1 1 
ATOM   677  C CG2 . VAL A 1 97  ? 39.159 -24.956 18.263  1.00 45.72  ?  97  VAL A CG2 1 
ATOM   678  N N   . THR A 1 98  ? 37.210 -23.689 22.271  1.00 55.12  ?  98  THR A N   1 
ATOM   679  C CA  . THR A 1 98  ? 36.067 -23.132 22.998  1.00 53.07  ?  98  THR A CA  1 
ATOM   680  C C   . THR A 1 98  ? 35.669 -21.832 22.327  1.00 47.56  ?  98  THR A C   1 
ATOM   681  O O   . THR A 1 98  ? 36.454 -20.884 22.318  1.00 52.41  ?  98  THR A O   1 
ATOM   682  C CB  . THR A 1 98  ? 36.399 -22.836 24.454  1.00 44.64  ?  98  THR A CB  1 
ATOM   683  O OG1 . THR A 1 98  ? 36.824 -24.021 25.114  1.00 54.17  ?  98  THR A OG1 1 
ATOM   684  C CG2 . THR A 1 98  ? 35.204 -22.298 25.130  1.00 52.55  ?  98  THR A CG2 1 
ATOM   685  N N   . GLY A 1 99  ? 34.460 -21.777 21.793  1.00 44.08  ?  99  GLY A N   1 
ATOM   686  C CA  . GLY A 1 99  ? 34.010 -20.580 21.113  1.00 51.31  ?  99  GLY A CA  1 
ATOM   687  C C   . GLY A 1 99  ? 32.914 -19.871 21.869  1.00 54.12  ?  99  GLY A C   1 
ATOM   688  O O   . GLY A 1 99  ? 32.296 -20.449 22.769  1.00 52.35  ?  99  GLY A O   1 
ATOM   689  N N   . ILE A 1 100 ? 32.679 -18.603 21.541  1.00 53.18  ?  100 ILE A N   1 
ATOM   690  C CA  . ILE A 1 100 ? 31.615 -17.830 22.171  1.00 50.92  ?  100 ILE A CA  1 
ATOM   691  C C   . ILE A 1 100 ? 30.936 -16.979 21.109  1.00 53.39  ?  100 ILE A C   1 
ATOM   692  O O   . ILE A 1 100 ? 31.529 -16.609 20.090  1.00 48.60  ?  100 ILE A O   1 
ATOM   693  C CB  . ILE A 1 100 ? 32.102 -16.944 23.360  1.00 50.18  ?  100 ILE A CB  1 
ATOM   694  C CG1 . ILE A 1 100 ? 32.753 -15.641 22.884  1.00 52.66  ?  100 ILE A CG1 1 
ATOM   695  C CG2 . ILE A 1 100 ? 33.065 -17.693 24.286  1.00 46.46  ?  100 ILE A CG2 1 
ATOM   696  C CD1 . ILE A 1 100 ? 33.283 -14.762 24.042  1.00 52.22  ?  100 ILE A CD1 1 
ATOM   697  N N   . SER A 1 101 ? 29.661 -16.714 21.333  1.00 49.01  ?  101 SER A N   1 
ATOM   698  C CA  . SER A 1 101 ? 28.942 -15.708 20.584  1.00 52.93  ?  101 SER A CA  1 
ATOM   699  C C   . SER A 1 101 ? 27.973 -15.036 21.548  1.00 55.94  ?  101 SER A C   1 
ATOM   700  O O   . SER A 1 101 ? 27.662 -15.572 22.610  1.00 55.90  ?  101 SER A O   1 
ATOM   701  C CB  . SER A 1 101 ? 28.236 -16.308 19.366  1.00 50.02  ?  101 SER A CB  1 
ATOM   702  O OG  . SER A 1 101 ? 27.371 -15.365 18.747  1.00 46.86  ?  101 SER A OG  1 
ATOM   703  N N   . VAL A 1 102 ? 27.571 -13.814 21.214  1.00 53.99  ?  102 VAL A N   1 
ATOM   704  C CA  . VAL A 1 102 ? 26.494 -13.168 21.942  1.00 51.89  ?  102 VAL A CA  1 
ATOM   705  C C   . VAL A 1 102 ? 25.142 -13.584 21.365  1.00 62.18  ?  102 VAL A C   1 
ATOM   706  O O   . VAL A 1 102 ? 24.108 -13.413 22.023  1.00 58.93  ?  102 VAL A O   1 
ATOM   707  C CB  . VAL A 1 102 ? 26.685 -11.637 21.929  1.00 53.50  ?  102 VAL A CB  1 
ATOM   708  C CG1 . VAL A 1 102 ? 28.022 -11.240 22.578  1.00 39.68  ?  102 VAL A CG1 1 
ATOM   709  C CG2 . VAL A 1 102 ? 26.562 -11.079 20.514  1.00 50.58  ?  102 VAL A CG2 1 
ATOM   710  N N   . SER A 1 103 ? 25.136 -14.152 20.166  1.00 64.04  ?  103 SER A N   1 
ATOM   711  C CA  . SER A 1 103 ? 23.944 -14.655 19.503  1.00 51.92  ?  103 SER A CA  1 
ATOM   712  C C   . SER A 1 103 ? 23.609 -16.052 20.009  1.00 53.62  ?  103 SER A C   1 
ATOM   713  O O   . SER A 1 103 ? 24.433 -16.969 19.911  1.00 52.62  ?  103 SER A O   1 
ATOM   714  C CB  . SER A 1 103 ? 24.188 -14.677 17.997  1.00 54.18  ?  103 SER A CB  1 
ATOM   715  O OG  . SER A 1 103 ? 23.186 -15.424 17.335  1.00 61.24  ?  103 SER A OG  1 
ATOM   716  N N   . HIS A 1 104 ? 22.392 -16.223 20.525  1.00 58.85  ?  104 HIS A N   1 
ATOM   717  C CA  . HIS A 1 104 ? 21.988 -17.529 21.021  1.00 50.26  ?  104 HIS A CA  1 
ATOM   718  C C   . HIS A 1 104 ? 21.825 -18.516 19.872  1.00 53.49  ?  104 HIS A C   1 
ATOM   719  O O   . HIS A 1 104 ? 22.270 -19.671 19.953  1.00 53.67  ?  104 HIS A O   1 
ATOM   720  C CB  . HIS A 1 104 ? 20.686 -17.422 21.808  1.00 49.54  ?  104 HIS A CB  1 
ATOM   721  C CG  . HIS A 1 104 ? 20.004 -18.741 21.982  1.00 52.15  ?  104 HIS A CG  1 
ATOM   722  N ND1 . HIS A 1 104 ? 20.345 -19.625 22.983  1.00 55.42  ?  104 HIS A ND1 1 
ATOM   723  C CD2 . HIS A 1 104 ? 19.066 -19.364 21.229  1.00 51.12  ?  104 HIS A CD2 1 
ATOM   724  C CE1 . HIS A 1 104 ? 19.632 -20.731 22.848  1.00 44.63  ?  104 HIS A CE1 1 
ATOM   725  N NE2 . HIS A 1 104 ? 18.838 -20.593 21.800  1.00 49.54  ?  104 HIS A NE2 1 
ATOM   726  N N   . GLU A 1 105 ? 21.163 -18.083 18.803  1.00 54.38  ?  105 GLU A N   1 
ATOM   727  C CA  . GLU A 1 105 ? 20.973 -18.952 17.652  1.00 58.04  ?  105 GLU A CA  1 
ATOM   728  C C   . GLU A 1 105 ? 22.302 -19.392 17.042  1.00 58.37  ?  105 GLU A C   1 
ATOM   729  O O   . GLU A 1 105 ? 22.418 -20.523 16.557  1.00 63.55  ?  105 GLU A O   1 
ATOM   730  C CB  . GLU A 1 105 ? 20.109 -18.242 16.625  1.00 52.57  ?  105 GLU A CB  1 
ATOM   731  C CG  . GLU A 1 105 ? 18.761 -17.880 17.174  1.00 56.88  ?  105 GLU A CG  1 
ATOM   732  C CD  . GLU A 1 105 ? 17.906 -19.092 17.335  1.00 61.15  ?  105 GLU A CD  1 
ATOM   733  O OE1 . GLU A 1 105 ? 18.213 -20.070 16.639  1.00 65.51  ?  105 GLU A OE1 1 
ATOM   734  O OE2 . GLU A 1 105 ? 16.939 -19.077 18.129  1.00 73.10  -1 105 GLU A OE2 1 
ATOM   735  N N   . GLN A 1 106 ? 23.317 -18.529 17.073  1.00 56.60  ?  106 GLN A N   1 
ATOM   736  C CA  . GLN A 1 106 ? 24.624 -18.917 16.564  1.00 50.44  ?  106 GLN A CA  1 
ATOM   737  C C   . GLN A 1 106 ? 25.226 -20.033 17.409  1.00 54.90  ?  106 GLN A C   1 
ATOM   738  O O   . GLN A 1 106 ? 25.705 -21.047 16.878  1.00 49.65  ?  106 GLN A O   1 
ATOM   739  C CB  . GLN A 1 106 ? 25.543 -17.699 16.519  1.00 47.38  ?  106 GLN A CB  1 
ATOM   740  C CG  . GLN A 1 106 ? 25.350 -16.865 15.264  1.00 42.11  ?  106 GLN A CG  1 
ATOM   741  C CD  . GLN A 1 106 ? 26.337 -15.744 15.157  1.00 42.96  ?  106 GLN A CD  1 
ATOM   742  O OE1 . GLN A 1 106 ? 27.058 -15.463 16.110  1.00 40.09  ?  106 GLN A OE1 1 
ATOM   743  N NE2 . GLN A 1 106 ? 26.380 -15.087 13.995  1.00 38.98  ?  106 GLN A NE2 1 
ATOM   744  N N   . VAL A 1 107 ? 25.201 -19.861 18.733  1.00 54.89  ?  107 VAL A N   1 
ATOM   745  C CA  . VAL A 1 107 ? 25.691 -20.896 19.644  1.00 47.14  ?  107 VAL A CA  1 
ATOM   746  C C   . VAL A 1 107 ? 25.021 -22.243 19.364  1.00 53.48  ?  107 VAL A C   1 
ATOM   747  O O   . VAL A 1 107 ? 25.666 -23.301 19.437  1.00 49.96  ?  107 VAL A O   1 
ATOM   748  C CB  . VAL A 1 107 ? 25.484 -20.437 21.099  1.00 49.59  ?  107 VAL A CB  1 
ATOM   749  C CG1 . VAL A 1 107 ? 25.802 -21.551 22.071  1.00 36.80  ?  107 VAL A CG1 1 
ATOM   750  C CG2 . VAL A 1 107 ? 26.377 -19.217 21.371  1.00 50.91  ?  107 VAL A CG2 1 
ATOM   751  N N   . VAL A 1 108 ? 23.722 -22.232 19.028  1.00 42.91  ?  108 VAL A N   1 
ATOM   752  C CA  . VAL A 1 108 ? 23.030 -23.485 18.751  1.00 39.02  ?  108 VAL A CA  1 
ATOM   753  C C   . VAL A 1 108 ? 23.591 -24.123 17.488  1.00 51.28  ?  108 VAL A C   1 
ATOM   754  O O   . VAL A 1 108 ? 24.030 -25.283 17.497  1.00 54.12  ?  108 VAL A O   1 
ATOM   755  C CB  . VAL A 1 108 ? 21.506 -23.263 18.656  1.00 47.65  ?  108 VAL A CB  1 
ATOM   756  C CG1 . VAL A 1 108 ? 20.795 -24.540 18.293  1.00 37.79  ?  108 VAL A CG1 1 
ATOM   757  C CG2 . VAL A 1 108 ? 20.947 -22.721 19.970  1.00 40.48  ?  108 VAL A CG2 1 
ATOM   758  N N   . ARG A 1 109 ? 23.644 -23.354 16.392  1.00 49.26  ?  109 ARG A N   1 
ATOM   759  C CA  . ARG A 1 109 ? 24.221 -23.876 15.161  1.00 44.07  ?  109 ARG A CA  1 
ATOM   760  C C   . ARG A 1 109 ? 25.657 -24.349 15.365  1.00 52.48  ?  109 ARG A C   1 
ATOM   761  O O   . ARG A 1 109 ? 26.059 -25.382 14.819  1.00 56.14  ?  109 ARG A O   1 
ATOM   762  C CB  . ARG A 1 109 ? 24.156 -22.825 14.064  1.00 44.53  ?  109 ARG A CB  1 
ATOM   763  C CG  . ARG A 1 109 ? 22.755 -22.438 13.715  1.00 46.96  ?  109 ARG A CG  1 
ATOM   764  C CD  . ARG A 1 109 ? 22.522 -22.520 12.216  1.00 62.65  ?  109 ARG A CD  1 
ATOM   765  N NE  . ARG A 1 109 ? 21.114 -22.333 11.912  1.00 81.42  ?  109 ARG A NE  1 
ATOM   766  C CZ  . ARG A 1 109 ? 20.164 -23.186 12.289  1.00 88.74  ?  109 ARG A CZ  1 
ATOM   767  N NH1 . ARG A 1 109 ? 20.474 -24.297 12.968  1.00 90.10  ?  109 ARG A NH1 1 
ATOM   768  N NH2 . ARG A 1 109 ? 18.900 -22.937 11.977  1.00 93.33  ?  109 ARG A NH2 1 
ATOM   769  N N   . ALA A 1 110 ? 26.444 -23.633 16.164  1.00 50.19  ?  110 ALA A N   1 
ATOM   770  C CA  . ALA A 1 110 ? 27.826 -24.057 16.331  1.00 50.45  ?  110 ALA A CA  1 
ATOM   771  C C   . ALA A 1 110 ? 27.904 -25.390 17.063  1.00 50.51  ?  110 ALA A C   1 
ATOM   772  O O   . ALA A 1 110 ? 28.703 -26.263 16.693  1.00 48.21  ?  110 ALA A O   1 
ATOM   773  C CB  . ALA A 1 110 ? 28.645 -22.978 17.041  1.00 34.58  ?  110 ALA A CB  1 
ATOM   774  N N   . ASN A 1 111 ? 27.089 -25.588 18.099  1.00 43.76  ?  111 ASN A N   1 
ATOM   775  C CA  . ASN A 1 111 ? 27.150 -26.897 18.744  1.00 45.89  ?  111 ASN A CA  1 
ATOM   776  C C   . ASN A 1 111 ? 26.616 -27.977 17.805  1.00 52.55  ?  111 ASN A C   1 
ATOM   777  O O   . ASN A 1 111 ? 27.173 -29.086 17.741  1.00 43.84  ?  111 ASN A O   1 
ATOM   778  C CB  . ASN A 1 111 ? 26.415 -26.878 20.084  1.00 42.15  ?  111 ASN A CB  1 
ATOM   779  C CG  . ASN A 1 111 ? 27.259 -26.246 21.183  1.00 58.06  ?  111 ASN A CG  1 
ATOM   780  O OD1 . ASN A 1 111 ? 28.435 -26.582 21.320  1.00 66.55  ?  111 ASN A OD1 1 
ATOM   781  N ND2 . ASN A 1 111 ? 26.691 -25.290 21.927  1.00 36.36  ?  111 ASN A ND2 1 
ATOM   782  N N   . ALA A 1 112 ? 25.583 -27.638 17.011  1.00 51.16  ?  112 ALA A N   1 
ATOM   783  C CA  . ALA A 1 112 ? 25.082 -28.560 16.002  1.00 43.54  ?  112 ALA A CA  1 
ATOM   784  C C   . ALA A 1 112 ? 26.196 -28.967 15.037  1.00 49.85  ?  112 ALA A C   1 
ATOM   785  O O   . ALA A 1 112 ? 26.354 -30.156 14.732  1.00 45.57  ?  112 ALA A O   1 
ATOM   786  C CB  . ALA A 1 112 ? 23.891 -27.940 15.260  1.00 42.59  ?  112 ALA A CB  1 
ATOM   787  N N   . LEU A 1 113 ? 27.015 -28.004 14.582  1.00 50.35  ?  113 LEU A N   1 
ATOM   788  C CA  . LEU A 1 113 ? 28.076 -28.351 13.636  1.00 46.52  ?  113 LEU A CA  1 
ATOM   789  C C   . LEU A 1 113 ? 29.101 -29.259 14.295  1.00 52.40  ?  113 LEU A C   1 
ATOM   790  O O   . LEU A 1 113 ? 29.538 -30.257 13.706  1.00 51.54  ?  113 LEU A O   1 
ATOM   791  C CB  . LEU A 1 113 ? 28.757 -27.099 13.084  1.00 37.74  ?  113 LEU A CB  1 
ATOM   792  C CG  . LEU A 1 113 ? 29.545 -27.300 11.779  1.00 37.16  ?  113 LEU A CG  1 
ATOM   793  C CD1 . LEU A 1 113 ? 28.609 -27.536 10.623  1.00 40.38  ?  113 LEU A CD1 1 
ATOM   794  C CD2 . LEU A 1 113 ? 30.432 -26.109 11.482  1.00 38.30  ?  113 LEU A CD2 1 
ATOM   795  N N   . ALA A 1 114 ? 29.481 -28.946 15.533  1.00 52.34  ?  114 ALA A N   1 
ATOM   796  C CA  . ALA A 1 114 ? 30.425 -29.814 16.231  1.00 51.44  ?  114 ALA A CA  1 
ATOM   797  C C   . ALA A 1 114 ? 29.900 -31.245 16.302  1.00 52.22  ?  114 ALA A C   1 
ATOM   798  O O   . ALA A 1 114 ? 30.647 -32.203 16.037  1.00 42.76  ?  114 ALA A O   1 
ATOM   799  C CB  . ALA A 1 114 ? 30.727 -29.266 17.623  1.00 45.40  ?  114 ALA A CB  1 
ATOM   800  N N   . GLU A 1 115 ? 28.600 -31.403 16.600  1.00 46.74  ?  115 GLU A N   1 
ATOM   801  C CA  . GLU A 1 115 ? 28.037 -32.742 16.710  1.00 43.17  ?  115 GLU A CA  1 
ATOM   802  C C   . GLU A 1 115 ? 28.099 -33.481 15.379  1.00 41.80  ?  115 GLU A C   1 
ATOM   803  O O   . GLU A 1 115 ? 28.490 -34.647 15.332  1.00 46.00  ?  115 GLU A O   1 
ATOM   804  C CB  . GLU A 1 115 ? 26.602 -32.682 17.245  1.00 66.14  ?  115 GLU A CB  1 
ATOM   805  C CG  . GLU A 1 115 ? 26.521 -32.392 18.761  1.00 75.48  ?  115 GLU A CG  1 
ATOM   806  C CD  . GLU A 1 115 ? 25.134 -31.980 19.228  1.00 77.40  ?  115 GLU A CD  1 
ATOM   807  O OE1 . GLU A 1 115 ? 25.043 -31.401 20.342  1.00 74.62  ?  115 GLU A OE1 1 
ATOM   808  O OE2 . GLU A 1 115 ? 24.150 -32.241 18.479  1.00 77.97  -1 115 GLU A OE2 1 
ATOM   809  N N   . GLU A 1 116 ? 27.776 -32.814 14.276  1.00 48.58  ?  116 GLU A N   1 
ATOM   810  C CA  . GLU A 1 116 ? 27.756 -33.550 13.025  1.00 45.14  ?  116 GLU A CA  1 
ATOM   811  C C   . GLU A 1 116 ? 29.155 -33.945 12.560  1.00 48.78  ?  116 GLU A C   1 
ATOM   812  O O   . GLU A 1 116 ? 29.288 -34.890 11.776  1.00 54.29  ?  116 GLU A O   1 
ATOM   813  C CB  . GLU A 1 116 ? 27.034 -32.758 11.939  1.00 37.50  ?  116 GLU A CB  1 
ATOM   814  C CG  . GLU A 1 116 ? 25.646 -32.272 12.293  1.00 45.34  ?  116 GLU A CG  1 
ATOM   815  C CD  . GLU A 1 116 ? 24.626 -33.384 12.442  1.00 52.18  ?  116 GLU A CD  1 
ATOM   816  O OE1 . GLU A 1 116 ? 24.586 -34.247 11.545  1.00 46.21  ?  116 GLU A OE1 1 
ATOM   817  O OE2 . GLU A 1 116 ? 23.872 -33.396 13.462  1.00 67.14  -1 116 GLU A OE2 1 
ATOM   818  N N   . ALA A 1 117 ? 30.201 -33.279 13.031  1.00 48.90  ?  117 ALA A N   1 
ATOM   819  C CA  . ALA A 1 117 ? 31.546 -33.623 12.582  1.00 49.77  ?  117 ALA A CA  1 
ATOM   820  C C   . ALA A 1 117 ? 32.216 -34.677 13.460  1.00 54.00  ?  117 ALA A C   1 
ATOM   821  O O   . ALA A 1 117 ? 33.291 -35.179 13.106  1.00 59.37  ?  117 ALA A O   1 
ATOM   822  C CB  . ALA A 1 117 ? 32.426 -32.371 12.517  1.00 38.25  ?  117 ALA A CB  1 
ATOM   823  N N   . GLY A 1 118 ? 31.602 -35.052 14.571  1.00 45.42  ?  118 GLY A N   1 
ATOM   824  C CA  . GLY A 1 118 ? 32.213 -36.011 15.455  1.00 45.58  ?  118 GLY A CA  1 
ATOM   825  C C   . GLY A 1 118 ? 33.103 -35.367 16.477  1.00 60.05  ?  118 GLY A C   1 
ATOM   826  O O   . GLY A 1 118 ? 33.881 -36.070 17.144  1.00 60.18  ?  118 GLY A O   1 
ATOM   827  N N   . LEU A 1 119 ? 33.007 -34.042 16.632  1.00 51.69  ?  119 LEU A N   1 
ATOM   828  C CA  . LEU A 1 119 ? 33.946 -33.296 17.448  1.00 43.94  ?  119 LEU A CA  1 
ATOM   829  C C   . LEU A 1 119 ? 33.278 -32.544 18.603  1.00 52.79  ?  119 LEU A C   1 
ATOM   830  O O   . LEU A 1 119 ? 33.877 -31.593 19.147  1.00 54.47  ?  119 LEU A O   1 
ATOM   831  C CB  . LEU A 1 119 ? 34.728 -32.339 16.553  1.00 40.65  ?  119 LEU A CB  1 
ATOM   832  C CG  . LEU A 1 119 ? 35.727 -32.984 15.602  1.00 45.75  ?  119 LEU A CG  1 
ATOM   833  C CD1 . LEU A 1 119 ? 36.150 -31.972 14.600  1.00 40.12  ?  119 LEU A CD1 1 
ATOM   834  C CD2 . LEU A 1 119 ? 36.949 -33.560 16.329  1.00 44.41  ?  119 LEU A CD2 1 
ATOM   835  N N   . ALA A 1 120 ? 32.067 -32.952 19.016  1.00 46.90  ?  120 ALA A N   1 
ATOM   836  C CA  . ALA A 1 120 ? 31.405 -32.255 20.123  1.00 47.51  ?  120 ALA A CA  1 
ATOM   837  C C   . ALA A 1 120 ? 32.235 -32.266 21.403  1.00 42.33  ?  120 ALA A C   1 
ATOM   838  O O   . ALA A 1 120 ? 32.032 -31.402 22.253  1.00 45.45  ?  120 ALA A O   1 
ATOM   839  C CB  . ALA A 1 120 ? 30.020 -32.841 20.394  1.00 38.80  ?  120 ALA A CB  1 
ATOM   840  N N   . ASP A 1 121 ? 33.185 -33.200 21.540  1.00 45.61  ?  121 ASP A N   1 
ATOM   841  C CA  . ASP A 1 121 ? 34.113 -33.207 22.667  1.00 50.15  ?  121 ASP A CA  1 
ATOM   842  C C   . ASP A 1 121 ? 35.297 -32.255 22.492  1.00 61.31  ?  121 ASP A C   1 
ATOM   843  O O   . ASP A 1 121 ? 35.894 -31.855 23.498  1.00 86.70  ?  121 ASP A O   1 
ATOM   844  C CB  . ASP A 1 121 ? 34.663 -34.617 22.930  1.00 46.57  ?  121 ASP A CB  1 
ATOM   845  C CG  . ASP A 1 121 ? 35.333 -35.217 21.736  1.00 52.07  ?  121 ASP A CG  1 
ATOM   846  O OD1 . ASP A 1 121 ? 34.909 -34.932 20.603  1.00 59.33  ?  121 ASP A OD1 1 
ATOM   847  O OD2 . ASP A 1 121 ? 36.306 -35.975 21.908  1.00 58.78  -1 121 ASP A OD2 1 
ATOM   848  N N   . ARG A 1 122 ? 35.640 -31.857 21.268  1.00 47.11  ?  122 ARG A N   1 
ATOM   849  C CA  . ARG A 1 122 ? 36.793 -30.991 21.063  1.00 45.91  ?  122 ARG A CA  1 
ATOM   850  C C   . ARG A 1 122 ? 36.448 -29.590 20.571  1.00 44.13  ?  122 ARG A C   1 
ATOM   851  O O   . ARG A 1 122 ? 37.305 -28.706 20.641  1.00 46.95  ?  122 ARG A O   1 
ATOM   852  C CB  . ARG A 1 122 ? 37.786 -31.668 20.098  1.00 52.22  ?  122 ARG A CB  1 
ATOM   853  C CG  . ARG A 1 122 ? 38.268 -33.057 20.623  1.00 56.90  ?  122 ARG A CG  1 
ATOM   854  C CD  . ARG A 1 122 ? 39.676 -33.460 20.199  1.00 66.17  ?  122 ARG A CD  1 
ATOM   855  N NE  . ARG A 1 122 ? 39.747 -33.649 18.749  1.00 88.91  ?  122 ARG A NE  1 
ATOM   856  C CZ  . ARG A 1 122 ? 40.085 -32.717 17.845  1.00 94.11  ?  122 ARG A CZ  1 
ATOM   857  N NH1 . ARG A 1 122 ? 40.438 -31.477 18.208  1.00 85.23  ?  122 ARG A NH1 1 
ATOM   858  N NH2 . ARG A 1 122 ? 40.080 -33.041 16.543  1.00 100.44 ?  122 ARG A NH2 1 
ATOM   859  N N   . ALA A 1 123 ? 35.223 -29.350 20.102  1.00 50.23  ?  123 ALA A N   1 
ATOM   860  C CA  . ALA A 1 123 ? 34.760 -28.010 19.727  1.00 46.81  ?  123 ALA A CA  1 
ATOM   861  C C   . ALA A 1 123 ? 33.501 -27.693 20.518  1.00 49.42  ?  123 ALA A C   1 
ATOM   862  O O   . ALA A 1 123 ? 32.429 -28.234 20.231  1.00 57.45  ?  123 ALA A O   1 
ATOM   863  C CB  . ALA A 1 123 ? 34.471 -27.893 18.231  1.00 38.85  ?  123 ALA A CB  1 
ATOM   864  N N   . ARG A 1 124 ? 33.613 -26.789 21.479  1.00 49.15  ?  124 ARG A N   1 
ATOM   865  C CA  . ARG A 1 124 ? 32.491 -26.407 22.323  1.00 35.47  ?  124 ARG A CA  1 
ATOM   866  C C   . ARG A 1 124 ? 32.140 -24.944 22.122  1.00 45.19  ?  124 ARG A C   1 
ATOM   867  O O   . ARG A 1 124 ? 33.028 -24.096 21.963  1.00 53.56  ?  124 ARG A O   1 
ATOM   868  C CB  . ARG A 1 124 ? 32.837 -26.616 23.759  1.00 39.43  ?  124 ARG A CB  1 
ATOM   869  C CG  . ARG A 1 124 ? 33.348 -27.940 24.054  1.00 45.20  ?  124 ARG A CG  1 
ATOM   870  C CD  . ARG A 1 124 ? 33.261 -28.121 25.527  1.00 65.42  ?  124 ARG A CD  1 
ATOM   871  N NE  . ARG A 1 124 ? 34.474 -27.801 26.256  1.00 71.26  ?  124 ARG A NE  1 
ATOM   872  C CZ  . ARG A 1 124 ? 35.358 -28.727 26.601  1.00 76.38  ?  124 ARG A CZ  1 
ATOM   873  N NH1 . ARG A 1 124 ? 35.150 -29.991 26.235  1.00 67.56  ?  124 ARG A NH1 1 
ATOM   874  N NH2 . ARG A 1 124 ? 36.441 -28.394 27.300  1.00 81.11  ?  124 ARG A NH2 1 
ATOM   875  N N   . PHE A 1 125 ? 30.852 -24.640 22.188  1.00 45.29  ?  125 PHE A N   1 
ATOM   876  C CA  . PHE A 1 125 ? 30.370 -23.282 21.994  1.00 48.81  ?  125 PHE A CA  1 
ATOM   877  C C   . PHE A 1 125 ? 29.380 -22.905 23.089  1.00 42.11  ?  125 PHE A C   1 
ATOM   878  O O   . PHE A 1 125 ? 28.611 -23.732 23.567  1.00 48.30  ?  125 PHE A O   1 
ATOM   879  C CB  . PHE A 1 125 ? 29.751 -23.157 20.592  1.00 47.75  ?  125 PHE A CB  1 
ATOM   880  C CG  . PHE A 1 125 ? 30.722 -23.450 19.520  1.00 45.01  ?  125 PHE A CG  1 
ATOM   881  C CD1 . PHE A 1 125 ? 31.670 -22.517 19.172  1.00 54.10  ?  125 PHE A CD1 1 
ATOM   882  C CD2 . PHE A 1 125 ? 30.754 -24.698 18.925  1.00 48.04  ?  125 PHE A CD2 1 
ATOM   883  C CE1 . PHE A 1 125 ? 32.609 -22.791 18.203  1.00 59.57  ?  125 PHE A CE1 1 
ATOM   884  C CE2 . PHE A 1 125 ? 31.679 -24.994 17.970  1.00 46.02  ?  125 PHE A CE2 1 
ATOM   885  C CZ  . PHE A 1 125 ? 32.618 -24.036 17.598  1.00 57.16  ?  125 PHE A CZ  1 
ATOM   886  N N   . GLN A 1 126 ? 29.385 -21.630 23.462  1.00 52.16  ?  126 GLN A N   1 
ATOM   887  C CA  . GLN A 1 126 ? 28.554 -21.167 24.567  1.00 55.16  ?  126 GLN A CA  1 
ATOM   888  C C   . GLN A 1 126 ? 28.274 -19.683 24.359  1.00 53.08  ?  126 GLN A C   1 
ATOM   889  O O   . GLN A 1 126 ? 29.054 -18.983 23.713  1.00 50.75  ?  126 GLN A O   1 
ATOM   890  C CB  . GLN A 1 126 ? 29.249 -21.416 25.920  1.00 40.76  ?  126 GLN A CB  1 
ATOM   891  C CG  . GLN A 1 126 ? 30.191 -20.303 26.281  1.00 56.08  ?  126 GLN A CG  1 
ATOM   892  C CD  . GLN A 1 126 ? 31.241 -20.670 27.302  1.00 66.79  ?  126 GLN A CD  1 
ATOM   893  O OE1 . GLN A 1 126 ? 31.785 -21.773 27.314  1.00 65.82  ?  126 GLN A OE1 1 
ATOM   894  N NE2 . GLN A 1 126 ? 31.513 -19.736 28.199  1.00 80.07  ?  126 GLN A NE2 1 
ATOM   895  N N   . ARG A 1 127 ? 27.158 -19.202 24.900  1.00 52.94  ?  127 ARG A N   1 
ATOM   896  C CA  . ARG A 1 127 ? 26.836 -17.782 24.765  1.00 55.92  ?  127 ARG A CA  1 
ATOM   897  C C   . ARG A 1 127 ? 27.620 -16.966 25.793  1.00 57.56  ?  127 ARG A C   1 
ATOM   898  O O   . ARG A 1 127 ? 27.605 -17.274 26.996  1.00 56.68  ?  127 ARG A O   1 
ATOM   899  C CB  . ARG A 1 127 ? 25.340 -17.541 24.912  1.00 54.29  ?  127 ARG A CB  1 
ATOM   900  C CG  . ARG A 1 127 ? 24.982 -16.072 24.904  1.00 61.93  ?  127 ARG A CG  1 
ATOM   901  C CD  . ARG A 1 127 ? 23.517 -15.840 24.501  1.00 69.30  ?  127 ARG A CD  1 
ATOM   902  N NE  . ARG A 1 127 ? 23.016 -14.600 25.087  1.00 80.93  ?  127 ARG A NE  1 
ATOM   903  C CZ  . ARG A 1 127 ? 22.695 -14.469 26.376  1.00 80.17  ?  127 ARG A CZ  1 
ATOM   904  N NH1 . ARG A 1 127 ? 22.830 -15.507 27.209  1.00 68.75  ?  127 ARG A NH1 1 
ATOM   905  N NH2 . ARG A 1 127 ? 22.243 -13.307 26.831  1.00 84.47  ?  127 ARG A NH2 1 
ATOM   906  N N   . ALA A 1 128 ? 28.331 -15.948 25.312  1.00 47.43  ?  128 ALA A N   1 
ATOM   907  C CA  . ALA A 1 128 ? 29.140 -15.095 26.172  1.00 53.54  ?  128 ALA A CA  1 
ATOM   908  C C   . ALA A 1 128 ? 29.577 -13.871 25.376  1.00 58.69  ?  128 ALA A C   1 
ATOM   909  O O   . ALA A 1 128 ? 29.374 -13.780 24.157  1.00 59.01  ?  128 ALA A O   1 
ATOM   910  C CB  . ALA A 1 128 ? 30.352 -15.836 26.753  1.00 49.79  ?  128 ALA A CB  1 
ATOM   911  N N   . ASP A 1 129 ? 30.190 -12.936 26.100  1.00 57.51  ?  129 ASP A N   1 
ATOM   912  C CA  . ASP A 1 129 ? 30.543 -11.597 25.643  1.00 49.55  ?  129 ASP A CA  1 
ATOM   913  C C   . ASP A 1 129 ? 32.023 -11.425 25.939  1.00 56.12  ?  129 ASP A C   1 
ATOM   914  O O   . ASP A 1 129 ? 32.469 -11.724 27.050  1.00 58.47  ?  129 ASP A O   1 
ATOM   915  C CB  . ASP A 1 129 ? 29.679 -10.560 26.380  1.00 56.17  ?  129 ASP A CB  1 
ATOM   916  C CG  . ASP A 1 129 ? 29.974 -9.127  25.996  1.00 65.82  ?  129 ASP A CG  1 
ATOM   917  O OD1 . ASP A 1 129 ? 31.109 -8.813  25.613  1.00 72.75  ?  129 ASP A OD1 1 
ATOM   918  O OD2 . ASP A 1 129 ? 29.034 -8.294  26.073  1.00 80.31  -1 129 ASP A OD2 1 
ATOM   919  N N   . ALA A 1 130 ? 32.793 -10.984 24.943  1.00 58.04  ?  130 ALA A N   1 
ATOM   920  C CA  . ALA A 1 130 ? 34.233 -10.888 25.154  1.00 57.52  ?  130 ALA A CA  1 
ATOM   921  C C   . ALA A 1 130 ? 34.608 -9.746  26.089  1.00 60.12  ?  130 ALA A C   1 
ATOM   922  O O   . ALA A 1 130 ? 35.735 -9.726  26.589  1.00 61.46  ?  130 ALA A O   1 
ATOM   923  C CB  . ALA A 1 130 ? 34.962 -10.750 23.820  1.00 55.59  ?  130 ALA A CB  1 
ATOM   924  N N   . MET A 1 131 ? 33.683 -8.826  26.365  1.00 55.41  ?  131 MET A N   1 
ATOM   925  C CA  . MET A 1 131 ? 33.928 -7.809  27.385  1.00 59.60  ?  131 MET A CA  1 
ATOM   926  C C   . MET A 1 131 ? 34.122 -8.426  28.759  1.00 64.30  ?  131 MET A C   1 
ATOM   927  O O   . MET A 1 131 ? 34.879 -7.901  29.586  1.00 70.18  ?  131 MET A O   1 
ATOM   928  C CB  . MET A 1 131 ? 32.782 -6.810  27.445  1.00 54.92  ?  131 MET A CB  1 
ATOM   929  C CG  . MET A 1 131 ? 32.490 -6.149  26.111  1.00 65.49  ?  131 MET A CG  1 
ATOM   930  S SD  . MET A 1 131 ? 33.651 -4.754  25.965  1.00 83.59  ?  131 MET A SD  1 
ATOM   931  C CE  . MET A 1 131 ? 32.633 -3.322  26.313  1.00 92.04  ?  131 MET A CE  1 
ATOM   932  N N   . ASP A 1 132 ? 33.425 -9.536  29.037  1.00 64.35  ?  132 ASP A N   1 
ATOM   933  C CA  . ASP A 1 132 ? 33.490 -10.187 30.347  1.00 66.73  ?  132 ASP A CA  1 
ATOM   934  C C   . ASP A 1 132 ? 33.638 -11.695 30.108  1.00 67.62  ?  132 ASP A C   1 
ATOM   935  O O   . ASP A 1 132 ? 32.662 -12.454 30.129  1.00 62.81  ?  132 ASP A O   1 
ATOM   936  C CB  . ASP A 1 132 ? 32.255 -9.819  31.156  1.00 65.99  ?  132 ASP A CB  1 
ATOM   937  C CG  . ASP A 1 132 ? 32.444 -10.039 32.636  1.00 73.65  ?  132 ASP A CG  1 
ATOM   938  O OD1 . ASP A 1 132 ? 33.541 -10.534 33.030  1.00 66.67  ?  132 ASP A OD1 1 
ATOM   939  O OD2 . ASP A 1 132 ? 31.496 -9.729  33.388  1.00 86.49  -1 132 ASP A OD2 1 
ATOM   940  N N   . LEU A 1 133 ? 34.881 -12.126 29.918  1.00 63.68  ?  133 LEU A N   1 
ATOM   941  C CA  . LEU A 1 133 ? 35.153 -13.509 29.529  1.00 62.69  ?  133 LEU A CA  1 
ATOM   942  C C   . LEU A 1 133 ? 34.969 -14.449 30.718  1.00 65.67  ?  133 LEU A C   1 
ATOM   943  O O   . LEU A 1 133 ? 35.694 -14.323 31.715  1.00 68.39  ?  133 LEU A O   1 
ATOM   944  C CB  . LEU A 1 133 ? 36.580 -13.638 28.966  1.00 60.12  ?  133 LEU A CB  1 
ATOM   945  C CG  . LEU A 1 133 ? 36.919 -13.285 27.507  1.00 61.24  ?  133 LEU A CG  1 
ATOM   946  C CD1 . LEU A 1 133 ? 38.447 -13.361 27.259  1.00 55.45  ?  133 LEU A CD1 1 
ATOM   947  C CD2 . LEU A 1 133 ? 36.176 -14.181 26.513  1.00 64.55  ?  133 LEU A CD2 1 
ATOM   948  N N   . PRO A 1 134 ? 34.060 -15.417 30.656  1.00 65.44  ?  134 PRO A N   1 
ATOM   949  C CA  . PRO A 1 134 ? 33.875 -16.335 31.794  1.00 53.01  ?  134 PRO A CA  1 
ATOM   950  C C   . PRO A 1 134 ? 34.946 -17.415 31.854  1.00 60.40  ?  134 PRO A C   1 
ATOM   951  O O   . PRO A 1 134 ? 34.648 -18.608 31.900  1.00 77.67  ?  134 PRO A O   1 
ATOM   952  C CB  . PRO A 1 134 ? 32.490 -16.921 31.510  1.00 44.32  ?  134 PRO A CB  1 
ATOM   953  C CG  . PRO A 1 134 ? 32.445 -16.986 30.010  1.00 55.79  ?  134 PRO A CG  1 
ATOM   954  C CD  . PRO A 1 134 ? 33.204 -15.777 29.509  1.00 59.16  ?  134 PRO A CD  1 
ATOM   955  N N   . PHE A 1 135 ? 36.215 -17.004 31.865  1.00 56.78  ?  135 PHE A N   1 
ATOM   956  C CA  . PHE A 1 135 ? 37.306 -17.969 31.833  1.00 55.78  ?  135 PHE A CA  1 
ATOM   957  C C   . PHE A 1 135 ? 38.436 -17.541 32.762  1.00 60.70  ?  135 PHE A C   1 
ATOM   958  O O   . PHE A 1 135 ? 38.734 -16.352 32.900  1.00 61.57  ?  135 PHE A O   1 
ATOM   959  C CB  . PHE A 1 135 ? 37.847 -18.142 30.396  1.00 63.38  ?  135 PHE A CB  1 
ATOM   960  C CG  . PHE A 1 135 ? 36.798 -18.529 29.371  1.00 65.12  ?  135 PHE A CG  1 
ATOM   961  C CD1 . PHE A 1 135 ? 36.363 -19.849 29.249  1.00 55.85  ?  135 PHE A CD1 1 
ATOM   962  C CD2 . PHE A 1 135 ? 36.268 -17.581 28.506  1.00 65.59  ?  135 PHE A CD2 1 
ATOM   963  C CE1 . PHE A 1 135 ? 35.412 -20.201 28.302  1.00 49.26  ?  135 PHE A CE1 1 
ATOM   964  C CE2 . PHE A 1 135 ? 35.302 -17.936 27.552  1.00 62.38  ?  135 PHE A CE2 1 
ATOM   965  C CZ  . PHE A 1 135 ? 34.872 -19.247 27.460  1.00 51.97  ?  135 PHE A CZ  1 
ATOM   966  N N   . GLU A 1 136 ? 39.093 -18.529 33.359  1.00 60.82  ?  136 GLU A N   1 
ATOM   967  C CA  . GLU A 1 136 ? 40.225 -18.303 34.248  1.00 57.94  ?  136 GLU A CA  1 
ATOM   968  C C   . GLU A 1 136 ? 41.373 -17.564 33.555  1.00 65.41  ?  136 GLU A C   1 
ATOM   969  O O   . GLU A 1 136 ? 41.539 -17.602 32.335  1.00 64.17  ?  136 GLU A O   1 
ATOM   970  C CB  . GLU A 1 136 ? 40.761 -19.636 34.780  1.00 61.85  ?  136 GLU A CB  1 
ATOM   971  C CG  . GLU A 1 136 ? 39.757 -20.436 35.591  1.00 74.03  ?  136 GLU A CG  1 
ATOM   972  C CD  . GLU A 1 136 ? 39.572 -19.876 36.977  1.00 90.22  ?  136 GLU A CD  1 
ATOM   973  O OE1 . GLU A 1 136 ? 40.442 -20.113 37.845  1.00 100.96 ?  136 GLU A OE1 1 
ATOM   974  O OE2 . GLU A 1 136 ? 38.563 -19.177 37.187  1.00 94.22  -1 136 GLU A OE2 1 
ATOM   975  N N   . ASP A 1 137 ? 42.197 -16.908 34.368  1.00 64.31  ?  137 ASP A N   1 
ATOM   976  C CA  . ASP A 1 137 ? 43.465 -16.392 33.882  1.00 67.77  ?  137 ASP A CA  1 
ATOM   977  C C   . ASP A 1 137 ? 44.308 -17.526 33.302  1.00 65.98  ?  137 ASP A C   1 
ATOM   978  O O   . ASP A 1 137 ? 44.252 -18.669 33.766  1.00 63.03  ?  137 ASP A O   1 
ATOM   979  C CB  . ASP A 1 137 ? 44.243 -15.707 35.014  1.00 71.07  ?  137 ASP A CB  1 
ATOM   980  C CG  . ASP A 1 137 ? 43.489 -14.547 35.659  1.00 74.62  ?  137 ASP A CG  1 
ATOM   981  O OD1 . ASP A 1 137 ? 42.345 -14.244 35.246  1.00 77.61  ?  137 ASP A OD1 1 
ATOM   982  O OD2 . ASP A 1 137 ? 44.082 -13.911 36.566  1.00 73.96  -1 137 ASP A OD2 1 
ATOM   983  N N   . GLU A 1 138 ? 45.087 -17.195 32.264  1.00 63.55  ?  138 GLU A N   1 
ATOM   984  C CA  . GLU A 1 138 ? 46.082 -18.101 31.675  1.00 66.99  ?  138 GLU A CA  1 
ATOM   985  C C   . GLU A 1 138 ? 45.482 -19.456 31.323  1.00 67.16  ?  138 GLU A C   1 
ATOM   986  O O   . GLU A 1 138 ? 46.097 -20.507 31.512  1.00 70.70  ?  138 GLU A O   1 
ATOM   987  C CB  . GLU A 1 138 ? 47.292 -18.248 32.594  1.00 67.37  ?  138 GLU A CB  1 
ATOM   988  C CG  . GLU A 1 138 ? 47.815 -16.876 32.969  1.00 71.25  ?  138 GLU A CG  1 
ATOM   989  C CD  . GLU A 1 138 ? 49.120 -16.888 33.687  1.00 67.33  ?  138 GLU A CD  1 
ATOM   990  O OE1 . GLU A 1 138 ? 49.800 -17.937 33.661  1.00 69.34  ?  138 GLU A OE1 1 
ATOM   991  O OE2 . GLU A 1 138 ? 49.441 -15.837 34.295  1.00 71.10  -1 138 GLU A OE2 1 
ATOM   992  N N   . SER A 1 139 ? 44.269 -19.422 30.782  1.00 62.66  ?  139 SER A N   1 
ATOM   993  C CA  . SER A 1 139 ? 43.555 -20.629 30.410  1.00 54.56  ?  139 SER A CA  1 
ATOM   994  C C   . SER A 1 139 ? 43.716 -21.003 28.947  1.00 61.54  ?  139 SER A C   1 
ATOM   995  O O   . SER A 1 139 ? 43.513 -22.170 28.602  1.00 72.23  ?  139 SER A O   1 
ATOM   996  C CB  . SER A 1 139 ? 42.073 -20.464 30.736  1.00 51.88  ?  139 SER A CB  1 
ATOM   997  O OG  . SER A 1 139 ? 41.639 -19.149 30.461  1.00 60.48  ?  139 SER A OG  1 
ATOM   998  N N   . PHE A 1 140 ? 44.096 -20.072 28.077  1.00 67.59  ?  140 PHE A N   1 
ATOM   999  C CA  . PHE A 1 140 ? 44.115 -20.336 26.641  1.00 68.01  ?  140 PHE A CA  1 
ATOM   1000 C C   . PHE A 1 140 ? 45.512 -20.205 26.053  1.00 63.54  ?  140 PHE A C   1 
ATOM   1001 O O   . PHE A 1 140 ? 46.222 -19.219 26.311  1.00 66.69  ?  140 PHE A O   1 
ATOM   1002 C CB  . PHE A 1 140 ? 43.157 -19.410 25.916  1.00 58.53  ?  140 PHE A CB  1 
ATOM   1003 C CG  . PHE A 1 140 ? 41.732 -19.786 26.104  1.00 50.95  ?  140 PHE A CG  1 
ATOM   1004 C CD1 . PHE A 1 140 ? 41.227 -20.953 25.524  1.00 47.04  ?  140 PHE A CD1 1 
ATOM   1005 C CD2 . PHE A 1 140 ? 40.892 -19.001 26.878  1.00 53.99  ?  140 PHE A CD2 1 
ATOM   1006 C CE1 . PHE A 1 140 ? 39.881 -21.312 25.689  1.00 53.47  ?  140 PHE A CE1 1 
ATOM   1007 C CE2 . PHE A 1 140 ? 39.539 -19.349 27.056  1.00 57.37  ?  140 PHE A CE2 1 
ATOM   1008 C CZ  . PHE A 1 140 ? 39.033 -20.507 26.460  1.00 54.20  ?  140 PHE A CZ  1 
ATOM   1009 N N   . ASP A 1 141 ? 45.895 -21.219 25.266  1.00 48.35  ?  141 ASP A N   1 
ATOM   1010 C CA  . ASP A 1 141 ? 47.142 -21.158 24.507  1.00 52.55  ?  141 ASP A CA  1 
ATOM   1011 C C   . ASP A 1 141 ? 47.081 -20.134 23.373  1.00 51.86  ?  141 ASP A C   1 
ATOM   1012 O O   . ASP A 1 141 ? 48.120 -19.618 22.958  1.00 61.47  ?  141 ASP A O   1 
ATOM   1013 C CB  . ASP A 1 141 ? 47.463 -22.515 23.911  1.00 52.15  ?  141 ASP A CB  1 
ATOM   1014 C CG  . ASP A 1 141 ? 47.688 -23.558 24.940  1.00 60.97  ?  141 ASP A CG  1 
ATOM   1015 O OD1 . ASP A 1 141 ? 48.477 -23.300 25.871  1.00 73.26  ?  141 ASP A OD1 1 
ATOM   1016 O OD2 . ASP A 1 141 ? 47.050 -24.629 24.830  1.00 65.36  -1 141 ASP A OD2 1 
ATOM   1017 N N   . ALA A 1 142 ? 45.892 -19.834 22.857  1.00 50.44  ?  142 ALA A N   1 
ATOM   1018 C CA  . ALA A 1 142 ? 45.747 -18.901 21.749  1.00 48.67  ?  142 ALA A CA  1 
ATOM   1019 C C   . ALA A 1 142 ? 44.295 -18.463 21.666  1.00 56.15  ?  142 ALA A C   1 
ATOM   1020 O O   . ALA A 1 142 ? 43.387 -19.256 21.925  1.00 67.71  ?  142 ALA A O   1 
ATOM   1021 C CB  . ALA A 1 142 ? 46.181 -19.529 20.411  1.00 43.55  ?  142 ALA A CB  1 
ATOM   1022 N N   . VAL A 1 143 ? 44.084 -17.208 21.294  1.00 53.30  ?  143 VAL A N   1 
ATOM   1023 C CA  . VAL A 1 143 ? 42.767 -16.694 20.963  1.00 49.05  ?  143 VAL A CA  1 
ATOM   1024 C C   . VAL A 1 143 ? 42.780 -16.321 19.488  1.00 56.75  ?  143 VAL A C   1 
ATOM   1025 O O   . VAL A 1 143 ? 43.775 -15.792 18.983  1.00 67.88  ?  143 VAL A O   1 
ATOM   1026 C CB  . VAL A 1 143 ? 42.413 -15.476 21.838  1.00 46.07  ?  143 VAL A CB  1 
ATOM   1027 C CG1 . VAL A 1 143 ? 41.020 -14.973 21.537  1.00 46.18  ?  143 VAL A CG1 1 
ATOM   1028 C CG2 . VAL A 1 143 ? 42.573 -15.822 23.297  1.00 43.14  ?  143 VAL A CG2 1 
ATOM   1029 N N   . ILE A 1 144 ? 41.694 -16.605 18.790  1.00 47.87  ?  144 ILE A N   1 
ATOM   1030 C CA  . ILE A 1 144 ? 41.503 -16.095 17.448  1.00 45.63  ?  144 ILE A CA  1 
ATOM   1031 C C   . ILE A 1 144 ? 40.177 -15.367 17.439  1.00 53.93  ?  144 ILE A C   1 
ATOM   1032 O O   . ILE A 1 144 ? 39.205 -15.837 18.043  1.00 51.56  ?  144 ILE A O   1 
ATOM   1033 C CB  . ILE A 1 144 ? 41.541 -17.206 16.377  1.00 52.75  ?  144 ILE A CB  1 
ATOM   1034 C CG1 . ILE A 1 144 ? 41.071 -16.650 15.032  1.00 49.02  ?  144 ILE A CG1 1 
ATOM   1035 C CG2 . ILE A 1 144 ? 40.689 -18.419 16.803  1.00 52.19  ?  144 ILE A CG2 1 
ATOM   1036 C CD1 . ILE A 1 144 ? 41.120 -17.656 13.937  1.00 54.57  ?  144 ILE A CD1 1 
ATOM   1037 N N   . ALA A 1 145 ? 40.149 -14.207 16.774  1.00 51.75  ?  145 ALA A N   1 
ATOM   1038 C CA  . ALA A 1 145 ? 38.983 -13.329 16.730  1.00 45.97  ?  145 ALA A CA  1 
ATOM   1039 C C   . ALA A 1 145 ? 38.778 -12.941 15.275  1.00 51.20  ?  145 ALA A C   1 
ATOM   1040 O O   . ALA A 1 145 ? 39.241 -11.892 14.821  1.00 60.22  ?  145 ALA A O   1 
ATOM   1041 C CB  . ALA A 1 145 ? 39.173 -12.127 17.624  1.00 39.70  ?  145 ALA A CB  1 
ATOM   1042 N N   . LEU A 1 146 ? 38.031 -13.770 14.565  1.00 46.68  ?  146 LEU A N   1 
ATOM   1043 C CA  . LEU A 1 146 ? 37.989 -13.750 13.116  1.00 44.49  ?  146 LEU A CA  1 
ATOM   1044 C C   . LEU A 1 146 ? 36.775 -12.928 12.705  1.00 49.67  ?  146 LEU A C   1 
ATOM   1045 O O   . LEU A 1 146 ? 35.638 -13.371 12.902  1.00 56.11  ?  146 LEU A O   1 
ATOM   1046 C CB  . LEU A 1 146 ? 37.910 -15.188 12.597  1.00 35.72  ?  146 LEU A CB  1 
ATOM   1047 C CG  . LEU A 1 146 ? 38.385 -15.584 11.186  1.00 43.16  ?  146 LEU A CG  1 
ATOM   1048 C CD1 . LEU A 1 146 ? 38.073 -17.039 10.944  1.00 40.56  ?  146 LEU A CD1 1 
ATOM   1049 C CD2 . LEU A 1 146 ? 37.863 -14.728 10.029  1.00 42.78  ?  146 LEU A CD2 1 
ATOM   1050 N N   . GLU A 1 147 ? 37.015 -11.750 12.104  1.00 46.80  ?  147 GLU A N   1 
ATOM   1051 C CA  . GLU A 1 147 ? 35.967 -10.745 11.864  1.00 49.97  ?  147 GLU A CA  1 
ATOM   1052 C C   . GLU A 1 147 ? 34.969 -10.613 13.007  1.00 55.85  ?  147 GLU A C   1 
ATOM   1053 O O   . GLU A 1 147 ? 33.763 -10.493 12.778  1.00 58.71  ?  147 GLU A O   1 
ATOM   1054 C CB  . GLU A 1 147 ? 35.168 -11.030 10.599  1.00 42.23  ?  147 GLU A CB  1 
ATOM   1055 C CG  . GLU A 1 147 ? 35.612 -10.278 9.436   1.00 38.71  ?  147 GLU A CG  1 
ATOM   1056 C CD  . GLU A 1 147 ? 34.878 -10.644 8.182   1.00 50.64  ?  147 GLU A CD  1 
ATOM   1057 O OE1 . GLU A 1 147 ? 33.631 -10.512 8.109   1.00 48.55  ?  147 GLU A OE1 1 
ATOM   1058 O OE2 . GLU A 1 147 ? 35.581 -11.147 7.268   1.00 60.40  -1 147 GLU A OE2 1 
ATOM   1059 N N   . SER A 1 148 ? 35.427 -10.654 14.237  1.00 51.67  ?  148 SER A N   1 
ATOM   1060 C CA  . SER A 1 148 ? 34.469 -10.614 15.319  1.00 49.02  ?  148 SER A CA  1 
ATOM   1061 C C   . SER A 1 148 ? 34.512 -9.297  16.080  1.00 52.33  ?  148 SER A C   1 
ATOM   1062 O O   . SER A 1 148 ? 33.453 -8.762  16.429  1.00 51.94  ?  148 SER A O   1 
ATOM   1063 C CB  . SER A 1 148 ? 34.710 -11.798 16.270  1.00 42.31  ?  148 SER A CB  1 
ATOM   1064 O OG  . SER A 1 148 ? 36.067 -11.884 16.651  1.00 54.87  ?  148 SER A OG  1 
ATOM   1065 N N   . ILE A 1 149 ? 35.716 -8.751  16.299  1.00 49.77  ?  149 ILE A N   1 
ATOM   1066 C CA  . ILE A 1 149 ? 35.881 -7.523  17.069  1.00 54.84  ?  149 ILE A CA  1 
ATOM   1067 C C   . ILE A 1 149 ? 35.187 -6.327  16.422  1.00 57.97  ?  149 ILE A C   1 
ATOM   1068 O O   . ILE A 1 149 ? 34.877 -5.354  17.107  1.00 63.19  ?  149 ILE A O   1 
ATOM   1069 C CB  . ILE A 1 149 ? 37.379 -7.250  17.263  1.00 53.65  ?  149 ILE A CB  1 
ATOM   1070 C CG1 . ILE A 1 149 ? 37.621 -6.548  18.592  1.00 49.98  ?  149 ILE A CG1 1 
ATOM   1071 C CG2 . ILE A 1 149 ? 37.975 -6.493  16.047  1.00 37.05  ?  149 ILE A CG2 1 
ATOM   1072 C CD1 . ILE A 1 149 ? 39.094 -6.426  18.962  1.00 44.69  ?  149 ILE A CD1 1 
ATOM   1073 N N   . ILE A 1 150 ? 34.921 -6.384  15.115  1.00 57.51  ?  150 ILE A N   1 
ATOM   1074 C CA  . ILE A 1 150 ? 34.231 -5.303  14.427  1.00 56.73  ?  150 ILE A CA  1 
ATOM   1075 C C   . ILE A 1 150 ? 32.844 -5.059  15.010  1.00 66.03  ?  150 ILE A C   1 
ATOM   1076 O O   . ILE A 1 150 ? 32.303 -3.957  14.875  1.00 70.81  ?  150 ILE A O   1 
ATOM   1077 C CB  . ILE A 1 150 ? 34.136 -5.611  12.922  1.00 58.20  ?  150 ILE A CB  1 
ATOM   1078 C CG1 . ILE A 1 150 ? 33.557 -7.015  12.719  1.00 59.70  ?  150 ILE A CG1 1 
ATOM   1079 C CG2 . ILE A 1 150 ? 35.483 -5.478  12.269  1.00 52.53  ?  150 ILE A CG2 1 
ATOM   1080 C CD1 . ILE A 1 150 ? 33.078 -7.294  11.309  1.00 56.25  ?  150 ILE A CD1 1 
ATOM   1081 N N   . HIS A 1 151 ? 32.229 -6.078  15.621  1.00 62.99  ?  151 HIS A N   1 
ATOM   1082 C CA  . HIS A 1 151 ? 30.909 -5.935  16.225  1.00 63.60  ?  151 HIS A CA  1 
ATOM   1083 C C   . HIS A 1 151 ? 30.958 -5.677  17.724  1.00 72.32  ?  151 HIS A C   1 
ATOM   1084 O O   . HIS A 1 151 ? 29.914 -5.395  18.317  1.00 85.02  ?  151 HIS A O   1 
ATOM   1085 C CB  . HIS A 1 151 ? 30.060 -7.194  16.007  1.00 62.13  ?  151 HIS A CB  1 
ATOM   1086 C CG  . HIS A 1 151 ? 29.710 -7.475  14.577  1.00 63.75  ?  151 HIS A CG  1 
ATOM   1087 N ND1 . HIS A 1 151 ? 30.236 -8.538  13.878  1.00 60.68  ?  151 HIS A ND1 1 
ATOM   1088 C CD2 . HIS A 1 151 ? 28.848 -6.863  13.734  1.00 62.98  ?  151 HIS A CD2 1 
ATOM   1089 C CE1 . HIS A 1 151 ? 29.729 -8.555  12.657  1.00 63.68  ?  151 HIS A CE1 1 
ATOM   1090 N NE2 . HIS A 1 151 ? 28.888 -7.544  12.545  1.00 63.91  ?  151 HIS A NE2 1 
ATOM   1091 N N   . MET A 1 152 ? 32.115 -5.803  18.353  1.00 66.69  ?  152 MET A N   1 
ATOM   1092 C CA  . MET A 1 152 ? 32.193 -5.754  19.806  1.00 70.21  ?  152 MET A CA  1 
ATOM   1093 C C   . MET A 1 152 ? 32.186 -4.310  20.311  1.00 73.40  ?  152 MET A C   1 
ATOM   1094 O O   . MET A 1 152 ? 32.589 -3.388  19.604  1.00 76.49  ?  152 MET A O   1 
ATOM   1095 C CB  . MET A 1 152 ? 33.447 -6.480  20.294  1.00 63.90  ?  152 MET A CB  1 
ATOM   1096 C CG  . MET A 1 152 ? 33.480 -7.952  19.955  1.00 56.46  ?  152 MET A CG  1 
ATOM   1097 S SD  . MET A 1 152 ? 34.836 -8.788  20.784  1.00 68.50  ?  152 MET A SD  1 
ATOM   1098 C CE  . MET A 1 152 ? 34.833 -10.329 19.869  1.00 53.90  ?  152 MET A CE  1 
ATOM   1099 N N   . PRO A 1 153 ? 31.710 -4.086  21.525  1.00 72.67  ?  153 PRO A N   1 
ATOM   1100 C CA  . PRO A 1 153 ? 31.513 -2.696  21.976  1.00 79.43  ?  153 PRO A CA  1 
ATOM   1101 C C   . PRO A 1 153 ? 32.787 -1.902  22.243  1.00 77.05  ?  153 PRO A C   1 
ATOM   1102 O O   . PRO A 1 153 ? 32.815 -0.747  21.817  1.00 74.76  ?  153 PRO A O   1 
ATOM   1103 C CB  . PRO A 1 153 ? 30.657 -2.844  23.247  1.00 72.49  ?  153 PRO A CB  1 
ATOM   1104 C CG  . PRO A 1 153 ? 30.692 -4.307  23.585  1.00 78.13  ?  153 PRO A CG  1 
ATOM   1105 C CD  . PRO A 1 153 ? 30.918 -5.045  22.312  1.00 71.53  ?  153 PRO A CD  1 
ATOM   1106 N N   . ASP A 1 154 ? 33.820 -2.440  22.914  1.00 74.31  ?  154 ASP A N   1 
ATOM   1107 C CA  . ASP A 1 154 ? 35.034 -1.660  23.193  1.00 69.10  ?  154 ASP A CA  1 
ATOM   1108 C C   . ASP A 1 154 ? 36.312 -2.495  23.020  1.00 63.69  ?  154 ASP A C   1 
ATOM   1109 O O   . ASP A 1 154 ? 36.560 -3.421  23.802  1.00 67.52  ?  154 ASP A O   1 
ATOM   1110 C CB  . ASP A 1 154 ? 34.973 -1.060  24.611  1.00 58.80  ?  154 ASP A CB  1 
ATOM   1111 C CG  . ASP A 1 154 ? 36.205 -0.210  24.936  1.00 70.72  ?  154 ASP A CG  1 
ATOM   1112 O OD1 . ASP A 1 154 ? 36.334 0.868   24.314  1.00 76.77  ?  154 ASP A OD1 1 
ATOM   1113 O OD2 . ASP A 1 154 ? 37.059 -0.626  25.769  1.00 76.33  -1 154 ASP A OD2 1 
ATOM   1114 N N   . ARG A 1 155 ? 37.166 -2.123  22.043  1.00 63.20  ?  155 ARG A N   1 
ATOM   1115 C CA  . ARG A 1 155 ? 38.349 -2.938  21.731  1.00 55.43  ?  155 ARG A CA  1 
ATOM   1116 C C   . ARG A 1 155 ? 39.332 -3.003  22.879  1.00 59.70  ?  155 ARG A C   1 
ATOM   1117 O O   . ARG A 1 155 ? 39.904 -4.067  23.140  1.00 63.90  ?  155 ARG A O   1 
ATOM   1118 C CB  . ARG A 1 155 ? 39.085 -2.423  20.502  1.00 55.00  ?  155 ARG A CB  1 
ATOM   1119 C CG  . ARG A 1 155 ? 38.453 -2.829  19.220  1.00 65.83  ?  155 ARG A CG  1 
ATOM   1120 C CD  . ARG A 1 155 ? 38.920 -1.978  18.081  1.00 62.92  ?  155 ARG A CD  1 
ATOM   1121 N NE  . ARG A 1 155 ? 37.768 -1.535  17.287  1.00 62.55  ?  155 ARG A NE  1 
ATOM   1122 C CZ  . ARG A 1 155 ? 37.400 -2.130  16.173  1.00 66.16  ?  155 ARG A CZ  1 
ATOM   1123 N NH1 . ARG A 1 155 ? 38.108 -3.166  15.773  1.00 66.38  ?  155 ARG A NH1 1 
ATOM   1124 N NH2 . ARG A 1 155 ? 36.363 -1.695  15.469  1.00 67.93  ?  155 ARG A NH2 1 
ATOM   1125 N N   . ALA A 1 156 ? 39.576 -1.880  23.557  1.00 67.64  ?  156 ALA A N   1 
ATOM   1126 C CA  . ALA A 1 156 ? 40.538 -1.901  24.658  1.00 64.04  ?  156 ALA A CA  1 
ATOM   1127 C C   . ALA A 1 156 ? 40.158 -2.940  25.711  1.00 66.87  ?  156 ALA A C   1 
ATOM   1128 O O   . ALA A 1 156 ? 40.988 -3.766  26.109  1.00 64.65  ?  156 ALA A O   1 
ATOM   1129 C CB  . ALA A 1 156 ? 40.645 -0.524  25.284  1.00 47.74  ?  156 ALA A CB  1 
ATOM   1130 N N   . GLN A 1 157 ? 38.890 -2.946  26.146  1.00 61.01  ?  157 GLN A N   1 
ATOM   1131 C CA  . GLN A 1 157 ? 38.494 -3.914  27.166  1.00 62.23  ?  157 GLN A CA  1 
ATOM   1132 C C   . GLN A 1 157 ? 38.539 -5.343  26.620  1.00 67.57  ?  157 GLN A C   1 
ATOM   1133 O O   . GLN A 1 157 ? 39.066 -6.260  27.280  1.00 63.90  ?  157 GLN A O   1 
ATOM   1134 C CB  . GLN A 1 157 ? 37.103 -3.589  27.722  1.00 59.02  ?  157 GLN A CB  1 
ATOM   1135 C CG  . GLN A 1 157 ? 36.835 -4.324  29.062  1.00 70.44  ?  157 GLN A CG  1 
ATOM   1136 C CD  . GLN A 1 157 ? 35.439 -4.083  29.620  1.00 83.74  ?  157 GLN A CD  1 
ATOM   1137 O OE1 . GLN A 1 157 ? 34.704 -3.209  29.151  1.00 86.36  ?  157 GLN A OE1 1 
ATOM   1138 N NE2 . GLN A 1 157 ? 35.053 -4.888  30.612  1.00 92.49  ?  157 GLN A NE2 1 
ATOM   1139 N N   . VAL A 1 158 ? 37.996 -5.553  25.414  1.00 64.98  ?  158 VAL A N   1 
ATOM   1140 C CA  . VAL A 1 158 ? 38.077 -6.873  24.793  1.00 62.05  ?  158 VAL A CA  1 
ATOM   1141 C C   . VAL A 1 158 ? 39.524 -7.362  24.786  1.00 58.23  ?  158 VAL A C   1 
ATOM   1142 O O   . VAL A 1 158 ? 39.819 -8.502  25.175  1.00 56.79  ?  158 VAL A O   1 
ATOM   1143 C CB  . VAL A 1 158 ? 37.473 -6.838  23.378  1.00 68.27  ?  158 VAL A CB  1 
ATOM   1144 C CG1 . VAL A 1 158 ? 37.901 -8.078  22.566  1.00 57.04  ?  158 VAL A CG1 1 
ATOM   1145 C CG2 . VAL A 1 158 ? 35.917 -6.718  23.445  1.00 69.35  ?  158 VAL A CG2 1 
ATOM   1146 N N   . LEU A 1 159 ? 40.461 -6.488  24.407  1.00 55.60  ?  159 LEU A N   1 
ATOM   1147 C CA  . LEU A 1 159 ? 41.859 -6.912  24.397  1.00 57.24  ?  159 LEU A CA  1 
ATOM   1148 C C   . LEU A 1 159 ? 42.365 -7.210  25.808  1.00 62.40  ?  159 LEU A C   1 
ATOM   1149 O O   . LEU A 1 159 ? 43.149 -8.152  26.005  1.00 57.95  ?  159 LEU A O   1 
ATOM   1150 C CB  . LEU A 1 159 ? 42.733 -5.871  23.692  1.00 53.96  ?  159 LEU A CB  1 
ATOM   1151 C CG  . LEU A 1 159 ? 42.408 -5.752  22.200  1.00 51.01  ?  159 LEU A CG  1 
ATOM   1152 C CD1 . LEU A 1 159 ? 42.922 -4.458  21.588  1.00 60.59  ?  159 LEU A CD1 1 
ATOM   1153 C CD2 . LEU A 1 159 ? 42.929 -6.923  21.451  1.00 42.82  ?  159 LEU A CD2 1 
ATOM   1154 N N   . ALA A 1 160 ? 41.929 -6.432  26.809  1.00 59.09  ?  160 ALA A N   1 
ATOM   1155 C CA  . ALA A 1 160 ? 42.354 -6.726  28.179  1.00 58.47  ?  160 ALA A CA  1 
ATOM   1156 C C   . ALA A 1 160 ? 41.933 -8.133  28.582  1.00 64.25  ?  160 ALA A C   1 
ATOM   1157 O O   . ALA A 1 160 ? 42.743 -8.913  29.109  1.00 66.69  ?  160 ALA A O   1 
ATOM   1158 C CB  . ALA A 1 160 ? 41.795 -5.700  29.155  1.00 43.97  ?  160 ALA A CB  1 
ATOM   1159 N N   . GLN A 1 161 ? 40.677 -8.492  28.296  1.00 59.32  ?  161 GLN A N   1 
ATOM   1160 C CA  . GLN A 1 161 ? 40.219 -9.851  28.573  1.00 62.47  ?  161 GLN A CA  1 
ATOM   1161 C C   . GLN A 1 161 ? 41.109 -10.898 27.895  1.00 63.93  ?  161 GLN A C   1 
ATOM   1162 O O   . GLN A 1 161 ? 41.618 -11.814 28.560  1.00 67.17  ?  161 GLN A O   1 
ATOM   1163 C CB  . GLN A 1 161 ? 38.762 -10.004 28.150  1.00 57.27  ?  161 GLN A CB  1 
ATOM   1164 C CG  . GLN A 1 161 ? 37.807 -9.118  28.954  1.00 67.84  ?  161 GLN A CG  1 
ATOM   1165 C CD  . GLN A 1 161 ? 37.844 -9.399  30.469  1.00 65.69  ?  161 GLN A CD  1 
ATOM   1166 O OE1 . GLN A 1 161 ? 37.613 -10.531 30.930  1.00 58.22  ?  161 GLN A OE1 1 
ATOM   1167 N NE2 . GLN A 1 161 ? 38.167 -8.368  31.238  1.00 67.19  ?  161 GLN A NE2 1 
ATOM   1168 N N   . VAL A 1 162 ? 41.327 -10.766 26.576  1.00 57.86  ?  162 VAL A N   1 
ATOM   1169 C CA  . VAL A 1 162 ? 42.195 -11.706 25.863  1.00 55.73  ?  162 VAL A CA  1 
ATOM   1170 C C   . VAL A 1 162 ? 43.552 -11.794 26.552  1.00 62.91  ?  162 VAL A C   1 
ATOM   1171 O O   . VAL A 1 162 ? 44.098 -12.889 26.765  1.00 65.06  ?  162 VAL A O   1 
ATOM   1172 C CB  . VAL A 1 162 ? 42.347 -11.281 24.389  1.00 55.73  ?  162 VAL A CB  1 
ATOM   1173 C CG1 . VAL A 1 162 ? 43.374 -12.150 23.671  1.00 45.07  ?  162 VAL A CG1 1 
ATOM   1174 C CG2 . VAL A 1 162 ? 41.008 -11.296 23.670  1.00 57.68  ?  162 VAL A CG2 1 
ATOM   1175 N N   . GLY A 1 163 ? 44.124 -10.636 26.905  1.00 59.69  ?  163 GLY A N   1 
ATOM   1176 C CA  . GLY A 1 163 ? 45.416 -10.640 27.578  1.00 49.04  ?  163 GLY A CA  1 
ATOM   1177 C C   . GLY A 1 163 ? 45.400 -11.410 28.885  1.00 50.09  ?  163 GLY A C   1 
ATOM   1178 O O   . GLY A 1 163 ? 46.358 -12.108 29.216  1.00 55.81  ?  163 GLY A O   1 
ATOM   1179 N N   . ARG A 1 164 ? 44.301 -11.307 29.634  1.00 46.75  ?  164 ARG A N   1 
ATOM   1180 C CA  . ARG A 1 164 ? 44.228 -11.972 30.932  1.00 52.04  ?  164 ARG A CA  1 
ATOM   1181 C C   . ARG A 1 164 ? 44.114 -13.494 30.797  1.00 68.83  ?  164 ARG A C   1 
ATOM   1182 O O   . ARG A 1 164 ? 44.709 -14.240 31.591  1.00 70.63  ?  164 ARG A O   1 
ATOM   1183 C CB  . ARG A 1 164 ? 43.051 -11.414 31.721  1.00 54.65  ?  164 ARG A CB  1 
ATOM   1184 C CG  . ARG A 1 164 ? 42.783 -12.173 32.979  1.00 58.72  ?  164 ARG A CG  1 
ATOM   1185 C CD  . ARG A 1 164 ? 41.622 -11.577 33.738  1.00 66.12  ?  164 ARG A CD  1 
ATOM   1186 N NE  . ARG A 1 164 ? 40.334 -11.705 33.055  1.00 70.55  ?  164 ARG A NE  1 
ATOM   1187 C CZ  . ARG A 1 164 ? 39.649 -12.843 32.973  1.00 67.56  ?  164 ARG A CZ  1 
ATOM   1188 N NH1 . ARG A 1 164 ? 40.144 -13.957 33.507  1.00 70.20  ?  164 ARG A NH1 1 
ATOM   1189 N NH2 . ARG A 1 164 ? 38.481 -12.877 32.344  1.00 61.05  ?  164 ARG A NH2 1 
ATOM   1190 N N   . VAL A 1 165 ? 43.343 -13.981 29.812  1.00 65.28  ?  165 VAL A N   1 
ATOM   1191 C CA  . VAL A 1 165 ? 43.162 -15.425 29.677  1.00 58.31  ?  165 VAL A CA  1 
ATOM   1192 C C   . VAL A 1 165 ? 44.256 -16.077 28.857  1.00 65.67  ?  165 VAL A C   1 
ATOM   1193 O O   . VAL A 1 165 ? 44.403 -17.303 28.912  1.00 73.99  ?  165 VAL A O   1 
ATOM   1194 C CB  . VAL A 1 165 ? 41.802 -15.803 29.059  1.00 52.16  ?  165 VAL A CB  1 
ATOM   1195 C CG1 . VAL A 1 165 ? 40.635 -15.281 29.921  1.00 53.14  ?  165 VAL A CG1 1 
ATOM   1196 C CG2 . VAL A 1 165 ? 41.691 -15.315 27.643  1.00 47.96  ?  165 VAL A CG2 1 
ATOM   1197 N N   . LEU A 1 166 ? 45.008 -15.311 28.071  1.00 64.44  ?  166 LEU A N   1 
ATOM   1198 C CA  . LEU A 1 166 ? 46.086 -15.892 27.286  1.00 57.32  ?  166 LEU A CA  1 
ATOM   1199 C C   . LEU A 1 166 ? 47.207 -16.378 28.192  1.00 60.33  ?  166 LEU A C   1 
ATOM   1200 O O   . LEU A 1 166 ? 47.484 -15.787 29.232  1.00 69.52  ?  166 LEU A O   1 
ATOM   1201 C CB  . LEU A 1 166 ? 46.620 -14.873 26.291  1.00 56.75  ?  166 LEU A CB  1 
ATOM   1202 C CG  . LEU A 1 166 ? 46.222 -15.056 24.823  1.00 58.33  ?  166 LEU A CG  1 
ATOM   1203 C CD1 . LEU A 1 166 ? 46.928 -14.015 23.925  1.00 53.30  ?  166 LEU A CD1 1 
ATOM   1204 C CD2 . LEU A 1 166 ? 46.539 -16.476 24.357  1.00 49.71  ?  166 LEU A CD2 1 
ATOM   1205 N N   . ARG A 1 167 ? 47.788 -17.383 27.834  1.00 63.21  ?  167 ARG A N   1 
ATOM   1206 C CA  . ARG A 1 167 ? 48.921 -17.835 28.623  1.00 63.24  ?  167 ARG A CA  1 
ATOM   1207 C C   . ARG A 1 167 ? 50.207 -17.157 28.159  1.00 67.94  ?  167 ARG A C   1 
ATOM   1208 O O   . ARG A 1 167 ? 50.341 -16.811 26.982  1.00 65.69  ?  167 ARG A O   1 
ATOM   1209 C CB  . ARG A 1 167 ? 49.082 -19.348 28.502  1.00 58.90  ?  167 ARG A CB  1 
ATOM   1210 C CG  . ARG A 1 167 ? 47.954 -20.118 29.111  1.00 59.69  ?  167 ARG A CG  1 
ATOM   1211 C CD  . ARG A 1 167 ? 48.167 -21.616 29.016  1.00 62.92  ?  167 ARG A CD  1 
ATOM   1212 N NE  . ARG A 1 167 ? 47.050 -22.329 29.632  1.00 68.34  ?  167 ARG A NE  1 
ATOM   1213 C CZ  . ARG A 1 167 ? 46.658 -23.554 29.297  1.00 67.64  ?  167 ARG A CZ  1 
ATOM   1214 N NH1 . ARG A 1 167 ? 47.273 -24.215 28.326  1.00 71.52  ?  167 ARG A NH1 1 
ATOM   1215 N NH2 . ARG A 1 167 ? 45.640 -24.115 29.932  1.00 66.41  ?  167 ARG A NH2 1 
ATOM   1216 N N   . PRO A 1 168 ? 51.169 -16.961 29.077  1.00 71.06  ?  168 PRO A N   1 
ATOM   1217 C CA  . PRO A 1 168 ? 52.495 -16.459 28.675  1.00 72.27  ?  168 PRO A CA  1 
ATOM   1218 C C   . PRO A 1 168 ? 53.031 -17.115 27.409  1.00 66.27  ?  168 PRO A C   1 
ATOM   1219 O O   . PRO A 1 168 ? 53.160 -18.340 27.354  1.00 68.37  ?  168 PRO A O   1 
ATOM   1220 C CB  . PRO A 1 168 ? 53.368 -16.798 29.894  1.00 72.22  ?  168 PRO A CB  1 
ATOM   1221 C CG  . PRO A 1 168 ? 52.419 -16.642 31.059  1.00 62.86  ?  168 PRO A CG  1 
ATOM   1222 C CD  . PRO A 1 168 ? 51.064 -17.118 30.543  1.00 72.19  ?  168 PRO A CD  1 
ATOM   1223 N N   . GLY A 1 169 ? 53.337 -16.310 26.389  1.00 59.18  ?  169 GLY A N   1 
ATOM   1224 C CA  . GLY A 1 169 ? 53.740 -16.827 25.105  1.00 48.59  ?  169 GLY A CA  1 
ATOM   1225 C C   . GLY A 1 169 ? 52.607 -17.113 24.138  1.00 65.71  ?  169 GLY A C   1 
ATOM   1226 O O   . GLY A 1 169 ? 52.871 -17.593 23.027  1.00 67.75  ?  169 GLY A O   1 
ATOM   1227 N N   . GLY A 1 170 ? 51.341 -16.851 24.525  1.00 67.39  ?  170 GLY A N   1 
ATOM   1228 C CA  . GLY A 1 170 ? 50.218 -17.155 23.666  1.00 55.35  ?  170 GLY A CA  1 
ATOM   1229 C C   . GLY A 1 170 ? 49.931 -16.014 22.715  1.00 59.50  ?  170 GLY A C   1 
ATOM   1230 O O   . GLY A 1 170 ? 50.338 -14.880 22.959  1.00 64.82  ?  170 GLY A O   1 
ATOM   1231 N N   . ARG A 1 171 ? 49.229 -16.320 21.621  1.00 53.60  ?  171 ARG A N   1 
ATOM   1232 C CA  . ARG A 1 171 ? 49.032 -15.359 20.554  1.00 56.79  ?  171 ARG A CA  1 
ATOM   1233 C C   . ARG A 1 171 ? 47.559 -15.102 20.290  1.00 58.62  ?  171 ARG A C   1 
ATOM   1234 O O   . ARG A 1 171 ? 46.713 -16.002 20.383  1.00 50.35  ?  171 ARG A O   1 
ATOM   1235 C CB  . ARG A 1 171 ? 49.667 -15.815 19.242  1.00 56.23  ?  171 ARG A CB  1 
ATOM   1236 C CG  . ARG A 1 171 ? 51.151 -15.865 19.227  1.00 60.32  ?  171 ARG A CG  1 
ATOM   1237 C CD  . ARG A 1 171 ? 51.658 -16.349 17.880  1.00 54.46  ?  171 ARG A CD  1 
ATOM   1238 N NE  . ARG A 1 171 ? 52.853 -17.145 18.077  1.00 65.89  ?  171 ARG A NE  1 
ATOM   1239 C CZ  . ARG A 1 171 ? 54.063 -16.629 18.206  1.00 75.55  ?  171 ARG A CZ  1 
ATOM   1240 N NH1 . ARG A 1 171 ? 54.215 -15.317 18.140  1.00 85.01  ?  171 ARG A NH1 1 
ATOM   1241 N NH2 . ARG A 1 171 ? 55.109 -17.424 18.397  1.00 70.98  ?  171 ARG A NH2 1 
ATOM   1242 N N   . LEU A 1 172 ? 47.299 -13.866 19.893  1.00 52.26  ?  172 LEU A N   1 
ATOM   1243 C CA  . LEU A 1 172 ? 45.993 -13.383 19.487  1.00 52.05  ?  172 LEU A CA  1 
ATOM   1244 C C   . LEU A 1 172 ? 46.062 -13.155 17.984  1.00 59.92  ?  172 LEU A C   1 
ATOM   1245 O O   . LEU A 1 172 ? 46.944 -12.428 17.515  1.00 63.46  ?  172 LEU A O   1 
ATOM   1246 C CB  . LEU A 1 172 ? 45.665 -12.078 20.218  1.00 44.58  ?  172 LEU A CB  1 
ATOM   1247 C CG  . LEU A 1 172 ? 44.514 -11.282 19.615  1.00 49.90  ?  172 LEU A CG  1 
ATOM   1248 C CD1 . LEU A 1 172 ? 43.284 -12.175 19.465  1.00 52.84  ?  172 LEU A CD1 1 
ATOM   1249 C CD2 . LEU A 1 172 ? 44.224 -10.043 20.410  1.00 47.13  ?  172 LEU A CD2 1 
ATOM   1250 N N   . VAL A 1 173 ? 45.154 -13.760 17.226  1.00 48.65  ?  173 VAL A N   1 
ATOM   1251 C CA  . VAL A 1 173 ? 45.076 -13.506 15.791  1.00 48.18  ?  173 VAL A CA  1 
ATOM   1252 C C   . VAL A 1 173 ? 43.681 -13.000 15.509  1.00 48.50  ?  173 VAL A C   1 
ATOM   1253 O O   . VAL A 1 173 ? 42.702 -13.711 15.760  1.00 63.23  ?  173 VAL A O   1 
ATOM   1254 C CB  . VAL A 1 173 ? 45.381 -14.753 14.941  1.00 43.84  ?  173 VAL A CB  1 
ATOM   1255 C CG1 . VAL A 1 173 ? 45.206 -14.434 13.457  1.00 51.36  ?  173 VAL A CG1 1 
ATOM   1256 C CG2 . VAL A 1 173 ? 46.777 -15.224 15.170  1.00 44.93  ?  173 VAL A CG2 1 
ATOM   1257 N N   . LEU A 1 174 ? 43.580 -11.786 14.978  1.00 48.09  ?  174 LEU A N   1 
ATOM   1258 C CA  . LEU A 1 174 ? 42.272 -11.226 14.656  1.00 51.18  ?  174 LEU A CA  1 
ATOM   1259 C C   . LEU A 1 174 ? 42.323 -10.590 13.283  1.00 45.80  ?  174 LEU A C   1 
ATOM   1260 O O   . LEU A 1 174 ? 43.390 -10.254 12.778  1.00 55.27  ?  174 LEU A O   1 
ATOM   1261 C CB  . LEU A 1 174 ? 41.820 -10.185 15.696  1.00 57.92  ?  174 LEU A CB  1 
ATOM   1262 C CG  . LEU A 1 174 ? 42.749 -8.983  15.919  1.00 47.26  ?  174 LEU A CG  1 
ATOM   1263 C CD1 . LEU A 1 174 ? 42.368 -7.851  14.978  1.00 42.24  ?  174 LEU A CD1 1 
ATOM   1264 C CD2 . LEU A 1 174 ? 42.712 -8.525  17.375  1.00 38.95  ?  174 LEU A CD2 1 
ATOM   1265 N N   . THR A 1 175 ? 41.172 -10.451 12.669  1.00 49.08  ?  175 THR A N   1 
ATOM   1266 C CA  . THR A 1 175 ? 41.019 -9.469  11.613  1.00 48.91  ?  175 THR A CA  1 
ATOM   1267 C C   . THR A 1 175 ? 40.161 -8.339  12.147  1.00 53.48  ?  175 THR A C   1 
ATOM   1268 O O   . THR A 1 175 ? 39.643 -8.407  13.261  1.00 58.81  ?  175 THR A O   1 
ATOM   1269 C CB  . THR A 1 175 ? 40.412 -10.055 10.338  1.00 46.65  ?  175 THR A CB  1 
ATOM   1270 O OG1 . THR A 1 175 ? 39.099 -10.530 10.608  1.00 51.81  ?  175 THR A OG1 1 
ATOM   1271 C CG2 . THR A 1 175 ? 41.265 -11.194 9.797   1.00 48.18  ?  175 THR A CG2 1 
ATOM   1272 N N   . ASP A 1 176 ? 40.016 -7.300  11.329  1.00 57.46  ?  176 ASP A N   1 
ATOM   1273 C CA  . ASP A 1 176 ? 39.389 -6.045  11.727  1.00 54.28  ?  176 ASP A CA  1 
ATOM   1274 C C   . ASP A 1 176 ? 39.277 -5.104  10.532  1.00 50.64  ?  176 ASP A C   1 
ATOM   1275 O O   . ASP A 1 176 ? 40.098 -5.171  9.610   1.00 50.98  ?  176 ASP A O   1 
ATOM   1276 C CB  . ASP A 1 176 ? 40.199 -5.375  12.844  1.00 55.93  ?  176 ASP A CB  1 
ATOM   1277 C CG  . ASP A 1 176 ? 39.411 -4.289  13.570  1.00 54.79  ?  176 ASP A CG  1 
ATOM   1278 O OD1 . ASP A 1 176 ? 38.318 -3.896  13.081  1.00 50.89  ?  176 ASP A OD1 1 
ATOM   1279 O OD2 . ASP A 1 176 ? 39.881 -3.843  14.646  1.00 50.05  -1 176 ASP A OD2 1 
ATOM   1280 N N   . PHE A 1 177 ? 38.278 -4.221  10.559  1.00 49.27  ?  177 PHE A N   1 
ATOM   1281 C CA  . PHE A 1 177 ? 38.131 -3.164  9.565   1.00 59.89  ?  177 PHE A CA  1 
ATOM   1282 C C   . PHE A 1 177 ? 38.979 -1.948  9.949   1.00 59.32  ?  177 PHE A C   1 
ATOM   1283 O O   . PHE A 1 177 ? 39.253 -1.698  11.129  1.00 60.69  ?  177 PHE A O   1 
ATOM   1284 C CB  . PHE A 1 177 ? 36.661 -2.758  9.440   1.00 60.22  ?  177 PHE A CB  1 
ATOM   1285 C CG  . PHE A 1 177 ? 35.823 -3.724  8.639   1.00 61.96  ?  177 PHE A CG  1 
ATOM   1286 C CD1 . PHE A 1 177 ? 36.357 -4.388  7.537   1.00 64.97  ?  177 PHE A CD1 1 
ATOM   1287 C CD2 . PHE A 1 177 ? 34.495 -3.967  8.989   1.00 57.16  ?  177 PHE A CD2 1 
ATOM   1288 C CE1 . PHE A 1 177 ? 35.573 -5.281  6.784   1.00 59.56  ?  177 PHE A CE1 1 
ATOM   1289 C CE2 . PHE A 1 177 ? 33.708 -4.851  8.257   1.00 58.43  ?  177 PHE A CE2 1 
ATOM   1290 C CZ  . PHE A 1 177 ? 34.245 -5.518  7.156   1.00 61.81  ?  177 PHE A CZ  1 
ATOM   1291 N N   . PHE A 1 178 ? 39.411 -1.190  8.944   1.00 51.98  ?  178 PHE A N   1 
ATOM   1292 C CA  . PHE A 1 178 ? 40.197 -0.000  9.249   1.00 57.50  ?  178 PHE A CA  1 
ATOM   1293 C C   . PHE A 1 178 ? 40.168 0.955   8.066   1.00 65.21  ?  178 PHE A C   1 
ATOM   1294 O O   . PHE A 1 178 ? 39.767 0.604   6.950   1.00 64.67  ?  178 PHE A O   1 
ATOM   1295 C CB  . PHE A 1 178 ? 41.643 -0.349  9.656   1.00 52.32  ?  178 PHE A CB  1 
ATOM   1296 C CG  . PHE A 1 178 ? 42.585 -0.606  8.485   1.00 58.17  ?  178 PHE A CG  1 
ATOM   1297 C CD1 . PHE A 1 178 ? 42.441 -1.733  7.667   1.00 57.42  ?  178 PHE A CD1 1 
ATOM   1298 C CD2 . PHE A 1 178 ? 43.643 0.261   8.227   1.00 48.96  ?  178 PHE A CD2 1 
ATOM   1299 C CE1 . PHE A 1 178 ? 43.339 -1.963  6.597   1.00 53.20  ?  178 PHE A CE1 1 
ATOM   1300 C CE2 . PHE A 1 178 ? 44.525 0.036   7.187   1.00 45.05  ?  178 PHE A CE2 1 
ATOM   1301 C CZ  . PHE A 1 178 ? 44.379 -1.081  6.370   1.00 50.39  ?  178 PHE A CZ  1 
ATOM   1302 N N   . GLU A 1 179 ? 40.604 2.180   8.342   1.00 63.35  ?  179 GLU A N   1 
ATOM   1303 C CA  . GLU A 1 179 ? 40.622 3.270   7.381   1.00 58.31  ?  179 GLU A CA  1 
ATOM   1304 C C   . GLU A 1 179 ? 42.035 3.362   6.807   1.00 60.64  ?  179 GLU A C   1 
ATOM   1305 O O   . GLU A 1 179 ? 42.991 3.666   7.531   1.00 56.70  ?  179 GLU A O   1 
ATOM   1306 C CB  . GLU A 1 179 ? 40.192 4.553   8.078   1.00 73.51  ?  179 GLU A CB  1 
ATOM   1307 C CG  . GLU A 1 179 ? 39.383 5.512   7.241   1.00 89.21  ?  179 GLU A CG  1 
ATOM   1308 C CD  . GLU A 1 179 ? 38.554 6.496   8.083   1.00 91.32  ?  179 GLU A CD  1 
ATOM   1309 O OE1 . GLU A 1 179 ? 38.537 6.401   9.349   1.00 73.03  ?  179 GLU A OE1 1 
ATOM   1310 O OE2 . GLU A 1 179 ? 37.937 7.383   7.447   1.00 99.49  -1 179 GLU A OE2 1 
ATOM   1311 N N   . ARG A 1 180 ? 42.179 3.046   5.519   1.00 59.22  ?  180 ARG A N   1 
ATOM   1312 C CA  . ARG A 1 180 ? 43.519 3.048   4.945   1.00 58.91  ?  180 ARG A CA  1 
ATOM   1313 C C   . ARG A 1 180 ? 44.001 4.473   4.710   1.00 63.87  ?  180 ARG A C   1 
ATOM   1314 O O   . ARG A 1 180 ? 45.187 4.778   4.880   1.00 71.75  ?  180 ARG A O   1 
ATOM   1315 C CB  . ARG A 1 180 ? 43.541 2.257   3.637   1.00 63.73  ?  180 ARG A CB  1 
ATOM   1316 C CG  . ARG A 1 180 ? 42.848 0.901   3.712   1.00 73.81  ?  180 ARG A CG  1 
ATOM   1317 C CD  . ARG A 1 180 ? 42.649 0.261   2.327   1.00 65.10  ?  180 ARG A CD  1 
ATOM   1318 N NE  . ARG A 1 180 ? 43.830 -0.500  1.931   1.00 57.22  ?  180 ARG A NE  1 
ATOM   1319 C CZ  . ARG A 1 180 ? 44.011 -1.004  0.718   1.00 50.31  ?  180 ARG A CZ  1 
ATOM   1320 N NH1 . ARG A 1 180 ? 43.086 -0.836  -0.215  1.00 52.38  ?  180 ARG A NH1 1 
ATOM   1321 N NH2 . ARG A 1 180 ? 45.105 -1.686  0.449   1.00 42.96  ?  180 ARG A NH2 1 
ATOM   1322 N N   . ALA A 1 181 ? 43.079 5.337   4.312   1.00 63.38  ?  181 ALA A N   1 
ATOM   1323 C CA  . ALA A 1 181 ? 43.306 6.752   4.034   1.00 66.18  ?  181 ALA A CA  1 
ATOM   1324 C C   . ALA A 1 181 ? 41.935 7.425   4.067   1.00 77.75  ?  181 ALA A C   1 
ATOM   1325 O O   . ALA A 1 181 ? 40.924 6.763   3.874   1.00 84.63  ?  181 ALA A O   1 
ATOM   1326 C CB  . ALA A 1 181 ? 43.971 6.948   2.666   1.00 56.43  ?  181 ALA A CB  1 
ATOM   1327 N N   . PRO A 1 182 ? 41.898 8.736   4.344   1.00 78.18  ?  182 PRO A N   1 
ATOM   1328 C CA  . PRO A 1 182 ? 40.579 9.395   4.453   1.00 78.22  ?  182 PRO A CA  1 
ATOM   1329 C C   . PRO A 1 182 ? 39.680 9.075   3.265   1.00 79.86  ?  182 PRO A C   1 
ATOM   1330 O O   . PRO A 1 182 ? 40.126 8.968   2.122   1.00 84.29  ?  182 PRO A O   1 
ATOM   1331 C CB  . PRO A 1 182 ? 40.957 10.880  4.512   1.00 66.65  ?  182 PRO A CB  1 
ATOM   1332 C CG  . PRO A 1 182 ? 42.312 10.879  5.183   1.00 65.08  ?  182 PRO A CG  1 
ATOM   1333 C CD  . PRO A 1 182 ? 43.007 9.652   4.653   1.00 70.92  ?  182 PRO A CD  1 
ATOM   1334 N N   . LEU A 1 183 ? 38.401 8.860   3.537   1.00 73.62  ?  183 LEU A N   1 
ATOM   1335 C CA  . LEU A 1 183 ? 37.504 8.447   2.474   1.00 65.75  ?  183 LEU A CA  1 
ATOM   1336 C C   . LEU A 1 183 ? 36.996 9.650   1.716   1.00 73.80  ?  183 LEU A C   1 
ATOM   1337 O O   . LEU A 1 183 ? 36.482 10.607  2.313   1.00 74.82  ?  183 LEU A O   1 
ATOM   1338 C CB  . LEU A 1 183 ? 36.308 7.665   3.008   1.00 81.19  ?  183 LEU A CB  1 
ATOM   1339 C CG  . LEU A 1 183 ? 36.466 6.164   3.222   1.00 85.19  ?  183 LEU A CG  1 
ATOM   1340 C CD1 . LEU A 1 183 ? 37.023 5.955   4.616   1.00 94.77  ?  183 LEU A CD1 1 
ATOM   1341 C CD2 . LEU A 1 183 ? 35.129 5.466   3.039   1.00 77.16  ?  183 LEU A CD2 1 
ATOM   1342 N N   . ALA A 1 184 ? 37.127 9.576   0.400   1.00 76.05  ?  184 ALA A N   1 
ATOM   1343 C CA  . ALA A 1 184 ? 36.419 10.396  -0.559  1.00 81.19  ?  184 ALA A CA  1 
ATOM   1344 C C   . ALA A 1 184 ? 34.949 10.463  -0.179  1.00 88.61  ?  184 ALA A C   1 
ATOM   1345 O O   . ALA A 1 184 ? 34.406 9.489   0.356   1.00 90.85  ?  184 ALA A O   1 
ATOM   1346 C CB  . ALA A 1 184 ? 36.585 9.813   -1.958  1.00 89.29  ?  184 ALA A CB  1 
ATOM   1347 N N   . PRO A 1 185 ? 34.277 11.590  -0.437  1.00 86.59  ?  185 PRO A N   1 
ATOM   1348 C CA  . PRO A 1 185 ? 32.850 11.689  -0.084  1.00 85.80  ?  185 PRO A CA  1 
ATOM   1349 C C   . PRO A 1 185 ? 32.005 10.579  -0.670  1.00 87.93  ?  185 PRO A C   1 
ATOM   1350 O O   . PRO A 1 185 ? 31.144 10.036  0.036   1.00 89.99  ?  185 PRO A O   1 
ATOM   1351 C CB  . PRO A 1 185 ? 32.447 13.058  -0.652  1.00 87.14  ?  185 PRO A CB  1 
ATOM   1352 C CG  . PRO A 1 185 ? 33.725 13.815  -0.747  1.00 84.83  ?  185 PRO A CG  1 
ATOM   1353 C CD  . PRO A 1 185 ? 34.767 12.806  -1.103  1.00 84.96  ?  185 PRO A CD  1 
ATOM   1354 N N   . GLU A 1 186 ? 32.225 10.227  -1.945  1.00 89.35  ?  186 GLU A N   1 
ATOM   1355 C CA  . GLU A 1 186 ? 31.430 9.172   -2.573  1.00 92.67  ?  186 GLU A CA  1 
ATOM   1356 C C   . GLU A 1 186 ? 31.506 7.890   -1.769  1.00 87.64  ?  186 GLU A C   1 
ATOM   1357 O O   . GLU A 1 186 ? 30.487 7.229   -1.532  1.00 86.50  ?  186 GLU A O   1 
ATOM   1358 C CB  . GLU A 1 186 ? 31.903 8.891   -4.000  1.00 94.34  ?  186 GLU A CB  1 
ATOM   1359 C CG  . GLU A 1 186 ? 32.116 10.098  -4.883  1.00 101.06 ?  186 GLU A CG  1 
ATOM   1360 C CD  . GLU A 1 186 ? 33.495 10.730  -4.714  1.00 108.67 ?  186 GLU A CD  1 
ATOM   1361 O OE1 . GLU A 1 186 ? 34.114 10.600  -3.622  1.00 101.67 ?  186 GLU A OE1 1 
ATOM   1362 O OE2 . GLU A 1 186 ? 33.957 11.343  -5.706  1.00 117.86 -1 186 GLU A OE2 1 
ATOM   1363 N N   . GLY A 1 187 ? 32.718 7.519   -1.355  1.00 85.28  ?  187 GLY A N   1 
ATOM   1364 C CA  . GLY A 1 187 ? 32.945 6.315   -0.588  1.00 85.05  ?  187 GLY A CA  1 
ATOM   1365 C C   . GLY A 1 187 ? 32.106 6.240   0.669   1.00 88.68  ?  187 GLY A C   1 
ATOM   1366 O O   . GLY A 1 187 ? 31.297 5.321   0.833   1.00 84.16  ?  187 GLY A O   1 
ATOM   1367 N N   . ARG A 1 188 ? 32.278 7.226   1.557   1.00 93.75  ?  188 ARG A N   1 
ATOM   1368 C CA  . ARG A 1 188 ? 31.693 7.156   2.894   1.00 88.99  ?  188 ARG A CA  1 
ATOM   1369 C C   . ARG A 1 188 ? 30.168 7.059   2.883   1.00 81.50  ?  188 ARG A C   1 
ATOM   1370 O O   . ARG A 1 188 ? 29.578 6.649   3.883   1.00 77.78  ?  188 ARG A O   1 
ATOM   1371 C CB  . ARG A 1 188 ? 32.173 8.348   3.724   1.00 89.40  ?  188 ARG A CB  1 
ATOM   1372 C CG  . ARG A 1 188 ? 31.805 9.737   3.231   1.00 96.62  ?  188 ARG A CG  1 
ATOM   1373 C CD  . ARG A 1 188 ? 33.027 10.668  3.326   1.00 99.45  ?  188 ARG A CD  1 
ATOM   1374 N NE  . ARG A 1 188 ? 33.418 10.918  4.713   1.00 95.72  ?  188 ARG A NE  1 
ATOM   1375 C CZ  . ARG A 1 188 ? 32.759 11.722  5.537   1.00 94.61  ?  188 ARG A CZ  1 
ATOM   1376 N NH1 . ARG A 1 188 ? 31.676 12.353  5.096   1.00 102.25 ?  188 ARG A NH1 1 
ATOM   1377 N NH2 . ARG A 1 188 ? 33.173 11.890  6.793   1.00 84.83  ?  188 ARG A NH2 1 
ATOM   1378 N N   . ALA A 1 189 ? 29.518 7.402   1.778   1.00 85.78  ?  189 ALA A N   1 
ATOM   1379 C CA  . ALA A 1 189 ? 28.114 7.046   1.607   1.00 89.70  ?  189 ALA A CA  1 
ATOM   1380 C C   . ALA A 1 189 ? 27.887 5.558   1.864   1.00 92.16  ?  189 ALA A C   1 
ATOM   1381 O O   . ALA A 1 189 ? 27.104 5.175   2.748   1.00 84.84  ?  189 ALA A O   1 
ATOM   1382 C CB  . ALA A 1 189 ? 27.654 7.418   0.196   1.00 94.69  ?  189 ALA A CB  1 
ATOM   1383 N N   . ALA A 1 190 ? 28.567 4.701   1.088   1.00 92.92  ?  190 ALA A N   1 
ATOM   1384 C CA  . ALA A 1 190 ? 28.356 3.256   1.200   1.00 82.95  ?  190 ALA A CA  1 
ATOM   1385 C C   . ALA A 1 190 ? 28.855 2.717   2.540   1.00 82.75  ?  190 ALA A C   1 
ATOM   1386 O O   . ALA A 1 190 ? 28.167 1.929   3.206   1.00 81.63  ?  190 ALA A O   1 
ATOM   1387 C CB  . ALA A 1 190 ? 29.041 2.532   0.045   1.00 71.34  ?  190 ALA A CB  1 
ATOM   1388 N N   . VAL A 1 191 ? 30.053 3.135   2.948   1.00 77.03  ?  191 VAL A N   1 
ATOM   1389 C CA  . VAL A 1 191 ? 30.661 2.621   4.168   1.00 72.45  ?  191 VAL A CA  1 
ATOM   1390 C C   . VAL A 1 191 ? 29.830 2.952   5.411   1.00 76.39  ?  191 VAL A C   1 
ATOM   1391 O O   . VAL A 1 191 ? 29.713 2.123   6.319   1.00 73.60  ?  191 VAL A O   1 
ATOM   1392 C CB  . VAL A 1 191 ? 32.107 3.154   4.257   1.00 67.09  ?  191 VAL A CB  1 
ATOM   1393 C CG1 . VAL A 1 191 ? 32.750 2.809   5.573   1.00 60.95  ?  191 VAL A CG1 1 
ATOM   1394 C CG2 . VAL A 1 191 ? 32.913 2.589   3.106   1.00 65.43  ?  191 VAL A CG2 1 
ATOM   1395 N N   . GLN A 1 192 ? 29.224 4.138   5.482   1.00 80.67  ?  192 GLN A N   1 
ATOM   1396 C CA  . GLN A 1 192 ? 28.500 4.475   6.706   1.00 80.12  ?  192 GLN A CA  1 
ATOM   1397 C C   . GLN A 1 192 ? 27.296 3.560   6.895   1.00 78.34  ?  192 GLN A C   1 
ATOM   1398 O O   . GLN A 1 192 ? 27.077 3.023   7.987   1.00 78.53  ?  192 GLN A O   1 
ATOM   1399 C CB  . GLN A 1 192 ? 28.055 5.942   6.715   1.00 79.14  ?  192 GLN A CB  1 
ATOM   1400 C CG  . GLN A 1 192 ? 26.941 6.197   7.748   1.00 95.33  ?  192 GLN A CG  1 
ATOM   1401 C CD  . GLN A 1 192 ? 26.721 7.666   8.120   1.00 102.85 ?  192 GLN A CD  1 
ATOM   1402 O OE1 . GLN A 1 192 ? 27.586 8.514   7.911   1.00 108.28 ?  192 GLN A OE1 1 
ATOM   1403 N NE2 . GLN A 1 192 ? 25.551 7.960   8.685   1.00 100.38 ?  192 GLN A NE2 1 
ATOM   1404 N N   . ARG A 1 193 ? 26.503 3.359   5.841   1.00 72.89  ?  193 ARG A N   1 
ATOM   1405 C CA  . ARG A 1 193 ? 25.332 2.506   5.997   1.00 80.14  ?  193 ARG A CA  1 
ATOM   1406 C C   . ARG A 1 193 ? 25.731 1.043   6.221   1.00 87.14  ?  193 ARG A C   1 
ATOM   1407 O O   . ARG A 1 193 ? 24.987 0.288   6.856   1.00 81.20  ?  193 ARG A O   1 
ATOM   1408 C CB  . ARG A 1 193 ? 24.411 2.664   4.786   1.00 77.61  ?  193 ARG A CB  1 
ATOM   1409 C CG  . ARG A 1 193 ? 22.913 2.660   5.117   1.00 92.31  ?  193 ARG A CG  1 
ATOM   1410 C CD  . ARG A 1 193 ? 22.529 3.732   6.163   1.00 104.23 ?  193 ARG A CD  1 
ATOM   1411 N NE  . ARG A 1 193 ? 22.918 5.107   5.815   1.00 115.44 ?  193 ARG A NE  1 
ATOM   1412 C CZ  . ARG A 1 193 ? 23.476 5.978   6.665   1.00 116.51 ?  193 ARG A CZ  1 
ATOM   1413 N NH1 . ARG A 1 193 ? 23.695 5.642   7.933   1.00 109.82 ?  193 ARG A NH1 1 
ATOM   1414 N NH2 . ARG A 1 193 ? 23.788 7.210   6.260   1.00 120.69 ?  193 ARG A NH2 1 
ATOM   1415 N N   . TYR A 1 194 ? 26.920 0.642   5.757   1.00 82.40  ?  194 TYR A N   1 
ATOM   1416 C CA  . TYR A 1 194 ? 27.429 -0.703  6.013   1.00 78.94  ?  194 TYR A CA  1 
ATOM   1417 C C   . TYR A 1 194 ? 27.819 -0.886  7.476   1.00 74.34  ?  194 TYR A C   1 
ATOM   1418 O O   . TYR A 1 194 ? 27.436 -1.879  8.107   1.00 70.80  ?  194 TYR A O   1 
ATOM   1419 C CB  . TYR A 1 194 ? 28.625 -0.962  5.096   1.00 78.97  ?  194 TYR A CB  1 
ATOM   1420 C CG  . TYR A 1 194 ? 29.258 -2.336  5.141   1.00 65.49  ?  194 TYR A CG  1 
ATOM   1421 C CD1 . TYR A 1 194 ? 28.532 -3.490  4.848   1.00 62.77  ?  194 TYR A CD1 1 
ATOM   1422 C CD2 . TYR A 1 194 ? 30.615 -2.468  5.403   1.00 70.57  ?  194 TYR A CD2 1 
ATOM   1423 C CE1 . TYR A 1 194 ? 29.145 -4.749  4.857   1.00 58.14  ?  194 TYR A CE1 1 
ATOM   1424 C CE2 . TYR A 1 194 ? 31.235 -3.708  5.411   1.00 67.91  ?  194 TYR A CE2 1 
ATOM   1425 C CZ  . TYR A 1 194 ? 30.500 -4.842  5.137   1.00 61.36  ?  194 TYR A CZ  1 
ATOM   1426 O OH  . TYR A 1 194 ? 31.155 -6.044  5.159   1.00 55.16  ?  194 TYR A OH  1 
ATOM   1427 N N   . LEU A 1 195 ? 28.600 0.046   8.027   1.00 63.47  ?  195 LEU A N   1 
ATOM   1428 C CA  . LEU A 1 195 ? 28.915 -0.017  9.449   1.00 61.31  ?  195 LEU A CA  1 
ATOM   1429 C C   . LEU A 1 195 ? 27.642 -0.011  10.281  1.00 74.41  ?  195 LEU A C   1 
ATOM   1430 O O   . LEU A 1 195 ? 27.503 -0.788  11.232  1.00 78.77  ?  195 LEU A O   1 
ATOM   1431 C CB  . LEU A 1 195 ? 29.806 1.155   9.846   1.00 67.32  ?  195 LEU A CB  1 
ATOM   1432 C CG  . LEU A 1 195 ? 31.291 1.014   9.521   1.00 80.60  ?  195 LEU A CG  1 
ATOM   1433 C CD1 . LEU A 1 195 ? 32.064 2.290   9.892   1.00 79.33  ?  195 LEU A CD1 1 
ATOM   1434 C CD2 . LEU A 1 195 ? 31.877 -0.229  10.220  1.00 81.59  ?  195 LEU A CD2 1 
ATOM   1435 N N   . HIS A 1 196 ? 26.687 0.845   9.906   1.00 78.49  ?  196 HIS A N   1 
ATOM   1436 C CA  . HIS A 1 196 ? 25.428 0.952   10.627  1.00 71.39  ?  196 HIS A CA  1 
ATOM   1437 C C   . HIS A 1 196 ? 24.621 -0.336  10.531  1.00 72.23  ?  196 HIS A C   1 
ATOM   1438 O O   . HIS A 1 196 ? 24.253 -0.928  11.551  1.00 61.65  ?  196 HIS A O   1 
ATOM   1439 C CB  . HIS A 1 196 ? 24.619 2.127   10.076  1.00 74.35  ?  196 HIS A CB  1 
ATOM   1440 C CG  . HIS A 1 196 ? 23.364 2.389   10.842  1.00 79.52  ?  196 HIS A CG  1 
ATOM   1441 N ND1 . HIS A 1 196 ? 22.145 1.854   10.478  1.00 76.63  ?  196 HIS A ND1 1 
ATOM   1442 C CD2 . HIS A 1 196 ? 23.144 3.102   11.974  1.00 83.49  ?  196 HIS A CD2 1 
ATOM   1443 C CE1 . HIS A 1 196 ? 21.228 2.238   11.347  1.00 82.68  ?  196 HIS A CE1 1 
ATOM   1444 N NE2 . HIS A 1 196 ? 21.805 2.996   12.263  1.00 85.52  ?  196 HIS A NE2 1 
ATOM   1445 N N   . ASP A 1 197 ? 24.334 -0.787  9.299   1.00 73.76  ?  197 ASP A N   1 
ATOM   1446 C CA  . ASP A 1 197 ? 23.369 -1.865  9.073   1.00 74.00  ?  197 ASP A CA  1 
ATOM   1447 C C   . ASP A 1 197 ? 23.822 -3.220  9.620   1.00 78.76  ?  197 ASP A C   1 
ATOM   1448 O O   . ASP A 1 197 ? 23.027 -4.167  9.630   1.00 82.69  ?  197 ASP A O   1 
ATOM   1449 C CB  . ASP A 1 197 ? 23.045 -1.996  7.577   1.00 70.71  ?  197 ASP A CB  1 
ATOM   1450 C CG  . ASP A 1 197 ? 22.308 -0.767  7.010   1.00 88.82  ?  197 ASP A CG  1 
ATOM   1451 O OD1 . ASP A 1 197 ? 22.018 0.175   7.783   1.00 97.11  ?  197 ASP A OD1 1 
ATOM   1452 O OD2 . ASP A 1 197 ? 22.020 -0.745  5.786   1.00 93.76  -1 197 ASP A OD2 1 
ATOM   1453 N N   . PHE A 1 198 ? 25.061 -3.345  10.083  1.00 81.37  ?  198 PHE A N   1 
ATOM   1454 C CA  . PHE A 1 198 ? 25.532 -4.605  10.634  1.00 75.14  ?  198 PHE A CA  1 
ATOM   1455 C C   . PHE A 1 198 ? 26.179 -4.416  11.998  1.00 67.38  ?  198 PHE A C   1 
ATOM   1456 O O   . PHE A 1 198 ? 26.831 -5.330  12.500  1.00 58.09  ?  198 PHE A O   1 
ATOM   1457 C CB  . PHE A 1 198 ? 26.482 -5.281  9.647   1.00 70.51  ?  198 PHE A CB  1 
ATOM   1458 C CG  . PHE A 1 198 ? 25.792 -5.776  8.421   1.00 73.14  ?  198 PHE A CG  1 
ATOM   1459 C CD1 . PHE A 1 198 ? 25.067 -6.957  8.454   1.00 77.03  ?  198 PHE A CD1 1 
ATOM   1460 C CD2 . PHE A 1 198 ? 25.824 -5.046  7.244   1.00 77.66  ?  198 PHE A CD2 1 
ATOM   1461 C CE1 . PHE A 1 198 ? 24.409 -7.418  7.335   1.00 70.87  ?  198 PHE A CE1 1 
ATOM   1462 C CE2 . PHE A 1 198 ? 25.166 -5.496  6.113   1.00 76.28  ?  198 PHE A CE2 1 
ATOM   1463 C CZ  . PHE A 1 198 ? 24.457 -6.685  6.159   1.00 72.56  ?  198 PHE A CZ  1 
ATOM   1464 N N   . MET A 1 199 ? 25.972 -3.257  12.619  1.00 69.49  ?  199 MET A N   1 
ATOM   1465 C CA  . MET A 1 199 ? 26.446 -2.975  13.970  1.00 67.11  ?  199 MET A CA  1 
ATOM   1466 C C   . MET A 1 199 ? 27.944 -3.250  14.080  1.00 69.77  ?  199 MET A C   1 
ATOM   1467 O O   . MET A 1 199 ? 28.388 -4.144  14.788  1.00 78.47  ?  199 MET A O   1 
ATOM   1468 C CB  . MET A 1 199 ? 25.666 -3.790  15.000  1.00 62.43  ?  199 MET A CB  1 
ATOM   1469 C CG  . MET A 1 199 ? 24.161 -3.622  14.858  1.00 67.08  ?  199 MET A CG  1 
ATOM   1470 S SD  . MET A 1 199 ? 23.229 -4.429  16.166  1.00 71.57  ?  199 MET A SD  1 
ATOM   1471 C CE  . MET A 1 199 ? 21.604 -4.433  15.432  1.00 77.05  ?  199 MET A CE  1 
ATOM   1472 N N   . MET A 1 200 ? 28.707 -2.456  13.336  1.00 62.35  ?  200 MET A N   1 
ATOM   1473 C CA  . MET A 1 200 ? 30.146 -2.620  13.248  1.00 64.68  ?  200 MET A CA  1 
ATOM   1474 C C   . MET A 1 200 ? 30.848 -1.271  13.351  1.00 66.88  ?  200 MET A C   1 
ATOM   1475 O O   . MET A 1 200 ? 30.288 -0.226  13.007  1.00 60.90  ?  200 MET A O   1 
ATOM   1476 C CB  . MET A 1 200 ? 30.571 -3.253  11.926  1.00 67.90  ?  200 MET A CB  1 
ATOM   1477 C CG  . MET A 1 200 ? 29.896 -4.507  11.551  1.00 75.73  ?  200 MET A CG  1 
ATOM   1478 S SD  . MET A 1 200 ? 30.584 -5.041  9.994   1.00 71.26  ?  200 MET A SD  1 
ATOM   1479 C CE  . MET A 1 200 ? 29.773 -3.921  8.858   1.00 63.06  ?  200 MET A CE  1 
ATOM   1480 N N   . THR A 1 201 ? 32.113 -1.319  13.782  1.00 62.72  ?  201 THR A N   1 
ATOM   1481 C CA  . THR A 1 201 ? 32.968 -0.139  13.746  1.00 66.09  ?  201 THR A CA  1 
ATOM   1482 C C   . THR A 1 201 ? 34.296 -0.451  13.065  1.00 71.30  ?  201 THR A C   1 
ATOM   1483 O O   . THR A 1 201 ? 34.454 -1.489  12.419  1.00 67.61  ?  201 THR A O   1 
ATOM   1484 C CB  . THR A 1 201 ? 33.248 0.421   15.137  1.00 62.52  ?  201 THR A CB  1 
ATOM   1485 O OG1 . THR A 1 201 ? 34.315 -0.325  15.715  1.00 58.27  ?  201 THR A OG1 1 
ATOM   1486 C CG2 . THR A 1 201 ? 32.006 0.369   16.036  1.00 64.95  ?  201 THR A CG2 1 
ATOM   1487 N N   . MET A 1 202 ? 35.258 0.451   13.225  1.00 76.92  ?  202 MET A N   1 
ATOM   1488 C CA  . MET A 1 202 ? 36.387 0.602   12.324  1.00 68.77  ?  202 MET A CA  1 
ATOM   1489 C C   . MET A 1 202 ? 37.460 1.379   13.073  1.00 66.37  ?  202 MET A C   1 
ATOM   1490 O O   . MET A 1 202 ? 37.148 2.216   13.918  1.00 69.98  ?  202 MET A O   1 
ATOM   1491 C CB  . MET A 1 202 ? 35.912 1.332   11.070  1.00 62.70  ?  202 MET A CB  1 
ATOM   1492 C CG  . MET A 1 202 ? 36.827 1.458   9.904   1.00 70.66  ?  202 MET A CG  1 
ATOM   1493 S SD  . MET A 1 202 ? 35.898 2.405   8.639   1.00 75.75  ?  202 MET A SD  1 
ATOM   1494 C CE  . MET A 1 202 ? 36.240 4.071   9.220   1.00 78.21  ?  202 MET A CE  1 
ATOM   1495 N N   . VAL A 1 203 ? 38.723 1.074   12.792  1.00 67.19  ?  203 VAL A N   1 
ATOM   1496 C CA  . VAL A 1 203 ? 39.820 1.718   13.509  1.00 60.99  ?  203 VAL A CA  1 
ATOM   1497 C C   . VAL A 1 203 ? 40.857 2.246   12.540  1.00 61.35  ?  203 VAL A C   1 
ATOM   1498 O O   . VAL A 1 203 ? 40.609 2.344   11.335  1.00 68.18  ?  203 VAL A O   1 
ATOM   1499 C CB  . VAL A 1 203 ? 40.464 0.781   14.540  1.00 60.47  ?  203 VAL A CB  1 
ATOM   1500 C CG1 . VAL A 1 203 ? 39.424 0.389   15.506  1.00 60.49  ?  203 VAL A CG1 1 
ATOM   1501 C CG2 . VAL A 1 203 ? 41.064 -0.453  13.877  1.00 52.89  ?  203 VAL A CG2 1 
ATOM   1502 N N   . SER A 1 204 ? 41.991 2.676   13.082  1.00 64.91  ?  204 SER A N   1 
ATOM   1503 C CA  . SER A 1 204 ? 43.114 3.178   12.302  1.00 72.59  ?  204 SER A CA  1 
ATOM   1504 C C   . SER A 1 204 ? 44.334 2.321   12.594  1.00 69.31  ?  204 SER A C   1 
ATOM   1505 O O   . SER A 1 204 ? 44.509 1.843   13.719  1.00 76.93  ?  204 SER A O   1 
ATOM   1506 C CB  . SER A 1 204 ? 43.421 4.650   12.639  1.00 71.26  ?  204 SER A CB  1 
ATOM   1507 O OG  . SER A 1 204 ? 43.855 4.785   13.984  1.00 73.69  ?  204 SER A OG  1 
ATOM   1508 N N   . ALA A 1 205 ? 45.180 2.131   11.582  1.00 58.83  ?  205 ALA A N   1 
ATOM   1509 C CA  . ALA A 1 205 ? 46.369 1.311   11.767  1.00 52.99  ?  205 ALA A CA  1 
ATOM   1510 C C   . ALA A 1 205 ? 47.170 1.714   13.005  1.00 66.38  ?  205 ALA A C   1 
ATOM   1511 O O   . ALA A 1 205 ? 47.679 0.849   13.730  1.00 72.89  ?  205 ALA A O   1 
ATOM   1512 C CB  . ALA A 1 205 ? 47.235 1.384   10.522  1.00 61.72  ?  205 ALA A CB  1 
ATOM   1513 N N   . GLU A 1 206 ? 47.291 3.018   13.279  1.00 66.02  ?  206 GLU A N   1 
ATOM   1514 C CA  . GLU A 1 206 ? 48.036 3.440   14.467  1.00 60.01  ?  206 GLU A CA  1 
ATOM   1515 C C   . GLU A 1 206 ? 47.253 3.220   15.759  1.00 66.35  ?  206 GLU A C   1 
ATOM   1516 O O   . GLU A 1 206 ? 47.855 3.260   16.836  1.00 71.66  ?  206 GLU A O   1 
ATOM   1517 C CB  . GLU A 1 206 ? 48.461 4.906   14.352  1.00 50.22  ?  206 GLU A CB  1 
ATOM   1518 C CG  . GLU A 1 206 ? 47.332 5.912   14.212  1.00 56.96  ?  206 GLU A CG  1 
ATOM   1519 C CD  . GLU A 1 206 ? 46.788 6.026   12.802  1.00 72.93  ?  206 GLU A CD  1 
ATOM   1520 O OE1 . GLU A 1 206 ? 46.769 5.015   12.070  1.00 69.37  ?  206 GLU A OE1 1 
ATOM   1521 O OE2 . GLU A 1 206 ? 46.372 7.141   12.420  1.00 83.43  -1 206 GLU A OE2 1 
ATOM   1522 N N   . ALA A 1 207 ? 45.937 2.965   15.678  1.00 72.70  ?  207 ALA A N   1 
ATOM   1523 C CA  . ALA A 1 207 ? 45.143 2.728   16.889  1.00 74.93  ?  207 ALA A CA  1 
ATOM   1524 C C   . ALA A 1 207 ? 45.636 1.510   17.668  1.00 74.91  ?  207 ALA A C   1 
ATOM   1525 O O   . ALA A 1 207 ? 45.684 1.536   18.905  1.00 66.18  ?  207 ALA A O   1 
ATOM   1526 C CB  . ALA A 1 207 ? 43.660 2.560   16.533  1.00 65.05  ?  207 ALA A CB  1 
ATOM   1527 N N   . TYR A 1 208 ? 46.030 0.431   16.957  1.00 71.63  ?  208 TYR A N   1 
ATOM   1528 C CA  . TYR A 1 208 ? 46.220 -0.872  17.599  1.00 67.46  ?  208 TYR A CA  1 
ATOM   1529 C C   . TYR A 1 208 ? 47.447 -1.004  18.494  1.00 67.79  ?  208 TYR A C   1 
ATOM   1530 O O   . TYR A 1 208 ? 47.359 -1.676  19.528  1.00 75.82  ?  208 TYR A O   1 
ATOM   1531 C CB  . TYR A 1 208 ? 46.248 -2.006  16.565  1.00 54.84  ?  208 TYR A CB  1 
ATOM   1532 C CG  . TYR A 1 208 ? 44.924 -2.703  16.411  1.00 50.36  ?  208 TYR A CG  1 
ATOM   1533 C CD1 . TYR A 1 208 ? 44.474 -3.596  17.381  1.00 51.62  ?  208 TYR A CD1 1 
ATOM   1534 C CD2 . TYR A 1 208 ? 44.108 -2.451  15.309  1.00 54.71  ?  208 TYR A CD2 1 
ATOM   1535 C CE1 . TYR A 1 208 ? 43.250 -4.227  17.263  1.00 54.72  ?  208 TYR A CE1 1 
ATOM   1536 C CE2 . TYR A 1 208 ? 42.876 -3.076  15.174  1.00 58.20  ?  208 TYR A CE2 1 
ATOM   1537 C CZ  . TYR A 1 208 ? 42.468 -3.968  16.159  1.00 61.83  ?  208 TYR A CZ  1 
ATOM   1538 O OH  . TYR A 1 208 ? 41.269 -4.595  16.041  1.00 63.96  ?  208 TYR A OH  1 
ATOM   1539 N N   . PRO A 1 209 ? 48.612 -0.477  18.147  1.00 63.88  ?  209 PRO A N   1 
ATOM   1540 C CA  . PRO A 1 209 ? 49.785 -0.725  19.011  1.00 65.21  ?  209 PRO A CA  1 
ATOM   1541 C C   . PRO A 1 209 ? 49.583 -0.194  20.424  1.00 73.99  ?  209 PRO A C   1 
ATOM   1542 O O   . PRO A 1 209 ? 49.960 -0.884  21.388  1.00 75.34  ?  209 PRO A O   1 
ATOM   1543 C CB  . PRO A 1 209 ? 50.936 -0.016  18.274  1.00 62.87  ?  209 PRO A CB  1 
ATOM   1544 C CG  . PRO A 1 209 ? 50.525 -0.042  16.865  1.00 54.47  ?  209 PRO A CG  1 
ATOM   1545 C CD  . PRO A 1 209 ? 49.009 0.110   16.856  1.00 57.57  ?  209 PRO A CD  1 
ATOM   1546 N N   . PRO A 1 210 ? 48.992 1.002   20.628  1.00 73.90  ?  210 PRO A N   1 
ATOM   1547 C CA  . PRO A 1 210 ? 48.609 1.359   22.018  1.00 71.84  ?  210 PRO A CA  1 
ATOM   1548 C C   . PRO A 1 210 ? 47.520 0.455   22.614  1.00 70.03  ?  210 PRO A C   1 
ATOM   1549 O O   . PRO A 1 210 ? 47.707 -0.080  23.713  1.00 56.06  ?  210 PRO A O   1 
ATOM   1550 C CB  . PRO A 1 210 ? 48.161 2.828   21.904  1.00 61.51  ?  210 PRO A CB  1 
ATOM   1551 C CG  . PRO A 1 210 ? 47.985 3.102   20.436  1.00 65.00  ?  210 PRO A CG  1 
ATOM   1552 C CD  . PRO A 1 210 ? 48.942 2.188   19.737  1.00 64.37  ?  210 PRO A CD  1 
ATOM   1553 N N   . LEU A 1 211 ? 46.399 0.253   21.915  1.00 68.38  ?  211 LEU A N   1 
ATOM   1554 C CA  . LEU A 1 211 ? 45.391 -0.708  22.377  1.00 64.18  ?  211 LEU A CA  1 
ATOM   1555 C C   . LEU A 1 211 ? 46.015 -2.022  22.822  1.00 61.10  ?  211 LEU A C   1 
ATOM   1556 O O   . LEU A 1 211 ? 45.739 -2.520  23.921  1.00 63.51  ?  211 LEU A O   1 
ATOM   1557 C CB  . LEU A 1 211 ? 44.397 -0.987  21.264  1.00 61.17  ?  211 LEU A CB  1 
ATOM   1558 C CG  . LEU A 1 211 ? 43.409 0.140   21.053  1.00 60.85  ?  211 LEU A CG  1 
ATOM   1559 C CD1 . LEU A 1 211 ? 42.666 -0.081  19.746  1.00 61.46  ?  211 LEU A CD1 1 
ATOM   1560 C CD2 . LEU A 1 211 ? 42.472 0.207   22.248  1.00 51.79  ?  211 LEU A CD2 1 
ATOM   1561 N N   . LEU A 1 212 ? 46.841 -2.614  21.966  1.00 66.43  ?  212 LEU A N   1 
ATOM   1562 C CA  . LEU A 1 212 ? 47.515 -3.845  22.354  1.00 68.45  ?  212 LEU A CA  1 
ATOM   1563 C C   . LEU A 1 212 ? 48.308 -3.655  23.638  1.00 71.24  ?  212 LEU A C   1 
ATOM   1564 O O   . LEU A 1 212 ? 48.326 -4.552  24.488  1.00 69.13  ?  212 LEU A O   1 
ATOM   1565 C CB  . LEU A 1 212 ? 48.427 -4.329  21.222  1.00 62.58  ?  212 LEU A CB  1 
ATOM   1566 C CG  . LEU A 1 212 ? 47.919 -5.313  20.170  1.00 66.60  ?  212 LEU A CG  1 
ATOM   1567 C CD1 . LEU A 1 212 ? 46.521 -4.986  19.667  1.00 70.86  ?  212 LEU A CD1 1 
ATOM   1568 C CD2 . LEU A 1 212 ? 48.912 -5.360  19.023  1.00 58.57  ?  212 LEU A CD2 1 
ATOM   1569 N N   . ARG A 1 213 ? 49.015 -2.566  23.757  1.00 71.93  ?  213 ARG A N   1 
ATOM   1570 C CA  . ARG A 1 213 ? 49.875 -2.347  24.901  1.00 74.68  ?  213 ARG A CA  1 
ATOM   1571 C C   . ARG A 1 213 ? 49.106 -2.251  26.161  1.00 80.78  ?  213 ARG A C   1 
ATOM   1572 O O   . ARG A 1 213 ? 49.463 -2.797  27.181  1.00 82.63  ?  213 ARG A O   1 
ATOM   1573 C CB  . ARG A 1 213 ? 50.569 -1.035  24.696  1.00 72.58  ?  213 ARG A CB  1 
ATOM   1574 C CG  . ARG A 1 213 ? 52.036 -1.019  25.050  1.00 83.23  ?  213 ARG A CG  1 
ATOM   1575 C CD  . ARG A 1 213 ? 52.500 0.395   25.348  1.00 83.64  ?  213 ARG A CD  1 
ATOM   1576 N NE  . ARG A 1 213 ? 52.067 1.349   24.335  1.00 87.14  ?  213 ARG A NE  1 
ATOM   1577 C CZ  . ARG A 1 213 ? 52.647 1.497   23.154  1.00 81.44  ?  213 ARG A CZ  1 
ATOM   1578 N NH1 . ARG A 1 213 ? 53.687 0.754   22.832  1.00 75.97  ?  213 ARG A NH1 1 
ATOM   1579 N NH2 . ARG A 1 213 ? 52.189 2.389   22.298  1.00 76.76  ?  213 ARG A NH2 1 
ATOM   1580 N N   . GLY A 1 214 ? 48.030 -1.533  26.087  1.00 71.90  ?  214 GLY A N   1 
ATOM   1581 C CA  . GLY A 1 214 ? 47.203 -1.401  27.217  1.00 64.93  ?  214 GLY A CA  1 
ATOM   1582 C C   . GLY A 1 214 ? 46.886 -2.711  27.789  1.00 81.83  ?  214 GLY A C   1 
ATOM   1583 O O   . GLY A 1 214 ? 46.739 -2.768  28.987  1.00 99.22  ?  214 GLY A O   1 
ATOM   1584 N N   . ALA A 1 215 ? 46.852 -3.756  27.000  1.00 74.78  ?  215 ALA A N   1 
ATOM   1585 C CA  . ALA A 1 215 ? 46.419 -5.032  27.480  1.00 70.45  ?  215 ALA A CA  1 
ATOM   1586 C C   . ALA A 1 215 ? 47.499 -5.974  27.737  1.00 65.74  ?  215 ALA A C   1 
ATOM   1587 O O   . ALA A 1 215 ? 47.290 -7.139  27.902  1.00 65.00  ?  215 ALA A O   1 
ATOM   1588 C CB  . ALA A 1 215 ? 45.566 -5.619  26.442  1.00 69.50  ?  215 ALA A CB  1 
ATOM   1589 N N   . GLY A 1 216 ? 48.673 -5.465  27.750  1.00 62.74  ?  216 GLY A N   1 
ATOM   1590 C CA  . GLY A 1 216 ? 49.813 -6.322  27.973  1.00 58.96  ?  216 GLY A CA  1 
ATOM   1591 C C   . GLY A 1 216 ? 50.169 -7.180  26.787  1.00 67.79  ?  216 GLY A C   1 
ATOM   1592 O O   . GLY A 1 216 ? 50.735 -8.264  26.967  1.00 71.39  ?  216 GLY A O   1 
ATOM   1593 N N   . LEU A 1 217 ? 49.870 -6.718  25.568  1.00 71.81  ?  217 LEU A N   1 
ATOM   1594 C CA  . LEU A 1 217 ? 50.136 -7.474  24.348  1.00 67.28  ?  217 LEU A CA  1 
ATOM   1595 C C   . LEU A 1 217 ? 51.086 -6.718  23.423  1.00 65.04  ?  217 LEU A C   1 
ATOM   1596 O O   . LEU A 1 217 ? 50.907 -5.516  23.179  1.00 74.19  ?  217 LEU A O   1 
ATOM   1597 C CB  . LEU A 1 217 ? 48.817 -7.786  23.618  1.00 66.07  ?  217 LEU A CB  1 
ATOM   1598 C CG  . LEU A 1 217 ? 47.948 -8.787  24.393  1.00 67.95  ?  217 LEU A CG  1 
ATOM   1599 C CD1 . LEU A 1 217 ? 46.570 -8.886  23.774  1.00 72.27  ?  217 LEU A CD1 1 
ATOM   1600 C CD2 . LEU A 1 217 ? 48.624 -10.168 24.480  1.00 57.24  ?  217 LEU A CD2 1 
ATOM   1601 N N   . TRP A 1 218 ? 52.081 -7.437  22.901  1.00 55.53  ?  218 TRP A N   1 
ATOM   1602 C CA  . TRP A 1 218 ? 53.055 -6.910  21.941  1.00 57.70  ?  218 TRP A CA  1 
ATOM   1603 C C   . TRP A 1 218 ? 52.632 -7.184  20.501  1.00 60.16  ?  218 TRP A C   1 
ATOM   1604 O O   . TRP A 1 218 ? 52.354 -8.336  20.150  1.00 64.60  ?  218 TRP A O   1 
ATOM   1605 C CB  . TRP A 1 218 ? 54.426 -7.541  22.158  1.00 53.18  ?  218 TRP A CB  1 
ATOM   1606 C CG  . TRP A 1 218 ? 55.041 -7.226  23.468  1.00 65.18  ?  218 TRP A CG  1 
ATOM   1607 C CD1 . TRP A 1 218 ? 54.442 -6.626  24.542  1.00 63.73  ?  218 TRP A CD1 1 
ATOM   1608 C CD2 . TRP A 1 218 ? 56.391 -7.475  23.848  1.00 72.22  ?  218 TRP A CD2 1 
ATOM   1609 N NE1 . TRP A 1 218 ? 55.334 -6.501  25.564  1.00 64.78  ?  218 TRP A NE1 1 
ATOM   1610 C CE2 . TRP A 1 218 ? 56.540 -7.018  25.171  1.00 70.82  ?  218 TRP A CE2 1 
ATOM   1611 C CE3 . TRP A 1 218 ? 57.493 -8.044  23.197  1.00 73.87  ?  218 TRP A CE3 1 
ATOM   1612 C CZ2 . TRP A 1 218 ? 57.751 -7.106  25.862  1.00 72.39  ?  218 TRP A CZ2 1 
ATOM   1613 C CZ3 . TRP A 1 218 ? 58.693 -8.136  23.883  1.00 83.31  ?  218 TRP A CZ3 1 
ATOM   1614 C CH2 . TRP A 1 218 ? 58.812 -7.666  25.207  1.00 81.16  ?  218 TRP A CH2 1 
ATOM   1615 N N   . LEU A 1 219 ? 52.626 -6.146  19.665  1.00 55.76  ?  219 LEU A N   1 
ATOM   1616 C CA  . LEU A 1 219 ? 52.312 -6.329  18.248  1.00 54.21  ?  219 LEU A CA  1 
ATOM   1617 C C   . LEU A 1 219 ? 53.370 -7.168  17.547  1.00 56.31  ?  219 LEU A C   1 
ATOM   1618 O O   . LEU A 1 219 ? 54.555 -6.836  17.563  1.00 58.74  ?  219 LEU A O   1 
ATOM   1619 C CB  . LEU A 1 219 ? 52.197 -4.986  17.539  1.00 55.97  ?  219 LEU A CB  1 
ATOM   1620 C CG  . LEU A 1 219 ? 52.072 -5.069  16.015  1.00 52.74  ?  219 LEU A CG  1 
ATOM   1621 C CD1 . LEU A 1 219 ? 50.823 -5.827  15.624  1.00 39.36  ?  219 LEU A CD1 1 
ATOM   1622 C CD2 . LEU A 1 219 ? 52.053 -3.668  15.378  1.00 48.82  ?  219 LEU A CD2 1 
ATOM   1623 N N   . GLU A 1 220 ? 52.936 -8.248  16.900  1.00 56.44  ?  220 GLU A N   1 
ATOM   1624 C CA  . GLU A 1 220 ? 53.864 -9.111  16.182  1.00 53.24  ?  220 GLU A CA  1 
ATOM   1625 C C   . GLU A 1 220 ? 53.752 -9.008  14.676  1.00 56.03  ?  220 GLU A C   1 
ATOM   1626 O O   . GLU A 1 220 ? 54.766 -9.148  13.989  1.00 59.10  ?  220 GLU A O   1 
ATOM   1627 C CB  . GLU A 1 220 ? 53.661 -10.571 16.588  1.00 61.99  ?  220 GLU A CB  1 
ATOM   1628 C CG  . GLU A 1 220 ? 54.502 -11.549 15.781  1.00 70.57  ?  220 GLU A CG  1 
ATOM   1629 C CD  . GLU A 1 220 ? 54.533 -12.915 16.406  1.00 81.61  ?  220 GLU A CD  1 
ATOM   1630 O OE1 . GLU A 1 220 ? 54.028 -13.038 17.543  1.00 86.09  ?  220 GLU A OE1 1 
ATOM   1631 O OE2 . GLU A 1 220 ? 55.064 -13.859 15.785  1.00 86.40  -1 220 GLU A OE2 1 
ATOM   1632 N N   . GLU A 1 221 ? 52.555 -8.748  14.149  1.00 52.23  ?  221 GLU A N   1 
ATOM   1633 C CA  . GLU A 1 221 ? 52.351 -8.687  12.710  1.00 49.80  ?  221 GLU A CA  1 
ATOM   1634 C C   . GLU A 1 221 ? 51.167 -7.785  12.430  1.00 47.84  ?  221 GLU A C   1 
ATOM   1635 O O   . GLU A 1 221 ? 50.108 -7.953  13.039  1.00 58.61  ?  221 GLU A O   1 
ATOM   1636 C CB  . GLU A 1 221 ? 52.119 -10.090 12.097  1.00 45.11  ?  221 GLU A CB  1 
ATOM   1637 C CG  . GLU A 1 221 ? 51.758 -10.062 10.594  1.00 44.75  ?  221 GLU A CG  1 
ATOM   1638 C CD  . GLU A 1 221 ? 51.652 -11.465 9.938   1.00 57.56  ?  221 GLU A CD  1 
ATOM   1639 O OE1 . GLU A 1 221 ? 51.567 -12.479 10.666  1.00 60.64  ?  221 GLU A OE1 1 
ATOM   1640 O OE2 . GLU A 1 221 ? 51.693 -11.554 8.681   1.00 57.58  -1 221 GLU A OE2 1 
ATOM   1641 N N   . PHE A 1 222 ? 51.351 -6.834  11.527  1.00 48.18  ?  222 PHE A N   1 
ATOM   1642 C CA  . PHE A 1 222 ? 50.250 -6.069  10.965  1.00 47.76  ?  222 PHE A CA  1 
ATOM   1643 C C   . PHE A 1 222 ? 50.288 -6.241  9.458   1.00 49.39  ?  222 PHE A C   1 
ATOM   1644 O O   . PHE A 1 222 ? 51.342 -6.054  8.847   1.00 51.70  ?  222 PHE A O   1 
ATOM   1645 C CB  . PHE A 1 222 ? 50.333 -4.575  11.331  1.00 44.23  ?  222 PHE A CB  1 
ATOM   1646 C CG  . PHE A 1 222 ? 49.159 -3.772  10.830  1.00 44.26  ?  222 PHE A CG  1 
ATOM   1647 C CD1 . PHE A 1 222 ? 49.026 -3.432  9.497   1.00 49.14  ?  222 PHE A CD1 1 
ATOM   1648 C CD2 . PHE A 1 222 ? 48.148 -3.440  11.692  1.00 45.63  ?  222 PHE A CD2 1 
ATOM   1649 C CE1 . PHE A 1 222 ? 47.912 -2.728  9.051   1.00 54.96  ?  222 PHE A CE1 1 
ATOM   1650 C CE2 . PHE A 1 222 ? 47.056 -2.739  11.275  1.00 52.80  ?  222 PHE A CE2 1 
ATOM   1651 C CZ  . PHE A 1 222 ? 46.925 -2.382  9.952   1.00 56.69  ?  222 PHE A CZ  1 
ATOM   1652 N N   . LEU A 1 223 ? 49.144 -6.557  8.863   1.00 47.34  ?  223 LEU A N   1 
ATOM   1653 C CA  . LEU A 1 223 ? 49.072 -6.985  7.473   1.00 48.61  ?  223 LEU A CA  1 
ATOM   1654 C C   . LEU A 1 223 ? 47.811 -6.398  6.860   1.00 54.74  ?  223 LEU A C   1 
ATOM   1655 O O   . LEU A 1 223 ? 46.704 -6.709  7.308   1.00 57.04  ?  223 LEU A O   1 
ATOM   1656 C CB  . LEU A 1 223 ? 49.077 -8.524  7.368   1.00 46.45  ?  223 LEU A CB  1 
ATOM   1657 C CG  . LEU A 1 223 ? 49.387 -9.161  5.987   1.00 55.42  ?  223 LEU A CG  1 
ATOM   1658 C CD1 . LEU A 1 223 ? 50.597 -8.534  5.329   1.00 51.52  ?  223 LEU A CD1 1 
ATOM   1659 C CD2 . LEU A 1 223 ? 49.611 -10.666 6.064   1.00 48.58  ?  223 LEU A CD2 1 
ATOM   1660 N N   . ASP A 1 224 ? 47.977 -5.535  5.856   1.00 61.07  ?  224 ASP A N   1 
ATOM   1661 C CA  . ASP A 1 224 ? 46.846 -5.032  5.083   1.00 50.78  ?  224 ASP A CA  1 
ATOM   1662 C C   . ASP A 1 224 ? 46.499 -6.079  4.040   1.00 49.28  ?  224 ASP A C   1 
ATOM   1663 O O   . ASP A 1 224 ? 47.223 -6.264  3.056   1.00 60.63  ?  224 ASP A O   1 
ATOM   1664 C CB  . ASP A 1 224 ? 47.153 -3.689  4.427   1.00 43.33  ?  224 ASP A CB  1 
ATOM   1665 C CG  . ASP A 1 224 ? 45.972 -3.152  3.610   1.00 57.17  ?  224 ASP A CG  1 
ATOM   1666 O OD1 . ASP A 1 224 ? 44.948 -3.861  3.496   1.00 65.28  ?  224 ASP A OD1 1 
ATOM   1667 O OD2 . ASP A 1 224 ? 46.040 -2.015  3.081   1.00 65.07  -1 224 ASP A OD2 1 
ATOM   1668 N N   . ILE A 1 225 ? 45.397 -6.767  4.240   1.00 42.82  ?  225 ILE A N   1 
ATOM   1669 C CA  . ILE A 1 225 ? 44.985 -7.769  3.299   1.00 43.58  ?  225 ILE A CA  1 
ATOM   1670 C C   . ILE A 1 225 ? 43.799 -7.287  2.465   1.00 50.86  ?  225 ILE A C   1 
ATOM   1671 O O   . ILE A 1 225 ? 43.130 -8.099  1.819   1.00 51.38  ?  225 ILE A O   1 
ATOM   1672 C CB  . ILE A 1 225 ? 44.704 -9.111  3.987   1.00 44.28  ?  225 ILE A CB  1 
ATOM   1673 C CG1 . ILE A 1 225 ? 43.605 -8.966  5.050   1.00 49.37  ?  225 ILE A CG1 1 
ATOM   1674 C CG2 . ILE A 1 225 ? 45.972 -9.651  4.591   1.00 36.24  ?  225 ILE A CG2 1 
ATOM   1675 C CD1 . ILE A 1 225 ? 42.987 -10.299 5.433   1.00 49.92  ?  225 ILE A CD1 1 
ATOM   1676 N N   . SER A 1 226 ? 43.576 -5.966  2.403   1.00 47.14  ?  226 SER A N   1 
ATOM   1677 C CA  . SER A 1 226 ? 42.435 -5.444  1.649   1.00 50.32  ?  226 SER A CA  1 
ATOM   1678 C C   . SER A 1 226 ? 42.414 -5.992  0.227   1.00 53.83  ?  226 SER A C   1 
ATOM   1679 O O   . SER A 1 226 ? 41.381 -6.488  -0.241  1.00 55.59  ?  226 SER A O   1 
ATOM   1680 C CB  . SER A 1 226 ? 42.450 -3.918  1.618   1.00 42.53  ?  226 SER A CB  1 
ATOM   1681 O OG  . SER A 1 226 ? 42.597 -3.386  2.924   1.00 51.16  ?  226 SER A OG  1 
ATOM   1682 N N   . ASP A 1 227 ? 43.552 -5.944  -0.472  1.00 50.91  ?  227 ASP A N   1 
ATOM   1683 C CA  . ASP A 1 227 ? 43.493 -6.227  -1.909  1.00 52.70  ?  227 ASP A CA  1 
ATOM   1684 C C   . ASP A 1 227 ? 43.335 -7.706  -2.213  1.00 54.43  ?  227 ASP A C   1 
ATOM   1685 O O   . ASP A 1 227 ? 43.193 -8.068  -3.375  1.00 57.06  ?  227 ASP A O   1 
ATOM   1686 C CB  . ASP A 1 227 ? 44.728 -5.690  -2.631  1.00 48.60  ?  227 ASP A CB  1 
ATOM   1687 C CG  . ASP A 1 227 ? 44.912 -4.203  -2.423  1.00 65.56  ?  227 ASP A CG  1 
ATOM   1688 O OD1 . ASP A 1 227 ? 43.880 -3.487  -2.355  1.00 51.97  ?  227 ASP A OD1 1 
ATOM   1689 O OD2 . ASP A 1 227 ? 46.093 -3.770  -2.295  1.00 73.28  -1 227 ASP A OD2 1 
ATOM   1690 N N   . GLN A 1 228 ? 43.337 -8.561  -1.204  1.00 49.56  ?  228 GLN A N   1 
ATOM   1691 C CA  . GLN A 1 228 ? 43.109 -9.979  -1.397  1.00 48.65  ?  228 GLN A CA  1 
ATOM   1692 C C   . GLN A 1 228 ? 41.704 -10.410 -0.979  1.00 48.33  ?  228 GLN A C   1 
ATOM   1693 O O   . GLN A 1 228 ? 41.345 -11.575 -1.183  1.00 48.03  ?  228 GLN A O   1 
ATOM   1694 C CB  . GLN A 1 228 ? 44.157 -10.771 -0.599  1.00 49.53  ?  228 GLN A CB  1 
ATOM   1695 C CG  . GLN A 1 228 ? 45.601 -10.591 -1.069  1.00 48.91  ?  228 GLN A CG  1 
ATOM   1696 C CD  . GLN A 1 228 ? 46.200 -9.242  -0.686  1.00 50.95  ?  228 GLN A CD  1 
ATOM   1697 O OE1 . GLN A 1 228 ? 46.244 -8.870  0.484   1.00 52.95  ?  228 GLN A OE1 1 
ATOM   1698 N NE2 . GLN A 1 228 ? 46.648 -8.494  -1.690  1.00 60.22  ?  228 GLN A NE2 1 
ATOM   1699 N N   . THR A 1 229 ? 40.942 -9.520  -0.331  1.00 41.49  ?  229 THR A N   1 
ATOM   1700 C CA  . THR A 1 229 ? 39.703 -9.893  0.339   1.00 47.49  ?  229 THR A CA  1 
ATOM   1701 C C   . THR A 1 229 ? 38.500 -9.090  -0.128  1.00 48.66  ?  229 THR A C   1 
ATOM   1702 O O   . THR A 1 229 ? 37.507 -9.675  -0.557  1.00 61.65  ?  229 THR A O   1 
ATOM   1703 C CB  . THR A 1 229 ? 39.869 -9.725  1.858   1.00 51.71  ?  229 THR A CB  1 
ATOM   1704 O OG1 . THR A 1 229 ? 40.062 -8.333  2.149   1.00 50.23  ?  229 THR A OG1 1 
ATOM   1705 C CG2 . THR A 1 229 ? 41.046 -10.564 2.389   1.00 36.42  ?  229 THR A CG2 1 
ATOM   1706 N N   . LEU A 1 230 ? 38.562 -7.764  -0.054  1.00 54.59  ?  230 LEU A N   1 
ATOM   1707 C CA  . LEU A 1 230 ? 37.354 -6.942  -0.134  1.00 52.21  ?  230 LEU A CA  1 
ATOM   1708 C C   . LEU A 1 230 ? 36.687 -7.045  -1.496  1.00 51.95  ?  230 LEU A C   1 
ATOM   1709 O O   . LEU A 1 230 ? 35.522 -7.432  -1.598  1.00 59.39  ?  230 LEU A O   1 
ATOM   1710 C CB  . LEU A 1 230 ? 37.695 -5.485  0.181   1.00 44.32  ?  230 LEU A CB  1 
ATOM   1711 C CG  . LEU A 1 230 ? 38.071 -5.344  1.649   1.00 49.30  ?  230 LEU A CG  1 
ATOM   1712 C CD1 . LEU A 1 230 ? 38.455 -3.943  2.033   1.00 45.86  ?  230 LEU A CD1 1 
ATOM   1713 C CD2 . LEU A 1 230 ? 36.913 -5.835  2.489   1.00 46.62  ?  230 LEU A CD2 1 
ATOM   1714 N N   . GLU A 1 231 ? 37.413 -6.715  -2.560  1.00 51.79  ?  231 GLU A N   1 
ATOM   1715 C CA  . GLU A 1 231 ? 36.744 -6.486  -3.832  1.00 62.41  ?  231 GLU A CA  1 
ATOM   1716 C C   . GLU A 1 231 ? 36.105 -7.762  -4.370  1.00 61.75  ?  231 GLU A C   1 
ATOM   1717 O O   . GLU A 1 231 ? 34.904 -7.775  -4.675  1.00 59.76  ?  231 GLU A O   1 
ATOM   1718 C CB  . GLU A 1 231 ? 37.710 -5.897  -4.847  1.00 62.52  ?  231 GLU A CB  1 
ATOM   1719 C CG  . GLU A 1 231 ? 37.099 -5.858  -6.216  1.00 72.33  ?  231 GLU A CG  1 
ATOM   1720 C CD  . GLU A 1 231 ? 37.781 -4.875  -7.118  1.00 86.33  ?  231 GLU A CD  1 
ATOM   1721 O OE1 . GLU A 1 231 ? 38.505 -3.992  -6.608  1.00 91.63  ?  231 GLU A OE1 1 
ATOM   1722 O OE2 . GLU A 1 231 ? 37.612 -4.999  -8.346  1.00 92.23  -1 231 GLU A OE2 1 
ATOM   1723 N N   . LYS A 1 232 ? 36.891 -8.844  -4.486  1.00 61.14  ?  232 LYS A N   1 
ATOM   1724 C CA  . LYS A 1 232 ? 36.356 -10.106 -5.006  1.00 55.84  ?  232 LYS A CA  1 
ATOM   1725 C C   . LYS A 1 232 ? 35.182 -10.622 -4.168  1.00 63.54  ?  232 LYS A C   1 
ATOM   1726 O O   . LYS A 1 232 ? 34.238 -11.209 -4.708  1.00 66.64  ?  232 LYS A O   1 
ATOM   1727 C CB  . LYS A 1 232 ? 37.444 -11.183 -5.079  1.00 51.63  ?  232 LYS A CB  1 
ATOM   1728 C CG  . LYS A 1 232 ? 38.522 -11.031 -6.171  1.00 60.76  ?  232 LYS A CG  1 
ATOM   1729 C CD  . LYS A 1 232 ? 39.580 -9.930  -5.795  1.00 81.83  ?  232 LYS A CD  1 
ATOM   1730 C CE  . LYS A 1 232 ? 39.844 -9.858  -4.247  1.00 76.01  ?  232 LYS A CE  1 
ATOM   1731 N NZ  . LYS A 1 232 ? 40.775 -8.779  -3.860  1.00 63.73  ?  232 LYS A NZ  1 
ATOM   1732 N N   . THR A 1 233 ? 35.233 -10.453 -2.839  1.00 66.24  ?  233 THR A N   1 
ATOM   1733 C CA  . THR A 1 233 ? 34.125 -10.915 -2.006  1.00 57.88  ?  233 THR A CA  1 
ATOM   1734 C C   . THR A 1 233 ? 32.890 -10.064 -2.228  1.00 61.86  ?  233 THR A C   1 
ATOM   1735 O O   . THR A 1 233 ? 31.787 -10.592 -2.421  1.00 55.63  ?  233 THR A O   1 
ATOM   1736 C CB  . THR A 1 233 ? 34.489 -10.898 -0.519  1.00 51.78  ?  233 THR A CB  1 
ATOM   1737 O OG1 . THR A 1 233 ? 35.525 -11.841 -0.259  1.00 60.90  ?  233 THR A OG1 1 
ATOM   1738 C CG2 . THR A 1 233 ? 33.283 -11.276 0.310   1.00 44.84  ?  233 THR A CG2 1 
ATOM   1739 N N   . PHE A 1 234 ? 33.056 -8.738  -2.179  1.00 56.31  ?  234 PHE A N   1 
ATOM   1740 C CA  . PHE A 1 234 ? 31.916 -7.849  -2.352  1.00 62.73  ?  234 PHE A CA  1 
ATOM   1741 C C   . PHE A 1 234 ? 31.271 -8.045  -3.712  1.00 70.92  ?  234 PHE A C   1 
ATOM   1742 O O   . PHE A 1 234 ? 30.044 -7.933  -3.840  1.00 75.39  ?  234 PHE A O   1 
ATOM   1743 C CB  . PHE A 1 234 ? 32.344 -6.397  -2.173  1.00 60.40  ?  234 PHE A CB  1 
ATOM   1744 C CG  . PHE A 1 234 ? 32.550 -6.003  -0.752  1.00 60.67  ?  234 PHE A CG  1 
ATOM   1745 C CD1 . PHE A 1 234 ? 31.849 -6.630  0.265   1.00 64.29  ?  234 PHE A CD1 1 
ATOM   1746 C CD2 . PHE A 1 234 ? 33.456 -5.016  -0.423  1.00 58.86  ?  234 PHE A CD2 1 
ATOM   1747 C CE1 . PHE A 1 234 ? 32.049 -6.273  1.595   1.00 65.45  ?  234 PHE A CE1 1 
ATOM   1748 C CE2 . PHE A 1 234 ? 33.668 -4.647  0.906   1.00 59.61  ?  234 PHE A CE2 1 
ATOM   1749 C CZ  . PHE A 1 234 ? 32.965 -5.272  1.912   1.00 69.76  ?  234 PHE A CZ  1 
ATOM   1750 N N   . ARG A 1 235 ? 32.074 -8.366  -4.731  1.00 60.42  ?  235 ARG A N   1 
ATOM   1751 C CA  . ARG A 1 235 ? 31.537 -8.479  -6.079  1.00 64.23  ?  235 ARG A CA  1 
ATOM   1752 C C   . ARG A 1 235 ? 30.715 -9.751  -6.232  1.00 73.25  ?  235 ARG A C   1 
ATOM   1753 O O   . ARG A 1 235 ? 29.563 -9.700  -6.683  1.00 81.14  ?  235 ARG A O   1 
ATOM   1754 C CB  . ARG A 1 235 ? 32.667 -8.415  -7.106  1.00 66.43  ?  235 ARG A CB  1 
ATOM   1755 C CG  . ARG A 1 235 ? 32.174 -8.197  -8.518  1.00 80.12  ?  235 ARG A CG  1 
ATOM   1756 C CD  . ARG A 1 235 ? 33.304 -8.254  -9.521  1.00 84.53  ?  235 ARG A CD  1 
ATOM   1757 N NE  . ARG A 1 235 ? 34.356 -7.279  -9.227  1.00 87.62  ?  235 ARG A NE  1 
ATOM   1758 C CZ  . ARG A 1 235 ? 34.268 -5.975  -9.482  1.00 85.35  ?  235 ARG A CZ  1 
ATOM   1759 N NH1 . ARG A 1 235 ? 33.167 -5.452  -10.019 1.00 67.47  ?  235 ARG A NH1 1 
ATOM   1760 N NH2 . ARG A 1 235 ? 35.286 -5.187  -9.188  1.00 95.72  ?  235 ARG A NH2 1 
ATOM   1761 N N   . LEU A 1 236 ? 31.277 -10.903 -5.839  1.00 75.24  ?  236 LEU A N   1 
ATOM   1762 C CA  . LEU A 1 236 ? 30.509 -12.148 -5.886  1.00 71.32  ?  236 LEU A CA  1 
ATOM   1763 C C   . LEU A 1 236 ? 29.229 -12.033 -5.072  1.00 74.37  ?  236 LEU A C   1 
ATOM   1764 O O   . LEU A 1 236 ? 28.214 -12.643 -5.416  1.00 81.15  ?  236 LEU A O   1 
ATOM   1765 C CB  . LEU A 1 236 ? 31.329 -13.329 -5.373  1.00 64.99  ?  236 LEU A CB  1 
ATOM   1766 C CG  . LEU A 1 236 ? 32.646 -13.650 -6.076  1.00 73.21  ?  236 LEU A CG  1 
ATOM   1767 C CD1 . LEU A 1 236 ? 33.487 -14.609 -5.248  1.00 73.56  ?  236 LEU A CD1 1 
ATOM   1768 C CD2 . LEU A 1 236 ? 32.373 -14.205 -7.449  1.00 69.80  ?  236 LEU A CD2 1 
ATOM   1769 N N   . LEU A 1 237 ? 29.251 -11.251 -3.992  1.00 74.73  ?  237 LEU A N   1 
ATOM   1770 C CA  . LEU A 1 237 ? 28.056 -11.151 -3.162  1.00 84.05  ?  237 LEU A CA  1 
ATOM   1771 C C   . LEU A 1 237 ? 26.965 -10.339 -3.846  1.00 89.93  ?  237 LEU A C   1 
ATOM   1772 O O   . LEU A 1 237 ? 25.783 -10.672 -3.717  1.00 88.37  ?  237 LEU A O   1 
ATOM   1773 C CB  . LEU A 1 237 ? 28.400 -10.559 -1.791  1.00 82.79  ?  237 LEU A CB  1 
ATOM   1774 C CG  . LEU A 1 237 ? 29.248 -11.493 -0.922  1.00 84.12  ?  237 LEU A CG  1 
ATOM   1775 C CD1 . LEU A 1 237 ? 29.316 -11.045 0.554   1.00 88.63  ?  237 LEU A CD1 1 
ATOM   1776 C CD2 . LEU A 1 237 ? 28.789 -12.953 -1.050  1.00 77.00  ?  237 LEU A CD2 1 
ATOM   1777 N N   . SER A 1 238 ? 27.333 -9.299  -4.594  1.00 91.44  ?  238 SER A N   1 
ATOM   1778 C CA  . SER A 1 238 ? 26.318 -8.480  -5.238  1.00 85.66  ?  238 SER A CA  1 
ATOM   1779 C C   . SER A 1 238 ? 25.778 -9.161  -6.486  1.00 94.43  ?  238 SER A C   1 
ATOM   1780 O O   . SER A 1 238 ? 24.592 -9.005  -6.809  1.00 94.82  ?  238 SER A O   1 
ATOM   1781 C CB  . SER A 1 238 ? 26.893 -7.106  -5.567  1.00 79.83  ?  238 SER A CB  1 
ATOM   1782 O OG  . SER A 1 238 ? 25.881 -6.213  -5.970  1.00 87.05  ?  238 SER A OG  1 
ATOM   1783 N N   . GLU A 1 239 ? 26.624 -9.952  -7.166  1.00 98.09  ?  239 GLU A N   1 
ATOM   1784 C CA  . GLU A 1 239 ? 26.212 -10.695 -8.359  1.00 95.63  ?  239 GLU A CA  1 
ATOM   1785 C C   . GLU A 1 239 ? 25.192 -11.786 -8.034  1.00 97.81  ?  239 GLU A C   1 
ATOM   1786 O O   . GLU A 1 239 ? 24.369 -12.132 -8.883  1.00 105.27 ?  239 GLU A O   1 
ATOM   1787 C CB  . GLU A 1 239 ? 27.442 -11.311 -9.036  1.00 94.15  ?  239 GLU A CB  1 
ATOM   1788 C CG  . GLU A 1 239 ? 28.416 -10.291 -9.678  1.00 100.72 ?  239 GLU A CG  1 
ATOM   1789 C CD  . GLU A 1 239 ? 29.683 -10.941 -10.258 1.00 99.17  ?  239 GLU A CD  1 
ATOM   1790 O OE1 . GLU A 1 239 ? 29.900 -12.156 -10.028 1.00 98.37  ?  239 GLU A OE1 1 
ATOM   1791 O OE2 . GLU A 1 239 ? 30.457 -10.232 -10.946 1.00 95.90  -1 239 GLU A OE2 1 
ATOM   1792 N N   . ARG A 1 240 ? 25.243 -12.346 -6.827  1.00 98.42  ?  240 ARG A N   1 
ATOM   1793 C CA  . ARG A 1 240 ? 24.265 -13.335 -6.390  1.00 103.53 ?  240 ARG A CA  1 
ATOM   1794 C C   . ARG A 1 240 ? 23.138 -12.721 -5.563  1.00 109.09 ?  240 ARG A C   1 
ATOM   1795 O O   . ARG A 1 240 ? 22.104 -13.373 -5.374  1.00 116.22 ?  240 ARG A O   1 
ATOM   1796 C CB  . ARG A 1 240 ? 24.945 -14.461 -5.585  1.00 99.01  ?  240 ARG A CB  1 
ATOM   1797 C CG  . ARG A 1 240 ? 24.925 -14.257 -4.081  1.00 97.63  ?  240 ARG A CG  1 
ATOM   1798 C CD  . ARG A 1 240 ? 24.997 -15.567 -3.324  1.00 103.68 ?  240 ARG A CD  1 
ATOM   1799 N NE  . ARG A 1 240 ? 26.356 -16.091 -3.198  1.00 113.01 ?  240 ARG A NE  1 
ATOM   1800 C CZ  . ARG A 1 240 ? 26.666 -17.213 -2.546  1.00 112.44 ?  240 ARG A CZ  1 
ATOM   1801 N NH1 . ARG A 1 240 ? 25.710 -17.931 -1.959  1.00 104.35 ?  240 ARG A NH1 1 
ATOM   1802 N NH2 . ARG A 1 240 ? 27.929 -17.624 -2.478  1.00 112.02 ?  240 ARG A NH2 1 
ATOM   1803 N N   . ILE A 1 241 ? 23.329 -11.510 -5.024  1.00 103.14 ?  241 ILE A N   1 
ATOM   1804 C CA  . ILE A 1 241 ? 22.190 -10.740 -4.536  1.00 102.22 ?  241 ILE A CA  1 
ATOM   1805 C C   . ILE A 1 241 ? 21.474 -10.078 -5.708  1.00 109.31 ?  241 ILE A C   1 
ATOM   1806 O O   . ILE A 1 241 ? 20.311 -9.671  -5.580  1.00 118.23 ?  241 ILE A O   1 
ATOM   1807 C CB  . ILE A 1 241 ? 22.635 -9.741  -3.448  1.00 102.28 ?  241 ILE A CB  1 
ATOM   1808 C CG1 . ILE A 1 241 ? 22.973 -10.501 -2.160  1.00 105.48 ?  241 ILE A CG1 1 
ATOM   1809 C CG2 . ILE A 1 241 ? 21.552 -8.732  -3.100  1.00 100.00 ?  241 ILE A CG2 1 
ATOM   1810 C CD1 . ILE A 1 241 ? 24.024 -9.859  -1.290  1.00 108.60 ?  241 ILE A CD1 1 
ATOM   1811 N N   . ASN A 1 242 ? 22.122 -10.008 -6.876  1.00 109.74 ?  242 ASN A N   1 
ATOM   1812 C CA  . ASN A 1 242 ? 21.414 -9.659  -8.103  1.00 109.31 ?  242 ASN A CA  1 
ATOM   1813 C C   . ASN A 1 242 ? 20.620 -10.844 -8.641  1.00 113.52 ?  242 ASN A C   1 
ATOM   1814 O O   . ASN A 1 242 ? 19.500 -10.672 -9.141  1.00 113.24 ?  242 ASN A O   1 
ATOM   1815 C CB  . ASN A 1 242 ? 22.400 -9.182  -9.156  1.00 104.61 ?  242 ASN A CB  1 
ATOM   1816 C CG  . ASN A 1 242 ? 21.943 -7.925  -9.834  1.00 106.31 ?  242 ASN A CG  1 
ATOM   1817 O OD1 . ASN A 1 242 ? 20.974 -7.290  -9.404  1.00 113.09 ?  242 ASN A OD1 1 
ATOM   1818 N ND2 . ASN A 1 242 ? 22.655 -7.527  -10.877 1.00 100.68 ?  242 ASN A ND2 1 
ATOM   1819 N N   . SER A 1 243 ? 21.180 -12.049 -8.545  1.00 116.24 ?  243 SER A N   1 
ATOM   1820 C CA  . SER A 1 243 ? 20.400 -13.268 -8.726  1.00 116.56 ?  243 SER A CA  1 
ATOM   1821 C C   . SER A 1 243 ? 19.049 -13.252 -8.010  1.00 122.56 ?  243 SER A C   1 
ATOM   1822 O O   . SER A 1 243 ? 18.101 -13.901 -8.453  1.00 125.02 ?  243 SER A O   1 
ATOM   1823 C CB  . SER A 1 243 ? 21.245 -14.449 -8.239  1.00 111.11 ?  243 SER A CB  1 
ATOM   1824 O OG  . SER A 1 243 ? 20.443 -15.546 -7.831  1.00 108.68 ?  243 SER A OG  1 
ATOM   1825 N N   . SER A 1 244 ? 18.953 -12.530 -6.902  1.00 124.54 ?  244 SER A N   1 
ATOM   1826 C CA  . SER A 1 244 ? 17.731 -12.447 -6.107  1.00 127.57 ?  244 SER A CA  1 
ATOM   1827 C C   . SER A 1 244 ? 16.732 -11.414 -6.632  1.00 133.06 ?  244 SER A C   1 
ATOM   1828 O O   . SER A 1 244 ? 16.301 -10.528 -5.882  1.00 133.91 ?  244 SER A O   1 
ATOM   1829 C CB  . SER A 1 244 ? 18.081 -12.100 -4.648  1.00 119.95 ?  244 SER A CB  1 
ATOM   1830 O OG  . SER A 1 244 ? 19.147 -12.913 -4.184  1.00 111.25 ?  244 SER A OG  1 
ATOM   1831 N N   . LYS A 1 245 ? 16.332 -11.521 -7.893  1.00 134.18 ?  245 LYS A N   1 
ATOM   1832 C CA  . LYS A 1 245 ? 15.255 -10.670 -8.374  1.00 131.99 ?  245 LYS A CA  1 
ATOM   1833 C C   . LYS A 1 245 ? 13.905 -11.403 -8.267  1.00 136.18 ?  245 LYS A C   1 
ATOM   1834 O O   . LYS A 1 245 ? 13.377 -11.629 -7.169  1.00 135.56 ?  245 LYS A O   1 
ATOM   1835 C CB  . LYS A 1 245 ? 15.516 -10.216 -9.813  1.00 126.49 ?  245 LYS A CB  1 
ATOM   1836 C CG  . LYS A 1 245 ? 14.706 -8.981  -10.176 1.00 126.92 ?  245 LYS A CG  1 
ATOM   1837 C CD  . LYS A 1 245 ? 14.923 -7.919  -9.095  1.00 124.63 ?  245 LYS A CD  1 
ATOM   1838 C CE  . LYS A 1 245 ? 13.662 -7.121  -8.771  1.00 122.99 ?  245 LYS A CE  1 
ATOM   1839 N NZ  . LYS A 1 245 ? 12.484 -7.958  -8.396  1.00 116.71 ?  245 LYS A NZ  1 
ATOM   1840 N N   . VAL A 1 257 ? 15.462 -7.441  0.424   1.00 155.34 ?  257 VAL A N   1 
ATOM   1841 C CA  . VAL A 1 257 ? 15.269 -6.932  1.759   1.00 154.94 ?  257 VAL A CA  1 
ATOM   1842 C C   . VAL A 1 257 ? 15.627 -5.456  1.697   1.00 164.29 ?  257 VAL A C   1 
ATOM   1843 O O   . VAL A 1 257 ? 15.702 -4.784  2.727   1.00 169.19 ?  257 VAL A O   1 
ATOM   1844 C CB  . VAL A 1 257 ? 16.060 -7.796  2.783   1.00 142.44 ?  257 VAL A CB  1 
ATOM   1845 C CG1 . VAL A 1 257 ? 16.903 -8.857  2.099   1.00 136.61 ?  257 VAL A CG1 1 
ATOM   1846 C CG2 . VAL A 1 257 ? 16.822 -7.011  3.836   1.00 138.31 ?  257 VAL A CG2 1 
ATOM   1847 N N   . ASN A 1 258 ? 15.761 -4.914  0.482   1.00 163.87 ?  258 ASN A N   1 
ATOM   1848 C CA  . ASN A 1 258 ? 16.204 -3.533  0.325   1.00 160.53 ?  258 ASN A CA  1 
ATOM   1849 C C   . ASN A 1 258 ? 17.341 -3.698  1.210   1.00 160.39 ?  258 ASN A C   1 
ATOM   1850 O O   . ASN A 1 258 ? 17.560 -2.882  2.088   1.00 163.03 ?  258 ASN A O   1 
ATOM   1851 C CB  . ASN A 1 258 ? 15.171 -2.544  0.867   1.00 153.36 ?  258 ASN A CB  1 
ATOM   1852 C CG  . ASN A 1 258 ? 13.980 -2.368  -0.058  1.00 145.63 ?  258 ASN A CG  1 
ATOM   1853 O OD1 . ASN A 1 258 ? 13.050 -1.629  0.251   1.00 144.35 ?  258 ASN A OD1 1 
ATOM   1854 N ND2 . ASN A 1 258 ? 14.004 -3.044  -1.197  1.00 142.36 ?  258 ASN A ND2 1 
ATOM   1855 N N   . GLN A 1 259 ? 18.087 -4.759  0.986   1.00 156.21 ?  259 GLN A N   1 
ATOM   1856 C CA  . GLN A 1 259 ? 19.100 -5.125  1.925   1.00 149.90 ?  259 GLN A CA  1 
ATOM   1857 C C   . GLN A 1 259 ? 20.409 -4.464  1.789   1.00 145.74 ?  259 GLN A C   1 
ATOM   1858 O O   . GLN A 1 259 ? 20.807 -3.822  2.717   1.00 143.49 ?  259 GLN A O   1 
ATOM   1859 C CB  . GLN A 1 259 ? 19.314 -6.633  1.789   1.00 144.98 ?  259 GLN A CB  1 
ATOM   1860 C CG  . GLN A 1 259 ? 19.313 -7.143  0.367   1.00 143.36 ?  259 GLN A CG  1 
ATOM   1861 C CD  . GLN A 1 259 ? 20.439 -8.118  0.142   1.00 142.09 ?  259 GLN A CD  1 
ATOM   1862 O OE1 . GLN A 1 259 ? 20.229 -9.327  0.103   1.00 141.80 ?  259 GLN A OE1 1 
ATOM   1863 N NE2 . GLN A 1 259 ? 21.652 -7.597  0.021   1.00 140.04 ?  259 GLN A NE2 1 
ATOM   1864 N N   . PHE A 1 260 ? 21.131 -4.749  0.717   1.00 143.89 ?  260 PHE A N   1 
ATOM   1865 C CA  . PHE A 1 260 ? 22.413 -4.131  0.461   1.00 136.74 ?  260 PHE A CA  1 
ATOM   1866 C C   . PHE A 1 260 ? 23.075 -4.664  -0.784  1.00 132.03 ?  260 PHE A C   1 
ATOM   1867 O O   . PHE A 1 260 ? 22.731 -5.661  -1.409  1.00 132.18 ?  260 PHE A O   1 
ATOM   1868 C CB  . PHE A 1 260 ? 23.358 -4.325  1.634   1.00 128.02 ?  260 PHE A CB  1 
ATOM   1869 C CG  . PHE A 1 260 ? 24.275 -3.160  1.844   1.00 124.38 ?  260 PHE A CG  1 
ATOM   1870 C CD1 . PHE A 1 260 ? 23.980 -1.936  1.275   1.00 119.83 ?  260 PHE A CD1 1 
ATOM   1871 C CD2 . PHE A 1 260 ? 25.436 -3.289  2.568   1.00 117.45 ?  260 PHE A CD2 1 
ATOM   1872 C CE1 . PHE A 1 260 ? 24.818 -0.859  1.443   1.00 110.99 ?  260 PHE A CE1 1 
ATOM   1873 C CE2 . PHE A 1 260 ? 26.278 -2.217  2.737   1.00 108.47 ?  260 PHE A CE2 1 
ATOM   1874 C CZ  . PHE A 1 260 ? 25.970 -1.002  2.177   1.00 105.97 ?  260 PHE A CZ  1 
ATOM   1875 N N   . ASP A 1 261 ? 23.940 -3.884  -1.323  1.00 118.80 ?  261 ASP A N   1 
ATOM   1876 C CA  . ASP A 1 261 ? 24.669 -4.480  -2.370  1.00 112.93 ?  261 ASP A CA  1 
ATOM   1877 C C   . ASP A 1 261 ? 25.850 -4.445  -1.522  1.00 109.88 ?  261 ASP A C   1 
ATOM   1878 O O   . ASP A 1 261 ? 25.903 -3.880  -0.428  1.00 113.48 ?  261 ASP A O   1 
ATOM   1879 C CB  . ASP A 1 261 ? 24.780 -3.633  -3.619  1.00 117.65 ?  261 ASP A CB  1 
ATOM   1880 C CG  . ASP A 1 261 ? 25.220 -2.208  -3.339  1.00 127.88 ?  261 ASP A CG  1 
ATOM   1881 O OD1 . ASP A 1 261 ? 25.223 -1.771  -2.171  1.00 132.62 ?  261 ASP A OD1 1 
ATOM   1882 O OD2 . ASP A 1 261 ? 25.558 -1.507  -4.313  1.00 128.43 -1 261 ASP A OD2 1 
ATOM   1883 N N   . PRO A 1 262 ? 26.733 -5.269  -1.862  1.00 100.92 ?  262 PRO A N   1 
ATOM   1884 C CA  . PRO A 1 262 ? 27.881 -5.019  -1.070  1.00 95.57  ?  262 PRO A CA  1 
ATOM   1885 C C   . PRO A 1 262 ? 28.649 -4.249  -2.109  1.00 90.41  ?  262 PRO A C   1 
ATOM   1886 O O   . PRO A 1 262 ? 29.650 -3.652  -1.812  1.00 79.18  ?  262 PRO A O   1 
ATOM   1887 C CB  . PRO A 1 262 ? 28.351 -6.413  -0.763  1.00 88.44  ?  262 PRO A CB  1 
ATOM   1888 C CG  . PRO A 1 262 ? 27.162 -7.285  -0.906  1.00 88.71  ?  262 PRO A CG  1 
ATOM   1889 C CD  . PRO A 1 262 ? 26.511 -6.695  -2.096  1.00 95.53  ?  262 PRO A CD  1 
ATOM   1890 N N   . GLY A 1 263 ? 28.115 -4.189  -3.314  1.00 89.03  ?  263 GLY A N   1 
ATOM   1891 C CA  . GLY A 1 263 ? 28.771 -3.527  -4.416  1.00 89.72  ?  263 GLY A CA  1 
ATOM   1892 C C   . GLY A 1 263 ? 28.943 -2.049  -4.410  1.00 84.78  ?  263 GLY A C   1 
ATOM   1893 O O   . GLY A 1 263 ? 29.758 -1.525  -5.126  1.00 86.14  ?  263 GLY A O   1 
ATOM   1894 N N   . ASP A 1 264 ? 28.192 -1.363  -3.603  1.00 82.66  ?  264 ASP A N   1 
ATOM   1895 C CA  . ASP A 1 264 ? 28.402 0.026   -3.499  1.00 90.16  ?  264 ASP A CA  1 
ATOM   1896 C C   . ASP A 1 264 ? 29.671 0.217   -2.776  1.00 87.78  ?  264 ASP A C   1 
ATOM   1897 O O   . ASP A 1 264 ? 30.106 1.323   -2.594  1.00 86.62  ?  264 ASP A O   1 
ATOM   1898 C CB  . ASP A 1 264 ? 27.300 0.626   -2.690  1.00 104.28 ?  264 ASP A CB  1 
ATOM   1899 C CG  . ASP A 1 264 ? 26.375 1.482   -3.516  1.00 125.46 ?  264 ASP A CG  1 
ATOM   1900 O OD1 . ASP A 1 264 ? 26.634 1.654   -4.721  1.00 131.42 -1 264 ASP A OD1 1 
ATOM   1901 O OD2 . ASP A 1 264 ? 25.382 1.986   -2.959  1.00 133.82 ?  264 ASP A OD2 1 
ATOM   1902 N N   . LEU A 1 265 ? 30.273 -0.866  -2.348  1.00 86.69  ?  265 LEU A N   1 
ATOM   1903 C CA  . LEU A 1 265 ? 31.490 -0.777  -1.598  1.00 83.49  ?  265 LEU A CA  1 
ATOM   1904 C C   . LEU A 1 265 ? 32.685 -1.121  -2.443  1.00 76.95  ?  265 LEU A C   1 
ATOM   1905 O O   . LEU A 1 265 ? 33.798 -0.832  -2.092  1.00 71.87  ?  265 LEU A O   1 
ATOM   1906 C CB  . LEU A 1 265 ? 31.386 -1.698  -0.416  1.00 79.53  ?  265 LEU A CB  1 
ATOM   1907 C CG  . LEU A 1 265 ? 30.429 -1.277  0.683   1.00 79.53  ?  265 LEU A CG  1 
ATOM   1908 C CD1 . LEU A 1 265 ? 30.029 -2.499  1.481   1.00 81.53  ?  265 LEU A CD1 1 
ATOM   1909 C CD2 . LEU A 1 265 ? 31.108 -0.267  1.580   1.00 75.20  ?  265 LEU A CD2 1 
ATOM   1910 N N   . VAL A 1 266 ? 32.449 -1.704  -3.587  1.00 74.32  ?  266 VAL A N   1 
ATOM   1911 C CA  . VAL A 1 266 ? 33.538 -1.992  -4.454  1.00 76.48  ?  266 VAL A CA  1 
ATOM   1912 C C   . VAL A 1 266 ? 34.066 -0.726  -5.022  1.00 81.80  ?  266 VAL A C   1 
ATOM   1913 O O   . VAL A 1 266 ? 33.340 0.211   -5.231  1.00 91.94  ?  266 VAL A O   1 
ATOM   1914 C CB  . VAL A 1 266 ? 33.102 -2.889  -5.602  1.00 82.86  ?  266 VAL A CB  1 
ATOM   1915 C CG1 . VAL A 1 266 ? 32.361 -2.114  -6.667  1.00 91.48  ?  266 VAL A CG1 1 
ATOM   1916 C CG2 . VAL A 1 266 ? 34.296 -3.598  -6.203  1.00 89.14  ?  266 VAL A CG2 1 
ATOM   1917 N N   . GLY A 1 267 ? 35.359 -0.664  -5.230  1.00 83.53  ?  267 GLY A N   1 
ATOM   1918 C CA  . GLY A 1 267 ? 35.888 0.591   -5.727  1.00 83.85  ?  267 GLY A CA  1 
ATOM   1919 C C   . GLY A 1 267 ? 36.026 1.685   -4.692  1.00 78.38  ?  267 GLY A C   1 
ATOM   1920 O O   . GLY A 1 267 ? 36.526 2.771   -5.021  1.00 77.48  ?  267 GLY A O   1 
ATOM   1921 N N   . VAL A 1 268 ? 35.610 1.441   -3.452  1.00 76.27  ?  268 VAL A N   1 
ATOM   1922 C CA  . VAL A 1 268 ? 35.979 2.323   -2.340  1.00 73.98  ?  268 VAL A CA  1 
ATOM   1923 C C   . VAL A 1 268 ? 37.334 1.825   -1.850  1.00 69.70  ?  268 VAL A C   1 
ATOM   1924 O O   . VAL A 1 268 ? 37.444 1.039   -0.916  1.00 76.83  ?  268 VAL A O   1 
ATOM   1925 C CB  . VAL A 1 268 ? 34.921 2.326   -1.241  1.00 65.02  ?  268 VAL A CB  1 
ATOM   1926 C CG1 . VAL A 1 268 ? 35.205 3.417   -0.226  1.00 60.50  ?  268 VAL A CG1 1 
ATOM   1927 C CG2 . VAL A 1 268 ? 33.558 2.461   -1.848  1.00 65.18  ?  268 VAL A CG2 1 
ATOM   1928 N N   . LYS A 1 269 ? 38.393 2.306   -2.492  1.00 73.69  ?  269 LYS A N   1 
ATOM   1929 C CA  . LYS A 1 269 ? 39.717 1.744   -2.217  1.00 67.99  ?  269 LYS A CA  1 
ATOM   1930 C C   . LYS A 1 269 ? 40.210 2.000   -0.793  1.00 71.22  ?  269 LYS A C   1 
ATOM   1931 O O   . LYS A 1 269 ? 41.147 1.324   -0.351  1.00 69.32  ?  269 LYS A O   1 
ATOM   1932 C CB  . LYS A 1 269 ? 40.741 2.281   -3.217  1.00 62.50  ?  269 LYS A CB  1 
ATOM   1933 C CG  . LYS A 1 269 ? 40.896 3.796   -3.226  1.00 79.55  ?  269 LYS A CG  1 
ATOM   1934 C CD  . LYS A 1 269 ? 42.173 4.197   -3.998  1.00 89.48  ?  269 LYS A CD  1 
ATOM   1935 C CE  . LYS A 1 269 ? 42.386 5.709   -4.073  1.00 86.47  ?  269 LYS A CE  1 
ATOM   1936 N NZ  . LYS A 1 269 ? 43.829 6.014   -4.334  1.00 89.35  ?  269 LYS A NZ  1 
ATOM   1937 N N   . GLU A 1 270 ? 39.613 2.943   -0.062  1.00 71.71  ?  270 GLU A N   1 
ATOM   1938 C CA  . GLU A 1 270 ? 40.171 3.401   1.207   1.00 64.23  ?  270 GLU A CA  1 
ATOM   1939 C C   . GLU A 1 270 ? 39.627 2.642   2.404   1.00 68.96  ?  270 GLU A C   1 
ATOM   1940 O O   . GLU A 1 270 ? 40.201 2.736   3.508   1.00 62.78  ?  270 GLU A O   1 
ATOM   1941 C CB  . GLU A 1 270 ? 39.907 4.893   1.385   1.00 62.50  ?  270 GLU A CB  1 
ATOM   1942 C CG  . GLU A 1 270 ? 40.742 5.755   0.455   1.00 66.29  ?  270 GLU A CG  1 
ATOM   1943 C CD  . GLU A 1 270 ? 40.000 6.118   -0.809  1.00 73.16  ?  270 GLU A CD  1 
ATOM   1944 O OE1 . GLU A 1 270 ? 38.786 5.809   -0.897  1.00 73.23  ?  270 GLU A OE1 1 
ATOM   1945 O OE2 . GLU A 1 270 ? 40.630 6.709   -1.712  1.00 80.72  -1 270 GLU A OE2 1 
ATOM   1946 N N   . PHE A 1 271 ? 38.544 1.896   2.201   1.00 66.53  ?  271 PHE A N   1 
ATOM   1947 C CA  . PHE A 1 271 ? 38.044 0.965   3.198   1.00 58.79  ?  271 PHE A CA  1 
ATOM   1948 C C   . PHE A 1 271 ? 38.943 -0.270  3.229   1.00 59.08  ?  271 PHE A C   1 
ATOM   1949 O O   . PHE A 1 271 ? 39.328 -0.791  2.179   1.00 66.52  ?  271 PHE A O   1 
ATOM   1950 C CB  . PHE A 1 271 ? 36.608 0.602   2.864   1.00 54.06  ?  271 PHE A CB  1 
ATOM   1951 C CG  . PHE A 1 271 ? 35.961 -0.260  3.881   1.00 61.83  ?  271 PHE A CG  1 
ATOM   1952 C CD1 . PHE A 1 271 ? 35.884 0.156   5.198   1.00 65.47  ?  271 PHE A CD1 1 
ATOM   1953 C CD2 . PHE A 1 271 ? 35.410 -1.482  3.525   1.00 55.39  ?  271 PHE A CD2 1 
ATOM   1954 C CE1 . PHE A 1 271 ? 35.277 -0.634  6.153   1.00 60.18  ?  271 PHE A CE1 1 
ATOM   1955 C CE2 . PHE A 1 271 ? 34.802 -2.270  4.465   1.00 62.20  ?  271 PHE A CE2 1 
ATOM   1956 C CZ  . PHE A 1 271 ? 34.736 -1.848  5.788   1.00 60.11  ?  271 PHE A CZ  1 
ATOM   1957 N N   . GLY A 1 272 ? 39.319 -0.715  4.416   1.00 56.06  ?  272 GLY A N   1 
ATOM   1958 C CA  . GLY A 1 272 ? 40.379 -1.697  4.548   1.00 58.49  ?  272 GLY A CA  1 
ATOM   1959 C C   . GLY A 1 272 ? 40.065 -2.855  5.468   1.00 58.27  ?  272 GLY A C   1 
ATOM   1960 O O   . GLY A 1 272 ? 39.322 -2.743  6.447   1.00 49.82  ?  272 GLY A O   1 
ATOM   1961 N N   . TYR A 1 273 ? 40.689 -3.983  5.164   1.00 52.06  ?  273 TYR A N   1 
ATOM   1962 C CA  . TYR A 1 273 ? 40.564 -5.179  5.970   1.00 49.95  ?  273 TYR A CA  1 
ATOM   1963 C C   . TYR A 1 273 ? 41.948 -5.566  6.452   1.00 45.00  ?  273 TYR A C   1 
ATOM   1964 O O   . TYR A 1 273 ? 42.861 -5.700  5.642   1.00 46.39  ?  273 TYR A O   1 
ATOM   1965 C CB  . TYR A 1 273 ? 39.906 -6.289  5.156   1.00 46.39  ?  273 TYR A CB  1 
ATOM   1966 C CG  . TYR A 1 273 ? 39.430 -7.451  5.993   1.00 56.01  ?  273 TYR A CG  1 
ATOM   1967 C CD1 . TYR A 1 273 ? 38.729 -7.248  7.169   1.00 54.69  ?  273 TYR A CD1 1 
ATOM   1968 C CD2 . TYR A 1 273 ? 39.686 -8.758  5.598   1.00 50.76  ?  273 TYR A CD2 1 
ATOM   1969 C CE1 . TYR A 1 273 ? 38.309 -8.328  7.935   1.00 52.57  ?  273 TYR A CE1 1 
ATOM   1970 C CE2 . TYR A 1 273 ? 39.265 -9.811  6.340   1.00 47.34  ?  273 TYR A CE2 1 
ATOM   1971 C CZ  . TYR A 1 273 ? 38.577 -9.603  7.503   1.00 50.15  ?  273 TYR A CZ  1 
ATOM   1972 O OH  . TYR A 1 273 ? 38.184 -10.694 8.237   1.00 49.16  ?  273 TYR A OH  1 
ATOM   1973 N N   . LEU A 1 274 ? 42.118 -5.711  7.768   1.00 48.89  ?  274 LEU A N   1 
ATOM   1974 C CA  . LEU A 1 274 ? 43.439 -5.995  8.317   1.00 56.15  ?  274 LEU A CA  1 
ATOM   1975 C C   . LEU A 1 274 ? 43.471 -7.347  9.020   1.00 56.33  ?  274 LEU A C   1 
ATOM   1976 O O   . LEU A 1 274 ? 42.486 -7.760  9.630   1.00 53.79  ?  274 LEU A O   1 
ATOM   1977 C CB  . LEU A 1 274 ? 43.899 -4.897  9.294   1.00 54.69  ?  274 LEU A CB  1 
ATOM   1978 C CG  . LEU A 1 274 ? 43.380 -4.907  10.731  1.00 56.52  ?  274 LEU A CG  1 
ATOM   1979 C CD1 . LEU A 1 274 ? 44.383 -5.600  11.649  1.00 54.14  ?  274 LEU A CD1 1 
ATOM   1980 C CD2 . LEU A 1 274 ? 43.126 -3.494  11.219  1.00 44.28  ?  274 LEU A CD2 1 
ATOM   1981 N N   . LEU A 1 275 ? 44.614 -8.029  8.904   1.00 47.06  ?  275 LEU A N   1 
ATOM   1982 C CA  . LEU A 1 275 ? 44.987 -9.181  9.712   1.00 47.85  ?  275 LEU A CA  1 
ATOM   1983 C C   . LEU A 1 275 ? 46.065 -8.757  10.713  1.00 52.08  ?  275 LEU A C   1 
ATOM   1984 O O   . LEU A 1 275 ? 47.006 -8.045  10.355  1.00 48.50  ?  275 LEU A O   1 
ATOM   1985 C CB  . LEU A 1 275 ? 45.517 -10.313 8.819   1.00 47.25  ?  275 LEU A CB  1 
ATOM   1986 C CG  . LEU A 1 275 ? 46.185 -11.524 9.482   1.00 45.98  ?  275 LEU A CG  1 
ATOM   1987 C CD1 . LEU A 1 275 ? 45.213 -12.266 10.354  1.00 53.72  ?  275 LEU A CD1 1 
ATOM   1988 C CD2 . LEU A 1 275 ? 46.838 -12.460 8.478   1.00 49.94  ?  275 LEU A CD2 1 
ATOM   1989 N N   . LEU A 1 276 ? 45.934 -9.192  11.968  1.00 45.11  ?  276 LEU A N   1 
ATOM   1990 C CA  . LEU A 1 276 ? 46.823 -8.734  13.029  1.00 47.37  ?  276 LEU A CA  1 
ATOM   1991 C C   . LEU A 1 276 ? 47.217 -9.891  13.931  1.00 51.62  ?  276 LEU A C   1 
ATOM   1992 O O   . LEU A 1 276 ? 46.367 -10.719 14.275  1.00 65.02  ?  276 LEU A O   1 
ATOM   1993 C CB  . LEU A 1 276 ? 46.144 -7.661  13.885  1.00 53.23  ?  276 LEU A CB  1 
ATOM   1994 C CG  . LEU A 1 276 ? 46.969 -6.965  14.971  1.00 57.58  ?  276 LEU A CG  1 
ATOM   1995 C CD1 . LEU A 1 276 ? 46.398 -5.575  15.151  1.00 62.87  ?  276 LEU A CD1 1 
ATOM   1996 C CD2 . LEU A 1 276 ? 46.969 -7.748  16.299  1.00 52.55  ?  276 LEU A CD2 1 
ATOM   1997 N N   . VAL A 1 277 ? 48.476 -9.912  14.379  1.00 46.77  ?  277 VAL A N   1 
ATOM   1998 C CA  . VAL A 1 277 ? 48.916 -10.894 15.365  1.00 49.42  ?  277 VAL A CA  1 
ATOM   1999 C C   . VAL A 1 277 ? 49.656 -10.203 16.513  1.00 54.41  ?  277 VAL A C   1 
ATOM   2000 O O   . VAL A 1 277 ? 50.596 -9.432  16.281  1.00 55.46  ?  277 VAL A O   1 
ATOM   2001 C CB  . VAL A 1 277 ? 49.815 -11.968 14.733  1.00 47.41  ?  277 VAL A CB  1 
ATOM   2002 C CG1 . VAL A 1 277 ? 50.361 -12.933 15.823  1.00 40.87  ?  277 VAL A CG1 1 
ATOM   2003 C CG2 . VAL A 1 277 ? 49.085 -12.689 13.601  1.00 49.70  ?  277 VAL A CG2 1 
ATOM   2004 N N   . ALA A 1 278 ? 49.263 -10.512 17.751  1.00 56.96  ?  278 ALA A N   1 
ATOM   2005 C CA  . ALA A 1 278 ? 49.922 -9.997  18.944  1.00 51.63  ?  278 ALA A CA  1 
ATOM   2006 C C   . ALA A 1 278 ? 50.241 -11.139 19.897  1.00 52.89  ?  278 ALA A C   1 
ATOM   2007 O O   . ALA A 1 278 ? 49.592 -12.186 19.889  1.00 60.56  ?  278 ALA A O   1 
ATOM   2008 C CB  . ALA A 1 278 ? 49.064 -8.954  19.653  1.00 45.67  ?  278 ALA A CB  1 
ATOM   2009 N N   . GLN A 1 279 ? 51.254 -10.938 20.726  1.00 54.64  ?  279 GLN A N   1 
ATOM   2010 C CA  . GLN A 1 279 ? 51.684 -11.963 21.664  1.00 59.18  ?  279 GLN A CA  1 
ATOM   2011 C C   . GLN A 1 279 ? 51.599 -11.438 23.091  1.00 66.21  ?  279 GLN A C   1 
ATOM   2012 O O   . GLN A 1 279 ? 51.589 -10.228 23.335  1.00 67.84  ?  279 GLN A O   1 
ATOM   2013 C CB  . GLN A 1 279 ? 53.111 -12.411 21.378  1.00 62.89  ?  279 GLN A CB  1 
ATOM   2014 C CG  . GLN A 1 279 ? 53.539 -13.723 22.034  1.00 72.44  ?  279 GLN A CG  1 
ATOM   2015 C CD  . GLN A 1 279 ? 54.874 -14.224 21.479  1.00 83.07  ?  279 GLN A CD  1 
ATOM   2016 O OE1 . GLN A 1 279 ? 55.675 -13.438 20.946  1.00 86.53  ?  279 GLN A OE1 1 
ATOM   2017 N NE2 . GLN A 1 279 ? 55.099 -15.539 21.555  1.00 81.84  ?  279 GLN A NE2 1 
ATOM   2018 N N   . ARG A 1 280 ? 51.493 -12.372 24.032  1.00 73.44  ?  280 ARG A N   1 
ATOM   2019 C CA  . ARG A 1 280 ? 51.721 -12.121 25.448  1.00 72.59  ?  280 ARG A CA  1 
ATOM   2020 C C   . ARG A 1 280 ? 53.104 -12.629 25.797  1.00 73.68  ?  280 ARG A C   1 
ATOM   2021 O O   . ARG A 1 280 ? 53.442 -13.763 25.432  1.00 81.57  ?  280 ARG A O   1 
ATOM   2022 C CB  . ARG A 1 280 ? 50.675 -12.816 26.310  1.00 61.94  ?  280 ARG A CB  1 
ATOM   2023 C CG  . ARG A 1 280 ? 51.006 -12.768 27.787  1.00 71.35  ?  280 ARG A CG  1 
ATOM   2024 C CD  . ARG A 1 280 ? 49.809 -13.115 28.655  1.00 63.01  ?  280 ARG A CD  1 
ATOM   2025 N NE  . ARG A 1 280 ? 50.203 -13.101 30.055  1.00 63.16  ?  280 ARG A NE  1 
ATOM   2026 C CZ  . ARG A 1 280 ? 49.357 -13.132 31.076  1.00 66.96  ?  280 ARG A CZ  1 
ATOM   2027 N NH1 . ARG A 1 280 ? 48.039 -13.207 30.874  1.00 67.48  ?  280 ARG A NH1 1 
ATOM   2028 N NH2 . ARG A 1 280 ? 49.843 -13.095 32.301  1.00 63.17  ?  280 ARG A NH2 1 
ATOM   2029 N N   . PRO A 1 281 ? 53.927 -11.834 26.465  1.00 67.38  ?  281 PRO A N   1 
ATOM   2030 C CA  . PRO A 1 281 ? 55.344 -12.194 26.607  1.00 67.13  ?  281 PRO A CA  1 
ATOM   2031 C C   . PRO A 1 281 ? 55.560 -13.438 27.450  1.00 68.02  ?  281 PRO A C   1 
ATOM   2032 O O   . PRO A 1 281 ? 54.826 -13.708 28.400  1.00 70.89  ?  281 PRO A O   1 
ATOM   2033 C CB  . PRO A 1 281 ? 55.952 -10.958 27.267  1.00 78.15  ?  281 PRO A CB  1 
ATOM   2034 C CG  . PRO A 1 281 ? 55.013 -9.831  26.835  1.00 81.54  ?  281 PRO A CG  1 
ATOM   2035 C CD  . PRO A 1 281 ? 53.652 -10.441 26.852  1.00 70.94  ?  281 PRO A CD  1 
ATOM   2036 N N   . GLY A 1 282 ? 56.600 -14.193 27.086  1.00 75.84  ?  282 GLY A N   1 
ATOM   2037 C CA  . GLY A 1 282 ? 56.891 -15.504 27.650  1.00 71.43  ?  282 GLY A CA  1 
ATOM   2038 C C   . GLY A 1 282 ? 57.295 -15.432 29.102  1.00 81.50  ?  282 GLY A C   1 
ATOM   2039 O O   . GLY A 1 282 ? 57.384 -14.343 29.662  1.00 87.37  ?  282 GLY A O   1 
ATOM   2040 N N   . LEU B 1 6   ? 56.666 4.190   25.425  1.00 135.78 ?  6   LEU B N   1 
ATOM   2041 C CA  . LEU B 1 6   ? 56.918 5.534   24.902  1.00 135.73 ?  6   LEU B CA  1 
ATOM   2042 C C   . LEU B 1 6   ? 58.420 5.813   24.929  1.00 140.59 ?  6   LEU B C   1 
ATOM   2043 O O   . LEU B 1 6   ? 59.159 5.123   25.643  1.00 142.77 ?  6   LEU B O   1 
ATOM   2044 C CB  . LEU B 1 6   ? 56.121 6.594   25.689  1.00 129.92 ?  6   LEU B CB  1 
ATOM   2045 C CG  . LEU B 1 6   ? 56.177 6.746   27.218  1.00 123.43 ?  6   LEU B CG  1 
ATOM   2046 C CD1 . LEU B 1 6   ? 55.721 8.142   27.646  1.00 122.82 ?  6   LEU B CD1 1 
ATOM   2047 C CD2 . LEU B 1 6   ? 55.323 5.701   27.906  1.00 117.44 ?  6   LEU B CD2 1 
ATOM   2048 N N   . SER B 1 7   ? 58.861 6.815   24.152  1.00 146.23 ?  7   SER B N   1 
ATOM   2049 C CA  . SER B 1 7   ? 60.288 7.090   23.912  1.00 146.28 ?  7   SER B CA  1 
ATOM   2050 C C   . SER B 1 7   ? 60.945 7.793   25.111  1.00 157.48 ?  7   SER B C   1 
ATOM   2051 O O   . SER B 1 7   ? 61.486 8.899   25.021  1.00 161.72 ?  7   SER B O   1 
ATOM   2052 C CB  . SER B 1 7   ? 60.454 7.908   22.637  1.00 137.65 ?  7   SER B CB  1 
ATOM   2053 O OG  . SER B 1 7   ? 59.990 7.211   21.483  1.00 131.06 ?  7   SER B OG  1 
ATOM   2054 N N   . GLU B 1 8   ? 60.925 7.086   26.247  1.00 160.75 ?  8   GLU B N   1 
ATOM   2055 C CA  . GLU B 1 8   ? 61.400 7.648   27.511  1.00 152.97 ?  8   GLU B CA  1 
ATOM   2056 C C   . GLU B 1 8   ? 62.918 7.824   27.510  1.00 148.65 ?  8   GLU B C   1 
ATOM   2057 O O   . GLU B 1 8   ? 63.428 8.900   27.850  1.00 136.07 ?  8   GLU B O   1 
ATOM   2058 C CB  . GLU B 1 8   ? 60.944 6.752   28.669  1.00 147.92 ?  8   GLU B CB  1 
ATOM   2059 C CG  . GLU B 1 8   ? 60.869 5.254   28.315  1.00 145.38 ?  8   GLU B CG  1 
ATOM   2060 C CD  . GLU B 1 8   ? 62.226 4.581   28.365  1.00 145.17 ?  8   GLU B CD  1 
ATOM   2061 O OE1 . GLU B 1 8   ? 63.154 5.236   28.879  1.00 146.58 ?  8   GLU B OE1 1 
ATOM   2062 O OE2 . GLU B 1 8   ? 62.371 3.422   27.903  1.00 140.77 -1 8   GLU B OE2 1 
ATOM   2063 N N   . LEU B 1 9   ? 63.646 6.776   27.117  1.00 157.24 ?  9   LEU B N   1 
ATOM   2064 C CA  . LEU B 1 9   ? 65.102 6.812   26.973  1.00 154.62 ?  9   LEU B CA  1 
ATOM   2065 C C   . LEU B 1 9   ? 65.467 7.644   25.748  1.00 153.16 ?  9   LEU B C   1 
ATOM   2066 O O   . LEU B 1 9   ? 65.066 7.293   24.628  1.00 150.91 ?  9   LEU B O   1 
ATOM   2067 C CB  . LEU B 1 9   ? 65.637 5.379   26.861  1.00 146.06 ?  9   LEU B CB  1 
ATOM   2068 C CG  . LEU B 1 9   ? 67.110 5.032   26.660  1.00 134.19 ?  9   LEU B CG  1 
ATOM   2069 C CD1 . LEU B 1 9   ? 67.439 5.105   25.181  1.00 126.51 ?  9   LEU B CD1 1 
ATOM   2070 C CD2 . LEU B 1 9   ? 68.012 5.917   27.506  1.00 133.71 ?  9   LEU B CD2 1 
ATOM   2071 N N   . PRO B 1 10  ? 66.235 8.741   25.908  1.00 150.13 ?  10  PRO B N   1 
ATOM   2072 C CA  . PRO B 1 10  ? 66.323 9.766   24.851  1.00 151.32 ?  10  PRO B CA  1 
ATOM   2073 C C   . PRO B 1 10  ? 66.957 9.336   23.527  1.00 154.11 ?  10  PRO B C   1 
ATOM   2074 O O   . PRO B 1 10  ? 67.342 8.177   23.326  1.00 154.69 ?  10  PRO B O   1 
ATOM   2075 C CB  . PRO B 1 10  ? 67.151 10.871  25.525  1.00 149.09 ?  10  PRO B CB  1 
ATOM   2076 C CG  . PRO B 1 10  ? 66.864 10.711  26.985  1.00 145.99 ?  10  PRO B CG  1 
ATOM   2077 C CD  . PRO B 1 10  ? 66.760 9.230   27.198  1.00 147.78 ?  10  PRO B CD  1 
ATOM   2078 N N   . MET B 1 11  ? 67.051 10.304  22.608  1.00 146.67 ?  11  MET B N   1 
ATOM   2079 C CA  . MET B 1 11  ? 67.505 10.106  21.230  1.00 135.08 ?  11  MET B CA  1 
ATOM   2080 C C   . MET B 1 11  ? 68.574 11.097  20.914  1.00 130.52 ?  11  MET B C   1 
ATOM   2081 O O   . MET B 1 11  ? 68.427 12.311  21.205  1.00 131.27 ?  11  MET B O   1 
ATOM   2082 C CB  . MET B 1 11  ? 66.335 10.295  20.245  1.00 127.10 ?  11  MET B CB  1 
ATOM   2083 C CG  . MET B 1 11  ? 65.049 9.553   20.570  1.00 120.90 ?  11  MET B CG  1 
ATOM   2084 S SD  . MET B 1 11  ? 64.837 7.950   19.777  1.00 112.69 ?  11  MET B SD  1 
ATOM   2085 C CE  . MET B 1 11  ? 65.079 6.855   21.158  1.00 111.74 ?  11  MET B CE  1 
ATOM   2086 N N   . PRO B 1 12  ? 69.691 10.705  20.281  1.00 124.42 ?  12  PRO B N   1 
ATOM   2087 C CA  . PRO B 1 12  ? 70.493 11.663  19.532  1.00 117.16 ?  12  PRO B CA  1 
ATOM   2088 C C   . PRO B 1 12  ? 69.718 12.144  18.314  1.00 114.51 ?  12  PRO B C   1 
ATOM   2089 O O   . PRO B 1 12  ? 68.747 11.523  17.880  1.00 115.04 ?  12  PRO B O   1 
ATOM   2090 C CB  . PRO B 1 12  ? 71.731 10.866  19.119  1.00 113.51 ?  12  PRO B CB  1 
ATOM   2091 C CG  . PRO B 1 12  ? 71.266 9.468   19.086  1.00 111.57 ?  12  PRO B CG  1 
ATOM   2092 C CD  . PRO B 1 12  ? 70.259 9.344   20.209  1.00 120.53 ?  12  PRO B CD  1 
ATOM   2093 N N   . SER B 1 13  ? 70.148 13.280  17.764  1.00 116.81 ?  13  SER B N   1 
ATOM   2094 C CA  . SER B 1 13  ? 69.587 13.780  16.510  1.00 117.50 ?  13  SER B CA  1 
ATOM   2095 C C   . SER B 1 13  ? 70.631 13.567  15.418  1.00 116.05 ?  13  SER B C   1 
ATOM   2096 O O   . SER B 1 13  ? 71.430 14.473  15.134  1.00 122.39 ?  13  SER B O   1 
ATOM   2097 C CB  . SER B 1 13  ? 69.193 15.259  16.622  1.00 116.19 ?  13  SER B CB  1 
ATOM   2098 O OG  . SER B 1 13  ? 67.895 15.425  17.186  1.00 112.60 ?  13  SER B OG  1 
ATOM   2099 N N   . PRO B 1 14  ? 70.670 12.393  14.774  1.00 107.11 ?  14  PRO B N   1 
ATOM   2100 C CA  . PRO B 1 14  ? 71.833 12.052  13.938  1.00 109.77 ?  14  PRO B CA  1 
ATOM   2101 C C   . PRO B 1 14  ? 71.844 12.838  12.632  1.00 114.02 ?  14  PRO B C   1 
ATOM   2102 O O   . PRO B 1 14  ? 70.803 13.042  12.003  1.00 118.22 ?  14  PRO B O   1 
ATOM   2103 C CB  . PRO B 1 14  ? 71.669 10.547  13.696  1.00 102.94 ?  14  PRO B CB  1 
ATOM   2104 C CG  . PRO B 1 14  ? 70.196 10.292  13.825  1.00 100.02 ?  14  PRO B CG  1 
ATOM   2105 C CD  . PRO B 1 14  ? 69.637 11.338  14.761  1.00 102.29 ?  14  PRO B CD  1 
ATOM   2106 N N   . ALA B 1 15  ? 73.040 13.286  12.238  1.00 113.55 ?  15  ALA B N   1 
ATOM   2107 C CA  . ALA B 1 15  ? 73.218 14.234  11.142  1.00 114.82 ?  15  ALA B CA  1 
ATOM   2108 C C   . ALA B 1 15  ? 73.792 13.532  9.915   1.00 116.16 ?  15  ALA B C   1 
ATOM   2109 O O   . ALA B 1 15  ? 74.688 12.693  10.039  1.00 121.63 ?  15  ALA B O   1 
ATOM   2110 C CB  . ALA B 1 15  ? 74.132 15.393  11.566  1.00 107.55 ?  15  ALA B CB  1 
ATOM   2111 N N   . SER B 1 16  ? 73.287 13.899  8.725   1.00 111.49 ?  16  SER B N   1 
ATOM   2112 C CA  . SER B 1 16  ? 73.537 13.147  7.489   1.00 104.31 ?  16  SER B CA  1 
ATOM   2113 C C   . SER B 1 16  ? 75.013 13.078  7.101   1.00 111.70 ?  16  SER B C   1 
ATOM   2114 O O   . SER B 1 16  ? 75.598 11.988  7.093   1.00 107.95 ?  16  SER B O   1 
ATOM   2115 C CB  . SER B 1 16  ? 72.725 13.733  6.328   1.00 86.58  ?  16  SER B CB  1 
ATOM   2116 O OG  . SER B 1 16  ? 71.493 13.048  6.174   1.00 81.23  ?  16  SER B OG  1 
ATOM   2117 N N   . GLU B 1 17  ? 75.629 14.226  6.785   1.00 119.78 ?  17  GLU B N   1 
ATOM   2118 C CA  . GLU B 1 17  ? 77.054 14.262  6.460   1.00 124.47 ?  17  GLU B CA  1 
ATOM   2119 C C   . GLU B 1 17  ? 77.952 14.241  7.729   1.00 123.01 ?  17  GLU B C   1 
ATOM   2120 O O   . GLU B 1 17  ? 79.134 14.592  7.644   1.00 127.56 ?  17  GLU B O   1 
ATOM   2121 C CB  . GLU B 1 17  ? 77.364 15.471  5.558   1.00 121.22 ?  17  GLU B CB  1 
ATOM   2122 C CG  . GLU B 1 17  ? 77.117 15.215  4.034   1.00 115.36 ?  17  GLU B CG  1 
ATOM   2123 C CD  . GLU B 1 17  ? 75.707 15.623  3.570   1.00 111.45 ?  17  GLU B CD  1 
ATOM   2124 O OE1 . GLU B 1 17  ? 75.041 16.392  4.306   1.00 109.46 ?  17  GLU B OE1 1 
ATOM   2125 O OE2 . GLU B 1 17  ? 75.257 15.171  2.482   1.00 105.27 -1 17  GLU B OE2 1 
ATOM   2126 N N   . GLU B 1 18  ? 77.394 13.834  8.882   1.00 122.01 ?  18  GLU B N   1 
ATOM   2127 C CA  . GLU B 1 18  ? 78.134 13.460  10.088  1.00 120.77 ?  18  GLU B CA  1 
ATOM   2128 C C   . GLU B 1 18  ? 78.078 11.963  10.386  1.00 125.68 ?  18  GLU B C   1 
ATOM   2129 O O   . GLU B 1 18  ? 79.040 11.428  10.946  1.00 124.40 ?  18  GLU B O   1 
ATOM   2130 C CB  . GLU B 1 18  ? 77.593 14.224  11.310  1.00 121.39 ?  18  GLU B CB  1 
ATOM   2131 C CG  . GLU B 1 18  ? 78.357 15.491  11.711  1.00 122.76 ?  18  GLU B CG  1 
ATOM   2132 C CD  . GLU B 1 18  ? 77.476 16.505  12.458  1.00 125.81 ?  18  GLU B CD  1 
ATOM   2133 O OE1 . GLU B 1 18  ? 77.371 17.668  12.004  1.00 125.95 ?  18  GLU B OE1 1 
ATOM   2134 O OE2 . GLU B 1 18  ? 76.882 16.134  13.498  1.00 128.11 -1 18  GLU B OE2 1 
ATOM   2135 N N   . VAL B 1 19  ? 76.977 11.282  10.020  1.00 130.23 ?  19  VAL B N   1 
ATOM   2136 C CA  . VAL B 1 19  ? 76.920 9.814   10.035  1.00 116.22 ?  19  VAL B CA  1 
ATOM   2137 C C   . VAL B 1 19  ? 77.835 9.245   8.954   1.00 108.81 ?  19  VAL B C   1 
ATOM   2138 O O   . VAL B 1 19  ? 78.382 8.141   9.103   1.00 104.10 ?  19  VAL B O   1 
ATOM   2139 C CB  . VAL B 1 19  ? 75.458 9.310   9.879   1.00 100.81 ?  19  VAL B CB  1 
ATOM   2140 C CG1 . VAL B 1 19  ? 75.391 7.862   9.369   1.00 93.54  ?  19  VAL B CG1 1 
ATOM   2141 C CG2 . VAL B 1 19  ? 74.691 9.406   11.205  1.00 94.16  ?  19  VAL B CG2 1 
ATOM   2142 N N   . GLY B 1 20  ? 78.038 9.994   7.866   1.00 105.41 ?  20  GLY B N   1 
ATOM   2143 C CA  . GLY B 1 20  ? 79.013 9.649   6.842   1.00 104.91 ?  20  GLY B CA  1 
ATOM   2144 C C   . GLY B 1 20  ? 80.462 9.794   7.266   1.00 108.69 ?  20  GLY B C   1 
ATOM   2145 O O   . GLY B 1 20  ? 81.337 9.288   6.556   1.00 104.69 ?  20  GLY B O   1 
ATOM   2146 N N   . ALA B 1 21  ? 80.735 10.469  8.393   1.00 111.69 ?  21  ALA B N   1 
ATOM   2147 C CA  . ALA B 1 21  ? 82.063 10.509  9.004   1.00 111.68 ?  21  ALA B CA  1 
ATOM   2148 C C   . ALA B 1 21  ? 82.283 9.349   9.974   1.00 114.19 ?  21  ALA B C   1 
ATOM   2149 O O   . ALA B 1 21  ? 83.333 8.698   9.929   1.00 110.16 ?  21  ALA B O   1 
ATOM   2150 C CB  . ALA B 1 21  ? 82.277 11.840  9.726   1.00 116.14 ?  21  ALA B CB  1 
ATOM   2151 N N   . LEU B 1 22  ? 81.300 9.084   10.852  1.00 121.66 ?  22  LEU B N   1 
ATOM   2152 C CA  . LEU B 1 22  ? 81.326 7.895   11.708  1.00 123.27 ?  22  LEU B CA  1 
ATOM   2153 C C   . LEU B 1 22  ? 81.541 6.613   10.913  1.00 126.98 ?  22  LEU B C   1 
ATOM   2154 O O   . LEU B 1 22  ? 82.040 5.630   11.469  1.00 131.55 ?  22  LEU B O   1 
ATOM   2155 C CB  . LEU B 1 22  ? 80.008 7.780   12.503  1.00 115.39 ?  22  LEU B CB  1 
ATOM   2156 C CG  . LEU B 1 22  ? 79.674 6.597   13.438  1.00 111.41 ?  22  LEU B CG  1 
ATOM   2157 C CD1 . LEU B 1 22  ? 80.848 6.078   14.288  1.00 107.73 ?  22  LEU B CD1 1 
ATOM   2158 C CD2 . LEU B 1 22  ? 78.479 6.961   14.304  1.00 110.31 ?  22  LEU B CD2 1 
ATOM   2159 N N   . TYR B 1 23  ? 81.174 6.603   9.626   1.00 128.56 ?  23  TYR B N   1 
ATOM   2160 C CA  . TYR B 1 23  ? 81.252 5.405   8.799   1.00 123.25 ?  23  TYR B CA  1 
ATOM   2161 C C   . TYR B 1 23  ? 82.211 5.521   7.608   1.00 122.48 ?  23  TYR B C   1 
ATOM   2162 O O   . TYR B 1 23  ? 82.603 4.482   7.070   1.00 122.29 ?  23  TYR B O   1 
ATOM   2163 C CB  . TYR B 1 23  ? 79.844 4.993   8.312   1.00 119.03 ?  23  TYR B CB  1 
ATOM   2164 C CG  . TYR B 1 23  ? 79.001 4.204   9.339   1.00 120.74 ?  23  TYR B CG  1 
ATOM   2165 C CD1 . TYR B 1 23  ? 78.366 4.845   10.400  1.00 122.24 ?  23  TYR B CD1 1 
ATOM   2166 C CD2 . TYR B 1 23  ? 78.836 2.824   9.230   1.00 115.86 ?  23  TYR B CD2 1 
ATOM   2167 C CE1 . TYR B 1 23  ? 77.610 4.130   11.323  1.00 118.63 ?  23  TYR B CE1 1 
ATOM   2168 C CE2 . TYR B 1 23  ? 78.078 2.099   10.146  1.00 110.08 ?  23  TYR B CE2 1 
ATOM   2169 C CZ  . TYR B 1 23  ? 77.466 2.759   11.191  1.00 113.10 ?  23  TYR B CZ  1 
ATOM   2170 O OH  . TYR B 1 23  ? 76.713 2.055   12.109  1.00 108.90 ?  23  TYR B OH  1 
ATOM   2171 N N   . ASP B 1 24  ? 82.611 6.738   7.183   1.00 118.34 ?  24  ASP B N   1 
ATOM   2172 C CA  . ASP B 1 24  ? 83.867 6.875   6.430   1.00 114.88 ?  24  ASP B CA  1 
ATOM   2173 C C   . ASP B 1 24  ? 85.054 6.399   7.269   1.00 118.04 ?  24  ASP B C   1 
ATOM   2174 O O   . ASP B 1 24  ? 86.075 5.975   6.709   1.00 112.08 ?  24  ASP B O   1 
ATOM   2175 C CB  . ASP B 1 24  ? 84.120 8.336   5.979   1.00 109.58 ?  24  ASP B CB  1 
ATOM   2176 C CG  . ASP B 1 24  ? 83.677 8.617   4.531   1.00 104.35 ?  24  ASP B CG  1 
ATOM   2177 O OD1 . ASP B 1 24  ? 83.497 7.654   3.765   1.00 105.83 ?  24  ASP B OD1 1 
ATOM   2178 O OD2 . ASP B 1 24  ? 83.520 9.801   4.145   1.00 100.77 -1 24  ASP B OD2 1 
ATOM   2179 N N   . ARG B 1 25  ? 84.924 6.468   8.607   1.00 126.25 ?  25  ARG B N   1 
ATOM   2180 C CA  . ARG B 1 25  ? 85.864 5.900   9.573   1.00 130.87 ?  25  ARG B CA  1 
ATOM   2181 C C   . ARG B 1 25  ? 85.659 4.394   9.755   1.00 140.33 ?  25  ARG B C   1 
ATOM   2182 O O   . ARG B 1 25  ? 86.640 3.640   9.781   1.00 144.35 ?  25  ARG B O   1 
ATOM   2183 C CB  . ARG B 1 25  ? 85.700 6.624   10.920  1.00 128.28 ?  25  ARG B CB  1 
ATOM   2184 C CG  . ARG B 1 25  ? 86.777 6.392   11.985  1.00 125.44 ?  25  ARG B CG  1 
ATOM   2185 C CD  . ARG B 1 25  ? 86.512 7.302   13.200  1.00 125.12 ?  25  ARG B CD  1 
ATOM   2186 N NE  . ARG B 1 25  ? 85.822 8.535   12.808  1.00 121.64 ?  25  ARG B NE  1 
ATOM   2187 C CZ  . ARG B 1 25  ? 84.703 8.992   13.366  1.00 112.31 ?  25  ARG B CZ  1 
ATOM   2188 N NH1 . ARG B 1 25  ? 84.150 10.118  12.927  1.00 102.59 ?  25  ARG B NH1 1 
ATOM   2189 N NH2 . ARG B 1 25  ? 84.135 8.321   14.359  1.00 115.03 ?  25  ARG B NH2 1 
ATOM   2190 N N   . PHE B 1 26  ? 84.414 3.944   9.898   1.00 146.74 ?  26  PHE B N   1 
ATOM   2191 C CA  . PHE B 1 26  ? 84.135 2.526   10.205  1.00 143.90 ?  26  PHE B CA  1 
ATOM   2192 C C   . PHE B 1 26  ? 83.926 1.526   9.048   1.00 146.33 ?  26  PHE B C   1 
ATOM   2193 O O   . PHE B 1 26  ? 84.326 0.370   9.156   1.00 149.63 ?  26  PHE B O   1 
ATOM   2194 C CB  . PHE B 1 26  ? 82.930 2.460   11.150  1.00 133.52 ?  26  PHE B CB  1 
ATOM   2195 C CG  . PHE B 1 26  ? 83.282 2.032   12.536  1.00 126.51 ?  26  PHE B CG  1 
ATOM   2196 C CD1 . PHE B 1 26  ? 84.449 2.468   13.126  1.00 124.07 ?  26  PHE B CD1 1 
ATOM   2197 C CD2 . PHE B 1 26  ? 82.458 1.187   13.243  1.00 123.87 ?  26  PHE B CD2 1 
ATOM   2198 C CE1 . PHE B 1 26  ? 84.787 2.072   14.400  1.00 122.87 ?  26  PHE B CE1 1 
ATOM   2199 C CE2 . PHE B 1 26  ? 82.789 0.783   14.519  1.00 124.66 ?  26  PHE B CE2 1 
ATOM   2200 C CZ  . PHE B 1 26  ? 83.956 1.229   15.099  1.00 125.05 ?  26  PHE B CZ  1 
ATOM   2201 N N   . THR B 1 27  ? 83.331 1.951   7.938   1.00 144.48 ?  27  THR B N   1 
ATOM   2202 C CA  . THR B 1 27  ? 83.150 1.061   6.783   1.00 136.11 ?  27  THR B CA  1 
ATOM   2203 C C   . THR B 1 27  ? 84.420 1.203   6.131   1.00 140.36 ?  27  THR B C   1 
ATOM   2204 O O   . THR B 1 27  ? 84.531 1.401   4.932   1.00 137.60 ?  27  THR B O   1 
ATOM   2205 C CB  . THR B 1 27  ? 81.990 1.533   5.907   1.00 120.48 ?  27  THR B CB  1 
ATOM   2206 O OG1 . THR B 1 27  ? 82.368 2.729   5.224   1.00 128.93 ?  27  THR B OG1 1 
ATOM   2207 C CG2 . THR B 1 27  ? 80.793 1.815   6.760   1.00 106.77 ?  27  THR B CG2 1 
ATOM   2208 N N   . ALA B 1 28  ? 85.412 1.112   6.959   1.00 145.19 ?  28  ALA B N   1 
ATOM   2209 C CA  . ALA B 1 28  ? 86.697 1.250   6.499   1.00 143.47 ?  28  ALA B CA  1 
ATOM   2210 C C   . ALA B 1 28  ? 87.372 0.992   7.799   1.00 156.80 ?  28  ALA B C   1 
ATOM   2211 O O   . ALA B 1 28  ? 86.846 1.324   8.846   1.00 163.25 ?  28  ALA B O   1 
ATOM   2212 C CB  . ALA B 1 28  ? 86.933 2.642   6.034   1.00 135.00 ?  28  ALA B CB  1 
ATOM   2213 N N   . LEU B 1 29  ? 88.477 0.312   7.759   1.00 162.77 ?  29  LEU B N   1 
ATOM   2214 C CA  . LEU B 1 29  ? 89.322 0.022   8.924   1.00 162.71 ?  29  LEU B CA  1 
ATOM   2215 C C   . LEU B 1 29  ? 88.718 -0.918  9.953   1.00 164.84 ?  29  LEU B C   1 
ATOM   2216 O O   . LEU B 1 29  ? 88.910 -0.748  11.139  1.00 165.68 ?  29  LEU B O   1 
ATOM   2217 C CB  . LEU B 1 29  ? 89.746 1.312   9.628   1.00 153.12 ?  29  LEU B CB  1 
ATOM   2218 C CG  . LEU B 1 29  ? 90.513 2.351   8.810   1.00 144.86 ?  29  LEU B CG  1 
ATOM   2219 C CD1 . LEU B 1 29  ? 91.193 1.740   7.590   1.00 140.34 ?  29  LEU B CD1 1 
ATOM   2220 C CD2 . LEU B 1 29  ? 89.592 3.494   8.415   1.00 141.62 ?  29  LEU B CD2 1 
ATOM   2221 N N   . GLY B 1 30  ? 87.970 -1.921  9.535   1.00 163.27 ?  30  GLY B N   1 
ATOM   2222 C CA  . GLY B 1 30  ? 87.519 -2.862  10.543  1.00 162.67 ?  30  GLY B CA  1 
ATOM   2223 C C   . GLY B 1 30  ? 86.087 -3.140  10.914  1.00 161.98 ?  30  GLY B C   1 
ATOM   2224 O O   . GLY B 1 30  ? 85.853 -4.115  11.632  1.00 162.84 ?  30  GLY B O   1 
ATOM   2225 N N   . ALA B 1 31  ? 85.144 -2.303  10.504  1.00 157.43 ?  31  ALA B N   1 
ATOM   2226 C CA  . ALA B 1 31  ? 83.752 -2.619  10.741  1.00 146.02 ?  31  ALA B CA  1 
ATOM   2227 C C   . ALA B 1 31  ? 83.229 -3.123  9.439   1.00 144.09 ?  31  ALA B C   1 
ATOM   2228 O O   . ALA B 1 31  ? 82.201 -3.786  9.408   1.00 143.86 ?  31  ALA B O   1 
ATOM   2229 C CB  . ALA B 1 31  ? 82.978 -1.408  11.166  1.00 138.24 ?  31  ALA B CB  1 
ATOM   2230 N N   . ALA B 1 32  ? 83.953 -2.852  8.360   1.00 140.92 ?  32  ALA B N   1 
ATOM   2231 C CA  . ALA B 1 32  ? 83.479 -3.230  7.056   1.00 134.38 ?  32  ALA B CA  1 
ATOM   2232 C C   . ALA B 1 32  ? 84.512 -3.011  6.021   1.00 142.81 ?  32  ALA B C   1 
ATOM   2233 O O   . ALA B 1 32  ? 84.859 -1.869  5.752   1.00 147.90 ?  32  ALA B O   1 
ATOM   2234 C CB  . ALA B 1 32  ? 82.317 -2.343  6.717   1.00 125.66 ?  32  ALA B CB  1 
ATOM   2235 N N   . SER B 1 33  ? 85.056 -4.070  5.433   1.00 142.84 ?  33  SER B N   1 
ATOM   2236 C CA  . SER B 1 33  ? 85.959 -3.761  4.325   1.00 140.61 ?  33  SER B CA  1 
ATOM   2237 C C   . SER B 1 33  ? 85.386 -4.159  2.957   1.00 142.67 ?  33  SER B C   1 
ATOM   2238 O O   . SER B 1 33  ? 85.031 -3.267  2.176   1.00 134.11 ?  33  SER B O   1 
ATOM   2239 C CB  . SER B 1 33  ? 87.345 -4.389  4.540   1.00 126.31 ?  33  SER B CB  1 
ATOM   2240 O OG  . SER B 1 33  ? 88.127 -3.699  5.514   1.00 113.30 ?  33  SER B OG  1 
ATOM   2241 N N   . LEU B 1 34  ? 85.193 -5.455  2.694   1.00 143.35 ?  34  LEU B N   1 
ATOM   2242 C CA  . LEU B 1 34  ? 85.124 -5.928  1.305   1.00 135.88 ?  34  LEU B CA  1 
ATOM   2243 C C   . LEU B 1 34  ? 84.167 -7.125  1.254   1.00 132.82 ?  34  LEU B C   1 
ATOM   2244 O O   . LEU B 1 34  ? 84.570 -8.281  1.428   1.00 136.72 ?  34  LEU B O   1 
ATOM   2245 C CB  . LEU B 1 34  ? 86.526 -6.252  0.776   1.00 127.08 ?  34  LEU B CB  1 
ATOM   2246 C CG  . LEU B 1 34  ? 87.477 -7.374  1.255   1.00 118.31 ?  34  LEU B CG  1 
ATOM   2247 C CD1 . LEU B 1 34  ? 88.803 -7.302  0.502   1.00 117.87 ?  34  LEU B CD1 1 
ATOM   2248 C CD2 . LEU B 1 34  ? 87.726 -7.394  2.772   1.00 99.66  ?  34  LEU B CD2 1 
ATOM   2249 N N   . GLY B 1 35  ? 82.898 -6.821  0.988   1.00 123.27 ?  35  GLY B N   1 
ATOM   2250 C CA  . GLY B 1 35  ? 81.853 -7.812  0.895   1.00 108.56 ?  35  GLY B CA  1 
ATOM   2251 C C   . GLY B 1 35  ? 81.055 -8.077  2.157   1.00 95.65  ?  35  GLY B C   1 
ATOM   2252 O O   . GLY B 1 35  ? 80.585 -9.208  2.333   1.00 94.11  ?  35  GLY B O   1 
ATOM   2253 N N   . GLU B 1 36  ? 80.862 -7.076  3.025   1.00 93.73  ?  36  GLU B N   1 
ATOM   2254 C CA  . GLU B 1 36  ? 80.151 -7.261  4.289   1.00 94.03  ?  36  GLU B CA  1 
ATOM   2255 C C   . GLU B 1 36  ? 78.768 -6.611  4.303   1.00 81.10  ?  36  GLU B C   1 
ATOM   2256 O O   . GLU B 1 36  ? 78.584 -5.470  3.851   1.00 77.76  ?  36  GLU B O   1 
ATOM   2257 C CB  . GLU B 1 36  ? 80.958 -6.718  5.474   1.00 101.99 ?  36  GLU B CB  1 
ATOM   2258 C CG  . GLU B 1 36  ? 80.477 -7.300  6.791   1.00 104.37 ?  36  GLU B CG  1 
ATOM   2259 C CD  . GLU B 1 36  ? 81.472 -7.135  7.907   1.00 112.57 ?  36  GLU B CD  1 
ATOM   2260 O OE1 . GLU B 1 36  ? 82.333 -6.241  7.786   1.00 118.05 ?  36  GLU B OE1 1 
ATOM   2261 O OE2 . GLU B 1 36  ? 81.412 -7.925  8.882   1.00 110.92 -1 36  GLU B OE2 1 
ATOM   2262 N N   . ASN B 1 37  ? 77.799 -7.350  4.842   1.00 70.09  ?  37  ASN B N   1 
ATOM   2263 C CA  . ASN B 1 37  ? 76.473 -6.813  5.124   1.00 73.80  ?  37  ASN B CA  1 
ATOM   2264 C C   . ASN B 1 37  ? 76.512 -5.981  6.410   1.00 78.34  ?  37  ASN B C   1 
ATOM   2265 O O   . ASN B 1 37  ? 76.908 -6.469  7.477   1.00 70.53  ?  37  ASN B O   1 
ATOM   2266 C CB  . ASN B 1 37  ? 75.462 -7.953  5.246   1.00 76.54  ?  37  ASN B CB  1 
ATOM   2267 C CG  . ASN B 1 37  ? 74.954 -8.441  3.903   1.00 74.76  ?  37  ASN B CG  1 
ATOM   2268 O OD1 . ASN B 1 37  ? 74.523 -7.651  3.061   1.00 77.21  ?  37  ASN B OD1 1 
ATOM   2269 N ND2 . ASN B 1 37  ? 74.994 -9.752  3.700   1.00 74.79  ?  37  ASN B ND2 1 
ATOM   2270 N N   . LEU B 1 38  ? 76.121 -4.721  6.309   1.00 82.31  ?  38  LEU B N   1 
ATOM   2271 C CA  . LEU B 1 38  ? 76.023 -3.882  7.497   1.00 69.43  ?  38  LEU B CA  1 
ATOM   2272 C C   . LEU B 1 38  ? 74.645 -4.014  8.129   1.00 75.08  ?  38  LEU B C   1 
ATOM   2273 O O   . LEU B 1 38  ? 73.926 -3.024  8.313   1.00 74.80  ?  38  LEU B O   1 
ATOM   2274 C CB  . LEU B 1 38  ? 76.334 -2.438  7.134   1.00 58.63  ?  38  LEU B CB  1 
ATOM   2275 C CG  . LEU B 1 38  ? 77.643 -2.366  6.354   1.00 70.71  ?  38  LEU B CG  1 
ATOM   2276 C CD1 . LEU B 1 38  ? 77.877 -0.978  5.780   1.00 65.38  ?  38  LEU B CD1 1 
ATOM   2277 C CD2 . LEU B 1 38  ? 78.787 -2.810  7.239   1.00 63.42  ?  38  LEU B CD2 1 
ATOM   2278 N N   . HIS B 1 39  ? 74.249 -5.250  8.441   1.00 70.48  ?  39  HIS B N   1 
ATOM   2279 C CA  . HIS B 1 39  ? 72.968 -5.442  9.115   1.00 77.17  ?  39  HIS B CA  1 
ATOM   2280 C C   . HIS B 1 39  ? 72.907 -6.807  9.799   1.00 76.65  ?  39  HIS B C   1 
ATOM   2281 O O   . HIS B 1 39  ? 73.698 -7.718  9.510   1.00 77.13  ?  39  HIS B O   1 
ATOM   2282 C CB  . HIS B 1 39  ? 71.781 -5.272  8.148   1.00 70.31  ?  39  HIS B CB  1 
ATOM   2283 C CG  . HIS B 1 39  ? 71.822 -6.185  6.957   1.00 69.01  ?  39  HIS B CG  1 
ATOM   2284 N ND1 . HIS B 1 39  ? 72.386 -5.815  5.754   1.00 72.67  ?  39  HIS B ND1 1 
ATOM   2285 C CD2 . HIS B 1 39  ? 71.343 -7.442  6.781   1.00 65.94  ?  39  HIS B CD2 1 
ATOM   2286 C CE1 . HIS B 1 39  ? 72.259 -6.811  4.893   1.00 76.58  ?  39  HIS B CE1 1 
ATOM   2287 N NE2 . HIS B 1 39  ? 71.637 -7.812  5.494   1.00 67.32  ?  39  HIS B NE2 1 
ATOM   2288 N N   . PHE B 1 40  ? 71.923 -6.918  10.699  1.00 63.02  ?  40  PHE B N   1 
ATOM   2289 C CA  . PHE B 1 40  ? 71.632 -8.109  11.477  1.00 61.00  ?  40  PHE B CA  1 
ATOM   2290 C C   . PHE B 1 40  ? 71.403 -9.321  10.584  1.00 64.93  ?  40  PHE B C   1 
ATOM   2291 O O   . PHE B 1 40  ? 71.035 -9.206  9.411   1.00 71.24  ?  40  PHE B O   1 
ATOM   2292 C CB  . PHE B 1 40  ? 70.387 -7.886  12.324  1.00 60.59  ?  40  PHE B CB  1 
ATOM   2293 C CG  . PHE B 1 40  ? 70.579 -6.897  13.432  1.00 64.05  ?  40  PHE B CG  1 
ATOM   2294 C CD1 . PHE B 1 40  ? 70.400 -5.549  13.210  1.00 66.80  ?  40  PHE B CD1 1 
ATOM   2295 C CD2 . PHE B 1 40  ? 70.918 -7.324  14.710  1.00 72.46  ?  40  PHE B CD2 1 
ATOM   2296 C CE1 . PHE B 1 40  ? 70.568 -4.623  14.232  1.00 75.56  ?  40  PHE B CE1 1 
ATOM   2297 C CE2 . PHE B 1 40  ? 71.080 -6.417  15.740  1.00 73.85  ?  40  PHE B CE2 1 
ATOM   2298 C CZ  . PHE B 1 40  ? 70.902 -5.058  15.500  1.00 75.56  ?  40  PHE B CZ  1 
ATOM   2299 N N   . GLY B 1 41  ? 71.624 -10.501 11.169  1.00 60.15  ?  41  GLY B N   1 
ATOM   2300 C CA  . GLY B 1 41  ? 71.246 -11.737 10.532  1.00 56.21  ?  41  GLY B CA  1 
ATOM   2301 C C   . GLY B 1 41  ? 69.839 -12.146 10.904  1.00 55.76  ?  41  GLY B C   1 
ATOM   2302 O O   . GLY B 1 41  ? 69.266 -11.675 11.882  1.00 58.83  ?  41  GLY B O   1 
ATOM   2303 N N   . TYR B 1 42  ? 69.269 -13.030 10.093  1.00 62.58  ?  42  TYR B N   1 
ATOM   2304 C CA  . TYR B 1 42  ? 67.952 -13.597 10.355  1.00 70.71  ?  42  TYR B CA  1 
ATOM   2305 C C   . TYR B 1 42  ? 68.092 -15.110 10.411  1.00 74.97  ?  42  TYR B C   1 
ATOM   2306 O O   . TYR B 1 42  ? 68.696 -15.714 9.516   1.00 75.58  ?  42  TYR B O   1 
ATOM   2307 C CB  . TYR B 1 42  ? 66.942 -13.160 9.290   1.00 61.81  ?  42  TYR B CB  1 
ATOM   2308 C CG  . TYR B 1 42  ? 65.515 -13.551 9.579   1.00 54.84  ?  42  TYR B CG  1 
ATOM   2309 C CD1 . TYR B 1 42  ? 65.079 -14.870 9.454   1.00 57.37  ?  42  TYR B CD1 1 
ATOM   2310 C CD2 . TYR B 1 42  ? 64.610 -12.607 10.032  1.00 55.36  ?  42  TYR B CD2 1 
ATOM   2311 C CE1 . TYR B 1 42  ? 63.760 -15.217 9.738   1.00 56.75  ?  42  TYR B CE1 1 
ATOM   2312 C CE2 . TYR B 1 42  ? 63.304 -12.941 10.320  1.00 53.56  ?  42  TYR B CE2 1 
ATOM   2313 C CZ  . TYR B 1 42  ? 62.888 -14.246 10.178  1.00 56.42  ?  42  TYR B CZ  1 
ATOM   2314 O OH  . TYR B 1 42  ? 61.589 -14.553 10.477  1.00 60.98  ?  42  TYR B OH  1 
ATOM   2315 N N   . TRP B 1 43  ? 67.567 -15.709 11.480  1.00 82.05  ?  43  TRP B N   1 
ATOM   2316 C CA  . TRP B 1 43  ? 67.659 -17.144 11.718  1.00 76.46  ?  43  TRP B CA  1 
ATOM   2317 C C   . TRP B 1 43  ? 66.277 -17.740 11.940  1.00 78.14  ?  43  TRP B C   1 
ATOM   2318 O O   . TRP B 1 43  ? 65.432 -17.140 12.615  1.00 75.72  ?  43  TRP B O   1 
ATOM   2319 C CB  . TRP B 1 43  ? 68.537 -17.456 12.923  1.00 69.19  ?  43  TRP B CB  1 
ATOM   2320 C CG  . TRP B 1 43  ? 69.983 -17.246 12.686  1.00 69.39  ?  43  TRP B CG  1 
ATOM   2321 C CD1 . TRP B 1 43  ? 70.875 -18.165 12.246  1.00 70.57  ?  43  TRP B CD1 1 
ATOM   2322 C CD2 . TRP B 1 43  ? 70.721 -16.033 12.894  1.00 64.22  ?  43  TRP B CD2 1 
ATOM   2323 N NE1 . TRP B 1 43  ? 72.129 -17.606 12.162  1.00 73.19  ?  43  TRP B NE1 1 
ATOM   2324 C CE2 . TRP B 1 43  ? 72.061 -16.298 12.561  1.00 61.60  ?  43  TRP B CE2 1 
ATOM   2325 C CE3 . TRP B 1 43  ? 70.381 -14.757 13.343  1.00 59.99  ?  43  TRP B CE3 1 
ATOM   2326 C CZ2 . TRP B 1 43  ? 73.059 -15.334 12.649  1.00 57.81  ?  43  TRP B CZ2 1 
ATOM   2327 C CZ3 . TRP B 1 43  ? 71.377 -13.800 13.426  1.00 56.32  ?  43  TRP B CZ3 1 
ATOM   2328 C CH2 . TRP B 1 43  ? 72.695 -14.093 13.075  1.00 52.26  ?  43  TRP B CH2 1 
ATOM   2329 N N   . ASP B 1 44  ? 66.073 -18.946 11.397  1.00 84.26  ?  44  ASP B N   1 
ATOM   2330 C CA  . ASP B 1 44  ? 64.766 -19.595 11.463  1.00 87.67  ?  44  ASP B CA  1 
ATOM   2331 C C   . ASP B 1 44  ? 64.383 -19.990 12.881  1.00 86.41  ?  44  ASP B C   1 
ATOM   2332 O O   . ASP B 1 44  ? 63.192 -20.013 13.213  1.00 83.91  ?  44  ASP B O   1 
ATOM   2333 C CB  . ASP B 1 44  ? 64.751 -20.828 10.574  1.00 91.50  ?  44  ASP B CB  1 
ATOM   2334 C CG  . ASP B 1 44  ? 64.473 -20.486 9.156   1.00 92.92  ?  44  ASP B CG  1 
ATOM   2335 O OD1 . ASP B 1 44  ? 63.635 -19.570 8.941   1.00 84.91  ?  44  ASP B OD1 1 
ATOM   2336 O OD2 . ASP B 1 44  ? 65.127 -21.086 8.267   1.00 99.78  -1 44  ASP B OD2 1 
ATOM   2337 N N   . SER B 1 45  ? 65.365 -20.325 13.714  1.00 87.22  ?  45  SER B N   1 
ATOM   2338 C CA  . SER B 1 45  ? 65.150 -20.712 15.100  1.00 94.91  ?  45  SER B CA  1 
ATOM   2339 C C   . SER B 1 45  ? 66.348 -20.225 15.902  1.00 99.76  ?  45  SER B C   1 
ATOM   2340 O O   . SER B 1 45  ? 67.468 -20.232 15.383  1.00 98.90  ?  45  SER B O   1 
ATOM   2341 C CB  . SER B 1 45  ? 64.994 -22.232 15.248  1.00 99.32  ?  45  SER B CB  1 
ATOM   2342 O OG  . SER B 1 45  ? 65.445 -22.668 16.520  1.00 107.39 ?  45  SER B OG  1 
ATOM   2343 N N   . PRO B 1 46  ? 66.147 -19.812 17.157  1.00 101.72 ?  46  PRO B N   1 
ATOM   2344 C CA  . PRO B 1 46  ? 67.285 -19.281 17.929  1.00 100.54 ?  46  PRO B CA  1 
ATOM   2345 C C   . PRO B 1 46  ? 68.405 -20.286 18.096  1.00 107.36 ?  46  PRO B C   1 
ATOM   2346 O O   . PRO B 1 46  ? 69.508 -19.901 18.505  1.00 112.28 ?  46  PRO B O   1 
ATOM   2347 C CB  . PRO B 1 46  ? 66.655 -18.913 19.280  1.00 94.69  ?  46  PRO B CB  1 
ATOM   2348 C CG  . PRO B 1 46  ? 65.181 -18.794 18.996  1.00 96.75  ?  46  PRO B CG  1 
ATOM   2349 C CD  . PRO B 1 46  ? 64.918 -19.849 17.964  1.00 100.60 ?  46  PRO B CD  1 
ATOM   2350 N N   . ASP B 1 47  ? 68.172 -21.553 17.761  1.00 108.47 ?  47  ASP B N   1 
ATOM   2351 C CA  . ASP B 1 47  ? 69.196 -22.578 17.847  1.00 111.53 ?  47  ASP B CA  1 
ATOM   2352 C C   . ASP B 1 47  ? 69.811 -22.930 16.496  1.00 109.76 ?  47  ASP B C   1 
ATOM   2353 O O   . ASP B 1 47  ? 70.758 -23.729 16.454  1.00 108.42 ?  47  ASP B O   1 
ATOM   2354 C CB  . ASP B 1 47  ? 68.620 -23.833 18.509  1.00 115.84 ?  47  ASP B CB  1 
ATOM   2355 C CG  . ASP B 1 47  ? 69.662 -24.586 19.308  1.00 128.22 ?  47  ASP B CG  1 
ATOM   2356 O OD1 . ASP B 1 47  ? 70.315 -23.954 20.173  1.00 129.38 ?  47  ASP B OD1 1 
ATOM   2357 O OD2 . ASP B 1 47  ? 69.826 -25.802 19.074  1.00 137.72 -1 47  ASP B OD2 1 
ATOM   2358 N N   . SER B 1 48  ? 69.302 -22.359 15.400  1.00 106.15 ?  48  SER B N   1 
ATOM   2359 C CA  . SER B 1 48  ? 69.956 -22.500 14.103  1.00 100.20 ?  48  SER B CA  1 
ATOM   2360 C C   . SER B 1 48  ? 71.385 -21.977 14.179  1.00 102.55 ?  48  SER B C   1 
ATOM   2361 O O   . SER B 1 48  ? 71.664 -20.969 14.836  1.00 112.66 ?  48  SER B O   1 
ATOM   2362 C CB  . SER B 1 48  ? 69.177 -21.744 13.022  1.00 91.94  ?  48  SER B CB  1 
ATOM   2363 O OG  . SER B 1 48  ? 69.912 -21.676 11.807  1.00 83.52  ?  48  SER B OG  1 
ATOM   2364 N N   . GLN B 1 49  ? 72.301 -22.668 13.511  1.00 89.58  ?  49  GLN B N   1 
ATOM   2365 C CA  . GLN B 1 49  ? 73.689 -22.239 13.535  1.00 91.55  ?  49  GLN B CA  1 
ATOM   2366 C C   . GLN B 1 49  ? 74.205 -22.047 12.123  1.00 90.60  ?  49  GLN B C   1 
ATOM   2367 O O   . GLN B 1 49  ? 75.312 -22.456 11.762  1.00 87.64  ?  49  GLN B O   1 
ATOM   2368 C CB  . GLN B 1 49  ? 74.522 -23.206 14.358  1.00 105.02 ?  49  GLN B CB  1 
ATOM   2369 C CG  . GLN B 1 49  ? 74.039 -23.252 15.798  1.00 116.79 ?  49  GLN B CG  1 
ATOM   2370 C CD  . GLN B 1 49  ? 74.591 -24.421 16.567  1.00 128.13 ?  49  GLN B CD  1 
ATOM   2371 O OE1 . GLN B 1 49  ? 74.503 -25.568 16.124  1.00 133.43 ?  49  GLN B OE1 1 
ATOM   2372 N NE2 . GLN B 1 49  ? 75.148 -24.141 17.746  1.00 132.17 ?  49  GLN B NE2 1 
ATOM   2373 N N   . VAL B 1 50  ? 73.377 -21.394 11.313  1.00 88.94  ?  50  VAL B N   1 
ATOM   2374 C CA  . VAL B 1 50  ? 73.833 -20.795 10.057  1.00 85.41  ?  50  VAL B CA  1 
ATOM   2375 C C   . VAL B 1 50  ? 74.896 -19.748 10.373  1.00 82.58  ?  50  VAL B C   1 
ATOM   2376 O O   . VAL B 1 50  ? 74.731 -18.980 11.344  1.00 79.19  ?  50  VAL B O   1 
ATOM   2377 C CB  . VAL B 1 50  ? 72.640 -20.168 9.315   1.00 83.60  ?  50  VAL B CB  1 
ATOM   2378 C CG1 . VAL B 1 50  ? 73.090 -19.542 8.021   1.00 82.55  ?  50  VAL B CG1 1 
ATOM   2379 C CG2 . VAL B 1 50  ? 71.506 -21.203 9.086   1.00 73.97  ?  50  VAL B CG2 1 
ATOM   2380 N N   . PRO B 1 51  ? 76.004 -19.661 9.631   1.00 81.40  ?  51  PRO B N   1 
ATOM   2381 C CA  . PRO B 1 51  ? 76.978 -18.595 9.901   1.00 76.95  ?  51  PRO B CA  1 
ATOM   2382 C C   . PRO B 1 51  ? 76.324 -17.243 9.714   1.00 78.80  ?  51  PRO B C   1 
ATOM   2383 O O   . PRO B 1 51  ? 75.264 -17.119 9.100   1.00 84.17  ?  51  PRO B O   1 
ATOM   2384 C CB  . PRO B 1 51  ? 78.082 -18.822 8.862   1.00 69.46  ?  51  PRO B CB  1 
ATOM   2385 C CG  . PRO B 1 51  ? 77.915 -20.240 8.443   1.00 77.67  ?  51  PRO B CG  1 
ATOM   2386 C CD  . PRO B 1 51  ? 76.426 -20.510 8.508   1.00 80.36  ?  51  PRO B CD  1 
ATOM   2387 N N   . LEU B 1 52  ? 76.966 -16.220 10.267  1.00 74.49  ?  52  LEU B N   1 
ATOM   2388 C CA  . LEU B 1 52  ? 76.401 -14.882 10.178  1.00 64.91  ?  52  LEU B CA  1 
ATOM   2389 C C   . LEU B 1 52  ? 76.223 -14.444 8.727   1.00 74.12  ?  52  LEU B C   1 
ATOM   2390 O O   . LEU B 1 52  ? 75.186 -13.871 8.359   1.00 74.91  ?  52  LEU B O   1 
ATOM   2391 C CB  . LEU B 1 52  ? 77.288 -13.894 10.915  1.00 59.33  ?  52  LEU B CB  1 
ATOM   2392 C CG  . LEU B 1 52  ? 76.764 -12.506 10.627  1.00 59.08  ?  52  LEU B CG  1 
ATOM   2393 C CD1 . LEU B 1 52  ? 75.392 -12.384 11.269  1.00 60.69  ?  52  LEU B CD1 1 
ATOM   2394 C CD2 . LEU B 1 52  ? 77.734 -11.483 11.154  1.00 58.09  ?  52  LEU B CD2 1 
ATOM   2395 N N   . ALA B 1 53  ? 77.229 -14.693 7.890   1.00 73.48  ?  53  ALA B N   1 
ATOM   2396 C CA  . ALA B 1 53  ? 77.187 -14.178 6.528   1.00 69.75  ?  53  ALA B CA  1 
ATOM   2397 C C   . ALA B 1 53  ? 75.922 -14.632 5.814   1.00 73.65  ?  53  ALA B C   1 
ATOM   2398 O O   . ALA B 1 53  ? 75.255 -13.837 5.136   1.00 75.39  ?  53  ALA B O   1 
ATOM   2399 C CB  . ALA B 1 53  ? 78.437 -14.620 5.761   1.00 55.09  ?  53  ALA B CB  1 
ATOM   2400 N N   . GLU B 1 54  ? 75.550 -15.897 5.993   1.00 66.53  ?  54  GLU B N   1 
ATOM   2401 C CA  . GLU B 1 54  ? 74.401 -16.434 5.284   1.00 59.33  ?  54  GLU B CA  1 
ATOM   2402 C C   . GLU B 1 54  ? 73.088 -15.932 5.879   1.00 64.75  ?  54  GLU B C   1 
ATOM   2403 O O   . GLU B 1 54  ? 72.093 -15.791 5.156   1.00 68.94  ?  54  GLU B O   1 
ATOM   2404 C CB  . GLU B 1 54  ? 74.485 -17.957 5.291   1.00 67.76  ?  54  GLU B CB  1 
ATOM   2405 C CG  . GLU B 1 54  ? 73.372 -18.668 4.574   1.00 74.65  ?  54  GLU B CG  1 
ATOM   2406 C CD  . GLU B 1 54  ? 73.521 -20.177 4.647   1.00 87.51  ?  54  GLU B CD  1 
ATOM   2407 O OE1 . GLU B 1 54  ? 74.658 -20.667 4.904   1.00 92.08  ?  54  GLU B OE1 1 
ATOM   2408 O OE2 . GLU B 1 54  ? 72.482 -20.863 4.483   1.00 84.75  -1 54  GLU B OE2 1 
ATOM   2409 N N   . ALA B 1 55  ? 73.073 -15.601 7.168   1.00 64.56  ?  55  ALA B N   1 
ATOM   2410 C CA  . ALA B 1 55  ? 71.866 -15.035 7.751   1.00 65.69  ?  55  ALA B CA  1 
ATOM   2411 C C   . ALA B 1 55  ? 71.690 -13.561 7.400   1.00 69.04  ?  55  ALA B C   1 
ATOM   2412 O O   . ALA B 1 55  ? 70.553 -13.084 7.324   1.00 62.81  ?  55  ALA B O   1 
ATOM   2413 C CB  . ALA B 1 55  ? 71.884 -15.219 9.267   1.00 64.42  ?  55  ALA B CB  1 
ATOM   2414 N N   . THR B 1 56  ? 72.789 -12.820 7.223   1.00 68.59  ?  56  THR B N   1 
ATOM   2415 C CA  . THR B 1 56  ? 72.682 -11.446 6.743   1.00 65.24  ?  56  THR B CA  1 
ATOM   2416 C C   . THR B 1 56  ? 72.052 -11.401 5.356   1.00 60.73  ?  56  THR B C   1 
ATOM   2417 O O   . THR B 1 56  ? 71.075 -10.679 5.137   1.00 53.78  ?  56  THR B O   1 
ATOM   2418 C CB  . THR B 1 56  ? 74.053 -10.764 6.774   1.00 66.85  ?  56  THR B CB  1 
ATOM   2419 O OG1 . THR B 1 56  ? 74.978 -11.469 5.955   1.00 66.11  ?  56  THR B OG1 1 
ATOM   2420 C CG2 . THR B 1 56  ? 74.578 -10.702 8.192   1.00 73.47  ?  56  THR B CG2 1 
ATOM   2421 N N   . ASP B 1 57  ? 72.578 -12.190 4.410   1.00 62.18  ?  57  ASP B N   1 
ATOM   2422 C CA  . ASP B 1 57  ? 71.951 -12.243 3.093   1.00 62.13  ?  57  ASP B CA  1 
ATOM   2423 C C   . ASP B 1 57  ? 70.527 -12.768 3.169   1.00 56.58  ?  57  ASP B C   1 
ATOM   2424 O O   . ASP B 1 57  ? 69.709 -12.467 2.289   1.00 61.58  ?  57  ASP B O   1 
ATOM   2425 C CB  . ASP B 1 57  ? 72.736 -13.118 2.120   1.00 60.99  ?  57  ASP B CB  1 
ATOM   2426 C CG  . ASP B 1 57  ? 74.051 -12.516 1.728   1.00 69.56  ?  57  ASP B CG  1 
ATOM   2427 O OD1 . ASP B 1 57  ? 74.234 -11.284 1.891   1.00 73.57  ?  57  ASP B OD1 1 
ATOM   2428 O OD2 . ASP B 1 57  ? 74.901 -13.292 1.245   1.00 68.21  -1 57  ASP B OD2 1 
ATOM   2429 N N   . ARG B 1 58  ? 70.206 -13.568 4.181   1.00 45.64  ?  58  ARG B N   1 
ATOM   2430 C CA  . ARG B 1 58  ? 68.830 -14.035 4.242   1.00 52.39  ?  58  ARG B CA  1 
ATOM   2431 C C   . ARG B 1 58  ? 67.876 -12.885 4.509   1.00 53.96  ?  58  ARG B C   1 
ATOM   2432 O O   . ARG B 1 58  ? 66.792 -12.823 3.906   1.00 54.87  ?  58  ARG B O   1 
ATOM   2433 C CB  . ARG B 1 58  ? 68.635 -15.132 5.285   1.00 48.86  ?  58  ARG B CB  1 
ATOM   2434 C CG  . ARG B 1 58  ? 67.206 -15.576 5.173   1.00 55.31  ?  58  ARG B CG  1 
ATOM   2435 C CD  . ARG B 1 58  ? 66.914 -16.867 5.751   1.00 71.47  ?  58  ARG B CD  1 
ATOM   2436 N NE  . ARG B 1 58  ? 65.471 -17.036 5.804   1.00 85.09  ?  58  ARG B NE  1 
ATOM   2437 C CZ  . ARG B 1 58  ? 64.889 -17.876 6.646   1.00 88.45  ?  58  ARG B CZ  1 
ATOM   2438 N NH1 . ARG B 1 58  ? 65.653 -18.563 7.475   1.00 86.04  ?  58  ARG B NH1 1 
ATOM   2439 N NH2 . ARG B 1 58  ? 63.571 -18.017 6.678   1.00 86.46  ?  58  ARG B NH2 1 
ATOM   2440 N N   . LEU B 1 59  ? 68.267 -11.958 5.399   1.00 49.57  ?  59  LEU B N   1 
ATOM   2441 C CA  . LEU B 1 59  ? 67.470 -10.757 5.625   1.00 54.91  ?  59  LEU B CA  1 
ATOM   2442 C C   . LEU B 1 59  ? 67.351 -9.933  4.340   1.00 57.73  ?  59  LEU B C   1 
ATOM   2443 O O   . LEU B 1 59  ? 66.248 -9.482  3.973   1.00 47.96  ?  59  LEU B O   1 
ATOM   2444 C CB  . LEU B 1 59  ? 68.061 -9.924  6.756   1.00 43.78  ?  59  LEU B CB  1 
ATOM   2445 C CG  . LEU B 1 59  ? 67.142 -8.735  7.027   1.00 51.11  ?  59  LEU B CG  1 
ATOM   2446 C CD1 . LEU B 1 59  ? 65.770 -9.252  7.436   1.00 50.07  ?  59  LEU B CD1 1 
ATOM   2447 C CD2 . LEU B 1 59  ? 67.706 -7.773  8.063   1.00 45.66  ?  59  LEU B CD2 1 
ATOM   2448 N N   . THR B 1 60  ? 68.473 -9.752  3.632   1.00 39.74  ?  60  THR B N   1 
ATOM   2449 C CA  . THR B 1 60  ? 68.410 -9.129  2.319   1.00 45.60  ?  60  THR B CA  1 
ATOM   2450 C C   . THR B 1 60  ? 67.373 -9.811  1.438   1.00 52.68  ?  60  THR B C   1 
ATOM   2451 O O   . THR B 1 60  ? 66.489 -9.150  0.872   1.00 49.90  ?  60  THR B O   1 
ATOM   2452 C CB  . THR B 1 60  ? 69.759 -9.165  1.624   1.00 51.75  ?  60  THR B CB  1 
ATOM   2453 O OG1 . THR B 1 60  ? 70.750 -8.508  2.425   1.00 57.73  ?  60  THR B OG1 1 
ATOM   2454 C CG2 . THR B 1 60  ? 69.623 -8.494  0.256   1.00 52.37  ?  60  THR B CG2 1 
ATOM   2455 N N   . ASP B 1 61  ? 67.458 -11.142 1.317   1.00 46.84  ?  61  ASP B N   1 
ATOM   2456 C CA  . ASP B 1 61  ? 66.578 -11.840 0.373   1.00 43.73  ?  61  ASP B CA  1 
ATOM   2457 C C   . ASP B 1 61  ? 65.123 -11.719 0.801   1.00 45.93  ?  61  ASP B C   1 
ATOM   2458 O O   . ASP B 1 61  ? 64.240 -11.447 -0.018  1.00 47.31  ?  61  ASP B O   1 
ATOM   2459 C CB  . ASP B 1 61  ? 66.969 -13.317 0.226   1.00 32.11  ?  61  ASP B CB  1 
ATOM   2460 C CG  . ASP B 1 61  ? 68.289 -13.518 -0.516  1.00 41.71  ?  61  ASP B CG  1 
ATOM   2461 O OD1 . ASP B 1 61  ? 68.904 -12.541 -1.002  1.00 47.94  ?  61  ASP B OD1 1 
ATOM   2462 O OD2 . ASP B 1 61  ? 68.720 -14.676 -0.629  1.00 55.47  -1 61  ASP B OD2 1 
ATOM   2463 N N   . MET B 1 62  ? 64.867 -11.899 2.091   1.00 51.07  ?  62  MET B N   1 
ATOM   2464 C CA  . MET B 1 62  ? 63.546 -11.676 2.652   1.00 44.85  ?  62  MET B CA  1 
ATOM   2465 C C   . MET B 1 62  ? 62.995 -10.326 2.227   1.00 51.54  ?  62  MET B C   1 
ATOM   2466 O O   . MET B 1 62  ? 61.849 -10.224 1.789   1.00 55.12  ?  62  MET B O   1 
ATOM   2467 C CB  . MET B 1 62  ? 63.672 -11.771 4.153   1.00 52.01  ?  62  MET B CB  1 
ATOM   2468 C CG  . MET B 1 62  ? 62.431 -11.921 4.932   1.00 68.54  ?  62  MET B CG  1 
ATOM   2469 S SD  . MET B 1 62  ? 63.130 -12.416 6.520   1.00 72.75  ?  62  MET B SD  1 
ATOM   2470 C CE  . MET B 1 62  ? 64.110 -13.800 5.928   1.00 71.69  ?  62  MET B CE  1 
ATOM   2471 N N   . MET B 1 63  ? 63.819 -9.275  2.311   1.00 43.47  ?  63  MET B N   1 
ATOM   2472 C CA  . MET B 1 63  ? 63.317 -7.947  1.976   1.00 48.38  ?  63  MET B CA  1 
ATOM   2473 C C   . MET B 1 63  ? 63.234 -7.738  0.470   1.00 53.14  ?  63  MET B C   1 
ATOM   2474 O O   . MET B 1 63  ? 62.326 -7.054  -0.018  1.00 54.64  ?  63  MET B O   1 
ATOM   2475 C CB  . MET B 1 63  ? 64.182 -6.866  2.611   1.00 47.54  ?  63  MET B CB  1 
ATOM   2476 C CG  . MET B 1 63  ? 64.117 -6.797  4.120   1.00 48.10  ?  63  MET B CG  1 
ATOM   2477 S SD  . MET B 1 63  ? 65.480 -5.801  4.775   1.00 57.61  ?  63  MET B SD  1 
ATOM   2478 C CE  . MET B 1 63  ? 64.819 -4.117  4.610   1.00 33.36  ?  63  MET B CE  1 
ATOM   2479 N N   . ALA B 1 64  ? 64.174 -8.287  -0.291  1.00 53.40  ?  64  ALA B N   1 
ATOM   2480 C CA  . ALA B 1 64  ? 64.076 -8.103  -1.735  1.00 51.72  ?  64  ALA B CA  1 
ATOM   2481 C C   . ALA B 1 64  ? 62.793 -8.720  -2.286  1.00 45.27  ?  64  ALA B C   1 
ATOM   2482 O O   . ALA B 1 64  ? 62.135 -8.131  -3.150  1.00 46.66  ?  64  ALA B O   1 
ATOM   2483 C CB  . ALA B 1 64  ? 65.295 -8.674  -2.433  1.00 38.48  ?  64  ALA B CB  1 
ATOM   2484 N N   . GLU B 1 65  ? 62.384 -9.873  -1.768  1.00 37.88  ?  65  GLU B N   1 
ATOM   2485 C CA  . GLU B 1 65  ? 61.144 -10.438 -2.280  1.00 42.09  ?  65  GLU B CA  1 
ATOM   2486 C C   . GLU B 1 65  ? 59.964 -9.519  -2.021  1.00 43.95  ?  65  GLU B C   1 
ATOM   2487 O O   . GLU B 1 65  ? 59.023 -9.500  -2.812  1.00 49.44  ?  65  GLU B O   1 
ATOM   2488 C CB  . GLU B 1 65  ? 60.875 -11.821 -1.697  1.00 48.46  ?  65  GLU B CB  1 
ATOM   2489 C CG  . GLU B 1 65  ? 59.965 -11.805 -0.498  1.00 74.99  ?  65  GLU B CG  1 
ATOM   2490 C CD  . GLU B 1 65  ? 59.274 -13.133 -0.248  1.00 89.69  ?  65  GLU B CD  1 
ATOM   2491 O OE1 . GLU B 1 65  ? 59.689 -14.148 -0.846  1.00 88.98  ?  65  GLU B OE1 1 
ATOM   2492 O OE2 . GLU B 1 65  ? 58.319 -13.156 0.569   1.00 100.23 -1 65  GLU B OE2 1 
ATOM   2493 N N   . ARG B 1 66  ? 60.004 -8.701  -0.966  1.00 42.40  ?  66  ARG B N   1 
ATOM   2494 C CA  . ARG B 1 66  ? 58.850 -7.837  -0.747  1.00 38.77  ?  66  ARG B CA  1 
ATOM   2495 C C   . ARG B 1 66  ? 58.792 -6.679  -1.725  1.00 42.90  ?  66  ARG B C   1 
ATOM   2496 O O   . ARG B 1 66  ? 57.707 -6.132  -1.938  1.00 52.27  ?  66  ARG B O   1 
ATOM   2497 C CB  . ARG B 1 66  ? 58.821 -7.345  0.683   1.00 42.52  ?  66  ARG B CB  1 
ATOM   2498 C CG  . ARG B 1 66  ? 58.240 -8.400  1.613   1.00 42.12  ?  66  ARG B CG  1 
ATOM   2499 C CD  . ARG B 1 66  ? 58.740 -8.252  3.012   1.00 38.64  ?  66  ARG B CD  1 
ATOM   2500 N NE  . ARG B 1 66  ? 57.958 -9.063  3.941   1.00 49.06  ?  66  ARG B NE  1 
ATOM   2501 C CZ  . ARG B 1 66  ? 58.330 -10.254 4.415   1.00 48.80  ?  66  ARG B CZ  1 
ATOM   2502 N NH1 . ARG B 1 66  ? 59.481 -10.797 4.058   1.00 54.15  ?  66  ARG B NH1 1 
ATOM   2503 N NH2 . ARG B 1 66  ? 57.562 -10.898 5.277   1.00 42.77  ?  66  ARG B NH2 1 
ATOM   2504 N N   . LEU B 1 67  ? 59.914 -6.332  -2.362  1.00 40.27  ?  67  LEU B N   1 
ATOM   2505 C CA  . LEU B 1 67  ? 59.908 -5.301  -3.399  1.00 39.09  ?  67  LEU B CA  1 
ATOM   2506 C C   . LEU B 1 67  ? 59.074 -5.686  -4.617  1.00 41.22  ?  67  LEU B C   1 
ATOM   2507 O O   . LEU B 1 67  ? 58.604 -4.800  -5.337  1.00 47.37  ?  67  LEU B O   1 
ATOM   2508 C CB  . LEU B 1 67  ? 61.337 -5.015  -3.851  1.00 44.84  ?  67  LEU B CB  1 
ATOM   2509 C CG  . LEU B 1 67  ? 62.257 -4.597  -2.711  1.00 48.37  ?  67  LEU B CG  1 
ATOM   2510 C CD1 . LEU B 1 67  ? 63.741 -4.760  -3.096  1.00 49.34  ?  67  LEU B CD1 1 
ATOM   2511 C CD2 . LEU B 1 67  ? 61.912 -3.171  -2.386  1.00 38.97  ?  67  LEU B CD2 1 
ATOM   2512 N N   . ARG B 1 68  ? 58.919 -6.987  -4.895  1.00 42.30  ?  68  ARG B N   1 
ATOM   2513 C CA  . ARG B 1 68  ? 58.194 -7.479  -6.077  1.00 40.85  ?  68  ARG B CA  1 
ATOM   2514 C C   . ARG B 1 68  ? 58.774 -6.918  -7.370  1.00 45.67  ?  68  ARG B C   1 
ATOM   2515 O O   . ARG B 1 68  ? 58.109 -6.190  -8.104  1.00 52.87  ?  68  ARG B O   1 
ATOM   2516 C CB  . ARG B 1 68  ? 56.700 -7.165  -5.996  1.00 42.89  ?  68  ARG B CB  1 
ATOM   2517 C CG  . ARG B 1 68  ? 56.070 -7.671  -4.725  1.00 52.09  ?  68  ARG B CG  1 
ATOM   2518 C CD  . ARG B 1 68  ? 54.579 -7.504  -4.734  1.00 58.03  ?  68  ARG B CD  1 
ATOM   2519 N NE  . ARG B 1 68  ? 54.044 -7.941  -3.449  1.00 79.84  ?  68  ARG B NE  1 
ATOM   2520 C CZ  . ARG B 1 68  ? 52.909 -8.621  -3.301  1.00 89.35  ?  68  ARG B CZ  1 
ATOM   2521 N NH1 . ARG B 1 68  ? 52.197 -8.953  -4.377  1.00 81.02  ?  68  ARG B NH1 1 
ATOM   2522 N NH2 . ARG B 1 68  ? 52.505 -8.998  -2.081  1.00 91.83  ?  68  ARG B NH2 1 
ATOM   2523 N N   . ILE B 1 69  ? 60.023 -7.288  -7.644  1.00 46.04  ?  69  ILE B N   1 
ATOM   2524 C CA  . ILE B 1 69  ? 60.793 -6.751  -8.755  1.00 49.26  ?  69  ILE B CA  1 
ATOM   2525 C C   . ILE B 1 69  ? 61.349 -7.888  -9.611  1.00 56.42  ?  69  ILE B C   1 
ATOM   2526 O O   . ILE B 1 69  ? 61.308 -9.064  -9.246  1.00 56.34  ?  69  ILE B O   1 
ATOM   2527 C CB  . ILE B 1 69  ? 61.947 -5.847  -8.276  1.00 46.84  ?  69  ILE B CB  1 
ATOM   2528 C CG1 . ILE B 1 69  ? 62.837 -6.622  -7.299  1.00 48.78  ?  69  ILE B CG1 1 
ATOM   2529 C CG2 . ILE B 1 69  ? 61.366 -4.613  -7.636  1.00 43.11  ?  69  ILE B CG2 1 
ATOM   2530 C CD1 . ILE B 1 69  ? 64.237 -6.178  -7.236  1.00 42.73  ?  69  ILE B CD1 1 
ATOM   2531 N N   . GLY B 1 70  ? 61.893 -7.511  -10.761 1.00 57.70  ?  70  GLY B N   1 
ATOM   2532 C CA  . GLY B 1 70  ? 62.427 -8.487  -11.683 1.00 46.94  ?  70  GLY B CA  1 
ATOM   2533 C C   . GLY B 1 70  ? 63.433 -7.813  -12.578 1.00 50.96  ?  70  GLY B C   1 
ATOM   2534 O O   . GLY B 1 70  ? 63.783 -6.665  -12.328 1.00 51.56  ?  70  GLY B O   1 
ATOM   2535 N N   . ALA B 1 71  ? 63.900 -8.488  -13.619 1.00 49.22  ?  71  ALA B N   1 
ATOM   2536 C CA  . ALA B 1 71  ? 64.825 -7.854  -14.541 1.00 47.77  ?  71  ALA B CA  1 
ATOM   2537 C C   . ALA B 1 71  ? 64.172 -6.625  -15.166 1.00 46.97  ?  71  ALA B C   1 
ATOM   2538 O O   . ALA B 1 71  ? 62.977 -6.621  -15.460 1.00 49.35  ?  71  ALA B O   1 
ATOM   2539 C CB  . ALA B 1 71  ? 65.256 -8.865  -15.598 1.00 41.60  ?  71  ALA B CB  1 
ATOM   2540 N N   . GLY B 1 72  ? 64.941 -5.546  -15.294 1.00 53.46  ?  72  GLY B N   1 
ATOM   2541 C CA  . GLY B 1 72  ? 64.406 -4.282  -15.775 1.00 64.31  ?  72  GLY B CA  1 
ATOM   2542 C C   . GLY B 1 72  ? 63.691 -3.424  -14.740 1.00 67.24  ?  72  GLY B C   1 
ATOM   2543 O O   . GLY B 1 72  ? 63.389 -2.249  -15.027 1.00 71.40  ?  72  GLY B O   1 
ATOM   2544 N N   . SER B 1 73  ? 63.382 -3.968  -13.564 1.00 53.41  ?  73  SER B N   1 
ATOM   2545 C CA  . SER B 1 73  ? 62.867 -3.162  -12.469 1.00 49.59  ?  73  SER B CA  1 
ATOM   2546 C C   . SER B 1 73  ? 63.928 -2.157  -12.044 1.00 54.94  ?  73  SER B C   1 
ATOM   2547 O O   . SER B 1 73  ? 65.123 -2.457  -12.050 1.00 55.76  ?  73  SER B O   1 
ATOM   2548 C CB  . SER B 1 73  ? 62.512 -4.048  -11.288 1.00 50.26  ?  73  SER B CB  1 
ATOM   2549 O OG  . SER B 1 73  ? 61.221 -4.613  -11.414 1.00 46.91  ?  73  SER B OG  1 
ATOM   2550 N N   . ARG B 1 74  ? 63.487 -0.947  -11.674 1.00 56.94  ?  74  ARG B N   1 
ATOM   2551 C CA  . ARG B 1 74  ? 64.380 0.099   -11.152 1.00 48.95  ?  74  ARG B CA  1 
ATOM   2552 C C   . ARG B 1 74  ? 64.245 0.171   -9.632  1.00 51.32  ?  74  ARG B C   1 
ATOM   2553 O O   . ARG B 1 74  ? 63.214 0.625   -9.123  1.00 64.25  ?  74  ARG B O   1 
ATOM   2554 C CB  . ARG B 1 74  ? 64.047 1.466   -11.735 1.00 47.84  ?  74  ARG B CB  1 
ATOM   2555 C CG  . ARG B 1 74  ? 63.815 1.571   -13.229 1.00 48.50  ?  74  ARG B CG  1 
ATOM   2556 C CD  . ARG B 1 74  ? 65.088 1.459   -14.022 1.00 46.37  ?  74  ARG B CD  1 
ATOM   2557 N NE  . ARG B 1 74  ? 66.050 2.539   -13.841 1.00 46.48  ?  74  ARG B NE  1 
ATOM   2558 C CZ  . ARG B 1 74  ? 67.305 2.473   -14.274 1.00 47.57  ?  74  ARG B CZ  1 
ATOM   2559 N NH1 . ARG B 1 74  ? 67.726 1.381   -14.892 1.00 55.04  ?  74  ARG B NH1 1 
ATOM   2560 N NH2 . ARG B 1 74  ? 68.142 3.478   -14.101 1.00 44.03  ?  74  ARG B NH2 1 
ATOM   2561 N N   . VAL B 1 75  ? 65.286 -0.205  -8.901  1.00 45.39  ?  75  VAL B N   1 
ATOM   2562 C CA  . VAL B 1 75  ? 65.257 -0.198  -7.438  1.00 45.30  ?  75  VAL B CA  1 
ATOM   2563 C C   . VAL B 1 75  ? 66.166 0.914   -6.920  1.00 41.41  ?  75  VAL B C   1 
ATOM   2564 O O   . VAL B 1 75  ? 67.304 1.049   -7.377  1.00 49.92  ?  75  VAL B O   1 
ATOM   2565 C CB  . VAL B 1 75  ? 65.680 -1.566  -6.863  1.00 44.36  ?  75  VAL B CB  1 
ATOM   2566 C CG1 . VAL B 1 75  ? 65.889 -1.481  -5.367  1.00 36.62  ?  75  VAL B CG1 1 
ATOM   2567 C CG2 . VAL B 1 75  ? 64.618 -2.608  -7.150  1.00 40.91  ?  75  VAL B CG2 1 
ATOM   2568 N N   . LEU B 1 76  ? 65.677 1.695   -5.950  1.00 41.76  ?  76  LEU B N   1 
ATOM   2569 C CA  . LEU B 1 76  ? 66.502 2.671   -5.225  1.00 43.94  ?  76  LEU B CA  1 
ATOM   2570 C C   . LEU B 1 76  ? 66.976 2.061   -3.906  1.00 47.02  ?  76  LEU B C   1 
ATOM   2571 O O   . LEU B 1 76  ? 66.158 1.612   -3.097  1.00 53.12  ?  76  LEU B O   1 
ATOM   2572 C CB  . LEU B 1 76  ? 65.718 3.960   -4.962  1.00 51.20  ?  76  LEU B CB  1 
ATOM   2573 C CG  . LEU B 1 76  ? 66.389 4.964   -4.011  1.00 52.84  ?  76  LEU B CG  1 
ATOM   2574 C CD1 . LEU B 1 76  ? 67.744 5.426   -4.570  1.00 46.44  ?  76  LEU B CD1 1 
ATOM   2575 C CD2 . LEU B 1 76  ? 65.489 6.180   -3.724  1.00 48.62  ?  76  LEU B CD2 1 
ATOM   2576 N N   . ASP B 1 77  ? 68.282 2.042   -3.694  1.00 45.04  ?  77  ASP B N   1 
ATOM   2577 C CA  . ASP B 1 77  ? 68.907 1.452   -2.502  1.00 43.50  ?  77  ASP B CA  1 
ATOM   2578 C C   . ASP B 1 77  ? 69.248 2.585   -1.527  1.00 44.81  ?  77  ASP B C   1 
ATOM   2579 O O   . ASP B 1 77  ? 70.306 3.201   -1.622  1.00 50.37  ?  77  ASP B O   1 
ATOM   2580 C CB  . ASP B 1 77  ? 70.137 0.674   -2.957  1.00 50.22  ?  77  ASP B CB  1 
ATOM   2581 C CG  . ASP B 1 77  ? 70.946 0.059   -1.817  1.00 56.97  ?  77  ASP B CG  1 
ATOM   2582 O OD1 . ASP B 1 77  ? 70.550 0.147   -0.622  1.00 60.78  ?  77  ASP B OD1 1 
ATOM   2583 O OD2 . ASP B 1 77  ? 72.025 -0.513  -2.148  1.00 66.09  -1 77  ASP B OD2 1 
ATOM   2584 N N   . LEU B 1 78  ? 68.331 2.881   -0.599  1.00 44.25  ?  78  LEU B N   1 
ATOM   2585 C CA  . LEU B 1 78  ? 68.430 4.058   0.286   1.00 47.91  ?  78  LEU B CA  1 
ATOM   2586 C C   . LEU B 1 78  ? 69.343 3.753   1.466   1.00 52.94  ?  78  LEU B C   1 
ATOM   2587 O O   . LEU B 1 78  ? 68.922 3.169   2.459   1.00 62.22  ?  78  LEU B O   1 
ATOM   2588 C CB  . LEU B 1 78  ? 67.056 4.457   0.797   1.00 53.62  ?  78  LEU B CB  1 
ATOM   2589 C CG  . LEU B 1 78  ? 66.593 5.889   1.088   1.00 55.15  ?  78  LEU B CG  1 
ATOM   2590 C CD1 . LEU B 1 78  ? 66.319 6.710   -0.186  1.00 52.79  ?  78  LEU B CD1 1 
ATOM   2591 C CD2 . LEU B 1 78  ? 65.328 5.817   1.887   1.00 45.16  ?  78  LEU B CD2 1 
ATOM   2592 N N   . GLY B 1 79  ? 70.613 4.119   1.355   1.00 42.68  ?  79  GLY B N   1 
ATOM   2593 C CA  . GLY B 1 79  ? 71.537 3.871   2.428   1.00 41.61  ?  79  GLY B CA  1 
ATOM   2594 C C   . GLY B 1 79  ? 72.122 2.534   2.069   1.00 56.38  ?  79  GLY B C   1 
ATOM   2595 O O   . GLY B 1 79  ? 71.540 1.498   2.387   1.00 65.27  ?  79  GLY B O   1 
ATOM   2596 N N   . CYS B 1 80  ? 73.267 2.527   1.415   1.00 49.56  ?  80  CYS B N   1 
ATOM   2597 C CA  . CYS B 1 80  ? 73.687 1.351   0.688   1.00 44.80  ?  80  CYS B CA  1 
ATOM   2598 C C   . CYS B 1 80  ? 74.877 0.684   1.303   1.00 41.72  ?  80  CYS B C   1 
ATOM   2599 O O   . CYS B 1 80  ? 75.396 -0.266  0.706   1.00 47.80  ?  80  CYS B O   1 
ATOM   2600 C CB  . CYS B 1 80  ? 74.076 1.720   -0.744  1.00 61.34  ?  80  CYS B CB  1 
ATOM   2601 S SG  . CYS B 1 80  ? 75.699 2.620   -0.782  1.00 69.27  ?  80  CYS B SG  1 
ATOM   2602 N N   . GLY B 1 81  ? 75.384 1.220   2.403   1.00 51.36  ?  81  GLY B N   1 
ATOM   2603 C CA  . GLY B 1 81  ? 76.555 0.644   3.012   1.00 51.50  ?  81  GLY B CA  1 
ATOM   2604 C C   . GLY B 1 81  ? 77.691 0.539   2.025   1.00 53.95  ?  81  GLY B C   1 
ATOM   2605 O O   . GLY B 1 81  ? 77.890 1.411   1.165   1.00 50.15  ?  81  GLY B O   1 
ATOM   2606 N N   . VAL B 1 82  ? 78.445 -0.553  2.140   1.00 55.63  ?  82  VAL B N   1 
ATOM   2607 C CA  . VAL B 1 82  ? 79.541 -0.816  1.222   1.00 59.95  ?  82  VAL B CA  1 
ATOM   2608 C C   . VAL B 1 82  ? 79.034 -1.652  0.058   1.00 59.08  ?  82  VAL B C   1 
ATOM   2609 O O   . VAL B 1 82  ? 79.824 -2.227  -0.701  1.00 65.07  ?  82  VAL B O   1 
ATOM   2610 C CB  . VAL B 1 82  ? 80.724 -1.494  1.931   1.00 63.46  ?  82  VAL B CB  1 
ATOM   2611 C CG1 . VAL B 1 82  ? 81.172 -0.657  3.099   1.00 60.51  ?  82  VAL B CG1 1 
ATOM   2612 C CG2 . VAL B 1 82  ? 80.366 -2.894  2.377   1.00 65.31  ?  82  VAL B CG2 1 
ATOM   2613 N N   . GLY B 1 83  ? 77.713 -1.726  -0.085  1.00 55.47  ?  83  GLY B N   1 
ATOM   2614 C CA  . GLY B 1 83  ? 77.094 -2.183  -1.312  1.00 58.78  ?  83  GLY B CA  1 
ATOM   2615 C C   . GLY B 1 83  ? 76.692 -3.645  -1.381  1.00 62.06  ?  83  GLY B C   1 
ATOM   2616 O O   . GLY B 1 83  ? 76.160 -4.069  -2.414  1.00 54.27  ?  83  GLY B O   1 
ATOM   2617 N N   . THR B 1 84  ? 76.900 -4.419  -0.322  1.00 59.14  ?  84  THR B N   1 
ATOM   2618 C CA  . THR B 1 84  ? 76.656 -5.858  -0.434  1.00 58.85  ?  84  THR B CA  1 
ATOM   2619 C C   . THR B 1 84  ? 75.203 -6.177  -0.741  1.00 58.52  ?  84  THR B C   1 
ATOM   2620 O O   . THR B 1 84  ? 74.958 -6.981  -1.665  1.00 57.12  ?  84  THR B O   1 
ATOM   2621 C CB  . THR B 1 84  ? 77.162 -6.560  0.832   1.00 57.37  ?  84  THR B CB  1 
ATOM   2622 O OG1 . THR B 1 84  ? 78.579 -6.418  0.894   1.00 59.92  ?  84  THR B OG1 1 
ATOM   2623 C CG2 . THR B 1 84  ? 76.825 -8.035  0.828   1.00 50.69  ?  84  THR B CG2 1 
ATOM   2624 N N   . PRO B 1 85  ? 74.194 -5.618  -0.067  1.00 54.49  ?  85  PRO B N   1 
ATOM   2625 C CA  . PRO B 1 85  ? 72.821 -5.963  -0.465  1.00 53.33  ?  85  PRO B CA  1 
ATOM   2626 C C   . PRO B 1 85  ? 72.468 -5.418  -1.834  1.00 58.53  ?  85  PRO B C   1 
ATOM   2627 O O   . PRO B 1 85  ? 71.737 -6.079  -2.583  1.00 52.63  ?  85  PRO B O   1 
ATOM   2628 C CB  . PRO B 1 85  ? 71.946 -5.358  0.638   1.00 41.90  ?  85  PRO B CB  1 
ATOM   2629 C CG  . PRO B 1 85  ? 72.918 -5.060  1.775   1.00 49.78  ?  85  PRO B CG  1 
ATOM   2630 C CD  . PRO B 1 85  ? 74.213 -4.741  1.123   1.00 49.04  ?  85  PRO B CD  1 
ATOM   2631 N N   . GLY B 1 86  ? 72.996 -4.245  -2.197  1.00 53.33  ?  86  GLY B N   1 
ATOM   2632 C CA  . GLY B 1 86  ? 72.620 -3.655  -3.468  1.00 43.69  ?  86  GLY B CA  1 
ATOM   2633 C C   . GLY B 1 86  ? 73.066 -4.497  -4.647  1.00 50.28  ?  86  GLY B C   1 
ATOM   2634 O O   . GLY B 1 86  ? 72.273 -4.802  -5.544  1.00 49.19  ?  86  GLY B O   1 
ATOM   2635 N N   . VAL B 1 87  ? 74.334 -4.922  -4.648  1.00 53.05  ?  87  VAL B N   1 
ATOM   2636 C CA  . VAL B 1 87  ? 74.773 -5.707  -5.786  1.00 53.29  ?  87  VAL B CA  1 
ATOM   2637 C C   . VAL B 1 87  ? 74.224 -7.123  -5.698  1.00 51.91  ?  87  VAL B C   1 
ATOM   2638 O O   . VAL B 1 87  ? 74.021 -7.760  -6.743  1.00 52.97  ?  87  VAL B O   1 
ATOM   2639 C CB  . VAL B 1 87  ? 76.305 -5.702  -5.958  1.00 50.31  ?  87  VAL B CB  1 
ATOM   2640 C CG1 . VAL B 1 87  ? 76.896 -4.282  -5.759  1.00 47.36  ?  87  VAL B CG1 1 
ATOM   2641 C CG2 . VAL B 1 87  ? 76.965 -6.776  -5.133  1.00 65.68  ?  87  VAL B CG2 1 
ATOM   2642 N N   . ARG B 1 88  ? 73.897 -7.611  -4.492  1.00 47.94  ?  88  ARG B N   1 
ATOM   2643 C CA  . ARG B 1 88  ? 73.240 -8.912  -4.393  1.00 47.22  ?  88  ARG B CA  1 
ATOM   2644 C C   . ARG B 1 88  ? 71.905 -8.907  -5.127  1.00 56.04  ?  88  ARG B C   1 
ATOM   2645 O O   . ARG B 1 88  ? 71.608 -9.815  -5.907  1.00 60.38  ?  88  ARG B O   1 
ATOM   2646 C CB  . ARG B 1 88  ? 73.029 -9.314  -2.940  1.00 40.09  ?  88  ARG B CB  1 
ATOM   2647 C CG  . ARG B 1 88  ? 72.372 -10.691 -2.808  1.00 41.20  ?  88  ARG B CG  1 
ATOM   2648 C CD  . ARG B 1 88  ? 72.294 -11.139 -1.373  1.00 44.83  ?  88  ARG B CD  1 
ATOM   2649 N NE  . ARG B 1 88  ? 71.645 -12.435 -1.175  1.00 52.38  ?  88  ARG B NE  1 
ATOM   2650 C CZ  . ARG B 1 88  ? 72.231 -13.628 -1.333  1.00 51.90  ?  88  ARG B CZ  1 
ATOM   2651 N NH1 . ARG B 1 88  ? 73.498 -13.723 -1.707  1.00 39.50  ?  88  ARG B NH1 1 
ATOM   2652 N NH2 . ARG B 1 88  ? 71.537 -14.740 -1.102  1.00 39.97  ?  88  ARG B NH2 1 
ATOM   2653 N N   . ILE B 1 89  ? 71.093 -7.878  -4.888  1.00 56.57  ?  89  ILE B N   1 
ATOM   2654 C CA  . ILE B 1 89  ? 69.775 -7.783  -5.498  1.00 41.49  ?  89  ILE B CA  1 
ATOM   2655 C C   . ILE B 1 89  ? 69.887 -7.696  -7.011  1.00 44.05  ?  89  ILE B C   1 
ATOM   2656 O O   . ILE B 1 89  ? 69.103 -8.323  -7.739  1.00 49.33  ?  89  ILE B O   1 
ATOM   2657 C CB  . ILE B 1 89  ? 69.025 -6.576  -4.904  1.00 44.82  ?  89  ILE B CB  1 
ATOM   2658 C CG1 . ILE B 1 89  ? 68.634 -6.880  -3.455  1.00 34.89  ?  89  ILE B CG1 1 
ATOM   2659 C CG2 . ILE B 1 89  ? 67.819 -6.163  -5.765  1.00 37.17  ?  89  ILE B CG2 1 
ATOM   2660 C CD1 . ILE B 1 89  ? 67.902 -5.743  -2.810  1.00 39.23  ?  89  ILE B CD1 1 
ATOM   2661 N N   . ALA B 1 90  ? 70.847 -6.913  -7.516  1.00 41.53  ?  90  ALA B N   1 
ATOM   2662 C CA  . ALA B 1 90  ? 70.975 -6.770  -8.965  1.00 48.36  ?  90  ALA B CA  1 
ATOM   2663 C C   . ALA B 1 90  ? 71.457 -8.072  -9.599  1.00 53.74  ?  90  ALA B C   1 
ATOM   2664 O O   . ALA B 1 90  ? 71.024 -8.440  -10.700 1.00 49.19  ?  90  ALA B O   1 
ATOM   2665 C CB  . ALA B 1 90  ? 71.926 -5.624  -9.305  1.00 46.05  ?  90  ALA B CB  1 
ATOM   2666 N N   . ARG B 1 91  ? 72.335 -8.796  -8.904  1.00 50.02  ?  91  ARG B N   1 
ATOM   2667 C CA  . ARG B 1 91  ? 72.825 -10.068 -9.420  1.00 50.16  ?  91  ARG B CA  1 
ATOM   2668 C C   . ARG B 1 91  ? 71.758 -11.160 -9.374  1.00 56.14  ?  91  ARG B C   1 
ATOM   2669 O O   . ARG B 1 91  ? 71.586 -11.913 -10.343 1.00 61.56  ?  91  ARG B O   1 
ATOM   2670 C CB  . ARG B 1 91  ? 74.034 -10.495 -8.623  1.00 48.80  ?  91  ARG B CB  1 
ATOM   2671 C CG  . ARG B 1 91  ? 74.733 -11.652 -9.180  1.00 52.89  ?  91  ARG B CG  1 
ATOM   2672 C CD  . ARG B 1 91  ? 75.918 -11.888 -8.315  1.00 55.18  ?  91  ARG B CD  1 
ATOM   2673 N NE  . ARG B 1 91  ? 75.457 -12.211 -6.988  1.00 50.27  ?  91  ARG B NE  1 
ATOM   2674 C CZ  . ARG B 1 91  ? 75.561 -13.421 -6.478  1.00 65.28  ?  91  ARG B CZ  1 
ATOM   2675 N NH1 . ARG B 1 91  ? 76.133 -14.358 -7.212  1.00 76.00  ?  91  ARG B NH1 1 
ATOM   2676 N NH2 . ARG B 1 91  ? 75.130 -13.683 -5.244  1.00 67.59  ?  91  ARG B NH2 1 
ATOM   2677 N N   . LEU B 1 92  ? 71.033 -11.280 -8.254  1.00 49.97  ?  92  LEU B N   1 
ATOM   2678 C CA  . LEU B 1 92  ? 70.090 -12.382 -8.166  1.00 48.17  ?  92  LEU B CA  1 
ATOM   2679 C C   . LEU B 1 92  ? 68.791 -12.086 -8.887  1.00 45.84  ?  92  LEU B C   1 
ATOM   2680 O O   . LEU B 1 92  ? 68.147 -13.008 -9.402  1.00 57.78  ?  92  LEU B O   1 
ATOM   2681 C CB  . LEU B 1 92  ? 69.824 -12.747 -6.707  1.00 48.68  ?  92  LEU B CB  1 
ATOM   2682 C CG  . LEU B 1 92  ? 71.044 -13.444 -6.078  1.00 47.18  ?  92  LEU B CG  1 
ATOM   2683 C CD1 . LEU B 1 92  ? 70.753 -13.950 -4.676  1.00 42.83  ?  92  LEU B CD1 1 
ATOM   2684 C CD2 . LEU B 1 92  ? 71.595 -14.554 -6.972  1.00 36.04  ?  92  LEU B CD2 1 
ATOM   2685 N N   . SER B 1 93  ? 68.382 -10.834 -8.953  1.00 43.52  ?  93  SER B N   1 
ATOM   2686 C CA  . SER B 1 93  ? 67.105 -10.536 -9.565  1.00 41.49  ?  93  SER B CA  1 
ATOM   2687 C C   . SER B 1 93  ? 67.218 -9.930  -10.953 1.00 45.59  ?  93  SER B C   1 
ATOM   2688 O O   . SER B 1 93  ? 66.205 -9.881  -11.655 1.00 46.93  ?  93  SER B O   1 
ATOM   2689 C CB  . SER B 1 93  ? 66.315 -9.596  -8.658  1.00 41.17  ?  93  SER B CB  1 
ATOM   2690 O OG  . SER B 1 93  ? 66.796 -8.273  -8.842  1.00 51.45  ?  93  SER B OG  1 
ATOM   2691 N N   . GLY B 1 94  ? 68.406 -9.463  -11.356 1.00 42.91  ?  94  GLY B N   1 
ATOM   2692 C CA  . GLY B 1 94  ? 68.600 -8.726  -12.591 1.00 48.92  ?  94  GLY B CA  1 
ATOM   2693 C C   . GLY B 1 94  ? 67.985 -7.335  -12.646 1.00 46.89  ?  94  GLY B C   1 
ATOM   2694 O O   . GLY B 1 94  ? 68.189 -6.638  -13.646 1.00 49.98  ?  94  GLY B O   1 
ATOM   2695 N N   . ALA B 1 95  ? 67.238 -6.914  -11.617 1.00 43.44  ?  95  ALA B N   1 
ATOM   2696 C CA  . ALA B 1 95  ? 66.795 -5.531  -11.480 1.00 42.48  ?  95  ALA B CA  1 
ATOM   2697 C C   . ALA B 1 95  ? 67.960 -4.554  -11.535 1.00 46.24  ?  95  ALA B C   1 
ATOM   2698 O O   . ALA B 1 95  ? 69.097 -4.896  -11.212 1.00 48.31  ?  95  ALA B O   1 
ATOM   2699 C CB  . ALA B 1 95  ? 66.075 -5.331  -10.142 1.00 43.34  ?  95  ALA B CB  1 
ATOM   2700 N N   . HIS B 1 96  ? 67.661 -3.305  -11.897 1.00 49.13  ?  96  HIS B N   1 
ATOM   2701 C CA  . HIS B 1 96  ? 68.646 -2.230  -11.823 1.00 43.38  ?  96  HIS B CA  1 
ATOM   2702 C C   . HIS B 1 96  ? 68.601 -1.528  -10.465 1.00 43.55  ?  96  HIS B C   1 
ATOM   2703 O O   . HIS B 1 96  ? 67.524 -1.207  -9.951  1.00 49.46  ?  96  HIS B O   1 
ATOM   2704 C CB  . HIS B 1 96  ? 68.427 -1.208  -12.927 1.00 39.86  ?  96  HIS B CB  1 
ATOM   2705 C CG  . HIS B 1 96  ? 69.519 -0.192  -12.994 1.00 48.55  ?  96  HIS B CG  1 
ATOM   2706 N ND1 . HIS B 1 96  ? 69.450 1.014   -12.330 1.00 50.64  ?  96  HIS B ND1 1 
ATOM   2707 C CD2 . HIS B 1 96  ? 70.727 -0.222  -13.601 1.00 43.25  ?  96  HIS B CD2 1 
ATOM   2708 C CE1 . HIS B 1 96  ? 70.559 1.694   -12.547 1.00 43.75  ?  96  HIS B CE1 1 
ATOM   2709 N NE2 . HIS B 1 96  ? 71.352 0.966   -13.310 1.00 49.17  ?  96  HIS B NE2 1 
ATOM   2710 N N   . VAL B 1 97  ? 69.769 -1.286  -9.891  1.00 43.16  ?  97  VAL B N   1 
ATOM   2711 C CA  . VAL B 1 97  ? 69.881 -0.716  -8.550  1.00 52.96  ?  97  VAL B CA  1 
ATOM   2712 C C   . VAL B 1 97  ? 70.652 0.591   -8.633  1.00 42.66  ?  97  VAL B C   1 
ATOM   2713 O O   . VAL B 1 97  ? 71.790 0.607   -9.112  1.00 51.59  ?  97  VAL B O   1 
ATOM   2714 C CB  . VAL B 1 97  ? 70.562 -1.682  -7.565  1.00 49.19  ?  97  VAL B CB  1 
ATOM   2715 C CG1 . VAL B 1 97  ? 70.627 -1.044  -6.193  1.00 41.12  ?  97  VAL B CG1 1 
ATOM   2716 C CG2 . VAL B 1 97  ? 69.799 -2.988  -7.496  1.00 38.27  ?  97  VAL B CG2 1 
ATOM   2717 N N   . THR B 1 98  ? 70.021 1.683   -8.186  1.00 38.50  ?  98  THR B N   1 
ATOM   2718 C CA  . THR B 1 98  ? 70.695 2.929   -7.825  1.00 43.88  ?  98  THR B CA  1 
ATOM   2719 C C   . THR B 1 98  ? 70.750 2.990   -6.301  1.00 47.62  ?  98  THR B C   1 
ATOM   2720 O O   . THR B 1 98  ? 69.712 3.123   -5.646  1.00 48.01  ?  98  THR B O   1 
ATOM   2721 C CB  . THR B 1 98  ? 69.951 4.156   -8.338  1.00 45.39  ?  98  THR B CB  1 
ATOM   2722 O OG1 . THR B 1 98  ? 69.493 3.960   -9.680  1.00 47.35  ?  98  THR B OG1 1 
ATOM   2723 C CG2 . THR B 1 98  ? 70.843 5.338   -8.281  1.00 50.75  ?  98  THR B CG2 1 
ATOM   2724 N N   . GLY B 1 99  ? 71.938 2.892   -5.734  1.00 50.38  ?  99  GLY B N   1 
ATOM   2725 C CA  . GLY B 1 99  ? 72.120 3.126   -4.314  1.00 53.45  ?  99  GLY B CA  1 
ATOM   2726 C C   . GLY B 1 99  ? 72.724 4.490   -4.017  1.00 54.13  ?  99  GLY B C   1 
ATOM   2727 O O   . GLY B 1 99  ? 73.563 4.997   -4.773  1.00 55.77  ?  99  GLY B O   1 
ATOM   2728 N N   . ILE B 1 100 ? 72.305 5.076   -2.891  1.00 46.69  ?  100 ILE B N   1 
ATOM   2729 C CA  . ILE B 1 100 ? 72.842 6.346   -2.404  1.00 39.33  ?  100 ILE B CA  1 
ATOM   2730 C C   . ILE B 1 100 ? 73.472 6.133   -1.030  1.00 53.37  ?  100 ILE B C   1 
ATOM   2731 O O   . ILE B 1 100 ? 72.995 5.327   -0.212  1.00 42.97  ?  100 ILE B O   1 
ATOM   2732 C CB  . ILE B 1 100 ? 71.766 7.443   -2.355  1.00 39.22  ?  100 ILE B CB  1 
ATOM   2733 C CG1 . ILE B 1 100 ? 70.842 7.234   -1.156  1.00 44.98  ?  100 ILE B CG1 1 
ATOM   2734 C CG2 . ILE B 1 100 ? 70.970 7.499   -3.682  1.00 42.59  ?  100 ILE B CG2 1 
ATOM   2735 C CD1 . ILE B 1 100 ? 69.632 8.170   -1.096  1.00 43.56  ?  100 ILE B CD1 1 
ATOM   2736 N N   . SER B 1 101 ? 74.588 6.822   -0.806  1.00 53.73  ?  101 SER B N   1 
ATOM   2737 C CA  . SER B 1 101 ? 75.183 6.933   0.516   1.00 45.16  ?  101 SER B CA  1 
ATOM   2738 C C   . SER B 1 101 ? 75.673 8.357   0.718   1.00 54.39  ?  101 SER B C   1 
ATOM   2739 O O   . SER B 1 101 ? 75.910 9.100   -0.243  1.00 55.37  ?  101 SER B O   1 
ATOM   2740 C CB  . SER B 1 101 ? 76.332 5.960   0.718   1.00 45.87  ?  101 SER B CB  1 
ATOM   2741 O OG  . SER B 1 101 ? 76.910 6.141   1.996   1.00 57.70  ?  101 SER B OG  1 
ATOM   2742 N N   . VAL B 1 102 ? 75.813 8.744   1.989   1.00 46.66  ?  102 VAL B N   1 
ATOM   2743 C CA  . VAL B 1 102 ? 76.385 10.049  2.285   1.00 52.63  ?  102 VAL B CA  1 
ATOM   2744 C C   . VAL B 1 102 ? 77.882 9.959   2.572   1.00 59.65  ?  102 VAL B C   1 
ATOM   2745 O O   . VAL B 1 102 ? 78.561 10.999  2.581   1.00 65.55  ?  102 VAL B O   1 
ATOM   2746 C CB  . VAL B 1 102 ? 75.619 10.765  3.426   1.00 58.71  ?  102 VAL B CB  1 
ATOM   2747 C CG1 . VAL B 1 102 ? 74.330 11.356  2.873   1.00 59.22  ?  102 VAL B CG1 1 
ATOM   2748 C CG2 . VAL B 1 102 ? 75.336 9.842   4.627   1.00 47.53  ?  102 VAL B CG2 1 
ATOM   2749 N N   . SER B 1 103 ? 78.422 8.752   2.732   1.00 56.83  ?  103 SER B N   1 
ATOM   2750 C CA  . SER B 1 103 ? 79.852 8.541   2.907   1.00 65.98  ?  103 SER B CA  1 
ATOM   2751 C C   . SER B 1 103 ? 80.550 8.322   1.560   1.00 65.56  ?  103 SER B C   1 
ATOM   2752 O O   . SER B 1 103 ? 80.061 7.573   0.703   1.00 64.47  ?  103 SER B O   1 
ATOM   2753 C CB  . SER B 1 103 ? 80.084 7.351   3.837   1.00 66.61  ?  103 SER B CB  1 
ATOM   2754 O OG  . SER B 1 103 ? 81.275 6.642   3.527   1.00 65.35  ?  103 SER B OG  1 
ATOM   2755 N N   . HIS B 1 104 ? 81.698 8.984   1.378   1.00 56.00  ?  104 HIS B N   1 
ATOM   2756 C CA  . HIS B 1 104 ? 82.488 8.796   0.165   1.00 60.24  ?  104 HIS B CA  1 
ATOM   2757 C C   . HIS B 1 104 ? 83.104 7.401   0.111   1.00 68.25  ?  104 HIS B C   1 
ATOM   2758 O O   . HIS B 1 104 ? 83.094 6.760   -0.949  1.00 74.36  ?  104 HIS B O   1 
ATOM   2759 C CB  . HIS B 1 104 ? 83.563 9.881   0.075   1.00 55.39  ?  104 HIS B CB  1 
ATOM   2760 C CG  . HIS B 1 104 ? 84.464 9.780   -1.124  1.00 54.54  ?  104 HIS B CG  1 
ATOM   2761 N ND1 . HIS B 1 104 ? 85.624 9.029   -1.126  1.00 48.31  ?  104 HIS B ND1 1 
ATOM   2762 C CD2 . HIS B 1 104 ? 84.401 10.379  -2.340  1.00 51.12  ?  104 HIS B CD2 1 
ATOM   2763 C CE1 . HIS B 1 104 ? 86.226 9.162   -2.295  1.00 53.86  ?  104 HIS B CE1 1 
ATOM   2764 N NE2 . HIS B 1 104 ? 85.504 9.974   -3.049  1.00 49.87  ?  104 HIS B NE2 1 
ATOM   2765 N N   . GLU B 1 105 ? 83.653 6.916   1.232   1.00 61.62  ?  105 GLU B N   1 
ATOM   2766 C CA  . GLU B 1 105 ? 84.241 5.577   1.243   1.00 68.78  ?  105 GLU B CA  1 
ATOM   2767 C C   . GLU B 1 105 ? 83.206 4.537   0.867   1.00 68.38  ?  105 GLU B C   1 
ATOM   2768 O O   . GLU B 1 105 ? 83.512 3.548   0.187   1.00 71.15  ?  105 GLU B O   1 
ATOM   2769 C CB  . GLU B 1 105 ? 84.830 5.230   2.616   1.00 72.77  ?  105 GLU B CB  1 
ATOM   2770 C CG  . GLU B 1 105 ? 86.057 5.999   2.995   1.00 77.23  ?  105 GLU B CG  1 
ATOM   2771 C CD  . GLU B 1 105 ? 87.112 5.945   1.920   1.00 93.36  ?  105 GLU B CD  1 
ATOM   2772 O OE1 . GLU B 1 105 ? 87.351 4.853   1.358   1.00 100.41 ?  105 GLU B OE1 1 
ATOM   2773 O OE2 . GLU B 1 105 ? 87.695 7.005   1.618   1.00 99.56  -1 105 GLU B OE2 1 
ATOM   2774 N N   . GLN B 1 106 ? 81.969 4.745   1.304   1.00 62.62  ?  106 GLN B N   1 
ATOM   2775 C CA  . GLN B 1 106 ? 80.931 3.783   0.995   1.00 63.06  ?  106 GLN B CA  1 
ATOM   2776 C C   . GLN B 1 106 ? 80.662 3.745   -0.509  1.00 65.36  ?  106 GLN B C   1 
ATOM   2777 O O   . GLN B 1 106 ? 80.673 2.667   -1.122  1.00 62.04  ?  106 GLN B O   1 
ATOM   2778 C CB  . GLN B 1 106 ? 79.682 4.113   1.809   1.00 60.42  ?  106 GLN B CB  1 
ATOM   2779 C CG  . GLN B 1 106 ? 79.752 3.562   3.248   1.00 57.75  ?  106 GLN B CG  1 
ATOM   2780 C CD  . GLN B 1 106 ? 78.432 3.674   4.018   1.00 62.57  ?  106 GLN B CD  1 
ATOM   2781 O OE1 . GLN B 1 106 ? 77.523 4.416   3.626   1.00 70.14  ?  106 GLN B OE1 1 
ATOM   2782 N NE2 . GLN B 1 106 ? 78.315 2.910   5.100   1.00 58.05  ?  106 GLN B NE2 1 
ATOM   2783 N N   . VAL B 1 107 ? 80.472 4.918   -1.133  1.00 56.12  ?  107 VAL B N   1 
ATOM   2784 C CA  . VAL B 1 107 ? 80.251 4.940   -2.575  1.00 48.14  ?  107 VAL B CA  1 
ATOM   2785 C C   . VAL B 1 107 ? 81.399 4.257   -3.293  1.00 60.56  ?  107 VAL B C   1 
ATOM   2786 O O   . VAL B 1 107 ? 81.186 3.409   -4.171  1.00 64.45  ?  107 VAL B O   1 
ATOM   2787 C CB  . VAL B 1 107 ? 80.056 6.368   -3.099  1.00 50.72  ?  107 VAL B CB  1 
ATOM   2788 C CG1 . VAL B 1 107 ? 80.147 6.360   -4.622  1.00 54.26  ?  107 VAL B CG1 1 
ATOM   2789 C CG2 . VAL B 1 107 ? 78.714 6.937   -2.664  1.00 47.14  ?  107 VAL B CG2 1 
ATOM   2790 N N   . VAL B 1 108 ? 82.631 4.586   -2.913  1.00 60.79  ?  108 VAL B N   1 
ATOM   2791 C CA  . VAL B 1 108 ? 83.792 3.982   -3.565  1.00 55.27  ?  108 VAL B CA  1 
ATOM   2792 C C   . VAL B 1 108 ? 83.766 2.464   -3.411  1.00 64.03  ?  108 VAL B C   1 
ATOM   2793 O O   . VAL B 1 108 ? 84.000 1.730   -4.380  1.00 63.35  ?  108 VAL B O   1 
ATOM   2794 C CB  . VAL B 1 108 ? 85.099 4.592   -3.020  1.00 51.30  ?  108 VAL B CB  1 
ATOM   2795 C CG1 . VAL B 1 108 ? 86.291 3.856   -3.568  1.00 43.93  ?  108 VAL B CG1 1 
ATOM   2796 C CG2 . VAL B 1 108 ? 85.189 6.076   -3.378  1.00 46.22  ?  108 VAL B CG2 1 
ATOM   2797 N N   . ARG B 1 109 ? 83.455 1.962   -2.202  1.00 59.76  ?  109 ARG B N   1 
ATOM   2798 C CA  . ARG B 1 109 ? 83.524 0.513   -1.991  1.00 50.99  ?  109 ARG B CA  1 
ATOM   2799 C C   . ARG B 1 109 ? 82.377 -0.210  -2.677  1.00 52.49  ?  109 ARG B C   1 
ATOM   2800 O O   . ARG B 1 109 ? 82.580 -1.270  -3.264  1.00 53.79  ?  109 ARG B O   1 
ATOM   2801 C CB  . ARG B 1 109 ? 83.561 0.165   -0.507  1.00 49.04  ?  109 ARG B CB  1 
ATOM   2802 C CG  . ARG B 1 109 ? 84.866 0.572   0.088   1.00 65.50  ?  109 ARG B CG  1 
ATOM   2803 C CD  . ARG B 1 109 ? 85.261 -0.093  1.384   1.00 88.61  ?  109 ARG B CD  1 
ATOM   2804 N NE  . ARG B 1 109 ? 86.572 0.456   1.743   1.00 112.33 ?  109 ARG B NE  1 
ATOM   2805 C CZ  . ARG B 1 109 ? 87.345 0.041   2.742   1.00 120.54 ?  109 ARG B CZ  1 
ATOM   2806 N NH1 . ARG B 1 109 ? 86.956 -0.945  3.526   1.00 127.93 ?  109 ARG B NH1 1 
ATOM   2807 N NH2 . ARG B 1 109 ? 88.520 0.623   2.958   1.00 117.55 ?  109 ARG B NH2 1 
ATOM   2808 N N   . ALA B 1 110 ? 81.169 0.350   -2.637  1.00 52.98  ?  110 ALA B N   1 
ATOM   2809 C CA  . ALA B 1 110 ? 80.055 -0.277  -3.346  1.00 52.38  ?  110 ALA B CA  1 
ATOM   2810 C C   . ALA B 1 110 ? 80.286 -0.307  -4.862  1.00 55.25  ?  110 ALA B C   1 
ATOM   2811 O O   . ALA B 1 110 ? 79.963 -1.301  -5.522  1.00 55.15  ?  110 ALA B O   1 
ATOM   2812 C CB  . ALA B 1 110 ? 78.744 0.443   -3.020  1.00 46.08  ?  110 ALA B CB  1 
ATOM   2813 N N   . ASN B 1 111 ? 80.829 0.768   -5.444  1.00 46.93  ?  111 ASN B N   1 
ATOM   2814 C CA  . ASN B 1 111 ? 81.094 0.723   -6.873  1.00 42.48  ?  111 ASN B CA  1 
ATOM   2815 C C   . ASN B 1 111 ? 82.146 -0.337  -7.192  1.00 54.04  ?  111 ASN B C   1 
ATOM   2816 O O   . ASN B 1 111 ? 82.090 -0.982  -8.239  1.00 54.18  ?  111 ASN B O   1 
ATOM   2817 C CB  . ASN B 1 111 ? 81.500 2.100   -7.385  1.00 42.86  ?  111 ASN B CB  1 
ATOM   2818 C CG  . ASN B 1 111 ? 80.297 3.011   -7.636  1.00 50.32  ?  111 ASN B CG  1 
ATOM   2819 O OD1 . ASN B 1 111 ? 79.198 2.539   -7.897  1.00 53.08  ?  111 ASN B OD1 1 
ATOM   2820 N ND2 . ASN B 1 111 ? 80.507 4.318   -7.567  1.00 65.80  ?  111 ASN B ND2 1 
ATOM   2821 N N   . ALA B 1 112 ? 83.099 -0.557  -6.281  1.00 63.02  ?  112 ALA B N   1 
ATOM   2822 C CA  . ALA B 1 112 ? 84.077 -1.628  -6.466  1.00 54.09  ?  112 ALA B CA  1 
ATOM   2823 C C   . ALA B 1 112 ? 83.417 -3.000  -6.422  1.00 46.92  ?  112 ALA B C   1 
ATOM   2824 O O   . ALA B 1 112 ? 83.805 -3.925  -7.149  1.00 48.89  ?  112 ALA B O   1 
ATOM   2825 C CB  . ALA B 1 112 ? 85.152 -1.535  -5.388  1.00 36.83  ?  112 ALA B CB  1 
ATOM   2826 N N   . LEU B 1 113 ? 82.441 -3.163  -5.546  1.00 42.99  ?  113 LEU B N   1 
ATOM   2827 C CA  . LEU B 1 113 ? 81.790 -4.451  -5.437  1.00 37.15  ?  113 LEU B CA  1 
ATOM   2828 C C   . LEU B 1 113 ? 81.009 -4.752  -6.700  1.00 58.52  ?  113 LEU B C   1 
ATOM   2829 O O   . LEU B 1 113 ? 81.076 -5.872  -7.224  1.00 59.08  ?  113 LEU B O   1 
ATOM   2830 C CB  . LEU B 1 113 ? 80.874 -4.454  -4.227  1.00 35.19  ?  113 LEU B CB  1 
ATOM   2831 C CG  . LEU B 1 113 ? 80.523 -5.840  -3.731  1.00 45.95  ?  113 LEU B CG  1 
ATOM   2832 C CD1 . LEU B 1 113 ? 81.786 -6.610  -3.413  1.00 36.77  ?  113 LEU B CD1 1 
ATOM   2833 C CD2 . LEU B 1 113 ? 79.646 -5.673  -2.512  1.00 49.54  ?  113 LEU B CD2 1 
ATOM   2834 N N   . ALA B 1 114 ? 80.272 -3.746  -7.204  1.00 48.67  ?  114 ALA B N   1 
ATOM   2835 C CA  . ALA B 1 114 ? 79.565 -3.895  -8.462  1.00 41.97  ?  114 ALA B CA  1 
ATOM   2836 C C   . ALA B 1 114 ? 80.528 -4.273  -9.575  1.00 51.14  ?  114 ALA B C   1 
ATOM   2837 O O   . ALA B 1 114 ? 80.243 -5.176  -10.372 1.00 56.27  ?  114 ALA B O   1 
ATOM   2838 C CB  . ALA B 1 114 ? 78.821 -2.604  -8.805  1.00 41.20  ?  114 ALA B CB  1 
ATOM   2839 N N   . GLU B 1 115 ? 81.691 -3.619  -9.624  1.00 42.88  ?  115 GLU B N   1 
ATOM   2840 C CA  . GLU B 1 115 ? 82.634 -3.906  -10.690 1.00 43.83  ?  115 GLU B CA  1 
ATOM   2841 C C   . GLU B 1 115 ? 83.221 -5.301  -10.548 1.00 50.62  ?  115 GLU B C   1 
ATOM   2842 O O   . GLU B 1 115 ? 83.349 -6.030  -11.537 1.00 55.69  ?  115 GLU B O   1 
ATOM   2843 C CB  . GLU B 1 115 ? 83.740 -2.877  -10.722 1.00 35.47  ?  115 GLU B CB  1 
ATOM   2844 C CG  . GLU B 1 115 ? 84.904 -3.436  -11.490 1.00 64.08  ?  115 GLU B CG  1 
ATOM   2845 C CD  . GLU B 1 115 ? 85.708 -2.379  -12.184 1.00 82.05  ?  115 GLU B CD  1 
ATOM   2846 O OE1 . GLU B 1 115 ? 85.292 -1.195  -12.146 1.00 85.96  ?  115 GLU B OE1 1 
ATOM   2847 O OE2 . GLU B 1 115 ? 86.738 -2.745  -12.798 1.00 96.40  -1 115 GLU B OE2 1 
ATOM   2848 N N   . GLU B 1 116 ? 83.606 -5.685  -9.331  1.00 47.77  ?  116 GLU B N   1 
ATOM   2849 C CA  . GLU B 1 116 ? 84.100 -7.037  -9.127  1.00 53.20  ?  116 GLU B CA  1 
ATOM   2850 C C   . GLU B 1 116 ? 83.062 -8.068  -9.565  1.00 52.88  ?  116 GLU B C   1 
ATOM   2851 O O   . GLU B 1 116 ? 83.410 -9.120  -10.112 1.00 55.45  ?  116 GLU B O   1 
ATOM   2852 C CB  . GLU B 1 116 ? 84.498 -7.223  -7.656  1.00 51.67  ?  116 GLU B CB  1 
ATOM   2853 C CG  . GLU B 1 116 ? 84.842 -8.658  -7.247  1.00 59.09  ?  116 GLU B CG  1 
ATOM   2854 C CD  . GLU B 1 116 ? 86.016 -9.250  -8.036  1.00 85.87  ?  116 GLU B CD  1 
ATOM   2855 O OE1 . GLU B 1 116 ? 86.790 -8.469  -8.660  1.00 86.67  ?  116 GLU B OE1 1 
ATOM   2856 O OE2 . GLU B 1 116 ? 86.173 -10.504 -8.010  1.00 92.82  -1 116 GLU B OE2 1 
ATOM   2857 N N   . ALA B 1 117 ? 81.782 -7.759  -9.380  1.00 43.91  ?  117 ALA B N   1 
ATOM   2858 C CA  . ALA B 1 117 ? 80.730 -8.665  -9.781  1.00 46.14  ?  117 ALA B CA  1 
ATOM   2859 C C   . ALA B 1 117 ? 80.532 -8.712  -11.285 1.00 48.30  ?  117 ALA B C   1 
ATOM   2860 O O   . ALA B 1 117 ? 79.764 -9.561  -11.760 1.00 52.13  ?  117 ALA B O   1 
ATOM   2861 C CB  . ALA B 1 117 ? 79.422 -8.255  -9.117  1.00 39.41  ?  117 ALA B CB  1 
ATOM   2862 N N   . GLY B 1 118 ? 81.167 -7.819  -12.035 1.00 40.67  ?  118 GLY B N   1 
ATOM   2863 C CA  . GLY B 1 118 ? 80.902 -7.757  -13.453 1.00 44.87  ?  118 GLY B CA  1 
ATOM   2864 C C   . GLY B 1 118 ? 79.573 -7.124  -13.793 1.00 51.76  ?  118 GLY B C   1 
ATOM   2865 O O   . GLY B 1 118 ? 78.955 -7.500  -14.796 1.00 51.46  ?  118 GLY B O   1 
ATOM   2866 N N   . LEU B 1 119 ? 79.146 -6.128  -13.005 1.00 48.82  ?  119 LEU B N   1 
ATOM   2867 C CA  . LEU B 1 119 ? 77.809 -5.557  -13.028 1.00 44.57  ?  119 LEU B CA  1 
ATOM   2868 C C   . LEU B 1 119 ? 77.844 -4.032  -12.888 1.00 52.15  ?  119 LEU B C   1 
ATOM   2869 O O   . LEU B 1 119 ? 76.859 -3.421  -12.439 1.00 53.70  ?  119 LEU B O   1 
ATOM   2870 C CB  . LEU B 1 119 ? 76.967 -6.149  -11.886 1.00 45.01  ?  119 LEU B CB  1 
ATOM   2871 C CG  . LEU B 1 119 ? 76.542 -7.615  -11.924 1.00 46.07  ?  119 LEU B CG  1 
ATOM   2872 C CD1 . LEU B 1 119 ? 75.785 -7.921  -10.663 1.00 46.56  ?  119 LEU B CD1 1 
ATOM   2873 C CD2 . LEU B 1 119 ? 75.652 -7.908  -13.122 1.00 44.07  ?  119 LEU B CD2 1 
ATOM   2874 N N   . ALA B 1 120 ? 78.963 -3.394  -13.253 1.00 57.46  ?  120 ALA B N   1 
ATOM   2875 C CA  . ALA B 1 120 ? 79.137 -1.971  -12.951 1.00 53.39  ?  120 ALA B CA  1 
ATOM   2876 C C   . ALA B 1 120 ? 78.030 -1.088  -13.516 1.00 64.72  ?  120 ALA B C   1 
ATOM   2877 O O   . ALA B 1 120 ? 77.916 0.072   -13.110 1.00 78.15  ?  120 ALA B O   1 
ATOM   2878 C CB  . ALA B 1 120 ? 80.475 -1.464  -13.485 1.00 42.67  ?  120 ALA B CB  1 
ATOM   2879 N N   . ASP B 1 121 ? 77.187 -1.605  -14.404 1.00 61.80  ?  121 ASP B N   1 
ATOM   2880 C CA  . ASP B 1 121 ? 76.125 -0.813  -14.992 1.00 49.22  ?  121 ASP B CA  1 
ATOM   2881 C C   . ASP B 1 121 ? 74.763 -1.208  -14.492 1.00 48.34  ?  121 ASP B C   1 
ATOM   2882 O O   . ASP B 1 121 ? 73.832 -0.407  -14.586 1.00 53.38  ?  121 ASP B O   1 
ATOM   2883 C CB  . ASP B 1 121 ? 76.180 -0.945  -16.511 1.00 63.20  ?  121 ASP B CB  1 
ATOM   2884 C CG  . ASP B 1 121 ? 77.565 -0.615  -17.027 1.00 106.13 ?  121 ASP B CG  1 
ATOM   2885 O OD1 . ASP B 1 121 ? 78.542 -1.284  -16.589 1.00 118.48 ?  121 ASP B OD1 1 
ATOM   2886 O OD2 . ASP B 1 121 ? 77.695 0.403   -17.761 1.00 113.75 -1 121 ASP B OD2 1 
ATOM   2887 N N   . ARG B 1 122 ? 74.628 -2.404  -13.955 1.00 37.78  ?  122 ARG B N   1 
ATOM   2888 C CA  . ARG B 1 122 ? 73.374 -2.787  -13.361 1.00 43.98  ?  122 ARG B CA  1 
ATOM   2889 C C   . ARG B 1 122 ? 73.237 -2.188  -11.959 1.00 48.66  ?  122 ARG B C   1 
ATOM   2890 O O   . ARG B 1 122 ? 72.150 -1.727  -11.597 1.00 49.73  ?  122 ARG B O   1 
ATOM   2891 C CB  . ARG B 1 122 ? 73.256 -4.317  -13.363 1.00 34.57  ?  122 ARG B CB  1 
ATOM   2892 C CG  . ARG B 1 122 ? 71.841 -4.789  -13.243 1.00 38.36  ?  122 ARG B CG  1 
ATOM   2893 C CD  . ARG B 1 122 ? 71.802 -6.251  -13.006 1.00 53.26  ?  122 ARG B CD  1 
ATOM   2894 N NE  . ARG B 1 122 ? 72.432 -6.936  -14.121 1.00 59.71  ?  122 ARG B NE  1 
ATOM   2895 C CZ  . ARG B 1 122 ? 72.561 -8.251  -14.214 1.00 52.56  ?  122 ARG B CZ  1 
ATOM   2896 N NH1 . ARG B 1 122 ? 72.102 -9.035  -13.244 1.00 62.76  ?  122 ARG B NH1 1 
ATOM   2897 N NH2 . ARG B 1 122 ? 73.169 -8.770  -15.269 1.00 48.81  ?  122 ARG B NH2 1 
ATOM   2898 N N   . ALA B 1 123 ? 74.330 -2.164  -11.175 1.00 42.44  ?  123 ALA B N   1 
ATOM   2899 C CA  . ALA B 1 123 ? 74.363 -1.556  -9.843  1.00 40.42  ?  123 ALA B CA  1 
ATOM   2900 C C   . ALA B 1 123 ? 75.325 -0.370  -9.811  1.00 48.67  ?  123 ALA B C   1 
ATOM   2901 O O   . ALA B 1 123 ? 76.544 -0.561  -9.851  1.00 59.44  ?  123 ALA B O   1 
ATOM   2902 C CB  . ALA B 1 123 ? 74.775 -2.579  -8.799  1.00 47.32  ?  123 ALA B CB  1 
ATOM   2903 N N   . ARG B 1 124 ? 74.778 0.849   -9.717  1.00 44.93  ?  124 ARG B N   1 
ATOM   2904 C CA  . ARG B 1 124 ? 75.545 2.096   -9.697  1.00 38.57  ?  124 ARG B CA  1 
ATOM   2905 C C   . ARG B 1 124 ? 75.289 2.822   -8.384  1.00 56.51  ?  124 ARG B C   1 
ATOM   2906 O O   . ARG B 1 124 ? 74.128 3.007   -7.971  1.00 61.20  ?  124 ARG B O   1 
ATOM   2907 C CB  . ARG B 1 124 ? 75.172 3.024   -10.854 1.00 39.55  ?  124 ARG B CB  1 
ATOM   2908 C CG  . ARG B 1 124 ? 75.821 2.654   -12.192 1.00 53.13  ?  124 ARG B CG  1 
ATOM   2909 C CD  . ARG B 1 124 ? 75.248 3.477   -13.331 1.00 47.35  ?  124 ARG B CD  1 
ATOM   2910 N NE  . ARG B 1 124 ? 75.910 3.164   -14.586 1.00 55.15  ?  124 ARG B NE  1 
ATOM   2911 C CZ  . ARG B 1 124 ? 75.408 3.431   -15.793 1.00 56.41  ?  124 ARG B CZ  1 
ATOM   2912 N NH1 . ARG B 1 124 ? 74.225 4.027   -15.942 1.00 52.17  ?  124 ARG B NH1 1 
ATOM   2913 N NH2 . ARG B 1 124 ? 76.108 3.108   -16.861 1.00 59.63  ?  124 ARG B NH2 1 
ATOM   2914 N N   . PHE B 1 125 ? 76.363 3.244   -7.735  1.00 52.26  ?  125 PHE B N   1 
ATOM   2915 C CA  . PHE B 1 125 ? 76.257 3.872   -6.431  1.00 46.80  ?  125 PHE B CA  1 
ATOM   2916 C C   . PHE B 1 125 ? 76.762 5.298   -6.506  1.00 45.84  ?  125 PHE B C   1 
ATOM   2917 O O   . PHE B 1 125 ? 77.670 5.624   -7.275  1.00 44.07  ?  125 PHE B O   1 
ATOM   2918 C CB  . PHE B 1 125 ? 76.985 3.056   -5.397  1.00 42.39  ?  125 PHE B CB  1 
ATOM   2919 C CG  . PHE B 1 125 ? 76.392 1.700   -5.228  1.00 45.00  ?  125 PHE B CG  1 
ATOM   2920 C CD1 . PHE B 1 125 ? 75.370 1.490   -4.306  1.00 40.00  ?  125 PHE B CD1 1 
ATOM   2921 C CD2 . PHE B 1 125 ? 76.803 0.642   -6.039  1.00 50.07  ?  125 PHE B CD2 1 
ATOM   2922 C CE1 . PHE B 1 125 ? 74.797 0.236   -4.136  1.00 52.91  ?  125 PHE B CE1 1 
ATOM   2923 C CE2 . PHE B 1 125 ? 76.230 -0.619  -5.904  1.00 48.69  ?  125 PHE B CE2 1 
ATOM   2924 C CZ  . PHE B 1 125 ? 75.224 -0.826  -4.936  1.00 58.98  ?  125 PHE B CZ  1 
ATOM   2925 N N   . GLN B 1 126 ? 76.126 6.140   -5.708  1.00 49.00  ?  126 GLN B N   1 
ATOM   2926 C CA  . GLN B 1 126 ? 76.111 7.576   -5.921  1.00 44.66  ?  126 GLN B CA  1 
ATOM   2927 C C   . GLN B 1 126 ? 76.111 8.290   -4.569  1.00 47.81  ?  126 GLN B C   1 
ATOM   2928 O O   . GLN B 1 126 ? 75.463 7.858   -3.603  1.00 43.68  ?  126 GLN B O   1 
ATOM   2929 C CB  . GLN B 1 126 ? 74.883 7.931   -6.772  1.00 39.64  ?  126 GLN B CB  1 
ATOM   2930 C CG  . GLN B 1 126 ? 74.240 9.242   -6.510  1.00 46.06  ?  126 GLN B CG  1 
ATOM   2931 C CD  . GLN B 1 126 ? 73.194 9.615   -7.542  1.00 49.50  ?  126 GLN B CD  1 
ATOM   2932 O OE1 . GLN B 1 126 ? 73.072 8.989   -8.612  1.00 48.89  ?  126 GLN B OE1 1 
ATOM   2933 N NE2 . GLN B 1 126 ? 72.440 10.663  -7.240  1.00 50.34  ?  126 GLN B NE2 1 
ATOM   2934 N N   . ARG B 1 127 ? 76.851 9.382   -4.500  1.00 44.42  ?  127 ARG B N   1 
ATOM   2935 C CA  . ARG B 1 127 ? 76.775 10.242  -3.334  1.00 44.55  ?  127 ARG B CA  1 
ATOM   2936 C C   . ARG B 1 127 ? 75.478 11.045  -3.393  1.00 43.97  ?  127 ARG B C   1 
ATOM   2937 O O   . ARG B 1 127 ? 75.219 11.753  -4.371  1.00 51.42  ?  127 ARG B O   1 
ATOM   2938 C CB  . ARG B 1 127 ? 78.003 11.136  -3.292  1.00 47.36  ?  127 ARG B CB  1 
ATOM   2939 C CG  . ARG B 1 127 ? 78.159 11.847  -2.002  1.00 63.27  ?  127 ARG B CG  1 
ATOM   2940 C CD  . ARG B 1 127 ? 79.002 11.088  -1.021  1.00 66.31  ?  127 ARG B CD  1 
ATOM   2941 N NE  . ARG B 1 127 ? 79.195 11.917  0.164   1.00 76.19  ?  127 ARG B NE  1 
ATOM   2942 C CZ  . ARG B 1 127 ? 80.078 12.909  0.236   1.00 76.18  ?  127 ARG B CZ  1 
ATOM   2943 N NH1 . ARG B 1 127 ? 80.878 13.179  -0.796  1.00 64.79  ?  127 ARG B NH1 1 
ATOM   2944 N NH2 . ARG B 1 127 ? 80.175 13.619  1.351   1.00 78.88  ?  127 ARG B NH2 1 
ATOM   2945 N N   . ALA B 1 128 ? 74.622 10.873  -2.389  1.00 44.28  ?  128 ALA B N   1 
ATOM   2946 C CA  . ALA B 1 128 ? 73.327 11.555  -2.310  1.00 51.90  ?  128 ALA B CA  1 
ATOM   2947 C C   . ALA B 1 128 ? 72.762 11.336  -0.915  1.00 60.70  ?  128 ALA B C   1 
ATOM   2948 O O   . ALA B 1 128 ? 73.177 10.414  -0.204  1.00 61.50  ?  128 ALA B O   1 
ATOM   2949 C CB  . ALA B 1 128 ? 72.336 11.068  -3.365  1.00 43.91  ?  128 ALA B CB  1 
ATOM   2950 N N   . ASP B 1 129 ? 71.815 12.199  -0.533  1.00 65.45  ?  129 ASP B N   1 
ATOM   2951 C CA  . ASP B 1 129 ? 71.257 12.258  0.818   1.00 63.60  ?  129 ASP B CA  1 
ATOM   2952 C C   . ASP B 1 129 ? 69.756 12.006  0.749   1.00 54.00  ?  129 ASP B C   1 
ATOM   2953 O O   . ASP B 1 129 ? 69.029 12.758  0.088   1.00 54.63  ?  129 ASP B O   1 
ATOM   2954 C CB  . ASP B 1 129 ? 71.561 13.633  1.435   1.00 73.67  ?  129 ASP B CB  1 
ATOM   2955 C CG  . ASP B 1 129 ? 71.108 13.781  2.899   1.00 69.03  ?  129 ASP B CG  1 
ATOM   2956 O OD1 . ASP B 1 129 ? 70.178 13.088  3.365   1.00 55.26  ?  129 ASP B OD1 1 
ATOM   2957 O OD2 . ASP B 1 129 ? 71.721 14.630  3.588   1.00 69.25  -1 129 ASP B OD2 1 
ATOM   2958 N N   . ALA B 1 130 ? 69.282 10.976  1.453   1.00 46.67  ?  130 ALA B N   1 
ATOM   2959 C CA  . ALA B 1 130 ? 67.851 10.667  1.379   1.00 54.60  ?  130 ALA B CA  1 
ATOM   2960 C C   . ALA B 1 130 ? 66.954 11.793  1.892   1.00 57.96  ?  130 ALA B C   1 
ATOM   2961 O O   . ALA B 1 130 ? 65.729 11.720  1.693   1.00 56.97  ?  130 ALA B O   1 
ATOM   2962 C CB  . ALA B 1 130 ? 67.529 9.394   2.156   1.00 53.45  ?  130 ALA B CB  1 
ATOM   2963 N N   . MET B 1 131 ? 67.520 12.812  2.557   1.00 51.09  ?  131 MET B N   1 
ATOM   2964 C CA  . MET B 1 131 ? 66.730 13.970  2.971   1.00 53.97  ?  131 MET B CA  1 
ATOM   2965 C C   . MET B 1 131 ? 66.340 14.820  1.788   1.00 58.79  ?  131 MET B C   1 
ATOM   2966 O O   . MET B 1 131 ? 65.440 15.655  1.897   1.00 66.45  ?  131 MET B O   1 
ATOM   2967 C CB  . MET B 1 131 ? 67.502 14.830  3.967   1.00 49.93  ?  131 MET B CB  1 
ATOM   2968 C CG  . MET B 1 131 ? 67.724 14.194  5.344   1.00 61.39  ?  131 MET B CG  1 
ATOM   2969 S SD  . MET B 1 131 ? 66.213 14.133  6.341   1.00 69.87  ?  131 MET B SD  1 
ATOM   2970 C CE  . MET B 1 131 ? 65.927 15.888  6.621   1.00 60.50  ?  131 MET B CE  1 
ATOM   2971 N N   . ASP B 1 132 ? 67.025 14.637  0.668   1.00 66.62  ?  132 ASP B N   1 
ATOM   2972 C CA  . ASP B 1 132 ? 66.826 15.478  -0.502  1.00 68.43  ?  132 ASP B CA  1 
ATOM   2973 C C   . ASP B 1 132 ? 67.287 14.656  -1.702  1.00 60.49  ?  132 ASP B C   1 
ATOM   2974 O O   . ASP B 1 132 ? 68.474 14.683  -2.041  1.00 55.65  ?  132 ASP B O   1 
ATOM   2975 C CB  . ASP B 1 132 ? 67.633 16.749  -0.356  1.00 67.03  ?  132 ASP B CB  1 
ATOM   2976 C CG  . ASP B 1 132 ? 67.455 17.683  -1.511  1.00 75.74  ?  132 ASP B CG  1 
ATOM   2977 O OD1 . ASP B 1 132 ? 66.524 17.478  -2.317  1.00 75.09  ?  132 ASP B OD1 1 
ATOM   2978 O OD2 . ASP B 1 132 ? 68.264 18.620  -1.619  1.00 82.26  -1 132 ASP B OD2 1 
ATOM   2979 N N   . LEU B 1 133 ? 66.356 13.966  -2.345  1.00 51.07  ?  133 LEU B N   1 
ATOM   2980 C CA  . LEU B 1 133 ? 66.739 12.922  -3.294  1.00 57.75  ?  133 LEU B CA  1 
ATOM   2981 C C   . LEU B 1 133 ? 66.926 13.515  -4.681  1.00 51.72  ?  133 LEU B C   1 
ATOM   2982 O O   . LEU B 1 133 ? 65.971 14.078  -5.239  1.00 48.92  ?  133 LEU B O   1 
ATOM   2983 C CB  . LEU B 1 133 ? 65.694 11.799  -3.329  1.00 57.43  ?  133 LEU B CB  1 
ATOM   2984 C CG  . LEU B 1 133 ? 65.622 10.757  -2.177  1.00 49.25  ?  133 LEU B CG  1 
ATOM   2985 C CD1 . LEU B 1 133 ? 64.384 9.876   -2.299  1.00 45.88  ?  133 LEU B CD1 1 
ATOM   2986 C CD2 . LEU B 1 133 ? 66.835 9.873   -2.111  1.00 37.23  ?  133 LEU B CD2 1 
ATOM   2987 N N   . PRO B 1 134 ? 68.100 13.391  -5.290  1.00 49.31  ?  134 PRO B N   1 
ATOM   2988 C CA  . PRO B 1 134 ? 68.358 14.019  -6.604  1.00 48.80  ?  134 PRO B CA  1 
ATOM   2989 C C   . PRO B 1 134 ? 67.863 13.160  -7.768  1.00 49.44  ?  134 PRO B C   1 
ATOM   2990 O O   . PRO B 1 134 ? 68.594 12.856  -8.709  1.00 59.54  ?  134 PRO B O   1 
ATOM   2991 C CB  . PRO B 1 134 ? 69.888 14.203  -6.593  1.00 39.11  ?  134 PRO B CB  1 
ATOM   2992 C CG  . PRO B 1 134 ? 70.410 13.047  -5.744  1.00 45.01  ?  134 PRO B CG  1 
ATOM   2993 C CD  . PRO B 1 134 ? 69.289 12.699  -4.743  1.00 49.58  ?  134 PRO B CD  1 
ATOM   2994 N N   . PHE B 1 135 ? 66.592 12.787  -7.711  1.00 47.04  ?  135 PHE B N   1 
ATOM   2995 C CA  . PHE B 1 135 ? 65.977 11.932  -8.711  1.00 57.17  ?  135 PHE B CA  1 
ATOM   2996 C C   . PHE B 1 135 ? 64.594 12.467  -9.004  1.00 64.95  ?  135 PHE B C   1 
ATOM   2997 O O   . PHE B 1 135 ? 63.918 12.989  -8.112  1.00 55.21  ?  135 PHE B O   1 
ATOM   2998 C CB  . PHE B 1 135 ? 65.858 10.484  -8.238  1.00 54.91  ?  135 PHE B CB  1 
ATOM   2999 C CG  . PHE B 1 135 ? 67.145 9.901   -7.704  1.00 49.51  ?  135 PHE B CG  1 
ATOM   3000 C CD1 . PHE B 1 135 ? 68.216 9.668   -8.540  1.00 39.80  ?  135 PHE B CD1 1 
ATOM   3001 C CD2 . PHE B 1 135 ? 67.269 9.595   -6.368  1.00 39.98  ?  135 PHE B CD2 1 
ATOM   3002 C CE1 . PHE B 1 135 ? 69.382 9.125   -8.048  1.00 44.10  ?  135 PHE B CE1 1 
ATOM   3003 C CE2 . PHE B 1 135 ? 68.417 9.055   -5.876  1.00 47.91  ?  135 PHE B CE2 1 
ATOM   3004 C CZ  . PHE B 1 135 ? 69.482 8.813   -6.717  1.00 48.65  ?  135 PHE B CZ  1 
ATOM   3005 N N   . GLU B 1 136 ? 64.171 12.330  -10.252 1.00 62.07  ?  136 GLU B N   1 
ATOM   3006 C CA  . GLU B 1 136 ? 62.892 12.902  -10.616 1.00 60.41  ?  136 GLU B CA  1 
ATOM   3007 C C   . GLU B 1 136 ? 61.751 12.059  -10.057 1.00 61.66  ?  136 GLU B C   1 
ATOM   3008 O O   . GLU B 1 136 ? 61.914 10.880  -9.728  1.00 57.93  ?  136 GLU B O   1 
ATOM   3009 C CB  . GLU B 1 136 ? 62.802 13.059  -12.135 1.00 59.50  ?  136 GLU B CB  1 
ATOM   3010 C CG  . GLU B 1 136 ? 63.540 14.328  -12.543 1.00 58.78  ?  136 GLU B CG  1 
ATOM   3011 C CD  . GLU B 1 136 ? 63.124 14.868  -13.864 1.00 71.06  ?  136 GLU B CD  1 
ATOM   3012 O OE1 . GLU B 1 136 ? 62.780 14.065  -14.767 1.00 72.75  ?  136 GLU B OE1 1 
ATOM   3013 O OE2 . GLU B 1 136 ? 63.092 16.122  -13.973 1.00 86.16  -1 136 GLU B OE2 1 
ATOM   3014 N N   . ASP B 1 137 ? 60.592 12.700  -9.915  1.00 62.31  ?  137 ASP B N   1 
ATOM   3015 C CA  . ASP B 1 137 ? 59.390 12.005  -9.487  1.00 50.26  ?  137 ASP B CA  1 
ATOM   3016 C C   . ASP B 1 137 ? 59.201 10.707  -10.252 1.00 62.28  ?  137 ASP B C   1 
ATOM   3017 O O   . ASP B 1 137 ? 59.438 10.633  -11.466 1.00 75.42  ?  137 ASP B O   1 
ATOM   3018 C CB  . ASP B 1 137 ? 58.152 12.860  -9.731  1.00 55.35  ?  137 ASP B CB  1 
ATOM   3019 C CG  . ASP B 1 137 ? 58.173 14.158  -8.987  1.00 61.68  ?  137 ASP B CG  1 
ATOM   3020 O OD1 . ASP B 1 137 ? 59.180 14.446  -8.270  1.00 57.24  ?  137 ASP B OD1 1 
ATOM   3021 O OD2 . ASP B 1 137 ? 57.140 14.862  -9.127  1.00 58.50  -1 137 ASP B OD2 1 
ATOM   3022 N N   . GLU B 1 138 ? 58.711 9.694   -9.536  1.00 56.62  ?  138 GLU B N   1 
ATOM   3023 C CA  . GLU B 1 138 ? 58.226 8.461   -10.155 1.00 55.63  ?  138 GLU B CA  1 
ATOM   3024 C C   . GLU B 1 138 ? 59.290 7.802   -11.018 1.00 51.13  ?  138 GLU B C   1 
ATOM   3025 O O   . GLU B 1 138 ? 58.991 7.207   -12.045 1.00 55.40  ?  138 GLU B O   1 
ATOM   3026 C CB  . GLU B 1 138 ? 56.961 8.709   -10.976 1.00 51.85  ?  138 GLU B CB  1 
ATOM   3027 C CG  . GLU B 1 138 ? 55.844 9.342   -10.178 1.00 52.00  ?  138 GLU B CG  1 
ATOM   3028 C CD  . GLU B 1 138 ? 54.549 9.413   -10.950 1.00 61.64  ?  138 GLU B CD  1 
ATOM   3029 O OE1 . GLU B 1 138 ? 54.372 8.626   -11.908 1.00 61.50  ?  138 GLU B OE1 1 
ATOM   3030 O OE2 . GLU B 1 138 ? 53.709 10.263  -10.587 1.00 68.89  -1 138 GLU B OE2 1 
ATOM   3031 N N   . SER B 1 139 ? 60.532 7.850   -10.556 1.00 50.90  ?  139 SER B N   1 
ATOM   3032 C CA  . SER B 1 139 ? 61.651 7.198   -11.218 1.00 53.74  ?  139 SER B CA  1 
ATOM   3033 C C   . SER B 1 139 ? 61.965 5.796   -10.701 1.00 50.50  ?  139 SER B C   1 
ATOM   3034 O O   . SER B 1 139 ? 62.841 5.134   -11.265 1.00 55.76  ?  139 SER B O   1 
ATOM   3035 C CB  . SER B 1 139 ? 62.893 8.081   -11.086 1.00 62.09  ?  139 SER B CB  1 
ATOM   3036 O OG  . SER B 1 139 ? 62.894 8.747   -9.846  1.00 59.55  ?  139 SER B OG  1 
ATOM   3037 N N   . PHE B 1 140 ? 61.289 5.314   -9.655  1.00 49.76  ?  140 PHE B N   1 
ATOM   3038 C CA  . PHE B 1 140 ? 61.638 4.016   -9.088  1.00 52.26  ?  140 PHE B CA  1 
ATOM   3039 C C   . PHE B 1 140 ? 60.425 3.104   -8.912  1.00 56.68  ?  140 PHE B C   1 
ATOM   3040 O O   . PHE B 1 140 ? 59.318 3.549   -8.555  1.00 53.88  ?  140 PHE B O   1 
ATOM   3041 C CB  . PHE B 1 140 ? 62.371 4.195   -7.770  1.00 43.62  ?  140 PHE B CB  1 
ATOM   3042 C CG  . PHE B 1 140 ? 63.756 4.718   -7.948  1.00 46.89  ?  140 PHE B CG  1 
ATOM   3043 C CD1 . PHE B 1 140 ? 64.722 3.928   -8.536  1.00 42.79  ?  140 PHE B CD1 1 
ATOM   3044 C CD2 . PHE B 1 140 ? 64.074 6.011   -7.581  1.00 41.90  ?  140 PHE B CD2 1 
ATOM   3045 C CE1 . PHE B 1 140 ? 65.988 4.387   -8.728  1.00 43.38  ?  140 PHE B CE1 1 
ATOM   3046 C CE2 . PHE B 1 140 ? 65.340 6.487   -7.782  1.00 51.69  ?  140 PHE B CE2 1 
ATOM   3047 C CZ  . PHE B 1 140 ? 66.305 5.670   -8.365  1.00 49.25  ?  140 PHE B CZ  1 
ATOM   3048 N N   . ASP B 1 141 ? 60.664 1.810   -9.180  1.00 52.88  ?  141 ASP B N   1 
ATOM   3049 C CA  . ASP B 1 141 ? 59.657 0.766   -9.031  1.00 51.17  ?  141 ASP B CA  1 
ATOM   3050 C C   . ASP B 1 141 ? 59.552 0.299   -7.590  1.00 47.67  ?  141 ASP B C   1 
ATOM   3051 O O   . ASP B 1 141 ? 58.486 -0.159  -7.162  1.00 48.57  ?  141 ASP B O   1 
ATOM   3052 C CB  . ASP B 1 141 ? 60.004 -0.429  -9.916  1.00 46.75  ?  141 ASP B CB  1 
ATOM   3053 C CG  . ASP B 1 141 ? 59.912 -0.120  -11.391 1.00 51.84  ?  141 ASP B CG  1 
ATOM   3054 O OD1 . ASP B 1 141 ? 58.892 0.477   -11.796 1.00 57.33  ?  141 ASP B OD1 1 
ATOM   3055 O OD2 . ASP B 1 141 ? 60.868 -0.477  -12.127 1.00 53.37  -1 141 ASP B OD2 1 
ATOM   3056 N N   . ALA B 1 142 ? 60.641 0.437   -6.840  1.00 42.50  ?  142 ALA B N   1 
ATOM   3057 C CA  . ALA B 1 142 ? 60.756 -0.063  -5.491  1.00 37.67  ?  142 ALA B CA  1 
ATOM   3058 C C   . ALA B 1 142 ? 61.873 0.703   -4.816  1.00 50.61  ?  142 ALA B C   1 
ATOM   3059 O O   . ALA B 1 142 ? 62.789 1.209   -5.485  1.00 54.25  ?  142 ALA B O   1 
ATOM   3060 C CB  . ALA B 1 142 ? 61.046 -1.563  -5.485  1.00 38.58  ?  142 ALA B CB  1 
ATOM   3061 N N   . VAL B 1 143 ? 61.787 0.788   -3.484  1.00 48.86  ?  143 VAL B N   1 
ATOM   3062 C CA  . VAL B 1 143 ? 62.834 1.354   -2.640  1.00 41.80  ?  143 VAL B CA  1 
ATOM   3063 C C   . VAL B 1 143 ? 63.075 0.412   -1.473  1.00 43.74  ?  143 VAL B C   1 
ATOM   3064 O O   . VAL B 1 143 ? 62.124 -0.027  -0.817  1.00 51.37  ?  143 VAL B O   1 
ATOM   3065 C CB  . VAL B 1 143 ? 62.444 2.742   -2.124  1.00 40.91  ?  143 VAL B CB  1 
ATOM   3066 C CG1 . VAL B 1 143 ? 63.446 3.193   -1.079  1.00 45.34  ?  143 VAL B CG1 1 
ATOM   3067 C CG2 . VAL B 1 143 ? 62.325 3.720   -3.280  1.00 34.76  ?  143 VAL B CG2 1 
ATOM   3068 N N   . ILE B 1 144 ? 64.330 0.079   -1.220  1.00 41.67  ?  144 ILE B N   1 
ATOM   3069 C CA  . ILE B 1 144 ? 64.705 -0.686  -0.041  1.00 39.97  ?  144 ILE B CA  1 
ATOM   3070 C C   . ILE B 1 144 ? 65.582 0.198   0.845   1.00 40.68  ?  144 ILE B C   1 
ATOM   3071 O O   . ILE B 1 144 ? 66.532 0.831   0.371   1.00 46.47  ?  144 ILE B O   1 
ATOM   3072 C CB  . ILE B 1 144 ? 65.415 -1.999  -0.428  1.00 47.38  ?  144 ILE B CB  1 
ATOM   3073 C CG1 . ILE B 1 144 ? 65.802 -2.807  0.827   1.00 53.57  ?  144 ILE B CG1 1 
ATOM   3074 C CG2 . ILE B 1 144 ? 66.619 -1.741  -1.299  1.00 36.37  ?  144 ILE B CG2 1 
ATOM   3075 C CD1 . ILE B 1 144 ? 66.330 -4.198  0.507   1.00 51.20  ?  144 ILE B CD1 1 
ATOM   3076 N N   . ALA B 1 145 ? 65.257 0.266   2.126   1.00 40.42  ?  145 ALA B N   1 
ATOM   3077 C CA  . ALA B 1 145 ? 66.129 0.939   3.088   1.00 44.54  ?  145 ALA B CA  1 
ATOM   3078 C C   . ALA B 1 145 ? 66.465 -0.127  4.114   1.00 49.39  ?  145 ALA B C   1 
ATOM   3079 O O   . ALA B 1 145 ? 65.686 -0.415  5.025   1.00 61.28  ?  145 ALA B O   1 
ATOM   3080 C CB  . ALA B 1 145 ? 65.498 2.161   3.701   1.00 33.82  ?  145 ALA B CB  1 
ATOM   3081 N N   . LEU B 1 146 ? 67.621 -0.741  3.943   1.00 48.02  ?  146 LEU B N   1 
ATOM   3082 C CA  . LEU B 1 146 ? 68.018 -1.853  4.780   1.00 47.73  ?  146 LEU B CA  1 
ATOM   3083 C C   . LEU B 1 146 ? 68.891 -1.308  5.909   1.00 49.29  ?  146 LEU B C   1 
ATOM   3084 O O   . LEU B 1 146 ? 70.007 -0.844  5.652   1.00 50.46  ?  146 LEU B O   1 
ATOM   3085 C CB  . LEU B 1 146 ? 68.742 -2.877  3.916   1.00 52.17  ?  146 LEU B CB  1 
ATOM   3086 C CG  . LEU B 1 146 ? 68.684 -4.327  4.348   1.00 55.02  ?  146 LEU B CG  1 
ATOM   3087 C CD1 . LEU B 1 146 ? 69.561 -5.112  3.392   1.00 61.15  ?  146 LEU B CD1 1 
ATOM   3088 C CD2 . LEU B 1 146 ? 69.059 -4.551  5.817   1.00 42.37  ?  146 LEU B CD2 1 
ATOM   3089 N N   . GLU B 1 147 ? 68.374 -1.359  7.149   1.00 47.84  ?  147 GLU B N   1 
ATOM   3090 C CA  . GLU B 1 147 ? 69.037 -0.834  8.367   1.00 52.72  ?  147 GLU B CA  1 
ATOM   3091 C C   . GLU B 1 147 ? 69.638 0.546   8.176   1.00 60.82  ?  147 GLU B C   1 
ATOM   3092 O O   . GLU B 1 147 ? 70.799 0.801   8.502   1.00 60.77  ?  147 GLU B O   1 
ATOM   3093 C CB  . GLU B 1 147 ? 70.118 -1.757  8.870   1.00 52.24  ?  147 GLU B CB  1 
ATOM   3094 C CG  . GLU B 1 147 ? 69.687 -2.522  10.015  1.00 62.17  ?  147 GLU B CG  1 
ATOM   3095 C CD  . GLU B 1 147 ? 70.785 -3.321  10.643  1.00 78.20  ?  147 GLU B CD  1 
ATOM   3096 O OE1 . GLU B 1 147 ? 71.950 -2.861  10.748  1.00 81.84  ?  147 GLU B OE1 1 
ATOM   3097 O OE2 . GLU B 1 147 ? 70.488 -4.496  10.916  1.00 86.75  -1 147 GLU B OE2 1 
ATOM   3098 N N   . SER B 1 148 ? 68.859 1.433   7.628   1.00 64.82  ?  148 SER B N   1 
ATOM   3099 C CA  . SER B 1 148 ? 69.455 2.700   7.256   1.00 57.01  ?  148 SER B CA  1 
ATOM   3100 C C   . SER B 1 148 ? 68.621 3.913   7.641   1.00 54.84  ?  148 SER B C   1 
ATOM   3101 O O   . SER B 1 148 ? 69.209 4.964   7.914   1.00 51.17  ?  148 SER B O   1 
ATOM   3102 C CB  . SER B 1 148 ? 69.735 2.702   5.732   1.00 48.10  ?  148 SER B CB  1 
ATOM   3103 O OG  . SER B 1 148 ? 68.537 2.815   4.981   1.00 48.12  ?  148 SER B OG  1 
ATOM   3104 N N   . ILE B 1 149 ? 67.288 3.815   7.700   1.00 58.43  ?  149 ILE B N   1 
ATOM   3105 C CA  . ILE B 1 149 ? 66.498 4.948   8.168   1.00 60.66  ?  149 ILE B CA  1 
ATOM   3106 C C   . ILE B 1 149 ? 66.780 5.234   9.637   1.00 62.83  ?  149 ILE B C   1 
ATOM   3107 O O   . ILE B 1 149 ? 66.512 6.336   10.110  1.00 60.54  ?  149 ILE B O   1 
ATOM   3108 C CB  . ILE B 1 149 ? 64.996 4.717   7.936   1.00 54.35  ?  149 ILE B CB  1 
ATOM   3109 C CG1 . ILE B 1 149 ? 64.275 6.055   7.782   1.00 52.57  ?  149 ILE B CG1 1 
ATOM   3110 C CG2 . ILE B 1 149 ? 64.397 3.918   9.072   1.00 57.57  ?  149 ILE B CG2 1 
ATOM   3111 C CD1 . ILE B 1 149 ? 62.820 5.925   7.379   1.00 56.45  ?  149 ILE B CD1 1 
ATOM   3112 N N   . ILE B 1 150 ? 67.333 4.261   10.365  1.00 67.55  ?  150 ILE B N   1 
ATOM   3113 C CA  . ILE B 1 150 ? 67.754 4.472   11.748  1.00 71.92  ?  150 ILE B CA  1 
ATOM   3114 C C   . ILE B 1 150 ? 68.719 5.652   11.845  1.00 73.12  ?  150 ILE B C   1 
ATOM   3115 O O   . ILE B 1 150 ? 68.614 6.493   12.750  1.00 74.05  ?  150 ILE B O   1 
ATOM   3116 C CB  . ILE B 1 150 ? 68.380 3.176   12.315  1.00 69.25  ?  150 ILE B CB  1 
ATOM   3117 C CG1 . ILE B 1 150 ? 69.504 2.674   11.411  1.00 66.71  ?  150 ILE B CG1 1 
ATOM   3118 C CG2 . ILE B 1 150 ? 67.340 2.083   12.465  1.00 64.48  ?  150 ILE B CG2 1 
ATOM   3119 C CD1 . ILE B 1 150 ? 70.164 1.411   11.893  1.00 71.39  ?  150 ILE B CD1 1 
ATOM   3120 N N   . HIS B 1 151 ? 69.679 5.730   10.924  1.00 66.04  ?  151 HIS B N   1 
ATOM   3121 C CA  . HIS B 1 151 ? 70.678 6.784   10.923  1.00 64.88  ?  151 HIS B CA  1 
ATOM   3122 C C   . HIS B 1 151 ? 70.170 8.079   10.308  1.00 68.41  ?  151 HIS B C   1 
ATOM   3123 O O   . HIS B 1 151 ? 70.967 8.993   10.096  1.00 70.45  ?  151 HIS B O   1 
ATOM   3124 C CB  . HIS B 1 151 ? 71.929 6.349   10.161  1.00 58.71  ?  151 HIS B CB  1 
ATOM   3125 C CG  . HIS B 1 151 ? 72.644 5.175   10.752  1.00 74.47  ?  151 HIS B CG  1 
ATOM   3126 N ND1 . HIS B 1 151 ? 72.462 3.888   10.296  1.00 78.84  ?  151 HIS B ND1 1 
ATOM   3127 C CD2 . HIS B 1 151 ? 73.580 5.097   11.727  1.00 81.14  ?  151 HIS B CD2 1 
ATOM   3128 C CE1 . HIS B 1 151 ? 73.244 3.064   10.973  1.00 79.51  ?  151 HIS B CE1 1 
ATOM   3129 N NE2 . HIS B 1 151 ? 73.933 3.773   11.847  1.00 79.35  ?  151 HIS B NE2 1 
ATOM   3130 N N   . MET B 1 152 ? 68.923 8.182   10.013  1.00 68.20  ?  152 MET B N   1 
ATOM   3131 C CA  . MET B 1 152 ? 68.639 9.391   9.261   1.00 69.03  ?  152 MET B CA  1 
ATOM   3132 C C   . MET B 1 152 ? 67.962 10.424  10.145  1.00 78.02  ?  152 MET B C   1 
ATOM   3133 O O   . MET B 1 152 ? 67.250 10.070  11.090  1.00 89.69  ?  152 MET B O   1 
ATOM   3134 C CB  . MET B 1 152 ? 67.760 9.086   8.047   1.00 58.47  ?  152 MET B CB  1 
ATOM   3135 C CG  . MET B 1 152 ? 68.483 8.202   7.054   1.00 56.68  ?  152 MET B CG  1 
ATOM   3136 S SD  . MET B 1 152 ? 67.566 7.790   5.561   1.00 67.73  ?  152 MET B SD  1 
ATOM   3137 C CE  . MET B 1 152 ? 68.672 6.565   4.839   1.00 67.88  ?  152 MET B CE  1 
ATOM   3138 N N   . PRO B 1 153 ? 68.198 11.713  9.881   1.00 81.19  ?  153 PRO B N   1 
ATOM   3139 C CA  . PRO B 1 153 ? 67.710 12.747  10.810  1.00 84.76  ?  153 PRO B CA  1 
ATOM   3140 C C   . PRO B 1 153 ? 66.201 12.732  11.027  1.00 78.76  ?  153 PRO B C   1 
ATOM   3141 O O   . PRO B 1 153 ? 65.746 12.412  12.130  1.00 82.64  ?  153 PRO B O   1 
ATOM   3142 C CB  . PRO B 1 153 ? 68.179 14.061  10.154  1.00 83.65  ?  153 PRO B CB  1 
ATOM   3143 C CG  . PRO B 1 153 ? 68.747 13.676  8.778   1.00 77.82  ?  153 PRO B CG  1 
ATOM   3144 C CD  . PRO B 1 153 ? 69.165 12.248  8.901   1.00 72.58  ?  153 PRO B CD  1 
ATOM   3145 N N   . ASP B 1 154 ? 65.413 12.981  9.984   1.00 67.86  ?  154 ASP B N   1 
ATOM   3146 C CA  . ASP B 1 154 ? 63.966 13.103  10.115  1.00 57.97  ?  154 ASP B CA  1 
ATOM   3147 C C   . ASP B 1 154 ? 63.264 12.036  9.271   1.00 61.28  ?  154 ASP B C   1 
ATOM   3148 O O   . ASP B 1 154 ? 63.239 12.124  8.035   1.00 64.63  ?  154 ASP B O   1 
ATOM   3149 C CB  . ASP B 1 154 ? 63.506 14.497  9.710   1.00 49.70  ?  154 ASP B CB  1 
ATOM   3150 C CG  . ASP B 1 154 ? 62.002 14.595  9.641   1.00 73.99  ?  154 ASP B CG  1 
ATOM   3151 O OD1 . ASP B 1 154 ? 61.364 14.298  10.665  1.00 85.62  ?  154 ASP B OD1 1 
ATOM   3152 O OD2 . ASP B 1 154 ? 61.446 14.939  8.575   1.00 85.77  -1 154 ASP B OD2 1 
ATOM   3153 N N   . ARG B 1 155 ? 62.676 11.036  9.935   1.00 58.70  ?  155 ARG B N   1 
ATOM   3154 C CA  . ARG B 1 155 ? 61.941 10.012  9.202   1.00 52.97  ?  155 ARG B CA  1 
ATOM   3155 C C   . ARG B 1 155 ? 60.846 10.607  8.328   1.00 59.25  ?  155 ARG B C   1 
ATOM   3156 O O   . ARG B 1 155 ? 60.586 10.093  7.231   1.00 59.68  ?  155 ARG B O   1 
ATOM   3157 C CB  . ARG B 1 155 ? 61.354 8.978   10.164  1.00 46.72  ?  155 ARG B CB  1 
ATOM   3158 C CG  . ARG B 1 155 ? 62.377 7.940   10.598  1.00 57.47  ?  155 ARG B CG  1 
ATOM   3159 C CD  . ARG B 1 155 ? 61.873 7.135   11.756  1.00 71.22  ?  155 ARG B CD  1 
ATOM   3160 N NE  . ARG B 1 155 ? 62.825 7.160   12.873  1.00 78.16  ?  155 ARG B NE  1 
ATOM   3161 C CZ  . ARG B 1 155 ? 63.694 6.194   13.116  1.00 77.73  ?  155 ARG B CZ  1 
ATOM   3162 N NH1 . ARG B 1 155 ? 63.719 5.137   12.333  1.00 78.50  ?  155 ARG B NH1 1 
ATOM   3163 N NH2 . ARG B 1 155 ? 64.531 6.272   14.131  1.00 74.22  ?  155 ARG B NH2 1 
ATOM   3164 N N   . ALA B 1 156 ? 60.196 11.687  8.772   1.00 66.05  ?  156 ALA B N   1 
ATOM   3165 C CA  . ALA B 1 156 ? 59.103 12.232  7.965   1.00 58.69  ?  156 ALA B CA  1 
ATOM   3166 C C   . ALA B 1 156 ? 59.606 12.732  6.614   1.00 65.28  ?  156 ALA B C   1 
ATOM   3167 O O   . ALA B 1 156 ? 58.963 12.497  5.585   1.00 56.32  ?  156 ALA B O   1 
ATOM   3168 C CB  . ALA B 1 156 ? 58.382 13.349  8.711   1.00 48.78  ?  156 ALA B CB  1 
ATOM   3169 N N   . GLN B 1 157 ? 60.762 13.405  6.588   1.00 66.39  ?  157 GLN B N   1 
ATOM   3170 C CA  . GLN B 1 157 ? 61.236 13.978  5.329   1.00 64.28  ?  157 GLN B CA  1 
ATOM   3171 C C   . GLN B 1 157 ? 61.660 12.883  4.359   1.00 64.64  ?  157 GLN B C   1 
ATOM   3172 O O   . GLN B 1 157 ? 61.230 12.854  3.194   1.00 47.57  ?  157 GLN B O   1 
ATOM   3173 C CB  . GLN B 1 157 ? 62.391 14.936  5.592   1.00 47.39  ?  157 GLN B CB  1 
ATOM   3174 C CG  . GLN B 1 157 ? 61.912 16.282  5.978   1.00 75.56  ?  157 GLN B CG  1 
ATOM   3175 C CD  . GLN B 1 157 ? 62.773 17.366  5.414   1.00 89.15  ?  157 GLN B CD  1 
ATOM   3176 O OE1 . GLN B 1 157 ? 63.651 17.110  4.584   1.00 86.42  ?  157 GLN B OE1 1 
ATOM   3177 N NE2 . GLN B 1 157 ? 62.536 18.596  5.864   1.00 89.81  ?  157 GLN B NE2 1 
ATOM   3178 N N   . VAL B 1 158 ? 62.524 11.987  4.842   1.00 58.01  ?  158 VAL B N   1 
ATOM   3179 C CA  . VAL B 1 158 ? 62.940 10.817  4.090   1.00 51.49  ?  158 VAL B CA  1 
ATOM   3180 C C   . VAL B 1 158 ? 61.734 10.108  3.482   1.00 54.74  ?  158 VAL B C   1 
ATOM   3181 O O   . VAL B 1 158 ? 61.693 9.854   2.270   1.00 51.75  ?  158 VAL B O   1 
ATOM   3182 C CB  . VAL B 1 158 ? 63.756 9.889   4.997   1.00 49.00  ?  158 VAL B CB  1 
ATOM   3183 C CG1 . VAL B 1 158 ? 64.069 8.620   4.295   1.00 44.73  ?  158 VAL B CG1 1 
ATOM   3184 C CG2 . VAL B 1 158 ? 65.015 10.594  5.402   1.00 54.95  ?  158 VAL B CG2 1 
ATOM   3185 N N   . LEU B 1 159 ? 60.713 9.820   4.302   1.00 55.29  ?  159 LEU B N   1 
ATOM   3186 C CA  . LEU B 1 159 ? 59.543 9.114   3.780   1.00 53.68  ?  159 LEU B CA  1 
ATOM   3187 C C   . LEU B 1 159 ? 58.818 9.906   2.694   1.00 55.02  ?  159 LEU B C   1 
ATOM   3188 O O   . LEU B 1 159 ? 58.307 9.314   1.742   1.00 60.69  ?  159 LEU B O   1 
ATOM   3189 C CB  . LEU B 1 159 ? 58.580 8.746   4.910   1.00 49.97  ?  159 LEU B CB  1 
ATOM   3190 C CG  . LEU B 1 159 ? 59.126 7.594   5.781   1.00 46.77  ?  159 LEU B CG  1 
ATOM   3191 C CD1 . LEU B 1 159 ? 58.243 7.289   6.993   1.00 46.39  ?  159 LEU B CD1 1 
ATOM   3192 C CD2 . LEU B 1 159 ? 59.352 6.357   4.952   1.00 38.69  ?  159 LEU B CD2 1 
ATOM   3193 N N   . ALA B 1 160 ? 58.767 11.234  2.791   1.00 62.05  ?  160 ALA B N   1 
ATOM   3194 C CA  . ALA B 1 160 ? 58.181 12.020  1.703   1.00 53.71  ?  160 ALA B CA  1 
ATOM   3195 C C   . ALA B 1 160 ? 59.036 11.981  0.436   1.00 51.31  ?  160 ALA B C   1 
ATOM   3196 O O   . ALA B 1 160 ? 58.497 12.009  -0.674  1.00 52.21  ?  160 ALA B O   1 
ATOM   3197 C CB  . ALA B 1 160 ? 57.991 13.470  2.149   1.00 44.59  ?  160 ALA B CB  1 
ATOM   3198 N N   . GLN B 1 161 ? 60.359 11.965  0.581   1.00 44.00  ?  161 GLN B N   1 
ATOM   3199 C CA  . GLN B 1 161 ? 61.220 11.813  -0.579  1.00 55.86  ?  161 GLN B CA  1 
ATOM   3200 C C   . GLN B 1 161 ? 60.962 10.470  -1.268  1.00 55.15  ?  161 GLN B C   1 
ATOM   3201 O O   . GLN B 1 161 ? 60.794 10.409  -2.496  1.00 55.21  ?  161 GLN B O   1 
ATOM   3202 C CB  . GLN B 1 161 ? 62.690 11.943  -0.152  1.00 54.36  ?  161 GLN B CB  1 
ATOM   3203 C CG  . GLN B 1 161 ? 63.078 13.317  0.282   1.00 58.22  ?  161 GLN B CG  1 
ATOM   3204 C CD  . GLN B 1 161 ? 62.781 14.347  -0.776  1.00 57.40  ?  161 GLN B CD  1 
ATOM   3205 O OE1 . GLN B 1 161 ? 63.146 14.181  -1.944  1.00 57.59  ?  161 GLN B OE1 1 
ATOM   3206 N NE2 . GLN B 1 161 ? 62.101 15.412  -0.383  1.00 45.00  ?  161 GLN B NE2 1 
ATOM   3207 N N   . VAL B 1 162 ? 60.918 9.385   -0.480  1.00 51.65  ?  162 VAL B N   1 
ATOM   3208 C CA  . VAL B 1 162 ? 60.627 8.058   -1.020  1.00 51.33  ?  162 VAL B CA  1 
ATOM   3209 C C   . VAL B 1 162 ? 59.299 8.071   -1.757  1.00 51.25  ?  162 VAL B C   1 
ATOM   3210 O O   . VAL B 1 162 ? 59.189 7.571   -2.880  1.00 56.80  ?  162 VAL B O   1 
ATOM   3211 C CB  . VAL B 1 162 ? 60.633 6.999   0.100   1.00 41.20  ?  162 VAL B CB  1 
ATOM   3212 C CG1 . VAL B 1 162 ? 60.156 5.643   -0.434  1.00 41.06  ?  162 VAL B CG1 1 
ATOM   3213 C CG2 . VAL B 1 162 ? 62.003 6.849   0.674   1.00 35.30  ?  162 VAL B CG2 1 
ATOM   3214 N N   . GLY B 1 163 ? 58.270 8.646   -1.139  1.00 44.55  ?  163 GLY B N   1 
ATOM   3215 C CA  . GLY B 1 163 ? 56.965 8.646   -1.763  1.00 49.82  ?  163 GLY B CA  1 
ATOM   3216 C C   . GLY B 1 163 ? 56.878 9.474   -3.027  1.00 53.24  ?  163 GLY B C   1 
ATOM   3217 O O   . GLY B 1 163 ? 55.958 9.267   -3.828  1.00 57.43  ?  163 GLY B O   1 
ATOM   3218 N N   . ARG B 1 164 ? 57.796 10.418  -3.220  1.00 44.96  ?  164 ARG B N   1 
ATOM   3219 C CA  . ARG B 1 164 ? 57.776 11.217  -4.440  1.00 45.94  ?  164 ARG B CA  1 
ATOM   3220 C C   . ARG B 1 164 ? 58.420 10.450  -5.594  1.00 50.83  ?  164 ARG B C   1 
ATOM   3221 O O   . ARG B 1 164 ? 57.879 10.401  -6.704  1.00 59.07  ?  164 ARG B O   1 
ATOM   3222 C CB  . ARG B 1 164 ? 58.484 12.554  -4.177  1.00 39.79  ?  164 ARG B CB  1 
ATOM   3223 C CG  . ARG B 1 164 ? 58.609 13.499  -5.361  1.00 40.45  ?  164 ARG B CG  1 
ATOM   3224 C CD  . ARG B 1 164 ? 59.465 14.720  -5.024  1.00 48.45  ?  164 ARG B CD  1 
ATOM   3225 N NE  . ARG B 1 164 ? 60.838 14.406  -4.614  1.00 49.72  ?  164 ARG B NE  1 
ATOM   3226 C CZ  . ARG B 1 164 ? 61.827 14.148  -5.463  1.00 49.22  ?  164 ARG B CZ  1 
ATOM   3227 N NH1 . ARG B 1 164 ? 61.582 14.162  -6.758  1.00 44.34  ?  164 ARG B NH1 1 
ATOM   3228 N NH2 . ARG B 1 164 ? 63.050 13.856  -5.019  1.00 48.83  ?  164 ARG B NH2 1 
ATOM   3229 N N   . VAL B 1 165 ? 59.567 9.822   -5.328  1.00 46.53  ?  165 VAL B N   1 
ATOM   3230 C CA  . VAL B 1 165 ? 60.313 9.094   -6.342  1.00 43.78  ?  165 VAL B CA  1 
ATOM   3231 C C   . VAL B 1 165 ? 59.735 7.712   -6.621  1.00 52.86  ?  165 VAL B C   1 
ATOM   3232 O O   . VAL B 1 165 ? 60.092 7.100   -7.635  1.00 65.89  ?  165 VAL B O   1 
ATOM   3233 C CB  . VAL B 1 165 ? 61.793 8.967   -5.935  1.00 43.28  ?  165 VAL B CB  1 
ATOM   3234 C CG1 . VAL B 1 165 ? 62.419 10.327  -5.772  1.00 41.98  ?  165 VAL B CG1 1 
ATOM   3235 C CG2 . VAL B 1 165 ? 61.945 8.197   -4.630  1.00 48.56  ?  165 VAL B CG2 1 
ATOM   3236 N N   . LEU B 1 166 ? 58.881 7.179   -5.745  1.00 46.90  ?  166 LEU B N   1 
ATOM   3237 C CA  . LEU B 1 166 ? 58.257 5.891   -6.006  1.00 46.23  ?  166 LEU B CA  1 
ATOM   3238 C C   . LEU B 1 166 ? 57.202 6.048   -7.092  1.00 51.76  ?  166 LEU B C   1 
ATOM   3239 O O   . LEU B 1 166 ? 56.386 6.970   -7.034  1.00 55.26  ?  166 LEU B O   1 
ATOM   3240 C CB  . LEU B 1 166 ? 57.619 5.333   -4.734  1.00 48.47  ?  166 LEU B CB  1 
ATOM   3241 C CG  . LEU B 1 166 ? 58.265 4.133   -4.024  1.00 50.58  ?  166 LEU B CG  1 
ATOM   3242 C CD1 . LEU B 1 166 ? 57.567 3.764   -2.722  1.00 47.55  ?  166 LEU B CD1 1 
ATOM   3243 C CD2 . LEU B 1 166 ? 58.285 2.938   -4.941  1.00 59.92  ?  166 LEU B CD2 1 
ATOM   3244 N N   . ARG B 1 167 ? 57.221 5.161   -8.090  1.00 48.42  ?  167 ARG B N   1 
ATOM   3245 C CA  . ARG B 1 167 ? 56.128 5.134   -9.050  1.00 54.35  ?  167 ARG B CA  1 
ATOM   3246 C C   . ARG B 1 167 ? 54.861 4.635   -8.363  1.00 53.30  ?  167 ARG B C   1 
ATOM   3247 O O   . ARG B 1 167 ? 54.939 3.987   -7.326  1.00 61.83  ?  167 ARG B O   1 
ATOM   3248 C CB  . ARG B 1 167 ? 56.489 4.247   -10.240 1.00 61.26  ?  167 ARG B CB  1 
ATOM   3249 C CG  . ARG B 1 167 ? 57.732 4.719   -10.981 1.00 49.65  ?  167 ARG B CG  1 
ATOM   3250 C CD  . ARG B 1 167 ? 58.242 3.747   -11.993 1.00 47.54  ?  167 ARG B CD  1 
ATOM   3251 N NE  . ARG B 1 167 ? 59.204 4.416   -12.865 1.00 62.65  ?  167 ARG B NE  1 
ATOM   3252 C CZ  . ARG B 1 167 ? 60.132 3.783   -13.573 1.00 56.52  ?  167 ARG B CZ  1 
ATOM   3253 N NH1 . ARG B 1 167 ? 60.208 2.464   -13.485 1.00 52.19  ?  167 ARG B NH1 1 
ATOM   3254 N NH2 . ARG B 1 167 ? 60.989 4.474   -14.326 1.00 48.65  ?  167 ARG B NH2 1 
ATOM   3255 N N   . PRO B 1 168 ? 53.681 4.957   -8.886  1.00 55.38  ?  168 PRO B N   1 
ATOM   3256 C CA  . PRO B 1 168 ? 52.450 4.430   -8.268  1.00 56.22  ?  168 PRO B CA  1 
ATOM   3257 C C   . PRO B 1 168 ? 52.383 2.913   -8.389  1.00 56.27  ?  168 PRO B C   1 
ATOM   3258 O O   . PRO B 1 168 ? 52.715 2.332   -9.425  1.00 49.09  ?  168 PRO B O   1 
ATOM   3259 C CB  . PRO B 1 168 ? 51.317 5.112   -9.051  1.00 46.97  ?  168 PRO B CB  1 
ATOM   3260 C CG  . PRO B 1 168 ? 51.957 6.343   -9.627  1.00 51.74  ?  168 PRO B CG  1 
ATOM   3261 C CD  . PRO B 1 168 ? 53.386 5.939   -9.941  1.00 55.36  ?  168 PRO B CD  1 
ATOM   3262 N N   . GLY B 1 169 ? 51.980 2.273   -7.291  1.00 58.49  ?  169 GLY B N   1 
ATOM   3263 C CA  . GLY B 1 169 ? 52.103 0.841   -7.131  1.00 51.47  ?  169 GLY B CA  1 
ATOM   3264 C C   . GLY B 1 169 ? 53.463 0.384   -6.654  1.00 49.68  ?  169 GLY B C   1 
ATOM   3265 O O   . GLY B 1 169 ? 53.638 -0.808  -6.395  1.00 52.86  ?  169 GLY B O   1 
ATOM   3266 N N   . GLY B 1 170 ? 54.438 1.280   -6.546  1.00 44.75  ?  170 GLY B N   1 
ATOM   3267 C CA  . GLY B 1 170 ? 55.734 0.903   -6.028  1.00 46.91  ?  170 GLY B CA  1 
ATOM   3268 C C   . GLY B 1 170 ? 55.654 0.565   -4.550  1.00 49.49  ?  170 GLY B C   1 
ATOM   3269 O O   . GLY B 1 170 ? 54.652 0.804   -3.890  1.00 52.68  ?  170 GLY B O   1 
ATOM   3270 N N   . ARG B 1 171 ? 56.725 -0.016  -4.021  1.00 42.80  ?  171 ARG B N   1 
ATOM   3271 C CA  . ARG B 1 171 ? 56.745 -0.471  -2.641  1.00 41.77  ?  171 ARG B CA  1 
ATOM   3272 C C   . ARG B 1 171 ? 58.053 -0.081  -1.987  1.00 44.42  ?  171 ARG B C   1 
ATOM   3273 O O   . ARG B 1 171 ? 59.125 -0.171  -2.600  1.00 46.95  ?  171 ARG B O   1 
ATOM   3274 C CB  . ARG B 1 171 ? 56.548 -2.015  -2.499  1.00 40.39  ?  171 ARG B CB  1 
ATOM   3275 C CG  . ARG B 1 171 ? 55.094 -2.482  -2.612  1.00 50.32  ?  171 ARG B CG  1 
ATOM   3276 C CD  . ARG B 1 171 ? 54.953 -3.990  -2.502  1.00 55.00  ?  171 ARG B CD  1 
ATOM   3277 N NE  . ARG B 1 171 ? 54.141 -4.528  -3.596  1.00 65.78  ?  171 ARG B NE  1 
ATOM   3278 C CZ  . ARG B 1 171 ? 52.859 -4.848  -3.487  1.00 68.58  ?  171 ARG B CZ  1 
ATOM   3279 N NH1 . ARG B 1 171 ? 52.231 -4.715  -2.342  1.00 77.36  ?  171 ARG B NH1 1 
ATOM   3280 N NH2 . ARG B 1 171 ? 52.210 -5.312  -4.523  1.00 69.48  ?  171 ARG B NH2 1 
ATOM   3281 N N   . LEU B 1 172 ? 57.932 0.353   -0.733  1.00 45.76  ?  172 LEU B N   1 
ATOM   3282 C CA  . LEU B 1 172 ? 59.048 0.603   0.165   1.00 44.87  ?  172 LEU B CA  1 
ATOM   3283 C C   . LEU B 1 172 ? 59.092 -0.538  1.171   1.00 48.22  ?  172 LEU B C   1 
ATOM   3284 O O   . LEU B 1 172 ? 58.055 -0.883  1.759   1.00 48.37  ?  172 LEU B O   1 
ATOM   3285 C CB  . LEU B 1 172 ? 58.867 1.945   0.882   1.00 38.42  ?  172 LEU B CB  1 
ATOM   3286 C CG  . LEU B 1 172 ? 59.656 2.233   2.162   1.00 43.84  ?  172 LEU B CG  1 
ATOM   3287 C CD1 . LEU B 1 172 ? 61.143 2.400   1.849   1.00 49.43  ?  172 LEU B CD1 1 
ATOM   3288 C CD2 . LEU B 1 172 ? 59.109 3.468   2.832   1.00 41.08  ?  172 LEU B CD2 1 
ATOM   3289 N N   . VAL B 1 173 ? 60.269 -1.152  1.325   1.00 39.35  ?  173 VAL B N   1 
ATOM   3290 C CA  . VAL B 1 173 ? 60.518 -2.135  2.372   1.00 47.96  ?  173 VAL B CA  1 
ATOM   3291 C C   . VAL B 1 173 ? 61.728 -1.638  3.132   1.00 48.23  ?  173 VAL B C   1 
ATOM   3292 O O   . VAL B 1 173 ? 62.697 -1.189  2.505   1.00 48.86  ?  173 VAL B O   1 
ATOM   3293 C CB  . VAL B 1 173 ? 60.758 -3.565  1.828   1.00 47.59  ?  173 VAL B CB  1 
ATOM   3294 C CG1 . VAL B 1 173 ? 61.846 -3.562  0.849   1.00 65.90  ?  173 VAL B CG1 1 
ATOM   3295 C CG2 . VAL B 1 173 ? 61.180 -4.504  2.928   1.00 47.66  ?  173 VAL B CG2 1 
ATOM   3296 N N   . LEU B 1 174 ? 61.649 -1.670  4.474   1.00 46.63  ?  174 LEU B N   1 
ATOM   3297 C CA  . LEU B 1 174 ? 62.693 -1.134  5.343   1.00 44.72  ?  174 LEU B CA  1 
ATOM   3298 C C   . LEU B 1 174 ? 62.760 -1.905  6.661   1.00 53.96  ?  174 LEU B C   1 
ATOM   3299 O O   . LEU B 1 174 ? 61.807 -2.572  7.068   1.00 58.29  ?  174 LEU B O   1 
ATOM   3300 C CB  . LEU B 1 174 ? 62.461 0.354   5.615   1.00 37.72  ?  174 LEU B CB  1 
ATOM   3301 C CG  . LEU B 1 174 ? 61.266 0.685   6.505   1.00 44.43  ?  174 LEU B CG  1 
ATOM   3302 C CD1 . LEU B 1 174 ? 61.679 0.703   7.976   1.00 43.09  ?  174 LEU B CD1 1 
ATOM   3303 C CD2 . LEU B 1 174 ? 60.633 2.039   6.091   1.00 41.15  ?  174 LEU B CD2 1 
ATOM   3304 N N   . THR B 1 175 ? 63.892 -1.788  7.338   1.00 50.70  ?  175 THR B N   1 
ATOM   3305 C CA  . THR B 1 175 ? 63.981 -2.147  8.740   1.00 51.11  ?  175 THR B CA  1 
ATOM   3306 C C   . THR B 1 175 ? 64.246 -0.901  9.580   1.00 53.15  ?  175 THR B C   1 
ATOM   3307 O O   . THR B 1 175 ? 64.631 0.146   9.059   1.00 66.63  ?  175 THR B O   1 
ATOM   3308 C CB  . THR B 1 175 ? 65.070 -3.198  8.982   1.00 52.31  ?  175 THR B CB  1 
ATOM   3309 O OG1 . THR B 1 175 ? 66.355 -2.674  8.606   1.00 54.01  ?  175 THR B OG1 1 
ATOM   3310 C CG2 . THR B 1 175 ? 64.746 -4.482  8.218   1.00 43.32  ?  175 THR B CG2 1 
ATOM   3311 N N   . ASP B 1 176 ? 64.043 -1.035  10.894  1.00 63.33  ?  176 ASP B N   1 
ATOM   3312 C CA  . ASP B 1 176 ? 64.059 0.076   11.845  1.00 66.64  ?  176 ASP B CA  1 
ATOM   3313 C C   . ASP B 1 176 ? 64.024 -0.446  13.282  1.00 63.58  ?  176 ASP B C   1 
ATOM   3314 O O   . ASP B 1 176 ? 63.491 -1.525  13.547  1.00 68.46  ?  176 ASP B O   1 
ATOM   3315 C CB  . ASP B 1 176 ? 62.866 0.999   11.593  1.00 68.16  ?  176 ASP B CB  1 
ATOM   3316 C CG  . ASP B 1 176 ? 63.116 2.404   12.074  1.00 65.68  ?  176 ASP B CG  1 
ATOM   3317 O OD1 . ASP B 1 176 ? 64.175 2.643   12.706  1.00 53.54  ?  176 ASP B OD1 1 
ATOM   3318 O OD2 . ASP B 1 176 ? 62.255 3.275   11.797  1.00 60.76  -1 176 ASP B OD2 1 
ATOM   3319 N N   . PHE B 1 177 ? 64.578 0.336   14.206  1.00 66.43  ?  177 PHE B N   1 
ATOM   3320 C CA  . PHE B 1 177 ? 64.487 0.020   15.632  1.00 70.06  ?  177 PHE B CA  1 
ATOM   3321 C C   . PHE B 1 177 ? 63.196 0.586   16.209  1.00 73.93  ?  177 PHE B C   1 
ATOM   3322 O O   . PHE B 1 177 ? 62.743 1.660   15.794  1.00 76.57  ?  177 PHE B O   1 
ATOM   3323 C CB  . PHE B 1 177 ? 65.692 0.569   16.400  1.00 58.38  ?  177 PHE B CB  1 
ATOM   3324 C CG  . PHE B 1 177 ? 66.957 -0.170  16.121  1.00 57.74  ?  177 PHE B CG  1 
ATOM   3325 C CD1 . PHE B 1 177 ? 66.984 -1.553  16.178  1.00 64.09  ?  177 PHE B CD1 1 
ATOM   3326 C CD2 . PHE B 1 177 ? 68.118 0.501   15.797  1.00 67.66  ?  177 PHE B CD2 1 
ATOM   3327 C CE1 . PHE B 1 177 ? 68.159 -2.264  15.907  1.00 64.97  ?  177 PHE B CE1 1 
ATOM   3328 C CE2 . PHE B 1 177 ? 69.299 -0.202  15.528  1.00 74.85  ?  177 PHE B CE2 1 
ATOM   3329 C CZ  . PHE B 1 177 ? 69.312 -1.587  15.582  1.00 70.72  ?  177 PHE B CZ  1 
ATOM   3330 N N   . PHE B 1 178 ? 62.588 -0.152  17.146  1.00 72.39  ?  178 PHE B N   1 
ATOM   3331 C CA  . PHE B 1 178 ? 61.372 0.325   17.809  1.00 68.16  ?  178 PHE B CA  1 
ATOM   3332 C C   . PHE B 1 178 ? 61.266 -0.262  19.211  1.00 77.56  ?  178 PHE B C   1 
ATOM   3333 O O   . PHE B 1 178 ? 61.993 -1.185  19.584  1.00 76.79  ?  178 PHE B O   1 
ATOM   3334 C CB  . PHE B 1 178 ? 60.104 0.018   16.995  1.00 58.11  ?  178 PHE B CB  1 
ATOM   3335 C CG  . PHE B 1 178 ? 59.569 -1.389  17.164  1.00 64.28  ?  178 PHE B CG  1 
ATOM   3336 C CD1 . PHE B 1 178 ? 60.268 -2.491  16.665  1.00 65.29  ?  178 PHE B CD1 1 
ATOM   3337 C CD2 . PHE B 1 178 ? 58.344 -1.608  17.776  1.00 61.56  ?  178 PHE B CD2 1 
ATOM   3338 C CE1 . PHE B 1 178 ? 59.763 -3.785  16.811  1.00 62.41  ?  178 PHE B CE1 1 
ATOM   3339 C CE2 . PHE B 1 178 ? 57.833 -2.893  17.918  1.00 61.21  ?  178 PHE B CE2 1 
ATOM   3340 C CZ  . PHE B 1 178 ? 58.539 -3.983  17.438  1.00 61.98  ?  178 PHE B CZ  1 
ATOM   3341 N N   . GLU B 1 179 ? 60.338 0.303   19.993  1.00 88.15  ?  179 GLU B N   1 
ATOM   3342 C CA  . GLU B 1 179 ? 60.173 -0.014  21.412  1.00 76.79  ?  179 GLU B CA  1 
ATOM   3343 C C   . GLU B 1 179 ? 59.000 -0.975  21.550  1.00 75.35  ?  179 GLU B C   1 
ATOM   3344 O O   . GLU B 1 179 ? 57.846 -0.578  21.373  1.00 76.05  ?  179 GLU B O   1 
ATOM   3345 C CB  . GLU B 1 179 ? 59.949 1.261   22.216  1.00 86.88  ?  179 GLU B CB  1 
ATOM   3346 C CG  . GLU B 1 179 ? 60.586 1.245   23.591  1.00 106.91 ?  179 GLU B CG  1 
ATOM   3347 C CD  . GLU B 1 179 ? 60.716 2.637   24.174  1.00 116.01 ?  179 GLU B CD  1 
ATOM   3348 O OE1 . GLU B 1 179 ? 60.151 3.570   23.565  1.00 111.90 ?  179 GLU B OE1 1 
ATOM   3349 O OE2 . GLU B 1 179 ? 61.373 2.793   25.234  1.00 124.18 -1 179 GLU B OE2 1 
ATOM   3350 N N   . ARG B 1 180 ? 59.296 -2.250  21.829  1.00 81.89  ?  180 ARG B N   1 
ATOM   3351 C CA  . ARG B 1 180 ? 58.241 -3.260  21.817  1.00 77.93  ?  180 ARG B CA  1 
ATOM   3352 C C   . ARG B 1 180 ? 57.261 -3.023  22.949  1.00 84.14  ?  180 ARG B C   1 
ATOM   3353 O O   . ARG B 1 180 ? 56.086 -3.393  22.847  1.00 84.87  ?  180 ARG B O   1 
ATOM   3354 C CB  . ARG B 1 180 ? 58.847 -4.667  21.900  1.00 75.26  ?  180 ARG B CB  1 
ATOM   3355 C CG  . ARG B 1 180 ? 59.703 -5.042  20.673  1.00 70.71  ?  180 ARG B CG  1 
ATOM   3356 C CD  . ARG B 1 180 ? 60.497 -6.346  20.838  1.00 66.15  ?  180 ARG B CD  1 
ATOM   3357 N NE  . ARG B 1 180 ? 59.703 -7.538  20.562  1.00 58.81  ?  180 ARG B NE  1 
ATOM   3358 C CZ  . ARG B 1 180 ? 60.129 -8.787  20.753  1.00 68.49  ?  180 ARG B CZ  1 
ATOM   3359 N NH1 . ARG B 1 180 ? 61.340 -9.033  21.238  1.00 70.69  ?  180 ARG B NH1 1 
ATOM   3360 N NH2 . ARG B 1 180 ? 59.339 -9.807  20.468  1.00 76.27  ?  180 ARG B NH2 1 
ATOM   3361 N N   . ALA B 1 181 ? 57.731 -2.372  24.006  1.00 87.16  ?  181 ALA B N   1 
ATOM   3362 C CA  . ALA B 1 181 ? 57.016 -1.989  25.206  1.00 91.40  ?  181 ALA B CA  1 
ATOM   3363 C C   . ALA B 1 181 ? 57.995 -1.155  26.024  1.00 99.70  ?  181 ALA B C   1 
ATOM   3364 O O   . ALA B 1 181 ? 59.212 -1.263  25.800  1.00 97.70  ?  181 ALA B O   1 
ATOM   3365 C CB  . ALA B 1 181 ? 56.546 -3.229  25.967  1.00 89.79  ?  181 ALA B CB  1 
ATOM   3366 N N   . PRO B 1 182 ? 57.514 -0.306  26.982  1.00 105.43 ?  182 PRO B N   1 
ATOM   3367 C CA  . PRO B 1 182 ? 58.434 0.513   27.789  1.00 102.86 ?  182 PRO B CA  1 
ATOM   3368 C C   . PRO B 1 182 ? 59.634 -0.268  28.296  1.00 98.31  ?  182 PRO B C   1 
ATOM   3369 O O   . PRO B 1 182 ? 59.509 -1.441  28.656  1.00 89.35  ?  182 PRO B O   1 
ATOM   3370 C CB  . PRO B 1 182 ? 57.544 0.988   28.938  1.00 100.02 ?  182 PRO B CB  1 
ATOM   3371 C CG  . PRO B 1 182 ? 56.200 1.092   28.319  1.00 95.60  ?  182 PRO B CG  1 
ATOM   3372 C CD  . PRO B 1 182 ? 56.106 -0.051  27.340  1.00 96.76  ?  182 PRO B CD  1 
ATOM   3373 N N   . LEU B 1 183 ? 60.802 0.365   28.293  1.00 100.76 ?  183 LEU B N   1 
ATOM   3374 C CA  . LEU B 1 183 ? 62.047 -0.343  28.548  1.00 108.14 ?  183 LEU B CA  1 
ATOM   3375 C C   . LEU B 1 183 ? 62.291 -0.515  30.040  1.00 123.26 ?  183 LEU B C   1 
ATOM   3376 O O   . LEU B 1 183 ? 61.999 0.380   30.841  1.00 127.39 ?  183 LEU B O   1 
ATOM   3377 C CB  . LEU B 1 183 ? 63.219 0.412   27.922  1.00 107.68 ?  183 LEU B CB  1 
ATOM   3378 C CG  . LEU B 1 183 ? 63.599 0.029   26.497  1.00 102.17 ?  183 LEU B CG  1 
ATOM   3379 C CD1 . LEU B 1 183 ? 64.353 1.178   25.850  1.00 102.73 ?  183 LEU B CD1 1 
ATOM   3380 C CD2 . LEU B 1 183 ? 64.407 -1.266  26.464  1.00 93.13  ?  183 LEU B CD2 1 
ATOM   3381 N N   . ALA B 1 184 ? 62.830 -1.685  30.411  1.00 128.04 ?  184 ALA B N   1 
ATOM   3382 C CA  . ALA B 1 184 ? 63.366 -1.911  31.750  1.00 124.99 ?  184 ALA B CA  1 
ATOM   3383 C C   . ALA B 1 184 ? 64.411 -0.838  32.019  1.00 129.46 ?  184 ALA B C   1 
ATOM   3384 O O   . ALA B 1 184 ? 65.076 -0.385  31.079  1.00 131.91 ?  184 ALA B O   1 
ATOM   3385 C CB  . ALA B 1 184 ? 63.979 -3.309  31.878  1.00 117.52 ?  184 ALA B CB  1 
ATOM   3386 N N   . PRO B 1 185 ? 64.576 -0.379  33.264  1.00 133.06 ?  185 PRO B N   1 
ATOM   3387 C CA  . PRO B 1 185 ? 65.597 0.654   33.506  1.00 131.27 ?  185 PRO B CA  1 
ATOM   3388 C C   . PRO B 1 185 ? 67.032 0.169   33.318  1.00 129.96 ?  185 PRO B C   1 
ATOM   3389 O O   . PRO B 1 185 ? 67.867 0.952   32.852  1.00 128.68 ?  185 PRO B O   1 
ATOM   3390 C CB  . PRO B 1 185 ? 65.305 1.093   34.946  1.00 127.24 ?  185 PRO B CB  1 
ATOM   3391 C CG  . PRO B 1 185 ? 63.855 0.766   35.142  1.00 122.37 ?  185 PRO B CG  1 
ATOM   3392 C CD  . PRO B 1 185 ? 63.658 -0.519  34.410  1.00 125.84 ?  185 PRO B CD  1 
ATOM   3393 N N   . GLU B 1 186 ? 67.354 -1.092  33.654  1.00 126.41 ?  186 GLU B N   1 
ATOM   3394 C CA  . GLU B 1 186 ? 68.720 -1.578  33.445  1.00 123.18 ?  186 GLU B CA  1 
ATOM   3395 C C   . GLU B 1 186 ? 69.088 -1.592  31.968  1.00 124.02 ?  186 GLU B C   1 
ATOM   3396 O O   . GLU B 1 186 ? 70.261 -1.426  31.614  1.00 122.30 ?  186 GLU B O   1 
ATOM   3397 C CB  . GLU B 1 186 ? 68.895 -2.984  34.023  1.00 122.75 ?  186 GLU B CB  1 
ATOM   3398 C CG  . GLU B 1 186 ? 68.188 -3.245  35.344  1.00 130.64 ?  186 GLU B CG  1 
ATOM   3399 C CD  . GLU B 1 186 ? 68.632 -2.315  36.459  1.00 143.84 ?  186 GLU B CD  1 
ATOM   3400 O OE1 . GLU B 1 186 ? 69.550 -2.709  37.212  1.00 147.50 ?  186 GLU B OE1 1 
ATOM   3401 O OE2 . GLU B 1 186 ? 68.052 -1.214  36.609  1.00 150.15 -1 186 GLU B OE2 1 
ATOM   3402 N N   . GLY B 1 187 ? 68.097 -1.774  31.094  1.00 125.99 ?  187 GLY B N   1 
ATOM   3403 C CA  . GLY B 1 187 ? 68.371 -1.861  29.673  1.00 124.22 ?  187 GLY B CA  1 
ATOM   3404 C C   . GLY B 1 187 ? 68.573 -0.528  28.986  1.00 128.52 ?  187 GLY B C   1 
ATOM   3405 O O   . GLY B 1 187 ? 69.337 -0.447  28.021  1.00 129.78 ?  187 GLY B O   1 
ATOM   3406 N N   . ARG B 1 188 ? 67.899 0.531   29.456  1.00 128.63 ?  188 ARG B N   1 
ATOM   3407 C CA  . ARG B 1 188 ? 67.940 1.809   28.744  1.00 121.75 ?  188 ARG B CA  1 
ATOM   3408 C C   . ARG B 1 188 ? 69.339 2.399   28.701  1.00 111.38 ?  188 ARG B C   1 
ATOM   3409 O O   . ARG B 1 188 ? 69.623 3.255   27.856  1.00 111.01 ?  188 ARG B O   1 
ATOM   3410 C CB  . ARG B 1 188 ? 67.012 2.828   29.367  1.00 124.84 ?  188 ARG B CB  1 
ATOM   3411 C CG  . ARG B 1 188 ? 65.662 2.331   29.776  1.00 127.47 ?  188 ARG B CG  1 
ATOM   3412 C CD  . ARG B 1 188 ? 64.885 3.474   30.380  1.00 130.45 ?  188 ARG B CD  1 
ATOM   3413 N NE  . ARG B 1 188 ? 65.734 4.608   30.755  1.00 131.56 ?  188 ARG B NE  1 
ATOM   3414 C CZ  . ARG B 1 188 ? 66.526 4.645   31.825  1.00 130.91 ?  188 ARG B CZ  1 
ATOM   3415 N NH1 . ARG B 1 188 ? 66.598 3.601   32.643  1.00 132.78 ?  188 ARG B NH1 1 
ATOM   3416 N NH2 . ARG B 1 188 ? 67.257 5.725   32.062  1.00 129.24 ?  188 ARG B NH2 1 
ATOM   3417 N N   . ALA B 1 189 ? 70.210 1.992   29.623  1.00 112.90 ?  189 ALA B N   1 
ATOM   3418 C CA  . ALA B 1 189 ? 71.598 2.430   29.559  1.00 120.03 ?  189 ALA B CA  1 
ATOM   3419 C C   . ALA B 1 189 ? 72.246 1.949   28.271  1.00 117.52 ?  189 ALA B C   1 
ATOM   3420 O O   . ALA B 1 189 ? 72.828 2.740   27.516  1.00 114.62 ?  189 ALA B O   1 
ATOM   3421 C CB  . ALA B 1 189 ? 72.367 1.920   30.780  1.00 120.74 ?  189 ALA B CB  1 
ATOM   3422 N N   . ALA B 1 190 ? 72.134 0.647   27.994  1.00 117.55 ?  190 ALA B N   1 
ATOM   3423 C CA  . ALA B 1 190 ? 72.729 0.098   26.784  1.00 108.20 ?  190 ALA B CA  1 
ATOM   3424 C C   . ALA B 1 190 ? 71.921 0.448   25.539  1.00 108.24 ?  190 ALA B C   1 
ATOM   3425 O O   . ALA B 1 190 ? 72.496 0.499   24.447  1.00 114.50 ?  190 ALA B O   1 
ATOM   3426 C CB  . ALA B 1 190 ? 72.894 -1.414  26.915  1.00 99.26  ?  190 ALA B CB  1 
ATOM   3427 N N   . VAL B 1 191 ? 70.611 0.714   25.655  1.00 105.07 ?  191 VAL B N   1 
ATOM   3428 C CA  . VAL B 1 191 ? 69.917 1.098   24.426  1.00 106.35 ?  191 VAL B CA  1 
ATOM   3429 C C   . VAL B 1 191 ? 70.251 2.544   24.036  1.00 112.18 ?  191 VAL B C   1 
ATOM   3430 O O   . VAL B 1 191 ? 70.270 2.858   22.844  1.00 115.32 ?  191 VAL B O   1 
ATOM   3431 C CB  . VAL B 1 191 ? 68.384 0.881   24.455  1.00 99.09  ?  191 VAL B CB  1 
ATOM   3432 C CG1 . VAL B 1 191 ? 67.998 -0.601  24.575  1.00 85.87  ?  191 VAL B CG1 1 
ATOM   3433 C CG2 . VAL B 1 191 ? 67.721 1.721   25.465  1.00 114.12 ?  191 VAL B CG2 1 
ATOM   3434 N N   . GLN B 1 192 ? 70.550 3.455   24.976  1.00 111.10 ?  192 GLN B N   1 
ATOM   3435 C CA  . GLN B 1 192 ? 71.032 4.739   24.466  1.00 111.50 ?  192 GLN B CA  1 
ATOM   3436 C C   . GLN B 1 192 ? 72.532 4.771   24.216  1.00 101.18 ?  192 GLN B C   1 
ATOM   3437 O O   . GLN B 1 192 ? 72.990 5.609   23.433  1.00 96.18  ?  192 GLN B O   1 
ATOM   3438 C CB  . GLN B 1 192 ? 70.679 5.942   25.348  1.00 123.84 ?  192 GLN B CB  1 
ATOM   3439 C CG  . GLN B 1 192 ? 70.844 7.226   24.491  1.00 139.53 ?  192 GLN B CG  1 
ATOM   3440 C CD  . GLN B 1 192 ? 70.069 8.465   24.925  1.00 150.27 ?  192 GLN B CD  1 
ATOM   3441 O OE1 . GLN B 1 192 ? 69.552 8.549   26.041  1.00 156.83 ?  192 GLN B OE1 1 
ATOM   3442 N NE2 . GLN B 1 192 ? 69.992 9.444   24.019  1.00 149.35 ?  192 GLN B NE2 1 
ATOM   3443 N N   . ARG B 1 193 ? 73.322 3.894   24.832  1.00 99.87  ?  193 ARG B N   1 
ATOM   3444 C CA  . ARG B 1 193 ? 74.722 3.857   24.432  1.00 107.45 ?  193 ARG B CA  1 
ATOM   3445 C C   . ARG B 1 193 ? 74.835 3.447   22.962  1.00 108.53 ?  193 ARG B C   1 
ATOM   3446 O O   . ARG B 1 193 ? 75.648 3.991   22.215  1.00 105.96 ?  193 ARG B O   1 
ATOM   3447 C CB  . ARG B 1 193 ? 75.547 2.922   25.322  1.00 108.26 ?  193 ARG B CB  1 
ATOM   3448 C CG  . ARG B 1 193 ? 77.018 3.345   25.299  1.00 111.28 ?  193 ARG B CG  1 
ATOM   3449 C CD  . ARG B 1 193 ? 78.073 2.243   25.314  1.00 117.24 ?  193 ARG B CD  1 
ATOM   3450 N NE  . ARG B 1 193 ? 79.351 2.797   24.842  1.00 126.31 ?  193 ARG B NE  1 
ATOM   3451 C CZ  . ARG B 1 193 ? 80.316 2.097   24.251  1.00 130.52 ?  193 ARG B CZ  1 
ATOM   3452 N NH1 . ARG B 1 193 ? 80.180 0.791   24.084  1.00 134.20 ?  193 ARG B NH1 1 
ATOM   3453 N NH2 . ARG B 1 193 ? 81.431 2.697   23.846  1.00 129.09 ?  193 ARG B NH2 1 
ATOM   3454 N N   . TYR B 1 194 ? 73.989 2.515   22.520  1.00 105.90 ?  194 TYR B N   1 
ATOM   3455 C CA  . TYR B 1 194 ? 73.904 2.149   21.108  1.00 95.39  ?  194 TYR B CA  1 
ATOM   3456 C C   . TYR B 1 194 ? 73.386 3.321   20.285  1.00 90.70  ?  194 TYR B C   1 
ATOM   3457 O O   . TYR B 1 194 ? 74.100 3.853   19.427  1.00 90.73  ?  194 TYR B O   1 
ATOM   3458 C CB  . TYR B 1 194 ? 72.991 0.926   20.972  1.00 92.54  ?  194 TYR B CB  1 
ATOM   3459 C CG  . TYR B 1 194 ? 73.145 0.093   19.724  1.00 90.11  ?  194 TYR B CG  1 
ATOM   3460 C CD1 . TYR B 1 194 ? 74.378 -0.400  19.331  1.00 92.98  ?  194 TYR B CD1 1 
ATOM   3461 C CD2 . TYR B 1 194 ? 72.031 -0.265  18.976  1.00 87.39  ?  194 TYR B CD2 1 
ATOM   3462 C CE1 . TYR B 1 194 ? 74.496 -1.197  18.194  1.00 83.70  ?  194 TYR B CE1 1 
ATOM   3463 C CE2 . TYR B 1 194 ? 72.142 -1.053  17.842  1.00 85.08  ?  194 TYR B CE2 1 
ATOM   3464 C CZ  . TYR B 1 194 ? 73.376 -1.520  17.459  1.00 79.54  ?  194 TYR B CZ  1 
ATOM   3465 O OH  . TYR B 1 194 ? 73.489 -2.313  16.345  1.00 78.90  ?  194 TYR B OH  1 
ATOM   3466 N N   . LEU B 1 195 ? 72.155 3.763   20.568  1.00 82.88  ?  195 LEU B N   1 
ATOM   3467 C CA  . LEU B 1 195 ? 71.523 4.795   19.753  1.00 86.82  ?  195 LEU B CA  1 
ATOM   3468 C C   . LEU B 1 195 ? 72.395 6.036   19.623  1.00 100.01 ?  195 LEU B C   1 
ATOM   3469 O O   . LEU B 1 195 ? 72.367 6.718   18.590  1.00 98.55  ?  195 LEU B O   1 
ATOM   3470 C CB  . LEU B 1 195 ? 70.162 5.182   20.337  1.00 83.83  ?  195 LEU B CB  1 
ATOM   3471 C CG  . LEU B 1 195 ? 68.980 4.212   20.390  1.00 83.87  ?  195 LEU B CG  1 
ATOM   3472 C CD1 . LEU B 1 195 ? 67.882 4.874   21.192  1.00 92.42  ?  195 LEU B CD1 1 
ATOM   3473 C CD2 . LEU B 1 195 ? 68.454 3.801   19.016  1.00 79.66  ?  195 LEU B CD2 1 
ATOM   3474 N N   . HIS B 1 196 ? 73.187 6.337   20.650  1.00 103.02 ?  196 HIS B N   1 
ATOM   3475 C CA  . HIS B 1 196 ? 74.021 7.526   20.646  1.00 95.71  ?  196 HIS B CA  1 
ATOM   3476 C C   . HIS B 1 196 ? 75.383 7.279   20.015  1.00 96.47  ?  196 HIS B C   1 
ATOM   3477 O O   . HIS B 1 196 ? 75.862 8.124   19.254  1.00 94.25  ?  196 HIS B O   1 
ATOM   3478 C CB  . HIS B 1 196 ? 74.190 8.042   22.070  1.00 99.73  ?  196 HIS B CB  1 
ATOM   3479 C CG  . HIS B 1 196 ? 74.847 9.381   22.151  1.00 109.91 ?  196 HIS B CG  1 
ATOM   3480 N ND1 . HIS B 1 196 ? 74.170 10.558  21.901  1.00 115.24 ?  196 HIS B ND1 1 
ATOM   3481 C CD2 . HIS B 1 196 ? 76.119 9.734   22.455  1.00 111.33 ?  196 HIS B CD2 1 
ATOM   3482 C CE1 . HIS B 1 196 ? 74.998 11.578  22.054  1.00 115.61 ?  196 HIS B CE1 1 
ATOM   3483 N NE2 . HIS B 1 196 ? 76.185 11.105  22.389  1.00 113.77 ?  196 HIS B NE2 1 
ATOM   3484 N N   . ASP B 1 197 ? 76.024 6.142   20.302  1.00 98.22  ?  197 ASP B N   1 
ATOM   3485 C CA  . ASP B 1 197 ? 77.365 5.921   19.766  1.00 101.05 ?  197 ASP B CA  1 
ATOM   3486 C C   . ASP B 1 197 ? 77.369 5.642   18.271  1.00 105.93 ?  197 ASP B C   1 
ATOM   3487 O O   . ASP B 1 197 ? 78.425 5.760   17.642  1.00 114.11 ?  197 ASP B O   1 
ATOM   3488 C CB  . ASP B 1 197 ? 78.075 4.767   20.480  1.00 104.04 ?  197 ASP B CB  1 
ATOM   3489 C CG  . ASP B 1 197 ? 78.403 5.087   21.926  1.00 114.72 ?  197 ASP B CG  1 
ATOM   3490 O OD1 . ASP B 1 197 ? 78.042 6.191   22.406  1.00 119.51 ?  197 ASP B OD1 1 
ATOM   3491 O OD2 . ASP B 1 197 ? 79.058 4.244   22.572  1.00 117.68 -1 197 ASP B OD2 1 
ATOM   3492 N N   . PHE B 1 198 ? 76.232 5.255   17.687  1.00 105.25 ?  198 PHE B N   1 
ATOM   3493 C CA  . PHE B 1 198 ? 76.127 5.148   16.237  1.00 104.16 ?  198 PHE B CA  1 
ATOM   3494 C C   . PHE B 1 198 ? 75.006 6.014   15.694  1.00 98.49  ?  198 PHE B C   1 
ATOM   3495 O O   . PHE B 1 198 ? 74.457 5.713   14.629  1.00 91.60  ?  198 PHE B O   1 
ATOM   3496 C CB  . PHE B 1 198 ? 75.932 3.704   15.784  1.00 108.11 ?  198 PHE B CB  1 
ATOM   3497 C CG  . PHE B 1 198 ? 76.991 2.763   16.265  1.00 115.73 ?  198 PHE B CG  1 
ATOM   3498 C CD1 . PHE B 1 198 ? 76.852 2.108   17.481  1.00 117.43 ?  198 PHE B CD1 1 
ATOM   3499 C CD2 . PHE B 1 198 ? 78.121 2.513   15.491  1.00 116.50 ?  198 PHE B CD2 1 
ATOM   3500 C CE1 . PHE B 1 198 ? 77.825 1.230   17.921  1.00 117.04 ?  198 PHE B CE1 1 
ATOM   3501 C CE2 . PHE B 1 198 ? 79.097 1.634   15.924  1.00 115.12 ?  198 PHE B CE2 1 
ATOM   3502 C CZ  . PHE B 1 198 ? 78.950 0.997   17.142  1.00 115.96 ?  198 PHE B CZ  1 
ATOM   3503 N N   . MET B 1 199 ? 74.651 7.072   16.418  1.00 100.24 ?  199 MET B N   1 
ATOM   3504 C CA  . MET B 1 199 ? 73.806 8.140   15.901  1.00 101.70 ?  199 MET B CA  1 
ATOM   3505 C C   . MET B 1 199 ? 72.526 7.574   15.292  1.00 95.93  ?  199 MET B C   1 
ATOM   3506 O O   . MET B 1 199 ? 72.295 7.655   14.084  1.00 87.30  ?  199 MET B O   1 
ATOM   3507 C CB  . MET B 1 199 ? 74.571 8.975   14.876  1.00 103.33 ?  199 MET B CB  1 
ATOM   3508 C CG  . MET B 1 199 ? 76.008 9.272   15.253  1.00 104.20 ?  199 MET B CG  1 
ATOM   3509 S SD  . MET B 1 199 ? 76.801 10.294  13.994  1.00 99.44  ?  199 MET B SD  1 
ATOM   3510 C CE  . MET B 1 199 ? 75.852 11.817  14.147  1.00 90.49  ?  199 MET B CE  1 
ATOM   3511 N N   . MET B 1 200 ? 71.718 6.953   16.151  1.00 95.67  ?  200 MET B N   1 
ATOM   3512 C CA  . MET B 1 200 ? 70.477 6.311   15.746  1.00 85.09  ?  200 MET B CA  1 
ATOM   3513 C C   . MET B 1 200 ? 69.333 6.830   16.592  1.00 87.76  ?  200 MET B C   1 
ATOM   3514 O O   . MET B 1 200 ? 69.515 7.212   17.747  1.00 98.16  ?  200 MET B O   1 
ATOM   3515 C CB  . MET B 1 200 ? 70.548 4.786   15.876  1.00 81.26  ?  200 MET B CB  1 
ATOM   3516 C CG  . MET B 1 200 ? 71.449 4.141   14.847  1.00 89.23  ?  200 MET B CG  1 
ATOM   3517 S SD  . MET B 1 200 ? 71.697 2.372   15.082  1.00 84.97  ?  200 MET B SD  1 
ATOM   3518 C CE  . MET B 1 200 ? 72.895 2.308   16.390  1.00 82.38  ?  200 MET B CE  1 
ATOM   3519 N N   . THR B 1 201 ? 68.155 6.845   15.999  1.00 86.91  ?  201 THR B N   1 
ATOM   3520 C CA  . THR B 1 201 ? 66.924 7.072   16.729  1.00 88.33  ?  201 THR B CA  1 
ATOM   3521 C C   . THR B 1 201 ? 66.051 5.821   16.618  1.00 87.69  ?  201 THR B C   1 
ATOM   3522 O O   . THR B 1 201 ? 66.455 4.796   16.060  1.00 84.95  ?  201 THR B O   1 
ATOM   3523 C CB  . THR B 1 201 ? 66.221 8.326   16.223  1.00 89.73  ?  201 THR B CB  1 
ATOM   3524 O OG1 . THR B 1 201 ? 65.865 8.148   14.848  1.00 96.38  ?  201 THR B OG1 1 
ATOM   3525 C CG2 . THR B 1 201 ? 67.145 9.501   16.342  1.00 83.30  ?  201 THR B CG2 1 
ATOM   3526 N N   . MET B 1 202 ? 64.830 5.924   17.137  1.00 86.63  ?  202 MET B N   1 
ATOM   3527 C CA  . MET B 1 202 ? 64.004 4.756   17.406  1.00 77.25  ?  202 MET B CA  1 
ATOM   3528 C C   . MET B 1 202 ? 62.575 5.239   17.571  1.00 81.52  ?  202 MET B C   1 
ATOM   3529 O O   . MET B 1 202 ? 62.328 6.168   18.347  1.00 96.53  ?  202 MET B O   1 
ATOM   3530 C CB  . MET B 1 202 ? 64.536 4.052   18.650  1.00 75.09  ?  202 MET B CB  1 
ATOM   3531 C CG  . MET B 1 202 ? 63.719 2.949   19.218  1.00 83.82  ?  202 MET B CG  1 
ATOM   3532 S SD  . MET B 1 202 ? 64.560 2.370   20.714  1.00 91.03  ?  202 MET B SD  1 
ATOM   3533 C CE  . MET B 1 202 ? 64.312 3.747   21.838  1.00 91.18  ?  202 MET B CE  1 
ATOM   3534 N N   . VAL B 1 203 ? 61.627 4.651   16.845  1.00 71.61  ?  203 VAL B N   1 
ATOM   3535 C CA  . VAL B 1 203 ? 60.288 5.232   16.818  1.00 72.11  ?  203 VAL B CA  1 
ATOM   3536 C C   . VAL B 1 203 ? 59.324 4.348   17.584  1.00 63.54  ?  203 VAL B C   1 
ATOM   3537 O O   . VAL B 1 203 ? 59.699 3.280   18.077  1.00 65.36  ?  203 VAL B O   1 
ATOM   3538 C CB  . VAL B 1 203 ? 59.790 5.448   15.379  1.00 76.55  ?  203 VAL B CB  1 
ATOM   3539 C CG1 . VAL B 1 203 ? 60.348 6.740   14.820  1.00 77.98  ?  203 VAL B CG1 1 
ATOM   3540 C CG2 . VAL B 1 203 ? 60.153 4.249   14.506  1.00 73.06  ?  203 VAL B CG2 1 
ATOM   3541 N N   . SER B 1 204 ? 58.091 4.808   17.713  1.00 59.99  ?  204 SER B N   1 
ATOM   3542 C CA  . SER B 1 204 ? 57.012 4.009   18.266  1.00 65.10  ?  204 SER B CA  1 
ATOM   3543 C C   . SER B 1 204 ? 56.247 3.353   17.122  1.00 65.62  ?  204 SER B C   1 
ATOM   3544 O O   . SER B 1 204 ? 56.100 3.931   16.045  1.00 65.56  ?  204 SER B O   1 
ATOM   3545 C CB  . SER B 1 204 ? 56.073 4.865   19.130  1.00 66.20  ?  204 SER B CB  1 
ATOM   3546 O OG  . SER B 1 204 ? 54.932 5.302   18.399  1.00 67.77  ?  204 SER B OG  1 
ATOM   3547 N N   . ALA B 1 205 ? 55.777 2.126   17.362  1.00 67.43  ?  205 ALA B N   1 
ATOM   3548 C CA  . ALA B 1 205 ? 55.137 1.349   16.304  1.00 63.83  ?  205 ALA B CA  1 
ATOM   3549 C C   . ALA B 1 205 ? 54.012 2.135   15.647  1.00 67.68  ?  205 ALA B C   1 
ATOM   3550 O O   . ALA B 1 205 ? 53.940 2.225   14.413  1.00 66.03  ?  205 ALA B O   1 
ATOM   3551 C CB  . ALA B 1 205 ? 54.620 0.017   16.860  1.00 57.47  ?  205 ALA B CB  1 
ATOM   3552 N N   . GLU B 1 206 ? 53.143 2.749   16.456  1.00 66.87  ?  206 GLU B N   1 
ATOM   3553 C CA  . GLU B 1 206 ? 52.055 3.545   15.896  1.00 64.35  ?  206 GLU B CA  1 
ATOM   3554 C C   . GLU B 1 206 ? 52.531 4.847   15.274  1.00 60.03  ?  206 GLU B C   1 
ATOM   3555 O O   . GLU B 1 206 ? 51.704 5.562   14.694  1.00 67.45  ?  206 GLU B O   1 
ATOM   3556 C CB  . GLU B 1 206 ? 50.996 3.843   16.963  1.00 69.73  ?  206 GLU B CB  1 
ATOM   3557 C CG  . GLU B 1 206 ? 51.456 4.764   18.089  1.00 67.22  ?  206 GLU B CG  1 
ATOM   3558 C CD  . GLU B 1 206 ? 52.178 4.030   19.215  1.00 73.64  ?  206 GLU B CD  1 
ATOM   3559 O OE1 . GLU B 1 206 ? 52.931 3.061   18.938  1.00 70.12  ?  206 GLU B OE1 1 
ATOM   3560 O OE2 . GLU B 1 206 ? 51.976 4.422   20.391  1.00 75.08  -1 206 GLU B OE2 1 
ATOM   3561 N N   . ALA B 1 207 ? 53.828 5.172   15.361  1.00 68.29  ?  207 ALA B N   1 
ATOM   3562 C CA  . ALA B 1 207 ? 54.335 6.348   14.651  1.00 61.31  ?  207 ALA B CA  1 
ATOM   3563 C C   . ALA B 1 207 ? 54.259 6.172   13.139  1.00 63.92  ?  207 ALA B C   1 
ATOM   3564 O O   . ALA B 1 207 ? 54.029 7.149   12.419  1.00 61.33  ?  207 ALA B O   1 
ATOM   3565 C CB  . ALA B 1 207 ? 55.780 6.659   15.066  1.00 48.35  ?  207 ALA B CB  1 
ATOM   3566 N N   . TYR B 1 208 ? 54.416 4.942   12.638  1.00 55.57  ?  208 TYR B N   1 
ATOM   3567 C CA  . TYR B 1 208 ? 54.617 4.738   11.203  1.00 61.63  ?  208 TYR B CA  1 
ATOM   3568 C C   . TYR B 1 208 ? 53.380 4.917   10.327  1.00 65.85  ?  208 TYR B C   1 
ATOM   3569 O O   . TYR B 1 208 ? 53.507 5.488   9.236   1.00 59.32  ?  208 TYR B O   1 
ATOM   3570 C CB  . TYR B 1 208 ? 55.224 3.366   10.957  1.00 53.35  ?  208 TYR B CB  1 
ATOM   3571 C CG  . TYR B 1 208 ? 56.689 3.475   10.651  1.00 63.15  ?  208 TYR B CG  1 
ATOM   3572 C CD1 . TYR B 1 208 ? 57.131 4.142   9.496   1.00 70.25  ?  208 TYR B CD1 1 
ATOM   3573 C CD2 . TYR B 1 208 ? 57.642 2.970   11.530  1.00 60.67  ?  208 TYR B CD2 1 
ATOM   3574 C CE1 . TYR B 1 208 ? 58.495 4.253   9.207   1.00 67.76  ?  208 TYR B CE1 1 
ATOM   3575 C CE2 . TYR B 1 208 ? 58.996 3.072   11.258  1.00 59.60  ?  208 TYR B CE2 1 
ATOM   3576 C CZ  . TYR B 1 208 ? 59.411 3.715   10.098  1.00 64.85  ?  208 TYR B CZ  1 
ATOM   3577 O OH  . TYR B 1 208 ? 60.745 3.814   9.828   1.00 73.15  ?  208 TYR B OH  1 
ATOM   3578 N N   . PRO B 1 209 ? 52.186 4.468   10.723  1.00 67.99  ?  209 PRO B N   1 
ATOM   3579 C CA  . PRO B 1 209 ? 51.007 4.679   9.851   1.00 66.79  ?  209 PRO B CA  1 
ATOM   3580 C C   . PRO B 1 209 ? 50.807 6.142   9.484   1.00 63.49  ?  209 PRO B C   1 
ATOM   3581 O O   . PRO B 1 209 ? 50.640 6.454   8.291   1.00 65.19  ?  209 PRO B O   1 
ATOM   3582 C CB  . PRO B 1 209 ? 49.839 4.118   10.680  1.00 65.67  ?  209 PRO B CB  1 
ATOM   3583 C CG  . PRO B 1 209 ? 50.482 3.008   11.470  1.00 65.70  ?  209 PRO B CG  1 
ATOM   3584 C CD  . PRO B 1 209 ? 51.869 3.549   11.839  1.00 66.16  ?  209 PRO B CD  1 
ATOM   3585 N N   . PRO B 1 210 ? 50.826 7.086   10.440  1.00 58.65  ?  210 PRO B N   1 
ATOM   3586 C CA  . PRO B 1 210 ? 50.584 8.480   10.025  1.00 60.91  ?  210 PRO B CA  1 
ATOM   3587 C C   . PRO B 1 210 ? 51.798 9.109   9.344   1.00 59.89  ?  210 PRO B C   1 
ATOM   3588 O O   . PRO B 1 210 ? 51.636 9.923   8.421   1.00 65.08  ?  210 PRO B O   1 
ATOM   3589 C CB  . PRO B 1 210 ? 50.221 9.169   11.340  1.00 51.46  ?  210 PRO B CB  1 
ATOM   3590 C CG  . PRO B 1 210 ? 51.096 8.461   12.324  1.00 55.39  ?  210 PRO B CG  1 
ATOM   3591 C CD  . PRO B 1 210 ? 51.091 7.012   11.891  1.00 58.95  ?  210 PRO B CD  1 
ATOM   3592 N N   . LEU B 1 211 ? 53.016 8.733   9.760   1.00 53.50  ?  211 LEU B N   1 
ATOM   3593 C CA  . LEU B 1 211 ? 54.210 9.083   8.989   1.00 58.26  ?  211 LEU B CA  1 
ATOM   3594 C C   . LEU B 1 211 ? 54.067 8.658   7.527   1.00 59.80  ?  211 LEU B C   1 
ATOM   3595 O O   . LEU B 1 211 ? 54.214 9.474   6.607   1.00 64.58  ?  211 LEU B O   1 
ATOM   3596 C CB  . LEU B 1 211 ? 55.435 8.409   9.591   1.00 58.98  ?  211 LEU B CB  1 
ATOM   3597 C CG  . LEU B 1 211 ? 56.203 8.948   10.771  1.00 60.92  ?  211 LEU B CG  1 
ATOM   3598 C CD1 . LEU B 1 211 ? 57.120 7.817   11.183  1.00 62.21  ?  211 LEU B CD1 1 
ATOM   3599 C CD2 . LEU B 1 211 ? 56.994 10.232  10.506  1.00 40.72  ?  211 LEU B CD2 1 
ATOM   3600 N N   . LEU B 1 212 ? 53.777 7.369   7.302   1.00 58.96  ?  212 LEU B N   1 
ATOM   3601 C CA  . LEU B 1 212 ? 53.621 6.849   5.951   1.00 57.16  ?  212 LEU B CA  1 
ATOM   3602 C C   . LEU B 1 212 ? 52.486 7.549   5.214   1.00 60.65  ?  212 LEU B C   1 
ATOM   3603 O O   . LEU B 1 212 ? 52.625 7.918   4.037   1.00 51.84  ?  212 LEU B O   1 
ATOM   3604 C CB  . LEU B 1 212 ? 53.385 5.339   6.008   1.00 53.55  ?  212 LEU B CB  1 
ATOM   3605 C CG  . LEU B 1 212 ? 54.558 4.484   6.514   1.00 54.23  ?  212 LEU B CG  1 
ATOM   3606 C CD1 . LEU B 1 212 ? 54.069 3.103   6.934   1.00 42.57  ?  212 LEU B CD1 1 
ATOM   3607 C CD2 . LEU B 1 212 ? 55.680 4.400   5.466   1.00 52.85  ?  212 LEU B CD2 1 
ATOM   3608 N N   . ARG B 1 213 ? 51.338 7.734   5.884   1.00 63.32  ?  213 ARG B N   1 
ATOM   3609 C CA  . ARG B 1 213 ? 50.219 8.383   5.198   1.00 62.26  ?  213 ARG B CA  1 
ATOM   3610 C C   . ARG B 1 213 ? 50.588 9.812   4.796   1.00 59.41  ?  213 ARG B C   1 
ATOM   3611 O O   . ARG B 1 213 ? 50.196 10.272  3.714   1.00 60.63  ?  213 ARG B O   1 
ATOM   3612 C CB  . ARG B 1 213 ? 48.942 8.352   6.067   1.00 69.27  ?  213 ARG B CB  1 
ATOM   3613 C CG  . ARG B 1 213 ? 48.060 7.043   5.954   1.00 73.17  ?  213 ARG B CG  1 
ATOM   3614 C CD  . ARG B 1 213 ? 46.635 7.216   6.577   1.00 70.30  ?  213 ARG B CD  1 
ATOM   3615 N NE  . ARG B 1 213 ? 46.713 8.068   7.764   1.00 70.53  ?  213 ARG B NE  1 
ATOM   3616 C CZ  . ARG B 1 213 ? 46.835 7.625   9.014   1.00 65.43  ?  213 ARG B CZ  1 
ATOM   3617 N NH1 . ARG B 1 213 ? 46.852 6.326   9.267   1.00 60.14  ?  213 ARG B NH1 1 
ATOM   3618 N NH2 . ARG B 1 213 ? 46.933 8.487   10.017  1.00 62.32  ?  213 ARG B NH2 1 
ATOM   3619 N N   . GLY B 1 214 ? 51.388 10.497  5.629   1.00 60.50  ?  214 GLY B N   1 
ATOM   3620 C CA  . GLY B 1 214 ? 51.877 11.821  5.273   1.00 52.77  ?  214 GLY B CA  1 
ATOM   3621 C C   . GLY B 1 214 ? 52.654 11.848  3.969   1.00 62.53  ?  214 GLY B C   1 
ATOM   3622 O O   . GLY B 1 214 ? 52.584 12.823  3.208   1.00 70.78  ?  214 GLY B O   1 
ATOM   3623 N N   . ALA B 1 215 ? 53.392 10.779  3.682   1.00 51.47  ?  215 ALA B N   1 
ATOM   3624 C CA  . ALA B 1 215 ? 54.253 10.727  2.518   1.00 47.72  ?  215 ALA B CA  1 
ATOM   3625 C C   . ALA B 1 215 ? 53.600 10.059  1.319   1.00 57.67  ?  215 ALA B C   1 
ATOM   3626 O O   . ALA B 1 215 ? 54.284 9.806   0.316   1.00 55.51  ?  215 ALA B O   1 
ATOM   3627 C CB  . ALA B 1 215 ? 55.543 10.003  2.873   1.00 59.47  ?  215 ALA B CB  1 
ATOM   3628 N N   . GLY B 1 216 ? 52.306 9.742   1.401   1.00 56.70  ?  216 GLY B N   1 
ATOM   3629 C CA  . GLY B 1 216 ? 51.594 9.130   0.297   1.00 59.23  ?  216 GLY B CA  1 
ATOM   3630 C C   . GLY B 1 216 ? 51.604 7.608   0.251   1.00 58.21  ?  216 GLY B C   1 
ATOM   3631 O O   . GLY B 1 216 ? 51.042 7.038   -0.691  1.00 65.97  ?  216 GLY B O   1 
ATOM   3632 N N   . LEU B 1 217 ? 52.217 6.937   1.222   1.00 48.07  ?  217 LEU B N   1 
ATOM   3633 C CA  . LEU B 1 217 ? 52.264 5.484   1.277   1.00 52.99  ?  217 LEU B CA  1 
ATOM   3634 C C   . LEU B 1 217 ? 51.252 4.917   2.278   1.00 55.59  ?  217 LEU B C   1 
ATOM   3635 O O   . LEU B 1 217 ? 50.935 5.537   3.300   1.00 54.57  ?  217 LEU B O   1 
ATOM   3636 C CB  . LEU B 1 217 ? 53.671 5.027   1.652   1.00 52.77  ?  217 LEU B CB  1 
ATOM   3637 C CG  . LEU B 1 217 ? 54.738 5.845   0.932   1.00 55.59  ?  217 LEU B CG  1 
ATOM   3638 C CD1 . LEU B 1 217 ? 56.108 5.557   1.500   1.00 56.99  ?  217 LEU B CD1 1 
ATOM   3639 C CD2 . LEU B 1 217 ? 54.706 5.570   -0.569  1.00 47.84  ?  217 LEU B CD2 1 
ATOM   3640 N N   . TRP B 1 218 ? 50.746 3.720   1.968   1.00 54.07  ?  218 TRP B N   1 
ATOM   3641 C CA  . TRP B 1 218 ? 49.881 2.944   2.860   1.00 45.87  ?  218 TRP B CA  1 
ATOM   3642 C C   . TRP B 1 218 ? 50.657 1.776   3.451   1.00 47.84  ?  218 TRP B C   1 
ATOM   3643 O O   . TRP B 1 218 ? 51.280 1.005   2.716   1.00 59.64  ?  218 TRP B O   1 
ATOM   3644 C CB  . TRP B 1 218 ? 48.664 2.416   2.111   1.00 42.61  ?  218 TRP B CB  1 
ATOM   3645 C CG  . TRP B 1 218 ? 47.746 3.476   1.658   1.00 58.68  ?  218 TRP B CG  1 
ATOM   3646 C CD1 . TRP B 1 218 ? 47.875 4.818   1.848   1.00 57.85  ?  218 TRP B CD1 1 
ATOM   3647 C CD2 . TRP B 1 218 ? 46.518 3.287   0.956   1.00 65.78  ?  218 TRP B CD2 1 
ATOM   3648 N NE1 . TRP B 1 218 ? 46.804 5.482   1.293   1.00 55.30  ?  218 TRP B NE1 1 
ATOM   3649 C CE2 . TRP B 1 218 ? 45.957 4.563   0.740   1.00 66.70  ?  218 TRP B CE2 1 
ATOM   3650 C CE3 . TRP B 1 218 ? 45.838 2.163   0.489   1.00 57.75  ?  218 TRP B CE3 1 
ATOM   3651 C CZ2 . TRP B 1 218 ? 44.754 4.743   0.076   1.00 68.57  ?  218 TRP B CZ2 1 
ATOM   3652 C CZ3 . TRP B 1 218 ? 44.642 2.343   -0.163  1.00 61.62  ?  218 TRP B CZ3 1 
ATOM   3653 C CH2 . TRP B 1 218 ? 44.112 3.622   -0.372  1.00 64.61  ?  218 TRP B CH2 1 
ATOM   3654 N N   . LEU B 1 219 ? 50.633 1.646   4.764   1.00 49.62  ?  219 LEU B N   1 
ATOM   3655 C CA  . LEU B 1 219 ? 51.307 0.516   5.385   1.00 46.30  ?  219 LEU B CA  1 
ATOM   3656 C C   . LEU B 1 219 ? 50.737 -0.784  4.823   1.00 55.45  ?  219 LEU B C   1 
ATOM   3657 O O   . LEU B 1 219 ? 49.514 -0.956  4.739   1.00 56.22  ?  219 LEU B O   1 
ATOM   3658 C CB  . LEU B 1 219 ? 51.130 0.571   6.898   1.00 38.55  ?  219 LEU B CB  1 
ATOM   3659 C CG  . LEU B 1 219 ? 51.622 -0.607  7.737   1.00 45.55  ?  219 LEU B CG  1 
ATOM   3660 C CD1 . LEU B 1 219 ? 53.099 -0.896  7.555   1.00 46.79  ?  219 LEU B CD1 1 
ATOM   3661 C CD2 . LEU B 1 219 ? 51.356 -0.286  9.176   1.00 41.84  ?  219 LEU B CD2 1 
ATOM   3662 N N   . GLU B 1 220 ? 51.622 -1.685  4.400   1.00 51.70  ?  220 GLU B N   1 
ATOM   3663 C CA  . GLU B 1 220 ? 51.207 -3.006  3.949   1.00 47.64  ?  220 GLU B CA  1 
ATOM   3664 C C   . GLU B 1 220 ? 51.559 -4.099  4.941   1.00 51.19  ?  220 GLU B C   1 
ATOM   3665 O O   . GLU B 1 220 ? 50.777 -5.034  5.129   1.00 47.84  ?  220 GLU B O   1 
ATOM   3666 C CB  . GLU B 1 220 ? 51.838 -3.338  2.592   1.00 49.27  ?  220 GLU B CB  1 
ATOM   3667 C CG  . GLU B 1 220 ? 51.000 -4.310  1.777   1.00 53.65  ?  220 GLU B CG  1 
ATOM   3668 C CD  . GLU B 1 220 ? 51.711 -4.908  0.551   1.00 66.04  ?  220 GLU B CD  1 
ATOM   3669 O OE1 . GLU B 1 220 ? 52.898 -4.615  0.281   1.00 59.07  ?  220 GLU B OE1 1 
ATOM   3670 O OE2 . GLU B 1 220 ? 51.059 -5.719  -0.148  1.00 79.48  -1 220 GLU B OE2 1 
ATOM   3671 N N   . GLU B 1 221 ? 52.702 -3.983  5.611   1.00 47.29  ?  221 GLU B N   1 
ATOM   3672 C CA  . GLU B 1 221 ? 53.162 -5.044  6.487   1.00 48.47  ?  221 GLU B CA  1 
ATOM   3673 C C   . GLU B 1 221 ? 54.046 -4.464  7.585   1.00 47.63  ?  221 GLU B C   1 
ATOM   3674 O O   . GLU B 1 221 ? 54.978 -3.699  7.306   1.00 48.02  ?  221 GLU B O   1 
ATOM   3675 C CB  . GLU B 1 221 ? 53.905 -6.130  5.683   1.00 49.91  ?  221 GLU B CB  1 
ATOM   3676 C CG  . GLU B 1 221 ? 54.552 -7.208  6.559   1.00 49.55  ?  221 GLU B CG  1 
ATOM   3677 C CD  . GLU B 1 221 ? 55.329 -8.269  5.783   1.00 51.15  ?  221 GLU B CD  1 
ATOM   3678 O OE1 . GLU B 1 221 ? 55.614 -8.099  4.578   1.00 51.91  ?  221 GLU B OE1 1 
ATOM   3679 O OE2 . GLU B 1 221 ? 55.647 -9.306  6.399   1.00 56.00  -1 221 GLU B OE2 1 
ATOM   3680 N N   . PHE B 1 222 ? 53.726 -4.805  8.830   1.00 47.44  ?  222 PHE B N   1 
ATOM   3681 C CA  . PHE B 1 222 ? 54.585 -4.527  9.975   1.00 45.78  ?  222 PHE B CA  1 
ATOM   3682 C C   . PHE B 1 222 ? 54.828 -5.855  10.668  1.00 53.24  ?  222 PHE B C   1 
ATOM   3683 O O   . PHE B 1 222 ? 53.876 -6.560  11.031  1.00 50.22  ?  222 PHE B O   1 
ATOM   3684 C CB  . PHE B 1 222 ? 53.951 -3.518  10.927  1.00 38.87  ?  222 PHE B CB  1 
ATOM   3685 C CG  . PHE B 1 222 ? 54.841 -3.108  12.056  1.00 45.84  ?  222 PHE B CG  1 
ATOM   3686 C CD1 . PHE B 1 222 ? 55.138 -3.978  13.093  1.00 43.45  ?  222 PHE B CD1 1 
ATOM   3687 C CD2 . PHE B 1 222 ? 55.379 -1.835  12.090  1.00 53.13  ?  222 PHE B CD2 1 
ATOM   3688 C CE1 . PHE B 1 222 ? 55.971 -3.593  14.124  1.00 50.69  ?  222 PHE B CE1 1 
ATOM   3689 C CE2 . PHE B 1 222 ? 56.204 -1.445  13.125  1.00 51.91  ?  222 PHE B CE2 1 
ATOM   3690 C CZ  . PHE B 1 222 ? 56.495 -2.332  14.145  1.00 49.71  ?  222 PHE B CZ  1 
ATOM   3691 N N   . LEU B 1 223 ? 56.095 -6.188  10.846  1.00 53.46  ?  223 LEU B N   1 
ATOM   3692 C CA  . LEU B 1 223 ? 56.520 -7.523  11.233  1.00 53.31  ?  223 LEU B CA  1 
ATOM   3693 C C   . LEU B 1 223 ? 57.659 -7.337  12.218  1.00 59.12  ?  223 LEU B C   1 
ATOM   3694 O O   . LEU B 1 223 ? 58.718 -6.814  11.852  1.00 62.68  ?  223 LEU B O   1 
ATOM   3695 C CB  . LEU B 1 223 ? 56.970 -8.360  10.022  1.00 52.53  ?  223 LEU B CB  1 
ATOM   3696 C CG  . LEU B 1 223 ? 57.146 -9.875  10.279  1.00 46.23  ?  223 LEU B CG  1 
ATOM   3697 C CD1 . LEU B 1 223 ? 55.778 -10.472 10.567  1.00 51.34  ?  223 LEU B CD1 1 
ATOM   3698 C CD2 . LEU B 1 223 ? 57.769 -10.596 9.135   1.00 36.18  ?  223 LEU B CD2 1 
ATOM   3699 N N   . ASP B 1 224 ? 57.426 -7.743  13.465  1.00 59.67  ?  224 ASP B N   1 
ATOM   3700 C CA  . ASP B 1 224 ? 58.451 -7.751  14.500  1.00 53.55  ?  224 ASP B CA  1 
ATOM   3701 C C   . ASP B 1 224 ? 59.364 -8.928  14.223  1.00 47.77  ?  224 ASP B C   1 
ATOM   3702 O O   . ASP B 1 224 ? 58.955 -10.080 14.341  1.00 63.83  ?  224 ASP B O   1 
ATOM   3703 C CB  . ASP B 1 224 ? 57.798 -7.850  15.877  1.00 58.41  ?  224 ASP B CB  1 
ATOM   3704 C CG  . ASP B 1 224 ? 58.787 -7.683  17.031  1.00 67.61  ?  224 ASP B CG  1 
ATOM   3705 O OD1 . ASP B 1 224 ? 59.945 -8.142  16.942  1.00 60.90  ?  224 ASP B OD1 1 
ATOM   3706 O OD2 . ASP B 1 224 ? 58.383 -7.071  18.044  1.00 69.91  -1 224 ASP B OD2 1 
ATOM   3707 N N   . ILE B 1 225 ? 60.590 -8.664  13.819  1.00 55.80  ?  225 ILE B N   1 
ATOM   3708 C CA  . ILE B 1 225 ? 61.532 -9.751  13.656  1.00 52.91  ?  225 ILE B CA  1 
ATOM   3709 C C   . ILE B 1 225 ? 62.594 -9.739  14.755  1.00 56.62  ?  225 ILE B C   1 
ATOM   3710 O O   . ILE B 1 225 ? 63.641 -10.360 14.595  1.00 60.00  ?  225 ILE B O   1 
ATOM   3711 C CB  . ILE B 1 225 ? 62.157 -9.747  12.254  1.00 52.59  ?  225 ILE B CB  1 
ATOM   3712 C CG1 . ILE B 1 225 ? 62.698 -8.359  11.894  1.00 49.84  ?  225 ILE B CG1 1 
ATOM   3713 C CG2 . ILE B 1 225 ? 61.122 -10.228 11.229  1.00 43.50  ?  225 ILE B CG2 1 
ATOM   3714 C CD1 . ILE B 1 225 ? 63.749 -8.411  10.812  1.00 49.00  ?  225 ILE B CD1 1 
ATOM   3715 N N   . SER B 1 226 ? 62.300 -9.094  15.898  1.00 49.91  ?  226 SER B N   1 
ATOM   3716 C CA  . SER B 1 226 ? 63.267 -9.006  16.994  1.00 57.69  ?  226 SER B CA  1 
ATOM   3717 C C   . SER B 1 226 ? 63.761 -10.381 17.427  1.00 61.68  ?  226 SER B C   1 
ATOM   3718 O O   . SER B 1 226 ? 64.966 -10.576 17.625  1.00 67.78  ?  226 SER B O   1 
ATOM   3719 C CB  . SER B 1 226 ? 62.672 -8.279  18.205  1.00 60.12  ?  226 SER B CB  1 
ATOM   3720 O OG  . SER B 1 226 ? 61.880 -7.153  17.845  1.00 68.24  ?  226 SER B OG  1 
ATOM   3721 N N   . ASP B 1 227 ? 62.863 -11.357 17.548  1.00 59.13  ?  227 ASP B N   1 
ATOM   3722 C CA  . ASP B 1 227 ? 63.300 -12.641 18.094  1.00 64.07  ?  227 ASP B CA  1 
ATOM   3723 C C   . ASP B 1 227 ? 64.083 -13.492 17.093  1.00 63.76  ?  227 ASP B C   1 
ATOM   3724 O O   . ASP B 1 227 ? 64.650 -14.514 17.493  1.00 69.52  ?  227 ASP B O   1 
ATOM   3725 C CB  . ASP B 1 227 ? 62.100 -13.431 18.646  1.00 64.25  ?  227 ASP B CB  1 
ATOM   3726 C CG  . ASP B 1 227 ? 61.322 -12.659 19.719  1.00 71.36  ?  227 ASP B CG  1 
ATOM   3727 O OD1 . ASP B 1 227 ? 61.936 -11.835 20.453  1.00 60.74  ?  227 ASP B OD1 1 
ATOM   3728 O OD2 . ASP B 1 227 ? 60.083 -12.879 19.813  1.00 78.29  -1 227 ASP B OD2 1 
ATOM   3729 N N   . GLN B 1 228 ? 64.175 -13.086 15.826  1.00 58.68  ?  228 GLN B N   1 
ATOM   3730 C CA  . GLN B 1 228 ? 64.955 -13.808 14.827  1.00 62.47  ?  228 GLN B CA  1 
ATOM   3731 C C   . GLN B 1 228 ? 66.242 -13.090 14.443  1.00 65.31  ?  228 GLN B C   1 
ATOM   3732 O O   . GLN B 1 228 ? 67.015 -13.639 13.647  1.00 66.14  ?  228 GLN B O   1 
ATOM   3733 C CB  . GLN B 1 228 ? 64.120 -14.052 13.555  1.00 62.84  ?  228 GLN B CB  1 
ATOM   3734 C CG  . GLN B 1 228 ? 62.957 -15.011 13.732  1.00 56.60  ?  228 GLN B CG  1 
ATOM   3735 C CD  . GLN B 1 228 ? 61.807 -14.405 14.527  1.00 59.56  ?  228 GLN B CD  1 
ATOM   3736 O OE1 . GLN B 1 228 ? 61.352 -13.306 14.235  1.00 58.03  ?  228 GLN B OE1 1 
ATOM   3737 N NE2 . GLN B 1 228 ? 61.361 -15.112 15.565  1.00 60.16  ?  228 GLN B NE2 1 
ATOM   3738 N N   . THR B 1 229 ? 66.477 -11.875 14.961  1.00 59.42  ?  229 THR B N   1 
ATOM   3739 C CA  . THR B 1 229 ? 67.582 -11.025 14.520  1.00 63.09  ?  229 THR B CA  1 
ATOM   3740 C C   . THR B 1 229 ? 68.534 -10.615 15.637  1.00 67.49  ?  229 THR B C   1 
ATOM   3741 O O   . THR B 1 229 ? 69.746 -10.848 15.524  1.00 60.12  ?  229 THR B O   1 
ATOM   3742 C CB  . THR B 1 229 ? 67.011 -9.762  13.867  1.00 62.00  ?  229 THR B CB  1 
ATOM   3743 O OG1 . THR B 1 229 ? 66.113 -9.128  14.792  1.00 62.97  ?  229 THR B OG1 1 
ATOM   3744 C CG2 . THR B 1 229 ? 66.289 -10.103 12.575  1.00 47.54  ?  229 THR B CG2 1 
ATOM   3745 N N   . LEU B 1 230 ? 68.012 -9.989  16.708  1.00 70.55  ?  230 LEU B N   1 
ATOM   3746 C CA  . LEU B 1 230 ? 68.831 -9.173  17.609  1.00 72.53  ?  230 LEU B CA  1 
ATOM   3747 C C   . LEU B 1 230 ? 69.794 -10.021 18.433  1.00 73.69  ?  230 LEU B C   1 
ATOM   3748 O O   . LEU B 1 230 ? 71.007 -9.788  18.419  1.00 74.70  ?  230 LEU B O   1 
ATOM   3749 C CB  . LEU B 1 230 ? 67.936 -8.341  18.540  1.00 62.87  ?  230 LEU B CB  1 
ATOM   3750 C CG  . LEU B 1 230 ? 67.041 -7.265  17.918  1.00 64.92  ?  230 LEU B CG  1 
ATOM   3751 C CD1 . LEU B 1 230 ? 66.232 -6.588  18.949  1.00 61.62  ?  230 LEU B CD1 1 
ATOM   3752 C CD2 . LEU B 1 230 ? 67.844 -6.233  17.132  1.00 69.60  ?  230 LEU B CD2 1 
ATOM   3753 N N   . GLU B 1 231 ? 69.270 -11.009 19.160  1.00 72.52  ?  231 GLU B N   1 
ATOM   3754 C CA  . GLU B 1 231 ? 70.089 -11.704 20.145  1.00 75.79  ?  231 GLU B CA  1 
ATOM   3755 C C   . GLU B 1 231 ? 71.252 -12.428 19.481  1.00 81.33  ?  231 GLU B C   1 
ATOM   3756 O O   . GLU B 1 231 ? 72.413 -12.234 19.861  1.00 82.46  ?  231 GLU B O   1 
ATOM   3757 C CB  . GLU B 1 231 ? 69.229 -12.677 20.959  1.00 81.29  ?  231 GLU B CB  1 
ATOM   3758 C CG  . GLU B 1 231 ? 70.040 -13.501 21.968  1.00 91.91  ?  231 GLU B CG  1 
ATOM   3759 C CD  . GLU B 1 231 ? 69.214 -14.077 23.118  1.00 98.04  ?  231 GLU B CD  1 
ATOM   3760 O OE1 . GLU B 1 231 ? 68.317 -13.377 23.642  1.00 98.58  ?  231 GLU B OE1 1 
ATOM   3761 O OE2 . GLU B 1 231 ? 69.487 -15.232 23.514  1.00 102.42 -1 231 GLU B OE2 1 
ATOM   3762 N N   . LYS B 1 232 ? 70.962 -13.245 18.463  1.00 77.65  ?  232 LYS B N   1 
ATOM   3763 C CA  . LYS B 1 232 ? 72.002 -14.089 17.883  1.00 73.43  ?  232 LYS B CA  1 
ATOM   3764 C C   . LYS B 1 232 ? 73.108 -13.256 17.242  1.00 80.56  ?  232 LYS B C   1 
ATOM   3765 O O   . LYS B 1 232 ? 74.290 -13.620 17.309  1.00 85.47  ?  232 LYS B O   1 
ATOM   3766 C CB  . LYS B 1 232 ? 71.391 -15.056 16.874  1.00 72.03  ?  232 LYS B CB  1 
ATOM   3767 C CG  . LYS B 1 232 ? 70.932 -16.390 17.467  1.00 80.88  ?  232 LYS B CG  1 
ATOM   3768 C CD  . LYS B 1 232 ? 70.664 -17.437 16.367  1.00 82.99  ?  232 LYS B CD  1 
ATOM   3769 C CE  . LYS B 1 232 ? 71.954 -17.985 15.741  1.00 83.54  ?  232 LYS B CE  1 
ATOM   3770 N NZ  . LYS B 1 232 ? 72.561 -19.144 16.464  1.00 88.36  ?  232 LYS B NZ  1 
ATOM   3771 N N   . THR B 1 233 ? 72.748 -12.130 16.622  1.00 75.28  ?  233 THR B N   1 
ATOM   3772 C CA  . THR B 1 233 ? 73.762 -11.238 16.071  1.00 75.36  ?  233 THR B CA  1 
ATOM   3773 C C   . THR B 1 233 ? 74.593 -10.610 17.179  1.00 77.89  ?  233 THR B C   1 
ATOM   3774 O O   . THR B 1 233 ? 75.821 -10.524 17.075  1.00 83.12  ?  233 THR B O   1 
ATOM   3775 C CB  . THR B 1 233 ? 73.107 -10.138 15.230  1.00 80.20  ?  233 THR B CB  1 
ATOM   3776 O OG1 . THR B 1 233 ? 72.221 -10.720 14.261  1.00 81.98  ?  233 THR B OG1 1 
ATOM   3777 C CG2 . THR B 1 233 ? 74.164 -9.299  14.527  1.00 65.20  ?  233 THR B CG2 1 
ATOM   3778 N N   . PHE B 1 234 ? 73.942 -10.156 18.246  1.00 78.32  ?  234 PHE B N   1 
ATOM   3779 C CA  . PHE B 1 234 ? 74.681 -9.519  19.323  1.00 82.98  ?  234 PHE B CA  1 
ATOM   3780 C C   . PHE B 1 234 ? 75.627 -10.505 20.002  1.00 89.93  ?  234 PHE B C   1 
ATOM   3781 O O   . PHE B 1 234 ? 76.775 -10.159 20.307  1.00 85.45  ?  234 PHE B O   1 
ATOM   3782 C CB  . PHE B 1 234 ? 73.696 -8.902  20.304  1.00 81.55  ?  234 PHE B CB  1 
ATOM   3783 C CG  . PHE B 1 234 ? 73.098 -7.610  19.815  1.00 84.45  ?  234 PHE B CG  1 
ATOM   3784 C CD1 . PHE B 1 234 ? 73.802 -6.789  18.944  1.00 85.30  ?  234 PHE B CD1 1 
ATOM   3785 C CD2 . PHE B 1 234 ? 71.833 -7.210  20.220  1.00 77.38  ?  234 PHE B CD2 1 
ATOM   3786 C CE1 . PHE B 1 234 ? 73.249 -5.584  18.496  1.00 76.07  ?  234 PHE B CE1 1 
ATOM   3787 C CE2 . PHE B 1 234 ? 71.280 -5.998  19.771  1.00 68.33  ?  234 PHE B CE2 1 
ATOM   3788 C CZ  . PHE B 1 234 ? 71.986 -5.191  18.920  1.00 64.15  ?  234 PHE B CZ  1 
ATOM   3789 N N   . ARG B 1 235 ? 75.177 -11.744 20.220  1.00 93.72  ?  235 ARG B N   1 
ATOM   3790 C CA  . ARG B 1 235 ? 76.088 -12.793 20.678  1.00 92.12  ?  235 ARG B CA  1 
ATOM   3791 C C   . ARG B 1 235 ? 77.274 -12.929 19.741  1.00 96.55  ?  235 ARG B C   1 
ATOM   3792 O O   . ARG B 1 235 ? 78.428 -12.754 20.144  1.00 104.05 ?  235 ARG B O   1 
ATOM   3793 C CB  . ARG B 1 235 ? 75.380 -14.141 20.764  1.00 85.18  ?  235 ARG B CB  1 
ATOM   3794 C CG  . ARG B 1 235 ? 74.335 -14.226 21.813  1.00 92.51  ?  235 ARG B CG  1 
ATOM   3795 C CD  . ARG B 1 235 ? 74.717 -15.165 22.919  1.00 104.24 ?  235 ARG B CD  1 
ATOM   3796 N NE  . ARG B 1 235 ? 73.845 -14.931 24.062  1.00 110.29 ?  235 ARG B NE  1 
ATOM   3797 C CZ  . ARG B 1 235 ? 72.553 -15.252 24.098  1.00 113.39 ?  235 ARG B CZ  1 
ATOM   3798 N NH1 . ARG B 1 235 ? 71.975 -15.856 23.061  1.00 110.40 ?  235 ARG B NH1 1 
ATOM   3799 N NH2 . ARG B 1 235 ? 71.840 -14.982 25.187  1.00 117.51 ?  235 ARG B NH2 1 
ATOM   3800 N N   . LEU B 1 236 ? 76.996 -13.253 18.473  1.00 96.92  ?  236 LEU B N   1 
ATOM   3801 C CA  . LEU B 1 236 ? 78.068 -13.563 17.537  1.00 94.60  ?  236 LEU B CA  1 
ATOM   3802 C C   . LEU B 1 236 ? 79.053 -12.407 17.413  1.00 101.13 ?  236 LEU B C   1 
ATOM   3803 O O   . LEU B 1 236 ? 80.243 -12.642 17.196  1.00 105.72 ?  236 LEU B O   1 
ATOM   3804 C CB  . LEU B 1 236 ? 77.489 -13.941 16.171  1.00 86.65  ?  236 LEU B CB  1 
ATOM   3805 C CG  . LEU B 1 236 ? 76.949 -15.364 15.942  1.00 82.85  ?  236 LEU B CG  1 
ATOM   3806 C CD1 . LEU B 1 236 ? 76.562 -15.587 14.465  1.00 69.12  ?  236 LEU B CD1 1 
ATOM   3807 C CD2 . LEU B 1 236 ? 77.934 -16.437 16.421  1.00 86.92  ?  236 LEU B CD2 1 
ATOM   3808 N N   . LEU B 1 237 ? 78.599 -11.165 17.609  1.00 100.89 ?  237 LEU B N   1 
ATOM   3809 C CA  . LEU B 1 237 ? 79.514 -10.033 17.488  1.00 108.21 ?  237 LEU B CA  1 
ATOM   3810 C C   . LEU B 1 237 ? 80.349 -9.829  18.754  1.00 116.60 ?  237 LEU B C   1 
ATOM   3811 O O   . LEU B 1 237 ? 81.560 -9.586  18.664  1.00 119.23 ?  237 LEU B O   1 
ATOM   3812 C CB  . LEU B 1 237 ? 78.748 -8.750  17.141  1.00 105.86 ?  237 LEU B CB  1 
ATOM   3813 C CG  . LEU B 1 237 ? 79.699 -7.577  16.870  1.00 104.28 ?  237 LEU B CG  1 
ATOM   3814 C CD1 . LEU B 1 237 ? 79.534 -7.029  15.464  1.00 104.57 ?  237 LEU B CD1 1 
ATOM   3815 C CD2 . LEU B 1 237 ? 79.523 -6.480  17.881  1.00 102.39 ?  237 LEU B CD2 1 
ATOM   3816 N N   . SER B 1 238 ? 79.732 -9.924  19.940  1.00 119.42 ?  238 SER B N   1 
ATOM   3817 C CA  . SER B 1 238 ? 80.495 -9.763  21.178  1.00 114.96 ?  238 SER B CA  1 
ATOM   3818 C C   . SER B 1 238 ? 81.503 -10.888 21.355  1.00 115.79 ?  238 SER B C   1 
ATOM   3819 O O   . SER B 1 238 ? 82.574 -10.669 21.930  1.00 117.26 ?  238 SER B O   1 
ATOM   3820 C CB  . SER B 1 238 ? 79.583 -9.730  22.397  1.00 105.31 ?  238 SER B CB  1 
ATOM   3821 O OG  . SER B 1 238 ? 80.303 -10.013 23.577  1.00 106.91 ?  238 SER B OG  1 
ATOM   3822 N N   . GLU B 1 239 ? 81.174 -12.099 20.884  1.00 116.39 ?  239 GLU B N   1 
ATOM   3823 C CA  . GLU B 1 239 ? 82.154 -13.176 20.909  1.00 117.50 ?  239 GLU B CA  1 
ATOM   3824 C C   . GLU B 1 239 ? 83.316 -12.888 19.965  1.00 120.74 ?  239 GLU B C   1 
ATOM   3825 O O   . GLU B 1 239 ? 84.444 -13.316 20.231  1.00 123.88 ?  239 GLU B O   1 
ATOM   3826 C CB  . GLU B 1 239 ? 81.489 -14.500 20.565  1.00 119.45 ?  239 GLU B CB  1 
ATOM   3827 C CG  . GLU B 1 239 ? 82.387 -15.693 20.849  1.00 129.38 ?  239 GLU B CG  1 
ATOM   3828 C CD  . GLU B 1 239 ? 82.921 -16.350 19.589  1.00 135.43 ?  239 GLU B CD  1 
ATOM   3829 O OE1 . GLU B 1 239 ? 82.835 -15.724 18.499  1.00 138.15 ?  239 GLU B OE1 1 
ATOM   3830 O OE2 . GLU B 1 239 ? 83.459 -17.478 19.704  1.00 134.28 -1 239 GLU B OE2 1 
ATOM   3831 N N   . ARG B 1 240 ? 83.068 -12.169 18.864  1.00 122.39 ?  240 ARG B N   1 
ATOM   3832 C CA  . ARG B 1 240 ? 84.171 -11.682 18.038  1.00 121.02 ?  240 ARG B CA  1 
ATOM   3833 C C   . ARG B 1 240 ? 85.018 -10.680 18.818  1.00 130.73 ?  240 ARG B C   1 
ATOM   3834 O O   . ARG B 1 240 ? 86.192 -10.936 19.115  1.00 139.69 ?  240 ARG B O   1 
ATOM   3835 C CB  . ARG B 1 240 ? 83.650 -11.037 16.744  1.00 114.74 ?  240 ARG B CB  1 
ATOM   3836 C CG  . ARG B 1 240 ? 82.696 -11.869 15.879  1.00 113.64 ?  240 ARG B CG  1 
ATOM   3837 C CD  . ARG B 1 240 ? 83.298 -13.150 15.298  1.00 118.34 ?  240 ARG B CD  1 
ATOM   3838 N NE  . ARG B 1 240 ? 84.166 -12.913 14.141  1.00 121.78 ?  240 ARG B NE  1 
ATOM   3839 C CZ  . ARG B 1 240 ? 83.747 -12.792 12.881  1.00 124.64 ?  240 ARG B CZ  1 
ATOM   3840 N NH1 . ARG B 1 240 ? 82.451 -12.870 12.583  1.00 117.41 ?  240 ARG B NH1 1 
ATOM   3841 N NH2 . ARG B 1 240 ? 84.633 -12.582 11.910  1.00 128.11 ?  240 ARG B NH2 1 
ATOM   3842 N N   . ILE B 1 241 ? 84.413 -9.550  19.208  1.00 129.07 ?  241 ILE B N   1 
ATOM   3843 C CA  . ILE B 1 241 ? 85.168 -8.414  19.741  1.00 127.69 ?  241 ILE B CA  1 
ATOM   3844 C C   . ILE B 1 241 ? 85.987 -8.809  20.974  1.00 133.91 ?  241 ILE B C   1 
ATOM   3845 O O   . ILE B 1 241 ? 87.099 -8.305  21.179  1.00 139.53 ?  241 ILE B O   1 
ATOM   3846 C CB  . ILE B 1 241 ? 84.216 -7.239  20.047  1.00 123.96 ?  241 ILE B CB  1 
ATOM   3847 C CG1 . ILE B 1 241 ? 83.339 -7.550  21.268  1.00 128.07 ?  241 ILE B CG1 1 
ATOM   3848 C CG2 . ILE B 1 241 ? 83.351 -6.920  18.841  1.00 119.14 ?  241 ILE B CG2 1 
ATOM   3849 C CD1 . ILE B 1 241 ? 82.344 -6.489  21.612  1.00 126.17 ?  241 ILE B CD1 1 
ATOM   3850 N N   . ASN B 1 242 ? 85.459 -9.713  21.812  1.00 136.37 ?  242 ASN B N   1 
ATOM   3851 C CA  . ASN B 1 242 ? 86.109 -10.057 23.074  1.00 134.49 ?  242 ASN B CA  1 
ATOM   3852 C C   . ASN B 1 242 ? 87.147 -11.161 22.928  1.00 138.16 ?  242 ASN B C   1 
ATOM   3853 O O   . ASN B 1 242 ? 88.044 -11.267 23.777  1.00 139.37 ?  242 ASN B O   1 
ATOM   3854 C CB  . ASN B 1 242 ? 85.061 -10.464 24.122  1.00 126.54 ?  242 ASN B CB  1 
ATOM   3855 C CG  . ASN B 1 242 ? 84.224 -9.284  24.600  1.00 120.15 ?  242 ASN B CG  1 
ATOM   3856 O OD1 . ASN B 1 242 ? 82.993 -9.291  24.506  1.00 114.64 ?  242 ASN B OD1 1 
ATOM   3857 N ND2 . ASN B 1 242 ? 84.898 -8.258  25.112  1.00 119.73 ?  242 ASN B ND2 1 
ATOM   3858 N N   . SER B 1 243 ? 87.050 -11.978 21.880  1.00 135.20 ?  243 SER B N   1 
ATOM   3859 C CA  . SER B 1 243 ? 88.069 -12.971 21.581  1.00 134.32 ?  243 SER B CA  1 
ATOM   3860 C C   . SER B 1 243 ? 89.261 -12.378 20.843  1.00 140.61 ?  243 SER B C   1 
ATOM   3861 O O   . SER B 1 243 ? 90.093 -13.142 20.341  1.00 144.37 ?  243 SER B O   1 
ATOM   3862 C CB  . SER B 1 243 ? 87.470 -14.118 20.764  1.00 125.27 ?  243 SER B CB  1 
ATOM   3863 O OG  . SER B 1 243 ? 88.428 -14.637 19.862  1.00 118.97 ?  243 SER B OG  1 
ATOM   3864 N N   . SER B 1 244 ? 89.346 -11.048 20.747  1.00 140.16 ?  244 SER B N   1 
ATOM   3865 C CA  . SER B 1 244 ? 90.407 -10.322 20.043  1.00 137.30 ?  244 SER B CA  1 
ATOM   3866 C C   . SER B 1 244 ? 91.007 -9.230  20.922  1.00 140.43 ?  244 SER B C   1 
ATOM   3867 O O   . SER B 1 244 ? 91.075 -8.065  20.523  1.00 139.59 ?  244 SER B O   1 
ATOM   3868 C CB  . SER B 1 244 ? 89.912 -9.712  18.732  1.00 132.89 ?  244 SER B CB  1 
ATOM   3869 O OG  . SER B 1 244 ? 89.501 -10.708 17.816  1.00 131.39 ?  244 SER B OG  1 
ATOM   3870 N N   . LYS B 1 245 ? 91.416 -9.597  22.144  1.00 142.60 ?  245 LYS B N   1 
ATOM   3871 C CA  . LYS B 1 245 ? 92.336 -8.819  23.003  1.00 143.99 ?  245 LYS B CA  1 
ATOM   3872 C C   . LYS B 1 245 ? 92.259 -7.291  22.878  1.00 140.30 ?  245 LYS B C   1 
ATOM   3873 O O   . LYS B 1 245 ? 92.575 -6.552  23.814  1.00 138.15 ?  245 LYS B O   1 
ATOM   3874 C CB  . LYS B 1 245 ? 93.784 -9.280  22.742  1.00 142.13 ?  245 LYS B CB  1 
ATOM   3875 C CG  . LYS B 1 245 ? 94.220 -9.218  21.281  1.00 133.39 ?  245 LYS B CG  1 
ATOM   3876 C CD  . LYS B 1 245 ? 95.717 -9.307  21.150  1.00 131.29 ?  245 LYS B CD  1 
ATOM   3877 C CE  . LYS B 1 245 ? 96.351 -8.163  21.886  1.00 127.57 ?  245 LYS B CE  1 
ATOM   3878 N NZ  . LYS B 1 245 ? 95.628 -6.898  21.560  1.00 119.99 ?  245 LYS B NZ  1 
ATOM   3879 N N   . VAL B 1 257 ? 87.819 0.819   16.902  1.00 130.34 ?  257 VAL B N   1 
ATOM   3880 C CA  . VAL B 1 257 ? 88.447 0.361   18.131  1.00 135.87 ?  257 VAL B CA  1 
ATOM   3881 C C   . VAL B 1 257 ? 87.918 1.097   19.341  1.00 147.01 ?  257 VAL B C   1 
ATOM   3882 O O   . VAL B 1 257 ? 88.295 2.237   19.610  1.00 151.06 ?  257 VAL B O   1 
ATOM   3883 C CB  . VAL B 1 257 ? 89.993 0.474   18.088  1.00 132.61 ?  257 VAL B CB  1 
ATOM   3884 C CG1 . VAL B 1 257 ? 90.437 1.791   17.476  1.00 128.85 ?  257 VAL B CG1 1 
ATOM   3885 C CG2 . VAL B 1 257 ? 90.593 0.280   19.471  1.00 133.34 ?  257 VAL B CG2 1 
ATOM   3886 N N   . ASN B 1 258 ? 87.026 0.452   20.067  1.00 155.19 ?  258 ASN B N   1 
ATOM   3887 C CA  . ASN B 1 258 ? 86.517 1.035   21.286  1.00 157.05 ?  258 ASN B CA  1 
ATOM   3888 C C   . ASN B 1 258 ? 85.663 0.060   22.029  1.00 157.09 ?  258 ASN B C   1 
ATOM   3889 O O   . ASN B 1 258 ? 85.416 -1.143  21.737  1.00 157.67 ?  258 ASN B O   1 
ATOM   3890 C CB  . ASN B 1 258 ? 85.694 2.282   21.030  1.00 155.38 ?  258 ASN B CB  1 
ATOM   3891 C CG  . ASN B 1 258 ? 85.759 3.263   22.172  1.00 154.89 ?  258 ASN B CG  1 
ATOM   3892 O OD1 . ASN B 1 258 ? 84.953 4.181   22.256  1.00 157.23 ?  258 ASN B OD1 1 
ATOM   3893 N ND2 . ASN B 1 258 ? 86.721 3.068   23.063  1.00 152.59 ?  258 ASN B ND2 1 
ATOM   3894 N N   . GLN B 1 259 ? 85.123 0.578   23.064  1.00 156.79 ?  259 GLN B N   1 
ATOM   3895 C CA  . GLN B 1 259 ? 84.438 -0.397  23.779  1.00 150.57 ?  259 GLN B CA  1 
ATOM   3896 C C   . GLN B 1 259 ? 82.965 -0.581  23.444  1.00 144.52 ?  259 GLN B C   1 
ATOM   3897 O O   . GLN B 1 259 ? 82.155 -0.726  24.350  1.00 145.40 ?  259 GLN B O   1 
ATOM   3898 C CB  . GLN B 1 259 ? 84.494 -0.032  25.249  1.00 144.95 ?  259 GLN B CB  1 
ATOM   3899 C CG  . GLN B 1 259 ? 83.961 1.358   25.551  1.00 145.28 ?  259 GLN B CG  1 
ATOM   3900 C CD  . GLN B 1 259 ? 85.011 2.273   26.146  1.00 150.63 ?  259 GLN B CD  1 
ATOM   3901 O OE1 . GLN B 1 259 ? 84.685 3.290   26.758  1.00 152.34 ?  259 GLN B OE1 1 
ATOM   3902 N NE2 . GLN B 1 259 ? 86.279 1.914   25.973  1.00 150.39 ?  259 GLN B NE2 1 
ATOM   3903 N N   . PHE B 1 260 ? 82.585 -0.615  22.186  1.00 139.32 ?  260 PHE B N   1 
ATOM   3904 C CA  . PHE B 1 260 ? 81.164 -0.893  21.917  1.00 140.72 ?  260 PHE B CA  1 
ATOM   3905 C C   . PHE B 1 260 ? 80.707 -2.332  22.321  1.00 147.44 ?  260 PHE B C   1 
ATOM   3906 O O   . PHE B 1 260 ? 81.134 -3.322  21.722  1.00 146.14 ?  260 PHE B O   1 
ATOM   3907 C CB  . PHE B 1 260 ? 80.788 -0.613  20.476  1.00 132.81 ?  260 PHE B CB  1 
ATOM   3908 C CG  . PHE B 1 260 ? 79.568 -1.357  20.050  1.00 136.40 ?  260 PHE B CG  1 
ATOM   3909 C CD1 . PHE B 1 260 ? 78.339 -1.049  20.603  1.00 139.35 ?  260 PHE B CD1 1 
ATOM   3910 C CD2 . PHE B 1 260 ? 79.652 -2.398  19.145  1.00 138.10 ?  260 PHE B CD2 1 
ATOM   3911 C CE1 . PHE B 1 260 ? 77.209 -1.746  20.235  1.00 140.27 ?  260 PHE B CE1 1 
ATOM   3912 C CE2 . PHE B 1 260 ? 78.523 -3.097  18.770  1.00 137.80 ?  260 PHE B CE2 1 
ATOM   3913 C CZ  . PHE B 1 260 ? 77.300 -2.770  19.315  1.00 138.45 ?  260 PHE B CZ  1 
ATOM   3914 N N   . ASP B 1 261 ? 79.819 -2.453  23.306  1.00 147.00 ?  261 ASP B N   1 
ATOM   3915 C CA  . ASP B 1 261 ? 79.395 -3.769  23.801  1.00 140.48 ?  261 ASP B CA  1 
ATOM   3916 C C   . ASP B 1 261 ? 78.024 -4.208  23.354  1.00 133.57 ?  261 ASP B C   1 
ATOM   3917 O O   . ASP B 1 261 ? 77.026 -3.571  23.677  1.00 129.23 ?  261 ASP B O   1 
ATOM   3918 C CB  . ASP B 1 261 ? 79.321 -3.687  25.299  1.00 141.00 ?  261 ASP B CB  1 
ATOM   3919 C CG  . ASP B 1 261 ? 78.738 -2.366  25.772  1.00 141.16 ?  261 ASP B CG  1 
ATOM   3920 O OD1 . ASP B 1 261 ? 79.280 -1.304  25.407  1.00 140.57 -1 261 ASP B OD1 1 
ATOM   3921 O OD2 . ASP B 1 261 ? 77.726 -2.385  26.495  1.00 141.36 ?  261 ASP B OD2 1 
ATOM   3922 N N   . PRO B 1 262 ? 77.958 -5.316  22.622  1.00 127.24 ?  262 PRO B N   1 
ATOM   3923 C CA  . PRO B 1 262 ? 76.666 -5.750  22.121  1.00 122.16 ?  262 PRO B CA  1 
ATOM   3924 C C   . PRO B 1 262 ? 75.894 -6.384  23.208  1.00 123.37 ?  262 PRO B C   1 
ATOM   3925 O O   . PRO B 1 262 ? 74.704 -6.184  23.357  1.00 128.57 ?  262 PRO B O   1 
ATOM   3926 C CB  . PRO B 1 262 ? 77.028 -6.791  21.088  1.00 116.12 ?  262 PRO B CB  1 
ATOM   3927 C CG  . PRO B 1 262 ? 78.464 -6.631  20.817  1.00 115.22 ?  262 PRO B CG  1 
ATOM   3928 C CD  . PRO B 1 262 ? 79.025 -6.186  22.101  1.00 121.75 ?  262 PRO B CD  1 
ATOM   3929 N N   . GLY B 1 263 ? 76.581 -7.133  24.017  1.00 120.50 ?  263 GLY B N   1 
ATOM   3930 C CA  . GLY B 1 263 ? 75.860 -7.820  25.026  1.00 118.06 ?  263 GLY B CA  1 
ATOM   3931 C C   . GLY B 1 263 ? 75.037 -7.088  25.986  1.00 118.30 ?  263 GLY B C   1 
ATOM   3932 O O   . GLY B 1 263 ? 74.114 -7.622  26.574  1.00 118.05 ?  263 GLY B O   1 
ATOM   3933 N N   . ASP B 1 264 ? 75.387 -5.870  26.191  1.00 116.94 ?  264 ASP B N   1 
ATOM   3934 C CA  . ASP B 1 264 ? 74.623 -5.217  27.114  1.00 114.43 ?  264 ASP B CA  1 
ATOM   3935 C C   . ASP B 1 264 ? 73.284 -5.180  26.513  1.00 112.63 ?  264 ASP B C   1 
ATOM   3936 O O   . ASP B 1 264 ? 72.364 -4.676  27.130  1.00 104.75 ?  264 ASP B O   1 
ATOM   3937 C CB  . ASP B 1 264 ? 75.152 -3.821  27.264  1.00 118.62 ?  264 ASP B CB  1 
ATOM   3938 C CG  . ASP B 1 264 ? 74.998 -3.274  28.671  1.00 131.96 ?  264 ASP B CG  1 
ATOM   3939 O OD1 . ASP B 1 264 ? 73.889 -3.361  29.240  1.00 134.98 ?  264 ASP B OD1 1 
ATOM   3940 O OD2 . ASP B 1 264 ? 75.987 -2.735  29.203  1.00 135.93 -1 264 ASP B OD2 1 
ATOM   3941 N N   . LEU B 1 265 ? 73.106 -5.739  25.307  1.00 117.91 ?  265 LEU B N   1 
ATOM   3942 C CA  . LEU B 1 265 ? 71.772 -5.514  24.808  1.00 106.80 ?  265 LEU B CA  1 
ATOM   3943 C C   . LEU B 1 265 ? 71.135 -6.834  24.759  1.00 101.83 ?  265 LEU B C   1 
ATOM   3944 O O   . LEU B 1 265 ? 69.946 -6.958  24.928  1.00 106.17 ?  265 LEU B O   1 
ATOM   3945 C CB  . LEU B 1 265 ? 71.830 -4.832  23.466  1.00 97.73  ?  265 LEU B CB  1 
ATOM   3946 C CG  . LEU B 1 265 ? 72.159 -3.347  23.495  1.00 89.24  ?  265 LEU B CG  1 
ATOM   3947 C CD1 . LEU B 1 265 ? 72.671 -2.912  22.140  1.00 85.44  ?  265 LEU B CD1 1 
ATOM   3948 C CD2 . LEU B 1 265 ? 70.930 -2.550  23.878  1.00 87.21  ?  265 LEU B CD2 1 
ATOM   3949 N N   . VAL B 1 266 ? 71.935 -7.850  24.573  1.00 96.47  ?  266 VAL B N   1 
ATOM   3950 C CA  . VAL B 1 266 ? 71.396 -9.158  24.661  1.00 95.80  ?  266 VAL B CA  1 
ATOM   3951 C C   . VAL B 1 266 ? 70.440 -9.187  25.829  1.00 102.73 ?  266 VAL B C   1 
ATOM   3952 O O   . VAL B 1 266 ? 70.793 -8.818  26.929  1.00 113.00 ?  266 VAL B O   1 
ATOM   3953 C CB  . VAL B 1 266 ? 72.498 -10.151 24.923  1.00 90.32  ?  266 VAL B CB  1 
ATOM   3954 C CG1 . VAL B 1 266 ? 71.978 -11.566 24.807  1.00 91.83  ?  266 VAL B CG1 1 
ATOM   3955 C CG2 . VAL B 1 266 ? 73.648 -9.909  23.974  1.00 84.76  ?  266 VAL B CG2 1 
ATOM   3956 N N   . GLY B 1 267 ? 69.217 -9.590  25.600  1.00 98.72  ?  267 GLY B N   1 
ATOM   3957 C CA  . GLY B 1 267 ? 68.247 -9.728  26.650  1.00 99.49  ?  267 GLY B CA  1 
ATOM   3958 C C   . GLY B 1 267 ? 67.550 -8.465  27.103  1.00 104.19 ?  267 GLY B C   1 
ATOM   3959 O O   . GLY B 1 267 ? 66.693 -8.559  27.989  1.00 113.26 ?  267 GLY B O   1 
ATOM   3960 N N   . VAL B 1 268 ? 67.841 -7.284  26.541  1.00 96.59  ?  268 VAL B N   1 
ATOM   3961 C CA  . VAL B 1 268 ? 66.974 -6.180  26.953  1.00 93.91  ?  268 VAL B CA  1 
ATOM   3962 C C   . VAL B 1 268 ? 65.730 -6.291  26.081  1.00 95.43  ?  268 VAL B C   1 
ATOM   3963 O O   . VAL B 1 268 ? 65.535 -5.561  25.104  1.00 102.56 ?  268 VAL B O   1 
ATOM   3964 C CB  . VAL B 1 268 ? 67.647 -4.793  26.887  1.00 84.62  ?  268 VAL B CB  1 
ATOM   3965 C CG1 . VAL B 1 268 ? 68.294 -4.527  25.567  1.00 91.13  ?  268 VAL B CG1 1 
ATOM   3966 C CG2 . VAL B 1 268 ? 66.642 -3.706  27.230  1.00 89.23  ?  268 VAL B CG2 1 
ATOM   3967 N N   . LYS B 1 269 ? 64.836 -7.177  26.497  1.00 95.55  ?  269 LYS B N   1 
ATOM   3968 C CA  . LYS B 1 269 ? 63.908 -7.816  25.581  1.00 87.52  ?  269 LYS B CA  1 
ATOM   3969 C C   . LYS B 1 269 ? 62.928 -6.832  24.948  1.00 81.30  ?  269 LYS B C   1 
ATOM   3970 O O   . LYS B 1 269 ? 62.316 -7.157  23.928  1.00 82.86  ?  269 LYS B O   1 
ATOM   3971 C CB  . LYS B 1 269 ? 63.195 -8.945  26.346  1.00 79.25  ?  269 LYS B CB  1 
ATOM   3972 C CG  . LYS B 1 269 ? 62.191 -9.741  25.566  1.00 86.63  ?  269 LYS B CG  1 
ATOM   3973 C CD  . LYS B 1 269 ? 62.498 -11.241 25.615  1.00 89.19  ?  269 LYS B CD  1 
ATOM   3974 C CE  . LYS B 1 269 ? 61.693 -11.964 24.548  1.00 91.72  ?  269 LYS B CE  1 
ATOM   3975 N NZ  . LYS B 1 269 ? 61.973 -11.351 23.201  1.00 97.67  ?  269 LYS B NZ  1 
ATOM   3976 N N   . GLU B 1 270 ? 62.807 -5.621  25.474  1.00 85.68  ?  270 GLU B N   1 
ATOM   3977 C CA  . GLU B 1 270 ? 61.847 -4.664  24.946  1.00 80.91  ?  270 GLU B CA  1 
ATOM   3978 C C   . GLU B 1 270 ? 62.384 -3.926  23.730  1.00 78.50  ?  270 GLU B C   1 
ATOM   3979 O O   . GLU B 1 270 ? 61.620 -3.211  23.071  1.00 72.61  ?  270 GLU B O   1 
ATOM   3980 C CB  . GLU B 1 270 ? 61.442 -3.661  26.038  1.00 77.91  ?  270 GLU B CB  1 
ATOM   3981 C CG  . GLU B 1 270 ? 60.659 -4.277  27.187  1.00 86.40  ?  270 GLU B CG  1 
ATOM   3982 C CD  . GLU B 1 270 ? 61.481 -5.246  28.051  1.00 95.51  ?  270 GLU B CD  1 
ATOM   3983 O OE1 . GLU B 1 270 ? 62.727 -5.309  27.920  1.00 96.63  ?  270 GLU B OE1 1 
ATOM   3984 O OE2 . GLU B 1 270 ? 60.869 -5.966  28.861  1.00 101.17 -1 270 GLU B OE2 1 
ATOM   3985 N N   . PHE B 1 271 ? 63.670 -4.101  23.419  1.00 75.23  ?  271 PHE B N   1 
ATOM   3986 C CA  . PHE B 1 271 ? 64.288 -3.485  22.250  1.00 70.89  ?  271 PHE B CA  1 
ATOM   3987 C C   . PHE B 1 271 ? 63.915 -4.254  20.975  1.00 69.66  ?  271 PHE B C   1 
ATOM   3988 O O   . PHE B 1 271 ? 63.960 -5.491  20.940  1.00 63.91  ?  271 PHE B O   1 
ATOM   3989 C CB  . PHE B 1 271 ? 65.805 -3.429  22.432  1.00 60.86  ?  271 PHE B CB  1 
ATOM   3990 C CG  . PHE B 1 271 ? 66.490 -2.550  21.435  1.00 70.12  ?  271 PHE B CG  1 
ATOM   3991 C CD1 . PHE B 1 271 ? 65.982 -1.286  21.145  1.00 71.72  ?  271 PHE B CD1 1 
ATOM   3992 C CD2 . PHE B 1 271 ? 67.633 -2.987  20.762  1.00 65.43  ?  271 PHE B CD2 1 
ATOM   3993 C CE1 . PHE B 1 271 ? 66.609 -0.470  20.207  1.00 70.57  ?  271 PHE B CE1 1 
ATOM   3994 C CE2 . PHE B 1 271 ? 68.260 -2.185  19.821  1.00 62.31  ?  271 PHE B CE2 1 
ATOM   3995 C CZ  . PHE B 1 271 ? 67.751 -0.922  19.544  1.00 65.17  ?  271 PHE B CZ  1 
ATOM   3996 N N   . GLY B 1 272 ? 63.544 -3.514  19.929  1.00 59.76  ?  272 GLY B N   1 
ATOM   3997 C CA  . GLY B 1 272 ? 62.843 -4.119  18.811  1.00 70.85  ?  272 GLY B CA  1 
ATOM   3998 C C   . GLY B 1 272 ? 63.275 -3.743  17.401  1.00 68.99  ?  272 GLY B C   1 
ATOM   3999 O O   . GLY B 1 272 ? 63.555 -2.579  17.073  1.00 64.84  ?  272 GLY B O   1 
ATOM   4000 N N   . TYR B 1 273 ? 63.293 -4.757  16.546  1.00 57.36  ?  273 TYR B N   1 
ATOM   4001 C CA  . TYR B 1 273 ? 63.701 -4.619  15.161  1.00 55.19  ?  273 TYR B CA  1 
ATOM   4002 C C   . TYR B 1 273 ? 62.532 -5.051  14.297  1.00 61.15  ?  273 TYR B C   1 
ATOM   4003 O O   . TYR B 1 273 ? 61.978 -6.136  14.500  1.00 59.18  ?  273 TYR B O   1 
ATOM   4004 C CB  . TYR B 1 273 ? 64.939 -5.460  14.903  1.00 57.51  ?  273 TYR B CB  1 
ATOM   4005 C CG  . TYR B 1 273 ? 65.651 -5.206  13.607  1.00 60.94  ?  273 TYR B CG  1 
ATOM   4006 C CD1 . TYR B 1 273 ? 66.001 -3.905  13.208  1.00 64.77  ?  273 TYR B CD1 1 
ATOM   4007 C CD2 . TYR B 1 273 ? 66.023 -6.272  12.791  1.00 59.40  ?  273 TYR B CD2 1 
ATOM   4008 C CE1 . TYR B 1 273 ? 66.683 -3.674  12.005  1.00 49.30  ?  273 TYR B CE1 1 
ATOM   4009 C CE2 . TYR B 1 273 ? 66.706 -6.058  11.612  1.00 64.96  ?  273 TYR B CE2 1 
ATOM   4010 C CZ  . TYR B 1 273 ? 67.033 -4.760  11.223  1.00 59.32  ?  273 TYR B CZ  1 
ATOM   4011 O OH  . TYR B 1 273 ? 67.694 -4.587  10.041  1.00 51.27  ?  273 TYR B OH  1 
ATOM   4012 N N   . LEU B 1 274 ? 62.137 -4.191  13.360  1.00 60.40  ?  274 LEU B N   1 
ATOM   4013 C CA  . LEU B 1 274 ? 60.908 -4.360  12.601  1.00 64.45  ?  274 LEU B CA  1 
ATOM   4014 C C   . LEU B 1 274 ? 61.202 -4.336  11.108  1.00 59.30  ?  274 LEU B C   1 
ATOM   4015 O O   . LEU B 1 274 ? 62.026 -3.545  10.649  1.00 47.19  ?  274 LEU B O   1 
ATOM   4016 C CB  . LEU B 1 274 ? 59.901 -3.254  12.927  1.00 61.86  ?  274 LEU B CB  1 
ATOM   4017 C CG  . LEU B 1 274 ? 60.266 -1.864  12.393  1.00 60.38  ?  274 LEU B CG  1 
ATOM   4018 C CD1 . LEU B 1 274 ? 59.575 -1.536  11.047  1.00 60.96  ?  274 LEU B CD1 1 
ATOM   4019 C CD2 . LEU B 1 274 ? 59.966 -0.834  13.454  1.00 54.17  ?  274 LEU B CD2 1 
ATOM   4020 N N   . LEU B 1 275 ? 60.511 -5.202  10.368  1.00 45.16  ?  275 LEU B N   1 
ATOM   4021 C CA  . LEU B 1 275 ? 60.479 -5.183  8.917   1.00 49.59  ?  275 LEU B CA  1 
ATOM   4022 C C   . LEU B 1 275 ? 59.169 -4.524  8.527   1.00 52.10  ?  275 LEU B C   1 
ATOM   4023 O O   . LEU B 1 275 ? 58.118 -4.893  9.055   1.00 59.71  ?  275 LEU B O   1 
ATOM   4024 C CB  . LEU B 1 275 ? 60.570 -6.601  8.340   1.00 48.81  ?  275 LEU B CB  1 
ATOM   4025 C CG  . LEU B 1 275 ? 60.958 -6.900  6.882   1.00 45.97  ?  275 LEU B CG  1 
ATOM   4026 C CD1 . LEU B 1 275 ? 60.907 -8.377  6.703   1.00 48.00  ?  275 LEU B CD1 1 
ATOM   4027 C CD2 . LEU B 1 275 ? 60.023 -6.282  5.900   1.00 48.31  ?  275 LEU B CD2 1 
ATOM   4028 N N   . LEU B 1 276 ? 59.226 -3.534  7.646   1.00 45.91  ?  276 LEU B N   1 
ATOM   4029 C CA  . LEU B 1 276 ? 58.035 -2.793  7.265   1.00 49.64  ?  276 LEU B CA  1 
ATOM   4030 C C   . LEU B 1 276 ? 57.921 -2.783  5.754   1.00 53.83  ?  276 LEU B C   1 
ATOM   4031 O O   . LEU B 1 276 ? 58.920 -2.732  5.031   1.00 58.35  ?  276 LEU B O   1 
ATOM   4032 C CB  . LEU B 1 276 ? 58.056 -1.352  7.780   1.00 51.76  ?  276 LEU B CB  1 
ATOM   4033 C CG  . LEU B 1 276 ? 56.797 -0.502  7.549   1.00 51.32  ?  276 LEU B CG  1 
ATOM   4034 C CD1 . LEU B 1 276 ? 56.570 0.471   8.704   1.00 45.02  ?  276 LEU B CD1 1 
ATOM   4035 C CD2 . LEU B 1 276 ? 56.845 0.272   6.221   1.00 43.21  ?  276 LEU B CD2 1 
ATOM   4036 N N   . VAL B 1 277 ? 56.695 -2.832  5.272   1.00 53.19  ?  277 VAL B N   1 
ATOM   4037 C CA  . VAL B 1 277 ? 56.441 -2.699  3.849   1.00 45.68  ?  277 VAL B CA  1 
ATOM   4038 C C   . VAL B 1 277 ? 55.315 -1.695  3.678   1.00 51.17  ?  277 VAL B C   1 
ATOM   4039 O O   . VAL B 1 277 ? 54.237 -1.866  4.260   1.00 55.89  ?  277 VAL B O   1 
ATOM   4040 C CB  . VAL B 1 277 ? 56.058 -4.034  3.196   1.00 44.18  ?  277 VAL B CB  1 
ATOM   4041 C CG1 . VAL B 1 277 ? 55.684 -3.778  1.743   1.00 47.10  ?  277 VAL B CG1 1 
ATOM   4042 C CG2 . VAL B 1 277 ? 57.183 -5.004  3.254   1.00 43.01  ?  277 VAL B CG2 1 
ATOM   4043 N N   . ALA B 1 278 ? 55.560 -0.654  2.886   1.00 43.14  ?  278 ALA B N   1 
ATOM   4044 C CA  . ALA B 1 278 ? 54.515 0.288   2.528   1.00 40.21  ?  278 ALA B CA  1 
ATOM   4045 C C   . ALA B 1 278 ? 54.417 0.334   1.021   1.00 53.42  ?  278 ALA B C   1 
ATOM   4046 O O   . ALA B 1 278 ? 55.342 -0.059  0.302   1.00 55.88  ?  278 ALA B O   1 
ATOM   4047 C CB  . ALA B 1 278 ? 54.764 1.688   3.077   1.00 44.62  ?  278 ALA B CB  1 
ATOM   4048 N N   . GLN B 1 279 ? 53.277 0.808   0.548   1.00 56.97  ?  279 GLN B N   1 
ATOM   4049 C CA  . GLN B 1 279 ? 52.970 0.801   -0.870  1.00 48.50  ?  279 GLN B CA  1 
ATOM   4050 C C   . GLN B 1 279 ? 52.440 2.176   -1.263  1.00 54.35  ?  279 GLN B C   1 
ATOM   4051 O O   . GLN B 1 279 ? 51.730 2.823   -0.485  1.00 64.30  ?  279 GLN B O   1 
ATOM   4052 C CB  . GLN B 1 279 ? 51.949 -0.304  -1.194  1.00 48.22  ?  279 GLN B CB  1 
ATOM   4053 C CG  . GLN B 1 279 ? 51.581 -0.355  -2.680  1.00 67.65  ?  279 GLN B CG  1 
ATOM   4054 C CD  . GLN B 1 279 ? 50.716 -1.534  -3.079  1.00 74.68  ?  279 GLN B CD  1 
ATOM   4055 O OE1 . GLN B 1 279 ? 49.950 -2.091  -2.266  1.00 80.02  ?  279 GLN B OE1 1 
ATOM   4056 N NE2 . GLN B 1 279 ? 50.883 -1.969  -4.334  1.00 65.07  ?  279 GLN B NE2 1 
ATOM   4057 N N   . ARG B 1 280 ? 52.807 2.644   -2.448  1.00 50.18  ?  280 ARG B N   1 
ATOM   4058 C CA  . ARG B 1 280 ? 52.223 3.870   -2.965  1.00 56.56  ?  280 ARG B CA  1 
ATOM   4059 C C   . ARG B 1 280 ? 51.008 3.536   -3.827  1.00 63.42  ?  280 ARG B C   1 
ATOM   4060 O O   . ARG B 1 280 ? 51.165 2.865   -4.859  1.00 57.77  ?  280 ARG B O   1 
ATOM   4061 C CB  . ARG B 1 280 ? 53.245 4.658   -3.773  1.00 49.81  ?  280 ARG B CB  1 
ATOM   4062 C CG  . ARG B 1 280 ? 52.585 5.810   -4.491  1.00 51.08  ?  280 ARG B CG  1 
ATOM   4063 C CD  . ARG B 1 280 ? 53.523 6.673   -5.256  1.00 48.58  ?  280 ARG B CD  1 
ATOM   4064 N NE  . ARG B 1 280 ? 52.754 7.735   -5.893  1.00 56.13  ?  280 ARG B NE  1 
ATOM   4065 C CZ  . ARG B 1 280 ? 53.295 8.755   -6.547  1.00 56.84  ?  280 ARG B CZ  1 
ATOM   4066 N NH1 . ARG B 1 280 ? 52.527 9.691   -7.084  1.00 53.17  ?  280 ARG B NH1 1 
ATOM   4067 N NH2 . ARG B 1 280 ? 54.611 8.836   -6.657  1.00 53.46  ?  280 ARG B NH2 1 
ATOM   4068 N N   . PRO B 1 281 ? 49.803 4.000   -3.471  1.00 67.46  ?  281 PRO B N   1 
ATOM   4069 C CA  . PRO B 1 281 ? 48.588 3.582   -4.197  1.00 64.20  ?  281 PRO B CA  1 
ATOM   4070 C C   . PRO B 1 281 ? 48.687 3.844   -5.694  1.00 58.28  ?  281 PRO B C   1 
ATOM   4071 O O   . PRO B 1 281 ? 49.367 4.771   -6.136  1.00 59.49  ?  281 PRO B O   1 
ATOM   4072 C CB  . PRO B 1 281 ? 47.483 4.433   -3.560  1.00 61.14  ?  281 PRO B CB  1 
ATOM   4073 C CG  . PRO B 1 281 ? 48.035 4.827   -2.203  1.00 64.44  ?  281 PRO B CG  1 
ATOM   4074 C CD  . PRO B 1 281 ? 49.512 4.996   -2.426  1.00 64.49  ?  281 PRO B CD  1 
ATOM   4075 N N   . GLY B 1 282 ? 47.968 3.027   -6.465  1.00 48.31  ?  282 GLY B N   1 
ATOM   4076 C CA  . GLY B 1 282 ? 48.022 2.938   -7.911  1.00 52.29  ?  282 GLY B CA  1 
ATOM   4077 C C   . GLY B 1 282 ? 48.519 1.566   -8.302  1.00 67.68  ?  282 GLY B C   1 
ATOM   4078 O O   . GLY B 1 282 ? 48.614 0.660   -7.470  1.00 68.89  ?  282 GLY B O   1 
ATOM   4079 N N   . LYS B 1 283 ? 48.889 1.454   -9.569  1.00 68.44  ?  283 LYS B N   1 
ATOM   4080 C CA  . LYS B 1 283 ? 49.468 0.236   -10.051 1.00 69.00  ?  283 LYS B CA  1 
ATOM   4081 C C   . LYS B 1 283 ? 50.522 0.395   -11.095 1.00 68.85  ?  283 LYS B C   1 
ATOM   4082 O O   . LYS B 1 283 ? 50.493 1.341   -11.834 1.00 71.32  ?  283 LYS B O   1 
ATOM   4083 C CB  . LYS B 1 283 ? 48.426 -0.622  -10.658 1.00 85.13  ?  283 LYS B CB  1 
ATOM   4084 C CG  . LYS B 1 283 ? 48.580 -2.081  -10.265 1.00 96.66  ?  283 LYS B CG  1 
ATOM   4085 C CD  . LYS B 1 283 ? 49.514 -2.233  -9.068  1.00 94.85  ?  283 LYS B CD  1 
ATOM   4086 C CE  . LYS B 1 283 ? 50.684 -3.148  -9.392  1.00 86.16  ?  283 LYS B CE  1 
ATOM   4087 N NZ  . LYS B 1 283 ? 51.909 -2.802  -8.630  1.00 72.98  ?  283 LYS B NZ  1 
ATOM   4088 N N   . HIS B 1 284 ? 51.383 -0.595  -11.241 1.00 80.98  ?  284 HIS B N   1 
ATOM   4089 C CA  . HIS B 1 284 ? 52.541 -0.543  -12.109 1.00 78.59  ?  284 HIS B CA  1 
ATOM   4090 C C   . HIS B 1 284 ? 52.581 -1.227  -13.460 1.00 80.39  ?  284 HIS B C   1 
ATOM   4091 O O   . HIS B 1 284 ? 51.750 -2.050  -13.727 1.00 85.79  ?  284 HIS B O   1 
ATOM   4092 C CB  . HIS B 1 284 ? 53.518 -1.342  -11.303 1.00 78.83  ?  284 HIS B CB  1 
ATOM   4093 C CG  . HIS B 1 284 ? 54.721 -0.604  -10.837 1.00 79.86  ?  284 HIS B CG  1 
ATOM   4094 N ND1 . HIS B 1 284 ? 55.669 -1.205  -10.044 1.00 71.48  ?  284 HIS B ND1 1 
ATOM   4095 C CD2 . HIS B 1 284 ? 55.147 0.658   -11.053 1.00 83.05  ?  284 HIS B CD2 1 
ATOM   4096 C CE1 . HIS B 1 284 ? 56.627 -0.339  -9.783  1.00 80.81  ?  284 HIS B CE1 1 
ATOM   4097 N NE2 . HIS B 1 284 ? 56.337 0.797   -10.385 1.00 84.04  ?  284 HIS B NE2 1 
ATOM   4098 N N   . HIS B 1 285 ? 53.579 -0.939  -14.290 1.00 88.07  ?  285 HIS B N   1 
ATOM   4099 C CA  . HIS B 1 285 ? 53.788 -1.572  -15.608 1.00 95.06  ?  285 HIS B CA  1 
ATOM   4100 C C   . HIS B 1 285 ? 53.969 -3.097  -15.513 1.00 96.89  ?  285 HIS B C   1 
ATOM   4101 O O   . HIS B 1 285 ? 55.025 -3.649  -15.849 1.00 99.15  ?  285 HIS B O   1 
ATOM   4102 C CB  . HIS B 1 285 ? 54.993 -0.945  -16.304 1.00 104.86 ?  285 HIS B CB  1 
ATOM   4103 C CG  . HIS B 1 285 ? 54.980 0.552   -16.282 1.00 121.80 ?  285 HIS B CG  1 
ATOM   4104 N ND1 . HIS B 1 285 ? 54.235 1.307   -17.166 1.00 125.95 ?  285 HIS B ND1 1 
ATOM   4105 C CD2 . HIS B 1 285 ? 55.601 1.437   -15.462 1.00 125.88 ?  285 HIS B CD2 1 
ATOM   4106 C CE1 . HIS B 1 285 ? 54.412 2.591   -16.906 1.00 126.78 ?  285 HIS B CE1 1 
ATOM   4107 N NE2 . HIS B 1 285 ? 55.234 2.697   -15.874 1.00 127.02 ?  285 HIS B NE2 1 
HETATM 4108 O O   . HOH C 2 .   ? 21.311 -21.364 10.404  1.00 68.00  ?  301 HOH A O   1 
HETATM 4109 O O   . HOH C 2 .   ? 35.896 7.635   12.227  1.00 73.34  ?  302 HOH A O   1 
HETATM 4110 O O   . HOH C 2 .   ? 19.984 -23.564 7.017   1.00 55.52  ?  303 HOH A O   1 
HETATM 4111 O O   . HOH C 2 .   ? 21.519 -19.194 24.655  1.00 64.00  ?  304 HOH A O   1 
HETATM 4112 O O   . HOH C 2 .   ? 29.284 9.272   -0.611  1.00 79.22  ?  305 HOH A O   1 
HETATM 4113 O O   . HOH C 2 .   ? 20.116 -25.517 11.241  1.00 67.90  ?  306 HOH A O   1 
HETATM 4114 O O   . HOH C 2 .   ? 46.483 3.255   6.176   1.00 61.22  ?  307 HOH A O   1 
HETATM 4115 O O   . HOH C 2 .   ? 36.050 -21.984 7.728   1.00 62.90  ?  308 HOH A O   1 
HETATM 4116 O O   . HOH C 2 .   ? 43.745 -27.664 29.355  1.00 74.46  ?  309 HOH A O   1 
HETATM 4117 O O   . HOH C 2 .   ? 27.351 -36.784 11.684  1.00 59.57  ?  310 HOH A O   1 
HETATM 4118 O O   . HOH C 2 .   ? 44.553 -18.242 -4.749  1.00 74.77  ?  311 HOH A O   1 
HETATM 4119 O O   . HOH C 2 .   ? 53.691 -3.735  20.545  1.00 34.22  ?  312 HOH A O   1 
HETATM 4120 O O   . HOH C 2 .   ? 33.848 -25.190 4.825   1.00 26.69  ?  313 HOH A O   1 
HETATM 4121 O O   . HOH C 2 .   ? 51.145 3.906   25.174  1.00 63.79  ?  314 HOH A O   1 
HETATM 4122 O O   . HOH C 2 .   ? 42.868 -23.315 2.492   1.00 56.61  ?  315 HOH A O   1 
HETATM 4123 O O   . HOH C 2 .   ? 44.835 -32.740 9.644   1.00 71.20  ?  316 HOH A O   1 
HETATM 4124 O O   . HOH C 2 .   ? 39.539 -30.108 4.979   1.00 62.16  ?  317 HOH A O   1 
HETATM 4125 O O   . HOH C 2 .   ? 41.249 -23.452 1.223   1.00 57.22  ?  318 HOH A O   1 
HETATM 4126 O O   . HOH C 2 .   ? 35.729 -0.407  19.970  1.00 66.22  ?  319 HOH A O   1 
HETATM 4127 O O   . HOH C 2 .   ? 45.067 -26.514 5.127   1.00 61.41  ?  320 HOH A O   1 
HETATM 4128 O O   . HOH C 2 .   ? 40.406 -34.469 6.580   1.00 66.15  ?  321 HOH A O   1 
HETATM 4129 O O   . HOH C 2 .   ? 39.666 -34.925 9.329   1.00 66.26  ?  322 HOH A O   1 
HETATM 4130 O O   . HOH C 2 .   ? 32.433 -26.724 8.559   1.00 63.87  ?  323 HOH A O   1 
HETATM 4131 O O   . HOH C 2 .   ? 55.239 -13.984 7.908   1.00 57.41  ?  324 HOH A O   1 
HETATM 4132 O O   . HOH D 2 .   ? 58.883 -3.818  -11.616 1.00 58.22  ?  301 HOH B O   1 
HETATM 4133 O O   . HOH D 2 .   ? 59.718 12.751  11.995  1.00 66.69  ?  302 HOH B O   1 
HETATM 4134 O O   . HOH D 2 .   ? 79.089 1.021   -10.955 1.00 62.90  ?  303 HOH B O   1 
HETATM 4135 O O   . HOH D 2 .   ? 54.977 -3.116  -6.220  1.00 49.38  ?  304 HOH B O   1 
HETATM 4136 O O   . HOH D 2 .   ? 81.746 11.601  3.235   1.00 73.34  ?  305 HOH B O   1 
HETATM 4137 O O   . HOH D 2 .   ? 54.015 -11.310 7.139   1.00 48.71  ?  306 HOH B O   1 
HETATM 4138 O O   . HOH D 2 .   ? 48.492 -5.404  -0.894  1.00 59.75  ?  307 HOH B O   1 
HETATM 4139 O O   . HOH D 2 .   ? 67.489 -21.007 9.595   1.00 77.53  ?  308 HOH B O   1 
HETATM 4140 O O   . HOH D 2 .   ? 64.548 17.105  -4.159  1.00 65.07  ?  309 HOH B O   1 
HETATM 4141 O O   . HOH D 2 .   ? 75.940 13.621  0.044   1.00 65.77  ?  310 HOH B O   1 
HETATM 4142 O O   . HOH D 2 .   ? 49.934 -10.495 -2.018  1.00 59.30  ?  311 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 6   ? 1.0526 0.7145 1.1148 -0.0212 0.2561  -0.0605 6   LEU A N   
2    C CA  . LEU A 6   ? 1.2092 0.8739 1.2542 -0.0250 0.2542  -0.0689 6   LEU A CA  
3    C C   . LEU A 6   ? 1.3491 1.0069 1.4128 -0.0175 0.2710  -0.0633 6   LEU A C   
4    O O   . LEU A 6   ? 1.3334 1.0018 1.3948 -0.0150 0.2658  -0.0600 6   LEU A O   
5    C CB  . LEU A 6   ? 1.2243 0.8762 1.2396 -0.0390 0.2584  -0.0908 6   LEU A CB  
6    C CG  . LEU A 6   ? 1.1355 0.7956 1.1267 -0.0456 0.2502  -0.0998 6   LEU A CG  
7    C CD1 . LEU A 6   ? 1.0755 0.7356 1.0366 -0.0598 0.2425  -0.1155 6   LEU A CD1 
8    C CD2 . LEU A 6   ? 1.0313 0.6797 1.0248 -0.0450 0.2682  -0.1049 6   LEU A CD2 
9    N N   . SER A 7   ? 1.5868 1.2266 1.6704 -0.0137 0.2920  -0.0617 7   SER A N   
10   C CA  . SER A 7   ? 1.6119 1.2383 1.7127 -0.0081 0.3142  -0.0603 7   SER A CA  
11   C C   . SER A 7   ? 1.6437 1.2729 1.7834 0.0055  0.3226  -0.0385 7   SER A C   
12   O O   . SER A 7   ? 1.6390 1.2491 1.7987 0.0098  0.3462  -0.0376 7   SER A O   
13   C CB  . SER A 7   ? 1.4795 1.0777 1.5669 -0.0178 0.3364  -0.0813 7   SER A CB  
14   O OG  . SER A 7   ? 1.3154 0.9129 1.3708 -0.0292 0.3328  -0.0989 7   SER A OG  
15   N N   . GLU A 8   ? 1.5689 1.2224 1.7204 0.0121  0.3037  -0.0201 8   GLU A N   
16   C CA  . GLU A 8   ? 1.3837 1.0456 1.5718 0.0242  0.3085  0.0032  8   GLU A CA  
17   C C   . GLU A 8   ? 1.3465 1.0265 1.5517 0.0327  0.3050  0.0194  8   GLU A C   
18   O O   . GLU A 8   ? 1.3205 0.9969 1.5556 0.0421  0.3216  0.0325  8   GLU A O   
19   C CB  . GLU A 8   ? 1.1384 0.8160 1.3293 0.0244  0.2909  0.0136  8   GLU A CB  
20   C CG  . GLU A 8   ? 1.2982 0.9613 1.4685 0.0148  0.2904  -0.0029 8   GLU A CG  
21   C CD  . GLU A 8   ? 1.2660 0.9376 1.4010 0.0045  0.2705  -0.0173 8   GLU A CD  
22   O OE1 . GLU A 8   ? 1.0970 0.7917 1.2293 0.0065  0.2508  -0.0078 8   GLU A OE1 
23   O OE2 . GLU A 8   ? 1.3312 0.9873 1.4422 -0.0057 0.2749  -0.0374 8   GLU A OE2 
24   N N   . LEU A 9   ? 1.2749 0.9741 1.4621 0.0294  0.2843  0.0187  9   LEU A N   
25   C CA  . LEU A 9   ? 1.2339 0.9505 1.4395 0.0371  0.2816  0.0352  9   LEU A CA  
26   C C   . LEU A 9   ? 1.2027 0.9084 1.4011 0.0363  0.2941  0.0248  9   LEU A C   
27   O O   . LEU A 9   ? 1.1687 0.8624 1.3378 0.0271  0.2943  0.0042  9   LEU A O   
28   C CB  . LEU A 9   ? 1.2048 0.9485 1.4002 0.0350  0.2550  0.0427  9   LEU A CB  
29   C CG  . LEU A 9   ? 1.1822 0.9495 1.4082 0.0437  0.2497  0.0689  9   LEU A CG  
30   C CD1 . LEU A 9   ? 1.1760 0.9402 1.4322 0.0509  0.2620  0.0839  9   LEU A CD1 
31   C CD2 . LEU A 9   ? 1.1508 0.9432 1.3656 0.0397  0.2242  0.0750  9   LEU A CD2 
32   N N   . PRO A 10  ? 1.1784 0.8890 1.4045 0.0457  0.3052  0.0400  10  PRO A N   
33   C CA  . PRO A 10  ? 1.2425 0.9491 1.4633 0.0458  0.3135  0.0338  10  PRO A CA  
34   C C   . PRO A 10  ? 1.2598 0.9868 1.4607 0.0413  0.2908  0.0329  10  PRO A C   
35   O O   . PRO A 10  ? 1.1314 0.8824 1.3418 0.0442  0.2735  0.0489  10  PRO A O   
36   C CB  . PRO A 10  ? 1.2515 0.9627 1.5120 0.0583  0.3289  0.0549  10  PRO A CB  
37   C CG  . PRO A 10  ? 1.2151 0.9246 1.5004 0.0639  0.3348  0.0679  10  PRO A CG  
38   C CD  . PRO A 10  ? 1.1883 0.9070 1.4537 0.0569  0.3132  0.0639  10  PRO A CD  
39   N N   . MET A 11  ? 1.3241 1.0415 1.4974 0.0336  0.2917  0.0142  11  MET A N   
40   C CA  . MET A 11  ? 1.3021 1.0342 1.4554 0.0289  0.2743  0.0108  11  MET A CA  
41   C C   . MET A 11  ? 1.3479 1.0748 1.5019 0.0303  0.2872  0.0074  11  MET A C   
42   O O   . MET A 11  ? 1.3208 1.0265 1.4721 0.0288  0.3080  -0.0044 11  MET A O   
43   C CB  . MET A 11  ? 1.1747 0.9020 1.2924 0.0174  0.2620  -0.0082 11  MET A CB  
44   C CG  . MET A 11  ? 1.1456 0.8715 1.2606 0.0149  0.2546  -0.0089 11  MET A CG  
45   S SD  . MET A 11  ? 1.0406 0.7675 1.1191 0.0028  0.2365  -0.0257 11  MET A SD  
46   C CE  . MET A 11  ? 0.9642 0.6699 1.0176 -0.0069 0.2517  -0.0485 11  MET A CE  
47   N N   . PRO A 12  ? 1.3469 1.0923 1.5045 0.0327  0.2763  0.0170  12  PRO A N   
48   C CA  . PRO A 12  ? 1.2219 0.9629 1.3742 0.0322  0.2862  0.0113  12  PRO A CA  
49   C C   . PRO A 12  ? 1.1919 0.9229 1.3081 0.0209  0.2831  -0.0105 12  PRO A C   
50   O O   . PRO A 12  ? 1.2247 0.9580 1.3210 0.0141  0.2685  -0.0180 12  PRO A O   
51   C CB  . PRO A 12  ? 1.1740 0.9397 1.3362 0.0359  0.2706  0.0270  12  PRO A CB  
52   C CG  . PRO A 12  ? 1.2028 0.9832 1.3562 0.0323  0.2476  0.0304  12  PRO A CG  
53   C CD  . PRO A 12  ? 1.3135 1.0839 1.4737 0.0334  0.2530  0.0301  12  PRO A CD  
54   N N   . SER A 13  ? 1.2079 0.9287 1.3158 0.0185  0.2971  -0.0201 13  SER A N   
55   C CA  . SER A 13  ? 1.2847 1.0020 1.3586 0.0072  0.2917  -0.0377 13  SER A CA  
56   C C   . SER A 13  ? 1.2114 0.9441 1.2827 0.0082  0.2830  -0.0319 13  SER A C   
57   O O   . SER A 13  ? 1.2349 0.9629 1.3118 0.0103  0.2976  -0.0325 13  SER A O   
58   C CB  . SER A 13  ? 1.3685 1.0624 1.4289 0.0005  0.3138  -0.0559 13  SER A CB  
59   O OG  . SER A 13  ? 1.4656 1.1579 1.4920 -0.0122 0.3052  -0.0724 13  SER A OG  
60   N N   . PRO A 14  ? 1.1739 0.9248 1.2386 0.0069  0.2604  -0.0258 14  PRO A N   
61   C CA  . PRO A 14  ? 1.1657 0.9323 1.2349 0.0095  0.2523  -0.0165 14  PRO A CA  
62   C C   . PRO A 14  ? 1.0971 0.8595 1.1458 0.0031  0.2578  -0.0281 14  PRO A C   
63   O O   . PRO A 14  ? 1.1333 0.8885 1.1560 -0.0062 0.2569  -0.0430 14  PRO A O   
64   C CB  . PRO A 14  ? 1.1989 0.9821 1.2618 0.0075  0.2279  -0.0109 14  PRO A CB  
65   C CG  . PRO A 14  ? 1.1825 0.9569 1.2269 0.0009  0.2233  -0.0229 14  PRO A CG  
66   C CD  . PRO A 14  ? 1.1877 0.9446 1.2411 0.0029  0.2422  -0.0273 14  PRO A CD  
67   N N   . ALA A 15  ? 1.0299 0.7986 1.0909 0.0078  0.2633  -0.0200 15  ALA A N   
68   C CA  . ALA A 15  ? 0.9698 0.7384 1.0138 0.0025  0.2669  -0.0278 15  ALA A CA  
69   C C   . ALA A 15  ? 0.9801 0.7676 1.0192 0.0014  0.2465  -0.0203 15  ALA A C   
70   O O   . ALA A 15  ? 1.0700 0.8708 1.1282 0.0075  0.2368  -0.0057 15  ALA A O   
71   C CB  . ALA A 15  ? 1.0028 0.7656 1.0636 0.0082  0.2877  -0.0242 15  ALA A CB  
72   N N   . SER A 16  ? 0.8568 0.6460 0.8707 -0.0069 0.2405  -0.0300 16  SER A N   
73   C CA  . SER A 16  ? 0.9210 0.7261 0.9295 -0.0085 0.2223  -0.0238 16  SER A CA  
74   C C   . SER A 16  ? 1.0999 0.9162 1.1295 -0.0016 0.2222  -0.0096 16  SER A C   
75   O O   . SER A 16  ? 1.1918 1.0210 1.2325 0.0012  0.2080  0.0014  16  SER A O   
76   C CB  . SER A 16  ? 0.9049 0.7102 0.8865 -0.0177 0.2201  -0.0345 16  SER A CB  
77   O OG  . SER A 16  ? 0.9811 0.7825 0.9436 -0.0247 0.2133  -0.0443 16  SER A OG  
78   N N   . GLU A 17  ? 1.0931 0.9051 1.1287 0.0006  0.2385  -0.0096 17  GLU A N   
79   C CA  . GLU A 17  ? 1.1414 0.9660 1.1959 0.0062  0.2373  0.0041  17  GLU A CA  
80   C C   . GLU A 17  ? 1.0775 0.9089 1.1612 0.0146  0.2364  0.0191  17  GLU A C   
81   O O   . GLU A 17  ? 1.0586 0.9056 1.1564 0.0174  0.2264  0.0322  17  GLU A O   
82   C CB  . GLU A 17  ? 1.2845 1.1036 1.3392 0.0067  0.2554  0.0011  17  GLU A CB  
83   C CG  . GLU A 17  ? 1.3811 1.2140 1.4569 0.0127  0.2547  0.0163  17  GLU A CG  
84   C CD  . GLU A 17  ? 1.5691 1.3954 1.6618 0.0186  0.2771  0.0191  17  GLU A CD  
85   O OE1 . GLU A 17  ? 1.6633 1.4749 1.7417 0.0149  0.2933  0.0057  17  GLU A OE1 
86   O OE2 . GLU A 17  ? 1.6585 1.4946 1.7790 0.0265  0.2791  0.0347  17  GLU A OE2 
87   N N   . GLU A 18  ? 1.0604 0.8816 1.1537 0.0181  0.2461  0.0180  18  GLU A N   
88   C CA  . GLU A 18  ? 1.0943 0.9246 1.2161 0.0258  0.2441  0.0341  18  GLU A CA  
89   C C   . GLU A 18  ? 1.0031 0.8458 1.1222 0.0232  0.2222  0.0391  18  GLU A C   
90   O O   . GLU A 18  ? 0.9796 0.8381 1.1184 0.0268  0.2140  0.0545  18  GLU A O   
91   C CB  . GLU A 18  ? 1.0688 0.8842 1.2034 0.0306  0.2621  0.0326  18  GLU A CB  
92   C CG  . GLU A 18  ? 1.0897 0.8959 1.2376 0.0357  0.2856  0.0332  18  GLU A CG  
93   C CD  . GLU A 18  ? 1.1949 0.9878 1.3635 0.0424  0.3046  0.0358  18  GLU A CD  
94   O OE1 . GLU A 18  ? 1.1546 0.9371 1.3157 0.0400  0.3041  0.0284  18  GLU A OE1 
95   O OE2 . GLU A 18  ? 1.2892 1.0828 1.4837 0.0505  0.3202  0.0468  18  GLU A OE2 
96   N N   . VAL A 19  ? 0.8828 0.7193 0.9777 0.0164  0.2128  0.0266  19  VAL A N   
97   C CA  . VAL A 19  ? 0.9680 0.8155 1.0583 0.0134  0.1927  0.0300  19  VAL A CA  
98   C C   . VAL A 19  ? 0.9468 0.8084 1.0348 0.0108  0.1802  0.0353  19  VAL A C   
99   O O   . VAL A 19  ? 0.9506 0.8262 1.0483 0.0107  0.1675  0.0453  19  VAL A O   
100  C CB  . VAL A 19  ? 1.0194 0.8570 1.0859 0.0072  0.1871  0.0157  19  VAL A CB  
101  C CG1 . VAL A 19  ? 0.9359 0.7845 0.9963 0.0037  0.1669  0.0183  19  VAL A CG1 
102  C CG2 . VAL A 19  ? 0.8305 0.6551 0.9015 0.0094  0.1983  0.0116  19  VAL A CG2 
103  N N   . GLY A 20  ? 0.9284 0.7868 1.0035 0.0080  0.1841  0.0288  20  GLY A N   
104  C CA  . GLY A 20  ? 0.8825 0.7531 0.9581 0.0062  0.1750  0.0348  20  GLY A CA  
105  C C   . GLY A 20  ? 0.8509 0.7353 0.9524 0.0111  0.1752  0.0509  20  GLY A C   
106  O O   . GLY A 20  ? 0.8197 0.7174 0.9254 0.0087  0.1620  0.0584  20  GLY A O   
107  N N   . ALA A 21  ? 0.8278 0.7095 0.9474 0.0175  0.1907  0.0568  21  ALA A N   
108  C CA  . ALA A 21  ? 0.8191 0.7162 0.9661 0.0225  0.1914  0.0742  21  ALA A CA  
109  C C   . ALA A 21  ? 0.9031 0.8126 1.0632 0.0228  0.1796  0.0848  21  ALA A C   
110  O O   . ALA A 21  ? 0.8859 0.8134 1.0587 0.0216  0.1697  0.0973  21  ALA A O   
111  C CB  . ALA A 21  ? 0.8454 0.7359 1.0102 0.0301  0.2125  0.0785  21  ALA A CB  
112  N N   . LEU A 22  ? 0.8895 0.7906 1.0466 0.0236  0.1806  0.0802  22  LEU A N   
113  C CA  . LEU A 22  ? 0.9099 0.8235 1.0773 0.0229  0.1690  0.0899  22  LEU A CA  
114  C C   . LEU A 22  ? 0.9612 0.8856 1.1157 0.0150  0.1497  0.0885  22  LEU A C   
115  O O   . LEU A 22  ? 0.7595 0.7020 0.9265 0.0129  0.1395  0.1007  22  LEU A O   
116  C CB  . LEU A 22  ? 0.8503 0.7513 1.0123 0.0240  0.1725  0.0828  22  LEU A CB  
117  C CG  . LEU A 22  ? 0.8465 0.7597 1.0137 0.0218  0.1588  0.0903  22  LEU A CG  
118  C CD1 . LEU A 22  ? 0.7896 0.7213 0.9873 0.0266  0.1602  0.1112  22  LEU A CD1 
119  C CD2 . LEU A 22  ? 0.8428 0.7424 0.9996 0.0215  0.1605  0.0807  22  LEU A CD2 
120  N N   . TYR A 23  ? 1.0635 0.9773 1.1931 0.0100  0.1450  0.0738  23  TYR A N   
121  C CA  . TYR A 23  ? 0.9568 0.8773 1.0737 0.0029  0.1283  0.0710  23  TYR A CA  
122  C C   . TYR A 23  ? 0.9124 0.8434 1.0320 -0.0003 0.1230  0.0762  23  TYR A C   
123  O O   . TYR A 23  ? 0.7629 0.7050 0.8824 -0.0059 0.1103  0.0798  23  TYR A O   
124  C CB  . TYR A 23  ? 0.8986 0.8045 0.9907 -0.0006 0.1256  0.0551  23  TYR A CB  
125  C CG  . TYR A 23  ? 0.8780 0.7799 0.9684 -0.0003 0.1234  0.0525  23  TYR A CG  
126  C CD1 . TYR A 23  ? 0.8590 0.7700 0.9484 -0.0045 0.1101  0.0552  23  TYR A CD1 
127  C CD2 . TYR A 23  ? 0.7775 0.6666 0.8679 0.0037  0.1355  0.0476  23  TYR A CD2 
128  C CE1 . TYR A 23  ? 0.8870 0.7953 0.9753 -0.0043 0.1080  0.0537  23  TYR A CE1 
129  C CE2 . TYR A 23  ? 0.8474 0.7330 0.9372 0.0039  0.1336  0.0459  23  TYR A CE2 
130  C CZ  . TYR A 23  ? 0.9142 0.8101 1.0032 0.0002  0.1194  0.0495  23  TYR A CZ  
131  O OH  . TYR A 23  ? 0.9955 0.8892 1.0843 0.0002  0.1172  0.0486  23  TYR A OH  
132  N N   . ASP A 24  ? 0.8484 0.7761 0.9703 0.0026  0.1331  0.0763  24  ASP A N   
133  C CA  . ASP A 24  ? 0.7501 0.6898 0.8801 0.0007  0.1298  0.0844  24  ASP A CA  
134  C C   . ASP A 24  ? 0.8201 0.7790 0.9713 0.0000  0.1235  0.0998  24  ASP A C   
135  O O   . ASP A 24  ? 0.7446 0.7153 0.8963 -0.0063 0.1124  0.1039  24  ASP A O   
136  C CB  . ASP A 24  ? 0.7167 0.6520 0.8520 0.0055  0.1443  0.0853  24  ASP A CB  
137  C CG  . ASP A 24  ? 0.8411 0.7634 0.9539 0.0031  0.1472  0.0720  24  ASP A CG  
138  O OD1 . ASP A 24  ? 0.8587 0.7787 0.9552 -0.0024 0.1362  0.0649  24  ASP A OD1 
139  O OD2 . ASP A 24  ? 0.8994 0.8143 1.0110 0.0063  0.1607  0.0689  24  ASP A OD2 
140  N N   . ARG A 25  ? 0.8388 0.8017 1.0078 0.0058  0.1306  0.1088  25  ARG A N   
141  C CA  . ARG A 25  ? 0.7444 0.7287 0.9355 0.0051  0.1248  0.1259  25  ARG A CA  
142  C C   . ARG A 25  ? 0.8546 0.8466 1.0374 -0.0026 0.1093  0.1247  25  ARG A C   
143  O O   . ARG A 25  ? 0.9520 0.9624 1.1419 -0.0091 0.0988  0.1338  25  ARG A O   
144  C CB  . ARG A 25  ? 0.8270 0.8127 1.0405 0.0141  0.1379  0.1366  25  ARG A CB  
145  C CG  . ARG A 25  ? 0.9200 0.9303 1.1619 0.0153  0.1355  0.1581  25  ARG A CG  
146  C CD  . ARG A 25  ? 1.0523 1.0610 1.3192 0.0265  0.1539  0.1689  25  ARG A CD  
147  N NE  . ARG A 25  ? 1.1564 1.1387 1.4121 0.0323  0.1695  0.1542  25  ARG A NE  
148  C CZ  . ARG A 25  ? 1.1799 1.1486 1.4347 0.0363  0.1771  0.1491  25  ARG A CZ  
149  N NH1 . ARG A 25  ? 1.1761 1.1553 1.4415 0.0363  0.1704  0.1585  25  ARG A NH1 
150  N NH2 . ARG A 25  ? 1.1205 1.0657 1.3633 0.0397  0.1916  0.1345  25  ARG A NH2 
151  N N   . PHE A 26  ? 0.8185 0.7969 0.9857 -0.0029 0.1079  0.1131  26  PHE A N   
152  C CA  . PHE A 26  ? 0.7837 0.7672 0.9403 -0.0105 0.0940  0.1099  26  PHE A CA  
153  C C   . PHE A 26  ? 0.8122 0.7982 0.9556 -0.0191 0.0836  0.1041  26  PHE A C   
154  O O   . PHE A 26  ? 0.8228 0.8238 0.9688 -0.0269 0.0730  0.1096  26  PHE A O   
155  C CB  . PHE A 26  ? 0.7725 0.7388 0.9124 -0.0091 0.0951  0.0966  26  PHE A CB  
156  C CG  . PHE A 26  ? 0.8455 0.8106 0.9977 -0.0029 0.1023  0.1022  26  PHE A CG  
157  C CD1 . PHE A 26  ? 0.9103 0.8930 1.0869 -0.0004 0.1033  0.1199  26  PHE A CD1 
158  C CD2 . PHE A 26  ? 0.8581 0.8049 0.9982 0.0001  0.1084  0.0906  26  PHE A CD2 
159  C CE1 . PHE A 26  ? 0.8740 0.8550 1.0636 0.0058  0.1109  0.1260  26  PHE A CE1 
160  C CE2 . PHE A 26  ? 0.9161 0.8600 1.0679 0.0056  0.1160  0.0953  26  PHE A CE2 
161  C CZ  . PHE A 26  ? 0.8653 0.8258 1.0424 0.0089  0.1176  0.1132  26  PHE A CZ  
162  N N   . THR A 27  ? 0.7624 0.7337 0.8914 -0.0183 0.0873  0.0930  27  THR A N   
163  C CA  . THR A 27  ? 0.6590 0.6297 0.7759 -0.0255 0.0792  0.0870  27  THR A CA  
164  C C   . THR A 27  ? 0.8007 0.7877 0.9312 -0.0296 0.0761  0.0980  27  THR A C   
165  O O   . THR A 27  ? 0.8782 0.8727 1.0050 -0.0385 0.0662  0.0978  27  THR A O   
166  C CB  . THR A 27  ? 0.6253 0.5795 0.7274 -0.0229 0.0851  0.0760  27  THR A CB  
167  O OG1 . THR A 27  ? 0.8056 0.7461 0.8958 -0.0197 0.0885  0.0664  27  THR A OG1 
168  C CG2 . THR A 27  ? 0.6789 0.6311 0.7695 -0.0296 0.0774  0.0703  27  THR A CG2 
169  N N   . ALA A 28  ? 0.8854 0.8776 1.0316 -0.0236 0.0851  0.1074  28  ALA A N   
170  C CA  . ALA A 28  ? 0.8532 0.8602 1.0122 -0.0270 0.0833  0.1177  28  ALA A CA  
171  C C   . ALA A 28  ? 0.8680 0.8977 1.0416 -0.0333 0.0745  0.1308  28  ALA A C   
172  O O   . ALA A 28  ? 0.8503 0.8941 1.0322 -0.0391 0.0702  0.1386  28  ALA A O   
173  C CB  . ALA A 28  ? 0.8110 0.8176 0.9836 -0.0184 0.0965  0.1245  28  ALA A CB  
174  N N   . LEU A 29  ? 0.8405 0.8752 1.0172 -0.0331 0.0715  0.1339  29  LEU A N   
175  C CA  . LEU A 29  ? 0.8581 0.9156 1.0442 -0.0418 0.0610  0.1450  29  LEU A CA  
176  C C   . LEU A 29  ? 0.9338 0.9891 1.1004 -0.0536 0.0491  0.1339  29  LEU A C   
177  O O   . LEU A 29  ? 1.1147 1.1875 1.2842 -0.0646 0.0399  0.1396  29  LEU A O   
178  C CB  . LEU A 29  ? 0.8744 0.9416 1.0751 -0.0367 0.0631  0.1559  29  LEU A CB  
179  C CG  . LEU A 29  ? 0.8907 0.9580 1.1127 -0.0241 0.0771  0.1670  29  LEU A CG  
180  C CD1 . LEU A 29  ? 0.9018 0.9864 1.1430 -0.0220 0.0763  0.1828  29  LEU A CD1 
181  C CD2 . LEU A 29  ? 0.8129 0.8901 1.0496 -0.0228 0.0815  0.1767  29  LEU A CD2 
182  N N   . GLY A 30  ? 0.8882 0.9228 1.0353 -0.0521 0.0497  0.1181  30  GLY A N   
183  C CA  . GLY A 30  ? 0.7882 0.8193 0.9182 -0.0619 0.0403  0.1077  30  GLY A CA  
184  C C   . GLY A 30  ? 0.7998 0.8275 0.9239 -0.0604 0.0385  0.1041  30  GLY A C   
185  O O   . GLY A 30  ? 0.9044 0.9271 1.0133 -0.0675 0.0320  0.0943  30  GLY A O   
186  N N   . ALA A 31  ? 0.7211 0.7513 0.8576 -0.0514 0.0447  0.1123  31  ALA A N   
187  C CA  . ALA A 31  ? 0.7320 0.7562 0.8630 -0.0485 0.0447  0.1085  31  ALA A CA  
188  C C   . ALA A 31  ? 0.8327 0.8355 0.9411 -0.0490 0.0440  0.0904  31  ALA A C   
189  O O   . ALA A 31  ? 0.9750 0.9770 1.0727 -0.0545 0.0375  0.0844  31  ALA A O   
190  C CB  . ALA A 31  ? 0.6242 0.6456 0.7702 -0.0366 0.0556  0.1162  31  ALA A CB  
191  N N   . ALA A 32  ? 0.7957 0.7824 0.8970 -0.0440 0.0505  0.0823  32  ALA A N   
192  C CA  . ALA A 32  ? 0.7206 0.6904 0.8022 -0.0458 0.0489  0.0674  32  ALA A CA  
193  C C   . ALA A 32  ? 0.8106 0.7810 0.8889 -0.0518 0.0459  0.0653  32  ALA A C   
194  O O   . ALA A 32  ? 0.8748 0.8425 0.9570 -0.0481 0.0514  0.0672  32  ALA A O   
195  C CB  . ALA A 32  ? 0.5598 0.5127 0.6345 -0.0373 0.0577  0.0601  32  ALA A CB  
196  N N   . SER A 33  ? 0.6411 0.6141 0.7117 -0.0613 0.0380  0.0608  33  SER A N   
197  C CA  . SER A 33  ? 0.6844 0.6580 0.7528 -0.0686 0.0352  0.0588  33  SER A CA  
198  C C   . SER A 33  ? 0.6504 0.6061 0.7034 -0.0694 0.0356  0.0458  33  SER A C   
199  O O   . SER A 33  ? 0.5667 0.5124 0.6100 -0.0665 0.0358  0.0384  33  SER A O   
200  C CB  . SER A 33  ? 0.6611 0.6516 0.7333 -0.0804 0.0272  0.0636  33  SER A CB  
201  O OG  . SER A 33  ? 1.0447 1.0430 1.1226 -0.0872 0.0256  0.0676  33  SER A OG  
202  N N   . LEU A 34  ? 0.6541 0.6065 0.7064 -0.0733 0.0358  0.0441  34  LEU A N   
203  C CA  . LEU A 34  ? 0.5942 0.5307 0.6353 -0.0735 0.0371  0.0343  34  LEU A CA  
204  C C   . LEU A 34  ? 0.6921 0.6223 0.7228 -0.0780 0.0336  0.0253  34  LEU A C   
205  O O   . LEU A 34  ? 0.6913 0.6286 0.7212 -0.0873 0.0288  0.0243  34  LEU A O   
206  C CB  . LEU A 34  ? 0.5735 0.5094 0.6176 -0.0795 0.0372  0.0347  34  LEU A CB  
207  C CG  . LEU A 34  ? 0.5932 0.5271 0.6426 -0.0734 0.0426  0.0395  34  LEU A CG  
208  C CD1 . LEU A 34  ? 0.5812 0.5170 0.6355 -0.0809 0.0419  0.0413  34  LEU A CD1 
209  C CD2 . LEU A 34  ? 0.7077 0.6279 0.7486 -0.0655 0.0470  0.0344  34  LEU A CD2 
210  N N   . GLY A 35  ? 0.7715 0.6887 0.7937 -0.0722 0.0362  0.0188  35  GLY A N   
211  C CA  . GLY A 35  ? 0.6088 0.5188 0.6217 -0.0752 0.0340  0.0104  35  GLY A CA  
212  C C   . GLY A 35  ? 0.5943 0.5096 0.6051 -0.0740 0.0314  0.0106  35  GLY A C   
213  O O   . GLY A 35  ? 0.6760 0.5876 0.6796 -0.0776 0.0292  0.0041  35  GLY A O   
214  N N   . GLU A 36  ? 0.5381 0.4615 0.5559 -0.0689 0.0324  0.0179  36  GLU A N   
215  C CA  . GLU A 36  ? 0.6262 0.5543 0.6437 -0.0673 0.0307  0.0191  36  GLU A CA  
216  C C   . GLU A 36  ? 0.5897 0.5076 0.6023 -0.0583 0.0351  0.0156  36  GLU A C   
217  O O   . GLU A 36  ? 0.6353 0.5472 0.6479 -0.0526 0.0401  0.0158  36  GLU A O   
218  C CB  . GLU A 36  ? 0.5894 0.5339 0.6199 -0.0679 0.0295  0.0305  36  GLU A CB  
219  C CG  . GLU A 36  ? 0.6724 0.6293 0.7053 -0.0794 0.0236  0.0331  36  GLU A CG  
220  C CD  . GLU A 36  ? 0.7544 0.7315 0.8008 -0.0819 0.0209  0.0460  36  GLU A CD  
221  O OE1 . GLU A 36  ? 0.8509 0.8321 0.9090 -0.0738 0.0254  0.0548  36  GLU A OE1 
222  O OE2 . GLU A 36  ? 0.7997 0.7892 0.8453 -0.0925 0.0147  0.0477  36  GLU A OE2 
223  N N   . ASN A 37  ? 0.6099 0.5259 0.6170 -0.0581 0.0332  0.0120  37  ASN A N   
224  C CA  . ASN A 37  ? 0.6480 0.5558 0.6503 -0.0512 0.0368  0.0086  37  ASN A CA  
225  C C   . ASN A 37  ? 0.6982 0.6122 0.7096 -0.0467 0.0397  0.0157  37  ASN A C   
226  O O   . ASN A 37  ? 0.7025 0.6277 0.7210 -0.0497 0.0364  0.0218  37  ASN A O   
227  C CB  . ASN A 37  ? 0.5579 0.4606 0.5506 -0.0535 0.0335  0.0013  37  ASN A CB  
228  C CG  . ASN A 37  ? 0.6802 0.5732 0.6649 -0.0546 0.0337  -0.0056 37  ASN A CG  
229  O OD1 . ASN A 37  ? 0.7632 0.6508 0.7470 -0.0509 0.0371  -0.0058 37  ASN A OD1 
230  N ND2 . ASN A 37  ? 0.6011 0.4922 0.5805 -0.0596 0.0306  -0.0109 37  ASN A ND2 
231  N N   . LEU A 38  ? 0.7360 0.6432 0.7477 -0.0401 0.0466  0.0153  38  LEU A N   
232  C CA  . LEU A 38  ? 0.6468 0.5567 0.6678 -0.0352 0.0518  0.0210  38  LEU A CA  
233  C C   . LEU A 38  ? 0.6099 0.5114 0.6236 -0.0328 0.0535  0.0150  38  LEU A C   
234  O O   . LEU A 38  ? 0.6284 0.5215 0.6402 -0.0283 0.0607  0.0122  38  LEU A O   
235  C CB  . LEU A 38  ? 0.6253 0.5329 0.6527 -0.0303 0.0601  0.0243  38  LEU A CB  
236  C CG  . LEU A 38  ? 0.6266 0.5424 0.6605 -0.0333 0.0579  0.0299  38  LEU A CG  
237  C CD1 . LEU A 38  ? 0.5108 0.4236 0.5486 -0.0290 0.0659  0.0319  38  LEU A CD1 
238  C CD2 . LEU A 38  ? 0.5795 0.5107 0.6267 -0.0362 0.0537  0.0402  38  LEU A CD2 
239  N N   . HIS A 39  ? 0.5295 0.4333 0.5385 -0.0365 0.0471  0.0127  39  HIS A N   
240  C CA  . HIS A 39  ? 0.6201 0.5165 0.6223 -0.0346 0.0483  0.0073  39  HIS A CA  
241  C C   . HIS A 39  ? 0.6074 0.5107 0.6089 -0.0389 0.0415  0.0082  39  HIS A C   
242  O O   . HIS A 39  ? 0.6638 0.5769 0.6680 -0.0442 0.0360  0.0117  39  HIS A O   
243  C CB  . HIS A 39  ? 0.7441 0.6291 0.7326 -0.0341 0.0495  -0.0023 39  HIS A CB  
244  C CG  . HIS A 39  ? 0.7680 0.6525 0.7492 -0.0382 0.0439  -0.0065 39  HIS A CG  
245  N ND1 . HIS A 39  ? 0.8363 0.7173 0.8142 -0.0381 0.0453  -0.0081 39  HIS A ND1 
246  C CD2 . HIS A 39  ? 0.7494 0.6353 0.7263 -0.0424 0.0382  -0.0095 39  HIS A CD2 
247  C CE1 . HIS A 39  ? 0.7236 0.6036 0.6970 -0.0416 0.0409  -0.0113 39  HIS A CE1 
248  N NE2 . HIS A 39  ? 0.6620 0.5444 0.6344 -0.0444 0.0369  -0.0128 39  HIS A NE2 
249  N N   . PHE A 40  ? 0.6338 0.5328 0.6317 -0.0373 0.0423  0.0052  40  PHE A N   
250  C CA  . PHE A 40  ? 0.6005 0.5069 0.5984 -0.0411 0.0366  0.0070  40  PHE A CA  
251  C C   . PHE A 40  ? 0.6414 0.5465 0.6278 -0.0468 0.0307  -0.0003 40  PHE A C   
252  O O   . PHE A 40  ? 0.7547 0.6506 0.7327 -0.0462 0.0316  -0.0076 40  PHE A O   
253  C CB  . PHE A 40  ? 0.7100 0.6108 0.7069 -0.0377 0.0396  0.0055  40  PHE A CB  
254  C CG  . PHE A 40  ? 0.7236 0.6266 0.7346 -0.0328 0.0461  0.0140  40  PHE A CG  
255  C CD1 . PHE A 40  ? 0.6621 0.5783 0.6854 -0.0336 0.0438  0.0249  40  PHE A CD1 
256  C CD2 . PHE A 40  ? 0.5824 0.4749 0.5951 -0.0277 0.0551  0.0118  40  PHE A CD2 
257  C CE1 . PHE A 40  ? 0.6379 0.5564 0.6773 -0.0282 0.0509  0.0347  40  PHE A CE1 
258  C CE2 . PHE A 40  ? 0.7035 0.5963 0.7304 -0.0229 0.0629  0.0194  40  PHE A CE2 
259  C CZ  . PHE A 40  ? 0.6625 0.5682 0.7042 -0.0225 0.0611  0.0315  40  PHE A CZ  
260  N N   . GLY A 41  ? 0.6618 0.5768 0.6485 -0.0526 0.0251  0.0020  41  GLY A N   
261  C CA  . GLY A 41  ? 0.5455 0.4576 0.5211 -0.0578 0.0213  -0.0061 41  GLY A CA  
262  C C   . GLY A 41  ? 0.6148 0.5197 0.5840 -0.0550 0.0221  -0.0112 41  GLY A C   
263  O O   . GLY A 41  ? 0.7316 0.6371 0.7054 -0.0512 0.0242  -0.0074 41  GLY A O   
264  N N   . TYR A 42  ? 0.6185 0.5162 0.5780 -0.0568 0.0212  -0.0196 42  TYR A N   
265  C CA  . TYR A 42  ? 0.7159 0.6088 0.6692 -0.0556 0.0212  -0.0243 42  TYR A CA  
266  C C   . TYR A 42  ? 0.7247 0.6212 0.6721 -0.0622 0.0177  -0.0282 42  TYR A C   
267  O O   . TYR A 42  ? 0.8345 0.7284 0.7782 -0.0661 0.0175  -0.0328 42  TYR A O   
268  C CB  . TYR A 42  ? 0.6529 0.5347 0.6006 -0.0514 0.0241  -0.0301 42  TYR A CB  
269  C CG  . TYR A 42  ? 0.6532 0.5311 0.5954 -0.0502 0.0240  -0.0342 42  TYR A CG  
270  C CD1 . TYR A 42  ? 0.6865 0.5636 0.6234 -0.0533 0.0222  -0.0388 42  TYR A CD1 
271  C CD2 . TYR A 42  ? 0.6899 0.5646 0.6323 -0.0464 0.0265  -0.0336 42  TYR A CD2 
272  C CE1 . TYR A 42  ? 0.6701 0.5447 0.6028 -0.0521 0.0221  -0.0418 42  TYR A CE1 
273  C CE2 . TYR A 42  ? 0.7726 0.6446 0.7102 -0.0459 0.0262  -0.0371 42  TYR A CE2 
274  C CZ  . TYR A 42  ? 0.7564 0.6290 0.6895 -0.0486 0.0236  -0.0407 42  TYR A CZ  
275  O OH  . TYR A 42  ? 0.8908 0.7616 0.8198 -0.0481 0.0233  -0.0435 42  TYR A OH  
276  N N   . TRP A 43  ? 0.7729 0.6748 0.7196 -0.0635 0.0157  -0.0267 43  TRP A N   
277  C CA  . TRP A 43  ? 0.7287 0.6346 0.6687 -0.0704 0.0131  -0.0307 43  TRP A CA  
278  C C   . TRP A 43  ? 0.8196 0.7210 0.7549 -0.0679 0.0137  -0.0344 43  TRP A C   
279  O O   . TRP A 43  ? 0.8331 0.7356 0.7723 -0.0638 0.0141  -0.0302 43  TRP A O   
280  C CB  . TRP A 43  ? 0.5806 0.5018 0.5239 -0.0767 0.0091  -0.0238 43  TRP A CB  
281  C CG  . TRP A 43  ? 0.7222 0.6522 0.6700 -0.0817 0.0072  -0.0192 43  TRP A CG  
282  C CD1 . TRP A 43  ? 0.6847 0.6191 0.6270 -0.0913 0.0053  -0.0231 43  TRP A CD1 
283  C CD2 . TRP A 43  ? 0.7046 0.6410 0.6639 -0.0781 0.0075  -0.0094 43  TRP A CD2 
284  N NE1 . TRP A 43  ? 0.7036 0.6475 0.6529 -0.0942 0.0035  -0.0161 43  TRP A NE1 
285  C CE2 . TRP A 43  ? 0.6591 0.6048 0.6196 -0.0858 0.0048  -0.0071 43  TRP A CE2 
286  C CE3 . TRP A 43  ? 0.6810 0.6155 0.6499 -0.0696 0.0106  -0.0027 43  TRP A CE3 
287  C CZ2 . TRP A 43  ? 0.6740 0.6286 0.6459 -0.0845 0.0045  0.0028  43  TRP A CZ2 
288  C CZ3 . TRP A 43  ? 0.7117 0.6535 0.6921 -0.0679 0.0115  0.0065  43  TRP A CZ3 
289  C CH2 . TRP A 43  ? 0.7264 0.6790 0.7087 -0.0750 0.0080  0.0097  43  TRP A CH2 
290  N N   . ASP A 44  ? 0.8831 0.7797 0.8110 -0.0709 0.0144  -0.0420 44  ASP A N   
291  C CA  . ASP A 44  ? 0.7921 0.6848 0.7157 -0.0689 0.0152  -0.0457 44  ASP A CA  
292  C C   . ASP A 44  ? 0.8701 0.7726 0.7932 -0.0722 0.0124  -0.0422 44  ASP A C   
293  O O   . ASP A 44  ? 1.0136 0.9142 0.9361 -0.0690 0.0128  -0.0423 44  ASP A O   
294  C CB  . ASP A 44  ? 0.8124 0.6982 0.7303 -0.0713 0.0179  -0.0538 44  ASP A CB  
295  C CG  . ASP A 44  ? 0.9850 0.8621 0.9051 -0.0679 0.0209  -0.0557 44  ASP A CG  
296  O OD1 . ASP A 44  ? 1.0531 0.9253 0.9752 -0.0615 0.0221  -0.0545 44  ASP A OD1 
297  O OD2 . ASP A 44  ? 1.0569 0.9327 0.9767 -0.0723 0.0221  -0.0581 44  ASP A OD2 
298  N N   . SER A 45  ? 0.9265 0.8406 0.8500 -0.0790 0.0094  -0.0383 45  SER A N   
299  C CA  . SER A 45  ? 0.9482 0.8738 0.8723 -0.0821 0.0064  -0.0330 45  SER A CA  
300  C C   . SER A 45  ? 0.9406 0.8809 0.8718 -0.0859 0.0029  -0.0228 45  SER A C   
301  O O   . SER A 45  ? 0.9330 0.8757 0.8652 -0.0892 0.0023  -0.0225 45  SER A O   
302  C CB  . SER A 45  ? 0.9679 0.8961 0.8820 -0.0896 0.0060  -0.0396 45  SER A CB  
303  O OG  . SER A 45  ? 1.0452 0.9836 0.9554 -0.0997 0.0037  -0.0396 45  SER A OG  
304  N N   . PRO A 46  ? 0.8567 0.8081 0.7940 -0.0856 0.0008  -0.0134 46  PRO A N   
305  C CA  . PRO A 46  ? 0.8516 0.8179 0.8001 -0.0869 -0.0018 -0.0005 46  PRO A CA  
306  C C   . PRO A 46  ? 0.9533 0.9351 0.8978 -0.0983 -0.0065 0.0014  46  PRO A C   
307  O O   . PRO A 46  ? 0.9735 0.9671 0.9272 -0.0999 -0.0086 0.0112  46  PRO A O   
308  C CB  . PRO A 46  ? 0.8168 0.7911 0.7729 -0.0841 -0.0024 0.0091  46  PRO A CB  
309  C CG  . PRO A 46  ? 0.8219 0.7818 0.7720 -0.0793 0.0007  0.0006  46  PRO A CG  
310  C CD  . PRO A 46  ? 0.8131 0.7641 0.7496 -0.0832 0.0011  -0.0127 46  PRO A CD  
311  N N   . ASP A 47  ? 0.9841 0.9670 0.9154 -0.1071 -0.0077 -0.0074 47  ASP A N   
312  C CA  . ASP A 47  ? 1.1414 1.1405 1.0669 -0.1204 -0.0119 -0.0062 47  ASP A CA  
313  C C   . ASP A 47  ? 1.2447 1.2348 1.1616 -0.1263 -0.0098 -0.0176 47  ASP A C   
314  O O   . ASP A 47  ? 1.4565 1.4597 1.3702 -0.1376 -0.0131 -0.0160 47  ASP A O   
315  C CB  . ASP A 47  ? 1.1537 1.1635 1.0696 -0.1290 -0.0143 -0.0076 47  ASP A CB  
316  C CG  . ASP A 47  ? 1.1699 1.1624 1.0757 -0.1262 -0.0095 -0.0209 47  ASP A CG  
317  O OD1 . ASP A 47  ? 1.1632 1.1372 1.0669 -0.1209 -0.0048 -0.0306 47  ASP A OD1 
318  O OD2 . ASP A 47  ? 1.1813 1.1798 1.0824 -0.1289 -0.0104 -0.0204 47  ASP A OD2 
319  N N   . SER A 48  ? 1.1453 1.1144 1.0592 -0.1194 -0.0044 -0.0281 48  SER A N   
320  C CA  . SER A 48  ? 1.0686 1.0279 0.9768 -0.1239 -0.0013 -0.0378 48  SER A CA  
321  C C   . SER A 48  ? 0.9369 0.9065 0.8519 -0.1277 -0.0044 -0.0304 48  SER A C   
322  O O   . SER A 48  ? 0.8983 0.8734 0.8252 -0.1205 -0.0062 -0.0195 48  SER A O   
323  C CB  . SER A 48  ? 1.0329 0.9711 0.9426 -0.1132 0.0043  -0.0447 48  SER A CB  
324  O OG  . SER A 48  ? 0.9178 0.8530 0.8368 -0.1065 0.0045  -0.0393 48  SER A OG  
325  N N   . GLN A 49  ? 0.9669 0.9396 0.8744 -0.1398 -0.0045 -0.0364 49  GLN A N   
326  C CA  . GLN A 49  ? 1.0664 1.0521 0.9796 -0.1458 -0.0083 -0.0290 49  GLN A CA  
327  C C   . GLN A 49  ? 0.9458 0.9171 0.8612 -0.1430 -0.0041 -0.0346 49  GLN A C   
328  O O   . GLN A 49  ? 0.9414 0.9209 0.8577 -0.1515 -0.0061 -0.0327 49  GLN A O   
329  C CB  . GLN A 49  ? 1.1447 1.1487 1.0485 -0.1639 -0.0124 -0.0297 49  GLN A CB  
330  C CG  . GLN A 49  ? 1.1745 1.2045 1.0838 -0.1677 -0.0198 -0.0146 49  GLN A CG  
331  C CD  . GLN A 49  ? 1.3143 1.3425 1.2258 -0.1586 -0.0194 -0.0112 49  GLN A CD  
332  O OE1 . GLN A 49  ? 1.5044 1.5179 1.4065 -0.1568 -0.0151 -0.0227 49  GLN A OE1 
333  N NE2 . GLN A 49  ? 1.2152 1.2574 1.1405 -0.1522 -0.0231 0.0048  49  GLN A NE2 
334  N N   . VAL A 50  ? 0.9280 0.8792 0.8442 -0.1321 0.0014  -0.0410 50  VAL A N   
335  C CA  . VAL A 50  ? 0.7897 0.7277 0.7103 -0.1270 0.0053  -0.0437 50  VAL A CA  
336  C C   . VAL A 50  ? 0.7875 0.7368 0.7196 -0.1243 0.0018  -0.0316 50  VAL A C   
337  O O   . VAL A 50  ? 0.8066 0.7633 0.7470 -0.1170 -0.0004 -0.0217 50  VAL A O   
338  C CB  . VAL A 50  ? 0.7596 0.6796 0.6816 -0.1142 0.0103  -0.0479 50  VAL A CB  
339  C CG1 . VAL A 50  ? 0.7339 0.6438 0.6618 -0.1085 0.0135  -0.0478 50  VAL A CG1 
340  C CG2 . VAL A 50  ? 0.6508 0.5599 0.5635 -0.1170 0.0147  -0.0591 50  VAL A CG2 
341  N N   . PRO A 51  ? 0.7734 0.7245 0.7072 -0.1302 0.0018  -0.0318 51  PRO A N   
342  C CA  . PRO A 51  ? 0.7597 0.7244 0.7051 -0.1289 -0.0017 -0.0193 51  PRO A CA  
343  C C   . PRO A 51  ? 0.7413 0.6964 0.6965 -0.1142 0.0016  -0.0147 51  PRO A C   
344  O O   . PRO A 51  ? 0.6756 0.6138 0.6279 -0.1062 0.0061  -0.0214 51  PRO A O   
345  C CB  . PRO A 51  ? 0.6843 0.6510 0.6273 -0.1401 -0.0017 -0.0231 51  PRO A CB  
346  C CG  . PRO A 51  ? 0.7146 0.6723 0.6435 -0.1499 0.0011  -0.0370 51  PRO A CG  
347  C CD  . PRO A 51  ? 0.6997 0.6415 0.6254 -0.1395 0.0054  -0.0431 51  PRO A CD  
348  N N   . LEU A 52  ? 0.7608 0.7284 0.7280 -0.1115 -0.0004 -0.0025 52  LEU A N   
349  C CA  . LEU A 52  ? 0.6873 0.6481 0.6641 -0.0985 0.0034  0.0029  52  LEU A CA  
350  C C   . LEU A 52  ? 0.7025 0.6464 0.6768 -0.0939 0.0081  -0.0045 52  LEU A C   
351  O O   . LEU A 52  ? 0.7050 0.6362 0.6783 -0.0846 0.0121  -0.0076 52  LEU A O   
352  C CB  . LEU A 52  ? 0.6529 0.6305 0.6443 -0.0977 0.0015  0.0174  52  LEU A CB  
353  C CG  . LEU A 52  ? 0.6402 0.6104 0.6418 -0.0848 0.0071  0.0224  52  LEU A CG  
354  C CD1 . LEU A 52  ? 0.6080 0.5691 0.6078 -0.0766 0.0101  0.0204  52  LEU A CD1 
355  C CD2 . LEU A 52  ? 0.4926 0.4790 0.5105 -0.0838 0.0066  0.0372  52  LEU A CD2 
356  N N   . ALA A 53  ? 0.7164 0.6604 0.6893 -0.1011 0.0078  -0.0073 53  ALA A N   
357  C CA  . ALA A 53  ? 0.7652 0.6949 0.7380 -0.0965 0.0125  -0.0120 53  ALA A CA  
358  C C   . ALA A 53  ? 0.7845 0.6972 0.7489 -0.0921 0.0162  -0.0219 53  ALA A C   
359  O O   . ALA A 53  ? 0.8949 0.7976 0.8608 -0.0833 0.0198  -0.0223 53  ALA A O   
360  C CB  . ALA A 53  ? 0.6668 0.5992 0.6397 -0.1063 0.0118  -0.0136 53  ALA A CB  
361  N N   . GLU A 54  ? 0.7070 0.6173 0.6630 -0.0984 0.0156  -0.0294 54  GLU A N   
362  C CA  . GLU A 54  ? 0.6859 0.5812 0.6361 -0.0940 0.0197  -0.0375 54  GLU A CA  
363  C C   . GLU A 54  ? 0.7454 0.6392 0.6953 -0.0851 0.0195  -0.0355 54  GLU A C   
364  O O   . GLU A 54  ? 0.7394 0.6224 0.6875 -0.0786 0.0227  -0.0389 54  GLU A O   
365  C CB  . GLU A 54  ? 0.7724 0.6646 0.7140 -0.1035 0.0207  -0.0466 54  GLU A CB  
366  C CG  . GLU A 54  ? 0.9474 0.8447 0.8878 -0.1157 0.0200  -0.0486 54  GLU A CG  
367  C CD  . GLU A 54  ? 1.1114 1.0070 1.0419 -0.1273 0.0216  -0.0584 54  GLU A CD  
368  O OE1 . GLU A 54  ? 1.1000 0.9874 1.0252 -0.1247 0.0246  -0.0645 54  GLU A OE1 
369  O OE2 . GLU A 54  ? 1.0993 1.0027 1.0271 -0.1399 0.0201  -0.0599 54  GLU A OE2 
370  N N   . ALA A 55  ? 0.6562 0.5614 0.6086 -0.0850 0.0159  -0.0293 55  ALA A N   
371  C CA  . ALA A 55  ? 0.6382 0.5414 0.5914 -0.0769 0.0165  -0.0273 55  ALA A CA  
372  C C   . ALA A 55  ? 0.6596 0.5573 0.6179 -0.0683 0.0198  -0.0239 55  ALA A C   
373  O O   . ALA A 55  ? 0.6794 0.5693 0.6352 -0.0620 0.0222  -0.0262 55  ALA A O   
374  C CB  . ALA A 55  ? 0.7035 0.6203 0.6603 -0.0791 0.0129  -0.0202 55  ALA A CB  
375  N N   . THR A 56  ? 0.6726 0.5752 0.6378 -0.0687 0.0201  -0.0184 56  THR A N   
376  C CA  . THR A 56  ? 0.6832 0.5812 0.6528 -0.0616 0.0239  -0.0154 56  THR A CA  
377  C C   . THR A 56  ? 0.6362 0.5228 0.6008 -0.0592 0.0266  -0.0212 56  THR A C   
378  O O   . THR A 56  ? 0.6758 0.5566 0.6390 -0.0531 0.0296  -0.0215 56  THR A O   
379  C CB  . THR A 56  ? 0.8085 0.7151 0.7873 -0.0632 0.0238  -0.0080 56  THR A CB  
380  O OG1 . THR A 56  ? 0.9348 0.8553 0.9186 -0.0684 0.0198  -0.0019 56  THR A OG1 
381  C CG2 . THR A 56  ? 1.0446 0.9501 1.0297 -0.0555 0.0282  -0.0029 56  THR A CG2 
382  N N   . ASP A 57  ? 0.6267 0.5101 0.5887 -0.0643 0.0262  -0.0254 57  ASP A N   
383  C CA  . ASP A 57  ? 0.6400 0.5132 0.5995 -0.0615 0.0293  -0.0293 57  ASP A CA  
384  C C   . ASP A 57  ? 0.6301 0.4981 0.5839 -0.0582 0.0297  -0.0334 57  ASP A C   
385  O O   . ASP A 57  ? 0.6616 0.5243 0.6143 -0.0535 0.0319  -0.0336 57  ASP A O   
386  C CB  . ASP A 57  ? 0.7093 0.5789 0.6693 -0.0677 0.0303  -0.0327 57  ASP A CB  
387  C CG  . ASP A 57  ? 0.8752 0.7481 0.8413 -0.0695 0.0308  -0.0281 57  ASP A CG  
388  O OD1 . ASP A 57  ? 0.8952 0.7699 0.8650 -0.0640 0.0319  -0.0229 57  ASP A OD1 
389  O OD2 . ASP A 57  ? 0.9015 0.7754 0.8685 -0.0772 0.0305  -0.0301 57  ASP A OD2 
390  N N   . ARG A 58  ? 0.6440 0.5150 0.5946 -0.0611 0.0274  -0.0358 58  ARG A N   
391  C CA  . ARG A 58  ? 0.6539 0.5211 0.5996 -0.0583 0.0277  -0.0392 58  ARG A CA  
392  C C   . ARG A 58  ? 0.6836 0.5499 0.6289 -0.0518 0.0286  -0.0367 58  ARG A C   
393  O O   . ARG A 58  ? 0.7027 0.5646 0.6451 -0.0487 0.0299  -0.0384 58  ARG A O   
394  C CB  . ARG A 58  ? 0.6394 0.5121 0.5822 -0.0627 0.0248  -0.0408 58  ARG A CB  
395  C CG  . ARG A 58  ? 0.7119 0.5820 0.6504 -0.0600 0.0248  -0.0436 58  ARG A CG  
396  C CD  . ARG A 58  ? 0.6393 0.5016 0.5753 -0.0597 0.0276  -0.0488 58  ARG A CD  
397  N NE  . ARG A 58  ? 0.8619 0.7224 0.7951 -0.0557 0.0277  -0.0498 58  ARG A NE  
398  C CZ  . ARG A 58  ? 0.9852 0.8476 0.9149 -0.0576 0.0265  -0.0524 58  ARG A CZ  
399  N NH1 . ARG A 58  ? 1.0100 0.8768 0.9376 -0.0639 0.0250  -0.0543 58  ARG A NH1 
400  N NH2 . ARG A 58  ? 1.0306 0.8917 0.9585 -0.0539 0.0266  -0.0529 58  ARG A NH2 
401  N N   . LEU A 59  ? 0.6380 0.5088 0.5866 -0.0502 0.0286  -0.0323 59  LEU A N   
402  C CA  . LEU A 59  ? 0.6787 0.5472 0.6261 -0.0454 0.0311  -0.0313 59  LEU A CA  
403  C C   . LEU A 59  ? 0.7201 0.5848 0.6662 -0.0431 0.0335  -0.0311 59  LEU A C   
404  O O   . LEU A 59  ? 0.6547 0.5169 0.5960 -0.0410 0.0347  -0.0326 59  LEU A O   
405  C CB  . LEU A 59  ? 0.6082 0.4810 0.5615 -0.0440 0.0326  -0.0265 59  LEU A CB  
406  C CG  . LEU A 59  ? 0.6693 0.5383 0.6212 -0.0401 0.0369  -0.0267 59  LEU A CG  
407  C CD1 . LEU A 59  ? 0.6238 0.4899 0.5699 -0.0400 0.0361  -0.0307 59  LEU A CD1 
408  C CD2 . LEU A 59  ? 0.6431 0.5154 0.6038 -0.0382 0.0402  -0.0211 59  LEU A CD2 
409  N N   . THR A 60  ? 0.6237 0.4893 0.5741 -0.0442 0.0341  -0.0287 60  THR A N   
410  C CA  . THR A 60  ? 0.6518 0.5150 0.6018 -0.0423 0.0363  -0.0273 60  THR A CA  
411  C C   . THR A 60  ? 0.7565 0.6165 0.7033 -0.0415 0.0361  -0.0293 60  THR A C   
412  O O   . THR A 60  ? 0.6971 0.5573 0.6407 -0.0394 0.0372  -0.0280 60  THR A O   
413  C CB  . THR A 60  ? 0.5950 0.4593 0.5509 -0.0442 0.0368  -0.0245 60  THR A CB  
414  O OG1 . THR A 60  ? 0.5918 0.4612 0.5526 -0.0449 0.0369  -0.0211 60  THR A OG1 
415  C CG2 . THR A 60  ? 0.6348 0.4976 0.5910 -0.0420 0.0392  -0.0219 60  THR A CG2 
416  N N   . ASP A 61  ? 0.6990 0.5566 0.6466 -0.0438 0.0349  -0.0322 61  ASP A N   
417  C CA  . ASP A 61  ? 0.6651 0.5195 0.6128 -0.0424 0.0360  -0.0328 61  ASP A CA  
418  C C   . ASP A 61  ? 0.6665 0.5226 0.6091 -0.0404 0.0349  -0.0337 61  ASP A C   
419  O O   . ASP A 61  ? 0.6235 0.4806 0.5660 -0.0383 0.0355  -0.0311 61  ASP A O   
420  C CB  . ASP A 61  ? 0.5805 0.4305 0.5305 -0.0457 0.0369  -0.0366 61  ASP A CB  
421  C CG  . ASP A 61  ? 0.6495 0.4971 0.6043 -0.0489 0.0387  -0.0362 61  ASP A CG  
422  O OD1 . ASP A 61  ? 0.6899 0.5394 0.6474 -0.0475 0.0391  -0.0319 61  ASP A OD1 
423  O OD2 . ASP A 61  ? 0.7132 0.5571 0.6687 -0.0535 0.0400  -0.0406 61  ASP A OD2 
424  N N   . MET A 62  ? 0.6547 0.5121 0.5938 -0.0414 0.0331  -0.0365 62  MET A N   
425  C CA  . MET A 62  ? 0.6289 0.4875 0.5629 -0.0403 0.0322  -0.0377 62  MET A CA  
426  C C   . MET A 62  ? 0.6291 0.4900 0.5594 -0.0391 0.0333  -0.0357 62  MET A C   
427  O O   . MET A 62  ? 0.7126 0.5759 0.6394 -0.0388 0.0328  -0.0351 62  MET A O   
428  C CB  . MET A 62  ? 0.5787 0.4381 0.5111 -0.0418 0.0307  -0.0403 62  MET A CB  
429  C CG  . MET A 62  ? 0.8159 0.6760 0.7439 -0.0410 0.0308  -0.0412 62  MET A CG  
430  S SD  . MET A 62  ? 1.0298 0.8911 0.9585 -0.0425 0.0293  -0.0426 62  MET A SD  
431  C CE  . MET A 62  ? 0.7954 0.6594 0.7298 -0.0447 0.0283  -0.0405 62  MET A CE  
432  N N   . MET A 63  ? 0.6347 0.4957 0.5656 -0.0390 0.0351  -0.0344 63  MET A N   
433  C CA  . MET A 63  ? 0.7020 0.5646 0.6281 -0.0389 0.0373  -0.0335 63  MET A CA  
434  C C   . MET A 63  ? 0.7089 0.5748 0.6354 -0.0385 0.0373  -0.0294 63  MET A C   
435  O O   . MET A 63  ? 0.6148 0.4849 0.5357 -0.0397 0.0374  -0.0283 63  MET A O   
436  C CB  . MET A 63  ? 0.6603 0.5216 0.5879 -0.0386 0.0407  -0.0332 63  MET A CB  
437  C CG  . MET A 63  ? 0.6663 0.5257 0.5960 -0.0384 0.0413  -0.0351 63  MET A CG  
438  S SD  . MET A 63  ? 0.8024 0.6610 0.7379 -0.0370 0.0465  -0.0327 63  MET A SD  
439  C CE  . MET A 63  ? 0.5585 0.4146 0.4851 -0.0379 0.0522  -0.0356 63  MET A CE  
440  N N   . ALA A 64  ? 0.6987 0.5634 0.6321 -0.0376 0.0373  -0.0266 64  ALA A N   
441  C CA  . ALA A 64  ? 0.7245 0.5924 0.6604 -0.0367 0.0380  -0.0212 64  ALA A CA  
442  C C   . ALA A 64  ? 0.7329 0.6043 0.6691 -0.0360 0.0365  -0.0187 64  ALA A C   
443  O O   . ALA A 64  ? 0.7797 0.6579 0.7151 -0.0361 0.0364  -0.0132 64  ALA A O   
444  C CB  . ALA A 64  ? 0.4628 0.3272 0.4071 -0.0361 0.0392  -0.0190 64  ALA A CB  
445  N N   . GLU A 65  ? 0.5912 0.4597 0.5290 -0.0357 0.0354  -0.0219 65  GLU A N   
446  C CA  . GLU A 65  ? 0.6736 0.5462 0.6133 -0.0346 0.0345  -0.0186 65  GLU A CA  
447  C C   . GLU A 65  ? 0.7338 0.6140 0.6650 -0.0367 0.0324  -0.0181 65  GLU A C   
448  O O   . GLU A 65  ? 0.7493 0.6379 0.6816 -0.0368 0.0313  -0.0120 65  GLU A O   
449  C CB  . GLU A 65  ? 0.6960 0.5634 0.6391 -0.0340 0.0348  -0.0225 65  GLU A CB  
450  C CG  . GLU A 65  ? 0.9592 0.8269 0.8953 -0.0356 0.0325  -0.0278 65  GLU A CG  
451  C CD  . GLU A 65  ? 1.1306 0.9957 1.0700 -0.0349 0.0329  -0.0301 65  GLU A CD  
452  O OE1 . GLU A 65  ? 1.0656 0.9262 1.0122 -0.0338 0.0359  -0.0296 65  GLU A OE1 
453  O OE2 . GLU A 65  ? 1.2220 1.0892 1.1569 -0.0358 0.0310  -0.0326 65  GLU A OE2 
454  N N   . ARG A 66  ? 0.7232 0.6012 0.6464 -0.0391 0.0322  -0.0240 66  ARG A N   
455  C CA  . ARG A 66  ? 0.6777 0.5614 0.5915 -0.0426 0.0314  -0.0251 66  ARG A CA  
456  C C   . ARG A 66  ? 0.7136 0.6047 0.6232 -0.0450 0.0321  -0.0207 66  ARG A C   
457  O O   . ARG A 66  ? 0.8177 0.7170 0.7201 -0.0491 0.0308  -0.0194 66  ARG A O   
458  C CB  . ARG A 66  ? 0.6502 0.5276 0.5583 -0.0442 0.0329  -0.0324 66  ARG A CB  
459  C CG  . ARG A 66  ? 0.6487 0.5224 0.5593 -0.0432 0.0313  -0.0357 66  ARG A CG  
460  C CD  . ARG A 66  ? 0.6052 0.4729 0.5138 -0.0437 0.0332  -0.0407 66  ARG A CD  
461  N NE  . ARG A 66  ? 0.7040 0.5709 0.6119 -0.0443 0.0315  -0.0434 66  ARG A NE  
462  C CZ  . ARG A 66  ? 0.7285 0.5935 0.6413 -0.0426 0.0299  -0.0439 66  ARG A CZ  
463  N NH1 . ARG A 66  ? 0.6007 0.4641 0.5192 -0.0410 0.0299  -0.0424 66  ARG A NH1 
464  N NH2 . ARG A 66  ? 0.6106 0.4756 0.5220 -0.0434 0.0286  -0.0462 66  ARG A NH2 
465  N N   . LEU A 67  ? 0.7636 0.6530 0.6770 -0.0433 0.0342  -0.0180 67  LEU A N   
466  C CA  . LEU A 67  ? 0.8183 0.7162 0.7284 -0.0456 0.0348  -0.0124 67  LEU A CA  
467  C C   . LEU A 67  ? 0.7760 0.6853 0.6905 -0.0455 0.0319  -0.0032 67  LEU A C   
468  O O   . LEU A 67  ? 0.7688 0.6894 0.6778 -0.0493 0.0310  0.0019  67  LEU A O   
469  C CB  . LEU A 67  ? 0.7409 0.6351 0.6565 -0.0432 0.0374  -0.0101 67  LEU A CB  
470  C CG  . LEU A 67  ? 0.7627 0.6484 0.6770 -0.0428 0.0407  -0.0161 67  LEU A CG  
471  C CD1 . LEU A 67  ? 0.6353 0.5191 0.5576 -0.0403 0.0424  -0.0121 67  LEU A CD1 
472  C CD2 . LEU A 67  ? 0.6931 0.5799 0.5960 -0.0470 0.0439  -0.0207 67  LEU A CD2 
473  N N   . ARG A 68  ? 0.7325 0.6397 0.6572 -0.0414 0.0309  -0.0003 68  ARG A N   
474  C CA  . ARG A 68  ? 0.7203 0.6381 0.6529 -0.0401 0.0293  0.0101  68  ARG A CA  
475  C C   . ARG A 68  ? 0.8517 0.7766 0.7895 -0.0393 0.0303  0.0197  68  ARG A C   
476  O O   . ARG A 68  ? 0.9622 0.9015 0.8964 -0.0428 0.0283  0.0273  68  ARG A O   
477  C CB  . ARG A 68  ? 0.7342 0.6640 0.6590 -0.0448 0.0257  0.0115  68  ARG A CB  
478  C CG  . ARG A 68  ? 0.8157 0.7381 0.7372 -0.0450 0.0250  0.0028  68  ARG A CG  
479  C CD  . ARG A 68  ? 0.8813 0.8154 0.7988 -0.0489 0.0214  0.0054  68  ARG A CD  
480  N NE  . ARG A 68  ? 1.1634 1.0894 1.0756 -0.0500 0.0212  -0.0042 68  ARG A NE  
481  C CZ  . ARG A 68  ? 1.1796 1.1130 1.0869 -0.0541 0.0184  -0.0047 68  ARG A CZ  
482  N NH1 . ARG A 68  ? 1.2061 1.1562 1.1130 -0.0579 0.0153  0.0041  68  ARG A NH1 
483  N NH2 . ARG A 68  ? 1.0684 0.9937 0.9716 -0.0548 0.0187  -0.0132 68  ARG A NH2 
484  N N   . ILE A 69  ? 0.8089 0.7240 0.7552 -0.0355 0.0336  0.0197  69  ILE A N   
485  C CA  . ILE A 69  ? 0.7027 0.6221 0.6548 -0.0345 0.0353  0.0280  69  ILE A CA  
486  C C   . ILE A 69  ? 0.7138 0.6261 0.6826 -0.0291 0.0387  0.0332  69  ILE A C   
487  O O   . ILE A 69  ? 0.7127 0.6154 0.6871 -0.0267 0.0404  0.0284  69  ILE A O   
488  C CB  . ILE A 69  ? 0.6708 0.5848 0.6153 -0.0365 0.0370  0.0222  69  ILE A CB  
489  C CG1 . ILE A 69  ? 0.6767 0.5758 0.6233 -0.0346 0.0387  0.0126  69  ILE A CG1 
490  C CG2 . ILE A 69  ? 0.6469 0.5685 0.5757 -0.0424 0.0356  0.0186  69  ILE A CG2 
491  C CD1 . ILE A 69  ? 0.7979 0.6912 0.7465 -0.0343 0.0412  0.0114  69  ILE A CD1 
492  N N   . GLY A 70  ? 0.5873 0.5041 0.5639 -0.0277 0.0406  0.0427  70  GLY A N   
493  C CA  . GLY A 70  ? 0.6138 0.5245 0.6077 -0.0230 0.0452  0.0492  70  GLY A CA  
494  C C   . GLY A 70  ? 0.7955 0.7086 0.7951 -0.0225 0.0474  0.0570  70  GLY A C   
495  O O   . GLY A 70  ? 0.8068 0.7234 0.7962 -0.0258 0.0459  0.0548  70  GLY A O   
496  N N   . ALA A 71  ? 0.8073 0.7181 0.8244 -0.0182 0.0520  0.0665  71  ALA A N   
497  C CA  . ALA A 71  ? 0.7069 0.6186 0.7317 -0.0174 0.0549  0.0744  71  ALA A CA  
498  C C   . ALA A 71  ? 0.7577 0.6887 0.7758 -0.0201 0.0509  0.0844  71  ALA A C   
499  O O   . ALA A 71  ? 0.9742 0.9205 0.9960 -0.0198 0.0487  0.0959  71  ALA A O   
500  C CB  . ALA A 71  ? 0.5418 0.4482 0.5882 -0.0122 0.0615  0.0841  71  ALA A CB  
501  N N   . GLY A 72  ? 0.7096 0.6410 0.7174 -0.0235 0.0500  0.0805  72  GLY A N   
502  C CA  . GLY A 72  ? 0.7147 0.6641 0.7144 -0.0272 0.0471  0.0888  72  GLY A CA  
503  C C   . GLY A 72  ? 0.8061 0.7630 0.7855 -0.0332 0.0428  0.0808  72  GLY A C   
504  O O   . GLY A 72  ? 0.8043 0.7769 0.7744 -0.0381 0.0407  0.0865  72  GLY A O   
505  N N   . SER A 73  ? 0.7662 0.7128 0.7383 -0.0337 0.0419  0.0678  73  SER A N   
506  C CA  . SER A 73  ? 0.6710 0.6207 0.6241 -0.0394 0.0397  0.0583  73  SER A CA  
507  C C   . SER A 73  ? 0.7592 0.7036 0.7047 -0.0414 0.0425  0.0522  73  SER A C   
508  O O   . SER A 73  ? 0.8037 0.7372 0.7575 -0.0380 0.0453  0.0504  73  SER A O   
509  C CB  . SER A 73  ? 0.6705 0.6097 0.6200 -0.0388 0.0387  0.0468  73  SER A CB  
510  O OG  . SER A 73  ? 0.7152 0.6553 0.6764 -0.0351 0.0378  0.0525  73  SER A OG  
511  N N   . ARG A 74  ? 0.6799 0.6322 0.6096 -0.0475 0.0423  0.0488  74  ARG A N   
512  C CA  . ARG A 74  ? 0.6957 0.6416 0.6181 -0.0491 0.0463  0.0415  74  ARG A CA  
513  C C   . ARG A 74  ? 0.7141 0.6495 0.6268 -0.0506 0.0476  0.0276  74  ARG A C   
514  O O   . ARG A 74  ? 0.7904 0.7307 0.6915 -0.0555 0.0463  0.0233  74  ARG A O   
515  C CB  . ARG A 74  ? 0.7766 0.7363 0.6886 -0.0550 0.0476  0.0463  74  ARG A CB  
516  C CG  . ARG A 74  ? 0.9566 0.9298 0.8785 -0.0540 0.0460  0.0624  74  ARG A CG  
517  C CD  . ARG A 74  ? 1.2264 1.2018 1.1472 -0.0550 0.0500  0.0656  74  ARG A CD  
518  N NE  . ARG A 74  ? 1.3602 1.3515 1.2646 -0.0635 0.0503  0.0674  74  ARG A NE  
519  C CZ  . ARG A 74  ? 1.3305 1.3202 1.2219 -0.0680 0.0553  0.0596  74  ARG A CZ  
520  N NH1 . ARG A 74  ? 1.2604 1.2342 1.1549 -0.0640 0.0602  0.0510  74  ARG A NH1 
521  N NH2 . ARG A 74  ? 1.1831 1.1881 1.0581 -0.0772 0.0560  0.0608  74  ARG A NH2 
522  N N   . VAL A 75  ? 0.6704 0.5925 0.5887 -0.0469 0.0501  0.0214  75  VAL A N   
523  C CA  . VAL A 75  ? 0.7244 0.6360 0.6383 -0.0467 0.0513  0.0104  75  VAL A CA  
524  C C   . VAL A 75  ? 0.7447 0.6516 0.6550 -0.0474 0.0569  0.0055  75  VAL A C   
525  O O   . VAL A 75  ? 0.7537 0.6591 0.6717 -0.0450 0.0587  0.0094  75  VAL A O   
526  C CB  . VAL A 75  ? 0.6864 0.5883 0.6117 -0.0420 0.0492  0.0085  75  VAL A CB  
527  C CG1 . VAL A 75  ? 0.6053 0.4981 0.5275 -0.0418 0.0506  -0.0011 75  VAL A CG1 
528  C CG2 . VAL A 75  ? 0.5435 0.4489 0.4729 -0.0410 0.0453  0.0125  75  VAL A CG2 
529  N N   . LEU A 76  ? 0.7190 0.6228 0.6187 -0.0506 0.0602  -0.0028 76  LEU A N   
530  C CA  . LEU A 76  ? 0.7404 0.6382 0.6383 -0.0505 0.0672  -0.0077 76  LEU A CA  
531  C C   . LEU A 76  ? 0.7126 0.5999 0.6184 -0.0465 0.0677  -0.0125 76  LEU A C   
532  O O   . LEU A 76  ? 0.7676 0.6513 0.6701 -0.0471 0.0664  -0.0177 76  LEU A O   
533  C CB  . LEU A 76  ? 0.7575 0.6575 0.6397 -0.0570 0.0726  -0.0140 76  LEU A CB  
534  C CG  . LEU A 76  ? 0.7399 0.6309 0.6204 -0.0568 0.0820  -0.0210 76  LEU A CG  
535  C CD1 . LEU A 76  ? 0.6188 0.5096 0.5086 -0.0530 0.0855  -0.0160 76  LEU A CD1 
536  C CD2 . LEU A 76  ? 0.6373 0.5298 0.5005 -0.0649 0.0885  -0.0284 76  LEU A CD2 
537  N N   . ASP A 77  ? 0.6626 0.5466 0.5791 -0.0427 0.0694  -0.0099 77  ASP A N   
538  C CA  . ASP A 77  ? 0.6809 0.5581 0.6064 -0.0394 0.0695  -0.0122 77  ASP A CA  
539  C C   . ASP A 77  ? 0.7259 0.5992 0.6497 -0.0393 0.0779  -0.0161 77  ASP A C   
540  O O   . ASP A 77  ? 0.7572 0.6308 0.6874 -0.0376 0.0824  -0.0131 77  ASP A O   
541  C CB  . ASP A 77  ? 0.6508 0.5286 0.5889 -0.0369 0.0663  -0.0065 77  ASP A CB  
542  C CG  . ASP A 77  ? 0.6038 0.4779 0.5511 -0.0349 0.0655  -0.0075 77  ASP A CG  
543  O OD1 . ASP A 77  ? 0.6666 0.5374 0.6119 -0.0345 0.0668  -0.0118 77  ASP A OD1 
544  O OD2 . ASP A 77  ? 0.6706 0.5460 0.6275 -0.0344 0.0634  -0.0035 77  ASP A OD2 
545  N N   . LEU A 78  ? 0.7371 0.6062 0.6528 -0.0414 0.0809  -0.0227 78  LEU A N   
546  C CA  . LEU A 78  ? 0.6805 0.5441 0.5928 -0.0422 0.0911  -0.0278 78  LEU A CA  
547  C C   . LEU A 78  ? 0.6865 0.5451 0.6128 -0.0371 0.0944  -0.0262 78  LEU A C   
548  O O   . LEU A 78  ? 0.8337 0.6873 0.7622 -0.0362 0.0954  -0.0293 78  LEU A O   
549  C CB  . LEU A 78  ? 0.6555 0.5157 0.5547 -0.0470 0.0934  -0.0358 78  LEU A CB  
550  C CG  . LEU A 78  ? 0.6890 0.5425 0.5815 -0.0499 0.1056  -0.0429 78  LEU A CG  
551  C CD1 . LEU A 78  ? 0.6586 0.5185 0.5373 -0.0562 0.1083  -0.0441 78  LEU A CD1 
552  C CD2 . LEU A 78  ? 0.5821 0.4285 0.4683 -0.0528 0.1079  -0.0507 78  LEU A CD2 
553  N N   . GLY A 79  ? 0.7026 0.5641 0.6395 -0.0341 0.0961  -0.0201 79  GLY A N   
554  C CA  . GLY A 79  ? 0.6559 0.5158 0.6078 -0.0296 0.0989  -0.0163 79  GLY A CA  
555  C C   . GLY A 79  ? 0.7685 0.6337 0.7290 -0.0286 0.0887  -0.0108 79  GLY A C   
556  O O   . GLY A 79  ? 0.6715 0.5357 0.6320 -0.0289 0.0834  -0.0125 79  GLY A O   
557  N N   . CYS A 80  ? 0.6798 0.5506 0.6480 -0.0280 0.0868  -0.0046 80  CYS A N   
558  C CA  . CYS A 80  ? 0.4769 0.3518 0.4482 -0.0294 0.0777  -0.0014 80  CYS A CA  
559  C C   . CYS A 80  ? 0.6765 0.5562 0.6614 -0.0288 0.0745  0.0043  80  CYS A C   
560  O O   . CYS A 80  ? 0.6907 0.5732 0.6780 -0.0313 0.0678  0.0060  80  CYS A O   
561  C CB  . CYS A 80  ? 0.6400 0.5177 0.6085 -0.0307 0.0774  0.0012  80  CYS A CB  
562  S SG  . CYS A 80  ? 0.7033 0.5856 0.6824 -0.0291 0.0831  0.0081  80  CYS A SG  
563  N N   . GLY A 81  ? 0.6885 0.5704 0.6832 -0.0263 0.0797  0.0082  81  GLY A N   
564  C CA  . GLY A 81  ? 0.6696 0.5595 0.6776 -0.0268 0.0759  0.0153  81  GLY A CA  
565  C C   . GLY A 81  ? 0.7327 0.6285 0.7462 -0.0291 0.0729  0.0203  81  GLY A C   
566  O O   . GLY A 81  ? 0.7175 0.6133 0.7312 -0.0280 0.0774  0.0220  81  GLY A O   
567  N N   . VAL A 82  ? 0.7281 0.6293 0.7460 -0.0331 0.0655  0.0226  82  VAL A N   
568  C CA  . VAL A 82  ? 0.6461 0.5524 0.6691 -0.0368 0.0624  0.0265  82  VAL A CA  
569  C C   . VAL A 82  ? 0.6225 0.5222 0.6359 -0.0395 0.0590  0.0210  82  VAL A C   
570  O O   . VAL A 82  ? 0.6670 0.5682 0.6831 -0.0435 0.0560  0.0224  82  VAL A O   
571  C CB  . VAL A 82  ? 0.6867 0.6032 0.7193 -0.0413 0.0569  0.0317  82  VAL A CB  
572  C CG1 . VAL A 82  ? 0.6500 0.5761 0.6968 -0.0383 0.0612  0.0412  82  VAL A CG1 
573  C CG2 . VAL A 82  ? 0.8062 0.7218 0.8340 -0.0433 0.0522  0.0277  82  VAL A CG2 
574  N N   . GLY A 83  ? 0.5386 0.4311 0.5416 -0.0374 0.0600  0.0152  83  GLY A N   
575  C CA  . GLY A 83  ? 0.5657 0.4529 0.5613 -0.0388 0.0577  0.0116  83  GLY A CA  
576  C C   . GLY A 83  ? 0.5640 0.4478 0.5566 -0.0420 0.0525  0.0074  83  GLY A C   
577  O O   . GLY A 83  ? 0.6138 0.4930 0.6020 -0.0422 0.0518  0.0053  83  GLY A O   
578  N N   . THR A 84  ? 0.5600 0.4468 0.5553 -0.0444 0.0494  0.0067  84  THR A N   
579  C CA  . THR A 84  ? 0.6294 0.5127 0.6216 -0.0486 0.0451  0.0021  84  THR A CA  
580  C C   . THR A 84  ? 0.7059 0.5823 0.6893 -0.0463 0.0449  -0.0032 84  THR A C   
581  O O   . THR A 84  ? 0.7583 0.6297 0.7404 -0.0480 0.0443  -0.0055 84  THR A O   
582  C CB  . THR A 84  ? 0.7114 0.6013 0.7070 -0.0529 0.0413  0.0026  84  THR A CB  
583  O OG1 . THR A 84  ? 0.6381 0.5367 0.6430 -0.0555 0.0412  0.0090  84  THR A OG1 
584  C CG2 . THR A 84  ? 0.4588 0.3450 0.4502 -0.0587 0.0379  -0.0032 84  THR A CG2 
585  N N   . PRO A 85  ? 0.6270 0.5027 0.6053 -0.0429 0.0459  -0.0050 85  PRO A N   
586  C CA  . PRO A 85  ? 0.5955 0.4662 0.5661 -0.0416 0.0452  -0.0093 85  PRO A CA  
587  C C   . PRO A 85  ? 0.5781 0.4473 0.5458 -0.0395 0.0475  -0.0075 85  PRO A C   
588  O O   . PRO A 85  ? 0.6194 0.4858 0.5849 -0.0393 0.0465  -0.0086 85  PRO A O   
589  C CB  . PRO A 85  ? 0.6176 0.4886 0.5840 -0.0395 0.0459  -0.0116 85  PRO A CB  
590  C CG  . PRO A 85  ? 0.4711 0.3474 0.4452 -0.0401 0.0460  -0.0082 85  PRO A CG  
591  C CD  . PRO A 85  ? 0.4763 0.3557 0.4567 -0.0407 0.0477  -0.0034 85  PRO A CD  
592  N N   . GLY A 86  ? 0.6591 0.5310 0.6277 -0.0380 0.0509  -0.0040 86  GLY A N   
593  C CA  . GLY A 86  ? 0.5704 0.4431 0.5365 -0.0370 0.0526  -0.0009 86  GLY A CA  
594  C C   . GLY A 86  ? 0.6371 0.5079 0.6095 -0.0382 0.0515  0.0020  86  GLY A C   
595  O O   . GLY A 86  ? 0.6068 0.4771 0.5781 -0.0373 0.0513  0.0039  86  GLY A O   
596  N N   . VAL A 87  ? 0.6056 0.4757 0.5854 -0.0407 0.0511  0.0029  87  VAL A N   
597  C CA  . VAL A 87  ? 0.6871 0.5537 0.6732 -0.0424 0.0516  0.0051  87  VAL A CA  
598  C C   . VAL A 87  ? 0.7067 0.5672 0.6925 -0.0438 0.0503  0.0005  87  VAL A C   
599  O O   . VAL A 87  ? 0.6611 0.5173 0.6509 -0.0432 0.0521  0.0023  87  VAL A O   
600  C CB  . VAL A 87  ? 0.6421 0.5097 0.6360 -0.0460 0.0521  0.0072  87  VAL A CB  
601  C CG1 . VAL A 87  ? 0.5389 0.4127 0.5345 -0.0441 0.0544  0.0124  87  VAL A CG1 
602  C CG2 . VAL A 87  ? 0.8442 0.7125 0.8386 -0.0502 0.0493  0.0029  87  VAL A CG2 
603  N N   . ARG A 88  ? 0.6952 0.5554 0.6771 -0.0454 0.0477  -0.0049 88  ARG A N   
604  C CA  . ARG A 88  ? 0.6132 0.4679 0.5936 -0.0468 0.0470  -0.0099 88  ARG A CA  
605  C C   . ARG A 88  ? 0.7124 0.5661 0.6904 -0.0425 0.0478  -0.0083 88  ARG A C   
606  O O   . ARG A 88  ? 0.7582 0.6067 0.7400 -0.0422 0.0497  -0.0087 88  ARG A O   
607  C CB  . ARG A 88  ? 0.5190 0.3758 0.4949 -0.0492 0.0438  -0.0148 88  ARG A CB  
608  C CG  . ARG A 88  ? 0.5643 0.4162 0.5374 -0.0505 0.0434  -0.0202 88  ARG A CG  
609  C CD  . ARG A 88  ? 0.6575 0.5128 0.6266 -0.0536 0.0401  -0.0241 88  ARG A CD  
610  N NE  . ARG A 88  ? 0.6124 0.4633 0.5781 -0.0548 0.0401  -0.0294 88  ARG A NE  
611  C CZ  . ARG A 88  ? 0.6239 0.4707 0.5898 -0.0605 0.0411  -0.0344 88  ARG A CZ  
612  N NH1 . ARG A 88  ? 0.5288 0.3755 0.4978 -0.0665 0.0418  -0.0349 88  ARG A NH1 
613  N NH2 . ARG A 88  ? 0.6863 0.5290 0.6488 -0.0611 0.0420  -0.0393 88  ARG A NH2 
614  N N   . ILE A 89  ? 0.6655 0.5245 0.6376 -0.0395 0.0470  -0.0063 89  ILE A N   
615  C CA  . ILE A 89  ? 0.6401 0.5011 0.6094 -0.0367 0.0470  -0.0040 89  ILE A CA  
616  C C   . ILE A 89  ? 0.6713 0.5333 0.6475 -0.0351 0.0494  0.0034  89  ILE A C   
617  O O   . ILE A 89  ? 0.7994 0.6612 0.7790 -0.0332 0.0501  0.0066  89  ILE A O   
618  C CB  . ILE A 89  ? 0.5916 0.4583 0.5517 -0.0358 0.0460  -0.0045 89  ILE A CB  
619  C CG1 . ILE A 89  ? 0.5000 0.3647 0.4553 -0.0367 0.0442  -0.0110 89  ILE A CG1 
620  C CG2 . ILE A 89  ? 0.6002 0.4724 0.5571 -0.0345 0.0457  -0.0002 89  ILE A CG2 
621  C CD1 . ILE A 89  ? 0.5077 0.3754 0.4553 -0.0366 0.0448  -0.0130 89  ILE A CD1 
622  N N   . ALA A 90  ? 0.5866 0.4500 0.5663 -0.0356 0.0511  0.0073  90  ALA A N   
623  C CA  . ALA A 90  ? 0.7119 0.5769 0.6993 -0.0340 0.0536  0.0155  90  ALA A CA  
624  C C   . ALA A 90  ? 0.6929 0.5488 0.6906 -0.0345 0.0565  0.0151  90  ALA A C   
625  O O   . ALA A 90  ? 0.7075 0.5630 0.7126 -0.0319 0.0590  0.0212  90  ALA A O   
626  C CB  . ALA A 90  ? 0.5902 0.4591 0.5789 -0.0347 0.0550  0.0199  90  ALA A CB  
627  N N   . ARG A 91  ? 0.5904 0.4395 0.5890 -0.0384 0.0567  0.0081  91  ARG A N   
628  C CA  . ARG A 91  ? 0.6479 0.4867 0.6546 -0.0408 0.0607  0.0054  91  ARG A CA  
629  C C   . ARG A 91  ? 0.6875 0.5217 0.6951 -0.0389 0.0623  0.0029  91  ARG A C   
630  O O   . ARG A 91  ? 0.6947 0.5224 0.7123 -0.0374 0.0676  0.0058  91  ARG A O   
631  C CB  . ARG A 91  ? 0.6508 0.4862 0.6552 -0.0472 0.0596  -0.0022 91  ARG A CB  
632  C CG  . ARG A 91  ? 0.6110 0.4356 0.6214 -0.0521 0.0643  -0.0071 91  ARG A CG  
633  C CD  . ARG A 91  ? 0.6966 0.5217 0.7047 -0.0600 0.0625  -0.0123 91  ARG A CD  
634  N NE  . ARG A 91  ? 0.7465 0.5764 0.7455 -0.0627 0.0576  -0.0182 91  ARG A NE  
635  C CZ  . ARG A 91  ? 0.6093 0.4343 0.6044 -0.0660 0.0582  -0.0256 91  ARG A CZ  
636  N NH1 . ARG A 91  ? 0.7913 0.6054 0.7909 -0.0667 0.0644  -0.0286 91  ARG A NH1 
637  N NH2 . ARG A 91  ? 0.6231 0.4541 0.6106 -0.0685 0.0534  -0.0294 91  ARG A NH2 
638  N N   . LEU A 92  ? 0.6675 0.5046 0.6661 -0.0389 0.0584  -0.0023 92  LEU A N   
639  C CA  . LEU A 92  ? 0.6104 0.4432 0.6098 -0.0376 0.0599  -0.0054 92  LEU A CA  
640  C C   . LEU A 92  ? 0.6914 0.5306 0.6933 -0.0320 0.0598  0.0025  92  LEU A C   
641  O O   . LEU A 92  ? 0.6868 0.5220 0.6947 -0.0299 0.0632  0.0032  92  LEU A O   
642  C CB  . LEU A 92  ? 0.4799 0.3136 0.4692 -0.0404 0.0559  -0.0138 92  LEU A CB  
643  C CG  . LEU A 92  ? 0.6174 0.4456 0.6051 -0.0473 0.0564  -0.0215 92  LEU A CG  
644  C CD1 . LEU A 92  ? 0.4794 0.3105 0.4583 -0.0497 0.0523  -0.0279 92  LEU A CD1 
645  C CD2 . LEU A 92  ? 0.4939 0.3108 0.4893 -0.0504 0.0632  -0.0248 92  LEU A CD2 
646  N N   . SER A 93  ? 0.6714 0.5210 0.6690 -0.0302 0.0564  0.0087  93  SER A N   
647  C CA  . SER A 93  ? 0.6596 0.5184 0.6578 -0.0267 0.0552  0.0164  93  SER A CA  
648  C C   . SER A 93  ? 0.7563 0.6218 0.7631 -0.0242 0.0571  0.0287  93  SER A C   
649  O O   . SER A 93  ? 0.6947 0.5695 0.7049 -0.0216 0.0564  0.0373  93  SER A O   
650  C CB  . SER A 93  ? 0.6305 0.4982 0.6151 -0.0280 0.0498  0.0139  93  SER A CB  
651  O OG  . SER A 93  ? 0.7548 0.6286 0.7346 -0.0291 0.0489  0.0170  93  SER A OG  
652  N N   . GLY A 94  ? 0.6795 0.5425 0.6900 -0.0252 0.0592  0.0307  94  GLY A N   
653  C CA  . GLY A 94  ? 0.6756 0.5466 0.6935 -0.0232 0.0606  0.0430  94  GLY A CA  
654  C C   . GLY A 94  ? 0.8102 0.6959 0.8175 -0.0242 0.0563  0.0478  94  GLY A C   
655  O O   . GLY A 94  ? 0.8145 0.7104 0.8270 -0.0229 0.0567  0.0597  94  GLY A O   
656  N N   . ALA A 95  ? 0.7048 0.5922 0.6978 -0.0270 0.0527  0.0393  95  ALA A N   
657  C CA  . ALA A 95  ? 0.6453 0.5453 0.6273 -0.0292 0.0502  0.0424  95  ALA A CA  
658  C C   . ALA A 95  ? 0.6672 0.5680 0.6472 -0.0306 0.0519  0.0433  95  ALA A C   
659  O O   . ALA A 95  ? 0.7473 0.6395 0.7342 -0.0302 0.0543  0.0414  95  ALA A O   
660  C CB  . ALA A 95  ? 0.5990 0.4997 0.5672 -0.0316 0.0472  0.0332  95  ALA A CB  
661  N N   . HIS A 96  ? 0.7412 0.6531 0.7113 -0.0332 0.0510  0.0462  96  HIS A N   
662  C CA  . HIS A 96  ? 0.7197 0.6332 0.6860 -0.0349 0.0533  0.0463  96  HIS A CA  
663  C C   . HIS A 96  ? 0.7136 0.6235 0.6676 -0.0372 0.0537  0.0353  96  HIS A C   
664  O O   . HIS A 96  ? 0.8230 0.7390 0.7648 -0.0402 0.0530  0.0324  96  HIS A O   
665  C CB  . HIS A 96  ? 0.6790 0.6074 0.6424 -0.0369 0.0534  0.0568  96  HIS A CB  
666  C CG  . HIS A 96  ? 0.8647 0.7971 0.8431 -0.0339 0.0539  0.0698  96  HIS A CG  
667  N ND1 . HIS A 96  ? 0.9366 0.8638 0.9264 -0.0319 0.0571  0.0743  96  HIS A ND1 
668  C CD2 . HIS A 96  ? 0.9311 0.8717 0.9169 -0.0323 0.0523  0.0797  96  HIS A CD2 
669  C CE1 . HIS A 96  ? 0.9209 0.8518 0.9245 -0.0292 0.0581  0.0863  96  HIS A CE1 
670  N NE2 . HIS A 96  ? 0.9107 0.8502 0.9128 -0.0290 0.0553  0.0903  96  HIS A NE2 
671  N N   . VAL A 97  ? 0.5448 0.4454 0.5027 -0.0362 0.0553  0.0296  97  VAL A N   
672  C CA  . VAL A 97  ? 0.6994 0.5961 0.6494 -0.0373 0.0566  0.0207  97  VAL A CA  
673  C C   . VAL A 97  ? 0.7238 0.6235 0.6709 -0.0384 0.0608  0.0218  97  VAL A C   
674  O O   . VAL A 97  ? 0.7982 0.6973 0.7538 -0.0374 0.0623  0.0263  97  VAL A O   
675  C CB  . VAL A 97  ? 0.6734 0.5605 0.6299 -0.0360 0.0554  0.0151  97  VAL A CB  
676  C CG1 . VAL A 97  ? 0.5439 0.4284 0.4963 -0.0364 0.0576  0.0090  97  VAL A CG1 
677  C CG2 . VAL A 97  ? 0.6322 0.5163 0.5884 -0.0355 0.0522  0.0121  97  VAL A CG2 
678  N N   . THR A 98  ? 0.7522 0.6550 0.6873 -0.0409 0.0635  0.0176  98  THR A N   
679  C CA  . THR A 98  ? 0.7272 0.6306 0.6586 -0.0419 0.0695  0.0160  98  THR A CA  
680  C C   . THR A 98  ? 0.6606 0.5563 0.5900 -0.0412 0.0726  0.0075  98  THR A C   
681  O O   . THR A 98  ? 0.7256 0.6199 0.6458 -0.0433 0.0730  0.0015  98  THR A O   
682  C CB  . THR A 98  ? 0.6217 0.5342 0.5403 -0.0465 0.0723  0.0173  98  THR A CB  
683  O OG1 . THR A 98  ? 0.7383 0.6602 0.6598 -0.0471 0.0692  0.0272  98  THR A OG1 
684  C CG2 . THR A 98  ? 0.7232 0.6348 0.6388 -0.0474 0.0798  0.0150  98  THR A CG2 
685  N N   . GLY A 99  ? 0.6148 0.5065 0.5536 -0.0386 0.0751  0.0078  99  GLY A N   
686  C CA  . GLY A 99  ? 0.7079 0.5935 0.6481 -0.0372 0.0784  0.0021  99  GLY A CA  
687  C C   . GLY A 99  ? 0.7437 0.6290 0.6835 -0.0368 0.0873  0.0013  99  GLY A C   
688  O O   . GLY A 99  ? 0.7197 0.6095 0.6598 -0.0375 0.0901  0.0056  99  GLY A O   
689  N N   . ILE A 100 ? 0.7337 0.6134 0.6735 -0.0358 0.0926  -0.0039 100 ILE A N   
690  C CA  . ILE A 100 ? 0.7052 0.5828 0.6468 -0.0347 0.1030  -0.0048 100 ILE A CA  
691  C C   . ILE A 100 ? 0.7337 0.6070 0.6879 -0.0306 0.1057  -0.0046 100 ILE A C   
692  O O   . ILE A 100 ? 0.6734 0.5440 0.6293 -0.0299 0.1010  -0.0065 100 ILE A O   
693  C CB  . ILE A 100 ? 0.7019 0.5771 0.6276 -0.0391 0.1111  -0.0123 100 ILE A CB  
694  C CG1 . ILE A 100 ? 0.7376 0.6047 0.6587 -0.0397 0.1143  -0.0202 100 ILE A CG1 
695  C CG2 . ILE A 100 ? 0.6569 0.5394 0.5691 -0.0444 0.1064  -0.0118 100 ILE A CG2 
696  C CD1 . ILE A 100 ? 0.7388 0.6028 0.6427 -0.0460 0.1228  -0.0291 100 ILE A CD1 
697  N N   . SER A 101 ? 0.6747 0.5485 0.6388 -0.0277 0.1132  -0.0008 101 SER A N   
698  C CA  . SER A 101 ? 0.7211 0.5919 0.6981 -0.0236 0.1186  0.0008  101 SER A CA  
699  C C   . SER A 101 ? 0.7592 0.6273 0.7390 -0.0218 0.1323  0.0006  101 SER A C   
700  O O   . SER A 101 ? 0.7597 0.6304 0.7337 -0.0237 0.1357  0.0009  101 SER A O   
701  C CB  . SER A 101 ? 0.6767 0.5543 0.6697 -0.0213 0.1110  0.0094  101 SER A CB  
702  O OG  . SER A 101 ? 0.6314 0.5095 0.6394 -0.0172 0.1167  0.0139  101 SER A OG  
703  N N   . VAL A 102 ? 0.7334 0.5959 0.7220 -0.0183 0.1413  -0.0001 102 VAL A N   
704  C CA  . VAL A 102 ? 0.7053 0.5648 0.7015 -0.0154 0.1558  0.0012  102 VAL A CA  
705  C C   . VAL A 102 ? 0.8254 0.6941 0.8431 -0.0105 0.1548  0.0137  102 VAL A C   
706  O O   . VAL A 102 ? 0.7812 0.6507 0.8071 -0.0078 0.1653  0.0172  102 VAL A O   
707  C CB  . VAL A 102 ? 0.7292 0.5771 0.7264 -0.0138 0.1682  -0.0051 102 VAL A CB  
708  C CG1 . VAL A 102 ? 0.5645 0.4042 0.5388 -0.0205 0.1692  -0.0180 102 VAL A CG1 
709  C CG2 . VAL A 102 ? 0.6862 0.5354 0.7003 -0.0090 0.1645  0.0014  102 VAL A CG2 
710  N N   . SER A 103 ? 0.8434 0.7199 0.8700 -0.0100 0.1425  0.0203  103 SER A N   
711  C CA  . SER A 103 ? 0.6798 0.5676 0.7255 -0.0074 0.1391  0.0325  103 SER A CA  
712  C C   . SER A 103 ? 0.7001 0.5947 0.7424 -0.0105 0.1331  0.0353  103 SER A C   
713  O O   . SER A 103 ? 0.6912 0.5860 0.7221 -0.0147 0.1231  0.0318  103 SER A O   
714  C CB  . SER A 103 ? 0.7038 0.5975 0.7574 -0.0078 0.1282  0.0370  103 SER A CB  
715  O OG  . SER A 103 ? 0.7840 0.6908 0.8522 -0.0082 0.1219  0.0479  103 SER A OG  
716  N N   . HIS A 104 ? 0.7608 0.6608 0.8144 -0.0082 0.1397  0.0423  104 HIS A N   
717  C CA  . HIS A 104 ? 0.6504 0.5569 0.7023 -0.0111 0.1349  0.0458  104 HIS A CA  
718  C C   . HIS A 104 ? 0.6857 0.6013 0.7454 -0.0140 0.1215  0.0521  104 HIS A C   
719  O O   . HIS A 104 ? 0.6904 0.6066 0.7421 -0.0182 0.1135  0.0504  104 HIS A O   
720  C CB  . HIS A 104 ? 0.6361 0.5468 0.6993 -0.0079 0.1456  0.0523  104 HIS A CB  
721  C CG  . HIS A 104 ? 0.6645 0.5846 0.7324 -0.0104 0.1397  0.0592  104 HIS A CG  
722  N ND1 . HIS A 104 ? 0.7108 0.6295 0.7656 -0.0137 0.1387  0.0559  104 HIS A ND1 
723  C CD2 . HIS A 104 ? 0.6422 0.5737 0.7264 -0.0110 0.1336  0.0695  104 HIS A CD2 
724  C CE1 . HIS A 104 ? 0.5682 0.4957 0.6317 -0.0155 0.1330  0.0636  104 HIS A CE1 
725  N NE2 . HIS A 104 ? 0.6222 0.5573 0.7029 -0.0144 0.1299  0.0714  104 HIS A NE2 
726  N N   . GLU A 105 ? 0.6891 0.6121 0.7650 -0.0123 0.1197  0.0597  105 GLU A N   
727  C CA  . GLU A 105 ? 0.7302 0.6628 0.8124 -0.0169 0.1074  0.0650  105 GLU A CA  
728  C C   . GLU A 105 ? 0.7412 0.6677 0.8089 -0.0212 0.0978  0.0567  105 GLU A C   
729  O O   . GLU A 105 ? 0.8064 0.7362 0.8722 -0.0264 0.0890  0.0569  105 GLU A O   
730  C CB  . GLU A 105 ? 0.6508 0.5944 0.7521 -0.0150 0.1074  0.0753  105 GLU A CB  
731  C CG  . GLU A 105 ? 0.6973 0.6482 0.8157 -0.0105 0.1170  0.0853  105 GLU A CG  
732  C CD  . GLU A 105 ? 0.7463 0.7071 0.8702 -0.0146 0.1125  0.0915  105 GLU A CD  
733  O OE1 . GLU A 105 ? 0.8020 0.7662 0.9207 -0.0213 0.1010  0.0901  105 GLU A OE1 
734  O OE2 . GLU A 105 ? 0.8931 0.8578 1.0265 -0.0114 0.1207  0.0974  105 GLU A OE2 
735  N N   . GLN A 106 ? 0.7251 0.6425 0.7830 -0.0192 0.1002  0.0491  106 GLN A N   
736  C CA  . GLN A 106 ? 0.6533 0.5652 0.6980 -0.0227 0.0919  0.0414  106 GLN A CA  
737  C C   . GLN A 106 ? 0.7154 0.6229 0.7478 -0.0255 0.0896  0.0369  106 GLN A C   
738  O O   . GLN A 106 ? 0.6498 0.5575 0.6790 -0.0295 0.0814  0.0356  106 GLN A O   
739  C CB  . GLN A 106 ? 0.6197 0.5232 0.6572 -0.0202 0.0958  0.0348  106 GLN A CB  
740  C CG  . GLN A 106 ? 0.5479 0.4560 0.5962 -0.0189 0.0938  0.0393  106 GLN A CG  
741  C CD  . GLN A 106 ? 0.5639 0.4631 0.6051 -0.0169 0.0971  0.0325  106 GLN A CD  
742  O OE1 . GLN A 106 ? 0.5350 0.4247 0.5634 -0.0166 0.1022  0.0244  106 GLN A OE1 
743  N NE2 . GLN A 106 ? 0.5095 0.4128 0.5587 -0.0163 0.0941  0.0362  106 GLN A NE2 
744  N N   . VAL A 107 ? 0.7185 0.6223 0.7446 -0.0236 0.0973  0.0348  107 VAL A N   
745  C CA  . VAL A 107 ? 0.6243 0.5266 0.6403 -0.0260 0.0956  0.0329  107 VAL A CA  
746  C C   . VAL A 107 ? 0.6998 0.6080 0.7242 -0.0288 0.0901  0.0392  107 VAL A C   
747  O O   . VAL A 107 ? 0.6576 0.5639 0.6766 -0.0316 0.0849  0.0380  107 VAL A O   
748  C CB  . VAL A 107 ? 0.6581 0.5585 0.6674 -0.0245 0.1056  0.0313  107 VAL A CB  
749  C CG1 . VAL A 107 ? 0.4983 0.4004 0.4995 -0.0271 0.1038  0.0322  107 VAL A CG1 
750  C CG2 . VAL A 107 ? 0.6812 0.5741 0.6791 -0.0239 0.1106  0.0229  107 VAL A CG2 
751  N N   . VAL A 108 ? 0.5587 0.4743 0.5973 -0.0282 0.0916  0.0465  108 VAL A N   
752  C CA  . VAL A 108 ? 0.5048 0.4263 0.5515 -0.0321 0.0867  0.0521  108 VAL A CA  
753  C C   . VAL A 108 ? 0.6605 0.5812 0.7066 -0.0370 0.0773  0.0496  108 VAL A C   
754  O O   . VAL A 108 ? 0.6988 0.6161 0.7413 -0.0406 0.0734  0.0480  108 VAL A O   
755  C CB  . VAL A 108 ? 0.6053 0.5369 0.6681 -0.0311 0.0902  0.0612  108 VAL A CB  
756  C CG1 . VAL A 108 ? 0.4757 0.4137 0.5464 -0.0365 0.0847  0.0667  108 VAL A CG1 
757  C CG2 . VAL A 108 ? 0.5145 0.4457 0.5777 -0.0263 0.1010  0.0631  108 VAL A CG2 
758  N N   . ARG A 109 ? 0.6331 0.5562 0.6824 -0.0373 0.0745  0.0491  109 ARG A N   
759  C CA  . ARG A 109 ? 0.5684 0.4908 0.6154 -0.0428 0.0664  0.0457  109 ARG A CA  
760  C C   . ARG A 109 ? 0.6829 0.5946 0.7166 -0.0430 0.0644  0.0376  109 ARG A C   
761  O O   . ARG A 109 ? 0.7308 0.6395 0.7628 -0.0478 0.0598  0.0351  109 ARG A O   
762  C CB  . ARG A 109 ? 0.5710 0.4986 0.6223 -0.0426 0.0642  0.0468  109 ARG A CB  
763  C CG  . ARG A 109 ? 0.5922 0.5330 0.6591 -0.0429 0.0653  0.0569  109 ARG A CG  
764  C CD  . ARG A 109 ? 0.7858 0.7366 0.8579 -0.0496 0.0574  0.0598  109 ARG A CD  
765  N NE  . ARG A 109 ? 1.0129 0.9795 1.1013 -0.0510 0.0575  0.0715  109 ARG A NE  
766  C CZ  . ARG A 109 ? 1.1012 1.0740 1.1965 -0.0542 0.0576  0.0766  109 ARG A CZ  
767  N NH1 . ARG A 109 ? 1.1242 1.0877 1.2116 -0.0563 0.0578  0.0711  109 ARG A NH1 
768  N NH2 . ARG A 109 ? 1.1486 1.1376 1.2599 -0.0555 0.0575  0.0884  109 ARG A NH2 
769  N N   . ALA A 110 ? 0.6587 0.5647 0.6836 -0.0384 0.0684  0.0337  110 ALA A N   
770  C CA  . ALA A 110 ? 0.6682 0.5665 0.6820 -0.0388 0.0661  0.0277  110 ALA A CA  
771  C C   . ALA A 110 ? 0.6696 0.5664 0.6832 -0.0403 0.0661  0.0299  110 ALA A C   
772  O O   . ALA A 110 ? 0.6429 0.5349 0.6542 -0.0426 0.0627  0.0275  110 ALA A O   
773  C CB  . ALA A 110 ? 0.4719 0.3662 0.4757 -0.0350 0.0700  0.0234  110 ALA A CB  
774  N N   . ASN A 111 ? 0.5818 0.4822 0.5986 -0.0389 0.0705  0.0350  111 ASN A N   
775  C CA  . ASN A 111 ? 0.6087 0.5082 0.6267 -0.0404 0.0704  0.0384  111 ASN A CA  
776  C C   . ASN A 111 ? 0.6901 0.5894 0.7173 -0.0454 0.0667  0.0400  111 ASN A C   
777  O O   . ASN A 111 ? 0.5813 0.4755 0.6089 -0.0476 0.0653  0.0396  111 ASN A O   
778  C CB  . ASN A 111 ? 0.5595 0.4638 0.5783 -0.0383 0.0762  0.0436  111 ASN A CB  
779  C CG  . ASN A 111 ? 0.7653 0.6688 0.7718 -0.0358 0.0797  0.0411  111 ASN A CG  
780  O OD1 . ASN A 111 ? 0.8762 0.7769 0.8757 -0.0362 0.0771  0.0392  111 ASN A OD1 
781  N ND2 . ASN A 111 ? 0.4906 0.3967 0.4943 -0.0338 0.0862  0.0410  111 ASN A ND2 
782  N N   . ALA A 112 ? 0.6680 0.5732 0.7028 -0.0479 0.0654  0.0418  112 ALA A N   
783  C CA  . ALA A 112 ? 0.5688 0.4750 0.6105 -0.0548 0.0614  0.0422  112 ALA A CA  
784  C C   . ALA A 112 ? 0.6533 0.5516 0.6893 -0.0582 0.0577  0.0349  112 ALA A C   
785  O O   . ALA A 112 ? 0.6002 0.4930 0.6383 -0.0629 0.0571  0.0333  112 ALA A O   
786  C CB  . ALA A 112 ? 0.5503 0.4673 0.6006 -0.0574 0.0598  0.0463  112 ALA A CB  
787  N N   . LEU A 113 ? 0.6624 0.5591 0.6915 -0.0557 0.0561  0.0302  113 LEU A N   
788  C CA  . LEU A 113 ? 0.6181 0.5077 0.6419 -0.0588 0.0531  0.0234  113 LEU A CA  
789  C C   . LEU A 113 ? 0.6965 0.5771 0.7174 -0.0567 0.0554  0.0220  113 LEU A C   
790  O O   . LEU A 113 ? 0.6875 0.5610 0.7097 -0.0608 0.0552  0.0187  113 LEU A O   
791  C CB  . LEU A 113 ? 0.5088 0.3990 0.5263 -0.0562 0.0512  0.0194  113 LEU A CB  
792  C CG  . LEU A 113 ? 0.5041 0.3901 0.5175 -0.0609 0.0476  0.0128  113 LEU A CG  
793  C CD1 . LEU A 113 ? 0.5411 0.4340 0.5593 -0.0692 0.0442  0.0133  113 LEU A CD1 
794  C CD2 . LEU A 113 ? 0.5211 0.4064 0.5275 -0.0571 0.0464  0.0093  113 LEU A CD2 
795  N N   . ALA A 114 ? 0.6967 0.5778 0.7141 -0.0508 0.0581  0.0251  114 ALA A N   
796  C CA  . ALA A 114 ? 0.6875 0.5632 0.7039 -0.0487 0.0599  0.0266  114 ALA A CA  
797  C C   . ALA A 114 ? 0.6954 0.5679 0.7211 -0.0521 0.0619  0.0301  114 ALA A C   
798  O O   . ALA A 114 ? 0.5771 0.4418 0.6056 -0.0532 0.0631  0.0289  114 ALA A O   
799  C CB  . ALA A 114 ? 0.6112 0.4915 0.6222 -0.0436 0.0622  0.0305  114 ALA A CB  
800  N N   . GLU A 115 ? 0.6221 0.5000 0.6537 -0.0541 0.0628  0.0346  115 GLU A N   
801  C CA  . GLU A 115 ? 0.5749 0.4498 0.6156 -0.0579 0.0650  0.0381  115 GLU A CA  
802  C C   . GLU A 115 ? 0.5591 0.4265 0.6025 -0.0653 0.0640  0.0318  115 GLU A C   
803  O O   . GLU A 115 ? 0.6136 0.4721 0.6621 -0.0673 0.0672  0.0315  115 GLU A O   
804  C CB  . GLU A 115 ? 0.8610 0.7444 0.9075 -0.0589 0.0660  0.0442  115 GLU A CB  
805  C CG  . GLU A 115 ? 0.9781 0.8670 1.0227 -0.0529 0.0693  0.0509  115 GLU A CG  
806  C CD  . GLU A 115 ? 0.9978 0.8959 1.0470 -0.0529 0.0709  0.0560  115 GLU A CD  
807  O OE1 . GLU A 115 ? 0.9623 0.8654 1.0076 -0.0483 0.0741  0.0594  115 GLU A OE1 
808  O OE2 . GLU A 115 ? 1.0016 0.9025 1.0583 -0.0580 0.0694  0.0565  115 GLU A OE2 
809  N N   . GLU A 116 ? 0.6448 0.5157 0.6852 -0.0697 0.0602  0.0267  116 GLU A N   
810  C CA  . GLU A 116 ? 0.6029 0.4679 0.6444 -0.0787 0.0596  0.0202  116 GLU A CA  
811  C C   . GLU A 116 ? 0.6543 0.5075 0.6918 -0.0779 0.0616  0.0137  116 GLU A C   
812  O O   . GLU A 116 ? 0.7263 0.5706 0.7658 -0.0849 0.0641  0.0081  116 GLU A O   
813  C CB  . GLU A 116 ? 0.5037 0.3782 0.5428 -0.0847 0.0546  0.0177  116 GLU A CB  
814  C CG  . GLU A 116 ? 0.5966 0.4844 0.6417 -0.0851 0.0529  0.0253  116 GLU A CG  
815  C CD  . GLU A 116 ? 0.6801 0.5689 0.7336 -0.0918 0.0545  0.0287  116 GLU A CD  
816  O OE1 . GLU A 116 ? 0.6062 0.4900 0.6598 -0.1016 0.0544  0.0231  116 GLU A OE1 
817  O OE2 . GLU A 116 ? 0.8657 0.7599 0.9253 -0.0878 0.0565  0.0365  116 GLU A OE2 
818  N N   . ALA A 117 ? 0.6577 0.5103 0.6899 -0.0700 0.0613  0.0142  117 ALA A N   
819  C CA  . ALA A 117 ? 0.6728 0.5155 0.7027 -0.0688 0.0633  0.0090  117 ALA A CA  
820  C C   . ALA A 117 ? 0.7264 0.5618 0.7636 -0.0644 0.0688  0.0143  117 ALA A C   
821  O O   . ALA A 117 ? 0.7969 0.6233 0.8356 -0.0634 0.0721  0.0114  117 ALA A O   
822  C CB  . ALA A 117 ? 0.5285 0.3751 0.5496 -0.0635 0.0600  0.0070  117 ALA A CB  
823  N N   . GLY A 118 ? 0.6144 0.4540 0.6573 -0.0619 0.0704  0.0227  118 GLY A N   
824  C CA  . GLY A 118 ? 0.6152 0.4503 0.6663 -0.0575 0.0753  0.0298  118 GLY A CA  
825  C C   . GLY A 118 ? 0.7975 0.6400 0.8443 -0.0496 0.0738  0.0360  118 GLY A C   
826  O O   . GLY A 118 ? 0.7973 0.6382 0.8509 -0.0454 0.0772  0.0431  118 GLY A O   
827  N N   . LEU A 119 ? 0.6921 0.5433 0.7285 -0.0479 0.0691  0.0340  119 LEU A N   
828  C CA  . LEU A 119 ? 0.5941 0.4520 0.6236 -0.0424 0.0675  0.0374  119 LEU A CA  
829  C C   . LEU A 119 ? 0.7043 0.5731 0.7283 -0.0405 0.0666  0.0421  119 LEU A C   
830  O O   . LEU A 119 ? 0.7266 0.6015 0.7414 -0.0380 0.0649  0.0420  119 LEU A O   
831  C CB  . LEU A 119 ? 0.5558 0.4119 0.5767 -0.0423 0.0643  0.0291  119 LEU A CB  
832  C CG  . LEU A 119 ? 0.6223 0.4687 0.6472 -0.0430 0.0662  0.0249  119 LEU A CG  
833  C CD1 . LEU A 119 ? 0.5543 0.4000 0.5703 -0.0443 0.0626  0.0162  119 LEU A CD1 
834  C CD2 . LEU A 119 ? 0.6034 0.4503 0.6336 -0.0380 0.0687  0.0325  119 LEU A CD2 
835  N N   . ALA A 120 ? 0.6272 0.4984 0.6564 -0.0422 0.0683  0.0461  120 ALA A N   
836  C CA  . ALA A 120 ? 0.6333 0.5143 0.6575 -0.0406 0.0687  0.0502  120 ALA A CA  
837  C C   . ALA A 120 ? 0.5668 0.4550 0.5867 -0.0374 0.0696  0.0572  120 ALA A C   
838  O O   . ALA A 120 ? 0.6067 0.5026 0.6178 -0.0368 0.0700  0.0579  120 ALA A O   
839  C CB  . ALA A 120 ? 0.5198 0.4027 0.5519 -0.0428 0.0709  0.0546  120 ALA A CB  
840  N N   . ASP A 121 ? 0.6069 0.4931 0.6330 -0.0359 0.0703  0.0626  121 ASP A N   
841  C CA  . ASP A 121 ? 0.6624 0.5581 0.6851 -0.0336 0.0701  0.0707  121 ASP A CA  
842  C C   . ASP A 121 ? 0.8063 0.7045 0.8186 -0.0328 0.0670  0.0660  121 ASP A C   
843  O O   . ASP A 121 ? 1.1268 1.0360 1.1316 -0.0327 0.0660  0.0709  121 ASP A O   
844  C CB  . ASP A 121 ? 0.6127 0.5072 0.6494 -0.0317 0.0727  0.0811  121 ASP A CB  
845  C CG  . ASP A 121 ? 0.6837 0.5658 0.7289 -0.0311 0.0738  0.0768  121 ASP A CG  
846  O OD1 . ASP A 121 ? 0.7794 0.6522 0.8225 -0.0337 0.0732  0.0662  121 ASP A OD1 
847  O OD2 . ASP A 121 ? 0.7656 0.6476 0.8200 -0.0283 0.0758  0.0845  121 ASP A OD2 
848  N N   . ARG A 122 ? 0.6298 0.5194 0.6408 -0.0331 0.0653  0.0568  122 ARG A N   
849  C CA  . ARG A 122 ? 0.6168 0.5085 0.6189 -0.0324 0.0624  0.0527  122 ARG A CA  
850  C C   . ARG A 122 ? 0.5986 0.4888 0.5894 -0.0338 0.0607  0.0424  122 ARG A C   
851  O O   . ARG A 122 ? 0.6363 0.5297 0.6179 -0.0339 0.0587  0.0391  122 ARG A O   
852  C CB  . ARG A 122 ? 0.6967 0.5804 0.7069 -0.0309 0.0625  0.0517  122 ARG A CB  
853  C CG  . ARG A 122 ? 0.7510 0.6359 0.7751 -0.0284 0.0657  0.0635  122 ARG A CG  
854  C CD  . ARG A 122 ? 0.8669 0.7497 0.8976 -0.0256 0.0663  0.0662  122 ARG A CD  
855  N NE  . ARG A 122 ? 1.1586 1.0269 1.1925 -0.0265 0.0681  0.0562  122 ARG A NE  
856  C CZ  . ARG A 122 ? 1.2287 1.0937 1.2534 -0.0278 0.0652  0.0458  122 ARG A CZ  
857  N NH1 . ARG A 122 ? 1.1176 0.9913 1.1295 -0.0280 0.0606  0.0435  122 ARG A NH1 
858  N NH2 . ARG A 122 ? 1.3118 1.1644 1.3399 -0.0297 0.0673  0.0374  122 ARG A NH2 
859  N N   . ALA A 123 ? 0.6766 0.5630 0.6689 -0.0352 0.0616  0.0382  123 ALA A N   
860  C CA  . ALA A 123 ? 0.6360 0.5221 0.6204 -0.0359 0.0611  0.0307  123 ALA A CA  
861  C C   . ALA A 123 ? 0.6678 0.5584 0.6516 -0.0363 0.0644  0.0330  123 ALA A C   
862  O O   . ALA A 123 ? 0.7672 0.6564 0.7594 -0.0371 0.0654  0.0350  123 ALA A O   
863  C CB  . ALA A 123 ? 0.5362 0.4151 0.5246 -0.0372 0.0592  0.0242  123 ALA A CB  
864  N N   . ARG A 124 ? 0.6659 0.5620 0.6397 -0.0363 0.0665  0.0323  124 ARG A N   
865  C CA  . ARG A 124 ? 0.4917 0.3919 0.4640 -0.0366 0.0712  0.0340  124 ARG A CA  
866  C C   . ARG A 124 ? 0.6175 0.5155 0.5838 -0.0363 0.0742  0.0269  124 ARG A C   
867  O O   . ARG A 124 ? 0.7271 0.6233 0.6848 -0.0368 0.0734  0.0214  124 ARG A O   
868  C CB  . ARG A 124 ? 0.5414 0.4499 0.5066 -0.0379 0.0732  0.0392  124 ARG A CB  
869  C CG  . ARG A 124 ? 0.6113 0.5231 0.5831 -0.0376 0.0709  0.0478  124 ARG A CG  
870  C CD  . ARG A 124 ? 0.8656 0.7881 0.8317 -0.0394 0.0735  0.0546  124 ARG A CD  
871  N NE  . ARG A 124 ? 0.9404 0.8714 0.8956 -0.0418 0.0717  0.0561  124 ARG A NE  
872  C CZ  . ARG A 124 ? 1.0016 0.9394 0.9613 -0.0416 0.0687  0.0654  124 ARG A CZ  
873  N NH1 . ARG A 124 ? 0.8858 0.8201 0.8610 -0.0387 0.0683  0.0726  124 ARG A NH1 
874  N NH2 . ARG A 124 ? 1.0612 1.0096 1.0110 -0.0446 0.0666  0.0680  124 ARG A NH2 
875  N N   . PHE A 125 ? 0.6169 0.5154 0.5885 -0.0355 0.0784  0.0278  125 PHE A N   
876  C CA  . PHE A 125 ? 0.6629 0.5590 0.6325 -0.0343 0.0830  0.0227  125 PHE A CA  
877  C C   . PHE A 125 ? 0.5773 0.4767 0.5458 -0.0340 0.0911  0.0246  125 PHE A C   
878  O O   . PHE A 125 ? 0.6523 0.5560 0.6269 -0.0341 0.0921  0.0308  125 PHE A O   
879  C CB  . PHE A 125 ? 0.6466 0.5402 0.6275 -0.0332 0.0802  0.0225  125 PHE A CB  
880  C CG  . PHE A 125 ? 0.6133 0.5033 0.5937 -0.0341 0.0734  0.0196  125 PHE A CG  
881  C CD1 . PHE A 125 ? 0.7321 0.6187 0.7048 -0.0338 0.0726  0.0136  125 PHE A CD1 
882  C CD2 . PHE A 125 ? 0.6496 0.5390 0.6366 -0.0358 0.0687  0.0223  125 PHE A CD2 
883  C CE1 . PHE A 125 ? 0.8026 0.6862 0.7747 -0.0347 0.0668  0.0109  125 PHE A CE1 
884  C CE2 . PHE A 125 ? 0.6257 0.5110 0.6119 -0.0369 0.0639  0.0189  125 PHE A CE2 
885  C CZ  . PHE A 125 ? 0.7701 0.6529 0.7487 -0.0361 0.0627  0.0134  125 PHE A CZ  
886  N N   . GLN A 126 ? 0.7079 0.6047 0.6693 -0.0339 0.0977  0.0189  126 GLN A N   
887  C CA  . GLN A 126 ? 0.7462 0.6448 0.7048 -0.0341 0.1073  0.0190  126 GLN A CA  
888  C C   . GLN A 126 ? 0.7221 0.6142 0.6803 -0.0324 0.1154  0.0128  126 GLN A C   
889  O O   . GLN A 126 ? 0.6956 0.5826 0.6502 -0.0325 0.1133  0.0073  126 GLN A O   
890  C CB  . GLN A 126 ? 0.5673 0.4708 0.5106 -0.0386 0.1089  0.0183  126 GLN A CB  
891  C CG  . GLN A 126 ? 0.7675 0.6676 0.6955 -0.0420 0.1122  0.0093  126 GLN A CG  
892  C CD  . GLN A 126 ? 0.9058 0.8135 0.8185 -0.0479 0.1096  0.0094  126 GLN A CD  
893  O OE1 . GLN A 126 ? 0.8906 0.8048 0.8056 -0.0482 0.1018  0.0163  126 GLN A OE1 
894  N NE2 . GLN A 126 ? 1.0791 0.9866 0.9766 -0.0531 0.1169  0.0022  126 GLN A NE2 
895  N N   . ARG A 127 ? 0.7187 0.6108 0.6820 -0.0306 0.1253  0.0139  127 ARG A N   
896  C CA  . ARG A 127 ? 0.7581 0.6430 0.7234 -0.0284 0.1353  0.0087  127 ARG A CA  
897  C C   . ARG A 127 ? 0.7869 0.6668 0.7333 -0.0332 0.1428  -0.0011 127 ARG A C   
898  O O   . ARG A 127 ? 0.7781 0.6619 0.7135 -0.0373 0.1469  -0.0021 127 ARG A O   
899  C CB  . ARG A 127 ? 0.7321 0.6185 0.7122 -0.0242 0.1445  0.0143  127 ARG A CB  
900  C CG  . ARG A 127 ? 0.8303 0.7084 0.8142 -0.0214 0.1573  0.0097  127 ARG A CG  
901  C CD  . ARG A 127 ? 0.9152 0.7966 0.9212 -0.0153 0.1636  0.0187  127 ARG A CD  
902  N NE  . ARG A 127 ? 1.0644 0.9377 1.0728 -0.0129 0.1806  0.0146  127 ARG A NE  
903  C CZ  . ARG A 127 ? 1.0586 0.9295 1.0580 -0.0151 0.1923  0.0103  127 ARG A CZ  
904  N NH1 . ARG A 127 ? 0.9157 0.7932 0.9035 -0.0197 0.1875  0.0108  127 ARG A NH1 
905  N NH2 . ARG A 127 ? 1.1151 0.9769 1.1175 -0.0130 0.2093  0.0057  127 ARG A NH2 
906  N N   . ALA A 128 ? 0.6626 0.5348 0.6046 -0.0336 0.1444  -0.0082 128 ALA A N   
907  C CA  . ALA A 128 ? 0.7479 0.6149 0.6715 -0.0396 0.1515  -0.0187 128 ALA A CA  
908  C C   . ALA A 128 ? 0.8158 0.6727 0.7415 -0.0381 0.1548  -0.0250 128 ALA A C   
909  O O   . ALA A 128 ? 0.8153 0.6711 0.7557 -0.0327 0.1499  -0.0203 128 ALA A O   
910  C CB  . ALA A 128 ? 0.7036 0.5779 0.6104 -0.0463 0.1424  -0.0200 128 ALA A CB  
911  N N   . ASP A 129 ? 0.8082 0.6583 0.7184 -0.0439 0.1633  -0.0355 129 ASP A N   
912  C CA  . ASP A 129 ? 0.7114 0.5496 0.6218 -0.0438 0.1707  -0.0432 129 ASP A CA  
913  C C   . ASP A 129 ? 0.8011 0.6396 0.6916 -0.0521 0.1653  -0.0514 129 ASP A C   
914  O O   . ASP A 129 ? 0.8350 0.6788 0.7079 -0.0600 0.1659  -0.0554 129 ASP A O   
915  C CB  . ASP A 129 ? 0.7981 0.6262 0.7098 -0.0437 0.1900  -0.0490 129 ASP A CB  
916  C CG  . ASP A 129 ? 0.9245 0.7384 0.8379 -0.0435 0.2003  -0.0571 129 ASP A CG  
917  O OD1 . ASP A 129 ? 1.0161 0.8277 0.9204 -0.0474 0.1941  -0.0624 129 ASP A OD1 
918  O OD2 . ASP A 129 ? 1.1071 0.9117 1.0326 -0.0391 0.2157  -0.0576 129 ASP A OD2 
919  N N   . ALA A 130 ? 0.8258 0.6603 0.7190 -0.0508 0.1594  -0.0530 130 ALA A N   
920  C CA  . ALA A 130 ? 0.8244 0.6610 0.7002 -0.0586 0.1531  -0.0594 130 ALA A CA  
921  C C   . ALA A 130 ? 0.8656 0.6937 0.7248 -0.0673 0.1659  -0.0722 130 ALA A C   
922  O O   . ALA A 130 ? 0.8871 0.7197 0.7285 -0.0763 0.1616  -0.0777 130 ALA A O   
923  C CB  . ALA A 130 ? 0.7979 0.6329 0.6813 -0.0549 0.1436  -0.0575 130 ALA A CB  
924  N N   . MET A 131 ? 0.8081 0.6245 0.6726 -0.0654 0.1821  -0.0769 131 MET A N   
925  C CA  . MET A 131 ? 0.8700 0.6772 0.7175 -0.0750 0.1966  -0.0904 131 MET A CA  
926  C C   . MET A 131 ? 0.9327 0.7504 0.7598 -0.0851 0.1965  -0.0933 131 MET A C   
927  O O   . MET A 131 ? 1.0146 0.8313 0.8205 -0.0972 0.2013  -0.1041 131 MET A O   
928  C CB  . MET A 131 ? 0.8115 0.6037 0.6714 -0.0701 0.2158  -0.0937 131 MET A CB  
929  C CG  . MET A 131 ? 0.9408 0.7244 0.8232 -0.0600 0.2169  -0.0887 131 MET A CG  
930  S SD  . MET A 131 ? 1.1786 0.9477 1.0497 -0.0675 0.2239  -0.1025 131 MET A SD  
931  C CE  . MET A 131 ? 1.2890 1.0370 1.1709 -0.0650 0.2510  -0.1097 131 MET A CE  
932  N N   . ASP A 132 ? 0.9278 0.7564 0.7608 -0.0811 0.1914  -0.0834 132 ASP A N   
933  C CA  . ASP A 132 ? 0.9598 0.8001 0.7754 -0.0899 0.1914  -0.0840 132 ASP A CA  
934  C C   . ASP A 132 ? 0.9636 0.8202 0.7856 -0.0858 0.1744  -0.0702 132 ASP A C   
935  O O   . ASP A 132 ? 0.8972 0.7579 0.7312 -0.0793 0.1739  -0.0615 132 ASP A O   
936  C CB  . ASP A 132 ? 0.9523 0.7860 0.7690 -0.0896 0.2085  -0.0876 132 ASP A CB  
937  C CG  . ASP A 132 ? 1.0541 0.8967 0.8473 -0.1023 0.2131  -0.0930 132 ASP A CG  
938  O OD1 . ASP A 132 ? 0.9667 0.8227 0.7437 -0.1111 0.2017  -0.0923 132 ASP A OD1 
939  O OD2 . ASP A 132 ? 1.2190 1.0564 1.0107 -0.1034 0.2281  -0.0971 132 ASP A OD2 
940  N N   . LEU A 133 ? 0.9132 0.7790 0.7273 -0.0899 0.1613  -0.0682 133 LEU A N   
941  C CA  . LEU A 133 ? 0.8935 0.7724 0.7160 -0.0853 0.1459  -0.0553 133 LEU A CA  
942  C C   . LEU A 133 ? 0.9292 0.8227 0.7431 -0.0904 0.1445  -0.0492 133 LEU A C   
943  O O   . LEU A 133 ? 0.9672 0.8698 0.7615 -0.1016 0.1449  -0.0530 133 LEU A O   
944  C CB  . LEU A 133 ? 0.8607 0.7448 0.6790 -0.0878 0.1338  -0.0545 133 LEU A CB  
945  C CG  . LEU A 133 ? 0.8735 0.7486 0.7049 -0.0806 0.1287  -0.0547 133 LEU A CG  
946  C CD1 . LEU A 133 ? 0.8006 0.6826 0.6237 -0.0855 0.1183  -0.0549 133 LEU A CD1 
947  C CD2 . LEU A 133 ? 0.9084 0.7834 0.7608 -0.0695 0.1223  -0.0445 133 LEU A CD2 
948  N N   . PRO A 134 ? 0.9206 0.8182 0.7478 -0.0834 0.1422  -0.0393 134 PRO A N   
949  C CA  . PRO A 134 ? 0.7607 0.6728 0.5807 -0.0881 0.1409  -0.0324 134 PRO A CA  
950  C C   . PRO A 134 ? 0.8497 0.7773 0.6680 -0.0903 0.1267  -0.0225 134 PRO A C   
951  O O   . PRO A 134 ? 1.0622 0.9982 0.8906 -0.0861 0.1206  -0.0108 134 PRO A O   
952  C CB  . PRO A 134 ? 0.6456 0.5546 0.4839 -0.0788 0.1438  -0.0252 134 PRO A CB  
953  C CG  . PRO A 134 ? 0.7875 0.6882 0.6442 -0.0694 0.1373  -0.0225 134 PRO A CG  
954  C CD  . PRO A 134 ? 0.8357 0.7266 0.6857 -0.0717 0.1397  -0.0329 134 PRO A CD  
955  N N   . PHE A 135 ? 0.8065 0.7382 0.6129 -0.0970 0.1219  -0.0264 135 PHE A N   
956  C CA  . PHE A 135 ? 0.7884 0.7350 0.5958 -0.0982 0.1088  -0.0159 135 PHE A CA  
957  C C   . PHE A 135 ? 0.8535 0.8132 0.6395 -0.1115 0.1074  -0.0192 135 PHE A C   
958  O O   . PHE A 135 ? 0.8715 0.8242 0.6438 -0.1186 0.1138  -0.0320 135 PHE A O   
959  C CB  . PHE A 135 ? 0.8823 0.8214 0.7045 -0.0898 0.1006  -0.0139 135 PHE A CB  
960  C CG  . PHE A 135 ? 0.9015 0.8290 0.7438 -0.0784 0.1011  -0.0111 135 PHE A CG  
961  C CD1 . PHE A 135 ? 0.7777 0.7107 0.6336 -0.0728 0.0960  0.0006  135 PHE A CD1 
962  C CD2 . PHE A 135 ? 0.9106 0.8226 0.7589 -0.0739 0.1068  -0.0194 135 PHE A CD2 
963  C CE1 . PHE A 135 ? 0.6916 0.6152 0.5648 -0.0642 0.0962  0.0028  135 PHE A CE1 
964  C CE2 . PHE A 135 ? 0.8664 0.7707 0.7329 -0.0647 0.1065  -0.0156 135 PHE A CE2 
965  C CZ  . PHE A 135 ? 0.7288 0.6392 0.6069 -0.0605 0.1010  -0.0051 135 PHE A CZ  
966  N N   . GLU A 136 ? 0.8490 0.8285 0.6334 -0.1151 0.0987  -0.0068 136 GLU A N   
967  C CA  . GLU A 136 ? 0.8128 0.8102 0.5785 -0.1283 0.0950  -0.0062 136 GLU A CA  
968  C C   . GLU A 136 ? 0.9099 0.9035 0.6718 -0.1309 0.0907  -0.0127 136 GLU A C   
969  O O   . GLU A 136 ? 0.8931 0.8751 0.6699 -0.1212 0.0869  -0.0127 136 GLU A O   
970  C CB  . GLU A 136 ? 0.8528 0.8731 0.6241 -0.1289 0.0850  0.0123  136 GLU A CB  
971  C CG  . GLU A 136 ? 1.0038 1.0312 0.7779 -0.1278 0.0884  0.0205  136 GLU A CG  
972  C CD  . GLU A 136 ? 1.2131 1.2516 0.9634 -0.1421 0.0956  0.0148  136 GLU A CD  
973  O OE1 . GLU A 136 ? 1.3455 1.4071 1.0835 -0.1531 0.0899  0.0223  136 GLU A OE1 
974  O OE2 . GLU A 136 ? 1.2704 1.2950 1.0143 -0.1429 0.1073  0.0028  136 GLU A OE2 
975  N N   . ASP A 137 ? 0.8992 0.9043 0.6401 -0.1454 0.0911  -0.0180 137 ASP A N   
976  C CA  . ASP A 137 ? 0.9434 0.9512 0.6803 -0.1496 0.0849  -0.0209 137 ASP A CA  
977  C C   . ASP A 137 ? 0.9108 0.9311 0.6649 -0.1420 0.0718  -0.0042 137 ASP A C   
978  O O   . ASP A 137 ? 0.8659 0.9014 0.6277 -0.1397 0.0667  0.0108  137 ASP A O   
979  C CB  . ASP A 137 ? 0.9886 1.0121 0.6995 -0.1685 0.0862  -0.0266 137 ASP A CB  
980  C CG  . ASP A 137 ? 1.0443 1.0546 0.7364 -0.1779 0.1012  -0.0447 137 ASP A CG  
981  O OD1 . ASP A 137 ? 1.0864 1.0756 0.7870 -0.1688 0.1109  -0.0518 137 ASP A OD1 
982  O OD2 . ASP A 137 ? 1.0400 1.0612 0.7088 -0.1950 0.1036  -0.0519 137 ASP A OD2 
983  N N   . GLU A 138 ? 0.8802 0.8931 0.6412 -0.1378 0.0672  -0.0067 138 GLU A N   
984  C CA  . GLU A 138 ? 0.9150 0.9391 0.6912 -0.1318 0.0561  0.0073  138 GLU A CA  
985  C C   . GLU A 138 ? 0.9103 0.9337 0.7077 -0.1193 0.0533  0.0205  138 GLU A C   
986  O O   . GLU A 138 ? 0.9463 0.9861 0.7537 -0.1173 0.0462  0.0363  138 GLU A O   
987  C CB  . GLU A 138 ? 0.9144 0.9658 0.6794 -0.1442 0.0490  0.0164  138 GLU A CB  
988  C CG  . GLU A 138 ? 0.9713 1.0223 0.7136 -0.1584 0.0526  0.0017  138 GLU A CG  
989  C CD  . GLU A 138 ? 0.9162 0.9944 0.6476 -0.1716 0.0446  0.0097  138 GLU A CD  
990  O OE1 . GLU A 138 ? 0.9308 1.0274 0.6762 -0.1673 0.0353  0.0280  138 GLU A OE1 
991  O OE2 . GLU A 138 ? 0.9703 1.0516 0.6794 -0.1868 0.0484  -0.0023 138 GLU A OE2 
992  N N   . SER A 139 ? 0.8571 0.8612 0.6624 -0.1108 0.0596  0.0142  139 SER A N   
993  C CA  . SER A 139 ? 0.7492 0.7502 0.5736 -0.1000 0.0583  0.0244  139 SER A CA  
994  C C   . SER A 139 ? 0.8359 0.8235 0.6786 -0.0888 0.0548  0.0252  139 SER A C   
995  O O   . SER A 139 ? 0.9658 0.9538 0.8250 -0.0811 0.0520  0.0355  139 SER A O   
996  C CB  . SER A 139 ? 0.7193 0.7098 0.5421 -0.0983 0.0670  0.0186  139 SER A CB  
997  O OG  . SER A 139 ? 0.8365 0.8114 0.6499 -0.1004 0.0746  0.0027  139 SER A OG  
998  N N   . PHE A 140 ? 0.9173 0.8932 0.7574 -0.0882 0.0552  0.0146  140 PHE A N   
999  C CA  . PHE A 140 ? 0.9220 0.8844 0.7779 -0.0784 0.0528  0.0137  140 PHE A CA  
1000 C C   . PHE A 140 ? 0.8633 0.8302 0.7206 -0.0790 0.0467  0.0152  140 PHE A C   
1001 O O   . PHE A 140 ? 0.9065 0.8770 0.7504 -0.0866 0.0465  0.0087  140 PHE A O   
1002 C CB  . PHE A 140 ? 0.8082 0.7518 0.6638 -0.0753 0.0591  0.0012  140 PHE A CB  
1003 C CG  . PHE A 140 ? 0.7123 0.6499 0.5738 -0.0713 0.0643  0.0021  140 PHE A CG  
1004 C CD1 . PHE A 140 ? 0.6581 0.5931 0.5361 -0.0637 0.0617  0.0099  140 PHE A CD1 
1005 C CD2 . PHE A 140 ? 0.7554 0.6900 0.6062 -0.0757 0.0724  -0.0050 140 PHE A CD2 
1006 C CE1 . PHE A 140 ? 0.7390 0.6695 0.6231 -0.0605 0.0663  0.0112  140 PHE A CE1 
1007 C CE2 . PHE A 140 ? 0.7974 0.7274 0.6550 -0.0718 0.0776  -0.0034 140 PHE A CE2 
1008 C CZ  . PHE A 140 ? 0.7521 0.6807 0.6264 -0.0642 0.0739  0.0050  140 PHE A CZ  
1009 N N   . ASP A 141 ? 0.6656 0.6318 0.5395 -0.0713 0.0424  0.0236  141 ASP A N   
1010 C CA  . ASP A 141 ? 0.7168 0.6849 0.5952 -0.0701 0.0375  0.0249  141 ASP A CA  
1011 C C   . ASP A 141 ? 0.7142 0.6661 0.5904 -0.0682 0.0392  0.0119  141 ASP A C   
1012 O O   . ASP A 141 ? 0.8360 0.7900 0.7095 -0.0702 0.0362  0.0097  141 ASP A O   
1013 C CB  . ASP A 141 ? 0.7049 0.6738 0.6027 -0.0620 0.0348  0.0362  141 ASP A CB  
1014 C CG  . ASP A 141 ? 0.8092 0.7951 0.7125 -0.0629 0.0330  0.0513  141 ASP A CG  
1015 O OD1 . ASP A 141 ? 0.9617 0.9657 0.8561 -0.0703 0.0299  0.0570  141 ASP A OD1 
1016 O OD2 . ASP A 141 ? 0.8616 0.8434 0.7783 -0.0569 0.0349  0.0579  141 ASP A OD2 
1017 N N   . ALA A 142 ? 0.7004 0.6374 0.5787 -0.0644 0.0439  0.0045  142 ALA A N   
1018 C CA  . ALA A 142 ? 0.6826 0.6056 0.5610 -0.0622 0.0455  -0.0058 142 ALA A CA  
1019 C C   . ALA A 142 ? 0.7810 0.6928 0.6597 -0.0602 0.0517  -0.0119 142 ALA A C   
1020 O O   . ALA A 142 ? 0.9252 0.8371 0.8104 -0.0573 0.0532  -0.0071 142 ALA A O   
1021 C CB  . ALA A 142 ? 0.6151 0.5325 0.5070 -0.0555 0.0418  -0.0035 142 ALA A CB  
1022 N N   . VAL A 143 ? 0.7499 0.6524 0.6230 -0.0617 0.0557  -0.0215 143 VAL A N   
1023 C CA  . VAL A 143 ? 0.6983 0.5899 0.5754 -0.0584 0.0619  -0.0263 143 VAL A CA  
1024 C C   . VAL A 143 ? 0.7960 0.6785 0.6818 -0.0537 0.0602  -0.0292 143 VAL A C   
1025 O O   . VAL A 143 ? 0.9382 0.8201 0.8208 -0.0551 0.0575  -0.0324 143 VAL A O   
1026 C CB  . VAL A 143 ? 0.6659 0.5541 0.5306 -0.0642 0.0701  -0.0343 143 VAL A CB  
1027 C CG1 . VAL A 143 ? 0.6684 0.5462 0.5401 -0.0599 0.0776  -0.0373 143 VAL A CG1 
1028 C CG2 . VAL A 143 ? 0.6287 0.5282 0.4821 -0.0709 0.0712  -0.0317 143 VAL A CG2 
1029 N N   . ILE A 144 ? 0.6817 0.5586 0.5784 -0.0486 0.0614  -0.0277 144 ILE A N   
1030 C CA  . ILE A 144 ? 0.6533 0.5230 0.5573 -0.0452 0.0606  -0.0303 144 ILE A CA  
1031 C C   . ILE A 144 ? 0.7589 0.6229 0.6674 -0.0433 0.0676  -0.0319 144 ILE A C   
1032 O O   . ILE A 144 ? 0.7272 0.5929 0.6388 -0.0423 0.0706  -0.0286 144 ILE A O   
1033 C CB  . ILE A 144 ? 0.7399 0.6103 0.6543 -0.0417 0.0547  -0.0257 144 ILE A CB  
1034 C CG1 . ILE A 144 ? 0.6920 0.5570 0.6136 -0.0393 0.0544  -0.0278 144 ILE A CG1 
1035 C CG2 . ILE A 144 ? 0.7297 0.6030 0.6504 -0.0402 0.0547  -0.0197 144 ILE A CG2 
1036 C CD1 . ILE A 144 ? 0.7595 0.6249 0.6890 -0.0378 0.0493  -0.0251 144 ILE A CD1 
1037 N N   . ALA A 145 ? 0.7327 0.5906 0.6428 -0.0425 0.0706  -0.0361 145 ALA A N   
1038 C CA  . ALA A 145 ? 0.6593 0.5117 0.5758 -0.0402 0.0785  -0.0367 145 ALA A CA  
1039 C C   . ALA A 145 ? 0.7225 0.5729 0.6498 -0.0366 0.0759  -0.0347 145 ALA A C   
1040 O O   . ALA A 145 ? 0.8386 0.6844 0.7651 -0.0369 0.0781  -0.0383 145 ALA A O   
1041 C CB  . ALA A 145 ? 0.5850 0.4316 0.4920 -0.0438 0.0875  -0.0438 145 ALA A CB  
1042 N N   . LEU A 146 ? 0.6605 0.5151 0.5980 -0.0341 0.0718  -0.0287 146 LEU A N   
1043 C CA  . LEU A 146 ? 0.6294 0.4857 0.5753 -0.0326 0.0667  -0.0261 146 LEU A CA  
1044 C C   . LEU A 146 ? 0.6910 0.5474 0.6490 -0.0296 0.0720  -0.0217 146 LEU A C   
1045 O O   . LEU A 146 ? 0.7687 0.6287 0.7344 -0.0281 0.0738  -0.0166 146 LEU A O   
1046 C CB  . LEU A 146 ? 0.5156 0.3771 0.4646 -0.0333 0.0595  -0.0226 146 LEU A CB  
1047 C CG  . LEU A 146 ? 0.6083 0.4718 0.5600 -0.0344 0.0526  -0.0223 146 LEU A CG  
1048 C CD1 . LEU A 146 ? 0.5733 0.4398 0.5281 -0.0359 0.0485  -0.0198 146 LEU A CD1 
1049 C CD2 . LEU A 146 ? 0.5999 0.4658 0.5597 -0.0337 0.0524  -0.0197 146 LEU A CD2 
1050 N N   . GLU A 147 ? 0.6546 0.5078 0.6157 -0.0285 0.0747  -0.0227 147 GLU A N   
1051 C CA  . GLU A 147 ? 0.6907 0.5432 0.6648 -0.0249 0.0821  -0.0177 147 GLU A CA  
1052 C C   . GLU A 147 ? 0.7650 0.6149 0.7421 -0.0231 0.0914  -0.0167 147 GLU A C   
1053 O O   . GLU A 147 ? 0.7952 0.6494 0.7864 -0.0198 0.0948  -0.0091 147 GLU A O   
1054 C CB  . GLU A 147 ? 0.5850 0.4471 0.5726 -0.0236 0.0766  -0.0086 147 GLU A CB  
1055 C CG  . GLU A 147 ? 0.5383 0.4021 0.5303 -0.0234 0.0740  -0.0067 147 GLU A CG  
1056 C CD  . GLU A 147 ? 0.6816 0.5577 0.6849 -0.0240 0.0676  0.0024  147 GLU A CD  
1057 O OE1 . GLU A 147 ? 0.6483 0.5311 0.6653 -0.0218 0.0706  0.0112  147 GLU A OE1 
1058 O OE2 . GLU A 147 ? 0.8057 0.6856 0.8036 -0.0275 0.0593  0.0006  147 GLU A OE2 
1059 N N   . SER A 148 ? 0.7182 0.5626 0.6826 -0.0256 0.0956  -0.0237 148 SER A N   
1060 C CA  . SER A 148 ? 0.6845 0.5271 0.6508 -0.0245 0.1046  -0.0231 148 SER A CA  
1061 C C   . SER A 148 ? 0.7311 0.5630 0.6941 -0.0249 0.1177  -0.0295 148 SER A C   
1062 O O   . SER A 148 ? 0.7237 0.5527 0.6969 -0.0215 0.1282  -0.0266 148 SER A O   
1063 C CB  . SER A 148 ? 0.6021 0.4483 0.5570 -0.0278 0.1006  -0.0250 148 SER A CB  
1064 O OG  . SER A 148 ? 0.7668 0.6114 0.7065 -0.0324 0.0968  -0.0318 148 SER A OG  
1065 N N   . ILE A 149 ? 0.7051 0.5310 0.6549 -0.0292 0.1180  -0.0380 149 ILE A N   
1066 C CA  . ILE A 149 ? 0.7751 0.5895 0.7191 -0.0316 0.1310  -0.0463 149 ILE A CA  
1067 C C   . ILE A 149 ? 0.8113 0.6189 0.7724 -0.0262 0.1408  -0.0426 149 ILE A C   
1068 O O   . ILE A 149 ? 0.8809 0.6777 0.8424 -0.0266 0.1552  -0.0477 149 ILE A O   
1069 C CB  . ILE A 149 ? 0.7666 0.5782 0.6938 -0.0382 0.1272  -0.0552 149 ILE A CB  
1070 C CG1 . ILE A 149 ? 0.7277 0.5308 0.6404 -0.0449 0.1388  -0.0657 149 ILE A CG1 
1071 C CG2 . ILE A 149 ? 0.5550 0.3636 0.4889 -0.0363 0.1244  -0.0543 149 ILE A CG2 
1072 C CD1 . ILE A 149 ? 0.6667 0.4703 0.5609 -0.0533 0.1340  -0.0740 149 ILE A CD1 
1073 N N   . ILE A 150 ? 0.7984 0.6124 0.7742 -0.0214 0.1340  -0.0333 150 ILE A N   
1074 C CA  . ILE A 150 ? 0.7833 0.5940 0.7783 -0.0158 0.1424  -0.0267 150 ILE A CA  
1075 C C   . ILE A 150 ? 0.8972 0.7062 0.9057 -0.0112 0.1546  -0.0216 150 ILE A C   
1076 O O   . ILE A 150 ? 0.9550 0.7571 0.9783 -0.0068 0.1670  -0.0183 150 ILE A O   
1077 C CB  . ILE A 150 ? 0.7939 0.6163 0.8013 -0.0128 0.1308  -0.0161 150 ILE A CB  
1078 C CG1 . ILE A 150 ? 0.8081 0.6435 0.8167 -0.0129 0.1202  -0.0099 150 ILE A CG1 
1079 C CG2 . ILE A 150 ? 0.7259 0.5472 0.7230 -0.0164 0.1226  -0.0212 150 ILE A CG2 
1080 C CD1 . ILE A 150 ? 0.7553 0.6037 0.7783 -0.0108 0.1113  0.0017  150 ILE A CD1 
1081 N N   . HIS A 151 ? 0.8574 0.6730 0.8630 -0.0116 0.1519  -0.0197 151 HIS A N   
1082 C CA  . HIS A 151 ? 0.8611 0.6761 0.8793 -0.0074 0.1633  -0.0146 151 HIS A CA  
1083 C C   . HIS A 151 ? 0.9800 0.7840 0.9841 -0.0113 0.1758  -0.0258 151 HIS A C   
1084 O O   . HIS A 151 ? 1.1385 0.9396 1.1523 -0.0079 0.1883  -0.0232 151 HIS A O   
1085 C CB  . HIS A 151 ? 0.8354 0.6650 0.8604 -0.0058 0.1539  -0.0050 151 HIS A CB  
1086 C CG  . HIS A 151 ? 0.8465 0.6890 0.8869 -0.0030 0.1432  0.0071  151 HIS A CG  
1087 N ND1 . HIS A 151 ? 0.8070 0.6587 0.8401 -0.0066 0.1275  0.0079  151 HIS A ND1 
1088 C CD2 . HIS A 151 ? 0.8271 0.6759 0.8899 0.0024  0.1464  0.0194  151 HIS A CD2 
1089 C CE1 . HIS A 151 ? 0.8361 0.6991 0.8844 -0.0046 0.1214  0.0189  151 HIS A CE1 
1090 N NE2 . HIS A 151 ? 0.8330 0.6956 0.8998 0.0008  0.1320  0.0268  151 HIS A NE2 
1091 N N   . MET A 152 ? 0.9177 0.7171 0.8993 -0.0188 0.1728  -0.0375 152 MET A N   
1092 C CA  . MET A 152 ? 0.9700 0.7627 0.9351 -0.0246 0.1823  -0.0479 152 MET A CA  
1093 C C   . MET A 152 ? 1.0159 0.7919 0.9809 -0.0260 0.2011  -0.0568 152 MET A C   
1094 O O   . MET A 152 ? 1.0553 0.8240 1.0269 -0.0245 0.2041  -0.0575 152 MET A O   
1095 C CB  . MET A 152 ? 0.8963 0.6936 0.8381 -0.0330 0.1712  -0.0554 152 MET A CB  
1096 C CG  . MET A 152 ? 0.7973 0.6089 0.7389 -0.0321 0.1551  -0.0477 152 MET A CG  
1097 S SD  . MET A 152 ? 0.9562 0.7737 0.8729 -0.0413 0.1453  -0.0547 152 MET A SD  
1098 C CE  . MET A 152 ? 0.7641 0.5950 0.6889 -0.0374 0.1280  -0.0438 152 MET A CE  
1099 N N   . PRO A 153 ? 1.0115 0.7806 0.9691 -0.0293 0.2149  -0.0637 153 PRO A N   
1100 C CA  . PRO A 153 ? 1.1021 0.8533 1.0625 -0.0301 0.2357  -0.0721 153 PRO A CA  
1101 C C   . PRO A 153 ? 1.0819 0.8221 1.0236 -0.0395 0.2389  -0.0862 153 PRO A C   
1102 O O   . PRO A 153 ? 1.0537 0.7808 1.0059 -0.0371 0.2501  -0.0883 153 PRO A O   
1103 C CB  . PRO A 153 ? 1.0169 0.7652 0.9722 -0.0321 0.2490  -0.0762 153 PRO A CB  
1104 C CG  . PRO A 153 ? 1.0864 0.8512 1.0311 -0.0345 0.2333  -0.0718 153 PRO A CG  
1105 C CD  . PRO A 153 ? 0.9949 0.7724 0.9503 -0.0291 0.2143  -0.0603 153 PRO A CD  
1106 N N   . ASP A 154 ? 1.0540 0.7994 0.9702 -0.0499 0.2300  -0.0951 154 ASP A N   
1107 C CA  . ASP A 154 ? 0.9970 0.7333 0.8952 -0.0601 0.2330  -0.1084 154 ASP A CA  
1108 C C   . ASP A 154 ? 0.9293 0.6794 0.8112 -0.0663 0.2130  -0.1085 154 ASP A C   
1109 O O   . ASP A 154 ? 0.9792 0.7405 0.8458 -0.0721 0.2055  -0.1094 154 ASP A O   
1110 C CB  . ASP A 154 ? 0.8763 0.6014 0.7565 -0.0706 0.2506  -0.1232 154 ASP A CB  
1111 C CG  . ASP A 154 ? 1.0369 0.7528 0.8975 -0.0831 0.2545  -0.1379 154 ASP A CG  
1112 O OD1 . ASP A 154 ? 1.1146 0.8163 0.9860 -0.0806 0.2635  -0.1404 154 ASP A OD1 
1113 O OD2 . ASP A 154 ? 1.1135 0.8375 0.9491 -0.0955 0.2480  -0.1457 154 ASP A OD2 
1114 N N   . ARG A 155 ? 0.9224 0.6714 0.8077 -0.0654 0.2055  -0.1076 155 ARG A N   
1115 C CA  . ARG A 155 ? 0.8233 0.5857 0.6970 -0.0694 0.1868  -0.1058 155 ARG A CA  
1116 C C   . ARG A 155 ? 0.8850 0.6507 0.7325 -0.0832 0.1861  -0.1168 155 ARG A C   
1117 O O   . ARG A 155 ? 0.9365 0.7173 0.7740 -0.0865 0.1724  -0.1131 155 ARG A O   
1118 C CB  . ARG A 155 ? 0.8159 0.5759 0.6978 -0.0664 0.1805  -0.1035 155 ARG A CB  
1119 C CG  . ARG A 155 ? 0.9439 0.7097 0.8478 -0.0547 0.1728  -0.0900 155 ARG A CG  
1120 C CD  . ARG A 155 ? 0.9053 0.6656 0.8197 -0.0516 0.1723  -0.0882 155 ARG A CD  
1121 N NE  . ARG A 155 ? 0.8935 0.6507 0.8325 -0.0413 0.1789  -0.0782 155 ARG A NE  
1122 C CZ  . ARG A 155 ? 0.9307 0.6989 0.8841 -0.0340 0.1679  -0.0658 155 ARG A CZ  
1123 N NH1 . ARG A 155 ? 0.9323 0.7125 0.8774 -0.0359 0.1516  -0.0638 155 ARG A NH1 
1124 N NH2 . ARG A 155 ? 0.9456 0.7137 0.9217 -0.0256 0.1735  -0.0555 155 ARG A NH2 
1125 N N   . ALA A 156 ? 0.9938 0.7461 0.8300 -0.0921 0.2006  -0.1299 156 ALA A N   
1126 C CA  . ALA A 156 ? 0.9554 0.7129 0.7651 -0.1074 0.1996  -0.1404 156 ALA A CA  
1127 C C   . ALA A 156 ? 0.9904 0.7611 0.7891 -0.1111 0.1963  -0.1380 156 ALA A C   
1128 O O   . ALA A 156 ? 0.9613 0.7485 0.7464 -0.1177 0.1832  -0.1355 156 ALA A O   
1129 C CB  . ALA A 156 ? 0.7584 0.4978 0.5578 -0.1173 0.2186  -0.1560 156 ALA A CB  
1130 N N   . GLN A 157 ? 0.9157 0.6804 0.7218 -0.1063 0.2080  -0.1371 157 GLN A N   
1131 C CA  . GLN A 157 ? 0.9304 0.7078 0.7264 -0.1099 0.2055  -0.1345 157 GLN A CA  
1132 C C   . GLN A 157 ? 0.9891 0.7840 0.7941 -0.1020 0.1865  -0.1195 157 GLN A C   
1133 O O   . GLN A 157 ? 0.9417 0.7526 0.7337 -0.1082 0.1765  -0.1165 157 GLN A O   
1134 C CB  . GLN A 157 ? 0.8908 0.6577 0.6940 -0.1061 0.2230  -0.1367 157 GLN A CB  
1135 C CG  . GLN A 157 ? 1.0374 0.8156 0.8235 -0.1143 0.2242  -0.1382 157 GLN A CG  
1136 C CD  . GLN A 157 ? 1.2063 0.9752 1.0001 -0.1101 0.2415  -0.1397 157 GLN A CD  
1137 O OE1 . GLN A 157 ? 1.2395 0.9919 1.0499 -0.1027 0.2554  -0.1413 157 GLN A OE1 
1138 N NE2 . GLN A 157 ? 1.3168 1.0973 1.1001 -0.1144 0.2407  -0.1377 157 GLN A NE2 
1139 N N   . VAL A 158 ? 0.9494 0.7422 0.7771 -0.0888 0.1817  -0.1097 158 VAL A N   
1140 C CA  . VAL A 158 ? 0.9046 0.7120 0.7410 -0.0820 0.1647  -0.0969 158 VAL A CA  
1141 C C   . VAL A 158 ? 0.8567 0.6757 0.6800 -0.0888 0.1508  -0.0967 158 VAL A C   
1142 O O   . VAL A 158 ? 0.8353 0.6689 0.6537 -0.0904 0.1405  -0.0901 158 VAL A O   
1143 C CB  . VAL A 158 ? 0.9769 0.7800 0.8371 -0.0695 0.1617  -0.0882 158 VAL A CB  
1144 C CG1 . VAL A 158 ? 0.8282 0.6445 0.6944 -0.0649 0.1438  -0.0779 158 VAL A CG1 
1145 C CG2 . VAL A 158 ? 0.9871 0.7849 0.8631 -0.0618 0.1727  -0.0838 158 VAL A CG2 
1146 N N   . LEU A 159 ? 0.8272 0.6402 0.6451 -0.0933 0.1512  -0.1036 159 LEU A N   
1147 C CA  . LEU A 159 ? 0.8476 0.6727 0.6543 -0.0998 0.1384  -0.1027 159 LEU A CA  
1148 C C   . LEU A 159 ? 0.9163 0.7530 0.7016 -0.1127 0.1383  -0.1065 159 LEU A C   
1149 O O   . LEU A 159 ? 0.8561 0.7095 0.6364 -0.1154 0.1257  -0.0994 159 LEU A O   
1150 C CB  . LEU A 159 ? 0.8093 0.6258 0.6152 -0.1023 0.1393  -0.1090 159 LEU A CB  
1151 C CG  . LEU A 159 ? 0.7670 0.5770 0.5940 -0.0900 0.1360  -0.1026 159 LEU A CG  
1152 C CD1 . LEU A 159 ? 0.8921 0.6895 0.7205 -0.0917 0.1419  -0.1097 159 LEU A CD1 
1153 C CD2 . LEU A 159 ? 0.6568 0.4798 0.4903 -0.0848 0.1200  -0.0922 159 LEU A CD2 
1154 N N   . ALA A 160 ? 0.8811 0.7101 0.6539 -0.1211 0.1526  -0.1171 160 ALA A N   
1155 C CA  . ALA A 160 ? 0.8762 0.7182 0.6271 -0.1347 0.1525  -0.1205 160 ALA A CA  
1156 C C   . ALA A 160 ? 0.9428 0.8009 0.6975 -0.1305 0.1438  -0.1081 160 ALA A C   
1157 O O   . ALA A 160 ? 0.9707 0.8475 0.7158 -0.1369 0.1331  -0.1020 160 ALA A O   
1158 C CB  . ALA A 160 ? 0.7013 0.5308 0.4385 -0.1443 0.1711  -0.1347 160 ALA A CB  
1159 N N   . GLN A 161 ? 0.8773 0.7289 0.6476 -0.1193 0.1481  -0.1030 161 GLN A N   
1160 C CA  . GLN A 161 ? 0.9107 0.7760 0.6870 -0.1145 0.1402  -0.0908 161 GLN A CA  
1161 C C   . GLN A 161 ? 0.9223 0.8008 0.7060 -0.1102 0.1231  -0.0793 161 GLN A C   
1162 O O   . GLN A 161 ? 0.9598 0.8554 0.7368 -0.1147 0.1150  -0.0719 161 GLN A O   
1163 C CB  . GLN A 161 ? 0.8419 0.6975 0.6364 -0.1027 0.1468  -0.0868 161 GLN A CB  
1164 C CG  . GLN A 161 ? 0.9817 0.8256 0.7704 -0.1063 0.1649  -0.0965 161 GLN A CG  
1165 C CD  . GLN A 161 ? 0.9577 0.8125 0.7258 -0.1184 0.1689  -0.0998 161 GLN A CD  
1166 O OE1 . GLN A 161 ? 0.8581 0.7271 0.6267 -0.1173 0.1618  -0.0900 161 GLN A OE1 
1167 N NE2 . GLN A 161 ? 0.9850 0.8334 0.7344 -0.1307 0.1804  -0.1136 161 GLN A NE2 
1168 N N   . VAL A 162 ? 0.8432 0.7142 0.6411 -0.1016 0.1181  -0.0772 162 VAL A N   
1169 C CA  . VAL A 162 ? 0.8102 0.6917 0.6155 -0.0975 0.1037  -0.0676 162 VAL A CA  
1170 C C   . VAL A 162 ? 0.9015 0.7976 0.6912 -0.1085 0.0972  -0.0674 162 VAL A C   
1171 O O   . VAL A 162 ? 0.9229 0.8347 0.7144 -0.1083 0.0874  -0.0569 162 VAL A O   
1172 C CB  . VAL A 162 ? 0.8093 0.6801 0.6282 -0.0895 0.1011  -0.0682 162 VAL A CB  
1173 C CG1 . VAL A 162 ? 0.6691 0.5496 0.4939 -0.0866 0.0878  -0.0601 162 VAL A CG1 
1174 C CG2 . VAL A 162 ? 0.8318 0.6922 0.6676 -0.0792 0.1059  -0.0658 162 VAL A CG2 
1175 N N   . GLY A 163 ? 0.8670 0.7588 0.6421 -0.1184 0.1030  -0.0785 163 GLY A N   
1176 C CA  . GLY A 163 ? 0.7320 0.6396 0.4916 -0.1305 0.0967  -0.0784 163 GLY A CA  
1177 C C   . GLY A 163 ? 0.7430 0.6689 0.4913 -0.1384 0.0947  -0.0724 163 GLY A C   
1178 O O   . GLY A 163 ? 0.8100 0.7554 0.5552 -0.1428 0.0844  -0.0631 163 GLY A O   
1179 N N   . ARG A 164 ? 0.7040 0.6250 0.4475 -0.1399 0.1046  -0.0764 164 ARG A N   
1180 C CA  . ARG A 164 ? 0.7689 0.7078 0.5004 -0.1483 0.1036  -0.0711 164 ARG A CA  
1181 C C   . ARG A 164 ? 0.9721 0.9244 0.7187 -0.1390 0.0931  -0.0538 164 ARG A C   
1182 O O   . ARG A 164 ? 0.9898 0.9636 0.7302 -0.1455 0.0860  -0.0440 164 ARG A O   
1183 C CB  . ARG A 164 ? 0.8084 0.7370 0.5312 -0.1520 0.1184  -0.0808 164 ARG A CB  
1184 C CG  . ARG A 164 ? 0.8574 0.8038 0.5698 -0.1591 0.1178  -0.0743 164 ARG A CG  
1185 C CD  . ARG A 164 ? 0.9578 0.8929 0.6614 -0.1629 0.1338  -0.0849 164 ARG A CD  
1186 N NE  . ARG A 164 ? 1.0128 0.9314 0.7362 -0.1479 0.1399  -0.0833 164 ARG A NE  
1187 C CZ  . ARG A 164 ? 0.9681 0.8931 0.7058 -0.1383 0.1348  -0.0707 164 ARG A CZ  
1188 N NH1 . ARG A 164 ? 0.9952 0.9414 0.7308 -0.1411 0.1240  -0.0581 164 ARG A NH1 
1189 N NH2 . ARG A 164 ? 0.8845 0.7954 0.6397 -0.1261 0.1405  -0.0697 164 ARG A NH2 
1190 N N   . VAL A 165 ? 0.9242 0.8649 0.6912 -0.1245 0.0924  -0.0493 165 VAL A N   
1191 C CA  . VAL A 165 ? 0.8277 0.7785 0.6093 -0.1163 0.0842  -0.0341 165 VAL A CA  
1192 C C   . VAL A 165 ? 0.9149 0.8728 0.7074 -0.1115 0.0726  -0.0251 165 VAL A C   
1193 O O   . VAL A 165 ? 1.0130 0.9823 0.8160 -0.1071 0.0658  -0.0117 165 VAL A O   
1194 C CB  . VAL A 165 ? 0.7489 0.6861 0.5470 -0.1043 0.0885  -0.0326 165 VAL A CB  
1195 C CG1 . VAL A 165 ? 0.7659 0.6971 0.5559 -0.1078 0.1007  -0.0397 165 VAL A CG1 
1196 C CG2 . VAL A 165 ? 0.6968 0.6176 0.5077 -0.0956 0.0885  -0.0372 165 VAL A CG2 
1197 N N   . LEU A 166 ? 0.9019 0.8528 0.6937 -0.1120 0.0710  -0.0316 166 LEU A N   
1198 C CA  . LEU A 166 ? 0.8061 0.7637 0.6082 -0.1076 0.0610  -0.0234 166 LEU A CA  
1199 C C   . LEU A 166 ? 0.8389 0.8202 0.6332 -0.1165 0.0539  -0.0138 166 LEU A C   
1200 O O   . LEU A 166 ? 0.9581 0.9492 0.7341 -0.1291 0.0562  -0.0182 166 LEU A O   
1201 C CB  . LEU A 166 ? 0.8029 0.7482 0.6049 -0.1069 0.0615  -0.0329 166 LEU A CB  
1202 C CG  . LEU A 166 ? 0.8221 0.7525 0.6418 -0.0944 0.0604  -0.0328 166 LEU A CG  
1203 C CD1 . LEU A 166 ? 0.7618 0.6832 0.5801 -0.0951 0.0603  -0.0409 166 LEU A CD1 
1204 C CD2 . LEU A 166 ? 0.7051 0.6434 0.5401 -0.0868 0.0524  -0.0196 166 LEU A CD2 
1205 N N   . ARG A 167 ? 0.8679 0.8584 0.6754 -0.1107 0.0463  -0.0014 167 ARG A N   
1206 C CA  . ARG A 167 ? 0.8616 0.8766 0.6645 -0.1185 0.0392  0.0100  167 ARG A CA  
1207 C C   . ARG A 167 ? 0.9211 0.9401 0.7202 -0.1231 0.0347  0.0070  167 ARG A C   
1208 O O   . ARG A 167 ? 0.8951 0.8988 0.7022 -0.1161 0.0349  0.0011  167 ARG A O   
1209 C CB  . ARG A 167 ? 0.7967 0.8221 0.6190 -0.1097 0.0335  0.0277  167 ARG A CB  
1210 C CG  . ARG A 167 ? 0.8054 0.8311 0.6315 -0.1066 0.0370  0.0330  167 ARG A CG  
1211 C CD  . ARG A 167 ? 0.8364 0.8716 0.6826 -0.0984 0.0323  0.0509  167 ARG A CD  
1212 N NE  . ARG A 167 ? 0.9039 0.9393 0.7535 -0.0960 0.0359  0.0559  167 ARG A NE  
1213 C CZ  . ARG A 167 ? 0.8895 0.9222 0.7584 -0.0864 0.0355  0.0664  167 ARG A CZ  
1214 N NH1 . ARG A 167 ? 0.9344 0.9625 0.8207 -0.0781 0.0325  0.0723  167 ARG A NH1 
1215 N NH2 . ARG A 167 ? 0.8731 0.9067 0.7436 -0.0855 0.0389  0.0706  167 ARG A NH2 
1216 N N   . PRO A 168 ? 0.9575 0.9984 0.7439 -0.1357 0.0304  0.0116  168 PRO A N   
1217 C CA  . PRO A 168 ? 0.9711 1.0194 0.7556 -0.1403 0.0249  0.0115  168 PRO A CA  
1218 C C   . PRO A 168 ? 0.8896 0.9325 0.6960 -0.1271 0.0202  0.0191  168 PRO A C   
1219 O O   . PRO A 168 ? 0.9077 0.9596 0.7306 -0.1193 0.0164  0.0341  168 PRO A O   
1220 C CB  . PRO A 168 ? 0.9629 1.0427 0.7385 -0.1529 0.0185  0.0240  168 PRO A CB  
1221 C CG  . PRO A 168 ? 0.8488 0.9313 0.6082 -0.1614 0.0244  0.0193  168 PRO A CG  
1222 C CD  . PRO A 168 ? 0.9701 1.0309 0.7420 -0.1476 0.0306  0.0165  168 PRO A CD  
1223 N N   . GLY A 169 ? 0.8046 0.8324 0.6116 -0.1246 0.0213  0.0087  169 GLY A N   
1224 C CA  . GLY A 169 ? 0.6668 0.6867 0.4928 -0.1125 0.0183  0.0132  169 GLY A CA  
1225 C C   . GLY A 169 ? 0.8874 0.8845 0.7247 -0.1004 0.0231  0.0078  169 GLY A C   
1226 O O   . GLY A 169 ? 0.9107 0.9004 0.7629 -0.0910 0.0214  0.0107  169 GLY A O   
1227 N N   . GLY A 170 ? 0.9144 0.9008 0.7452 -0.1008 0.0294  0.0004  170 GLY A N   
1228 C CA  . GLY A 170 ? 0.7644 0.7322 0.6064 -0.0902 0.0334  -0.0032 170 GLY A CA  
1229 C C   . GLY A 170 ? 0.8240 0.7734 0.6634 -0.0887 0.0374  -0.0165 170 GLY A C   
1230 O O   . GLY A 170 ? 0.8960 0.8445 0.7225 -0.0966 0.0395  -0.0251 170 GLY A O   
1231 N N   . ARG A 171 ? 0.7497 0.6850 0.6018 -0.0790 0.0388  -0.0178 171 ARG A N   
1232 C CA  . ARG A 171 ? 0.7949 0.7150 0.6479 -0.0764 0.0415  -0.0276 171 ARG A CA  
1233 C C   . ARG A 171 ? 0.8215 0.7280 0.6780 -0.0720 0.0478  -0.0327 171 ARG A C   
1234 O O   . ARG A 171 ? 0.7143 0.6205 0.5784 -0.0674 0.0483  -0.0275 171 ARG A O   
1235 C CB  . ARG A 171 ? 0.7847 0.7019 0.6501 -0.0696 0.0369  -0.0245 171 ARG A CB  
1236 C CG  . ARG A 171 ? 0.8330 0.7616 0.6974 -0.0727 0.0314  -0.0202 171 ARG A CG  
1237 C CD  . ARG A 171 ? 0.7560 0.6799 0.6333 -0.0654 0.0285  -0.0178 171 ARG A CD  
1238 N NE  . ARG A 171 ? 0.8941 0.8321 0.7772 -0.0654 0.0238  -0.0076 171 ARG A NE  
1239 C CZ  . ARG A 171 ? 1.0148 0.9625 0.8932 -0.0704 0.0204  -0.0066 171 ARG A CZ  
1240 N NH1 . ARG A 171 ? 1.1400 1.0830 1.0069 -0.0763 0.0217  -0.0164 171 ARG A NH1 
1241 N NH2 . ARG A 171 ? 0.9495 0.9115 0.8359 -0.0696 0.0164  0.0048  171 ARG A NH2 
1242 N N   . LEU A 172 ? 0.7460 0.6413 0.5983 -0.0733 0.0528  -0.0421 172 LEU A N   
1243 C CA  . LEU A 172 ? 0.7458 0.6283 0.6034 -0.0689 0.0593  -0.0465 172 LEU A CA  
1244 C C   . LEU A 172 ? 0.8447 0.7194 0.7127 -0.0629 0.0570  -0.0474 172 LEU A C   
1245 O O   . LEU A 172 ? 0.8911 0.7642 0.7558 -0.0651 0.0557  -0.0512 172 LEU A O   
1246 C CB  . LEU A 172 ? 0.6572 0.5332 0.5034 -0.0752 0.0684  -0.0559 172 LEU A CB  
1247 C CG  . LEU A 172 ? 0.7267 0.5886 0.5806 -0.0702 0.0762  -0.0603 172 LEU A CG  
1248 C CD1 . LEU A 172 ? 0.7602 0.6220 0.6255 -0.0634 0.0764  -0.0539 172 LEU A CD1 
1249 C CD2 . LEU A 172 ? 0.6976 0.5516 0.5413 -0.0765 0.0871  -0.0696 172 LEU A CD2 
1250 N N   . VAL A 173 ? 0.6994 0.5701 0.5792 -0.0562 0.0565  -0.0437 173 VAL A N   
1251 C CA  . VAL A 173 ? 0.6924 0.5570 0.5813 -0.0517 0.0546  -0.0444 173 VAL A CA  
1252 C C   . VAL A 173 ? 0.6965 0.5540 0.5922 -0.0484 0.0605  -0.0452 173 VAL A C   
1253 O O   . VAL A 173 ? 0.8809 0.7397 0.7819 -0.0460 0.0614  -0.0413 173 VAL A O   
1254 C CB  . VAL A 173 ? 0.6333 0.5015 0.5308 -0.0478 0.0480  -0.0388 173 VAL A CB  
1255 C CG1 . VAL A 173 ? 0.7278 0.5907 0.6328 -0.0446 0.0466  -0.0401 173 VAL A CG1 
1256 C CG2 . VAL A 173 ? 0.6459 0.5215 0.5396 -0.0500 0.0432  -0.0365 173 VAL A CG2 
1257 N N   . LEU A 174 ? 0.6932 0.5438 0.5902 -0.0481 0.0645  -0.0494 174 LEU A N   
1258 C CA  . LEU A 174 ? 0.7312 0.5762 0.6374 -0.0445 0.0706  -0.0483 174 LEU A CA  
1259 C C   . LEU A 174 ? 0.6611 0.5033 0.5757 -0.0416 0.0691  -0.0474 174 LEU A C   
1260 O O   . LEU A 174 ? 0.7823 0.6243 0.6932 -0.0433 0.0657  -0.0499 174 LEU A O   
1261 C CB  . LEU A 174 ? 0.8204 0.6589 0.7212 -0.0471 0.0813  -0.0536 174 LEU A CB  
1262 C CG  . LEU A 174 ? 0.6904 0.5232 0.5820 -0.0521 0.0855  -0.0613 174 LEU A CG  
1263 C CD1 . LEU A 174 ? 0.6261 0.4506 0.5280 -0.0485 0.0906  -0.0616 174 LEU A CD1 
1264 C CD2 . LEU A 174 ? 0.5903 0.4203 0.4692 -0.0585 0.0938  -0.0678 174 LEU A CD2 
1265 N N   . THR A 175 ? 0.6988 0.5405 0.6254 -0.0376 0.0713  -0.0428 175 THR A N   
1266 C CA  . THR A 175 ? 0.6948 0.5338 0.6299 -0.0354 0.0730  -0.0412 175 THR A CA  
1267 C C   . THR A 175 ? 0.7531 0.5851 0.6937 -0.0337 0.0843  -0.0418 175 THR A C   
1268 O O   . THR A 175 ? 0.8227 0.6522 0.7598 -0.0345 0.0905  -0.0438 175 THR A O   
1269 C CB  . THR A 175 ? 0.6601 0.5060 0.6063 -0.0327 0.0668  -0.0341 175 THR A CB  
1270 O OG1 . THR A 175 ? 0.7217 0.5708 0.6760 -0.0306 0.0690  -0.0289 175 THR A OG1 
1271 C CG2 . THR A 175 ? 0.6796 0.5304 0.6206 -0.0347 0.0575  -0.0348 175 THR A CG2 
1272 N N   . ASP A 176 ? 0.8015 0.6304 0.7514 -0.0313 0.0877  -0.0395 176 ASP A N   
1273 C CA  . ASP A 176 ? 0.7617 0.5818 0.7186 -0.0294 0.1004  -0.0402 176 ASP A CA  
1274 C C   . ASP A 176 ? 0.7113 0.5312 0.6818 -0.0260 0.1017  -0.0344 176 ASP A C   
1275 O O   . ASP A 176 ? 0.7149 0.5388 0.6834 -0.0272 0.0937  -0.0338 176 ASP A O   
1276 C CB  . ASP A 176 ? 0.7908 0.6010 0.7333 -0.0347 0.1076  -0.0511 176 ASP A CB  
1277 C CG  . ASP A 176 ? 0.7784 0.5774 0.7261 -0.0337 0.1232  -0.0538 176 ASP A CG  
1278 O OD1 . ASP A 176 ? 0.7231 0.5220 0.6885 -0.0275 0.1288  -0.0457 176 ASP A OD1 
1279 O OD2 . ASP A 176 ? 0.7254 0.5165 0.6598 -0.0395 0.1305  -0.0637 176 ASP A OD2 
1280 N N   . PHE A 177 ? 0.6904 0.5060 0.6755 -0.0217 0.1123  -0.0294 177 PHE A N   
1281 C CA  . PHE A 177 ? 0.8201 0.6351 0.8203 -0.0181 0.1158  -0.0226 177 PHE A CA  
1282 C C   . PHE A 177 ? 0.8194 0.6203 0.8141 -0.0206 0.1250  -0.0313 177 PHE A C   
1283 O O   . PHE A 177 ? 0.8442 0.6346 0.8272 -0.0244 0.1329  -0.0416 177 PHE A O   
1284 C CB  . PHE A 177 ? 0.8164 0.6341 0.8376 -0.0118 0.1241  -0.0115 177 PHE A CB  
1285 C CG  . PHE A 177 ? 0.8297 0.6641 0.8603 -0.0100 0.1141  -0.0001 177 PHE A CG  
1286 C CD1 . PHE A 177 ? 0.8654 0.7109 0.8922 -0.0126 0.1004  0.0026  177 PHE A CD1 
1287 C CD2 . PHE A 177 ? 0.7632 0.6024 0.8063 -0.0063 0.1189  0.0075  177 PHE A CD2 
1288 C CE1 . PHE A 177 ? 0.7893 0.6502 0.8235 -0.0127 0.0917  0.0120  177 PHE A CE1 
1289 C CE2 . PHE A 177 ? 0.7711 0.6265 0.8225 -0.0059 0.1095  0.0179  177 PHE A CE2 
1290 C CZ  . PHE A 177 ? 0.8119 0.6781 0.8583 -0.0097 0.0959  0.0197  177 PHE A CZ  
1291 N N   . PHE A 178 ? 0.7238 0.5249 0.7263 -0.0193 0.1240  -0.0272 178 PHE A N   
1292 C CA  . PHE A 178 ? 0.7996 0.5867 0.7982 -0.0220 0.1333  -0.0352 178 PHE A CA  
1293 C C   . PHE A 178 ? 0.8913 0.6795 0.9071 -0.0179 0.1352  -0.0259 178 PHE A C   
1294 O O   . PHE A 178 ? 0.8760 0.6781 0.9031 -0.0145 0.1267  -0.0140 178 PHE A O   
1295 C CB  . PHE A 178 ? 0.7421 0.5273 0.7185 -0.0297 0.1262  -0.0471 178 PHE A CB  
1296 C CG  . PHE A 178 ? 0.8139 0.6079 0.7883 -0.0306 0.1137  -0.0441 178 PHE A CG  
1297 C CD1 . PHE A 178 ? 0.7992 0.6076 0.7750 -0.0289 0.1010  -0.0372 178 PHE A CD1 
1298 C CD2 . PHE A 178 ? 0.7008 0.4883 0.6711 -0.0339 0.1154  -0.0490 178 PHE A CD2 
1299 C CE1 . PHE A 178 ? 0.7441 0.5599 0.7172 -0.0303 0.0908  -0.0355 178 PHE A CE1 
1300 C CE2 . PHE A 178 ? 0.6493 0.4449 0.6175 -0.0348 0.1047  -0.0465 178 PHE A CE2 
1301 C CZ  . PHE A 178 ? 0.7119 0.5215 0.6813 -0.0330 0.0926  -0.0399 178 PHE A CZ  
1302 N N   . GLU A 179 ? 0.8720 0.6456 0.8893 -0.0192 0.1469  -0.0314 179 GLU A N   
1303 C CA  . GLU A 179 ? 0.8031 0.5749 0.8377 -0.0154 0.1516  -0.0230 179 GLU A CA  
1304 C C   . GLU A 179 ? 0.8362 0.6091 0.8586 -0.0206 0.1426  -0.0283 179 GLU A C   
1305 O O   . GLU A 179 ? 0.7952 0.5572 0.8019 -0.0271 0.1458  -0.0414 179 GLU A O   
1306 C CB  . GLU A 179 ? 0.9983 0.7514 1.0434 -0.0137 0.1719  -0.0261 179 GLU A CB  
1307 C CG  . GLU A 179 ? 1.1872 0.9411 1.2611 -0.0055 0.1807  -0.0107 179 GLU A CG  
1308 C CD  . GLU A 179 ? 1.2153 0.9516 1.3031 -0.0019 0.2028  -0.0120 179 GLU A CD  
1309 O OE1 . GLU A 179 ? 0.9925 0.7163 1.0661 -0.0063 0.2113  -0.0258 179 GLU A OE1 
1310 O OE2 . GLU A 179 ? 1.3103 1.0459 1.4241 0.0053  0.2121  0.0014  179 GLU A OE2 
1311 N N   . ARG A 180 ? 0.8112 0.5988 0.8401 -0.0185 0.1310  -0.0181 180 ARG A N   
1312 C CA  . ARG A 180 ? 0.8103 0.6001 0.8278 -0.0232 0.1223  -0.0228 180 ARG A CA  
1313 C C   . ARG A 180 ? 0.8743 0.6524 0.9000 -0.0233 0.1323  -0.0231 180 ARG A C   
1314 O O   . ARG A 180 ? 0.9806 0.7522 0.9934 -0.0291 0.1313  -0.0328 180 ARG A O   
1315 C CB  . ARG A 180 ? 0.8641 0.6727 0.8845 -0.0219 0.1077  -0.0130 180 ARG A CB  
1316 C CG  . ARG A 180 ? 0.9893 0.8094 1.0059 -0.0214 0.0993  -0.0105 180 ARG A CG  
1317 C CD  . ARG A 180 ? 0.8711 0.7095 0.8930 -0.0210 0.0873  0.0001  180 ARG A CD  
1318 N NE  . ARG A 180 ? 0.7753 0.6179 0.7809 -0.0258 0.0766  -0.0069 180 ARG A NE  
1319 C CZ  . ARG A 180 ? 0.6832 0.5394 0.6890 -0.0274 0.0668  -0.0013 180 ARG A CZ  
1320 N NH1 . ARG A 180 ? 0.7004 0.5691 0.7209 -0.0253 0.0651  0.0118  180 ARG A NH1 
1321 N NH2 . ARG A 180 ? 0.5942 0.4522 0.5857 -0.0314 0.0590  -0.0085 180 ARG A NH2 
1322 N N   . ALA A 181 ? 0.8612 0.6375 0.9096 -0.0170 0.1422  -0.0117 181 ALA A N   
1323 C CA  . ALA A 181 ? 0.8960 0.6607 0.9578 -0.0155 0.1540  -0.0092 181 ALA A CA  
1324 C C   . ALA A 181 ? 1.0351 0.7966 1.1225 -0.0075 0.1677  0.0029  181 ALA A C   
1325 O O   . ALA A 181 ? 1.1150 0.8893 1.2111 -0.0030 0.1635  0.0128  181 ALA A O   
1326 C CB  . ALA A 181 ? 0.7670 0.5433 0.8337 -0.0153 0.1443  -0.0004 181 ALA A CB  
1327 N N   . PRO A 182 ? 1.0422 0.7861 1.1424 -0.0058 0.1850  0.0020  182 PRO A N   
1328 C CA  . PRO A 182 ? 1.0352 0.7749 1.1620 0.0026  0.2002  0.0139  182 PRO A CA  
1329 C C   . PRO A 182 ? 1.0409 0.8043 1.1892 0.0099  0.1913  0.0364  182 PRO A C   
1330 O O   . PRO A 182 ? 1.0913 0.8698 1.2416 0.0094  0.1791  0.0453  182 PRO A O   
1331 C CB  . PRO A 182 ? 0.8912 0.6109 1.0302 0.0030  0.2176  0.0119  182 PRO A CB  
1332 C CG  . PRO A 182 ? 0.8852 0.5918 0.9958 -0.0079 0.2157  -0.0093 182 PRO A CG  
1333 C CD  . PRO A 182 ? 0.9589 0.6853 1.0504 -0.0119 0.1927  -0.0103 182 PRO A CD  
1334 N N   . LEU A 183 ? 0.9551 0.7236 1.1186 0.0159  0.1968  0.0457  183 LEU A N   
1335 C CA  . LEU A 183 ? 0.8408 0.6346 1.0229 0.0212  0.1871  0.0670  183 LEU A CA  
1336 C C   . LEU A 183 ? 0.9310 0.7273 1.1456 0.0287  0.1979  0.0863  183 LEU A C   
1337 O O   . LEU A 183 ? 0.9437 0.7231 1.1762 0.0341  0.2178  0.0879  183 LEU A O   
1338 C CB  . LEU A 183 ? 1.0323 0.8338 1.2187 0.0242  0.1873  0.0712  183 LEU A CB  
1339 C CG  . LEU A 183 ? 1.0875 0.8998 1.2495 0.0183  0.1707  0.0622  183 LEU A CG  
1340 C CD1 . LEU A 183 ? 1.2235 1.0151 1.3621 0.0134  0.1770  0.0403  183 LEU A CD1 
1341 C CD2 . LEU A 183 ? 0.9751 0.8057 1.1509 0.0223  0.1666  0.0764  183 LEU A CD2 
1342 N N   . ALA A 184 ? 0.9497 0.7675 1.1722 0.0289  0.1851  0.1013  184 ALA A N   
1343 C CA  . ALA A 184 ? 0.9993 0.8307 1.2548 0.0361  0.1899  0.1261  184 ALA A CA  
1344 C C   . ALA A 184 ? 1.0835 0.9197 1.3636 0.0440  0.2002  0.1398  184 ALA A C   
1345 O O   . ALA A 184 ? 1.1137 0.9551 1.3832 0.0424  0.1948  0.1347  184 ALA A O   
1346 C CB  . ALA A 184 ? 1.0926 0.9536 1.3465 0.0327  0.1697  0.1394  184 ALA A CB  
1347 N N   . PRO A 185 ? 1.0469 0.8819 1.3611 0.0526  0.2155  0.1580  185 PRO A N   
1348 C CA  . PRO A 185 ? 1.0262 0.8669 1.3670 0.0609  0.2265  0.1728  185 PRO A CA  
1349 C C   . PRO A 185 ? 1.0420 0.9146 1.3842 0.0597  0.2091  0.1868  185 PRO A C   
1350 O O   . PRO A 185 ? 1.0673 0.9406 1.4111 0.0617  0.2123  0.1857  185 PRO A O   
1351 C CB  . PRO A 185 ? 1.0303 0.8709 1.4097 0.0701  0.2420  0.1947  185 PRO A CB  
1352 C CG  . PRO A 185 ? 1.0112 0.8322 1.3798 0.0663  0.2462  0.1822  185 PRO A CG  
1353 C CD  . PRO A 185 ? 1.0220 0.8520 1.3543 0.0557  0.2236  0.1676  185 PRO A CD  
1354 N N   . GLU A 186 ? 1.0513 0.9508 1.3928 0.0557  0.1911  0.1996  186 GLU A N   
1355 C CA  . GLU A 186 ? 1.0826 1.0138 1.4246 0.0526  0.1743  0.2126  186 GLU A CA  
1356 C C   . GLU A 186 ? 1.0308 0.9561 1.3428 0.0464  0.1660  0.1921  186 GLU A C   
1357 O O   . GLU A 186 ? 1.0102 0.9480 1.3282 0.0474  0.1636  0.1988  186 GLU A O   
1358 C CB  . GLU A 186 ? 1.0967 1.0543 1.4334 0.0460  0.1556  0.2232  186 GLU A CB  
1359 C CG  . GLU A 186 ? 1.1716 1.1354 1.5327 0.0503  0.1612  0.2414  186 GLU A CG  
1360 C CD  . GLU A 186 ? 1.2817 1.2199 1.6273 0.0484  0.1663  0.2239  186 GLU A CD  
1361 O OE1 . GLU A 186 ? 1.2097 1.1195 1.5339 0.0466  0.1730  0.1990  186 GLU A OE1 
1362 O OE2 . GLU A 186 ? 1.3915 1.3403 1.7464 0.0479  0.1630  0.2359  186 GLU A OE2 
1363 N N   . GLY A 187 ? 1.0175 0.9250 1.2979 0.0398  0.1613  0.1680  187 GLY A N   
1364 C CA  . GLY A 187 ? 1.0263 0.9275 1.2777 0.0338  0.1534  0.1485  187 GLY A CA  
1365 C C   . GLY A 187 ? 1.0751 0.9629 1.3316 0.0384  0.1666  0.1435  187 GLY A C   
1366 O O   . GLY A 187 ? 1.0139 0.9146 1.2693 0.0375  0.1602  0.1470  187 GLY A O   
1367 N N   . ARG A 188 ? 1.1461 1.0077 1.4084 0.0429  0.1859  0.1352  188 ARG A N   
1368 C CA  . ARG A 188 ? 1.0919 0.9364 1.3529 0.0456  0.1997  0.1253  188 ARG A CA  
1369 C C   . ARG A 188 ? 0.9828 0.8427 1.2711 0.0528  0.2048  0.1447  188 ARG A C   
1370 O O   . ARG A 188 ? 0.9396 0.7918 1.2241 0.0539  0.2115  0.1377  188 ARG A O   
1371 C CB  . ARG A 188 ? 1.1065 0.9204 1.3698 0.0480  0.2208  0.1134  188 ARG A CB  
1372 C CG  . ARG A 188 ? 1.1880 0.9981 1.4852 0.0564  0.2367  0.1303  188 ARG A CG  
1373 C CD  . ARG A 188 ? 1.2345 1.0218 1.5223 0.0531  0.2448  0.1168  188 ARG A CD  
1374 N NE  . ARG A 188 ? 1.2032 0.9606 1.4732 0.0494  0.2597  0.0931  188 ARG A NE  
1375 C CZ  . ARG A 188 ? 1.1900 0.9280 1.4767 0.0548  0.2832  0.0920  188 ARG A CZ  
1376 N NH1 . ARG A 188 ? 1.2718 1.0175 1.5959 0.0654  0.2945  0.1146  188 ARG A NH1 
1377 N NH2 . ARG A 188 ? 1.0814 0.7935 1.3481 0.0493  0.2958  0.0688  188 ARG A NH2 
1378 N N   . ALA A 189 ? 1.0201 0.9034 1.3357 0.0571  0.2012  0.1697  189 ALA A N   
1379 C CA  . ALA A 189 ? 1.0547 0.9600 1.3933 0.0617  0.2004  0.1897  189 ALA A CA  
1380 C C   . ALA A 189 ? 1.0898 1.0063 1.4056 0.0547  0.1849  0.1810  189 ALA A C   
1381 O O   . ALA A 189 ? 0.9978 0.9101 1.3158 0.0572  0.1916  0.1785  189 ALA A O   
1382 C CB  . ALA A 189 ? 1.0992 1.0343 1.4644 0.0640  0.1928  0.2177  189 ALA A CB  
1383 N N   . ALA A 190 ? 1.1021 1.0326 1.3961 0.0457  0.1646  0.1765  190 ALA A N   
1384 C CA  . ALA A 190 ? 0.9786 0.9206 1.2525 0.0386  0.1497  0.1695  190 ALA A CA  
1385 C C   . ALA A 190 ? 0.9930 0.9102 1.2409 0.0362  0.1542  0.1447  190 ALA A C   
1386 O O   . ALA A 190 ? 0.9793 0.8987 1.2236 0.0357  0.1537  0.1421  190 ALA A O   
1387 C CB  . ALA A 190 ? 0.8312 0.7912 1.0882 0.0293  0.1294  0.1692  190 ALA A CB  
1388 N N   . VAL A 191 ? 0.9339 0.8290 1.1640 0.0342  0.1584  0.1271  191 VAL A N   
1389 C CA  . VAL A 191 ? 0.8916 0.7660 1.0952 0.0304  0.1611  0.1041  191 VAL A CA  
1390 C C   . VAL A 191 ? 0.9431 0.8031 1.1561 0.0359  0.1788  0.1015  191 VAL A C   
1391 O O   . VAL A 191 ? 0.9150 0.7699 1.1118 0.0330  0.1776  0.0901  191 VAL A O   
1392 C CB  . VAL A 191 ? 0.8358 0.6920 1.0214 0.0267  0.1624  0.0885  191 VAL A CB  
1393 C CG1 . VAL A 191 ? 0.7733 0.6089 0.9337 0.0225  0.1669  0.0663  191 VAL A CG1 
1394 C CG2 . VAL A 191 ? 0.8139 0.6850 0.9872 0.0206  0.1439  0.0895  191 VAL A CG2 
1395 N N   . GLN A 192 ? 0.9906 0.8441 1.2303 0.0440  0.1962  0.1123  192 GLN A N   
1396 C CA  . GLN A 192 ? 0.9866 0.8240 1.2338 0.0488  0.2149  0.1078  192 GLN A CA  
1397 C C   . GLN A 192 ? 0.9556 0.8100 1.2108 0.0505  0.2104  0.1176  192 GLN A C   
1398 O O   . GLN A 192 ? 0.9657 0.8105 1.2077 0.0489  0.2149  0.1056  192 GLN A O   
1399 C CB  . GLN A 192 ? 0.9679 0.7939 1.2451 0.0577  0.2365  0.1182  192 GLN A CB  
1400 C CG  . GLN A 192 ? 1.1709 0.9873 1.4639 0.0641  0.2559  0.1201  192 GLN A CG  
1401 C CD  . GLN A 192 ? 1.2654 1.0605 1.5818 0.0717  0.2821  0.1225  192 GLN A CD  
1402 O OE1 . GLN A 192 ? 1.3399 1.1203 1.6541 0.0705  0.2879  0.1163  192 GLN A OE1 
1403 N NE2 . GLN A 192 ? 1.2273 1.0199 1.5669 0.0794  0.2991  0.1314  192 GLN A NE2 
1404 N N   . ARG A 193 ? 0.8706 0.7517 1.1471 0.0530  0.2013  0.1397  193 ARG A N   
1405 C CA  . ARG A 193 ? 0.9538 0.8522 1.2388 0.0539  0.1969  0.1497  193 ARG A CA  
1406 C C   . ARG A 193 ? 1.0511 0.9541 1.3056 0.0447  0.1798  0.1357  193 ARG A C   
1407 O O   . ARG A 193 ? 0.9751 0.8820 1.2280 0.0444  0.1797  0.1352  193 ARG A O   
1408 C CB  . ARG A 193 ? 0.9018 0.8301 1.2169 0.0573  0.1906  0.1775  193 ARG A CB  
1409 C CG  . ARG A 193 ? 1.0747 1.0151 1.4174 0.0641  0.1997  0.1946  193 ARG A CG  
1410 C CD  . ARG A 193 ? 1.2282 1.1444 1.5879 0.0738  0.2262  0.1923  193 ARG A CD  
1411 N NE  . ARG A 193 ? 1.3680 1.2726 1.7456 0.0799  0.2397  0.1980  193 ARG A NE  
1412 C CZ  . ARG A 193 ? 1.3937 1.2669 1.7662 0.0825  0.2586  0.1822  193 ARG A CZ  
1413 N NH1 . ARG A 193 ? 1.3238 1.1754 1.6735 0.0794  0.2663  0.1602  193 ARG A NH1 
1414 N NH2 . ARG A 193 ? 1.4436 1.3073 1.8345 0.0877  0.2707  0.1888  193 ARG A NH2 
1415 N N   . TYR A 194 ? 0.9996 0.9009 1.2303 0.0374  0.1665  0.1242  194 TYR A N   
1416 C CA  . TYR A 194 ? 0.9649 0.8674 1.1671 0.0291  0.1523  0.1101  194 TYR A CA  
1417 C C   . TYR A 194 ? 0.9208 0.8004 1.1036 0.0282  0.1614  0.0905  194 TYR A C   
1418 O O   . TYR A 194 ? 0.8784 0.7604 1.0513 0.0256  0.1576  0.0858  194 TYR A O   
1419 C CB  . TYR A 194 ? 0.9698 0.8759 1.1547 0.0225  0.1379  0.1041  194 TYR A CB  
1420 C CG  . TYR A 194 ? 0.8074 0.7157 0.9653 0.0141  0.1230  0.0912  194 TYR A CG  
1421 C CD1 . TYR A 194 ? 0.7672 0.6930 0.9248 0.0102  0.1122  0.0972  194 TYR A CD1 
1422 C CD2 . TYR A 194 ? 0.8844 0.7783 1.0185 0.0098  0.1197  0.0740  194 TYR A CD2 
1423 C CE1 . TYR A 194 ? 0.7161 0.6424 0.8504 0.0027  0.0999  0.0854  194 TYR A CE1 
1424 C CE2 . TYR A 194 ? 0.8576 0.7534 0.9695 0.0029  0.1071  0.0635  194 TYR A CE2 
1425 C CZ  . TYR A 194 ? 0.7692 0.6804 0.8816 -0.0004 0.0978  0.0690  194 TYR A CZ  
1426 O OH  . TYR A 194 ? 0.6978 0.6086 0.7895 -0.0069 0.0871  0.0584  194 TYR A OH  
1427 N N   . LEU A 195 ? 0.7923 0.6504 0.9687 0.0292  0.1732  0.0789  195 LEU A N   
1428 C CA  . LEU A 195 ? 0.7777 0.6156 0.9362 0.0272  0.1832  0.0611  195 LEU A CA  
1429 C C   . LEU A 195 ? 0.9392 0.7761 1.1120 0.0324  0.1960  0.0665  195 LEU A C   
1430 O O   . LEU A 195 ? 1.0005 0.8339 1.1586 0.0294  0.1957  0.0572  195 LEU A O   
1431 C CB  . LEU A 195 ? 0.8630 0.6789 1.0160 0.0269  0.1961  0.0495  195 LEU A CB  
1432 C CG  . LEU A 195 ? 1.0404 0.8518 1.1702 0.0198  0.1849  0.0373  195 LEU A CG  
1433 C CD1 . LEU A 195 ? 1.0322 0.8223 1.1596 0.0193  0.1992  0.0272  195 LEU A CD1 
1434 C CD2 . LEU A 195 ? 1.0622 0.8737 1.1640 0.0125  0.1740  0.0234  195 LEU A CD2 
1435 N N   . HIS A 196 ? 0.9791 0.8206 1.1824 0.0405  0.2073  0.0830  196 HIS A N   
1436 C CA  . HIS A 196 ? 0.8833 0.7246 1.1044 0.0465  0.2211  0.0902  196 HIS A CA  
1437 C C   . HIS A 196 ? 0.8872 0.7491 1.1082 0.0447  0.2080  0.0980  196 HIS A C   
1438 O O   . HIS A 196 ? 0.7581 0.6149 0.9694 0.0434  0.2119  0.0903  196 HIS A O   
1439 C CB  . HIS A 196 ? 0.9076 0.7524 1.1648 0.0561  0.2349  0.1093  196 HIS A CB  
1440 C CG  . HIS A 196 ? 0.9670 0.8093 1.2451 0.0633  0.2523  0.1168  196 HIS A CG  
1441 N ND1 . HIS A 196 ? 0.9156 0.7812 1.2146 0.0671  0.2474  0.1360  196 HIS A ND1 
1442 C CD2 . HIS A 196 ? 1.0241 0.8437 1.3047 0.0668  0.2750  0.1073  196 HIS A CD2 
1443 C CE1 . HIS A 196 ? 0.9897 0.8471 1.3046 0.0736  0.2663  0.1387  196 HIS A CE1 
1444 N NE2 . HIS A 196 ? 1.0389 0.8679 1.3427 0.0735  0.2838  0.1211  196 HIS A NE2 
1445 N N   . ASP A 197 ? 0.8952 0.7809 1.1265 0.0436  0.1924  0.1134  197 ASP A N   
1446 C CA  . ASP A 197 ? 0.8890 0.7964 1.1262 0.0419  0.1817  0.1243  197 ASP A CA  
1447 C C   . ASP A 197 ? 0.9597 0.8651 1.1679 0.0339  0.1698  0.1091  197 ASP A C   
1448 O O   . ASP A 197 ? 1.0036 0.9235 1.2147 0.0320  0.1626  0.1156  197 ASP A O   
1449 C CB  . ASP A 197 ? 0.8333 0.7674 1.0860 0.0404  0.1676  0.1432  197 ASP A CB  
1450 C CG  . ASP A 197 ? 1.0482 0.9907 1.3360 0.0492  0.1789  0.1642  197 ASP A CG  
1451 O OD1 . ASP A 197 ? 1.1543 1.0800 1.4555 0.0570  0.1989  0.1636  197 ASP A OD1 
1452 O OD2 . ASP A 197 ? 1.0980 1.0643 1.4004 0.0479  0.1683  0.1817  197 ASP A OD2 
1453 N N   . PHE A 198 ? 1.0072 0.8957 1.1889 0.0291  0.1677  0.0901  198 PHE A N   
1454 C CA  . PHE A 198 ? 0.9373 0.8240 1.0936 0.0222  0.1575  0.0771  198 PHE A CA  
1455 C C   . PHE A 198 ? 0.8529 0.7176 0.9898 0.0209  0.1680  0.0591  198 PHE A C   
1456 O O   . PHE A 198 ? 0.7437 0.6053 0.8580 0.0151  0.1600  0.0474  198 PHE A O   
1457 C CB  . PHE A 198 ? 0.8810 0.7756 1.0224 0.0154  0.1395  0.0738  198 PHE A CB  
1458 C CG  . PHE A 198 ? 0.9018 0.8201 1.0570 0.0137  0.1275  0.0896  198 PHE A CG  
1459 C CD1 . PHE A 198 ? 0.9471 0.8782 1.1015 0.0100  0.1193  0.0934  198 PHE A CD1 
1460 C CD2 . PHE A 198 ? 0.9508 0.8797 1.1203 0.0149  0.1247  0.1012  198 PHE A CD2 
1461 C CE1 . PHE A 198 ? 0.8576 0.8116 1.0236 0.0065  0.1084  0.1074  198 PHE A CE1 
1462 C CE2 . PHE A 198 ? 0.9212 0.8745 1.1026 0.0117  0.1133  0.1162  198 PHE A CE2 
1463 C CZ  . PHE A 198 ? 0.8707 0.8365 1.0497 0.0069  0.1051  0.1189  198 PHE A CZ  
1464 N N   . MET A 199 ? 0.8813 0.7316 1.0275 0.0259  0.1864  0.0572  199 MET A N   
1465 C CA  . MET A 199 ? 0.8638 0.6939 0.9923 0.0235  0.1987  0.0402  199 MET A CA  
1466 C C   . MET A 199 ? 0.9094 0.7316 1.0100 0.0158  0.1894  0.0246  199 MET A C   
1467 O O   . MET A 199 ? 1.0268 0.8480 1.1066 0.0102  0.1831  0.0148  199 MET A O   
1468 C CB  . MET A 199 ? 0.8052 0.6374 0.9294 0.0230  0.2018  0.0386  199 MET A CB  
1469 C CG  . MET A 199 ? 0.8511 0.6937 1.0039 0.0305  0.2098  0.0554  199 MET A CG  
1470 S SD  . MET A 199 ? 0.9092 0.7523 1.0578 0.0302  0.2163  0.0530  199 MET A SD  
1471 C CE  . MET A 199 ? 0.9597 0.8233 1.1445 0.0382  0.2177  0.0774  199 MET A CE  
1472 N N   . MET A 200 ? 0.8163 0.6341 0.9186 0.0159  0.1886  0.0240  200 MET A N   
1473 C CA  . MET A 200 ? 0.8553 0.6675 0.9347 0.0091  0.1793  0.0115  200 MET A CA  
1474 C C   . MET A 200 ? 0.8890 0.6844 0.9678 0.0089  0.1915  0.0040  200 MET A C   
1475 O O   . MET A 200 ? 0.8075 0.5987 0.9078 0.0150  0.2036  0.0122  200 MET A O   
1476 C CB  . MET A 200 ? 0.8908 0.7184 0.9705 0.0076  0.1610  0.0186  200 MET A CB  
1477 C CG  . MET A 200 ? 0.9834 0.8281 1.0660 0.0069  0.1487  0.0269  200 MET A CG  
1478 S SD  . MET A 200 ? 0.9229 0.7818 1.0030 0.0034  0.1301  0.0320  200 MET A SD  
1479 C CE  . MET A 200 ? 0.8059 0.6746 0.9154 0.0096  0.1349  0.0500  200 MET A CE  
1480 N N   . THR A 201 ? 0.8472 0.6338 0.9021 0.0017  0.1879  -0.0108 201 THR A N   
1481 C CA  . THR A 201 ? 0.8958 0.6677 0.9476 -0.0004 0.1965  -0.0187 201 THR A CA  
1482 C C   . THR A 201 ? 0.9652 0.7415 1.0022 -0.0056 0.1812  -0.0231 201 THR A C   
1483 O O   . THR A 201 ? 0.9148 0.7058 0.9483 -0.0062 0.1650  -0.0181 201 THR A O   
1484 C CB  . THR A 201 ? 0.8617 0.6153 0.8984 -0.0057 0.2120  -0.0346 201 THR A CB  
1485 O OG1 . THR A 201 ? 0.8166 0.5717 0.8258 -0.0148 0.2015  -0.0466 201 THR A OG1 
1486 C CG2 . THR A 201 ? 0.8908 0.6413 0.9358 -0.0023 0.2254  -0.0327 201 THR A CG2 
1487 N N   . MET A 202 ? 1.0438 0.8069 1.0721 -0.0097 0.1874  -0.0331 202 MET A N   
1488 C CA  . MET A 202 ? 0.9414 0.7072 0.9643 -0.0123 0.1769  -0.0340 202 MET A CA  
1489 C C   . MET A 202 ? 0.9219 0.6718 0.9279 -0.0199 0.1849  -0.0496 202 MET A C   
1490 O O   . MET A 202 ? 0.9724 0.7071 0.9792 -0.0210 0.2021  -0.0566 202 MET A O   
1491 C CB  . MET A 202 ? 0.8547 0.6252 0.9025 -0.0050 0.1784  -0.0195 202 MET A CB  
1492 C CG  . MET A 202 ? 0.9535 0.7304 1.0007 -0.0062 0.1671  -0.0163 202 MET A CG  
1493 S SD  . MET A 202 ? 1.0046 0.7884 1.0854 0.0030  0.1726  0.0037  202 MET A SD  
1494 C CE  . MET A 202 ? 1.0420 0.8011 1.1285 0.0033  0.1943  -0.0043 202 MET A CE  
1495 N N   . VAL A 203 ? 0.9365 0.6899 0.9266 -0.0257 0.1730  -0.0553 203 VAL A N   
1496 C CA  . VAL A 203 ? 0.8680 0.6090 0.8402 -0.0346 0.1787  -0.0700 203 VAL A CA  
1497 C C   . VAL A 203 ? 0.8723 0.6135 0.8453 -0.0359 0.1726  -0.0694 203 VAL A C   
1498 O O   . VAL A 203 ? 0.9509 0.6993 0.9404 -0.0293 0.1674  -0.0575 203 VAL A O   
1499 C CB  . VAL A 203 ? 0.8681 0.6138 0.8158 -0.0430 0.1714  -0.0798 203 VAL A CB  
1500 C CG1 . VAL A 203 ? 0.8687 0.6134 0.8162 -0.0419 0.1790  -0.0804 203 VAL A CG1 
1501 C CG2 . VAL A 203 ? 0.7684 0.5309 0.7104 -0.0427 0.1517  -0.0744 203 VAL A CG2 
1502 N N   . SER A 204 ? 0.9258 0.6591 0.8814 -0.0449 0.1743  -0.0819 204 SER A N   
1503 C CA  . SER A 204 ? 1.0238 0.7568 0.9775 -0.0476 0.1688  -0.0830 204 SER A CA  
1504 C C   . SER A 204 ? 0.9862 0.7289 0.9182 -0.0554 0.1548  -0.0895 204 SER A C   
1505 O O   . SER A 204 ? 1.0881 0.8314 1.0036 -0.0620 0.1551  -0.0976 204 SER A O   
1506 C CB  . SER A 204 ? 1.0130 0.7268 0.9677 -0.0520 0.1854  -0.0918 204 SER A CB  
1507 O OG  . SER A 204 ? 1.0536 0.7587 0.9875 -0.0628 0.1926  -0.1070 204 SER A OG  
1508 N N   . ALA A 205 ? 0.8505 0.6016 0.7832 -0.0548 0.1430  -0.0852 205 ALA A N   
1509 C CA  . ALA A 205 ? 0.7790 0.5401 0.6943 -0.0611 0.1300  -0.0895 205 ALA A CA  
1510 C C   . ALA A 205 ? 0.9572 0.7117 0.8531 -0.0726 0.1355  -0.1028 205 ALA A C   
1511 O O   . ALA A 205 ? 1.0416 0.8054 0.9226 -0.0781 0.1281  -0.1060 205 ALA A O   
1512 C CB  . ALA A 205 ? 0.8860 0.6534 0.8056 -0.0595 0.1205  -0.0846 205 ALA A CB  
1513 N N   . GLU A 206 ? 0.9577 0.6969 0.8539 -0.0771 0.1490  -0.1104 206 GLU A N   
1514 C CA  . GLU A 206 ? 0.8902 0.6235 0.7663 -0.0902 0.1548  -0.1241 206 GLU A CA  
1515 C C   . GLU A 206 ? 0.9747 0.7041 0.8421 -0.0939 0.1638  -0.1303 206 GLU A C   
1516 O O   . GLU A 206 ? 1.0485 0.7782 0.8961 -0.1060 0.1657  -0.1408 206 GLU A O   
1517 C CB  . GLU A 206 ? 0.7711 0.4880 0.6492 -0.0953 0.1672  -0.1316 206 GLU A CB  
1518 C CG  . GLU A 206 ? 0.8562 0.5556 0.7523 -0.0889 0.1850  -0.1305 206 GLU A CG  
1519 C CD  . GLU A 206 ? 1.0493 0.7518 0.9699 -0.0757 0.1818  -0.1157 206 GLU A CD  
1520 O OE1 . GLU A 206 ? 0.9975 0.7164 0.9218 -0.0696 0.1665  -0.1055 206 GLU A OE1 
1521 O OE2 . GLU A 206 ? 1.1816 0.8702 1.1182 -0.0720 0.1952  -0.1139 206 GLU A OE2 
1522 N N   . ALA A 207 ? 1.0513 0.7786 0.9325 -0.0845 0.1688  -0.1236 207 ALA A N   
1523 C CA  . ALA A 207 ? 1.0831 0.8071 0.9567 -0.0875 0.1778  -0.1289 207 ALA A CA  
1524 C C   . ALA A 207 ? 1.0836 0.8236 0.9389 -0.0937 0.1655  -0.1300 207 ALA A C   
1525 O O   . ALA A 207 ? 0.9791 0.7176 0.8179 -0.1035 0.1717  -0.1394 207 ALA A O   
1526 C CB  . ALA A 207 ? 0.9519 0.6739 0.8460 -0.0752 0.1834  -0.1190 207 ALA A CB  
1527 N N   . TYR A 208 ? 1.0358 0.7917 0.8941 -0.0887 0.1484  -0.1203 208 TYR A N   
1528 C CA  . TYR A 208 ? 0.9815 0.7528 0.8288 -0.0912 0.1377  -0.1177 208 TYR A CA  
1529 C C   . TYR A 208 ? 0.9901 0.7696 0.8160 -0.1043 0.1329  -0.1250 208 TYR A C   
1530 O O   . TYR A 208 ? 1.0929 0.8807 0.9071 -0.1096 0.1314  -0.1261 208 TYR A O   
1531 C CB  . TYR A 208 ? 0.8138 0.5981 0.6719 -0.0820 0.1228  -0.1055 208 TYR A CB  
1532 C CG  . TYR A 208 ? 0.7523 0.5386 0.6228 -0.0729 0.1233  -0.0976 208 TYR A CG  
1533 C CD1 . TYR A 208 ? 0.7684 0.5613 0.6318 -0.0746 0.1222  -0.0970 208 TYR A CD1 
1534 C CD2 . TYR A 208 ? 0.8020 0.5848 0.6918 -0.0632 0.1248  -0.0900 208 TYR A CD2 
1535 C CE1 . TYR A 208 ? 0.8031 0.5980 0.6780 -0.0668 0.1229  -0.0898 208 TYR A CE1 
1536 C CE2 . TYR A 208 ? 0.8413 0.6274 0.7428 -0.0559 0.1251  -0.0822 208 TYR A CE2 
1537 C CZ  . TYR A 208 ? 0.8880 0.6796 0.7817 -0.0578 0.1242  -0.0826 208 TYR A CZ  
1538 O OH  . TYR A 208 ? 0.9099 0.7051 0.8151 -0.0511 0.1243  -0.0750 208 TYR A OH  
1539 N N   . PRO A 209 ? 0.9422 0.7222 0.7627 -0.1101 0.1292  -0.1284 209 PRO A N   
1540 C CA  . PRO A 209 ? 0.9616 0.7536 0.7626 -0.1230 0.1230  -0.1331 209 PRO A CA  
1541 C C   . PRO A 209 ? 1.0803 0.8671 0.8638 -0.1357 0.1346  -0.1448 209 PRO A C   
1542 O O   . PRO A 209 ? 1.0975 0.8987 0.8664 -0.1439 0.1290  -0.1448 209 PRO A O   
1543 C CB  . PRO A 209 ? 0.9323 0.7230 0.7334 -0.1265 0.1195  -0.1352 209 PRO A CB  
1544 C CG  . PRO A 209 ? 0.8207 0.6070 0.6420 -0.1129 0.1167  -0.1268 209 PRO A CG  
1545 C CD  . PRO A 209 ? 0.8598 0.6349 0.6929 -0.1045 0.1270  -0.1252 209 PRO A CD  
1546 N N   . PRO A 210 ? 1.0855 0.8525 0.8698 -0.1382 0.1514  -0.1547 210 PRO A N   
1547 C CA  . PRO A 210 ? 1.0669 0.8285 0.8343 -0.1499 0.1639  -0.1661 210 PRO A CA  
1548 C C   . PRO A 210 ? 1.0415 0.8085 0.8107 -0.1444 0.1647  -0.1610 210 PRO A C   
1549 O O   . PRO A 210 ? 0.8664 0.6451 0.6185 -0.1542 0.1624  -0.1635 210 PRO A O   
1550 C CB  . PRO A 210 ? 0.9425 0.6793 0.7152 -0.1513 0.1833  -0.1767 210 PRO A CB  
1551 C CG  . PRO A 210 ? 0.9811 0.7114 0.7774 -0.1371 0.1807  -0.1675 210 PRO A CG  
1552 C CD  . PRO A 210 ? 0.9664 0.7160 0.7633 -0.1342 0.1604  -0.1576 210 PRO A CD  
1553 N N   . LEU A 211 ? 1.0161 0.7765 0.8056 -0.1296 0.1675  -0.1530 211 LEU A N   
1554 C CA  . LEU A 211 ? 0.9595 0.7267 0.7524 -0.1237 0.1664  -0.1466 211 LEU A CA  
1555 C C   . LEU A 211 ? 0.9166 0.7060 0.6991 -0.1272 0.1505  -0.1398 211 LEU A C   
1556 O O   . LEU A 211 ? 0.9487 0.7455 0.7191 -0.1333 0.1521  -0.1414 211 LEU A O   
1557 C CB  . LEU A 211 ? 0.9143 0.6780 0.7319 -0.1072 0.1651  -0.1353 211 LEU A CB  
1558 C CG  . LEU A 211 ? 0.9123 0.6562 0.7435 -0.1021 0.1829  -0.1389 211 LEU A CG  
1559 C CD1 . LEU A 211 ? 0.9115 0.6559 0.7678 -0.0868 0.1785  -0.1257 211 LEU A CD1 
1560 C CD2 . LEU A 211 ? 0.8018 0.5398 0.6263 -0.1057 0.1966  -0.1450 211 LEU A CD2 
1561 N N   . LEU A 212 ? 0.9785 0.7789 0.7667 -0.1229 0.1357  -0.1315 212 LEU A N   
1562 C CA  . LEU A 212 ? 0.9996 0.8207 0.7805 -0.1257 0.1216  -0.1239 212 LEU A CA  
1563 C C   . LEU A 212 ? 1.0395 0.8699 0.7973 -0.1424 0.1225  -0.1314 212 LEU A C   
1564 O O   . LEU A 212 ? 1.0104 0.8560 0.7600 -0.1463 0.1172  -0.1266 212 LEU A O   
1565 C CB  . LEU A 212 ? 0.9193 0.7488 0.7096 -0.1198 0.1079  -0.1155 212 LEU A CB  
1566 C CG  . LEU A 212 ? 0.9631 0.7957 0.7719 -0.1056 0.0997  -0.1038 212 LEU A CG  
1567 C CD1 . LEU A 212 ? 1.0167 0.8357 0.8398 -0.0960 0.1085  -0.1031 212 LEU A CD1 
1568 C CD2 . LEU A 212 ? 0.8579 0.6940 0.6735 -0.1022 0.0903  -0.0997 212 LEU A CD2 
1569 N N   . ARG A 213 ? 1.0539 0.8774 0.8015 -0.1527 0.1281  -0.1418 213 ARG A N   
1570 C CA  . ARG A 213 ? 1.0929 0.9273 0.8175 -0.1706 0.1279  -0.1489 213 ARG A CA  
1571 C C   . ARG A 213 ? 1.1753 1.0076 0.8861 -0.1789 0.1389  -0.1564 213 ARG A C   
1572 O O   . ARG A 213 ? 1.1982 1.0479 0.8934 -0.1895 0.1343  -0.1551 213 ARG A O   
1573 C CB  . ARG A 213 ? 1.0725 0.8948 0.7903 -0.1797 0.1350  -0.1606 213 ARG A CB  
1574 C CG  . ARG A 213 ? 1.2067 1.0463 0.9094 -0.1938 0.1253  -0.1614 213 ARG A CG  
1575 C CD  . ARG A 213 ? 1.2209 1.0470 0.9101 -0.2084 0.1369  -0.1774 213 ARG A CD  
1576 N NE  . ARG A 213 ? 1.2681 1.0700 0.9728 -0.1990 0.1469  -0.1820 213 ARG A NE  
1577 C CZ  . ARG A 213 ? 1.1919 0.9924 0.9102 -0.1911 0.1398  -0.1762 213 ARG A CZ  
1578 N NH1 . ARG A 213 ? 1.1157 0.9364 0.8343 -0.1911 0.1234  -0.1665 213 ARG A NH1 
1579 N NH2 . ARG A 213 ? 1.1348 0.9143 0.8674 -0.1831 0.1495  -0.1795 213 ARG A NH2 
1580 N N   . GLY A 214 ? 1.0677 0.8790 0.7850 -0.1741 0.1542  -0.1636 214 GLY A N   
1581 C CA  . GLY A 214 ? 0.9847 0.7917 0.6905 -0.1808 0.1667  -0.1711 214 GLY A CA  
1582 C C   . GLY A 214 ? 1.1931 1.0189 0.8972 -0.1783 0.1574  -0.1604 214 GLY A C   
1583 O O   . GLY A 214 ? 1.4171 1.2493 1.1036 -0.1901 0.1627  -0.1660 214 GLY A O   
1584 N N   . ALA A 215 ? 1.0950 0.9306 0.8158 -0.1649 0.1439  -0.1457 215 ALA A N   
1585 C CA  . ALA A 215 ? 1.0344 0.8855 0.7568 -0.1609 0.1365  -0.1348 215 ALA A CA  
1586 C C   . ALA A 215 ? 0.9688 0.8440 0.6852 -0.1659 0.1208  -0.1250 215 ALA A C   
1587 O O   . ALA A 215 ? 0.9529 0.8416 0.6750 -0.1604 0.1126  -0.1133 215 ALA A O   
1588 C CB  . ALA A 215 ? 1.0166 0.8616 0.7627 -0.1430 0.1334  -0.1249 215 ALA A CB  
1589 N N   . GLY A 216 ? 0.9323 0.8133 0.6384 -0.1761 0.1168  -0.1291 216 GLY A N   
1590 C CA  . GLY A 216 ? 0.8774 0.7833 0.5794 -0.1809 0.1017  -0.1182 216 GLY A CA  
1591 C C   . GLY A 216 ? 0.9809 0.8913 0.7036 -0.1663 0.0894  -0.1048 216 GLY A C   
1592 O O   . GLY A 216 ? 1.0187 0.9493 0.7445 -0.1653 0.0779  -0.0919 216 GLY A O   
1593 N N   . LEU A 217 ? 1.0327 0.9253 0.7702 -0.1552 0.0921  -0.1073 217 LEU A N   
1594 C CA  . LEU A 217 ? 0.9683 0.8632 0.7249 -0.1417 0.0819  -0.0963 217 LEU A CA  
1595 C C   . LEU A 217 ? 0.9408 0.8305 0.7000 -0.1423 0.0793  -0.0998 217 LEU A C   
1596 O O   . LEU A 217 ? 1.0630 0.9363 0.8195 -0.1450 0.0887  -0.1108 217 LEU A O   
1597 C CB  . LEU A 217 ? 0.9520 0.8330 0.7255 -0.1272 0.0860  -0.0936 217 LEU A CB  
1598 C CG  . LEU A 217 ? 0.9730 0.8614 0.7472 -0.1248 0.0861  -0.0871 217 LEU A CG  
1599 C CD1 . LEU A 217 ? 1.0274 0.9017 0.8166 -0.1127 0.0919  -0.0861 217 LEU A CD1 
1600 C CD2 . LEU A 217 ? 0.8292 0.7376 0.6080 -0.1226 0.0732  -0.0733 217 LEU A CD2 
1601 N N   . TRP A 218 ? 0.8135 0.7169 0.5794 -0.1393 0.0674  -0.0899 218 TRP A N   
1602 C CA  . TRP A 218 ? 0.8403 0.7415 0.6107 -0.1386 0.0633  -0.0909 218 TRP A CA  
1603 C C   . TRP A 218 ? 0.8687 0.7589 0.6583 -0.1235 0.0615  -0.0866 218 TRP A C   
1604 O O   . TRP A 218 ? 0.9193 0.8151 0.7202 -0.1143 0.0557  -0.0769 218 TRP A O   
1605 C CB  . TRP A 218 ? 0.7764 0.6998 0.5443 -0.1439 0.0519  -0.0818 218 TRP A CB  
1606 C CG  . TRP A 218 ? 0.9300 0.8681 0.6785 -0.1607 0.0518  -0.0849 218 TRP A CG  
1607 C CD1 . TRP A 218 ? 0.9185 0.8524 0.6507 -0.1714 0.0609  -0.0948 218 TRP A CD1 
1608 C CD2 . TRP A 218 ? 1.0135 0.9742 0.7565 -0.1699 0.0425  -0.0778 218 TRP A CD2 
1609 N NE1 . TRP A 218 ? 0.9309 0.8840 0.6463 -0.1877 0.0574  -0.0949 218 TRP A NE1 
1610 C CE2 . TRP A 218 ? 0.9993 0.9701 0.7215 -0.1870 0.0456  -0.0837 218 TRP A CE2 
1611 C CE3 . TRP A 218 ? 1.0261 1.0002 0.7804 -0.1655 0.0323  -0.0666 218 TRP A CE3 
1612 C CZ2 . TRP A 218 ? 1.0143 1.0100 0.7263 -0.2006 0.0377  -0.0780 218 TRP A CZ2 
1613 C CZ3 . TRP A 218 ? 1.1404 1.1386 0.8864 -0.1776 0.0250  -0.0602 218 TRP A CZ3 
1614 C CH2 . TRP A 218 ? 1.1163 1.1261 0.8412 -0.1954 0.0272  -0.0656 218 TRP A CH2 
1615 N N   . LEU A 219 ? 0.8166 0.6921 0.6099 -0.1217 0.0663  -0.0935 219 LEU A N   
1616 C CA  . LEU A 219 ? 0.7940 0.6614 0.6043 -0.1090 0.0640  -0.0892 219 LEU A CA  
1617 C C   . LEU A 219 ? 0.8141 0.6941 0.6313 -0.1053 0.0528  -0.0803 219 LEU A C   
1618 O O   . LEU A 219 ? 0.8442 0.7317 0.6560 -0.1118 0.0489  -0.0808 219 LEU A O   
1619 C CB  . LEU A 219 ? 0.8208 0.6721 0.6338 -0.1088 0.0715  -0.0971 219 LEU A CB  
1620 C CG  . LEU A 219 ? 0.7763 0.6223 0.6054 -0.0977 0.0680  -0.0921 219 LEU A CG  
1621 C CD1 . LEU A 219 ? 0.6038 0.4470 0.4445 -0.0876 0.0684  -0.0864 219 LEU A CD1 
1622 C CD2 . LEU A 219 ? 0.7304 0.5621 0.5624 -0.0984 0.0755  -0.0987 219 LEU A CD2 
1623 N N   . GLU A 220 ? 0.8111 0.6927 0.6408 -0.0950 0.0484  -0.0722 220 GLU A N   
1624 C CA  . GLU A 220 ? 0.7645 0.6559 0.6024 -0.0906 0.0397  -0.0641 220 GLU A CA  
1625 C C   . GLU A 220 ? 0.7989 0.6814 0.6486 -0.0823 0.0388  -0.0638 220 GLU A C   
1626 O O   . GLU A 220 ? 0.8349 0.7225 0.6882 -0.0813 0.0338  -0.0609 220 GLU A O   
1627 C CB  . GLU A 220 ? 0.8701 0.7717 0.7134 -0.0865 0.0354  -0.0546 220 GLU A CB  
1628 C CG  . GLU A 220 ? 0.9726 0.8818 0.8271 -0.0806 0.0286  -0.0461 220 GLU A CG  
1629 C CD  . GLU A 220 ? 1.1069 1.0276 0.9663 -0.0783 0.0253  -0.0361 220 GLU A CD  
1630 O OE1 . GLU A 220 ? 1.1644 1.0898 1.0169 -0.0826 0.0271  -0.0354 220 GLU A OE1 
1631 O OE2 . GLU A 220 ? 1.1623 1.0873 1.0330 -0.0725 0.0216  -0.0288 220 GLU A OE2 
1632 N N   . GLU A 221 ? 0.7527 0.6233 0.6084 -0.0768 0.0437  -0.0661 221 GLU A N   
1633 C CA  . GLU A 221 ? 0.7204 0.5848 0.5868 -0.0698 0.0425  -0.0649 221 GLU A CA  
1634 C C   . GLU A 221 ? 0.6985 0.5506 0.5684 -0.0675 0.0499  -0.0688 221 GLU A C   
1635 O O   . GLU A 221 ? 0.8359 0.6850 0.7062 -0.0664 0.0542  -0.0688 221 GLU A O   
1636 C CB  . GLU A 221 ? 0.6564 0.5252 0.5323 -0.0629 0.0375  -0.0579 221 GLU A CB  
1637 C CG  . GLU A 221 ? 0.6505 0.5137 0.5359 -0.0572 0.0367  -0.0571 221 GLU A CG  
1638 C CD  . GLU A 221 ? 0.8090 0.6758 0.7023 -0.0522 0.0326  -0.0518 221 GLU A CD  
1639 O OE1 . GLU A 221 ? 0.8463 0.7177 0.7399 -0.0517 0.0315  -0.0482 221 GLU A OE1 
1640 O OE2 . GLU A 221 ? 0.8080 0.6729 0.7070 -0.0494 0.0310  -0.0515 221 GLU A OE2 
1641 N N   . PHE A 222 ? 0.7037 0.5496 0.5774 -0.0666 0.0516  -0.0710 222 PHE A N   
1642 C CA  . PHE A 222 ? 0.6988 0.5350 0.5808 -0.0626 0.0579  -0.0715 222 PHE A CA  
1643 C C   . PHE A 222 ? 0.7156 0.5533 0.6076 -0.0572 0.0532  -0.0668 222 PHE A C   
1644 O O   . PHE A 222 ? 0.7444 0.5849 0.6352 -0.0586 0.0493  -0.0671 222 PHE A O   
1645 C CB  . PHE A 222 ? 0.6587 0.4849 0.5368 -0.0673 0.0666  -0.0783 222 PHE A CB  
1646 C CG  . PHE A 222 ? 0.6586 0.4751 0.5480 -0.0623 0.0745  -0.0770 222 PHE A CG  
1647 C CD1 . PHE A 222 ? 0.7168 0.5327 0.6177 -0.0573 0.0727  -0.0721 222 PHE A CD1 
1648 C CD2 . PHE A 222 ? 0.6783 0.4877 0.5678 -0.0625 0.0837  -0.0795 222 PHE A CD2 
1649 C CE1 . PHE A 222 ? 0.7884 0.5981 0.7019 -0.0525 0.0798  -0.0684 222 PHE A CE1 
1650 C CE2 . PHE A 222 ? 0.7674 0.5691 0.6696 -0.0574 0.0916  -0.0767 222 PHE A CE2 
1651 C CZ  . PHE A 222 ? 0.8123 0.6146 0.7272 -0.0522 0.0894  -0.0704 222 PHE A CZ  
1652 N N   . LEU A 223 ? 0.6868 0.5237 0.5883 -0.0519 0.0537  -0.0623 223 LEU A N   
1653 C CA  . LEU A 223 ? 0.6988 0.5399 0.6083 -0.0482 0.0484  -0.0574 223 LEU A CA  
1654 C C   . LEU A 223 ? 0.7738 0.6120 0.6942 -0.0445 0.0525  -0.0532 223 LEU A C   
1655 O O   . LEU A 223 ? 0.8017 0.6394 0.7260 -0.0425 0.0554  -0.0510 223 LEU A O   
1656 C CB  . LEU A 223 ? 0.6692 0.5170 0.5786 -0.0467 0.0424  -0.0546 223 LEU A CB  
1657 C CG  . LEU A 223 ? 0.7798 0.6323 0.6936 -0.0451 0.0368  -0.0519 223 LEU A CG  
1658 C CD1 . LEU A 223 ? 0.7309 0.5842 0.6425 -0.0468 0.0349  -0.0536 223 LEU A CD1 
1659 C CD2 . LEU A 223 ? 0.6920 0.5487 0.6050 -0.0445 0.0329  -0.0506 223 LEU A CD2 
1660 N N   . ASP A 224 ? 0.8521 0.6897 0.7784 -0.0437 0.0530  -0.0511 224 ASP A N   
1661 C CA  . ASP A 224 ? 0.7173 0.5558 0.6564 -0.0400 0.0557  -0.0443 224 ASP A CA  
1662 C C   . ASP A 224 ? 0.6938 0.5421 0.6364 -0.0391 0.0481  -0.0392 224 ASP A C   
1663 O O   . ASP A 224 ? 0.8365 0.6897 0.7776 -0.0404 0.0428  -0.0387 224 ASP A O   
1664 C CB  . ASP A 224 ? 0.6221 0.4571 0.5672 -0.0397 0.0594  -0.0427 224 ASP A CB  
1665 C CG  . ASP A 224 ? 0.7909 0.6294 0.7517 -0.0357 0.0622  -0.0331 224 ASP A CG  
1666 O OD1 . ASP A 224 ? 0.8899 0.7346 0.8560 -0.0338 0.0603  -0.0280 224 ASP A OD1 
1667 O OD2 . ASP A 224 ? 0.8891 0.7251 0.8581 -0.0346 0.0664  -0.0296 224 ASP A OD2 
1668 N N   . ILE A 225 ? 0.6096 0.4610 0.5565 -0.0375 0.0480  -0.0357 225 ILE A N   
1669 C CA  . ILE A 225 ? 0.6153 0.4756 0.5648 -0.0381 0.0416  -0.0317 225 ILE A CA  
1670 C C   . ILE A 225 ? 0.7010 0.5683 0.6633 -0.0367 0.0423  -0.0226 225 ILE A C   
1671 O O   . ILE A 225 ? 0.7038 0.5796 0.6690 -0.0382 0.0378  -0.0185 225 ILE A O   
1672 C CB  . ILE A 225 ? 0.6256 0.4864 0.5705 -0.0387 0.0396  -0.0339 225 ILE A CB  
1673 C CG1 . ILE A 225 ? 0.6897 0.5474 0.6388 -0.0365 0.0453  -0.0321 225 ILE A CG1 
1674 C CG2 . ILE A 225 ? 0.5283 0.3858 0.4628 -0.0403 0.0378  -0.0402 225 ILE A CG2 
1675 C CD1 . ILE A 225 ? 0.6959 0.5565 0.6442 -0.0369 0.0429  -0.0314 225 ILE A CD1 
1676 N N   . SER A 226 ? 0.6520 0.5164 0.6226 -0.0342 0.0481  -0.0187 226 SER A N   
1677 C CA  . SER A 226 ? 0.6845 0.5573 0.6701 -0.0322 0.0493  -0.0076 226 SER A CA  
1678 C C   . SER A 226 ? 0.7241 0.6107 0.7106 -0.0358 0.0407  -0.0025 226 SER A C   
1679 O O   . SER A 226 ? 0.7406 0.6379 0.7337 -0.0370 0.0377  0.0047  226 SER A O   
1680 C CB  . SER A 226 ? 0.5842 0.4517 0.5798 -0.0291 0.0570  -0.0037 226 SER A CB  
1681 O OG  . SER A 226 ? 0.6994 0.5528 0.6916 -0.0275 0.0659  -0.0107 226 SER A OG  
1682 N N   . ASP A 227 ? 0.6894 0.5766 0.6684 -0.0384 0.0367  -0.0063 227 ASP A N   
1683 C CA  . ASP A 227 ? 0.7071 0.6079 0.6873 -0.0425 0.0300  -0.0009 227 ASP A CA  
1684 C C   . ASP A 227 ? 0.7300 0.6361 0.7021 -0.0473 0.0241  -0.0046 227 ASP A C   
1685 O O   . ASP A 227 ? 0.7597 0.6774 0.7310 -0.0524 0.0189  -0.0013 227 ASP A O   
1686 C CB  . ASP A 227 ? 0.6570 0.5573 0.6323 -0.0441 0.0282  -0.0034 227 ASP A CB  
1687 C CG  . ASP A 227 ? 0.8710 0.7654 0.8547 -0.0401 0.0345  0.0003  227 ASP A CG  
1688 O OD1 . ASP A 227 ? 0.6932 0.5904 0.6910 -0.0368 0.0390  0.0095  227 ASP A OD1 
1689 O OD2 . ASP A 227 ? 0.9735 0.8603 0.9506 -0.0404 0.0356  -0.0060 227 ASP A OD2 
1690 N N   . GLN A 228 ? 0.6728 0.5710 0.6391 -0.0465 0.0254  -0.0112 228 GLN A N   
1691 C CA  . GLN A 228 ? 0.6623 0.5636 0.6227 -0.0507 0.0214  -0.0146 228 GLN A CA  
1692 C C   . GLN A 228 ? 0.6544 0.5601 0.6219 -0.0505 0.0221  -0.0094 228 GLN A C   
1693 O O   . GLN A 228 ? 0.6507 0.5596 0.6147 -0.0548 0.0191  -0.0114 228 GLN A O   
1694 C CB  . GLN A 228 ? 0.6805 0.5709 0.6306 -0.0499 0.0222  -0.0245 228 GLN A CB  
1695 C CG  . GLN A 228 ? 0.6759 0.5635 0.6189 -0.0508 0.0210  -0.0297 228 GLN A CG  
1696 C CD  . GLN A 228 ? 0.7028 0.5856 0.6474 -0.0474 0.0242  -0.0292 228 GLN A CD  
1697 O OE1 . GLN A 228 ? 0.7307 0.6059 0.6751 -0.0443 0.0282  -0.0312 228 GLN A OE1 
1698 N NE2 . GLN A 228 ? 0.8182 0.7056 0.7642 -0.0487 0.0227  -0.0267 228 GLN A NE2 
1699 N N   . THR A 229 ? 0.5647 0.4693 0.5424 -0.0456 0.0270  -0.0033 229 THR A N   
1700 C CA  . THR A 229 ? 0.6377 0.5443 0.6224 -0.0441 0.0291  0.0010  229 THR A CA  
1701 C C   . THR A 229 ? 0.6434 0.5615 0.6439 -0.0427 0.0305  0.0140  229 THR A C   
1702 O O   . THR A 229 ? 0.8023 0.7322 0.8080 -0.0462 0.0270  0.0203  229 THR A O   
1703 C CB  . THR A 229 ? 0.6965 0.5897 0.6786 -0.0392 0.0357  -0.0044 229 THR A CB  
1704 O OG1 . THR A 229 ? 0.6778 0.5653 0.6653 -0.0350 0.0419  -0.0026 229 THR A OG1 
1705 C CG2 . THR A 229 ? 0.5104 0.3949 0.4785 -0.0406 0.0340  -0.0150 229 THR A CG2 
1706 N N   . LEU A 230 ? 0.7165 0.6319 0.7258 -0.0379 0.0359  0.0187  230 LEU A N   
1707 C CA  . LEU A 230 ? 0.6775 0.6011 0.7052 -0.0342 0.0403  0.0320  230 LEU A CA  
1708 C C   . LEU A 230 ? 0.6644 0.6089 0.7005 -0.0390 0.0332  0.0439  230 LEU A C   
1709 O O   . LEU A 230 ? 0.7517 0.7081 0.7968 -0.0404 0.0316  0.0525  230 LEU A O   
1710 C CB  . LEU A 230 ? 0.5780 0.4923 0.6138 -0.0282 0.0489  0.0338  230 LEU A CB  
1711 C CG  . LEU A 230 ? 0.6497 0.5454 0.6783 -0.0248 0.0570  0.0231  230 LEU A CG  
1712 C CD1 . LEU A 230 ? 0.6080 0.4921 0.6424 -0.0204 0.0668  0.0224  230 LEU A CD1 
1713 C CD2 . LEU A 230 ? 0.6137 0.5099 0.6479 -0.0227 0.0606  0.0257  230 LEU A CD2 
1714 N N   . GLU A 231 ? 0.6615 0.6121 0.6942 -0.0424 0.0287  0.0450  231 GLU A N   
1715 C CA  . GLU A 231 ? 0.7854 0.7578 0.8282 -0.0468 0.0232  0.0590  231 GLU A CA  
1716 C C   . GLU A 231 ? 0.7744 0.7606 0.8114 -0.0557 0.0153  0.0593  231 GLU A C   
1717 O O   . GLU A 231 ? 0.7394 0.7422 0.7891 -0.0575 0.0134  0.0721  231 GLU A O   
1718 C CB  . GLU A 231 ? 0.7868 0.7630 0.8257 -0.0493 0.0201  0.0595  231 GLU A CB  
1719 C CG  . GLU A 231 ? 0.9004 0.9017 0.9462 -0.0561 0.0129  0.0731  231 GLU A CG  
1720 C CD  . GLU A 231 ? 1.0747 1.0818 1.1239 -0.0561 0.0122  0.0790  231 GLU A CD  
1721 O OE1 . GLU A 231 ? 1.1461 1.1378 1.1976 -0.0491 0.0188  0.0755  231 GLU A OE1 
1722 O OE2 . GLU A 231 ? 1.1427 1.1702 1.1916 -0.0639 0.0049  0.0870  231 GLU A OE2 
1723 N N   . LYS A 232 ? 0.7750 0.7545 0.7936 -0.0615 0.0112  0.0457  232 LYS A N   
1724 C CA  . LYS A 232 ? 0.7066 0.6966 0.7183 -0.0711 0.0048  0.0439  232 LYS A CA  
1725 C C   . LYS A 232 ? 0.8013 0.7922 0.8206 -0.0695 0.0068  0.0474  232 LYS A C   
1726 O O   . LYS A 232 ? 0.8342 0.8411 0.8567 -0.0769 0.0020  0.0538  232 LYS A O   
1727 C CB  . LYS A 232 ? 0.6637 0.6418 0.6561 -0.0760 0.0030  0.0277  232 LYS A CB  
1728 C CG  . LYS A 232 ? 0.7818 0.7626 0.7643 -0.0810 -0.0002 0.0234  232 LYS A CG  
1729 C CD  . LYS A 232 ? 1.0522 1.0211 1.0359 -0.0725 0.0042  0.0215  232 LYS A CD  
1730 C CE  . LYS A 232 ? 0.9848 0.9343 0.9688 -0.0635 0.0107  0.0150  232 LYS A CE  
1731 N NZ  . LYS A 232 ? 0.8326 0.7715 0.8174 -0.0570 0.0151  0.0130  232 LYS A NZ  
1732 N N   . THR A 233 ? 0.8403 0.8148 0.8618 -0.0608 0.0138  0.0430  233 THR A N   
1733 C CA  . THR A 233 ? 0.7318 0.7069 0.7606 -0.0589 0.0163  0.0465  233 THR A CA  
1734 C C   . THR A 233 ? 0.7700 0.7611 0.8195 -0.0561 0.0179  0.0639  233 THR A C   
1735 O O   . THR A 233 ? 0.6838 0.6892 0.7405 -0.0605 0.0147  0.0719  233 THR A O   
1736 C CB  . THR A 233 ? 0.6623 0.6172 0.6877 -0.0510 0.0238  0.0378  233 THR A CB  
1737 O OG1 . THR A 233 ? 0.7876 0.7303 0.7961 -0.0537 0.0220  0.0238  233 THR A OG1 
1738 C CG2 . THR A 233 ? 0.5708 0.5278 0.6051 -0.0488 0.0269  0.0427  233 THR A CG2 
1739 N N   . PHE A 234 ? 0.6968 0.6856 0.7573 -0.0488 0.0235  0.0706  234 PHE A N   
1740 C CA  . PHE A 234 ? 0.7656 0.7689 0.8491 -0.0446 0.0269  0.0887  234 PHE A CA  
1741 C C   . PHE A 234 ? 0.8581 0.8886 0.9478 -0.0535 0.0176  0.1019  234 PHE A C   
1742 O O   . PHE A 234 ? 0.9034 0.9511 1.0101 -0.0536 0.0173  0.1170  234 PHE A O   
1743 C CB  . PHE A 234 ? 0.7355 0.7300 0.8295 -0.0359 0.0353  0.0928  234 PHE A CB  
1744 C CG  . PHE A 234 ? 0.7467 0.7185 0.8401 -0.0275 0.0464  0.0840  234 PHE A CG  
1745 C CD1 . PHE A 234 ? 0.7943 0.7608 0.8878 -0.0257 0.0500  0.0810  234 PHE A CD1 
1746 C CD2 . PHE A 234 ? 0.7295 0.6855 0.8212 -0.0225 0.0535  0.0783  234 PHE A CD2 
1747 C CE1 . PHE A 234 ? 0.8163 0.7629 0.9075 -0.0193 0.0605  0.0723  234 PHE A CE1 
1748 C CE2 . PHE A 234 ? 0.7468 0.6823 0.8359 -0.0166 0.0641  0.0690  234 PHE A CE2 
1749 C CZ  . PHE A 234 ? 0.8770 0.8081 0.9654 -0.0152 0.0676  0.0660  234 PHE A CZ  
1750 N N   . ARG A 235 ? 0.7280 0.7639 0.8038 -0.0617 0.0101  0.0966  235 ARG A N   
1751 C CA  . ARG A 235 ? 0.7657 0.8290 0.8455 -0.0718 0.0012  0.1089  235 ARG A CA  
1752 C C   . ARG A 235 ? 0.8780 0.9528 0.9522 -0.0820 -0.0050 0.1079  235 ARG A C   
1753 O O   . ARG A 235 ? 0.9655 1.0638 1.0537 -0.0862 -0.0087 0.1237  235 ARG A O   
1754 C CB  . ARG A 235 ? 0.7979 0.8628 0.8634 -0.0781 -0.0039 0.1027  235 ARG A CB  
1755 C CG  . ARG A 235 ? 0.9593 1.0542 1.0308 -0.0878 -0.0120 0.1178  235 ARG A CG  
1756 C CD  . ARG A 235 ? 1.0202 1.1163 1.0752 -0.0951 -0.0168 0.1100  235 ARG A CD  
1757 N NE  . ARG A 235 ? 1.0647 1.1436 1.1207 -0.0852 -0.0108 0.1061  235 ARG A NE  
1758 C CZ  . ARG A 235 ? 1.0278 1.1139 1.1012 -0.0786 -0.0077 0.1209  235 ARG A CZ  
1759 N NH1 . ARG A 235 ? 0.7863 0.8974 0.8796 -0.0797 -0.0099 0.1421  235 ARG A NH1 
1760 N NH2 . ARG A 235 ? 1.1654 1.2340 1.2375 -0.0710 -0.0020 0.1150  235 ARG A NH2 
1761 N N   . LEU A 236 ? 0.9149 0.9739 0.9700 -0.0861 -0.0059 0.0900  236 LEU A N   
1762 C CA  . LEU A 236 ? 0.8643 0.9312 0.9143 -0.0957 -0.0104 0.0876  236 LEU A CA  
1763 C C   . LEU A 236 ? 0.8952 0.9676 0.9629 -0.0901 -0.0069 0.0989  236 LEU A C   
1764 O O   . LEU A 236 ? 0.9736 1.0639 1.0457 -0.0985 -0.0118 0.1062  236 LEU A O   
1765 C CB  . LEU A 236 ? 0.7980 0.8432 0.8282 -0.0981 -0.0092 0.0674  236 LEU A CB  
1766 C CG  . LEU A 236 ? 0.9109 0.9479 0.9228 -0.1036 -0.0113 0.0542  236 LEU A CG  
1767 C CD1 . LEU A 236 ? 0.9281 0.9407 0.9262 -0.1013 -0.0073 0.0368  236 LEU A CD1 
1768 C CD2 . LEU A 236 ? 0.8636 0.9206 0.8679 -0.1192 -0.0190 0.0559  236 LEU A CD2 
1769 N N   . LEU A 237 ? 0.9012 0.9589 0.9793 -0.0766 0.0021  0.1003  237 LEU A N   
1770 C CA  . LEU A 237 ? 1.0124 1.0739 1.1073 -0.0708 0.0070  0.1101  237 LEU A CA  
1771 C C   . LEU A 237 ? 1.0702 1.1585 1.1883 -0.0708 0.0054  0.1329  237 LEU A C   
1772 O O   . LEU A 237 ? 1.0414 1.1444 1.1716 -0.0730 0.0042  0.1435  237 LEU A O   
1773 C CB  . LEU A 237 ? 1.0034 1.0409 1.1012 -0.0575 0.0182  0.1038  237 LEU A CB  
1774 C CG  . LEU A 237 ? 1.0347 1.0492 1.1124 -0.0575 0.0197  0.0842  237 LEU A CG  
1775 C CD1 . LEU A 237 ? 1.0974 1.0922 1.1781 -0.0464 0.0305  0.0794  237 LEU A CD1 
1776 C CD2 . LEU A 237 ? 0.9455 0.9657 1.0145 -0.0673 0.0134  0.0796  237 LEU A CD2 
1777 N N   . SER A 238 ? 1.0842 1.1804 1.2098 -0.0687 0.0051  0.1419  238 SER A N   
1778 C CA  . SER A 238 ? 0.9937 1.1169 1.1441 -0.0679 0.0041  0.1659  238 SER A CA  
1779 C C   . SER A 238 ? 1.0959 1.2492 1.2429 -0.0837 -0.0085 0.1744  238 SER A C   
1780 O O   . SER A 238 ? 1.0858 1.2649 1.2520 -0.0861 -0.0112 0.1939  238 SER A O   
1781 C CB  . SER A 238 ? 0.9171 1.0380 1.0783 -0.0599 0.0091  0.1736  238 SER A CB  
1782 O OG  . SER A 238 ? 0.9912 1.1354 1.1809 -0.0560 0.0110  0.1984  238 SER A OG  
1783 N N   . GLU A 239 ? 1.1512 1.3018 1.2738 -0.0951 -0.0159 0.1597  239 GLU A N   
1784 C CA  . GLU A 239 ? 1.1139 1.2911 1.2286 -0.1126 -0.0273 0.1641  239 GLU A CA  
1785 C C   . GLU A 239 ? 1.1390 1.3239 1.2533 -0.1203 -0.0304 0.1638  239 GLU A C   
1786 O O   . GLU A 239 ? 1.2227 1.4367 1.3404 -0.1334 -0.0387 0.1753  239 GLU A O   
1787 C CB  . GLU A 239 ? 1.1075 1.2746 1.1951 -0.1222 -0.0317 0.1454  239 GLU A CB  
1788 C CG  . GLU A 239 ? 1.1913 1.3577 1.2782 -0.1184 -0.0312 0.1476  239 GLU A CG  
1789 C CD  . GLU A 239 ? 1.1845 1.3388 1.2447 -0.1270 -0.0342 0.1280  239 GLU A CD  
1790 O OE1 . GLU A 239 ? 1.1844 1.3262 1.2271 -0.1338 -0.0349 0.1113  239 GLU A OE1 
1791 O OE2 . GLU A 239 ? 1.1430 1.3000 1.2007 -0.1266 -0.0352 0.1298  239 GLU A OE2 
1792 N N   . ARG A 240 ? 1.1564 1.3170 1.2662 -0.1134 -0.0239 0.1510  240 ARG A N   
1793 C CA  . ARG A 240 ? 1.2189 1.3847 1.3301 -0.1191 -0.0255 0.1511  240 ARG A CA  
1794 C C   . ARG A 240 ? 1.2785 1.4508 1.4157 -0.1079 -0.0194 0.1677  240 ARG A C   
1795 O O   . ARG A 240 ? 1.3625 1.5472 1.5062 -0.1133 -0.0217 0.1736  240 ARG A O   
1796 C CB  . ARG A 240 ? 1.1781 1.3150 1.2688 -0.1194 -0.0223 0.1278  240 ARG A CB  
1797 C CG  . ARG A 240 ? 1.1660 1.2799 1.2636 -0.1041 -0.0122 0.1238  240 ARG A CG  
1798 C CD  . ARG A 240 ? 1.2529 1.3497 1.3369 -0.1073 -0.0110 0.1084  240 ARG A CD  
1799 N NE  . ARG A 240 ? 1.3860 1.4591 1.4489 -0.1076 -0.0096 0.0886  240 ARG A NE  
1800 C CZ  . ARG A 240 ? 1.3886 1.4442 1.4393 -0.1093 -0.0076 0.0744  240 ARG A CZ  
1801 N NH1 . ARG A 240 ? 1.2834 1.3417 1.3397 -0.1113 -0.0069 0.0770  240 ARG A NH1 
1802 N NH2 . ARG A 240 ? 1.3955 1.4313 1.4296 -0.1089 -0.0060 0.0586  240 ARG A NH2 
1803 N N   . ILE A 241 ? 1.2013 1.3639 1.3535 -0.0925 -0.0105 0.1743  241 ILE A N   
1804 C CA  . ILE A 241 ? 1.1763 1.3506 1.3571 -0.0828 -0.0042 0.1942  241 ILE A CA  
1805 C C   . ILE A 241 ? 1.2476 1.4578 1.4478 -0.0881 -0.0106 0.2187  241 ILE A C   
1806 O O   . ILE A 241 ? 1.3457 1.5751 1.5714 -0.0842 -0.0083 0.2390  241 ILE A O   
1807 C CB  . ILE A 241 ? 1.1829 1.3312 1.3722 -0.0652 0.0097  0.1906  241 ILE A CB  
1808 C CG1 . ILE A 241 ? 1.2379 1.3578 1.4120 -0.0612 0.0155  0.1709  241 ILE A CG1 
1809 C CG2 . ILE A 241 ? 1.1393 1.2995 1.3607 -0.0544 0.0182  0.2124  241 ILE A CG2 
1810 C CD1 . ILE A 241 ? 1.2900 1.3798 1.4566 -0.0499 0.0255  0.1573  241 ILE A CD1 
1811 N N   . ASN A 242 ? 1.2531 1.4748 1.4419 -0.0978 -0.0189 0.2181  242 ASN A N   
1812 C CA  . ASN A 242 ? 1.2300 1.4906 1.4328 -0.1073 -0.0278 0.2409  242 ASN A CA  
1813 C C   . ASN A 242 ? 1.2783 1.5622 1.4728 -0.1254 -0.0387 0.2423  242 ASN A C   
1814 O O   . ASN A 242 ? 1.2569 1.5745 1.4710 -0.1310 -0.0439 0.2649  242 ASN A O   
1815 C CB  . ASN A 242 ? 1.1725 1.4377 1.3646 -0.1123 -0.0327 0.2393  242 ASN A CB  
1816 C CG  . ASN A 242 ? 1.1762 1.4678 1.3954 -0.1076 -0.0327 0.2665  242 ASN A CG  
1817 O OD1 . ASN A 242 ? 1.2490 1.5512 1.4970 -0.0980 -0.0267 0.2861  242 ASN A OD1 
1818 N ND2 . ASN A 242 ? 1.1040 1.4058 1.3155 -0.1138 -0.0383 0.2686  242 ASN A ND2 
1819 N N   . SER A 243 ? 1.3277 1.5945 1.4944 -0.1352 -0.0419 0.2189  243 SER A N   
1820 C CA  . SER A 243 ? 1.3297 1.6105 1.4886 -0.1507 -0.0490 0.2165  243 SER A CA  
1821 C C   . SER A 243 ? 1.3936 1.6868 1.5764 -0.1453 -0.0461 0.2325  243 SER A C   
1822 O O   . SER A 243 ? 1.4152 1.7341 1.6008 -0.1591 -0.0538 0.2413  243 SER A O   
1823 C CB  . SER A 243 ? 1.2805 1.5298 1.4112 -0.1547 -0.0472 0.1878  243 SER A CB  
1824 O OG  . SER A 243 ? 1.2500 1.5014 1.3782 -0.1627 -0.0488 0.1840  243 SER A OG  
1825 N N   . SER A 244 ? 1.4191 1.6942 1.6186 -0.1262 -0.0346 0.2359  244 SER A N   
1826 C CA  . SER A 244 ? 1.4468 1.7302 1.6700 -0.1189 -0.0295 0.2502  244 SER A CA  
1827 C C   . SER A 244 ? 1.4941 1.8117 1.7500 -0.1154 -0.0302 0.2816  244 SER A C   
1828 O O   . SER A 244 ? 1.4984 1.8106 1.7788 -0.0989 -0.0191 0.2935  244 SER A O   
1829 C CB  . SER A 244 ? 1.3611 1.6091 1.5872 -0.1002 -0.0153 0.2393  244 SER A CB  
1830 O OG  . SER A 244 ? 1.2707 1.4878 1.4683 -0.1020 -0.0144 0.2123  244 SER A OG  
1831 N N   . LYS A 245 ? 1.4958 1.8492 1.7533 -0.1310 -0.0424 0.2958  245 LYS A N   
1832 C CA  . LYS A 245 ? 1.4445 1.8350 1.7354 -0.1289 -0.0439 0.3283  245 LYS A CA  
1833 C C   . LYS A 245 ? 1.4852 1.9012 1.7877 -0.1380 -0.0490 0.3408  245 LYS A C   
1834 O O   . LYS A 245 ? 1.4792 1.8807 1.7908 -0.1285 -0.0407 0.3384  245 LYS A O   
1835 C CB  . LYS A 245 ? 1.3652 1.7855 1.6552 -0.1403 -0.0543 0.3414  245 LYS A CB  
1836 C CG  . LYS A 245 ? 1.3475 1.7991 1.6759 -0.1317 -0.0522 0.3759  245 LYS A CG  
1837 C CD  . LYS A 245 ? 1.3216 1.7437 1.6702 -0.1067 -0.0347 0.3771  245 LYS A CD  
1838 C CE  . LYS A 245 ? 1.2794 1.7234 1.6705 -0.0950 -0.0272 0.4079  245 LYS A CE  
1839 N NZ  . LYS A 245 ? 1.1918 1.6524 1.5904 -0.1014 -0.0305 0.4145  245 LYS A NZ  
1840 N N   . VAL A 257 ? 1.7858 1.9822 2.1342 -0.0141 0.0627  0.2858  257 VAL A N   
1841 C CA  . VAL A 257 ? 1.7859 1.9579 2.1433 -0.0002 0.0807  0.2808  257 VAL A CA  
1842 C C   . VAL A 257 ? 1.9015 2.0642 2.2767 0.0119  0.0935  0.2882  257 VAL A C   
1843 O O   . VAL A 257 ? 1.9696 2.1079 2.3509 0.0236  0.1106  0.2820  257 VAL A O   
1844 C CB  . VAL A 257 ? 1.6486 1.7896 1.9739 -0.0020 0.0818  0.2520  257 VAL A CB  
1845 C CG1 . VAL A 257 ? 1.5846 1.7263 1.8796 -0.0162 0.0653  0.2370  257 VAL A CG1 
1846 C CG2 . VAL A 257 ? 1.6098 1.7167 1.9289 0.0094  0.0978  0.2370  257 VAL A CG2 
1847 N N   . ASN A 258 ? 1.8857 2.0693 2.2713 0.0087  0.0861  0.3033  258 ASN A N   
1848 C CA  . ASN A 258 ? 1.8412 2.0154 2.2428 0.0193  0.0976  0.3101  258 ASN A CA  
1849 C C   . ASN A 258 ? 1.8618 1.9986 2.2339 0.0209  0.1030  0.2808  258 ASN A C   
1850 O O   . ASN A 258 ? 1.9015 2.0134 2.2796 0.0319  0.1200  0.2745  258 ASN A O   
1851 C CB  . ASN A 258 ? 1.7367 1.9137 2.1766 0.0335  0.1158  0.3301  258 ASN A CB  
1852 C CG  . ASN A 258 ? 1.6137 1.8328 2.0868 0.0320  0.1098  0.3632  258 ASN A CG  
1853 O OD1 . ASN A 258 ? 1.5835 1.8100 2.0912 0.0431  0.1235  0.3832  258 ASN A OD1 
1854 N ND2 . ASN A 258 ? 1.5662 1.8137 2.0291 0.0176  0.0898  0.3695  258 ASN A ND2 
1855 N N   . GLN A 259 ? 1.8208 1.9535 2.1608 0.0094  0.0891  0.2627  259 GLN A N   
1856 C CA  . GLN A 259 ? 1.7614 1.8611 2.0729 0.0100  0.0930  0.2354  259 GLN A CA  
1857 C C   . GLN A 259 ? 1.7201 1.7998 2.0176 0.0120  0.0955  0.2226  259 GLN A C   
1858 O O   . GLN A 259 ? 1.7006 1.7548 1.9967 0.0203  0.1095  0.2124  259 GLN A O   
1859 C CB  . GLN A 259 ? 1.7067 1.8103 1.9915 -0.0029 0.0779  0.2221  259 GLN A CB  
1860 C CG  . GLN A 259 ? 1.6785 1.8094 1.9591 -0.0156 0.0607  0.2305  259 GLN A CG  
1861 C CD  . GLN A 259 ? 1.6779 1.7965 1.9245 -0.0258 0.0502  0.2084  259 GLN A CD  
1862 O OE1 . GLN A 259 ? 1.6770 1.8009 1.9100 -0.0355 0.0414  0.2017  259 GLN A OE1 
1863 N NE2 . GLN A 259 ? 1.6621 1.7632 1.8957 -0.0234 0.0519  0.1968  259 GLN A NE2 
1864 N N   . PHE A 260 ? 1.6981 1.7876 1.9815 0.0029  0.0818  0.2203  260 PHE A N   
1865 C CA  . PHE A 260 ? 1.6173 1.6904 1.8878 0.0040  0.0829  0.2092  260 PHE A CA  
1866 C C   . PHE A 260 ? 1.5582 1.6459 1.8124 -0.0077 0.0664  0.2073  260 PHE A C   
1867 O O   . PHE A 260 ? 1.5563 1.6632 1.8027 -0.0185 0.0534  0.2095  260 PHE A O   
1868 C CB  . PHE A 260 ? 1.5259 1.5655 1.7727 0.0066  0.0899  0.1840  260 PHE A CB  
1869 C CG  . PHE A 260 ? 1.4867 1.5056 1.7335 0.0134  0.1005  0.1776  260 PHE A CG  
1870 C CD1 . PHE A 260 ? 1.4178 1.4448 1.6905 0.0199  0.1077  0.1952  260 PHE A CD1 
1871 C CD2 . PHE A 260 ? 1.4160 1.4087 1.6378 0.0127  0.1031  0.1549  260 PHE A CD2 
1872 C CE1 . PHE A 260 ? 1.3123 1.3196 1.5854 0.0255  0.1179  0.1892  260 PHE A CE1 
1873 C CE2 . PHE A 260 ? 1.3085 1.2830 1.5298 0.0175  0.1125  0.1489  260 PHE A CE2 
1874 C CZ  . PHE A 260 ? 1.2663 1.2472 1.5130 0.0239  0.1202  0.1653  260 PHE A CZ  
1875 N N   . ASP A 261 ? 1.3929 1.4756 1.6454 -0.0062 0.0671  0.2064  261 ASP A N   
1876 C CA  . ASP A 261 ? 1.3215 1.4145 1.5547 -0.0176 0.0525  0.2009  261 ASP A CA  
1877 C C   . ASP A 261 ? 1.3007 1.3613 1.5130 -0.0140 0.0586  0.1780  261 ASP A C   
1878 O O   . ASP A 261 ? 1.3520 1.3911 1.5687 -0.0046 0.0720  0.1720  261 ASP A O   
1879 C CB  . ASP A 261 ? 1.3701 1.4831 1.6168 -0.0190 0.0484  0.2178  261 ASP A CB  
1880 C CG  . ASP A 261 ? 1.5000 1.5972 1.7617 -0.0071 0.0620  0.2215  261 ASP A CG  
1881 O OD1 . ASP A 261 ? 1.5668 1.6398 1.8324 0.0025  0.0760  0.2136  261 ASP A OD1 
1882 O OD2 . ASP A 261 ? 1.5003 1.6095 1.7698 -0.0080 0.0590  0.2324  261 ASP A OD2 
1883 N N   . PRO A 262 ? 1.1969 1.2533 1.3841 -0.0225 0.0489  0.1632  262 PRO A N   
1884 C CA  . PRO A 262 ? 1.1442 1.1717 1.3155 -0.0180 0.0556  0.1445  262 PRO A CA  
1885 C C   . PRO A 262 ? 1.0766 1.1096 1.2489 -0.0193 0.0524  0.1490  262 PRO A C   
1886 O O   . PRO A 262 ? 0.9433 0.9574 1.1078 -0.0155 0.0578  0.1387  262 PRO A O   
1887 C CB  . PRO A 262 ? 1.0648 1.0847 1.2107 -0.0257 0.0479  0.1270  262 PRO A CB  
1888 C CG  . PRO A 262 ? 1.0599 1.0984 1.2124 -0.0309 0.0423  0.1359  262 PRO A CG  
1889 C CD  . PRO A 262 ? 1.1309 1.1966 1.3023 -0.0334 0.0376  0.1568  262 PRO A CD  
1890 N N   . GLY A 263 ? 1.0462 1.1067 1.2296 -0.0248 0.0441  0.1659  263 GLY A N   
1891 C CA  . GLY A 263 ? 1.0515 1.1213 1.2360 -0.0273 0.0397  0.1721  263 GLY A CA  
1892 C C   . GLY A 263 ? 0.9845 1.0484 1.1886 -0.0174 0.0504  0.1821  263 GLY A C   
1893 O O   . GLY A 263 ? 1.0026 1.0673 1.2031 -0.0188 0.0480  0.1824  263 GLY A O   
1894 N N   . ASP A 264 ? 0.9529 1.0099 1.1780 -0.0073 0.0632  0.1902  264 ASP A N   
1895 C CA  . ASP A 264 ? 1.0451 1.0921 1.2885 0.0023  0.0756  0.1975  264 ASP A CA  
1896 C C   . ASP A 264 ? 1.0321 1.0483 1.2549 0.0040  0.0813  0.1749  264 ASP A C   
1897 O O   . ASP A 264 ? 1.0190 1.0213 1.2510 0.0105  0.0921  0.1755  264 ASP A O   
1898 C CB  . ASP A 264 ? 1.2163 1.2600 1.4860 0.0125  0.0900  0.2091  264 ASP A CB  
1899 C CG  . ASP A 264 ? 1.4646 1.5337 1.7686 0.0169  0.0924  0.2383  264 ASP A CG  
1900 O OD1 . ASP A 264 ? 1.5325 1.6221 1.8388 0.0115  0.0825  0.2495  264 ASP A OD1 
1901 O OD2 . ASP A 264 ? 1.5619 1.6315 1.8914 0.0257  0.1046  0.2509  264 ASP A OD2 
1902 N N   . LEU A 265 ? 1.0308 1.0367 1.2262 -0.0021 0.0745  0.1553  265 LEU A N   
1903 C CA  . LEU A 265 ? 1.0062 0.9850 1.1813 -0.0013 0.0791  0.1342  265 LEU A CA  
1904 C C   . LEU A 265 ? 0.9292 0.9101 1.0844 -0.0088 0.0680  0.1255  265 LEU A C   
1905 O O   . LEU A 265 ? 0.8755 0.8379 1.0173 -0.0083 0.0710  0.1118  265 LEU A O   
1906 C CB  . LEU A 265 ? 0.9656 0.9306 1.1256 -0.0020 0.0807  0.1192  265 LEU A CB  
1907 C CG  . LEU A 265 ? 0.9633 0.9194 1.1390 0.0059  0.0946  0.1229  265 LEU A CG  
1908 C CD1 . LEU A 265 ? 0.9936 0.9476 1.1564 0.0028  0.0912  0.1138  265 LEU A CD1 
1909 C CD2 . LEU A 265 ? 0.9178 0.8476 1.0919 0.0116  0.1091  0.1122  265 LEU A CD2 
1910 N N   . VAL A 266 ? 0.8885 0.8929 1.0423 -0.0163 0.0556  0.1341  266 VAL A N   
1911 C CA  . VAL A 266 ? 0.9208 0.9280 1.0570 -0.0235 0.0462  0.1267  266 VAL A CA  
1912 C C   . VAL A 266 ? 0.9846 0.9915 1.1319 -0.0197 0.0505  0.1347  266 VAL A C   
1913 O O   . VAL A 266 ? 1.1019 1.1177 1.2738 -0.0140 0.0567  0.1523  266 VAL A O   
1914 C CB  . VAL A 266 ? 0.9943 1.0279 1.1261 -0.0340 0.0327  0.1340  266 VAL A CB  
1915 C CG1 . VAL A 266 ? 1.0872 1.1472 1.2415 -0.0344 0.0305  0.1578  266 VAL A CG1 
1916 C CG2 . VAL A 266 ? 1.0833 1.1137 1.1899 -0.0425 0.0240  0.1193  266 VAL A CG2 
1917 N N   . GLY A 267 ? 1.0158 1.0117 1.1463 -0.0223 0.0481  0.1222  267 GLY A N   
1918 C CA  . GLY A 267 ? 1.0166 1.0110 1.1583 -0.0185 0.0530  0.1296  267 GLY A CA  
1919 C C   . GLY A 267 ? 0.9516 0.9226 1.1040 -0.0091 0.0684  0.1264  267 GLY A C   
1920 O O   . GLY A 267 ? 0.9385 0.9049 1.1004 -0.0059 0.0740  0.1313  267 GLY A O   
1921 N N   . VAL A 268 ? 0.9304 0.8862 1.0813 -0.0053 0.0761  0.1180  268 VAL A N   
1922 C CA  . VAL A 268 ? 0.9093 0.8390 1.0625 0.0009  0.0909  0.1087  268 VAL A CA  
1923 C C   . VAL A 268 ? 0.8700 0.7831 0.9952 -0.0040 0.0872  0.0868  268 VAL A C   
1924 O O   . VAL A 268 ? 0.9688 0.8718 1.0786 -0.0057 0.0868  0.0734  268 VAL A O   
1925 C CB  . VAL A 268 ? 0.7949 0.7168 0.9588 0.0065  0.1015  0.1098  268 VAL A CB  
1926 C CG1 . VAL A 268 ? 0.7445 0.6408 0.9136 0.0122  0.1188  0.1021  268 VAL A CG1 
1927 C CG2 . VAL A 268 ? 0.7808 0.7251 0.9706 0.0098  0.1013  0.1324  268 VAL A CG2 
1928 N N   . LYS A 269 ? 0.9230 0.8343 1.0425 -0.0063 0.0844  0.0844  269 LYS A N   
1929 C CA  . LYS A 269 ? 0.8630 0.7632 0.9570 -0.0116 0.0789  0.0660  269 LYS A CA  
1930 C C   . LYS A 269 ? 0.9152 0.7913 0.9994 -0.0101 0.0889  0.0503  269 LYS A C   
1931 O O   . LYS A 269 ? 0.9007 0.7695 0.9638 -0.0146 0.0840  0.0357  269 LYS A O   
1932 C CB  . LYS A 269 ? 0.7931 0.6971 0.8846 -0.0142 0.0746  0.0676  269 LYS A CB  
1933 C CG  . LYS A 269 ? 1.0066 0.9011 1.1148 -0.0092 0.0863  0.0739  269 LYS A CG  
1934 C CD  . LYS A 269 ? 1.1351 1.0295 1.2353 -0.0127 0.0818  0.0708  269 LYS A CD  
1935 C CE  . LYS A 269 ? 1.0946 0.9791 1.2117 -0.0083 0.0934  0.0773  269 LYS A CE  
1936 N NZ  . LYS A 269 ? 1.1381 1.0151 1.2417 -0.0125 0.0909  0.0675  269 LYS A NZ  
1937 N N   . GLU A 270 ? 0.9206 0.7847 1.0194 -0.0046 0.1032  0.0531  270 GLU A N   
1938 C CA  . GLU A 270 ? 0.8368 0.6777 0.9258 -0.0048 0.1140  0.0379  270 GLU A CA  
1939 C C   . GLU A 270 ? 0.9017 0.7364 0.9820 -0.0051 0.1168  0.0295  270 GLU A C   
1940 O O   . GLU A 270 ? 0.8336 0.6518 0.8998 -0.0077 0.1229  0.0148  270 GLU A O   
1941 C CB  . GLU A 270 ? 0.8126 0.6410 0.9211 0.0003  0.1303  0.0433  270 GLU A CB  
1942 C CG  . GLU A 270 ? 0.8587 0.6878 0.9723 -0.0004 0.1295  0.0477  270 GLU A CG  
1943 C CD  . GLU A 270 ? 0.9314 0.7799 1.0684 0.0039  0.1266  0.0695  270 GLU A CD  
1944 O OE1 . GLU A 270 ? 0.9235 0.7841 1.0748 0.0077  0.1267  0.0817  270 GLU A OE1 
1945 O OE2 . GLU A 270 ? 1.0241 0.8772 1.1656 0.0031  0.1239  0.0753  270 GLU A OE2 
1946 N N   . PHE A 271 ? 0.8637 0.7124 0.9517 -0.0032 0.1122  0.0388  271 PHE A N   
1947 C CA  . PHE A 271 ? 0.7697 0.6158 0.8484 -0.0040 0.1121  0.0319  271 PHE A CA  
1948 C C   . PHE A 271 ? 0.7801 0.6293 0.8352 -0.0104 0.0991  0.0206  271 PHE A C   
1949 O O   . PHE A 271 ? 0.8714 0.7332 0.9228 -0.0134 0.0875  0.0241  271 PHE A O   
1950 C CB  . PHE A 271 ? 0.6987 0.5602 0.7950 -0.0003 0.1110  0.0468  271 PHE A CB  
1951 C CG  . PHE A 271 ? 0.8001 0.6591 0.8900 -0.0004 0.1123  0.0414  271 PHE A CG  
1952 C CD1 . PHE A 271 ? 0.8532 0.6944 0.9399 0.0013  0.1254  0.0320  271 PHE A CD1 
1953 C CD2 . PHE A 271 ? 0.7144 0.5889 0.8014 -0.0030 0.1011  0.0457  271 PHE A CD2 
1954 C CE1 . PHE A 271 ? 0.7887 0.6284 0.8694 0.0010  0.1267  0.0276  271 PHE A CE1 
1955 C CE2 . PHE A 271 ? 0.8029 0.6753 0.8851 -0.0030 0.1026  0.0415  271 PHE A CE2 
1956 C CZ  . PHE A 271 ? 0.7832 0.6385 0.8622 -0.0008 0.1152  0.0328  271 PHE A CZ  
1957 N N   . GLY A 272 ? 0.7510 0.5888 0.7904 -0.0128 0.1015  0.0075  272 GLY A N   
1958 C CA  . GLY A 272 ? 0.7885 0.6268 0.8070 -0.0183 0.0914  -0.0031 272 GLY A CA  
1959 C C   . GLY A 272 ? 0.7891 0.6276 0.7973 -0.0199 0.0889  -0.0087 272 GLY A C   
1960 O O   . GLY A 272 ? 0.6831 0.5155 0.6942 -0.0179 0.0974  -0.0098 272 GLY A O   
1961 N N   . TYR A 273 ? 0.7123 0.5574 0.7083 -0.0236 0.0778  -0.0124 273 TYR A N   
1962 C CA  . TYR A 273 ? 0.6887 0.5343 0.6746 -0.0254 0.0745  -0.0173 273 TYR A CA  
1963 C C   . TYR A 273 ? 0.6335 0.4741 0.6022 -0.0295 0.0707  -0.0278 273 TYR A C   
1964 O O   . TYR A 273 ? 0.6514 0.4954 0.6157 -0.0315 0.0642  -0.0289 273 TYR A O   
1965 C CB  . TYR A 273 ? 0.6378 0.4967 0.6279 -0.0260 0.0657  -0.0105 273 TYR A CB  
1966 C CG  . TYR A 273 ? 0.7614 0.6209 0.7460 -0.0268 0.0642  -0.0130 273 TYR A CG  
1967 C CD1 . TYR A 273 ? 0.7460 0.5994 0.7327 -0.0246 0.0726  -0.0139 273 TYR A CD1 
1968 C CD2 . TYR A 273 ? 0.6950 0.5607 0.6729 -0.0301 0.0554  -0.0144 273 TYR A CD2 
1969 C CE1 . TYR A 273 ? 0.7203 0.5750 0.7021 -0.0255 0.0711  -0.0156 273 TYR A CE1 
1970 C CE2 . TYR A 273 ? 0.6529 0.5187 0.6271 -0.0307 0.0545  -0.0160 273 TYR A CE2 
1971 C CZ  . TYR A 273 ? 0.6894 0.5505 0.6656 -0.0284 0.0618  -0.0161 273 TYR A CZ  
1972 O OH  . TYR A 273 ? 0.6778 0.5398 0.6504 -0.0292 0.0606  -0.0170 273 TYR A OH  
1973 N N   . LEU A 274 ? 0.6883 0.5218 0.6475 -0.0312 0.0752  -0.0349 274 LEU A N   
1974 C CA  . LEU A 274 ? 0.7862 0.6170 0.7301 -0.0356 0.0719  -0.0433 274 LEU A CA  
1975 C C   . LEU A 274 ? 0.7897 0.6249 0.7256 -0.0371 0.0671  -0.0449 274 LEU A C   
1976 O O   . LEU A 274 ? 0.7564 0.5920 0.6953 -0.0356 0.0701  -0.0428 274 LEU A O   
1977 C CB  . LEU A 274 ? 0.7736 0.5937 0.7108 -0.0385 0.0811  -0.0509 274 LEU A CB  
1978 C CG  . LEU A 274 ? 0.8005 0.6152 0.7319 -0.0403 0.0889  -0.0555 274 LEU A CG  
1979 C CD1 . LEU A 274 ? 0.7750 0.5924 0.6898 -0.0461 0.0843  -0.0618 274 LEU A CD1 
1980 C CD2 . LEU A 274 ? 0.6487 0.4511 0.5827 -0.0410 0.1021  -0.0598 274 LEU A CD2 
1981 N N   . LEU A 275 ? 0.6741 0.5128 0.6012 -0.0397 0.0600  -0.0477 275 LEU A N   
1982 C CA  . LEU A 275 ? 0.6856 0.5278 0.6048 -0.0416 0.0564  -0.0493 275 LEU A CA  
1983 C C   . LEU A 275 ? 0.7439 0.5839 0.6510 -0.0463 0.0581  -0.0553 275 LEU A C   
1984 O O   . LEU A 275 ? 0.7001 0.5386 0.6041 -0.0485 0.0575  -0.0583 275 LEU A O   
1985 C CB  . LEU A 275 ? 0.6756 0.5240 0.5957 -0.0411 0.0480  -0.0468 275 LEU A CB  
1986 C CG  . LEU A 275 ? 0.6602 0.5125 0.5743 -0.0425 0.0442  -0.0471 275 LEU A CG  
1987 C CD1 . LEU A 275 ? 0.7575 0.6108 0.6730 -0.0416 0.0461  -0.0448 275 LEU A CD1 
1988 C CD2 . LEU A 275 ? 0.7083 0.5644 0.6247 -0.0419 0.0382  -0.0457 275 LEU A CD2 
1989 N N   . LEU A 276 ? 0.6575 0.4988 0.5578 -0.0487 0.0601  -0.0568 276 LEU A N   
1990 C CA  . LEU A 276 ? 0.6903 0.5315 0.5781 -0.0549 0.0622  -0.0624 276 LEU A CA  
1991 C C   . LEU A 276 ? 0.7433 0.5933 0.6247 -0.0572 0.0578  -0.0600 276 LEU A C   
1992 O O   . LEU A 276 ? 0.9111 0.7631 0.7960 -0.0547 0.0579  -0.0562 276 LEU A O   
1993 C CB  . LEU A 276 ? 0.7685 0.6012 0.6529 -0.0575 0.0729  -0.0677 276 LEU A CB  
1994 C CG  . LEU A 276 ? 0.8289 0.6602 0.6987 -0.0663 0.0769  -0.0753 276 LEU A CG  
1995 C CD1 . LEU A 276 ? 0.8998 0.7182 0.7706 -0.0676 0.0889  -0.0815 276 LEU A CD1 
1996 C CD2 . LEU A 276 ? 0.7661 0.6050 0.6255 -0.0709 0.0762  -0.0753 276 LEU A CD2 
1997 N N   . VAL A 277 ? 0.6828 0.5389 0.5553 -0.0624 0.0542  -0.0614 277 VAL A N   
1998 C CA  . VAL A 277 ? 0.7148 0.5814 0.5817 -0.0654 0.0505  -0.0577 277 VAL A CA  
1999 C C   . VAL A 277 ? 0.7813 0.6521 0.6340 -0.0748 0.0527  -0.0624 277 VAL A C   
2000 O O   . VAL A 277 ? 0.7962 0.6669 0.6442 -0.0790 0.0519  -0.0662 277 VAL A O   
2001 C CB  . VAL A 277 ? 0.6847 0.5593 0.5575 -0.0623 0.0425  -0.0512 277 VAL A CB  
2002 C CG1 . VAL A 277 ? 0.5989 0.4861 0.4679 -0.0653 0.0391  -0.0453 277 VAL A CG1 
2003 C CG2 . VAL A 277 ? 0.7110 0.5813 0.5960 -0.0550 0.0410  -0.0479 277 VAL A CG2 
2004 N N   . ALA A 278 ? 0.8144 0.6901 0.6597 -0.0789 0.0552  -0.0620 278 ALA A N   
2005 C CA  . ALA A 278 ? 0.7498 0.6322 0.5798 -0.0898 0.0569  -0.0662 278 ALA A CA  
2006 C C   . ALA A 278 ? 0.7614 0.6600 0.5880 -0.0925 0.0516  -0.0580 278 ALA A C   
2007 O O   . ALA A 278 ? 0.8551 0.7559 0.6902 -0.0862 0.0499  -0.0511 278 ALA A O   
2008 C CB  . ALA A 278 ? 0.6807 0.5524 0.5022 -0.0946 0.0679  -0.0756 278 ALA A CB  
2009 N N   . GLN A 279 ? 0.7835 0.6945 0.5982 -0.1024 0.0489  -0.0580 279 GLN A N   
2010 C CA  . GLN A 279 ? 0.8356 0.7652 0.6477 -0.1059 0.0434  -0.0483 279 GLN A CA  
2011 C C   . GLN A 279 ? 0.9285 0.8650 0.7223 -0.1186 0.0477  -0.0533 279 GLN A C   
2012 O O   . GLN A 279 ? 0.9558 0.8840 0.7377 -0.1266 0.0543  -0.0650 279 GLN A O   
2013 C CB  . GLN A 279 ? 0.8764 0.8205 0.6925 -0.1069 0.0346  -0.0400 279 GLN A CB  
2014 C CG  . GLN A 279 ? 0.9892 0.9528 0.8105 -0.1064 0.0283  -0.0257 279 GLN A CG  
2015 C CD  . GLN A 279 ? 1.1167 1.0921 0.9477 -0.1041 0.0209  -0.0163 279 GLN A CD  
2016 O OE1 . GLN A 279 ? 1.1619 1.1357 0.9901 -0.1071 0.0196  -0.0212 279 GLN A OE1 
2017 N NE2 . GLN A 279 ? 1.0931 1.0795 0.9370 -0.0981 0.0168  -0.0026 279 GLN A NE2 
2018 N N   . ARG A 280 ? 1.0156 0.9671 0.8077 -0.1208 0.0449  -0.0445 280 ARG A N   
2019 C CA  . ARG A 280 ? 1.0062 0.9717 0.7802 -0.1347 0.0462  -0.0459 280 ARG A CA  
2020 C C   . ARG A 280 ? 1.0125 1.0018 0.7853 -0.1408 0.0363  -0.0348 280 ARG A C   
2021 O O   . ARG A 280 ? 1.1041 1.1028 0.8924 -0.1323 0.0295  -0.0211 280 ARG A O   
2022 C CB  . ARG A 280 ? 0.8706 0.8394 0.6435 -0.1338 0.0495  -0.0419 280 ARG A CB  
2023 C CG  . ARG A 280 ? 0.9896 0.9774 0.7440 -0.1486 0.0493  -0.0406 280 ARG A CG  
2024 C CD  . ARG A 280 ? 0.8858 0.8725 0.6358 -0.1491 0.0556  -0.0409 280 ARG A CD  
2025 N NE  . ARG A 280 ? 0.8870 0.8944 0.6184 -0.1645 0.0549  -0.0390 280 ARG A NE  
2026 C CZ  . ARG A 280 ? 0.9380 0.9476 0.6584 -0.1702 0.0614  -0.0418 280 ARG A CZ  
2027 N NH1 . ARG A 280 ? 0.9480 0.9401 0.6757 -0.1610 0.0694  -0.0459 280 ARG A NH1 
2028 N NH2 . ARG A 280 ? 0.8891 0.9197 0.5913 -0.1858 0.0599  -0.0399 280 ARG A NH2 
2029 N N   . PRO A 281 ? 0.9347 0.9345 0.6909 -0.1555 0.0357  -0.0397 281 PRO A N   
2030 C CA  . PRO A 281 ? 0.9234 0.9466 0.6808 -0.1610 0.0258  -0.0285 281 PRO A CA  
2031 C C   . PRO A 281 ? 0.9249 0.9729 0.6868 -0.1616 0.0192  -0.0111 281 PRO A C   
2032 O O   . PRO A 281 ? 0.9623 1.0151 0.7162 -0.1659 0.0223  -0.0103 281 PRO A O   
2033 C CB  . PRO A 281 ? 1.0687 1.0966 0.8042 -0.1789 0.0282  -0.0399 281 PRO A CB  
2034 C CG  . PRO A 281 ? 1.1232 1.1217 0.8531 -0.1773 0.0399  -0.0583 281 PRO A CG  
2035 C CD  . PRO A 281 ? 0.9901 0.9774 0.7280 -0.1666 0.0450  -0.0570 281 PRO A CD  
2036 N N   . GLY A 282 ? 1.0139 1.0779 0.7899 -0.1573 0.0105  0.0037  282 GLY A N   
2037 C CA  . GLY A 282 ? 0.9466 1.0334 0.7340 -0.1544 0.0043  0.0236  282 GLY A CA  
2038 C C   . GLY A 282 ? 1.0706 1.1847 0.8413 -0.1711 0.0010  0.0296  282 GLY A C   
2039 O O   . GLY A 282 ? 1.1521 1.2667 0.9009 -0.1859 0.0038  0.0168  282 GLY A O   
2040 N N   . LEU B 6   ? 1.8944 1.7171 1.5476 -0.2621 0.1427  -0.2093 6   LEU B N   
2041 C CA  . LEU B 6   ? 1.8968 1.7016 1.5589 -0.2629 0.1529  -0.2159 6   LEU B CA  
2042 C C   . LEU B 6   ? 1.9553 1.7773 1.6093 -0.2761 0.1431  -0.2147 6   LEU B C   
2043 O O   . LEU B 6   ? 1.9788 1.8266 1.6191 -0.2873 0.1314  -0.2100 6   LEU B O   
2044 C CB  . LEU B 6   ? 1.8294 1.6167 1.4901 -0.2686 0.1728  -0.2266 6   LEU B CB  
2045 C CG  . LEU B 6   ? 1.7498 1.5482 1.3917 -0.2869 0.1780  -0.2331 6   LEU B CG  
2046 C CD1 . LEU B 6   ? 1.7485 1.5257 1.3923 -0.2933 0.1988  -0.2449 6   LEU B CD1 
2047 C CD2 . LEU B 6   ? 1.6733 1.4797 1.3090 -0.2840 0.1760  -0.2300 6   LEU B CD2 
2048 N N   . SER B 7   ? 2.0279 1.8367 1.6914 -0.2747 0.1479  -0.2178 7   SER B N   
2049 C CA  . SER B 7   ? 2.0251 1.8483 1.6844 -0.2846 0.1383  -0.2157 7   SER B CA  
2050 C C   . SER B 7   ? 2.1690 2.0026 1.8119 -0.3059 0.1431  -0.2227 7   SER B C   
2051 O O   . SER B 7   ? 2.2252 2.0511 1.8684 -0.3136 0.1504  -0.2289 7   SER B O   
2052 C CB  . SER B 7   ? 1.9167 1.7213 1.5923 -0.2751 0.1424  -0.2164 7   SER B CB  
2053 O OG  . SER B 7   ? 1.8305 1.6285 1.5207 -0.2571 0.1363  -0.2090 7   SER B OG  
2054 N N   . GLU B 8   ? 2.2088 2.0619 1.8371 -0.3160 0.1384  -0.2209 8   GLU B N   
2055 C CA  . GLU B 8   ? 2.1120 1.9765 1.7237 -0.3372 0.1435  -0.2273 8   GLU B CA  
2056 C C   . GLU B 8   ? 2.0523 1.9382 1.6576 -0.3506 0.1325  -0.2234 8   GLU B C   
2057 O O   . GLU B 8   ? 1.8963 1.7781 1.4957 -0.3641 0.1411  -0.2315 8   GLU B O   
2058 C CB  . GLU B 8   ? 2.0465 1.9280 1.6457 -0.3436 0.1402  -0.2247 8   GLU B CB  
2059 C CG  . GLU B 8   ? 2.0076 1.9060 1.6101 -0.3321 0.1238  -0.2114 8   GLU B CG  
2060 C CD  . GLU B 8   ? 1.9959 1.9268 1.5930 -0.3406 0.1053  -0.1998 8   GLU B CD  
2061 O OE1 . GLU B 8   ? 2.0127 1.9552 1.6015 -0.3572 0.1053  -0.2023 8   GLU B OE1 
2062 O OE2 . GLU B 8   ? 1.9338 1.8791 1.5356 -0.3310 0.0914  -0.1878 8   GLU B OE2 
2063 N N   . LEU B 9   ? 2.1528 2.0619 1.7597 -0.3472 0.1140  -0.2106 9   LEU B N   
2064 C CA  . LEU B 9   ? 2.1132 2.0446 1.7171 -0.3574 0.1019  -0.2041 9   LEU B CA  
2065 C C   . LEU B 9   ? 2.0967 2.0092 1.7133 -0.3497 0.1053  -0.2074 9   LEU B C   
2066 O O   . LEU B 9   ? 2.0679 1.9675 1.6986 -0.3320 0.1026  -0.2037 9   LEU B O   
2067 C CB  . LEU B 9   ? 1.9947 1.9555 1.5996 -0.3536 0.0823  -0.1882 9   LEU B CB  
2068 C CG  . LEU B 9   ? 1.8345 1.8245 1.4395 -0.3611 0.0663  -0.1764 9   LEU B CG  
2069 C CD1 . LEU B 9   ? 1.7362 1.7142 1.3564 -0.3471 0.0619  -0.1739 9   LEU B CD1 
2070 C CD2 . LEU B 9   ? 1.8281 1.8309 1.4213 -0.3828 0.0695  -0.1808 9   LEU B CD2 
2071 N N   . PRO B 10  ? 2.0605 1.9714 1.6723 -0.3630 0.1112  -0.2138 10  PRO B N   
2072 C CA  . PRO B 10  ? 2.0796 1.9665 1.7034 -0.3558 0.1193  -0.2194 10  PRO B CA  
2073 C C   . PRO B 10  ? 2.1092 2.0000 1.7464 -0.3437 0.1065  -0.2100 10  PRO B C   
2074 O O   . PRO B 10  ? 2.1091 2.0208 1.7476 -0.3396 0.0907  -0.1986 10  PRO B O   
2075 C CB  . PRO B 10  ? 2.0539 1.9447 1.6661 -0.3761 0.1265  -0.2273 10  PRO B CB  
2076 C CG  . PRO B 10  ? 2.0162 1.9190 1.6117 -0.3912 0.1307  -0.2311 10  PRO B CG  
2077 C CD  . PRO B 10  ? 2.0315 1.9573 1.6260 -0.3857 0.1151  -0.2188 10  PRO B CD  
2078 N N   . MET B 11  ? 2.0182 1.8882 1.6662 -0.3382 0.1141  -0.2148 11  MET B N   
2079 C CA  . MET B 11  ? 1.8674 1.7350 1.5300 -0.3260 0.1053  -0.2078 11  MET B CA  
2080 C C   . MET B 11  ? 1.8095 1.6775 1.4722 -0.3355 0.1066  -0.2105 11  MET B C   
2081 O O   . MET B 11  ? 1.8254 1.6766 1.4857 -0.3425 0.1216  -0.2209 11  MET B O   
2082 C CB  . MET B 11  ? 1.7704 1.6091 1.4497 -0.3065 0.1145  -0.2098 11  MET B CB  
2083 C CG  . MET B 11  ? 1.6938 1.5258 1.3740 -0.2966 0.1177  -0.2095 11  MET B CG  
2084 S SD  . MET B 11  ? 1.5836 1.4265 1.2715 -0.2812 0.1015  -0.1972 11  MET B SD  
2085 C CE  . MET B 11  ? 1.5676 1.4404 1.2374 -0.2930 0.0914  -0.1926 11  MET B CE  
2086 N N   . PRO B 12  ? 1.7250 1.6110 1.3913 -0.3364 0.0923  -0.2016 12  PRO B N   
2087 C CA  . PRO B 12  ? 1.6333 1.5123 1.3059 -0.3391 0.0945  -0.2036 12  PRO B CA  
2088 C C   . PRO B 12  ? 1.6037 1.4534 1.2939 -0.3218 0.1031  -0.2060 12  PRO B C   
2089 O O   . PRO B 12  ? 1.6108 1.4505 1.3095 -0.3069 0.1034  -0.2033 12  PRO B O   
2090 C CB  . PRO B 12  ? 1.5772 1.4845 1.2513 -0.3417 0.0758  -0.1913 12  PRO B CB  
2091 C CG  . PRO B 12  ? 1.5479 1.4669 1.2244 -0.3317 0.0652  -0.1825 12  PRO B CG  
2092 C CD  . PRO B 12  ? 1.6665 1.5806 1.3325 -0.3345 0.0737  -0.1885 12  PRO B CD  
2093 N N   . SER B 13  ? 1.6352 1.4717 1.3313 -0.3242 0.1106  -0.2105 13  SER B N   
2094 C CA  . SER B 13  ? 1.6460 1.4578 1.3606 -0.3087 0.1176  -0.2104 13  SER B CA  
2095 C C   . SER B 13  ? 1.6214 1.4437 1.3444 -0.3062 0.1050  -0.2022 13  SER B C   
2096 O O   . SER B 13  ? 1.7019 1.5220 1.4263 -0.3136 0.1078  -0.2046 13  SER B O   
2097 C CB  . SER B 13  ? 1.6366 1.4239 1.3543 -0.3117 0.1369  -0.2208 13  SER B CB  
2098 O OG  . SER B 13  ? 1.5965 1.3671 1.3145 -0.3068 0.1504  -0.2266 13  SER B OG  
2099 N N   . PRO B 14  ? 1.5023 1.3359 1.2313 -0.2965 0.0917  -0.1926 14  PRO B N   
2100 C CA  . PRO B 14  ? 1.5288 1.3786 1.2633 -0.2974 0.0783  -0.1842 14  PRO B CA  
2101 C C   . PRO B 14  ? 1.5838 1.4142 1.3343 -0.2889 0.0839  -0.1841 14  PRO B C   
2102 O O   . PRO B 14  ? 1.6398 1.4493 1.4028 -0.2743 0.0925  -0.1839 14  PRO B O   
2103 C CB  . PRO B 14  ? 1.4339 1.3025 1.1750 -0.2833 0.0650  -0.1703 14  PRO B CB  
2104 C CG  . PRO B 14  ? 1.4019 1.2526 1.1459 -0.2715 0.0734  -0.1734 14  PRO B CG  
2105 C CD  . PRO B 14  ? 1.4411 1.2727 1.1727 -0.2842 0.0890  -0.1891 14  PRO B CD  
2106 N N   . ALA B 15  ? 1.5741 1.4142 1.3259 -0.2970 0.0789  -0.1818 15  ALA B N   
2107 C CA  . ALA B 15  ? 1.5912 1.4146 1.3569 -0.2922 0.0852  -0.1819 15  ALA B CA  
2108 C C   . ALA B 15  ? 1.5971 1.4369 1.3794 -0.2764 0.0726  -0.1653 15  ALA B C   
2109 O O   . ALA B 15  ? 1.6581 1.5250 1.4381 -0.2785 0.0590  -0.1563 15  ALA B O   
2110 C CB  . ALA B 15  ? 1.5010 1.3255 1.2601 -0.3076 0.0905  -0.1880 15  ALA B CB  
2111 N N   . SER B 16  ? 1.5376 1.3614 1.3372 -0.2611 0.0777  -0.1608 16  SER B N   
2112 C CA  . SER B 16  ? 1.4371 1.2735 1.2526 -0.2439 0.0676  -0.1457 16  SER B CA  
2113 C C   . SER B 16  ? 1.5232 1.3806 1.3402 -0.2498 0.0573  -0.1388 16  SER B C   
2114 O O   . SER B 16  ? 1.4676 1.3488 1.2852 -0.2460 0.0450  -0.1290 16  SER B O   
2115 C CB  . SER B 16  ? 1.2139 1.0296 1.0462 -0.2294 0.0760  -0.1429 16  SER B CB  
2116 O OG  . SER B 16  ? 1.1461 0.9561 0.9840 -0.2148 0.0773  -0.1392 16  SER B OG  
2117 N N   . GLU B 17  ? 1.6279 1.4766 1.4465 -0.2591 0.0628  -0.1434 17  GLU B N   
2118 C CA  . GLU B 17  ? 1.6802 1.5488 1.5003 -0.2663 0.0537  -0.1373 17  GLU B CA  
2119 C C   . GLU B 17  ? 1.6616 1.5481 1.4641 -0.2877 0.0487  -0.1426 17  GLU B C   
2120 O O   . GLU B 17  ? 1.7149 1.6151 1.5167 -0.2986 0.0438  -0.1404 17  GLU B O   
2121 C CB  . GLU B 17  ? 1.6407 1.4941 1.4708 -0.2673 0.0612  -0.1388 17  GLU B CB  
2122 C CG  . GLU B 17  ? 1.5608 1.4124 1.4101 -0.2469 0.0591  -0.1266 17  GLU B CG  
2123 C CD  . GLU B 17  ? 1.5166 1.3431 1.3749 -0.2347 0.0704  -0.1285 17  GLU B CD  
2124 O OE1 . GLU B 17  ? 1.5001 1.3064 1.3524 -0.2425 0.0823  -0.1400 17  GLU B OE1 
2125 O OE2 . GLU B 17  ? 1.4336 1.2612 1.3051 -0.2178 0.0677  -0.1183 17  GLU B OE2 
2126 N N   . GLU B 18  ? 1.6530 1.5409 1.4418 -0.2942 0.0496  -0.1489 18  GLU B N   
2127 C CA  . GLU B 18  ? 1.6348 1.5463 1.4074 -0.3121 0.0420  -0.1502 18  GLU B CA  
2128 C C   . GLU B 18  ? 1.6887 1.6239 1.4626 -0.3025 0.0302  -0.1380 18  GLU B C   
2129 O O   . GLU B 18  ? 1.6648 1.6284 1.4335 -0.3122 0.0196  -0.1309 18  GLU B O   
2130 C CB  . GLU B 18  ? 1.6543 1.5503 1.4076 -0.3302 0.0532  -0.1677 18  GLU B CB  
2131 C CG  . GLU B 18  ? 1.6744 1.5684 1.4213 -0.3448 0.0602  -0.1743 18  GLU B CG  
2132 C CD  . GLU B 18  ? 1.7239 1.5933 1.4631 -0.3480 0.0779  -0.1877 18  GLU B CD  
2133 O OE1 . GLU B 18  ? 1.7307 1.5783 1.4763 -0.3475 0.0899  -0.1939 18  GLU B OE1 
2134 O OE2 . GLU B 18  ? 1.7559 1.6282 1.4834 -0.3511 0.0803  -0.1915 18  GLU B OE2 
2135 N N   . VAL B 19  ? 1.7473 1.6719 1.5289 -0.2840 0.0322  -0.1348 19  VAL B N   
2136 C CA  . VAL B 19  ? 1.5613 1.5060 1.3485 -0.2716 0.0217  -0.1217 19  VAL B CA  
2137 C C   . VAL B 19  ? 1.4566 1.4179 1.2599 -0.2605 0.0126  -0.1072 19  VAL B C   
2138 O O   . VAL B 19  ? 1.3873 1.3730 1.1949 -0.2565 0.0025  -0.0950 19  VAL B O   
2139 C CB  . VAL B 19  ? 1.3706 1.2977 1.1619 -0.2557 0.0272  -0.1231 19  VAL B CB  
2140 C CG1 . VAL B 19  ? 1.2695 1.2119 1.0727 -0.2382 0.0179  -0.1087 19  VAL B CG1 
2141 C CG2 . VAL B 19  ? 1.2941 1.2147 1.0687 -0.2665 0.0330  -0.1339 19  VAL B CG2 
2142 N N   . GLY B 20  ? 1.4143 1.3632 1.2274 -0.2557 0.0166  -0.1077 20  GLY B N   
2143 C CA  . GLY B 20  ? 1.3984 1.3623 1.2254 -0.2479 0.0094  -0.0956 20  GLY B CA  
2144 C C   . GLY B 20  ? 1.4391 1.4276 1.2628 -0.2631 0.0018  -0.0910 20  GLY B C   
2145 O O   . GLY B 20  ? 1.3788 1.3844 1.2146 -0.2562 -0.0051 -0.0789 20  GLY B O   
2146 N N   . ALA B 21  ? 1.4815 1.4728 1.2892 -0.2839 0.0034  -0.1002 21  ALA B N   
2147 C CA  . ALA B 21  ? 1.4739 1.4929 1.2764 -0.3009 -0.0050 -0.0952 21  ALA B CA  
2148 C C   . ALA B 21  ? 1.4979 1.5446 1.2961 -0.3036 -0.0146 -0.0858 21  ALA B C   
2149 O O   . ALA B 21  ? 1.4345 1.5101 1.2410 -0.3038 -0.0245 -0.0714 21  ALA B O   
2150 C CB  . ALA B 21  ? 1.5391 1.5484 1.3254 -0.3243 0.0016  -0.1103 21  ALA B CB  
2151 N N   . LEU B 22  ? 1.5990 1.6378 1.3856 -0.3055 -0.0111 -0.0928 22  LEU B N   
2152 C CA  . LEU B 22  ? 1.6121 1.6752 1.3964 -0.3052 -0.0194 -0.0828 22  LEU B CA  
2153 C C   . LEU B 22  ? 1.6479 1.7246 1.4523 -0.2842 -0.0263 -0.0653 22  LEU B C   
2154 O O   . LEU B 22  ? 1.6954 1.7995 1.5033 -0.2845 -0.0349 -0.0521 22  LEU B O   
2155 C CB  . LEU B 22  ? 1.5222 1.5685 1.2937 -0.3053 -0.0128 -0.0933 22  LEU B CB  
2156 C CG  . LEU B 22  ? 1.4668 1.5317 1.2346 -0.3037 -0.0188 -0.0853 22  LEU B CG  
2157 C CD1 . LEU B 22  ? 1.4081 1.5122 1.1729 -0.3177 -0.0306 -0.0725 22  LEU B CD1 
2158 C CD2 . LEU B 22  ? 1.4652 1.5103 1.2160 -0.3104 -0.0098 -0.1004 22  LEU B CD2 
2159 N N   . TYR B 23  ? 1.6695 1.7278 1.4875 -0.2663 -0.0221 -0.0647 23  TYR B N   
2160 C CA  . TYR B 23  ? 1.5935 1.6601 1.4295 -0.2463 -0.0263 -0.0508 23  TYR B CA  
2161 C C   . TYR B 23  ? 1.5767 1.6492 1.4277 -0.2396 -0.0283 -0.0428 23  TYR B C   
2162 O O   . TYR B 23  ? 1.5649 1.6509 1.4308 -0.2265 -0.0324 -0.0297 23  TYR B O   
2163 C CB  . TYR B 23  ? 1.5472 1.5894 1.3860 -0.2296 -0.0199 -0.0557 23  TYR B CB  
2164 C CG  . TYR B 23  ? 1.5706 1.6152 1.4018 -0.2291 -0.0205 -0.0560 23  TYR B CG  
2165 C CD1 . TYR B 23  ? 1.5986 1.6338 1.4121 -0.2427 -0.0160 -0.0683 23  TYR B CD1 
2166 C CD2 . TYR B 23  ? 1.5016 1.5569 1.3436 -0.2152 -0.0246 -0.0442 23  TYR B CD2 
2167 C CE1 . TYR B 23  ? 1.5542 1.5923 1.3607 -0.2424 -0.0165 -0.0683 23  TYR B CE1 
2168 C CE2 . TYR B 23  ? 1.4297 1.4874 1.2657 -0.2146 -0.0252 -0.0437 23  TYR B CE2 
2169 C CZ  . TYR B 23  ? 1.4765 1.5263 1.2945 -0.2281 -0.0215 -0.0555 23  TYR B CZ  
2170 O OH  . TYR B 23  ? 1.4245 1.4773 1.2361 -0.2279 -0.0219 -0.0550 23  TYR B OH  
2171 N N   . ASP B 24  ? 1.5285 1.5913 1.3767 -0.2482 -0.0247 -0.0502 24  ASP B N   
2172 C CA  . ASP B 24  ? 1.4756 1.5538 1.3357 -0.2482 -0.0289 -0.0409 24  ASP B CA  
2173 C C   . ASP B 24  ? 1.5037 1.6169 1.3646 -0.2597 -0.0385 -0.0290 24  ASP B C   
2174 O O   . ASP B 24  ? 1.4169 1.5494 1.2924 -0.2548 -0.0434 -0.0158 24  ASP B O   
2175 C CB  . ASP B 24  ? 1.4150 1.4776 1.2709 -0.2581 -0.0234 -0.0511 24  ASP B CB  
2176 C CG  . ASP B 24  ? 1.3521 1.3935 1.2191 -0.2423 -0.0173 -0.0524 24  ASP B CG  
2177 O OD1 . ASP B 24  ? 1.3662 1.4100 1.2449 -0.2251 -0.0188 -0.0439 24  ASP B OD1 
2178 O OD2 . ASP B 24  ? 1.3140 1.3367 1.1782 -0.2476 -0.0107 -0.0616 24  ASP B OD2 
2179 N N   . ARG B 25  ? 1.6095 1.7320 1.4553 -0.2753 -0.0410 -0.0329 25  ARG B N   
2180 C CA  . ARG B 25  ? 1.6562 1.8146 1.5017 -0.2868 -0.0507 -0.0203 25  ARG B CA  
2181 C C   . ARG B 25  ? 1.7672 1.9406 1.6242 -0.2722 -0.0551 -0.0058 25  ARG B C   
2182 O O   . ARG B 25  ? 1.8036 2.0063 1.6746 -0.2700 -0.0623 0.0118  25  ARG B O   
2183 C CB  . ARG B 25  ? 1.6301 1.7912 1.4526 -0.3106 -0.0507 -0.0317 25  ARG B CB  
2184 C CG  . ARG B 25  ? 1.5826 1.7827 1.4007 -0.3292 -0.0610 -0.0205 25  ARG B CG  
2185 C CD  . ARG B 25  ? 1.5883 1.7853 1.3802 -0.3547 -0.0587 -0.0361 25  ARG B CD  
2186 N NE  . ARG B 25  ? 1.5603 1.7198 1.3417 -0.3581 -0.0469 -0.0571 25  ARG B NE  
2187 C CZ  . ARG B 25  ? 1.4560 1.5905 1.2210 -0.3631 -0.0380 -0.0740 25  ARG B CZ  
2188 N NH1 . ARG B 25  ? 1.3458 1.4468 1.1052 -0.3648 -0.0264 -0.0909 25  ARG B NH1 
2189 N NH2 . ARG B 25  ? 1.4908 1.6339 1.2460 -0.3659 -0.0400 -0.0732 25  ARG B NH2 
2190 N N   . PHE B 26  ? 1.8561 2.0106 1.7086 -0.2625 -0.0504 -0.0122 26  PHE B N   
2191 C CA  . PHE B 26  ? 1.8127 1.9801 1.6747 -0.2502 -0.0539 0.0005  26  PHE B CA  
2192 C C   . PHE B 26  ? 1.8394 1.9992 1.7214 -0.2262 -0.0513 0.0089  26  PHE B C   
2193 O O   . PHE B 26  ? 1.8698 2.0494 1.7659 -0.2178 -0.0553 0.0245  26  PHE B O   
2194 C CB  . PHE B 26  ? 1.6908 1.8456 1.5366 -0.2542 -0.0508 -0.0097 26  PHE B CB  
2195 C CG  . PHE B 26  ? 1.5951 1.7787 1.4331 -0.2684 -0.0580 -0.0017 26  PHE B CG  
2196 C CD1 . PHE B 26  ? 1.5564 1.7676 1.3903 -0.2869 -0.0650 0.0043  26  PHE B CD1 
2197 C CD2 . PHE B 26  ? 1.5623 1.7469 1.3971 -0.2638 -0.0581 0.0007  26  PHE B CD2 
2198 C CE1 . PHE B 26  ? 1.5339 1.7745 1.3602 -0.3012 -0.0723 0.0130  26  PHE B CE1 
2199 C CE2 . PHE B 26  ? 1.5652 1.7783 1.3929 -0.2772 -0.0651 0.0093  26  PHE B CE2 
2200 C CZ  . PHE B 26  ? 1.5621 1.8040 1.3853 -0.2962 -0.0723 0.0157  26  PHE B CZ  
2201 N N   . THR B 27  ? 1.8245 1.9568 1.7084 -0.2158 -0.0443 -0.0008 27  THR B N   
2202 C CA  . THR B 27  ? 1.7153 1.8402 1.6160 -0.1951 -0.0414 0.0055  27  THR B CA  
2203 C C   . THR B 27  ? 1.7599 1.9003 1.6729 -0.1954 -0.0440 0.0147  27  THR B C   
2204 O O   . THR B 27  ? 1.7262 1.8550 1.6469 -0.1862 -0.0401 0.0131  27  THR B O   
2205 C CB  . THR B 27  ? 1.5297 1.6218 1.4260 -0.1862 -0.0335 -0.0081 27  THR B CB  
2206 O OG1 . THR B 27  ? 1.6407 1.7232 1.5347 -0.1917 -0.0310 -0.0149 27  THR B OG1 
2207 C CG2 . THR B 27  ? 1.3665 1.4431 1.2472 -0.1915 -0.0306 -0.0195 27  THR B CG2 
2208 N N   . ALA B 28  ? 1.8110 1.9799 1.7255 -0.2069 -0.0509 0.0251  28  ALA B N   
2209 C CA  . ALA B 28  ? 1.7790 1.9668 1.7055 -0.2089 -0.0541 0.0353  28  ALA B CA  
2210 C C   . ALA B 28  ? 1.9380 2.1573 1.8623 -0.2229 -0.0623 0.0462  28  ALA B C   
2211 O O   . ALA B 28  ? 2.0257 2.2442 1.9329 -0.2356 -0.0640 0.0387  28  ALA B O   
2212 C CB  . ALA B 28  ? 1.6788 1.8540 1.5965 -0.2189 -0.0520 0.0238  28  ALA B CB  
2213 N N   . LEU B 29  ? 1.9981 2.2459 1.9404 -0.2200 -0.0670 0.0648  29  LEU B N   
2214 C CA  . LEU B 29  ? 1.9844 2.2691 1.9286 -0.2335 -0.0759 0.0797  29  LEU B CA  
2215 C C   . LEU B 29  ? 2.0088 2.3032 1.9511 -0.2323 -0.0784 0.0861  29  LEU B C   
2216 O O   . LEU B 29  ? 2.0162 2.3314 1.9474 -0.2491 -0.0850 0.0893  29  LEU B O   
2217 C CB  . LEU B 29  ? 1.8666 2.1593 1.7918 -0.2582 -0.0805 0.0709  29  LEU B CB  
2218 C CG  . LEU B 29  ? 1.7630 2.0514 1.6895 -0.2638 -0.0794 0.0661  29  LEU B CG  
2219 C CD1 . LEU B 29  ? 1.6960 1.9887 1.6474 -0.2456 -0.0770 0.0788  29  LEU B CD1 
2220 C CD2 . LEU B 29  ? 1.7404 1.9915 1.6488 -0.2673 -0.0719 0.0427  29  LEU B CD2 
2221 N N   . GLY B 30  ? 1.9905 2.2704 1.9426 -0.2134 -0.0732 0.0880  30  GLY B N   
2222 C CA  . GLY B 30  ? 1.9785 2.2710 1.9312 -0.2124 -0.0760 0.0968  30  GLY B CA  
2223 C C   . GLY B 30  ? 1.9818 2.2510 1.9216 -0.2079 -0.0718 0.0848  30  GLY B C   
2224 O O   . GLY B 30  ? 1.9864 2.2690 1.9319 -0.2044 -0.0739 0.0959  30  GLY B O   
2225 N N   . ALA B 31  ? 1.9406 2.1771 1.8639 -0.2086 -0.0661 0.0639  31  ALA B N   
2226 C CA  . ALA B 31  ? 1.8070 2.0207 1.7206 -0.2023 -0.0614 0.0535  31  ALA B CA  
2227 C C   . ALA B 31  ? 1.7864 1.9762 1.7123 -0.1820 -0.0541 0.0505  31  ALA B C   
2228 O O   . ALA B 31  ? 1.7886 1.9630 1.7145 -0.1716 -0.0502 0.0471  31  ALA B O   
2229 C CB  . ALA B 31  ? 1.7233 1.9169 1.6123 -0.2158 -0.0588 0.0333  31  ALA B CB  
2230 N N   . ALA B 32  ? 1.7432 1.9313 1.6798 -0.1767 -0.0524 0.0522  32  ALA B N   
2231 C CA  . ALA B 32  ? 1.6648 1.8304 1.6107 -0.1595 -0.0452 0.0480  32  ALA B CA  
2232 C C   . ALA B 32  ? 1.7655 1.9365 1.7241 -0.1556 -0.0442 0.0532  32  ALA B C   
2233 O O   . ALA B 32  ? 1.8339 2.0010 1.7844 -0.1649 -0.0449 0.0456  32  ALA B O   
2234 C CB  . ALA B 32  ? 1.5701 1.7049 1.4993 -0.1607 -0.0403 0.0286  32  ALA B CB  
2235 N N   . SER B 33  ? 1.7560 1.9361 1.7352 -0.1423 -0.0417 0.0661  33  SER B N   
2236 C CA  . SER B 33  ? 1.7236 1.9054 1.7135 -0.1384 -0.0394 0.0688  33  SER B CA  
2237 C C   . SER B 33  ? 1.7559 1.9135 1.7513 -0.1228 -0.0307 0.0619  33  SER B C   
2238 O O   . SER B 33  ? 1.6568 1.7959 1.6428 -0.1240 -0.0281 0.0494  33  SER B O   
2239 C CB  . SER B 33  ? 1.5250 1.7388 1.5354 -0.1376 -0.0426 0.0894  33  SER B CB  
2240 O OG  . SER B 33  ? 1.3539 1.5924 1.3587 -0.1549 -0.0513 0.0952  33  SER B OG  
2241 N N   . LEU B 34  ? 1.7603 1.9168 1.7696 -0.1092 -0.0258 0.0690  34  LEU B N   
2242 C CA  . LEU B 34  ? 1.6676 1.8089 1.6862 -0.0958 -0.0173 0.0661  34  LEU B CA  
2243 C C   . LEU B 34  ? 1.6320 1.7601 1.6544 -0.0844 -0.0116 0.0650  34  LEU B C   
2244 O O   . LEU B 34  ? 1.6720 1.8111 1.7118 -0.0764 -0.0084 0.0775  34  LEU B O   
2245 C CB  . LEU B 34  ? 1.5433 1.7035 1.5818 -0.0917 -0.0153 0.0798  34  LEU B CB  
2246 C CG  . LEU B 34  ? 1.4161 1.6013 1.4779 -0.0860 -0.0146 0.1001  34  LEU B CG  
2247 C CD1 . LEU B 34  ? 1.4002 1.5997 1.4786 -0.0832 -0.0119 0.1099  34  LEU B CD1 
2248 C CD2 . LEU B 34  ? 1.1721 1.3815 1.2329 -0.0963 -0.0238 0.1110  34  LEU B CD2 
2249 N N   . GLY B 35  ? 1.5239 1.6284 1.5312 -0.0838 -0.0098 0.0502  35  GLY B N   
2250 C CA  . GLY B 35  ? 1.3424 1.4321 1.3504 -0.0747 -0.0047 0.0467  35  GLY B CA  
2251 C C   . GLY B 35  ? 1.1810 1.2719 1.1814 -0.0785 -0.0088 0.0469  35  GLY B C   
2252 O O   . GLY B 35  ? 1.1599 1.2478 1.1680 -0.0705 -0.0051 0.0508  35  GLY B O   
2253 N N   . GLU B 36  ? 1.1604 1.2548 1.1459 -0.0908 -0.0154 0.0422  36  GLU B N   
2254 C CA  . GLU B 36  ? 1.1662 1.2633 1.1431 -0.0960 -0.0191 0.0421  36  GLU B CA  
2255 C C   . GLU B 36  ? 1.0162 1.0900 0.9752 -0.0986 -0.0178 0.0261  36  GLU B C   
2256 O O   . GLU B 36  ? 0.9813 1.0437 0.9297 -0.1039 -0.0176 0.0157  36  GLU B O   
2257 C CB  . GLU B 36  ? 1.2605 1.3815 1.2334 -0.1097 -0.0270 0.0495  36  GLU B CB  
2258 C CG  . GLU B 36  ? 1.2885 1.4193 1.2579 -0.1133 -0.0305 0.0548  36  GLU B CG  
2259 C CD  . GLU B 36  ? 1.3818 1.5431 1.3523 -0.1255 -0.0382 0.0672  36  GLU B CD  
2260 O OE1 . GLU B 36  ? 1.4490 1.6198 1.4166 -0.1348 -0.0416 0.0670  36  GLU B OE1 
2261 O OE2 . GLU B 36  ? 1.3543 1.5311 1.3292 -0.1262 -0.0411 0.0780  36  GLU B OE2 
2262 N N   . ASN B 37  ? 0.8796 0.9470 0.8365 -0.0947 -0.0166 0.0253  37  ASN B N   
2263 C CA  . ASN B 37  ? 0.9381 0.9870 0.8791 -0.0978 -0.0157 0.0124  37  ASN B CA  
2264 C C   . ASN B 37  ? 0.9971 1.0550 0.9244 -0.1122 -0.0208 0.0101  37  ASN B C   
2265 O O   . ASN B 37  ? 0.8912 0.9682 0.8204 -0.1169 -0.0250 0.0196  37  ASN B O   
2266 C CB  . ASN B 37  ? 0.9745 1.0146 0.9191 -0.0888 -0.0124 0.0129  37  ASN B CB  
2267 C CG  . ASN B 37  ? 0.9557 0.9785 0.9062 -0.0777 -0.0061 0.0081  37  ASN B CG  
2268 O OD1 . ASN B 37  ? 0.9939 1.0024 0.9374 -0.0781 -0.0042 -0.0017 37  ASN B OD1 
2269 N ND2 . ASN B 37  ? 0.9512 0.9758 0.9148 -0.0684 -0.0024 0.0153  37  ASN B ND2 
2270 N N   . LEU B 38  ? 1.0562 1.1012 0.9701 -0.1197 -0.0200 -0.0021 38  LEU B N   
2271 C CA  . LEU B 38  ? 0.8966 0.9459 0.7954 -0.1342 -0.0227 -0.0072 38  LEU B CA  
2272 C C   . LEU B 38  ? 0.9761 1.0115 0.8650 -0.1337 -0.0199 -0.0148 38  LEU B C   
2273 O O   . LEU B 38  ? 0.9820 1.0020 0.8582 -0.1399 -0.0167 -0.0269 38  LEU B O   
2274 C CB  . LEU B 38  ? 0.7653 0.8067 0.6557 -0.1433 -0.0216 -0.0165 38  LEU B CB  
2275 C CG  . LEU B 38  ? 0.9103 0.9644 0.8120 -0.1421 -0.0239 -0.0087 38  LEU B CG  
2276 C CD1 . LEU B 38  ? 0.8484 0.8918 0.7438 -0.1490 -0.0218 -0.0179 38  LEU B CD1 
2277 C CD2 . LEU B 38  ? 0.8066 0.8899 0.7131 -0.1494 -0.0305 0.0043  38  LEU B CD2 
2278 N N   . HIS B 39  ? 0.9140 0.9540 0.8098 -0.1258 -0.0203 -0.0074 39  HIS B N   
2279 C CA  . HIS B 39  ? 1.0054 1.0343 0.8925 -0.1256 -0.0179 -0.0135 39  HIS B CA  
2280 C C   . HIS B 39  ? 0.9916 1.0340 0.8867 -0.1206 -0.0201 -0.0019 39  HIS B C   
2281 O O   . HIS B 39  ? 0.9882 1.0440 0.8984 -0.1139 -0.0217 0.0106  39  HIS B O   
2282 C CB  . HIS B 39  ? 0.9272 0.9305 0.8138 -0.1164 -0.0119 -0.0234 39  HIS B CB  
2283 C CG  . HIS B 39  ? 0.9073 0.9066 0.8082 -0.1030 -0.0100 -0.0185 39  HIS B CG  
2284 N ND1 . HIS B 39  ? 0.9529 0.9484 0.8596 -0.0995 -0.0087 -0.0195 39  HIS B ND1 
2285 C CD2 . HIS B 39  ? 0.8660 0.8635 0.7757 -0.0930 -0.0083 -0.0136 39  HIS B CD2 
2286 C CE1 . HIS B 39  ? 1.0001 0.9920 0.9177 -0.0885 -0.0061 -0.0158 39  HIS B CE1 
2287 N NE2 . HIS B 39  ? 0.8818 0.8744 0.8017 -0.0844 -0.0056 -0.0124 39  HIS B NE2 
2288 N N   . PHE B 40  ? 0.8238 0.8615 0.7092 -0.1236 -0.0192 -0.0059 40  PHE B N   
2289 C CA  . PHE B 40  ? 0.7929 0.8412 0.6836 -0.1199 -0.0207 0.0038  40  PHE B CA  
2290 C C   . PHE B 40  ? 0.8392 0.8809 0.7469 -0.1043 -0.0175 0.0099  40  PHE B C   
2291 O O   . PHE B 40  ? 0.9239 0.9481 0.8349 -0.0966 -0.0134 0.0031  40  PHE B O   
2292 C CB  . PHE B 40  ? 0.7958 0.8336 0.6725 -0.1243 -0.0184 -0.0050 40  PHE B CB  
2293 C CG  . PHE B 40  ? 0.8429 0.8888 0.7021 -0.1409 -0.0204 -0.0105 40  PHE B CG  
2294 C CD1 . PHE B 40  ? 0.8865 0.9179 0.7337 -0.1485 -0.0169 -0.0244 40  PHE B CD1 
2295 C CD2 . PHE B 40  ? 0.9433 1.0117 0.7982 -0.1498 -0.0251 -0.0017 40  PHE B CD2 
2296 C CE1 . PHE B 40  ? 1.0014 1.0382 0.8315 -0.1651 -0.0173 -0.0312 40  PHE B CE1 
2297 C CE2 . PHE B 40  ? 0.9644 1.0405 0.8011 -0.1670 -0.0265 -0.0080 40  PHE B CE2 
2298 C CZ  . PHE B 40  ? 0.9959 1.0553 0.8198 -0.1750 -0.0221 -0.0237 40  PHE B CZ  
2299 N N   . GLY B 41  ? 0.7702 0.8267 0.6887 -0.1003 -0.0191 0.0232  41  GLY B N   
2300 C CA  . GLY B 41  ? 0.7178 0.7665 0.6513 -0.0866 -0.0147 0.0281  41  GLY B CA  
2301 C C   . GLY B 41  ? 0.7187 0.7535 0.6463 -0.0837 -0.0119 0.0224  41  GLY B C   
2302 O O   . GLY B 41  ? 0.7616 0.7978 0.6757 -0.0919 -0.0137 0.0181  41  GLY B O   
2303 N N   . TYR B 42  ? 0.8063 0.8275 0.7439 -0.0724 -0.0068 0.0218  42  TYR B N   
2304 C CA  . TYR B 42  ? 0.9143 0.9231 0.8493 -0.0686 -0.0039 0.0179  42  TYR B CA  
2305 C C   . TYR B 42  ? 0.9606 0.9749 0.9132 -0.0596 -0.0012 0.0302  42  TYR B C   
2306 O O   . TYR B 42  ? 0.9642 0.9769 0.9308 -0.0522 0.0024  0.0343  42  TYR B O   
2307 C CB  . TYR B 42  ? 0.8114 0.7967 0.7405 -0.0648 0.0003  0.0041  42  TYR B CB  
2308 C CG  . TYR B 42  ? 0.7285 0.7016 0.6534 -0.0624 0.0028  -0.0007 42  TYR B CG  
2309 C CD1 . TYR B 42  ? 0.7581 0.7278 0.6941 -0.0545 0.0061  0.0045  42  TYR B CD1 
2310 C CD2 . TYR B 42  ? 0.7427 0.7078 0.6531 -0.0683 0.0027  -0.0102 42  TYR B CD2 
2311 C CE1 . TYR B 42  ? 0.7549 0.7142 0.6871 -0.0528 0.0082  0.0003  42  TYR B CE1 
2312 C CE2 . TYR B 42  ? 0.7242 0.6792 0.6316 -0.0660 0.0052  -0.0139 42  TYR B CE2 
2313 C CZ  . TYR B 42  ? 0.7576 0.7104 0.6756 -0.0585 0.0074  -0.0085 42  TYR B CZ  
2314 O OH  . TYR B 42  ? 0.8195 0.7631 0.7345 -0.0569 0.0096  -0.0119 42  TYR B OH  
2315 N N   . TRP B 43  ? 1.0481 1.0689 1.0004 -0.0607 -0.0022 0.0362  43  TRP B N   
2316 C CA  . TRP B 43  ? 0.9694 0.9964 0.9393 -0.0528 0.0006  0.0493  43  TRP B CA  
2317 C C   . TRP B 43  ? 0.9962 1.0093 0.9634 -0.0493 0.0039  0.0447  43  TRP B C   
2318 O O   . TRP B 43  ? 0.9716 0.9817 0.9236 -0.0556 0.0017  0.0377  43  TRP B O   
2319 C CB  . TRP B 43  ? 0.8661 0.9206 0.8423 -0.0574 -0.0044 0.0661  43  TRP B CB  
2320 C CG  . TRP B 43  ? 0.8599 0.9312 0.8453 -0.0586 -0.0069 0.0753  43  TRP B CG  
2321 C CD1 . TRP B 43  ? 0.8648 0.9439 0.8726 -0.0501 -0.0032 0.0886  43  TRP B CD1 
2322 C CD2 . TRP B 43  ? 0.7946 0.8774 0.7681 -0.0694 -0.0129 0.0723  43  TRP B CD2 
2323 N NE1 . TRP B 43  ? 0.8913 0.9873 0.9024 -0.0544 -0.0071 0.0948  43  TRP B NE1 
2324 C CE2 . TRP B 43  ? 0.7507 0.8495 0.7405 -0.0667 -0.0135 0.0849  43  TRP B CE2 
2325 C CE3 . TRP B 43  ? 0.7492 0.8297 0.7005 -0.0812 -0.0169 0.0602  43  TRP B CE3 
2326 C CZ2 . TRP B 43  ? 0.6996 0.8131 0.6837 -0.0759 -0.0190 0.0859  43  TRP B CZ2 
2327 C CZ3 . TRP B 43  ? 0.7003 0.7939 0.6456 -0.0906 -0.0216 0.0603  43  TRP B CZ3 
2328 C CH2 . TRP B 43  ? 0.6381 0.7484 0.5994 -0.0881 -0.0231 0.0731  43  TRP B CH2 
2329 N N   . ASP B 44  ? 1.0714 1.0762 1.0540 -0.0397 0.0100  0.0489  44  ASP B N   
2330 C CA  . ASP B 44  ? 1.1196 1.1102 1.1013 -0.0362 0.0137  0.0444  44  ASP B CA  
2331 C C   . ASP B 44  ? 1.0998 1.1031 1.0802 -0.0394 0.0108  0.0535  44  ASP B C   
2332 O O   . ASP B 44  ? 1.0741 1.0678 1.0461 -0.0404 0.0116  0.0472  44  ASP B O   
2333 C CB  . ASP B 44  ? 1.1662 1.1454 1.1651 -0.0265 0.0218  0.0468  44  ASP B CB  
2334 C CG  . ASP B 44  ? 1.1918 1.1525 1.1863 -0.0247 0.0255  0.0331  44  ASP B CG  
2335 O OD1 . ASP B 44  ? 1.0987 1.0501 1.0773 -0.0292 0.0229  0.0209  44  ASP B OD1 
2336 O OD2 . ASP B 44  ? 1.2758 1.2324 1.2830 -0.0192 0.0313  0.0349  44  ASP B OD2 
2337 N N   . SER B 45  ? 1.0995 1.1255 1.0889 -0.0410 0.0076  0.0693  45  SER B N   
2338 C CA  . SER B 45  ? 1.1917 1.2342 1.1804 -0.0449 0.0042  0.0804  45  SER B CA  
2339 C C   . SER B 45  ? 1.2443 1.3142 1.2319 -0.0530 -0.0027 0.0917  45  SER B C   
2340 O O   . SER B 45  ? 1.2271 1.3051 1.2257 -0.0507 -0.0029 0.0982  45  SER B O   
2341 C CB  . SER B 45  ? 1.2403 1.2834 1.2499 -0.0357 0.0096  0.0936  45  SER B CB  
2342 O OG  . SER B 45  ? 1.3320 1.4005 1.3480 -0.0389 0.0055  0.1115  45  SER B OG  
2343 N N   . PRO B 46  ? 1.2685 1.3538 1.2427 -0.0631 -0.0083 0.0945  46  PRO B N   
2344 C CA  . PRO B 46  ? 1.2454 1.3585 1.2161 -0.0732 -0.0155 0.1046  46  PRO B CA  
2345 C C   . PRO B 46  ? 1.3160 1.4517 1.3115 -0.0677 -0.0162 0.1275  46  PRO B C   
2346 O O   . PRO B 46  ? 1.3699 1.5297 1.3664 -0.0749 -0.0221 0.1375  46  PRO B O   
2347 C CB  . PRO B 46  ? 1.1738 1.2978 1.1263 -0.0846 -0.0197 0.1036  46  PRO B CB  
2348 C CG  . PRO B 46  ? 1.2124 1.3091 1.1544 -0.0813 -0.0145 0.0873  46  PRO B CG  
2349 C CD  . PRO B 46  ? 1.2601 1.3401 1.2220 -0.0665 -0.0081 0.0895  46  PRO B CD  
2350 N N   . ASP B 47  ? 1.3256 1.4538 1.3419 -0.0552 -0.0097 0.1363  47  ASP B N   
2351 C CA  . ASP B 47  ? 1.3489 1.4961 1.3926 -0.0481 -0.0080 0.1589  47  ASP B CA  
2352 C C   . ASP B 47  ? 1.3253 1.4585 1.3865 -0.0372 -0.0006 0.1575  47  ASP B C   
2353 O O   . ASP B 47  ? 1.2953 1.4429 1.3814 -0.0304 0.0023  0.1760  47  ASP B O   
2354 C CB  . ASP B 47  ? 1.3976 1.5481 1.4557 -0.0419 -0.0044 0.1724  47  ASP B CB  
2355 C CG  . ASP B 47  ? 1.5360 1.7193 1.6163 -0.0408 -0.0069 0.2003  47  ASP B CG  
2356 O OD1 . ASP B 47  ? 1.5443 1.7559 1.6157 -0.0525 -0.0162 0.2087  47  ASP B OD1 
2357 O OD2 . ASP B 47  ? 1.6480 1.8295 1.7551 -0.0289 0.0007  0.2142  47  ASP B OD2 
2358 N N   . SER B 48  ? 1.2925 1.3988 1.3421 -0.0355 0.0029  0.1367  48  SER B N   
2359 C CA  . SER B 48  ? 1.2167 1.3114 1.2789 -0.0276 0.0092  0.1336  48  SER B CA  
2360 C C   . SER B 48  ? 1.2368 1.3549 1.3047 -0.0317 0.0042  0.1442  48  SER B C   
2361 O O   . SER B 48  ? 1.3652 1.4988 1.4167 -0.0434 -0.0048 0.1428  48  SER B O   
2362 C CB  . SER B 48  ? 1.1274 1.1940 1.1720 -0.0282 0.0116  0.1098  48  SER B CB  
2363 O OG  . SER B 48  ? 1.0206 1.0792 1.0737 -0.0230 0.0164  0.1062  48  SER B OG  
2364 N N   . GLN B 49  ? 1.0637 1.1844 1.1553 -0.0224 0.0107  0.1549  49  GLN B N   
2365 C CA  . GLN B 49  ? 1.0781 1.2221 1.1781 -0.0255 0.0064  0.1665  49  GLN B CA  
2366 C C   . GLN B 49  ? 1.0697 1.1977 1.1752 -0.0194 0.0131  0.1573  49  GLN B C   
2367 O O   . GLN B 49  ? 1.0212 1.1605 1.1481 -0.0135 0.0171  0.1705  49  GLN B O   
2368 C CB  . GLN B 49  ? 1.2306 1.4031 1.3568 -0.0216 0.0065  0.1943  49  GLN B CB  
2369 C CG  . GLN B 49  ? 1.3763 1.5677 1.4935 -0.0299 -0.0015 0.2032  49  GLN B CG  
2370 C CD  . GLN B 49  ? 1.5023 1.7184 1.6477 -0.0241 0.0002  0.2313  49  GLN B CD  
2371 O OE1 . GLN B 49  ? 1.5655 1.7698 1.7345 -0.0110 0.0110  0.2386  49  GLN B OE1 
2372 N NE2 . GLN B 49  ? 1.5425 1.7937 1.6857 -0.0345 -0.0102 0.2478  49  GLN B NE2 
2373 N N   . VAL B 50  ? 1.0638 1.1659 1.1498 -0.0211 0.0144  0.1348  50  VAL B N   
2374 C CA  . VAL B 50  ? 1.0241 1.1139 1.1073 -0.0196 0.0175  0.1233  50  VAL B CA  
2375 C C   . VAL B 50  ? 0.9827 1.0948 1.0602 -0.0287 0.0087  0.1283  50  VAL B C   
2376 O O   . VAL B 50  ? 0.9409 1.0659 1.0019 -0.0399 -0.0006 0.1276  50  VAL B O   
2377 C CB  . VAL B 50  ? 1.0177 1.0797 1.0790 -0.0218 0.0186  0.0998  50  VAL B CB  
2378 C CG1 . VAL B 50  ? 1.0092 1.0600 1.0672 -0.0209 0.0215  0.0890  50  VAL B CG1 
2379 C CG2 . VAL B 50  ? 0.9012 0.9427 0.9666 -0.0146 0.0265  0.0949  50  VAL B CG2 
2380 N N   . PRO B 51  ? 0.9616 1.0795 1.0517 -0.0253 0.0116  0.1332  51  PRO B N   
2381 C CA  . PRO B 51  ? 0.9005 1.0392 0.9839 -0.0351 0.0028  0.1368  51  PRO B CA  
2382 C C   . PRO B 51  ? 0.9381 1.0630 0.9929 -0.0451 -0.0026 0.1161  51  PRO B C   
2383 O O   . PRO B 51  ? 1.0186 1.1177 1.0617 -0.0427 0.0013  0.0995  51  PRO B O   
2384 C CB  . PRO B 51  ? 0.7989 0.9390 0.9012 -0.0275 0.0094  0.1424  51  PRO B CB  
2385 C CG  . PRO B 51  ? 0.8992 1.0282 1.0238 -0.0138 0.0215  0.1490  51  PRO B CG  
2386 C CD  . PRO B 51  ? 0.9457 1.0514 1.0561 -0.0132 0.0235  0.1351  51  PRO B CD  
2387 N N   . LEU B 52  ? 0.8810 1.0241 0.9252 -0.0570 -0.0114 0.1178  52  LEU B N   
2388 C CA  . LEU B 52  ? 0.7725 0.9030 0.7909 -0.0671 -0.0157 0.0990  52  LEU B CA  
2389 C C   . LEU B 52  ? 0.8982 1.0047 0.9133 -0.0618 -0.0100 0.0842  52  LEU B C   
2390 O O   . LEU B 52  ? 0.9208 1.0057 0.9196 -0.0633 -0.0088 0.0675  52  LEU B O   
2391 C CB  . LEU B 52  ? 0.6968 0.8510 0.7064 -0.0812 -0.0247 0.1036  52  LEU B CB  
2392 C CG  . LEU B 52  ? 0.7072 0.8445 0.6930 -0.0903 -0.0265 0.0835  52  LEU B CG  
2393 C CD1 . LEU B 52  ? 0.7380 0.8611 0.7070 -0.0936 -0.0264 0.0725  52  LEU B CD1 
2394 C CD2 . LEU B 52  ? 0.6905 0.8485 0.6682 -0.1046 -0.0339 0.0861  52  LEU B CD2 
2395 N N   . ALA B 53  ? 0.8833 0.9945 0.9143 -0.0557 -0.0062 0.0907  53  ALA B N   
2396 C CA  . ALA B 53  ? 0.8438 0.9357 0.8706 -0.0525 -0.0015 0.0774  53  ALA B CA  
2397 C C   . ALA B 53  ? 0.9040 0.9686 0.9257 -0.0454 0.0053  0.0645  53  ALA B C   
2398 O O   . ALA B 53  ? 0.9368 0.9840 0.9436 -0.0479 0.0055  0.0492  53  ALA B O   
2399 C CB  . ALA B 53  ? 0.6483 0.7495 0.6955 -0.0456 0.0033  0.0879  53  ALA B CB  
2400 N N   . GLU B 54  ? 0.8107 0.8722 0.8450 -0.0372 0.0107  0.0710  54  GLU B N   
2401 C CA  . GLU B 54  ? 0.7289 0.7658 0.7597 -0.0311 0.0176  0.0594  54  GLU B CA  
2402 C C   . GLU B 54  ? 0.8072 0.8342 0.8189 -0.0369 0.0131  0.0489  54  GLU B C   
2403 O O   . GLU B 54  ? 0.8702 0.8769 0.8723 -0.0356 0.0161  0.0356  54  GLU B O   
2404 C CB  . GLU B 54  ? 0.8289 0.8651 0.8806 -0.0210 0.0260  0.0699  54  GLU B CB  
2405 C CG  . GLU B 54  ? 0.9249 0.9368 0.9747 -0.0154 0.0340  0.0588  54  GLU B CG  
2406 C CD  . GLU B 54  ? 1.0808 1.0916 1.1525 -0.0060 0.0434  0.0695  54  GLU B CD  
2407 O OE1 . GLU B 54  ? 1.1267 1.1539 1.2183 -0.0018 0.0459  0.0855  54  GLU B OE1 
2408 O OE2 . GLU B 54  ? 1.0521 1.0460 1.1219 -0.0031 0.0485  0.0627  54  GLU B OE2 
2409 N N   . ALA B 55  ? 0.8019 0.8437 0.8072 -0.0442 0.0059  0.0547  55  ALA B N   
2410 C CA  . ALA B 55  ? 0.8255 0.8579 0.8124 -0.0502 0.0026  0.0443  55  ALA B CA  
2411 C C   . ALA B 55  ? 0.8764 0.9010 0.8457 -0.0581 -0.0007 0.0310  55  ALA B C   
2412 O O   . ALA B 55  ? 0.8071 0.8159 0.7634 -0.0599 -0.0002 0.0192  55  ALA B O   
2413 C CB  . ALA B 55  ? 0.8039 0.8546 0.7891 -0.0561 -0.0029 0.0544  55  ALA B CB  
2414 N N   . THR B 56  ? 0.8669 0.9028 0.8365 -0.0629 -0.0038 0.0335  56  THR B N   
2415 C CA  . THR B 56  ? 0.8322 0.8591 0.7875 -0.0695 -0.0056 0.0212  56  THR B CA  
2416 C C   . THR B 56  ? 0.7823 0.7880 0.7370 -0.0628 0.0000  0.0108  56  THR B C   
2417 O O   . THR B 56  ? 0.7033 0.6943 0.6458 -0.0652 0.0004  -0.0005 56  THR B O   
2418 C CB  . THR B 56  ? 0.8462 0.8901 0.8038 -0.0758 -0.0096 0.0270  56  THR B CB  
2419 O OG1 . THR B 56  ? 0.8291 0.8787 0.8042 -0.0677 -0.0061 0.0355  56  THR B OG1 
2420 C CG2 . THR B 56  ? 0.9232 0.9898 0.8786 -0.0851 -0.0160 0.0366  56  THR B CG2 
2421 N N   . ASP B 57  ? 0.7966 0.8011 0.7649 -0.0545 0.0049  0.0149  57  ASP B N   
2422 C CA  . ASP B 57  ? 0.8026 0.7886 0.7693 -0.0494 0.0102  0.0051  57  ASP B CA  
2423 C C   . ASP B 57  ? 0.7388 0.7104 0.7006 -0.0466 0.0127  -0.0011 57  ASP B C   
2424 O O   . ASP B 57  ? 0.8093 0.7662 0.7643 -0.0458 0.0149  -0.0108 57  ASP B O   
2425 C CB  . ASP B 57  ? 0.7830 0.7697 0.7646 -0.0417 0.0166  0.0098  57  ASP B CB  
2426 C CG  . ASP B 57  ? 0.8861 0.8843 0.8725 -0.0438 0.0152  0.0142  57  ASP B CG  
2427 O OD1 . ASP B 57  ? 0.9393 0.9409 0.9152 -0.0515 0.0098  0.0105  57  ASP B OD1 
2428 O OD2 . ASP B 57  ? 0.8623 0.8658 0.8637 -0.0378 0.0204  0.0214  57  ASP B OD2 
2429 N N   . ARG B 58  ? 0.5974 0.5739 0.5630 -0.0453 0.0122  0.0052  58  ARG B N   
2430 C CA  . ARG B 58  ? 0.6889 0.6517 0.6499 -0.0430 0.0145  -0.0008 58  ARG B CA  
2431 C C   . ARG B 58  ? 0.7167 0.6719 0.6616 -0.0492 0.0110  -0.0104 58  ARG B C   
2432 O O   . ARG B 58  ? 0.7347 0.6756 0.6745 -0.0476 0.0133  -0.0185 58  ARG B O   
2433 C CB  . ARG B 58  ? 0.6393 0.6089 0.6082 -0.0403 0.0150  0.0084  58  ARG B CB  
2434 C CG  . ARG B 58  ? 0.7277 0.6818 0.6918 -0.0380 0.0178  0.0012  58  ARG B CG  
2435 C CD  . ARG B 58  ? 0.9286 0.8840 0.9029 -0.0332 0.0209  0.0086  58  ARG B CD  
2436 N NE  . ARG B 58  ? 1.1081 1.0502 1.0749 -0.0332 0.0220  0.0011  58  ARG B NE  
2437 C CZ  . ARG B 58  ? 1.1489 1.0922 1.1197 -0.0314 0.0228  0.0063  58  ARG B CZ  
2438 N NH1 . ARG B 58  ? 1.1098 1.0673 1.0920 -0.0295 0.0225  0.0193  58  ARG B NH1 
2439 N NH2 . ARG B 58  ? 1.1296 1.0615 1.0941 -0.0315 0.0238  -0.0004 58  ARG B NH2 
2440 N N   . LEU B 59  ? 0.6605 0.6252 0.5978 -0.0569 0.0061  -0.0094 59  LEU B N   
2441 C CA  . LEU B 59  ? 0.7357 0.6919 0.6588 -0.0630 0.0046  -0.0189 59  LEU B CA  
2442 C C   . LEU B 59  ? 0.7760 0.7211 0.6964 -0.0624 0.0064  -0.0266 59  LEU B C   
2443 O O   . LEU B 59  ? 0.6585 0.5907 0.5729 -0.0620 0.0082  -0.0339 59  LEU B O   
2444 C CB  . LEU B 59  ? 0.5934 0.5616 0.5086 -0.0727 0.0002  -0.0172 59  LEU B CB  
2445 C CG  . LEU B 59  ? 0.6946 0.6511 0.5961 -0.0787 0.0011  -0.0278 59  LEU B CG  
2446 C CD1 . LEU B 59  ? 0.6854 0.6325 0.5844 -0.0755 0.0035  -0.0306 59  LEU B CD1 
2447 C CD2 . LEU B 59  ? 0.6259 0.5917 0.5173 -0.0903 -0.0018 -0.0290 59  LEU B CD2 
2448 N N   . THR B 60  ? 0.5443 0.4955 0.4701 -0.0620 0.0062  -0.0239 60  THR B N   
2449 C CA  . THR B 60  ? 0.6220 0.5642 0.5465 -0.0607 0.0082  -0.0298 60  THR B CA  
2450 C C   . THR B 60  ? 0.7152 0.6453 0.6412 -0.0548 0.0120  -0.0338 60  THR B C   
2451 O O   . THR B 60  ? 0.6851 0.6055 0.6053 -0.0557 0.0127  -0.0400 60  THR B O   
2452 C CB  . THR B 60  ? 0.6944 0.6453 0.6265 -0.0596 0.0084  -0.0252 60  THR B CB  
2453 O OG1 . THR B 60  ? 0.7663 0.7302 0.6971 -0.0662 0.0043  -0.0209 60  THR B OG1 
2454 C CG2 . THR B 60  ? 0.7059 0.6481 0.6357 -0.0589 0.0104  -0.0312 60  THR B CG2 
2455 N N   . ASP B 61  ? 0.6380 0.5692 0.5726 -0.0493 0.0149  -0.0298 61  ASP B N   
2456 C CA  . ASP B 61  ? 0.6020 0.5222 0.5375 -0.0452 0.0191  -0.0344 61  ASP B CA  
2457 C C   . ASP B 61  ? 0.6349 0.5468 0.5636 -0.0463 0.0183  -0.0387 61  ASP B C   
2458 O O   . ASP B 61  ? 0.6564 0.5602 0.5810 -0.0465 0.0193  -0.0441 61  ASP B O   
2459 C CB  . ASP B 61  ? 0.4508 0.3720 0.3974 -0.0396 0.0240  -0.0299 61  ASP B CB  
2460 C CG  . ASP B 61  ? 0.5676 0.4946 0.5225 -0.0374 0.0271  -0.0265 61  ASP B CG  
2461 O OD1 . ASP B 61  ? 0.6465 0.5770 0.5981 -0.0403 0.0249  -0.0278 61  ASP B OD1 
2462 O OD2 . ASP B 61  ? 0.7381 0.6657 0.7040 -0.0325 0.0326  -0.0222 61  ASP B OD2 
2463 N N   . MET B 62  ? 0.6991 0.6146 0.6268 -0.0474 0.0164  -0.0356 62  MET B N   
2464 C CA  . MET B 62  ? 0.6248 0.5334 0.5460 -0.0488 0.0159  -0.0392 62  MET B CA  
2465 C C   . MET B 62  ? 0.7140 0.6164 0.6277 -0.0522 0.0151  -0.0451 62  MET B C   
2466 O O   . MET B 62  ? 0.7626 0.6572 0.6744 -0.0513 0.0164  -0.0487 62  MET B O   
2467 C CB  . MET B 62  ? 0.7134 0.6296 0.6330 -0.0513 0.0136  -0.0348 62  MET B CB  
2468 C CG  . MET B 62  ? 0.9259 0.8370 0.8411 -0.0518 0.0140  -0.0367 62  MET B CG  
2469 S SD  . MET B 62  ? 0.9742 0.8997 0.8904 -0.0544 0.0113  -0.0282 62  MET B SD  
2470 C CE  . MET B 62  ? 0.9536 0.8852 0.8851 -0.0477 0.0133  -0.0198 62  MET B CE  
2471 N N   . MET B 63  ? 0.6114 0.5181 0.5222 -0.0563 0.0133  -0.0454 63  MET B N   
2472 C CA  . MET B 63  ? 0.6776 0.5776 0.5830 -0.0594 0.0138  -0.0503 63  MET B CA  
2473 C C   . MET B 63  ? 0.7383 0.6347 0.6463 -0.0572 0.0149  -0.0518 63  MET B C   
2474 O O   . MET B 63  ? 0.7598 0.6499 0.6663 -0.0575 0.0159  -0.0542 63  MET B O   
2475 C CB  . MET B 63  ? 0.6669 0.5713 0.5680 -0.0656 0.0123  -0.0508 63  MET B CB  
2476 C CG  . MET B 63  ? 0.6748 0.5828 0.5702 -0.0704 0.0114  -0.0507 63  MET B CG  
2477 S SD  . MET B 63  ? 0.7936 0.7111 0.6840 -0.0795 0.0091  -0.0506 63  MET B SD  
2478 C CE  . MET B 63  ? 0.4934 0.3970 0.3773 -0.0844 0.0133  -0.0590 63  MET B CE  
2479 N N   . ALA B 64  ? 0.7384 0.6398 0.6508 -0.0553 0.0150  -0.0497 64  ALA B N   
2480 C CA  . ALA B 64  ? 0.7176 0.6166 0.6309 -0.0543 0.0162  -0.0514 64  ALA B CA  
2481 C C   . ALA B 64  ? 0.6379 0.5312 0.5508 -0.0524 0.0177  -0.0535 64  ALA B C   
2482 O O   . ALA B 64  ? 0.6568 0.5478 0.5682 -0.0535 0.0178  -0.0547 64  ALA B O   
2483 C CB  . ALA B 64  ? 0.5464 0.4513 0.4644 -0.0527 0.0174  -0.0494 64  ALA B CB  
2484 N N   . GLU B 65  ? 0.5442 0.4360 0.4590 -0.0501 0.0189  -0.0531 65  GLU B N   
2485 C CA  . GLU B 65  ? 0.5995 0.4863 0.5135 -0.0494 0.0202  -0.0553 65  GLU B CA  
2486 C C   . GLU B 65  ? 0.6251 0.5086 0.5363 -0.0509 0.0188  -0.0557 65  GLU B C   
2487 O O   . GLU B 65  ? 0.6952 0.5773 0.6060 -0.0516 0.0190  -0.0563 65  GLU B O   
2488 C CB  . GLU B 65  ? 0.6798 0.5647 0.5969 -0.0469 0.0222  -0.0546 65  GLU B CB  
2489 C CG  . GLU B 65  ? 1.0170 0.8997 0.9328 -0.0466 0.0210  -0.0536 65  GLU B CG  
2490 C CD  . GLU B 65  ? 1.2031 1.0826 1.1219 -0.0446 0.0232  -0.0535 65  GLU B CD  
2491 O OE1 . GLU B 65  ? 1.1932 1.0716 1.1159 -0.0432 0.0264  -0.0540 65  GLU B OE1 
2492 O OE2 . GLU B 65  ? 1.3378 1.2151 1.2554 -0.0446 0.0225  -0.0529 65  GLU B OE2 
2493 N N   . ARG B 66  ? 0.6063 0.4890 0.5158 -0.0520 0.0180  -0.0551 66  ARG B N   
2494 C CA  . ARG B 66  ? 0.5621 0.4403 0.4706 -0.0528 0.0187  -0.0555 66  ARG B CA  
2495 C C   . ARG B 66  ? 0.6141 0.4922 0.5238 -0.0541 0.0188  -0.0547 66  ARG B C   
2496 O O   . ARG B 66  ? 0.7329 0.6084 0.6447 -0.0539 0.0199  -0.0533 66  ARG B O   
2497 C CB  . ARG B 66  ? 0.6114 0.4873 0.5170 -0.0543 0.0194  -0.0563 66  ARG B CB  
2498 C CG  . ARG B 66  ? 0.6066 0.4821 0.5119 -0.0527 0.0196  -0.0558 66  ARG B CG  
2499 C CD  . ARG B 66  ? 0.5631 0.4407 0.4644 -0.0553 0.0195  -0.0560 66  ARG B CD  
2500 N NE  . ARG B 66  ? 0.6954 0.5724 0.5963 -0.0541 0.0201  -0.0550 66  ARG B NE  
2501 C CZ  . ARG B 66  ? 0.6898 0.5718 0.5927 -0.0525 0.0189  -0.0518 66  ARG B CZ  
2502 N NH1 . ARG B 66  ? 0.7544 0.6424 0.6608 -0.0515 0.0175  -0.0491 66  ARG B NH1 
2503 N NH2 . ARG B 66  ? 0.6137 0.4950 0.5163 -0.0516 0.0197  -0.0506 66  ARG B NH2 
2504 N N   . LEU B 67  ? 0.5796 0.4614 0.4892 -0.0553 0.0180  -0.0546 67  LEU B N   
2505 C CA  . LEU B 67  ? 0.5637 0.4466 0.4751 -0.0566 0.0181  -0.0528 67  LEU B CA  
2506 C C   . LEU B 67  ? 0.5891 0.4751 0.5020 -0.0563 0.0175  -0.0509 67  LEU B C   
2507 O O   . LEU B 67  ? 0.6654 0.5531 0.5812 -0.0572 0.0175  -0.0475 67  LEU B O   
2508 C CB  . LEU B 67  ? 0.6352 0.5224 0.5462 -0.0580 0.0173  -0.0529 67  LEU B CB  
2509 C CG  . LEU B 67  ? 0.6807 0.5674 0.5898 -0.0599 0.0172  -0.0542 67  LEU B CG  
2510 C CD1 . LEU B 67  ? 0.6905 0.5840 0.6002 -0.0608 0.0160  -0.0534 67  LEU B CD1 
2511 C CD2 . LEU B 67  ? 0.5634 0.4447 0.4728 -0.0624 0.0192  -0.0546 67  LEU B CD2 
2512 N N   . ARG B 68  ? 0.6028 0.4903 0.5140 -0.0559 0.0172  -0.0528 68  ARG B N   
2513 C CA  . ARG B 68  ? 0.5834 0.4749 0.4940 -0.0577 0.0166  -0.0521 68  ARG B CA  
2514 C C   . ARG B 68  ? 0.6426 0.5403 0.5524 -0.0603 0.0160  -0.0506 68  ARG B C   
2515 O O   . ARG B 68  ? 0.7315 0.6340 0.6432 -0.0621 0.0147  -0.0463 68  ARG B O   
2516 C CB  . ARG B 68  ? 0.6082 0.4999 0.5216 -0.0579 0.0160  -0.0487 68  ARG B CB  
2517 C CG  . ARG B 68  ? 0.7265 0.6123 0.6405 -0.0555 0.0170  -0.0500 68  ARG B CG  
2518 C CD  . ARG B 68  ? 0.8001 0.6870 0.7178 -0.0556 0.0168  -0.0463 68  ARG B CD  
2519 N NE  . ARG B 68  ? 1.0782 0.9593 0.9963 -0.0532 0.0182  -0.0477 68  ARG B NE  
2520 C CZ  . ARG B 68  ? 1.1980 1.0795 1.1176 -0.0533 0.0181  -0.0466 68  ARG B CZ  
2521 N NH1 . ARG B 68  ? 1.0900 0.9782 1.0104 -0.0563 0.0163  -0.0443 68  ARG B NH1 
2522 N NH2 . ARG B 68  ? 1.2310 1.1075 1.1508 -0.0511 0.0197  -0.0478 68  ARG B NH2 
2523 N N   . ILE B 69  ? 0.6476 0.5463 0.5555 -0.0604 0.0170  -0.0533 69  ILE B N   
2524 C CA  . ILE B 69  ? 0.6867 0.5912 0.5937 -0.0626 0.0169  -0.0522 69  ILE B CA  
2525 C C   . ILE B 69  ? 0.7779 0.6845 0.6812 -0.0644 0.0194  -0.0565 69  ILE B C   
2526 O O   . ILE B 69  ? 0.7786 0.6810 0.6812 -0.0632 0.0218  -0.0603 69  ILE B O   
2527 C CB  . ILE B 69  ? 0.6555 0.5593 0.5648 -0.0613 0.0168  -0.0510 69  ILE B CB  
2528 C CG1 . ILE B 69  ? 0.6809 0.5820 0.5906 -0.0589 0.0180  -0.0537 69  ILE B CG1 
2529 C CG2 . ILE B 69  ? 0.6083 0.5089 0.5209 -0.0610 0.0160  -0.0477 69  ILE B CG2 
2530 C CD1 . ILE B 69  ? 0.6027 0.5069 0.5140 -0.0590 0.0181  -0.0529 69  ILE B CD1 
2531 N N   . GLY B 70  ? 0.7929 0.7056 0.6940 -0.0673 0.0197  -0.0559 70  GLY B N   
2532 C CA  . GLY B 70  ? 0.6574 0.5717 0.5542 -0.0699 0.0235  -0.0608 70  GLY B CA  
2533 C C   . GLY B 70  ? 0.7065 0.6270 0.6025 -0.0716 0.0240  -0.0593 70  GLY B C   
2534 O O   . GLY B 70  ? 0.7124 0.6348 0.6120 -0.0702 0.0214  -0.0546 70  GLY B O   
2535 N N   . ALA B 71  ? 0.6852 0.6084 0.5765 -0.0750 0.0280  -0.0636 71  ALA B N   
2536 C CA  . ALA B 71  ? 0.6650 0.5950 0.5550 -0.0771 0.0288  -0.0620 71  ALA B CA  
2537 C C   . ALA B 71  ? 0.6523 0.5908 0.5415 -0.0806 0.0237  -0.0554 71  ALA B C   
2538 O O   . ALA B 71  ? 0.6821 0.6242 0.5687 -0.0840 0.0211  -0.0535 71  ALA B O   
2539 C CB  . ALA B 71  ? 0.5887 0.5196 0.4724 -0.0813 0.0352  -0.0688 71  ALA B CB  
2540 N N   . GLY B 72  ? 0.7320 0.6742 0.6249 -0.0794 0.0223  -0.0506 72  GLY B N   
2541 C CA  . GLY B 72  ? 0.8663 0.8157 0.7615 -0.0815 0.0183  -0.0426 72  GLY B CA  
2542 C C   . GLY B 72  ? 0.9026 0.8470 0.8051 -0.0779 0.0154  -0.0376 72  GLY B C   
2543 O O   . GLY B 72  ? 0.9522 0.9010 0.8598 -0.0784 0.0135  -0.0301 72  GLY B O   
2544 N N   . SER B 73  ? 0.7300 0.6653 0.6338 -0.0743 0.0158  -0.0412 73  SER B N   
2545 C CA  . SER B 73  ? 0.6818 0.6108 0.5917 -0.0711 0.0146  -0.0380 73  SER B CA  
2546 C C   . SER B 73  ? 0.7490 0.6756 0.6630 -0.0697 0.0151  -0.0366 73  SER B C   
2547 O O   . SER B 73  ? 0.7597 0.6869 0.6722 -0.0695 0.0162  -0.0395 73  SER B O   
2548 C CB  . SER B 73  ? 0.6932 0.6140 0.6024 -0.0682 0.0153  -0.0429 73  SER B CB  
2549 O OG  . SER B 73  ? 0.6510 0.5726 0.5587 -0.0692 0.0144  -0.0426 73  SER B OG  
2550 N N   . ARG B 74  ? 0.7733 0.6970 0.6933 -0.0691 0.0150  -0.0317 74  ARG B N   
2551 C CA  . ARG B 74  ? 0.6722 0.5918 0.5959 -0.0690 0.0161  -0.0310 74  ARG B CA  
2552 C C   . ARG B 74  ? 0.7054 0.6150 0.6295 -0.0676 0.0172  -0.0350 74  ARG B C   
2553 O O   . ARG B 74  ? 0.8699 0.7740 0.7975 -0.0665 0.0186  -0.0333 74  ARG B O   
2554 C CB  . ARG B 74  ? 0.6552 0.5766 0.5860 -0.0700 0.0169  -0.0234 74  ARG B CB  
2555 C CG  . ARG B 74  ? 0.6594 0.5927 0.5908 -0.0721 0.0154  -0.0170 74  ARG B CG  
2556 C CD  . ARG B 74  ? 0.6314 0.5714 0.5591 -0.0743 0.0151  -0.0182 74  ARG B CD  
2557 N NE  . ARG B 74  ? 0.6320 0.5693 0.5645 -0.0747 0.0165  -0.0163 74  ARG B NE  
2558 C CZ  . ARG B 74  ? 0.6452 0.5870 0.5753 -0.0762 0.0165  -0.0179 74  ARG B CZ  
2559 N NH1 . ARG B 74  ? 0.7399 0.6879 0.6634 -0.0769 0.0163  -0.0216 74  ARG B NH1 
2560 N NH2 . ARG B 74  ? 0.5995 0.5393 0.5342 -0.0773 0.0176  -0.0159 74  ARG B NH2 
2561 N N   . VAL B 75  ? 0.6317 0.5399 0.5529 -0.0679 0.0170  -0.0393 75  VAL B N   
2562 C CA  . VAL B 75  ? 0.6334 0.5346 0.5533 -0.0680 0.0177  -0.0430 75  VAL B CA  
2563 C C   . VAL B 75  ? 0.5845 0.4834 0.5057 -0.0716 0.0187  -0.0435 75  VAL B C   
2564 O O   . VAL B 75  ? 0.6902 0.5949 0.6117 -0.0732 0.0178  -0.0426 75  VAL B O   
2565 C CB  . VAL B 75  ? 0.6218 0.5254 0.5382 -0.0665 0.0164  -0.0464 75  VAL B CB  
2566 C CG1 . VAL B 75  ? 0.5258 0.4254 0.4402 -0.0680 0.0164  -0.0491 75  VAL B CG1 
2567 C CG2 . VAL B 75  ? 0.5788 0.4818 0.4938 -0.0639 0.0163  -0.0470 75  VAL B CG2 
2568 N N   . LEU B 76  ? 0.5917 0.4818 0.5133 -0.0733 0.0214  -0.0454 76  LEU B N   
2569 C CA  . LEU B 76  ? 0.6208 0.5072 0.5415 -0.0785 0.0231  -0.0480 76  LEU B CA  
2570 C C   . LEU B 76  ? 0.6616 0.5490 0.5760 -0.0813 0.0215  -0.0526 76  LEU B C   
2571 O O   . LEU B 76  ? 0.7412 0.6243 0.6529 -0.0802 0.0223  -0.0549 76  LEU B O   
2572 C CB  . LEU B 76  ? 0.7151 0.5903 0.6401 -0.0800 0.0287  -0.0480 76  LEU B CB  
2573 C CG  . LEU B 76  ? 0.7389 0.6072 0.6615 -0.0870 0.0321  -0.0529 76  LEU B CG  
2574 C CD1 . LEU B 76  ? 0.6554 0.5302 0.5788 -0.0907 0.0302  -0.0514 76  LEU B CD1 
2575 C CD2 . LEU B 76  ? 0.6883 0.5428 0.6162 -0.0879 0.0400  -0.0536 76  LEU B CD2 
2576 N N   . ASP B 77  ? 0.6347 0.5293 0.5474 -0.0851 0.0191  -0.0528 77  ASP B N   
2577 C CA  . ASP B 77  ? 0.6150 0.5150 0.5227 -0.0885 0.0167  -0.0549 77  ASP B CA  
2578 C C   . ASP B 77  ? 0.6347 0.5300 0.5381 -0.0973 0.0189  -0.0592 77  ASP B C   
2579 O O   . ASP B 77  ? 0.7035 0.6033 0.6071 -0.1026 0.0181  -0.0588 77  ASP B O   
2580 C CB  . ASP B 77  ? 0.6950 0.6079 0.6053 -0.0872 0.0130  -0.0509 77  ASP B CB  
2581 C CG  . ASP B 77  ? 0.7781 0.7006 0.6860 -0.0907 0.0100  -0.0500 77  ASP B CG  
2582 O OD1 . ASP B 77  ? 0.8290 0.7488 0.7313 -0.0948 0.0101  -0.0530 77  ASP B OD1 
2583 O OD2 . ASP B 77  ? 0.8884 0.8223 0.8006 -0.0894 0.0077  -0.0454 77  ASP B OD2 
2584 N N   . LEU B 78  ? 0.6322 0.5179 0.5313 -0.0995 0.0224  -0.0638 78  LEU B N   
2585 C CA  . LEU B 78  ? 0.6830 0.5605 0.5771 -0.1086 0.0269  -0.0698 78  LEU B CA  
2586 C C   . LEU B 78  ? 0.7461 0.6335 0.6320 -0.1171 0.0233  -0.0721 78  LEU B C   
2587 O O   . LEU B 78  ? 0.8651 0.7538 0.7451 -0.1184 0.0227  -0.0741 78  LEU B O   
2588 C CB  . LEU B 78  ? 0.7602 0.6234 0.6535 -0.1075 0.0334  -0.0740 78  LEU B CB  
2589 C CG  . LEU B 78  ? 0.7847 0.6321 0.6787 -0.1125 0.0425  -0.0793 78  LEU B CG  
2590 C CD1 . LEU B 78  ? 0.7530 0.5944 0.6585 -0.1075 0.0460  -0.0744 78  LEU B CD1 
2591 C CD2 . LEU B 78  ? 0.6622 0.4995 0.5541 -0.1110 0.0479  -0.0831 78  LEU B CD2 
2592 N N   . GLY B 79  ? 0.6132 0.5095 0.4989 -0.1231 0.0205  -0.0707 79  GLY B N   
2593 C CA  . GLY B 79  ? 0.5978 0.5067 0.4765 -0.1322 0.0164  -0.0711 79  GLY B CA  
2594 C C   . GLY B 79  ? 0.7777 0.7024 0.6621 -0.1251 0.0100  -0.0626 79  GLY B C   
2595 O O   . GLY B 79  ? 0.8895 0.8163 0.7741 -0.1194 0.0086  -0.0606 79  GLY B O   
2596 N N   . CYS B 80  ? 0.6858 0.6213 0.5758 -0.1253 0.0068  -0.0575 80  CYS B N   
2597 C CA  . CYS B 80  ? 0.6193 0.5653 0.5177 -0.1161 0.0035  -0.0497 80  CYS B CA  
2598 C C   . CYS B 80  ? 0.5729 0.5386 0.4735 -0.1195 -0.0016 -0.0429 80  CYS B C   
2599 O O   . CYS B 80  ? 0.6440 0.6188 0.5535 -0.1121 -0.0031 -0.0359 80  CYS B O   
2600 C CB  . CYS B 80  ? 0.8269 0.7713 0.7323 -0.1115 0.0048  -0.0475 80  CYS B CB  
2601 S SG  . CYS B 80  ? 0.9228 0.8791 0.8299 -0.1212 0.0024  -0.0449 80  CYS B SG  
2602 N N   . GLY B 81  ? 0.6950 0.6679 0.5886 -0.1312 -0.0038 -0.0445 81  GLY B N   
2603 C CA  . GLY B 81  ? 0.6884 0.6832 0.5850 -0.1356 -0.0093 -0.0361 81  GLY B CA  
2604 C C   . GLY B 81  ? 0.7123 0.7176 0.6199 -0.1320 -0.0109 -0.0289 81  GLY B C   
2605 O O   . GLY B 81  ? 0.6663 0.6641 0.5749 -0.1327 -0.0086 -0.0320 81  GLY B O   
2606 N N   . VAL B 82  ? 0.7246 0.7475 0.6417 -0.1276 -0.0141 -0.0183 82  VAL B N   
2607 C CA  . VAL B 82  ? 0.7716 0.8053 0.7008 -0.1229 -0.0145 -0.0104 82  VAL B CA  
2608 C C   . VAL B 82  ? 0.7614 0.7851 0.6984 -0.1090 -0.0099 -0.0101 82  VAL B C   
2609 O O   . VAL B 82  ? 0.8307 0.8627 0.7790 -0.1028 -0.0086 -0.0032 82  VAL B O   
2610 C CB  . VAL B 82  ? 0.8047 0.8640 0.7425 -0.1259 -0.0193 0.0022  82  VAL B CB  
2611 C CG1 . VAL B 82  ? 0.7669 0.8374 0.6949 -0.1418 -0.0243 0.0011  82  VAL B CG1 
2612 C CG2 . VAL B 82  ? 0.8240 0.8886 0.7686 -0.1175 -0.0191 0.0090  82  VAL B CG2 
2613 N N   . GLY B 83  ? 0.7235 0.7299 0.6543 -0.1048 -0.0068 -0.0175 83  GLY B N   
2614 C CA  . GLY B 83  ? 0.7681 0.7628 0.7026 -0.0947 -0.0024 -0.0198 83  GLY B CA  
2615 C C   . GLY B 83  ? 0.8076 0.8023 0.7482 -0.0853 -0.0002 -0.0164 83  GLY B C   
2616 O O   . GLY B 83  ? 0.7114 0.6966 0.6539 -0.0783 0.0038  -0.0192 83  GLY B O   
2617 N N   . THR B 84  ? 0.7660 0.7712 0.7098 -0.0857 -0.0025 -0.0105 84  THR B N   
2618 C CA  . THR B 84  ? 0.7594 0.7649 0.7118 -0.0763 0.0006  -0.0060 84  THR B CA  
2619 C C   . THR B 84  ? 0.7631 0.7510 0.7093 -0.0718 0.0037  -0.0139 84  THR B C   
2620 O O   . THR B 84  ? 0.7458 0.7274 0.6972 -0.0643 0.0085  -0.0147 84  THR B O   
2621 C CB  . THR B 84  ? 0.7332 0.7552 0.6913 -0.0781 -0.0027 0.0037  84  THR B CB  
2622 O OG1 . THR B 84  ? 0.7564 0.7968 0.7234 -0.0810 -0.0050 0.0129  84  THR B OG1 
2623 C CG2 . THR B 84  ? 0.6457 0.6664 0.6137 -0.0685 0.0014  0.0086  84  THR B CG2 
2624 N N   . PRO B 85  ? 0.7184 0.6978 0.6541 -0.0761 0.0020  -0.0201 85  PRO B N   
2625 C CA  . PRO B 85  ? 0.7102 0.6743 0.6418 -0.0713 0.0051  -0.0263 85  PRO B CA  
2626 C C   . PRO B 85  ? 0.7799 0.7340 0.7098 -0.0693 0.0078  -0.0316 85  PRO B C   
2627 O O   . PRO B 85  ? 0.7074 0.6539 0.6383 -0.0639 0.0110  -0.0340 85  PRO B O   
2628 C CB  . PRO B 85  ? 0.5704 0.5293 0.4922 -0.0770 0.0031  -0.0308 85  PRO B CB  
2629 C CG  . PRO B 85  ? 0.6657 0.6392 0.5863 -0.0848 -0.0011 -0.0261 85  PRO B CG  
2630 C CD  . PRO B 85  ? 0.6511 0.6344 0.5780 -0.0859 -0.0020 -0.0217 85  PRO B CD  
2631 N N   . GLY B 86  ? 0.7145 0.6696 0.6421 -0.0742 0.0067  -0.0329 86  GLY B N   
2632 C CA  . GLY B 86  ? 0.5956 0.5427 0.5219 -0.0728 0.0090  -0.0365 86  GLY B CA  
2633 C C   . GLY B 86  ? 0.6760 0.6259 0.6085 -0.0671 0.0122  -0.0344 86  GLY B C   
2634 O O   . GLY B 86  ? 0.6653 0.6079 0.5960 -0.0639 0.0148  -0.0377 86  GLY B O   
2635 N N   . VAL B 87  ? 0.7048 0.6660 0.6449 -0.0661 0.0124  -0.0289 87  VAL B N   
2636 C CA  . VAL B 87  ? 0.7054 0.6679 0.6515 -0.0609 0.0172  -0.0278 87  VAL B CA  
2637 C C   . VAL B 87  ? 0.6882 0.6465 0.6375 -0.0551 0.0211  -0.0281 87  VAL B C   
2638 O O   . VAL B 87  ? 0.7031 0.6564 0.6532 -0.0517 0.0263  -0.0311 87  VAL B O   
2639 C CB  . VAL B 87  ? 0.6604 0.6358 0.6153 -0.0609 0.0178  -0.0212 87  VAL B CB  
2640 C CG1 . VAL B 87  ? 0.6224 0.6029 0.5742 -0.0681 0.0133  -0.0204 87  VAL B CG1 
2641 C CG2 . VAL B 87  ? 0.8484 0.8335 0.8135 -0.0574 0.0186  -0.0137 87  VAL B CG2 
2642 N N   . ARG B 88  ? 0.6373 0.5968 0.5876 -0.0546 0.0190  -0.0258 88  ARG B N   
2643 C CA  . ARG B 88  ? 0.6290 0.5828 0.5824 -0.0494 0.0230  -0.0264 88  ARG B CA  
2644 C C   . ARG B 88  ? 0.7479 0.6887 0.6928 -0.0493 0.0246  -0.0345 88  ARG B C   
2645 O O   . ARG B 88  ? 0.8040 0.7394 0.7506 -0.0461 0.0300  -0.0373 88  ARG B O   
2646 C CB  . ARG B 88  ? 0.5367 0.4947 0.4917 -0.0497 0.0199  -0.0221 88  ARG B CB  
2647 C CG  . ARG B 88  ? 0.5512 0.5032 0.5109 -0.0441 0.0244  -0.0219 88  ARG B CG  
2648 C CD  . ARG B 88  ? 0.5940 0.5526 0.5568 -0.0442 0.0214  -0.0157 88  ARG B CD  
2649 N NE  . ARG B 88  ? 0.6899 0.6425 0.6580 -0.0389 0.0258  -0.0148 88  ARG B NE  
2650 C CZ  . ARG B 88  ? 0.6784 0.6335 0.6601 -0.0328 0.0320  -0.0089 88  ARG B CZ  
2651 N NH1 . ARG B 88  ? 0.5149 0.4791 0.5070 -0.0307 0.0347  -0.0027 88  ARG B NH1 
2652 N NH2 . ARG B 88  ? 0.5283 0.4763 0.5143 -0.0287 0.0363  -0.0088 88  ARG B NH2 
2653 N N   . ILE B 89  ? 0.7590 0.6953 0.6953 -0.0534 0.0204  -0.0379 89  ILE B N   
2654 C CA  . ILE B 89  ? 0.5733 0.4999 0.5031 -0.0537 0.0211  -0.0435 89  ILE B CA  
2655 C C   . ILE B 89  ? 0.6065 0.5323 0.5349 -0.0539 0.0241  -0.0461 89  ILE B C   
2656 O O   . ILE B 89  ? 0.6760 0.5967 0.6016 -0.0532 0.0270  -0.0498 89  ILE B O   
2657 C CB  . ILE B 89  ? 0.6189 0.5417 0.5424 -0.0577 0.0172  -0.0451 89  ILE B CB  
2658 C CG1 . ILE B 89  ? 0.4936 0.4158 0.4163 -0.0579 0.0153  -0.0442 89  ILE B CG1 
2659 C CG2 . ILE B 89  ? 0.5259 0.4417 0.4448 -0.0583 0.0177  -0.0486 89  ILE B CG2 
2660 C CD1 . ILE B 89  ? 0.5522 0.4694 0.4690 -0.0620 0.0133  -0.0467 89  ILE B CD1 
2661 N N   . ALA B 90  ? 0.5721 0.5037 0.5019 -0.0557 0.0235  -0.0441 90  ALA B N   
2662 C CA  . ALA B 90  ? 0.6592 0.5914 0.5870 -0.0567 0.0263  -0.0461 90  ALA B CA  
2663 C C   . ALA B 90  ? 0.7260 0.6584 0.6575 -0.0535 0.0329  -0.0475 90  ALA B C   
2664 O O   . ALA B 90  ? 0.6708 0.6004 0.5978 -0.0547 0.0366  -0.0519 90  ALA B O   
2665 C CB  . ALA B 90  ? 0.6274 0.5660 0.5564 -0.0594 0.0244  -0.0431 90  ALA B CB  
2666 N N   . ARG B 91  ? 0.6747 0.6109 0.6150 -0.0498 0.0352  -0.0437 91  ARG B N   
2667 C CA  . ARG B 91  ? 0.6748 0.6097 0.6214 -0.0460 0.0434  -0.0445 91  ARG B CA  
2668 C C   . ARG B 91  ? 0.7545 0.6798 0.6988 -0.0447 0.0471  -0.0493 91  ARG B C   
2669 O O   . ARG B 91  ? 0.8256 0.7456 0.7679 -0.0450 0.0541  -0.0548 91  ARG B O   
2670 C CB  . ARG B 91  ? 0.6506 0.5936 0.6098 -0.0420 0.0448  -0.0367 91  ARG B CB  
2671 C CG  . ARG B 91  ? 0.6995 0.6418 0.6682 -0.0374 0.0546  -0.0361 91  ARG B CG  
2672 C CD  . ARG B 91  ? 0.7201 0.6734 0.7030 -0.0336 0.0547  -0.0257 91  ARG B CD  
2673 N NE  . ARG B 91  ? 0.6567 0.6112 0.6421 -0.0325 0.0502  -0.0213 91  ARG B NE  
2674 C CZ  . ARG B 91  ? 0.8433 0.7971 0.8401 -0.0271 0.0557  -0.0167 91  ARG B CZ  
2675 N NH1 . ARG B 91  ? 0.9767 0.9275 0.9836 -0.0223 0.0665  -0.0165 91  ARG B NH1 
2676 N NH2 . ARG B 91  ? 0.8710 0.8274 0.8697 -0.0265 0.0512  -0.0120 91  ARG B NH2 
2677 N N   . LEU B 92  ? 0.6773 0.6002 0.6213 -0.0439 0.0429  -0.0478 92  LEU B N   
2678 C CA  . LEU B 92  ? 0.6576 0.5719 0.6009 -0.0425 0.0468  -0.0517 92  LEU B CA  
2679 C C   . LEU B 92  ? 0.6338 0.5422 0.5657 -0.0471 0.0449  -0.0583 92  LEU B C   
2680 O O   . LEU B 92  ? 0.7881 0.6898 0.7176 -0.0479 0.0500  -0.0636 92  LEU B O   
2681 C CB  . LEU B 92  ? 0.6621 0.5769 0.6104 -0.0397 0.0437  -0.0468 92  LEU B CB  
2682 C CG  . LEU B 92  ? 0.6363 0.5581 0.5984 -0.0348 0.0472  -0.0388 92  LEU B CG  
2683 C CD1 . LEU B 92  ? 0.5788 0.5026 0.5460 -0.0325 0.0446  -0.0331 92  LEU B CD1 
2684 C CD2 . LEU B 92  ? 0.4940 0.4114 0.4639 -0.0313 0.0580  -0.0405 92  LEU B CD2 
2685 N N   . SER B 93  ? 0.6056 0.5168 0.5313 -0.0504 0.0384  -0.0577 93  SER B N   
2686 C CA  . SER B 93  ? 0.5837 0.4917 0.5009 -0.0544 0.0363  -0.0615 93  SER B CA  
2687 C C   . SER B 93  ? 0.6361 0.5483 0.5478 -0.0587 0.0367  -0.0633 93  SER B C   
2688 O O   . SER B 93  ? 0.6555 0.5673 0.5605 -0.0628 0.0358  -0.0659 93  SER B O   
2689 C CB  . SER B 93  ? 0.5804 0.4881 0.4959 -0.0550 0.0297  -0.0588 93  SER B CB  
2690 O OG  . SER B 93  ? 0.7092 0.6216 0.6241 -0.0568 0.0263  -0.0559 93  SER B OG  
2691 N N   . GLY B 94  ? 0.5994 0.5170 0.5138 -0.0584 0.0378  -0.0612 94  GLY B N   
2692 C CA  . GLY B 94  ? 0.6754 0.5984 0.5849 -0.0625 0.0376  -0.0615 94  GLY B CA  
2693 C C   . GLY B 94  ? 0.6495 0.5758 0.5563 -0.0652 0.0310  -0.0576 94  GLY B C   
2694 O O   . GLY B 94  ? 0.6876 0.6198 0.5917 -0.0685 0.0305  -0.0562 94  GLY B O   
2695 N N   . ALA B 95  ? 0.6065 0.5292 0.5147 -0.0639 0.0268  -0.0556 95  ALA B N   
2696 C CA  . ALA B 95  ? 0.5938 0.5179 0.5024 -0.0654 0.0224  -0.0514 95  ALA B CA  
2697 C C   . ALA B 95  ? 0.6389 0.5671 0.5508 -0.0658 0.0216  -0.0482 95  ALA B C   
2698 O O   . ALA B 95  ? 0.6635 0.5935 0.5785 -0.0641 0.0232  -0.0483 95  ALA B O   
2699 C CB  . ALA B 95  ? 0.6061 0.5241 0.5165 -0.0635 0.0200  -0.0507 95  ALA B CB  
2700 N N   . HIS B 96  ? 0.6747 0.6047 0.5872 -0.0680 0.0193  -0.0444 96  HIS B N   
2701 C CA  . HIS B 96  ? 0.5999 0.5324 0.5159 -0.0691 0.0186  -0.0413 96  HIS B CA  
2702 C C   . HIS B 96  ? 0.6032 0.5298 0.5218 -0.0689 0.0170  -0.0410 96  HIS B C   
2703 O O   . HIS B 96  ? 0.6800 0.6007 0.5985 -0.0687 0.0164  -0.0409 96  HIS B O   
2704 C CB  . HIS B 96  ? 0.5535 0.4908 0.4701 -0.0718 0.0179  -0.0367 96  HIS B CB  
2705 C CG  . HIS B 96  ? 0.6615 0.6014 0.5819 -0.0733 0.0178  -0.0337 96  HIS B CG  
2706 N ND1 . HIS B 96  ? 0.6882 0.6233 0.6127 -0.0743 0.0171  -0.0313 96  HIS B ND1 
2707 C CD2 . HIS B 96  ? 0.5920 0.5384 0.5130 -0.0741 0.0190  -0.0331 96  HIS B CD2 
2708 C CE1 . HIS B 96  ? 0.5988 0.5375 0.5260 -0.0763 0.0173  -0.0293 96  HIS B CE1 
2709 N NE2 . HIS B 96  ? 0.6655 0.6117 0.5909 -0.0759 0.0182  -0.0299 96  HIS B NE2 
2710 N N   . VAL B 97  ? 0.5968 0.5255 0.5176 -0.0698 0.0167  -0.0407 97  VAL B N   
2711 C CA  . VAL B 97  ? 0.7222 0.6465 0.6434 -0.0715 0.0155  -0.0415 97  VAL B CA  
2712 C C   . VAL B 97  ? 0.5905 0.5161 0.5141 -0.0755 0.0153  -0.0395 97  VAL B C   
2713 O O   . VAL B 97  ? 0.7005 0.6334 0.6262 -0.0764 0.0152  -0.0376 97  VAL B O   
2714 C CB  . VAL B 97  ? 0.6733 0.6009 0.5949 -0.0704 0.0148  -0.0425 97  VAL B CB  
2715 C CG1 . VAL B 97  ? 0.5725 0.4973 0.4925 -0.0742 0.0132  -0.0436 97  VAL B CG1 
2716 C CG2 . VAL B 97  ? 0.5362 0.4614 0.4565 -0.0664 0.0158  -0.0444 97  VAL B CG2 
2717 N N   . THR B 98  ? 0.5402 0.4581 0.4643 -0.0780 0.0163  -0.0398 98  THR B N   
2718 C CA  . THR B 98  ? 0.6086 0.5243 0.5344 -0.0830 0.0171  -0.0396 98  THR B CA  
2719 C C   . THR B 98  ? 0.6586 0.5700 0.5807 -0.0868 0.0169  -0.0440 98  THR B C   
2720 O O   . THR B 98  ? 0.6671 0.5698 0.5873 -0.0864 0.0188  -0.0466 98  THR B O   
2721 C CB  . THR B 98  ? 0.6286 0.5373 0.5586 -0.0837 0.0201  -0.0371 98  THR B CB  
2722 O OG1 . THR B 98  ? 0.6509 0.5647 0.5834 -0.0803 0.0198  -0.0323 98  THR B OG1 
2723 C CG2 . THR B 98  ? 0.6960 0.6036 0.6287 -0.0890 0.0216  -0.0365 98  THR B CG2 
2724 N N   . GLY B 99  ? 0.6916 0.6101 0.6124 -0.0907 0.0148  -0.0443 99  GLY B N   
2725 C CA  . GLY B 99  ? 0.7327 0.6494 0.6488 -0.0968 0.0144  -0.0481 99  GLY B CA  
2726 C C   . GLY B 99  ? 0.7425 0.6560 0.6581 -0.1051 0.0162  -0.0501 99  GLY B C   
2727 O O   . GLY B 99  ? 0.7604 0.6786 0.6799 -0.1066 0.0159  -0.0471 99  GLY B O   
2728 N N   . ILE B 100 ? 0.6530 0.5580 0.5632 -0.1112 0.0187  -0.0556 100 ILE B N   
2729 C CA  . ILE B 100 ? 0.5621 0.4622 0.4701 -0.1211 0.0217  -0.0595 100 ILE B CA  
2730 C C   . ILE B 100 ? 0.7403 0.6475 0.6399 -0.1303 0.0189  -0.0632 100 ILE B C   
2731 O O   . ILE B 100 ? 0.6096 0.5187 0.5044 -0.1292 0.0174  -0.0645 100 ILE B O   
2732 C CB  . ILE B 100 ? 0.5663 0.4483 0.4757 -0.1220 0.0294  -0.0636 100 ILE B CB  
2733 C CG1 . ILE B 100 ? 0.6442 0.5180 0.5467 -0.1238 0.0322  -0.0697 100 ILE B CG1 
2734 C CG2 . ILE B 100 ? 0.6071 0.4854 0.5256 -0.1124 0.0311  -0.0578 100 ILE B CG2 
2735 C CD1 . ILE B 100 ? 0.6312 0.4867 0.5372 -0.1227 0.0411  -0.0730 100 ILE B CD1 
2736 N N   . SER B 101 ? 0.7435 0.6565 0.6416 -0.1398 0.0179  -0.0639 101 SER B N   
2737 C CA  . SER B 101 ? 0.6356 0.5554 0.5246 -0.1518 0.0160  -0.0678 101 SER B CA  
2738 C C   . SER B 101 ? 0.7560 0.6684 0.6421 -0.1638 0.0204  -0.0736 101 SER B C   
2739 O O   . SER B 101 ? 0.7678 0.6749 0.6609 -0.1622 0.0231  -0.0718 101 SER B O   
2740 C CB  . SER B 101 ? 0.6367 0.5790 0.5272 -0.1525 0.0080  -0.0605 101 SER B CB  
2741 O OG  . SER B 101 ? 0.7865 0.7379 0.6680 -0.1657 0.0056  -0.0632 101 SER B OG  
2742 N N   . VAL B 102 ? 0.6619 0.5739 0.5370 -0.1768 0.0216  -0.0807 102 VAL B N   
2743 C CA  . VAL B 102 ? 0.7410 0.6466 0.6119 -0.1907 0.0262  -0.0873 102 VAL B CA  
2744 C C   . VAL B 102 ? 0.8235 0.7506 0.6922 -0.2010 0.0187  -0.0833 102 VAL B C   
2745 O O   . VAL B 102 ? 0.8997 0.8243 0.7667 -0.2122 0.0213  -0.0871 102 VAL B O   
2746 C CB  . VAL B 102 ? 0.8273 0.7165 0.6868 -0.2010 0.0344  -0.0995 102 VAL B CB  
2747 C CG1 . VAL B 102 ? 0.8394 0.7048 0.7058 -0.1920 0.0444  -0.1027 102 VAL B CG1 
2748 C CG2 . VAL B 102 ? 0.6862 0.5850 0.5350 -0.2043 0.0304  -0.1012 102 VAL B CG2 
2749 N N   . SER B 103 ? 0.7802 0.7285 0.6506 -0.1970 0.0100  -0.0747 103 SER B N   
2750 C CA  . SER B 103 ? 0.8878 0.8597 0.7596 -0.2047 0.0024  -0.0678 103 SER B CA  
2751 C C   . SER B 103 ? 0.8755 0.8546 0.7611 -0.1946 0.0000  -0.0584 103 SER B C   
2752 O O   . SER B 103 ? 0.8598 0.8363 0.7535 -0.1796 0.0001  -0.0536 103 SER B O   
2753 C CB  . SER B 103 ? 0.8900 0.8821 0.7586 -0.2055 -0.0048 -0.0618 103 SER B CB  
2754 O OG  . SER B 103 ? 0.8629 0.8791 0.7410 -0.2032 -0.0122 -0.0494 103 SER B OG  
2755 N N   . HIS B 104 ? 0.7504 0.7392 0.6382 -0.2037 -0.0019 -0.0563 104 HIS B N   
2756 C CA  . HIS B 104 ? 0.7968 0.7947 0.6973 -0.1956 -0.0042 -0.0471 104 HIS B CA  
2757 C C   . HIS B 104 ? 0.8883 0.9084 0.7965 -0.1875 -0.0109 -0.0355 104 HIS B C   
2758 O O   . HIS B 104 ? 0.9621 0.9830 0.8804 -0.1741 -0.0104 -0.0295 104 HIS B O   
2759 C CB  . HIS B 104 ? 0.7335 0.7365 0.6344 -0.2084 -0.0043 -0.0477 104 HIS B CB  
2760 C CG  . HIS B 104 ? 0.7151 0.7285 0.6287 -0.2015 -0.0063 -0.0384 104 HIS B CG  
2761 N ND1 . HIS B 104 ? 0.6252 0.6640 0.5462 -0.2012 -0.0130 -0.0275 104 HIS B ND1 
2762 C CD2 . HIS B 104 ? 0.6730 0.6757 0.5938 -0.1954 -0.0020 -0.0377 104 HIS B CD2 
2763 C CE1 . HIS B 104 ? 0.6910 0.7330 0.6224 -0.1951 -0.0122 -0.0217 104 HIS B CE1 
2764 N NE2 . HIS B 104 ? 0.6477 0.6686 0.5785 -0.1918 -0.0059 -0.0277 104 HIS B NE2 
2765 N N   . GLU B 105 ? 0.7994 0.8381 0.7038 -0.1959 -0.0166 -0.0319 105 GLU B N   
2766 C CA  . GLU B 105 ? 0.8797 0.9398 0.7940 -0.1878 -0.0219 -0.0193 105 GLU B CA  
2767 C C   . GLU B 105 ? 0.8769 0.9268 0.7945 -0.1721 -0.0194 -0.0188 105 GLU B C   
2768 O O   . GLU B 105 ? 0.9054 0.9634 0.8347 -0.1603 -0.0199 -0.0102 105 GLU B O   
2769 C CB  . GLU B 105 ? 0.9243 1.0067 0.8338 -0.1998 -0.0284 -0.0145 105 GLU B CB  
2770 C CG  . GLU B 105 ? 0.9755 1.0752 0.8836 -0.2158 -0.0327 -0.0117 105 GLU B CG  
2771 C CD  . GLU B 105 ? 1.1710 1.2819 1.0942 -0.2098 -0.0337 -0.0021 105 GLU B CD  
2772 O OE1 . GLU B 105 ? 1.2527 1.3729 1.1894 -0.1958 -0.0344 0.0084  105 GLU B OE1 
2773 O OE2 . GLU B 105 ? 1.2506 1.3600 1.1723 -0.2191 -0.0329 -0.0054 105 GLU B OE2 
2774 N N   . GLN B 106 ? 0.8133 0.8450 0.7210 -0.1723 -0.0159 -0.0284 106 GLN B N   
2775 C CA  . GLN B 106 ? 0.8211 0.8434 0.7313 -0.1586 -0.0136 -0.0283 106 GLN B CA  
2776 C C   . GLN B 106 ? 0.8512 0.8626 0.7695 -0.1465 -0.0096 -0.0277 106 GLN B C   
2777 O O   . GLN B 106 ? 0.8049 0.8208 0.7315 -0.1351 -0.0096 -0.0217 106 GLN B O   
2778 C CB  . GLN B 106 ? 0.7973 0.8031 0.6954 -0.1623 -0.0104 -0.0383 106 GLN B CB  
2779 C CG  . GLN B 106 ? 0.7613 0.7806 0.6524 -0.1701 -0.0147 -0.0366 106 GLN B CG  
2780 C CD  . GLN B 106 ? 0.8313 0.8346 0.7113 -0.1716 -0.0109 -0.0460 106 GLN B CD  
2781 O OE1 . GLN B 106 ? 0.9356 0.9172 0.8122 -0.1697 -0.0046 -0.0548 106 GLN B OE1 
2782 N NE2 . GLN B 106 ? 0.7718 0.7865 0.6473 -0.1746 -0.0144 -0.0430 106 GLN B NE2 
2783 N N   . VAL B 107 ? 0.7393 0.7372 0.6556 -0.1495 -0.0058 -0.0335 107 VAL B N   
2784 C CA  . VAL B 107 ? 0.6385 0.6288 0.5620 -0.1394 -0.0025 -0.0319 107 VAL B CA  
2785 C C   . VAL B 107 ? 0.7866 0.7938 0.7205 -0.1344 -0.0048 -0.0226 107 VAL B C   
2786 O O   . VAL B 107 ? 0.8342 0.8409 0.7739 -0.1234 -0.0031 -0.0195 107 VAL B O   
2787 C CB  . VAL B 107 ? 0.6763 0.6527 0.5981 -0.1443 0.0017  -0.0372 107 VAL B CB  
2788 C CG1 . VAL B 107 ? 0.7188 0.6939 0.6488 -0.1354 0.0037  -0.0329 107 VAL B CG1 
2789 C CG2 . VAL B 107 ? 0.6399 0.5965 0.5548 -0.1454 0.0065  -0.0456 107 VAL B CG2 
2790 N N   . VAL B 108 ? 0.7836 0.8063 0.7200 -0.1429 -0.0083 -0.0181 108 VAL B N   
2791 C CA  . VAL B 108 ? 0.7040 0.7438 0.6521 -0.1383 -0.0098 -0.0083 108 VAL B CA  
2792 C C   . VAL B 108 ? 0.8098 0.8586 0.7646 -0.1286 -0.0104 -0.0018 108 VAL B C   
2793 O O   . VAL B 108 ? 0.7975 0.8484 0.7611 -0.1185 -0.0074 0.0026  108 VAL B O   
2794 C CB  . VAL B 108 ? 0.6473 0.7046 0.5974 -0.1503 -0.0141 -0.0035 108 VAL B CB  
2795 C CG1 . VAL B 108 ? 0.5428 0.6197 0.5068 -0.1448 -0.0154 0.0081  108 VAL B CG1 
2796 C CG2 . VAL B 108 ? 0.5880 0.6348 0.5334 -0.1591 -0.0121 -0.0098 108 VAL B CG2 
2797 N N   . ARG B 109 ? 0.7555 0.8089 0.7061 -0.1316 -0.0134 -0.0014 109 ARG B N   
2798 C CA  . ARG B 109 ? 0.6384 0.7016 0.5976 -0.1226 -0.0136 0.0064  109 ARG B CA  
2799 C C   . ARG B 109 ? 0.6632 0.7095 0.6217 -0.1110 -0.0086 0.0016  109 ARG B C   
2800 O O   . ARG B 109 ? 0.6752 0.7250 0.6435 -0.1011 -0.0054 0.0068  109 ARG B O   
2801 C CB  . ARG B 109 ? 0.6108 0.6861 0.5665 -0.1296 -0.0185 0.0099  109 ARG B CB  
2802 C CG  . ARG B 109 ? 0.8106 0.9084 0.7698 -0.1404 -0.0239 0.0178  109 ARG B CG  
2803 C CD  . ARG B 109 ? 1.0955 1.2145 1.0569 -0.1457 -0.0294 0.0271  109 ARG B CD  
2804 N NE  . ARG B 109 ? 1.3872 1.5287 1.3522 -0.1572 -0.0346 0.0348  109 ARG B NE  
2805 C CZ  . ARG B 109 ? 1.4806 1.6487 1.4506 -0.1643 -0.0408 0.0466  109 ARG B CZ  
2806 N NH1 . ARG B 109 ? 1.5711 1.7465 1.5432 -0.1606 -0.0423 0.0526  109 ARG B NH1 
2807 N NH2 . ARG B 109 ? 1.4349 1.6235 1.4080 -0.1755 -0.0456 0.0534  109 ARG B NH2 
2808 N N   . ALA B 110 ? 0.6791 0.7071 0.6267 -0.1122 -0.0071 -0.0082 110 ALA B N   
2809 C CA  . ALA B 110 ? 0.6767 0.6901 0.6235 -0.1023 -0.0028 -0.0125 110 ALA B CA  
2810 C C   . ALA B 110 ? 0.7122 0.7225 0.6645 -0.0959 0.0012  -0.0119 110 ALA B C   
2811 O O   . ALA B 110 ? 0.7107 0.7180 0.6669 -0.0872 0.0049  -0.0113 110 ALA B O   
2812 C CB  . ALA B 110 ? 0.6064 0.6024 0.5420 -0.1054 -0.0019 -0.0218 110 ALA B CB  
2813 N N   . ASN B 111 ? 0.6068 0.6175 0.5589 -0.1006 0.0012  -0.0124 111 ASN B N   
2814 C CA  . ASN B 111 ? 0.5492 0.5589 0.5059 -0.0951 0.0049  -0.0113 111 ASN B CA  
2815 C C   . ASN B 111 ? 0.6872 0.7109 0.6552 -0.0895 0.0068  -0.0036 111 ASN B C   
2816 O O   . ASN B 111 ? 0.6887 0.7098 0.6601 -0.0824 0.0117  -0.0037 111 ASN B O   
2817 C CB  . ASN B 111 ? 0.5549 0.5632 0.5102 -0.1015 0.0046  -0.0123 111 ASN B CB  
2818 C CG  . ASN B 111 ? 0.6576 0.6490 0.6053 -0.1031 0.0061  -0.0190 111 ASN B CG  
2819 O OD1 . ASN B 111 ? 0.6968 0.6788 0.6413 -0.0977 0.0079  -0.0222 111 ASN B OD1 
2820 N ND2 . ASN B 111 ? 0.8553 0.8433 0.8013 -0.1106 0.0058  -0.0205 111 ASN B ND2 
2821 N N   . ALA B 112 ? 0.7938 0.8328 0.7680 -0.0929 0.0034  0.0035  112 ALA B N   
2822 C CA  . ALA B 112 ? 0.6714 0.7245 0.6593 -0.0867 0.0060  0.0126  112 ALA B CA  
2823 C C   . ALA B 112 ? 0.5814 0.6290 0.5724 -0.0776 0.0102  0.0125  112 ALA B C   
2824 O O   . ALA B 112 ? 0.6024 0.6520 0.6031 -0.0697 0.0165  0.0158  112 ALA B O   
2825 C CB  . ALA B 112 ? 0.4440 0.5171 0.4385 -0.0932 0.0006  0.0219  112 ALA B CB  
2826 N N   . LEU B 113 ? 0.5365 0.5769 0.5201 -0.0789 0.0076  0.0086  113 LEU B N   
2827 C CA  . LEU B 113 ? 0.4633 0.4983 0.4501 -0.0709 0.0114  0.0085  113 LEU B CA  
2828 C C   . LEU B 113 ? 0.7403 0.7600 0.7230 -0.0652 0.0176  0.0009  113 LEU B C   
2829 O O   . LEU B 113 ? 0.7456 0.7637 0.7356 -0.0578 0.0241  0.0021  113 LEU B O   
2830 C CB  . LEU B 113 ? 0.4425 0.4732 0.4211 -0.0744 0.0070  0.0058  113 LEU B CB  
2831 C CG  . LEU B 113 ? 0.5764 0.6077 0.5617 -0.0675 0.0096  0.0097  113 LEU B CG  
2832 C CD1 . LEU B 113 ? 0.4484 0.4985 0.4502 -0.0644 0.0107  0.0227  113 LEU B CD1 
2833 C CD2 . LEU B 113 ? 0.6262 0.6543 0.6020 -0.0723 0.0048  0.0068  113 LEU B CD2 
2834 N N   . ALA B 114 ? 0.6229 0.6318 0.5944 -0.0691 0.0161  -0.0068 114 ALA B N   
2835 C CA  . ALA B 114 ? 0.5434 0.5411 0.5103 -0.0655 0.0209  -0.0130 114 ALA B CA  
2836 C C   . ALA B 114 ? 0.6549 0.6586 0.6295 -0.0620 0.0266  -0.0101 114 ALA B C   
2837 O O   . ALA B 114 ? 0.7215 0.7198 0.6968 -0.0570 0.0332  -0.0131 114 ALA B O   
2838 C CB  . ALA B 114 ? 0.5399 0.5290 0.4967 -0.0707 0.0179  -0.0184 114 ALA B CB  
2839 N N   . GLU B 115 ? 0.5446 0.5597 0.5248 -0.0651 0.0249  -0.0046 115 GLU B N   
2840 C CA  . GLU B 115 ? 0.5521 0.5734 0.5399 -0.0618 0.0309  -0.0017 115 GLU B CA  
2841 C C   . GLU B 115 ? 0.6320 0.6587 0.6326 -0.0546 0.0374  0.0036  115 GLU B C   
2842 O O   . GLU B 115 ? 0.6964 0.7195 0.7000 -0.0497 0.0460  0.0014  115 GLU B O   
2843 C CB  . GLU B 115 ? 0.4410 0.4740 0.4329 -0.0670 0.0275  0.0038  115 GLU B CB  
2844 C CG  . GLU B 115 ? 0.7961 0.8389 0.7998 -0.0625 0.0341  0.0094  115 GLU B CG  
2845 C CD  . GLU B 115 ? 1.0212 1.0708 1.0255 -0.0670 0.0330  0.0116  115 GLU B CD  
2846 O OE1 . GLU B 115 ? 1.0752 1.1203 1.0705 -0.0735 0.0276  0.0083  115 GLU B OE1 
2847 O OE2 . GLU B 115 ? 1.1965 1.2553 1.2111 -0.0637 0.0386  0.0167  115 GLU B OE2 
2848 N N   . GLU B 116 ? 0.5901 0.6260 0.5988 -0.0541 0.0341  0.0110  116 GLU B N   
2849 C CA  . GLU B 116 ? 0.6523 0.6934 0.6757 -0.0465 0.0408  0.0176  116 GLU B CA  
2850 C C   . GLU B 116 ? 0.6549 0.6800 0.6743 -0.0411 0.0478  0.0099  116 GLU B C   
2851 O O   . GLU B 116 ? 0.6848 0.7080 0.7141 -0.0345 0.0579  0.0110  116 GLU B O   
2852 C CB  . GLU B 116 ? 0.6257 0.6805 0.6571 -0.0480 0.0346  0.0277  116 GLU B CB  
2853 C CG  . GLU B 116 ? 0.7123 0.7724 0.7605 -0.0396 0.0411  0.0365  116 GLU B CG  
2854 C CD  . GLU B 116 ? 1.0431 1.1111 1.1086 -0.0331 0.0507  0.0437  116 GLU B CD  
2855 O OE1 . GLU B 116 ? 1.0508 1.1257 1.1167 -0.0362 0.0500  0.0448  116 GLU B OE1 
2856 O OE2 . GLU B 116 ? 1.1266 1.1938 1.2065 -0.0247 0.0596  0.0488  116 GLU B OE2 
2857 N N   . ALA B 117 ? 0.5500 0.5632 0.5553 -0.0442 0.0435  0.0016  117 ALA B N   
2858 C CA  . ALA B 117 ? 0.5847 0.5835 0.5850 -0.0406 0.0493  -0.0061 117 ALA B CA  
2859 C C   . ALA B 117 ? 0.6169 0.6076 0.6108 -0.0406 0.0562  -0.0140 117 ALA B C   
2860 O O   . ALA B 117 ? 0.6704 0.6500 0.6603 -0.0385 0.0624  -0.0208 117 ALA B O   
2861 C CB  . ALA B 117 ? 0.5064 0.4967 0.4942 -0.0443 0.0422  -0.0115 117 ALA B CB  
2862 N N   . GLY B 118 ? 0.5189 0.5153 0.5109 -0.0438 0.0553  -0.0135 118 GLY B N   
2863 C CA  . GLY B 118 ? 0.5769 0.5672 0.5606 -0.0453 0.0609  -0.0209 118 GLY B CA  
2864 C C   . GLY B 118 ? 0.6723 0.6539 0.6404 -0.0502 0.0557  -0.0282 118 GLY B C   
2865 O O   . GLY B 118 ? 0.6735 0.6484 0.6336 -0.0514 0.0607  -0.0352 118 GLY B O   
2866 N N   . LEU B 119 ? 0.6362 0.6186 0.6002 -0.0538 0.0464  -0.0264 119 LEU B N   
2867 C CA  . LEU B 119 ? 0.5889 0.5632 0.5414 -0.0573 0.0414  -0.0314 119 LEU B CA  
2868 C C   . LEU B 119 ? 0.6850 0.6622 0.6342 -0.0624 0.0345  -0.0289 119 LEU B C   
2869 O O   . LEU B 119 ? 0.7086 0.6798 0.6520 -0.0648 0.0297  -0.0308 119 LEU B O   
2870 C CB  . LEU B 119 ? 0.5967 0.5648 0.5487 -0.0554 0.0390  -0.0325 119 LEU B CB  
2871 C CG  . LEU B 119 ? 0.6116 0.5733 0.5655 -0.0511 0.0456  -0.0359 119 LEU B CG  
2872 C CD1 . LEU B 119 ? 0.6192 0.5767 0.5730 -0.0499 0.0415  -0.0353 119 LEU B CD1 
2873 C CD2 . LEU B 119 ? 0.5919 0.5464 0.5361 -0.0532 0.0496  -0.0435 119 LEU B CD2 
2874 N N   . ALA B 120 ? 0.7478 0.7336 0.7017 -0.0640 0.0345  -0.0247 120 ALA B N   
2875 C CA  . ALA B 120 ? 0.6958 0.6840 0.6486 -0.0691 0.0286  -0.0220 120 ALA B CA  
2876 C C   . ALA B 120 ? 0.8445 0.8256 0.7890 -0.0723 0.0265  -0.0249 120 ALA B C   
2877 O O   . ALA B 120 ? 1.0154 0.9948 0.9593 -0.0762 0.0225  -0.0234 120 ALA B O   
2878 C CB  . ALA B 120 ? 0.5546 0.5532 0.5136 -0.0706 0.0298  -0.0171 120 ALA B CB  
2879 N N   . ASP B 121 ? 0.8108 0.7878 0.7496 -0.0711 0.0293  -0.0285 121 ASP B N   
2880 C CA  . ASP B 121 ? 0.6547 0.6280 0.5874 -0.0739 0.0272  -0.0290 121 ASP B CA  
2881 C C   . ASP B 121 ? 0.6478 0.6128 0.5760 -0.0729 0.0257  -0.0324 121 ASP B C   
2882 O O   . ASP B 121 ? 0.7135 0.6752 0.6395 -0.0749 0.0231  -0.0312 121 ASP B O   
2883 C CB  . ASP B 121 ? 0.8313 0.8098 0.7601 -0.0754 0.0308  -0.0293 121 ASP B CB  
2884 C CG  . ASP B 121 ? 1.3706 1.3577 1.3043 -0.0760 0.0330  -0.0259 121 ASP B CG  
2885 O OD1 . ASP B 121 ? 1.5240 1.5140 1.4638 -0.0731 0.0358  -0.0256 121 ASP B OD1 
2886 O OD2 . ASP B 121 ? 1.4657 1.4572 1.3990 -0.0793 0.0318  -0.0221 121 ASP B OD2 
2887 N N   . ARG B 122 ? 0.5151 0.4771 0.4435 -0.0697 0.0277  -0.0357 122 ARG B N   
2888 C CA  . ARG B 122 ? 0.5973 0.5517 0.5221 -0.0687 0.0261  -0.0386 122 ARG B CA  
2889 C C   . ARG B 122 ? 0.6572 0.6076 0.5842 -0.0691 0.0220  -0.0372 122 ARG B C   
2890 O O   . ARG B 122 ? 0.6736 0.6180 0.5979 -0.0700 0.0199  -0.0380 122 ARG B O   
2891 C CB  . ARG B 122 ? 0.4792 0.4310 0.4034 -0.0655 0.0305  -0.0426 122 ARG B CB  
2892 C CG  . ARG B 122 ? 0.5312 0.4763 0.4501 -0.0656 0.0298  -0.0461 122 ARG B CG  
2893 C CD  . ARG B 122 ? 0.7208 0.6620 0.6408 -0.0625 0.0344  -0.0499 122 ARG B CD  
2894 N NE  . ARG B 122 ? 0.8019 0.7457 0.7212 -0.0629 0.0411  -0.0527 122 ARG B NE  
2895 C CZ  . ARG B 122 ? 0.7121 0.6518 0.6331 -0.0605 0.0480  -0.0567 122 ARG B CZ  
2896 N NH1 . ARG B 122 ? 0.8423 0.7760 0.7664 -0.0573 0.0483  -0.0574 122 ARG B NH1 
2897 N NH2 . ARG B 122 ? 0.6644 0.6056 0.5844 -0.0616 0.0554  -0.0599 122 ARG B NH2 
2898 N N   . ALA B 123 ? 0.5752 0.5300 0.5072 -0.0690 0.0212  -0.0350 123 ALA B N   
2899 C CA  . ALA B 123 ? 0.5500 0.5031 0.4827 -0.0715 0.0176  -0.0343 123 ALA B CA  
2900 C C   . ALA B 123 ? 0.6521 0.6100 0.5873 -0.0761 0.0159  -0.0313 123 ALA B C   
2901 O O   . ALA B 123 ? 0.7837 0.7508 0.7239 -0.0763 0.0162  -0.0281 123 ALA B O   
2902 C CB  . ALA B 123 ? 0.6351 0.5915 0.5711 -0.0691 0.0174  -0.0333 123 ALA B CB  
2903 N N   . ARG B 124 ? 0.6075 0.5593 0.5405 -0.0798 0.0147  -0.0320 124 ARG B N   
2904 C CA  . ARG B 124 ? 0.5255 0.4794 0.4607 -0.0851 0.0139  -0.0300 124 ARG B CA  
2905 C C   . ARG B 124 ? 0.7556 0.7031 0.6883 -0.0902 0.0126  -0.0327 124 ARG B C   
2906 O O   . ARG B 124 ? 0.8194 0.7570 0.7490 -0.0897 0.0135  -0.0357 124 ARG B O   
2907 C CB  . ARG B 124 ? 0.5384 0.4897 0.4745 -0.0857 0.0155  -0.0280 124 ARG B CB  
2908 C CG  . ARG B 124 ? 0.7069 0.6671 0.6448 -0.0837 0.0170  -0.0250 124 ARG B CG  
2909 C CD  . ARG B 124 ? 0.6339 0.5931 0.5720 -0.0845 0.0181  -0.0220 124 ARG B CD  
2910 N NE  . ARG B 124 ? 0.7294 0.6980 0.6679 -0.0838 0.0197  -0.0195 124 ARG B NE  
2911 C CZ  . ARG B 124 ? 0.7449 0.7166 0.6819 -0.0841 0.0206  -0.0166 124 ARG B CZ  
2912 N NH1 . ARG B 124 ? 0.6927 0.6598 0.6296 -0.0845 0.0199  -0.0144 124 ARG B NH1 
2913 N NH2 . ARG B 124 ? 0.7829 0.7636 0.7191 -0.0843 0.0227  -0.0152 124 ARG B NH2 
2914 N N   . PHE B 125 ? 0.6994 0.6530 0.6333 -0.0958 0.0109  -0.0317 125 PHE B N   
2915 C CA  . PHE B 125 ? 0.6331 0.5821 0.5628 -0.1027 0.0100  -0.0353 125 PHE B CA  
2916 C C   . PHE B 125 ? 0.6216 0.5678 0.5523 -0.1101 0.0113  -0.0359 125 PHE B C   
2917 O O   . PHE B 125 ? 0.5953 0.5486 0.5305 -0.1110 0.0110  -0.0320 125 PHE B O   
2918 C CB  . PHE B 125 ? 0.5738 0.5337 0.5030 -0.1047 0.0066  -0.0339 125 PHE B CB  
2919 C CG  . PHE B 125 ? 0.6067 0.5673 0.5359 -0.0975 0.0064  -0.0334 125 PHE B CG  
2920 C CD1 . PHE B 125 ? 0.5478 0.5006 0.4714 -0.0978 0.0065  -0.0374 125 PHE B CD1 
2921 C CD2 . PHE B 125 ? 0.6666 0.6343 0.6015 -0.0905 0.0073  -0.0294 125 PHE B CD2 
2922 C CE1 . PHE B 125 ? 0.7111 0.6641 0.6352 -0.0913 0.0064  -0.0368 125 PHE B CE1 
2923 C CE2 . PHE B 125 ? 0.6493 0.6159 0.5848 -0.0842 0.0082  -0.0295 125 PHE B CE2 
2924 C CZ  . PHE B 125 ? 0.7838 0.7433 0.7140 -0.0846 0.0074  -0.0329 125 PHE B CZ  
2925 N N   . GLN B 126 ? 0.6668 0.6014 0.5933 -0.1155 0.0136  -0.0410 126 GLN B N   
2926 C CA  . GLN B 126 ? 0.6145 0.5397 0.5428 -0.1210 0.0176  -0.0426 126 GLN B CA  
2927 C C   . GLN B 126 ? 0.6589 0.5769 0.5808 -0.1312 0.0195  -0.0494 126 GLN B C   
2928 O O   . GLN B 126 ? 0.6099 0.5240 0.5258 -0.1319 0.0196  -0.0538 126 GLN B O   
2929 C CB  . GLN B 126 ? 0.5533 0.4674 0.4855 -0.1145 0.0217  -0.0412 126 GLN B CB  
2930 C CG  . GLN B 126 ? 0.6390 0.5378 0.5732 -0.1186 0.0279  -0.0441 126 GLN B CG  
2931 C CD  . GLN B 126 ? 0.6823 0.5747 0.6239 -0.1117 0.0315  -0.0391 126 GLN B CD  
2932 O OE1 . GLN B 126 ? 0.6708 0.5718 0.6150 -0.1052 0.0287  -0.0334 126 GLN B OE1 
2933 N NE2 . GLN B 126 ? 0.6964 0.5742 0.6419 -0.1136 0.0383  -0.0407 126 GLN B NE2 
2934 N N   . ARG B 127 ? 0.6162 0.5327 0.5390 -0.1400 0.0215  -0.0508 127 ARG B N   
2935 C CA  . ARG B 127 ? 0.6233 0.5300 0.5393 -0.1513 0.0253  -0.0589 127 ARG B CA  
2936 C C   . ARG B 127 ? 0.6222 0.5082 0.5403 -0.1489 0.0337  -0.0628 127 ARG B C   
2937 O O   . ARG B 127 ? 0.7159 0.5950 0.6427 -0.1449 0.0377  -0.0590 127 ARG B O   
2938 C CB  . ARG B 127 ? 0.6571 0.5687 0.5735 -0.1622 0.0251  -0.0593 127 ARG B CB  
2939 C CG  . ARG B 127 ? 0.8638 0.7693 0.7709 -0.1765 0.0281  -0.0683 127 ARG B CG  
2940 C CD  . ARG B 127 ? 0.8988 0.8227 0.7981 -0.1839 0.0207  -0.0681 127 ARG B CD  
2941 N NE  . ARG B 127 ? 1.0292 0.9477 0.9179 -0.2002 0.0240  -0.0775 127 ARG B NE  
2942 C CZ  . ARG B 127 ? 1.0293 0.9483 0.9170 -0.2127 0.0256  -0.0802 127 ARG B CZ  
2943 N NH1 . ARG B 127 ? 0.8795 0.8053 0.7770 -0.2099 0.0237  -0.0732 127 ARG B NH1 
2944 N NH2 . ARG B 127 ? 1.0691 0.9823 0.9455 -0.2288 0.0294  -0.0903 127 ARG B NH2 
2945 N N   . ALA B 128 ? 0.6313 0.5086 0.5427 -0.1504 0.0365  -0.0691 128 ALA B N   
2946 C CA  . ALA B 128 ? 0.7332 0.5911 0.6476 -0.1477 0.0454  -0.0726 128 ALA B CA  
2947 C C   . ALA B 128 ? 0.8502 0.7018 0.7541 -0.1531 0.0478  -0.0812 128 ALA B C   
2948 O O   . ALA B 128 ? 0.8589 0.7232 0.7545 -0.1558 0.0412  -0.0821 128 ALA B O   
2949 C CB  . ALA B 128 ? 0.6294 0.4865 0.5525 -0.1341 0.0450  -0.0652 128 ALA B CB  
2950 N N   . ASP B 129 ? 0.9164 0.7487 0.8216 -0.1548 0.0580  -0.0869 129 ASP B N   
2951 C CA  . ASP B 129 ? 0.8995 0.7226 0.7944 -0.1618 0.0631  -0.0967 129 ASP B CA  
2952 C C   . ASP B 129 ? 0.7798 0.5920 0.6799 -0.1514 0.0682  -0.0954 129 ASP B C   
2953 O O   . ASP B 129 ? 0.7882 0.5876 0.7000 -0.1457 0.0759  -0.0923 129 ASP B O   
2954 C CB  . ASP B 129 ? 1.0333 0.8412 0.9246 -0.1753 0.0732  -0.1063 129 ASP B CB  
2955 C CG  . ASP B 129 ? 0.9822 0.7805 0.8602 -0.1856 0.0797  -0.1184 129 ASP B CG  
2956 O OD1 . ASP B 129 ? 0.8092 0.6061 0.6843 -0.1799 0.0798  -0.1192 129 ASP B OD1 
2957 O OD2 . ASP B 129 ? 0.9898 0.7820 0.8596 -0.2006 0.0850  -0.1277 129 ASP B OD2 
2958 N N   . ALA B 130 ? 0.6876 0.5055 0.5802 -0.1492 0.0641  -0.0969 130 ALA B N   
2959 C CA  . ALA B 130 ? 0.7891 0.5984 0.6871 -0.1393 0.0682  -0.0950 130 ALA B CA  
2960 C C   . ALA B 130 ? 0.8380 0.6254 0.7389 -0.1423 0.0823  -0.1017 130 ALA B C   
2961 O O   . ALA B 130 ? 0.8254 0.6050 0.7343 -0.1334 0.0871  -0.0984 130 ALA B O   
2962 C CB  . ALA B 130 ? 0.7744 0.5930 0.6634 -0.1375 0.0621  -0.0961 130 ALA B CB  
2963 N N   . MET B 131 ? 0.7562 0.5336 0.6513 -0.1549 0.0897  -0.1108 131 MET B N   
2964 C CA  . MET B 131 ? 0.7989 0.5531 0.6985 -0.1580 0.1054  -0.1176 131 MET B CA  
2965 C C   . MET B 131 ? 0.8566 0.6015 0.7755 -0.1495 0.1119  -0.1090 131 MET B C   
2966 O O   . MET B 131 ? 0.9568 0.6829 0.8852 -0.1474 0.1254  -0.1106 131 MET B O   
2967 C CB  . MET B 131 ? 0.7548 0.5003 0.6420 -0.1755 0.1122  -0.1307 131 MET B CB  
2968 C CG  . MET B 131 ? 0.9041 0.6570 0.7714 -0.1864 0.1087  -0.1402 131 MET B CG  
2969 S SD  . MET B 131 ? 1.0182 0.7547 0.8820 -0.1844 0.1203  -0.1477 131 MET B SD  
2970 C CE  . MET B 131 ? 0.9079 0.6143 0.7765 -0.1933 0.1418  -0.1589 131 MET B CE  
2971 N N   . ASP B 132 ? 0.9493 0.7073 0.8746 -0.1449 0.1031  -0.0996 132 ASP B N   
2972 C CA  . ASP B 132 ? 0.9682 0.7205 0.9114 -0.1383 0.1081  -0.0902 132 ASP B CA  
2973 C C   . ASP B 132 ? 0.8595 0.6324 0.8063 -0.1304 0.0948  -0.0787 132 ASP B C   
2974 O O   . ASP B 132 ? 0.7962 0.5788 0.7394 -0.1354 0.0887  -0.0782 132 ASP B O   
2975 C CB  . ASP B 132 ? 0.9540 0.6944 0.8983 -0.1492 0.1166  -0.0962 132 ASP B CB  
2976 C CG  . ASP B 132 ? 1.0600 0.7940 1.0238 -0.1428 0.1227  -0.0858 132 ASP B CG  
2977 O OD1 . ASP B 132 ? 1.0463 0.7832 1.0235 -0.1304 0.1225  -0.0743 132 ASP B OD1 
2978 O OD2 . ASP B 132 ? 1.1440 0.8716 1.1100 -0.1509 0.1276  -0.0885 132 ASP B OD2 
2979 N N   . LEU B 133 ? 0.7358 0.5150 0.6897 -0.1189 0.0912  -0.0699 133 LEU B N   
2980 C CA  . LEU B 133 ? 0.8140 0.6132 0.7671 -0.1127 0.0785  -0.0618 133 LEU B CA  
2981 C C   . LEU B 133 ? 0.7317 0.5352 0.6981 -0.1083 0.0784  -0.0508 133 LEU B C   
2982 O O   . LEU B 133 ? 0.6937 0.4912 0.6740 -0.1020 0.0846  -0.0429 133 LEU B O   
2983 C CB  . LEU B 133 ? 0.8082 0.6135 0.7604 -0.1042 0.0740  -0.0584 133 LEU B CB  
2984 C CG  . LEU B 133 ? 0.7083 0.5165 0.6465 -0.1068 0.0699  -0.0665 133 LEU B CG  
2985 C CD1 . LEU B 133 ? 0.6638 0.4748 0.6047 -0.0979 0.0680  -0.0622 133 LEU B CD1 
2986 C CD2 . LEU B 133 ? 0.5544 0.3780 0.4823 -0.1104 0.0596  -0.0681 133 LEU B CD2 
2987 N N   . PRO B 134 ? 0.6982 0.5136 0.6619 -0.1110 0.0716  -0.0486 134 PRO B N   
2988 C CA  . PRO B 134 ? 0.6861 0.5063 0.6619 -0.1078 0.0717  -0.0381 134 PRO B CA  
2989 C C   . PRO B 134 ? 0.6878 0.5232 0.6674 -0.0988 0.0644  -0.0277 134 PRO B C   
2990 O O   . PRO B 134 ? 0.8114 0.6603 0.7905 -0.0980 0.0581  -0.0226 134 PRO B O   
2991 C CB  . PRO B 134 ? 0.5634 0.3898 0.5328 -0.1159 0.0678  -0.0418 134 PRO B CB  
2992 C CG  . PRO B 134 ? 0.6402 0.4754 0.5944 -0.1192 0.0601  -0.0494 134 PRO B CG  
2993 C CD  . PRO B 134 ? 0.7028 0.5283 0.6528 -0.1176 0.0638  -0.0552 134 PRO B CD  
2994 N N   . PHE B 135 ? 0.6569 0.4902 0.6401 -0.0926 0.0658  -0.0248 135 PHE B N   
2995 C CA  . PHE B 135 ? 0.7798 0.6274 0.7652 -0.0855 0.0593  -0.0160 135 PHE B CA  
2996 C C   . PHE B 135 ? 0.8751 0.7179 0.8746 -0.0798 0.0654  -0.0071 135 PHE B C   
2997 O O   . PHE B 135 ? 0.7553 0.5832 0.7590 -0.0798 0.0738  -0.0108 135 PHE B O   
2998 C CB  . PHE B 135 ? 0.7530 0.6074 0.7257 -0.0842 0.0522  -0.0220 135 PHE B CB  
2999 C CG  . PHE B 135 ? 0.6873 0.5462 0.6477 -0.0895 0.0471  -0.0303 135 PHE B CG  
3000 C CD1 . PHE B 135 ? 0.5609 0.4317 0.5196 -0.0906 0.0419  -0.0275 135 PHE B CD1 
3001 C CD2 . PHE B 135 ? 0.5718 0.4242 0.5231 -0.0935 0.0478  -0.0399 135 PHE B CD2 
3002 C CE1 . PHE B 135 ? 0.6165 0.4929 0.5663 -0.0949 0.0376  -0.0333 135 PHE B CE1 
3003 C CE2 . PHE B 135 ? 0.6731 0.5323 0.6150 -0.0984 0.0429  -0.0452 135 PHE B CE2 
3004 C CZ  . PHE B 135 ? 0.6785 0.5498 0.6203 -0.0987 0.0378  -0.0415 135 PHE B CZ  
3005 N N   . GLU B 136 ? 0.8316 0.6879 0.8387 -0.0753 0.0616  0.0051  136 GLU B N   
3006 C CA  . GLU B 136 ? 0.8058 0.6607 0.8289 -0.0699 0.0671  0.0165  136 GLU B CA  
3007 C C   . GLU B 136 ? 0.8227 0.6772 0.8428 -0.0663 0.0660  0.0144  136 GLU B C   
3008 O O   . GLU B 136 ? 0.7785 0.6381 0.7844 -0.0672 0.0591  0.0066  136 GLU B O   
3009 C CB  . GLU B 136 ? 0.7855 0.6578 0.8175 -0.0676 0.0628  0.0314  136 GLU B CB  
3010 C CG  . GLU B 136 ? 0.7744 0.6421 0.8168 -0.0699 0.0684  0.0366  136 GLU B CG  
3011 C CD  . GLU B 136 ? 0.9203 0.8019 0.9777 -0.0668 0.0679  0.0545  136 GLU B CD  
3012 O OE1 . GLU B 136 ? 0.9367 0.8373 0.9902 -0.0656 0.0596  0.0613  136 GLU B OE1 
3013 O OE2 . GLU B 136 ? 1.1089 0.9821 1.1827 -0.0660 0.0767  0.0622  136 GLU B OE2 
3014 N N   . ASP B 137 ? 0.8280 0.6761 0.8632 -0.0619 0.0738  0.0220  137 ASP B N   
3015 C CA  . ASP B 137 ? 0.6751 0.5240 0.7105 -0.0579 0.0734  0.0225  137 ASP B CA  
3016 C C   . ASP B 137 ? 0.8240 0.6922 0.8503 -0.0572 0.0617  0.0254  137 ASP B C   
3017 O O   . ASP B 137 ? 0.9846 0.8684 1.0127 -0.0576 0.0560  0.0343  137 ASP B O   
3018 C CB  . ASP B 137 ? 0.7330 0.5797 0.7903 -0.0522 0.0819  0.0363  137 ASP B CB  
3019 C CG  . ASP B 137 ? 0.8165 0.6419 0.8852 -0.0524 0.0960  0.0338  137 ASP B CG  
3020 O OD1 . ASP B 137 ? 0.7681 0.5806 0.8262 -0.0583 0.0989  0.0205  137 ASP B OD1 
3021 O OD2 . ASP B 137 ? 0.7705 0.5929 0.8593 -0.0469 0.1045  0.0456  137 ASP B OD2 
3022 N N   . GLU B 138 ? 0.7559 0.6228 0.7725 -0.0565 0.0589  0.0179  138 GLU B N   
3023 C CA  . GLU B 138 ? 0.7403 0.6230 0.7503 -0.0558 0.0499  0.0206  138 GLU B CA  
3024 C C   . GLU B 138 ? 0.6832 0.5781 0.6816 -0.0594 0.0418  0.0183  138 GLU B C   
3025 O O   . GLU B 138 ? 0.7325 0.6431 0.7294 -0.0599 0.0358  0.0246  138 GLU B O   
3026 C CB  . GLU B 138 ? 0.6835 0.5779 0.7085 -0.0521 0.0502  0.0364  138 GLU B CB  
3027 C CG  . GLU B 138 ? 0.6845 0.5677 0.7234 -0.0476 0.0593  0.0402  138 GLU B CG  
3028 C CD  . GLU B 138 ? 0.7966 0.6945 0.8508 -0.0439 0.0585  0.0569  138 GLU B CD  
3029 O OE1 . GLU B 138 ? 0.7902 0.7072 0.8391 -0.0462 0.0492  0.0623  138 GLU B OE1 
3030 O OE2 . GLU B 138 ? 0.8850 0.7755 0.9569 -0.0393 0.0677  0.0648  138 GLU B OE2 
3031 N N   . SER B 139 ? 0.6855 0.5735 0.6751 -0.0626 0.0418  0.0086  139 SER B N   
3032 C CA  . SER B 139 ? 0.7217 0.6195 0.7008 -0.0657 0.0354  0.0052  139 SER B CA  
3033 C C   . SER B 139 ? 0.6850 0.5838 0.6500 -0.0665 0.0306  -0.0050 139 SER B C   
3034 O O   . SER B 139 ? 0.7515 0.6584 0.7087 -0.0684 0.0263  -0.0076 139 SER B O   
3035 C CB  . SER B 139 ? 0.8293 0.7210 0.8089 -0.0688 0.0382  0.0024  139 SER B CB  
3036 O OG  . SER B 139 ? 0.8019 0.6773 0.7832 -0.0697 0.0447  -0.0040 139 SER B OG  
3037 N N   . PHE B 140 ? 0.6790 0.5701 0.6414 -0.0649 0.0320  -0.0103 140 PHE B N   
3038 C CA  . PHE B 140 ? 0.7145 0.6061 0.6651 -0.0655 0.0282  -0.0190 140 PHE B CA  
3039 C C   . PHE B 140 ? 0.7702 0.6636 0.7198 -0.0630 0.0267  -0.0187 140 PHE B C   
3040 O O   . PHE B 140 ? 0.7338 0.6226 0.6907 -0.0607 0.0301  -0.0148 140 PHE B O   
3041 C CB  . PHE B 140 ? 0.6101 0.4913 0.5558 -0.0676 0.0306  -0.0277 140 PHE B CB  
3042 C CG  . PHE B 140 ? 0.6518 0.5342 0.5957 -0.0711 0.0302  -0.0294 140 PHE B CG  
3043 C CD1 . PHE B 140 ? 0.5985 0.4906 0.5368 -0.0719 0.0255  -0.0305 140 PHE B CD1 
3044 C CD2 . PHE B 140 ? 0.5898 0.4635 0.5386 -0.0738 0.0353  -0.0295 140 PHE B CD2 
3045 C CE1 . PHE B 140 ? 0.6054 0.4999 0.5431 -0.0750 0.0251  -0.0312 140 PHE B CE1 
3046 C CE2 . PHE B 140 ? 0.7135 0.5893 0.6611 -0.0777 0.0347  -0.0307 140 PHE B CE2 
3047 C CZ  . PHE B 140 ? 0.6807 0.5678 0.6228 -0.0781 0.0292  -0.0310 140 PHE B CZ  
3048 N N   . ASP B 141 ? 0.7227 0.6226 0.6637 -0.0636 0.0222  -0.0226 141 ASP B N   
3049 C CA  . ASP B 141 ? 0.7014 0.6031 0.6398 -0.0622 0.0205  -0.0235 141 ASP B CA  
3050 C C   . ASP B 141 ? 0.6615 0.5534 0.5962 -0.0609 0.0221  -0.0305 141 ASP B C   
3051 O O   . ASP B 141 ? 0.6733 0.5634 0.6089 -0.0592 0.0225  -0.0302 141 ASP B O   
3052 C CB  . ASP B 141 ? 0.6448 0.5557 0.5758 -0.0641 0.0166  -0.0258 141 ASP B CB  
3053 C CG  . ASP B 141 ? 0.7046 0.6275 0.6374 -0.0667 0.0148  -0.0189 141 ASP B CG  
3054 O OD1 . ASP B 141 ? 0.7702 0.6978 0.7103 -0.0665 0.0147  -0.0105 141 ASP B OD1 
3055 O OD2 . ASP B 141 ? 0.7242 0.6524 0.6514 -0.0691 0.0136  -0.0213 141 ASP B OD2 
3056 N N   . ALA B 142 ? 0.5990 0.4861 0.5296 -0.0623 0.0228  -0.0360 142 ALA B N   
3057 C CA  . ALA B 142 ? 0.5417 0.4224 0.4672 -0.0623 0.0235  -0.0422 142 ALA B CA  
3058 C C   . ALA B 142 ? 0.7076 0.5843 0.6311 -0.0656 0.0251  -0.0457 142 ALA B C   
3059 O O   . ALA B 142 ? 0.7520 0.6325 0.6766 -0.0674 0.0244  -0.0441 142 ALA B O   
3060 C CB  . ALA B 142 ? 0.5535 0.4391 0.4733 -0.0614 0.0201  -0.0453 142 ALA B CB  
3061 N N   . VAL B 143 ? 0.6888 0.5587 0.6088 -0.0673 0.0273  -0.0504 143 VAL B N   
3062 C CA  . VAL B 143 ? 0.6017 0.4692 0.5174 -0.0723 0.0283  -0.0547 143 VAL B CA  
3063 C C   . VAL B 143 ? 0.6280 0.4975 0.5366 -0.0737 0.0262  -0.0586 143 VAL B C   
3064 O O   . VAL B 143 ? 0.7262 0.5919 0.6336 -0.0720 0.0275  -0.0599 143 VAL B O   
3065 C CB  . VAL B 143 ? 0.5933 0.4496 0.5117 -0.0753 0.0350  -0.0566 143 VAL B CB  
3066 C CG1 . VAL B 143 ? 0.6525 0.5065 0.5638 -0.0826 0.0361  -0.0627 143 VAL B CG1 
3067 C CG2 . VAL B 143 ? 0.5127 0.3680 0.4401 -0.0738 0.0373  -0.0509 143 VAL B CG2 
3068 N N   . ILE B 144 ? 0.6004 0.4773 0.5055 -0.0767 0.0229  -0.0594 144 ILE B N   
3069 C CA  . ILE B 144 ? 0.5794 0.4605 0.4789 -0.0789 0.0208  -0.0613 144 ILE B CA  
3070 C C   . ILE B 144 ? 0.5899 0.4714 0.4842 -0.0873 0.0216  -0.0647 144 ILE B C   
3071 O O   . ILE B 144 ? 0.6618 0.5465 0.5575 -0.0904 0.0209  -0.0639 144 ILE B O   
3072 C CB  . ILE B 144 ? 0.6690 0.5608 0.5704 -0.0754 0.0165  -0.0577 144 ILE B CB  
3073 C CG1 . ILE B 144 ? 0.7465 0.6447 0.6443 -0.0774 0.0143  -0.0573 144 ILE B CG1 
3074 C CG2 . ILE B 144 ? 0.5263 0.4248 0.4306 -0.0762 0.0149  -0.0552 144 ILE B CG2 
3075 C CD1 . ILE B 144 ? 0.7120 0.6189 0.6144 -0.0725 0.0118  -0.0528 144 ILE B CD1 
3076 N N   . ALA B 145 ? 0.5897 0.4684 0.4776 -0.0918 0.0233  -0.0686 145 ALA B N   
3077 C CA  . ALA B 145 ? 0.6435 0.5249 0.5241 -0.1018 0.0235  -0.0724 145 ALA B CA  
3078 C C   . ALA B 145 ? 0.7027 0.5955 0.5785 -0.1038 0.0191  -0.0705 145 ALA B C   
3079 O O   . ALA B 145 ? 0.8558 0.7455 0.7268 -0.1047 0.0208  -0.0730 145 ALA B O   
3080 C CB  . ALA B 145 ? 0.5137 0.3813 0.3901 -0.1077 0.0309  -0.0795 145 ALA B CB  
3081 N N   . LEU B 146 ? 0.6797 0.5867 0.5581 -0.1039 0.0137  -0.0650 146 LEU B N   
3082 C CA  . LEU B 146 ? 0.6720 0.5922 0.5493 -0.1044 0.0093  -0.0603 146 LEU B CA  
3083 C C   . LEU B 146 ? 0.6912 0.6212 0.5602 -0.1166 0.0073  -0.0616 146 LEU B C   
3084 O O   . LEU B 146 ? 0.7030 0.6409 0.5732 -0.1214 0.0050  -0.0597 146 LEU B O   
3085 C CB  . LEU B 146 ? 0.7216 0.6518 0.6088 -0.0969 0.0058  -0.0525 146 LEU B CB  
3086 C CG  . LEU B 146 ? 0.7533 0.6921 0.6449 -0.0917 0.0036  -0.0462 146 LEU B CG  
3087 C CD1 . LEU B 146 ? 0.8248 0.7715 0.7270 -0.0853 0.0023  -0.0395 146 LEU B CD1 
3088 C CD2 . LEU B 146 ? 0.5909 0.5419 0.4771 -0.0991 0.0006  -0.0433 146 LEU B CD2 
3089 N N   . GLU B 147 ? 0.6758 0.6059 0.5359 -0.1224 0.0083  -0.0647 147 GLU B N   
3090 C CA  . GLU B 147 ? 0.7381 0.6778 0.5871 -0.1365 0.0069  -0.0673 147 GLU B CA  
3091 C C   . GLU B 147 ? 0.8440 0.7785 0.6885 -0.1459 0.0095  -0.0737 147 GLU B C   
3092 O O   . GLU B 147 ? 0.8396 0.7881 0.6812 -0.1551 0.0054  -0.0714 147 GLU B O   
3093 C CB  . GLU B 147 ? 0.7232 0.6864 0.5751 -0.1388 -0.0006 -0.0569 147 GLU B CB  
3094 C CG  . GLU B 147 ? 0.8480 0.8193 0.6949 -0.1409 -0.0022 -0.0542 147 GLU B CG  
3095 C CD  . GLU B 147 ? 1.0413 1.0382 0.8916 -0.1447 -0.0095 -0.0424 147 GLU B CD  
3096 O OE1 . GLU B 147 ? 1.0833 1.0939 0.9325 -0.1533 -0.0132 -0.0395 147 GLU B OE1 
3097 O OE2 . GLU B 147 ? 1.1453 1.1490 1.0018 -0.1377 -0.0113 -0.0346 147 GLU B OE2 
3098 N N   . SER B 148 ? 0.9009 0.8160 0.7460 -0.1435 0.0165  -0.0809 148 SER B N   
3099 C CA  . SER B 148 ? 0.8044 0.7135 0.6482 -0.1508 0.0196  -0.0858 148 SER B CA  
3100 C C   . SER B 148 ? 0.7859 0.6748 0.6231 -0.1567 0.0296  -0.0969 148 SER B C   
3101 O O   . SER B 148 ? 0.7425 0.6280 0.5737 -0.1682 0.0329  -0.1031 148 SER B O   
3102 C CB  . SER B 148 ? 0.6880 0.5951 0.5444 -0.1407 0.0183  -0.0804 148 SER B CB  
3103 O OG  . SER B 148 ? 0.6914 0.5829 0.5539 -0.1309 0.0234  -0.0817 148 SER B OG  
3104 N N   . ILE B 149 ? 0.8353 0.7105 0.6740 -0.1499 0.0353  -0.0997 149 ILE B N   
3105 C CA  . ILE B 149 ? 0.8718 0.7277 0.7055 -0.1556 0.0464  -0.1099 149 ILE B CA  
3106 C C   . ILE B 149 ? 0.9035 0.7627 0.7210 -0.1711 0.0486  -0.1181 149 ILE B C   
3107 O O   . ILE B 149 ? 0.8817 0.7260 0.6927 -0.1801 0.0585  -0.1284 149 ILE B O   
3108 C CB  . ILE B 149 ? 0.7940 0.6368 0.6343 -0.1445 0.0520  -0.1096 149 ILE B CB  
3109 C CG1 . ILE B 149 ? 0.7775 0.5986 0.6212 -0.1458 0.0645  -0.1165 149 ILE B CG1 
3110 C CG2 . ILE B 149 ? 0.8362 0.6832 0.6680 -0.1462 0.0514  -0.1112 149 ILE B CG2 
3111 C CD1 . ILE B 149 ? 0.8272 0.6369 0.6809 -0.1341 0.0701  -0.1139 149 ILE B CD1 
3112 N N   . ILE B 150 ? 0.9589 0.8379 0.7698 -0.1750 0.0400  -0.1134 150 ILE B N   
3113 C CA  . ILE B 150 ? 1.0169 0.9043 0.8113 -0.1916 0.0403  -0.1196 150 ILE B CA  
3114 C C   . ILE B 150 ? 1.0349 0.9209 0.8224 -0.2062 0.0429  -0.1265 150 ILE B C   
3115 O O   . ILE B 150 ? 1.0539 0.9317 0.8278 -0.2206 0.0506  -0.1381 150 ILE B O   
3116 C CB  . ILE B 150 ? 0.9751 0.8885 0.7674 -0.1923 0.0288  -0.1093 150 ILE B CB  
3117 C CG1 . ILE B 150 ? 0.9339 0.8630 0.7378 -0.1865 0.0196  -0.0980 150 ILE B CG1 
3118 C CG2 . ILE B 150 ? 0.9135 0.8264 0.7101 -0.1807 0.0280  -0.1045 150 ILE B CG2 
3119 C CD1 . ILE B 150 ? 0.9840 0.9388 0.7898 -0.1859 0.0096  -0.0860 150 ILE B CD1 
3120 N N   . HIS B 151 ? 0.9397 0.8335 0.7361 -0.2034 0.0372  -0.1200 151 HIS B N   
3121 C CA  . HIS B 151 ? 0.9264 0.8208 0.7180 -0.2168 0.0386  -0.1252 151 HIS B CA  
3122 C C   . HIS B 151 ? 0.9784 0.8466 0.7744 -0.2160 0.0505  -0.1339 151 HIS B C   
3123 O O   . HIS B 151 ? 1.0053 0.8714 0.8002 -0.2253 0.0525  -0.1376 151 HIS B O   
3124 C CB  . HIS B 151 ? 0.8387 0.7525 0.6394 -0.2137 0.0281  -0.1138 151 HIS B CB  
3125 C CG  . HIS B 151 ? 1.0296 0.9711 0.8286 -0.2156 0.0169  -0.1035 151 HIS B CG  
3126 N ND1 . HIS B 151 ? 1.0782 1.0290 0.8884 -0.2005 0.0108  -0.0920 151 HIS B ND1 
3127 C CD2 . HIS B 151 ? 1.1104 1.0733 0.8992 -0.2309 0.0109  -0.1018 151 HIS B CD2 
3128 C CE1 . HIS B 151 ? 1.0789 1.0548 0.8874 -0.2054 0.0022  -0.0831 151 HIS B CE1 
3129 N NE2 . HIS B 151 ? 1.0782 1.0631 0.8738 -0.2238 0.0015  -0.0881 151 HIS B NE2 
3130 N N   . MET B 152 ? 0.9797 0.8295 0.7820 -0.2055 0.0584  -0.1361 152 MET B N   
3131 C CA  . MET B 152 ? 0.9945 0.8231 0.8051 -0.2037 0.0687  -0.1408 152 MET B CA  
3132 C C   . MET B 152 ? 1.1185 0.9260 0.9200 -0.2142 0.0834  -0.1549 152 MET B C   
3133 O O   . MET B 152 ? 1.2700 1.0754 1.0623 -0.2168 0.0867  -0.1598 152 MET B O   
3134 C CB  . MET B 152 ? 0.8576 0.6783 0.6856 -0.1845 0.0693  -0.1324 152 MET B CB  
3135 C CG  . MET B 152 ? 0.8260 0.6647 0.6628 -0.1752 0.0570  -0.1201 152 MET B CG  
3136 S SD  . MET B 152 ? 0.9618 0.7948 0.8167 -0.1553 0.0565  -0.1103 152 MET B SD  
3137 C CE  . MET B 152 ? 0.9544 0.8115 0.8133 -0.1496 0.0424  -0.0992 152 MET B CE  
3138 N N   . PRO B 153 ? 1.1633 0.9546 0.9670 -0.2210 0.0932  -0.1619 153 PRO B N   
3139 C CA  . PRO B 153 ? 1.2188 0.9893 1.0125 -0.2338 0.1089  -0.1771 153 PRO B CA  
3140 C C   . PRO B 153 ? 1.1471 0.8997 0.9459 -0.2242 0.1198  -0.1797 153 PRO B C   
3141 O O   . PRO B 153 ? 1.2005 0.9535 0.9860 -0.2310 0.1228  -0.1868 153 PRO B O   
3142 C CB  . PRO B 153 ? 1.2073 0.9624 1.0088 -0.2383 0.1175  -0.1809 153 PRO B CB  
3143 C CG  . PRO B 153 ? 1.1240 0.8918 0.9410 -0.2253 0.1061  -0.1663 153 PRO B CG  
3144 C CD  . PRO B 153 ? 1.0503 0.8446 0.8627 -0.2211 0.0898  -0.1572 153 PRO B CD  
3145 N N   . ASP B 154 ? 1.0067 0.7467 0.8249 -0.2084 0.1248  -0.1727 154 ASP B N   
3146 C CA  . ASP B 154 ? 0.8846 0.6074 0.7107 -0.1992 0.1365  -0.1740 154 ASP B CA  
3147 C C   . ASP B 154 ? 0.9186 0.6518 0.7580 -0.1803 0.1270  -0.1597 154 ASP B C   
3148 O O   . ASP B 154 ? 0.9553 0.6893 0.8109 -0.1690 0.1239  -0.1495 154 ASP B O   
3149 C CB  . ASP B 154 ? 0.7842 0.4810 0.6232 -0.1984 0.1539  -0.1783 154 ASP B CB  
3150 C CG  . ASP B 154 ? 1.0926 0.7738 0.9448 -0.1860 0.1654  -0.1759 154 ASP B CG  
3151 O OD1 . ASP B 154 ? 1.2447 0.9220 1.0864 -0.1899 0.1706  -0.1833 154 ASP B OD1 
3152 O OD2 . ASP B 154 ? 1.2371 0.9115 1.1103 -0.1726 0.1688  -0.1657 154 ASP B OD2 
3153 N N   . ARG B 155 ? 0.8856 0.6268 0.7180 -0.1775 0.1227  -0.1590 155 ARG B N   
3154 C CA  . ARG B 155 ? 0.8062 0.5561 0.6505 -0.1610 0.1148  -0.1467 155 ARG B CA  
3155 C C   . ARG B 155 ? 0.8842 0.6186 0.7482 -0.1485 0.1243  -0.1411 155 ARG B C   
3156 O O   . ARG B 155 ? 0.8828 0.6252 0.7597 -0.1360 0.1169  -0.1293 155 ARG B O   
3157 C CB  . ARG B 155 ? 0.7278 0.4854 0.5620 -0.1609 0.1114  -0.1480 155 ARG B CB  
3158 C CG  . ARG B 155 ? 0.8603 0.6412 0.6821 -0.1667 0.0969  -0.1453 155 ARG B CG  
3159 C CD  . ARG B 155 ? 1.0363 0.8234 0.8464 -0.1700 0.0958  -0.1481 155 ARG B CD  
3160 N NE  . ARG B 155 ? 1.1268 0.9249 0.9181 -0.1871 0.0929  -0.1551 155 ARG B NE  
3161 C CZ  . ARG B 155 ? 1.1155 0.9368 0.9009 -0.1899 0.0795  -0.1485 155 ARG B CZ  
3162 N NH1 . ARG B 155 ? 1.1176 0.9507 0.9143 -0.1766 0.0692  -0.1363 155 ARG B NH1 
3163 N NH2 . ARG B 155 ? 1.0726 0.9059 0.8416 -0.2063 0.0768  -0.1536 155 ARG B NH2 
3164 N N   . ALA B 156 ? 0.9765 0.6894 0.8436 -0.1519 0.1412  -0.1490 156 ALA B N   
3165 C CA  . ALA B 156 ? 0.8805 0.5805 0.7691 -0.1393 0.1506  -0.1413 156 ALA B CA  
3166 C C   . ALA B 156 ? 0.9582 0.6606 0.8616 -0.1336 0.1472  -0.1317 156 ALA B C   
3167 O O   . ALA B 156 ? 0.8378 0.5447 0.7576 -0.1205 0.1440  -0.1190 156 ALA B O   
3168 C CB  . ALA B 156 ? 0.7624 0.4378 0.6534 -0.1441 0.1713  -0.1514 156 ALA B CB  
3169 N N   . GLN B 157 ? 0.9748 0.6755 0.8722 -0.1439 0.1474  -0.1372 157 GLN B N   
3170 C CA  . GLN B 157 ? 0.9429 0.6448 0.8548 -0.1390 0.1455  -0.1282 157 GLN B CA  
3171 C C   . GLN B 157 ? 0.9393 0.6640 0.8529 -0.1308 0.1276  -0.1165 157 GLN B C   
3172 O O   . GLN B 157 ? 0.7164 0.4452 0.6460 -0.1196 0.1252  -0.1043 157 GLN B O   
3173 C CB  . GLN B 157 ? 0.7338 0.4286 0.6381 -0.1529 0.1500  -0.1375 157 GLN B CB  
3174 C CG  . GLN B 157 ? 1.0969 0.7658 1.0082 -0.1576 0.1702  -0.1454 157 GLN B CG  
3175 C CD  . GLN B 157 ? 1.2694 0.9307 1.1871 -0.1634 0.1750  -0.1459 157 GLN B CD  
3176 O OE1 . GLN B 157 ? 1.2292 0.9058 1.1484 -0.1619 0.1625  -0.1384 157 GLN B OE1 
3177 N NE2 . GLN B 157 ? 1.2845 0.9213 1.2065 -0.1703 0.1940  -0.1551 157 GLN B NE2 
3178 N N   . VAL B 158 ? 0.8554 0.5956 0.7530 -0.1371 0.1158  -0.1200 158 VAL B N   
3179 C CA  . VAL B 158 ? 0.7659 0.5268 0.6638 -0.1301 0.1003  -0.1105 158 VAL B CA  
3180 C C   . VAL B 158 ? 0.8023 0.5663 0.7112 -0.1164 0.0982  -0.1011 158 VAL B C   
3181 O O   . VAL B 158 ? 0.7582 0.5304 0.6776 -0.1080 0.0923  -0.0907 158 VAL B O   
3182 C CB  . VAL B 158 ? 0.7353 0.5107 0.6158 -0.1381 0.0907  -0.1155 158 VAL B CB  
3183 C CG1 . VAL B 158 ? 0.6743 0.4686 0.5567 -0.1300 0.0771  -0.1060 158 VAL B CG1 
3184 C CG2 . VAL B 158 ? 0.8135 0.5895 0.6848 -0.1519 0.0912  -0.1225 158 VAL B CG2 
3185 N N   . LEU B 159 ? 0.8123 0.5698 0.7186 -0.1149 0.1035  -0.1046 159 LEU B N   
3186 C CA  . LEU B 159 ? 0.7872 0.5488 0.7037 -0.1029 0.1012  -0.0957 159 LEU B CA  
3187 C C   . LEU B 159 ? 0.7997 0.5547 0.7359 -0.0945 0.1075  -0.0861 159 LEU B C   
3188 O O   . LEU B 159 ? 0.8651 0.6305 0.8103 -0.0855 0.1010  -0.0754 159 LEU B O   
3189 C CB  . LEU B 159 ? 0.7442 0.4995 0.6549 -0.1033 0.1067  -0.1012 159 LEU B CB  
3190 C CG  . LEU B 159 ? 0.7051 0.4730 0.5987 -0.1087 0.0971  -0.1059 159 LEU B CG  
3191 C CD1 . LEU B 159 ? 0.7047 0.4668 0.5911 -0.1106 0.1031  -0.1120 159 LEU B CD1 
3192 C CD2 . LEU B 159 ? 0.5962 0.3816 0.4920 -0.1013 0.0834  -0.0968 159 LEU B CD2 
3193 N N   . ALA B 160 ? 0.8917 0.6305 0.8354 -0.0976 0.1204  -0.0890 160 ALA B N   
3194 C CA  . ALA B 160 ? 0.7803 0.5151 0.7452 -0.0895 0.1262  -0.0775 160 ALA B CA  
3195 C C   . ALA B 160 ? 0.7442 0.4922 0.7133 -0.0877 0.1163  -0.0690 160 ALA B C   
3196 O O   . ALA B 160 ? 0.7483 0.5034 0.7321 -0.0793 0.1142  -0.0561 160 ALA B O   
3197 C CB  . ALA B 160 ? 0.6695 0.3822 0.6426 -0.0935 0.1440  -0.0828 160 ALA B CB  
3198 N N   . GLN B 161 ? 0.6543 0.4064 0.6111 -0.0960 0.1107  -0.0756 161 GLN B N   
3199 C CA  . GLN B 161 ? 0.7991 0.5648 0.7585 -0.0944 0.1010  -0.0681 161 GLN B CA  
3200 C C   . GLN B 161 ? 0.7846 0.5684 0.7425 -0.0872 0.0884  -0.0606 161 GLN B C   
3201 O O   . GLN B 161 ? 0.7789 0.5720 0.7468 -0.0811 0.0842  -0.0497 161 GLN B O   
3202 C CB  . GLN B 161 ? 0.7838 0.5519 0.7298 -0.1051 0.0973  -0.0768 161 GLN B CB  
3203 C CG  . GLN B 161 ? 0.8377 0.5889 0.7855 -0.1135 0.1092  -0.0837 161 GLN B CG  
3204 C CD  . GLN B 161 ? 0.8230 0.5678 0.7903 -0.1080 0.1162  -0.0739 161 GLN B CD  
3205 O OE1 . GLN B 161 ? 0.8189 0.5764 0.7928 -0.1032 0.1085  -0.0638 161 GLN B OE1 
3206 N NE2 . GLN B 161 ? 0.6692 0.3943 0.6463 -0.1086 0.1316  -0.0763 161 GLN B NE2 
3207 N N   . VAL B 162 ? 0.7426 0.5317 0.6879 -0.0884 0.0828  -0.0663 162 VAL B N   
3208 C CA  . VAL B 162 ? 0.7343 0.5382 0.6778 -0.0823 0.0724  -0.0606 162 VAL B CA  
3209 C C   . VAL B 162 ? 0.7284 0.5332 0.6857 -0.0737 0.0747  -0.0507 162 VAL B C   
3210 O O   . VAL B 162 ? 0.7930 0.6101 0.7549 -0.0691 0.0678  -0.0422 162 VAL B O   
3211 C CB  . VAL B 162 ? 0.6095 0.4163 0.5395 -0.0848 0.0684  -0.0679 162 VAL B CB  
3212 C CG1 . VAL B 162 ? 0.6036 0.4229 0.5336 -0.0781 0.0598  -0.0622 162 VAL B CG1 
3213 C CG2 . VAL B 162 ? 0.5373 0.3488 0.4550 -0.0931 0.0640  -0.0746 162 VAL B CG2 
3214 N N   . GLY B 163 ? 0.6454 0.4378 0.6096 -0.0719 0.0847  -0.0514 163 GLY B N   
3215 C CA  . GLY B 163 ? 0.7064 0.5014 0.6851 -0.0639 0.0869  -0.0406 163 GLY B CA  
3216 C C   . GLY B 163 ? 0.7430 0.5419 0.7378 -0.0602 0.0885  -0.0285 163 GLY B C   
3217 O O   . GLY B 163 ? 0.7893 0.5975 0.7953 -0.0541 0.0864  -0.0169 163 GLY B O   
3218 N N   . ARG B 164 ? 0.6396 0.4326 0.6360 -0.0643 0.0921  -0.0302 164 ARG B N   
3219 C CA  . ARG B 164 ? 0.6452 0.4430 0.6573 -0.0610 0.0935  -0.0176 164 ARG B CA  
3220 C C   . ARG B 164 ? 0.7025 0.5196 0.7094 -0.0608 0.0805  -0.0122 164 ARG B C   
3221 O O   . ARG B 164 ? 0.7992 0.6287 0.8164 -0.0564 0.0771  0.0006  164 ARG B O   
3222 C CB  . ARG B 164 ? 0.5708 0.3535 0.5875 -0.0658 0.1036  -0.0217 164 ARG B CB  
3223 C CG  . ARG B 164 ? 0.5724 0.3587 0.6059 -0.0631 0.1061  -0.0088 164 ARG B CG  
3224 C CD  . ARG B 164 ? 0.6782 0.4487 0.7139 -0.0693 0.1157  -0.0149 164 ARG B CD  
3225 N NE  . ARG B 164 ? 0.7002 0.4720 0.7171 -0.0780 0.1093  -0.0271 164 ARG B NE  
3226 C CZ  . ARG B 164 ? 0.6907 0.4761 0.7033 -0.0797 0.0997  -0.0239 164 ARG B CZ  
3227 N NH1 . ARG B 164 ? 0.6208 0.4193 0.6447 -0.0739 0.0953  -0.0098 164 ARG B NH1 
3228 N NH2 . ARG B 164 ? 0.6903 0.4775 0.6874 -0.0874 0.0944  -0.0341 164 ARG B NH2 
3229 N N   . VAL B 165 ? 0.6522 0.4728 0.6431 -0.0660 0.0736  -0.0215 165 VAL B N   
3230 C CA  . VAL B 165 ? 0.6138 0.4506 0.5989 -0.0663 0.0630  -0.0182 165 VAL B CA  
3231 C C   . VAL B 165 ? 0.7268 0.5756 0.7060 -0.0631 0.0550  -0.0167 165 VAL B C   
3232 O O   . VAL B 165 ? 0.8882 0.7507 0.8645 -0.0629 0.0476  -0.0127 165 VAL B O   
3233 C CB  . VAL B 165 ? 0.6118 0.4482 0.5843 -0.0727 0.0597  -0.0277 165 VAL B CB  
3234 C CG1 . VAL B 165 ? 0.5973 0.4227 0.5752 -0.0771 0.0673  -0.0292 165 VAL B CG1 
3235 C CG2 . VAL B 165 ? 0.6845 0.5166 0.6438 -0.0758 0.0584  -0.0388 165 VAL B CG2 
3236 N N   . LEU B 166 ? 0.6538 0.4976 0.6304 -0.0614 0.0566  -0.0206 166 LEU B N   
3237 C CA  . LEU B 166 ? 0.6434 0.4976 0.6154 -0.0588 0.0498  -0.0190 166 LEU B CA  
3238 C C   . LEU B 166 ? 0.7060 0.5701 0.6905 -0.0549 0.0491  -0.0060 166 LEU B C   
3239 O O   . LEU B 166 ? 0.7475 0.6063 0.7458 -0.0520 0.0562  0.0009  166 LEU B O   
3240 C CB  . LEU B 166 ? 0.6763 0.5226 0.6429 -0.0582 0.0521  -0.0260 166 LEU B CB  
3241 C CG  . LEU B 166 ? 0.7072 0.5556 0.6590 -0.0607 0.0464  -0.0352 166 LEU B CG  
3242 C CD1 . LEU B 166 ? 0.6728 0.5133 0.6206 -0.0605 0.0498  -0.0410 166 LEU B CD1 
3243 C CD2 . LEU B 166 ? 0.8223 0.6841 0.7705 -0.0592 0.0383  -0.0322 166 LEU B CD2 
3244 N N   . ARG B 167 ? 0.6602 0.5391 0.6404 -0.0552 0.0411  -0.0023 167 ARG B N   
3245 C CA  . ARG B 167 ? 0.7279 0.6193 0.7179 -0.0531 0.0391  0.0099  167 ARG B CA  
3246 C C   . ARG B 167 ? 0.7145 0.6034 0.7073 -0.0502 0.0407  0.0103  167 ARG B C   
3247 O O   . ARG B 167 ? 0.8284 0.7089 0.8121 -0.0505 0.0411  0.0002  167 ARG B O   
3248 C CB  . ARG B 167 ? 0.8127 0.7202 0.7946 -0.0562 0.0307  0.0117  167 ARG B CB  
3249 C CG  . ARG B 167 ? 0.6652 0.5764 0.6447 -0.0589 0.0294  0.0119  167 ARG B CG  
3250 C CD  . ARG B 167 ? 0.6376 0.5621 0.6066 -0.0625 0.0226  0.0104  167 ARG B CD  
3251 N NE  . ARG B 167 ? 0.8266 0.7567 0.7969 -0.0647 0.0221  0.0141  167 ARG B NE  
3252 C CZ  . ARG B 167 ? 0.7499 0.6875 0.7101 -0.0681 0.0183  0.0100  167 ARG B CZ  
3253 N NH1 . ARG B 167 ? 0.6983 0.6373 0.6473 -0.0694 0.0154  0.0019  167 ARG B NH1 
3254 N NH2 . ARG B 167 ? 0.6479 0.5904 0.6100 -0.0699 0.0184  0.0139  167 ARG B NH2 
3255 N N   . PRO B 168 ? 0.7336 0.6307 0.7398 -0.0476 0.0419  0.0228  168 PRO B N   
3256 C CA  . PRO B 168 ? 0.7434 0.6397 0.7529 -0.0450 0.0431  0.0238  168 PRO B CA  
3257 C C   . PRO B 168 ? 0.7461 0.6503 0.7416 -0.0479 0.0350  0.0177  168 PRO B C   
3258 O O   . PRO B 168 ? 0.6529 0.5701 0.6421 -0.0515 0.0283  0.0193  168 PRO B O   
3259 C CB  . PRO B 168 ? 0.6161 0.5240 0.6445 -0.0421 0.0450  0.0412  168 PRO B CB  
3260 C CG  . PRO B 168 ? 0.6737 0.5806 0.7117 -0.0417 0.0488  0.0479  168 PRO B CG  
3261 C CD  . PRO B 168 ? 0.7250 0.6320 0.7465 -0.0465 0.0432  0.0377  168 PRO B CD  
3262 N N   . GLY B 169 ? 0.7789 0.6744 0.7693 -0.0465 0.0366  0.0101  169 GLY B N   
3263 C CA  . GLY B 169 ? 0.6935 0.5918 0.6704 -0.0490 0.0308  0.0021  169 GLY B CA  
3264 C C   . GLY B 169 ? 0.6776 0.5687 0.6412 -0.0510 0.0294  -0.0098 169 GLY B C   
3265 O O   . GLY B 169 ? 0.7210 0.6126 0.6748 -0.0524 0.0258  -0.0164 169 GLY B O   
3266 N N   . GLY B 170 ? 0.6173 0.5021 0.5810 -0.0516 0.0322  -0.0119 170 GLY B N   
3267 C CA  . GLY B 170 ? 0.6500 0.5297 0.6025 -0.0538 0.0308  -0.0218 170 GLY B CA  
3268 C C   . GLY B 170 ? 0.6880 0.5573 0.6352 -0.0533 0.0337  -0.0296 170 GLY B C   
3269 O O   . GLY B 170 ? 0.7285 0.5922 0.6808 -0.0512 0.0380  -0.0283 170 GLY B O   
3270 N N   . ARG B 171 ? 0.6071 0.4748 0.5444 -0.0555 0.0314  -0.0371 171 ARG B N   
3271 C CA  . ARG B 171 ? 0.5983 0.4593 0.5294 -0.0561 0.0329  -0.0438 171 ARG B CA  
3272 C C   . ARG B 171 ? 0.6351 0.4927 0.5598 -0.0598 0.0334  -0.0495 171 ARG B C   
3273 O O   . ARG B 171 ? 0.6661 0.5292 0.5885 -0.0614 0.0301  -0.0495 171 ARG B O   
3274 C CB  . ARG B 171 ? 0.5811 0.4470 0.5067 -0.0550 0.0284  -0.0457 171 ARG B CB  
3275 C CG  . ARG B 171 ? 0.7049 0.5722 0.6351 -0.0525 0.0287  -0.0419 171 ARG B CG  
3276 C CD  . ARG B 171 ? 0.7646 0.6355 0.6897 -0.0522 0.0251  -0.0443 171 ARG B CD  
3277 N NE  . ARG B 171 ? 0.8976 0.7760 0.8258 -0.0522 0.0224  -0.0399 171 ARG B NE  
3278 C CZ  . ARG B 171 ? 0.9313 0.8110 0.8635 -0.0511 0.0228  -0.0367 171 ARG B CZ  
3279 N NH1 . ARG B 171 ? 1.0441 0.9172 0.9779 -0.0491 0.0262  -0.0377 171 ARG B NH1 
3280 N NH2 . ARG B 171 ? 0.9392 0.8276 0.8732 -0.0528 0.0199  -0.0327 171 ARG B NH2 
3281 N N   . LEU B 172 ? 0.6559 0.5051 0.5776 -0.0620 0.0380  -0.0543 172 LEU B N   
3282 C CA  . LEU B 172 ? 0.6479 0.4952 0.5616 -0.0674 0.0383  -0.0603 172 LEU B CA  
3283 C C   . LEU B 172 ? 0.6919 0.5424 0.5981 -0.0680 0.0354  -0.0634 172 LEU B C   
3284 O O   . LEU B 172 ? 0.6948 0.5417 0.6012 -0.0661 0.0376  -0.0638 172 LEU B O   
3285 C CB  . LEU B 172 ? 0.5699 0.4055 0.4844 -0.0711 0.0464  -0.0642 172 LEU B CB  
3286 C CG  . LEU B 172 ? 0.6431 0.4753 0.5473 -0.0788 0.0483  -0.0720 172 LEU B CG  
3287 C CD1 . LEU B 172 ? 0.7129 0.5520 0.6134 -0.0834 0.0439  -0.0726 172 LEU B CD1 
3288 C CD2 . LEU B 172 ? 0.6125 0.4306 0.5179 -0.0822 0.0587  -0.0767 172 LEU B CD2 
3289 N N   . VAL B 173 ? 0.5785 0.4369 0.4796 -0.0704 0.0306  -0.0643 173 VAL B N   
3290 C CA  . VAL B 173 ? 0.6881 0.5512 0.5831 -0.0717 0.0280  -0.0658 173 VAL B CA  
3291 C C   . VAL B 173 ? 0.6924 0.5590 0.5811 -0.0790 0.0273  -0.0687 173 VAL B C   
3292 O O   . VAL B 173 ? 0.6987 0.5688 0.5888 -0.0808 0.0257  -0.0678 173 VAL B O   
3293 C CB  . VAL B 173 ? 0.6798 0.5513 0.5771 -0.0672 0.0230  -0.0620 173 VAL B CB  
3294 C CG1 . VAL B 173 ? 0.9089 0.7864 0.8087 -0.0671 0.0204  -0.0599 173 VAL B CG1 
3295 C CG2 . VAL B 173 ? 0.6800 0.5576 0.5733 -0.0686 0.0207  -0.0617 173 VAL B CG2 
3296 N N   . LEU B 174 ? 0.6747 0.5411 0.5561 -0.0839 0.0286  -0.0721 174 LEU B N   
3297 C CA  . LEU B 174 ? 0.6516 0.5224 0.5252 -0.0931 0.0281  -0.0754 174 LEU B CA  
3298 C C   . LEU B 174 ? 0.7685 0.6471 0.6347 -0.0970 0.0260  -0.0754 174 LEU B C   
3299 O O   . LEU B 174 ? 0.8240 0.7004 0.6903 -0.0933 0.0270  -0.0747 174 LEU B O   
3300 C CB  . LEU B 174 ? 0.5680 0.4266 0.4384 -0.0992 0.0354  -0.0820 174 LEU B CB  
3301 C CG  . LEU B 174 ? 0.6580 0.5055 0.5246 -0.1005 0.0426  -0.0871 174 LEU B CG  
3302 C CD1 . LEU B 174 ? 0.6439 0.4956 0.4976 -0.1109 0.0432  -0.0924 174 LEU B CD1 
3303 C CD2 . LEU B 174 ? 0.6199 0.4518 0.4919 -0.1004 0.0517  -0.0906 174 LEU B CD2 
3304 N N   . THR B 175 ? 0.7258 0.6148 0.5858 -0.1052 0.0228  -0.0753 175 THR B N   
3305 C CA  . THR B 175 ? 0.7313 0.6284 0.5822 -0.1123 0.0216  -0.0760 175 THR B CA  
3306 C C   . THR B 175 ? 0.7624 0.6552 0.6018 -0.1250 0.0261  -0.0845 175 THR B C   
3307 O O   . THR B 175 ? 0.9353 0.8212 0.7752 -0.1283 0.0290  -0.0885 175 THR B O   
3308 C CB  . THR B 175 ? 0.7392 0.6558 0.5926 -0.1126 0.0140  -0.0673 175 THR B CB  
3309 O OG1 . THR B 175 ? 0.7579 0.6824 0.6120 -0.1175 0.0110  -0.0658 175 THR B OG1 
3310 C CG2 . THR B 175 ? 0.6211 0.5393 0.4857 -0.1005 0.0116  -0.0602 175 THR B CG2 
3311 N N   . ASP B 176 ? 0.8935 0.7907 0.7222 -0.1329 0.0270  -0.0873 176 ASP B N   
3312 C CA  . ASP B 176 ? 0.9418 0.8330 0.7572 -0.1463 0.0332  -0.0974 176 ASP B CA  
3313 C C   . ASP B 176 ? 0.9031 0.8060 0.7065 -0.1550 0.0315  -0.0976 176 ASP B C   
3314 O O   . ASP B 176 ? 0.9619 0.8706 0.7685 -0.1484 0.0286  -0.0916 176 ASP B O   
3315 C CB  . ASP B 176 ? 0.9681 0.8364 0.7852 -0.1433 0.0441  -0.1056 176 ASP B CB  
3316 C CG  . ASP B 176 ? 0.9435 0.8012 0.7510 -0.1559 0.0523  -0.1166 176 ASP B CG  
3317 O OD1 . ASP B 176 ? 0.7894 0.6585 0.5865 -0.1687 0.0490  -0.1188 176 ASP B OD1 
3318 O OD2 . ASP B 176 ? 0.8864 0.7246 0.6977 -0.1533 0.0626  -0.1226 176 ASP B OD2 
3319 N N   . PHE B 177 ? 0.9428 0.8493 0.7320 -0.1707 0.0337  -0.1048 177 PHE B N   
3320 C CA  . PHE B 177 ? 0.9898 0.9073 0.7649 -0.1816 0.0333  -0.1064 177 PHE B CA  
3321 C C   . PHE B 177 ? 1.0478 0.9460 0.8154 -0.1835 0.0448  -0.1175 177 PHE B C   
3322 O O   . PHE B 177 ? 1.0877 0.9653 0.8565 -0.1834 0.0545  -0.1267 177 PHE B O   
3323 C CB  . PHE B 177 ? 0.8413 0.7739 0.6029 -0.1998 0.0301  -0.1091 177 PHE B CB  
3324 C CG  . PHE B 177 ? 0.8227 0.7796 0.5916 -0.1989 0.0182  -0.0958 177 PHE B CG  
3325 C CD1 . PHE B 177 ? 0.8947 0.8675 0.6728 -0.1897 0.0106  -0.0824 177 PHE B CD1 
3326 C CD2 . PHE B 177 ? 0.9463 0.9100 0.7144 -0.2070 0.0153  -0.0962 177 PHE B CD2 
3327 C CE1 . PHE B 177 ? 0.8954 0.8904 0.6829 -0.1878 0.0010  -0.0690 177 PHE B CE1 
3328 C CE2 . PHE B 177 ? 1.0267 1.0138 0.8035 -0.2055 0.0048  -0.0827 177 PHE B CE2 
3329 C CZ  . PHE B 177 ? 0.9658 0.9684 0.7529 -0.1955 -0.0019 -0.0689 177 PHE B CZ  
3330 N N   . PHE B 178 ? 1.0280 0.9329 0.7896 -0.1845 0.0445  -0.1158 178 PHE B N   
3331 C CA  . PHE B 178 ? 0.9826 0.8707 0.7365 -0.1869 0.0560  -0.1260 178 PHE B CA  
3332 C C   . PHE B 178 ? 1.1014 1.0044 0.8410 -0.1968 0.0543  -0.1255 178 PHE B C   
3333 O O   . PHE B 178 ? 1.0841 1.0106 0.8229 -0.1990 0.0436  -0.1149 178 PHE B O   
3334 C CB  . PHE B 178 ? 0.8555 0.7276 0.6246 -0.1696 0.0603  -0.1235 178 PHE B CB  
3335 C CG  . PHE B 178 ? 0.9281 0.8110 0.7031 -0.1602 0.0540  -0.1132 178 PHE B CG  
3336 C CD1 . PHE B 178 ? 0.9322 0.8318 0.7165 -0.1533 0.0425  -0.1007 178 PHE B CD1 
3337 C CD2 . PHE B 178 ? 0.8971 0.7722 0.6698 -0.1578 0.0606  -0.1161 178 PHE B CD2 
3338 C CE1 . PHE B 178 ? 0.8910 0.7986 0.6818 -0.1448 0.0380  -0.0915 178 PHE B CE1 
3339 C CE2 . PHE B 178 ? 0.8876 0.7719 0.6663 -0.1494 0.0552  -0.1067 178 PHE B CE2 
3340 C CZ  . PHE B 178 ? 0.8891 0.7891 0.6768 -0.1430 0.0440  -0.0945 178 PHE B CZ  
3341 N N   . GLU B 179 ? 1.2437 1.1329 0.9726 -0.2029 0.0658  -0.1367 179 GLU B N   
3342 C CA  . GLU B 179 ? 1.1015 1.0026 0.8134 -0.2152 0.0667  -0.1392 179 GLU B CA  
3343 C C   . GLU B 179 ? 1.0815 0.9806 0.8009 -0.2028 0.0673  -0.1331 179 GLU B C   
3344 O O   . GLU B 179 ? 1.0959 0.9742 0.8197 -0.1960 0.0780  -0.1396 179 GLU B O   
3345 C CB  . GLU B 179 ? 1.2402 1.1267 0.9341 -0.2315 0.0804  -0.1568 179 GLU B CB  
3346 C CG  . GLU B 179 ? 1.4949 1.4012 1.1659 -0.2526 0.0780  -0.1604 179 GLU B CG  
3347 C CD  . GLU B 179 ? 1.6210 1.5130 1.2738 -0.2712 0.0910  -0.1791 179 GLU B CD  
3348 O OE1 . GLU B 179 ? 1.5758 1.4403 1.2357 -0.2658 0.1034  -0.1888 179 GLU B OE1 
3349 O OE2 . GLU B 179 ? 1.7258 1.6344 1.3583 -0.2914 0.0892  -0.1835 179 GLU B OE2 
3350 N N   . ARG B 180 ? 1.1559 1.0770 0.8787 -0.1994 0.0561  -0.1196 180 ARG B N   
3351 C CA  . ARG B 180 ? 1.1030 1.0225 0.8355 -0.1864 0.0558  -0.1125 180 ARG B CA  
3352 C C   . ARG B 180 ? 1.1883 1.1015 0.9072 -0.1938 0.0656  -0.1211 180 ARG B C   
3353 O O   . ARG B 180 ? 1.1985 1.1010 0.9251 -0.1833 0.0705  -0.1203 180 ARG B O   
3354 C CB  . ARG B 180 ? 1.0584 1.0025 0.7985 -0.1817 0.0427  -0.0958 180 ARG B CB  
3355 C CG  . ARG B 180 ? 0.9940 0.9425 0.7503 -0.1718 0.0343  -0.0866 180 ARG B CG  
3356 C CD  . ARG B 180 ? 0.9252 0.8988 0.6895 -0.1689 0.0228  -0.0700 180 ARG B CD  
3357 N NE  . ARG B 180 ? 0.8282 0.8002 0.6061 -0.1547 0.0215  -0.0612 180 ARG B NE  
3358 C CZ  . ARG B 180 ? 0.9415 0.9320 0.7287 -0.1503 0.0139  -0.0464 180 ARG B CZ  
3359 N NH1 . ARG B 180 ? 0.9622 0.9763 0.7475 -0.1582 0.0064  -0.0371 180 ARG B NH1 
3360 N NH2 . ARG B 180 ? 1.0375 1.0234 0.8368 -0.1380 0.0141  -0.0400 180 ARG B NH2 
3361 N N   . ALA B 181 ? 1.2312 1.1510 0.9296 -0.2125 0.0691  -0.1299 181 ALA B N   
3362 C CA  . ALA B 181 ? 1.2922 1.2075 0.9731 -0.2241 0.0795  -0.1405 181 ALA B CA  
3363 C C   . ALA B 181 ? 1.4016 1.3260 1.0606 -0.2466 0.0809  -0.1500 181 ALA B C   
3364 O O   . ALA B 181 ? 1.3704 1.3121 1.0296 -0.2517 0.0702  -0.1434 181 ALA B O   
3365 C CB  . ALA B 181 ? 1.2664 1.1987 0.9467 -0.2214 0.0740  -0.1298 181 ALA B CB  
3366 N N   . PRO B 182 ? 1.4841 1.3978 1.1239 -0.2613 0.0943  -0.1659 182 PRO B N   
3367 C CA  . PRO B 182 ? 1.4564 1.3787 1.0731 -0.2852 0.0963  -0.1766 182 PRO B CA  
3368 C C   . PRO B 182 ? 1.3889 1.3476 0.9987 -0.2954 0.0797  -0.1633 182 PRO B C   
3369 O O   . PRO B 182 ? 1.2674 1.2459 0.8817 -0.2898 0.0705  -0.1489 182 PRO B O   
3370 C CB  . PRO B 182 ? 1.4282 1.3413 1.0307 -0.2953 0.1108  -0.1887 182 PRO B CB  
3371 C CG  . PRO B 182 ? 1.3779 1.2623 0.9922 -0.2788 0.1226  -0.1939 182 PRO B CG  
3372 C CD  . PRO B 182 ? 1.3817 1.2745 1.0202 -0.2570 0.1091  -0.1750 182 PRO B CD  
3373 N N   . LEU B 183 ? 1.4199 1.3878 1.0208 -0.3098 0.0758  -0.1667 183 LEU B N   
3374 C CA  . LEU B 183 ? 1.5020 1.5053 1.1016 -0.3172 0.0590  -0.1513 183 LEU B CA  
3375 C C   . LEU B 183 ? 1.6904 1.7195 1.2736 -0.3358 0.0571  -0.1488 183 LEU B C   
3376 O O   . LEU B 183 ? 1.7485 1.7687 1.3231 -0.3475 0.0691  -0.1608 183 LEU B O   
3377 C CB  . LEU B 183 ? 1.4949 1.4998 1.0965 -0.3236 0.0553  -0.1534 183 LEU B CB  
3378 C CG  . LEU B 183 ? 1.4180 1.4189 1.0450 -0.3034 0.0475  -0.1419 183 LEU B CG  
3379 C CD1 . LEU B 183 ? 1.4294 1.4187 1.0553 -0.3102 0.0506  -0.1515 183 LEU B CD1 
3380 C CD2 . LEU B 183 ? 1.2886 1.3225 0.9275 -0.2976 0.0306  -0.1193 183 LEU B CD2 
3381 N N   . ALA B 184 ? 1.7402 1.8024 1.3223 -0.3375 0.0423  -0.1312 184 ALA B N   
3382 C CA  . ALA B 184 ? 1.6943 1.7885 1.2663 -0.3551 0.0370  -0.1236 184 ALA B CA  
3383 C C   . ALA B 184 ? 1.7503 1.8508 1.3179 -0.3720 0.0384  -0.1294 184 ALA B C   
3384 O O   . ALA B 184 ? 1.7812 1.8743 1.3563 -0.3683 0.0361  -0.1307 184 ALA B O   
3385 C CB  . ALA B 184 ? 1.5858 1.7164 1.1630 -0.3521 0.0197  -0.0999 184 ALA B CB  
3386 N N   . PRO B 185 ? 1.7956 1.9091 1.3509 -0.3913 0.0428  -0.1336 185 PRO B N   
3387 C CA  . PRO B 185 ? 1.7726 1.8923 1.3226 -0.4085 0.0447  -0.1391 185 PRO B CA  
3388 C C   . PRO B 185 ? 1.7425 1.8966 1.2987 -0.4135 0.0279  -0.1214 185 PRO B C   
3389 O O   . PRO B 185 ? 1.7268 1.8779 1.2847 -0.4189 0.0282  -0.1252 185 PRO B O   
3390 C CB  . PRO B 185 ? 1.7244 1.8512 1.2589 -0.4280 0.0534  -0.1470 185 PRO B CB  
3391 C CG  . PRO B 185 ? 1.6700 1.7764 1.2030 -0.4173 0.0626  -0.1536 185 PRO B CG  
3392 C CD  . PRO B 185 ? 1.7076 1.8216 1.2522 -0.3980 0.0505  -0.1383 185 PRO B CD  
3393 N N   . GLU B 186 ? 1.6849 1.8720 1.2460 -0.4113 0.0136  -0.1010 186 GLU B N   
3394 C CA  . GLU B 186 ? 1.6296 1.8506 1.2000 -0.4147 -0.0020 -0.0820 186 GLU B CA  
3395 C C   . GLU B 186 ? 1.6406 1.8476 1.2242 -0.3988 -0.0064 -0.0801 186 GLU B C   
3396 O O   . GLU B 186 ? 1.6110 1.8349 1.2010 -0.4035 -0.0144 -0.0720 186 GLU B O   
3397 C CB  . GLU B 186 ? 1.6097 1.8675 1.1867 -0.4124 -0.0154 -0.0584 186 GLU B CB  
3398 C CG  . GLU B 186 ? 1.7100 1.9778 1.2760 -0.4225 -0.0112 -0.0594 186 GLU B CG  
3399 C CD  . GLU B 186 ? 1.8782 2.1570 1.4300 -0.4477 -0.0054 -0.0683 186 GLU B CD  
3400 O OE1 . GLU B 186 ? 1.9109 2.2290 1.4645 -0.4611 -0.0155 -0.0521 186 GLU B OE1 
3401 O OE2 . GLU B 186 ? 1.9721 2.2211 1.5117 -0.4544 0.0097  -0.0906 186 GLU B OE2 
3402 N N   . GLY B 187 ? 1.6740 1.8508 1.2621 -0.3804 -0.0011 -0.0875 187 GLY B N   
3403 C CA  . GLY B 187 ? 1.6519 1.8155 1.2525 -0.3653 -0.0053 -0.0857 187 GLY B CA  
3404 C C   . GLY B 187 ? 1.7155 1.8517 1.3159 -0.3675 0.0042  -0.1027 187 GLY B C   
3405 O O   . GLY B 187 ? 1.7279 1.8651 1.3380 -0.3623 -0.0021 -0.0984 187 GLY B O   
3406 N N   . ARG B 188 ? 1.7284 1.8401 1.3187 -0.3748 0.0198  -0.1213 188 ARG B N   
3407 C CA  . ARG B 188 ? 1.6506 1.7327 1.2426 -0.3744 0.0307  -0.1368 188 ARG B CA  
3408 C C   . ARG B 188 ? 1.5135 1.6132 1.1054 -0.3876 0.0251  -0.1332 188 ARG B C   
3409 O O   . ARG B 188 ? 1.5135 1.5939 1.1105 -0.3847 0.0301  -0.1413 188 ARG B O   
3410 C CB  . ARG B 188 ? 1.7018 1.7576 1.2841 -0.3807 0.0491  -0.1552 188 ARG B CB  
3411 C CG  . ARG B 188 ? 1.7401 1.7834 1.3198 -0.3727 0.0558  -0.1589 188 ARG B CG  
3412 C CD  . ARG B 188 ? 1.7888 1.8071 1.3604 -0.3804 0.0748  -0.1767 188 ARG B CD  
3413 N NE  . ARG B 188 ? 1.8047 1.8252 1.3689 -0.3981 0.0803  -0.1841 188 ARG B NE  
3414 C CZ  . ARG B 188 ? 1.7912 1.8397 1.3433 -0.4185 0.0759  -0.1804 188 ARG B CZ  
3415 N NH1 . ARG B 188 ? 1.8066 1.8845 1.3538 -0.4235 0.0655  -0.1683 188 ARG B NH1 
3416 N NH2 . ARG B 188 ? 1.7724 1.8201 1.3179 -0.4341 0.0820  -0.1881 188 ARG B NH2 
3417 N N   . ALA B 189 ? 1.5223 1.6587 1.1087 -0.4025 0.0155  -0.1209 189 ALA B N   
3418 C CA  . ALA B 189 ? 1.6053 1.7622 1.1929 -0.4146 0.0088  -0.1148 189 ALA B CA  
3419 C C   . ALA B 189 ? 1.5668 1.7278 1.1707 -0.4004 -0.0024 -0.1039 189 ALA B C   
3420 O O   . ALA B 189 ? 1.5325 1.6822 1.1404 -0.4008 -0.0004 -0.1094 189 ALA B O   
3421 C CB  . ALA B 189 ? 1.6024 1.8014 1.1838 -0.4319 -0.0004 -0.1004 189 ALA B CB  
3422 N N   . ALA B 190 ? 1.5587 1.7355 1.1723 -0.3878 -0.0139 -0.0881 190 ALA B N   
3423 C CA  . ALA B 190 ? 1.4331 1.6154 1.0627 -0.3744 -0.0245 -0.0768 190 ALA B CA  
3424 C C   . ALA B 190 ? 1.4441 1.5863 1.0824 -0.3561 -0.0158 -0.0892 190 ALA B C   
3425 O O   . ALA B 190 ? 1.5189 1.6567 1.1748 -0.3445 -0.0189 -0.0837 190 ALA B O   
3426 C CB  . ALA B 190 ? 1.3056 1.5175 0.9484 -0.3641 -0.0373 -0.0530 190 ALA B CB  
3427 N N   . VAL B 191 ? 1.4160 1.5286 1.0475 -0.3507 -0.0036 -0.1038 191 VAL B N   
3428 C CA  . VAL B 191 ? 1.4393 1.5159 1.0854 -0.3313 0.0053  -0.1120 191 VAL B CA  
3429 C C   . VAL B 191 ? 1.5227 1.5791 1.1605 -0.3423 0.0137  -0.1292 191 VAL B C   
3430 O O   . VAL B 191 ? 1.5634 1.6012 1.2170 -0.3283 0.0161  -0.1300 191 VAL B O   
3431 C CB  . VAL B 191 ? 1.3556 1.4064 1.0030 -0.3183 0.0156  -0.1195 191 VAL B CB  
3432 C CG1 . VAL B 191 ? 1.1786 1.2450 0.8392 -0.3033 0.0078  -0.1018 191 VAL B CG1 
3433 C CG2 . VAL B 191 ? 1.5583 1.5961 1.1815 -0.3357 0.0276  -0.1383 191 VAL B CG2 
3434 N N   . GLN B 192 ? 1.5122 1.5716 1.1375 -0.3599 0.0208  -0.1370 192 GLN B N   
3435 C CA  . GLN B 192 ? 1.5224 1.5648 1.1492 -0.3647 0.0287  -0.1472 192 GLN B CA  
3436 C C   . GLN B 192 ? 1.3819 1.4503 1.0123 -0.3732 0.0170  -0.1367 192 GLN B C   
3437 O O   . GLN B 192 ? 1.3212 1.3761 0.9570 -0.3725 0.0204  -0.1422 192 GLN B O   
3438 C CB  . GLN B 192 ? 1.6880 1.7152 1.3021 -0.3783 0.0446  -0.1624 192 GLN B CB  
3439 C CG  . GLN B 192 ? 1.8938 1.8942 1.5137 -0.3764 0.0550  -0.1735 192 GLN B CG  
3440 C CD  . GLN B 192 ? 2.0414 2.0132 1.6549 -0.3815 0.0748  -0.1905 192 GLN B CD  
3441 O OE1 . GLN B 192 ? 2.1279 2.1013 1.7295 -0.3911 0.0821  -0.1959 192 GLN B OE1 
3442 N NE2 . GLN B 192 ? 2.0354 1.9812 1.6579 -0.3750 0.0841  -0.1983 192 GLN B NE2 
3443 N N   . ARG B 193 ? 1.3531 1.4593 0.9821 -0.3807 0.0033  -0.1206 193 ARG B N   
3444 C CA  . ARG B 193 ? 1.4384 1.5693 1.0748 -0.3860 -0.0081 -0.1087 193 ARG B CA  
3445 C C   . ARG B 193 ? 1.4495 1.5713 1.1027 -0.3685 -0.0144 -0.1039 193 ARG B C   
3446 O O   . ARG B 193 ? 1.4150 1.5359 1.0751 -0.3695 -0.0163 -0.1037 193 ARG B O   
3447 C CB  . ARG B 193 ? 1.4340 1.6095 1.0698 -0.3956 -0.0218 -0.0892 193 ARG B CB  
3448 C CG  . ARG B 193 ? 1.4632 1.6631 1.1017 -0.4081 -0.0287 -0.0807 193 ARG B CG  
3449 C CD  . ARG B 193 ? 1.5201 1.7627 1.1717 -0.4073 -0.0460 -0.0554 193 ARG B CD  
3450 N NE  . ARG B 193 ? 1.6287 1.8841 1.2865 -0.4142 -0.0506 -0.0504 193 ARG B NE  
3451 C CZ  . ARG B 193 ? 1.6673 1.9492 1.3426 -0.4082 -0.0637 -0.0310 193 ARG B CZ  
3452 N NH1 . ARG B 193 ? 1.7035 2.0032 1.3924 -0.3952 -0.0735 -0.0140 193 ARG B NH1 
3453 N NH2 . ARG B 193 ? 1.6443 1.9359 1.3245 -0.4151 -0.0665 -0.0279 193 ARG B NH2 
3454 N N   . TYR B 194 ? 1.4151 1.5279 1.0807 -0.3481 -0.0150 -0.0977 194 TYR B N   
3455 C CA  . TYR B 194 ? 1.2786 1.3768 0.9690 -0.3234 -0.0154 -0.0905 194 TYR B CA  
3456 C C   . TYR B 194 ? 1.2317 1.2930 0.9217 -0.3198 -0.0032 -0.1081 194 TYR B C   
3457 O O   . TYR B 194 ? 1.2304 1.2881 0.9288 -0.3183 -0.0042 -0.1078 194 TYR B O   
3458 C CB  . TYR B 194 ? 1.2392 1.3346 0.9425 -0.3031 -0.0163 -0.0808 194 TYR B CB  
3459 C CG  . TYR B 194 ? 1.2002 1.2939 0.9296 -0.2796 -0.0207 -0.0672 194 TYR B CG  
3460 C CD1 . TYR B 194 ? 1.2236 1.3423 0.9669 -0.2775 -0.0307 -0.0510 194 TYR B CD1 
3461 C CD2 . TYR B 194 ? 1.1706 1.2391 0.9108 -0.2599 -0.0145 -0.0700 194 TYR B CD2 
3462 C CE1 . TYR B 194 ? 1.0993 1.2151 0.8659 -0.2562 -0.0331 -0.0395 194 TYR B CE1 
3463 C CE2 . TYR B 194 ? 1.1346 1.2013 0.8968 -0.2399 -0.0178 -0.0588 194 TYR B CE2 
3464 C CZ  . TYR B 194 ? 1.0525 1.1422 0.8275 -0.2382 -0.0266 -0.0441 194 TYR B CZ  
3465 O OH  . TYR B 194 ? 1.0382 1.1252 0.8344 -0.2190 -0.0283 -0.0341 194 TYR B OH  
3466 N N   . LEU B 195 ? 1.1447 1.1791 0.8253 -0.3190 0.0089  -0.1230 195 LEU B N   
3467 C CA  . LEU B 195 ? 1.2052 1.2040 0.8893 -0.3127 0.0215  -0.1373 195 LEU B CA  
3468 C C   . LEU B 195 ? 1.3762 1.3709 1.0526 -0.3290 0.0248  -0.1471 195 LEU B C   
3469 O O   . LEU B 195 ? 1.3611 1.3350 1.0482 -0.3207 0.0303  -0.1514 195 LEU B O   
3470 C CB  . LEU B 195 ? 1.1794 1.1534 0.8524 -0.3139 0.0350  -0.1520 195 LEU B CB  
3471 C CG  . LEU B 195 ? 1.1793 1.1477 0.8597 -0.2971 0.0361  -0.1466 195 LEU B CG  
3472 C CD1 . LEU B 195 ? 1.2999 1.2466 0.9650 -0.3052 0.0506  -0.1635 195 LEU B CD1 
3473 C CD2 . LEU B 195 ? 1.1232 1.0765 0.8272 -0.2720 0.0360  -0.1393 195 LEU B CD2 
3474 N N   . HIS B 196 ? 1.4119 1.4278 1.0747 -0.3484 0.0223  -0.1470 196 HIS B N   
3475 C CA  . HIS B 196 ? 1.3210 1.3348 0.9809 -0.3605 0.0272  -0.1527 196 HIS B CA  
3476 C C   . HIS B 196 ? 1.3199 1.3573 0.9881 -0.3631 0.0137  -0.1407 196 HIS B C   
3477 O O   . HIS B 196 ? 1.2938 1.3194 0.9678 -0.3632 0.0172  -0.1449 196 HIS B O   
3478 C CB  . HIS B 196 ? 1.3740 1.3985 1.0167 -0.3796 0.0330  -0.1578 196 HIS B CB  
3479 C CG  . HIS B 196 ? 1.5073 1.5242 1.1446 -0.3926 0.0415  -0.1667 196 HIS B CG  
3480 N ND1 . HIS B 196 ? 1.5861 1.5690 1.2235 -0.3904 0.0585  -0.1819 196 HIS B ND1 
3481 C CD2 . HIS B 196 ? 1.5195 1.5590 1.1516 -0.4081 0.0357  -0.1620 196 HIS B CD2 
3482 C CE1 . HIS B 196 ? 1.5923 1.5763 1.2240 -0.4042 0.0629  -0.1869 196 HIS B CE1 
3483 N NE2 . HIS B 196 ? 1.5589 1.5769 1.1868 -0.4154 0.0492  -0.1754 196 HIS B NE2 
3484 N N   . ASP B 197 ? 1.3300 1.4015 1.0004 -0.3648 -0.0014 -0.1246 197 ASP B N   
3485 C CA  . ASP B 197 ? 1.3541 1.4510 1.0342 -0.3677 -0.0140 -0.1116 197 ASP B CA  
3486 C C   . ASP B 197 ? 1.4123 1.4960 1.1166 -0.3438 -0.0148 -0.1041 197 ASP B C   
3487 O O   . ASP B 197 ? 1.5081 1.6046 1.2228 -0.3438 -0.0209 -0.0958 197 ASP B O   
3488 C CB  . ASP B 197 ? 1.3774 1.5165 1.0592 -0.3724 -0.0286 -0.0921 197 ASP B CB  
3489 C CG  . ASP B 197 ? 1.5118 1.6698 1.1773 -0.3919 -0.0268 -0.0923 197 ASP B CG  
3490 O OD1 . ASP B 197 ? 1.5837 1.7209 1.2362 -0.4015 -0.0135 -0.1083 197 ASP B OD1 
3491 O OD2 . ASP B 197 ? 1.5365 1.7312 1.2038 -0.3976 -0.0384 -0.0752 197 ASP B OD2 
3492 N N   . PHE B 198 ? 1.4084 1.4684 1.1224 -0.3234 -0.0086 -0.1058 198 PHE B N   
3493 C CA  . PHE B 198 ? 1.3927 1.4371 1.1276 -0.3021 -0.0074 -0.1011 198 PHE B CA  
3494 C C   . PHE B 198 ? 1.3339 1.3402 1.0680 -0.2952 0.0063  -0.1167 198 PHE B C   
3495 O O   . PHE B 198 ? 1.2464 1.2378 0.9963 -0.2753 0.0084  -0.1129 198 PHE B O   
3496 C CB  . PHE B 198 ? 1.4332 1.4887 1.1858 -0.2813 -0.0143 -0.0845 198 PHE B CB  
3497 C CG  . PHE B 198 ? 1.5154 1.6083 1.2733 -0.2853 -0.0268 -0.0666 198 PHE B CG  
3498 C CD1 . PHE B 198 ? 1.5336 1.6464 1.2820 -0.2937 -0.0312 -0.0613 198 PHE B CD1 
3499 C CD2 . PHE B 198 ? 1.5145 1.6238 1.2883 -0.2800 -0.0337 -0.0537 198 PHE B CD2 
3500 C CE1 . PHE B 198 ? 1.5140 1.6633 1.2698 -0.2968 -0.0425 -0.0424 198 PHE B CE1 
3501 C CE2 . PHE B 198 ? 1.4826 1.6272 1.2641 -0.2827 -0.0444 -0.0353 198 PHE B CE2 
3502 C CZ  . PHE B 198 ? 1.4893 1.6543 1.2623 -0.2910 -0.0489 -0.0292 198 PHE B CZ  
3503 N N   . MET B 199 ? 1.3671 1.3580 1.0835 -0.3118 0.0162  -0.1336 199 MET B N   
3504 C CA  . MET B 199 ? 1.3972 1.3525 1.1143 -0.3082 0.0306  -0.1481 199 MET B CA  
3505 C C   . MET B 199 ? 1.3260 1.2632 1.0558 -0.2858 0.0349  -0.1455 199 MET B C   
3506 O O   . MET B 199 ? 1.2156 1.1397 0.9618 -0.2699 0.0366  -0.1417 199 MET B O   
3507 C CB  . MET B 199 ? 1.4170 1.3654 1.1438 -0.3078 0.0315  -0.1484 199 MET B CB  
3508 C CG  . MET B 199 ? 1.4225 1.3951 1.1417 -0.3266 0.0236  -0.1459 199 MET B CG  
3509 S SD  . MET B 199 ? 1.3618 1.3233 1.0933 -0.3251 0.0260  -0.1467 199 MET B SD  
3510 C CE  . MET B 199 ? 1.2642 1.1861 0.9880 -0.3312 0.0463  -0.1673 199 MET B CE  
3511 N N   . MET B 200 ? 1.3247 1.2637 1.0465 -0.2856 0.0361  -0.1466 200 MET B N   
3512 C CA  . MET B 200 ? 1.1918 1.1170 0.9241 -0.2663 0.0394  -0.1437 200 MET B CA  
3513 C C   . MET B 200 ? 1.2366 1.1417 0.9562 -0.2725 0.0523  -0.1579 200 MET B C   
3514 O O   . MET B 200 ? 1.3730 1.2832 1.0734 -0.2916 0.0554  -0.1670 200 MET B O   
3515 C CB  . MET B 200 ? 1.1333 1.0817 0.8724 -0.2561 0.0276  -0.1281 200 MET B CB  
3516 C CG  . MET B 200 ? 1.2236 1.1871 0.9796 -0.2449 0.0173  -0.1135 200 MET B CG  
3517 S SD  . MET B 200 ? 1.1573 1.1488 0.9225 -0.2348 0.0049  -0.0948 200 MET B SD  
3518 C CE  . MET B 200 ? 1.1182 1.1426 0.8693 -0.2568 -0.0036 -0.0900 200 MET B CE  
3519 N N   . THR B 201 ? 1.2295 1.1126 0.9600 -0.2567 0.0602  -0.1594 201 THR B N   
3520 C CA  . THR B 201 ? 1.2559 1.1216 0.9785 -0.2581 0.0719  -0.1696 201 THR B CA  
3521 C C   . THR B 201 ? 1.2431 1.1139 0.9748 -0.2413 0.0669  -0.1593 201 THR B C   
3522 O O   . THR B 201 ? 1.1991 1.0868 0.9417 -0.2305 0.0550  -0.1454 201 THR B O   
3523 C CB  . THR B 201 ? 1.2824 1.1164 1.0106 -0.2556 0.0878  -0.1808 201 THR B CB  
3524 O OG1 . THR B 201 ? 1.3620 1.1882 1.1119 -0.2356 0.0860  -0.1713 201 THR B OG1 
3525 C CG2 . THR B 201 ? 1.2050 1.0348 0.9251 -0.2722 0.0926  -0.1901 201 THR B CG2 
3526 N N   . MET B 202 ? 1.2361 1.0912 0.9641 -0.2393 0.0773  -0.1665 202 MET B N   
3527 C CA  . MET B 202 ? 1.1139 0.9759 0.8455 -0.2284 0.0732  -0.1589 202 MET B CA  
3528 C C   . MET B 202 ? 1.1758 1.0129 0.9087 -0.2233 0.0879  -0.1677 202 MET B C   
3529 O O   . MET B 202 ? 1.3746 1.1983 1.0946 -0.2364 0.1002  -0.1816 202 MET B O   
3530 C CB  . MET B 202 ? 1.0837 0.9704 0.7992 -0.2417 0.0654  -0.1563 202 MET B CB  
3531 C CG  . MET B 202 ? 1.1917 1.0860 0.9071 -0.2347 0.0628  -0.1501 202 MET B CG  
3532 S SD  . MET B 202 ? 1.2791 1.2051 0.9744 -0.2541 0.0539  -0.1469 202 MET B SD  
3533 C CE  . MET B 202 ? 1.2943 1.2054 0.9649 -0.2771 0.0690  -0.1685 202 MET B CE  
3534 N N   . VAL B 203 ? 1.0473 0.8776 0.7961 -0.2050 0.0876  -0.1601 203 VAL B N   
3535 C CA  . VAL B 203 ? 1.0597 0.8661 0.8140 -0.1988 0.1020  -0.1669 203 VAL B CA  
3536 C C   . VAL B 203 ? 0.9510 0.7615 0.7017 -0.1950 0.1024  -0.1649 203 VAL B C   
3537 O O   . VAL B 203 ? 0.9690 0.8004 0.7139 -0.1966 0.0913  -0.1577 203 VAL B O   
3538 C CB  . VAL B 203 ? 1.1128 0.9067 0.8889 -0.1818 0.1035  -0.1602 203 VAL B CB  
3539 C CG1 . VAL B 203 ? 1.1343 0.9151 0.9136 -0.1870 0.1105  -0.1662 203 VAL B CG1 
3540 C CG2 . VAL B 203 ? 1.0591 0.8707 0.8462 -0.1696 0.0882  -0.1457 203 VAL B CG2 
3541 N N   . SER B 204 ? 0.9112 0.7021 0.6662 -0.1902 0.1157  -0.1706 204 SER B N   
3542 C CA  . SER B 204 ? 0.9753 0.7677 0.7304 -0.1841 0.1171  -0.1678 204 SER B CA  
3543 C C   . SER B 204 ? 0.9754 0.7660 0.7518 -0.1643 0.1125  -0.1558 204 SER B C   
3544 O O   . SER B 204 ? 0.9735 0.7531 0.7644 -0.1560 0.1155  -0.1535 204 SER B O   
3545 C CB  . SER B 204 ? 0.9983 0.7710 0.7459 -0.1907 0.1354  -0.1810 204 SER B CB  
3546 O OG  . SER B 204 ? 1.0184 0.7718 0.7846 -0.1769 0.1457  -0.1793 204 SER B OG  
3547 N N   . ALA B 205 ? 0.9937 0.7965 0.7717 -0.1577 0.1051  -0.1477 205 ALA B N   
3548 C CA  . ALA B 205 ? 0.9416 0.7458 0.7378 -0.1408 0.0992  -0.1362 205 ALA B CA  
3549 C C   . ALA B 205 ? 0.9921 0.7765 0.8027 -0.1318 0.1108  -0.1375 205 ALA B C   
3550 O O   . ALA B 205 ? 0.9671 0.7490 0.7928 -0.1219 0.1079  -0.1307 205 ALA B O   
3551 C CB  . ALA B 205 ? 0.8574 0.6741 0.6521 -0.1367 0.0928  -0.1295 205 ALA B CB  
3552 N N   . GLU B 206 ? 0.9878 0.7585 0.7943 -0.1355 0.1247  -0.1458 206 GLU B N   
3553 C CA  . GLU B 206 ? 0.9567 0.7091 0.7792 -0.1267 0.1373  -0.1457 206 GLU B CA  
3554 C C   . GLU B 206 ? 0.9047 0.6436 0.7328 -0.1292 0.1449  -0.1501 206 GLU B C   
3555 O O   . GLU B 206 ? 0.9980 0.7226 0.8423 -0.1212 0.1552  -0.1480 206 GLU B O   
3556 C CB  . GLU B 206 ? 1.0302 0.7711 0.8480 -0.1297 0.1517  -0.1532 206 GLU B CB  
3557 C CG  . GLU B 206 ? 1.0079 0.7392 0.8070 -0.1463 0.1635  -0.1688 206 GLU B CG  
3558 C CD  . GLU B 206 ? 1.0911 0.8395 0.8676 -0.1592 0.1551  -0.1727 206 GLU B CD  
3559 O OE1 . GLU B 206 ? 1.0404 0.8085 0.8153 -0.1577 0.1385  -0.1639 206 GLU B OE1 
3560 O OE2 . GLU B 206 ? 1.1165 0.8590 0.8773 -0.1712 0.1659  -0.1841 206 GLU B OE2 
3561 N N   . ALA B 207 ? 1.0114 0.7552 0.8281 -0.1398 0.1401  -0.1551 207 ALA B N   
3562 C CA  . ALA B 207 ? 0.9246 0.6566 0.7483 -0.1415 0.1461  -0.1580 207 ALA B CA  
3563 C C   . ALA B 207 ? 0.9499 0.6856 0.7933 -0.1276 0.1385  -0.1451 207 ALA B C   
3564 O O   . ALA B 207 ? 0.9169 0.6395 0.7739 -0.1235 0.1471  -0.1440 207 ALA B O   
3565 C CB  . ALA B 207 ? 0.7638 0.5026 0.5707 -0.1566 0.1414  -0.1654 207 ALA B CB  
3566 N N   . TYR B 208 ? 0.8375 0.5907 0.6833 -0.1205 0.1235  -0.1351 208 TYR B N   
3567 C CA  . TYR B 208 ? 0.9073 0.6665 0.7677 -0.1105 0.1150  -0.1244 208 TYR B CA  
3568 C C   . TYR B 208 ? 0.9564 0.7088 0.8367 -0.0978 0.1200  -0.1159 208 TYR B C   
3569 O O   . TYR B 208 ? 0.8705 0.6204 0.7633 -0.0930 0.1201  -0.1103 208 TYR B O   
3570 C CB  . TYR B 208 ? 0.7972 0.5762 0.6536 -0.1080 0.0988  -0.1174 208 TYR B CB  
3571 C CG  . TYR B 208 ? 0.9205 0.7082 0.7709 -0.1144 0.0911  -0.1180 208 TYR B CG  
3572 C CD1 . TYR B 208 ? 1.0080 0.7927 0.8685 -0.1111 0.0906  -0.1146 208 TYR B CD1 
3573 C CD2 . TYR B 208 ? 0.8899 0.6900 0.7252 -0.1241 0.0845  -0.1212 208 TYR B CD2 
3574 C CE1 . TYR B 208 ? 0.9753 0.7684 0.8309 -0.1170 0.0837  -0.1148 208 TYR B CE1 
3575 C CE2 . TYR B 208 ? 0.8745 0.6842 0.7057 -0.1299 0.0774  -0.1206 208 TYR B CE2 
3576 C CZ  . TYR B 208 ? 0.9390 0.7445 0.7802 -0.1262 0.0772  -0.1179 208 TYR B CZ  
3577 O OH  . TYR B 208 ? 1.0422 0.8575 0.8798 -0.1319 0.0705  -0.1170 208 TYR B OH  
3578 N N   . PRO B 209 ? 0.9828 0.7333 0.8673 -0.0924 0.1239  -0.1137 209 PRO B N   
3579 C CA  . PRO B 209 ? 0.9622 0.7085 0.8670 -0.0808 0.1284  -0.1040 209 PRO B CA  
3580 C C   . PRO B 209 ? 0.9216 0.6518 0.8388 -0.0801 0.1421  -0.1049 209 PRO B C   
3581 O O   . PRO B 209 ? 0.9371 0.6695 0.8704 -0.0727 0.1402  -0.0949 209 PRO B O   
3582 C CB  . PRO B 209 ? 0.9486 0.6936 0.8531 -0.0780 0.1331  -0.1043 209 PRO B CB  
3583 C CG  . PRO B 209 ? 0.9509 0.7081 0.8373 -0.0842 0.1228  -0.1083 209 PRO B CG  
3584 C CD  . PRO B 209 ? 0.9617 0.7182 0.8340 -0.0956 0.1218  -0.1170 209 PRO B CD  
3585 N N   . PRO B 210 ? 0.8678 0.5820 0.7787 -0.0879 0.1565  -0.1163 210 PRO B N   
3586 C CA  . PRO B 210 ? 0.8970 0.5943 0.8229 -0.0862 0.1711  -0.1161 210 PRO B CA  
3587 C C   . PRO B 210 ? 0.8844 0.5817 0.8092 -0.0908 0.1673  -0.1170 210 PRO B C   
3588 O O   . PRO B 210 ? 0.9462 0.6376 0.8888 -0.0850 0.1725  -0.1096 210 PRO B O   
3589 C CB  . PRO B 210 ? 0.7862 0.4655 0.7037 -0.0942 0.1886  -0.1296 210 PRO B CB  
3590 C CG  . PRO B 210 ? 0.8415 0.5299 0.7331 -0.1062 0.1799  -0.1399 210 PRO B CG  
3591 C CD  . PRO B 210 ? 0.8798 0.5897 0.7703 -0.0995 0.1614  -0.1298 210 PRO B CD  
3592 N N   . LEU B 211 ? 0.8073 0.5127 0.7128 -0.1010 0.1579  -0.1246 211 LEU B N   
3593 C CA  . LEU B 211 ? 0.8663 0.5763 0.7711 -0.1042 0.1509  -0.1233 211 LEU B CA  
3594 C C   . LEU B 211 ? 0.8765 0.5986 0.7971 -0.0925 0.1404  -0.1082 211 LEU B C   
3595 O O   . LEU B 211 ? 0.9340 0.6518 0.8680 -0.0893 0.1436  -0.1026 211 LEU B O   
3596 C CB  . LEU B 211 ? 0.8782 0.6010 0.7618 -0.1148 0.1393  -0.1300 211 LEU B CB  
3597 C CG  . LEU B 211 ? 0.9112 0.6278 0.7759 -0.1308 0.1453  -0.1445 211 LEU B CG  
3598 C CD1 . LEU B 211 ? 0.9258 0.6632 0.7747 -0.1364 0.1296  -0.1442 211 LEU B CD1 
3599 C CD2 . LEU B 211 ? 0.6587 0.3636 0.5247 -0.1385 0.1530  -0.1504 211 LEU B CD2 
3600 N N   . LEU B 212 ? 0.8611 0.5988 0.7801 -0.0868 0.1281  -0.1017 212 LEU B N   
3601 C CA  . LEU B 212 ? 0.8302 0.5804 0.7614 -0.0774 0.1180  -0.0887 212 LEU B CA  
3602 C C   . LEU B 212 ? 0.8692 0.6131 0.8220 -0.0685 0.1267  -0.0788 212 LEU B C   
3603 O O   . LEU B 212 ? 0.7520 0.5005 0.7170 -0.0641 0.1239  -0.0696 212 LEU B O   
3604 C CB  . LEU B 212 ? 0.7814 0.5466 0.7064 -0.0741 0.1060  -0.0852 212 LEU B CB  
3605 C CG  . LEU B 212 ? 0.7924 0.5680 0.6999 -0.0810 0.0956  -0.0908 212 LEU B CG  
3606 C CD1 . LEU B 212 ? 0.6431 0.4286 0.5456 -0.0780 0.0885  -0.0887 212 LEU B CD1 
3607 C CD2 . LEU B 212 ? 0.7716 0.5567 0.6799 -0.0811 0.0862  -0.0867 212 LEU B CD2 
3608 N N   . ARG B 213 ? 0.9042 0.6389 0.8630 -0.0656 0.1374  -0.0795 213 ARG B N   
3609 C CA  . ARG B 213 ? 0.8842 0.6149 0.8663 -0.0564 0.1459  -0.0679 213 ARG B CA  
3610 C C   . ARG B 213 ? 0.8487 0.5665 0.8422 -0.0575 0.1569  -0.0673 213 ARG B C   
3611 O O   . ARG B 213 ? 0.8563 0.5781 0.8692 -0.0503 0.1577  -0.0540 213 ARG B O   
3612 C CB  . ARG B 213 ? 0.9741 0.6966 0.9614 -0.0531 0.1569  -0.0689 213 ARG B CB  
3613 C CG  . ARG B 213 ? 1.0181 0.7558 1.0064 -0.0471 0.1469  -0.0614 213 ARG B CG  
3614 C CD  . ARG B 213 ? 0.9803 0.7104 0.9804 -0.0418 0.1594  -0.0586 213 ARG B CD  
3615 N NE  . ARG B 213 ? 0.9920 0.7021 0.9856 -0.0479 0.1756  -0.0717 213 ARG B NE  
3616 C CZ  . ARG B 213 ? 0.9352 0.6410 0.9100 -0.0550 0.1775  -0.0843 213 ARG B CZ  
3617 N NH1 . ARG B 213 ? 0.8675 0.5874 0.8303 -0.0556 0.1645  -0.0843 213 ARG B NH1 
3618 N NH2 . ARG B 213 ? 0.9039 0.5915 0.8722 -0.0620 0.1931  -0.0968 213 ARG B NH2 
3619 N N   . GLY B 214 ? 0.8712 0.5749 0.8525 -0.0673 0.1649  -0.0812 214 GLY B N   
3620 C CA  . GLY B 214 ? 0.7746 0.4652 0.7651 -0.0698 0.1752  -0.0820 214 GLY B CA  
3621 C C   . GLY B 214 ? 0.8922 0.5954 0.8883 -0.0676 0.1639  -0.0725 214 GLY B C   
3622 O O   . GLY B 214 ? 0.9927 0.6903 1.0065 -0.0639 0.1709  -0.0645 214 GLY B O   
3623 N N   . ALA B 215 ? 0.7510 0.4713 0.7331 -0.0696 0.1469  -0.0727 215 ALA B N   
3624 C CA  . ALA B 215 ? 0.6988 0.4312 0.6831 -0.0688 0.1361  -0.0657 215 ALA B CA  
3625 C C   . ALA B 215 ? 0.8151 0.5645 0.8116 -0.0593 0.1265  -0.0503 215 ALA B C   
3626 O O   . ALA B 215 ? 0.7837 0.5457 0.7798 -0.0588 0.1162  -0.0447 215 ALA B O   
3627 C CB  . ALA B 215 ? 0.8518 0.5928 0.8148 -0.0771 0.1246  -0.0748 215 ALA B CB  
3628 N N   . GLY B 216 ? 0.7990 0.5499 0.8053 -0.0525 0.1295  -0.0437 216 GLY B N   
3629 C CA  . GLY B 216 ? 0.8217 0.5897 0.8392 -0.0450 0.1208  -0.0291 216 GLY B CA  
3630 C C   . GLY B 216 ? 0.8081 0.5912 0.8123 -0.0451 0.1067  -0.0304 216 GLY B C   
3631 O O   . GLY B 216 ? 0.8991 0.6969 0.9106 -0.0405 0.0991  -0.0194 216 GLY B O   
3632 N N   . LEU B 217 ? 0.6868 0.4673 0.6722 -0.0507 0.1033  -0.0428 217 LEU B N   
3633 C CA  . LEU B 217 ? 0.7488 0.5418 0.7227 -0.0508 0.0915  -0.0442 217 LEU B CA  
3634 C C   . LEU B 217 ? 0.7836 0.5731 0.7554 -0.0491 0.0952  -0.0471 217 LEU B C   
3635 O O   . LEU B 217 ? 0.7755 0.5513 0.7466 -0.0511 0.1062  -0.0535 217 LEU B O   
3636 C CB  . LEU B 217 ? 0.7512 0.5464 0.7075 -0.0577 0.0846  -0.0538 217 LEU B CB  
3637 C CG  . LEU B 217 ? 0.7863 0.5813 0.7444 -0.0605 0.0841  -0.0531 217 LEU B CG  
3638 C CD1 . LEU B 217 ? 0.8090 0.6054 0.7509 -0.0681 0.0792  -0.0626 217 LEU B CD1 
3639 C CD2 . LEU B 217 ? 0.6809 0.4895 0.6475 -0.0560 0.0763  -0.0419 217 LEU B CD2 
3640 N N   . TRP B 218 ? 0.7609 0.5625 0.7312 -0.0461 0.0863  -0.0426 218 TRP B N   
3641 C CA  . TRP B 218 ? 0.6583 0.4593 0.6252 -0.0448 0.0874  -0.0449 218 TRP B CA  
3642 C C   . TRP B 218 ? 0.6873 0.4935 0.6368 -0.0491 0.0788  -0.0526 218 TRP B C   
3643 O O   . TRP B 218 ? 0.8347 0.6514 0.7801 -0.0493 0.0689  -0.0506 218 TRP B O   
3644 C CB  . TRP B 218 ? 0.6094 0.4208 0.5887 -0.0387 0.0841  -0.0334 218 TRP B CB  
3645 C CG  . TRP B 218 ? 0.8075 0.6160 0.8062 -0.0338 0.0930  -0.0235 218 TRP B CG  
3646 C CD1 . TRP B 218 ? 0.7985 0.5942 0.8055 -0.0337 0.1044  -0.0242 218 TRP B CD1 
3647 C CD2 . TRP B 218 ? 0.8886 0.7077 0.9028 -0.0284 0.0918  -0.0104 218 TRP B CD2 
3648 N NE1 . TRP B 218 ? 0.7584 0.5559 0.7868 -0.0275 0.1110  -0.0113 218 TRP B NE1 
3649 C CE2 . TRP B 218 ? 0.8960 0.7091 0.9291 -0.0243 0.1028  -0.0021 218 TRP B CE2 
3650 C CE3 . TRP B 218 ? 0.7822 0.6157 0.7966 -0.0272 0.0828  -0.0045 218 TRP B CE3 
3651 C CZ2 . TRP B 218 ? 0.9097 0.7329 0.9627 -0.0187 0.1044  0.0133  218 TRP B CZ2 
3652 C CZ3 . TRP B 218 ? 0.8218 0.6652 0.8541 -0.0228 0.0839  0.0096  218 TRP B CZ3 
3653 C CH2 . TRP B 218 ? 0.8546 0.6940 0.9064 -0.0184 0.0943  0.0191  218 TRP B CH2 
3654 N N   . LEU B 219 ? 0.7154 0.5147 0.6552 -0.0526 0.0832  -0.0608 219 LEU B N   
3655 C CA  . LEU B 219 ? 0.6760 0.4819 0.6014 -0.0563 0.0754  -0.0660 219 LEU B CA  
3656 C C   . LEU B 219 ? 0.7871 0.6041 0.7155 -0.0516 0.0671  -0.0596 219 LEU B C   
3657 O O   . LEU B 219 ? 0.7940 0.6113 0.7310 -0.0472 0.0696  -0.0545 219 LEU B O   
3658 C CB  . LEU B 219 ? 0.5834 0.3820 0.4991 -0.0609 0.0819  -0.0741 219 LEU B CB  
3659 C CG  . LEU B 219 ? 0.6739 0.4804 0.5763 -0.0645 0.0750  -0.0776 219 LEU B CG  
3660 C CD1 . LEU B 219 ? 0.6899 0.5042 0.5839 -0.0690 0.0670  -0.0794 219 LEU B CD1 
3661 C CD2 . LEU B 219 ? 0.6324 0.4315 0.5257 -0.0700 0.0831  -0.0853 219 LEU B CD2 
3662 N N   . GLU B 220 ? 0.7388 0.5647 0.6609 -0.0528 0.0578  -0.0596 220 GLU B N   
3663 C CA  . GLU B 220 ? 0.6841 0.5189 0.6073 -0.0498 0.0509  -0.0555 220 GLU B CA  
3664 C C   . GLU B 220 ? 0.7314 0.5688 0.6449 -0.0518 0.0477  -0.0593 220 GLU B C   
3665 O O   . GLU B 220 ? 0.6875 0.5277 0.6024 -0.0494 0.0461  -0.0571 220 GLU B O   
3666 C CB  . GLU B 220 ? 0.7014 0.5442 0.6265 -0.0491 0.0440  -0.0519 220 GLU B CB  
3667 C CG  . GLU B 220 ? 0.7527 0.6030 0.6828 -0.0463 0.0396  -0.0466 220 GLU B CG  
3668 C CD  . GLU B 220 ? 0.9074 0.7656 0.8361 -0.0472 0.0332  -0.0452 220 GLU B CD  
3669 O OE1 . GLU B 220 ? 0.8204 0.6790 0.7452 -0.0490 0.0317  -0.0476 220 GLU B OE1 
3670 O OE2 . GLU B 220 ? 1.0748 0.9390 1.0060 -0.0466 0.0300  -0.0420 220 GLU B OE2 
3671 N N   . GLU B 221 ? 0.6850 0.5226 0.5893 -0.0564 0.0468  -0.0643 221 GLU B N   
3672 C CA  . GLU B 221 ? 0.7007 0.5438 0.5973 -0.0584 0.0430  -0.0656 221 GLU B CA  
3673 C C   . GLU B 221 ? 0.6937 0.5359 0.5803 -0.0653 0.0451  -0.0712 221 GLU B C   
3674 O O   . GLU B 221 ? 0.6995 0.5412 0.5839 -0.0688 0.0450  -0.0733 221 GLU B O   
3675 C CB  . GLU B 221 ? 0.7156 0.5672 0.6136 -0.0564 0.0356  -0.0623 221 GLU B CB  
3676 C CG  . GLU B 221 ? 0.7106 0.5689 0.6032 -0.0579 0.0322  -0.0619 221 GLU B CG  
3677 C CD  . GLU B 221 ? 0.7275 0.5926 0.6233 -0.0555 0.0270  -0.0586 221 GLU B CD  
3678 O OE1 . GLU B 221 ? 0.7359 0.6011 0.6355 -0.0540 0.0256  -0.0579 221 GLU B OE1 
3679 O OE2 . GLU B 221 ? 0.7874 0.6579 0.6825 -0.0551 0.0249  -0.0562 221 GLU B OE2 
3680 N N   . PHE B 222 ? 0.6933 0.5359 0.5733 -0.0681 0.0471  -0.0733 222 PHE B N   
3681 C CA  . PHE B 222 ? 0.6750 0.5208 0.5435 -0.0764 0.0477  -0.0778 222 PHE B CA  
3682 C C   . PHE B 222 ? 0.7670 0.6239 0.6321 -0.0765 0.0421  -0.0738 222 PHE B C   
3683 O O   . PHE B 222 ? 0.7281 0.5846 0.5954 -0.0731 0.0430  -0.0716 222 PHE B O   
3684 C CB  . PHE B 222 ? 0.5929 0.4287 0.4555 -0.0814 0.0572  -0.0847 222 PHE B CB  
3685 C CG  . PHE B 222 ? 0.6845 0.5237 0.5332 -0.0922 0.0582  -0.0906 222 PHE B CG  
3686 C CD1 . PHE B 222 ? 0.6533 0.5039 0.4936 -0.0965 0.0541  -0.0891 222 PHE B CD1 
3687 C CD2 . PHE B 222 ? 0.7808 0.6128 0.6250 -0.0990 0.0635  -0.0974 222 PHE B CD2 
3688 C CE1 . PHE B 222 ? 0.7475 0.6041 0.5743 -0.1081 0.0543  -0.0937 222 PHE B CE1 
3689 C CE2 . PHE B 222 ? 0.7686 0.6048 0.5988 -0.1109 0.0643  -0.1034 222 PHE B CE2 
3690 C CZ  . PHE B 222 ? 0.7394 0.5889 0.5604 -0.1157 0.0594  -0.1014 222 PHE B CZ  
3691 N N   . LEU B 223 ? 0.7675 0.6349 0.6287 -0.0803 0.0365  -0.0718 223 LEU B N   
3692 C CA  . LEU B 223 ? 0.7612 0.6407 0.6235 -0.0788 0.0307  -0.0652 223 LEU B CA  
3693 C C   . LEU B 223 ? 0.8342 0.7251 0.6872 -0.0879 0.0281  -0.0651 223 LEU B C   
3694 O O   . LEU B 223 ? 0.8783 0.7730 0.7303 -0.0913 0.0258  -0.0656 223 LEU B O   
3695 C CB  . LEU B 223 ? 0.7468 0.6297 0.6194 -0.0718 0.0260  -0.0596 223 LEU B CB  
3696 C CG  . LEU B 223 ? 0.6623 0.5543 0.5401 -0.0681 0.0222  -0.0522 223 LEU B CG  
3697 C CD1 . LEU B 223 ? 0.7280 0.6145 0.6079 -0.0643 0.0248  -0.0518 223 LEU B CD1 
3698 C CD2 . LEU B 223 ? 0.5311 0.4253 0.4180 -0.0626 0.0194  -0.0482 223 LEU B CD2 
3699 N N   . ASP B 224 ? 0.8412 0.7386 0.6872 -0.0923 0.0284  -0.0640 224 ASP B N   
3700 C CA  . ASP B 224 ? 0.7617 0.6743 0.5988 -0.1019 0.0248  -0.0619 224 ASP B CA  
3701 C C   . ASP B 224 ? 0.6805 0.6077 0.5269 -0.0975 0.0176  -0.0507 224 ASP B C   
3702 O O   . ASP B 224 ? 0.8803 0.8111 0.7338 -0.0914 0.0162  -0.0438 224 ASP B O   
3703 C CB  . ASP B 224 ? 0.8257 0.7412 0.6525 -0.1081 0.0278  -0.0636 224 ASP B CB  
3704 C CG  . ASP B 224 ? 0.9406 0.8731 0.7552 -0.1209 0.0246  -0.0623 224 ASP B CG  
3705 O OD1 . ASP B 224 ? 0.8491 0.7972 0.6675 -0.1222 0.0176  -0.0542 224 ASP B OD1 
3706 O OD2 . ASP B 224 ? 0.9749 0.9055 0.7759 -0.1303 0.0295  -0.0695 224 ASP B OD2 
3707 N N   . ILE B 225 ? 0.7790 0.7140 0.6270 -0.1001 0.0138  -0.0484 225 ILE B N   
3708 C CA  . ILE B 225 ? 0.7341 0.6841 0.5922 -0.0962 0.0081  -0.0368 225 ILE B CA  
3709 C C   . ILE B 225 ? 0.7762 0.7470 0.6281 -0.1064 0.0035  -0.0307 225 ILE B C   
3710 O O   . ILE B 225 ? 0.8112 0.7965 0.6720 -0.1046 -0.0012 -0.0206 225 ILE B O   
3711 C CB  . ILE B 225 ? 0.7280 0.6739 0.5963 -0.0897 0.0071  -0.0359 225 ILE B CB  
3712 C CG1 . ILE B 225 ? 0.6970 0.6385 0.5583 -0.0962 0.0080  -0.0435 225 ILE B CG1 
3713 C CG2 . ILE B 225 ? 0.6152 0.5461 0.4915 -0.0794 0.0104  -0.0382 225 ILE B CG2 
3714 C CD1 . ILE B 225 ? 0.6820 0.6273 0.5523 -0.0925 0.0053  -0.0397 225 ILE B CD1 
3715 N N   . SER B 226 ? 0.6954 0.6687 0.5322 -0.1173 0.0051  -0.0362 226 SER B N   
3716 C CA  . SER B 226 ? 0.7894 0.7846 0.6179 -0.1295 0.0003  -0.0309 226 SER B CA  
3717 C C   . SER B 226 ? 0.8294 0.8451 0.6689 -0.1256 -0.0053 -0.0144 226 SER B C   
3718 O O   . SER B 226 ? 0.8987 0.9344 0.7421 -0.1298 -0.0110 -0.0046 226 SER B O   
3719 C CB  . SER B 226 ? 0.8268 0.8208 0.6366 -0.1420 0.0042  -0.0399 226 SER B CB  
3720 O OG  . SER B 226 ? 0.9397 0.9108 0.7422 -0.1430 0.0120  -0.0546 226 SER B OG  
3721 N N   . ASP B 227 ? 0.7964 0.8077 0.6427 -0.1172 -0.0036 -0.0102 227 ASP B N   
3722 C CA  . ASP B 227 ? 0.8488 0.8797 0.7060 -0.1141 -0.0079 0.0062  227 ASP B CA  
3723 C C   . ASP B 227 ? 0.8370 0.8712 0.7145 -0.1032 -0.0096 0.0164  227 ASP B C   
3724 O O   . ASP B 227 ? 0.9001 0.9518 0.7896 -0.1004 -0.0126 0.0317  227 ASP B O   
3725 C CB  . ASP B 227 ? 0.8523 0.8783 0.7105 -0.1096 -0.0050 0.0078  227 ASP B CB  
3726 C CG  . ASP B 227 ? 0.9497 0.9734 0.7881 -0.1206 -0.0022 -0.0017 227 ASP B CG  
3727 O OD1 . ASP B 227 ? 0.8162 0.8514 0.6404 -0.1342 -0.0041 -0.0048 227 ASP B OD1 
3728 O OD2 . ASP B 227 ? 1.0423 1.0525 0.8797 -0.1160 0.0025  -0.0066 227 ASP B OD2 
3729 N N   . GLN B 228 ? 0.7764 0.7951 0.6582 -0.0973 -0.0073 0.0091  228 GLN B N   
3730 C CA  . GLN B 228 ? 0.8179 0.8384 0.7174 -0.0878 -0.0076 0.0171  228 GLN B CA  
3731 C C   . GLN B 228 ? 0.8506 0.8807 0.7503 -0.0927 -0.0108 0.0182  228 GLN B C   
3732 O O   . GLN B 228 ? 0.8551 0.8883 0.7696 -0.0855 -0.0107 0.0253  228 GLN B O   
3733 C CB  . GLN B 228 ? 0.8282 0.8254 0.7339 -0.0773 -0.0024 0.0091  228 GLN B CB  
3734 C CG  . GLN B 228 ? 0.7506 0.7393 0.6607 -0.0708 0.0009  0.0102  228 GLN B CG  
3735 C CD  . GLN B 228 ? 0.7953 0.7772 0.6906 -0.0766 0.0022  0.0017  228 GLN B CD  
3736 O OE1 . GLN B 228 ? 0.7834 0.7533 0.6681 -0.0801 0.0041  -0.0100 228 GLN B OE1 
3737 N NE2 . GLN B 228 ? 0.8002 0.7903 0.6954 -0.0776 0.0018  0.0085  228 GLN B NE2 
3738 N N   . THR B 229 ? 0.7802 0.8137 0.6638 -0.1049 -0.0129 0.0107  229 THR B N   
3739 C CA  . THR B 229 ? 0.8252 0.8647 0.7073 -0.1105 -0.0154 0.0092  229 THR B CA  
3740 C C   . THR B 229 ? 0.8754 0.9396 0.7493 -0.1246 -0.0212 0.0155  229 THR B C   
3741 O O   . THR B 229 ? 0.7727 0.8553 0.6564 -0.1254 -0.0255 0.0267  229 THR B O   
3742 C CB  . THR B 229 ? 0.8223 0.8401 0.6932 -0.1128 -0.0113 -0.0075 229 THR B CB  
3743 O OG1 . THR B 229 ? 0.8422 0.8536 0.6968 -0.1212 -0.0088 -0.0167 229 THR B OG1 
3744 C CG2 . THR B 229 ? 0.6429 0.6403 0.5231 -0.0999 -0.0067 -0.0119 229 THR B CG2 
3745 N N   . LEU B 230 ? 0.9198 0.9853 0.7756 -0.1365 -0.0210 0.0083  230 LEU B N   
3746 C CA  . LEU B 230 ? 0.9434 1.0272 0.7854 -0.1536 -0.0254 0.0080  230 LEU B CA  
3747 C C   . LEU B 230 ? 0.9445 1.0613 0.7943 -0.1578 -0.0327 0.0273  230 LEU B C   
3748 O O   . LEU B 230 ? 0.9497 1.0854 0.8031 -0.1641 -0.0379 0.0349  230 LEU B O   
3749 C CB  . LEU B 230 ? 0.8313 0.9062 0.6514 -0.1655 -0.0215 -0.0058 230 LEU B CB  
3750 C CG  . LEU B 230 ? 0.8702 0.9150 0.6816 -0.1644 -0.0134 -0.0245 230 LEU B CG  
3751 C CD1 . LEU B 230 ? 0.8371 0.8753 0.6290 -0.1759 -0.0085 -0.0361 230 LEU B CD1 
3752 C CD2 . LEU B 230 ? 0.9315 0.9710 0.7421 -0.1682 -0.0133 -0.0308 230 LEU B CD2 
3753 N N   . GLU B 231 ? 0.9256 1.0508 0.7793 -0.1545 -0.0334 0.0365  231 GLU B N   
3754 C CA  . GLU B 231 ? 0.9539 1.1128 0.8131 -0.1609 -0.0404 0.0555  231 GLU B CA  
3755 C C   . GLU B 231 ? 1.0110 1.1851 0.8940 -0.1518 -0.0436 0.0725  231 GLU B C   
3756 O O   . GLU B 231 ? 1.0159 1.2163 0.9007 -0.1611 -0.0500 0.0832  231 GLU B O   
3757 C CB  . GLU B 231 ? 1.0215 1.1846 0.8825 -0.1573 -0.0395 0.0628  231 GLU B CB  
3758 C CG  . GLU B 231 ? 1.1409 1.3408 1.0105 -0.1626 -0.0468 0.0854  231 GLU B CG  
3759 C CD  . GLU B 231 ? 1.2180 1.4264 1.0808 -0.1663 -0.0469 0.0902  231 GLU B CD  
3760 O OE1 . GLU B 231 ? 1.2363 1.4320 1.0772 -0.1751 -0.0436 0.0743  231 GLU B OE1 
3761 O OE2 . GLU B 231 ? 1.2611 1.4893 1.1412 -0.1604 -0.0497 0.1106  231 GLU B OE2 
3762 N N   . LYS B 232 ? 0.9637 1.1214 0.8652 -0.1342 -0.0388 0.0750  232 LYS B N   
3763 C CA  . LYS B 232 ? 0.8975 1.0688 0.8238 -0.1244 -0.0399 0.0920  232 LYS B CA  
3764 C C   . LYS B 232 ? 0.9860 1.1624 0.9127 -0.1289 -0.0423 0.0900  232 LYS B C   
3765 O O   . LYS B 232 ? 1.0349 1.2359 0.9765 -0.1292 -0.0464 0.1068  232 LYS B O   
3766 C CB  . LYS B 232 ? 0.8815 1.0305 0.8247 -0.1062 -0.0325 0.0915  232 LYS B CB  
3767 C CG  . LYS B 232 ? 0.9868 1.1427 0.9434 -0.0987 -0.0309 0.1053  232 LYS B CG  
3768 C CD  . LYS B 232 ? 1.0129 1.1499 0.9902 -0.0813 -0.0231 0.1072  232 LYS B CD  
3769 C CE  . LYS B 232 ? 1.0079 1.1575 1.0086 -0.0740 -0.0219 0.1218  232 LYS B CE  
3770 N NZ  . LYS B 232 ? 1.0534 1.2280 1.0760 -0.0698 -0.0227 0.1462  232 LYS B NZ  
3771 N N   . THR B 233 ? 0.9314 1.0859 0.8431 -0.1325 -0.0397 0.0707  233 THR B N   
3772 C CA  . THR B 233 ? 0.9312 1.0903 0.8416 -0.1383 -0.0420 0.0679  233 THR B CA  
3773 C C   . THR B 233 ? 0.9577 1.1451 0.8565 -0.1568 -0.0496 0.0735  233 THR B C   
3774 O O   . THR B 233 ? 1.0140 1.2224 0.9217 -0.1606 -0.0542 0.0845  233 THR B O   
3775 C CB  . THR B 233 ? 1.0070 1.1362 0.9040 -0.1384 -0.0370 0.0465  233 THR B CB  
3776 O OG1 . THR B 233 ? 1.0348 1.1395 0.9405 -0.1230 -0.0305 0.0413  233 THR B OG1 
3777 C CG2 . THR B 233 ? 0.8155 0.9481 0.7138 -0.1426 -0.0387 0.0445  233 THR B CG2 
3778 N N   . PHE B 234 ? 0.9695 1.1583 0.8478 -0.1695 -0.0506 0.0658  234 PHE B N   
3779 C CA  . PHE B 234 ? 1.0243 1.2400 0.8885 -0.1896 -0.0575 0.0692  234 PHE B CA  
3780 C C   . PHE B 234 ? 1.0944 1.3479 0.9746 -0.1908 -0.0649 0.0949  234 PHE B C   
3781 O O   . PHE B 234 ? 1.0286 1.3088 0.9094 -0.2022 -0.0715 0.1042  234 PHE B O   
3782 C CB  . PHE B 234 ? 1.0176 1.2248 0.8563 -0.2025 -0.0553 0.0547  234 PHE B CB  
3783 C CG  . PHE B 234 ? 1.0700 1.2469 0.8917 -0.2070 -0.0486 0.0309  234 PHE B CG  
3784 C CD1 . PHE B 234 ? 1.0826 1.2525 0.9061 -0.2082 -0.0483 0.0249  234 PHE B CD1 
3785 C CD2 . PHE B 234 ? 0.9930 1.1485 0.7985 -0.2096 -0.0421 0.0153  234 PHE B CD2 
3786 C CE1 . PHE B 234 ? 0.9795 1.1216 0.7891 -0.2120 -0.0415 0.0042  234 PHE B CE1 
3787 C CE2 . PHE B 234 ? 0.8922 1.0197 0.6845 -0.2131 -0.0349 -0.0054 234 PHE B CE2 
3788 C CZ  . PHE B 234 ? 0.8406 0.9615 0.6352 -0.2143 -0.0346 -0.0106 234 PHE B CZ  
3789 N N   . ARG B 235 ? 1.1363 1.3935 1.0312 -0.1790 -0.0637 0.1076  235 ARG B N   
3790 C CA  . ARG B 235 ? 1.0974 1.3889 1.0139 -0.1762 -0.0692 0.1347  235 ARG B CA  
3791 C C   . ARG B 235 ? 1.1436 1.4433 1.0816 -0.1684 -0.0699 0.1453  235 ARG B C   
3792 O O   . ARG B 235 ? 1.2265 1.5576 1.1692 -0.1784 -0.0770 0.1593  235 ARG B O   
3793 C CB  . ARG B 235 ? 1.0054 1.2923 0.9387 -0.1609 -0.0652 0.1454  235 ARG B CB  
3794 C CG  . ARG B 235 ? 1.1043 1.3902 1.0206 -0.1680 -0.0653 0.1406  235 ARG B CG  
3795 C CD  . ARG B 235 ? 1.2373 1.5589 1.1645 -0.1714 -0.0711 0.1652  235 ARG B CD  
3796 N NE  . ARG B 235 ? 1.3205 1.6451 1.2248 -0.1839 -0.0724 0.1583  235 ARG B NE  
3797 C CZ  . ARG B 235 ? 1.3698 1.6700 1.2685 -0.1765 -0.0663 0.1479  235 ARG B CZ  
3798 N NH1 . ARG B 235 ? 1.3361 1.6081 1.2504 -0.1574 -0.0588 0.1437  235 ARG B NH1 
3799 N NH2 . ARG B 235 ? 1.4275 1.7327 1.3047 -0.1892 -0.0673 0.1420  235 ARG B NH2 
3800 N N   . LEU B 236 ? 1.1531 1.4252 1.1044 -0.1511 -0.0622 0.1389  236 LEU B N   
3801 C CA  . LEU B 236 ? 1.1138 1.3924 1.0881 -0.1414 -0.0611 0.1499  236 LEU B CA  
3802 C C   . LEU B 236 ? 1.1956 1.4861 1.1606 -0.1548 -0.0663 0.1460  236 LEU B C   
3803 O O   . LEU B 236 ? 1.2403 1.5533 1.2234 -0.1533 -0.0692 0.1624  236 LEU B O   
3804 C CB  . LEU B 236 ? 1.0214 1.2654 1.0057 -0.1233 -0.0513 0.1393  236 LEU B CB  
3805 C CG  . LEU B 236 ? 0.9695 1.2046 0.9741 -0.1064 -0.0446 0.1485  236 LEU B CG  
3806 C CD1 . LEU B 236 ? 0.8036 1.0064 0.8161 -0.0915 -0.0352 0.1365  236 LEU B CD1 
3807 C CD2 . LEU B 236 ? 1.0014 1.2683 1.0330 -0.1017 -0.0465 0.1767  236 LEU B CD2 
3808 N N   . LEU B 237 ? 1.2062 1.4833 1.1439 -0.1684 -0.0673 0.1256  237 LEU B N   
3809 C CA  . LEU B 237 ? 1.2988 1.5856 1.2272 -0.1820 -0.0717 0.1209  237 LEU B CA  
3810 C C   . LEU B 237 ? 1.3940 1.7206 1.3157 -0.2014 -0.0815 0.1343  237 LEU B C   
3811 O O   . LEU B 237 ? 1.4165 1.7668 1.3467 -0.2076 -0.0867 0.1455  237 LEU B O   
3812 C CB  . LEU B 237 ? 1.2876 1.5433 1.1915 -0.1890 -0.0674 0.0939  237 LEU B CB  
3813 C CG  . LEU B 237 ? 1.2680 1.5301 1.1642 -0.2018 -0.0705 0.0883  237 LEU B CG  
3814 C CD1 . LEU B 237 ? 1.2808 1.5125 1.1799 -0.1914 -0.0639 0.0745  237 LEU B CD1 
3815 C CD2 . LEU B 237 ? 1.2519 1.5181 1.1202 -0.2244 -0.0733 0.0755  237 LEU B CD2 
3816 N N   . SER B 238 ? 1.4317 1.7676 1.3381 -0.2120 -0.0842 0.1340  238 SER B N   
3817 C CA  . SER B 238 ? 1.3644 1.7407 1.2629 -0.2321 -0.0939 0.1472  238 SER B CA  
3818 C C   . SER B 238 ? 1.3529 1.7656 1.2809 -0.2251 -0.0994 0.1785  238 SER B C   
3819 O O   . SER B 238 ? 1.3588 1.8081 1.2883 -0.2394 -0.1080 0.1929  238 SER B O   
3820 C CB  . SER B 238 ? 1.2486 1.6276 1.1251 -0.2442 -0.0949 0.1411  238 SER B CB  
3821 O OG  . SER B 238 ? 1.2545 1.6775 1.1301 -0.2596 -0.1045 0.1607  238 SER B OG  
3822 N N   . GLU B 239 ? 1.3553 1.7594 1.3076 -0.2037 -0.0940 0.1897  239 GLU B N   
3823 C CA  . GLU B 239 ? 1.3482 1.7834 1.3328 -0.1945 -0.0967 0.2197  239 GLU B CA  
3824 C C   . GLU B 239 ? 1.3820 1.8228 1.3828 -0.1903 -0.0968 0.2252  239 GLU B C   
3825 O O   . GLU B 239 ? 1.4027 1.8798 1.4242 -0.1918 -0.1022 0.2500  239 GLU B O   
3826 C CB  . GLU B 239 ? 1.3707 1.7907 1.3773 -0.1726 -0.0889 0.2280  239 GLU B CB  
3827 C CG  . GLU B 239 ? 1.4737 1.9280 1.5142 -0.1641 -0.0908 0.2612  239 GLU B CG  
3828 C CD  . GLU B 239 ? 1.5444 1.9860 1.6154 -0.1434 -0.0822 0.2685  239 GLU B CD  
3829 O OE1 . GLU B 239 ? 1.5907 2.0033 1.6550 -0.1388 -0.0771 0.2490  239 GLU B OE1 
3830 O OE2 . GLU B 239 ? 1.5125 1.9745 1.6148 -0.1322 -0.0802 0.2945  239 GLU B OE2 
3831 N N   . ARG B 240 ? 1.4169 1.8238 1.4097 -0.1852 -0.0907 0.2036  240 ARG B N   
3832 C CA  . ARG B 240 ? 1.3940 1.8068 1.3973 -0.1848 -0.0914 0.2063  240 ARG B CA  
3833 C C   . ARG B 240 ? 1.5122 1.9553 1.4996 -0.2090 -0.1018 0.2084  240 ARG B C   
3834 O O   . ARG B 240 ? 1.6076 2.0880 1.6119 -0.2136 -0.1083 0.2311  240 ARG B O   
3835 C CB  . ARG B 240 ? 1.3313 1.7019 1.3265 -0.1761 -0.0831 0.1818  240 ARG B CB  
3836 C CG  . ARG B 240 ? 1.3248 1.6620 1.3308 -0.1547 -0.0726 0.1751  240 ARG B CG  
3837 C CD  . ARG B 240 ? 1.3702 1.7156 1.4107 -0.1361 -0.0675 0.1957  240 ARG B CD  
3838 N NE  . ARG B 240 ? 1.4107 1.7518 1.4648 -0.1292 -0.0638 0.1960  240 ARG B NE  
3839 C CZ  . ARG B 240 ? 1.4580 1.7657 1.5119 -0.1177 -0.0552 0.1801  240 ARG B CZ  
3840 N NH1 . ARG B 240 ? 1.3814 1.6570 1.4227 -0.1119 -0.0497 0.1625  240 ARG B NH1 
3841 N NH2 . ARG B 240 ? 1.4978 1.8058 1.5641 -0.1128 -0.0524 0.1822  240 ARG B NH2 
3842 N N   . ILE B 241 ? 1.5070 1.9351 1.4619 -0.2255 -0.1029 0.1854  241 ILE B N   
3843 C CA  . ILE B 241 ? 1.4887 1.9374 1.4253 -0.2494 -0.1106 0.1814  241 ILE B CA  
3844 C C   . ILE B 241 ? 1.5493 2.0486 1.4902 -0.2645 -0.1216 0.2060  241 ILE B C   
3845 O O   . ILE B 241 ? 1.6104 2.1391 1.5522 -0.2789 -0.1291 0.2152  241 ILE B O   
3846 C CB  . ILE B 241 ? 1.4625 1.8835 1.3638 -0.2639 -0.1077 0.1518  241 ILE B CB  
3847 C CG1 . ILE B 241 ? 1.5181 1.9450 1.4030 -0.2725 -0.1092 0.1506  241 ILE B CG1 
3848 C CG2 . ILE B 241 ? 1.4178 1.7914 1.3174 -0.2481 -0.0971 0.1305  241 ILE B CG2 
3849 C CD1 . ILE B 241 ? 1.5142 1.9132 1.3665 -0.2855 -0.1044 0.1223  241 ILE B CD1 
3850 N N   . ASN B 242 ? 1.5751 2.0871 1.5193 -0.2620 -0.1230 0.2179  242 ASN B N   
3851 C CA  . ASN B 242 ? 1.5343 2.0955 1.4800 -0.2780 -0.1338 0.2411  242 ASN B CA  
3852 C C   . ASN B 242 ? 1.5566 2.1520 1.5411 -0.2653 -0.1370 0.2754  242 ASN B C   
3853 O O   . ASN B 242 ? 1.5545 2.1967 1.5443 -0.2799 -0.1473 0.2977  242 ASN B O   
3854 C CB  . ASN B 242 ? 1.4388 2.0001 1.3690 -0.2829 -0.1340 0.2388  242 ASN B CB  
3855 C CG  . ASN B 242 ? 1.3788 1.9177 1.2688 -0.3018 -0.1322 0.2085  242 ASN B CG  
3856 O OD1 . ASN B 242 ? 1.3244 1.8288 1.2024 -0.2944 -0.1244 0.1903  242 ASN B OD1 
3857 N ND2 . ASN B 242 ? 1.3736 1.9322 1.2435 -0.3268 -0.1388 0.2030  242 ASN B ND2 
3858 N N   . SER B 243 ? 1.5170 2.0909 1.5289 -0.2393 -0.1281 0.2803  243 SER B N   
3859 C CA  . SER B 243 ? 1.4837 2.0850 1.5348 -0.2254 -0.1283 0.3112  243 SER B CA  
3860 C C   . SER B 243 ? 1.5564 2.1681 1.6179 -0.2277 -0.1302 0.3148  243 SER B C   
3861 O O   . SER B 243 ? 1.5874 2.2146 1.6833 -0.2132 -0.1276 0.3374  243 SER B O   
3862 C CB  . SER B 243 ? 1.3705 1.9429 1.4464 -0.1973 -0.1162 0.3139  243 SER B CB  
3863 O OG  . SER B 243 ? 1.2774 1.8562 1.3867 -0.1818 -0.1115 0.3302  243 SER B OG  
3864 N N   . SER B 244 ? 1.5632 2.1653 1.5969 -0.2450 -0.1334 0.2930  244 SER B N   
3865 C CA  . SER B 244 ? 1.5229 2.1318 1.5621 -0.2493 -0.1353 0.2928  244 SER B CA  
3866 C C   . SER B 244 ? 1.5608 2.1992 1.5757 -0.2796 -0.1468 0.2902  244 SER B C   
3867 O O   . SER B 244 ? 1.5629 2.1835 1.5574 -0.2906 -0.1463 0.2687  244 SER B O   
3868 C CB  . SER B 244 ? 1.4859 2.0460 1.5173 -0.2380 -0.1252 0.2657  244 SER B CB  
3869 O OG  . SER B 244 ? 1.4674 2.0026 1.5222 -0.2114 -0.1145 0.2686  244 SER B OG  
3870 N N   . LYS B 245 ? 1.5728 2.2564 1.5890 -0.2941 -0.1569 0.3120  245 LYS B N   
3871 C CA  . LYS B 245 ? 1.5823 2.3044 1.5841 -0.3221 -0.1676 0.3187  245 LYS B CA  
3872 C C   . LYS B 245 ? 1.5549 2.2537 1.5221 -0.3415 -0.1664 0.2878  245 LYS B C   
3873 O O   . LYS B 245 ? 1.5321 2.2408 1.4762 -0.3642 -0.1667 0.2820  245 LYS B O   
3874 C CB  . LYS B 245 ? 1.5361 2.2921 1.5721 -0.3160 -0.1692 0.3488  245 LYS B CB  
3875 C CG  . LYS B 245 ? 1.4228 2.1643 1.4811 -0.2988 -0.1661 0.3473  245 LYS B CG  
3876 C CD  . LYS B 245 ? 1.3768 2.1520 1.4596 -0.2998 -0.1684 0.3725  245 LYS B CD  
3877 C CE  . LYS B 245 ? 1.3360 2.1220 1.3892 -0.3272 -0.1718 0.3643  245 LYS B CE  
3878 N NZ  . LYS B 245 ? 1.2636 2.0137 1.2817 -0.3393 -0.1708 0.3274  245 LYS B NZ  
3879 N N   . VAL B 257 ? 1.5828 1.9497 1.4198 -0.3391 -0.1033 0.0668  257 VAL B N   
3880 C CA  . VAL B 257 ? 1.6393 2.0496 1.4737 -0.3553 -0.1137 0.0836  257 VAL B CA  
3881 C C   . VAL B 257 ? 1.7914 2.2007 1.5936 -0.3802 -0.1136 0.0674  257 VAL B C   
3882 O O   . VAL B 257 ? 1.8489 2.2579 1.6327 -0.4020 -0.1136 0.0543  257 VAL B O   
3883 C CB  . VAL B 257 ? 1.5808 2.0295 1.4283 -0.3656 -0.1230 0.1019  257 VAL B CB  
3884 C CG1 . VAL B 257 ? 1.5416 1.9744 1.3798 -0.3764 -0.1199 0.0860  257 VAL B CG1 
3885 C CG2 . VAL B 257 ? 1.5778 2.0720 1.4166 -0.3884 -0.1341 0.1163  257 VAL B CG2 
3886 N N   . ASN B 258 ? 1.8978 2.3056 1.6931 -0.3773 -0.1126 0.0675  258 ASN B N   
3887 C CA  . ASN B 258 ? 1.9310 2.3396 1.6964 -0.4002 -0.1115 0.0535  258 ASN B CA  
3888 C C   . ASN B 258 ? 1.9303 2.3445 1.6937 -0.3944 -0.1125 0.0597  258 ASN B C   
3889 O O   . ASN B 258 ? 1.9291 2.3470 1.7145 -0.3723 -0.1135 0.0760  258 ASN B O   
3890 C CB  . ASN B 258 ? 1.9320 2.2953 1.6765 -0.4049 -0.0985 0.0234  258 ASN B CB  
3891 C CG  . ASN B 258 ? 1.9347 2.2957 1.6549 -0.4260 -0.0907 0.0116  258 ASN B CG  
3892 O OD1 . ASN B 258 ? 1.9815 2.3080 1.6846 -0.4301 -0.0786 -0.0114 258 ASN B OD1 
3893 N ND2 . ASN B 258 ? 1.8931 2.2917 1.6130 -0.4395 -0.0971 0.0281  258 ASN B ND2 
3894 N N   . GLN B 259 ? 1.9370 2.3429 1.6773 -0.4084 -0.1058 0.0468  259 GLN B N   
3895 C CA  . GLN B 259 ? 1.8549 2.2712 1.5951 -0.4038 -0.1081 0.0554  259 GLN B CA  
3896 C C   . GLN B 259 ? 1.7927 2.1724 1.5260 -0.3905 -0.1008 0.0391  259 GLN B C   
3897 O O   . GLN B 259 ? 1.8099 2.1859 1.5287 -0.3957 -0.0970 0.0333  259 GLN B O   
3898 C CB  . GLN B 259 ? 1.7851 2.2160 1.5064 -0.4243 -0.1047 0.0536  259 GLN B CB  
3899 C CG  . GLN B 259 ? 1.8090 2.2064 1.5046 -0.4380 -0.0912 0.0252  259 GLN B CG  
3900 C CD  . GLN B 259 ? 1.8746 2.2886 1.5600 -0.4596 -0.0899 0.0250  259 GLN B CD  
3901 O OE1 . GLN B 259 ? 1.9093 2.3056 1.5732 -0.4745 -0.0793 0.0061  259 GLN B OE1 
3902 N NE2 . GLN B 259 ? 1.8548 2.3032 1.5560 -0.4613 -0.1002 0.0466  259 GLN B NE2 
3903 N N   . PHE B 260 ? 1.7323 2.0798 1.4815 -0.3677 -0.0939 0.0336  260 PHE B N   
3904 C CA  . PHE B 260 ? 1.7624 2.0740 1.5102 -0.3509 -0.0842 0.0215  260 PHE B CA  
3905 C C   . PHE B 260 ? 1.8383 2.1643 1.5995 -0.3368 -0.0876 0.0394  260 PHE B C   
3906 O O   . PHE B 260 ? 1.8093 2.1466 1.5969 -0.3187 -0.0914 0.0586  260 PHE B O   
3907 C CB  . PHE B 260 ? 1.6702 1.9451 1.4310 -0.3306 -0.0761 0.0119  260 PHE B CB  
3908 C CG  . PHE B 260 ? 1.7213 1.9706 1.4908 -0.3086 -0.0696 0.0096  260 PHE B CG  
3909 C CD1 . PHE B 260 ? 1.7721 1.9990 1.5234 -0.3122 -0.0620 -0.0068 260 PHE B CD1 
3910 C CD2 . PHE B 260 ? 1.7342 1.9831 1.5299 -0.2852 -0.0707 0.0242  260 PHE B CD2 
3911 C CE1 . PHE B 260 ? 1.7882 1.9935 1.5478 -0.2927 -0.0565 -0.0081 260 PHE B CE1 
3912 C CE2 . PHE B 260 ? 1.7356 1.9619 1.5384 -0.2666 -0.0649 0.0217  260 PHE B CE2 
3913 C CZ  . PHE B 260 ? 1.7568 1.9619 1.5417 -0.2703 -0.0583 0.0060  260 PHE B CZ  
3914 N N   . ASP B 261 ? 1.8392 2.1631 1.5830 -0.3444 -0.0852 0.0327  261 ASP B N   
3915 C CA  . ASP B 261 ? 1.7478 2.0869 1.5029 -0.3334 -0.0886 0.0498  261 ASP B CA  
3916 C C   . ASP B 261 ? 1.6706 1.9747 1.4298 -0.3134 -0.0794 0.0404  261 ASP B C   
3917 O O   . ASP B 261 ? 1.6307 1.9098 1.3698 -0.3193 -0.0714 0.0203  261 ASP B O   
3918 C CB  . ASP B 261 ? 1.7534 2.1180 1.4859 -0.3565 -0.0928 0.0505  261 ASP B CB  
3919 C CG  . ASP B 261 ? 1.7738 2.1155 1.4741 -0.3763 -0.0847 0.0223  261 ASP B CG  
3920 O OD1 . ASP B 261 ? 1.7717 2.1052 1.4641 -0.3871 -0.0827 0.0103  261 ASP B OD1 
3921 O OD2 . ASP B 261 ? 1.7854 2.1161 1.4694 -0.3806 -0.0792 0.0121  261 ASP B OD2 
3922 N N   . PRO B 262 ? 1.5823 1.8844 1.3678 -0.2901 -0.0798 0.0551  262 PRO B N   
3923 C CA  . PRO B 262 ? 1.5275 1.7967 1.3175 -0.2715 -0.0714 0.0463  262 PRO B CA  
3924 C C   . PRO B 262 ? 1.5427 1.8206 1.3243 -0.2749 -0.0718 0.0501  262 PRO B C   
3925 O O   . PRO B 262 ? 1.6210 1.8736 1.3906 -0.2726 -0.0643 0.0350  262 PRO B O   
3926 C CB  . PRO B 262 ? 1.4405 1.7103 1.2610 -0.2487 -0.0724 0.0626  262 PRO B CB  
3927 C CG  . PRO B 262 ? 1.4172 1.7122 1.2486 -0.2540 -0.0792 0.0752  262 PRO B CG  
3928 C CD  . PRO B 262 ? 1.4953 1.8217 1.3089 -0.2788 -0.0865 0.0790  262 PRO B CD  
3929 N N   . GLY B 263 ? 1.4915 1.8074 1.2797 -0.2811 -0.0806 0.0713  263 GLY B N   
3930 C CA  . GLY B 263 ? 1.4592 1.7851 1.2414 -0.2833 -0.0812 0.0770  263 GLY B CA  
3931 C C   . GLY B 263 ? 1.4751 1.7924 1.2272 -0.3005 -0.0770 0.0588  263 GLY B C   
3932 O O   . GLY B 263 ? 1.4748 1.7883 1.2223 -0.2975 -0.0743 0.0588  263 GLY B O   
3933 N N   . ASP B 264 ? 1.4657 1.7806 1.1971 -0.3194 -0.0759 0.0435  264 ASP B N   
3934 C CA  . ASP B 264 ? 1.4461 1.7524 1.1495 -0.3359 -0.0705 0.0262  264 ASP B CA  
3935 C C   . ASP B 264 ? 1.4367 1.7013 1.1415 -0.3190 -0.0593 0.0107  264 ASP B C   
3936 O O   . ASP B 264 ? 1.3491 1.5977 1.0334 -0.3277 -0.0517 -0.0058 264 ASP B O   
3937 C CB  . ASP B 264 ? 1.5074 1.8105 1.1891 -0.3579 -0.0686 0.0089  264 ASP B CB  
3938 C CG  . ASP B 264 ? 1.6811 1.9971 1.3358 -0.3832 -0.0665 0.0000  264 ASP B CG  
3939 O OD1 . ASP B 264 ? 1.7280 2.0290 1.3715 -0.3827 -0.0591 -0.0096 264 ASP B OD1 
3940 O OD2 . ASP B 264 ? 1.7251 2.0621 1.3776 -0.3996 -0.0686 0.0036  264 ASP B OD2 
3941 N N   . LEU B 265 ? 1.5015 1.7480 1.2307 -0.2947 -0.0575 0.0159  265 LEU B N   
3942 C CA  . LEU B 265 ? 1.3746 1.5820 1.1013 -0.2825 -0.0465 -0.0011 265 LEU B CA  
3943 C C   . LEU B 265 ? 1.3057 1.5143 1.0492 -0.2646 -0.0474 0.0123  265 LEU B C   
3944 O O   . LEU B 265 ? 1.3690 1.5578 1.1072 -0.2590 -0.0405 0.0035  265 LEU B O   
3945 C CB  . LEU B 265 ? 1.2662 1.4456 1.0013 -0.2720 -0.0414 -0.0119 265 LEU B CB  
3946 C CG  . LEU B 265 ? 1.1686 1.3373 0.8849 -0.2893 -0.0370 -0.0301 265 LEU B CG  
3947 C CD1 . LEU B 265 ? 1.1206 1.2744 0.8513 -0.2788 -0.0361 -0.0322 265 LEU B CD1 
3948 C CD2 . LEU B 265 ? 1.1589 1.2986 0.8562 -0.2947 -0.0251 -0.0518 265 LEU B CD2 
3949 N N   . VAL B 266 ? 1.2227 1.4554 0.9874 -0.2562 -0.0554 0.0345  266 VAL B N   
3950 C CA  . VAL B 266 ? 1.2075 1.4440 0.9884 -0.2411 -0.0559 0.0486  266 VAL B CA  
3951 C C   . VAL B 266 ? 1.3012 1.5388 1.0633 -0.2507 -0.0532 0.0428  266 VAL B C   
3952 O O   . VAL B 266 ? 1.4296 1.6903 1.1737 -0.2708 -0.0571 0.0436  266 VAL B O   
3953 C CB  . VAL B 266 ? 1.1193 1.3930 0.9195 -0.2394 -0.0654 0.0756  266 VAL B CB  
3954 C CG1 . VAL B 266 ? 1.1313 1.4048 0.9531 -0.2208 -0.0644 0.0907  266 VAL B CG1 
3955 C CG2 . VAL B 266 ? 1.0425 1.3208 0.8572 -0.2355 -0.0685 0.0809  266 VAL B CG2 
3956 N N   . GLY B 267 ? 1.2575 1.4708 1.0228 -0.2376 -0.0463 0.0364  267 GLY B N   
3957 C CA  . GLY B 267 ? 1.2722 1.4856 1.0222 -0.2444 -0.0431 0.0320  267 GLY B CA  
3958 C C   . GLY B 267 ? 1.3474 1.5412 1.0700 -0.2589 -0.0349 0.0078  267 GLY B C   
3959 O O   . GLY B 267 ? 1.4672 1.6599 1.1763 -0.2647 -0.0310 0.0031  267 GLY B O   
3960 N N   . VAL B 268 ? 1.2597 1.4366 0.9738 -0.2648 -0.0309 -0.0080 268 VAL B N   
3961 C CA  . VAL B 268 ? 1.2412 1.3948 0.9322 -0.2758 -0.0202 -0.0312 268 VAL B CA  
3962 C C   . VAL B 268 ? 1.2684 1.3870 0.9703 -0.2560 -0.0113 -0.0397 268 VAL B C   
3963 O O   . VAL B 268 ? 1.3661 1.4588 1.0720 -0.2491 -0.0054 -0.0514 268 VAL B O   
3964 C CB  . VAL B 268 ? 1.1306 1.2789 0.8057 -0.2925 -0.0175 -0.0463 268 VAL B CB  
3965 C CG1 . VAL B 268 ? 1.2110 1.3487 0.9029 -0.2814 -0.0192 -0.0451 268 VAL B CG1 
3966 C CG2 . VAL B 268 ? 1.2054 1.3249 0.8601 -0.3012 -0.0038 -0.0703 268 VAL B CG2 
3967 N N   . LYS B 269 ? 1.2686 1.3873 0.9745 -0.2479 -0.0101 -0.0338 269 LYS B N   
3968 C CA  . LYS B 269 ? 1.1682 1.2647 0.8925 -0.2260 -0.0063 -0.0324 269 LYS B CA  
3969 C C   . LYS B 269 ? 1.1028 1.1636 0.8225 -0.2215 0.0053  -0.0522 269 LYS B C   
3970 O O   . LYS B 269 ? 1.1235 1.1653 0.8593 -0.2040 0.0079  -0.0520 269 LYS B O   
3971 C CB  . LYS B 269 ? 1.0588 1.1661 0.7862 -0.2215 -0.0075 -0.0216 269 LYS B CB  
3972 C CG  . LYS B 269 ? 1.1527 1.2404 0.8982 -0.2009 -0.0041 -0.0190 269 LYS B CG  
3973 C CD  . LYS B 269 ? 1.1721 1.2798 0.9368 -0.1906 -0.0116 0.0028  269 LYS B CD  
3974 C CE  . LYS B 269 ? 1.2050 1.2909 0.9892 -0.1702 -0.0081 0.0040  269 LYS B CE  
3975 N NZ  . LYS B 269 ? 1.2842 1.3510 1.0758 -0.1627 -0.0063 -0.0043 269 LYS B NZ  
3976 N N   . GLU B 270 ? 1.1682 1.2198 0.8675 -0.2369 0.0126  -0.0688 270 GLU B N   
3977 C CA  . GLU B 270 ? 1.1198 1.1379 0.8165 -0.2326 0.0250  -0.0863 270 GLU B CA  
3978 C C   . GLU B 270 ? 1.0910 1.0948 0.7968 -0.2273 0.0256  -0.0910 270 GLU B C   
3979 O O   . GLU B 270 ? 1.0244 1.0011 0.7335 -0.2205 0.0351  -0.1023 270 GLU B O   
3980 C CB  . GLU B 270 ? 1.0923 1.1039 0.7641 -0.2513 0.0350  -0.1030 270 GLU B CB  
3981 C CG  . GLU B 270 ? 1.2001 1.2206 0.8620 -0.2556 0.0370  -0.1010 270 GLU B CG  
3982 C CD  . GLU B 270 ? 1.3042 1.3620 0.9628 -0.2640 0.0245  -0.0840 270 GLU B CD  
3983 O OE1 . GLU B 270 ? 1.3106 1.3891 0.9717 -0.2698 0.0149  -0.0751 270 GLU B OE1 
3984 O OE2 . GLU B 270 ? 1.3739 1.4414 1.0288 -0.2643 0.0244  -0.0783 270 GLU B OE2 
3985 N N   . PHE B 271 ? 1.0415 1.0643 0.7528 -0.2301 0.0159  -0.0814 271 PHE B N   
3986 C CA  . PHE B 271 ? 0.9869 0.9992 0.7076 -0.2251 0.0155  -0.0841 271 PHE B CA  
3987 C C   . PHE B 271 ? 0.9671 0.9688 0.7109 -0.2029 0.0137  -0.0758 271 PHE B C   
3988 O O   . PHE B 271 ? 0.8858 0.9009 0.6415 -0.1934 0.0071  -0.0616 271 PHE B O   
3989 C CB  . PHE B 271 ? 0.8519 0.8902 0.5703 -0.2366 0.0060  -0.0760 271 PHE B CB  
3990 C CG  . PHE B 271 ? 0.9710 0.9988 0.6942 -0.2362 0.0068  -0.0815 271 PHE B CG  
3991 C CD1 . PHE B 271 ? 1.0029 1.0039 0.7183 -0.2401 0.0178  -0.0991 271 PHE B CD1 
3992 C CD2 . PHE B 271 ? 0.9015 0.9459 0.6387 -0.2314 -0.0025 -0.0685 271 PHE B CD2 
3993 C CE1 . PHE B 271 ? 0.9897 0.9811 0.7104 -0.2395 0.0188  -0.1033 271 PHE B CE1 
3994 C CE2 . PHE B 271 ? 0.8635 0.8986 0.6054 -0.2309 -0.0016 -0.0732 271 PHE B CE2 
3995 C CZ  . PHE B 271 ? 0.9113 0.9201 0.6447 -0.2351 0.0087  -0.0905 271 PHE B CZ  
3996 N N   . GLY B 272 ? 0.8476 0.8254 0.5976 -0.1952 0.0199  -0.0846 272 GLY B N   
3997 C CA  . GLY B 272 ? 0.9866 0.9507 0.7546 -0.1761 0.0206  -0.0802 272 GLY B CA  
3998 C C   . GLY B 272 ? 0.9622 0.9164 0.7428 -0.1674 0.0199  -0.0802 272 GLY B C   
3999 O O   . GLY B 272 ? 0.9148 0.8582 0.6906 -0.1734 0.0243  -0.0895 272 GLY B O   
4000 N N   . TYR B 273 ? 0.8085 0.7655 0.6054 -0.1532 0.0150  -0.0698 273 TYR B N   
4001 C CA  . TYR B 273 ? 0.7792 0.7292 0.5886 -0.1442 0.0137  -0.0682 273 TYR B CA  
4002 C C   . TYR B 273 ? 0.8565 0.7901 0.6767 -0.1299 0.0174  -0.0685 273 TYR B C   
4003 O O   . TYR B 273 ? 0.8286 0.7658 0.6542 -0.1231 0.0158  -0.0622 273 TYR B O   
4004 C CB  . TYR B 273 ? 0.7985 0.7691 0.6174 -0.1419 0.0050  -0.0552 273 TYR B CB  
4005 C CG  . TYR B 273 ? 0.8397 0.8068 0.6690 -0.1360 0.0035  -0.0538 273 TYR B CG  
4006 C CD1 . TYR B 273 ? 0.8930 0.8511 0.7168 -0.1424 0.0065  -0.0627 273 TYR B CD1 
4007 C CD2 . TYR B 273 ? 0.8129 0.7861 0.6577 -0.1245 -0.0003 -0.0435 273 TYR B CD2 
4008 C CE1 . TYR B 273 ? 0.6945 0.6506 0.5279 -0.1372 0.0050  -0.0607 273 TYR B CE1 
4009 C CE2 . TYR B 273 ? 0.8813 0.8521 0.7348 -0.1196 -0.0012 -0.0423 273 TYR B CE2 
4010 C CZ  . TYR B 273 ? 0.8144 0.7774 0.6621 -0.1259 0.0010  -0.0505 273 TYR B CZ  
4011 O OH  . TYR B 273 ? 0.7101 0.6716 0.5666 -0.1209 0.0000  -0.0487 273 TYR B OH  
4012 N N   . LEU B 274 ? 0.8517 0.7679 0.6752 -0.1260 0.0225  -0.0754 274 LEU B N   
4013 C CA  . LEU B 274 ? 0.9054 0.8062 0.7374 -0.1149 0.0268  -0.0767 274 LEU B CA  
4014 C C   . LEU B 274 ? 0.8376 0.7341 0.6814 -0.1064 0.0249  -0.0739 274 LEU B C   
4015 O O   . LEU B 274 ? 0.6845 0.5809 0.5277 -0.1103 0.0245  -0.0760 274 LEU B O   
4016 C CB  . LEU B 274 ? 0.8804 0.7640 0.7062 -0.1183 0.0364  -0.0870 274 LEU B CB  
4017 C CG  . LEU B 274 ? 0.8655 0.7383 0.6902 -0.1228 0.0413  -0.0941 274 LEU B CG  
4018 C CD1 . LEU B 274 ? 0.8730 0.7325 0.7107 -0.1120 0.0445  -0.0932 274 LEU B CD1 
4019 C CD2 . LEU B 274 ? 0.7941 0.6582 0.6059 -0.1341 0.0501  -0.1047 274 LEU B CD2 
4020 N N   . LEU B 275 ? 0.6563 0.5495 0.5100 -0.0958 0.0241  -0.0695 275 LEU B N   
4021 C CA  . LEU B 275 ? 0.7111 0.5986 0.5747 -0.0881 0.0236  -0.0679 275 LEU B CA  
4022 C C   . LEU B 275 ? 0.7472 0.6196 0.6129 -0.0846 0.0298  -0.0724 275 LEU B C   
4023 O O   . LEU B 275 ? 0.8450 0.7135 0.7102 -0.0825 0.0325  -0.0728 275 LEU B O   
4024 C CB  . LEU B 275 ? 0.6959 0.5901 0.5685 -0.0800 0.0192  -0.0604 275 LEU B CB  
4025 C CG  . LEU B 275 ? 0.6572 0.5508 0.5388 -0.0737 0.0174  -0.0577 275 LEU B CG  
4026 C CD1 . LEU B 275 ? 0.6788 0.5775 0.5673 -0.0676 0.0153  -0.0519 275 LEU B CD1 
4027 C CD2 . LEU B 275 ? 0.6897 0.5717 0.5744 -0.0702 0.0208  -0.0611 275 LEU B CD2 
4028 N N   . LEU B 276 ? 0.6701 0.5350 0.5393 -0.0841 0.0324  -0.0748 276 LEU B N   
4029 C CA  . LEU B 276 ? 0.7201 0.5721 0.5937 -0.0809 0.0389  -0.0772 276 LEU B CA  
4030 C C   . LEU B 276 ? 0.7702 0.6213 0.6537 -0.0743 0.0371  -0.0730 276 LEU B C   
4031 O O   . LEU B 276 ? 0.8252 0.6816 0.7102 -0.0747 0.0333  -0.0713 276 LEU B O   
4032 C CB  . LEU B 276 ? 0.7520 0.5941 0.6207 -0.0878 0.0464  -0.0842 276 LEU B CB  
4033 C CG  . LEU B 276 ? 0.7487 0.5770 0.6241 -0.0843 0.0552  -0.0859 276 LEU B CG  
4034 C CD1 . LEU B 276 ? 0.6751 0.4931 0.5425 -0.0921 0.0647  -0.0943 276 LEU B CD1 
4035 C CD2 . LEU B 276 ? 0.6440 0.4680 0.5297 -0.0803 0.0564  -0.0827 276 LEU B CD2 
4036 N N   . VAL B 277 ? 0.7616 0.6074 0.6521 -0.0688 0.0397  -0.0708 277 VAL B N   
4037 C CA  . VAL B 277 ? 0.6635 0.5096 0.5627 -0.0640 0.0384  -0.0664 277 VAL B CA  
4038 C C   . VAL B 277 ? 0.7337 0.5707 0.6399 -0.0620 0.0453  -0.0656 277 VAL B C   
4039 O O   . VAL B 277 ? 0.7942 0.6273 0.7020 -0.0602 0.0490  -0.0656 277 VAL B O   
4040 C CB  . VAL B 277 ? 0.6411 0.4938 0.5438 -0.0591 0.0333  -0.0621 277 VAL B CB  
4041 C CG1 . VAL B 277 ? 0.6750 0.5290 0.5854 -0.0560 0.0324  -0.0579 277 VAL B CG1 
4042 C CG2 . VAL B 277 ? 0.6248 0.4855 0.5238 -0.0600 0.0281  -0.0618 277 VAL B CG2 
4043 N N   . ALA B 278 ? 0.6311 0.4652 0.5429 -0.0622 0.0477  -0.0641 278 ALA B N   
4044 C CA  . ALA B 278 ? 0.5930 0.4199 0.5151 -0.0591 0.0545  -0.0606 278 ALA B CA  
4045 C C   . ALA B 278 ? 0.7550 0.5889 0.6860 -0.0555 0.0506  -0.0529 278 ALA B C   
4046 O O   . ALA B 278 ? 0.7847 0.6260 0.7126 -0.0565 0.0445  -0.0523 278 ALA B O   
4047 C CB  . ALA B 278 ? 0.6526 0.4680 0.5749 -0.0632 0.0633  -0.0653 278 ALA B CB  
4048 N N   . GLN B 279 ? 0.7964 0.6290 0.7390 -0.0515 0.0546  -0.0463 279 GLN B N   
4049 C CA  . GLN B 279 ? 0.6831 0.5251 0.6344 -0.0488 0.0506  -0.0373 279 GLN B CA  
4050 C C   . GLN B 279 ? 0.7542 0.5915 0.7193 -0.0466 0.0580  -0.0307 279 GLN B C   
4051 O O   . GLN B 279 ? 0.8816 0.7090 0.8526 -0.0451 0.0668  -0.0313 279 GLN B O   
4052 C CB  . GLN B 279 ? 0.6761 0.5265 0.6294 -0.0462 0.0461  -0.0329 279 GLN B CB  
4053 C CG  . GLN B 279 ? 0.9157 0.7782 0.8764 -0.0452 0.0416  -0.0235 279 GLN B CG  
4054 C CD  . GLN B 279 ? 1.0018 0.8738 0.9621 -0.0449 0.0364  -0.0204 279 GLN B CD  
4055 O OE1 . GLN B 279 ? 1.0704 0.9395 1.0303 -0.0436 0.0379  -0.0221 279 GLN B OE1 
4056 N NE2 . GLN B 279 ? 0.8764 0.7600 0.8358 -0.0471 0.0304  -0.0166 279 GLN B NE2 
4057 N N   . ARG B 280 ? 0.6971 0.5412 0.6681 -0.0464 0.0555  -0.0241 280 ARG B N   
4058 C CA  . ARG B 280 ? 0.7733 0.6155 0.7604 -0.0436 0.0622  -0.0148 280 ARG B CA  
4059 C C   . ARG B 280 ? 0.8521 0.7071 0.8504 -0.0400 0.0592  -0.0025 280 ARG B C   
4060 O O   . ARG B 280 ? 0.7769 0.6460 0.7721 -0.0415 0.0505  0.0015  280 ARG B O   
4061 C CB  . ARG B 280 ? 0.6867 0.5303 0.6756 -0.0456 0.0615  -0.0128 280 ARG B CB  
4062 C CG  . ARG B 280 ? 0.6961 0.5408 0.7039 -0.0421 0.0675  -0.0002 280 ARG B CG  
4063 C CD  . ARG B 280 ? 0.6630 0.5085 0.6742 -0.0439 0.0678  0.0028  280 ARG B CD  
4064 N NE  . ARG B 280 ? 0.7512 0.5985 0.7830 -0.0398 0.0742  0.0168  280 ARG B NE  
4065 C CZ  . ARG B 280 ? 0.7574 0.6041 0.7981 -0.0401 0.0774  0.0227  280 ARG B CZ  
4066 N NH1 . ARG B 280 ? 0.7032 0.5522 0.7650 -0.0357 0.0838  0.0372  280 ARG B NH1 
4067 N NH2 . ARG B 280 ? 0.7190 0.5636 0.7487 -0.0448 0.0742  0.0151  280 ARG B NH2 
4068 N N   . PRO B 281 ? 0.8999 0.7516 0.9116 -0.0358 0.0663  0.0040  281 PRO B N   
4069 C CA  . PRO B 281 ? 0.8502 0.7165 0.8725 -0.0331 0.0627  0.0164  281 PRO B CA  
4070 C C   . PRO B 281 ? 0.7674 0.6500 0.7971 -0.0340 0.0570  0.0283  281 PRO B C   
4071 O O   . PRO B 281 ? 0.7819 0.6621 0.8162 -0.0343 0.0596  0.0309  281 PRO B O   
4072 C CB  . PRO B 281 ? 0.8085 0.6666 0.8478 -0.0279 0.0742  0.0226  281 PRO B CB  
4073 C CG  . PRO B 281 ? 0.8601 0.6976 0.8908 -0.0292 0.0829  0.0086  281 PRO B CG  
4074 C CD  . PRO B 281 ? 0.8658 0.7004 0.8843 -0.0339 0.0791  0.0007  281 PRO B CD  
4075 N N   . GLY B 282 ? 0.6351 0.5349 0.6657 -0.0353 0.0493  0.0357  282 GLY B N   
4076 C CA  . GLY B 282 ? 0.6784 0.5973 0.7111 -0.0385 0.0417  0.0457  282 GLY B CA  
4077 C C   . GLY B 282 ? 0.8772 0.8032 0.8912 -0.0443 0.0323  0.0368  282 GLY B C   
4078 O O   . GLY B 282 ? 0.8990 0.8167 0.9018 -0.0447 0.0315  0.0257  282 GLY B O   
4079 N N   . LYS B 283 ? 0.8829 0.8237 0.8940 -0.0488 0.0260  0.0418  283 LYS B N   
4080 C CA  . LYS B 283 ? 0.8938 0.8401 0.8878 -0.0546 0.0188  0.0329  283 LYS B CA  
4081 C C   . LYS B 283 ? 0.8917 0.8450 0.8792 -0.0588 0.0153  0.0325  283 LYS B C   
4082 O O   . LYS B 283 ? 0.9168 0.8787 0.9144 -0.0586 0.0158  0.0436  283 LYS B O   
4083 C CB  . LYS B 283 ? 1.0929 1.0552 1.0864 -0.0589 0.0133  0.0385  283 LYS B CB  
4084 C CG  . LYS B 283 ? 1.2457 1.2031 1.2238 -0.0622 0.0103  0.0254  283 LYS B CG  
4085 C CD  . LYS B 283 ? 1.2319 1.1694 1.2025 -0.0583 0.0144  0.0123  283 LYS B CD  
4086 C CE  . LYS B 283 ? 1.1276 1.0631 1.0829 -0.0623 0.0114  0.0012  283 LYS B CE  
4087 N NZ  . LYS B 283 ? 0.9666 0.8883 0.9178 -0.0592 0.0146  -0.0069 283 LYS B NZ  
4088 N N   . HIS B 284 ? 1.0512 1.0027 1.0228 -0.0627 0.0119  0.0210  284 HIS B N   
4089 C CA  . HIS B 284 ? 1.0221 0.9779 0.9861 -0.0664 0.0097  0.0183  284 HIS B CA  
4090 C C   . HIS B 284 ? 1.0421 1.0146 0.9976 -0.0741 0.0041  0.0198  284 HIS B C   
4091 O O   . HIS B 284 ? 1.1089 1.0897 1.0611 -0.0781 0.0011  0.0204  284 HIS B O   
4092 C CB  . HIS B 284 ? 1.0337 0.9757 0.9857 -0.0656 0.0107  0.0037  284 HIS B CB  
4093 C CG  . HIS B 284 ? 1.0504 0.9818 1.0021 -0.0630 0.0139  -0.0007 284 HIS B CG  
4094 N ND1 . HIS B 284 ? 0.9508 0.8716 0.8936 -0.0623 0.0148  -0.0119 284 HIS B ND1 
4095 C CD2 . HIS B 284 ? 1.0885 1.0189 1.0481 -0.0616 0.0165  0.0050  284 HIS B CD2 
4096 C CE1 . HIS B 284 ? 1.0705 0.9851 1.0148 -0.0612 0.0172  -0.0131 284 HIS B CE1 
4097 N NE2 . HIS B 284 ? 1.1066 1.0259 1.0607 -0.0608 0.0186  -0.0036 284 HIS B NE2 
4098 N N   . HIS B 285 ? 1.1394 1.1166 1.0902 -0.0770 0.0031  0.0194  285 HIS B N   
4099 C CA  . HIS B 285 ? 1.2264 1.2188 1.1668 -0.0854 -0.0010 0.0190  285 HIS B CA  
4100 C C   . HIS B 285 ? 1.2560 1.2438 1.1818 -0.0895 -0.0015 0.0055  285 HIS B C   
4101 O O   . HIS B 285 ? 1.2892 1.2736 1.2046 -0.0920 -0.0004 -0.0037 285 HIS B O   
4102 C CB  . HIS B 285 ? 1.3504 1.3452 1.2886 -0.0865 -0.0005 0.0194  285 HIS B CB  
4103 C CG  . HIS B 285 ? 1.5596 1.5552 1.5128 -0.0819 0.0014  0.0313  285 HIS B CG  
4104 N ND1 . HIS B 285 ? 1.6029 1.6160 1.5665 -0.0841 -0.0008 0.0473  285 HIS B ND1 
4105 C CD2 . HIS B 285 ? 1.6138 1.5948 1.5742 -0.0756 0.0060  0.0300  285 HIS B CD2 
4106 C CE1 . HIS B 285 ? 1.6105 1.6185 1.5882 -0.0785 0.0031  0.0554  285 HIS B CE1 
4107 N NE2 . HIS B 285 ? 1.6210 1.6089 1.5962 -0.0737 0.0074  0.0443  285 HIS B NE2 
# 
