data_8RLO
# 
_entry.id   8RLO 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.400 
_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   8RLO         pdb_00008rlo 10.2210/pdb8rlo/pdb 
WWPDB D_1292135715 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-01-15 
# 
_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                        8RLO 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              andrea.angeli@unifi.it 
_pdbx_contact_author.name_first         Andrea 
_pdbx_contact_author.name_last          Angeli 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-1470-7192 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Angeli, A.'    1 0000-0002-1470-7192 
'Ferraroni, M.' 2 0000-0001-7258-738X 
# 
_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                     'Human Carbonic Anhydrase I in complex with veralipride' 
_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 'Angeli, A.'    1 0000-0002-1470-7192 
primary 'Ferraroni, M.' 2 0000-0001-7258-738X 
# 
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 'Carbonic anhydrase 1' 28906.186 2   4.2.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'             65.409    2   ?       ? ? ? 
3 non-polymer syn 'Veralipride, (S)-'    383.463   2   ?       ? ? ? 
4 water       nat water                  18.015    296 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Carbonate dehydratase I,Carbonic anhydrase B,CAB,Carbonic anhydrase I,CA-I' 
# 
_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       
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_entity_poly.pdbx_strand_id                 AAA,BBB 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'          ZN    
3 'Veralipride, (S)-' A1H1P 
4 water               HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   PRO n 
1 5   ASP n 
1 6   TRP n 
1 7   GLY n 
1 8   TYR n 
1 9   ASP n 
1 10  ASP n 
1 11  LYS n 
1 12  ASN n 
1 13  GLY n 
1 14  PRO n 
1 15  GLU n 
1 16  GLN n 
1 17  TRP n 
1 18  SER n 
1 19  LYS n 
1 20  LEU n 
1 21  TYR n 
1 22  PRO n 
1 23  ILE n 
1 24  ALA n 
1 25  ASN n 
1 26  GLY n 
1 27  ASN n 
1 28  ASN n 
1 29  GLN n 
1 30  SER n 
1 31  PRO n 
1 32  VAL n 
1 33  ASP n 
1 34  ILE n 
1 35  LYS n 
1 36  THR n 
1 37  SER n 
1 38  GLU n 
1 39  THR n 
1 40  LYS n 
1 41  HIS n 
1 42  ASP n 
1 43  THR n 
1 44  SER n 
1 45  LEU n 
1 46  LYS n 
1 47  PRO n 
1 48  ILE n 
1 49  SER n 
1 50  VAL n 
1 51  SER n 
1 52  TYR n 
1 53  ASN n 
1 54  PRO n 
1 55  ALA n 
1 56  THR n 
1 57  ALA n 
1 58  LYS n 
1 59  GLU n 
1 60  ILE n 
1 61  ILE n 
1 62  ASN n 
1 63  VAL n 
1 64  GLY n 
1 65  HIS n 
1 66  SER n 
1 67  PHE n 
1 68  HIS n 
1 69  VAL n 
1 70  ASN n 
1 71  PHE n 
1 72  GLU n 
1 73  ASP n 
1 74  ASN n 
1 75  ASP n 
1 76  ASN n 
1 77  ARG n 
1 78  SER n 
1 79  VAL n 
1 80  LEU n 
1 81  LYS n 
1 82  GLY n 
1 83  GLY n 
1 84  PRO n 
1 85  PHE n 
1 86  SER n 
1 87  ASP n 
1 88  SER n 
1 89  TYR n 
1 90  ARG n 
1 91  LEU n 
1 92  PHE n 
1 93  GLN n 
1 94  PHE n 
1 95  HIS n 
1 96  PHE n 
1 97  HIS n 
1 98  TRP n 
1 99  GLY n 
1 100 SER n 
1 101 THR n 
1 102 ASN n 
1 103 GLU n 
1 104 HIS n 
1 105 GLY n 
1 106 SER n 
1 107 GLU n 
1 108 HIS n 
1 109 THR n 
1 110 VAL n 
1 111 ASP n 
1 112 GLY n 
1 113 VAL n 
1 114 LYS n 
1 115 TYR n 
1 116 SER n 
1 117 ALA n 
1 118 GLU n 
1 119 LEU n 
1 120 HIS n 
1 121 VAL n 
1 122 ALA n 
1 123 HIS n 
1 124 TRP n 
1 125 ASN n 
1 126 SER n 
1 127 ALA n 
1 128 LYS n 
1 129 TYR n 
1 130 SER n 
1 131 SER n 
1 132 LEU n 
1 133 ALA n 
1 134 GLU n 
1 135 ALA n 
1 136 ALA n 
1 137 SER n 
1 138 LYS n 
1 139 ALA n 
1 140 ASP n 
1 141 GLY n 
1 142 LEU n 
1 143 ALA n 
1 144 VAL n 
1 145 ILE n 
1 146 GLY n 
1 147 VAL n 
1 148 LEU n 
1 149 MET n 
1 150 LYS n 
1 151 VAL n 
1 152 GLY n 
1 153 GLU n 
1 154 ALA n 
1 155 ASN n 
1 156 PRO n 
1 157 LYS n 
1 158 LEU n 
1 159 GLN n 
1 160 LYS n 
1 161 VAL n 
1 162 LEU n 
1 163 ASP n 
1 164 ALA n 
1 165 LEU n 
1 166 GLN n 
1 167 ALA n 
1 168 ILE n 
1 169 LYS n 
1 170 THR n 
1 171 LYS n 
1 172 GLY n 
1 173 LYS n 
1 174 ARG n 
1 175 ALA n 
1 176 PRO n 
1 177 PHE n 
1 178 THR n 
1 179 ASN n 
1 180 PHE n 
1 181 ASP n 
1 182 PRO n 
1 183 SER n 
1 184 THR n 
1 185 LEU n 
1 186 LEU n 
1 187 PRO n 
1 188 SER n 
1 189 SER n 
1 190 LEU n 
1 191 ASP n 
1 192 PHE n 
1 193 TRP n 
1 194 THR n 
1 195 TYR n 
1 196 PRO n 
1 197 GLY n 
1 198 SER n 
1 199 LEU n 
1 200 THR n 
1 201 HIS n 
1 202 PRO n 
1 203 PRO n 
1 204 LEU n 
1 205 TYR n 
1 206 GLU n 
1 207 SER n 
1 208 VAL n 
1 209 THR n 
1 210 TRP n 
1 211 ILE n 
1 212 ILE n 
1 213 CYS n 
1 214 LYS n 
1 215 GLU n 
1 216 SER n 
1 217 ILE n 
1 218 SER n 
1 219 VAL n 
1 220 SER n 
1 221 SER n 
1 222 GLU n 
1 223 GLN n 
1 224 LEU n 
1 225 ALA n 
1 226 GLN n 
1 227 PHE n 
1 228 ARG n 
1 229 SER n 
1 230 LEU n 
1 231 LEU n 
1 232 SER n 
1 233 ASN n 
1 234 VAL n 
1 235 GLU n 
1 236 GLY n 
1 237 ASP n 
1 238 ASN n 
1 239 ALA n 
1 240 VAL n 
1 241 PRO n 
1 242 MET n 
1 243 GLN n 
1 244 HIS n 
1 245 ASN n 
1 246 ASN n 
1 247 ARG n 
1 248 PRO n 
1 249 THR n 
1 250 GLN n 
1 251 PRO n 
1 252 LEU n 
1 253 LYS n 
1 254 GLY n 
1 255 ARG n 
1 256 THR n 
1 257 VAL n 
1 258 ARG n 
1 259 ALA n 
1 260 SER n 
1 261 PHE 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                   261 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 CA1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1H1P non-polymer         . 'Veralipride, (S)-' 
'2,3-dimethoxy-N-[[(2S)-1-prop-2-enylpyrrolidin-2-yl]methyl]-5-sulfamoyl-benzamide; Veralipride' 'C17 H25 N3 O5 S' 383.463 
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 
ZN    non-polymer         . 'ZINC ION'          ? 'Zn 2'            65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   ?   ?   ?   AAA . n 
A 1 2   ALA 2   1   ?   ?   ?   AAA . n 
A 1 3   SER 3   2   ?   ?   ?   AAA . n 
A 1 4   PRO 4   3   ?   ?   ?   AAA . n 
A 1 5   ASP 5   4   ?   ?   ?   AAA . n 
A 1 6   TRP 6   5   5   TRP TRP AAA . n 
A 1 7   GLY 7   6   6   GLY GLY AAA . n 
A 1 8   TYR 8   7   7   TYR TYR AAA . n 
A 1 9   ASP 9   8   8   ASP ASP AAA . n 
A 1 10  ASP 10  9   9   ASP ASP AAA . n 
A 1 11  LYS 11  10  10  LYS LYS AAA . n 
A 1 12  ASN 12  11  11  ASN ASN AAA . n 
A 1 13  GLY 13  12  12  GLY GLY AAA . n 
A 1 14  PRO 14  13  13  PRO PRO AAA . n 
A 1 15  GLU 15  14  14  GLU GLU AAA . n 
A 1 16  GLN 16  15  15  GLN GLN AAA . n 
A 1 17  TRP 17  16  16  TRP TRP AAA . n 
A 1 18  SER 18  17  17  SER SER AAA . n 
A 1 19  LYS 19  18  18  LYS LYS AAA . n 
A 1 20  LEU 20  19  19  LEU LEU AAA . n 
A 1 21  TYR 21  20  20  TYR TYR AAA . n 
A 1 22  PRO 22  21  21  PRO PRO AAA . n 
A 1 23  ILE 23  22  22  ILE ILE AAA . n 
A 1 24  ALA 24  23  23  ALA ALA AAA . n 
A 1 25  ASN 25  24  24  ASN ASN AAA . n 
A 1 26  GLY 26  25  25  GLY GLY AAA . n 
A 1 27  ASN 27  26  26  ASN ASN AAA . n 
A 1 28  ASN 28  27  27  ASN ASN AAA . n 
A 1 29  GLN 29  28  28  GLN GLN AAA . n 
A 1 30  SER 30  29  29  SER SER AAA . n 
A 1 31  PRO 31  30  30  PRO PRO AAA . n 
A 1 32  VAL 32  31  31  VAL VAL AAA . n 
A 1 33  ASP 33  32  32  ASP ASP AAA . n 
A 1 34  ILE 34  33  33  ILE ILE AAA . n 
A 1 35  LYS 35  34  34  LYS LYS AAA . n 
A 1 36  THR 36  35  35  THR THR AAA . n 
A 1 37  SER 37  36  36  SER SER AAA . n 
A 1 38  GLU 38  37  37  GLU GLU AAA . n 
A 1 39  THR 39  38  38  THR THR AAA . n 
A 1 40  LYS 40  39  39  LYS LYS AAA . n 
A 1 41  HIS 41  40  40  HIS HIS AAA . n 
A 1 42  ASP 42  41  41  ASP ASP AAA . n 
A 1 43  THR 43  42  42  THR THR AAA . n 
A 1 44  SER 44  43  43  SER SER AAA . n 
A 1 45  LEU 45  44  44  LEU LEU AAA . n 
A 1 46  LYS 46  45  45  LYS LYS AAA . n 
A 1 47  PRO 47  46  46  PRO PRO AAA . n 
A 1 48  ILE 48  47  47  ILE ILE AAA . n 
A 1 49  SER 49  48  48  SER SER AAA . n 
A 1 50  VAL 50  49  49  VAL VAL AAA . n 
A 1 51  SER 51  50  50  SER SER AAA . n 
A 1 52  TYR 52  51  51  TYR TYR AAA . n 
A 1 53  ASN 53  52  52  ASN ASN AAA . n 
A 1 54  PRO 54  53  53  PRO PRO AAA . n 
A 1 55  ALA 55  54  54  ALA ALA AAA . n 
A 1 56  THR 56  55  55  THR THR AAA . n 
A 1 57  ALA 57  56  56  ALA ALA AAA . n 
A 1 58  LYS 58  57  57  LYS LYS AAA . n 
A 1 59  GLU 59  58  58  GLU GLU AAA . n 
A 1 60  ILE 60  59  59  ILE ILE AAA . n 
A 1 61  ILE 61  60  60  ILE ILE AAA . n 
A 1 62  ASN 62  61  61  ASN ASN AAA . n 
A 1 63  VAL 63  62  62  VAL VAL AAA . n 
A 1 64  GLY 64  63  63  GLY GLY AAA . n 
A 1 65  HIS 65  64  64  HIS HIS AAA . n 
A 1 66  SER 66  65  65  SER SER AAA . n 
A 1 67  PHE 67  66  66  PHE PHE AAA . n 
A 1 68  HIS 68  67  67  HIS HIS AAA . n 
A 1 69  VAL 69  68  68  VAL VAL AAA . n 
A 1 70  ASN 70  69  69  ASN ASN AAA . n 
A 1 71  PHE 71  70  70  PHE PHE AAA . n 
A 1 72  GLU 72  71  71  GLU GLU AAA . n 
A 1 73  ASP 73  72  72  ASP ASP AAA . n 
A 1 74  ASN 74  73  73  ASN ASN AAA . n 
A 1 75  ASP 75  74  74  ASP ASP AAA . n 
A 1 76  ASN 76  75  75  ASN ASN AAA . n 
A 1 77  ARG 77  76  76  ARG ARG AAA . n 
A 1 78  SER 78  77  77  SER SER AAA . n 
A 1 79  VAL 79  78  78  VAL VAL AAA . n 
A 1 80  LEU 80  79  79  LEU LEU AAA . n 
A 1 81  LYS 81  80  80  LYS LYS AAA . n 
A 1 82  GLY 82  81  81  GLY GLY AAA . n 
A 1 83  GLY 83  82  82  GLY GLY AAA . n 
A 1 84  PRO 84  83  83  PRO PRO AAA . n 
A 1 85  PHE 85  84  84  PHE PHE AAA . n 
A 1 86  SER 86  85  85  SER SER AAA . n 
A 1 87  ASP 87  86  86  ASP ASP AAA . n 
A 1 88  SER 88  87  87  SER SER AAA . n 
A 1 89  TYR 89  88  88  TYR TYR AAA . n 
A 1 90  ARG 90  89  89  ARG ARG AAA . n 
A 1 91  LEU 91  90  90  LEU LEU AAA . n 
A 1 92  PHE 92  91  91  PHE PHE AAA . n 
A 1 93  GLN 93  92  92  GLN GLN AAA . n 
A 1 94  PHE 94  93  93  PHE PHE AAA . n 
A 1 95  HIS 95  94  94  HIS HIS AAA . n 
A 1 96  PHE 96  95  95  PHE PHE AAA . n 
A 1 97  HIS 97  96  96  HIS HIS AAA . n 
A 1 98  TRP 98  97  97  TRP TRP AAA . n 
A 1 99  GLY 99  98  98  GLY GLY AAA . n 
A 1 100 SER 100 99  99  SER SER AAA . n 
A 1 101 THR 101 100 100 THR THR AAA . n 
A 1 102 ASN 102 101 101 ASN ASN AAA . n 
A 1 103 GLU 103 102 102 GLU GLU AAA . n 
A 1 104 HIS 104 103 103 HIS HIS AAA . n 
A 1 105 GLY 105 104 104 GLY GLY AAA . n 
A 1 106 SER 106 105 105 SER SER AAA . n 
A 1 107 GLU 107 106 106 GLU GLU AAA . n 
A 1 108 HIS 108 107 107 HIS HIS AAA . n 
A 1 109 THR 109 108 108 THR THR AAA . n 
A 1 110 VAL 110 109 109 VAL VAL AAA . n 
A 1 111 ASP 111 110 110 ASP ASP AAA . n 
A 1 112 GLY 112 111 111 GLY GLY AAA . n 
A 1 113 VAL 113 112 112 VAL VAL AAA . n 
A 1 114 LYS 114 113 113 LYS LYS AAA . n 
A 1 115 TYR 115 114 114 TYR TYR AAA . n 
A 1 116 SER 116 115 115 SER SER AAA . n 
A 1 117 ALA 117 116 116 ALA ALA AAA . n 
A 1 118 GLU 118 117 117 GLU GLU AAA . n 
A 1 119 LEU 119 118 118 LEU LEU AAA . n 
A 1 120 HIS 120 119 119 HIS HIS AAA . n 
A 1 121 VAL 121 120 120 VAL VAL AAA . n 
A 1 122 ALA 122 121 121 ALA ALA AAA . n 
A 1 123 HIS 123 122 122 HIS HIS AAA . n 
A 1 124 TRP 124 123 123 TRP TRP AAA . n 
A 1 125 ASN 125 124 124 ASN ASN AAA . n 
A 1 126 SER 126 125 125 SER SER AAA . n 
A 1 127 ALA 127 126 126 ALA ALA AAA . n 
A 1 128 LYS 128 127 127 LYS LYS AAA . n 
A 1 129 TYR 129 128 128 TYR TYR AAA . n 
A 1 130 SER 130 129 129 SER SER AAA . n 
A 1 131 SER 131 130 130 SER SER AAA . n 
A 1 132 LEU 132 131 131 LEU LEU AAA . n 
A 1 133 ALA 133 132 132 ALA ALA AAA . n 
A 1 134 GLU 134 133 133 GLU GLU AAA . n 
A 1 135 ALA 135 134 134 ALA ALA AAA . n 
A 1 136 ALA 136 135 135 ALA ALA AAA . n 
A 1 137 SER 137 136 136 SER SER AAA . n 
A 1 138 LYS 138 137 137 LYS LYS AAA . n 
A 1 139 ALA 139 138 138 ALA ALA AAA . n 
A 1 140 ASP 140 139 139 ASP ASP AAA . n 
A 1 141 GLY 141 140 140 GLY GLY AAA . n 
A 1 142 LEU 142 141 141 LEU LEU AAA . n 
A 1 143 ALA 143 142 142 ALA ALA AAA . n 
A 1 144 VAL 144 143 143 VAL VAL AAA . n 
A 1 145 ILE 145 144 144 ILE ILE AAA . n 
A 1 146 GLY 146 145 145 GLY GLY AAA . n 
A 1 147 VAL 147 146 146 VAL VAL AAA . n 
A 1 148 LEU 148 147 147 LEU LEU AAA . n 
A 1 149 MET 149 148 148 MET MET AAA . n 
A 1 150 LYS 150 149 149 LYS LYS AAA . n 
A 1 151 VAL 151 150 150 VAL VAL AAA . n 
A 1 152 GLY 152 151 151 GLY GLY AAA . n 
A 1 153 GLU 153 152 152 GLU GLU AAA . n 
A 1 154 ALA 154 153 153 ALA ALA AAA . n 
A 1 155 ASN 155 154 154 ASN ASN AAA . n 
A 1 156 PRO 156 155 155 PRO PRO AAA . n 
A 1 157 LYS 157 156 156 LYS LYS AAA . n 
A 1 158 LEU 158 157 157 LEU LEU AAA . n 
A 1 159 GLN 159 158 158 GLN GLN AAA . n 
A 1 160 LYS 160 159 159 LYS LYS AAA . n 
A 1 161 VAL 161 160 160 VAL VAL AAA . n 
A 1 162 LEU 162 161 161 LEU LEU AAA . n 
A 1 163 ASP 163 162 162 ASP ASP AAA . n 
A 1 164 ALA 164 163 163 ALA ALA AAA . n 
A 1 165 LEU 165 164 164 LEU LEU AAA . n 
A 1 166 GLN 166 165 165 GLN GLN AAA . n 
A 1 167 ALA 167 166 166 ALA ALA AAA . n 
A 1 168 ILE 168 167 167 ILE ILE AAA . n 
A 1 169 LYS 169 168 168 LYS LYS AAA . n 
A 1 170 THR 170 169 169 THR THR AAA . n 
A 1 171 LYS 171 170 170 LYS LYS AAA . n 
A 1 172 GLY 172 171 171 GLY GLY AAA . n 
A 1 173 LYS 173 172 172 LYS LYS AAA . n 
A 1 174 ARG 174 173 173 ARG ARG AAA . n 
A 1 175 ALA 175 174 174 ALA ALA AAA . n 
A 1 176 PRO 176 175 175 PRO PRO AAA . n 
A 1 177 PHE 177 176 176 PHE PHE AAA . n 
A 1 178 THR 178 177 177 THR THR AAA . n 
A 1 179 ASN 179 178 178 ASN ASN AAA . n 
A 1 180 PHE 180 179 179 PHE PHE AAA . n 
A 1 181 ASP 181 180 180 ASP ASP AAA . n 
A 1 182 PRO 182 181 181 PRO PRO AAA . n 
A 1 183 SER 183 182 182 SER SER AAA . n 
A 1 184 THR 184 183 183 THR THR AAA . n 
A 1 185 LEU 185 184 184 LEU LEU AAA . n 
A 1 186 LEU 186 185 185 LEU LEU AAA . n 
A 1 187 PRO 187 186 186 PRO PRO AAA . n 
A 1 188 SER 188 187 187 SER SER AAA . n 
A 1 189 SER 189 188 188 SER SER AAA . n 
A 1 190 LEU 190 189 189 LEU LEU AAA . n 
A 1 191 ASP 191 190 190 ASP ASP AAA . n 
A 1 192 PHE 192 191 191 PHE PHE AAA . n 
A 1 193 TRP 193 192 192 TRP TRP AAA . n 
A 1 194 THR 194 193 193 THR THR AAA . n 
A 1 195 TYR 195 194 194 TYR TYR AAA . n 
A 1 196 PRO 196 195 195 PRO PRO AAA . n 
A 1 197 GLY 197 196 196 GLY GLY AAA . n 
A 1 198 SER 198 197 197 SER SER AAA . n 
A 1 199 LEU 199 198 198 LEU LEU AAA . n 
A 1 200 THR 200 199 199 THR THR AAA . n 
A 1 201 HIS 201 200 200 HIS HIS AAA . n 
A 1 202 PRO 202 201 201 PRO PRO AAA . n 
A 1 203 PRO 203 202 202 PRO PRO AAA . n 
A 1 204 LEU 204 203 203 LEU LEU AAA . n 
A 1 205 TYR 205 204 204 TYR TYR AAA . n 
A 1 206 GLU 206 205 205 GLU GLU AAA . n 
A 1 207 SER 207 206 206 SER SER AAA . n 
A 1 208 VAL 208 207 207 VAL VAL AAA . n 
A 1 209 THR 209 208 208 THR THR AAA . n 
A 1 210 TRP 210 209 209 TRP TRP AAA . n 
A 1 211 ILE 211 210 210 ILE ILE AAA . n 
A 1 212 ILE 212 211 211 ILE ILE AAA . n 
A 1 213 CYS 213 212 212 CYS CYS AAA . n 
A 1 214 LYS 214 213 213 LYS LYS AAA . n 
A 1 215 GLU 215 214 214 GLU GLU AAA . n 
A 1 216 SER 216 215 215 SER SER AAA . n 
A 1 217 ILE 217 216 216 ILE ILE AAA . n 
A 1 218 SER 218 217 217 SER SER AAA . n 
A 1 219 VAL 219 218 218 VAL VAL AAA . n 
A 1 220 SER 220 219 219 SER SER AAA . n 
A 1 221 SER 221 220 220 SER SER AAA . n 
A 1 222 GLU 222 221 221 GLU GLU AAA . n 
A 1 223 GLN 223 222 222 GLN GLN AAA . n 
A 1 224 LEU 224 223 223 LEU LEU AAA . n 
A 1 225 ALA 225 224 224 ALA ALA AAA . n 
A 1 226 GLN 226 225 225 GLN GLN AAA . n 
A 1 227 PHE 227 226 226 PHE PHE AAA . n 
A 1 228 ARG 228 227 227 ARG ARG AAA . n 
A 1 229 SER 229 228 228 SER SER AAA . n 
A 1 230 LEU 230 229 229 LEU LEU AAA . n 
A 1 231 LEU 231 230 230 LEU LEU AAA . n 
A 1 232 SER 232 231 231 SER SER AAA . n 
A 1 233 ASN 233 232 232 ASN ASN AAA . n 
A 1 234 VAL 234 233 233 VAL VAL AAA . n 
A 1 235 GLU 235 234 234 GLU GLU AAA . n 
A 1 236 GLY 236 235 235 GLY GLY AAA . n 
A 1 237 ASP 237 236 236 ASP ASP AAA . n 
A 1 238 ASN 238 237 237 ASN ASN AAA . n 
A 1 239 ALA 239 238 238 ALA ALA AAA . n 
A 1 240 VAL 240 239 239 VAL VAL AAA . n 
A 1 241 PRO 241 240 240 PRO PRO AAA . n 
A 1 242 MET 242 241 241 MET MET AAA . n 
A 1 243 GLN 243 242 242 GLN GLN AAA . n 
A 1 244 HIS 244 243 243 HIS HIS AAA . n 
A 1 245 ASN 245 244 244 ASN ASN AAA . n 
A 1 246 ASN 246 245 245 ASN ASN AAA . n 
A 1 247 ARG 247 246 246 ARG ARG AAA . n 
A 1 248 PRO 248 247 247 PRO PRO AAA . n 
A 1 249 THR 249 248 248 THR THR AAA . n 
A 1 250 GLN 250 249 249 GLN GLN AAA . n 
A 1 251 PRO 251 250 250 PRO PRO AAA . n 
A 1 252 LEU 252 251 251 LEU LEU AAA . n 
A 1 253 LYS 253 252 252 LYS LYS AAA . n 
A 1 254 GLY 254 253 253 GLY GLY AAA . n 
A 1 255 ARG 255 254 254 ARG ARG AAA . n 
A 1 256 THR 256 255 255 THR THR AAA . n 
A 1 257 VAL 257 256 256 VAL VAL AAA . n 
A 1 258 ARG 258 257 257 ARG ARG AAA . n 
A 1 259 ALA 259 258 258 ALA ALA AAA . n 
A 1 260 SER 260 259 259 SER SER AAA . n 
A 1 261 PHE 261 260 260 PHE PHE AAA . n 
B 1 1   MET 1   0   ?   ?   ?   BBB . n 
B 1 2   ALA 2   1   ?   ?   ?   BBB . n 
B 1 3   SER 3   2   ?   ?   ?   BBB . n 
B 1 4   PRO 4   3   ?   ?   ?   BBB . n 
B 1 5   ASP 5   4   4   ASP ASP BBB . n 
B 1 6   TRP 6   5   5   TRP TRP BBB . n 
B 1 7   GLY 7   6   6   GLY GLY BBB . n 
B 1 8   TYR 8   7   7   TYR TYR BBB . n 
B 1 9   ASP 9   8   8   ASP ASP BBB . n 
B 1 10  ASP 10  9   9   ASP ASP BBB . n 
B 1 11  LYS 11  10  10  LYS LYS BBB . n 
B 1 12  ASN 12  11  11  ASN ASN BBB . n 
B 1 13  GLY 13  12  12  GLY GLY BBB . n 
B 1 14  PRO 14  13  13  PRO PRO BBB . n 
B 1 15  GLU 15  14  14  GLU GLU BBB . n 
B 1 16  GLN 16  15  15  GLN GLN BBB . n 
B 1 17  TRP 17  16  16  TRP TRP BBB . n 
B 1 18  SER 18  17  17  SER SER BBB . n 
B 1 19  LYS 19  18  18  LYS LYS BBB . n 
B 1 20  LEU 20  19  19  LEU LEU BBB . n 
B 1 21  TYR 21  20  20  TYR TYR BBB . n 
B 1 22  PRO 22  21  21  PRO PRO BBB . n 
B 1 23  ILE 23  22  22  ILE ILE BBB . n 
B 1 24  ALA 24  23  23  ALA ALA BBB . n 
B 1 25  ASN 25  24  24  ASN ASN BBB . n 
B 1 26  GLY 26  25  25  GLY GLY BBB . n 
B 1 27  ASN 27  26  26  ASN ASN BBB . n 
B 1 28  ASN 28  27  27  ASN ASN BBB . n 
B 1 29  GLN 29  28  28  GLN GLN BBB . n 
B 1 30  SER 30  29  29  SER SER BBB . n 
B 1 31  PRO 31  30  30  PRO PRO BBB . n 
B 1 32  VAL 32  31  31  VAL VAL BBB . n 
B 1 33  ASP 33  32  32  ASP ASP BBB . n 
B 1 34  ILE 34  33  33  ILE ILE BBB . n 
B 1 35  LYS 35  34  34  LYS LYS BBB . n 
B 1 36  THR 36  35  35  THR THR BBB . n 
B 1 37  SER 37  36  36  SER SER BBB . n 
B 1 38  GLU 38  37  37  GLU GLU BBB . n 
B 1 39  THR 39  38  38  THR THR BBB . n 
B 1 40  LYS 40  39  39  LYS LYS BBB . n 
B 1 41  HIS 41  40  40  HIS HIS BBB . n 
B 1 42  ASP 42  41  41  ASP ASP BBB . n 
B 1 43  THR 43  42  42  THR THR BBB . n 
B 1 44  SER 44  43  43  SER SER BBB . n 
B 1 45  LEU 45  44  44  LEU LEU BBB . n 
B 1 46  LYS 46  45  45  LYS LYS BBB . n 
B 1 47  PRO 47  46  46  PRO PRO BBB . n 
B 1 48  ILE 48  47  47  ILE ILE BBB . n 
B 1 49  SER 49  48  48  SER SER BBB . n 
B 1 50  VAL 50  49  49  VAL VAL BBB . n 
B 1 51  SER 51  50  50  SER SER BBB . n 
B 1 52  TYR 52  51  51  TYR TYR BBB . n 
B 1 53  ASN 53  52  52  ASN ASN BBB . n 
B 1 54  PRO 54  53  53  PRO PRO BBB . n 
B 1 55  ALA 55  54  54  ALA ALA BBB . n 
B 1 56  THR 56  55  55  THR THR BBB . n 
B 1 57  ALA 57  56  56  ALA ALA BBB . n 
B 1 58  LYS 58  57  57  LYS LYS BBB . n 
B 1 59  GLU 59  58  58  GLU GLU BBB . n 
B 1 60  ILE 60  59  59  ILE ILE BBB . n 
B 1 61  ILE 61  60  60  ILE ILE BBB . n 
B 1 62  ASN 62  61  61  ASN ASN BBB . n 
B 1 63  VAL 63  62  62  VAL VAL BBB . n 
B 1 64  GLY 64  63  63  GLY GLY BBB . n 
B 1 65  HIS 65  64  64  HIS HIS BBB . n 
B 1 66  SER 66  65  65  SER SER BBB . n 
B 1 67  PHE 67  66  66  PHE PHE BBB . n 
B 1 68  HIS 68  67  67  HIS HIS BBB . n 
B 1 69  VAL 69  68  68  VAL VAL BBB . n 
B 1 70  ASN 70  69  69  ASN ASN BBB . n 
B 1 71  PHE 71  70  70  PHE PHE BBB . n 
B 1 72  GLU 72  71  71  GLU GLU BBB . n 
B 1 73  ASP 73  72  72  ASP ASP BBB . n 
B 1 74  ASN 74  73  73  ASN ASN BBB . n 
B 1 75  ASP 75  74  74  ASP ASP BBB . n 
B 1 76  ASN 76  75  75  ASN ASN BBB . n 
B 1 77  ARG 77  76  76  ARG ARG BBB . n 
B 1 78  SER 78  77  77  SER SER BBB . n 
B 1 79  VAL 79  78  78  VAL VAL BBB . n 
B 1 80  LEU 80  79  79  LEU LEU BBB . n 
B 1 81  LYS 81  80  80  LYS LYS BBB . n 
B 1 82  GLY 82  81  81  GLY GLY BBB . n 
B 1 83  GLY 83  82  82  GLY GLY BBB . n 
B 1 84  PRO 84  83  83  PRO PRO BBB . n 
B 1 85  PHE 85  84  84  PHE PHE BBB . n 
B 1 86  SER 86  85  85  SER SER BBB . n 
B 1 87  ASP 87  86  86  ASP ASP BBB . n 
B 1 88  SER 88  87  87  SER SER BBB . n 
B 1 89  TYR 89  88  88  TYR TYR BBB . n 
B 1 90  ARG 90  89  89  ARG ARG BBB . n 
B 1 91  LEU 91  90  90  LEU LEU BBB . n 
B 1 92  PHE 92  91  91  PHE PHE BBB . n 
B 1 93  GLN 93  92  92  GLN GLN BBB . n 
B 1 94  PHE 94  93  93  PHE PHE BBB . n 
B 1 95  HIS 95  94  94  HIS HIS BBB . n 
B 1 96  PHE 96  95  95  PHE PHE BBB . n 
B 1 97  HIS 97  96  96  HIS HIS BBB . n 
B 1 98  TRP 98  97  97  TRP TRP BBB . n 
B 1 99  GLY 99  98  98  GLY GLY BBB . n 
B 1 100 SER 100 99  99  SER SER BBB . n 
B 1 101 THR 101 100 100 THR THR BBB . n 
B 1 102 ASN 102 101 101 ASN ASN BBB . n 
B 1 103 GLU 103 102 102 GLU GLU BBB . n 
B 1 104 HIS 104 103 103 HIS HIS BBB . n 
B 1 105 GLY 105 104 104 GLY GLY BBB . n 
B 1 106 SER 106 105 105 SER SER BBB . n 
B 1 107 GLU 107 106 106 GLU GLU BBB . n 
B 1 108 HIS 108 107 107 HIS HIS BBB . n 
B 1 109 THR 109 108 108 THR THR BBB . n 
B 1 110 VAL 110 109 109 VAL VAL BBB . n 
B 1 111 ASP 111 110 110 ASP ASP BBB . n 
B 1 112 GLY 112 111 111 GLY GLY BBB . n 
B 1 113 VAL 113 112 112 VAL VAL BBB . n 
B 1 114 LYS 114 113 113 LYS LYS BBB . n 
B 1 115 TYR 115 114 114 TYR TYR BBB . n 
B 1 116 SER 116 115 115 SER SER BBB . n 
B 1 117 ALA 117 116 116 ALA ALA BBB . n 
B 1 118 GLU 118 117 117 GLU GLU BBB . n 
B 1 119 LEU 119 118 118 LEU LEU BBB . n 
B 1 120 HIS 120 119 119 HIS HIS BBB . n 
B 1 121 VAL 121 120 120 VAL VAL BBB . n 
B 1 122 ALA 122 121 121 ALA ALA BBB . n 
B 1 123 HIS 123 122 122 HIS HIS BBB . n 
B 1 124 TRP 124 123 123 TRP TRP BBB . n 
B 1 125 ASN 125 124 124 ASN ASN BBB . n 
B 1 126 SER 126 125 125 SER SER BBB . n 
B 1 127 ALA 127 126 126 ALA ALA BBB . n 
B 1 128 LYS 128 127 127 LYS LYS BBB . n 
B 1 129 TYR 129 128 128 TYR TYR BBB . n 
B 1 130 SER 130 129 129 SER SER BBB . n 
B 1 131 SER 131 130 130 SER SER BBB . n 
B 1 132 LEU 132 131 131 LEU LEU BBB . n 
B 1 133 ALA 133 132 132 ALA ALA BBB . n 
B 1 134 GLU 134 133 133 GLU GLU BBB . n 
B 1 135 ALA 135 134 134 ALA ALA BBB . n 
B 1 136 ALA 136 135 135 ALA ALA BBB . n 
B 1 137 SER 137 136 136 SER SER BBB . n 
B 1 138 LYS 138 137 137 LYS LYS BBB . n 
B 1 139 ALA 139 138 138 ALA ALA BBB . n 
B 1 140 ASP 140 139 139 ASP ASP BBB . n 
B 1 141 GLY 141 140 140 GLY GLY BBB . n 
B 1 142 LEU 142 141 141 LEU LEU BBB . n 
B 1 143 ALA 143 142 142 ALA ALA BBB . n 
B 1 144 VAL 144 143 143 VAL VAL BBB . n 
B 1 145 ILE 145 144 144 ILE ILE BBB . n 
B 1 146 GLY 146 145 145 GLY GLY BBB . n 
B 1 147 VAL 147 146 146 VAL VAL BBB . n 
B 1 148 LEU 148 147 147 LEU LEU BBB . n 
B 1 149 MET 149 148 148 MET MET BBB . n 
B 1 150 LYS 150 149 149 LYS LYS BBB . n 
B 1 151 VAL 151 150 150 VAL VAL BBB . n 
B 1 152 GLY 152 151 151 GLY GLY BBB . n 
B 1 153 GLU 153 152 152 GLU GLU BBB . n 
B 1 154 ALA 154 153 153 ALA ALA BBB . n 
B 1 155 ASN 155 154 154 ASN ASN BBB . n 
B 1 156 PRO 156 155 155 PRO PRO BBB . n 
B 1 157 LYS 157 156 156 LYS LYS BBB . n 
B 1 158 LEU 158 157 157 LEU LEU BBB . n 
B 1 159 GLN 159 158 158 GLN GLN BBB . n 
B 1 160 LYS 160 159 159 LYS LYS BBB . n 
B 1 161 VAL 161 160 160 VAL VAL BBB . n 
B 1 162 LEU 162 161 161 LEU LEU BBB . n 
B 1 163 ASP 163 162 162 ASP ASP BBB . n 
B 1 164 ALA 164 163 163 ALA ALA BBB . n 
B 1 165 LEU 165 164 164 LEU LEU BBB . n 
B 1 166 GLN 166 165 165 GLN GLN BBB . n 
B 1 167 ALA 167 166 166 ALA ALA BBB . n 
B 1 168 ILE 168 167 167 ILE ILE BBB . n 
B 1 169 LYS 169 168 168 LYS LYS BBB . n 
B 1 170 THR 170 169 169 THR THR BBB . n 
B 1 171 LYS 171 170 170 LYS LYS BBB . n 
B 1 172 GLY 172 171 171 GLY GLY BBB . n 
B 1 173 LYS 173 172 172 LYS LYS BBB . n 
B 1 174 ARG 174 173 173 ARG ARG BBB . n 
B 1 175 ALA 175 174 174 ALA ALA BBB . n 
B 1 176 PRO 176 175 175 PRO PRO BBB . n 
B 1 177 PHE 177 176 176 PHE PHE BBB . n 
B 1 178 THR 178 177 177 THR THR BBB . n 
B 1 179 ASN 179 178 178 ASN ASN BBB . n 
B 1 180 PHE 180 179 179 PHE PHE BBB . n 
B 1 181 ASP 181 180 180 ASP ASP BBB . n 
B 1 182 PRO 182 181 181 PRO PRO BBB . n 
B 1 183 SER 183 182 182 SER SER BBB . n 
B 1 184 THR 184 183 183 THR THR BBB . n 
B 1 185 LEU 185 184 184 LEU LEU BBB . n 
B 1 186 LEU 186 185 185 LEU LEU BBB . n 
B 1 187 PRO 187 186 186 PRO PRO BBB . n 
B 1 188 SER 188 187 187 SER SER BBB . n 
B 1 189 SER 189 188 188 SER SER BBB . n 
B 1 190 LEU 190 189 189 LEU LEU BBB . n 
B 1 191 ASP 191 190 190 ASP ASP BBB . n 
B 1 192 PHE 192 191 191 PHE PHE BBB . n 
B 1 193 TRP 193 192 192 TRP TRP BBB . n 
B 1 194 THR 194 193 193 THR THR BBB . n 
B 1 195 TYR 195 194 194 TYR TYR BBB . n 
B 1 196 PRO 196 195 195 PRO PRO BBB . n 
B 1 197 GLY 197 196 196 GLY GLY BBB . n 
B 1 198 SER 198 197 197 SER SER BBB . n 
B 1 199 LEU 199 198 198 LEU LEU BBB . n 
B 1 200 THR 200 199 199 THR THR BBB . n 
B 1 201 HIS 201 200 200 HIS HIS BBB . n 
B 1 202 PRO 202 201 201 PRO PRO BBB . n 
B 1 203 PRO 203 202 202 PRO PRO BBB . n 
B 1 204 LEU 204 203 203 LEU LEU BBB . n 
B 1 205 TYR 205 204 204 TYR TYR BBB . n 
B 1 206 GLU 206 205 205 GLU GLU BBB . n 
B 1 207 SER 207 206 206 SER SER BBB . n 
B 1 208 VAL 208 207 207 VAL VAL BBB . n 
B 1 209 THR 209 208 208 THR THR BBB . n 
B 1 210 TRP 210 209 209 TRP TRP BBB . n 
B 1 211 ILE 211 210 210 ILE ILE BBB . n 
B 1 212 ILE 212 211 211 ILE ILE BBB . n 
B 1 213 CYS 213 212 212 CYS CYS BBB . n 
B 1 214 LYS 214 213 213 LYS LYS BBB . n 
B 1 215 GLU 215 214 214 GLU GLU BBB . n 
B 1 216 SER 216 215 215 SER SER BBB . n 
B 1 217 ILE 217 216 216 ILE ILE BBB . n 
B 1 218 SER 218 217 217 SER SER BBB . n 
B 1 219 VAL 219 218 218 VAL VAL BBB . n 
B 1 220 SER 220 219 219 SER SER BBB . n 
B 1 221 SER 221 220 220 SER SER BBB . n 
B 1 222 GLU 222 221 221 GLU GLU BBB . n 
B 1 223 GLN 223 222 222 GLN GLN BBB . n 
B 1 224 LEU 224 223 223 LEU LEU BBB . n 
B 1 225 ALA 225 224 224 ALA ALA BBB . n 
B 1 226 GLN 226 225 225 GLN GLN BBB . n 
B 1 227 PHE 227 226 226 PHE PHE BBB . n 
B 1 228 ARG 228 227 227 ARG ARG BBB . n 
B 1 229 SER 229 228 228 SER SER BBB . n 
B 1 230 LEU 230 229 229 LEU LEU BBB . n 
B 1 231 LEU 231 230 230 LEU LEU BBB . n 
B 1 232 SER 232 231 231 SER SER BBB . n 
B 1 233 ASN 233 232 232 ASN ASN BBB . n 
B 1 234 VAL 234 233 233 VAL VAL BBB . n 
B 1 235 GLU 235 234 234 GLU GLU BBB . n 
B 1 236 GLY 236 235 235 GLY GLY BBB . n 
B 1 237 ASP 237 236 236 ASP ASP BBB . n 
B 1 238 ASN 238 237 237 ASN ASN BBB . n 
B 1 239 ALA 239 238 238 ALA ALA BBB . n 
B 1 240 VAL 240 239 239 VAL VAL BBB . n 
B 1 241 PRO 241 240 240 PRO PRO BBB . n 
B 1 242 MET 242 241 241 MET MET BBB . n 
B 1 243 GLN 243 242 242 GLN GLN BBB . n 
B 1 244 HIS 244 243 243 HIS HIS BBB . n 
B 1 245 ASN 245 244 244 ASN ASN BBB . n 
B 1 246 ASN 246 245 245 ASN ASN BBB . n 
B 1 247 ARG 247 246 246 ARG ARG BBB . n 
B 1 248 PRO 248 247 247 PRO PRO BBB . n 
B 1 249 THR 249 248 248 THR THR BBB . n 
B 1 250 GLN 250 249 249 GLN GLN BBB . n 
B 1 251 PRO 251 250 250 PRO PRO BBB . n 
B 1 252 LEU 252 251 251 LEU LEU BBB . n 
B 1 253 LYS 253 252 252 LYS LYS BBB . n 
B 1 254 GLY 254 253 253 GLY GLY BBB . n 
B 1 255 ARG 255 254 254 ARG ARG BBB . n 
B 1 256 THR 256 255 255 THR THR BBB . n 
B 1 257 VAL 257 256 256 VAL VAL BBB . n 
B 1 258 ARG 258 257 257 ARG ARG BBB . n 
B 1 259 ALA 259 258 258 ALA ALA BBB . n 
B 1 260 SER 260 259 259 SER SER BBB . n 
B 1 261 PHE 261 260 260 PHE PHE BBB . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1H1P 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1H1P 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 ZN    1   301 261 ZN    ZN  AAA . 
D 3 A1H1P 1   302 301 A1H1P VER AAA . 
E 2 ZN    1   301 1   ZN    ZN  BBB . 
F 3 A1H1P 1   302 1   A1H1P VER BBB . 
G 4 HOH   1   401 286 HOH   HOH AAA . 
G 4 HOH   2   402 201 HOH   HOH AAA . 
G 4 HOH   3   403 213 HOH   HOH AAA . 
G 4 HOH   4   404 204 HOH   HOH AAA . 
G 4 HOH   5   405 299 HOH   HOH AAA . 
G 4 HOH   6   406 29  HOH   HOH AAA . 
G 4 HOH   7   407 82  HOH   HOH AAA . 
G 4 HOH   8   408 282 HOH   HOH AAA . 
G 4 HOH   9   409 265 HOH   HOH AAA . 
G 4 HOH   10  410 180 HOH   HOH AAA . 
G 4 HOH   11  411 160 HOH   HOH AAA . 
G 4 HOH   12  412 73  HOH   HOH AAA . 
G 4 HOH   13  413 156 HOH   HOH AAA . 
G 4 HOH   14  414 202 HOH   HOH AAA . 
G 4 HOH   15  415 243 HOH   HOH AAA . 
G 4 HOH   16  416 17  HOH   HOH AAA . 
G 4 HOH   17  417 256 HOH   HOH AAA . 
G 4 HOH   18  418 147 HOH   HOH AAA . 
G 4 HOH   19  419 192 HOH   HOH AAA . 
G 4 HOH   20  420 67  HOH   HOH AAA . 
G 4 HOH   21  421 76  HOH   HOH AAA . 
G 4 HOH   22  422 65  HOH   HOH AAA . 
G 4 HOH   23  423 216 HOH   HOH AAA . 
G 4 HOH   24  424 187 HOH   HOH AAA . 
G 4 HOH   25  425 197 HOH   HOH AAA . 
G 4 HOH   26  426 301 HOH   HOH AAA . 
G 4 HOH   27  427 222 HOH   HOH AAA . 
G 4 HOH   28  428 8   HOH   HOH AAA . 
G 4 HOH   29  429 98  HOH   HOH AAA . 
G 4 HOH   30  430 105 HOH   HOH AAA . 
G 4 HOH   31  431 175 HOH   HOH AAA . 
G 4 HOH   32  432 246 HOH   HOH AAA . 
G 4 HOH   33  433 89  HOH   HOH AAA . 
G 4 HOH   34  434 254 HOH   HOH AAA . 
G 4 HOH   35  435 295 HOH   HOH AAA . 
G 4 HOH   36  436 101 HOH   HOH AAA . 
G 4 HOH   37  437 131 HOH   HOH AAA . 
G 4 HOH   38  438 37  HOH   HOH AAA . 
G 4 HOH   39  439 103 HOH   HOH AAA . 
G 4 HOH   40  440 224 HOH   HOH AAA . 
G 4 HOH   41  441 111 HOH   HOH AAA . 
G 4 HOH   42  442 226 HOH   HOH AAA . 
G 4 HOH   43  443 11  HOH   HOH AAA . 
G 4 HOH   44  444 230 HOH   HOH AAA . 
G 4 HOH   45  445 174 HOH   HOH AAA . 
G 4 HOH   46  446 85  HOH   HOH AAA . 
G 4 HOH   47  447 185 HOH   HOH AAA . 
G 4 HOH   48  448 69  HOH   HOH AAA . 
G 4 HOH   49  449 92  HOH   HOH AAA . 
G 4 HOH   50  450 117 HOH   HOH AAA . 
G 4 HOH   51  451 250 HOH   HOH AAA . 
G 4 HOH   52  452 219 HOH   HOH AAA . 
G 4 HOH   53  453 94  HOH   HOH AAA . 
G 4 HOH   54  454 206 HOH   HOH AAA . 
G 4 HOH   55  455 18  HOH   HOH AAA . 
G 4 HOH   56  456 15  HOH   HOH AAA . 
G 4 HOH   57  457 221 HOH   HOH AAA . 
G 4 HOH   58  458 255 HOH   HOH AAA . 
G 4 HOH   59  459 19  HOH   HOH AAA . 
G 4 HOH   60  460 208 HOH   HOH AAA . 
G 4 HOH   61  461 120 HOH   HOH AAA . 
G 4 HOH   62  462 80  HOH   HOH AAA . 
G 4 HOH   63  463 283 HOH   HOH AAA . 
G 4 HOH   64  464 51  HOH   HOH AAA . 
G 4 HOH   65  465 231 HOH   HOH AAA . 
G 4 HOH   66  466 54  HOH   HOH AAA . 
G 4 HOH   67  467 115 HOH   HOH AAA . 
G 4 HOH   68  468 34  HOH   HOH AAA . 
G 4 HOH   69  469 277 HOH   HOH AAA . 
G 4 HOH   70  470 9   HOH   HOH AAA . 
G 4 HOH   71  471 87  HOH   HOH AAA . 
G 4 HOH   72  472 106 HOH   HOH AAA . 
G 4 HOH   73  473 234 HOH   HOH AAA . 
G 4 HOH   74  474 45  HOH   HOH AAA . 
G 4 HOH   75  475 287 HOH   HOH AAA . 
G 4 HOH   76  476 169 HOH   HOH AAA . 
G 4 HOH   77  477 236 HOH   HOH AAA . 
G 4 HOH   78  478 159 HOH   HOH AAA . 
G 4 HOH   79  479 12  HOH   HOH AAA . 
G 4 HOH   80  480 126 HOH   HOH AAA . 
G 4 HOH   81  481 53  HOH   HOH AAA . 
G 4 HOH   82  482 90  HOH   HOH AAA . 
G 4 HOH   83  483 102 HOH   HOH AAA . 
G 4 HOH   84  484 27  HOH   HOH AAA . 
G 4 HOH   85  485 128 HOH   HOH AAA . 
G 4 HOH   86  486 43  HOH   HOH AAA . 
G 4 HOH   87  487 281 HOH   HOH AAA . 
G 4 HOH   88  488 154 HOH   HOH AAA . 
G 4 HOH   89  489 32  HOH   HOH AAA . 
G 4 HOH   90  490 151 HOH   HOH AAA . 
G 4 HOH   91  491 61  HOH   HOH AAA . 
G 4 HOH   92  492 130 HOH   HOH AAA . 
G 4 HOH   93  493 285 HOH   HOH AAA . 
G 4 HOH   94  494 198 HOH   HOH AAA . 
G 4 HOH   95  495 137 HOH   HOH AAA . 
G 4 HOH   96  496 71  HOH   HOH AAA . 
G 4 HOH   97  497 78  HOH   HOH AAA . 
G 4 HOH   98  498 13  HOH   HOH AAA . 
G 4 HOH   99  499 178 HOH   HOH AAA . 
G 4 HOH   100 500 182 HOH   HOH AAA . 
G 4 HOH   101 501 20  HOH   HOH AAA . 
G 4 HOH   102 502 72  HOH   HOH AAA . 
G 4 HOH   103 503 86  HOH   HOH AAA . 
G 4 HOH   104 504 110 HOH   HOH AAA . 
G 4 HOH   105 505 251 HOH   HOH AAA . 
G 4 HOH   106 506 84  HOH   HOH AAA . 
G 4 HOH   107 507 297 HOH   HOH AAA . 
G 4 HOH   108 508 63  HOH   HOH AAA . 
G 4 HOH   109 509 74  HOH   HOH AAA . 
G 4 HOH   110 510 129 HOH   HOH AAA . 
G 4 HOH   111 511 75  HOH   HOH AAA . 
G 4 HOH   112 512 253 HOH   HOH AAA . 
G 4 HOH   113 513 59  HOH   HOH AAA . 
G 4 HOH   114 514 176 HOH   HOH AAA . 
G 4 HOH   115 515 288 HOH   HOH AAA . 
G 4 HOH   116 516 245 HOH   HOH AAA . 
G 4 HOH   117 517 168 HOH   HOH AAA . 
G 4 HOH   118 518 136 HOH   HOH AAA . 
G 4 HOH   119 519 263 HOH   HOH AAA . 
G 4 HOH   120 520 233 HOH   HOH AAA . 
G 4 HOH   121 521 278 HOH   HOH AAA . 
G 4 HOH   122 522 272 HOH   HOH AAA . 
G 4 HOH   123 523 152 HOH   HOH AAA . 
G 4 HOH   124 524 190 HOH   HOH AAA . 
G 4 HOH   125 525 186 HOH   HOH AAA . 
G 4 HOH   126 526 259 HOH   HOH AAA . 
G 4 HOH   127 527 262 HOH   HOH AAA . 
G 4 HOH   128 528 260 HOH   HOH AAA . 
G 4 HOH   129 529 116 HOH   HOH AAA . 
G 4 HOH   130 530 143 HOH   HOH AAA . 
G 4 HOH   131 531 279 HOH   HOH AAA . 
G 4 HOH   132 532 229 HOH   HOH AAA . 
G 4 HOH   133 533 132 HOH   HOH AAA . 
G 4 HOH   134 534 232 HOH   HOH AAA . 
H 4 HOH   1   401 289 HOH   HOH BBB . 
H 4 HOH   2   402 269 HOH   HOH BBB . 
H 4 HOH   3   403 237 HOH   HOH BBB . 
H 4 HOH   4   404 39  HOH   HOH BBB . 
H 4 HOH   5   405 196 HOH   HOH BBB . 
H 4 HOH   6   406 138 HOH   HOH BBB . 
H 4 HOH   7   407 46  HOH   HOH BBB . 
H 4 HOH   8   408 298 HOH   HOH BBB . 
H 4 HOH   9   409 303 HOH   HOH BBB . 
H 4 HOH   10  410 68  HOH   HOH BBB . 
H 4 HOH   11  411 112 HOH   HOH BBB . 
H 4 HOH   12  412 214 HOH   HOH BBB . 
H 4 HOH   13  413 238 HOH   HOH BBB . 
H 4 HOH   14  414 223 HOH   HOH BBB . 
H 4 HOH   15  415 145 HOH   HOH BBB . 
H 4 HOH   16  416 215 HOH   HOH BBB . 
H 4 HOH   17  417 96  HOH   HOH BBB . 
H 4 HOH   18  418 134 HOH   HOH BBB . 
H 4 HOH   19  419 247 HOH   HOH BBB . 
H 4 HOH   20  420 24  HOH   HOH BBB . 
H 4 HOH   21  421 188 HOH   HOH BBB . 
H 4 HOH   22  422 124 HOH   HOH BBB . 
H 4 HOH   23  423 179 HOH   HOH BBB . 
H 4 HOH   24  424 113 HOH   HOH BBB . 
H 4 HOH   25  425 275 HOH   HOH BBB . 
H 4 HOH   26  426 33  HOH   HOH BBB . 
H 4 HOH   27  427 244 HOH   HOH BBB . 
H 4 HOH   28  428 218 HOH   HOH BBB . 
H 4 HOH   29  429 165 HOH   HOH BBB . 
H 4 HOH   30  430 50  HOH   HOH BBB . 
H 4 HOH   31  431 146 HOH   HOH BBB . 
H 4 HOH   32  432 127 HOH   HOH BBB . 
H 4 HOH   33  433 122 HOH   HOH BBB . 
H 4 HOH   34  434 26  HOH   HOH BBB . 
H 4 HOH   35  435 64  HOH   HOH BBB . 
H 4 HOH   36  436 161 HOH   HOH BBB . 
H 4 HOH   37  437 173 HOH   HOH BBB . 
H 4 HOH   38  438 150 HOH   HOH BBB . 
H 4 HOH   39  439 164 HOH   HOH BBB . 
H 4 HOH   40  440 141 HOH   HOH BBB . 
H 4 HOH   41  441 177 HOH   HOH BBB . 
H 4 HOH   42  442 57  HOH   HOH BBB . 
H 4 HOH   43  443 123 HOH   HOH BBB . 
H 4 HOH   44  444 140 HOH   HOH BBB . 
H 4 HOH   45  445 118 HOH   HOH BBB . 
H 4 HOH   46  446 4   HOH   HOH BBB . 
H 4 HOH   47  447 66  HOH   HOH BBB . 
H 4 HOH   48  448 166 HOH   HOH BBB . 
H 4 HOH   49  449 142 HOH   HOH BBB . 
H 4 HOH   50  450 133 HOH   HOH BBB . 
H 4 HOH   51  451 7   HOH   HOH BBB . 
H 4 HOH   52  452 47  HOH   HOH BBB . 
H 4 HOH   53  453 121 HOH   HOH BBB . 
H 4 HOH   54  454 21  HOH   HOH BBB . 
H 4 HOH   55  455 81  HOH   HOH BBB . 
H 4 HOH   56  456 42  HOH   HOH BBB . 
H 4 HOH   57  457 240 HOH   HOH BBB . 
H 4 HOH   58  458 25  HOH   HOH BBB . 
H 4 HOH   59  459 163 HOH   HOH BBB . 
H 4 HOH   60  460 200 HOH   HOH BBB . 
H 4 HOH   61  461 170 HOH   HOH BBB . 
H 4 HOH   62  462 207 HOH   HOH BBB . 
H 4 HOH   63  463 209 HOH   HOH BBB . 
H 4 HOH   64  464 62  HOH   HOH BBB . 
H 4 HOH   65  465 56  HOH   HOH BBB . 
H 4 HOH   66  466 284 HOH   HOH BBB . 
H 4 HOH   67  467 274 HOH   HOH BBB . 
H 4 HOH   68  468 88  HOH   HOH BBB . 
H 4 HOH   69  469 44  HOH   HOH BBB . 
H 4 HOH   70  470 10  HOH   HOH BBB . 
H 4 HOH   71  471 104 HOH   HOH BBB . 
H 4 HOH   72  472 97  HOH   HOH BBB . 
H 4 HOH   73  473 235 HOH   HOH BBB . 
H 4 HOH   74  474 52  HOH   HOH BBB . 
H 4 HOH   75  475 22  HOH   HOH BBB . 
H 4 HOH   76  476 189 HOH   HOH BBB . 
H 4 HOH   77  477 149 HOH   HOH BBB . 
H 4 HOH   78  478 267 HOH   HOH BBB . 
H 4 HOH   79  479 119 HOH   HOH BBB . 
H 4 HOH   80  480 158 HOH   HOH BBB . 
H 4 HOH   81  481 290 HOH   HOH BBB . 
H 4 HOH   82  482 114 HOH   HOH BBB . 
H 4 HOH   83  483 16  HOH   HOH BBB . 
H 4 HOH   84  484 38  HOH   HOH BBB . 
H 4 HOH   85  485 91  HOH   HOH BBB . 
H 4 HOH   86  486 23  HOH   HOH BBB . 
H 4 HOH   87  487 70  HOH   HOH BBB . 
H 4 HOH   88  488 14  HOH   HOH BBB . 
H 4 HOH   89  489 77  HOH   HOH BBB . 
H 4 HOH   90  490 48  HOH   HOH BBB . 
H 4 HOH   91  491 172 HOH   HOH BBB . 
H 4 HOH   92  492 294 HOH   HOH BBB . 
H 4 HOH   93  493 252 HOH   HOH BBB . 
H 4 HOH   94  494 241 HOH   HOH BBB . 
H 4 HOH   95  495 191 HOH   HOH BBB . 
H 4 HOH   96  496 249 HOH   HOH BBB . 
H 4 HOH   97  497 304 HOH   HOH BBB . 
H 4 HOH   98  498 58  HOH   HOH BBB . 
H 4 HOH   99  499 193 HOH   HOH BBB . 
H 4 HOH   100 500 30  HOH   HOH BBB . 
H 4 HOH   101 501 153 HOH   HOH BBB . 
H 4 HOH   102 502 212 HOH   HOH BBB . 
H 4 HOH   103 503 41  HOH   HOH BBB . 
H 4 HOH   104 504 139 HOH   HOH BBB . 
H 4 HOH   105 505 36  HOH   HOH BBB . 
H 4 HOH   106 506 144 HOH   HOH BBB . 
H 4 HOH   107 507 93  HOH   HOH BBB . 
H 4 HOH   108 508 125 HOH   HOH BBB . 
H 4 HOH   109 509 181 HOH   HOH BBB . 
H 4 HOH   110 510 55  HOH   HOH BBB . 
H 4 HOH   111 511 171 HOH   HOH BBB . 
H 4 HOH   112 512 109 HOH   HOH BBB . 
H 4 HOH   113 513 79  HOH   HOH BBB . 
H 4 HOH   114 514 157 HOH   HOH BBB . 
H 4 HOH   115 515 2   HOH   HOH BBB . 
H 4 HOH   116 516 83  HOH   HOH BBB . 
H 4 HOH   117 517 3   HOH   HOH BBB . 
H 4 HOH   118 518 95  HOH   HOH BBB . 
H 4 HOH   119 519 99  HOH   HOH BBB . 
H 4 HOH   120 520 217 HOH   HOH BBB . 
H 4 HOH   121 521 31  HOH   HOH BBB . 
H 4 HOH   122 522 220 HOH   HOH BBB . 
H 4 HOH   123 523 162 HOH   HOH BBB . 
H 4 HOH   124 524 35  HOH   HOH BBB . 
H 4 HOH   125 525 203 HOH   HOH BBB . 
H 4 HOH   126 526 28  HOH   HOH BBB . 
H 4 HOH   127 527 60  HOH   HOH BBB . 
H 4 HOH   128 528 49  HOH   HOH BBB . 
H 4 HOH   129 529 155 HOH   HOH BBB . 
H 4 HOH   130 530 205 HOH   HOH BBB . 
H 4 HOH   131 531 100 HOH   HOH BBB . 
H 4 HOH   132 532 270 HOH   HOH BBB . 
H 4 HOH   133 533 183 HOH   HOH BBB . 
H 4 HOH   134 534 5   HOH   HOH BBB . 
H 4 HOH   135 535 40  HOH   HOH BBB . 
H 4 HOH   136 536 248 HOH   HOH BBB . 
H 4 HOH   137 537 6   HOH   HOH BBB . 
H 4 HOH   138 538 195 HOH   HOH BBB . 
H 4 HOH   139 539 293 HOH   HOH BBB . 
H 4 HOH   140 540 225 HOH   HOH BBB . 
H 4 HOH   141 541 239 HOH   HOH BBB . 
H 4 HOH   142 542 210 HOH   HOH BBB . 
H 4 HOH   143 543 280 HOH   HOH BBB . 
H 4 HOH   144 544 108 HOH   HOH BBB . 
H 4 HOH   145 545 242 HOH   HOH BBB . 
H 4 HOH   146 546 268 HOH   HOH BBB . 
H 4 HOH   147 547 300 HOH   HOH BBB . 
H 4 HOH   148 548 257 HOH   HOH BBB . 
H 4 HOH   149 549 148 HOH   HOH BBB . 
H 4 HOH   150 550 167 HOH   HOH BBB . 
H 4 HOH   151 551 258 HOH   HOH BBB . 
H 4 HOH   152 552 107 HOH   HOH BBB . 
H 4 HOH   153 553 184 HOH   HOH BBB . 
H 4 HOH   154 554 266 HOH   HOH BBB . 
H 4 HOH   155 555 296 HOH   HOH BBB . 
H 4 HOH   156 556 211 HOH   HOH BBB . 
H 4 HOH   157 557 228 HOH   HOH BBB . 
H 4 HOH   158 558 291 HOH   HOH BBB . 
H 4 HOH   159 559 302 HOH   HOH BBB . 
H 4 HOH   160 560 261 HOH   HOH BBB . 
H 4 HOH   161 561 264 HOH   HOH BBB . 
H 4 HOH   162 562 276 HOH   HOH BBB . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 AAA LYS 10 ? CG ? A LYS 11 CG 
2 1 Y 1 AAA LYS 10 ? CD ? A LYS 11 CD 
3 1 Y 1 AAA LYS 10 ? CE ? A LYS 11 CE 
4 1 Y 1 AAA LYS 10 ? NZ ? A LYS 11 NZ 
5 1 Y 1 BBB LYS 10 ? CG ? B LYS 11 CG 
6 1 Y 1 BBB LYS 10 ? CD ? B LYS 11 CD 
7 1 Y 1 BBB LYS 10 ? CE ? B LYS 11 CE 
8 1 Y 1 BBB LYS 10 ? NZ ? B LYS 11 NZ 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? 5.8.0258 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS    ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC ? ? ? .        4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8RLO 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     63.140 
_cell.length_a_esd                 ? 
_cell.length_b                     71.250 
_cell.length_b_esd                 ? 
_cell.length_c                     121.160 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8RLO 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   8RLO 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.82 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              9.0 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '28-31% PEG4000, 0.2 M sodium acetate, 0.1 M Tris pH 9.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            296 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-03 
_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   0.97170 
_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                        'ELETTRA BEAMLINE 11.2C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97170 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   11.2C 
_diffrn_source.pdbx_synchrotron_site       ELETTRA 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8RLO 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.55 
_reflns.d_resolution_low                               46.19 
_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                                     80418 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.9 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.4 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.03 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.084 
_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                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.08 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.55 
_reflns_shell.d_res_low                                     1.59 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.21 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             5894 
_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                               12.7 
_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                               1.338 
_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                                  0.851 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  1.386 
_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]                            -3.748 
_refine.aniso_B[1][2]                            -0.000 
_refine.aniso_B[1][3]                            0.000 
_refine.aniso_B[2][2]                            7.125 
_refine.aniso_B[2][3]                            -0.000 
_refine.aniso_B[3][3]                            -3.378 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               29.202 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.974 
_refine.correlation_coeff_Fo_to_Fc_free          0.960 
_refine.details                                  'Hydrogens have been added in their riding positions' 
_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                                 8RLO 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.55 
_refine.ls_d_res_low                             46.19 
_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                     80418 
_refine.ls_number_reflns_R_free                  4095 
_refine.ls_number_reflns_R_work                  76323 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.938 
_refine.ls_percent_reflns_R_free                 5.092 
_refine.ls_R_factor_all                          0.171 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.2182 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1686 
_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                    'MASK BULK SOLVENT' 
_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                          ? 
_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               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.091 
_refine.pdbx_overall_ESU_R_Free                  0.082 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                 ? 
_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                             8.338 
_refine.overall_SU_ML                            0.113 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        46.19 
_refine_hist.number_atoms_solvent             296 
_refine_hist.number_atoms_total               4366 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        4016 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.014  0.013  4201 ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.017  3689 ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.817  1.636  5727 ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.481  1.591  8625 ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 7.876  5.000  517  ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 36.236 23.738 206  ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 14.057 15.000 656  ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 16.886 15.000 14   ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.100  0.200  538  ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  4812 ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  860  ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.213  0.200  763  ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.202  0.200  3453 ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.169  0.200  1964 ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.079  0.200  1782 ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.146  0.200  247  ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.119  0.200  5    ? r_metal_ion_refined            ? ? 
'X-RAY DIFFRACTION' ? 0.173  0.200  10   ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.238  0.200  57   ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.219  0.200  12   ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 5.237  2.885  2056 ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 5.238  2.885  2055 ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 5.834  4.353  2570 ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 5.825  4.354  2569 ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 6.166  3.245  2145 ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 6.167  3.245  2146 ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 6.981  4.715  3154 ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 6.980  4.716  3155 ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 6.687  34.433 4570 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 6.686  34.443 4571 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 13.557 3.000  7890 ? r_rigid_bond_restr             ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.55  1.587 . . 313 5571 99.8812  . . . . 0.309 . . . . . . . . . . . 0.337 
'X-RAY DIFFRACTION' 1.587 1.631 . . 319 5382 99.8774  . . . . 0.287 . . . . . . . . . . . 0.338 
'X-RAY DIFFRACTION' 1.631 1.678 . . 292 5269 100.0000 . . . . 0.253 . . . . . . . . . . . 0.303 
'X-RAY DIFFRACTION' 1.678 1.729 . . 276 5162 99.9632  . . . . 0.237 . . . . . . . . . . . 0.289 
'X-RAY DIFFRACTION' 1.729 1.786 . . 278 4975 99.9810  . . . . 0.223 . . . . . . . . . . . 0.263 
'X-RAY DIFFRACTION' 1.786 1.849 . . 239 4841 99.9410  . . . . 0.200 . . . . . . . . . . . 0.268 
'X-RAY DIFFRACTION' 1.849 1.918 . . 256 4651 99.9389  . . . . 0.178 . . . . . . . . . . . 0.232 
'X-RAY DIFFRACTION' 1.918 1.997 . . 223 4509 99.9789  . . . . 0.173 . . . . . . . . . . . 0.255 
'X-RAY DIFFRACTION' 1.997 2.085 . . 236 4329 100.0000 . . . . 0.165 . . . . . . . . . . . 0.236 
'X-RAY DIFFRACTION' 2.085 2.187 . . 228 4121 99.9770  . . . . 0.164 . . . . . . . . . . . 0.226 
'X-RAY DIFFRACTION' 2.187 2.305 . . 205 3958 99.9040  . . . . 0.167 . . . . . . . . . . . 0.231 
'X-RAY DIFFRACTION' 2.305 2.445 . . 201 3739 99.9493  . . . . 0.145 . . . . . . . . . . . 0.194 
'X-RAY DIFFRACTION' 2.445 2.613 . . 188 3508 99.9459  . . . . 0.147 . . . . . . . . . . . 0.215 
'X-RAY DIFFRACTION' 2.613 2.822 . . 160 3307 99.7985  . . . . 0.138 . . . . . . . . . . . 0.195 
'X-RAY DIFFRACTION' 2.822 3.091 . . 154 3031 99.9686  . . . . 0.154 . . . . . . . . . . . 0.231 
'X-RAY DIFFRACTION' 3.091 3.455 . . 143 2763 99.8969  . . . . 0.179 . . . . . . . . . . . 0.225 
'X-RAY DIFFRACTION' 3.455 3.987 . . 126 2473 99.9615  . . . . 0.167 . . . . . . . . . . . 0.200 
'X-RAY DIFFRACTION' 3.987 4.878 . . 114 2093 100.0000 . . . . 0.135 . . . . . . . . . . . 0.173 
'X-RAY DIFFRACTION' 4.878 6.877 . . 86  1661 100.0000 . . . . 0.151 . . . . . . . . . . . 0.180 
'X-RAY DIFFRACTION' 6.877 46.19 . . 58  980  99.5206  . . . . 0.171 . . . . . . . . . . . 0.174 
# 
_struct.entry_id                     8RLO 
_struct.title                        'Human Carbonic Anhydrase I in complex with veralipride' 
_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        8RLO 
_struct_keywords.text            'carbonic anhydrase I, sulfonamide, veralipride, inhibitor, metalloenzyme, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    CAH1_HUMAN 
_struct_ref.pdbx_db_accession          P00915 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVL
KGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQK
VLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAV
PMQHNNRPTQPLKGRTVRASF
;
_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 8RLO AAA 1 ? 261 ? P00915 1 ? 261 ? 0 260 
2 1 8RLO BBB 1 ? 261 ? P00915 1 ? 261 ? 0 260 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 GLN A 16  ? LEU A 20  ? GLN AAA 15  LEU AAA 19  5 ? 5  
HELX_P HELX_P2  AA2 TYR A 21  ? GLY A 26  ? TYR AAA 20  GLY AAA 25  5 ? 6  
HELX_P HELX_P3  AA3 LYS A 35  ? THR A 39  ? LYS AAA 34  THR AAA 38  5 ? 5  
HELX_P HELX_P4  AA4 ASN A 53  ? ALA A 55  ? ASN AAA 52  ALA AAA 54  5 ? 3  
HELX_P HELX_P5  AA5 SER A 131 ? ALA A 136 ? SER AAA 130 ALA AAA 135 1 ? 6  
HELX_P HELX_P6  AA6 ASN A 155 ? LYS A 157 ? ASN AAA 154 LYS AAA 156 5 ? 3  
HELX_P HELX_P7  AA7 LEU A 158 ? LEU A 165 ? LEU AAA 157 LEU AAA 164 1 ? 8  
HELX_P HELX_P8  AA8 GLN A 166 ? ILE A 168 ? GLN AAA 165 ILE AAA 167 5 ? 3  
HELX_P HELX_P9  AA9 ASP A 181 ? LEU A 186 ? ASP AAA 180 LEU AAA 185 5 ? 6  
HELX_P HELX_P10 AB1 SER A 220 ? SER A 229 ? SER AAA 219 SER AAA 228 1 ? 10 
HELX_P HELX_P11 AB2 GLY B 13  ? LEU B 20  ? GLY BBB 12  LEU BBB 19  5 ? 8  
HELX_P HELX_P12 AB3 TYR B 21  ? GLY B 26  ? TYR BBB 20  GLY BBB 25  5 ? 6  
HELX_P HELX_P13 AB4 LYS B 35  ? THR B 39  ? LYS BBB 34  THR BBB 38  5 ? 5  
HELX_P HELX_P14 AB5 ASN B 53  ? ALA B 55  ? ASN BBB 52  ALA BBB 54  5 ? 3  
HELX_P HELX_P15 AB6 SER B 131 ? ALA B 136 ? SER BBB 130 ALA BBB 135 1 ? 6  
HELX_P HELX_P16 AB7 ASN B 155 ? LYS B 157 ? ASN BBB 154 LYS BBB 156 5 ? 3  
HELX_P HELX_P17 AB8 LEU B 158 ? LEU B 165 ? LEU BBB 157 LEU BBB 164 1 ? 8  
HELX_P HELX_P18 AB9 GLN B 166 ? ILE B 168 ? GLN BBB 165 ILE BBB 167 5 ? 3  
HELX_P HELX_P19 AC1 ASP B 181 ? LEU B 186 ? ASP BBB 180 LEU BBB 185 5 ? 6  
HELX_P HELX_P20 AC2 SER B 220 ? SER B 229 ? SER BBB 219 SER BBB 228 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 95  NE2 ? ? ? 1_555 C ZN    . ZN ? ? AAA HIS 94  AAA ZN    301 1_555 ? ? ? ? ? ? ? 2.087 ? ? 
metalc2 metalc ? ? A HIS 97  NE2 ? ? ? 1_555 C ZN    . ZN ? ? AAA HIS 96  AAA ZN    301 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc3 metalc ? ? A HIS 120 ND1 ? ? ? 1_555 C ZN    . ZN ? ? AAA HIS 119 AAA ZN    301 1_555 ? ? ? ? ? ? ? 1.959 ? ? 
metalc4 metalc ? ? C ZN  .   ZN  ? ? ? 1_555 D A1H1P . N  ? ? AAA ZN  301 AAA A1H1P 302 1_555 ? ? ? ? ? ? ? 1.898 ? ? 
metalc5 metalc ? ? B HIS 95  NE2 ? ? ? 1_555 E ZN    . ZN ? ? BBB HIS 94  BBB ZN    301 1_555 ? ? ? ? ? ? ? 2.093 ? ? 
metalc6 metalc ? ? B HIS 97  NE2 ? ? ? 1_555 E ZN    . ZN ? ? BBB HIS 96  BBB ZN    301 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
metalc7 metalc ? ? B HIS 120 ND1 ? ? ? 1_555 E ZN    . ZN ? ? BBB HIS 119 BBB ZN    301 1_555 ? ? ? ? ? ? ? 1.996 ? ? 
metalc8 metalc ? ? E ZN  .   ZN  ? ? ? 1_555 F A1H1P . N  ? ? BBB ZN  301 BBB A1H1P 302 1_555 ? ? ? ? ? ? ? 1.892 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 95  ? AAA HIS 94  ? 1_555 ZN ? C ZN . ? AAA ZN 301 ? 1_555 NE2 ? A HIS   97  ? AAA HIS   96  ? 1_555 112.0 ? 
2  NE2 ? A HIS 95  ? AAA HIS 94  ? 1_555 ZN ? C ZN . ? AAA ZN 301 ? 1_555 ND1 ? A HIS   120 ? AAA HIS   119 ? 1_555 107.9 ? 
3  NE2 ? A HIS 97  ? AAA HIS 96  ? 1_555 ZN ? C ZN . ? AAA ZN 301 ? 1_555 ND1 ? A HIS   120 ? AAA HIS   119 ? 1_555 97.8  ? 
4  NE2 ? A HIS 95  ? AAA HIS 94  ? 1_555 ZN ? C ZN . ? AAA ZN 301 ? 1_555 N   ? D A1H1P .   ? AAA A1H1P 302 ? 1_555 108.7 ? 
5  NE2 ? A HIS 97  ? AAA HIS 96  ? 1_555 ZN ? C ZN . ? AAA ZN 301 ? 1_555 N   ? D A1H1P .   ? AAA A1H1P 302 ? 1_555 112.0 ? 
6  ND1 ? A HIS 120 ? AAA HIS 119 ? 1_555 ZN ? C ZN . ? AAA ZN 301 ? 1_555 N   ? D A1H1P .   ? AAA A1H1P 302 ? 1_555 118.1 ? 
7  NE2 ? B HIS 95  ? BBB HIS 94  ? 1_555 ZN ? E ZN . ? BBB ZN 301 ? 1_555 NE2 ? B HIS   97  ? BBB HIS   96  ? 1_555 109.3 ? 
8  NE2 ? B HIS 95  ? BBB HIS 94  ? 1_555 ZN ? E ZN . ? BBB ZN 301 ? 1_555 ND1 ? B HIS   120 ? BBB HIS   119 ? 1_555 107.5 ? 
9  NE2 ? B HIS 97  ? BBB HIS 96  ? 1_555 ZN ? E ZN . ? BBB ZN 301 ? 1_555 ND1 ? B HIS   120 ? BBB HIS   119 ? 1_555 95.2  ? 
10 NE2 ? B HIS 95  ? BBB HIS 94  ? 1_555 ZN ? E ZN . ? BBB ZN 301 ? 1_555 N   ? F A1H1P .   ? BBB A1H1P 302 ? 1_555 106.7 ? 
11 NE2 ? B HIS 97  ? BBB HIS 96  ? 1_555 ZN ? E ZN . ? BBB ZN 301 ? 1_555 N   ? F A1H1P .   ? BBB A1H1P 302 ? 1_555 117.2 ? 
12 ND1 ? B HIS 120 ? BBB HIS 119 ? 1_555 ZN ? E ZN . ? BBB ZN 301 ? 1_555 N   ? F A1H1P .   ? BBB A1H1P 302 ? 1_555 120.2 ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 SER 30  A . ? SER 29  AAA PRO 31  A ? PRO 30  AAA 1 1.18  
2 PRO 202 A . ? PRO 201 AAA PRO 203 A ? PRO 202 AAA 1 6.94  
3 SER 30  B . ? SER 29  BBB PRO 31  B ? PRO 30  BBB 1 -2.39 
4 PRO 202 B . ? PRO 201 BBB PRO 203 B ? PRO 202 BBB 1 8.43  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 2  ? 
AA2 ? 10 ? 
AA3 ? 6  ? 
AA4 ? 2  ? 
AA5 ? 10 ? 
AA6 ? 6  ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? parallel      
AA2 1 2  ? parallel      
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-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 
AA3 1 2  ? anti-parallel 
AA3 2 3  ? anti-parallel 
AA3 3 4  ? anti-parallel 
AA3 4 5  ? anti-parallel 
AA3 5 6  ? parallel      
AA4 1 2  ? parallel      
AA5 1 2  ? parallel      
AA5 2 3  ? anti-parallel 
AA5 3 4  ? anti-parallel 
AA5 4 5  ? parallel      
AA5 5 6  ? anti-parallel 
AA5 6 7  ? anti-parallel 
AA5 7 8  ? anti-parallel 
AA5 8 9  ? anti-parallel 
AA5 9 10 ? anti-parallel 
AA6 1 2  ? anti-parallel 
AA6 2 3  ? anti-parallel 
AA6 3 4  ? anti-parallel 
AA6 4 5  ? anti-parallel 
AA6 5 6  ? 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  ASP A 33  ? ILE A 34  ? ASP AAA 32  ILE AAA 33  
AA1 2  THR A 109 ? VAL A 110 ? THR AAA 108 VAL AAA 109 
AA2 1  LYS A 40  ? HIS A 41  ? LYS AAA 39  HIS AAA 40  
AA2 2  ARG A 258 ? ALA A 259 ? ARG AAA 257 ALA AAA 258 
AA2 3  PHE A 192 ? GLY A 197 ? PHE AAA 191 GLY AAA 196 
AA2 4  VAL A 208 ? CYS A 213 ? VAL AAA 207 CYS AAA 212 
AA2 5  LEU A 142 ? VAL A 151 ? LEU AAA 141 VAL AAA 150 
AA2 6  ALA A 117 ? ASN A 125 ? ALA AAA 116 ASN AAA 124 
AA2 7  TYR A 89  ? TRP A 98  ? TYR AAA 88  TRP AAA 97  
AA2 8  PHE A 67  ? PHE A 71  ? PHE AAA 66  PHE AAA 70  
AA2 9  ALA A 57  ? ASN A 62  ? ALA AAA 56  ASN AAA 61  
AA2 10 ARG A 174 ? PRO A 176 ? ARG AAA 173 PRO AAA 175 
AA3 1  ILE A 48  ? SER A 51  ? ILE AAA 47  SER AAA 50  
AA3 2  VAL A 79  ? GLY A 82  ? VAL AAA 78  GLY AAA 81  
AA3 3  TYR A 89  ? TRP A 98  ? TYR AAA 88  TRP AAA 97  
AA3 4  ALA A 117 ? ASN A 125 ? ALA AAA 116 ASN AAA 124 
AA3 5  LEU A 142 ? VAL A 151 ? LEU AAA 141 VAL AAA 150 
AA3 6  ILE A 217 ? VAL A 219 ? ILE AAA 216 VAL AAA 218 
AA4 1  ASP B 33  ? ILE B 34  ? ASP BBB 32  ILE BBB 33  
AA4 2  THR B 109 ? VAL B 110 ? THR BBB 108 VAL BBB 109 
AA5 1  LYS B 40  ? HIS B 41  ? LYS BBB 39  HIS BBB 40  
AA5 2  ARG B 258 ? ALA B 259 ? ARG BBB 257 ALA BBB 258 
AA5 3  PHE B 192 ? GLY B 197 ? PHE BBB 191 GLY BBB 196 
AA5 4  VAL B 208 ? CYS B 213 ? VAL BBB 207 CYS BBB 212 
AA5 5  LEU B 142 ? VAL B 151 ? LEU BBB 141 VAL BBB 150 
AA5 6  ALA B 117 ? TRP B 124 ? ALA BBB 116 TRP BBB 123 
AA5 7  TYR B 89  ? TRP B 98  ? TYR BBB 88  TRP BBB 97  
AA5 8  PHE B 67  ? PHE B 71  ? PHE BBB 66  PHE BBB 70  
AA5 9  ALA B 57  ? ASN B 62  ? ALA BBB 56  ASN BBB 61  
AA5 10 ARG B 174 ? PRO B 176 ? ARG BBB 173 PRO BBB 175 
AA6 1  ILE B 48  ? SER B 51  ? ILE BBB 47  SER BBB 50  
AA6 2  VAL B 79  ? GLY B 82  ? VAL BBB 78  GLY BBB 81  
AA6 3  TYR B 89  ? TRP B 98  ? TYR BBB 88  TRP BBB 97  
AA6 4  ALA B 117 ? TRP B 124 ? ALA BBB 116 TRP BBB 123 
AA6 5  LEU B 142 ? VAL B 151 ? LEU BBB 141 VAL BBB 150 
AA6 6  ILE B 217 ? VAL B 219 ? ILE BBB 216 VAL BBB 218 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2  N ILE A 34  ? N ILE AAA 33  O THR A 109 ? O THR AAA 108 
AA2 1 2  N LYS A 40  ? N LYS AAA 39  O ALA A 259 ? O ALA AAA 258 
AA2 2 3  O ARG A 258 ? O ARG AAA 257 N THR A 194 ? N THR AAA 193 
AA2 3 4  N GLY A 197 ? N GLY AAA 196 O VAL A 208 ? O VAL AAA 207 
AA2 4 5  O ILE A 211 ? O ILE AAA 210 N GLY A 146 ? N GLY AAA 145 
AA2 5 6  O MET A 149 ? O MET AAA 148 N ALA A 117 ? N ALA AAA 116 
AA2 6 7  O TRP A 124 ? O TRP AAA 123 N ARG A 90  ? N ARG AAA 89  
AA2 7 8  O PHE A 94  ? O PHE AAA 93  N VAL A 69  ? N VAL AAA 68  
AA2 8 9  O ASN A 70  ? O ASN AAA 69  N LYS A 58  ? N LYS AAA 57  
AA2 9 10 N ILE A 60  ? N ILE AAA 59  O ALA A 175 ? O ALA AAA 174 
AA3 1 2  N SER A 49  ? N SER AAA 48  O LYS A 81  ? O LYS AAA 80  
AA3 2 3  N LEU A 80  ? N LEU AAA 79  O TYR A 89  ? O TYR AAA 88  
AA3 3 4  N ARG A 90  ? N ARG AAA 89  O TRP A 124 ? O TRP AAA 123 
AA3 4 5  N ALA A 117 ? N ALA AAA 116 O MET A 149 ? O MET AAA 148 
AA3 5 6  N LYS A 150 ? N LYS AAA 149 O ILE A 217 ? O ILE AAA 216 
AA4 1 2  N ILE B 34  ? N ILE BBB 33  O THR B 109 ? O THR BBB 108 
AA5 1 2  N LYS B 40  ? N LYS BBB 39  O ALA B 259 ? O ALA BBB 258 
AA5 2 3  O ARG B 258 ? O ARG BBB 257 N THR B 194 ? N THR BBB 193 
AA5 3 4  N GLY B 197 ? N GLY BBB 196 O VAL B 208 ? O VAL BBB 207 
AA5 4 5  O ILE B 211 ? O ILE BBB 210 N GLY B 146 ? N GLY BBB 145 
AA5 5 6  O MET B 149 ? O MET BBB 148 N ALA B 117 ? N ALA BBB 116 
AA5 6 7  O TRP B 124 ? O TRP BBB 123 N ARG B 90  ? N ARG BBB 89  
AA5 7 8  O PHE B 94  ? O PHE BBB 93  N VAL B 69  ? N VAL BBB 68  
AA5 8 9  O ASN B 70  ? O ASN BBB 69  N GLU B 59  ? N GLU BBB 58  
AA5 9 10 N ILE B 60  ? N ILE BBB 59  O ALA B 175 ? O ALA BBB 174 
AA6 1 2  N SER B 49  ? N SER BBB 48  O LYS B 81  ? O LYS BBB 80  
AA6 2 3  N LEU B 80  ? N LEU BBB 79  O TYR B 89  ? O TYR BBB 88  
AA6 3 4  N ARG B 90  ? N ARG BBB 89  O TRP B 124 ? O TRP BBB 123 
AA6 4 5  N ALA B 117 ? N ALA BBB 116 O MET B 149 ? O MET BBB 148 
AA6 5 6  N LYS B 150 ? N LYS BBB 149 O ILE B 217 ? O ILE BBB 216 
# 
_pdbx_entry_details.entry_id                   8RLO 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   NE2 
_pdbx_validate_close_contact.auth_asym_id_1   AAA 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    103 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   A 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   AAA 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    401 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.13 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            C 
_pdbx_validate_rmsd_bond.auth_asym_id_1            BBB 
_pdbx_validate_rmsd_bond.auth_comp_id_1            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_1             17 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            O 
_pdbx_validate_rmsd_bond.auth_asym_id_2            BBB 
_pdbx_validate_rmsd_bond.auth_comp_id_2            SER 
_pdbx_validate_rmsd_bond.auth_seq_id_2             17 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.506 
_pdbx_validate_rmsd_bond.bond_target_value         1.229 
_pdbx_validate_rmsd_bond.bond_deviation            0.277 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.019 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU AAA 106 ? ? -96.68  -60.61 
2 1 ASN AAA 244 ? ? -159.42 29.24  
3 1 LYS BBB 57  ? ? -122.25 -59.48 
4 1 ASN BBB 75  ? ? -99.26  35.25  
5 1 HIS BBB 103 ? ? -158.25 84.20  
6 1 GLU BBB 106 ? ? -98.17  -65.52 
7 1 ASN BBB 244 ? ? -162.66 37.85  
# 
_pdbx_validate_main_chain_plane.id                       1 
_pdbx_validate_main_chain_plane.PDB_model_num            1 
_pdbx_validate_main_chain_plane.auth_comp_id             SER 
_pdbx_validate_main_chain_plane.auth_asym_id             BBB 
_pdbx_validate_main_chain_plane.auth_seq_id              17 
_pdbx_validate_main_chain_plane.PDB_ins_code             ? 
_pdbx_validate_main_chain_plane.label_alt_id             ? 
_pdbx_validate_main_chain_plane.improper_torsion_angle   -14.92 
# 
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 AAA MET 0 ? A MET 1 
2 1 Y 1 AAA ALA 1 ? A ALA 2 
3 1 Y 1 AAA SER 2 ? A SER 3 
4 1 Y 1 AAA PRO 3 ? A PRO 4 
5 1 Y 1 AAA ASP 4 ? A ASP 5 
6 1 Y 1 BBB MET 0 ? B MET 1 
7 1 Y 1 BBB ALA 1 ? B ALA 2 
8 1 Y 1 BBB SER 2 ? B SER 3 
9 1 Y 1 BBB PRO 3 ? B PRO 4 
# 
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 
A1H1P O    O  N N 1   
A1H1P C1   C  Y N 2   
A1H1P O4   O  N N 3   
A1H1P S    S  N N 4   
A1H1P O3   O  N N 5   
A1H1P N    N  N N 6   
A1H1P C    C  Y N 7   
A1H1P C16  C  Y N 8   
A1H1P C6   C  Y N 9   
A1H1P C4   C  Y N 10  
A1H1P O1   O  N N 11  
A1H1P C5   C  N N 12  
A1H1P C2   C  Y N 13  
A1H1P C3   C  N N 14  
A1H1P C7   C  N N 15  
A1H1P O2   O  N N 16  
A1H1P N1   N  N N 17  
A1H1P C8   C  N N 18  
A1H1P C9   C  N S 19  
A1H1P N2   N  N N 20  
A1H1P C13  C  N N 21  
A1H1P C14  C  N N 22  
A1H1P C15  C  N N 23  
A1H1P C12  C  N N 24  
A1H1P C11  C  N N 25  
A1H1P C10  C  N N 26  
A1H1P H2   H  N N 27  
A1H1P H    H  N N 28  
A1H1P H1   H  N N 29  
A1H1P H24  H  N N 30  
A1H1P H7   H  N N 31  
A1H1P H6   H  N N 32  
A1H1P H8   H  N N 33  
A1H1P H5   H  N N 34  
A1H1P H3   H  N N 35  
A1H1P H4   H  N N 36  
A1H1P H9   H  N N 37  
A1H1P H11  H  N N 38  
A1H1P H10  H  N N 39  
A1H1P H12  H  N N 40  
A1H1P H20  H  N N 41  
A1H1P H19  H  N N 42  
A1H1P H21  H  N N 43  
A1H1P H22  H  N N 44  
A1H1P H23  H  N N 45  
A1H1P H18  H  N N 46  
A1H1P H17  H  N N 47  
A1H1P H16  H  N N 48  
A1H1P H15  H  N N 49  
A1H1P H14  H  N N 50  
A1H1P H13  H  N N 51  
ALA   N    N  N N 52  
ALA   CA   C  N S 53  
ALA   C    C  N N 54  
ALA   O    O  N N 55  
ALA   CB   C  N N 56  
ALA   OXT  O  N N 57  
ALA   H    H  N N 58  
ALA   H2   H  N N 59  
ALA   HA   H  N N 60  
ALA   HB1  H  N N 61  
ALA   HB2  H  N N 62  
ALA   HB3  H  N N 63  
ALA   HXT  H  N N 64  
ARG   N    N  N N 65  
ARG   CA   C  N S 66  
ARG   C    C  N N 67  
ARG   O    O  N N 68  
ARG   CB   C  N N 69  
ARG   CG   C  N N 70  
ARG   CD   C  N N 71  
ARG   NE   N  N N 72  
ARG   CZ   C  N N 73  
ARG   NH1  N  N N 74  
ARG   NH2  N  N N 75  
ARG   OXT  O  N N 76  
ARG   H    H  N N 77  
ARG   H2   H  N N 78  
ARG   HA   H  N N 79  
ARG   HB2  H  N N 80  
ARG   HB3  H  N N 81  
ARG   HG2  H  N N 82  
ARG   HG3  H  N N 83  
ARG   HD2  H  N N 84  
ARG   HD3  H  N N 85  
ARG   HE   H  N N 86  
ARG   HH11 H  N N 87  
ARG   HH12 H  N N 88  
ARG   HH21 H  N N 89  
ARG   HH22 H  N N 90  
ARG   HXT  H  N N 91  
ASN   N    N  N N 92  
ASN   CA   C  N S 93  
ASN   C    C  N N 94  
ASN   O    O  N N 95  
ASN   CB   C  N N 96  
ASN   CG   C  N N 97  
ASN   OD1  O  N N 98  
ASN   ND2  N  N N 99  
ASN   OXT  O  N N 100 
ASN   H    H  N N 101 
ASN   H2   H  N N 102 
ASN   HA   H  N N 103 
ASN   HB2  H  N N 104 
ASN   HB3  H  N N 105 
ASN   HD21 H  N N 106 
ASN   HD22 H  N N 107 
ASN   HXT  H  N N 108 
ASP   N    N  N N 109 
ASP   CA   C  N S 110 
ASP   C    C  N N 111 
ASP   O    O  N N 112 
ASP   CB   C  N N 113 
ASP   CG   C  N N 114 
ASP   OD1  O  N N 115 
ASP   OD2  O  N N 116 
ASP   OXT  O  N N 117 
ASP   H    H  N N 118 
ASP   H2   H  N N 119 
ASP   HA   H  N N 120 
ASP   HB2  H  N N 121 
ASP   HB3  H  N N 122 
ASP   HD2  H  N N 123 
ASP   HXT  H  N N 124 
CYS   N    N  N N 125 
CYS   CA   C  N R 126 
CYS   C    C  N N 127 
CYS   O    O  N N 128 
CYS   CB   C  N N 129 
CYS   SG   S  N N 130 
CYS   OXT  O  N N 131 
CYS   H    H  N N 132 
CYS   H2   H  N N 133 
CYS   HA   H  N N 134 
CYS   HB2  H  N N 135 
CYS   HB3  H  N N 136 
CYS   HG   H  N N 137 
CYS   HXT  H  N N 138 
GLN   N    N  N N 139 
GLN   CA   C  N S 140 
GLN   C    C  N N 141 
GLN   O    O  N N 142 
GLN   CB   C  N N 143 
GLN   CG   C  N N 144 
GLN   CD   C  N N 145 
GLN   OE1  O  N N 146 
GLN   NE2  N  N N 147 
GLN   OXT  O  N N 148 
GLN   H    H  N N 149 
GLN   H2   H  N N 150 
GLN   HA   H  N N 151 
GLN   HB2  H  N N 152 
GLN   HB3  H  N N 153 
GLN   HG2  H  N N 154 
GLN   HG3  H  N N 155 
GLN   HE21 H  N N 156 
GLN   HE22 H  N N 157 
GLN   HXT  H  N N 158 
GLU   N    N  N N 159 
GLU   CA   C  N S 160 
GLU   C    C  N N 161 
GLU   O    O  N N 162 
GLU   CB   C  N N 163 
GLU   CG   C  N N 164 
GLU   CD   C  N N 165 
GLU   OE1  O  N N 166 
GLU   OE2  O  N N 167 
GLU   OXT  O  N N 168 
GLU   H    H  N N 169 
GLU   H2   H  N N 170 
GLU   HA   H  N N 171 
GLU   HB2  H  N N 172 
GLU   HB3  H  N N 173 
GLU   HG2  H  N N 174 
GLU   HG3  H  N N 175 
GLU   HE2  H  N N 176 
GLU   HXT  H  N N 177 
GLY   N    N  N N 178 
GLY   CA   C  N N 179 
GLY   C    C  N N 180 
GLY   O    O  N N 181 
GLY   OXT  O  N N 182 
GLY   H    H  N N 183 
GLY   H2   H  N N 184 
GLY   HA2  H  N N 185 
GLY   HA3  H  N N 186 
GLY   HXT  H  N N 187 
HIS   N    N  N N 188 
HIS   CA   C  N S 189 
HIS   C    C  N N 190 
HIS   O    O  N N 191 
HIS   CB   C  N N 192 
HIS   CG   C  Y N 193 
HIS   ND1  N  Y N 194 
HIS   CD2  C  Y N 195 
HIS   CE1  C  Y N 196 
HIS   NE2  N  Y N 197 
HIS   OXT  O  N N 198 
HIS   H    H  N N 199 
HIS   H2   H  N N 200 
HIS   HA   H  N N 201 
HIS   HB2  H  N N 202 
HIS   HB3  H  N N 203 
HIS   HD1  H  N N 204 
HIS   HD2  H  N N 205 
HIS   HE1  H  N N 206 
HIS   HE2  H  N N 207 
HIS   HXT  H  N N 208 
HOH   O    O  N N 209 
HOH   H1   H  N N 210 
HOH   H2   H  N N 211 
ILE   N    N  N N 212 
ILE   CA   C  N S 213 
ILE   C    C  N N 214 
ILE   O    O  N N 215 
ILE   CB   C  N S 216 
ILE   CG1  C  N N 217 
ILE   CG2  C  N N 218 
ILE   CD1  C  N N 219 
ILE   OXT  O  N N 220 
ILE   H    H  N N 221 
ILE   H2   H  N N 222 
ILE   HA   H  N N 223 
ILE   HB   H  N N 224 
ILE   HG12 H  N N 225 
ILE   HG13 H  N N 226 
ILE   HG21 H  N N 227 
ILE   HG22 H  N N 228 
ILE   HG23 H  N N 229 
ILE   HD11 H  N N 230 
ILE   HD12 H  N N 231 
ILE   HD13 H  N N 232 
ILE   HXT  H  N N 233 
LEU   N    N  N N 234 
LEU   CA   C  N S 235 
LEU   C    C  N N 236 
LEU   O    O  N N 237 
LEU   CB   C  N N 238 
LEU   CG   C  N N 239 
LEU   CD1  C  N N 240 
LEU   CD2  C  N N 241 
LEU   OXT  O  N N 242 
LEU   H    H  N N 243 
LEU   H2   H  N N 244 
LEU   HA   H  N N 245 
LEU   HB2  H  N N 246 
LEU   HB3  H  N N 247 
LEU   HG   H  N N 248 
LEU   HD11 H  N N 249 
LEU   HD12 H  N N 250 
LEU   HD13 H  N N 251 
LEU   HD21 H  N N 252 
LEU   HD22 H  N N 253 
LEU   HD23 H  N N 254 
LEU   HXT  H  N N 255 
LYS   N    N  N N 256 
LYS   CA   C  N S 257 
LYS   C    C  N N 258 
LYS   O    O  N N 259 
LYS   CB   C  N N 260 
LYS   CG   C  N N 261 
LYS   CD   C  N N 262 
LYS   CE   C  N N 263 
LYS   NZ   N  N N 264 
LYS   OXT  O  N N 265 
LYS   H    H  N N 266 
LYS   H2   H  N N 267 
LYS   HA   H  N N 268 
LYS   HB2  H  N N 269 
LYS   HB3  H  N N 270 
LYS   HG2  H  N N 271 
LYS   HG3  H  N N 272 
LYS   HD2  H  N N 273 
LYS   HD3  H  N N 274 
LYS   HE2  H  N N 275 
LYS   HE3  H  N N 276 
LYS   HZ1  H  N N 277 
LYS   HZ2  H  N N 278 
LYS   HZ3  H  N N 279 
LYS   HXT  H  N N 280 
MET   N    N  N N 281 
MET   CA   C  N S 282 
MET   C    C  N N 283 
MET   O    O  N N 284 
MET   CB   C  N N 285 
MET   CG   C  N N 286 
MET   SD   S  N N 287 
MET   CE   C  N N 288 
MET   OXT  O  N N 289 
MET   H    H  N N 290 
MET   H2   H  N N 291 
MET   HA   H  N N 292 
MET   HB2  H  N N 293 
MET   HB3  H  N N 294 
MET   HG2  H  N N 295 
MET   HG3  H  N N 296 
MET   HE1  H  N N 297 
MET   HE2  H  N N 298 
MET   HE3  H  N N 299 
MET   HXT  H  N N 300 
PHE   N    N  N N 301 
PHE   CA   C  N S 302 
PHE   C    C  N N 303 
PHE   O    O  N N 304 
PHE   CB   C  N N 305 
PHE   CG   C  Y N 306 
PHE   CD1  C  Y N 307 
PHE   CD2  C  Y N 308 
PHE   CE1  C  Y N 309 
PHE   CE2  C  Y N 310 
PHE   CZ   C  Y N 311 
PHE   OXT  O  N N 312 
PHE   H    H  N N 313 
PHE   H2   H  N N 314 
PHE   HA   H  N N 315 
PHE   HB2  H  N N 316 
PHE   HB3  H  N N 317 
PHE   HD1  H  N N 318 
PHE   HD2  H  N N 319 
PHE   HE1  H  N N 320 
PHE   HE2  H  N N 321 
PHE   HZ   H  N N 322 
PHE   HXT  H  N N 323 
PRO   N    N  N N 324 
PRO   CA   C  N S 325 
PRO   C    C  N N 326 
PRO   O    O  N N 327 
PRO   CB   C  N N 328 
PRO   CG   C  N N 329 
PRO   CD   C  N N 330 
PRO   OXT  O  N N 331 
PRO   H    H  N N 332 
PRO   HA   H  N N 333 
PRO   HB2  H  N N 334 
PRO   HB3  H  N N 335 
PRO   HG2  H  N N 336 
PRO   HG3  H  N N 337 
PRO   HD2  H  N N 338 
PRO   HD3  H  N N 339 
PRO   HXT  H  N N 340 
SER   N    N  N N 341 
SER   CA   C  N S 342 
SER   C    C  N N 343 
SER   O    O  N N 344 
SER   CB   C  N N 345 
SER   OG   O  N N 346 
SER   OXT  O  N N 347 
SER   H    H  N N 348 
SER   H2   H  N N 349 
SER   HA   H  N N 350 
SER   HB2  H  N N 351 
SER   HB3  H  N N 352 
SER   HG   H  N N 353 
SER   HXT  H  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
ZN    ZN   ZN N N 442 
# 
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 
A1H1P N   S    sing N N 1   
A1H1P C   S    sing N N 2   
A1H1P C   C1   doub Y N 3   
A1H1P C1  C2   sing Y N 4   
A1H1P O   C2   sing N N 5   
A1H1P C3  O    sing N N 6   
A1H1P C2  C4   doub Y N 7   
A1H1P O1  C4   sing N N 8   
A1H1P C5  O1   sing N N 9   
A1H1P C4  C6   sing Y N 10  
A1H1P C7  C6   sing N N 11  
A1H1P N1  C7   sing N N 12  
A1H1P C8  N1   sing N N 13  
A1H1P C9  C8   sing N N 14  
A1H1P C9  C10  sing N N 15  
A1H1P C10 C11  sing N N 16  
A1H1P C11 C12  sing N N 17  
A1H1P C12 N2   sing N N 18  
A1H1P N2  C9   sing N N 19  
A1H1P C13 N2   sing N N 20  
A1H1P C14 C13  sing N N 21  
A1H1P C15 C14  doub N N 22  
A1H1P O2  C7   doub N N 23  
A1H1P C6  C16  doub Y N 24  
A1H1P C16 C    sing Y N 25  
A1H1P O3  S    doub N N 26  
A1H1P S   O4   doub N N 27  
A1H1P C1  H2   sing N N 28  
A1H1P N   H    sing N N 29  
A1H1P N   H1   sing N N 30  
A1H1P C16 H24  sing N N 31  
A1H1P C5  H7   sing N N 32  
A1H1P C5  H6   sing N N 33  
A1H1P C5  H8   sing N N 34  
A1H1P C3  H5   sing N N 35  
A1H1P C3  H3   sing N N 36  
A1H1P C3  H4   sing N N 37  
A1H1P N1  H9   sing N N 38  
A1H1P C8  H11  sing N N 39  
A1H1P C8  H10  sing N N 40  
A1H1P C9  H12  sing N N 41  
A1H1P C13 H20  sing N N 42  
A1H1P C13 H19  sing N N 43  
A1H1P C14 H21  sing N N 44  
A1H1P C15 H22  sing N N 45  
A1H1P C15 H23  sing N N 46  
A1H1P C12 H18  sing N N 47  
A1H1P C12 H17  sing N N 48  
A1H1P C11 H16  sing N N 49  
A1H1P C11 H15  sing N N 50  
A1H1P C10 H14  sing N N 51  
A1H1P C10 H13  sing N N 52  
ALA   N   CA   sing N N 53  
ALA   N   H    sing N N 54  
ALA   N   H2   sing N N 55  
ALA   CA  C    sing N N 56  
ALA   CA  CB   sing N N 57  
ALA   CA  HA   sing N N 58  
ALA   C   O    doub N N 59  
ALA   C   OXT  sing N N 60  
ALA   CB  HB1  sing N N 61  
ALA   CB  HB2  sing N N 62  
ALA   CB  HB3  sing N N 63  
ALA   OXT HXT  sing N N 64  
ARG   N   CA   sing N N 65  
ARG   N   H    sing N N 66  
ARG   N   H2   sing N N 67  
ARG   CA  C    sing N N 68  
ARG   CA  CB   sing N N 69  
ARG   CA  HA   sing N N 70  
ARG   C   O    doub N N 71  
ARG   C   OXT  sing N N 72  
ARG   CB  CG   sing N N 73  
ARG   CB  HB2  sing N N 74  
ARG   CB  HB3  sing N N 75  
ARG   CG  CD   sing N N 76  
ARG   CG  HG2  sing N N 77  
ARG   CG  HG3  sing N N 78  
ARG   CD  NE   sing N N 79  
ARG   CD  HD2  sing N N 80  
ARG   CD  HD3  sing N N 81  
ARG   NE  CZ   sing N N 82  
ARG   NE  HE   sing N N 83  
ARG   CZ  NH1  sing N N 84  
ARG   CZ  NH2  doub N N 85  
ARG   NH1 HH11 sing N N 86  
ARG   NH1 HH12 sing N N 87  
ARG   NH2 HH21 sing N N 88  
ARG   NH2 HH22 sing N N 89  
ARG   OXT HXT  sing N N 90  
ASN   N   CA   sing N N 91  
ASN   N   H    sing N N 92  
ASN   N   H2   sing N N 93  
ASN   CA  C    sing N N 94  
ASN   CA  CB   sing N N 95  
ASN   CA  HA   sing N N 96  
ASN   C   O    doub N N 97  
ASN   C   OXT  sing N N 98  
ASN   CB  CG   sing N N 99  
ASN   CB  HB2  sing N N 100 
ASN   CB  HB3  sing N N 101 
ASN   CG  OD1  doub N N 102 
ASN   CG  ND2  sing N N 103 
ASN   ND2 HD21 sing N N 104 
ASN   ND2 HD22 sing N N 105 
ASN   OXT HXT  sing N N 106 
ASP   N   CA   sing N N 107 
ASP   N   H    sing N N 108 
ASP   N   H2   sing N N 109 
ASP   CA  C    sing N N 110 
ASP   CA  CB   sing N N 111 
ASP   CA  HA   sing N N 112 
ASP   C   O    doub N N 113 
ASP   C   OXT  sing N N 114 
ASP   CB  CG   sing N N 115 
ASP   CB  HB2  sing N N 116 
ASP   CB  HB3  sing N N 117 
ASP   CG  OD1  doub N N 118 
ASP   CG  OD2  sing N N 119 
ASP   OD2 HD2  sing N N 120 
ASP   OXT HXT  sing N N 121 
CYS   N   CA   sing N N 122 
CYS   N   H    sing N N 123 
CYS   N   H2   sing N N 124 
CYS   CA  C    sing N N 125 
CYS   CA  CB   sing N N 126 
CYS   CA  HA   sing N N 127 
CYS   C   O    doub N N 128 
CYS   C   OXT  sing N N 129 
CYS   CB  SG   sing N N 130 
CYS   CB  HB2  sing N N 131 
CYS   CB  HB3  sing N N 132 
CYS   SG  HG   sing N N 133 
CYS   OXT HXT  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HIS   N   CA   sing N N 181 
HIS   N   H    sing N N 182 
HIS   N   H2   sing N N 183 
HIS   CA  C    sing N N 184 
HIS   CA  CB   sing N N 185 
HIS   CA  HA   sing N N 186 
HIS   C   O    doub N N 187 
HIS   C   OXT  sing N N 188 
HIS   CB  CG   sing N N 189 
HIS   CB  HB2  sing N N 190 
HIS   CB  HB3  sing N N 191 
HIS   CG  ND1  sing Y N 192 
HIS   CG  CD2  doub Y N 193 
HIS   ND1 CE1  doub Y N 194 
HIS   ND1 HD1  sing N N 195 
HIS   CD2 NE2  sing Y N 196 
HIS   CD2 HD2  sing N N 197 
HIS   CE1 NE2  sing Y N 198 
HIS   CE1 HE1  sing N N 199 
HIS   NE2 HE2  sing N N 200 
HIS   OXT HXT  sing N N 201 
HOH   O   H1   sing N N 202 
HOH   O   H2   sing N N 203 
ILE   N   CA   sing N N 204 
ILE   N   H    sing N N 205 
ILE   N   H2   sing N N 206 
ILE   CA  C    sing N N 207 
ILE   CA  CB   sing N N 208 
ILE   CA  HA   sing N N 209 
ILE   C   O    doub N N 210 
ILE   C   OXT  sing N N 211 
ILE   CB  CG1  sing N N 212 
ILE   CB  CG2  sing N N 213 
ILE   CB  HB   sing N N 214 
ILE   CG1 CD1  sing N N 215 
ILE   CG1 HG12 sing N N 216 
ILE   CG1 HG13 sing N N 217 
ILE   CG2 HG21 sing N N 218 
ILE   CG2 HG22 sing N N 219 
ILE   CG2 HG23 sing N N 220 
ILE   CD1 HD11 sing N N 221 
ILE   CD1 HD12 sing N N 222 
ILE   CD1 HD13 sing N N 223 
ILE   OXT HXT  sing N N 224 
LEU   N   CA   sing N N 225 
LEU   N   H    sing N N 226 
LEU   N   H2   sing N N 227 
LEU   CA  C    sing N N 228 
LEU   CA  CB   sing N N 229 
LEU   CA  HA   sing N N 230 
LEU   C   O    doub N N 231 
LEU   C   OXT  sing N N 232 
LEU   CB  CG   sing N N 233 
LEU   CB  HB2  sing N N 234 
LEU   CB  HB3  sing N N 235 
LEU   CG  CD1  sing N N 236 
LEU   CG  CD2  sing N N 237 
LEU   CG  HG   sing N N 238 
LEU   CD1 HD11 sing N N 239 
LEU   CD1 HD12 sing N N 240 
LEU   CD1 HD13 sing N N 241 
LEU   CD2 HD21 sing N N 242 
LEU   CD2 HD22 sing N N 243 
LEU   CD2 HD23 sing N N 244 
LEU   OXT HXT  sing N N 245 
LYS   N   CA   sing N N 246 
LYS   N   H    sing N N 247 
LYS   N   H2   sing N N 248 
LYS   CA  C    sing N N 249 
LYS   CA  CB   sing N N 250 
LYS   CA  HA   sing N N 251 
LYS   C   O    doub N N 252 
LYS   C   OXT  sing N N 253 
LYS   CB  CG   sing N N 254 
LYS   CB  HB2  sing N N 255 
LYS   CB  HB3  sing N N 256 
LYS   CG  CD   sing N N 257 
LYS   CG  HG2  sing N N 258 
LYS   CG  HG3  sing N N 259 
LYS   CD  CE   sing N N 260 
LYS   CD  HD2  sing N N 261 
LYS   CD  HD3  sing N N 262 
LYS   CE  NZ   sing N N 263 
LYS   CE  HE2  sing N N 264 
LYS   CE  HE3  sing N N 265 
LYS   NZ  HZ1  sing N N 266 
LYS   NZ  HZ2  sing N N 267 
LYS   NZ  HZ3  sing N N 268 
LYS   OXT HXT  sing N N 269 
MET   N   CA   sing N N 270 
MET   N   H    sing N N 271 
MET   N   H2   sing N N 272 
MET   CA  C    sing N N 273 
MET   CA  CB   sing N N 274 
MET   CA  HA   sing N N 275 
MET   C   O    doub N N 276 
MET   C   OXT  sing N N 277 
MET   CB  CG   sing N N 278 
MET   CB  HB2  sing N N 279 
MET   CB  HB3  sing N N 280 
MET   CG  SD   sing N N 281 
MET   CG  HG2  sing N N 282 
MET   CG  HG3  sing N N 283 
MET   SD  CE   sing N N 284 
MET   CE  HE1  sing N N 285 
MET   CE  HE2  sing N N 286 
MET   CE  HE3  sing N N 287 
MET   OXT HXT  sing N N 288 
PHE   N   CA   sing N N 289 
PHE   N   H    sing N N 290 
PHE   N   H2   sing N N 291 
PHE   CA  C    sing N N 292 
PHE   CA  CB   sing N N 293 
PHE   CA  HA   sing N N 294 
PHE   C   O    doub N N 295 
PHE   C   OXT  sing N N 296 
PHE   CB  CG   sing N N 297 
PHE   CB  HB2  sing N N 298 
PHE   CB  HB3  sing N N 299 
PHE   CG  CD1  doub Y N 300 
PHE   CG  CD2  sing Y N 301 
PHE   CD1 CE1  sing Y N 302 
PHE   CD1 HD1  sing N N 303 
PHE   CD2 CE2  doub Y N 304 
PHE   CD2 HD2  sing N N 305 
PHE   CE1 CZ   doub Y N 306 
PHE   CE1 HE1  sing N N 307 
PHE   CE2 CZ   sing Y N 308 
PHE   CE2 HE2  sing N N 309 
PHE   CZ  HZ   sing N N 310 
PHE   OXT HXT  sing N N 311 
PRO   N   CA   sing N N 312 
PRO   N   CD   sing N N 313 
PRO   N   H    sing N N 314 
PRO   CA  C    sing N N 315 
PRO   CA  CB   sing N N 316 
PRO   CA  HA   sing N N 317 
PRO   C   O    doub N N 318 
PRO   C   OXT  sing N N 319 
PRO   CB  CG   sing N N 320 
PRO   CB  HB2  sing N N 321 
PRO   CB  HB3  sing N N 322 
PRO   CG  CD   sing N N 323 
PRO   CG  HG2  sing N N 324 
PRO   CG  HG3  sing N N 325 
PRO   CD  HD2  sing N N 326 
PRO   CD  HD3  sing N N 327 
PRO   OXT HXT  sing N N 328 
SER   N   CA   sing N N 329 
SER   N   H    sing N N 330 
SER   N   H2   sing N N 331 
SER   CA  C    sing N N 332 
SER   CA  CB   sing N N 333 
SER   CA  HA   sing N N 334 
SER   C   O    doub N N 335 
SER   C   OXT  sing N N 336 
SER   CB  OG   sing N N 337 
SER   CB  HB2  sing N N 338 
SER   CB  HB3  sing N N 339 
SER   OG  HG   sing N N 340 
SER   OXT HXT  sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_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             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1JV0 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8RLO 
_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]   0.015838 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014035 
_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]   0.008254 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.pdbx_scat_Z 
_atom_type.pdbx_N_electrons 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C  6  6  2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
H  1  1  0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N  7  7  12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O  8  8  3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
S  16 16 6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 1.047   
ZN 30 30 14.082 3.266  7.036 0.233  5.165 10.316 2.411 58.710 1.019   
# 
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_site.calc_flag 
ATOM   1    N  N   . TRP   A 1 6   ? -15.463 25.883 52.769 1.000 44.955  ? 5   TRP   AAA N   1 ? 
ATOM   2    C  CA  . TRP   A 1 6   ? -14.911 25.537 51.397 1.000 38.777  ? 5   TRP   AAA CA  1 ? 
ATOM   3    C  C   . TRP   A 1 6   ? -13.591 26.287 51.158 1.000 34.121  ? 5   TRP   AAA C   1 ? 
ATOM   4    O  O   . TRP   A 1 6   ? -13.390 27.360 51.761 1.000 38.941  ? 5   TRP   AAA O   1 ? 
ATOM   5    C  CB  . TRP   A 1 6   ? -15.943 25.853 50.301 1.000 31.027  ? 5   TRP   AAA CB  1 ? 
ATOM   6    C  CG  . TRP   A 1 6   ? -16.195 27.316 50.088 1.000 29.011  ? 5   TRP   AAA CG  1 ? 
ATOM   7    C  CD1 . TRP   A 1 6   ? -17.178 28.050 50.639 1.000 35.852  ? 5   TRP   AAA CD1 1 ? 
ATOM   8    C  CD2 . TRP   A 1 6   ? -15.442 28.158 49.212 1.000 27.003  ? 5   TRP   AAA CD2 1 ? 
ATOM   9    N  NE1 . TRP   A 1 6   ? -17.086 29.354 50.180 1.000 30.677  ? 5   TRP   AAA NE1 1 ? 
ATOM   10   C  CE2 . TRP   A 1 6   ? -16.027 29.429 49.292 1.000 30.173  ? 5   TRP   AAA CE2 1 ? 
ATOM   11   C  CE3 . TRP   A 1 6   ? -14.333 27.943 48.378 1.000 30.622  ? 5   TRP   AAA CE3 1 ? 
ATOM   12   C  CZ2 . TRP   A 1 6   ? -15.513 30.478 48.544 1.000 26.523  ? 5   TRP   AAA CZ2 1 ? 
ATOM   13   C  CZ3 . TRP   A 1 6   ? -13.840 28.992 47.625 1.000 28.317  ? 5   TRP   AAA CZ3 1 ? 
ATOM   14   C  CH2 . TRP   A 1 6   ? -14.413 30.257 47.751 1.000 24.560  ? 5   TRP   AAA CH2 1 ? 
ATOM   15   N  N   . GLY   A 1 7   ? -12.704 25.724 50.337 1.000 34.812  ? 6   GLY   AAA N   1 ? 
ATOM   16   C  CA  . GLY   A 1 7   ? -11.410 26.330 49.995 1.000 35.129  ? 6   GLY   AAA CA  1 ? 
ATOM   17   C  C   . GLY   A 1 7   ? -10.933 25.822 48.658 1.000 36.777  ? 6   GLY   AAA C   1 ? 
ATOM   18   O  O   . GLY   A 1 7   ? -11.768 25.425 47.800 1.000 34.864  ? 6   GLY   AAA O   1 ? 
ATOM   19   N  N   . TYR   A 1 8   ? -9.618  25.805 48.508 1.000 34.712  ? 7   TYR   AAA N   1 ? 
ATOM   20   C  CA  . TYR   A 1 8   ? -8.908  25.239 47.341 1.000 39.172  ? 7   TYR   AAA CA  1 ? 
ATOM   21   C  C   . TYR   A 1 8   ? -7.955  24.147 47.849 1.000 43.299  ? 7   TYR   AAA C   1 ? 
ATOM   22   O  O   . TYR   A 1 8   ? -7.198  23.640 47.014 1.000 46.593  ? 7   TYR   AAA O   1 ? 
ATOM   23   C  CB  . TYR   A 1 8   ? -8.256  26.381 46.545 1.000 33.068  ? 7   TYR   AAA CB  1 ? 
ATOM   24   C  CG  . TYR   A 1 8   ? -9.250  27.290 45.865 1.000 28.776  ? 7   TYR   AAA CG  1 ? 
ATOM   25   C  CD1 . TYR   A 1 8   ? -9.812  26.974 44.637 1.000 32.904  ? 7   TYR   AAA CD1 1 ? 
ATOM   26   C  CD2 . TYR   A 1 8   ? -9.620  28.499 46.444 1.000 29.865  ? 7   TYR   AAA CD2 1 ? 
ATOM   27   C  CE1 . TYR   A 1 8   ? -10.727 27.817 44.013 1.000 29.067  ? 7   TYR   AAA CE1 1 ? 
ATOM   28   C  CE2 . TYR   A 1 8   ? -10.548 29.326 45.846 1.000 25.599  ? 7   TYR   AAA CE2 1 ? 
ATOM   29   C  CZ  . TYR   A 1 8   ? -11.100 29.004 44.619 1.000 26.145  ? 7   TYR   AAA CZ  1 ? 
ATOM   30   O  OH  . TYR   A 1 8   ? -11.972 29.836 43.974 1.000 25.838  ? 7   TYR   AAA OH  1 ? 
ATOM   31   N  N   . ASP   A 1 9   ? -7.985  23.790 49.149 1.000 44.971  ? 8   ASP   AAA N   1 ? 
ATOM   32   C  CA  . ASP   A 1 9   ? -7.240  22.612 49.702 1.000 47.798  ? 8   ASP   AAA CA  1 ? 
ATOM   33   C  C   . ASP   A 1 9   ? -7.808  21.350 49.064 1.000 49.950  ? 8   ASP   AAA C   1 ? 
ATOM   34   O  O   . ASP   A 1 9   ? -8.918  21.398 48.519 1.000 51.709  ? 8   ASP   AAA O   1 ? 
ATOM   35   C  CB  . ASP   A 1 9   ? -7.398  22.343 51.211 1.000 62.060  ? 8   ASP   AAA CB  1 ? 
ATOM   36   C  CG  . ASP   A 1 9   ? -6.874  23.393 52.181 1.000 76.120  ? 8   ASP   AAA CG  1 ? 
ATOM   37   O  OD1 . ASP   A 1 9   ? -6.914  24.609 51.850 1.000 92.514  ? 8   ASP   AAA OD1 1 ? 
ATOM   38   O  OD2 . ASP   A 1 9   ? -6.450  22.979 53.287 1.000 76.282  ? 8   ASP   AAA OD2 1 ? 
ATOM   39   N  N   . ASP   A 1 10  ? -7.100  20.244 49.200 1.000 58.839  ? 9   ASP   AAA N   1 ? 
ATOM   40   C  CA  . ASP   A 1 10  ? -7.632  18.930 48.753 1.000 60.615  ? 9   ASP   AAA CA  1 ? 
ATOM   41   C  C   . ASP   A 1 10  ? -8.883  18.593 49.583 1.000 53.920  ? 9   ASP   AAA C   1 ? 
ATOM   42   O  O   . ASP   A 1 10  ? -9.885  18.179 48.957 1.000 72.805  ? 9   ASP   AAA O   1 ? 
ATOM   43   C  CB  . ASP   A 1 10  ? -6.561  17.832 48.727 1.000 69.273  ? 9   ASP   AAA CB  1 ? 
ATOM   44   C  CG  . ASP   A 1 10  ? -5.633  17.819 49.917 1.000 88.465  ? 9   ASP   AAA CG  1 ? 
ATOM   45   O  OD1 . ASP   A 1 10  ? -6.013  18.375 50.961 1.000 110.895 ? 9   ASP   AAA OD1 1 ? 
ATOM   46   O  OD2 . ASP   A 1 10  ? -4.542  17.244 49.786 1.000 95.267  ? 9   ASP   AAA OD2 1 ? 
ATOM   47   N  N   . LYS   A 1 11  ? -8.863  18.788 50.914 1.000 58.965  ? 10  LYS   AAA N   1 ? 
ATOM   48   C  CA  . LYS   A 1 11  ? -9.977  18.372 51.824 1.000 51.474  ? 10  LYS   AAA CA  1 ? 
ATOM   49   C  C   . LYS   A 1 11  ? -11.244 19.232 51.614 1.000 43.508  ? 10  LYS   AAA C   1 ? 
ATOM   50   O  O   . LYS   A 1 11  ? -12.326 18.713 51.902 1.000 196.699 ? 10  LYS   AAA O   1 ? 
ATOM   51   C  CB  . LYS   A 1 11  ? -9.525  18.376 53.289 1.000 48.992  ? 10  LYS   AAA CB  1 ? 
ATOM   52   N  N   . ASN   A 1 12  ? -11.134 20.511 51.144 1.000 66.165  ? 11  ASN   AAA N   1 ? 
ATOM   53   C  CA  . ASN   A 1 12  ? -12.288 21.457 51.023 1.000 44.683  ? 11  ASN   AAA CA  1 ? 
ATOM   54   C  C   . ASN   A 1 12  ? -12.397 22.117 49.625 1.000 47.038  ? 11  ASN   AAA C   1 ? 
ATOM   55   O  O   . ASN   A 1 12  ? -13.149 23.144 49.467 1.000 37.719  ? 11  ASN   AAA O   1 ? 
ATOM   56   C  CB  . ASN   A 1 12  ? -12.149 22.519 52.101 1.000 45.689  ? 11  ASN   AAA CB  1 ? 
ATOM   57   C  CG  . ASN   A 1 12  ? -10.970 23.460 51.891 1.000 56.155  ? 11  ASN   AAA CG  1 ? 
ATOM   58   O  OD1 . ASN   A 1 12  ? -10.265 23.412 50.860 1.000 42.220  ? 11  ASN   AAA OD1 1 ? 
ATOM   59   N  ND2 . ASN   A 1 12  ? -10.785 24.361 52.854 1.000 42.949  ? 11  ASN   AAA ND2 1 ? 
ATOM   60   N  N   . GLY   A 1 13  ? -11.713 21.542 48.627 1.000 42.944  ? 12  GLY   AAA N   1 ? 
ATOM   61   C  CA  . GLY   A 1 13  ? -11.480 22.084 47.280 1.000 34.808  ? 12  GLY   AAA CA  1 ? 
ATOM   62   C  C   . GLY   A 1 13  ? -12.522 21.726 46.227 1.000 33.149  ? 12  GLY   AAA C   1 ? 
ATOM   63   O  O   . GLY   A 1 13  ? -13.499 21.016 46.470 1.000 40.820  ? 12  GLY   AAA O   1 ? 
ATOM   64   N  N   . PRO   A 1 14  ? -12.277 22.191 44.981 1.000 33.128  ? 13  PRO   AAA N   1 ? 
ATOM   65   C  CA  . PRO   A 1 14  ? -13.188 21.969 43.870 1.000 31.015  ? 13  PRO   AAA CA  1 ? 
ATOM   66   C  C   . PRO   A 1 14  ? -13.786 20.569 43.810 1.000 34.665  ? 13  PRO   AAA C   1 ? 
ATOM   67   O  O   . PRO   A 1 14  ? -14.971 20.489 43.557 1.000 42.772  ? 13  PRO   AAA O   1 ? 
ATOM   68   C  CB  . PRO   A 1 14  ? -12.260 22.207 42.691 1.000 32.839  ? 13  PRO   AAA CB  1 ? 
ATOM   69   C  CG  . PRO   A 1 14  ? -11.495 23.433 43.143 1.000 32.359  ? 13  PRO   AAA CG  1 ? 
ATOM   70   C  CD  . PRO   A 1 14  ? -11.213 23.148 44.607 1.000 35.460  ? 13  PRO   AAA CD  1 ? 
ATOM   71   N  N   . GLU   A 1 15  ? -12.991 19.531 44.043 1.000 43.108  ? 14  GLU   AAA N   1 ? 
ATOM   72   C  CA  . GLU   A 1 15  ? -13.459 18.129 43.853 1.000 45.243  ? 14  GLU   AAA CA  1 ? 
ATOM   73   C  C   . GLU   A 1 15  ? -14.449 17.733 44.961 1.000 39.436  ? 14  GLU   AAA C   1 ? 
ATOM   74   O  O   . GLU   A 1 15  ? -15.132 16.667 44.834 1.000 55.938  ? 14  GLU   AAA O   1 ? 
ATOM   75   C  CB  . GLU   A 1 15  ? -12.247 17.192 43.752 1.000 56.574  ? 14  GLU   AAA CB  1 ? 
ATOM   76   C  CG  . GLU   A 1 15  ? -11.316 17.547 42.601 1.000 65.201  ? 14  GLU   AAA CG  1 ? 
ATOM   77   C  CD  . GLU   A 1 15  ? -11.967 17.711 41.232 1.000 76.685  ? 14  GLU   AAA CD  1 ? 
ATOM   78   O  OE1 . GLU   A 1 15  ? -11.444 18.521 40.416 1.000 91.128  ? 14  GLU   AAA OE1 1 ? 
ATOM   79   O  OE2 . GLU   A 1 15  ? -12.984 17.020 40.971 1.000 88.385  ? 14  GLU   AAA OE2 1 ? 
ATOM   80   N  N   . GLN   A 1 16  ? -14.479 18.512 46.038 1.000 52.829  ? 15  GLN   AAA N   1 ? 
ATOM   81   C  CA  . GLN   A 1 16  ? -15.317 18.271 47.246 1.000 44.721  ? 15  GLN   AAA CA  1 ? 
ATOM   82   C  C   . GLN   A 1 16  ? -16.554 19.185 47.266 1.000 44.756  ? 15  GLN   AAA C   1 ? 
ATOM   83   O  O   . GLN   A 1 16  ? -17.523 18.851 47.972 1.000 38.118  ? 15  GLN   AAA O   1 ? 
ATOM   84   C  CB  . GLN   A 1 16  ? -14.488 18.530 48.506 1.000 55.065  ? 15  GLN   AAA CB  1 ? 
ATOM   85   C  CG  . GLN   A 1 16  ? -13.098 17.913 48.472 1.000 63.863  ? 15  GLN   AAA CG  1 ? 
ATOM   86   C  CD  . GLN   A 1 16  ? -13.112 16.403 48.487 1.000 81.272  ? 15  GLN   AAA CD  1 ? 
ATOM   87   O  OE1 . GLN   A 1 16  ? -14.168 15.758 48.390 1.000 70.835  ? 15  GLN   AAA OE1 1 ? 
ATOM   88   N  NE2 . GLN   A 1 16  ? -11.921 15.826 48.613 1.000 89.758  ? 15  GLN   AAA NE2 1 ? 
ATOM   89   N  N   . TRP   A 1 17  ? -16.540 20.329 46.569 1.000 35.279  ? 16  TRP   AAA N   1 ? 
ATOM   90   C  CA  . TRP   A 1 17  ? -17.623 21.336 46.740 1.000 35.700  ? 16  TRP   AAA CA  1 ? 
ATOM   91   C  C   . TRP   A 1 17  ? -19.019 20.712 46.572 1.000 32.405  ? 16  TRP   AAA C   1 ? 
ATOM   92   O  O   . TRP   A 1 17  ? -19.921 21.223 47.184 1.000 32.966  ? 16  TRP   AAA O   1 ? 
ATOM   93   C  CB  . TRP   A 1 17  ? -17.440 22.536 45.812 1.000 31.039  ? 16  TRP   AAA CB  1 ? 
ATOM   94   C  CG  . TRP   A 1 17  ? -16.204 23.323 46.059 1.000 26.492  ? 16  TRP   AAA CG  1 ? 
ATOM   95   C  CD1 . TRP   A 1 17  ? -15.447 23.389 47.188 1.000 31.409  ? 16  TRP   AAA CD1 1 ? 
ATOM   96   C  CD2 . TRP   A 1 17  ? -15.633 24.256 45.124 1.000 29.783  ? 16  TRP   AAA CD2 1 ? 
ATOM   97   N  NE1 . TRP   A 1 17  ? -14.431 24.300 47.019 1.000 30.056  ? 16  TRP   AAA NE1 1 ? 
ATOM   98   C  CE2 . TRP   A 1 17  ? -14.512 24.830 45.756 1.000 29.768  ? 16  TRP   AAA CE2 1 ? 
ATOM   99   C  CE3 . TRP   A 1 17  ? -15.949 24.622 43.814 1.000 26.647  ? 16  TRP   AAA CE3 1 ? 
ATOM   100  C  CZ2 . TRP   A 1 17  ? -13.730 25.792 45.129 1.000 28.955  ? 16  TRP   AAA CZ2 1 ? 
ATOM   101  C  CZ3 . TRP   A 1 17  ? -15.170 25.570 43.194 1.000 28.294  ? 16  TRP   AAA CZ3 1 ? 
ATOM   102  C  CH2 . TRP   A 1 17  ? -14.064 26.125 43.839 1.000 27.462  ? 16  TRP   AAA CH2 1 ? 
ATOM   103  N  N   . SER   A 1 18  ? -19.207 19.633 45.796 1.000 34.234  ? 17  SER   AAA N   1 ? 
ATOM   104  C  CA  . SER   A 1 18  ? -20.579 19.140 45.461 1.000 35.438  ? 17  SER   AAA CA  1 ? 
ATOM   105  C  C   . SER   A 1 18  ? -21.295 18.569 46.724 1.000 36.140  ? 17  SER   AAA C   1 ? 
ATOM   106  O  O   . SER   A 1 18  ? -22.627 18.443 46.728 1.000 45.614  ? 17  SER   AAA O   1 ? 
ATOM   107  C  CB  . SER   A 1 18  ? -20.574 18.129 44.309 1.000 39.732  ? 17  SER   AAA CB  1 ? 
ATOM   108  O  OG  . SER   A 1 18  ? -20.013 16.908 44.736 1.000 36.494  ? 17  SER   AAA OG  1 ? 
ATOM   109  N  N   . LYS   A 1 19  ? -20.506 18.225 47.773 1.000 36.748  ? 18  LYS   AAA N   1 ? 
ATOM   110  C  CA  . LYS   A 1 19  ? -21.096 17.628 48.999 1.000 38.946  ? 18  LYS   AAA CA  1 ? 
ATOM   111  C  C   . LYS   A 1 19  ? -21.964 18.683 49.685 1.000 39.197  ? 18  LYS   AAA C   1 ? 
ATOM   112  O  O   . LYS   A 1 19  ? -23.017 18.356 50.158 1.000 50.482  ? 18  LYS   AAA O   1 ? 
ATOM   113  C  CB  . LYS   A 1 19  ? -20.006 17.088 49.920 1.000 48.383  ? 18  LYS   AAA CB  1 ? 
ATOM   114  C  CG  . LYS   A 1 19  ? -19.134 16.004 49.300 1.000 58.663  ? 18  LYS   AAA CG  1 ? 
ATOM   115  C  CD  . LYS   A 1 19  ? -17.837 15.800 50.056 1.000 68.404  ? 18  LYS   AAA CD  1 ? 
ATOM   116  C  CE  . LYS   A 1 19  ? -17.109 14.531 49.683 1.000 63.963  ? 18  LYS   AAA CE  1 ? 
ATOM   117  N  NZ  . LYS   A 1 19  ? -15.867 14.401 50.483 1.000 76.343  ? 18  LYS   AAA NZ  1 ? 
ATOM   118  N  N   . LEU   A 1 20  ? -21.551 19.961 49.680 1.000 46.684  ? 19  LEU   AAA N   1 ? 
ATOM   119  C  CA  . LEU   A 1 20  ? -22.314 21.045 50.364 1.000 39.405  ? 19  LEU   AAA CA  1 ? 
ATOM   120  C  C   . LEU   A 1 20  ? -23.111 21.835 49.318 1.000 33.328  ? 19  LEU   AAA C   1 ? 
ATOM   121  O  O   . LEU   A 1 20  ? -24.191 22.333 49.666 1.000 35.372  ? 19  LEU   AAA O   1 ? 
ATOM   122  C  CB  . LEU   A 1 20  ? -21.372 21.936 51.189 1.000 55.920  ? 19  LEU   AAA CB  1 ? 
ATOM   123  C  CG  . LEU   A 1 20  ? -19.956 21.403 51.469 1.000 73.776  ? 19  LEU   AAA CG  1 ? 
ATOM   124  C  CD1 . LEU   A 1 20  ? -18.950 22.052 50.521 1.000 98.747  ? 19  LEU   AAA CD1 1 ? 
ATOM   125  C  CD2 . LEU   A 1 20  ? -19.523 21.638 52.918 1.000 60.286  ? 19  LEU   AAA CD2 1 ? 
ATOM   126  N  N   . TYR   A 1 21  ? -22.633 21.871 48.076 1.000 31.376  ? 20  TYR   AAA N   1 ? 
ATOM   127  C  CA  . TYR   A 1 21  ? -23.256 22.607 46.938 1.000 28.123  ? 20  TYR   AAA CA  1 ? 
ATOM   128  C  C   . TYR   A 1 21  ? -23.491 21.714 45.728 1.000 43.302  ? 20  TYR   AAA C   1 ? 
ATOM   129  O  O   . TYR   A 1 21  ? -22.694 21.707 44.771 1.000 48.792  ? 20  TYR   AAA O   1 ? 
ATOM   130  C  CB  . TYR   A 1 21  ? -22.374 23.792 46.553 1.000 33.448  ? 20  TYR   AAA CB  1 ? 
ATOM   131  C  CG  . TYR   A 1 21  ? -22.136 24.703 47.730 1.000 35.665  ? 20  TYR   AAA CG  1 ? 
ATOM   132  C  CD1 . TYR   A 1 21  ? -23.094 25.637 48.098 1.000 41.775  ? 20  TYR   AAA CD1 1 ? 
ATOM   133  C  CD2 . TYR   A 1 21  ? -20.994 24.616 48.518 1.000 32.871  ? 20  TYR   AAA CD2 1 ? 
ATOM   134  C  CE1 . TYR   A 1 21  ? -22.900 26.504 49.162 1.000 37.943  ? 20  TYR   AAA CE1 1 ? 
ATOM   135  C  CE2 . TYR   A 1 21  ? -20.805 25.452 49.609 1.000 36.377  ? 20  TYR   AAA CE2 1 ? 
ATOM   136  C  CZ  . TYR   A 1 21  ? -21.753 26.405 49.924 1.000 37.653  ? 20  TYR   AAA CZ  1 ? 
ATOM   137  O  OH  . TYR   A 1 21  ? -21.589 27.221 51.001 1.000 48.941  ? 20  TYR   AAA OH  1 ? 
ATOM   138  N  N   . PRO   A 1 22  ? -24.582 20.906 45.761 1.000 32.215  ? 21  PRO   AAA N   1 ? 
ATOM   139  C  CA  . PRO   A 1 22  ? -24.791 19.861 44.742 1.000 42.606  ? 21  PRO   AAA CA  1 ? 
ATOM   140  C  C   . PRO   A 1 22  ? -24.896 20.426 43.320 1.000 33.858  ? 21  PRO   AAA C   1 ? 
ATOM   141  O  O   . PRO   A 1 22  ? -24.628 19.718 42.449 1.000 45.210  ? 21  PRO   AAA O   1 ? 
ATOM   142  C  CB  . PRO   A 1 22  ? -26.129 19.285 45.221 1.000 38.932  ? 21  PRO   AAA CB  1 ? 
ATOM   143  C  CG  . PRO   A 1 22  ? -26.015 19.369 46.712 1.000 42.498  ? 21  PRO   AAA CG  1 ? 
ATOM   144  C  CD  . PRO   A 1 22  ? -25.578 20.847 46.849 1.000 36.588  ? 21  PRO   AAA CD  1 ? 
ATOM   145  N  N   . ILE   A 1 23  ? -25.184 21.756 43.165 1.000 30.782  ? 22  ILE   AAA N   1 ? 
ATOM   146  C  CA  . ILE   A 1 23  ? -25.187 22.435 41.834 1.000 30.558  ? 22  ILE   AAA CA  1 ? 
ATOM   147  C  C   . ILE   A 1 23  ? -23.798 22.338 41.166 1.000 27.680  ? 22  ILE   AAA C   1 ? 
ATOM   148  O  O   . ILE   A 1 23  ? -23.696 22.613 39.937 1.000 34.650  ? 22  ILE   AAA O   1 ? 
ATOM   149  C  CB  . ILE   A 1 23  ? -25.642 23.906 41.956 1.000 28.583  ? 22  ILE   AAA CB  1 ? 
ATOM   150  C  CG1 . ILE   A 1 23  ? -26.099 24.466 40.598 1.000 32.231  ? 22  ILE   AAA CG1 1 ? 
ATOM   151  C  CG2 . ILE   A 1 23  ? -24.534 24.752 42.580 1.000 32.111  ? 22  ILE   AAA CG2 1 ? 
ATOM   152  C  CD1 . ILE   A 1 23  ? -27.375 23.854 39.988 1.000 36.187  ? 22  ILE   AAA CD1 1 ? 
ATOM   153  N  N   . ALA   A 1 24  ? -22.731 22.037 41.907 1.000 30.860  ? 23  ALA   AAA N   1 ? 
ATOM   154  C  CA  . ALA   A 1 24  ? -21.348 21.902 41.370 1.000 31.302  ? 23  ALA   AAA CA  1 ? 
ATOM   155  C  C   . ALA   A 1 24  ? -21.363 20.945 40.180 1.000 34.987  ? 23  ALA   AAA C   1 ? 
ATOM   156  O  O   . ALA   A 1 24  ? -20.508 21.076 39.294 1.000 37.077  ? 23  ALA   AAA O   1 ? 
ATOM   157  C  CB  . ALA   A 1 24  ? -20.381 21.425 42.433 1.000 30.704  ? 23  ALA   AAA CB  1 ? 
ATOM   158  N  N   . ASN   A 1 25  ? -22.320 20.019 40.158 1.000 37.425  ? 24  ASN   AAA N   1 ? 
ATOM   159  C  CA  . ASN   A 1 25  ? -22.447 19.033 39.067 1.000 35.385  ? 24  ASN   AAA CA  1 ? 
ATOM   160  C  C   . ASN   A 1 25  ? -23.624 19.412 38.158 1.000 36.769  ? 24  ASN   AAA C   1 ? 
ATOM   161  O  O   . ASN   A 1 25  ? -24.117 18.486 37.479 1.000 42.049  ? 24  ASN   AAA O   1 ? 
ATOM   162  C  CB  . ASN   A 1 25  ? -22.621 17.624 39.633 1.000 34.818  ? 24  ASN   AAA CB  1 ? 
ATOM   163  C  CG  . ASN   A 1 25  ? -21.469 17.146 40.510 1.000 42.487  ? 24  ASN   AAA CG  1 ? 
ATOM   164  O  OD1 . ASN   A 1 25  ? -21.704 16.477 41.523 1.000 42.884  ? 24  ASN   AAA OD1 1 ? 
ATOM   165  N  ND2 . ASN   A 1 25  ? -20.220 17.423 40.130 1.000 44.671  ? 24  ASN   AAA ND2 1 ? 
ATOM   166  N  N   . GLY   A 1 26  ? -24.005 20.706 38.128 1.000 32.500  ? 25  GLY   AAA N   1 ? 
ATOM   167  C  CA  . GLY   A 1 26  ? -25.134 21.254 37.346 1.000 35.480  ? 25  GLY   AAA CA  1 ? 
ATOM   168  C  C   . GLY   A 1 26  ? -24.834 21.335 35.845 1.000 29.221  ? 25  GLY   AAA C   1 ? 
ATOM   169  O  O   . GLY   A 1 26  ? -23.739 20.908 35.403 1.000 32.936  ? 25  GLY   AAA O   1 ? 
ATOM   170  N  N   . ASN   A 1 27  ? -25.788 21.824 35.053 1.000 29.936  ? 26  ASN   AAA N   1 ? 
ATOM   171  C  CA  . ASN   A 1 27  ? -25.702 21.924 33.572 1.000 31.772  ? 26  ASN   AAA CA  1 ? 
ATOM   172  C  C   . ASN   A 1 27  ? -25.134 23.264 33.118 1.000 30.201  ? 26  ASN   AAA C   1 ? 
ATOM   173  O  O   . ASN   A 1 27  ? -24.889 23.422 31.883 1.000 33.687  ? 26  ASN   AAA O   1 ? 
ATOM   174  C  CB  . ASN   A 1 27  ? -27.080 21.720 32.948 1.000 33.646  ? 26  ASN   AAA CB  1 ? 
ATOM   175  C  CG  . ASN   A 1 27  ? -27.546 20.302 33.203 1.000 38.588  ? 26  ASN   AAA CG  1 ? 
ATOM   176  O  OD1 . ASN   A 1 27  ? -26.745 19.357 33.235 1.000 51.477  ? 26  ASN   AAA OD1 1 ? 
ATOM   177  N  ND2 . ASN   A 1 27  ? -28.833 20.150 33.438 1.000 44.063  ? 26  ASN   AAA ND2 1 ? 
ATOM   178  N  N   . ASN   A 1 28  ? -24.931 24.205 34.040 1.000 30.287  ? 27  ASN   AAA N   1 ? 
ATOM   179  C  CA  . ASN   A 1 28  ? -24.474 25.567 33.646 1.000 29.668  ? 27  ASN   AAA CA  1 ? 
ATOM   180  C  C   . ASN   A 1 28  ? -23.304 25.950 34.513 1.000 26.365  ? 27  ASN   AAA C   1 ? 
ATOM   181  O  O   . ASN   A 1 28  ? -23.265 27.159 34.883 1.000 27.272  ? 27  ASN   AAA O   1 ? 
ATOM   182  C  CB  . ASN   A 1 28  ? -25.576 26.632 33.716 1.000 30.279  ? 27  ASN   AAA CB  1 ? 
ATOM   183  C  CG  . ASN   A 1 28  ? -26.761 26.303 32.836 1.000 31.256  ? 27  ASN   AAA CG  1 ? 
ATOM   184  O  OD1 . ASN   A 1 28  ? -26.827 26.727 31.690 1.000 43.614  ? 27  ASN   AAA OD1 1 ? 
ATOM   185  N  ND2 . ASN   A 1 28  ? -27.711 25.569 33.377 1.000 33.843  ? 27  ASN   AAA ND2 1 ? 
ATOM   186  N  N   . GLN   A 1 29  ? -22.325 25.069 34.701 1.000 27.136  ? 28  GLN   AAA N   1 ? 
ATOM   187  C  CA  . GLN   A 1 29  ? -21.165 25.358 35.594 1.000 28.303  ? 28  GLN   AAA CA  1 ? 
ATOM   188  C  C   . GLN   A 1 29  ? -20.026 26.032 34.833 1.000 25.639  ? 28  GLN   AAA C   1 ? 
ATOM   189  O  O   . GLN   A 1 29  ? -19.908 25.891 33.618 1.000 27.487  ? 28  GLN   AAA O   1 ? 
ATOM   190  C  CB  . GLN   A 1 29  ? -20.693 24.120 36.333 1.000 27.247  ? 28  GLN   AAA CB  1 ? 
ATOM   191  C  CG  . GLN   A 1 29  ? -21.686 23.705 37.412 1.000 30.445  ? 28  GLN   AAA CG  1 ? 
ATOM   192  C  CD  . GLN   A 1 29  ? -21.744 24.698 38.534 1.000 26.008  ? 28  GLN   AAA CD  1 ? 
ATOM   193  O  OE1 . GLN   A 1 29  ? -20.779 24.806 39.296 1.000 28.952  ? 28  GLN   AAA OE1 1 ? 
ATOM   194  N  NE2 . GLN   A 1 29  ? -22.891 25.382 38.664 1.000 26.681  ? 28  GLN   AAA NE2 1 ? 
ATOM   195  N  N   . SER   A 1 30  ? -19.273 26.847 35.558 1.000 26.996  ? 29  SER   AAA N   1 ? 
ATOM   196  C  CA  . SER   A 1 30  ? -18.130 27.594 35.003 1.000 23.628  ? 29  SER   AAA CA  1 ? 
ATOM   197  C  C   . SER   A 1 30  ? -16.911 27.316 35.854 1.000 24.657  ? 29  SER   AAA C   1 ? 
ATOM   198  O  O   . SER   A 1 30  ? -17.046 27.069 37.063 1.000 25.333  ? 29  SER   AAA O   1 ? 
ATOM   199  C  CB  . SER   A 1 30  ? -18.403 29.125 34.966 1.000 24.782  ? 29  SER   AAA CB  1 ? 
ATOM   200  O  OG  . SER   A 1 30  ? -19.479 29.422 34.099 1.000 23.801  ? 29  SER   AAA OG  1 ? 
ATOM   201  N  N   . PRO   A 1 31  ? -15.676 27.426 35.313 1.000 23.180  ? 30  PRO   AAA N   1 ? 
ATOM   202  C  CA  . PRO   A 1 31  ? -15.408 27.826 33.940 1.000 23.718  ? 30  PRO   AAA CA  1 ? 
ATOM   203  C  C   . PRO   A 1 31  ? -15.487 26.663 32.942 1.000 27.972  ? 30  PRO   AAA C   1 ? 
ATOM   204  O  O   . PRO   A 1 31  ? -15.776 25.498 33.322 1.000 27.056  ? 30  PRO   AAA O   1 ? 
ATOM   205  C  CB  . PRO   A 1 31  ? -13.957 28.271 34.060 1.000 25.145  ? 30  PRO   AAA CB  1 ? 
ATOM   206  C  CG  . PRO   A 1 31  ? -13.373 27.255 35.021 1.000 26.271  ? 30  PRO   AAA CG  1 ? 
ATOM   207  C  CD  . PRO   A 1 31  ? -14.441 27.129 36.059 1.000 27.880  ? 30  PRO   AAA CD  1 ? 
ATOM   208  N  N   . VAL   A 1 32  ? -15.221 27.001 31.689 1.000 24.494  ? 31  VAL   AAA N   1 ? 
ATOM   209  C  CA  . VAL   A 1 32  ? -15.262 26.005 30.587 1.000 29.050  ? 31  VAL   AAA CA  1 ? 
ATOM   210  C  C   . VAL   A 1 32  ? -14.039 26.183 29.702 1.000 26.468  ? 31  VAL   AAA C   1 ? 
ATOM   211  O  O   . VAL   A 1 32  ? -13.373 27.299 29.741 1.000 25.827  ? 31  VAL   AAA O   1 ? 
ATOM   212  C  CB  . VAL   A 1 32  ? -16.569 26.123 29.782 1.000 25.657  ? 31  VAL   AAA CB  1 ? 
ATOM   213  C  CG1 . VAL   A 1 32  ? -17.766 25.930 30.672 1.000 24.507  ? 31  VAL   AAA CG1 1 ? 
ATOM   214  C  CG2 . VAL   A 1 32  ? -16.675 27.411 28.974 1.000 28.310  ? 31  VAL   AAA CG2 1 ? 
ATOM   215  N  N   . ASP   A 1 33  ? -13.788 25.157 28.909 1.000 25.571  ? 32  ASP   AAA N   1 ? 
ATOM   216  C  CA  . ASP   A 1 33  ? -12.864 25.184 27.755 1.000 24.836  ? 32  ASP   AAA CA  1 ? 
ATOM   217  C  C   . ASP   A 1 33  ? -13.622 25.695 26.536 1.000 27.185  ? 32  ASP   AAA C   1 ? 
ATOM   218  O  O   . ASP   A 1 33  ? -14.619 25.071 26.153 1.000 30.252  ? 32  ASP   AAA O   1 ? 
ATOM   219  C  CB  . ASP   A 1 33  ? -12.248 23.807 27.516 1.000 28.534  ? 32  ASP   AAA CB  1 ? 
ATOM   220  C  CG  . ASP   A 1 33  ? -11.207 23.829 26.395 1.000 29.512  ? 32  ASP   AAA CG  1 ? 
ATOM   221  O  OD1 . ASP   A 1 33  ? -10.331 24.741 26.358 1.000 30.841  ? 32  ASP   AAA OD1 1 ? 
ATOM   222  O  OD2 . ASP   A 1 33  ? -11.316 23.017 25.513 1.000 33.971  ? 32  ASP   AAA OD2 1 ? 
ATOM   223  N  N   . ILE   A 1 34  ? -13.210 26.853 26.004 1.000 27.445  ? 33  ILE   AAA N   1 ? 
ATOM   224  C  CA  . ILE   A 1 34  ? -13.799 27.394 24.762 1.000 25.301  ? 33  ILE   AAA CA  1 ? 
ATOM   225  C  C   . ILE   A 1 34  ? -13.124 26.701 23.585 1.000 28.839  ? 33  ILE   AAA C   1 ? 
ATOM   226  O  O   . ILE   A 1 34  ? -11.921 26.967 23.330 1.000 29.635  ? 33  ILE   AAA O   1 ? 
ATOM   227  C  CB  . ILE   A 1 34  ? -13.660 28.941 24.724 1.000 26.698  ? 33  ILE   AAA CB  1 ? 
ATOM   228  C  CG1 . ILE   A 1 34  ? -14.423 29.570 25.890 1.000 27.593  ? 33  ILE   AAA CG1 1 ? 
ATOM   229  C  CG2 . ILE   A 1 34  ? -14.068 29.479 23.364 1.000 28.687  ? 33  ILE   AAA CG2 1 ? 
ATOM   230  C  CD1 . ILE   A 1 34  ? -14.315 31.052 25.951 1.000 34.218  ? 33  ILE   AAA CD1 1 ? 
ATOM   231  N  N   . LYS   A 1 35  ? -13.854 25.836 22.874 1.000 30.057  ? 34  LYS   AAA N   1 ? 
ATOM   232  C  CA  . LYS   A 1 35  ? -13.333 25.235 21.617 1.000 32.697  ? 34  LYS   AAA CA  1 ? 
ATOM   233  C  C   . LYS   A 1 35  ? -13.741 26.102 20.426 1.000 28.339  ? 34  LYS   AAA C   1 ? 
ATOM   234  O  O   . LYS   A 1 35  ? -14.964 26.141 20.099 1.000 34.188  ? 34  LYS   AAA O   1 ? 
ATOM   235  C  CB  . LYS   A 1 35  ? -13.822 23.802 21.452 1.000 34.574  ? 34  LYS   AAA CB  1 ? 
ATOM   236  C  CG  . LYS   A 1 35  ? -13.299 22.858 22.510 1.000 40.446  ? 34  LYS   AAA CG  1 ? 
ATOM   237  C  CD  . LYS   A 1 35  ? -13.899 21.466 22.443 1.000 46.202  ? 34  LYS   AAA CD  1 ? 
ATOM   238  C  CE  . LYS   A 1 35  ? -13.385 20.603 23.572 1.000 53.042  ? 34  LYS   AAA CE  1 ? 
ATOM   239  N  NZ  . LYS   A 1 35  ? -13.387 21.351 24.866 1.000 45.959  ? 34  LYS   AAA NZ  1 ? 
ATOM   240  N  N   . THR   A 1 36  ? -12.762 26.723 19.771 1.000 27.466  ? 35  THR   AAA N   1 ? 
ATOM   241  C  CA  . THR   A 1 36  ? -13.030 27.762 18.743 1.000 32.182  ? 35  THR   AAA CA  1 ? 
ATOM   242  C  C   . THR   A 1 36  ? -13.716 27.133 17.527 1.000 32.475  ? 35  THR   AAA C   1 ? 
ATOM   243  O  O   . THR   A 1 36  ? -14.506 27.844 16.886 1.000 36.945  ? 35  THR   AAA O   1 ? 
ATOM   244  C  CB  . THR   A 1 36  ? -11.778 28.598 18.423 1.000 34.227  ? 35  THR   AAA CB  1 ? 
ATOM   245  O  OG1 . THR   A 1 36  ? -10.655 27.783 18.104 1.000 34.083  ? 35  THR   AAA OG1 1 ? 
ATOM   246  C  CG2 . THR   A 1 36  ? -11.413 29.514 19.572 1.000 36.217  ? 35  THR   AAA CG2 1 ? 
ATOM   247  N  N   . SER   A 1 37  ? -13.492 25.847 17.243 1.000 34.046  ? 36  SER   AAA N   1 ? 
ATOM   248  C  CA  . SER   A 1 37  ? -14.124 25.163 16.082 1.000 35.396  ? 36  SER   AAA CA  1 ? 
ATOM   249  C  C   . SER   A 1 37  ? -15.620 24.931 16.350 1.000 36.868  ? 36  SER   AAA C   1 ? 
ATOM   250  O  O   . SER   A 1 37  ? -16.319 24.696 15.364 1.000 38.247  ? 36  SER   AAA O   1 ? 
ATOM   251  C  CB  . SER   A 1 37  ? -13.418 23.878 15.780 1.000 34.738  ? 36  SER   AAA CB  1 ? 
ATOM   252  O  OG  . SER   A 1 37  ? -13.649 22.925 16.815 1.000 40.613  ? 36  SER   AAA OG  1 ? 
ATOM   253  N  N   . GLU   A 1 38  ? -16.062 24.990 17.631 1.000 35.510  ? 37  GLU   AAA N   1 ? 
ATOM   254  C  CA  . GLU   A 1 38  ? -17.456 24.718 18.065 1.000 39.233  ? 37  GLU   AAA CA  1 ? 
ATOM   255  C  C   . GLU   A 1 38  ? -18.204 26.026 18.437 1.000 35.851  ? 37  GLU   AAA C   1 ? 
ATOM   256  O  O   . GLU   A 1 38  ? -19.415 25.946 18.669 1.000 40.333  ? 37  GLU   AAA O   1 ? 
ATOM   257  C  CB  . GLU   A 1 38  ? -17.425 23.670 19.193 1.000 40.312  ? 37  GLU   AAA CB  1 ? 
ATOM   258  C  CG  . GLU   A 1 38  ? -16.714 22.357 18.830 1.000 47.000  ? 37  GLU   AAA CG  1 ? 
ATOM   259  C  CD  . GLU   A 1 38  ? -16.891 21.191 19.807 1.000 55.260  ? 37  GLU   AAA CD  1 ? 
ATOM   260  O  OE1 . GLU   A 1 38  ? -17.652 21.328 20.768 1.000 59.247  ? 37  GLU   AAA OE1 1 ? 
ATOM   261  O  OE2 . GLU   A 1 38  ? -16.257 20.129 19.614 1.000 74.369  ? 37  GLU   AAA OE2 1 ? 
ATOM   262  N  N   . THR   A 1 39  ? -17.566 27.206 18.452 1.000 34.554  ? 38  THR   AAA N   1 ? 
ATOM   263  C  CA  . THR   A 1 39  ? -18.243 28.501 18.767 1.000 35.011  ? 38  THR   AAA CA  1 ? 
ATOM   264  C  C   . THR   A 1 39  ? -19.147 28.931 17.600 1.000 39.986  ? 38  THR   AAA C   1 ? 
ATOM   265  O  O   . THR   A 1 39  ? -18.822 28.643 16.438 1.000 46.246  ? 38  THR   AAA O   1 ? 
ATOM   266  C  CB  . THR   A 1 39  ? -17.246 29.628 19.081 1.000 37.153  ? 38  THR   AAA CB  1 ? 
ATOM   267  O  OG1 . THR   A 1 39  ? -16.408 29.804 17.935 1.000 40.937  ? 38  THR   AAA OG1 1 ? 
ATOM   268  C  CG2 . THR   A 1 39  ? -16.421 29.351 20.324 1.000 36.317  ? 38  THR   AAA CG2 1 ? 
ATOM   269  N  N   . LYS   A 1 40  ? -20.272 29.579 17.866 1.000 37.782  ? 39  LYS   AAA N   1 ? 
ATOM   270  C  CA  . LYS   A 1 40  ? -21.162 30.029 16.766 1.000 37.876  ? 39  LYS   AAA CA  1 ? 
ATOM   271  C  C   . LYS   A 1 40  ? -21.137 31.543 16.757 1.000 39.570  ? 39  LYS   AAA C   1 ? 
ATOM   272  O  O   . LYS   A 1 40  ? -21.412 32.110 17.824 1.000 40.314  ? 39  LYS   AAA O   1 ? 
ATOM   273  C  CB  . LYS   A 1 40  ? -22.573 29.480 16.941 1.000 47.002  ? 39  LYS   AAA CB  1 ? 
ATOM   274  C  CG  . LYS   A 1 40  ? -22.605 27.963 17.118 1.000 53.470  ? 39  LYS   AAA CG  1 ? 
ATOM   275  C  CD  . LYS   A 1 40  ? -23.486 27.224 16.150 1.000 63.397  ? 39  LYS   AAA CD  1 ? 
ATOM   276  C  CE  . LYS   A 1 40  ? -22.998 25.813 15.918 1.000 77.981  ? 39  LYS   AAA CE  1 ? 
ATOM   277  N  NZ  . LYS   A 1 40  ? -24.137 24.881 15.812 1.000 83.225  ? 39  LYS   AAA NZ  1 ? 
ATOM   278  N  N   . HIS   A 1 41  ? -20.727 32.128 15.624 1.000 36.025  ? 40  HIS   AAA N   1 ? 
ATOM   279  C  CA  . HIS   A 1 41  ? -20.773 33.594 15.400 1.000 38.121  ? 40  HIS   AAA CA  1 ? 
ATOM   280  C  C   . HIS   A 1 41  ? -22.240 33.973 15.535 1.000 46.177  ? 40  HIS   AAA C   1 ? 
ATOM   281  O  O   . HIS   A 1 41  ? -23.070 33.215 14.996 1.000 69.410  ? 40  HIS   AAA O   1 ? 
ATOM   282  C  CB  . HIS   A 1 41  ? -20.220 34.019 14.035 1.000 40.029  ? 40  HIS   AAA CB  1 ? 
ATOM   283  C  CG  . HIS   A 1 41  ? -20.279 35.505 13.855 1.000 42.448  ? 40  HIS   AAA CG  1 ? 
ATOM   284  N  ND1 . HIS   A 1 41  ? -19.418 36.368 14.507 1.000 57.820  ? 40  HIS   AAA ND1 1 ? 
ATOM   285  C  CD2 . HIS   A 1 41  ? -21.115 36.295 13.143 1.000 52.468  ? 40  HIS   AAA CD2 1 ? 
ATOM   286  C  CE1 . HIS   A 1 41  ? -19.712 37.620 14.185 1.000 53.652  ? 40  HIS   AAA CE1 1 ? 
ATOM   287  N  NE2 . HIS   A 1 41  ? -20.740 37.602 13.355 1.000 53.749  ? 40  HIS   AAA NE2 1 ? 
ATOM   288  N  N   . ASP   A 1 42  ? -22.540 35.042 16.269 1.000 48.453  ? 41  ASP   AAA N   1 ? 
ATOM   289  C  CA  . ASP   A 1 42  ? -23.922 35.526 16.475 1.000 41.720  ? 41  ASP   AAA CA  1 ? 
ATOM   290  C  C   . ASP   A 1 42  ? -23.961 37.002 16.098 1.000 44.632  ? 41  ASP   AAA C   1 ? 
ATOM   291  O  O   . ASP   A 1 42  ? -23.436 37.837 16.867 1.000 46.201  ? 41  ASP   AAA O   1 ? 
ATOM   292  C  CB  . ASP   A 1 42  ? -24.386 35.251 17.899 1.000 39.513  ? 41  ASP   AAA CB  1 ? 
ATOM   293  C  CG  . ASP   A 1 42  ? -25.810 35.705 18.102 1.000 46.650  ? 41  ASP   AAA CG  1 ? 
ATOM   294  O  OD1 . ASP   A 1 42  ? -26.290 36.459 17.263 1.000 49.066  ? 41  ASP   AAA OD1 1 ? 
ATOM   295  O  OD2 . ASP   A 1 42  ? -26.413 35.291 19.080 1.000 51.417  ? 41  ASP   AAA OD2 1 ? 
ATOM   296  N  N   . THR   A 1 43  ? -24.607 37.277 14.971 1.000 43.029  ? 42  THR   AAA N   1 ? 
ATOM   297  C  CA  . THR   A 1 43  ? -24.665 38.587 14.276 1.000 50.384  ? 42  THR   AAA CA  1 ? 
ATOM   298  C  C   . THR   A 1 43  ? -25.369 39.638 15.151 1.000 48.109  ? 42  THR   AAA C   1 ? 
ATOM   299  O  O   . THR   A 1 43  ? -25.081 40.864 14.974 1.000 50.407  ? 42  THR   AAA O   1 ? 
ATOM   300  C  CB  . THR   A 1 43  ? -25.309 38.381 12.894 1.000 53.757  ? 42  THR   AAA CB  1 ? 
ATOM   301  O  OG1 . THR   A 1 43  ? -24.452 39.058 11.983 1.000 64.939  ? 42  THR   AAA OG1 1 ? 
ATOM   302  C  CG2 . THR   A 1 43  ? -26.733 38.879 12.776 1.000 49.692  ? 42  THR   AAA CG2 1 ? 
ATOM   303  N  N   . SER   A 1 44  ? -26.248 39.201 16.055 1.000 45.463  ? 43  SER   AAA N   1 ? 
ATOM   304  C  CA  . SER   A 1 44  ? -27.080 40.090 16.909 1.000 50.917  ? 43  SER   AAA CA  1 ? 
ATOM   305  C  C   . SER   A 1 44  ? -26.278 40.631 18.107 1.000 48.221  ? 43  SER   AAA C   1 ? 
ATOM   306  O  O   . SER   A 1 44  ? -26.763 41.582 18.737 1.000 51.614  ? 43  SER   AAA O   1 ? 
ATOM   307  C  CB  . SER   A 1 44  ? -28.308 39.373 17.376 1.000 49.270  ? 43  SER   AAA CB  1 ? 
ATOM   308  O  OG  . SER   A 1 44  ? -27.951 38.409 18.349 1.000 41.386  ? 43  SER   AAA OG  1 ? 
ATOM   309  N  N   . LEU   A 1 45  ? -25.132 40.026 18.456 1.000 48.648  ? 44  LEU   AAA N   1 ? 
ATOM   310  C  CA  . LEU   A 1 45  ? -24.304 40.483 19.603 1.000 37.213  ? 44  LEU   AAA CA  1 ? 
ATOM   311  C  C   . LEU   A 1 45  ? -23.776 41.885 19.307 1.000 35.507  ? 44  LEU   AAA C   1 ? 
ATOM   312  O  O   . LEU   A 1 45  ? -23.161 42.100 18.258 1.000 39.341  ? 44  LEU   AAA O   1 ? 
ATOM   313  C  CB  . LEU   A 1 45  ? -23.166 39.493 19.851 1.000 41.913  ? 44  LEU   AAA CB  1 ? 
ATOM   314  C  CG  . LEU   A 1 45  ? -23.554 38.156 20.490 1.000 39.760  ? 44  LEU   AAA CG  1 ? 
ATOM   315  C  CD1 . LEU   A 1 45  ? -22.365 37.217 20.462 1.000 37.625  ? 44  LEU   AAA CD1 1 ? 
ATOM   316  C  CD2 . LEU   A 1 45  ? -24.025 38.340 21.925 1.000 39.165  ? 44  LEU   AAA CD2 1 ? 
ATOM   317  N  N   . LYS   A 1 46  ? -24.042 42.806 20.220 1.000 35.199  ? 45  LYS   AAA N   1 ? 
ATOM   318  C  CA  . LYS   A 1 46  ? -23.590 44.204 20.087 1.000 40.371  ? 45  LYS   AAA CA  1 ? 
ATOM   319  C  C   . LYS   A 1 46  ? -22.202 44.315 20.719 1.000 36.399  ? 45  LYS   AAA C   1 ? 
ATOM   320  O  O   . LYS   A 1 46  ? -21.761 43.439 21.480 1.000 33.862  ? 45  LYS   AAA O   1 ? 
ATOM   321  C  CB  . LYS   A 1 46  ? -24.637 45.140 20.706 1.000 44.853  ? 45  LYS   AAA CB  1 ? 
ATOM   322  C  CG  . LYS   A 1 46  ? -25.992 45.148 20.015 1.000 51.685  ? 45  LYS   AAA CG  1 ? 
ATOM   323  C  CD  . LYS   A 1 46  ? -26.985 46.042 20.731 1.000 60.530  ? 45  LYS   AAA CD  1 ? 
ATOM   324  C  CE  . LYS   A 1 46  ? -27.780 46.927 19.797 1.000 70.181  ? 45  LYS   AAA CE  1 ? 
ATOM   325  N  NZ  . LYS   A 1 46  ? -28.719 46.115 18.993 1.000 72.829  ? 45  LYS   AAA NZ  1 ? 
ATOM   326  N  N   . PRO   A 1 47  ? -21.448 45.392 20.399 1.000 36.743  ? 46  PRO   AAA N   1 ? 
ATOM   327  C  CA  . PRO   A 1 47  ? -20.202 45.658 21.096 1.000 35.178  ? 46  PRO   AAA CA  1 ? 
ATOM   328  C  C   . PRO   A 1 47  ? -20.472 45.814 22.592 1.000 33.371  ? 46  PRO   AAA C   1 ? 
ATOM   329  O  O   . PRO   A 1 47  ? -21.535 46.288 22.964 1.000 36.799  ? 46  PRO   AAA O   1 ? 
ATOM   330  C  CB  . PRO   A 1 47  ? -19.676 46.952 20.452 1.000 36.383  ? 46  PRO   AAA CB  1 ? 
ATOM   331  C  CG  . PRO   A 1 47  ? -20.312 46.957 19.079 1.000 38.948  ? 46  PRO   AAA CG  1 ? 
ATOM   332  C  CD  . PRO   A 1 47  ? -21.676 46.333 19.287 1.000 39.672  ? 46  PRO   AAA CD  1 ? 
ATOM   333  N  N   . ILE   A 1 48  ? -19.511 45.367 23.394 1.000 36.572  ? 47  ILE   AAA N   1 ? 
ATOM   334  C  CA  . ILE   A 1 48  ? -19.437 45.596 24.866 1.000 34.145  ? 47  ILE   AAA CA  1 ? 
ATOM   335  C  C   . ILE   A 1 48  ? -19.205 47.082 25.098 1.000 29.396  ? 47  ILE   AAA C   1 ? 
ATOM   336  O  O   . ILE   A 1 48  ? -18.327 47.678 24.439 1.000 34.752  ? 47  ILE   AAA O   1 ? 
ATOM   337  C  CB  . ILE   A 1 48  ? -18.312 44.756 25.502 1.000 37.246  ? 47  ILE   AAA CB  1 ? 
ATOM   338  C  CG1 . ILE   A 1 48  ? -18.624 43.258 25.519 1.000 36.209  ? 47  ILE   AAA CG1 1 ? 
ATOM   339  C  CG2 . ILE   A 1 48  ? -17.973 45.267 26.887 1.000 40.644  ? 47  ILE   AAA CG2 1 ? 
ATOM   340  C  CD1 . ILE   A 1 48  ? -19.909 42.897 26.228 1.000 38.944  ? 47  ILE   AAA CD1 1 ? 
ATOM   341  N  N   . SER   A 1 49  ? -19.960 47.649 26.018 1.000 31.232  ? 48  SER   AAA N   1 ? 
ATOM   342  C  CA  . SER   A 1 49  ? -19.829 49.075 26.402 1.000 33.053  ? 48  SER   AAA CA  1 ? 
ATOM   343  C  C   . SER   A 1 49  ? -19.567 49.104 27.903 1.000 31.962  ? 48  SER   AAA C   1 ? 
ATOM   344  O  O   . SER   A 1 49  ? -20.456 48.644 28.668 1.000 32.638  ? 48  SER   AAA O   1 ? 
ATOM   345  C  CB  . SER   A 1 49  ? -21.053 49.867 25.986 1.000 38.534  ? 48  SER   AAA CB  1 ? 
ATOM   346  O  OG  . SER   A 1 49  ? -21.143 51.070 26.731 1.000 42.092  ? 48  SER   AAA OG  1 ? 
ATOM   347  N  N   . VAL   A 1 50  ? -18.377 49.558 28.309 1.000 25.967  ? 49  VAL   AAA N   1 ? 
ATOM   348  C  CA  . VAL   A 1 50  ? -18.079 49.781 29.754 1.000 25.288  ? 49  VAL   AAA CA  1 ? 
ATOM   349  C  C   . VAL   A 1 50  ? -17.926 51.278 29.985 1.000 27.468  ? 49  VAL   AAA C   1 ? 
ATOM   350  O  O   . VAL   A 1 50  ? -17.276 51.942 29.197 1.000 30.375  ? 49  VAL   AAA O   1 ? 
ATOM   351  C  CB  . VAL   A 1 50  ? -16.866 48.991 30.271 1.000 29.065  ? 49  VAL   AAA CB  1 ? 
ATOM   352  C  CG1 . VAL   A 1 50  ? -17.208 47.506 30.270 1.000 32.098  ? 49  VAL   AAA CG1 1 ? 
ATOM   353  C  CG2 . VAL   A 1 50  ? -15.595 49.264 29.491 1.000 32.205  ? 49  VAL   AAA CG2 1 ? 
ATOM   354  N  N   . SER   A 1 51  ? -18.549 51.744 31.033 1.000 28.062  ? 50  SER   AAA N   1 ? 
ATOM   355  C  CA  . SER   A 1 51  ? -18.398 53.156 31.412 1.000 26.086  ? 50  SER   AAA CA  1 ? 
ATOM   356  C  C   . SER   A 1 51  ? -18.323 53.180 32.945 1.000 23.725  ? 50  SER   AAA C   1 ? 
ATOM   357  O  O   . SER   A 1 51  ? -19.388 53.113 33.614 1.000 29.799  ? 50  SER   AAA O   1 ? 
ATOM   358  C  CB  . SER   A 1 51  ? -19.541 53.899 30.826 1.000 32.276  ? 50  SER   AAA CB  1 ? 
ATOM   359  O  OG  . SER   A 1 51  ? -19.461 55.216 31.266 1.000 37.532  ? 50  SER   AAA OG  1 ? 
ATOM   360  N  N   . TYR   A 1 52  ? -17.113 53.207 33.487 1.000 24.623  ? 51  TYR   AAA N   1 ? 
ATOM   361  C  CA  . TYR   A 1 52  ? -16.876 53.107 34.953 1.000 28.280  ? 51  TYR   AAA CA  1 ? 
ATOM   362  C  C   . TYR   A 1 52  ? -16.319 54.417 35.490 1.000 34.201  ? 51  TYR   AAA C   1 ? 
ATOM   363  O  O   . TYR   A 1 52  ? -15.410 54.992 34.868 1.000 37.557  ? 51  TYR   AAA O   1 ? 
ATOM   364  C  CB  . TYR   A 1 52  ? -15.872 52.012 35.299 1.000 27.699  ? 51  TYR   AAA CB  1 ? 
ATOM   365  C  CG  . TYR   A 1 52  ? -16.176 50.608 34.827 1.000 26.402  ? 51  TYR   AAA CG  1 ? 
ATOM   366  C  CD1 . TYR   A 1 52  ? -17.460 50.102 34.735 1.000 25.194  ? 51  TYR   AAA CD1 1 ? 
ATOM   367  C  CD2 . TYR   A 1 52  ? -15.138 49.788 34.421 1.000 22.156  ? 51  TYR   AAA CD2 1 ? 
ATOM   368  C  CE1 . TYR   A 1 52  ? -17.704 48.783 34.348 1.000 23.369  ? 51  TYR   AAA CE1 1 ? 
ATOM   369  C  CE2 . TYR   A 1 52  ? -15.368 48.445 34.075 1.000 24.734  ? 51  TYR   AAA CE2 1 ? 
ATOM   370  C  CZ  . TYR   A 1 52  ? -16.650 47.980 33.932 1.000 22.893  ? 51  TYR   AAA CZ  1 ? 
ATOM   371  O  OH  . TYR   A 1 52  ? -16.813 46.644 33.598 1.000 21.796  ? 51  TYR   AAA OH  1 ? 
ATOM   372  N  N   . ASN   A 1 53  ? -16.821 54.826 36.644 1.000 28.405  ? 52  ASN   AAA N   1 ? 
ATOM   373  C  CA  . ASN   A 1 53  ? -16.436 56.084 37.314 1.000 27.799  ? 52  ASN   AAA CA  1 ? 
ATOM   374  C  C   . ASN   A 1 53  ? -15.374 55.746 38.358 1.000 28.243  ? 52  ASN   AAA C   1 ? 
ATOM   375  O  O   . ASN   A 1 53  ? -15.660 54.967 39.276 1.000 28.028  ? 52  ASN   AAA O   1 ? 
ATOM   376  C  CB  . ASN   A 1 53  ? -17.700 56.707 37.902 1.000 32.174  ? 52  ASN   AAA CB  1 ? 
ATOM   377  C  CG  . ASN   A 1 53  ? -17.454 58.078 38.481 1.000 33.299  ? 52  ASN   AAA CG  1 ? 
ATOM   378  O  OD1 . ASN   A 1 53  ? -16.386 58.330 39.036 1.000 44.027  ? 52  ASN   AAA OD1 1 ? 
ATOM   379  N  ND2 . ASN   A 1 53  ? -18.475 58.913 38.404 1.000 32.780  ? 52  ASN   AAA ND2 1 ? 
ATOM   380  N  N   . PRO   A 1 54  ? -14.124 56.257 38.244 1.000 25.861  ? 53  PRO   AAA N   1 ? 
ATOM   381  C  CA  . PRO   A 1 54  ? -13.100 55.928 39.227 1.000 28.319  ? 53  PRO   AAA CA  1 ? 
ATOM   382  C  C   . PRO   A 1 54  ? -13.507 56.286 40.666 1.000 24.659  ? 53  PRO   AAA C   1 ? 
ATOM   383  O  O   . PRO   A 1 54  ? -12.992 55.689 41.587 1.000 28.171  ? 53  PRO   AAA O   1 ? 
ATOM   384  C  CB  . PRO   A 1 54  ? -11.859 56.722 38.761 1.000 30.140  ? 53  PRO   AAA CB  1 ? 
ATOM   385  C  CG  . PRO   A 1 54  ? -12.418 57.844 37.932 1.000 33.529  ? 53  PRO   AAA CG  1 ? 
ATOM   386  C  CD  . PRO   A 1 54  ? -13.660 57.290 37.282 1.000 27.870  ? 53  PRO   AAA CD  1 ? 
ATOM   387  N  N   . ALA   A 1 55  ? -14.426 57.230 40.874 1.000 27.617  ? 54  ALA   AAA N   1 ? 
ATOM   388  C  CA  . ALA   A 1 55  ? -14.878 57.578 42.243 1.000 27.623  ? 54  ALA   AAA CA  1 ? 
ATOM   389  C  C   . ALA   A 1 55  ? -15.732 56.437 42.884 1.000 32.928  ? 54  ALA   AAA C   1 ? 
ATOM   390  O  O   . ALA   A 1 55  ? -16.031 56.500 44.101 1.000 31.093  ? 54  ALA   AAA O   1 ? 
ATOM   391  C  CB  . ALA   A 1 55  ? -15.577 58.910 42.221 1.000 34.075  ? 54  ALA   AAA CB  1 ? 
ATOM   392  N  N   . THR   A 1 56  ? -16.152 55.416 42.136 1.000 29.879  ? 55  THR   AAA N   1 ? 
ATOM   393  C  CA  . THR   A 1 56  ? -16.906 54.285 42.721 1.000 29.623  ? 55  THR   AAA CA  1 ? 
ATOM   394  C  C   . THR   A 1 56  ? -15.979 53.248 43.374 1.000 24.249  ? 55  THR   AAA C   1 ? 
ATOM   395  O  O   . THR   A 1 56  ? -16.506 52.463 44.167 1.000 26.539  ? 55  THR   AAA O   1 ? 
ATOM   396  C  CB  . THR   A 1 56  ? -17.853 53.627 41.711 1.000 26.393  ? 55  THR   AAA CB  1 ? 
ATOM   397  O  OG1 . THR   A 1 56  ? -17.096 53.161 40.609 1.000 25.265  ? 55  THR   AAA OG1 1 ? 
ATOM   398  C  CG2 . THR   A 1 56  ? -18.925 54.562 41.212 1.000 30.569  ? 55  THR   AAA CG2 1 ? 
ATOM   399  N  N   . ALA   A 1 57  ? -14.666 53.289 43.162 1.000 22.222  ? 56  ALA   AAA N   1 ? 
ATOM   400  C  CA  . ALA   A 1 57  ? -13.742 52.369 43.866 1.000 24.944  ? 56  ALA   AAA CA  1 ? 
ATOM   401  C  C   . ALA   A 1 57  ? -13.841 52.610 45.384 1.000 23.350  ? 56  ALA   AAA C   1 ? 
ATOM   402  O  O   . ALA   A 1 57  ? -13.860 53.811 45.836 1.000 25.817  ? 56  ALA   AAA O   1 ? 
ATOM   403  C  CB  . ALA   A 1 57  ? -12.345 52.507 43.353 1.000 26.234  ? 56  ALA   AAA CB  1 ? 
ATOM   404  N  N   . LYS   A 1 58  ? -13.972 51.528 46.164 1.000 22.951  ? 57  LYS   AAA N   1 ? 
ATOM   405  C  CA  . LYS   A 1 58  ? -14.245 51.599 47.612 1.000 24.033  ? 57  LYS   AAA CA  1 ? 
ATOM   406  C  C   . LYS   A 1 58  ? -13.125 50.994 48.455 1.000 25.015  ? 57  LYS   AAA C   1 ? 
ATOM   407  O  O   . LYS   A 1 58  ? -12.624 51.689 49.361 1.000 27.090  ? 57  LYS   AAA O   1 ? 
ATOM   408  C  CB  . LYS   A 1 58  ? -15.588 50.982 47.964 1.000 28.867  ? 57  LYS   AAA CB  1 ? 
ATOM   409  C  CG  . LYS   A 1 58  ? -16.050 51.235 49.395 1.000 34.475  ? 57  LYS   AAA CG  1 ? 
ATOM   410  C  CD  . LYS   A 1 58  ? -17.445 50.680 49.686 1.000 45.139  ? 57  LYS   AAA CD  1 ? 
ATOM   411  C  CE  . LYS   A 1 58  ? -17.649 49.281 49.135 1.000 47.866  ? 57  LYS   AAA CE  1 ? 
ATOM   412  N  NZ  . LYS   A 1 58  ? -19.062 48.835 49.217 1.000 55.210  ? 57  LYS   AAA NZ  1 ? 
ATOM   413  N  N   . GLU   A 1 59  ? -12.785 49.706 48.242 1.000 23.259  ? 58  GLU   AAA N   1 ? 
ATOM   414  C  CA  . GLU   A 1 59  ? -11.975 49.017 49.259 1.000 24.445  ? 58  GLU   AAA CA  1 ? 
ATOM   415  C  C   . GLU   A 1 59  ? -11.376 47.759 48.646 1.000 21.078  ? 58  GLU   AAA C   1 ? 
ATOM   416  O  O   . GLU   A 1 59  ? -11.825 47.295 47.611 1.000 22.413  ? 58  GLU   AAA O   1 ? 
ATOM   417  C  CB  . GLU   A 1 59  ? -12.809 48.644 50.486 1.000 25.288  ? 58  GLU   AAA CB  1 ? 
ATOM   418  C  CG  . GLU   A 1 59  ? -13.788 47.554 50.144 1.000 30.318  ? 58  GLU   AAA CG  1 ? 
ATOM   419  C  CD  . GLU   A 1 59  ? -14.846 47.242 51.176 1.000 31.584  ? 58  GLU   AAA CD  1 ? 
ATOM   420  O  OE1 . GLU   A 1 59  ? -14.715 47.786 52.312 1.000 28.393  ? 58  GLU   AAA OE1 1 ? 
ATOM   421  O  OE2 . GLU   A 1 59  ? -15.792 46.430 50.829 1.000 36.286  ? 58  GLU   AAA OE2 1 ? 
ATOM   422  N  N   . ILE   A 1 60  ? -10.339 47.302 49.290 1.000 23.535  ? 59  ILE   AAA N   1 ? 
ATOM   423  C  CA  . ILE   A 1 60  ? -9.648  46.040 48.909 1.000 22.205  ? 59  ILE   AAA CA  1 ? 
ATOM   424  C  C   . ILE   A 1 60  ? -9.613  45.158 50.152 1.000 24.371  ? 59  ILE   AAA C   1 ? 
ATOM   425  O  O   . ILE   A 1 60  ? -9.301  45.667 51.264 1.000 25.111  ? 59  ILE   AAA O   1 ? 
ATOM   426  C  CB  . ILE   A 1 60  ? -8.266  46.340 48.291 1.000 25.002  ? 59  ILE   AAA CB  1 ? 
ATOM   427  C  CG1 . ILE   A 1 60  ? -7.661  45.091 47.657 1.000 24.634  ? 59  ILE   AAA CG1 1 ? 
ATOM   428  C  CG2 . ILE   A 1 60  ? -7.323  47.003 49.295 1.000 25.588  ? 59  ILE   AAA CG2 1 ? 
ATOM   429  C  CD1 . ILE   A 1 60  ? -6.426  45.377 46.880 1.000 24.643  ? 59  ILE   AAA CD1 1 ? 
ATOM   430  N  N   . ILE   A 1 61  ? -9.925  43.848 49.979 1.000 23.274  ? 60  ILE   AAA N   1 ? 
ATOM   431  C  CA  . ILE   A 1 61  ? -10.187 43.001 51.170 1.000 23.389  ? 60  ILE   AAA CA  1 ? 
ATOM   432  C  C   . ILE   A 1 61  ? -9.549  41.649 50.929 1.000 23.534  ? 60  ILE   AAA C   1 ? 
ATOM   433  O  O   . ILE   A 1 61  ? -9.651  41.183 49.787 1.000 25.414  ? 60  ILE   AAA O   1 ? 
ATOM   434  C  CB  . ILE   A 1 61  ? -11.683 42.835 51.502 1.000 23.982  ? 60  ILE   AAA CB  1 ? 
ATOM   435  C  CG1 . ILE   A 1 61  ? -12.481 42.127 50.417 1.000 32.056  ? 60  ILE   AAA CG1 1 ? 
ATOM   436  C  CG2 . ILE   A 1 61  ? -12.345 44.154 51.774 1.000 24.959  ? 60  ILE   AAA CG2 1 ? 
ATOM   437  C  CD1 . ILE   A 1 61  ? -13.964 41.976 50.738 1.000 40.821  ? 60  ILE   AAA CD1 1 ? 
ATOM   438  N  N   . ASN   A 1 62  ? -8.904  41.111 51.964 1.000 25.203  ? 61  ASN   AAA N   1 ? 
ATOM   439  C  CA  . ASN   A 1 62  ? -8.279  39.770 51.947 1.000 24.464  ? 61  ASN   AAA CA  1 ? 
ATOM   440  C  C   . ASN   A 1 62  ? -9.341  38.816 52.498 1.000 26.105  ? 61  ASN   AAA C   1 ? 
ATOM   441  O  O   . ASN   A 1 62  ? -9.720  38.907 53.693 1.000 24.097  ? 61  ASN   AAA O   1 ? 
ATOM   442  C  CB  . ASN   A 1 62  ? -6.933  39.723 52.672 1.000 26.121  ? 61  ASN   AAA CB  1 ? 
ATOM   443  C  CG  . ASN   A 1 62  ? -6.318  38.337 52.800 1.000 26.065  ? 61  ASN   AAA CG  1 ? 
ATOM   444  O  OD1 . ASN   A 1 62  ? -7.025  37.303 52.786 1.000 26.600  ? 61  ASN   AAA OD1 1 ? 
ATOM   445  N  ND2 . ASN   A 1 62  ? -5.000  38.322 52.928 1.000 29.008  ? 61  ASN   AAA ND2 1 ? 
ATOM   446  N  N   . VAL   A 1 63  ? -9.851  37.962 51.618 1.000 27.702  ? 62  VAL   AAA N   1 ? 
ATOM   447  C  CA  . VAL   A 1 63  ? -10.990 37.057 51.949 1.000 28.288  ? 62  VAL   AAA CA  1 ? 
ATOM   448  C  C   . VAL   A 1 63  ? -10.477 35.630 52.145 1.000 24.574  ? 62  VAL   AAA C   1 ? 
ATOM   449  O  O   . VAL   A 1 63  ? -11.330 34.771 52.191 1.000 30.846  ? 62  VAL   AAA O   1 ? 
ATOM   450  C  CB  . VAL   A 1 63  ? -12.130 37.141 50.913 1.000 25.529  ? 62  VAL   AAA CB  1 ? 
ATOM   451  C  CG1 . VAL   A 1 63  ? -12.662 38.569 50.872 1.000 29.114  ? 62  VAL   AAA CG1 1 ? 
ATOM   452  C  CG2 . VAL   A 1 63  ? -11.729 36.687 49.518 1.000 28.422  ? 62  VAL   AAA CG2 1 ? 
ATOM   453  N  N   . GLY   A 1 64  ? -9.188  35.439 52.388 1.000 28.832  ? 63  GLY   AAA N   1 ? 
ATOM   454  C  CA  . GLY   A 1 64  ? -8.592  34.137 52.753 1.000 33.143  ? 63  GLY   AAA CA  1 ? 
ATOM   455  C  C   . GLY   A 1 64  ? -8.181  33.328 51.535 1.000 30.309  ? 63  GLY   AAA C   1 ? 
ATOM   456  O  O   . GLY   A 1 64  ? -7.014  32.902 51.480 1.000 35.995  ? 63  GLY   AAA O   1 ? 
ATOM   457  N  N   . HIS   A 1 65  ? -9.096  33.148 50.581 1.000 26.754  ? 64  HIS   AAA N   1 ? 
ATOM   458  C  CA  . HIS   A 1 65  ? -8.908  32.378 49.331 1.000 29.345  ? 64  HIS   AAA CA  1 ? 
ATOM   459  C  C   . HIS   A 1 65  ? -8.402  33.298 48.215 1.000 25.938  ? 64  HIS   AAA C   1 ? 
ATOM   460  O  O   . HIS   A 1 65  ? -7.960  32.790 47.179 1.000 26.656  ? 64  HIS   AAA O   1 ? 
ATOM   461  C  CB  . HIS   A 1 65  ? -10.216 31.640 49.007 1.000 30.236  ? 64  HIS   AAA CB  1 ? 
ATOM   462  C  CG  . HIS   A 1 65  ? -11.344 32.476 48.487 1.000 26.635  ? 64  HIS   AAA CG  1 ? 
ATOM   463  N  ND1 . HIS   A 1 65  ? -12.407 32.899 49.305 1.000 31.212  ? 64  HIS   AAA ND1 1 ? 
ATOM   464  C  CD2 . HIS   A 1 65  ? -11.641 32.897 47.242 1.000 27.477  ? 64  HIS   AAA CD2 1 ? 
ATOM   465  C  CE1 . HIS   A 1 65  ? -13.279 33.584 48.588 1.000 28.240  ? 64  HIS   AAA CE1 1 ? 
ATOM   466  N  NE2 . HIS   A 1 65  ? -12.825 33.626 47.324 1.000 33.022  ? 64  HIS   AAA NE2 1 ? 
ATOM   467  N  N   . SER   A 1 66  ? -8.588  34.638 48.359 1.000 21.279  ? 65  SER   AAA N   1 ? 
ATOM   468  C  CA  . SER   A 1 66  ? -8.348  35.590 47.262 1.000 20.663  ? 65  SER   AAA CA  1 ? 
ATOM   469  C  C   . SER   A 1 66  ? -8.354  36.982 47.903 1.000 21.171  ? 65  SER   AAA C   1 ? 
ATOM   470  O  O   . SER   A 1 66  ? -8.423  37.079 49.186 1.000 23.162  ? 65  SER   AAA O   1 ? 
ATOM   471  C  CB  . SER   A 1 66  ? -9.404  35.464 46.185 1.000 22.497  ? 65  SER   AAA CB  1 ? 
ATOM   472  O  OG  . SER   A 1 66  ? -9.063  36.187 44.998 1.000 23.709  ? 65  SER   AAA OG  1 ? 
ATOM   473  N  N   . PHE   A 1 67  ? -8.273  38.010 47.054 1.000 22.400  ? 66  PHE   AAA N   1 ? 
ATOM   474  C  CA  . PHE   A 1 67  ? -8.571  39.417 47.464 1.000 22.404  ? 66  PHE   AAA CA  1 ? 
ATOM   475  C  C   . PHE   A 1 67  ? -9.574  40.005 46.481 1.000 20.369  ? 66  PHE   AAA C   1 ? 
ATOM   476  O  O   . PHE   A 1 67  ? -9.583  39.636 45.285 1.000 23.847  ? 66  PHE   AAA O   1 ? 
ATOM   477  C  CB  . PHE   A 1 67  ? -7.290  40.251 47.546 1.000 24.110  ? 66  PHE   AAA CB  1 ? 
ATOM   478  C  CG  . PHE   A 1 67  ? -6.654  40.612 46.230 1.000 22.668  ? 66  PHE   AAA CG  1 ? 
ATOM   479  C  CD1 . PHE   A 1 67  ? -5.765  39.758 45.602 1.000 28.182  ? 66  PHE   AAA CD1 1 ? 
ATOM   480  C  CD2 . PHE   A 1 67  ? -6.908  41.839 45.637 1.000 26.211  ? 66  PHE   AAA CD2 1 ? 
ATOM   481  C  CE1 . PHE   A 1 67  ? -5.147  40.121 44.424 1.000 25.313  ? 66  PHE   AAA CE1 1 ? 
ATOM   482  C  CE2 . PHE   A 1 67  ? -6.313  42.176 44.433 1.000 25.674  ? 66  PHE   AAA CE2 1 ? 
ATOM   483  C  CZ  . PHE   A 1 67  ? -5.473  41.292 43.808 1.000 25.104  ? 66  PHE   AAA CZ  1 ? 
ATOM   484  N  N   . HIS   A 1 68  ? -10.439 40.866 46.984 1.000 20.863  ? 67  HIS   AAA N   1 ? 
ATOM   485  C  CA  . HIS   A 1 68  ? -11.484 41.519 46.181 1.000 20.753  ? 67  HIS   AAA CA  1 ? 
ATOM   486  C  C   . HIS   A 1 68  ? -11.266 43.044 46.217 1.000 20.748  ? 67  HIS   AAA C   1 ? 
ATOM   487  O  O   . HIS   A 1 68  ? -10.970 43.565 47.294 1.000 24.468  ? 67  HIS   AAA O   1 ? 
ATOM   488  C  CB  . HIS   A 1 68  ? -12.851 41.157 46.743 1.000 21.294  ? 67  HIS   AAA CB  1 ? 
ATOM   489  C  CG  . HIS   A 1 68  ? -13.186 39.687 46.649 1.000 22.653  ? 67  HIS   AAA CG  1 ? 
ATOM   490  N  ND1 . HIS   A 1 68  ? -14.219 39.097 47.350 1.000 27.634  ? 67  HIS   AAA ND1 1 ? 
ATOM   491  C  CD2 . HIS   A 1 68  ? -12.656 38.735 45.855 1.000 25.594  ? 67  HIS   AAA CD2 1 ? 
ATOM   492  C  CE1 . HIS   A 1 68  ? -14.318 37.811 46.972 1.000 29.239  ? 67  HIS   AAA CE1 1 ? 
ATOM   493  N  NE2 . HIS   A 1 68  ? -13.368 37.554 46.031 1.000 25.978  ? 67  HIS   AAA NE2 1 ? 
ATOM   494  N  N   . VAL   A 1 69  ? -11.497 43.692 45.101 1.000 19.137  ? 68  VAL   AAA N   1 ? 
ATOM   495  C  CA  . VAL   A 1 69  ? -11.605 45.203 45.060 1.000 19.507  ? 68  VAL   AAA CA  1 ? 
ATOM   496  C  C   . VAL   A 1 69  ? -13.085 45.499 44.822 1.000 21.181  ? 68  VAL   AAA C   1 ? 
ATOM   497  O  O   . VAL   A 1 69  ? -13.599 45.206 43.737 1.000 21.470  ? 68  VAL   AAA O   1 ? 
ATOM   498  C  CB  . VAL   A 1 69  ? -10.704 45.755 43.961 1.000 20.096  ? 68  VAL   AAA CB  1 ? 
ATOM   499  C  CG1 . VAL   A 1 69  ? -10.770 47.288 43.890 1.000 24.241  ? 68  VAL   AAA CG1 1 ? 
ATOM   500  C  CG2 . VAL   A 1 69  ? -9.261  45.292 44.110 1.000 26.251  ? 68  VAL   AAA CG2 1 ? 
ATOM   501  N  N   . ASN   A 1 70  ? -13.746 46.086 45.811 1.000 21.913  ? 69  ASN   AAA N   1 ? 
ATOM   502  C  CA  . ASN   A 1 70  ? -15.187 46.405 45.784 1.000 20.006  ? 69  ASN   AAA CA  1 ? 
ATOM   503  C  C   . ASN   A 1 70  ? -15.384 47.876 45.424 1.000 20.263  ? 69  ASN   AAA C   1 ? 
ATOM   504  O  O   . ASN   A 1 70  ? -14.436 48.653 45.627 1.000 22.568  ? 69  ASN   AAA O   1 ? 
ATOM   505  C  CB  . ASN   A 1 70  ? -15.863 46.129 47.128 1.000 24.284  ? 69  ASN   AAA CB  1 ? 
ATOM   506  C  CG  . ASN   A 1 70  ? -15.881 44.658 47.465 1.000 24.035  ? 69  ASN   AAA CG  1 ? 
ATOM   507  O  OD1 . ASN   A 1 70  ? -15.975 43.812 46.540 1.000 29.374  ? 69  ASN   AAA OD1 1 ? 
ATOM   508  N  ND2 . ASN   A 1 70  ? -15.847 44.370 48.756 1.000 23.012  ? 69  ASN   AAA ND2 1 ? 
ATOM   509  N  N   . PHE   A 1 71  ? -16.511 48.090 44.774 1.000 21.916  ? 70  PHE   AAA N   1 ? 
ATOM   510  C  CA  . PHE   A 1 71  ? -16.993 49.393 44.263 1.000 22.041  ? 70  PHE   AAA CA  1 ? 
ATOM   511  C  C   . PHE   A 1 71  ? -18.329 49.699 44.923 1.000 22.095  ? 70  PHE   AAA C   1 ? 
ATOM   512  O  O   . PHE   A 1 71  ? -19.164 48.856 45.161 1.000 24.115  ? 70  PHE   AAA O   1 ? 
ATOM   513  C  CB  . PHE   A 1 71  ? -17.102 49.386 42.735 1.000 22.826  ? 70  PHE   AAA CB  1 ? 
ATOM   514  C  CG  . PHE   A 1 71  ? -15.764 49.283 42.062 1.000 22.700  ? 70  PHE   AAA CG  1 ? 
ATOM   515  C  CD1 . PHE   A 1 71  ? -15.054 48.093 42.041 1.000 25.937  ? 70  PHE   AAA CD1 1 ? 
ATOM   516  C  CD2 . PHE   A 1 71  ? -15.185 50.389 41.460 1.000 22.267  ? 70  PHE   AAA CD2 1 ? 
ATOM   517  C  CE1 . PHE   A 1 71  ? -13.794 48.030 41.477 1.000 25.103  ? 70  PHE   AAA CE1 1 ? 
ATOM   518  C  CE2 . PHE   A 1 71  ? -13.913 50.348 40.943 1.000 22.167  ? 70  PHE   AAA CE2 1 ? 
ATOM   519  C  CZ  . PHE   A 1 71  ? -13.229 49.136 40.910 1.000 22.188  ? 70  PHE   AAA CZ  1 ? 
ATOM   520  N  N   . GLU   A 1 72  ? -18.531 50.990 45.200 1.000 23.159  ? 71  GLU   AAA N   1 ? 
ATOM   521  C  CA  . GLU   A 1 72  ? -19.841 51.533 45.595 1.000 25.312  ? 71  GLU   AAA CA  1 ? 
ATOM   522  C  C   . GLU   A 1 72  ? -20.791 51.171 44.463 1.000 26.669  ? 71  GLU   AAA C   1 ? 
ATOM   523  O  O   . GLU   A 1 72  ? -20.441 51.431 43.292 1.000 32.839  ? 71  GLU   AAA O   1 ? 
ATOM   524  C  CB  . GLU   A 1 72  ? -19.758 53.064 45.799 1.000 28.926  ? 71  GLU   AAA CB  1 ? 
ATOM   525  C  CG  . GLU   A 1 72  ? -18.814 53.522 46.924 1.000 29.007  ? 71  GLU   AAA CG  1 ? 
ATOM   526  C  CD  . GLU   A 1 72  ? -18.782 55.024 47.136 1.000 36.776  ? 71  GLU   AAA CD  1 ? 
ATOM   527  O  OE1 . GLU   A 1 72  ? -19.496 55.730 46.414 1.000 37.948  ? 71  GLU   AAA OE1 1 ? 
ATOM   528  O  OE2 . GLU   A 1 72  ? -18.015 55.477 47.989 1.000 42.682  ? 71  GLU   AAA OE2 1 ? 
ATOM   529  N  N   . ASP   A 1 73  ? -21.910 50.531 44.840 1.000 27.321  ? 72  ASP   AAA N   1 ? 
ATOM   530  C  CA  . ASP   A 1 73  ? -22.939 50.030 43.897 1.000 24.159  ? 72  ASP   AAA CA  1 ? 
ATOM   531  C  C   . ASP   A 1 73  ? -24.335 50.470 44.323 1.000 29.772  ? 72  ASP   AAA C   1 ? 
ATOM   532  O  O   . ASP   A 1 73  ? -25.298 49.692 44.113 1.000 30.035  ? 72  ASP   AAA O   1 ? 
ATOM   533  C  CB  . ASP   A 1 73  ? -22.845 48.512 43.808 1.000 27.025  ? 72  ASP   AAA CB  1 ? 
ATOM   534  C  CG  . ASP   A 1 73  ? -23.306 47.756 45.044 1.000 30.255  ? 72  ASP   AAA CG  1 ? 
ATOM   535  O  OD1 . ASP   A 1 73  ? -23.298 48.346 46.128 1.000 28.131  ? 72  ASP   AAA OD1 1 ? 
ATOM   536  O  OD2 . ASP   A 1 73  ? -23.592 46.539 44.915 1.000 30.797  ? 72  ASP   AAA OD2 1 ? 
ATOM   537  N  N   . ASN   A 1 74  ? -24.451 51.729 44.756 1.000 30.361  ? 73  ASN   AAA N   1 ? 
ATOM   538  C  CA  . ASN   A 1 74  ? -25.735 52.321 45.192 1.000 33.675  ? 73  ASN   AAA CA  1 ? 
ATOM   539  C  C   . ASN   A 1 74  ? -26.413 52.966 43.990 1.000 29.851  ? 73  ASN   AAA C   1 ? 
ATOM   540  O  O   . ASN   A 1 74  ? -27.596 53.252 44.092 1.000 37.252  ? 73  ASN   AAA O   1 ? 
ATOM   541  C  CB  . ASN   A 1 74  ? -25.581 53.305 46.358 1.000 35.600  ? 73  ASN   AAA CB  1 ? 
ATOM   542  C  CG  . ASN   A 1 74  ? -24.561 54.383 46.081 1.000 45.218  ? 73  ASN   AAA CG  1 ? 
ATOM   543  O  OD1 . ASN   A 1 74  ? -24.909 55.543 45.866 1.000 62.958  ? 73  ASN   AAA OD1 1 ? 
ATOM   544  N  ND2 . ASN   A 1 74  ? -23.302 53.998 46.035 1.000 33.247  ? 73  ASN   AAA ND2 1 ? 
ATOM   545  N  N   . ASP   A 1 75  ? -25.712 53.150 42.885 1.000 29.119  ? 74  ASP   AAA N   1 ? 
ATOM   546  C  CA  . ASP   A 1 75  ? -26.308 53.799 41.692 1.000 30.827  ? 74  ASP   AAA CA  1 ? 
ATOM   547  C  C   . ASP   A 1 75  ? -25.581 53.318 40.451 1.000 33.763  ? 74  ASP   AAA C   1 ? 
ATOM   548  O  O   . ASP   A 1 75  ? -24.671 52.462 40.576 1.000 32.896  ? 74  ASP   AAA O   1 ? 
ATOM   549  C  CB  . ASP   A 1 75  ? -26.258 55.337 41.821 1.000 33.208  ? 74  ASP   AAA CB  1 ? 
ATOM   550  C  CG  . ASP   A 1 75  ? -24.868 55.959 41.985 1.000 39.785  ? 74  ASP   AAA CG  1 ? 
ATOM   551  O  OD1 . ASP   A 1 75  ? -23.839 55.325 41.629 1.000 33.745  ? 74  ASP   AAA OD1 1 ? 
ATOM   552  O  OD2 . ASP   A 1 75  ? -24.811 57.128 42.404 1.000 38.683  ? 74  ASP   AAA OD2 1 ? 
ATOM   553  N  N   . ASN   A 1 76  ? -25.940 53.896 39.308 1.000 34.347  ? 75  ASN   AAA N   1 ? 
ATOM   554  C  CA  . ASN   A 1 76  ? -25.479 53.452 37.973 1.000 37.289  ? 75  ASN   AAA CA  1 ? 
ATOM   555  C  C   . ASN   A 1 76  ? -24.341 54.354 37.473 1.000 31.149  ? 75  ASN   AAA C   1 ? 
ATOM   556  O  O   . ASN   A 1 76  ? -24.199 54.491 36.224 1.000 32.648  ? 75  ASN   AAA O   1 ? 
ATOM   557  C  CB  . ASN   A 1 76  ? -26.664 53.350 37.008 1.000 33.891  ? 75  ASN   AAA CB  1 ? 
ATOM   558  C  CG  . ASN   A 1 76  ? -27.197 51.932 36.929 1.000 39.428  ? 75  ASN   AAA CG  1 ? 
ATOM   559  O  OD1 . ASN   A 1 76  ? -26.899 51.103 37.770 1.000 36.065  ? 75  ASN   AAA OD1 1 ? 
ATOM   560  N  ND2 . ASN   A 1 76  ? -27.966 51.628 35.906 1.000 53.151  ? 75  ASN   AAA ND2 1 ? 
ATOM   561  N  N   . ARG   A 1 77  ? -23.489 54.862 38.374 1.000 34.971  ? 76  ARG   AAA N   1 ? 
ATOM   562  C  CA  . ARG   A 1 77  ? -22.238 55.558 37.962 1.000 31.140  ? 76  ARG   AAA CA  1 ? 
ATOM   563  C  C   . ARG   A 1 77  ? -21.330 54.643 37.128 1.000 30.984  ? 76  ARG   AAA C   1 ? 
ATOM   564  O  O   . ARG   A 1 77  ? -20.592 55.204 36.266 1.000 30.660  ? 76  ARG   AAA O   1 ? 
ATOM   565  C  CB  . ARG   A 1 77  ? -21.512 56.103 39.180 1.000 32.483  ? 76  ARG   AAA CB  1 ? 
ATOM   566  C  CG  . ARG   A 1 77  ? -22.104 57.442 39.655 1.000 30.388  ? 76  ARG   AAA CG  1 ? 
ATOM   567  C  CD  . ARG   A 1 77  ? -21.472 57.937 40.934 1.000 31.771  ? 76  ARG   AAA CD  1 ? 
ATOM   568  N  NE  . ARG   A 1 77  ? -21.637 56.988 42.020 1.000 34.748  ? 76  ARG   AAA NE  1 ? 
ATOM   569  C  CZ  . ARG   A 1 77  ? -20.868 56.931 43.103 1.000 34.418  ? 76  ARG   AAA CZ  1 ? 
ATOM   570  N  NH1 . ARG   A 1 77  ? -19.881 57.796 43.262 1.000 33.590  ? 76  ARG   AAA NH1 1 ? 
ATOM   571  N  NH2 . ARG   A 1 77  ? -21.094 56.010 44.038 1.000 36.053  ? 76  ARG   AAA NH2 1 ? 
ATOM   572  N  N   . SER   A 1 78  ? -21.337 53.323 37.359 1.000 29.367  ? 77  SER   AAA N   1 ? 
ATOM   573  C  CA  . SER   A 1 78  ? -20.345 52.393 36.773 1.000 28.976  ? 77  SER   AAA CA  1 ? 
ATOM   574  C  C   . SER   A 1 78  ? -21.093 51.192 36.180 1.000 26.720  ? 77  SER   AAA C   1 ? 
ATOM   575  O  O   . SER   A 1 78  ? -21.701 50.473 36.979 1.000 25.295  ? 77  SER   AAA O   1 ? 
ATOM   576  C  CB  . SER   A 1 78  ? -19.330 51.938 37.797 1.000 26.442  ? 77  SER   AAA CB  1 ? 
ATOM   577  O  OG  . SER   A 1 78  ? -18.473 52.982 38.214 1.000 27.230  ? 77  SER   AAA OG  1 ? 
ATOM   578  N  N   . VAL   A 1 79  ? -21.190 51.116 34.851 1.000 24.434  ? 78  VAL   AAA N   1 ? 
ATOM   579  C  CA  . VAL   A 1 79  ? -22.136 50.187 34.190 1.000 28.932  ? 78  VAL   AAA CA  1 ? 
ATOM   580  C  C   . VAL   A 1 79  ? -21.490 49.509 32.999 1.000 28.032  ? 78  VAL   AAA C   1 ? 
ATOM   581  O  O   . VAL   A 1 79  ? -20.598 50.066 32.390 1.000 27.607  ? 78  VAL   AAA O   1 ? 
ATOM   582  C  CB  . VAL   A 1 79  ? -23.436 50.867 33.760 1.000 31.478  ? 78  VAL   AAA CB  1 ? 
ATOM   583  C  CG1 . VAL   A 1 79  ? -24.209 51.348 34.992 1.000 36.097  ? 78  VAL   AAA CG1 1 ? 
ATOM   584  C  CG2 . VAL   A 1 79  ? -23.192 51.983 32.745 1.000 36.809  ? 78  VAL   AAA CG2 1 ? 
ATOM   585  N  N   . LEU   A 1 80  ? -21.968 48.285 32.770 1.000 28.259  ? 79  LEU   AAA N   1 ? 
ATOM   586  C  CA  . LEU   A 1 80  ? -21.782 47.483 31.558 1.000 23.132  ? 79  LEU   AAA CA  1 ? 
ATOM   587  C  C   . LEU   A 1 80  ? -23.087 47.431 30.771 1.000 24.229  ? 79  LEU   AAA C   1 ? 
ATOM   588  O  O   . LEU   A 1 80  ? -24.140 47.134 31.371 1.000 28.159  ? 79  LEU   AAA O   1 ? 
ATOM   589  C  CB  . LEU   A 1 80  ? -21.391 46.055 31.995 1.000 24.251  ? 79  LEU   AAA CB  1 ? 
ATOM   590  C  CG  . LEU   A 1 80  ? -21.332 44.971 30.906 1.000 29.051  ? 79  LEU   AAA CG  1 ? 
ATOM   591  C  CD1 . LEU   A 1 80  ? -20.319 45.286 29.821 1.000 28.769  ? 79  LEU   AAA CD1 1 ? 
ATOM   592  C  CD2 . LEU   A 1 80  ? -20.999 43.641 31.532 1.000 30.806  ? 79  LEU   AAA CD2 1 ? 
ATOM   593  N  N   . LYS   A 1 81  ? -22.995 47.619 29.459 1.000 27.818  ? 80  LYS   AAA N   1 ? 
ATOM   594  C  CA  . LYS   A 1 81  ? -24.136 47.521 28.509 1.000 33.927  ? 80  LYS   AAA CA  1 ? 
ATOM   595  C  C   . LYS   A 1 81  ? -23.650 46.841 27.202 1.000 35.518  ? 80  LYS   AAA C   1 ? 
ATOM   596  O  O   . LYS   A 1 81  ? -22.414 46.533 27.048 1.000 36.081  ? 80  LYS   AAA O   1 ? 
ATOM   597  C  CB  . LYS   A 1 81  ? -24.765 48.892 28.203 1.000 41.240  ? 80  LYS   AAA CB  1 ? 
ATOM   598  C  CG  . LYS   A 1 81  ? -25.129 49.781 29.385 1.000 41.322  ? 80  LYS   AAA CG  1 ? 
ATOM   599  C  CD  . LYS   A 1 81  ? -25.512 51.206 28.983 1.000 55.248  ? 80  LYS   AAA CD  1 ? 
ATOM   600  C  CE  . LYS   A 1 81  ? -24.619 51.800 27.909 1.000 61.988  ? 80  LYS   AAA CE  1 ? 
ATOM   601  N  NZ  . LYS   A 1 81  ? -24.551 53.291 27.970 1.000 80.039  ? 80  LYS   AAA NZ  1 ? 
ATOM   602  N  N   . GLY   A 1 82  ? -24.596 46.575 26.297 1.000 36.547  ? 81  GLY   AAA N   1 ? 
ATOM   603  C  CA  . GLY   A 1 82  ? -24.362 45.943 24.987 1.000 38.419  ? 81  GLY   AAA CA  1 ? 
ATOM   604  C  C   . GLY   A 1 82  ? -24.035 44.462 25.102 1.000 31.453  ? 81  GLY   AAA C   1 ? 
ATOM   605  O  O   . GLY   A 1 82  ? -24.583 43.786 25.996 1.000 31.848  ? 81  GLY   AAA O   1 ? 
ATOM   606  N  N   . GLY   A 1 83  ? -23.186 43.978 24.209 1.000 34.466  ? 82  GLY   AAA N   1 ? 
ATOM   607  C  CA  . GLY   A 1 83  ? -22.875 42.535 24.116 1.000 33.287  ? 82  GLY   AAA CA  1 ? 
ATOM   608  C  C   . GLY   A 1 83  ? -24.173 41.766 23.934 1.000 35.138  ? 82  GLY   AAA C   1 ? 
ATOM   609  O  O   . GLY   A 1 83  ? -24.947 42.122 23.041 1.000 39.690  ? 82  GLY   AAA O   1 ? 
ATOM   610  N  N   . PRO   A 1 84  ? -24.472 40.746 24.781 1.000 30.274  ? 83  PRO   AAA N   1 ? 
ATOM   611  C  CA  . PRO   A 1 84  ? -25.746 40.024 24.713 1.000 34.808  ? 83  PRO   AAA CA  1 ? 
ATOM   612  C  C   . PRO   A 1 84  ? -26.890 40.612 25.551 1.000 34.712  ? 83  PRO   AAA C   1 ? 
ATOM   613  O  O   . PRO   A 1 84  ? -27.970 40.074 25.516 1.000 39.417  ? 83  PRO   AAA O   1 ? 
ATOM   614  C  CB  . PRO   A 1 84  ? -25.360 38.648 25.281 1.000 33.718  ? 83  PRO   AAA CB  1 ? 
ATOM   615  C  CG  . PRO   A 1 84  ? -24.348 38.978 26.358 1.000 34.324  ? 83  PRO   AAA CG  1 ? 
ATOM   616  C  CD  . PRO   A 1 84  ? -23.584 40.172 25.801 1.000 32.668  ? 83  PRO   AAA CD  1 ? 
ATOM   617  N  N   . PHE   A 1 85  ? -26.642 41.705 26.268 1.000 36.473  ? 84  PHE   AAA N   1 ? 
ATOM   618  C  CA  . PHE   A 1 85  ? -27.564 42.224 27.296 1.000 36.614  ? 84  PHE   AAA CA  1 ? 
ATOM   619  C  C   . PHE   A 1 85  ? -28.518 43.264 26.723 1.000 38.798  ? 84  PHE   AAA C   1 ? 
ATOM   620  O  O   . PHE   A 1 85  ? -28.071 44.069 25.872 1.000 40.126  ? 84  PHE   AAA O   1 ? 
ATOM   621  C  CB  . PHE   A 1 85  ? -26.747 42.868 28.398 1.000 35.160  ? 84  PHE   AAA CB  1 ? 
ATOM   622  C  CG  . PHE   A 1 85  ? -25.795 41.928 29.061 1.000 36.747  ? 84  PHE   AAA CG  1 ? 
ATOM   623  C  CD1 . PHE   A 1 85  ? -26.267 40.755 29.630 1.000 37.461  ? 84  PHE   AAA CD1 1 ? 
ATOM   624  C  CD2 . PHE   A 1 85  ? -24.430 42.178 29.054 1.000 37.621  ? 84  PHE   AAA CD2 1 ? 
ATOM   625  C  CE1 . PHE   A 1 85  ? -25.386 39.873 30.231 1.000 40.105  ? 84  PHE   AAA CE1 1 ? 
ATOM   626  C  CE2 . PHE   A 1 85  ? -23.553 41.303 29.670 1.000 41.095  ? 84  PHE   AAA CE2 1 ? 
ATOM   627  C  CZ  . PHE   A 1 85  ? -24.035 40.150 30.252 1.000 40.543  ? 84  PHE   AAA CZ  1 ? 
ATOM   628  N  N   . SER   A 1 86  ? -29.760 43.254 27.225 1.000 41.037  ? 85  SER   AAA N   1 ? 
ATOM   629  C  CA  . SER   A 1 86  ? -30.782 44.319 27.053 1.000 42.746  ? 85  SER   AAA CA  1 ? 
ATOM   630  C  C   . SER   A 1 86  ? -30.737 45.300 28.233 1.000 40.201  ? 85  SER   AAA C   1 ? 
ATOM   631  O  O   . SER   A 1 86  ? -31.108 46.469 28.079 1.000 42.036  ? 85  SER   AAA O   1 ? 
ATOM   632  C  CB  . SER   A 1 86  ? -32.140 43.692 26.942 1.000 53.354  ? 85  SER   AAA CB  1 ? 
ATOM   633  O  OG  . SER   A 1 86  ? -32.137 42.692 25.940 1.000 66.389  ? 85  SER   AAA OG  1 ? 
ATOM   634  N  N   . ASP   A 1 87  ? -30.348 44.804 29.396 1.000 35.202  ? 86  ASP   AAA N   1 ? 
ATOM   635  C  CA  . ASP   A 1 87  ? -30.379 45.524 30.691 1.000 42.803  ? 86  ASP   AAA CA  1 ? 
ATOM   636  C  C   . ASP   A 1 87  ? -28.990 46.124 30.968 1.000 33.883  ? 86  ASP   AAA C   1 ? 
ATOM   637  O  O   . ASP   A 1 87  ? -28.006 45.599 30.464 1.000 38.161  ? 86  ASP   AAA O   1 ? 
ATOM   638  C  CB  . ASP   A 1 87  ? -30.809 44.556 31.799 1.000 44.488  ? 86  ASP   AAA CB  1 ? 
ATOM   639  C  CG  . ASP   A 1 87  ? -32.237 44.026 31.693 1.000 41.141  ? 86  ASP   AAA CG  1 ? 
ATOM   640  O  OD1 . ASP   A 1 87  ? -33.160 44.813 31.362 1.000 55.523  ? 86  ASP   AAA OD1 1 ? 
ATOM   641  O  OD2 . ASP   A 1 87  ? -32.423 42.837 31.976 1.000 44.293  ? 86  ASP   AAA OD2 1 ? 
ATOM   642  N  N   . SER   A 1 88  ? -28.920 47.199 31.740 1.000 34.908  ? 87  SER   AAA N   1 ? 
ATOM   643  C  CA  . SER   A 1 88  ? -27.670 47.773 32.282 1.000 34.195  ? 87  SER   AAA CA  1 ? 
ATOM   644  C  C   . SER   A 1 88  ? -27.209 46.894 33.451 1.000 27.370  ? 87  SER   AAA C   1 ? 
ATOM   645  O  O   . SER   A 1 88  ? -28.049 46.608 34.307 1.000 32.574  ? 87  SER   AAA O   1 ? 
ATOM   646  C  CB  . SER   A 1 88  ? -27.949 49.200 32.708 1.000 38.899  ? 87  SER   AAA CB  1 ? 
ATOM   647  O  OG  . SER   A 1 88  ? -26.757 49.906 32.956 1.000 40.498  ? 87  SER   AAA OG  1 ? 
ATOM   648  N  N   . TYR   A 1 89  ? -25.932 46.535 33.526 1.000 25.041  ? 88  TYR   AAA N   1 ? 
ATOM   649  C  CA  . TYR   A 1 89  ? -25.346 45.819 34.690 1.000 24.854  ? 88  TYR   AAA CA  1 ? 
ATOM   650  C  C   . TYR   A 1 89  ? -24.384 46.718 35.472 1.000 23.578  ? 88  TYR   AAA C   1 ? 
ATOM   651  O  O   . TYR   A 1 89  ? -23.476 47.363 34.901 1.000 25.654  ? 88  TYR   AAA O   1 ? 
ATOM   652  C  CB  . TYR   A 1 89  ? -24.634 44.556 34.223 1.000 24.230  ? 88  TYR   AAA CB  1 ? 
ATOM   653  C  CG  . TYR   A 1 89  ? -25.590 43.459 33.838 1.000 25.592  ? 88  TYR   AAA CG  1 ? 
ATOM   654  C  CD1 . TYR   A 1 89  ? -26.320 43.513 32.671 1.000 26.324  ? 88  TYR   AAA CD1 1 ? 
ATOM   655  C  CD2 . TYR   A 1 89  ? -25.769 42.366 34.661 1.000 25.874  ? 88  TYR   AAA CD2 1 ? 
ATOM   656  C  CE1 . TYR   A 1 89  ? -27.190 42.490 32.298 1.000 31.317  ? 88  TYR   AAA CE1 1 ? 
ATOM   657  C  CE2 . TYR   A 1 89  ? -26.640 41.354 34.314 1.000 28.614  ? 88  TYR   AAA CE2 1 ? 
ATOM   658  C  CZ  . TYR   A 1 89  ? -27.341 41.396 33.120 1.000 28.158  ? 88  TYR   AAA CZ  1 ? 
ATOM   659  O  OH  . TYR   A 1 89  ? -28.188 40.377 32.791 1.000 30.283  ? 88  TYR   AAA OH  1 ? 
ATOM   660  N  N   . ARG   A 1 90  ? -24.577 46.751 36.771 1.000 23.576  ? 89  ARG   AAA N   1 ? 
ATOM   661  C  CA  . ARG   A 1 90  ? -23.826 47.618 37.688 1.000 24.795  ? 89  ARG   AAA CA  1 ? 
ATOM   662  C  C   . ARG   A 1 90  ? -22.542 46.951 38.173 1.000 22.080  ? 89  ARG   AAA C   1 ? 
ATOM   663  O  O   . ARG   A 1 90  ? -22.599 45.863 38.777 1.000 23.077  ? 89  ARG   AAA O   1 ? 
ATOM   664  C  CB  . ARG   A 1 90  ? -24.722 47.983 38.872 1.000 25.886  ? 89  ARG   AAA CB  1 ? 
ATOM   665  C  CG  . ARG   A 1 90  ? -24.147 49.083 39.737 1.000 25.840  ? 89  ARG   AAA CG  1 ? 
ATOM   666  C  CD  . ARG   A 1 90  ? -25.112 49.435 40.828 1.000 28.994  ? 89  ARG   AAA CD  1 ? 
ATOM   667  N  NE  . ARG   A 1 90  ? -26.280 50.064 40.221 1.000 30.995  ? 89  ARG   AAA NE  1 ? 
ATOM   668  C  CZ  . ARG   A 1 90  ? -27.364 50.469 40.887 1.000 29.043  ? 89  ARG   AAA CZ  1 ? 
ATOM   669  N  NH1 . ARG   A 1 90  ? -27.448 50.307 42.206 1.000 27.913  ? 89  ARG   AAA NH1 1 ? 
ATOM   670  N  NH2 . ARG   A 1 90  ? -28.370 51.022 40.217 1.000 36.899  ? 89  ARG   AAA NH2 1 ? 
ATOM   671  N  N   . LEU   A 1 91  ? -21.411 47.589 37.964 1.000 21.010  ? 90  LEU   AAA N   1 ? 
ATOM   672  C  CA  . LEU   A 1 91  ? -20.113 47.161 38.522 1.000 21.517  ? 90  LEU   AAA CA  1 ? 
ATOM   673  C  C   . LEU   A 1 91  ? -20.189 47.079 40.035 1.000 20.998  ? 90  LEU   AAA C   1 ? 
ATOM   674  O  O   . LEU   A 1 91  ? -20.643 48.017 40.676 1.000 24.444  ? 90  LEU   AAA O   1 ? 
ATOM   675  C  CB  . LEU   A 1 91  ? -18.999 48.112 38.091 1.000 20.087  ? 90  LEU   AAA CB  1 ? 
ATOM   676  C  CG  . LEU   A 1 91  ? -17.614 47.894 38.680 1.000 21.760  ? 90  LEU   AAA CG  1 ? 
ATOM   677  C  CD1 . LEU   A 1 91  ? -17.017 46.596 38.156 1.000 22.959  ? 90  LEU   AAA CD1 1 ? 
ATOM   678  C  CD2 . LEU   A 1 91  ? -16.702 49.072 38.350 1.000 23.812  ? 90  LEU   AAA CD2 1 ? 
ATOM   679  N  N   . PHE   A 1 92  ? -19.690 45.990 40.616 1.000 21.966  ? 91  PHE   AAA N   1 ? 
ATOM   680  C  CA  . PHE   A 1 92  ? -19.487 45.957 42.089 1.000 21.971  ? 91  PHE   AAA CA  1 ? 
ATOM   681  C  C   . PHE   A 1 92  ? -18.100 45.484 42.535 1.000 19.642  ? 91  PHE   AAA C   1 ? 
ATOM   682  O  O   . PHE   A 1 92  ? -17.790 45.680 43.731 1.000 22.032  ? 91  PHE   AAA O   1 ? 
ATOM   683  C  CB  . PHE   A 1 92  ? -20.628 45.213 42.764 1.000 20.063  ? 91  PHE   AAA CB  1 ? 
ATOM   684  C  CG  . PHE   A 1 92  ? -20.598 43.703 42.586 1.000 21.157  ? 91  PHE   AAA CG  1 ? 
ATOM   685  C  CD1 . PHE   A 1 92  ? -21.138 43.094 41.453 1.000 21.681  ? 91  PHE   AAA CD1 1 ? 
ATOM   686  C  CD2 . PHE   A 1 92  ? -19.996 42.932 43.549 1.000 23.483  ? 91  PHE   AAA CD2 1 ? 
ATOM   687  C  CE1 . PHE   A 1 92  ? -21.108 41.694 41.312 1.000 21.206  ? 91  PHE   AAA CE1 1 ? 
ATOM   688  C  CE2 . PHE   A 1 92  ? -19.954 41.528 43.398 1.000 24.756  ? 91  PHE   AAA CE2 1 ? 
ATOM   689  C  CZ  . PHE   A 1 92  ? -20.526 40.927 42.291 1.000 24.469  ? 91  PHE   AAA CZ  1 ? 
ATOM   690  N  N   . GLN   A 1 93  ? -17.338 44.788 41.687 1.000 22.055  ? 92  GLN   AAA N   1 ? 
ATOM   691  C  CA  . GLN   A 1 93  ? -16.057 44.182 42.144 1.000 21.837  ? 92  GLN   AAA CA  1 ? 
ATOM   692  C  C   . GLN   A 1 93  ? -15.190 43.787 40.961 1.000 17.348  ? 92  GLN   AAA C   1 ? 
ATOM   693  O  O   . GLN   A 1 93  ? -15.746 43.484 39.889 1.000 19.191  ? 92  GLN   AAA O   1 ? 
ATOM   694  C  CB  . GLN   A 1 93  ? -16.379 42.929 42.952 1.000 25.270  ? 92  GLN   AAA CB  1 ? 
ATOM   695  C  CG  . GLN   A 1 93  ? -15.222 42.255 43.661 1.000 25.149  ? 92  GLN   AAA CG  1 ? 
ATOM   696  C  CD  . GLN   A 1 93  ? -15.700 41.017 44.409 1.000 27.119  ? 92  GLN   AAA CD  1 ? 
ATOM   697  O  OE1 . GLN   A 1 93  ? -16.217 41.067 45.532 1.000 30.656  ? 92  GLN   AAA OE1 1 ? 
ATOM   698  N  NE2 . GLN   A 1 93  ? -15.483 39.869 43.790 1.000 23.814  ? 92  GLN   AAA NE2 1 ? 
ATOM   699  N  N   . PHE   A 1 94  ? -13.884 43.731 41.180 1.000 20.137  ? 93  PHE   AAA N   1 ? 
ATOM   700  C  CA  . PHE   A 1 94  ? -13.002 42.888 40.355 1.000 21.401  ? 93  PHE   AAA CA  1 ? 
ATOM   701  C  C   . PHE   A 1 94  ? -12.060 42.136 41.271 1.000 21.586  ? 93  PHE   AAA C   1 ? 
ATOM   702  O  O   . PHE   A 1 94  ? -11.845 42.494 42.449 1.000 20.644  ? 93  PHE   AAA O   1 ? 
ATOM   703  C  CB  . PHE   A 1 94  ? -12.282 43.650 39.247 1.000 22.465  ? 93  PHE   AAA CB  1 ? 
ATOM   704  C  CG  . PHE   A 1 94  ? -11.161 44.537 39.708 1.000 19.665  ? 93  PHE   AAA CG  1 ? 
ATOM   705  C  CD1 . PHE   A 1 94  ? -9.894  44.004 39.875 1.000 27.987  ? 93  PHE   AAA CD1 1 ? 
ATOM   706  C  CD2 . PHE   A 1 94  ? -11.386 45.903 39.966 1.000 20.518  ? 93  PHE   AAA CD2 1 ? 
ATOM   707  C  CE1 . PHE   A 1 94  ? -8.833  44.794 40.295 1.000 22.903  ? 93  PHE   AAA CE1 1 ? 
ATOM   708  C  CE2 . PHE   A 1 94  ? -10.310 46.676 40.352 1.000 21.129  ? 93  PHE   AAA CE2 1 ? 
ATOM   709  C  CZ  . PHE   A 1 94  ? -9.057  46.141 40.533 1.000 21.967  ? 93  PHE   AAA CZ  1 ? 
ATOM   710  N  N   . HIS   A 1 95  ? -11.640 40.986 40.752 1.000 20.018  ? 94  HIS   AAA N   1 ? 
ATOM   711  C  CA  . HIS   A 1 95  ? -10.648 40.138 41.458 1.000 24.029  ? 94  HIS   AAA CA  1 ? 
ATOM   712  C  C   . HIS   A 1 95  ? -9.925  39.259 40.435 1.000 22.225  ? 94  HIS   AAA C   1 ? 
ATOM   713  O  O   . HIS   A 1 95  ? -10.241 39.354 39.223 1.000 20.331  ? 94  HIS   AAA O   1 ? 
ATOM   714  C  CB  . HIS   A 1 95  ? -11.359 39.283 42.518 1.000 21.109  ? 94  HIS   AAA CB  1 ? 
ATOM   715  C  CG  . HIS   A 1 95  ? -12.372 38.360 41.885 1.000 23.166  ? 94  HIS   AAA CG  1 ? 
ATOM   716  N  ND1 . HIS   A 1 95  ? -13.722 38.591 41.989 1.000 20.539  ? 94  HIS   AAA ND1 1 ? 
ATOM   717  C  CD2 . HIS   A 1 95  ? -12.255 37.215 41.138 1.000 20.898  ? 94  HIS   AAA CD2 1 ? 
ATOM   718  C  CE1 . HIS   A 1 95  ? -14.385 37.632 41.357 1.000 24.095  ? 94  HIS   AAA CE1 1 ? 
ATOM   719  N  NE2 . HIS   A 1 95  ? -13.512 36.853 40.735 1.000 23.724  ? 94  HIS   AAA NE2 1 ? 
ATOM   720  N  N   . PHE   A 1 96  ? -8.958  38.466 40.902 1.000 19.160  ? 95  PHE   AAA N   1 ? 
ATOM   721  C  CA  . PHE   A 1 96  ? -8.110  37.649 40.012 1.000 17.307  ? 95  PHE   AAA CA  1 ? 
ATOM   722  C  C   . PHE   A 1 96  ? -8.209  36.207 40.507 1.000 19.731  ? 95  PHE   AAA C   1 ? 
ATOM   723  O  O   . PHE   A 1 96  ? -8.566  35.961 41.675 1.000 25.200  ? 95  PHE   AAA O   1 ? 
ATOM   724  C  CB  . PHE   A 1 96  ? -6.650  38.077 39.979 1.000 18.054  ? 95  PHE   AAA CB  1 ? 
ATOM   725  C  CG  . PHE   A 1 96  ? -6.509  39.530 39.592 1.000 21.543  ? 95  PHE   AAA CG  1 ? 
ATOM   726  C  CD1 . PHE   A 1 96  ? -6.602  40.501 40.560 1.000 22.216  ? 95  PHE   AAA CD1 1 ? 
ATOM   727  C  CD2 . PHE   A 1 96  ? -6.261  39.882 38.284 1.000 21.232  ? 95  PHE   AAA CD2 1 ? 
ATOM   728  C  CE1 . PHE   A 1 96  ? -6.506  41.829 40.190 1.000 23.139  ? 95  PHE   AAA CE1 1 ? 
ATOM   729  C  CE2 . PHE   A 1 96  ? -6.131  41.220 37.926 1.000 22.224  ? 95  PHE   AAA CE2 1 ? 
ATOM   730  C  CZ  . PHE   A 1 96  ? -6.248  42.162 38.890 1.000 21.551  ? 95  PHE   AAA CZ  1 ? 
ATOM   731  N  N   . HIS   A 1 97  ? -7.926  35.290 39.590 1.000 21.609  ? 96  HIS   AAA N   1 ? 
ATOM   732  C  CA  . HIS   A 1 97  ? -7.550  33.906 39.955 1.000 21.884  ? 96  HIS   AAA CA  1 ? 
ATOM   733  C  C   . HIS   A 1 97  ? -6.158  33.607 39.423 1.000 22.693  ? 96  HIS   AAA C   1 ? 
ATOM   734  O  O   . HIS   A 1 97  ? -5.765  34.137 38.363 1.000 21.041  ? 96  HIS   AAA O   1 ? 
ATOM   735  C  CB  . HIS   A 1 97  ? -8.530  32.869 39.400 1.000 22.078  ? 96  HIS   AAA CB  1 ? 
ATOM   736  C  CG  . HIS   A 1 97  ? -9.951  33.063 39.796 1.000 21.678  ? 96  HIS   AAA CG  1 ? 
ATOM   737  N  ND1 . HIS   A 1 97  ? -10.540 32.363 40.830 1.000 19.830  ? 96  HIS   AAA ND1 1 ? 
ATOM   738  C  CD2 . HIS   A 1 97  ? -10.862 34.017 39.474 1.000 19.188  ? 96  HIS   AAA CD2 1 ? 
ATOM   739  C  CE1 . HIS   A 1 97  ? -11.789 32.772 40.988 1.000 19.665  ? 96  HIS   AAA CE1 1 ? 
ATOM   740  N  NE2 . HIS   A 1 97  ? -12.015 33.762 40.181 1.000 21.799  ? 96  HIS   AAA NE2 1 ? 
ATOM   741  N  N   . TRP   A 1 98  ? -5.449  32.740 40.112 1.000 24.479  ? 97  TRP   AAA N   1 ? 
ATOM   742  C  CA  . TRP   A 1 98  ? -4.083  32.365 39.706 1.000 23.644  ? 97  TRP   AAA CA  1 ? 
ATOM   743  C  C   . TRP   A 1 98  ? -3.816  30.915 40.149 1.000 24.460  ? 97  TRP   AAA C   1 ? 
ATOM   744  O  O   . TRP   A 1 98  ? -4.668  30.342 40.822 1.000 26.151  ? 97  TRP   AAA O   1 ? 
ATOM   745  C  CB  . TRP   A 1 98  ? -3.051  33.341 40.262 1.000 23.450  ? 97  TRP   AAA CB  1 ? 
ATOM   746  C  CG  . TRP   A 1 98  ? -3.066  33.395 41.761 1.000 25.226  ? 97  TRP   AAA CG  1 ? 
ATOM   747  C  CD1 . TRP   A 1 98  ? -2.444  32.563 42.652 1.000 31.469  ? 97  TRP   AAA CD1 1 ? 
ATOM   748  C  CD2 . TRP   A 1 98  ? -3.781  34.352 42.553 1.000 25.339  ? 97  TRP   AAA CD2 1 ? 
ATOM   749  N  NE1 . TRP   A 1 98  ? -2.681  32.970 43.932 1.000 27.378  ? 97  TRP   AAA NE1 1 ? 
ATOM   750  C  CE2 . TRP   A 1 98  ? -3.537  34.034 43.905 1.000 26.929  ? 97  TRP   AAA CE2 1 ? 
ATOM   751  C  CE3 . TRP   A 1 98  ? -4.644  35.416 42.257 1.000 30.228  ? 97  TRP   AAA CE3 1 ? 
ATOM   752  C  CZ2 . TRP   A 1 98  ? -4.062  34.782 44.954 1.000 26.176  ? 97  TRP   AAA CZ2 1 ? 
ATOM   753  C  CZ3 . TRP   A 1 98  ? -5.145  36.172 43.308 1.000 24.287  ? 97  TRP   AAA CZ3 1 ? 
ATOM   754  C  CH2 . TRP   A 1 98  ? -4.868  35.849 44.628 1.000 24.612  ? 97  TRP   AAA CH2 1 ? 
ATOM   755  N  N   . GLY   A 1 99  ? -2.676  30.382 39.771 1.000 26.982  ? 98  GLY   AAA N   1 ? 
ATOM   756  C  CA  . GLY   A 1 99  ? -2.302  28.959 39.992 1.000 30.161  ? 98  GLY   AAA CA  1 ? 
ATOM   757  C  C   . GLY   A 1 99  ? -1.028  28.794 40.785 1.000 31.047  ? 98  GLY   AAA C   1 ? 
ATOM   758  O  O   . GLY   A 1 99  ? -0.330  29.767 40.957 1.000 28.282  ? 98  GLY   AAA O   1 ? 
ATOM   759  N  N   . SER   A 1 100 ? -0.688  27.556 41.179 1.000 38.593  ? 99  SER   AAA N   1 ? 
ATOM   760  C  CA  A SER   A 1 100 ? 0.560   27.245 41.921 0.500 39.938  ? 99  SER   AAA CA  1 ? 
ATOM   761  C  CA  B SER   A 1 100 ? 0.561   27.220 41.913 0.500 40.970  ? 99  SER   AAA CA  1 ? 
ATOM   762  C  C   . SER   A 1 100 ? 1.765   27.564 41.033 1.000 41.665  ? 99  SER   AAA C   1 ? 
ATOM   763  O  O   . SER   A 1 100 ? 2.773   27.976 41.589 1.000 47.690  ? 99  SER   AAA O   1 ? 
ATOM   764  C  CB  A SER   A 1 100 ? 0.591   25.818 42.405 0.500 42.165  ? 99  SER   AAA CB  1 ? 
ATOM   765  C  CB  B SER   A 1 100 ? 0.604   25.765 42.333 0.500 40.749  ? 99  SER   AAA CB  1 ? 
ATOM   766  O  OG  A SER   A 1 100 ? 0.099   24.937 41.409 0.500 41.879  ? 99  SER   AAA OG  1 ? 
ATOM   767  O  OG  B SER   A 1 100 ? -0.525  25.411 43.122 0.500 42.786  ? 99  SER   AAA OG  1 ? 
ATOM   768  N  N   . THR   A 1 101 ? 1.625   27.400 39.704 1.000 40.895  ? 100 THR   AAA N   1 ? 
ATOM   769  C  CA  . THR   A 1 101 ? 2.695   27.582 38.689 1.000 42.088  ? 100 THR   AAA CA  1 ? 
ATOM   770  C  C   . THR   A 1 101 ? 2.216   28.570 37.630 1.000 37.808  ? 100 THR   AAA C   1 ? 
ATOM   771  O  O   . THR   A 1 101 ? 0.996   28.690 37.480 1.000 33.701  ? 100 THR   AAA O   1 ? 
ATOM   772  C  CB  . THR   A 1 101 ? 3.052   26.257 37.993 1.000 44.564  ? 100 THR   AAA CB  1 ? 
ATOM   773  O  OG1 . THR   A 1 101 ? 2.001   25.913 37.084 1.000 51.639  ? 100 THR   AAA OG1 1 ? 
ATOM   774  C  CG2 . THR   A 1 101 ? 3.262   25.112 38.961 1.000 53.742  ? 100 THR   AAA CG2 1 ? 
ATOM   775  N  N   . ASN   A 1 102 ? 3.139   29.188 36.880 1.000 37.612  ? 101 ASN   AAA N   1 ? 
ATOM   776  C  CA  . ASN   A 1 102 ? 2.819   29.999 35.673 1.000 34.460  ? 101 ASN   AAA CA  1 ? 
ATOM   777  C  C   . ASN   A 1 102 ? 2.064   29.158 34.615 1.000 35.920  ? 101 ASN   AAA C   1 ? 
ATOM   778  O  O   . ASN   A 1 102 ? 1.309   29.741 33.774 1.000 35.628  ? 101 ASN   AAA O   1 ? 
ATOM   779  C  CB  . ASN   A 1 102 ? 4.093   30.612 35.090 1.000 36.502  ? 101 ASN   AAA CB  1 ? 
ATOM   780  C  CG  . ASN   A 1 102 ? 4.713   31.688 35.961 1.000 34.160  ? 101 ASN   AAA CG  1 ? 
ATOM   781  O  OD1 . ASN   A 1 102 ? 4.143   32.106 36.952 1.000 39.959  ? 101 ASN   AAA OD1 1 ? 
ATOM   782  N  ND2 . ASN   A 1 102 ? 5.889   32.149 35.581 1.000 35.514  ? 101 ASN   AAA ND2 1 ? 
ATOM   783  N  N   . GLU   A 1 103 ? 2.248   27.841 34.611 1.000 35.238  ? 102 GLU   AAA N   1 ? 
ATOM   784  C  CA  . GLU   A 1 103 ? 1.738   26.925 33.535 1.000 37.477  ? 102 GLU   AAA CA  1 ? 
ATOM   785  C  C   . GLU   A 1 103 ? 0.212   26.876 33.567 1.000 32.703  ? 102 GLU   AAA C   1 ? 
ATOM   786  O  O   . GLU   A 1 103 ? -0.388  26.613 32.530 1.000 35.483  ? 102 GLU   AAA O   1 ? 
ATOM   787  C  CB  . GLU   A 1 103 ? 2.238   25.488 33.691 1.000 47.525  ? 102 GLU   AAA CB  1 ? 
ATOM   788  C  CG  . GLU   A 1 103 ? 3.751   25.346 33.608 1.000 55.251  ? 102 GLU   AAA CG  1 ? 
ATOM   789  C  CD  . GLU   A 1 103 ? 4.452   25.132 34.946 1.000 72.293  ? 102 GLU   AAA CD  1 ? 
ATOM   790  O  OE1 . GLU   A 1 103 ? 4.908   26.144 35.510 1.000 72.504  ? 102 GLU   AAA OE1 1 ? 
ATOM   791  O  OE2 . GLU   A 1 103 ? 4.543   23.948 35.434 1.000 80.530  ? 102 GLU   AAA OE2 1 ? 
ATOM   792  N  N   . HIS   A 1 104 ? -0.391  27.123 34.728 1.000 34.962  ? 103 HIS   AAA N   1 ? 
ATOM   793  C  CA  A HIS   A 1 104 ? -1.856  27.182 34.921 0.500 34.482  ? 103 HIS   AAA CA  1 ? 
ATOM   794  C  CA  B HIS   A 1 104 ? -1.876  27.232 34.838 0.500 31.057  ? 103 HIS   AAA CA  1 ? 
ATOM   795  C  C   . HIS   A 1 104 ? -2.158  28.351 35.855 1.000 39.450  ? 103 HIS   AAA C   1 ? 
ATOM   796  O  O   . HIS   A 1 104 ? -1.186  29.060 36.332 1.000 49.947  ? 103 HIS   AAA O   1 ? 
ATOM   797  C  CB  A HIS   A 1 104 ? -2.340  25.831 35.467 0.500 39.993  ? 103 HIS   AAA CB  1 ? 
ATOM   798  C  CB  B HIS   A 1 104 ? -2.528  25.805 35.009 0.500 25.785  ? 103 HIS   AAA CB  1 ? 
ATOM   799  C  CG  A HIS   A 1 104 ? -2.016  25.661 36.911 0.500 41.014  ? 103 HIS   AAA CG  1 ? 
ATOM   800  C  CG  B HIS   A 1 104 ? -4.027  25.719 34.838 0.500 27.468  ? 103 HIS   AAA CG  1 ? 
ATOM   801  N  ND1 A HIS   A 1 104 ? -0.720  25.521 37.373 0.500 29.768  ? 103 HIS   AAA ND1 1 ? 
ATOM   802  N  ND1 B HIS   A 1 104 ? -4.727  24.531 35.052 0.500 26.995  ? 103 HIS   AAA ND1 1 ? 
ATOM   803  C  CD2 A HIS   A 1 104 ? -2.801  25.678 37.999 0.500 38.767  ? 103 HIS   AAA CD2 1 ? 
ATOM   804  C  CD2 B HIS   A 1 104 ? -4.978  26.656 34.543 0.500 23.024  ? 103 HIS   AAA CD2 1 ? 
ATOM   805  C  CE1 A HIS   A 1 104 ? -0.727  25.412 38.670 0.500 31.051  ? 103 HIS   AAA CE1 1 ? 
ATOM   806  C  CE1 B HIS   A 1 104 ? -6.027  24.727 34.859 0.500 27.103  ? 103 HIS   AAA CE1 1 ? 
ATOM   807  N  NE2 A HIS   A 1 104 ? -1.986  25.498 39.081 0.500 40.070  ? 103 HIS   AAA NE2 1 ? 
ATOM   808  N  NE2 B HIS   A 1 104 ? -6.199  26.011 34.535 0.500 28.423  ? 103 HIS   AAA NE2 1 ? 
ATOM   809  N  N   . GLY   A 1 105 ? -3.403  28.623 36.080 1.000 35.904  ? 104 GLY   AAA N   1 ? 
ATOM   810  C  CA  . GLY   A 1 105 ? -3.782  29.778 36.910 1.000 29.686  ? 104 GLY   AAA CA  1 ? 
ATOM   811  C  C   . GLY   A 1 105 ? -5.075  30.324 36.400 1.000 25.831  ? 104 GLY   AAA C   1 ? 
ATOM   812  O  O   . GLY   A 1 105 ? -5.861  30.767 37.201 1.000 27.548  ? 104 GLY   AAA O   1 ? 
ATOM   813  N  N   . SER   A 1 106 ? -5.281  30.325 35.088 1.000 22.538  ? 105 SER   AAA N   1 ? 
ATOM   814  C  CA  . SER   A 1 106 ? -6.581  30.805 34.552 1.000 25.873  ? 105 SER   AAA CA  1 ? 
ATOM   815  C  C   . SER   A 1 106 ? -7.682  29.803 34.907 1.000 23.473  ? 105 SER   AAA C   1 ? 
ATOM   816  O  O   . SER   A 1 106 ? -7.373  28.647 35.332 1.000 24.667  ? 105 SER   AAA O   1 ? 
ATOM   817  C  CB  . SER   A 1 106 ? -6.551  31.103 33.089 1.000 24.525  ? 105 SER   AAA CB  1 ? 
ATOM   818  O  OG  . SER   A 1 106 ? -6.387  29.925 32.271 1.000 26.247  ? 105 SER   AAA OG  1 ? 
ATOM   819  N  N   . GLU   A 1 107 ? -8.923  30.250 34.821 1.000 25.204  ? 106 GLU   AAA N   1 ? 
ATOM   820  C  CA  . GLU   A 1 107 ? -10.128 29.429 35.056 1.000 25.342  ? 106 GLU   AAA CA  1 ? 
ATOM   821  C  C   . GLU   A 1 107 ? -10.621 28.961 33.706 1.000 23.893  ? 106 GLU   AAA C   1 ? 
ATOM   822  O  O   . GLU   A 1 107 ? -10.584 27.733 33.433 1.000 26.487  ? 106 GLU   AAA O   1 ? 
ATOM   823  C  CB  . GLU   A 1 107 ? -11.147 30.222 35.865 1.000 22.907  ? 106 GLU   AAA CB  1 ? 
ATOM   824  C  CG  . GLU   A 1 107 ? -10.704 30.349 37.297 1.000 25.767  ? 106 GLU   AAA CG  1 ? 
ATOM   825  C  CD  . GLU   A 1 107 ? -11.799 30.483 38.333 1.000 25.401  ? 106 GLU   AAA CD  1 ? 
ATOM   826  O  OE1 . GLU   A 1 107 ? -11.766 29.712 39.280 1.000 22.165  ? 106 GLU   AAA OE1 1 ? 
ATOM   827  O  OE2 . GLU   A 1 107 ? -12.633 31.429 38.217 1.000 24.257  ? 106 GLU   AAA OE2 1 ? 
ATOM   828  N  N   . HIS   A 1 108 ? -10.971 29.873 32.827 1.000 21.120  ? 107 HIS   AAA N   1 ? 
ATOM   829  C  CA  . HIS   A 1 108 ? -11.304 29.499 31.432 1.000 25.094  ? 107 HIS   AAA CA  1 ? 
ATOM   830  C  C   . HIS   A 1 108 ? -10.034 29.031 30.727 1.000 24.715  ? 107 HIS   AAA C   1 ? 
ATOM   831  O  O   . HIS   A 1 108 ? -8.935  29.476 31.071 1.000 24.458  ? 107 HIS   AAA O   1 ? 
ATOM   832  C  CB  . HIS   A 1 108 ? -12.018 30.652 30.702 1.000 25.789  ? 107 HIS   AAA CB  1 ? 
ATOM   833  C  CG  . HIS   A 1 108 ? -13.373 30.913 31.267 1.000 22.083  ? 107 HIS   AAA CG  1 ? 
ATOM   834  N  ND1 . HIS   A 1 108 ? -13.560 31.733 32.368 1.000 21.318  ? 107 HIS   AAA ND1 1 ? 
ATOM   835  C  CD2 . HIS   A 1 108 ? -14.589 30.433 30.918 1.000 27.065  ? 107 HIS   AAA CD2 1 ? 
ATOM   836  C  CE1 . HIS   A 1 108 ? -14.852 31.736 32.666 1.000 22.787  ? 107 HIS   AAA CE1 1 ? 
ATOM   837  N  NE2 . HIS   A 1 108 ? -15.497 30.916 31.807 1.000 24.620  ? 107 HIS   AAA NE2 1 ? 
ATOM   838  N  N   . THR   A 1 109 ? -10.206 28.167 29.732 1.000 25.700  ? 108 THR   AAA N   1 ? 
ATOM   839  C  CA  . THR   A 1 109 ? -9.133  27.794 28.783 1.000 24.575  ? 108 THR   AAA CA  1 ? 
ATOM   840  C  C   . THR   A 1 109 ? -9.659  27.961 27.360 1.000 22.246  ? 108 THR   AAA C   1 ? 
ATOM   841  O  O   . THR   A 1 109 ? -10.883 27.968 27.166 1.000 27.908  ? 108 THR   AAA O   1 ? 
ATOM   842  C  CB  . THR   A 1 109 ? -8.652  26.353 29.000 1.000 23.764  ? 108 THR   AAA CB  1 ? 
ATOM   843  O  OG1 . THR   A 1 109 ? -9.767  25.483 28.846 1.000 30.889  ? 108 THR   AAA OG1 1 ? 
ATOM   844  C  CG2 . THR   A 1 109 ? -8.063  26.175 30.377 1.000 28.759  ? 108 THR   AAA CG2 1 ? 
ATOM   845  N  N   . VAL   A 1 110 ? -8.754  28.138 26.406 1.000 26.551  ? 109 VAL   AAA N   1 ? 
ATOM   846  C  CA  . VAL   A 1 110 ? -9.144  28.318 24.981 1.000 24.834  ? 109 VAL   AAA CA  1 ? 
ATOM   847  C  C   . VAL   A 1 110 ? -8.448  27.257 24.139 1.000 27.704  ? 109 VAL   AAA C   1 ? 
ATOM   848  O  O   . VAL   A 1 110 ? -7.199  27.273 24.076 1.000 25.307  ? 109 VAL   AAA O   1 ? 
ATOM   849  C  CB  . VAL   A 1 110 ? -8.838  29.745 24.499 1.000 26.500  ? 109 VAL   AAA CB  1 ? 
ATOM   850  C  CG1 . VAL   A 1 110 ? -9.276  29.905 23.052 1.000 28.231  ? 109 VAL   AAA CG1 1 ? 
ATOM   851  C  CG2 . VAL   A 1 110 ? -9.503  30.752 25.421 1.000 25.594  ? 109 VAL   AAA CG2 1 ? 
ATOM   852  N  N   . ASP   A 1 111 ? -9.233  26.380 23.524 1.000 28.444  ? 110 ASP   AAA N   1 ? 
ATOM   853  C  CA  . ASP   A 1 111 ? -8.715  25.179 22.788 1.000 34.288  ? 110 ASP   AAA CA  1 ? 
ATOM   854  C  C   . ASP   A 1 111 ? -7.674  24.456 23.645 1.000 31.262  ? 110 ASP   AAA C   1 ? 
ATOM   855  O  O   . ASP   A 1 111 ? -6.600  24.136 23.121 1.000 28.869  ? 110 ASP   AAA O   1 ? 
ATOM   856  C  CB  . ASP   A 1 111 ? -8.110  25.559 21.426 1.000 30.517  ? 110 ASP   AAA CB  1 ? 
ATOM   857  C  CG  . ASP   A 1 111 ? -9.148  26.151 20.495 1.000 28.855  ? 110 ASP   AAA CG  1 ? 
ATOM   858  O  OD1 . ASP   A 1 111 ? -10.224 25.533 20.400 1.000 31.902  ? 110 ASP   AAA OD1 1 ? 
ATOM   859  O  OD2 . ASP   A 1 111 ? -8.903  27.272 19.925 1.000 34.794  ? 110 ASP   AAA OD2 1 ? 
ATOM   860  N  N   . GLY   A 1 112 ? -7.998  24.241 24.917 1.000 30.942  ? 111 GLY   AAA N   1 ? 
ATOM   861  C  CA  . GLY   A 1 112 ? -7.189  23.509 25.907 1.000 31.384  ? 111 GLY   AAA CA  1 ? 
ATOM   862  C  C   . GLY   A 1 112 ? -6.001  24.269 26.461 1.000 26.034  ? 111 GLY   AAA C   1 ? 
ATOM   863  O  O   . GLY   A 1 112 ? -5.371  23.772 27.339 1.000 28.668  ? 111 GLY   AAA O   1 ? 
ATOM   864  N  N   . VAL   A 1 113 ? -5.777  25.533 26.069 1.000 29.672  ? 112 VAL   AAA N   1 ? 
ATOM   865  C  CA  . VAL   A 1 113 ? -4.558  26.258 26.508 1.000 24.267  ? 112 VAL   AAA CA  1 ? 
ATOM   866  C  C   . VAL   A 1 113 ? -4.877  26.964 27.826 1.000 25.791  ? 112 VAL   AAA C   1 ? 
ATOM   867  O  O   . VAL   A 1 113 ? -5.909  27.664 27.901 1.000 28.396  ? 112 VAL   AAA O   1 ? 
ATOM   868  C  CB  . VAL   A 1 113 ? -4.054  27.206 25.403 1.000 28.547  ? 112 VAL   AAA CB  1 ? 
ATOM   869  C  CG1 . VAL   A 1 113 ? -2.909  28.063 25.919 1.000 30.367  ? 112 VAL   AAA CG1 1 ? 
ATOM   870  C  CG2 . VAL   A 1 113 ? -3.656  26.431 24.130 1.000 36.439  ? 112 VAL   AAA CG2 1 ? 
ATOM   871  N  N   . LYS   A 1 114 ? -4.005  26.781 28.813 1.000 25.481  ? 113 LYS   AAA N   1 ? 
ATOM   872  C  CA  . LYS   A 1 114 ? -4.166  27.327 30.190 1.000 27.405  ? 113 LYS   AAA CA  1 ? 
ATOM   873  C  C   . LYS   A 1 114 ? -3.308  28.582 30.283 1.000 27.758  ? 113 LYS   AAA C   1 ? 
ATOM   874  O  O   . LYS   A 1 114 ? -2.156  28.525 29.863 1.000 26.977  ? 113 LYS   AAA O   1 ? 
ATOM   875  C  CB  . LYS   A 1 114 ? -3.757  26.304 31.253 1.000 30.956  ? 113 LYS   AAA CB  1 ? 
ATOM   876  C  CG  . LYS   A 1 114 ? -4.591  25.030 31.215 1.000 35.286  ? 113 LYS   AAA CG  1 ? 
ATOM   877  C  CD  . LYS   A 1 114 ? -4.030  23.870 32.001 1.000 40.862  ? 113 LYS   AAA CD  1 ? 
ATOM   878  C  CE  . LYS   A 1 114 ? -3.309  22.825 31.174 1.000 49.072  ? 113 LYS   AAA CE  1 ? 
ATOM   879  N  NZ  . LYS   A 1 114 ? -3.827  21.448 31.412 1.000 60.091  ? 113 LYS   AAA NZ  1 ? 
ATOM   880  N  N   . TYR   A 1 115 ? -3.878  29.693 30.734 1.000 25.804  ? 114 TYR   AAA N   1 ? 
ATOM   881  C  CA  . TYR   A 1 115 ? -3.099  30.924 30.939 1.000 24.087  ? 114 TYR   AAA CA  1 ? 
ATOM   882  C  C   . TYR   A 1 115 ? -2.657  30.957 32.398 1.000 25.525  ? 114 TYR   AAA C   1 ? 
ATOM   883  O  O   . TYR   A 1 115 ? -3.008  30.028 33.154 1.000 27.791  ? 114 TYR   AAA O   1 ? 
ATOM   884  C  CB  . TYR   A 1 115 ? -3.912  32.085 30.362 1.000 25.895  ? 114 TYR   AAA CB  1 ? 
ATOM   885  C  CG  . TYR   A 1 115 ? -3.941  32.011 28.862 1.000 25.499  ? 114 TYR   AAA CG  1 ? 
ATOM   886  C  CD1 . TYR   A 1 115 ? -2.885  32.519 28.105 1.000 29.256  ? 114 TYR   AAA CD1 1 ? 
ATOM   887  C  CD2 . TYR   A 1 115 ? -4.948  31.328 28.195 1.000 26.798  ? 114 TYR   AAA CD2 1 ? 
ATOM   888  C  CE1 . TYR   A 1 115 ? -2.846  32.358 26.731 1.000 34.711  ? 114 TYR   AAA CE1 1 ? 
ATOM   889  C  CE2 . TYR   A 1 115 ? -4.915  31.157 26.821 1.000 26.797  ? 114 TYR   AAA CE2 1 ? 
ATOM   890  C  CZ  . TYR   A 1 115 ? -3.855  31.656 26.078 1.000 26.715  ? 114 TYR   AAA CZ  1 ? 
ATOM   891  O  OH  . TYR   A 1 115 ? -3.825  31.560 24.712 1.000 30.802  ? 114 TYR   AAA OH  1 ? 
ATOM   892  N  N   . SER   A 1 116 ? -1.899  31.998 32.783 1.000 27.468  ? 115 SER   AAA N   1 ? 
ATOM   893  C  CA  . SER   A 1 116 ? -1.198  32.096 34.087 1.000 26.154  ? 115 SER   AAA CA  1 ? 
ATOM   894  C  C   . SER   A 1 116 ? -2.114  32.670 35.160 1.000 25.851  ? 115 SER   AAA C   1 ? 
ATOM   895  O  O   . SER   A 1 116 ? -1.821  32.461 36.368 1.000 26.145  ? 115 SER   AAA O   1 ? 
ATOM   896  C  CB  . SER   A 1 116 ? 0.039   32.901 33.967 1.000 30.790  ? 115 SER   AAA CB  1 ? 
ATOM   897  O  OG  . SER   A 1 116 ? 0.991   32.176 33.224 1.000 35.669  ? 115 SER   AAA OG  1 ? 
ATOM   898  N  N   . ALA   A 1 117 ? -3.127  33.439 34.738 1.000 22.221  ? 116 ALA   AAA N   1 ? 
ATOM   899  C  CA  . ALA   A 1 117 ? -4.084  34.070 35.659 1.000 26.017  ? 116 ALA   AAA CA  1 ? 
ATOM   900  C  C   . ALA   A 1 117 ? -5.312  34.529 34.878 1.000 21.747  ? 116 ALA   AAA C   1 ? 
ATOM   901  O  O   . ALA   A 1 117 ? -5.314  34.477 33.593 1.000 22.771  ? 116 ALA   AAA O   1 ? 
ATOM   902  C  CB  . ALA   A 1 117 ? -3.397  35.190 36.404 1.000 29.579  ? 116 ALA   AAA CB  1 ? 
ATOM   903  N  N   . GLU   A 1 118 ? -6.328  34.969 35.600 1.000 23.899  ? 117 GLU   AAA N   1 ? 
ATOM   904  C  CA  . GLU   A 1 118 ? -7.551  35.499 34.948 1.000 23.250  ? 117 GLU   AAA CA  1 ? 
ATOM   905  C  C   . GLU   A 1 118 ? -8.121  36.645 35.784 1.000 21.769  ? 117 GLU   AAA C   1 ? 
ATOM   906  O  O   . GLU   A 1 118 ? -8.177  36.514 37.022 1.000 21.436  ? 117 GLU   AAA O   1 ? 
ATOM   907  C  CB  . GLU   A 1 118 ? -8.560  34.383 34.754 1.000 22.216  ? 117 GLU   AAA CB  1 ? 
ATOM   908  C  CG  . GLU   A 1 118 ? -9.769  34.732 33.874 1.000 19.581  ? 117 GLU   AAA CG  1 ? 
ATOM   909  C  CD  . GLU   A 1 118 ? -10.596 33.457 33.568 1.000 21.777  ? 117 GLU   AAA CD  1 ? 
ATOM   910  O  OE1 . GLU   A 1 118 ? -11.889 33.542 33.518 1.000 22.333  ? 117 GLU   AAA OE1 1 ? 
ATOM   911  O  OE2 . GLU   A 1 118 ? -9.933  32.379 33.292 1.000 24.671  ? 117 GLU   AAA OE2 1 ? 
ATOM   912  N  N   . LEU   A 1 119 ? -8.507  37.727 35.093 1.000 21.554  ? 118 LEU   AAA N   1 ? 
ATOM   913  C  CA  . LEU   A 1 119 ? -9.226  38.868 35.697 1.000 22.673  ? 118 LEU   AAA CA  1 ? 
ATOM   914  C  C   . LEU   A 1 119 ? -10.737 38.707 35.508 1.000 18.155  ? 118 LEU   AAA C   1 ? 
ATOM   915  O  O   . LEU   A 1 119 ? -11.182 38.484 34.357 1.000 20.815  ? 118 LEU   AAA O   1 ? 
ATOM   916  C  CB  . LEU   A 1 119 ? -8.732  40.141 35.002 1.000 20.871  ? 118 LEU   AAA CB  1 ? 
ATOM   917  C  CG  . LEU   A 1 119 ? -9.599  41.383 35.195 1.000 18.874  ? 118 LEU   AAA CG  1 ? 
ATOM   918  C  CD1 . LEU   A 1 119 ? -9.501  41.850 36.641 1.000 20.280  ? 118 LEU   AAA CD1 1 ? 
ATOM   919  C  CD2 . LEU   A 1 119 ? -9.131  42.436 34.206 1.000 21.791  ? 118 LEU   AAA CD2 1 ? 
ATOM   920  N  N   . HIS   A 1 120 ? -11.477 38.818 36.582 1.000 19.801  ? 119 HIS   AAA N   1 ? 
ATOM   921  C  CA  . HIS   A 1 120 ? -12.963 38.843 36.604 1.000 21.625  ? 119 HIS   AAA CA  1 ? 
ATOM   922  C  C   . HIS   A 1 120 ? -13.459 40.247 37.004 1.000 20.328  ? 119 HIS   AAA C   1 ? 
ATOM   923  O  O   . HIS   A 1 120 ? -13.169 40.674 38.140 1.000 21.282  ? 119 HIS   AAA O   1 ? 
ATOM   924  C  CB  . HIS   A 1 120 ? -13.505 37.803 37.583 1.000 22.081  ? 119 HIS   AAA CB  1 ? 
ATOM   925  C  CG  . HIS   A 1 120 ? -13.261 36.438 37.064 1.000 19.250  ? 119 HIS   AAA CG  1 ? 
ATOM   926  N  ND1 . HIS   A 1 120 ? -13.360 35.272 37.875 1.000 20.333  ? 119 HIS   AAA ND1 1 ? 
ATOM   927  C  CD2 . HIS   A 1 120 ? -12.957 36.042 35.800 1.000 20.950  ? 119 HIS   AAA CD2 1 ? 
ATOM   928  C  CE1 . HIS   A 1 120 ? -13.094 34.226 37.079 1.000 20.606  ? 119 HIS   AAA CE1 1 ? 
ATOM   929  N  NE2 . HIS   A 1 120 ? -12.901 34.629 35.808 1.000 20.480  ? 119 HIS   AAA NE2 1 ? 
ATOM   930  N  N   . VAL   A 1 121 ? -14.251 40.891 36.146 1.000 19.936  ? 120 VAL   AAA N   1 ? 
ATOM   931  C  CA  . VAL   A 1 121 ? -14.912 42.178 36.501 1.000 19.554  ? 120 VAL   AAA CA  1 ? 
ATOM   932  C  C   . VAL   A 1 121 ? -16.409 41.867 36.626 1.000 19.750  ? 120 VAL   AAA C   1 ? 
ATOM   933  O  O   . VAL   A 1 121 ? -17.055 41.546 35.605 1.000 20.268  ? 120 VAL   AAA O   1 ? 
ATOM   934  C  CB  . VAL   A 1 121 ? -14.573 43.216 35.420 1.000 19.538  ? 120 VAL   AAA CB  1 ? 
ATOM   935  C  CG1 . VAL   A 1 121 ? -15.109 44.595 35.788 1.000 22.191  ? 120 VAL   AAA CG1 1 ? 
ATOM   936  C  CG2 . VAL   A 1 121 ? -13.069 43.323 35.147 1.000 21.357  ? 120 VAL   AAA CG2 1 ? 
ATOM   937  N  N   . ALA   A 1 122 ? -16.943 41.958 37.830 1.000 20.585  ? 121 ALA   AAA N   1 ? 
ATOM   938  C  CA  . ALA   A 1 122 ? -18.257 41.409 38.243 1.000 22.337  ? 121 ALA   AAA CA  1 ? 
ATOM   939  C  C   . ALA   A 1 122 ? -19.306 42.511 38.316 1.000 21.619  ? 121 ALA   AAA C   1 ? 
ATOM   940  O  O   . ALA   A 1 122 ? -18.988 43.596 38.930 1.000 22.236  ? 121 ALA   AAA O   1 ? 
ATOM   941  C  CB  . ALA   A 1 122 ? -18.144 40.738 39.602 1.000 25.534  ? 121 ALA   AAA CB  1 ? 
ATOM   942  N  N   . HIS   A 1 123 ? -20.509 42.218 37.851 1.000 19.849  ? 122 HIS   AAA N   1 ? 
ATOM   943  C  CA  . HIS   A 1 123 ? -21.640 43.168 37.740 1.000 22.213  ? 122 HIS   AAA CA  1 ? 
ATOM   944  C  C   . HIS   A 1 123 ? -22.923 42.448 38.162 1.000 24.007  ? 122 HIS   AAA C   1 ? 
ATOM   945  O  O   . HIS   A 1 123 ? -22.990 41.209 38.025 1.000 23.369  ? 122 HIS   AAA O   1 ? 
ATOM   946  C  CB  . HIS   A 1 123 ? -21.754 43.719 36.313 1.000 21.102  ? 122 HIS   AAA CB  1 ? 
ATOM   947  C  CG  . HIS   A 1 123 ? -20.479 44.135 35.646 1.000 22.583  ? 122 HIS   AAA CG  1 ? 
ATOM   948  N  ND1 . HIS   A 1 123 ? -19.526 43.241 35.183 1.000 24.393  ? 122 HIS   AAA ND1 1 ? 
ATOM   949  C  CD2 . HIS   A 1 123 ? -20.071 45.367 35.234 1.000 23.211  ? 122 HIS   AAA CD2 1 ? 
ATOM   950  C  CE1 . HIS   A 1 123 ? -18.537 43.913 34.615 1.000 23.986  ? 122 HIS   AAA CE1 1 ? 
ATOM   951  N  NE2 . HIS   A 1 123 ? -18.864 45.245 34.639 1.000 21.795  ? 122 HIS   AAA NE2 1 ? 
ATOM   952  N  N   . TRP   A 1 124 ? -23.924 43.195 38.596 1.000 21.796  ? 123 TRP   AAA N   1 ? 
ATOM   953  C  CA  . TRP   A 1 124 ? -25.272 42.667 38.908 1.000 22.706  ? 123 TRP   AAA CA  1 ? 
ATOM   954  C  C   . TRP   A 1 124 ? -26.330 43.479 38.186 1.000 24.530  ? 123 TRP   AAA C   1 ? 
ATOM   955  O  O   . TRP   A 1 124 ? -26.053 44.685 37.848 1.000 27.804  ? 123 TRP   AAA O   1 ? 
ATOM   956  C  CB  . TRP   A 1 124 ? -25.515 42.550 40.415 1.000 22.874  ? 123 TRP   AAA CB  1 ? 
ATOM   957  C  CG  . TRP   A 1 124 ? -25.521 43.843 41.190 1.000 22.065  ? 123 TRP   AAA CG  1 ? 
ATOM   958  C  CD1 . TRP   A 1 124 ? -24.478 44.345 41.907 1.000 25.640  ? 123 TRP   AAA CD1 1 ? 
ATOM   959  C  CD2 . TRP   A 1 124 ? -26.665 44.636 41.531 1.000 24.910  ? 123 TRP   AAA CD2 1 ? 
ATOM   960  N  NE1 . TRP   A 1 124 ? -24.876 45.464 42.592 1.000 27.275  ? 123 TRP   AAA NE1 1 ? 
ATOM   961  C  CE2 . TRP   A 1 124 ? -26.213 45.664 42.393 1.000 24.234  ? 123 TRP   AAA CE2 1 ? 
ATOM   962  C  CE3 . TRP   A 1 124 ? -28.013 44.619 41.158 1.000 27.085  ? 123 TRP   AAA CE3 1 ? 
ATOM   963  C  CZ2 . TRP   A 1 124 ? -27.053 46.658 42.879 1.000 27.075  ? 123 TRP   AAA CZ2 1 ? 
ATOM   964  C  CZ3 . TRP   A 1 124 ? -28.850 45.612 41.642 1.000 31.184  ? 123 TRP   AAA CZ3 1 ? 
ATOM   965  C  CH2 . TRP   A 1 124 ? -28.365 46.611 42.484 1.000 26.199  ? 123 TRP   AAA CH2 1 ? 
ATOM   966  N  N   . ASN   A 1 125 ? -27.446 42.829 37.885 1.000 23.736  ? 124 ASN   AAA N   1 ? 
ATOM   967  C  CA  . ASN   A 1 125 ? -28.544 43.403 37.062 1.000 27.019  ? 124 ASN   AAA CA  1 ? 
ATOM   968  C  C   . ASN   A 1 125 ? -29.379 44.391 37.895 1.000 26.433  ? 124 ASN   AAA C   1 ? 
ATOM   969  O  O   . ASN   A 1 125 ? -30.362 44.006 38.546 1.000 25.599  ? 124 ASN   AAA O   1 ? 
ATOM   970  C  CB  . ASN   A 1 125 ? -29.418 42.312 36.478 1.000 28.403  ? 124 ASN   AAA CB  1 ? 
ATOM   971  C  CG  . ASN   A 1 125 ? -30.375 42.816 35.427 1.000 28.550  ? 124 ASN   AAA CG  1 ? 
ATOM   972  O  OD1 . ASN   A 1 125 ? -30.756 44.009 35.377 1.000 31.211  ? 124 ASN   AAA OD1 1 ? 
ATOM   973  N  ND2 . ASN   A 1 125 ? -30.786 41.888 34.586 1.000 34.579  ? 124 ASN   AAA ND2 1 ? 
ATOM   974  N  N   . SER   A 1 126 ? -29.029 45.668 37.824 1.000 29.323  ? 125 SER   AAA N   1 ? 
ATOM   975  C  CA  . SER   A 1 126 ? -29.763 46.744 38.553 1.000 29.218  ? 125 SER   AAA CA  1 ? 
ATOM   976  C  C   . SER   A 1 126 ? -31.025 47.162 37.774 1.000 30.974  ? 125 SER   AAA C   1 ? 
ATOM   977  O  O   . SER   A 1 126 ? -31.874 47.880 38.350 1.000 33.587  ? 125 SER   AAA O   1 ? 
ATOM   978  C  CB  . SER   A 1 126 ? -28.832 47.893 38.841 1.000 29.165  ? 125 SER   AAA CB  1 ? 
ATOM   979  O  OG  . SER   A 1 126 ? -28.369 48.495 37.629 1.000 29.061  ? 125 SER   AAA OG  1 ? 
ATOM   980  N  N   . ALA   A 1 127 ? -31.193 46.758 36.514 1.000 31.222  ? 126 ALA   AAA N   1 ? 
ATOM   981  C  CA  . ALA   A 1 127 ? -32.450 47.042 35.785 1.000 36.515  ? 126 ALA   AAA CA  1 ? 
ATOM   982  C  C   . ALA   A 1 127 ? -33.573 46.217 36.421 1.000 34.273  ? 126 ALA   AAA C   1 ? 
ATOM   983  O  O   . ALA   A 1 127 ? -34.675 46.737 36.585 1.000 34.486  ? 126 ALA   AAA O   1 ? 
ATOM   984  C  CB  . ALA   A 1 127 ? -32.312 46.753 34.312 1.000 39.908  ? 126 ALA   AAA CB  1 ? 
ATOM   985  N  N   . LYS   A 1 128 ? -33.282 44.974 36.802 1.000 30.365  ? 127 LYS   AAA N   1 ? 
ATOM   986  C  CA  . LYS   A 1 128 ? -34.332 43.982 37.181 1.000 34.135  ? 127 LYS   AAA CA  1 ? 
ATOM   987  C  C   . LYS   A 1 128 ? -34.397 43.843 38.712 1.000 29.783  ? 127 LYS   AAA C   1 ? 
ATOM   988  O  O   . LYS   A 1 128 ? -35.483 43.581 39.208 1.000 40.438  ? 127 LYS   AAA O   1 ? 
ATOM   989  C  CB  . LYS   A 1 128 ? -34.090 42.657 36.444 1.000 38.012  ? 127 LYS   AAA CB  1 ? 
ATOM   990  C  CG  . LYS   A 1 128 ? -34.423 42.698 34.951 1.000 40.772  ? 127 LYS   AAA CG  1 ? 
ATOM   991  C  CD  . LYS   A 1 128 ? -34.709 41.355 34.299 1.000 55.391  ? 127 LYS   AAA CD  1 ? 
ATOM   992  C  CE  . LYS   A 1 128 ? -35.653 40.458 35.073 1.000 53.902  ? 127 LYS   AAA CE  1 ? 
ATOM   993  N  NZ  . LYS   A 1 128 ? -35.830 39.149 34.392 1.000 52.324  ? 127 LYS   AAA NZ  1 ? 
ATOM   994  N  N   . TYR   A 1 129 ? -33.282 44.012 39.433 1.000 28.738  ? 128 TYR   AAA N   1 ? 
ATOM   995  C  CA  . TYR   A 1 129 ? -33.174 43.676 40.879 1.000 32.557  ? 128 TYR   AAA CA  1 ? 
ATOM   996  C  C   . TYR   A 1 129 ? -32.657 44.892 41.634 1.000 28.451  ? 128 TYR   AAA C   1 ? 
ATOM   997  O  O   . TYR   A 1 129 ? -32.185 45.894 40.976 1.000 31.352  ? 128 TYR   AAA O   1 ? 
ATOM   998  C  CB  . TYR   A 1 129 ? -32.329 42.416 41.091 1.000 30.084  ? 128 TYR   AAA CB  1 ? 
ATOM   999  C  CG  . TYR   A 1 129 ? -32.777 41.290 40.206 1.000 31.292  ? 128 TYR   AAA CG  1 ? 
ATOM   1000 C  CD1 . TYR   A 1 129 ? -34.030 40.692 40.373 1.000 29.271  ? 128 TYR   AAA CD1 1 ? 
ATOM   1001 C  CD2 . TYR   A 1 129 ? -31.983 40.880 39.155 1.000 30.128  ? 128 TYR   AAA CD2 1 ? 
ATOM   1002 C  CE1 . TYR   A 1 129 ? -34.464 39.714 39.499 1.000 31.919  ? 128 TYR   AAA CE1 1 ? 
ATOM   1003 C  CE2 . TYR   A 1 129 ? -32.395 39.868 38.304 1.000 32.122  ? 128 TYR   AAA CE2 1 ? 
ATOM   1004 C  CZ  . TYR   A 1 129 ? -33.645 39.313 38.461 1.000 30.832  ? 128 TYR   AAA CZ  1 ? 
ATOM   1005 O  OH  . TYR   A 1 129 ? -34.065 38.340 37.603 1.000 28.122  ? 128 TYR   AAA OH  1 ? 
ATOM   1006 N  N   . SER   A 1 130 ? -32.854 44.892 42.944 1.000 29.448  ? 129 SER   AAA N   1 ? 
ATOM   1007 C  CA  . SER   A 1 130 ? -32.601 46.079 43.796 1.000 32.929  ? 129 SER   AAA CA  1 ? 
ATOM   1008 C  C   . SER   A 1 130 ? -31.330 45.871 44.619 1.000 30.016  ? 129 SER   AAA C   1 ? 
ATOM   1009 O  O   . SER   A 1 130 ? -30.881 46.828 45.254 1.000 32.879  ? 129 SER   AAA O   1 ? 
ATOM   1010 C  CB  . SER   A 1 130 ? -33.784 46.402 44.650 1.000 34.938  ? 129 SER   AAA CB  1 ? 
ATOM   1011 O  OG  . SER   A 1 130 ? -33.937 45.475 45.721 1.000 39.968  ? 129 SER   AAA OG  1 ? 
ATOM   1012 N  N   . SER   A 1 131 ? -30.697 44.702 44.563 1.000 26.527  ? 130 SER   AAA N   1 ? 
ATOM   1013 C  CA  . SER   A 1 131 ? -29.447 44.518 45.343 1.000 29.486  ? 130 SER   AAA CA  1 ? 
ATOM   1014 C  C   . SER   A 1 131 ? -28.672 43.351 44.758 1.000 25.142  ? 130 SER   AAA C   1 ? 
ATOM   1015 O  O   . SER   A 1 131 ? -29.333 42.503 44.097 1.000 26.189  ? 130 SER   AAA O   1 ? 
ATOM   1016 C  CB  . SER   A 1 131 ? -29.709 44.280 46.831 1.000 34.120  ? 130 SER   AAA CB  1 ? 
ATOM   1017 O  OG  . SER   A 1 131 ? -30.189 42.953 47.049 1.000 30.041  ? 130 SER   AAA OG  1 ? 
ATOM   1018 N  N   . LEU   A 1 132 ? -27.356 43.364 44.967 1.000 24.506  ? 131 LEU   AAA N   1 ? 
ATOM   1019 C  CA  . LEU   A 1 132 ? -26.501 42.187 44.681 1.000 22.139  ? 131 LEU   AAA CA  1 ? 
ATOM   1020 C  C   . LEU   A 1 132 ? -27.158 40.961 45.315 1.000 22.425  ? 131 LEU   AAA C   1 ? 
ATOM   1021 O  O   . LEU   A 1 132 ? -27.191 39.912 44.612 1.000 25.680  ? 131 LEU   AAA O   1 ? 
ATOM   1022 C  CB  . LEU   A 1 132 ? -25.077 42.386 45.220 1.000 27.975  ? 131 LEU   AAA CB  1 ? 
ATOM   1023 C  CG  . LEU   A 1 132 ? -24.192 41.140 45.100 1.000 26.202  ? 131 LEU   AAA CG  1 ? 
ATOM   1024 C  CD1 . LEU   A 1 132 ? -24.064 40.736 43.646 1.000 26.001  ? 131 LEU   AAA CD1 1 ? 
ATOM   1025 C  CD2 . LEU   A 1 132 ? -22.823 41.317 45.754 1.000 28.609  ? 131 LEU   AAA CD2 1 ? 
ATOM   1026 N  N   . ALA   A 1 133 ? -27.565 41.037 46.578 1.000 22.929  ? 132 ALA   AAA N   1 ? 
ATOM   1027 C  CA  . ALA   A 1 133 ? -28.018 39.819 47.288 1.000 26.740  ? 132 ALA   AAA CA  1 ? 
ATOM   1028 C  C   . ALA   A 1 133 ? -29.225 39.240 46.549 1.000 23.001  ? 132 ALA   AAA C   1 ? 
ATOM   1029 O  O   . ALA   A 1 133 ? -29.372 37.962 46.450 1.000 27.156  ? 132 ALA   AAA O   1 ? 
ATOM   1030 C  CB  . ALA   A 1 133 ? -28.345 40.104 48.732 1.000 28.695  ? 132 ALA   AAA CB  1 ? 
ATOM   1031 N  N   . GLU   A 1 134 ? -30.120 40.070 46.054 1.000 24.730  ? 133 GLU   AAA N   1 ? 
ATOM   1032 C  CA  . GLU   A 1 134 ? -31.326 39.598 45.314 1.000 27.856  ? 133 GLU   AAA CA  1 ? 
ATOM   1033 C  C   . GLU   A 1 134 ? -30.880 39.001 43.976 1.000 26.048  ? 133 GLU   AAA C   1 ? 
ATOM   1034 O  O   . GLU   A 1 134 ? -31.378 37.938 43.613 1.000 28.631  ? 133 GLU   AAA O   1 ? 
ATOM   1035 C  CB  . GLU   A 1 134 ? -32.349 40.732 45.136 1.000 30.502  ? 133 GLU   AAA CB  1 ? 
ATOM   1036 C  CG  . GLU   A 1 134 ? -33.548 40.399 44.246 1.000 26.857  ? 133 GLU   AAA CG  1 ? 
ATOM   1037 C  CD  . GLU   A 1 134 ? -34.576 41.502 43.946 1.000 33.116  ? 133 GLU   AAA CD  1 ? 
ATOM   1038 O  OE1 . GLU   A 1 134 ? -34.243 42.700 44.054 1.000 29.482  ? 133 GLU   AAA OE1 1 ? 
ATOM   1039 O  OE2 . GLU   A 1 134 ? -35.704 41.158 43.535 1.000 36.712  ? 133 GLU   AAA OE2 1 ? 
ATOM   1040 N  N   . ALA   A 1 135 ? -29.972 39.652 43.267 1.000 24.029  ? 134 ALA   AAA N   1 ? 
ATOM   1041 C  CA  . ALA   A 1 135 ? -29.572 39.336 41.873 1.000 23.644  ? 134 ALA   AAA CA  1 ? 
ATOM   1042 C  C   . ALA   A 1 135 ? -28.783 38.011 41.815 1.000 23.666  ? 134 ALA   AAA C   1 ? 
ATOM   1043 O  O   . ALA   A 1 135 ? -28.879 37.312 40.822 1.000 25.489  ? 134 ALA   AAA O   1 ? 
ATOM   1044 C  CB  . ALA   A 1 135 ? -28.772 40.499 41.289 1.000 23.363  ? 134 ALA   AAA CB  1 ? 
ATOM   1045 N  N   . ALA   A 1 136 ? -28.037 37.690 42.859 1.000 23.434  ? 135 ALA   AAA N   1 ? 
ATOM   1046 C  CA  . ALA   A 1 136 ? -26.931 36.721 42.840 1.000 25.771  ? 135 ALA   AAA CA  1 ? 
ATOM   1047 C  C   . ALA   A 1 136 ? -27.449 35.333 42.468 1.000 25.511  ? 135 ALA   AAA C   1 ? 
ATOM   1048 O  O   . ALA   A 1 136 ? -26.667 34.576 41.907 1.000 30.484  ? 135 ALA   AAA O   1 ? 
ATOM   1049 C  CB  . ALA   A 1 136 ? -26.242 36.674 44.165 1.000 27.250  ? 135 ALA   AAA CB  1 ? 
ATOM   1050 N  N   . SER   A 1 137 ? -28.712 35.016 42.743 1.000 26.503  ? 136 SER   AAA N   1 ? 
ATOM   1051 C  CA  . SER   A 1 137 ? -29.248 33.649 42.501 1.000 29.161  ? 136 SER   AAA CA  1 ? 
ATOM   1052 C  C   . SER   A 1 137 ? -30.149 33.578 41.252 1.000 27.704  ? 136 SER   AAA C   1 ? 
ATOM   1053 O  O   . SER   A 1 137 ? -30.652 32.481 40.946 1.000 33.262  ? 136 SER   AAA O   1 ? 
ATOM   1054 C  CB  . SER   A 1 137 ? -29.952 33.173 43.736 1.000 34.084  ? 136 SER   AAA CB  1 ? 
ATOM   1055 O  OG  . SER   A 1 137 ? -31.165 33.869 43.950 1.000 31.732  ? 136 SER   AAA OG  1 ? 
ATOM   1056 N  N   . LYS   A 1 138 ? -30.310 34.667 40.518 1.000 26.689  ? 137 LYS   AAA N   1 ? 
ATOM   1057 C  CA  . LYS   A 1 138 ? -31.219 34.810 39.347 1.000 26.880  ? 137 LYS   AAA CA  1 ? 
ATOM   1058 C  C   . LYS   A 1 138 ? -30.453 34.448 38.060 1.000 26.476  ? 137 LYS   AAA C   1 ? 
ATOM   1059 O  O   . LYS   A 1 138 ? -29.285 34.827 37.924 1.000 24.100  ? 137 LYS   AAA O   1 ? 
ATOM   1060 C  CB  . LYS   A 1 138 ? -31.775 36.246 39.310 1.000 29.735  ? 137 LYS   AAA CB  1 ? 
ATOM   1061 C  CG  . LYS   A 1 138 ? -32.590 36.633 40.538 1.000 30.858  ? 137 LYS   AAA CG  1 ? 
ATOM   1062 C  CD  . LYS   A 1 138 ? -34.054 36.111 40.520 1.000 38.882  ? 137 LYS   AAA CD  1 ? 
ATOM   1063 C  CE  . LYS   A 1 138 ? -34.916 36.587 41.665 1.000 45.759  ? 137 LYS   AAA CE  1 ? 
ATOM   1064 N  NZ  . LYS   A 1 138 ? -34.445 36.025 42.952 1.000 64.460  ? 137 LYS   AAA NZ  1 ? 
ATOM   1065 N  N   . ALA   A 1 139 ? -31.095 33.760 37.124 1.000 29.275  ? 138 ALA   AAA N   1 ? 
ATOM   1066 C  CA  . ALA   A 1 139 ? -30.442 33.318 35.875 1.000 29.476  ? 138 ALA   AAA CA  1 ? 
ATOM   1067 C  C   . ALA   A 1 139 ? -29.830 34.528 35.166 1.000 27.407  ? 138 ALA   AAA C   1 ? 
ATOM   1068 O  O   . ALA   A 1 139 ? -28.777 34.379 34.556 1.000 30.937  ? 138 ALA   AAA O   1 ? 
ATOM   1069 C  CB  . ALA   A 1 139 ? -31.401 32.581 34.964 1.000 31.637  ? 138 ALA   AAA CB  1 ? 
ATOM   1070 N  N   . ASP   A 1 140 ? -30.517 35.672 35.222 1.000 27.753  ? 139 ASP   AAA N   1 ? 
ATOM   1071 C  CA  . ASP   A 1 140 ? -30.068 36.921 34.539 1.000 28.623  ? 139 ASP   AAA CA  1 ? 
ATOM   1072 C  C   . ASP   A 1 140 ? -29.470 37.921 35.541 1.000 26.647  ? 139 ASP   AAA C   1 ? 
ATOM   1073 O  O   . ASP   A 1 140 ? -29.355 39.136 35.191 1.000 32.891  ? 139 ASP   AAA O   1 ? 
ATOM   1074 C  CB  . ASP   A 1 140 ? -31.220 37.541 33.758 1.000 29.575  ? 139 ASP   AAA CB  1 ? 
ATOM   1075 C  CG  . ASP   A 1 140 ? -32.419 37.906 34.603 1.000 30.630  ? 139 ASP   AAA CG  1 ? 
ATOM   1076 O  OD1 . ASP   A 1 140 ? -32.367 37.696 35.816 1.000 27.187  ? 139 ASP   AAA OD1 1 ? 
ATOM   1077 O  OD2 . ASP   A 1 140 ? -33.387 38.453 34.030 1.000 39.604  ? 139 ASP   AAA OD2 1 ? 
ATOM   1078 N  N   . GLY   A 1 141 ? -29.110 37.484 36.732 1.000 24.503  ? 140 GLY   AAA N   1 ? 
ATOM   1079 C  CA  . GLY   A 1 141 ? -28.682 38.402 37.808 1.000 23.274  ? 140 GLY   AAA CA  1 ? 
ATOM   1080 C  C   . GLY   A 1 141 ? -27.282 38.983 37.664 1.000 22.623  ? 140 GLY   AAA C   1 ? 
ATOM   1081 O  O   . GLY   A 1 141 ? -27.088 40.167 38.094 1.000 27.955  ? 140 GLY   AAA O   1 ? 
ATOM   1082 N  N   . LEU   A 1 142 ? -26.324 38.238 37.110 1.000 21.964  ? 141 LEU   AAA N   1 ? 
ATOM   1083 C  CA  . LEU   A 1 142 ? -24.893 38.553 37.160 1.000 22.867  ? 141 LEU   AAA CA  1 ? 
ATOM   1084 C  C   . LEU   A 1 142 ? -24.263 38.518 35.782 1.000 24.453  ? 141 LEU   AAA C   1 ? 
ATOM   1085 O  O   . LEU   A 1 142 ? -24.699 37.746 34.899 1.000 26.779  ? 141 LEU   AAA O   1 ? 
ATOM   1086 C  CB  . LEU   A 1 142 ? -24.125 37.632 38.106 1.000 22.771  ? 141 LEU   AAA CB  1 ? 
ATOM   1087 C  CG  . LEU   A 1 142 ? -24.643 37.551 39.541 1.000 20.650  ? 141 LEU   AAA CG  1 ? 
ATOM   1088 C  CD1 . LEU   A 1 142 ? -23.816 36.548 40.330 1.000 27.233  ? 141 LEU   AAA CD1 1 ? 
ATOM   1089 C  CD2 . LEU   A 1 142 ? -24.697 38.915 40.231 1.000 21.076  ? 141 LEU   AAA CD2 1 ? 
ATOM   1090 N  N   . ALA   A 1 143 ? -23.196 39.304 35.658 1.000 24.248  ? 142 ALA   AAA N   1 ? 
ATOM   1091 C  CA  . ALA   A 1 143 ? -22.374 39.388 34.453 1.000 22.689  ? 142 ALA   AAA CA  1 ? 
ATOM   1092 C  C   . ALA   A 1 143 ? -20.921 39.541 34.884 1.000 23.395  ? 142 ALA   AAA C   1 ? 
ATOM   1093 O  O   . ALA   A 1 143 ? -20.592 40.383 35.786 1.000 25.488  ? 142 ALA   AAA O   1 ? 
ATOM   1094 C  CB  . ALA   A 1 143 ? -22.832 40.501 33.527 1.000 24.988  ? 142 ALA   AAA CB  1 ? 
ATOM   1095 N  N   . VAL   A 1 144 ? -20.064 38.788 34.231 1.000 19.687  ? 143 VAL   AAA N   1 ? 
ATOM   1096 C  CA  . VAL   A 1 144 ? -18.607 38.837 34.481 1.000 18.672  ? 143 VAL   AAA CA  1 ? 
ATOM   1097 C  C   . VAL   A 1 144 ? -17.869 38.994 33.143 1.000 21.249  ? 143 VAL   AAA C   1 ? 
ATOM   1098 O  O   . VAL   A 1 144 ? -18.133 38.241 32.207 1.000 23.790  ? 143 VAL   AAA O   1 ? 
ATOM   1099 C  CB  . VAL   A 1 144 ? -18.068 37.617 35.244 1.000 19.391  ? 143 VAL   AAA CB  1 ? 
ATOM   1100 C  CG1 . VAL   A 1 144 ? -16.576 37.743 35.390 1.000 20.400  ? 143 VAL   AAA CG1 1 ? 
ATOM   1101 C  CG2 . VAL   A 1 144 ? -18.721 37.401 36.586 1.000 21.424  ? 143 VAL   AAA CG2 1 ? 
ATOM   1102 N  N   . ILE   A 1 145 ? -17.024 40.034 33.035 1.000 19.603  ? 144 ILE   AAA N   1 ? 
ATOM   1103 C  CA  . ILE   A 1 145 ? -16.003 40.112 31.963 1.000 20.684  ? 144 ILE   AAA CA  1 ? 
ATOM   1104 C  C   . ILE   A 1 145 ? -14.793 39.352 32.487 1.000 22.660  ? 144 ILE   AAA C   1 ? 
ATOM   1105 O  O   . ILE   A 1 145 ? -14.234 39.764 33.511 1.000 23.462  ? 144 ILE   AAA O   1 ? 
ATOM   1106 C  CB  . ILE   A 1 145 ? -15.635 41.574 31.631 1.000 21.856  ? 144 ILE   AAA CB  1 ? 
ATOM   1107 C  CG1 . ILE   A 1 145 ? -16.851 42.341 31.141 1.000 19.872  ? 144 ILE   AAA CG1 1 ? 
ATOM   1108 C  CG2 . ILE   A 1 145 ? -14.519 41.606 30.595 1.000 27.139  ? 144 ILE   AAA CG2 1 ? 
ATOM   1109 C  CD1 . ILE   A 1 145 ? -16.575 43.836 30.987 1.000 23.842  ? 144 ILE   AAA CD1 1 ? 
ATOM   1110 N  N   . GLY   A 1 146 ? -14.423 38.258 31.824 1.000 23.848  ? 145 GLY   AAA N   1 ? 
ATOM   1111 C  CA  . GLY   A 1 146 ? -13.156 37.564 32.084 1.000 22.770  ? 145 GLY   AAA CA  1 ? 
ATOM   1112 C  C   . GLY   A 1 146 ? -12.099 37.895 31.048 1.000 21.410  ? 145 GLY   AAA C   1 ? 
ATOM   1113 O  O   . GLY   A 1 146 ? -12.375 37.900 29.817 1.000 22.746  ? 145 GLY   AAA O   1 ? 
ATOM   1114 N  N   . VAL   A 1 147 ? -10.903 38.146 31.544 1.000 23.859  ? 146 VAL   AAA N   1 ? 
ATOM   1115 C  CA  . VAL   A 1 147 ? -9.703  38.416 30.723 1.000 19.620  ? 146 VAL   AAA CA  1 ? 
ATOM   1116 C  C   . VAL   A 1 147 ? -8.608  37.401 31.092 1.000 19.545  ? 146 VAL   AAA C   1 ? 
ATOM   1117 O  O   . VAL   A 1 147 ? -8.214  37.312 32.259 1.000 20.145  ? 146 VAL   AAA O   1 ? 
ATOM   1118 C  CB  . VAL   A 1 147 ? -9.219  39.862 30.922 1.000 20.842  ? 146 VAL   AAA CB  1 ? 
ATOM   1119 C  CG1 . VAL   A 1 147 ? -8.089  40.157 29.951 1.000 23.658  ? 146 VAL   AAA CG1 1 ? 
ATOM   1120 C  CG2 . VAL   A 1 147 ? -10.390 40.848 30.786 1.000 23.457  ? 146 VAL   AAA CG2 1 ? 
ATOM   1121 N  N   . LEU   A 1 148 ? -8.171  36.623 30.108 1.000 22.192  ? 147 LEU   AAA N   1 ? 
ATOM   1122 C  CA  . LEU   A 1 148 ? -7.031  35.706 30.282 1.000 25.693  ? 147 LEU   AAA CA  1 ? 
ATOM   1123 C  C   . LEU   A 1 148 ? -5.754  36.513 30.409 1.000 20.853  ? 147 LEU   AAA C   1 ? 
ATOM   1124 O  O   . LEU   A 1 148 ? -5.562  37.483 29.601 1.000 23.818  ? 147 LEU   AAA O   1 ? 
ATOM   1125 C  CB  . LEU   A 1 148 ? -7.006  34.729 29.109 1.000 26.220  ? 147 LEU   AAA CB  1 ? 
ATOM   1126 C  CG  . LEU   A 1 148 ? -8.249  33.839 29.080 1.000 31.306  ? 147 LEU   AAA CG  1 ? 
ATOM   1127 C  CD1 . LEU   A 1 148 ? -8.464  33.251 27.720 1.000 32.357  ? 147 LEU   AAA CD1 1 ? 
ATOM   1128 C  CD2 . LEU   A 1 148 ? -8.160  32.784 30.157 1.000 26.727  ? 147 LEU   AAA CD2 1 ? 
ATOM   1129 N  N   . MET   A 1 149 ? -4.950  36.150 31.396 1.000 23.182  ? 148 MET   AAA N   1 ? 
ATOM   1130 C  CA  . MET   A 1 149 ? -3.648  36.780 31.669 1.000 20.781  ? 148 MET   AAA CA  1 ? 
ATOM   1131 C  C   . MET   A 1 149 ? -2.475  35.880 31.270 1.000 24.157  ? 148 MET   AAA C   1 ? 
ATOM   1132 O  O   . MET   A 1 149 ? -2.330  34.775 31.835 1.000 25.874  ? 148 MET   AAA O   1 ? 
ATOM   1133 C  CB  . MET   A 1 149 ? -3.583  37.247 33.130 1.000 26.879  ? 148 MET   AAA CB  1 ? 
ATOM   1134 C  CG  . MET   A 1 149 ? -4.706  38.254 33.469 1.000 23.447  ? 148 MET   AAA CG  1 ? 
ATOM   1135 S  SD  . MET   A 1 149 ? -4.880  38.693 35.199 1.000 25.372  ? 148 MET   AAA SD  1 ? 
ATOM   1136 C  CE  . MET   A 1 149 ? -3.265  39.354 35.546 1.000 25.050  ? 148 MET   AAA CE  1 ? 
ATOM   1137 N  N   . LYS   A 1 150 ? -1.699  36.350 30.286 1.000 26.991  ? 149 LYS   AAA N   1 ? 
ATOM   1138 C  CA  . LYS   A 1 150 ? -0.575  35.589 29.694 1.000 27.897  ? 149 LYS   AAA CA  1 ? 
ATOM   1139 C  C   . LYS   A 1 150 ? 0.741   36.048 30.326 1.000 23.785  ? 149 LYS   AAA C   1 ? 
ATOM   1140 O  O   . LYS   A 1 150 ? 1.061   37.246 30.245 1.000 28.214  ? 149 LYS   AAA O   1 ? 
ATOM   1141 C  CB  . LYS   A 1 150 ? -0.485  35.707 28.175 1.000 27.919  ? 149 LYS   AAA CB  1 ? 
ATOM   1142 C  CG  . LYS   A 1 150 ? 0.548   34.742 27.568 1.000 29.560  ? 149 LYS   AAA CG  1 ? 
ATOM   1143 C  CD  . LYS   A 1 150 ? 0.635   34.739 26.064 1.000 37.568  ? 149 LYS   AAA CD  1 ? 
ATOM   1144 C  CE  . LYS   A 1 150 ? 0.999   36.094 25.475 1.000 46.155  ? 149 LYS   AAA CE  1 ? 
ATOM   1145 N  NZ  . LYS   A 1 150 ? 2.440   36.438 25.614 1.000 54.515  ? 149 LYS   AAA NZ  1 ? 
ATOM   1146 N  N   . VAL   A 1 151 ? 1.495   35.139 30.935 1.000 27.720  ? 150 VAL   AAA N   1 ? 
ATOM   1147 C  CA  . VAL   A 1 151 ? 2.820   35.460 31.552 1.000 29.283  ? 150 VAL   AAA CA  1 ? 
ATOM   1148 C  C   . VAL   A 1 151 ? 3.761   36.019 30.469 1.000 27.951  ? 150 VAL   AAA C   1 ? 
ATOM   1149 O  O   . VAL   A 1 151 ? 3.824   35.472 29.343 1.000 29.009  ? 150 VAL   AAA O   1 ? 
ATOM   1150 C  CB  . VAL   A 1 151 ? 3.407   34.260 32.324 1.000 29.698  ? 150 VAL   AAA CB  1 ? 
ATOM   1151 C  CG1 . VAL   A 1 151 ? 3.822   33.109 31.423 1.000 32.958  ? 150 VAL   AAA CG1 1 ? 
ATOM   1152 C  CG2 . VAL   A 1 151 ? 4.552   34.667 33.232 1.000 30.735  ? 150 VAL   AAA CG2 1 ? 
ATOM   1153 N  N   . GLY   A 1 152 ? 4.400   37.144 30.781 1.000 28.929  ? 151 GLY   AAA N   1 ? 
ATOM   1154 C  CA  . GLY   A 1 152 ? 5.358   37.824 29.897 1.000 30.864  ? 151 GLY   AAA CA  1 ? 
ATOM   1155 C  C   . GLY   A 1 152 ? 5.822   39.113 30.561 1.000 31.373  ? 151 GLY   AAA C   1 ? 
ATOM   1156 O  O   . GLY   A 1 152 ? 6.239   39.075 31.750 1.000 38.697  ? 151 GLY   AAA O   1 ? 
ATOM   1157 N  N   . GLU   A 1 153 ? 5.697   40.219 29.832 1.000 30.235  ? 152 GLU   AAA N   1 ? 
ATOM   1158 C  CA  . GLU   A 1 153 ? 6.062   41.589 30.267 1.000 34.254  ? 152 GLU   AAA CA  1 ? 
ATOM   1159 C  C   . GLU   A 1 153 ? 5.218   41.972 31.494 1.000 33.663  ? 152 GLU   AAA C   1 ? 
ATOM   1160 O  O   . GLU   A 1 153 ? 3.959   41.742 31.525 1.000 33.585  ? 152 GLU   AAA O   1 ? 
ATOM   1161 C  CB  . GLU   A 1 153 ? 5.790   42.585 29.127 1.000 38.599  ? 152 GLU   AAA CB  1 ? 
ATOM   1162 C  CG  . GLU   A 1 153 ? 6.718   42.468 27.944 1.000 48.058  ? 152 GLU   AAA CG  1 ? 
ATOM   1163 C  CD  . GLU   A 1 153 ? 8.138   42.911 28.234 1.000 63.151  ? 152 GLU   AAA CD  1 ? 
ATOM   1164 O  OE1 . GLU   A 1 153 ? 9.032   42.049 28.213 1.000 72.821  ? 152 GLU   AAA OE1 1 ? 
ATOM   1165 O  OE2 . GLU   A 1 153 ? 8.340   44.124 28.489 1.000 77.795  ? 152 GLU   AAA OE2 1 ? 
ATOM   1166 N  N   . ALA   A 1 154 ? 5.850   42.626 32.445 1.000 36.111  ? 153 ALA   AAA N   1 ? 
ATOM   1167 C  CA  . ALA   A 1 154 ? 5.157   43.286 33.571 1.000 35.405  ? 153 ALA   AAA CA  1 ? 
ATOM   1168 C  C   . ALA   A 1 154 ? 4.058   44.197 33.013 1.000 31.008  ? 153 ALA   AAA C   1 ? 
ATOM   1169 O  O   . ALA   A 1 154 ? 4.244   44.773 31.952 1.000 32.104  ? 153 ALA   AAA O   1 ? 
ATOM   1170 C  CB  . ALA   A 1 154 ? 6.150   44.007 34.439 1.000 36.976  ? 153 ALA   AAA CB  1 ? 
ATOM   1171 N  N   . ASN   A 1 155 ? 2.915   44.236 33.692 1.000 29.280  ? 154 ASN   AAA N   1 ? 
ATOM   1172 C  CA  . ASN   A 1 155 ? 1.730   44.996 33.270 1.000 30.053  ? 154 ASN   AAA CA  1 ? 
ATOM   1173 C  C   . ASN   A 1 155 ? 1.676   46.217 34.173 1.000 28.393  ? 154 ASN   AAA C   1 ? 
ATOM   1174 O  O   . ASN   A 1 155 ? 1.282   46.106 35.327 1.000 32.522  ? 154 ASN   AAA O   1 ? 
ATOM   1175 C  CB  . ASN   A 1 155 ? 0.449   44.183 33.392 1.000 29.981  ? 154 ASN   AAA CB  1 ? 
ATOM   1176 C  CG  . ASN   A 1 155 ? -0.733  44.849 32.737 1.000 28.955  ? 154 ASN   AAA CG  1 ? 
ATOM   1177 O  OD1 . ASN   A 1 155 ? -0.816  46.084 32.715 1.000 31.997  ? 154 ASN   AAA OD1 1 ? 
ATOM   1178 N  ND2 . ASN   A 1 155 ? -1.645  44.054 32.208 1.000 28.113  ? 154 ASN   AAA ND2 1 ? 
ATOM   1179 N  N   . PRO   A 1 156 ? 2.127   47.401 33.711 1.000 33.801  ? 155 PRO   AAA N   1 ? 
ATOM   1180 C  CA  . PRO   A 1 156 ? 2.078   48.586 34.574 1.000 34.635  ? 155 PRO   AAA CA  1 ? 
ATOM   1181 C  C   . PRO   A 1 156 ? 0.655   48.948 35.068 1.000 32.327  ? 155 PRO   AAA C   1 ? 
ATOM   1182 O  O   . PRO   A 1 156 ? 0.565   49.558 36.131 1.000 35.691  ? 155 PRO   AAA O   1 ? 
ATOM   1183 C  CB  . PRO   A 1 156 ? 2.714   49.676 33.684 1.000 36.908  ? 155 PRO   AAA CB  1 ? 
ATOM   1184 C  CG  . PRO   A 1 156 ? 2.592   49.159 32.258 1.000 37.840  ? 155 PRO   AAA CG  1 ? 
ATOM   1185 C  CD  . PRO   A 1 156 ? 2.696   47.656 32.379 1.000 34.200  ? 155 PRO   AAA CD  1 ? 
ATOM   1186 N  N   . LYS   A 1 157 ? -0.417  48.579 34.337 1.000 28.298  ? 156 LYS   AAA N   1 ? 
ATOM   1187 C  CA  . LYS   A 1 157 ? -1.828  48.897 34.730 1.000 33.317  ? 156 LYS   AAA CA  1 ? 
ATOM   1188 C  C   . LYS   A 1 157 ? -2.198  48.173 36.040 1.000 34.062  ? 156 LYS   AAA C   1 ? 
ATOM   1189 O  O   . LYS   A 1 157 ? -3.143  48.641 36.714 1.000 32.749  ? 156 LYS   AAA O   1 ? 
ATOM   1190 C  CB  . LYS   A 1 157 ? -2.884  48.512 33.681 1.000 37.974  ? 156 LYS   AAA CB  1 ? 
ATOM   1191 C  CG  . LYS   A 1 157 ? -2.603  48.866 32.225 1.000 45.017  ? 156 LYS   AAA CG  1 ? 
ATOM   1192 C  CD  . LYS   A 1 157 ? -3.108  50.209 31.791 1.000 52.080  ? 156 LYS   AAA CD  1 ? 
ATOM   1193 C  CE  . LYS   A 1 157 ? -3.424  50.275 30.305 1.000 63.824  ? 156 LYS   AAA CE  1 ? 
ATOM   1194 N  NZ  . LYS   A 1 157 ? -3.069  51.596 29.745 1.000 76.213  ? 156 LYS   AAA NZ  1 ? 
ATOM   1195 N  N   . LEU   A 1 158 ? -1.525  47.067 36.392 1.000 27.415  ? 157 LEU   AAA N   1 ? 
ATOM   1196 C  CA  . LEU   A 1 158 ? -1.767  46.349 37.664 1.000 32.299  ? 157 LEU   AAA CA  1 ? 
ATOM   1197 C  C   . LEU   A 1 158 ? -1.160  47.061 38.870 1.000 32.659  ? 157 LEU   AAA C   1 ? 
ATOM   1198 O  O   . LEU   A 1 158 ? -1.445  46.580 39.975 1.000 35.800  ? 157 LEU   AAA O   1 ? 
ATOM   1199 C  CB  . LEU   A 1 158 ? -1.126  44.967 37.588 1.000 36.001  ? 157 LEU   AAA CB  1 ? 
ATOM   1200 C  CG  . LEU   A 1 158 ? -1.863  43.959 36.734 1.000 36.043  ? 157 LEU   AAA CG  1 ? 
ATOM   1201 C  CD1 . LEU   A 1 158 ? -1.030  42.702 36.582 1.000 35.271  ? 157 LEU   AAA CD1 1 ? 
ATOM   1202 C  CD2 . LEU   A 1 158 ? -3.210  43.617 37.330 1.000 40.627  ? 157 LEU   AAA CD2 1 ? 
ATOM   1203 N  N   . GLN   A 1 159 ? -0.357  48.127 38.686 1.000 40.643  ? 158 GLN   AAA N   1 ? 
ATOM   1204 C  CA  . GLN   A 1 159 ? 0.545   48.658 39.732 1.000 41.406  ? 158 GLN   AAA CA  1 ? 
ATOM   1205 C  C   . GLN   A 1 159 ? -0.238  49.116 40.962 1.000 36.110  ? 158 GLN   AAA C   1 ? 
ATOM   1206 O  O   . GLN   A 1 159 ? 0.194   48.737 42.083 1.000 38.962  ? 158 GLN   AAA O   1 ? 
ATOM   1207 C  CB  . GLN   A 1 159 ? 1.396   49.830 39.233 1.000 45.041  ? 158 GLN   AAA CB  1 ? 
ATOM   1208 C  CG  . GLN   A 1 159 ? 2.474   50.229 40.235 1.000 51.732  ? 158 GLN   AAA CG  1 ? 
ATOM   1209 C  CD  . GLN   A 1 159 ? 3.482   49.110 40.349 1.000 53.722  ? 158 GLN   AAA CD  1 ? 
ATOM   1210 O  OE1 . GLN   A 1 159 ? 4.062   48.703 39.351 1.000 49.189  ? 158 GLN   AAA OE1 1 ? 
ATOM   1211 N  NE2 . GLN   A 1 159 ? 3.675   48.582 41.546 1.000 52.752  ? 158 GLN   AAA NE2 1 ? 
ATOM   1212 N  N   . LYS   A 1 160 ? -1.312  49.901 40.791 1.000 35.522  ? 159 LYS   AAA N   1 ? 
ATOM   1213 C  CA  . LYS   A 1 160 ? -2.047  50.470 41.946 1.000 33.099  ? 159 LYS   AAA CA  1 ? 
ATOM   1214 C  C   . LYS   A 1 160 ? -2.533  49.280 42.753 1.000 34.635  ? 159 LYS   AAA C   1 ? 
ATOM   1215 O  O   . LYS   A 1 160 ? -2.443  49.317 43.991 1.000 33.838  ? 159 LYS   AAA O   1 ? 
ATOM   1216 C  CB  . LYS   A 1 160 ? -3.203  51.389 41.560 1.000 40.347  ? 159 LYS   AAA CB  1 ? 
ATOM   1217 C  CG  . LYS   A 1 160 ? -3.865  52.108 42.740 1.000 48.601  ? 159 LYS   AAA CG  1 ? 
ATOM   1218 C  CD  . LYS   A 1 160 ? -5.285  52.593 42.426 1.000 47.386  ? 159 LYS   AAA CD  1 ? 
ATOM   1219 C  CE  . LYS   A 1 160 ? -6.105  52.906 43.653 1.000 41.056  ? 159 LYS   AAA CE  1 ? 
ATOM   1220 N  NZ  . LYS   A 1 160 ? -5.598  54.115 44.305 1.000 36.790  ? 159 LYS   AAA NZ  1 ? 
ATOM   1221 N  N   . VAL   A 1 161 ? -2.968  48.227 42.062 1.000 31.170  ? 160 VAL   AAA N   1 ? 
ATOM   1222 C  CA  . VAL   A 1 161 ? -3.531  47.042 42.762 1.000 27.284  ? 160 VAL   AAA CA  1 ? 
ATOM   1223 C  C   . VAL   A 1 161 ? -2.427  46.353 43.558 1.000 26.567  ? 160 VAL   AAA C   1 ? 
ATOM   1224 O  O   . VAL   A 1 161 ? -2.647  46.078 44.768 1.000 30.564  ? 160 VAL   AAA O   1 ? 
ATOM   1225 C  CB  . VAL   A 1 161 ? -4.222  46.064 41.818 1.000 28.518  ? 160 VAL   AAA CB  1 ? 
ATOM   1226 C  CG1 . VAL   A 1 161 ? -4.684  44.839 42.599 1.000 34.473  ? 160 VAL   AAA CG1 1 ? 
ATOM   1227 C  CG2 . VAL   A 1 161 ? -5.362  46.718 41.070 1.000 29.952  ? 160 VAL   AAA CG2 1 ? 
ATOM   1228 N  N   . LEU   A 1 162 ? -1.325  46.012 42.900 1.000 32.291  ? 161 LEU   AAA N   1 ? 
ATOM   1229 C  CA  . LEU   A 1 162 ? -0.210  45.294 43.553 1.000 33.575  ? 161 LEU   AAA CA  1 ? 
ATOM   1230 C  C   . LEU   A 1 162 ? 0.323   46.119 44.724 1.000 30.423  ? 161 LEU   AAA C   1 ? 
ATOM   1231 O  O   . LEU   A 1 162 ? 0.551   45.523 45.763 1.000 33.661  ? 161 LEU   AAA O   1 ? 
ATOM   1232 C  CB  . LEU   A 1 162 ? 0.858   45.017 42.506 1.000 36.771  ? 161 LEU   AAA CB  1 ? 
ATOM   1233 C  CG  . LEU   A 1 162 ? 0.414   44.062 41.397 1.000 40.812  ? 161 LEU   AAA CG  1 ? 
ATOM   1234 C  CD1 . LEU   A 1 162 ? 1.427   44.043 40.242 1.000 48.262  ? 161 LEU   AAA CD1 1 ? 
ATOM   1235 C  CD2 . LEU   A 1 162 ? 0.146   42.672 41.952 1.000 44.812  ? 161 LEU   AAA CD2 1 ? 
ATOM   1236 N  N   . ASP   A 1 163 ? 0.475   47.447 44.564 1.000 31.524  ? 162 ASP   AAA N   1 ? 
ATOM   1237 C  CA  . ASP   A 1 163 ? 0.980   48.347 45.636 1.000 32.968  ? 162 ASP   AAA CA  1 ? 
ATOM   1238 C  C   . ASP   A 1 163 ? 0.087   48.197 46.875 1.000 35.295  ? 162 ASP   AAA C   1 ? 
ATOM   1239 O  O   . ASP   A 1 163 ? 0.640   48.316 47.991 1.000 38.794  ? 162 ASP   AAA O   1 ? 
ATOM   1240 C  CB  . ASP   A 1 163 ? 1.088   49.813 45.172 1.000 37.445  ? 162 ASP   AAA CB  1 ? 
ATOM   1241 C  CG  . ASP   A 1 163 ? 2.204   50.113 44.173 1.000 40.191  ? 162 ASP   AAA CG  1 ? 
ATOM   1242 O  OD1 . ASP   A 1 163 ? 2.986   49.186 43.863 1.000 44.384  ? 162 ASP   AAA OD1 1 ? 
ATOM   1243 O  OD2 . ASP   A 1 163 ? 2.300   51.277 43.717 1.000 44.471  ? 162 ASP   AAA OD2 1 ? 
ATOM   1244 N  N   . ALA   A 1 164 ? -1.221  47.930 46.706 1.000 30.819  ? 163 ALA   AAA N   1 ? 
ATOM   1245 C  CA  . ALA   A 1 164 ? -2.219  47.931 47.807 1.000 32.443  ? 163 ALA   AAA CA  1 ? 
ATOM   1246 C  C   . ALA   A 1 164 ? -2.103  46.664 48.668 1.000 28.737  ? 163 ALA   AAA C   1 ? 
ATOM   1247 O  O   . ALA   A 1 164 ? -2.573  46.718 49.798 1.000 29.461  ? 163 ALA   AAA O   1 ? 
ATOM   1248 C  CB  . ALA   A 1 164 ? -3.640  48.133 47.289 1.000 30.802  ? 163 ALA   AAA CB  1 ? 
ATOM   1249 N  N   . LEU   A 1 165 ? -1.523  45.573 48.155 1.000 33.539  ? 164 LEU   AAA N   1 ? 
ATOM   1250 C  CA  . LEU   A 1 165 ? -1.597  44.246 48.835 1.000 32.910  ? 164 LEU   AAA CA  1 ? 
ATOM   1251 C  C   . LEU   A 1 165 ? -0.816  44.257 50.154 1.000 31.904  ? 164 LEU   AAA C   1 ? 
ATOM   1252 O  O   . LEU   A 1 165 ? -1.159  43.438 51.044 1.000 29.535  ? 164 LEU   AAA O   1 ? 
ATOM   1253 C  CB  . LEU   A 1 165 ? -1.042  43.164 47.916 1.000 32.064  ? 164 LEU   AAA CB  1 ? 
ATOM   1254 C  CG  . LEU   A 1 165 ? -1.806  42.977 46.607 1.000 31.257  ? 164 LEU   AAA CG  1 ? 
ATOM   1255 C  CD1 . LEU   A 1 165 ? -1.129  41.955 45.720 1.000 32.181  ? 164 LEU   AAA CD1 1 ? 
ATOM   1256 C  CD2 . LEU   A 1 165 ? -3.250  42.588 46.872 1.000 31.649  ? 164 LEU   AAA CD2 1 ? 
ATOM   1257 N  N   . GLN   A 1 166 ? 0.233   45.099 50.264 1.000 32.989  ? 165 GLN   AAA N   1 ? 
ATOM   1258 C  CA  . GLN   A 1 166 ? 1.058   45.239 51.507 1.000 31.596  ? 165 GLN   AAA CA  1 ? 
ATOM   1259 C  C   . GLN   A 1 166 ? 0.177   45.661 52.706 1.000 31.819  ? 165 GLN   AAA C   1 ? 
ATOM   1260 O  O   . GLN   A 1 166 ? 0.596   45.378 53.855 1.000 30.628  ? 165 GLN   AAA O   1 ? 
ATOM   1261 C  CB  . GLN   A 1 166 ? 2.267   46.178 51.364 1.000 35.051  ? 165 GLN   AAA CB  1 ? 
ATOM   1262 C  CG  . GLN   A 1 166 ? 1.962   47.558 50.775 1.000 39.138  ? 165 GLN   AAA CG  1 ? 
ATOM   1263 C  CD  . GLN   A 1 166 ? 1.102   48.455 51.641 1.000 52.372  ? 165 GLN   AAA CD  1 ? 
ATOM   1264 O  OE1 . GLN   A 1 166 ? 1.241   48.495 52.871 1.000 51.585  ? 165 GLN   AAA OE1 1 ? 
ATOM   1265 N  NE2 . GLN   A 1 166 ? 0.211   49.210 51.003 1.000 55.073  ? 165 GLN   AAA NE2 1 ? 
ATOM   1266 N  N   . ALA   A 1 167 ? -1.000  46.280 52.487 1.000 32.062  ? 166 ALA   AAA N   1 ? 
ATOM   1267 C  CA  . ALA   A 1 167 ? -1.927  46.731 53.573 1.000 32.714  ? 166 ALA   AAA CA  1 ? 
ATOM   1268 C  C   . ALA   A 1 167 ? -2.974  45.653 53.937 1.000 30.534  ? 166 ALA   AAA C   1 ? 
ATOM   1269 O  O   . ALA   A 1 167 ? -3.659  45.832 54.957 1.000 31.677  ? 166 ALA   AAA O   1 ? 
ATOM   1270 C  CB  . ALA   A 1 167 ? -2.602  48.030 53.181 1.000 33.857  ? 166 ALA   AAA CB  1 ? 
ATOM   1271 N  N   . ILE   A 1 168 ? -3.099  44.567 53.146 1.000 27.934  ? 167 ILE   AAA N   1 ? 
ATOM   1272 C  CA  . ILE   A 1 168 ? -4.124  43.502 53.401 1.000 29.610  ? 167 ILE   AAA CA  1 ? 
ATOM   1273 C  C   . ILE   A 1 168 ? -3.446  42.135 53.333 1.000 26.607  ? 167 ILE   AAA C   1 ? 
ATOM   1274 O  O   . ILE   A 1 168 ? -4.015  41.217 52.683 1.000 35.059  ? 167 ILE   AAA O   1 ? 
ATOM   1275 C  CB  . ILE   A 1 168 ? -5.314  43.595 52.423 1.000 25.954  ? 167 ILE   AAA CB  1 ? 
ATOM   1276 C  CG1 . ILE   A 1 168 ? -4.870  43.453 50.963 1.000 29.853  ? 167 ILE   AAA CG1 1 ? 
ATOM   1277 C  CG2 . ILE   A 1 168 ? -6.098  44.888 52.684 1.000 31.343  ? 167 ILE   AAA CG2 1 ? 
ATOM   1278 C  CD1 . ILE   A 1 168 ? -5.874  42.793 50.085 1.000 31.145  ? 167 ILE   AAA CD1 1 ? 
ATOM   1279 N  N   . LYS   A 1 169 ? -2.289  42.010 53.966 1.000 30.091  ? 168 LYS   AAA N   1 ? 
ATOM   1280 C  CA  . LYS   A 1 169 ? -1.426  40.804 53.846 1.000 30.097  ? 168 LYS   AAA CA  1 ? 
ATOM   1281 C  C   . LYS   A 1 169 ? -2.136  39.545 54.346 1.000 27.044  ? 168 LYS   AAA C   1 ? 
ATOM   1282 O  O   . LYS   A 1 169 ? -1.888  38.493 53.743 1.000 31.581  ? 168 LYS   AAA O   1 ? 
ATOM   1283 C  CB  . LYS   A 1 169 ? -0.089  40.983 54.573 1.000 41.523  ? 168 LYS   AAA CB  1 ? 
ATOM   1284 C  CG  . LYS   A 1 169 ? 1.038   41.425 53.661 1.000 52.696  ? 168 LYS   AAA CG  1 ? 
ATOM   1285 C  CD  . LYS   A 1 169 ? 1.536   40.306 52.740 1.000 61.245  ? 168 LYS   AAA CD  1 ? 
ATOM   1286 C  CE  . LYS   A 1 169 ? 2.515   40.832 51.721 1.000 56.509  ? 168 LYS   AAA CE  1 ? 
ATOM   1287 N  NZ  . LYS   A 1 169 ? 2.492   40.005 50.503 1.000 49.975  ? 168 LYS   AAA NZ  1 ? 
ATOM   1288 N  N   . THR   A 1 170 ? -2.944  39.631 55.389 1.000 23.838  ? 169 THR   AAA N   1 ? 
ATOM   1289 C  CA  . THR   A 1 170 ? -3.540  38.463 56.093 1.000 28.262  ? 169 THR   AAA CA  1 ? 
ATOM   1290 C  C   . THR   A 1 170 ? -5.069  38.518 56.008 1.000 30.779  ? 169 THR   AAA C   1 ? 
ATOM   1291 O  O   . THR   A 1 170 ? -5.660  39.649 55.826 1.000 31.634  ? 169 THR   AAA O   1 ? 
ATOM   1292 C  CB  . THR   A 1 170 ? -3.063  38.356 57.550 1.000 30.072  ? 169 THR   AAA CB  1 ? 
ATOM   1293 O  OG1 . THR   A 1 170 ? -3.264  39.593 58.223 1.000 30.441  ? 169 THR   AAA OG1 1 ? 
ATOM   1294 C  CG2 . THR   A 1 170 ? -1.598  37.987 57.656 1.000 29.591  ? 169 THR   AAA CG2 1 ? 
ATOM   1295 N  N   . LYS   A 1 171 ? -5.699  37.350 56.171 1.000 30.955  ? 170 LYS   AAA N   1 ? 
ATOM   1296 C  CA  . LYS   A 1 171 ? -7.162  37.173 56.099 1.000 30.888  ? 170 LYS   AAA CA  1 ? 
ATOM   1297 C  C   . LYS   A 1 171 ? -7.915  38.127 57.028 1.000 31.980  ? 170 LYS   AAA C   1 ? 
ATOM   1298 O  O   . LYS   A 1 171 ? -7.631  38.112 58.245 1.000 36.773  ? 170 LYS   AAA O   1 ? 
ATOM   1299 C  CB  . LYS   A 1 171 ? -7.568  35.801 56.601 1.000 32.870  ? 170 LYS   AAA CB  1 ? 
ATOM   1300 C  CG  . LYS   A 1 171 ? -9.025  35.507 56.338 1.000 32.762  ? 170 LYS   AAA CG  1 ? 
ATOM   1301 C  CD  . LYS   A 1 171 ? -9.350  34.047 56.497 1.000 36.249  ? 170 LYS   AAA CD  1 ? 
ATOM   1302 C  CE  . LYS   A 1 171 ? -10.810 33.779 56.182 1.000 45.634  ? 170 LYS   AAA CE  1 ? 
ATOM   1303 N  NZ  . LYS   A 1 171 ? -11.155 32.334 56.154 1.000 55.657  ? 170 LYS   AAA NZ  1 ? 
ATOM   1304 N  N   . GLY   A 1 172 ? -8.945  38.796 56.508 1.000 32.317  ? 171 GLY   AAA N   1 ? 
ATOM   1305 C  CA  . GLY   A 1 172 ? -9.748  39.738 57.307 1.000 35.387  ? 171 GLY   AAA CA  1 ? 
ATOM   1306 C  C   . GLY   A 1 172 ? -9.249  41.160 57.169 1.000 32.202  ? 171 GLY   AAA C   1 ? 
ATOM   1307 O  O   . GLY   A 1 172 ? -10.022 42.087 57.475 1.000 35.922  ? 171 GLY   AAA O   1 ? 
ATOM   1308 N  N   . LYS   A 1 173 ? -8.037  41.361 56.675 1.000 29.871  ? 172 LYS   AAA N   1 ? 
ATOM   1309 C  CA  . LYS   A 1 173 ? -7.526  42.736 56.542 1.000 31.349  ? 172 LYS   AAA CA  1 ? 
ATOM   1310 C  C   . LYS   A 1 173 ? -8.274  43.390 55.381 1.000 32.526  ? 172 LYS   AAA C   1 ? 
ATOM   1311 O  O   . LYS   A 1 173 ? -8.486  42.748 54.347 1.000 33.105  ? 172 LYS   AAA O   1 ? 
ATOM   1312 C  CB  . LYS   A 1 173 ? -5.997  42.795 56.502 1.000 32.148  ? 172 LYS   AAA CB  1 ? 
ATOM   1313 C  CG  . LYS   A 1 173 ? -5.350  42.762 57.897 1.000 38.381  ? 172 LYS   AAA CG  1 ? 
ATOM   1314 C  CD  . LYS   A 1 173 ? -3.998  43.462 58.064 1.000 47.289  ? 172 LYS   AAA CD  1 ? 
ATOM   1315 C  CE  . LYS   A 1 173 ? -4.050  44.953 58.384 1.000 52.760  ? 172 LYS   AAA CE  1 ? 
ATOM   1316 N  NZ  . LYS   A 1 173 ? -2.797  45.665 57.998 1.000 46.840  ? 172 LYS   AAA NZ  1 ? 
ATOM   1317 N  N   . ARG   A 1 174 ? -8.705  44.628 55.599 1.000 30.172  ? 173 ARG   AAA N   1 ? 
ATOM   1318 C  CA  . ARG   A 1 174 ? -9.388  45.441 54.569 1.000 31.235  ? 173 ARG   AAA CA  1 ? 
ATOM   1319 C  C   . ARG   A 1 174 ? -8.869  46.877 54.668 1.000 32.613  ? 173 ARG   AAA C   1 ? 
ATOM   1320 O  O   . ARG   A 1 174 ? -8.487  47.317 55.766 1.000 32.350  ? 173 ARG   AAA O   1 ? 
ATOM   1321 C  CB  . ARG   A 1 174 ? -10.925 45.368 54.624 1.000 41.059  ? 173 ARG   AAA CB  1 ? 
ATOM   1322 C  CG  . ARG   A 1 174 ? -11.575 45.124 55.968 1.000 52.798  ? 173 ARG   AAA CG  1 ? 
ATOM   1323 C  CD  . ARG   A 1 174 ? -13.090 44.999 55.835 1.000 53.545  ? 173 ARG   AAA CD  1 ? 
ATOM   1324 N  NE  . ARG   A 1 174 ? -13.441 43.595 55.701 1.000 52.796  ? 173 ARG   AAA NE  1 ? 
ATOM   1325 C  CZ  . ARG   A 1 174 ? -14.421 43.088 54.959 1.000 49.655  ? 173 ARG   AAA CZ  1 ? 
ATOM   1326 N  NH1 . ARG   A 1 174 ? -15.233 43.856 54.257 1.000 53.629  ? 173 ARG   AAA NH1 1 ? 
ATOM   1327 N  NH2 . ARG   A 1 174 ? -14.589 41.778 54.926 1.000 51.220  ? 173 ARG   AAA NH2 1 ? 
ATOM   1328 N  N   . ALA   A 1 175 ? -8.835  47.541 53.524 1.000 29.100  ? 174 ALA   AAA N   1 ? 
ATOM   1329 C  CA  . ALA   A 1 175 ? -8.284  48.897 53.402 1.000 28.186  ? 174 ALA   AAA CA  1 ? 
ATOM   1330 C  C   . ALA   A 1 175 ? -9.057  49.648 52.337 1.000 32.387  ? 174 ALA   AAA C   1 ? 
ATOM   1331 O  O   . ALA   A 1 175 ? -9.576  49.037 51.389 1.000 30.879  ? 174 ALA   AAA O   1 ? 
ATOM   1332 C  CB  . ALA   A 1 175 ? -6.817  48.850 53.092 1.000 30.304  ? 174 ALA   AAA CB  1 ? 
ATOM   1333 N  N   . PRO   A 1 176 ? -9.112  51.003 52.449 1.000 33.066  ? 175 PRO   AAA N   1 ? 
ATOM   1334 C  CA  . PRO   A 1 176 ? -9.704  51.807 51.388 1.000 28.060  ? 175 PRO   AAA CA  1 ? 
ATOM   1335 C  C   . PRO   A 1 176 ? -8.912  51.619 50.088 1.000 28.365  ? 175 PRO   AAA C   1 ? 
ATOM   1336 O  O   . PRO   A 1 176 ? -7.701  51.358 50.161 1.000 31.307  ? 175 PRO   AAA O   1 ? 
ATOM   1337 C  CB  . PRO   A 1 176 ? -9.555  53.245 51.862 1.000 30.940  ? 175 PRO   AAA CB  1 ? 
ATOM   1338 C  CG  . PRO   A 1 176 ? -9.312  53.127 53.323 1.000 38.119  ? 175 PRO   AAA CG  1 ? 
ATOM   1339 C  CD  . PRO   A 1 176 ? -8.551  51.838 53.518 1.000 35.547  ? 175 PRO   AAA CD  1 ? 
ATOM   1340 N  N   . PHE   A 1 177 ? -9.600  51.759 48.951 1.000 26.994  ? 176 PHE   AAA N   1 ? 
ATOM   1341 C  CA  . PHE   A 1 177 ? -8.994  51.600 47.610 1.000 24.861  ? 176 PHE   AAA CA  1 ? 
ATOM   1342 C  C   . PHE   A 1 177 ? -9.791  52.496 46.682 1.000 26.884  ? 176 PHE   AAA C   1 ? 
ATOM   1343 O  O   . PHE   A 1 177 ? -10.970 52.190 46.435 1.000 27.048  ? 176 PHE   AAA O   1 ? 
ATOM   1344 C  CB  . PHE   A 1 177 ? -8.940  50.118 47.196 1.000 25.515  ? 176 PHE   AAA CB  1 ? 
ATOM   1345 C  CG  . PHE   A 1 177 ? -8.237  49.907 45.883 1.000 26.291  ? 176 PHE   AAA CG  1 ? 
ATOM   1346 C  CD1 . PHE   A 1 177 ? -8.890  50.111 44.674 1.000 26.979  ? 176 PHE   AAA CD1 1 ? 
ATOM   1347 C  CD2 . PHE   A 1 177 ? -6.885  49.579 45.855 1.000 25.543  ? 176 PHE   AAA CD2 1 ? 
ATOM   1348 C  CE1 . PHE   A 1 177 ? -8.223  49.887 43.469 1.000 29.994  ? 176 PHE   AAA CE1 1 ? 
ATOM   1349 C  CE2 . PHE   A 1 177 ? -6.216  49.399 44.653 1.000 30.988  ? 176 PHE   AAA CE2 1 ? 
ATOM   1350 C  CZ  . PHE   A 1 177 ? -6.894  49.522 43.460 1.000 26.780  ? 176 PHE   AAA CZ  1 ? 
ATOM   1351 N  N   . THR   A 1 178 ? -9.260  53.687 46.401 1.000 28.175  ? 177 THR   AAA N   1 ? 
ATOM   1352 C  CA  . THR   A 1 178 ? -10.095 54.764 45.817 1.000 27.748  ? 177 THR   AAA CA  1 ? 
ATOM   1353 C  C   . THR   A 1 178 ? -9.519  55.221 44.479 1.000 25.484  ? 177 THR   AAA C   1 ? 
ATOM   1354 O  O   . THR   A 1 178 ? -8.333  54.981 44.201 1.000 32.733  ? 177 THR   AAA O   1 ? 
ATOM   1355 C  CB  . THR   A 1 178 ? -10.236 55.874 46.853 1.000 29.173  ? 177 THR   AAA CB  1 ? 
ATOM   1356 O  OG1 . THR   A 1 178 ? -8.911  56.336 47.113 1.000 39.285  ? 177 THR   AAA OG1 1 ? 
ATOM   1357 C  CG2 . THR   A 1 178 ? -10.912 55.379 48.113 1.000 32.234  ? 177 THR   AAA CG2 1 ? 
ATOM   1358 N  N   . ASN   A 1 179 ? -10.373 55.851 43.682 1.000 29.256  ? 178 ASN   AAA N   1 ? 
ATOM   1359 C  CA  . ASN   A 1 179 ? -9.961  56.590 42.465 1.000 28.346  ? 178 ASN   AAA CA  1 ? 
ATOM   1360 C  C   . ASN   A 1 179 ? -9.343  55.593 41.492 1.000 27.203  ? 178 ASN   AAA C   1 ? 
ATOM   1361 O  O   . ASN   A 1 179 ? -8.176  55.715 41.203 1.000 29.131  ? 178 ASN   AAA O   1 ? 
ATOM   1362 C  CB  . ASN   A 1 179 ? -9.017  57.752 42.801 1.000 31.224  ? 178 ASN   AAA CB  1 ? 
ATOM   1363 C  CG  . ASN   A 1 179 ? -8.956  58.756 41.671 1.000 35.235  ? 178 ASN   AAA CG  1 ? 
ATOM   1364 O  OD1 . ASN   A 1 179 ? -9.918  58.869 40.914 1.000 35.543  ? 178 ASN   AAA OD1 1 ? 
ATOM   1365 N  ND2 . ASN   A 1 179 ? -7.884  59.528 41.583 1.000 37.441  ? 178 ASN   AAA ND2 1 ? 
ATOM   1366 N  N   . PHE   A 1 180 ? -10.102 54.583 41.082 1.000 26.541  ? 179 PHE   AAA N   1 ? 
ATOM   1367 C  CA  . PHE   A 1 180 ? -9.591  53.591 40.117 1.000 28.271  ? 179 PHE   AAA CA  1 ? 
ATOM   1368 C  C   . PHE   A 1 180 ? -10.717 53.157 39.178 1.000 23.770  ? 179 PHE   AAA C   1 ? 
ATOM   1369 O  O   . PHE   A 1 180 ? -11.842 52.836 39.618 1.000 28.096  ? 179 PHE   AAA O   1 ? 
ATOM   1370 C  CB  . PHE   A 1 180 ? -8.941  52.440 40.876 1.000 29.901  ? 179 PHE   AAA CB  1 ? 
ATOM   1371 C  CG  . PHE   A 1 180 ? -8.289  51.438 39.965 1.000 29.516  ? 179 PHE   AAA CG  1 ? 
ATOM   1372 C  CD1 . PHE   A 1 180 ? -7.046  51.696 39.409 1.000 30.861  ? 179 PHE   AAA CD1 1 ? 
ATOM   1373 C  CD2 . PHE   A 1 180 ? -8.937  50.261 39.607 1.000 27.894  ? 179 PHE   AAA CD2 1 ? 
ATOM   1374 C  CE1 . PHE   A 1 180 ? -6.444  50.798 38.534 1.000 33.207  ? 179 PHE   AAA CE1 1 ? 
ATOM   1375 C  CE2 . PHE   A 1 180 ? -8.340  49.373 38.714 1.000 27.060  ? 179 PHE   AAA CE2 1 ? 
ATOM   1376 C  CZ  . PHE   A 1 180 ? -7.090  49.620 38.208 1.000 28.310  ? 179 PHE   AAA CZ  1 ? 
ATOM   1377 N  N   . ASP   A 1 181 ? -10.402 53.207 37.896 1.000 26.333  ? 180 ASP   AAA N   1 ? 
ATOM   1378 C  CA  . ASP   A 1 181 ? -11.281 52.778 36.780 1.000 28.813  ? 180 ASP   AAA CA  1 ? 
ATOM   1379 C  C   . ASP   A 1 181 ? -10.763 51.449 36.243 1.000 28.370  ? 180 ASP   AAA C   1 ? 
ATOM   1380 O  O   . ASP   A 1 181 ? -9.742  51.373 35.562 1.000 26.229  ? 180 ASP   AAA O   1 ? 
ATOM   1381 C  CB  . ASP   A 1 181 ? -11.263 53.819 35.665 1.000 27.484  ? 180 ASP   AAA CB  1 ? 
ATOM   1382 C  CG  . ASP   A 1 181 ? -12.068 53.446 34.450 1.000 28.805  ? 180 ASP   AAA CG  1 ? 
ATOM   1383 O  OD1 . ASP   A 1 181 ? -12.596 52.344 34.430 1.000 29.315  ? 180 ASP   AAA OD1 1 ? 
ATOM   1384 O  OD2 . ASP   A 1 181 ? -12.148 54.270 33.554 1.000 32.780  ? 180 ASP   AAA OD2 1 ? 
ATOM   1385 N  N   . PRO   A 1 182 ? -11.416 50.327 36.543 1.000 22.781  ? 181 PRO   AAA N   1 ? 
ATOM   1386 C  CA  . PRO   A 1 182 ? -10.856 49.042 36.127 1.000 26.707  ? 181 PRO   AAA CA  1 ? 
ATOM   1387 C  C   . PRO   A 1 182 ? -11.064 48.722 34.647 1.000 25.924  ? 181 PRO   AAA C   1 ? 
ATOM   1388 O  O   . PRO   A 1 182 ? -10.477 47.753 34.204 1.000 29.028  ? 181 PRO   AAA O   1 ? 
ATOM   1389 C  CB  . PRO   A 1 182 ? -11.575 48.061 37.044 1.000 29.605  ? 181 PRO   AAA CB  1 ? 
ATOM   1390 C  CG  . PRO   A 1 182 ? -12.912 48.732 37.272 1.000 24.145  ? 181 PRO   AAA CG  1 ? 
ATOM   1391 C  CD  . PRO   A 1 182 ? -12.651 50.237 37.323 1.000 22.422  ? 181 PRO   AAA CD  1 ? 
ATOM   1392 N  N   . SER   A 1 183 ? -11.738 49.565 33.860 1.000 26.961  ? 182 SER   AAA N   1 ? 
ATOM   1393 C  CA  . SER   A 1 183 ? -11.672 49.433 32.372 1.000 28.094  ? 182 SER   AAA CA  1 ? 
ATOM   1394 C  C   . SER   A 1 183 ? -10.227 49.592 31.857 1.000 25.078  ? 182 SER   AAA C   1 ? 
ATOM   1395 O  O   . SER   A 1 183 ? -9.943  49.179 30.726 1.000 28.305  ? 182 SER   AAA O   1 ? 
ATOM   1396 C  CB  . SER   A 1 183 ? -12.601 50.390 31.673 1.000 25.979  ? 182 SER   AAA CB  1 ? 
ATOM   1397 O  OG  . SER   A 1 183 ? -12.198 51.755 31.851 1.000 29.994  ? 182 SER   AAA OG  1 ? 
ATOM   1398 N  N   . THR   A 1 184 ? -9.344  50.236 32.632 1.000 23.681  ? 183 THR   AAA N   1 ? 
ATOM   1399 C  CA  . THR   A 1 184 ? -7.903  50.434 32.288 1.000 25.824  ? 183 THR   AAA CA  1 ? 
ATOM   1400 C  C   . THR   A 1 184 ? -7.175  49.082 32.200 1.000 26.341  ? 183 THR   AAA C   1 ? 
ATOM   1401 O  O   . THR   A 1 184 ? -6.098  49.031 31.597 1.000 25.916  ? 183 THR   AAA O   1 ? 
ATOM   1402 C  CB  . THR   A 1 184 ? -7.213  51.378 33.291 1.000 27.746  ? 183 THR   AAA CB  1 ? 
ATOM   1403 O  OG1 . THR   A 1 184 ? -7.223  50.804 34.609 1.000 30.202  ? 183 THR   AAA OG1 1 ? 
ATOM   1404 C  CG2 . THR   A 1 184 ? -7.816  52.780 33.260 1.000 29.432  ? 183 THR   AAA CG2 1 ? 
ATOM   1405 N  N   . LEU   A 1 185 ? -7.745  48.046 32.825 1.000 26.207  ? 184 LEU   AAA N   1 ? 
ATOM   1406 C  CA  . LEU   A 1 185 ? -7.167  46.686 32.861 1.000 25.536  ? 184 LEU   AAA CA  1 ? 
ATOM   1407 C  C   . LEU   A 1 185 ? -7.587  45.842 31.664 1.000 23.151  ? 184 LEU   AAA C   1 ? 
ATOM   1408 O  O   . LEU   A 1 185 ? -6.951  44.768 31.456 1.000 26.328  ? 184 LEU   AAA O   1 ? 
ATOM   1409 C  CB  . LEU   A 1 185 ? -7.646  45.992 34.137 1.000 28.875  ? 184 LEU   AAA CB  1 ? 
ATOM   1410 C  CG  . LEU   A 1 185 ? -7.148  46.569 35.447 1.000 27.401  ? 184 LEU   AAA CG  1 ? 
ATOM   1411 C  CD1 . LEU   A 1 185 ? -7.656  45.749 36.623 1.000 29.401  ? 184 LEU   AAA CD1 1 ? 
ATOM   1412 C  CD2 . LEU   A 1 185 ? -5.644  46.665 35.444 1.000 31.814  ? 184 LEU   AAA CD2 1 ? 
ATOM   1413 N  N   . LEU   A 1 186 ? -8.645  46.211 30.974 1.000 26.954  ? 185 LEU   AAA N   1 ? 
ATOM   1414 C  CA  . LEU   A 1 186 ? -9.155  45.410 29.827 1.000 25.487  ? 185 LEU   AAA CA  1 ? 
ATOM   1415 C  C   . LEU   A 1 186 ? -8.269  45.564 28.600 1.000 26.046  ? 185 LEU   AAA C   1 ? 
ATOM   1416 O  O   . LEU   A 1 186 ? -7.585  46.587 28.360 1.000 29.218  ? 185 LEU   AAA O   1 ? 
ATOM   1417 C  CB  . LEU   A 1 186 ? -10.562 45.892 29.477 1.000 26.080  ? 185 LEU   AAA CB  1 ? 
ATOM   1418 C  CG  . LEU   A 1 186 ? -11.600 45.797 30.595 1.000 22.449  ? 185 LEU   AAA CG  1 ? 
ATOM   1419 C  CD1 . LEU   A 1 186 ? -12.950 46.325 30.150 1.000 27.427  ? 185 LEU   AAA CD1 1 ? 
ATOM   1420 C  CD2 . LEU   A 1 186 ? -11.760 44.346 31.028 1.000 22.620  ? 185 LEU   AAA CD2 1 ? 
ATOM   1421 N  N   . PRO   A 1 187 ? -8.301  44.578 27.705 1.000 24.063  ? 186 PRO   AAA N   1 ? 
ATOM   1422 C  CA  . PRO   A 1 187 ? -7.504  44.638 26.486 1.000 25.520  ? 186 PRO   AAA CA  1 ? 
ATOM   1423 C  C   . PRO   A 1 187 ? -8.065  45.664 25.495 1.000 31.310  ? 186 PRO   AAA C   1 ? 
ATOM   1424 O  O   . PRO   A 1 187 ? -9.225  46.099 25.649 1.000 33.949  ? 186 PRO   AAA O   1 ? 
ATOM   1425 C  CB  . PRO   A 1 187 ? -7.585  43.179 25.934 1.000 24.706  ? 186 PRO   AAA CB  1 ? 
ATOM   1426 C  CG  . PRO   A 1 187 ? -8.896  42.658 26.479 1.000 27.496  ? 186 PRO   AAA CG  1 ? 
ATOM   1427 C  CD  . PRO   A 1 187 ? -9.031  43.304 27.853 1.000 23.441  ? 186 PRO   AAA CD  1 ? 
ATOM   1428 N  N   . SER   A 1 188 ? -7.242  46.043 24.524 1.000 31.032  ? 187 SER   AAA N   1 ? 
ATOM   1429 C  CA  . SER   A 1 188 ? -7.612  47.107 23.553 1.000 35.130  ? 187 SER   AAA CA  1 ? 
ATOM   1430 C  C   . SER   A 1 188 ? -8.779  46.619 22.678 1.000 35.411  ? 187 SER   AAA C   1 ? 
ATOM   1431 O  O   . SER   A 1 188 ? -9.687  47.433 22.436 1.000 40.498  ? 187 SER   AAA O   1 ? 
ATOM   1432 C  CB  . SER   A 1 188 ? -6.436  47.566 22.763 1.000 45.405  ? 187 SER   AAA CB  1 ? 
ATOM   1433 O  OG  . SER   A 1 188 ? -5.775  46.439 22.224 1.000 52.052  ? 187 SER   AAA OG  1 ? 
ATOM   1434 N  N   . SER   A 1 189 ? -8.802  45.325 22.295 1.000 33.342  ? 188 SER   AAA N   1 ? 
ATOM   1435 C  CA  . SER   A 1 189 ? -9.957  44.693 21.617 1.000 33.385  ? 188 SER   AAA CA  1 ? 
ATOM   1436 C  C   . SER   A 1 189 ? -10.894 44.105 22.668 1.000 31.625  ? 188 SER   AAA C   1 ? 
ATOM   1437 O  O   . SER   A 1 189 ? -10.392 43.393 23.573 1.000 31.273  ? 188 SER   AAA O   1 ? 
ATOM   1438 C  CB  . SER   A 1 189 ? -9.538  43.617 20.647 1.000 36.311  ? 188 SER   AAA CB  1 ? 
ATOM   1439 O  OG  . SER   A 1 189 ? -10.679 43.011 20.077 1.000 32.678  ? 188 SER   AAA OG  1 ? 
ATOM   1440 N  N   . LEU   A 1 190 ? -12.196 44.377 22.527 1.000 32.585  ? 189 LEU   AAA N   1 ? 
ATOM   1441 C  CA  . LEU   A 1 190 ? -13.287 43.792 23.361 1.000 34.845  ? 189 LEU   AAA CA  1 ? 
ATOM   1442 C  C   . LEU   A 1 190 ? -14.120 42.799 22.540 1.000 31.125  ? 189 LEU   AAA C   1 ? 
ATOM   1443 O  O   . LEU   A 1 190 ? -15.281 42.515 22.972 1.000 32.512  ? 189 LEU   AAA O   1 ? 
ATOM   1444 C  CB  . LEU   A 1 190 ? -14.145 44.917 23.958 1.000 31.470  ? 189 LEU   AAA CB  1 ? 
ATOM   1445 C  CG  . LEU   A 1 190 ? -13.391 45.829 24.936 1.000 34.788  ? 189 LEU   AAA CG  1 ? 
ATOM   1446 C  CD1 . LEU   A 1 190 ? -14.275 46.916 25.541 1.000 34.040  ? 189 LEU   AAA CD1 1 ? 
ATOM   1447 C  CD2 . LEU   A 1 190 ? -12.760 45.024 26.057 1.000 39.087  ? 189 LEU   AAA CD2 1 ? 
ATOM   1448 N  N   . ASP   A 1 191 ? -13.553 42.253 21.443 1.000 32.092  ? 190 ASP   AAA N   1 ? 
ATOM   1449 C  CA  . ASP   A 1 191 ? -14.084 41.014 20.799 1.000 31.416  ? 190 ASP   AAA CA  1 ? 
ATOM   1450 C  C   . ASP   A 1 191 ? -14.188 39.978 21.901 1.000 27.636  ? 190 ASP   AAA C   1 ? 
ATOM   1451 O  O   . ASP   A 1 191 ? -13.262 39.923 22.715 1.000 30.631  ? 190 ASP   AAA O   1 ? 
ATOM   1452 C  CB  . ASP   A 1 191 ? -13.197 40.461 19.689 1.000 29.407  ? 190 ASP   AAA CB  1 ? 
ATOM   1453 C  CG  . ASP   A 1 191 ? -13.213 41.314 18.456 1.000 34.530  ? 190 ASP   AAA CG  1 ? 
ATOM   1454 O  OD1 . ASP   A 1 191 ? -14.102 42.163 18.351 1.000 35.045  ? 190 ASP   AAA OD1 1 ? 
ATOM   1455 O  OD2 . ASP   A 1 191 ? -12.335 41.124 17.632 1.000 38.297  ? 190 ASP   AAA OD2 1 ? 
ATOM   1456 N  N   . PHE   A 1 192 ? -15.260 39.182 21.913 1.000 27.680  ? 191 PHE   AAA N   1 ? 
ATOM   1457 C  CA  . PHE   A 1 192 ? -15.567 38.327 23.081 1.000 24.829  ? 191 PHE   AAA CA  1 ? 
ATOM   1458 C  C   . PHE   A 1 192 ? -16.324 37.061 22.697 1.000 29.003  ? 191 PHE   AAA C   1 ? 
ATOM   1459 O  O   . PHE   A 1 192 ? -16.980 37.037 21.643 1.000 28.517  ? 191 PHE   AAA O   1 ? 
ATOM   1460 C  CB  . PHE   A 1 192 ? -16.351 39.120 24.121 1.000 30.703  ? 191 PHE   AAA CB  1 ? 
ATOM   1461 C  CG  . PHE   A 1 192 ? -17.755 39.474 23.704 1.000 22.944  ? 191 PHE   AAA CG  1 ? 
ATOM   1462 C  CD1 . PHE   A 1 192 ? -18.806 38.615 23.943 1.000 29.567  ? 191 PHE   AAA CD1 1 ? 
ATOM   1463 C  CD2 . PHE   A 1 192 ? -18.018 40.698 23.108 1.000 28.164  ? 191 PHE   AAA CD2 1 ? 
ATOM   1464 C  CE1 . PHE   A 1 192 ? -20.090 38.928 23.549 1.000 24.947  ? 191 PHE   AAA CE1 1 ? 
ATOM   1465 C  CE2 . PHE   A 1 192 ? -19.307 41.031 22.726 1.000 27.048  ? 191 PHE   AAA CE2 1 ? 
ATOM   1466 C  CZ  . PHE   A 1 192 ? -20.344 40.134 22.935 1.000 31.250  ? 191 PHE   AAA CZ  1 ? 
ATOM   1467 N  N   . TRP   A 1 193 ? -16.206 36.055 23.565 1.000 23.911  ? 192 TRP   AAA N   1 ? 
ATOM   1468 C  CA  . TRP   A 1 193 ? -17.125 34.896 23.654 1.000 28.852  ? 192 TRP   AAA CA  1 ? 
ATOM   1469 C  C   . TRP   A 1 193 ? -18.154 35.144 24.757 1.000 28.034  ? 192 TRP   AAA C   1 ? 
ATOM   1470 O  O   . TRP   A 1 193 ? -17.808 35.788 25.789 1.000 28.374  ? 192 TRP   AAA O   1 ? 
ATOM   1471 C  CB  . TRP   A 1 193 ? -16.336 33.618 23.917 1.000 26.948  ? 192 TRP   AAA CB  1 ? 
ATOM   1472 C  CG  . TRP   A 1 193 ? -15.374 33.274 22.817 1.000 27.759  ? 192 TRP   AAA CG  1 ? 
ATOM   1473 C  CD1 . TRP   A 1 193 ? -15.682 32.839 21.558 1.000 31.870  ? 192 TRP   AAA CD1 1 ? 
ATOM   1474 C  CD2 . TRP   A 1 193 ? -13.943 33.356 22.872 1.000 25.311  ? 192 TRP   AAA CD2 1 ? 
ATOM   1475 N  NE1 . TRP   A 1 193 ? -14.543 32.631 20.825 1.000 33.208  ? 192 TRP   AAA NE1 1 ? 
ATOM   1476 C  CE2 . TRP   A 1 193 ? -13.457 32.921 21.616 1.000 30.866  ? 192 TRP   AAA CE2 1 ? 
ATOM   1477 C  CE3 . TRP   A 1 193 ? -13.020 33.747 23.850 1.000 31.756  ? 192 TRP   AAA CE3 1 ? 
ATOM   1478 C  CZ2 . TRP   A 1 193 ? -12.096 32.898 21.324 1.000 26.498  ? 192 TRP   AAA CZ2 1 ? 
ATOM   1479 C  CZ3 . TRP   A 1 193 ? -11.666 33.691 23.571 1.000 29.466  ? 192 TRP   AAA CZ3 1 ? 
ATOM   1480 C  CH2 . TRP   A 1 193 ? -11.218 33.258 22.327 1.000 31.051  ? 192 TRP   AAA CH2 1 ? 
ATOM   1481 N  N   . THR   A 1 194 ? -19.358 34.603 24.603 1.000 25.147  ? 193 THR   AAA N   1 ? 
ATOM   1482 C  CA  . THR   A 1 194 ? -20.353 34.621 25.699 1.000 25.660  ? 193 THR   AAA CA  1 ? 
ATOM   1483 C  C   . THR   A 1 194 ? -21.036 33.255 25.831 1.000 27.634  ? 193 THR   AAA C   1 ? 
ATOM   1484 O  O   . THR   A 1 194 ? -21.298 32.571 24.821 1.000 33.038  ? 193 THR   AAA O   1 ? 
ATOM   1485 C  CB  . THR   A 1 194 ? -21.349 35.765 25.528 1.000 25.111  ? 193 THR   AAA CB  1 ? 
ATOM   1486 O  OG1 . THR   A 1 194 ? -22.197 35.772 26.674 1.000 27.145  ? 193 THR   AAA OG1 1 ? 
ATOM   1487 C  CG2 . THR   A 1 194 ? -22.140 35.669 24.241 1.000 27.835  ? 193 THR   AAA CG2 1 ? 
ATOM   1488 N  N   . TYR   A 1 195 ? -21.298 32.875 27.064 1.000 25.659  ? 194 TYR   AAA N   1 ? 
ATOM   1489 C  CA  . TYR   A 1 195 ? -22.088 31.660 27.346 1.000 27.488  ? 194 TYR   AAA CA  1 ? 
ATOM   1490 C  C   . TYR   A 1 195 ? -22.744 31.825 28.711 1.000 28.442  ? 194 TYR   AAA C   1 ? 
ATOM   1491 O  O   . TYR   A 1 195 ? -22.274 32.611 29.559 1.000 25.119  ? 194 TYR   AAA O   1 ? 
ATOM   1492 C  CB  . TYR   A 1 195 ? -21.219 30.402 27.241 1.000 29.465  ? 194 TYR   AAA CB  1 ? 
ATOM   1493 C  CG  . TYR   A 1 195 ? -20.316 30.188 28.421 1.000 25.062  ? 194 TYR   AAA CG  1 ? 
ATOM   1494 C  CD1 . TYR   A 1 195 ? -19.110 30.866 28.530 1.000 25.097  ? 194 TYR   AAA CD1 1 ? 
ATOM   1495 C  CD2 . TYR   A 1 195 ? -20.692 29.375 29.468 1.000 25.508  ? 194 TYR   AAA CD2 1 ? 
ATOM   1496 C  CE1 . TYR   A 1 195 ? -18.292 30.737 29.646 1.000 27.011  ? 194 TYR   AAA CE1 1 ? 
ATOM   1497 C  CE2 . TYR   A 1 195 ? -19.884 29.226 30.587 1.000 26.637  ? 194 TYR   AAA CE2 1 ? 
ATOM   1498 C  CZ  . TYR   A 1 195 ? -18.688 29.931 30.701 1.000 22.240  ? 194 TYR   AAA CZ  1 ? 
ATOM   1499 O  OH  . TYR   A 1 195 ? -17.889 29.795 31.795 1.000 25.483  ? 194 TYR   AAA OH  1 ? 
ATOM   1500 N  N   . PRO   A 1 196 ? -23.863 31.087 28.926 1.000 27.955  ? 195 PRO   AAA N   1 ? 
ATOM   1501 C  CA  . PRO   A 1 196 ? -24.551 31.054 30.213 1.000 27.195  ? 195 PRO   AAA CA  1 ? 
ATOM   1502 C  C   . PRO   A 1 196 ? -23.849 30.104 31.188 1.000 26.811  ? 195 PRO   AAA C   1 ? 
ATOM   1503 O  O   . PRO   A 1 196 ? -23.561 28.981 30.825 1.000 29.428  ? 195 PRO   AAA O   1 ? 
ATOM   1504 C  CB  . PRO   A 1 196 ? -25.968 30.564 29.839 1.000 28.687  ? 195 PRO   AAA CB  1 ? 
ATOM   1505 C  CG  . PRO   A 1 196 ? -25.727 29.641 28.672 1.000 30.424  ? 195 PRO   AAA CG  1 ? 
ATOM   1506 C  CD  . PRO   A 1 196 ? -24.568 30.260 27.918 1.000 27.686  ? 195 PRO   AAA CD  1 ? 
ATOM   1507 N  N   . GLY   A 1 197 ? -23.566 30.572 32.392 1.000 26.711  ? 196 GLY   AAA N   1 ? 
ATOM   1508 C  CA  . GLY   A 1 197 ? -22.675 29.886 33.330 1.000 23.162  ? 196 GLY   AAA CA  1 ? 
ATOM   1509 C  C   . GLY   A 1 197 ? -22.961 30.276 34.759 1.000 21.723  ? 196 GLY   AAA C   1 ? 
ATOM   1510 O  O   . GLY   A 1 197 ? -24.119 30.640 35.071 1.000 23.638  ? 196 GLY   AAA O   1 ? 
ATOM   1511 N  N   . SER   A 1 198 ? -21.943 30.153 35.604 1.000 23.164  ? 197 SER   AAA N   1 ? 
ATOM   1512 C  CA  . SER   A 1 198 ? -22.080 30.133 37.078 1.000 23.643  ? 197 SER   AAA CA  1 ? 
ATOM   1513 C  C   . SER   A 1 198 ? -20.970 30.944 37.735 1.000 21.788  ? 197 SER   AAA C   1 ? 
ATOM   1514 O  O   . SER   A 1 198 ? -19.957 31.240 37.048 1.000 21.439  ? 197 SER   AAA O   1 ? 
ATOM   1515 C  CB  . SER   A 1 198 ? -22.054 28.688 37.587 1.000 23.596  ? 197 SER   AAA CB  1 ? 
ATOM   1516 O  OG  . SER   A 1 198 ? -20.723 28.214 37.670 1.000 27.489  ? 197 SER   AAA OG  1 ? 
ATOM   1517 N  N   . LEU   A 1 199 ? -21.137 31.201 39.038 1.000 23.739  ? 198 LEU   AAA N   1 ? 
ATOM   1518 C  CA  . LEU   A 1 199 ? -20.002 31.546 39.922 1.000 24.068  ? 198 LEU   AAA CA  1 ? 
ATOM   1519 C  C   . LEU   A 1 199 ? -19.004 30.402 39.880 1.000 21.859  ? 198 LEU   AAA C   1 ? 
ATOM   1520 O  O   . LEU   A 1 199 ? -19.475 29.243 39.773 1.000 23.378  ? 198 LEU   AAA O   1 ? 
ATOM   1521 C  CB  . LEU   A 1 199 ? -20.461 31.740 41.357 1.000 23.420  ? 198 LEU   AAA CB  1 ? 
ATOM   1522 C  CG  . LEU   A 1 199 ? -21.492 32.841 41.582 1.000 21.924  ? 198 LEU   AAA CG  1 ? 
ATOM   1523 C  CD1 . LEU   A 1 199 ? -21.875 32.862 43.050 1.000 29.164  ? 198 LEU   AAA CD1 1 ? 
ATOM   1524 C  CD2 . LEU   A 1 199 ? -20.934 34.157 41.131 1.000 25.983  ? 198 LEU   AAA CD2 1 ? 
ATOM   1525 N  N   . THR   A 1 200 ? -17.720 30.694 39.842 1.000 21.580  ? 199 THR   AAA N   1 ? 
ATOM   1526 C  CA  . THR   A 1 200 ? -16.654 29.654 39.743 1.000 22.013  ? 199 THR   AAA CA  1 ? 
ATOM   1527 C  C   . THR   A 1 200 ? -16.244 29.109 41.117 1.000 23.961  ? 199 THR   AAA C   1 ? 
ATOM   1528 O  O   . THR   A 1 200 ? -15.342 28.249 41.177 1.000 26.195  ? 199 THR   AAA O   1 ? 
ATOM   1529 C  CB  . THR   A 1 200 ? -15.404 30.154 39.009 1.000 25.486  ? 199 THR   AAA CB  1 ? 
ATOM   1530 O  OG1 . THR   A 1 200 ? -14.796 31.213 39.741 1.000 21.101  ? 199 THR   AAA OG1 1 ? 
ATOM   1531 C  CG2 . THR   A 1 200 ? -15.721 30.597 37.588 1.000 27.114  ? 199 THR   AAA CG2 1 ? 
ATOM   1532 N  N   . HIS   A 1 201 ? -16.880 29.561 42.182 1.000 23.336  ? 200 HIS   AAA N   1 ? 
ATOM   1533 C  CA  . HIS   A 1 201 ? -16.663 29.052 43.554 1.000 25.494  ? 200 HIS   AAA CA  1 ? 
ATOM   1534 C  C   . HIS   A 1 201 ? -17.982 29.128 44.302 1.000 25.545  ? 200 HIS   AAA C   1 ? 
ATOM   1535 O  O   . HIS   A 1 201 ? -18.949 29.756 43.848 1.000 24.987  ? 200 HIS   AAA O   1 ? 
ATOM   1536 C  CB  . HIS   A 1 201 ? -15.480 29.706 44.263 1.000 25.923  ? 200 HIS   AAA CB  1 ? 
ATOM   1537 C  CG  . HIS   A 1 201 ? -15.661 31.170 44.505 1.000 26.209  ? 200 HIS   AAA CG  1 ? 
ATOM   1538 N  ND1 . HIS   A 1 201 ? -14.865 32.113 43.907 1.000 35.308  ? 200 HIS   AAA ND1 1 ? 
ATOM   1539 C  CD2 . HIS   A 1 201 ? -16.558 31.817 45.262 1.000 22.890  ? 200 HIS   AAA CD2 1 ? 
ATOM   1540 C  CE1 . HIS   A 1 201 ? -15.272 33.347 44.289 1.000 25.082  ? 200 HIS   AAA CE1 1 ? 
ATOM   1541 N  NE2 . HIS   A 1 201 ? -16.306 33.185 45.129 1.000 31.092  ? 200 HIS   AAA NE2 1 ? 
ATOM   1542 N  N   . PRO   A 1 202 ? -18.115 28.378 45.407 1.000 24.050  ? 201 PRO   AAA N   1 ? 
ATOM   1543 C  CA  . PRO   A 1 202 ? -19.329 28.427 46.204 1.000 23.809  ? 201 PRO   AAA CA  1 ? 
ATOM   1544 C  C   . PRO   A 1 202 ? -19.826 29.833 46.419 1.000 23.968  ? 201 PRO   AAA C   1 ? 
ATOM   1545 O  O   . PRO   A 1 202 ? -19.030 30.757 46.670 1.000 24.746  ? 201 PRO   AAA O   1 ? 
ATOM   1546 C  CB  . PRO   A 1 202 ? -18.882 27.827 47.531 1.000 26.605  ? 201 PRO   AAA CB  1 ? 
ATOM   1547 C  CG  . PRO   A 1 202 ? -17.948 26.759 47.036 1.000 28.777  ? 201 PRO   AAA CG  1 ? 
ATOM   1548 C  CD  . PRO   A 1 202 ? -17.160 27.378 45.904 1.000 29.711  ? 201 PRO   AAA CD  1 ? 
ATOM   1549 N  N   . PRO   A 1 203 ? -21.148 30.017 46.353 1.000 25.053  ? 202 PRO   AAA N   1 ? 
ATOM   1550 C  CA  . PRO   A 1 203 ? -22.163 28.963 46.234 1.000 29.022  ? 202 PRO   AAA CA  1 ? 
ATOM   1551 C  C   . PRO   A 1 203 ? -22.515 28.457 44.829 1.000 26.783  ? 202 PRO   AAA C   1 ? 
ATOM   1552 O  O   . PRO   A 1 203 ? -23.502 27.733 44.695 1.000 30.157  ? 202 PRO   AAA O   1 ? 
ATOM   1553 C  CB  . PRO   A 1 203 ? -23.415 29.631 46.831 1.000 26.441  ? 202 PRO   AAA CB  1 ? 
ATOM   1554 C  CG  . PRO   A 1 203 ? -23.252 31.084 46.499 1.000 27.522  ? 202 PRO   AAA CG  1 ? 
ATOM   1555 C  CD  . PRO   A 1 203 ? -21.754 31.343 46.522 1.000 27.946  ? 202 PRO   AAA CD  1 ? 
ATOM   1556 N  N   . LEU   A 1 204 ? -21.724 28.826 43.823 1.000 24.281  ? 203 LEU   AAA N   1 ? 
ATOM   1557 C  CA  . LEU   A 1 204 ? -21.755 28.225 42.463 1.000 25.398  ? 203 LEU   AAA CA  1 ? 
ATOM   1558 C  C   . LEU   A 1 204 ? -23.106 28.435 41.758 1.000 28.127  ? 203 LEU   AAA C   1 ? 
ATOM   1559 O  O   . LEU   A 1 204 ? -23.400 27.678 40.789 1.000 25.493  ? 203 LEU   AAA O   1 ? 
ATOM   1560 C  CB  . LEU   A 1 204 ? -21.468 26.726 42.609 1.000 25.537  ? 203 LEU   AAA CB  1 ? 
ATOM   1561 C  CG  . LEU   A 1 204 ? -20.051 26.376 43.031 1.000 25.096  ? 203 LEU   AAA CG  1 ? 
ATOM   1562 C  CD1 . LEU   A 1 204 ? -20.031 24.881 43.359 1.000 27.890  ? 203 LEU   AAA CD1 1 ? 
ATOM   1563 C  CD2 . LEU   A 1 204 ? -19.034 26.648 41.941 1.000 25.214  ? 203 LEU   AAA CD2 1 ? 
ATOM   1564 N  N   . TYR   A 1 205 ? -23.861 29.472 42.124 1.000 24.812  ? 204 TYR   AAA N   1 ? 
ATOM   1565 C  CA  . TYR   A 1 205 ? -25.154 29.808 41.489 1.000 24.238  ? 204 TYR   AAA CA  1 ? 
ATOM   1566 C  C   . TYR   A 1 205 ? -24.998 29.940 39.956 1.000 24.399  ? 204 TYR   AAA C   1 ? 
ATOM   1567 O  O   . TYR   A 1 205 ? -23.971 30.552 39.430 1.000 21.955  ? 204 TYR   AAA O   1 ? 
ATOM   1568 C  CB  . TYR   A 1 205 ? -25.654 31.145 42.023 1.000 24.218  ? 204 TYR   AAA CB  1 ? 
ATOM   1569 C  CG  . TYR   A 1 205 ? -26.000 31.208 43.494 1.000 27.232  ? 204 TYR   AAA CG  1 ? 
ATOM   1570 C  CD1 . TYR   A 1 205 ? -26.505 30.115 44.181 1.000 34.218  ? 204 TYR   AAA CD1 1 ? 
ATOM   1571 C  CD2 . TYR   A 1 205 ? -25.940 32.402 44.203 1.000 25.069  ? 204 TYR   AAA CD2 1 ? 
ATOM   1572 C  CE1 . TYR   A 1 205 ? -26.841 30.163 45.525 1.000 35.609  ? 204 TYR   AAA CE1 1 ? 
ATOM   1573 C  CE2 . TYR   A 1 205 ? -26.298 32.482 45.550 1.000 27.154  ? 204 TYR   AAA CE2 1 ? 
ATOM   1574 C  CZ  . TYR   A 1 205 ? -26.758 31.359 46.227 1.000 31.047  ? 204 TYR   AAA CZ  1 ? 
ATOM   1575 O  OH  . TYR   A 1 205 ? -27.132 31.404 47.552 1.000 33.453  ? 204 TYR   AAA OH  1 ? 
ATOM   1576 N  N   . GLU   A 1 206 ? -26.011 29.459 39.236 1.000 25.557  ? 205 GLU   AAA N   1 ? 
ATOM   1577 C  CA  . GLU   A 1 206 ? -26.055 29.455 37.751 1.000 26.786  ? 205 GLU   AAA CA  1 ? 
ATOM   1578 C  C   . GLU   A 1 206 ? -26.720 30.773 37.295 1.000 25.569  ? 205 GLU   AAA C   1 ? 
ATOM   1579 O  O   . GLU   A 1 206 ? -27.767 30.785 36.618 1.000 25.349  ? 205 GLU   AAA O   1 ? 
ATOM   1580 C  CB  . GLU   A 1 206 ? -26.650 28.134 37.251 1.000 27.512  ? 205 GLU   AAA CB  1 ? 
ATOM   1581 C  CG  . GLU   A 1 206 ? -25.701 26.958 37.531 1.000 30.624  ? 205 GLU   AAA CG  1 ? 
ATOM   1582 C  CD  . GLU   A 1 206 ? -26.100 25.601 36.982 1.000 30.967  ? 205 GLU   AAA CD  1 ? 
ATOM   1583 O  OE1 . GLU   A 1 206 ? -25.226 24.683 36.946 1.000 28.734  ? 205 GLU   AAA OE1 1 ? 
ATOM   1584 O  OE2 . GLU   A 1 206 ? -27.261 25.457 36.599 1.000 32.393  ? 205 GLU   AAA OE2 1 ? 
ATOM   1585 N  N   . SER   A 1 207 ? -26.034 31.869 37.623 1.000 21.857  ? 206 SER   AAA N   1 ? 
ATOM   1586 C  CA  . SER   A 1 207 ? -26.576 33.246 37.589 1.000 22.046  ? 206 SER   AAA CA  1 ? 
ATOM   1587 C  C   . SER   A 1 207 ? -25.703 34.144 36.722 1.000 25.061  ? 206 SER   AAA C   1 ? 
ATOM   1588 O  O   . SER   A 1 207 ? -26.068 35.346 36.605 1.000 27.763  ? 206 SER   AAA O   1 ? 
ATOM   1589 C  CB  . SER   A 1 207 ? -26.714 33.768 38.971 1.000 22.171  ? 206 SER   AAA CB  1 ? 
ATOM   1590 O  OG  . SER   A 1 207 ? -25.477 33.688 39.628 1.000 26.197  ? 206 SER   AAA OG  1 ? 
ATOM   1591 N  N   . VAL   A 1 208 ? -24.676 33.601 36.073 1.000 21.858  ? 207 VAL   AAA N   1 ? 
ATOM   1592 C  CA  . VAL   A 1 208 ? -23.626 34.403 35.376 1.000 22.226  ? 207 VAL   AAA CA  1 ? 
ATOM   1593 C  C   . VAL   A 1 208 ? -23.752 34.288 33.856 1.000 22.265  ? 207 VAL   AAA C   1 ? 
ATOM   1594 O  O   . VAL   A 1 208 ? -23.594 33.171 33.274 1.000 25.227  ? 207 VAL   AAA O   1 ? 
ATOM   1595 C  CB  . VAL   A 1 208 ? -22.198 34.102 35.879 1.000 23.105  ? 207 VAL   AAA CB  1 ? 
ATOM   1596 C  CG1 . VAL   A 1 208 ? -21.172 35.063 35.237 1.000 23.656  ? 207 VAL   AAA CG1 1 ? 
ATOM   1597 C  CG2 . VAL   A 1 208 ? -22.128 34.179 37.399 1.000 24.938  ? 207 VAL   AAA CG2 1 ? 
ATOM   1598 N  N   . THR   A 1 209 ? -23.989 35.424 33.202 1.000 27.543  ? 208 THR   AAA N   1 ? 
ATOM   1599 C  CA  . THR   A 1 209 ? -23.670 35.624 31.771 1.000 24.255  ? 208 THR   AAA CA  1 ? 
ATOM   1600 C  C   . THR   A 1 209 ? -22.177 35.968 31.660 1.000 23.079  ? 208 THR   AAA C   1 ? 
ATOM   1601 O  O   . THR   A 1 209 ? -21.757 37.112 32.084 1.000 25.664  ? 208 THR   AAA O   1 ? 
ATOM   1602 C  CB  . THR   A 1 209 ? -24.554 36.680 31.100 1.000 27.011  ? 208 THR   AAA CB  1 ? 
ATOM   1603 O  OG1 . THR   A 1 209 ? -25.935 36.385 31.339 1.000 29.523  ? 208 THR   AAA OG1 1 ? 
ATOM   1604 C  CG2 . THR   A 1 209 ? -24.267 36.775 29.611 1.000 29.911  ? 208 THR   AAA CG2 1 ? 
ATOM   1605 N  N   . TRP   A 1 210 ? -21.390 35.074 31.105 1.000 24.346  ? 209 TRP   AAA N   1 ? 
ATOM   1606 C  CA  . TRP   A 1 210 ? -19.925 35.226 30.953 1.000 21.113  ? 209 TRP   AAA CA  1 ? 
ATOM   1607 C  C   . TRP   A 1 210 ? -19.618 35.945 29.644 1.000 23.542  ? 209 TRP   AAA C   1 ? 
ATOM   1608 O  O   . TRP   A 1 210 ? -20.262 35.646 28.617 1.000 24.548  ? 209 TRP   AAA O   1 ? 
ATOM   1609 C  CB  . TRP   A 1 210 ? -19.249 33.848 30.990 1.000 23.398  ? 209 TRP   AAA CB  1 ? 
ATOM   1610 C  CG  . TRP   A 1 210 ? -19.042 33.399 32.391 1.000 23.891  ? 209 TRP   AAA CG  1 ? 
ATOM   1611 C  CD1 . TRP   A 1 210 ? -19.864 32.597 33.124 1.000 23.699  ? 209 TRP   AAA CD1 1 ? 
ATOM   1612 C  CD2 . TRP   A 1 210 ? -18.005 33.841 33.287 1.000 22.983  ? 209 TRP   AAA CD2 1 ? 
ATOM   1613 N  NE1 . TRP   A 1 210 ? -19.408 32.502 34.409 1.000 24.368  ? 209 TRP   AAA NE1 1 ? 
ATOM   1614 C  CE2 . TRP   A 1 210 ? -18.252 33.227 34.528 1.000 22.062  ? 209 TRP   AAA CE2 1 ? 
ATOM   1615 C  CE3 . TRP   A 1 210 ? -16.845 34.614 33.145 1.000 20.749  ? 209 TRP   AAA CE3 1 ? 
ATOM   1616 C  CZ2 . TRP   A 1 210 ? -17.439 33.440 35.634 1.000 25.192  ? 209 TRP   AAA CZ2 1 ? 
ATOM   1617 C  CZ3 . TRP   A 1 210 ? -16.032 34.806 34.237 1.000 23.509  ? 209 TRP   AAA CZ3 1 ? 
ATOM   1618 C  CH2 . TRP   A 1 210 ? -16.296 34.178 35.457 1.000 22.538  ? 209 TRP   AAA CH2 1 ? 
ATOM   1619 N  N   . ILE   A 1 211 ? -18.686 36.890 29.730 1.000 24.124  ? 210 ILE   AAA N   1 ? 
ATOM   1620 C  CA  . ILE   A 1 211 ? -18.066 37.611 28.585 1.000 22.303  ? 210 ILE   AAA CA  1 ? 
ATOM   1621 C  C   . ILE   A 1 211 ? -16.555 37.348 28.655 1.000 25.075  ? 210 ILE   AAA C   1 ? 
ATOM   1622 O  O   . ILE   A 1 211 ? -15.919 37.789 29.620 1.000 26.695  ? 210 ILE   AAA O   1 ? 
ATOM   1623 C  CB  . ILE   A 1 211 ? -18.377 39.130 28.634 1.000 24.467  ? 210 ILE   AAA CB  1 ? 
ATOM   1624 C  CG1 . ILE   A 1 211 ? -19.879 39.436 28.735 1.000 26.574  ? 210 ILE   AAA CG1 1 ? 
ATOM   1625 C  CG2 . ILE   A 1 211 ? -17.704 39.806 27.447 1.000 24.644  ? 210 ILE   AAA CG2 1 ? 
ATOM   1626 C  CD1 . ILE   A 1 211 ? -20.698 39.033 27.575 1.000 29.988  ? 210 ILE   AAA CD1 1 ? 
ATOM   1627 N  N   . ILE   A 1 212 ? -16.002 36.530 27.755 1.000 25.261  ? 211 ILE   AAA N   1 ? 
ATOM   1628 C  CA  . ILE   A 1 212 ? -14.552 36.192 27.778 1.000 21.295  ? 211 ILE   AAA CA  1 ? 
ATOM   1629 C  C   . ILE   A 1 212 ? -13.904 36.929 26.621 1.000 23.546  ? 211 ILE   AAA C   1 ? 
ATOM   1630 O  O   . ILE   A 1 212 ? -14.329 36.730 25.485 1.000 21.739  ? 211 ILE   AAA O   1 ? 
ATOM   1631 C  CB  . ILE   A 1 212 ? -14.325 34.652 27.675 1.000 22.050  ? 211 ILE   AAA CB  1 ? 
ATOM   1632 C  CG1 . ILE   A 1 212 ? -15.130 33.853 28.702 1.000 26.512  ? 211 ILE   AAA CG1 1 ? 
ATOM   1633 C  CG2 . ILE   A 1 212 ? -12.845 34.351 27.759 1.000 24.760  ? 211 ILE   AAA CG2 1 ? 
ATOM   1634 C  CD1 . ILE   A 1 212 ? -14.839 34.223 30.129 1.000 26.362  ? 211 ILE   AAA CD1 1 ? 
ATOM   1635 N  N   . CYS   A 1 213 ? -12.917 37.767 26.932 1.000 22.933  ? 212 CYS   AAA N   1 ? 
ATOM   1636 C  CA  . CYS   A 1 213 ? -12.190 38.530 25.911 1.000 26.078  ? 212 CYS   AAA CA  1 ? 
ATOM   1637 C  C   . CYS   A 1 213 ? -11.332 37.579 25.073 1.000 22.912  ? 212 CYS   AAA C   1 ? 
ATOM   1638 O  O   . CYS   A 1 213 ? -10.686 36.719 25.636 1.000 25.316  ? 212 CYS   AAA O   1 ? 
ATOM   1639 C  CB  . CYS   A 1 213 ? -11.380 39.647 26.543 1.000 27.755  ? 212 CYS   AAA CB  1 ? 
ATOM   1640 S  SG  . CYS   A 1 213 ? -12.410 40.962 27.271 1.000 27.117  ? 212 CYS   AAA SG  1 ? 
ATOM   1641 N  N   . LYS   A 1 214 ? -11.326 37.781 23.758 1.000 25.089  ? 213 LYS   AAA N   1 ? 
ATOM   1642 C  CA  . LYS   A 1 214 ? -10.427 37.068 22.811 1.000 28.390  ? 213 LYS   AAA CA  1 ? 
ATOM   1643 C  C   . LYS   A 1 214 ? -8.957  37.409 23.108 1.000 26.410  ? 213 LYS   AAA C   1 ? 
ATOM   1644 O  O   . LYS   A 1 214 ? -8.085  36.503 23.053 1.000 26.103  ? 213 LYS   AAA O   1 ? 
ATOM   1645 C  CB  . LYS   A 1 214 ? -10.902 37.434 21.397 1.000 30.232  ? 213 LYS   AAA CB  1 ? 
ATOM   1646 C  CG  . LYS   A 1 214 ? -10.009 37.049 20.240 1.000 37.972  ? 213 LYS   AAA CG  1 ? 
ATOM   1647 C  CD  . LYS   A 1 214 ? -10.567 37.477 18.888 1.000 39.860  ? 213 LYS   AAA CD  1 ? 
ATOM   1648 C  CE  . LYS   A 1 214 ? -9.801  38.569 18.164 1.000 42.725  ? 213 LYS   AAA CE  1 ? 
ATOM   1649 N  NZ  . LYS   A 1 214 ? -9.457  39.692 19.044 1.000 50.658  ? 213 LYS   AAA NZ  1 ? 
ATOM   1650 N  N   . GLU   A 1 215 ? -8.674  38.704 23.346 1.000 24.759  ? 214 GLU   AAA N   1 ? 
ATOM   1651 C  CA  . GLU   A 1 215 ? -7.313  39.235 23.550 1.000 20.366  ? 214 GLU   AAA CA  1 ? 
ATOM   1652 C  C   . GLU   A 1 215 ? -6.952  39.022 25.018 1.000 22.945  ? 214 GLU   AAA C   1 ? 
ATOM   1653 O  O   . GLU   A 1 215 ? -7.806  39.304 25.955 1.000 25.217  ? 214 GLU   AAA O   1 ? 
ATOM   1654 C  CB  . GLU   A 1 215 ? -7.192  40.742 23.266 1.000 26.483  ? 214 GLU   AAA CB  1 ? 
ATOM   1655 C  CG  . GLU   A 1 215 ? -6.976  41.091 21.846 1.000 33.273  ? 214 GLU   AAA CG  1 ? 
ATOM   1656 C  CD  . GLU   A 1 215 ? -6.466  42.509 21.632 1.000 33.058  ? 214 GLU   AAA CD  1 ? 
ATOM   1657 O  OE1 . GLU   A 1 215 ? -6.127  43.204 22.619 1.000 43.787  ? 214 GLU   AAA OE1 1 ? 
ATOM   1658 O  OE2 . GLU   A 1 215 ? -6.359  42.865 20.467 1.000 43.897  ? 214 GLU   AAA OE2 1 ? 
ATOM   1659 N  N   . SER   A 1 216 ? -5.733  38.573 25.240 1.000 24.354  ? 215 SER   AAA N   1 ? 
ATOM   1660 C  CA  . SER   A 1 216 ? -5.176  38.400 26.599 1.000 24.185  ? 215 SER   AAA CA  1 ? 
ATOM   1661 C  C   . SER   A 1 216 ? -4.600  39.746 27.051 1.000 23.279  ? 215 SER   AAA C   1 ? 
ATOM   1662 O  O   . SER   A 1 216 ? -4.437  40.657 26.172 1.000 26.960  ? 215 SER   AAA O   1 ? 
ATOM   1663 C  CB  . SER   A 1 216 ? -4.142  37.296 26.662 1.000 26.861  ? 215 SER   AAA CB  1 ? 
ATOM   1664 O  OG  . SER   A 1 216 ? -2.998  37.609 25.861 1.000 28.967  ? 215 SER   AAA OG  1 ? 
ATOM   1665 N  N   . ILE   A 1 217 ? -4.268  39.842 28.325 1.000 27.563  ? 216 ILE   AAA N   1 ? 
ATOM   1666 C  CA  . ILE   A 1 217 ? -3.401  40.939 28.829 1.000 24.680  ? 216 ILE   AAA CA  1 ? 
ATOM   1667 C  C   . ILE   A 1 217 ? -2.146  40.299 29.437 1.000 24.006  ? 216 ILE   AAA C   1 ? 
ATOM   1668 O  O   . ILE   A 1 217 ? -2.206  39.086 29.816 1.000 24.297  ? 216 ILE   AAA O   1 ? 
ATOM   1669 C  CB  . ILE   A 1 217 ? -4.133  41.837 29.848 1.000 23.590  ? 216 ILE   AAA CB  1 ? 
ATOM   1670 C  CG1 . ILE   A 1 217 ? -4.562  41.073 31.108 1.000 24.203  ? 216 ILE   AAA CG1 1 ? 
ATOM   1671 C  CG2 . ILE   A 1 217 ? -5.281  42.570 29.193 1.000 22.990  ? 216 ILE   AAA CG2 1 ? 
ATOM   1672 C  CD1 . ILE   A 1 217 ? -5.117  41.960 32.220 1.000 22.943  ? 216 ILE   AAA CD1 1 ? 
ATOM   1673 N  N   . SER   A 1 218 ? -1.068  41.065 29.586 1.000 28.580  ? 217 SER   AAA N   1 ? 
ATOM   1674 C  CA  . SER   A 1 218 ? 0.207   40.538 30.134 1.000 27.902  ? 217 SER   AAA CA  1 ? 
ATOM   1675 C  C   . SER   A 1 218 ? 0.175   40.596 31.659 1.000 25.463  ? 217 SER   AAA C   1 ? 
ATOM   1676 O  O   . SER   A 1 218 ? -0.651  41.311 32.295 1.000 28.777  ? 217 SER   AAA O   1 ? 
ATOM   1677 C  CB  . SER   A 1 218 ? 1.426   41.233 29.585 1.000 31.247  ? 217 SER   AAA CB  1 ? 
ATOM   1678 O  OG  . SER   A 1 218 ? 1.515   42.500 30.223 1.000 41.354  ? 217 SER   AAA OG  1 ? 
ATOM   1679 N  N   . VAL   A 1 219 ? 1.109   39.856 32.214 1.000 26.161  ? 218 VAL   AAA N   1 ? 
ATOM   1680 C  CA  . VAL   A 1 219 ? 1.453   39.828 33.649 1.000 23.868  ? 218 VAL   AAA CA  1 ? 
ATOM   1681 C  C   . VAL   A 1 219 ? 2.857   39.223 33.715 1.000 30.466  ? 218 VAL   AAA C   1 ? 
ATOM   1682 O  O   . VAL   A 1 219 ? 3.138   38.294 32.905 1.000 31.348  ? 218 VAL   AAA O   1 ? 
ATOM   1683 C  CB  . VAL   A 1 219 ? 0.407   39.094 34.505 1.000 27.235  ? 218 VAL   AAA CB  1 ? 
ATOM   1684 C  CG1 . VAL   A 1 219 ? 0.303   37.590 34.180 1.000 28.299  ? 218 VAL   AAA CG1 1 ? 
ATOM   1685 C  CG2 . VAL   A 1 219 ? 0.657   39.318 35.985 1.000 26.509  ? 218 VAL   AAA CG2 1 ? 
ATOM   1686 N  N   . SER   A 1 220 ? 3.743   39.754 34.569 1.000 33.159  ? 219 SER   AAA N   1 ? 
ATOM   1687 C  CA  . SER   A 1 220 ? 5.086   39.147 34.778 1.000 33.271  ? 219 SER   AAA CA  1 ? 
ATOM   1688 C  C   . SER   A 1 220 ? 5.001   38.012 35.814 1.000 33.716  ? 219 SER   AAA C   1 ? 
ATOM   1689 O  O   . SER   A 1 220 ? 4.052   37.977 36.661 1.000 29.745  ? 219 SER   AAA O   1 ? 
ATOM   1690 C  CB  . SER   A 1 220 ? 6.097   40.173 35.136 1.000 30.923  ? 219 SER   AAA CB  1 ? 
ATOM   1691 O  OG  . SER   A 1 220 ? 5.806   40.686 36.411 1.000 31.743  ? 219 SER   AAA OG  1 ? 
ATOM   1692 N  N   . SER   A 1 221 ? 5.947   37.083 35.742 1.000 31.218  ? 220 SER   AAA N   1 ? 
ATOM   1693 C  CA  . SER   A 1 221 ? 6.131   35.982 36.731 1.000 33.961  ? 220 SER   AAA CA  1 ? 
ATOM   1694 C  C   . SER   A 1 221 ? 6.268   36.549 38.162 1.000 33.300  ? 220 SER   AAA C   1 ? 
ATOM   1695 O  O   . SER   A 1 221 ? 5.741   35.938 39.102 1.000 33.814  ? 220 SER   AAA O   1 ? 
ATOM   1696 C  CB  . SER   A 1 221 ? 7.296   35.101 36.348 1.000 38.890  ? 220 SER   AAA CB  1 ? 
ATOM   1697 O  OG  . SER   A 1 221 ? 7.444   34.005 37.280 1.000 42.984  ? 220 SER   AAA OG  1 ? 
ATOM   1698 N  N   . GLU   A 1 222 ? 6.887   37.720 38.320 1.000 33.133  ? 221 GLU   AAA N   1 ? 
ATOM   1699 C  CA  . GLU   A 1 222 ? 7.075   38.410 39.626 1.000 34.905  ? 221 GLU   AAA CA  1 ? 
ATOM   1700 C  C   . GLU   A 1 222 ? 5.741   39.029 40.056 1.000 35.085  ? 221 GLU   AAA C   1 ? 
ATOM   1701 O  O   . GLU   A 1 222 ? 5.436   38.955 41.246 1.000 34.610  ? 221 GLU   AAA O   1 ? 
ATOM   1702 C  CB  . GLU   A 1 222 ? 8.149   39.510 39.569 1.000 36.204  ? 221 GLU   AAA CB  1 ? 
ATOM   1703 C  CG  . GLU   A 1 222 ? 9.544   39.016 39.225 1.000 34.022  ? 221 GLU   AAA CG  1 ? 
ATOM   1704 C  CD  . GLU   A 1 222 ? 9.740   38.612 37.764 1.000 39.220  ? 221 GLU   AAA CD  1 ? 
ATOM   1705 O  OE1 . GLU   A 1 222 ? 9.231   39.338 36.834 1.000 35.711  ? 221 GLU   AAA OE1 1 ? 
ATOM   1706 O  OE2 . GLU   A 1 222 ? 10.393  37.540 37.542 1.000 48.236  ? 221 GLU   AAA OE2 1 ? 
ATOM   1707 N  N   . GLN   A 1 223 ? 4.972   39.627 39.135 1.000 34.424  ? 222 GLN   AAA N   1 ? 
ATOM   1708 C  CA  . GLN   A 1 223 ? 3.625   40.151 39.484 1.000 30.807  ? 222 GLN   AAA CA  1 ? 
ATOM   1709 C  C   . GLN   A 1 223 ? 2.780   38.986 40.054 1.000 30.689  ? 222 GLN   AAA C   1 ? 
ATOM   1710 O  O   . GLN   A 1 223 ? 2.140   39.139 41.135 1.000 34.471  ? 222 GLN   AAA O   1 ? 
ATOM   1711 C  CB  . GLN   A 1 223 ? 3.030   40.874 38.284 1.000 29.221  ? 222 GLN   AAA CB  1 ? 
ATOM   1712 C  CG  . GLN   A 1 223 ? 3.550   42.305 38.128 1.000 33.929  ? 222 GLN   AAA CG  1 ? 
ATOM   1713 C  CD  . GLN   A 1 223 ? 2.980   42.990 36.911 1.000 28.775  ? 222 GLN   AAA CD  1 ? 
ATOM   1714 O  OE1 . GLN   A 1 223 ? 2.739   42.339 35.878 1.000 26.627  ? 222 GLN   AAA OE1 1 ? 
ATOM   1715 N  NE2 . GLN   A 1 223 ? 2.701   44.294 37.040 1.000 31.328  ? 222 GLN   AAA NE2 1 ? 
ATOM   1716 N  N   . LEU   A 1 224 ? 2.789   37.836 39.398 1.000 31.027  ? 223 LEU   AAA N   1 ? 
ATOM   1717 C  CA  . LEU   A 1 224 ? 2.075   36.613 39.898 1.000 30.830  ? 223 LEU   AAA CA  1 ? 
ATOM   1718 C  C   . LEU   A 1 224 ? 2.610   36.233 41.292 1.000 30.865  ? 223 LEU   AAA C   1 ? 
ATOM   1719 O  O   . LEU   A 1 224 ? 1.801   35.810 42.153 1.000 36.577  ? 223 LEU   AAA O   1 ? 
ATOM   1720 C  CB  . LEU   A 1 224 ? 2.225   35.463 38.894 1.000 32.435  ? 223 LEU   AAA CB  1 ? 
ATOM   1721 C  CG  . LEU   A 1 224 ? 1.441   35.644 37.581 1.000 33.864  ? 223 LEU   AAA CG  1 ? 
ATOM   1722 C  CD1 . LEU   A 1 224 ? 1.836   34.623 36.523 1.000 45.759  ? 223 LEU   AAA CD1 1 ? 
ATOM   1723 C  CD2 . LEU   A 1 224 ? -0.042  35.552 37.781 1.000 30.864  ? 223 LEU   AAA CD2 1 ? 
ATOM   1724 N  N   . ALA   A 1 225 ? 3.926   36.335 41.505 1.000 31.985  ? 224 ALA   AAA N   1 ? 
ATOM   1725 C  CA  . ALA   A 1 225 ? 4.542   36.032 42.812 1.000 33.908  ? 224 ALA   AAA CA  1 ? 
ATOM   1726 C  C   . ALA   A 1 225 ? 3.918   36.926 43.891 1.000 30.612  ? 224 ALA   AAA C   1 ? 
ATOM   1727 O  O   . ALA   A 1 225 ? 3.742   36.428 44.982 1.000 35.394  ? 224 ALA   AAA O   1 ? 
ATOM   1728 C  CB  . ALA   A 1 225 ? 6.044   36.190 42.773 1.000 36.080  ? 224 ALA   AAA CB  1 ? 
ATOM   1729 N  N   . GLN   A 1 226 ? 3.608   38.200 43.591 1.000 33.880  ? 225 GLN   AAA N   1 ? 
ATOM   1730 C  CA  . GLN   A 1 226 ? 2.974   39.162 44.539 1.000 29.392  ? 225 GLN   AAA CA  1 ? 
ATOM   1731 C  C   . GLN   A 1 226 ? 1.625   38.579 44.965 1.000 28.127  ? 225 GLN   AAA C   1 ? 
ATOM   1732 O  O   . GLN   A 1 226 ? 1.419   38.510 46.171 1.000 34.781  ? 225 GLN   AAA O   1 ? 
ATOM   1733 C  CB  . GLN   A 1 226 ? 2.844   40.574 43.949 1.000 30.892  ? 225 GLN   AAA CB  1 ? 
ATOM   1734 C  CG  . GLN   A 1 226 ? 4.165   41.337 43.932 1.000 30.305  ? 225 GLN   AAA CG  1 ? 
ATOM   1735 C  CD  . GLN   A 1 226 ? 4.025   42.806 43.634 1.000 30.690  ? 225 GLN   AAA CD  1 ? 
ATOM   1736 O  OE1 . GLN   A 1 226 ? 4.315   43.241 42.513 1.000 36.950  ? 225 GLN   AAA OE1 1 ? 
ATOM   1737 N  NE2 . GLN   A 1 226 ? 3.587   43.565 44.640 1.000 33.753  ? 225 GLN   AAA NE2 1 ? 
ATOM   1738 N  N   . PHE   A 1 227 ? 0.755   38.152 44.034 1.000 28.478  ? 226 PHE   AAA N   1 ? 
ATOM   1739 C  CA  . PHE   A 1 227 ? -0.528  37.470 44.392 1.000 26.695  ? 226 PHE   AAA CA  1 ? 
ATOM   1740 C  C   . PHE   A 1 227 ? -0.270  36.268 45.319 1.000 27.210  ? 226 PHE   AAA C   1 ? 
ATOM   1741 O  O   . PHE   A 1 227 ? -0.985  36.153 46.338 1.000 30.392  ? 226 PHE   AAA O   1 ? 
ATOM   1742 C  CB  . PHE   A 1 227 ? -1.299  36.923 43.195 1.000 27.837  ? 226 PHE   AAA CB  1 ? 
ATOM   1743 C  CG  . PHE   A 1 227 ? -1.795  37.900 42.173 1.000 27.580  ? 226 PHE   AAA CG  1 ? 
ATOM   1744 C  CD1 . PHE   A 1 227 ? -1.980  39.236 42.489 1.000 31.642  ? 226 PHE   AAA CD1 1 ? 
ATOM   1745 C  CD2 . PHE   A 1 227 ? -2.053  37.477 40.878 1.000 34.586  ? 226 PHE   AAA CD2 1 ? 
ATOM   1746 C  CE1 . PHE   A 1 227 ? -2.423  40.128 41.521 1.000 33.742  ? 226 PHE   AAA CE1 1 ? 
ATOM   1747 C  CE2 . PHE   A 1 227 ? -2.532  38.366 39.923 1.000 34.904  ? 226 PHE   AAA CE2 1 ? 
ATOM   1748 C  CZ  . PHE   A 1 227 ? -2.734  39.689 40.259 1.000 35.939  ? 226 PHE   AAA CZ  1 ? 
ATOM   1749 N  N   . ARG   A 1 228 ? 0.677   35.386 44.985 1.000 30.318  ? 227 ARG   AAA N   1 ? 
ATOM   1750 C  CA  . ARG   A 1 228 ? 0.910   34.140 45.787 1.000 31.020  ? 227 ARG   AAA CA  1 ? 
ATOM   1751 C  C   . ARG   A 1 228 ? 1.532   34.485 47.152 1.000 29.574  ? 227 ARG   AAA C   1 ? 
ATOM   1752 O  O   . ARG   A 1 228 ? 1.590   33.604 48.029 1.000 29.773  ? 227 ARG   AAA O   1 ? 
ATOM   1753 C  CB  . ARG   A 1 228 ? 1.822   33.106 45.091 1.000 32.274  ? 227 ARG   AAA CB  1 ? 
ATOM   1754 C  CG  . ARG   A 1 228 ? 1.361   32.630 43.722 1.000 35.831  ? 227 ARG   AAA CG  1 ? 
ATOM   1755 C  CD  . ARG   A 1 228 ? 1.971   31.302 43.259 1.000 40.606  ? 227 ARG   AAA CD  1 ? 
ATOM   1756 N  NE  . ARG   A 1 228 ? 1.747   31.163 41.822 1.000 42.182  ? 227 ARG   AAA NE  1 ? 
ATOM   1757 C  CZ  . ARG   A 1 228 ? 2.522   31.668 40.849 1.000 33.886  ? 227 ARG   AAA CZ  1 ? 
ATOM   1758 N  NH1 . ARG   A 1 228 ? 2.177   31.517 39.585 1.000 39.621  ? 227 ARG   AAA NH1 1 ? 
ATOM   1759 N  NH2 . ARG   A 1 228 ? 3.638   32.320 41.128 1.000 37.217  ? 227 ARG   AAA NH2 1 ? 
ATOM   1760 N  N   . SER   A 1 229 ? 2.048   35.695 47.343 1.000 28.394  ? 228 SER   AAA N   1 ? 
ATOM   1761 C  CA  . SER   A 1 229 ? 2.665   36.123 48.617 1.000 31.889  ? 228 SER   AAA CA  1 ? 
ATOM   1762 C  C   . SER   A 1 229 ? 1.581   36.623 49.576 1.000 30.413  ? 228 SER   AAA C   1 ? 
ATOM   1763 O  O   . SER   A 1 229 ? 1.891   36.798 50.780 1.000 34.993  ? 228 SER   AAA O   1 ? 
ATOM   1764 C  CB  . SER   A 1 229 ? 3.754   37.159 48.392 1.000 36.481  ? 228 SER   AAA CB  1 ? 
ATOM   1765 O  OG  . SER   A 1 229 ? 3.220   38.408 47.932 1.000 40.042  ? 228 SER   AAA OG  1 ? 
ATOM   1766 N  N   . LEU   A 1 230 ? 0.355   36.863 49.105 1.000 28.602  ? 229 LEU   AAA N   1 ? 
ATOM   1767 C  CA  . LEU   A 1 230 ? -0.791  37.102 50.034 1.000 26.383  ? 229 LEU   AAA CA  1 ? 
ATOM   1768 C  C   . LEU   A 1 230 ? -0.964  35.874 50.942 1.000 27.766  ? 229 LEU   AAA C   1 ? 
ATOM   1769 O  O   . LEU   A 1 230 ? -0.610  34.738 50.523 1.000 31.479  ? 229 LEU   AAA O   1 ? 
ATOM   1770 C  CB  . LEU   A 1 230 ? -2.080  37.398 49.267 1.000 29.258  ? 229 LEU   AAA CB  1 ? 
ATOM   1771 C  CG  . LEU   A 1 230 ? -2.220  38.821 48.737 1.000 33.639  ? 229 LEU   AAA CG  1 ? 
ATOM   1772 C  CD1 . LEU   A 1 230 ? -3.411  38.913 47.791 1.000 38.276  ? 229 LEU   AAA CD1 1 ? 
ATOM   1773 C  CD2 . LEU   A 1 230 ? -2.325  39.827 49.878 1.000 37.811  ? 229 LEU   AAA CD2 1 ? 
ATOM   1774 N  N   . LEU   A 1 231 ? -1.414  36.110 52.156 1.000 32.330  ? 230 LEU   AAA N   1 ? 
ATOM   1775 C  CA  . LEU   A 1 231 ? -1.532  35.060 53.194 1.000 28.506  ? 230 LEU   AAA CA  1 ? 
ATOM   1776 C  C   . LEU   A 1 231 ? -3.002  34.774 53.472 1.000 29.613  ? 230 LEU   AAA C   1 ? 
ATOM   1777 O  O   . LEU   A 1 231 ? -3.799  35.731 53.703 1.000 32.283  ? 230 LEU   AAA O   1 ? 
ATOM   1778 C  CB  . LEU   A 1 231 ? -0.800  35.514 54.458 1.000 36.215  ? 230 LEU   AAA CB  1 ? 
ATOM   1779 C  CG  . LEU   A 1 231 ? 0.701   35.733 54.288 1.000 37.676  ? 230 LEU   AAA CG  1 ? 
ATOM   1780 C  CD1 . LEU   A 1 231 ? 1.334   36.153 55.609 1.000 39.989  ? 230 LEU   AAA CD1 1 ? 
ATOM   1781 C  CD2 . LEU   A 1 231 ? 1.391   34.489 53.739 1.000 36.875  ? 230 LEU   AAA CD2 1 ? 
ATOM   1782 N  N   . SER   A 1 232 ? -3.314  33.475 53.544 1.000 33.471  ? 231 SER   AAA N   1 ? 
ATOM   1783 C  CA  . SER   A 1 232 ? -4.670  32.936 53.789 1.000 29.643  ? 231 SER   AAA CA  1 ? 
ATOM   1784 C  C   . SER   A 1 232 ? -4.961  32.890 55.308 1.000 34.670  ? 231 SER   AAA C   1 ? 
ATOM   1785 O  O   . SER   A 1 232 ? -6.163  32.815 55.680 1.000 36.414  ? 231 SER   AAA O   1 ? 
ATOM   1786 C  CB  . SER   A 1 232 ? -4.800  31.581 53.132 1.000 34.607  ? 231 SER   AAA CB  1 ? 
ATOM   1787 O  OG  . SER   A 1 232 ? -4.061  30.609 53.856 1.000 40.117  ? 231 SER   AAA OG  1 ? 
ATOM   1788 N  N   . ASN   A 1 233 ? -3.923  32.909 56.151 1.000 35.626  ? 232 ASN   AAA N   1 ? 
ATOM   1789 C  CA  . ASN   A 1 233 ? -4.034  32.840 57.646 1.000 36.302  ? 232 ASN   AAA CA  1 ? 
ATOM   1790 C  C   . ASN   A 1 233 ? -4.340  34.230 58.219 1.000 35.009  ? 232 ASN   AAA C   1 ? 
ATOM   1791 O  O   . ASN   A 1 233 ? -4.038  35.216 57.541 1.000 34.954  ? 232 ASN   AAA O   1 ? 
ATOM   1792 C  CB  . ASN   A 1 233 ? -2.754  32.345 58.317 1.000 34.744  ? 232 ASN   AAA CB  1 ? 
ATOM   1793 C  CG  . ASN   A 1 233 ? -1.547  33.203 57.970 1.000 36.325  ? 232 ASN   AAA CG  1 ? 
ATOM   1794 O  OD1 . ASN   A 1 233 ? -1.082  34.019 58.774 1.000 37.704  ? 232 ASN   AAA OD1 1 ? 
ATOM   1795 N  ND2 . ASN   A 1 233 ? -1.045  33.041 56.765 1.000 34.011  ? 232 ASN   AAA ND2 1 ? 
ATOM   1796 N  N   . VAL   A 1 234 ? -4.836  34.306 59.459 1.000 39.465  ? 233 VAL   AAA N   1 ? 
ATOM   1797 C  CA  . VAL   A 1 234 ? -5.025  35.598 60.177 1.000 39.437  ? 233 VAL   AAA CA  1 ? 
ATOM   1798 C  C   . VAL   A 1 234 ? -3.692  36.007 60.793 1.000 34.245  ? 233 VAL   AAA C   1 ? 
ATOM   1799 O  O   . VAL   A 1 234 ? -2.857  35.121 61.084 1.000 34.924  ? 233 VAL   AAA O   1 ? 
ATOM   1800 C  CB  . VAL   A 1 234 ? -6.127  35.531 61.243 1.000 41.511  ? 233 VAL   AAA CB  1 ? 
ATOM   1801 C  CG1 . VAL   A 1 234 ? -7.470  35.140 60.628 1.000 41.459  ? 233 VAL   AAA CG1 1 ? 
ATOM   1802 C  CG2 . VAL   A 1 234 ? -5.740  34.600 62.389 1.000 47.360  ? 233 VAL   AAA CG2 1 ? 
ATOM   1803 N  N   . GLU   A 1 235 ? -3.527  37.314 60.973 1.000 32.670  ? 234 GLU   AAA N   1 ? 
ATOM   1804 C  CA  . GLU   A 1 235 ? -2.343  37.948 61.579 1.000 37.896  ? 234 GLU   AAA CA  1 ? 
ATOM   1805 C  C   . GLU   A 1 235 ? -1.992  37.183 62.854 1.000 34.343  ? 234 GLU   AAA C   1 ? 
ATOM   1806 O  O   . GLU   A 1 235 ? -2.904  36.934 63.663 1.000 37.133  ? 234 GLU   AAA O   1 ? 
ATOM   1807 C  CB  . GLU   A 1 235 ? -2.653  39.418 61.879 1.000 45.211  ? 234 GLU   AAA CB  1 ? 
ATOM   1808 C  CG  . GLU   A 1 235 ? -1.493  40.171 62.491 1.000 37.764  ? 234 GLU   AAA CG  1 ? 
ATOM   1809 C  CD  . GLU   A 1 235 ? -1.727  41.657 62.571 1.000 44.227  ? 234 GLU   AAA CD  1 ? 
ATOM   1810 O  OE1 . GLU   A 1 235 ? -1.784  42.298 61.506 1.000 37.590  ? 234 GLU   AAA OE1 1 ? 
ATOM   1811 O  OE2 . GLU   A 1 235 ? -1.869  42.158 63.699 1.000 54.943  ? 234 GLU   AAA OE2 1 ? 
ATOM   1812 N  N   . GLY   A 1 236 ? -0.723  36.832 63.021 1.000 30.395  ? 235 GLY   AAA N   1 ? 
ATOM   1813 C  CA  . GLY   A 1 236 ? -0.199  36.216 64.251 1.000 41.313  ? 235 GLY   AAA CA  1 ? 
ATOM   1814 C  C   . GLY   A 1 236 ? -0.076  34.718 64.109 1.000 40.628  ? 235 GLY   AAA C   1 ? 
ATOM   1815 O  O   . GLY   A 1 236 ? 0.670   34.123 64.886 1.000 56.723  ? 235 GLY   AAA O   1 ? 
ATOM   1816 N  N   . ASP   A 1 237 ? -0.794  34.112 63.168 1.000 43.065  ? 236 ASP   AAA N   1 ? 
ATOM   1817 C  CA  . ASP   A 1 237 ? -0.701  32.648 62.924 1.000 45.579  ? 236 ASP   AAA CA  1 ? 
ATOM   1818 C  C   . ASP   A 1 237 ? 0.453   32.370 61.946 1.000 45.601  ? 236 ASP   AAA C   1 ? 
ATOM   1819 O  O   . ASP   A 1 237 ? 1.061   33.352 61.352 1.000 40.978  ? 236 ASP   AAA O   1 ? 
ATOM   1820 C  CB  . ASP   A 1 237 ? -2.029  32.055 62.439 1.000 44.612  ? 236 ASP   AAA CB  1 ? 
ATOM   1821 C  CG  . ASP   A 1 237 ? -3.110  31.956 63.495 1.000 45.350  ? 236 ASP   AAA CG  1 ? 
ATOM   1822 O  OD1 . ASP   A 1 237 ? -2.776  32.076 64.691 1.000 55.433  ? 236 ASP   AAA OD1 1 ? 
ATOM   1823 O  OD2 . ASP   A 1 237 ? -4.278  31.740 63.114 1.000 50.153  ? 236 ASP   AAA OD2 1 ? 
ATOM   1824 N  N   . ASN   A 1 238 ? 0.774   31.081 61.801 1.000 42.601  ? 237 ASN   AAA N   1 ? 
ATOM   1825 C  CA  . ASN   A 1 238 ? 1.796   30.610 60.834 1.000 42.918  ? 237 ASN   AAA CA  1 ? 
ATOM   1826 C  C   . ASN   A 1 238 ? 1.332   30.944 59.421 1.000 41.422  ? 237 ASN   AAA C   1 ? 
ATOM   1827 O  O   . ASN   A 1 238 ? 0.149   30.759 59.100 1.000 36.936  ? 237 ASN   AAA O   1 ? 
ATOM   1828 C  CB  . ASN   A 1 238 ? 2.143   29.134 60.972 1.000 50.309  ? 237 ASN   AAA CB  1 ? 
ATOM   1829 C  CG  . ASN   A 1 238 ? 3.336   28.948 61.887 1.000 65.510  ? 237 ASN   AAA CG  1 ? 
ATOM   1830 O  OD1 . ASN   A 1 238 ? 4.495   29.165 61.483 1.000 60.340  ? 237 ASN   AAA OD1 1 ? 
ATOM   1831 N  ND2 . ASN   A 1 238 ? 3.051   28.559 63.118 1.000 60.435  ? 237 ASN   AAA ND2 1 ? 
ATOM   1832 N  N   . ALA   A 1 239 ? 2.281   31.413 58.626 1.000 42.290  ? 238 ALA   AAA N   1 ? 
ATOM   1833 C  CA  . ALA   A 1 239 ? 2.083   31.899 57.249 1.000 47.097  ? 238 ALA   AAA CA  1 ? 
ATOM   1834 C  C   . ALA   A 1 239 ? 1.591   30.748 56.367 1.000 42.329  ? 238 ALA   AAA C   1 ? 
ATOM   1835 O  O   . ALA   A 1 239 ? 2.239   29.694 56.367 1.000 46.091  ? 238 ALA   AAA O   1 ? 
ATOM   1836 C  CB  . ALA   A 1 239 ? 3.381   32.487 56.743 1.000 50.202  ? 238 ALA   AAA CB  1 ? 
ATOM   1837 N  N   . VAL   A 1 240 ? 0.488   30.958 55.649 1.000 40.515  ? 239 VAL   AAA N   1 ? 
ATOM   1838 C  CA  . VAL   A 1 240 ? -0.047  30.024 54.617 1.000 40.971  ? 239 VAL   AAA CA  1 ? 
ATOM   1839 C  C   . VAL   A 1 240 ? -0.265  30.858 53.356 1.000 37.465  ? 239 VAL   AAA C   1 ? 
ATOM   1840 O  O   . VAL   A 1 240 ? -1.274  31.548 53.187 1.000 37.876  ? 239 VAL   AAA O   1 ? 
ATOM   1841 C  CB  . VAL   A 1 240 ? -1.317  29.288 55.086 1.000 43.311  ? 239 VAL   AAA CB  1 ? 
ATOM   1842 C  CG1 . VAL   A 1 240 ? -1.807  28.286 54.045 1.000 41.298  ? 239 VAL   AAA CG1 1 ? 
ATOM   1843 C  CG2 . VAL   A 1 240 ? -1.111  28.614 56.439 1.000 36.955  ? 239 VAL   AAA CG2 1 ? 
ATOM   1844 N  N   . PRO   A 1 241 ? 0.735   30.873 52.455 1.000 33.168  ? 240 PRO   AAA N   1 ? 
ATOM   1845 C  CA  . PRO   A 1 241 ? 0.591   31.598 51.207 1.000 32.415  ? 240 PRO   AAA CA  1 ? 
ATOM   1846 C  C   . PRO   A 1 241 ? -0.636  31.083 50.443 1.000 32.860  ? 240 PRO   AAA C   1 ? 
ATOM   1847 O  O   . PRO   A 1 241 ? -0.990  29.904 50.506 1.000 38.572  ? 240 PRO   AAA O   1 ? 
ATOM   1848 C  CB  . PRO   A 1 241 ? 1.906   31.331 50.462 1.000 42.702  ? 240 PRO   AAA CB  1 ? 
ATOM   1849 C  CG  . PRO   A 1 241 ? 2.886   30.878 51.548 1.000 45.125  ? 240 PRO   AAA CG  1 ? 
ATOM   1850 C  CD  . PRO   A 1 241 ? 2.033   30.194 52.587 1.000 41.313  ? 240 PRO   AAA CD  1 ? 
ATOM   1851 N  N   . MET   A 1 242 ? -1.258  32.029 49.759 1.000 35.114  ? 241 MET   AAA N   1 ? 
ATOM   1852 C  CA  . MET   A 1 242 ? -2.422  31.888 48.869 1.000 33.757  ? 241 MET   AAA CA  1 ? 
ATOM   1853 C  C   . MET   A 1 242 ? -1.898  31.430 47.489 1.000 31.934  ? 241 MET   AAA C   1 ? 
ATOM   1854 O  O   . MET   A 1 242 ? -1.745  32.242 46.560 1.000 30.934  ? 241 MET   AAA O   1 ? 
ATOM   1855 C  CB  . MET   A 1 242 ? -3.095  33.264 48.809 1.000 35.621  ? 241 MET   AAA CB  1 ? 
ATOM   1856 C  CG  . MET   A 1 242 ? -4.556  33.247 49.031 1.000 37.601  ? 241 MET   AAA CG  1 ? 
ATOM   1857 S  SD  . MET   A 1 242 ? -5.154  34.926 48.754 1.000 33.431  ? 241 MET   AAA SD  1 ? 
ATOM   1858 C  CE  . MET   A 1 242 ? -5.354  35.549 50.422 1.000 31.653  ? 241 MET   AAA CE  1 ? 
ATOM   1859 N  N   . GLN   A 1 243 ? -1.517  30.164 47.389 1.000 31.105  ? 242 GLN   AAA N   1 ? 
ATOM   1860 C  CA  . GLN   A 1 243 ? -0.780  29.598 46.224 1.000 35.674  ? 242 GLN   AAA CA  1 ? 
ATOM   1861 C  C   . GLN   A 1 243 ? -1.675  29.467 44.983 1.000 33.775  ? 242 GLN   AAA C   1 ? 
ATOM   1862 O  O   . GLN   A 1 243 ? -1.148  29.662 43.892 1.000 33.717  ? 242 GLN   AAA O   1 ? 
ATOM   1863 C  CB  . GLN   A 1 243 ? -0.156  28.255 46.606 1.000 44.387  ? 242 GLN   AAA CB  1 ? 
ATOM   1864 C  CG  . GLN   A 1 243 ? 1.019   28.448 47.547 1.000 43.926  ? 242 GLN   AAA CG  1 ? 
ATOM   1865 C  CD  . GLN   A 1 243 ? 2.009   27.325 47.422 1.000 49.169  ? 242 GLN   AAA CD  1 ? 
ATOM   1866 O  OE1 . GLN   A 1 243 ? 2.475   27.006 46.334 1.000 57.388  ? 242 GLN   AAA OE1 1 ? 
ATOM   1867 N  NE2 . GLN   A 1 243 ? 2.333   26.721 48.547 1.000 50.127  ? 242 GLN   AAA NE2 1 ? 
ATOM   1868 N  N   . HIS   A 1 244 ? -2.952  29.100 45.110 1.000 33.482  ? 243 HIS   AAA N   1 ? 
ATOM   1869 C  CA  . HIS   A 1 244 ? -3.863  28.956 43.938 1.000 28.521  ? 243 HIS   AAA CA  1 ? 
ATOM   1870 C  C   . HIS   A 1 244 ? -5.347  29.116 44.323 1.000 26.400  ? 243 HIS   AAA C   1 ? 
ATOM   1871 O  O   . HIS   A 1 244 ? -5.707  28.962 45.489 1.000 27.560  ? 243 HIS   AAA O   1 ? 
ATOM   1872 C  CB  . HIS   A 1 244 ? -3.625  27.608 43.235 1.000 31.249  ? 243 HIS   AAA CB  1 ? 
ATOM   1873 C  CG  . HIS   A 1 244 ? -3.820  26.454 44.149 1.000 33.950  ? 243 HIS   AAA CG  1 ? 
ATOM   1874 N  ND1 . HIS   A 1 244 ? -5.011  25.795 44.217 1.000 36.265  ? 243 HIS   AAA ND1 1 ? 
ATOM   1875 C  CD2 . HIS   A 1 244 ? -3.007  25.896 45.076 1.000 38.526  ? 243 HIS   AAA CD2 1 ? 
ATOM   1876 C  CE1 . HIS   A 1 244 ? -4.919  24.830 45.114 1.000 40.504  ? 243 HIS   AAA CE1 1 ? 
ATOM   1877 N  NE2 . HIS   A 1 244 ? -3.687  24.870 45.657 1.000 33.153  ? 243 HIS   AAA NE2 1 ? 
ATOM   1878 N  N   . ASN   A 1 245 ? -6.191  29.454 43.353 1.000 29.905  ? 244 ASN   AAA N   1 ? 
ATOM   1879 C  CA  . ASN   A 1 245 ? -7.649  29.659 43.585 1.000 25.518  ? 244 ASN   AAA CA  1 ? 
ATOM   1880 C  C   . ASN   A 1 245 ? -8.421  29.529 42.253 1.000 27.198  ? 244 ASN   AAA C   1 ? 
ATOM   1881 O  O   . ASN   A 1 245 ? -9.535  30.122 42.119 1.000 25.497  ? 244 ASN   AAA O   1 ? 
ATOM   1882 C  CB  . ASN   A 1 245 ? -7.866  31.005 44.303 1.000 25.813  ? 244 ASN   AAA CB  1 ? 
ATOM   1883 C  CG  . ASN   A 1 245 ? -7.312  32.185 43.546 1.000 26.880  ? 244 ASN   AAA CG  1 ? 
ATOM   1884 O  OD1 . ASN   A 1 245 ? -6.986  32.064 42.358 1.000 24.216  ? 244 ASN   AAA OD1 1 ? 
ATOM   1885 N  ND2 . ASN   A 1 245 ? -7.276  33.352 44.218 1.000 26.107  ? 244 ASN   AAA ND2 1 ? 
ATOM   1886 N  N   . ASN   A 1 246 ? -7.891  28.718 41.321 1.000 24.406  ? 245 ASN   AAA N   1 ? 
ATOM   1887 C  CA  . ASN   A 1 246 ? -8.523  28.447 40.002 1.000 23.608  ? 245 ASN   AAA CA  1 ? 
ATOM   1888 C  C   . ASN   A 1 246 ? -9.284  27.116 40.037 1.000 28.840  ? 245 ASN   AAA C   1 ? 
ATOM   1889 O  O   . ASN   A 1 246 ? -8.755  26.070 40.507 1.000 31.919  ? 245 ASN   AAA O   1 ? 
ATOM   1890 C  CB  . ASN   A 1 246 ? -7.573  28.586 38.820 1.000 25.382  ? 245 ASN   AAA CB  1 ? 
ATOM   1891 C  CG  . ASN   A 1 246 ? -6.479  27.539 38.782 1.000 26.466  ? 245 ASN   AAA CG  1 ? 
ATOM   1892 O  OD1 . ASN   A 1 246 ? -6.108  27.036 37.711 1.000 31.890  ? 245 ASN   AAA OD1 1 ? 
ATOM   1893 N  ND2 . ASN   A 1 246 ? -5.928  27.246 39.939 1.000 24.923  ? 245 ASN   AAA ND2 1 ? 
ATOM   1894 N  N   . ARG   A 1 247 ? -10.515 27.182 39.552 1.000 22.996  ? 246 ARG   AAA N   1 ? 
ATOM   1895 C  CA  . ARG   A 1 247 ? -11.358 25.980 39.423 1.000 24.335  ? 246 ARG   AAA CA  1 ? 
ATOM   1896 C  C   . ARG   A 1 247 ? -11.055 25.337 38.075 1.000 23.985  ? 246 ARG   AAA C   1 ? 
ATOM   1897 O  O   . ARG   A 1 247 ? -10.901 26.029 37.038 1.000 25.154  ? 246 ARG   AAA O   1 ? 
ATOM   1898 C  CB  . ARG   A 1 247 ? -12.856 26.301 39.483 1.000 22.964  ? 246 ARG   AAA CB  1 ? 
ATOM   1899 C  CG  . ARG   A 1 247 ? -13.712 25.051 39.646 1.000 26.169  ? 246 ARG   AAA CG  1 ? 
ATOM   1900 C  CD  . ARG   A 1 247 ? -15.189 25.298 39.409 1.000 27.818  ? 246 ARG   AAA CD  1 ? 
ATOM   1901 N  NE  . ARG   A 1 247 ? -16.079 24.233 39.878 1.000 24.693  ? 246 ARG   AAA NE  1 ? 
ATOM   1902 C  CZ  . ARG   A 1 247 ? -17.393 24.157 39.633 1.000 27.194  ? 246 ARG   AAA CZ  1 ? 
ATOM   1903 N  NH1 . ARG   A 1 247 ? -17.997 25.071 38.894 1.000 29.326  ? 246 ARG   AAA NH1 1 ? 
ATOM   1904 N  NH2 . ARG   A 1 247 ? -18.119 23.133 40.072 1.000 32.723  ? 246 ARG   AAA NH2 1 ? 
ATOM   1905 N  N   . PRO   A 1 248 ? -11.003 23.980 38.031 1.000 25.120  ? 247 PRO   AAA N   1 ? 
ATOM   1906 C  CA  . PRO   A 1 248 ? -10.921 23.307 36.742 1.000 25.077  ? 247 PRO   AAA CA  1 ? 
ATOM   1907 C  C   . PRO   A 1 248 ? -12.125 23.553 35.847 1.000 25.185  ? 247 PRO   AAA C   1 ? 
ATOM   1908 O  O   . PRO   A 1 248 ? -13.188 23.839 36.365 1.000 28.315  ? 247 PRO   AAA O   1 ? 
ATOM   1909 C  CB  . PRO   A 1 248 ? -10.950 21.793 37.086 1.000 27.443  ? 247 PRO   AAA CB  1 ? 
ATOM   1910 C  CG  . PRO   A 1 248 ? -10.681 21.720 38.581 1.000 29.752  ? 247 PRO   AAA CG  1 ? 
ATOM   1911 C  CD  . PRO   A 1 248 ? -11.089 23.066 39.181 1.000 27.539  ? 247 PRO   AAA CD  1 ? 
ATOM   1912 N  N   . THR   A 1 249 ? -11.940 23.410 34.546 1.000 23.298  ? 248 THR   AAA N   1 ? 
ATOM   1913 C  CA  . THR   A 1 249 ? -13.043 23.561 33.584 1.000 24.423  ? 248 THR   AAA CA  1 ? 
ATOM   1914 C  C   . THR   A 1 249 ? -14.064 22.415 33.763 1.000 29.044  ? 248 THR   AAA C   1 ? 
ATOM   1915 O  O   . THR   A 1 249 ? -13.701 21.296 34.222 1.000 31.892  ? 248 THR   AAA O   1 ? 
ATOM   1916 C  CB  . THR   A 1 249 ? -12.505 23.672 32.157 1.000 27.858  ? 248 THR   AAA CB  1 ? 
ATOM   1917 O  OG1 . THR   A 1 249 ? -11.721 22.517 31.871 1.000 30.107  ? 248 THR   AAA OG1 1 ? 
ATOM   1918 C  CG2 . THR   A 1 249 ? -11.677 24.926 31.924 1.000 25.964  ? 248 THR   AAA CG2 1 ? 
ATOM   1919 N  N   . GLN   A 1 250 ? -15.311 22.764 33.452 1.000 28.037  ? 249 GLN   AAA N   1 ? 
ATOM   1920 C  CA  . GLN   A 1 250 ? -16.551 22.019 33.696 1.000 28.610  ? 249 GLN   AAA CA  1 ? 
ATOM   1921 C  C   . GLN   A 1 250 ? -17.187 21.680 32.349 1.000 27.676  ? 249 GLN   AAA C   1 ? 
ATOM   1922 O  O   . GLN   A 1 250 ? -17.024 22.399 31.356 1.000 30.187  ? 249 GLN   AAA O   1 ? 
ATOM   1923 C  CB  . GLN   A 1 250 ? -17.446 22.861 34.607 1.000 26.652  ? 249 GLN   AAA CB  1 ? 
ATOM   1924 C  CG  . GLN   A 1 250 ? -16.804 23.161 35.959 1.000 27.935  ? 249 GLN   AAA CG  1 ? 
ATOM   1925 C  CD  . GLN   A 1 250 ? -16.348 21.938 36.721 1.000 33.145  ? 249 GLN   AAA CD  1 ? 
ATOM   1926 O  OE1 . GLN   A 1 250 ? -17.089 20.983 36.879 1.000 37.532  ? 249 GLN   AAA OE1 1 ? 
ATOM   1927 N  NE2 . GLN   A 1 250 ? -15.112 21.961 37.194 1.000 31.829  ? 249 GLN   AAA NE2 1 ? 
ATOM   1928 N  N   . PRO   A 1 251 ? -17.943 20.562 32.269 1.000 36.282  ? 250 PRO   AAA N   1 ? 
ATOM   1929 C  CA  . PRO   A 1 251 ? -18.618 20.200 31.026 1.000 37.362  ? 250 PRO   AAA CA  1 ? 
ATOM   1930 C  C   . PRO   A 1 251 ? -19.633 21.222 30.484 1.000 34.751  ? 250 PRO   AAA C   1 ? 
ATOM   1931 O  O   . PRO   A 1 251 ? -20.422 21.769 31.253 1.000 35.113  ? 250 PRO   AAA O   1 ? 
ATOM   1932 C  CB  . PRO   A 1 251 ? -19.358 18.890 31.385 1.000 38.938  ? 250 PRO   AAA CB  1 ? 
ATOM   1933 C  CG  . PRO   A 1 251 ? -18.722 18.380 32.673 1.000 41.737  ? 250 PRO   AAA CG  1 ? 
ATOM   1934 C  CD  . PRO   A 1 251 ? -18.174 19.603 33.368 1.000 35.628  ? 250 PRO   AAA CD  1 ? 
ATOM   1935 N  N   . LEU   A 1 252 ? -19.570 21.469 29.174 1.000 32.658  ? 251 LEU   AAA N   1 ? 
ATOM   1936 C  CA  . LEU   A 1 252 ? -20.543 22.334 28.453 1.000 34.178  ? 251 LEU   AAA CA  1 ? 
ATOM   1937 C  C   . LEU   A 1 252 ? -21.979 21.802 28.592 1.000 32.959  ? 251 LEU   AAA C   1 ? 
ATOM   1938 O  O   . LEU   A 1 252 ? -22.908 22.626 28.725 1.000 33.159  ? 251 LEU   AAA O   1 ? 
ATOM   1939 C  CB  . LEU   A 1 252 ? -20.124 22.502 26.986 1.000 42.681  ? 251 LEU   AAA CB  1 ? 
ATOM   1940 C  CG  . LEU   A 1 252 ? -19.123 23.627 26.715 1.000 44.805  ? 251 LEU   AAA CG  1 ? 
ATOM   1941 C  CD1 . LEU   A 1 252 ? -18.872 23.796 25.222 1.000 48.269  ? 251 LEU   AAA CD1 1 ? 
ATOM   1942 C  CD2 . LEU   A 1 252 ? -19.604 24.926 27.335 1.000 37.348  ? 251 LEU   AAA CD2 1 ? 
ATOM   1943 N  N   . LYS   A 1 253 ? -22.177 20.477 28.579 1.000 40.488  ? 252 LYS   AAA N   1 ? 
ATOM   1944 C  CA  . LYS   A 1 253 ? -23.529 19.892 28.750 1.000 43.421  ? 252 LYS   AAA CA  1 ? 
ATOM   1945 C  C   . LYS   A 1 253 ? -24.465 20.572 27.749 1.000 35.796  ? 252 LYS   AAA C   1 ? 
ATOM   1946 O  O   . LYS   A 1 253 ? -25.594 20.885 28.098 1.000 35.621  ? 252 LYS   AAA O   1 ? 
ATOM   1947 C  CB  . LYS   A 1 253 ? -24.022 20.071 30.189 1.000 34.073  ? 252 LYS   AAA CB  1 ? 
ATOM   1948 C  CG  . LYS   A 1 253 ? -23.170 19.365 31.221 1.000 45.892  ? 252 LYS   AAA CG  1 ? 
ATOM   1949 C  CD  . LYS   A 1 253 ? -23.969 18.475 32.103 1.000 43.503  ? 252 LYS   AAA CD  1 ? 
ATOM   1950 C  CE  . LYS   A 1 253 ? -23.148 17.335 32.609 1.000 46.576  ? 252 LYS   AAA CE  1 ? 
ATOM   1951 N  NZ  . LYS   A 1 253 ? -24.034 16.379 33.294 1.000 66.547  ? 252 LYS   AAA NZ  1 ? 
ATOM   1952 N  N   . GLY   A 1 254 ? -24.002 20.783 26.526 1.000 39.520  ? 253 GLY   AAA N   1 ? 
ATOM   1953 C  CA  . GLY   A 1 254 ? -24.893 21.183 25.429 1.000 37.640  ? 253 GLY   AAA CA  1 ? 
ATOM   1954 C  C   . GLY   A 1 254 ? -24.999 22.681 25.267 1.000 37.175  ? 253 GLY   AAA C   1 ? 
ATOM   1955 O  O   . GLY   A 1 254 ? -25.612 23.083 24.259 1.000 41.551  ? 253 GLY   AAA O   1 ? 
ATOM   1956 N  N   . ARG   A 1 255 ? -24.468 23.476 26.195 1.000 33.916  ? 254 ARG   AAA N   1 ? 
ATOM   1957 C  CA  . ARG   A 1 255 ? -24.478 24.952 26.004 1.000 34.449  ? 254 ARG   AAA CA  1 ? 
ATOM   1958 C  C   . ARG   A 1 255 ? -23.698 25.305 24.733 1.000 33.472  ? 254 ARG   AAA C   1 ? 
ATOM   1959 O  O   . ARG   A 1 255 ? -22.790 24.541 24.323 1.000 37.864  ? 254 ARG   AAA O   1 ? 
ATOM   1960 C  CB  . ARG   A 1 255 ? -23.899 25.711 27.199 1.000 32.557  ? 254 ARG   AAA CB  1 ? 
ATOM   1961 C  CG  . ARG   A 1 255 ? -24.743 25.651 28.453 1.000 30.660  ? 254 ARG   AAA CG  1 ? 
ATOM   1962 C  CD  . ARG   A 1 255 ? -23.986 26.195 29.645 1.000 35.290  ? 254 ARG   AAA CD  1 ? 
ATOM   1963 N  NE  . ARG   A 1 255 ? -22.985 25.268 30.136 1.000 30.001  ? 254 ARG   AAA NE  1 ? 
ATOM   1964 C  CZ  . ARG   A 1 255 ? -22.085 25.512 31.064 1.000 28.828  ? 254 ARG   AAA CZ  1 ? 
ATOM   1965 N  NH1 . ARG   A 1 255 ? -21.972 26.766 31.511 1.000 29.638  ? 254 ARG   AAA NH1 1 ? 
ATOM   1966 N  NH2 . ARG   A 1 255 ? -21.219 24.575 31.431 1.000 26.845  ? 254 ARG   AAA NH2 1 ? 
ATOM   1967 N  N   . THR   A 1 256 ? -24.056 26.435 24.135 1.000 34.200  ? 255 THR   AAA N   1 ? 
ATOM   1968 C  CA  . THR   A 1 256 ? -23.407 27.013 22.935 1.000 35.013  ? 255 THR   AAA CA  1 ? 
ATOM   1969 C  C   . THR   A 1 256 ? -22.580 28.204 23.396 1.000 32.437  ? 255 THR   AAA C   1 ? 
ATOM   1970 O  O   . THR   A 1 256 ? -23.182 29.127 24.047 1.000 38.030  ? 255 THR   AAA O   1 ? 
ATOM   1971 C  CB  . THR   A 1 256 ? -24.464 27.427 21.907 1.000 39.460  ? 255 THR   AAA CB  1 ? 
ATOM   1972 O  OG1 . THR   A 1 256 ? -25.100 26.259 21.409 1.000 53.217  ? 255 THR   AAA OG1 1 ? 
ATOM   1973 C  CG2 . THR   A 1 256 ? -23.915 28.208 20.737 1.000 51.824  ? 255 THR   AAA CG2 1 ? 
ATOM   1974 N  N   . VAL   A 1 257 ? -21.288 28.194 23.094 1.000 30.881  ? 256 VAL   AAA N   1 ? 
ATOM   1975 C  CA  . VAL   A 1 257 ? -20.427 29.409 23.224 1.000 33.633  ? 256 VAL   AAA CA  1 ? 
ATOM   1976 C  C   . VAL   A 1 257 ? -20.564 30.244 21.949 1.000 34.358  ? 256 VAL   AAA C   1 ? 
ATOM   1977 O  O   . VAL   A 1 257 ? -20.138 29.799 20.896 1.000 35.083  ? 256 VAL   AAA O   1 ? 
ATOM   1978 C  CB  . VAL   A 1 257 ? -18.947 29.096 23.527 1.000 32.294  ? 256 VAL   AAA CB  1 ? 
ATOM   1979 C  CG1 . VAL   A 1 257 ? -18.165 30.369 23.799 1.000 34.088  ? 256 VAL   AAA CG1 1 ? 
ATOM   1980 C  CG2 . VAL   A 1 257 ? -18.796 28.144 24.706 1.000 35.566  ? 256 VAL   AAA CG2 1 ? 
ATOM   1981 N  N   . ARG   A 1 258 ? -21.031 31.488 22.087 1.000 32.624  ? 257 ARG   AAA N   1 ? 
ATOM   1982 C  CA  . ARG   A 1 258 ? -21.209 32.390 20.929 1.000 33.917  ? 257 ARG   AAA CA  1 ? 
ATOM   1983 C  C   . ARG   A 1 258 ? -20.005 33.336 20.848 1.000 32.483  ? 257 ARG   AAA C   1 ? 
ATOM   1984 O  O   . ARG   A 1 258 ? -19.411 33.673 21.904 1.000 32.703  ? 257 ARG   AAA O   1 ? 
ATOM   1985 C  CB  . ARG   A 1 258 ? -22.534 33.133 21.068 1.000 34.672  ? 257 ARG   AAA CB  1 ? 
ATOM   1986 C  CG  . ARG   A 1 258 ? -23.760 32.229 21.117 1.000 33.720  ? 257 ARG   AAA CG  1 ? 
ATOM   1987 C  CD  . ARG   A 1 258 ? -25.059 32.981 21.210 1.000 35.166  ? 257 ARG   AAA CD  1 ? 
ATOM   1988 N  NE  . ARG   A 1 258 ? -25.210 33.521 22.551 1.000 41.383  ? 257 ARG   AAA NE  1 ? 
ATOM   1989 C  CZ  . ARG   A 1 258 ? -25.826 34.658 22.839 1.000 36.293  ? 257 ARG   AAA CZ  1 ? 
ATOM   1990 N  NH1 . ARG   A 1 258 ? -26.313 35.422 21.879 1.000 42.410  ? 257 ARG   AAA NH1 1 ? 
ATOM   1991 N  NH2 . ARG   A 1 258 ? -25.930 35.050 24.087 1.000 44.923  ? 257 ARG   AAA NH2 1 ? 
ATOM   1992 N  N   . ALA   A 1 259 ? -19.640 33.721 19.627 1.000 32.121  ? 258 ALA   AAA N   1 ? 
ATOM   1993 C  CA  . ALA   A 1 259 ? -18.488 34.607 19.343 1.000 34.346  ? 258 ALA   AAA CA  1 ? 
ATOM   1994 C  C   . ALA   A 1 259 ? -19.035 35.890 18.726 1.000 35.120  ? 258 ALA   AAA C   1 ? 
ATOM   1995 O  O   . ALA   A 1 259 ? -19.949 35.837 17.861 1.000 39.458  ? 258 ALA   AAA O   1 ? 
ATOM   1996 C  CB  . ALA   A 1 259 ? -17.474 33.925 18.439 1.000 35.187  ? 258 ALA   AAA CB  1 ? 
ATOM   1997 N  N   . SER   A 1 260 ? -18.522 37.016 19.174 1.000 33.140  ? 259 SER   AAA N   1 ? 
ATOM   1998 C  CA  . SER   A 1 260 ? -18.924 38.343 18.671 1.000 33.985  ? 259 SER   AAA CA  1 ? 
ATOM   1999 C  C   . SER   A 1 260 ? -18.203 38.639 17.358 1.000 36.062  ? 259 SER   AAA C   1 ? 
ATOM   2000 O  O   . SER   A 1 260 ? -18.474 39.698 16.775 1.000 37.414  ? 259 SER   AAA O   1 ? 
ATOM   2001 C  CB  . SER   A 1 260 ? -18.609 39.379 19.704 1.000 31.938  ? 259 SER   AAA CB  1 ? 
ATOM   2002 O  OG  . SER   A 1 260 ? -17.226 39.664 19.721 1.000 31.369  ? 259 SER   AAA OG  1 ? 
ATOM   2003 N  N   . PHE   A 1 261 ? -17.299 37.756 16.940 1.000 39.512  ? 260 PHE   AAA N   1 ? 
ATOM   2004 C  CA  . PHE   A 1 261 ? -16.273 37.992 15.886 1.000 40.748  ? 260 PHE   AAA CA  1 ? 
ATOM   2005 C  C   . PHE   A 1 261 ? -16.074 36.703 15.062 1.000 40.938  ? 260 PHE   AAA C   1 ? 
ATOM   2006 O  O   . PHE   A 1 261 ? -15.418 36.662 14.021 1.000 43.323  ? 260 PHE   AAA O   1 ? 
ATOM   2007 C  CB  . PHE   A 1 261 ? -14.963 38.419 16.557 1.000 42.366  ? 260 PHE   AAA CB  1 ? 
ATOM   2008 C  CG  . PHE   A 1 261 ? -14.312 37.311 17.368 1.000 38.941  ? 260 PHE   AAA CG  1 ? 
ATOM   2009 C  CD1 . PHE   A 1 261 ? -14.697 37.068 18.682 1.000 35.176  ? 260 PHE   AAA CD1 1 ? 
ATOM   2010 C  CD2 . PHE   A 1 261 ? -13.343 36.483 16.804 1.000 42.685  ? 260 PHE   AAA CD2 1 ? 
ATOM   2011 C  CE1 . PHE   A 1 261 ? -14.120 36.043 19.420 1.000 37.484  ? 260 PHE   AAA CE1 1 ? 
ATOM   2012 C  CE2 . PHE   A 1 261 ? -12.777 35.441 17.540 1.000 43.606  ? 260 PHE   AAA CE2 1 ? 
ATOM   2013 C  CZ  . PHE   A 1 261 ? -13.154 35.236 18.855 1.000 39.870  ? 260 PHE   AAA CZ  1 ? 
ATOM   2014 O  OXT . PHE   A 1 261 ? -16.563 35.629 15.403 1.000 41.072  ? 260 PHE   AAA OXT 1 ? 
ATOM   2015 N  N   . ASP   B 1 5   ? 25.222  25.940 42.466 1.000 40.346  ? 4   ASP   BBB N   1 ? 
ATOM   2016 C  CA  . ASP   B 1 5   ? 26.415  25.149 42.893 1.000 36.351  ? 4   ASP   BBB CA  1 ? 
ATOM   2017 C  C   . ASP   B 1 5   ? 26.123  24.655 44.315 1.000 37.062  ? 4   ASP   BBB C   1 ? 
ATOM   2018 O  O   . ASP   B 1 5   ? 26.315  23.437 44.611 1.000 38.409  ? 4   ASP   BBB O   1 ? 
ATOM   2019 C  CB  . ASP   B 1 5   ? 27.709  25.964 42.691 1.000 39.770  ? 4   ASP   BBB CB  1 ? 
ATOM   2020 C  CG  . ASP   B 1 5   ? 28.980  25.128 42.799 1.000 42.821  ? 4   ASP   BBB CG  1 ? 
ATOM   2021 O  OD1 . ASP   B 1 5   ? 29.102  24.119 42.008 1.000 42.942  ? 4   ASP   BBB OD1 1 ? 
ATOM   2022 O  OD2 . ASP   B 1 5   ? 29.846  25.424 43.717 1.000 44.038  ? 4   ASP   BBB OD2 1 ? 
ATOM   2023 N  N   . TRP   B 1 6   ? 25.617  25.512 45.190 1.000 43.826  ? 5   TRP   BBB N   1 ? 
ATOM   2024 C  CA  . TRP   B 1 6   ? 25.218  25.126 46.572 1.000 35.393  ? 5   TRP   BBB CA  1 ? 
ATOM   2025 C  C   . TRP   B 1 6   ? 23.969  25.929 46.930 1.000 36.558  ? 5   TRP   BBB C   1 ? 
ATOM   2026 O  O   . TRP   B 1 6   ? 23.824  27.081 46.425 1.000 36.750  ? 5   TRP   BBB O   1 ? 
ATOM   2027 C  CB  . TRP   B 1 6   ? 26.357  25.378 47.584 1.000 32.508  ? 5   TRP   BBB CB  1 ? 
ATOM   2028 C  CG  . TRP   B 1 6   ? 26.631  26.846 47.826 1.000 29.076  ? 5   TRP   BBB CG  1 ? 
ATOM   2029 C  CD1 . TRP   B 1 6   ? 27.522  27.635 47.156 1.000 30.985  ? 5   TRP   BBB CD1 1 ? 
ATOM   2030 C  CD2 . TRP   B 1 6   ? 26.004  27.697 48.807 1.000 27.172  ? 5   TRP   BBB CD2 1 ? 
ATOM   2031 N  NE1 . TRP   B 1 6   ? 27.462  28.917 47.620 1.000 30.268  ? 5   TRP   BBB NE1 1 ? 
ATOM   2032 C  CE2 . TRP   B 1 6   ? 26.555  28.978 48.652 1.000 30.660  ? 5   TRP   BBB CE2 1 ? 
ATOM   2033 C  CE3 . TRP   B 1 6   ? 25.008  27.500 49.767 1.000 31.969  ? 5   TRP   BBB CE3 1 ? 
ATOM   2034 C  CZ2 . TRP   B 1 6   ? 26.145  30.043 49.454 1.000 28.811  ? 5   TRP   BBB CZ2 1 ? 
ATOM   2035 C  CZ3 . TRP   B 1 6   ? 24.633  28.537 50.583 1.000 30.835  ? 5   TRP   BBB CZ3 1 ? 
ATOM   2036 C  CH2 . TRP   B 1 6   ? 25.180  29.804 50.410 1.000 26.221  ? 5   TRP   BBB CH2 1 ? 
ATOM   2037 N  N   . GLY   B 1 7   ? 23.110  25.355 47.756 1.000 30.090  ? 6   GLY   BBB N   1 ? 
ATOM   2038 C  CA  . GLY   B 1 7   ? 21.931  26.041 48.318 1.000 35.774  ? 6   GLY   BBB CA  1 ? 
ATOM   2039 C  C   . GLY   B 1 7   ? 21.507  25.407 49.636 1.000 33.997  ? 6   GLY   BBB C   1 ? 
ATOM   2040 O  O   . GLY   B 1 7   ? 22.384  24.951 50.417 1.000 36.335  ? 6   GLY   BBB O   1 ? 
ATOM   2041 N  N   . TYR   B 1 8   ? 20.206  25.377 49.895 1.000 34.145  ? 7   TYR   BBB N   1 ? 
ATOM   2042 C  CA  . TYR   B 1 8   ? 19.645  24.809 51.137 1.000 35.438  ? 7   TYR   BBB CA  1 ? 
ATOM   2043 C  C   . TYR   B 1 8   ? 18.647  23.703 50.784 1.000 36.917  ? 7   TYR   BBB C   1 ? 
ATOM   2044 O  O   . TYR   B 1 8   ? 17.974  23.298 51.704 1.000 36.655  ? 7   TYR   BBB O   1 ? 
ATOM   2045 C  CB  . TYR   B 1 8   ? 19.062  25.945 51.973 1.000 30.907  ? 7   TYR   BBB CB  1 ? 
ATOM   2046 C  CG  . TYR   B 1 8   ? 20.116  26.865 52.551 1.000 28.886  ? 7   TYR   BBB CG  1 ? 
ATOM   2047 C  CD1 . TYR   B 1 8   ? 20.710  26.630 53.789 1.000 26.423  ? 7   TYR   BBB CD1 1 ? 
ATOM   2048 C  CD2 . TYR   B 1 8   ? 20.474  28.027 51.877 1.000 27.862  ? 7   TYR   BBB CD2 1 ? 
ATOM   2049 C  CE1 . TYR   B 1 8   ? 21.670  27.491 54.313 1.000 25.476  ? 7   TYR   BBB CE1 1 ? 
ATOM   2050 C  CE2 . TYR   B 1 8   ? 21.423  28.904 52.396 1.000 26.546  ? 7   TYR   BBB CE2 1 ? 
ATOM   2051 C  CZ  . TYR   B 1 8   ? 21.975  28.673 53.644 1.000 24.593  ? 7   TYR   BBB CZ  1 ? 
ATOM   2052 O  OH  . TYR   B 1 8   ? 22.959  29.448 54.168 1.000 25.426  ? 7   TYR   BBB OH  1 ? 
ATOM   2053 N  N   . ASP   B 1 9   ? 18.565  23.250 49.530 1.000 43.548  ? 8   ASP   BBB N   1 ? 
ATOM   2054 C  CA  . ASP   B 1 9   ? 17.660  22.125 49.124 1.000 48.203  ? 8   ASP   BBB CA  1 ? 
ATOM   2055 C  C   . ASP   B 1 9   ? 18.273  20.777 49.508 1.000 46.503  ? 8   ASP   BBB C   1 ? 
ATOM   2056 O  O   . ASP   B 1 9   ? 19.428  20.759 49.941 1.000 51.133  ? 8   ASP   BBB O   1 ? 
ATOM   2057 C  CB  . ASP   B 1 9   ? 17.424  22.087 47.613 1.000 62.766  ? 8   ASP   BBB CB  1 ? 
ATOM   2058 C  CG  . ASP   B 1 9   ? 16.477  23.160 47.131 1.000 77.956  ? 8   ASP   BBB CG  1 ? 
ATOM   2059 O  OD1 . ASP   B 1 9   ? 15.440  23.368 47.808 1.000 87.564  ? 8   ASP   BBB OD1 1 ? 
ATOM   2060 O  OD2 . ASP   B 1 9   ? 16.781  23.773 46.080 1.000 105.718 ? 8   ASP   BBB OD2 1 ? 
ATOM   2061 N  N   . ASP   B 1 10  ? 17.583  19.661 49.259 1.000 57.006  ? 9   ASP   BBB N   1 ? 
ATOM   2062 C  CA  . ASP   B 1 10  ? 18.161  18.320 49.565 1.000 60.861  ? 9   ASP   BBB CA  1 ? 
ATOM   2063 C  C   . ASP   B 1 10  ? 19.244  17.930 48.542 1.000 48.026  ? 9   ASP   BBB C   1 ? 
ATOM   2064 O  O   . ASP   B 1 10  ? 20.095  17.098 48.905 1.000 62.995  ? 9   ASP   BBB O   1 ? 
ATOM   2065 C  CB  . ASP   B 1 10  ? 17.056  17.281 49.711 1.000 66.412  ? 9   ASP   BBB CB  1 ? 
ATOM   2066 C  CG  . ASP   B 1 10  ? 16.074  17.701 50.785 1.000 74.728  ? 9   ASP   BBB CG  1 ? 
ATOM   2067 O  OD1 . ASP   B 1 10  ? 16.384  18.682 51.508 1.000 66.231  ? 9   ASP   BBB OD1 1 ? 
ATOM   2068 O  OD2 . ASP   B 1 10  ? 15.015  17.066 50.876 1.000 94.730  ? 9   ASP   BBB OD2 1 ? 
ATOM   2069 N  N   . LYS   B 1 11  ? 19.235  18.534 47.344 1.000 48.643  ? 10  LYS   BBB N   1 ? 
ATOM   2070 C  CA  . LYS   B 1 11  ? 20.214  18.235 46.260 1.000 47.888  ? 10  LYS   BBB CA  1 ? 
ATOM   2071 C  C   . LYS   B 1 11  ? 21.520  18.981 46.532 1.000 46.593  ? 10  LYS   BBB C   1 ? 
ATOM   2072 O  O   . LYS   B 1 11  ? 22.551  18.417 46.178 1.000 47.153  ? 10  LYS   BBB O   1 ? 
ATOM   2073 C  CB  . LYS   B 1 11  ? 19.694  18.595 44.861 1.000 42.293  ? 10  LYS   BBB CB  1 ? 
ATOM   2074 N  N   . ASN   B 1 12  ? 21.475  20.202 47.096 1.000 55.175  ? 11  ASN   BBB N   1 ? 
ATOM   2075 C  CA  . ASN   B 1 12  ? 22.648  21.114 47.151 1.000 47.210  ? 11  ASN   BBB CA  1 ? 
ATOM   2076 C  C   . ASN   B 1 12  ? 22.829  21.722 48.551 1.000 39.516  ? 11  ASN   BBB C   1 ? 
ATOM   2077 O  O   . ASN   B 1 12  ? 23.698  22.618 48.680 1.000 36.695  ? 11  ASN   BBB O   1 ? 
ATOM   2078 C  CB  . ASN   B 1 12  ? 22.523  22.226 46.104 1.000 47.406  ? 11  ASN   BBB CB  1 ? 
ATOM   2079 C  CG  . ASN   B 1 12  ? 21.328  23.148 46.272 1.000 47.054  ? 11  ASN   BBB CG  1 ? 
ATOM   2080 O  OD1 . ASN   B 1 12  ? 20.613  23.155 47.281 1.000 42.663  ? 11  ASN   BBB OD1 1 ? 
ATOM   2081 N  ND2 . ASN   B 1 12  ? 21.132  23.973 45.270 1.000 48.865  ? 11  ASN   BBB ND2 1 ? 
ATOM   2082 N  N   . GLY   B 1 13  ? 22.074  21.217 49.534 1.000 41.097  ? 12  GLY   BBB N   1 ? 
ATOM   2083 C  CA  . GLY   B 1 13  ? 21.940  21.766 50.892 1.000 37.702  ? 12  GLY   BBB CA  1 ? 
ATOM   2084 C  C   . GLY   B 1 13  ? 23.061  21.327 51.824 1.000 40.688  ? 12  GLY   BBB C   1 ? 
ATOM   2085 O  O   . GLY   B 1 13  ? 23.984  20.612 51.428 1.000 41.564  ? 12  GLY   BBB O   1 ? 
ATOM   2086 N  N   . PRO   B 1 14  ? 22.986  21.780 53.095 1.000 33.440  ? 13  PRO   BBB N   1 ? 
ATOM   2087 C  CA  . PRO   B 1 14  ? 24.048  21.598 54.096 1.000 34.857  ? 13  PRO   BBB CA  1 ? 
ATOM   2088 C  C   . PRO   B 1 14  ? 24.651  20.193 54.159 1.000 32.946  ? 13  PRO   BBB C   1 ? 
ATOM   2089 O  O   . PRO   B 1 14  ? 25.880  20.072 54.323 1.000 32.310  ? 13  PRO   BBB O   1 ? 
ATOM   2090 C  CB  . PRO   B 1 14  ? 23.331  21.934 55.415 1.000 34.666  ? 13  PRO   BBB CB  1 ? 
ATOM   2091 C  CG  . PRO   B 1 14  ? 22.290  22.984 55.008 1.000 34.005  ? 13  PRO   BBB CG  1 ? 
ATOM   2092 C  CD  . PRO   B 1 14  ? 21.887  22.625 53.591 1.000 36.554  ? 13  PRO   BBB CD  1 ? 
ATOM   2093 N  N   . GLU   B 1 15  ? 23.817  19.157 54.010 1.000 37.601  ? 14  GLU   BBB N   1 ? 
ATOM   2094 C  CA  . GLU   B 1 15  ? 24.300  17.741 54.096 1.000 39.564  ? 14  GLU   BBB CA  1 ? 
ATOM   2095 C  C   . GLU   B 1 15  ? 25.179  17.373 52.900 1.000 40.138  ? 14  GLU   BBB C   1 ? 
ATOM   2096 O  O   . GLU   B 1 15  ? 25.976  16.437 53.073 1.000 43.521  ? 14  GLU   BBB O   1 ? 
ATOM   2097 C  CB  . GLU   B 1 15  ? 23.139  16.770 54.281 1.000 47.086  ? 14  GLU   BBB CB  1 ? 
ATOM   2098 C  CG  . GLU   B 1 15  ? 22.354  17.074 55.553 1.000 55.419  ? 14  GLU   BBB CG  1 ? 
ATOM   2099 C  CD  . GLU   B 1 15  ? 23.201  17.342 56.797 1.000 61.441  ? 14  GLU   BBB CD  1 ? 
ATOM   2100 O  OE1 . GLU   B 1 15  ? 22.983  18.420 57.472 1.000 75.291  ? 14  GLU   BBB OE1 1 ? 
ATOM   2101 O  OE2 . GLU   B 1 15  ? 24.088  16.488 57.103 1.000 59.341  ? 14  GLU   BBB OE2 1 ? 
ATOM   2102 N  N   . GLN   B 1 16  ? 25.081  18.103 51.776 1.000 36.541  ? 15  GLN   BBB N   1 ? 
ATOM   2103 C  CA  . GLN   B 1 16  ? 25.889  17.874 50.544 1.000 40.429  ? 15  GLN   BBB CA  1 ? 
ATOM   2104 C  C   . GLN   B 1 16  ? 27.111  18.801 50.471 1.000 45.795  ? 15  GLN   BBB C   1 ? 
ATOM   2105 O  O   . GLN   B 1 16  ? 27.922  18.563 49.596 1.000 45.672  ? 15  GLN   BBB O   1 ? 
ATOM   2106 C  CB  . GLN   B 1 16  ? 25.088  18.111 49.257 1.000 47.241  ? 15  GLN   BBB CB  1 ? 
ATOM   2107 C  CG  . GLN   B 1 16  ? 23.771  17.378 49.214 1.000 49.355  ? 15  GLN   BBB CG  1 ? 
ATOM   2108 C  CD  . GLN   B 1 16  ? 24.064  15.900 49.225 1.000 52.989  ? 15  GLN   BBB CD  1 ? 
ATOM   2109 O  OE1 . GLN   B 1 16  ? 23.552  15.158 50.060 1.000 87.072  ? 15  GLN   BBB OE1 1 ? 
ATOM   2110 N  NE2 . GLN   B 1 16  ? 24.917  15.458 48.302 1.000 54.259  ? 15  GLN   BBB NE2 1 ? 
ATOM   2111 N  N   . TRP   B 1 17  ? 27.165  19.951 51.196 1.000 35.996  ? 16  TRP   BBB N   1 ? 
ATOM   2112 C  CA  . TRP   B 1 17  ? 28.273  20.925 51.039 1.000 30.445  ? 16  TRP   BBB CA  1 ? 
ATOM   2113 C  C   . TRP   B 1 17  ? 29.683  20.302 51.032 1.000 31.178  ? 16  TRP   BBB C   1 ? 
ATOM   2114 O  O   . TRP   B 1 17  ? 30.532  20.807 50.266 1.000 33.337  ? 16  TRP   BBB O   1 ? 
ATOM   2115 C  CB  . TRP   B 1 17  ? 28.146  22.055 52.064 1.000 32.144  ? 16  TRP   BBB CB  1 ? 
ATOM   2116 C  CG  . TRP   B 1 17  ? 26.943  22.932 51.865 1.000 28.560  ? 16  TRP   BBB CG  1 ? 
ATOM   2117 C  CD1 . TRP   B 1 17  ? 26.132  23.003 50.770 1.000 29.132  ? 16  TRP   BBB CD1 1 ? 
ATOM   2118 C  CD2 . TRP   B 1 17  ? 26.452  23.915 52.800 1.000 26.707  ? 16  TRP   BBB CD2 1 ? 
ATOM   2119 N  NE1 . TRP   B 1 17  ? 25.156  23.947 50.980 1.000 34.457  ? 16  TRP   BBB NE1 1 ? 
ATOM   2120 C  CE2 . TRP   B 1 17  ? 25.292  24.480 52.235 1.000 28.024  ? 16  TRP   BBB CE2 1 ? 
ATOM   2121 C  CE3 . TRP   B 1 17  ? 26.826  24.296 54.098 1.000 27.435  ? 16  TRP   BBB CE3 1 ? 
ATOM   2122 C  CZ2 . TRP   B 1 17  ? 24.573  25.506 52.876 1.000 29.264  ? 16  TRP   BBB CZ2 1 ? 
ATOM   2123 C  CZ3 . TRP   B 1 17  ? 26.119  25.319 54.736 1.000 24.955  ? 16  TRP   BBB CZ3 1 ? 
ATOM   2124 C  CH2 . TRP   B 1 17  ? 24.957  25.840 54.163 1.000 32.284  ? 16  TRP   BBB CH2 1 ? 
ATOM   2125 N  N   . SER   B 1 18  ? 29.955  19.217 51.760 1.000 34.526  ? 17  SER   BBB N   1 ? 
ATOM   2126 C  CA  . SER   B 1 18  ? 31.346  18.696 51.970 1.000 36.533  ? 17  SER   BBB CA  1 ? 
ATOM   2127 C  C   . SER   B 1 18  ? 32.041  18.133 50.683 1.000 41.576  ? 17  SER   BBB C   1 ? 
ATOM   2128 O  O   . SER   B 1 18  ? 33.516  18.435 50.691 1.000 47.287  ? 17  SER   BBB O   1 ? 
ATOM   2129 C  CB  . SER   B 1 18  ? 31.325  17.717 53.093 1.000 36.640  ? 17  SER   BBB CB  1 ? 
ATOM   2130 O  OG  . SER   B 1 18  ? 30.562  16.597 52.686 1.000 36.947  ? 17  SER   BBB OG  1 ? 
ATOM   2131 N  N   . LYS   B 1 19  ? 31.165  17.978 49.590 1.000 37.687  ? 18  LYS   BBB N   1 ? 
ATOM   2132 C  CA  . LYS   B 1 19  ? 31.650  17.418 48.292 1.000 33.347  ? 18  LYS   BBB CA  1 ? 
ATOM   2133 C  C   . LYS   B 1 19  ? 32.435  18.535 47.580 1.000 38.816  ? 18  LYS   BBB C   1 ? 
ATOM   2134 O  O   . LYS   B 1 19  ? 33.550  18.275 47.123 1.000 38.241  ? 18  LYS   BBB O   1 ? 
ATOM   2135 C  CB  . LYS   B 1 19  ? 30.499  16.862 47.447 1.000 33.506  ? 18  LYS   BBB CB  1 ? 
ATOM   2136 C  CG  . LYS   B 1 19  ? 29.728  15.712 48.089 1.000 39.752  ? 18  LYS   BBB CG  1 ? 
ATOM   2137 C  CD  . LYS   B 1 19  ? 28.509  15.264 47.314 1.000 58.588  ? 18  LYS   BBB CD  1 ? 
ATOM   2138 C  CE  . LYS   B 1 19  ? 27.842  14.084 47.996 1.000 51.321  ? 18  LYS   BBB CE  1 ? 
ATOM   2139 N  NZ  . LYS   B 1 19  ? 26.892  13.386 47.100 1.000 54.575  ? 18  LYS   BBB NZ  1 ? 
ATOM   2140 N  N   . LEU   B 1 20  ? 31.918  19.767 47.580 1.000 38.044  ? 19  LEU   BBB N   1 ? 
ATOM   2141 C  CA  . LEU   B 1 20  ? 32.581  20.940 46.923 1.000 35.610  ? 19  LEU   BBB CA  1 ? 
ATOM   2142 C  C   . LEU   B 1 20  ? 33.448  21.718 47.928 1.000 35.838  ? 19  LEU   BBB C   1 ? 
ATOM   2143 O  O   . LEU   B 1 20  ? 34.472  22.320 47.500 1.000 40.797  ? 19  LEU   BBB O   1 ? 
ATOM   2144 C  CB  . LEU   B 1 20  ? 31.504  21.841 46.301 1.000 42.930  ? 19  LEU   BBB CB  1 ? 
ATOM   2145 C  CG  . LEU   B 1 20  ? 30.691  21.195 45.177 1.000 50.916  ? 19  LEU   BBB CG  1 ? 
ATOM   2146 C  CD1 . LEU   B 1 20  ? 29.654  22.143 44.605 1.000 54.497  ? 19  LEU   BBB CD1 1 ? 
ATOM   2147 C  CD2 . LEU   B 1 20  ? 31.599  20.690 44.065 1.000 54.933  ? 19  LEU   BBB CD2 1 ? 
ATOM   2148 N  N   . TYR   B 1 21  ? 33.108  21.662 49.211 1.000 38.089  ? 20  TYR   BBB N   1 ? 
ATOM   2149 C  CA  . TYR   B 1 21  ? 33.772  22.439 50.286 1.000 31.041  ? 20  TYR   BBB CA  1 ? 
ATOM   2150 C  C   . TYR   B 1 21  ? 34.128  21.498 51.422 1.000 38.527  ? 20  TYR   BBB C   1 ? 
ATOM   2151 O  O   . TYR   B 1 21  ? 33.424  21.427 52.408 1.000 33.982  ? 20  TYR   BBB O   1 ? 
ATOM   2152 C  CB  . TYR   B 1 21  ? 32.867  23.599 50.747 1.000 31.227  ? 20  TYR   BBB CB  1 ? 
ATOM   2153 C  CG  . TYR   B 1 21  ? 32.452  24.535 49.627 1.000 30.397  ? 20  TYR   BBB CG  1 ? 
ATOM   2154 C  CD1 . TYR   B 1 21  ? 33.265  25.569 49.215 1.000 33.553  ? 20  TYR   BBB CD1 1 ? 
ATOM   2155 C  CD2 . TYR   B 1 21  ? 31.241  24.394 48.973 1.000 32.798  ? 20  TYR   BBB CD2 1 ? 
ATOM   2156 C  CE1 . TYR   B 1 21  ? 32.904  26.398 48.154 1.000 34.507  ? 20  TYR   BBB CE1 1 ? 
ATOM   2157 C  CE2 . TYR   B 1 21  ? 30.883  25.138 47.869 1.000 36.647  ? 20  TYR   BBB CE2 1 ? 
ATOM   2158 C  CZ  . TYR   B 1 21  ? 31.699  26.196 47.497 1.000 36.271  ? 20  TYR   BBB CZ  1 ? 
ATOM   2159 O  OH  . TYR   B 1 21  ? 31.321  26.992 46.454 1.000 40.554  ? 20  TYR   BBB OH  1 ? 
ATOM   2160 N  N   . PRO   B 1 22  ? 35.199  20.686 51.270 1.000 30.720  ? 21  PRO   BBB N   1 ? 
ATOM   2161 C  CA  . PRO   B 1 22  ? 35.557  19.690 52.286 1.000 31.045  ? 21  PRO   BBB CA  1 ? 
ATOM   2162 C  C   . PRO   B 1 22  ? 35.747  20.246 53.701 1.000 28.715  ? 21  PRO   BBB C   1 ? 
ATOM   2163 O  O   . PRO   B 1 22  ? 35.539  19.502 54.616 1.000 30.718  ? 21  PRO   BBB O   1 ? 
ATOM   2164 C  CB  . PRO   B 1 22  ? 36.882  19.150 51.745 1.000 35.246  ? 21  PRO   BBB CB  1 ? 
ATOM   2165 C  CG  . PRO   B 1 22  ? 36.707  19.270 50.241 1.000 34.811  ? 21  PRO   BBB CG  1 ? 
ATOM   2166 C  CD  . PRO   B 1 22  ? 36.109  20.660 50.115 1.000 32.592  ? 21  PRO   BBB CD  1 ? 
ATOM   2167 N  N   . ILE   B 1 23  ? 36.033  21.561 53.841 1.000 32.199  ? 22  ILE   BBB N   1 ? 
ATOM   2168 C  CA  . ILE   B 1 23  ? 36.151  22.233 55.183 1.000 29.419  ? 22  ILE   BBB CA  1 ? 
ATOM   2169 C  C   . ILE   B 1 23  ? 34.836  22.111 55.979 1.000 38.710  ? 22  ILE   BBB C   1 ? 
ATOM   2170 O  O   . ILE   B 1 23  ? 34.865  22.331 57.168 1.000 35.123  ? 22  ILE   BBB O   1 ? 
ATOM   2171 C  CB  . ILE   B 1 23  ? 36.626  23.696 55.066 1.000 28.282  ? 22  ILE   BBB CB  1 ? 
ATOM   2172 C  CG1 . ILE   B 1 23  ? 37.113  24.254 56.407 1.000 31.392  ? 22  ILE   BBB CG1 1 ? 
ATOM   2173 C  CG2 . ILE   B 1 23  ? 35.549  24.553 54.432 1.000 32.659  ? 22  ILE   BBB CG2 1 ? 
ATOM   2174 C  CD1 . ILE   B 1 23  ? 38.237  23.455 57.014 1.000 37.015  ? 22  ILE   BBB CD1 1 ? 
ATOM   2175 N  N   . ALA   B 1 24  ? 33.721  21.777 55.343 1.000 39.395  ? 23  ALA   BBB N   1 ? 
ATOM   2176 C  CA  . ALA   B 1 24  ? 32.402  21.604 55.984 1.000 32.198  ? 23  ALA   BBB CA  1 ? 
ATOM   2177 C  C   . ALA   B 1 24  ? 32.496  20.619 57.143 1.000 30.628  ? 23  ALA   BBB C   1 ? 
ATOM   2178 O  O   . ALA   B 1 24  ? 31.655  20.731 58.074 1.000 33.834  ? 23  ALA   BBB O   1 ? 
ATOM   2179 C  CB  . ALA   B 1 24  ? 31.354  21.170 54.990 1.000 33.426  ? 23  ALA   BBB CB  1 ? 
ATOM   2180 N  N   . ASN   B 1 25  ? 33.391  19.621 57.025 1.000 30.617  ? 24  ASN   BBB N   1 ? 
ATOM   2181 C  CA  . ASN   B 1 25  ? 33.583  18.641 58.098 1.000 29.978  ? 24  ASN   BBB CA  1 ? 
ATOM   2182 C  C   . ASN   B 1 25  ? 34.747  19.052 59.001 1.000 32.123  ? 24  ASN   BBB C   1 ? 
ATOM   2183 O  O   . ASN   B 1 25  ? 35.214  18.203 59.748 1.000 31.299  ? 24  ASN   BBB O   1 ? 
ATOM   2184 C  CB  . ASN   B 1 25  ? 33.770  17.213 57.532 1.000 34.299  ? 24  ASN   BBB CB  1 ? 
ATOM   2185 C  CG  . ASN   B 1 25  ? 32.619  16.654 56.702 1.000 38.662  ? 24  ASN   BBB CG  1 ? 
ATOM   2186 O  OD1 . ASN   B 1 25  ? 32.924  16.199 55.504 1.000 56.224  ? 24  ASN   BBB OD1 1 ? 
ATOM   2187 N  ND2 . ASN   B 1 25  ? 31.329  16.854 57.299 1.000 48.256  ? 24  ASN   BBB ND2 1 ? 
ATOM   2188 N  N   . GLY   B 1 26  ? 35.155  20.327 59.049 1.000 30.994  ? 25  GLY   BBB N   1 ? 
ATOM   2189 C  CA  . GLY   B 1 26  ? 36.320  20.744 59.848 1.000 30.301  ? 25  GLY   BBB CA  1 ? 
ATOM   2190 C  C   . GLY   B 1 26  ? 36.047  20.837 61.337 1.000 28.405  ? 25  GLY   BBB C   1 ? 
ATOM   2191 O  O   . GLY   B 1 26  ? 34.924  20.553 61.776 1.000 30.699  ? 25  GLY   BBB O   1 ? 
ATOM   2192 N  N   . ASN   B 1 27  ? 37.057  21.274 62.088 1.000 29.079  ? 26  ASN   BBB N   1 ? 
ATOM   2193 C  CA  . ASN   B 1 27  ? 37.084  21.296 63.568 1.000 31.654  ? 26  ASN   BBB CA  1 ? 
ATOM   2194 C  C   . ASN   B 1 27  ? 36.593  22.642 64.147 1.000 32.534  ? 26  ASN   BBB C   1 ? 
ATOM   2195 O  O   . ASN   B 1 27  ? 36.450  22.736 65.387 1.000 32.770  ? 26  ASN   BBB O   1 ? 
ATOM   2196 C  CB  . ASN   B 1 27  ? 38.501  20.980 64.030 1.000 32.258  ? 26  ASN   BBB CB  1 ? 
ATOM   2197 C  CG  . ASN   B 1 27  ? 38.878  19.554 63.698 1.000 43.295  ? 26  ASN   BBB CG  1 ? 
ATOM   2198 O  OD1 . ASN   B 1 27  ? 38.034  18.660 63.754 1.000 41.584  ? 26  ASN   BBB OD1 1 ? 
ATOM   2199 N  ND2 . ASN   B 1 27  ? 40.120  19.342 63.292 1.000 50.239  ? 26  ASN   BBB ND2 1 ? 
ATOM   2200 N  N   . ASN   B 1 28  ? 36.304  23.639 63.310 1.000 28.881  ? 27  ASN   BBB N   1 ? 
ATOM   2201 C  CA  . ASN   B 1 28  ? 35.873  24.991 63.777 1.000 27.800  ? 27  ASN   BBB CA  1 ? 
ATOM   2202 C  C   . ASN   B 1 28  ? 34.650  25.410 62.988 1.000 29.088  ? 27  ASN   BBB C   1 ? 
ATOM   2203 O  O   . ASN   B 1 28  ? 34.575  26.639 62.602 1.000 27.787  ? 27  ASN   BBB O   1 ? 
ATOM   2204 C  CB  . ASN   B 1 28  ? 36.966  26.047 63.659 1.000 30.180  ? 27  ASN   BBB CB  1 ? 
ATOM   2205 C  CG  . ASN   B 1 28  ? 38.110  25.779 64.605 1.000 33.399  ? 27  ASN   BBB CG  1 ? 
ATOM   2206 O  OD1 . ASN   B 1 28  ? 39.094  25.163 64.222 1.000 39.150  ? 27  ASN   BBB OD1 1 ? 
ATOM   2207 N  ND2 . ASN   B 1 28  ? 37.979  26.210 65.842 1.000 41.325  ? 27  ASN   BBB ND2 1 ? 
ATOM   2208 N  N   . GLN   B 1 29  ? 33.645  24.562 62.838 1.000 31.196  ? 28  GLN   BBB N   1 ? 
ATOM   2209 C  CA  . GLN   B 1 29  ? 32.481  24.878 61.976 1.000 25.075  ? 28  GLN   BBB CA  1 ? 
ATOM   2210 C  C   . GLN   B 1 29  ? 31.358  25.530 62.790 1.000 25.219  ? 28  GLN   BBB C   1 ? 
ATOM   2211 O  O   . GLN   B 1 29  ? 31.267  25.314 64.014 1.000 30.857  ? 28  GLN   BBB O   1 ? 
ATOM   2212 C  CB  . GLN   B 1 29  ? 32.002  23.650 61.213 1.000 28.637  ? 28  GLN   BBB CB  1 ? 
ATOM   2213 C  CG  . GLN   B 1 29  ? 32.941  23.285 60.070 1.000 30.823  ? 28  GLN   BBB CG  1 ? 
ATOM   2214 C  CD  . GLN   B 1 29  ? 32.921  24.297 58.944 1.000 27.716  ? 28  GLN   BBB CD  1 ? 
ATOM   2215 O  OE1 . GLN   B 1 29  ? 31.940  24.403 58.209 1.000 27.072  ? 28  GLN   BBB OE1 1 ? 
ATOM   2216 N  NE2 . GLN   B 1 29  ? 34.073  24.893 58.698 1.000 36.291  ? 28  GLN   BBB NE2 1 ? 
ATOM   2217 N  N   . SER   B 1 30  ? 30.628  26.464 62.133 1.000 24.453  ? 29  SER   BBB N   1 ? 
ATOM   2218 C  CA  . SER   B 1 30  ? 29.452  27.105 62.724 1.000 27.996  ? 29  SER   BBB CA  1 ? 
ATOM   2219 C  C   . SER   B 1 30  ? 28.198  26.857 61.906 1.000 31.559  ? 29  SER   BBB C   1 ? 
ATOM   2220 O  O   . SER   B 1 30  ? 28.268  26.659 60.711 1.000 31.637  ? 29  SER   BBB O   1 ? 
ATOM   2221 C  CB  . SER   B 1 30  ? 29.720  28.661 62.756 1.000 27.319  ? 29  SER   BBB CB  1 ? 
ATOM   2222 O  OG  . SER   B 1 30  ? 30.863  28.916 63.527 1.000 28.159  ? 29  SER   BBB OG  1 ? 
ATOM   2223 N  N   . PRO   B 1 31  ? 26.989  27.079 62.463 1.000 28.354  ? 30  PRO   BBB N   1 ? 
ATOM   2224 C  CA  . PRO   B 1 31  ? 26.806  27.506 63.853 1.000 24.794  ? 30  PRO   BBB CA  1 ? 
ATOM   2225 C  C   . PRO   B 1 31  ? 26.998  26.332 64.853 1.000 22.713  ? 30  PRO   BBB C   1 ? 
ATOM   2226 O  O   . PRO   B 1 31  ? 27.200  25.087 64.491 1.000 27.111  ? 30  PRO   BBB O   1 ? 
ATOM   2227 C  CB  . PRO   B 1 31  ? 25.333  27.988 63.796 1.000 22.430  ? 30  PRO   BBB CB  1 ? 
ATOM   2228 C  CG  . PRO   B 1 31  ? 24.685  26.963 62.840 1.000 29.070  ? 30  PRO   BBB CG  1 ? 
ATOM   2229 C  CD  . PRO   B 1 31  ? 25.709  26.913 61.758 1.000 28.818  ? 30  PRO   BBB CD  1 ? 
ATOM   2230 N  N   . VAL   B 1 32  ? 26.904  26.619 66.145 1.000 24.406  ? 31  VAL   BBB N   1 ? 
ATOM   2231 C  CA  . VAL   B 1 32  ? 26.995  25.604 67.235 1.000 25.812  ? 31  VAL   BBB CA  1 ? 
ATOM   2232 C  C   . VAL   B 1 32  ? 25.820  25.768 68.184 1.000 27.453  ? 31  VAL   BBB C   1 ? 
ATOM   2233 O  O   . VAL   B 1 32  ? 25.144  26.810 68.191 1.000 26.721  ? 31  VAL   BBB O   1 ? 
ATOM   2234 C  CB  . VAL   B 1 32  ? 28.317  25.677 68.003 1.000 26.555  ? 31  VAL   BBB CB  1 ? 
ATOM   2235 C  CG1 . VAL   B 1 32  ? 29.462  25.474 67.060 1.000 30.971  ? 31  VAL   BBB CG1 1 ? 
ATOM   2236 C  CG2 . VAL   B 1 32  ? 28.513  26.988 68.763 1.000 26.201  ? 31  VAL   BBB CG2 1 ? 
ATOM   2237 N  N   . ASP   B 1 33  ? 25.519  24.715 68.929 1.000 30.035  ? 32  ASP   BBB N   1 ? 
ATOM   2238 C  CA  . ASP   B 1 33  ? 24.674  24.832 70.150 1.000 29.311  ? 32  ASP   BBB CA  1 ? 
ATOM   2239 C  C   . ASP   B 1 33  ? 25.500  25.396 71.310 1.000 29.342  ? 32  ASP   BBB C   1 ? 
ATOM   2240 O  O   . ASP   B 1 33  ? 26.632  24.906 71.502 1.000 31.417  ? 32  ASP   BBB O   1 ? 
ATOM   2241 C  CB  . ASP   B 1 33  ? 24.098  23.493 70.613 1.000 28.359  ? 32  ASP   BBB CB  1 ? 
ATOM   2242 C  CG  . ASP   B 1 33  ? 23.171  23.610 71.824 1.000 31.567  ? 32  ASP   BBB CG  1 ? 
ATOM   2243 O  OD1 . ASP   B 1 33  ? 22.175  24.378 71.774 1.000 26.891  ? 32  ASP   BBB OD1 1 ? 
ATOM   2244 O  OD2 . ASP   B 1 33  ? 23.444  22.942 72.822 1.000 35.008  ? 32  ASP   BBB OD2 1 ? 
ATOM   2245 N  N   . ILE   B 1 34  ? 24.989  26.424 72.007 1.000 25.740  ? 33  ILE   BBB N   1 ? 
ATOM   2246 C  CA  . ILE   B 1 34  ? 25.607  26.895 73.265 1.000 24.041  ? 33  ILE   BBB CA  1 ? 
ATOM   2247 C  C   . ILE   B 1 34  ? 24.923  26.232 74.459 1.000 23.036  ? 33  ILE   BBB C   1 ? 
ATOM   2248 O  O   . ILE   B 1 34  ? 23.706  26.543 74.710 1.000 27.257  ? 33  ILE   BBB O   1 ? 
ATOM   2249 C  CB  . ILE   B 1 34  ? 25.521  28.425 73.339 1.000 24.488  ? 33  ILE   BBB CB  1 ? 
ATOM   2250 C  CG1 . ILE   B 1 34  ? 26.251  29.012 72.136 1.000 25.987  ? 33  ILE   BBB CG1 1 ? 
ATOM   2251 C  CG2 . ILE   B 1 34  ? 26.073  28.926 74.657 1.000 25.816  ? 33  ILE   BBB CG2 1 ? 
ATOM   2252 C  CD1 . ILE   B 1 34  ? 26.047  30.516 72.003 1.000 24.162  ? 33  ILE   BBB CD1 1 ? 
ATOM   2253 N  N   . LYS   B 1 35  ? 25.609  25.270 75.099 1.000 28.551  ? 34  LYS   BBB N   1 ? 
ATOM   2254 C  CA  . LYS   B 1 35  ? 25.120  24.677 76.375 1.000 29.818  ? 34  LYS   BBB CA  1 ? 
ATOM   2255 C  C   . LYS   B 1 35  ? 25.617  25.547 77.511 1.000 25.267  ? 34  LYS   BBB C   1 ? 
ATOM   2256 O  O   . LYS   B 1 35  ? 26.820  25.500 77.749 1.000 30.926  ? 34  LYS   BBB O   1 ? 
ATOM   2257 C  CB  . LYS   B 1 35  ? 25.602  23.246 76.615 1.000 36.033  ? 34  LYS   BBB CB  1 ? 
ATOM   2258 C  CG  . LYS   B 1 35  ? 25.264  22.303 75.505 1.000 46.776  ? 34  LYS   BBB CG  1 ? 
ATOM   2259 C  CD  . LYS   B 1 35  ? 25.932  20.939 75.697 1.000 65.033  ? 34  LYS   BBB CD  1 ? 
ATOM   2260 C  CE  . LYS   B 1 35  ? 26.047  20.182 74.390 1.000 65.830  ? 34  LYS   BBB CE  1 ? 
ATOM   2261 N  NZ  . LYS   B 1 35  ? 25.068  20.696 73.386 1.000 125.681 ? 34  LYS   BBB NZ  1 ? 
ATOM   2262 N  N   . THR   B 1 36  ? 24.711  26.253 78.192 1.000 30.864  ? 35  THR   BBB N   1 ? 
ATOM   2263 C  CA  . THR   B 1 36  ? 25.069  27.305 79.188 1.000 30.634  ? 35  THR   BBB CA  1 ? 
ATOM   2264 C  C   . THR   B 1 36  ? 25.689  26.651 80.421 1.000 32.168  ? 35  THR   BBB C   1 ? 
ATOM   2265 O  O   . THR   B 1 36  ? 26.432  27.323 81.092 1.000 40.622  ? 35  THR   BBB O   1 ? 
ATOM   2266 C  CB  . THR   B 1 36  ? 23.872  28.188 79.528 1.000 32.228  ? 35  THR   BBB CB  1 ? 
ATOM   2267 O  OG1 . THR   B 1 36  ? 22.783  27.435 80.048 1.000 30.934  ? 35  THR   BBB OG1 1 ? 
ATOM   2268 C  CG2 . THR   B 1 36  ? 23.364  28.892 78.304 1.000 27.163  ? 35  THR   BBB CG2 1 ? 
ATOM   2269 N  N   . SER   B 1 37  ? 25.421  25.369 80.705 1.000 36.506  ? 36  SER   BBB N   1 ? 
ATOM   2270 C  CA  . SER   B 1 37  ? 26.103  24.687 81.837 1.000 37.371  ? 36  SER   BBB CA  1 ? 
ATOM   2271 C  C   . SER   B 1 37  ? 27.604  24.510 81.541 1.000 37.591  ? 36  SER   BBB C   1 ? 
ATOM   2272 O  O   . SER   B 1 37  ? 28.375  24.322 82.503 1.000 45.981  ? 36  SER   BBB O   1 ? 
ATOM   2273 C  CB  . SER   B 1 37  ? 25.456  23.353 82.178 1.000 41.376  ? 36  SER   BBB CB  1 ? 
ATOM   2274 O  OG  . SER   B 1 37  ? 25.609  22.427 81.105 1.000 40.312  ? 36  SER   BBB OG  1 ? 
ATOM   2275 N  N   . GLU   B 1 38  ? 28.014  24.524 80.268 1.000 36.639  ? 37  GLU   BBB N   1 ? 
ATOM   2276 C  CA  . GLU   B 1 38  ? 29.428  24.217 79.876 1.000 40.648  ? 37  GLU   BBB CA  1 ? 
ATOM   2277 C  C   . GLU   B 1 38  ? 30.175  25.515 79.535 1.000 32.483  ? 37  GLU   BBB C   1 ? 
ATOM   2278 O  O   . GLU   B 1 38  ? 31.364  25.436 79.185 1.000 31.904  ? 37  GLU   BBB O   1 ? 
ATOM   2279 C  CB  . GLU   B 1 38  ? 29.500  23.233 78.699 1.000 38.660  ? 37  GLU   BBB CB  1 ? 
ATOM   2280 C  CG  . GLU   B 1 38  ? 28.712  21.905 78.890 1.000 51.876  ? 37  GLU   BBB CG  1 ? 
ATOM   2281 C  CD  . GLU   B 1 38  ? 28.951  21.028 80.115 1.000 57.730  ? 37  GLU   BBB CD  1 ? 
ATOM   2282 O  OE1 . GLU   B 1 38  ? 29.740  20.094 80.011 1.000 70.114  ? 37  GLU   BBB OE1 1 ? 
ATOM   2283 O  OE2 . GLU   B 1 38  ? 28.282  21.245 81.158 1.000 80.233  ? 37  GLU   BBB OE2 1 ? 
ATOM   2284 N  N   . THR   B 1 39  ? 29.496  26.673 79.542 1.000 26.985  ? 38  THR   BBB N   1 ? 
ATOM   2285 C  CA  . THR   B 1 39  ? 30.173  27.943 79.198 1.000 30.535  ? 38  THR   BBB CA  1 ? 
ATOM   2286 C  C   . THR   B 1 39  ? 31.112  28.292 80.347 1.000 32.272  ? 38  THR   BBB C   1 ? 
ATOM   2287 O  O   . THR   B 1 39  ? 30.769  28.000 81.510 1.000 34.618  ? 38  THR   BBB O   1 ? 
ATOM   2288 C  CB  . THR   B 1 39  ? 29.194  29.064 78.848 1.000 28.931  ? 38  THR   BBB CB  1 ? 
ATOM   2289 O  OG1 . THR   B 1 39  ? 28.375  29.274 79.990 1.000 31.760  ? 38  THR   BBB OG1 1 ? 
ATOM   2290 C  CG2 . THR   B 1 39  ? 28.382  28.776 77.607 1.000 33.148  ? 38  THR   BBB CG2 1 ? 
ATOM   2291 N  N   . LYS   B 1 40  ? 32.246  28.897 80.002 1.000 28.805  ? 39  LYS   BBB N   1 ? 
ATOM   2292 C  CA  . LYS   B 1 40  ? 33.290  29.320 80.957 1.000 34.782  ? 39  LYS   BBB CA  1 ? 
ATOM   2293 C  C   . LYS   B 1 40  ? 33.313  30.872 80.988 1.000 24.368  ? 39  LYS   BBB C   1 ? 
ATOM   2294 O  O   . LYS   B 1 40  ? 33.413  31.514 79.906 1.000 26.789  ? 39  LYS   BBB O   1 ? 
ATOM   2295 C  CB  . LYS   B 1 40  ? 34.639  28.715 80.525 1.000 38.571  ? 39  LYS   BBB CB  1 ? 
ATOM   2296 C  CG  . LYS   B 1 40  ? 34.738  27.193 80.493 1.000 36.784  ? 39  LYS   BBB CG  1 ? 
ATOM   2297 C  CD  . LYS   B 1 40  ? 34.471  26.528 81.789 1.000 37.944  ? 39  LYS   BBB CD  1 ? 
ATOM   2298 C  CE  . LYS   B 1 40  ? 34.419  25.019 81.635 1.000 46.646  ? 39  LYS   BBB CE  1 ? 
ATOM   2299 N  NZ  . LYS   B 1 40  ? 34.161  24.431 82.953 1.000 46.957  ? 39  LYS   BBB NZ  1 ? 
ATOM   2300 N  N   . HIS   B 1 41  ? 33.219  31.478 82.176 1.000 29.161  ? 40  HIS   BBB N   1 ? 
ATOM   2301 C  CA  . HIS   B 1 41  ? 33.456  32.941 82.293 1.000 27.075  ? 40  HIS   BBB CA  1 ? 
ATOM   2302 C  C   . HIS   B 1 41  ? 34.944  33.228 82.142 1.000 31.323  ? 40  HIS   BBB C   1 ? 
ATOM   2303 O  O   . HIS   B 1 41  ? 35.785  32.695 82.900 1.000 29.551  ? 40  HIS   BBB O   1 ? 
ATOM   2304 C  CB  . HIS   B 1 41  ? 32.911  33.554 83.578 1.000 31.967  ? 40  HIS   BBB CB  1 ? 
ATOM   2305 C  CG  . HIS   B 1 41  ? 33.112  35.029 83.621 1.000 33.732  ? 40  HIS   BBB CG  1 ? 
ATOM   2306 N  ND1 . HIS   B 1 41  ? 34.028  35.630 84.466 1.000 31.664  ? 40  HIS   BBB ND1 1 ? 
ATOM   2307 C  CD2 . HIS   B 1 41  ? 32.581  36.023 82.873 1.000 33.291  ? 40  HIS   BBB CD2 1 ? 
ATOM   2308 C  CE1 . HIS   B 1 41  ? 34.015  36.952 84.268 1.000 31.112  ? 40  HIS   BBB CE1 1 ? 
ATOM   2309 N  NE2 . HIS   B 1 41  ? 33.158  37.206 83.283 1.000 31.662  ? 40  HIS   BBB NE2 1 ? 
ATOM   2310 N  N   . ASP   B 1 42  ? 35.243  34.167 81.258 1.000 30.788  ? 41  ASP   BBB N   1 ? 
ATOM   2311 C  CA  . ASP   B 1 42  ? 36.634  34.591 80.971 1.000 24.878  ? 41  ASP   BBB CA  1 ? 
ATOM   2312 C  C   . ASP   B 1 42  ? 36.764  36.061 81.368 1.000 24.857  ? 41  ASP   BBB C   1 ? 
ATOM   2313 O  O   . ASP   B 1 42  ? 36.174  36.880 80.676 1.000 29.584  ? 41  ASP   BBB O   1 ? 
ATOM   2314 C  CB  . ASP   B 1 42  ? 36.979  34.365 79.509 1.000 29.146  ? 41  ASP   BBB CB  1 ? 
ATOM   2315 C  CG  . ASP   B 1 42  ? 38.365  34.830 79.094 1.000 29.428  ? 41  ASP   BBB CG  1 ? 
ATOM   2316 O  OD1 . ASP   B 1 42  ? 39.062  35.506 79.908 1.000 28.632  ? 41  ASP   BBB OD1 1 ? 
ATOM   2317 O  OD2 . ASP   B 1 42  ? 38.734  34.502 77.927 1.000 35.676  ? 41  ASP   BBB OD2 1 ? 
ATOM   2318 N  N   . THR   B 1 43  ? 37.526  36.345 82.413 1.000 24.295  ? 42  THR   BBB N   1 ? 
ATOM   2319 C  CA  . THR   B 1 43  ? 37.700  37.727 82.955 1.000 24.909  ? 42  THR   BBB CA  1 ? 
ATOM   2320 C  C   . THR   B 1 43  ? 38.409  38.636 81.971 1.000 24.620  ? 42  THR   BBB C   1 ? 
ATOM   2321 O  O   . THR   B 1 43  ? 38.311  39.910 82.209 1.000 26.819  ? 42  THR   BBB O   1 ? 
ATOM   2322 C  CB  . THR   B 1 43  ? 38.446  37.749 84.290 1.000 28.082  ? 42  THR   BBB CB  1 ? 
ATOM   2323 O  OG1 . THR   B 1 43  ? 39.817  37.385 84.118 1.000 28.247  ? 42  THR   BBB OG1 1 ? 
ATOM   2324 C  CG2 . THR   B 1 43  ? 37.768  36.869 85.321 1.000 29.469  ? 42  THR   BBB CG2 1 ? 
ATOM   2325 N  N   . SER   B 1 44  ? 39.054  38.105 80.928 1.000 26.612  ? 43  SER   BBB N   1 ? 
ATOM   2326 C  CA  . SER   B 1 44  ? 39.803  38.949 79.954 1.000 27.979  ? 43  SER   BBB CA  1 ? 
ATOM   2327 C  C   . SER   B 1 44  ? 38.842  39.540 78.936 1.000 29.651  ? 43  SER   BBB C   1 ? 
ATOM   2328 O  O   . SER   B 1 44  ? 39.305  40.374 78.158 1.000 34.340  ? 43  SER   BBB O   1 ? 
ATOM   2329 C  CB  . SER   B 1 44  ? 40.913  38.232 79.267 1.000 29.196  ? 43  SER   BBB CB  1 ? 
ATOM   2330 O  OG  . SER   B 1 44  ? 40.409  37.264 78.373 1.000 31.206  ? 43  SER   BBB OG  1 ? 
ATOM   2331 N  N   . LEU   B 1 45  ? 37.577  39.091 78.897 1.000 25.222  ? 44  LEU   BBB N   1 ? 
ATOM   2332 C  CA  . LEU   B 1 45  ? 36.611  39.569 77.860 1.000 24.380  ? 44  LEU   BBB CA  1 ? 
ATOM   2333 C  C   . LEU   B 1 45  ? 36.092  40.942 78.256 1.000 24.792  ? 44  LEU   BBB C   1 ? 
ATOM   2334 O  O   . LEU   B 1 45  ? 35.348  41.020 79.199 1.000 26.932  ? 44  LEU   BBB O   1 ? 
ATOM   2335 C  CB  . LEU   B 1 45  ? 35.412  38.646 77.680 1.000 23.260  ? 44  LEU   BBB CB  1 ? 
ATOM   2336 C  CG  . LEU   B 1 45  ? 35.718  37.314 77.019 1.000 24.087  ? 44  LEU   BBB CG  1 ? 
ATOM   2337 C  CD1 . LEU   B 1 45  ? 34.462  36.482 77.086 1.000 26.645  ? 44  LEU   BBB CD1 1 ? 
ATOM   2338 C  CD2 . LEU   B 1 45  ? 36.141  37.466 75.558 1.000 28.334  ? 44  LEU   BBB CD2 1 ? 
ATOM   2339 N  N   . LYS   B 1 46  ? 36.470  41.957 77.492 1.000 26.851  ? 45  LYS   BBB N   1 ? 
ATOM   2340 C  CA  . LYS   B 1 46  ? 35.976  43.341 77.699 1.000 23.560  ? 45  LYS   BBB CA  1 ? 
ATOM   2341 C  C   . LYS   B 1 46  ? 34.554  43.479 77.175 1.000 23.771  ? 45  LYS   BBB C   1 ? 
ATOM   2342 O  O   . LYS   B 1 46  ? 34.073  42.687 76.364 1.000 26.109  ? 45  LYS   BBB O   1 ? 
ATOM   2343 C  CB  . LYS   B 1 46  ? 36.882  44.320 76.951 1.000 26.137  ? 45  LYS   BBB CB  1 ? 
ATOM   2344 C  CG  . LYS   B 1 46  ? 38.208  44.619 77.598 1.000 27.432  ? 45  LYS   BBB CG  1 ? 
ATOM   2345 C  CD  . LYS   B 1 46  ? 38.848  45.899 77.041 1.000 29.834  ? 45  LYS   BBB CD  1 ? 
ATOM   2346 C  CE  . LYS   B 1 46  ? 40.242  46.082 77.598 1.000 40.069  ? 45  LYS   BBB CE  1 ? 
ATOM   2347 N  NZ  . LYS   B 1 46  ? 41.135  46.824 76.690 1.000 44.161  ? 45  LYS   BBB NZ  1 ? 
ATOM   2348 N  N   . PRO   B 1 47  ? 33.815  44.561 77.520 1.000 25.334  ? 46  PRO   BBB N   1 ? 
ATOM   2349 C  CA  . PRO   B 1 47  ? 32.533  44.817 76.884 1.000 23.133  ? 46  PRO   BBB CA  1 ? 
ATOM   2350 C  C   . PRO   B 1 47  ? 32.756  45.037 75.386 1.000 24.771  ? 46  PRO   BBB C   1 ? 
ATOM   2351 O  O   . PRO   B 1 47  ? 33.878  45.485 74.998 1.000 29.238  ? 46  PRO   BBB O   1 ? 
ATOM   2352 C  CB  . PRO   B 1 47  ? 32.023  46.104 77.536 1.000 27.557  ? 46  PRO   BBB CB  1 ? 
ATOM   2353 C  CG  . PRO   B 1 47  ? 32.806  46.225 78.806 1.000 31.574  ? 46  PRO   BBB CG  1 ? 
ATOM   2354 C  CD  . PRO   B 1 47  ? 34.142  45.560 78.540 1.000 27.069  ? 46  PRO   BBB CD  1 ? 
ATOM   2355 N  N   . ILE   B 1 48  ? 31.778  44.657 74.569 1.000 26.967  ? 47  ILE   BBB N   1 ? 
ATOM   2356 C  CA  . ILE   B 1 48  ? 31.877  45.003 73.122 1.000 25.344  ? 47  ILE   BBB CA  1 ? 
ATOM   2357 C  C   . ILE   B 1 48  ? 31.440  46.472 72.958 1.000 23.207  ? 47  ILE   BBB C   1 ? 
ATOM   2358 O  O   . ILE   B 1 48  ? 30.504  46.912 73.599 1.000 29.020  ? 47  ILE   BBB O   1 ? 
ATOM   2359 C  CB  . ILE   B 1 48  ? 31.198  44.043 72.145 1.000 32.398  ? 47  ILE   BBB CB  1 ? 
ATOM   2360 C  CG1 . ILE   B 1 48  ? 29.719  43.867 72.402 1.000 36.464  ? 47  ILE   BBB CG1 1 ? 
ATOM   2361 C  CG2 . ILE   B 1 48  ? 31.893  42.675 72.096 1.000 31.950  ? 47  ILE   BBB CG2 1 ? 
ATOM   2362 C  CD1 . ILE   B 1 48  ? 29.003  43.399 71.164 1.000 46.910  ? 47  ILE   BBB CD1 1 ? 
ATOM   2363 N  N   . SER   B 1 49  ? 32.104  47.165 72.061 1.000 25.735  ? 48  SER   BBB N   1 ? 
ATOM   2364 C  CA  . SER   B 1 49  ? 31.867  48.592 71.718 1.000 26.642  ? 48  SER   BBB CA  1 ? 
ATOM   2365 C  C   . SER   B 1 49  ? 31.565  48.646 70.214 1.000 22.469  ? 48  SER   BBB C   1 ? 
ATOM   2366 O  O   . SER   B 1 49  ? 32.430  48.197 69.398 1.000 26.327  ? 48  SER   BBB O   1 ? 
ATOM   2367 C  CB  . SER   B 1 49  ? 33.047  49.390 72.150 1.000 35.482  ? 48  SER   BBB CB  1 ? 
ATOM   2368 O  OG  . SER   B 1 49  ? 33.134  50.570 71.398 1.000 41.079  ? 48  SER   BBB OG  1 ? 
ATOM   2369 N  N   . VAL   B 1 50  ? 30.339  49.006 69.832 1.000 22.516  ? 49  VAL   BBB N   1 ? 
ATOM   2370 C  CA  . VAL   B 1 50  ? 30.042  49.223 68.394 1.000 23.460  ? 49  VAL   BBB CA  1 ? 
ATOM   2371 C  C   . VAL   B 1 50  ? 29.812  50.729 68.192 1.000 25.120  ? 49  VAL   BBB C   1 ? 
ATOM   2372 O  O   . VAL   B 1 50  ? 29.135  51.348 69.019 1.000 28.663  ? 49  VAL   BBB O   1 ? 
ATOM   2373 C  CB  . VAL   B 1 50  ? 28.898  48.385 67.814 1.000 28.183  ? 49  VAL   BBB CB  1 ? 
ATOM   2374 C  CG1 . VAL   B 1 50  ? 29.240  46.917 68.016 1.000 32.046  ? 49  VAL   BBB CG1 1 ? 
ATOM   2375 C  CG2 . VAL   B 1 50  ? 27.543  48.669 68.404 1.000 34.482  ? 49  VAL   BBB CG2 1 ? 
ATOM   2376 N  N   . SER   B 1 51  ? 30.353  51.230 67.099 1.000 27.574  ? 50  SER   BBB N   1 ? 
ATOM   2377 C  CA  . SER   B 1 51  ? 30.112  52.637 66.691 1.000 31.971  ? 50  SER   BBB CA  1 ? 
ATOM   2378 C  C   . SER   B 1 51  ? 30.035  52.669 65.176 1.000 45.291  ? 50  SER   BBB C   1 ? 
ATOM   2379 O  O   . SER   B 1 51  ? 31.049  52.626 64.546 1.000 40.970  ? 50  SER   BBB O   1 ? 
ATOM   2380 C  CB  . SER   B 1 51  ? 31.124  53.577 67.228 1.000 32.612  ? 50  SER   BBB CB  1 ? 
ATOM   2381 O  OG  . SER   B 1 51  ? 30.644  54.890 66.963 1.000 38.949  ? 50  SER   BBB OG  1 ? 
ATOM   2382 N  N   . TYR   B 1 52  ? 28.827  52.699 64.670 1.000 43.242  ? 51  TYR   BBB N   1 ? 
ATOM   2383 C  CA  . TYR   B 1 52  ? 28.537  52.685 63.233 1.000 30.780  ? 51  TYR   BBB CA  1 ? 
ATOM   2384 C  C   . TYR   B 1 52  ? 28.063  54.083 62.792 1.000 33.843  ? 51  TYR   BBB C   1 ? 
ATOM   2385 O  O   . TYR   B 1 52  ? 27.212  54.689 63.455 1.000 32.499  ? 51  TYR   BBB O   1 ? 
ATOM   2386 C  CB  . TYR   B 1 52  ? 27.538  51.584 62.909 1.000 25.954  ? 51  TYR   BBB CB  1 ? 
ATOM   2387 C  CG  . TYR   B 1 52  ? 27.917  50.184 63.364 1.000 25.220  ? 51  TYR   BBB CG  1 ? 
ATOM   2388 C  CD1 . TYR   B 1 52  ? 29.216  49.726 63.462 1.000 22.020  ? 51  TYR   BBB CD1 1 ? 
ATOM   2389 C  CD2 . TYR   B 1 52  ? 26.899  49.305 63.667 1.000 24.784  ? 51  TYR   BBB CD2 1 ? 
ATOM   2390 C  CE1 . TYR   B 1 52  ? 29.480  48.405 63.875 1.000 23.182  ? 51  TYR   BBB CE1 1 ? 
ATOM   2391 C  CE2 . TYR   B 1 52  ? 27.130  47.955 63.987 1.000 22.194  ? 51  TYR   BBB CE2 1 ? 
ATOM   2392 C  CZ  . TYR   B 1 52  ? 28.419  47.556 64.178 1.000 19.945  ? 51  TYR   BBB CZ  1 ? 
ATOM   2393 O  OH  . TYR   B 1 52  ? 28.493  46.206 64.488 1.000 22.834  ? 51  TYR   BBB OH  1 ? 
ATOM   2394 N  N   . ASN   B 1 53  ? 28.547  54.464 61.623 1.000 35.613  ? 52  ASN   BBB N   1 ? 
ATOM   2395 C  CA  . ASN   B 1 53  ? 28.254  55.765 60.980 1.000 31.917  ? 52  ASN   BBB CA  1 ? 
ATOM   2396 C  C   . ASN   B 1 53  ? 27.173  55.427 59.966 1.000 30.106  ? 52  ASN   BBB C   1 ? 
ATOM   2397 O  O   . ASN   B 1 53  ? 27.432  54.632 59.064 1.000 31.228  ? 52  ASN   BBB O   1 ? 
ATOM   2398 C  CB  . ASN   B 1 53  ? 29.519  56.291 60.348 1.000 33.242  ? 52  ASN   BBB CB  1 ? 
ATOM   2399 C  CG  . ASN   B 1 53  ? 29.263  57.704 59.848 1.000 39.474  ? 52  ASN   BBB CG  1 ? 
ATOM   2400 O  OD1 . ASN   B 1 53  ? 28.131  57.989 59.451 1.000 44.423  ? 52  ASN   BBB OD1 1 ? 
ATOM   2401 N  ND2 . ASN   B 1 53  ? 30.330  58.475 59.817 1.000 37.575  ? 52  ASN   BBB ND2 1 ? 
ATOM   2402 N  N   . PRO   B 1 54  ? 25.930  55.931 60.134 1.000 29.115  ? 53  PRO   BBB N   1 ? 
ATOM   2403 C  CA  . PRO   B 1 54  ? 24.851  55.592 59.198 1.000 30.124  ? 53  PRO   BBB CA  1 ? 
ATOM   2404 C  C   . PRO   B 1 54  ? 25.168  55.946 57.734 1.000 27.681  ? 53  PRO   BBB C   1 ? 
ATOM   2405 O  O   . PRO   B 1 54  ? 24.548  55.388 56.874 1.000 33.620  ? 53  PRO   BBB O   1 ? 
ATOM   2406 C  CB  . PRO   B 1 54  ? 23.647  56.394 59.705 1.000 31.732  ? 53  PRO   BBB CB  1 ? 
ATOM   2407 C  CG  . PRO   B 1 54  ? 24.310  57.576 60.434 1.000 32.014  ? 53  PRO   BBB CG  1 ? 
ATOM   2408 C  CD  . PRO   B 1 54  ? 25.528  56.976 61.109 1.000 33.836  ? 53  PRO   BBB CD  1 ? 
ATOM   2409 N  N   . ALA   B 1 55  ? 26.065  56.906 57.483 1.000 29.233  ? 54  ALA   BBB N   1 ? 
ATOM   2410 C  CA  . ALA   B 1 55  ? 26.436  57.317 56.107 1.000 27.895  ? 54  ALA   BBB CA  1 ? 
ATOM   2411 C  C   . ALA   B 1 55  ? 27.319  56.260 55.415 1.000 27.192  ? 54  ALA   BBB C   1 ? 
ATOM   2412 O  O   . ALA   B 1 55  ? 27.642  56.387 54.219 1.000 28.727  ? 54  ALA   BBB O   1 ? 
ATOM   2413 C  CB  . ALA   B 1 55  ? 27.116  58.680 56.126 1.000 34.470  ? 54  ALA   BBB CB  1 ? 
ATOM   2414 N  N   . THR   B 1 56  ? 27.667  55.174 56.132 1.000 29.569  ? 55  THR   BBB N   1 ? 
ATOM   2415 C  CA  . THR   B 1 56  ? 28.369  54.028 55.489 1.000 26.437  ? 55  THR   BBB CA  1 ? 
ATOM   2416 C  C   . THR   B 1 56  ? 27.386  53.045 54.859 1.000 21.973  ? 55  THR   BBB C   1 ? 
ATOM   2417 O  O   . THR   B 1 56  ? 27.892  52.190 54.050 1.000 24.218  ? 55  THR   BBB O   1 ? 
ATOM   2418 C  CB  . THR   B 1 56  ? 29.334  53.322 56.455 1.000 26.206  ? 55  THR   BBB CB  1 ? 
ATOM   2419 O  OG1 . THR   B 1 56  ? 28.614  52.880 57.619 1.000 23.813  ? 55  THR   BBB OG1 1 ? 
ATOM   2420 C  CG2 . THR   B 1 56  ? 30.535  54.198 56.799 1.000 27.919  ? 55  THR   BBB CG2 1 ? 
ATOM   2421 N  N   . ALA   B 1 57  ? 26.105  53.096 55.189 1.000 28.447  ? 56  ALA   BBB N   1 ? 
ATOM   2422 C  CA  . ALA   B 1 57  ? 25.112  52.255 54.492 1.000 25.669  ? 56  ALA   BBB CA  1 ? 
ATOM   2423 C  C   . ALA   B 1 57  ? 25.207  52.452 52.971 1.000 25.043  ? 56  ALA   BBB C   1 ? 
ATOM   2424 O  O   . ALA   B 1 57  ? 25.255  53.599 52.470 1.000 24.388  ? 56  ALA   BBB O   1 ? 
ATOM   2425 C  CB  . ALA   B 1 57  ? 23.764  52.498 55.050 1.000 26.848  ? 56  ALA   BBB CB  1 ? 
ATOM   2426 N  N   . LYS   B 1 58  ? 25.290  51.366 52.185 1.000 22.630  ? 57  LYS   BBB N   1 ? 
ATOM   2427 C  CA  . LYS   B 1 58  ? 25.509  51.511 50.714 1.000 23.395  ? 57  LYS   BBB CA  1 ? 
ATOM   2428 C  C   . LYS   B 1 58  ? 24.411  50.858 49.858 1.000 23.809  ? 57  LYS   BBB C   1 ? 
ATOM   2429 O  O   . LYS   B 1 58  ? 23.901  51.526 48.955 1.000 23.952  ? 57  LYS   BBB O   1 ? 
ATOM   2430 C  CB  . LYS   B 1 58  ? 26.932  51.070 50.373 1.000 27.824  ? 57  LYS   BBB CB  1 ? 
ATOM   2431 C  CG  . LYS   B 1 58  ? 27.408  51.261 48.940 1.000 33.381  ? 57  LYS   BBB CG  1 ? 
ATOM   2432 C  CD  . LYS   B 1 58  ? 28.623  50.358 48.669 1.000 44.014  ? 57  LYS   BBB CD  1 ? 
ATOM   2433 C  CE  . LYS   B 1 58  ? 28.739  49.923 47.228 1.000 53.743  ? 57  LYS   BBB CE  1 ? 
ATOM   2434 N  NZ  . LYS   B 1 58  ? 29.535  50.890 46.440 1.000 75.195  ? 57  LYS   BBB NZ  1 ? 
ATOM   2435 N  N   . GLU   B 1 59  ? 24.185  49.517 49.989 1.000 23.333  ? 58  GLU   BBB N   1 ? 
ATOM   2436 C  CA  . GLU   B 1 59  ? 23.454  48.766 48.940 1.000 24.214  ? 58  GLU   BBB CA  1 ? 
ATOM   2437 C  C   . GLU   B 1 59  ? 22.771  47.553 49.569 1.000 22.513  ? 58  GLU   BBB C   1 ? 
ATOM   2438 O  O   . GLU   B 1 59  ? 23.261  47.054 50.584 1.000 24.522  ? 58  GLU   BBB O   1 ? 
ATOM   2439 C  CB  . GLU   B 1 59  ? 24.467  48.373 47.874 1.000 26.036  ? 58  GLU   BBB CB  1 ? 
ATOM   2440 C  CG  . GLU   B 1 59  ? 23.886  47.706 46.675 1.000 34.641  ? 58  GLU   BBB CG  1 ? 
ATOM   2441 C  CD  . GLU   B 1 59  ? 24.913  47.557 45.569 1.000 34.672  ? 58  GLU   BBB CD  1 ? 
ATOM   2442 O  OE1 . GLU   B 1 59  ? 26.031  47.024 45.835 1.000 33.780  ? 58  GLU   BBB OE1 1 ? 
ATOM   2443 O  OE2 . GLU   B 1 59  ? 24.608  48.015 44.470 1.000 41.035  ? 58  GLU   BBB OE2 1 ? 
ATOM   2444 N  N   . ILE   B 1 60  ? 21.623  47.180 49.035 1.000 20.788  ? 59  ILE   BBB N   1 ? 
ATOM   2445 C  CA  . ILE   B 1 60  ? 20.913  45.943 49.432 1.000 20.195  ? 59  ILE   BBB CA  1 ? 
ATOM   2446 C  C   . ILE   B 1 60  ? 20.840  45.069 48.176 1.000 23.200  ? 59  ILE   BBB C   1 ? 
ATOM   2447 O  O   . ILE   B 1 60  ? 20.612  45.583 47.069 1.000 23.393  ? 59  ILE   BBB O   1 ? 
ATOM   2448 C  CB  . ILE   B 1 60  ? 19.549  46.246 50.071 1.000 24.068  ? 59  ILE   BBB CB  1 ? 
ATOM   2449 C  CG1 . ILE   B 1 60  ? 18.886  45.003 50.646 1.000 24.925  ? 59  ILE   BBB CG1 1 ? 
ATOM   2450 C  CG2 . ILE   B 1 60  ? 18.623  47.024 49.123 1.000 22.781  ? 59  ILE   BBB CG2 1 ? 
ATOM   2451 C  CD1 . ILE   B 1 60  ? 17.603  45.244 51.358 1.000 25.337  ? 59  ILE   BBB CD1 1 ? 
ATOM   2452 N  N   . ILE   B 1 61  ? 21.098  43.758 48.333 1.000 22.322  ? 60  ILE   BBB N   1 ? 
ATOM   2453 C  CA  . ILE   B 1 61  ? 21.383  42.892 47.160 1.000 21.013  ? 60  ILE   BBB CA  1 ? 
ATOM   2454 C  C   . ILE   B 1 61  ? 20.690  41.553 47.427 1.000 21.089  ? 60  ILE   BBB C   1 ? 
ATOM   2455 O  O   . ILE   B 1 61  ? 20.789  41.106 48.548 1.000 21.849  ? 60  ILE   BBB O   1 ? 
ATOM   2456 C  CB  . ILE   B 1 61  ? 22.878  42.612 46.881 1.000 28.637  ? 60  ILE   BBB CB  1 ? 
ATOM   2457 C  CG1 . ILE   B 1 61  ? 23.763  43.835 46.818 1.000 38.474  ? 60  ILE   BBB CG1 1 ? 
ATOM   2458 C  CG2 . ILE   B 1 61  ? 22.978  41.822 45.563 1.000 30.736  ? 60  ILE   BBB CG2 1 ? 
ATOM   2459 C  CD1 . ILE   B 1 61  ? 25.211  43.509 46.567 1.000 50.774  ? 60  ILE   BBB CD1 1 ? 
ATOM   2460 N  N   . ASN   B 1 62  ? 19.957  41.046 46.454 1.000 21.915  ? 61  ASN   BBB N   1 ? 
ATOM   2461 C  CA  . ASN   B 1 62  ? 19.421  39.656 46.486 1.000 21.542  ? 61  ASN   BBB CA  1 ? 
ATOM   2462 C  C   . ASN   B 1 62  ? 20.518  38.733 45.970 1.000 23.893  ? 61  ASN   BBB C   1 ? 
ATOM   2463 O  O   . ASN   B 1 62  ? 20.886  38.853 44.766 1.000 22.496  ? 61  ASN   BBB O   1 ? 
ATOM   2464 C  CB  . ASN   B 1 62  ? 18.139  39.552 45.678 1.000 24.205  ? 61  ASN   BBB CB  1 ? 
ATOM   2465 C  CG  . ASN   B 1 62  ? 17.459  38.198 45.689 1.000 21.997  ? 61  ASN   BBB CG  1 ? 
ATOM   2466 O  OD1 . ASN   B 1 62  ? 18.156  37.174 45.705 1.000 25.482  ? 61  ASN   BBB OD1 1 ? 
ATOM   2467 N  ND2 . ASN   B 1 62  ? 16.137  38.212 45.577 1.000 22.408  ? 61  ASN   BBB ND2 1 ? 
ATOM   2468 N  N   . VAL   B 1 63  ? 21.023  37.861 46.855 1.000 24.388  ? 62  VAL   BBB N   1 ? 
ATOM   2469 C  CA  . VAL   B 1 63  ? 22.143  36.926 46.511 1.000 23.196  ? 62  VAL   BBB CA  1 ? 
ATOM   2470 C  C   . VAL   B 1 63  ? 21.580  35.527 46.300 1.000 23.079  ? 62  VAL   BBB C   1 ? 
ATOM   2471 O  O   . VAL   B 1 63  ? 22.389  34.569 46.348 1.000 26.851  ? 62  VAL   BBB O   1 ? 
ATOM   2472 C  CB  . VAL   B 1 63  ? 23.278  36.915 47.533 1.000 24.416  ? 62  VAL   BBB CB  1 ? 
ATOM   2473 C  CG1 . VAL   B 1 63  ? 23.873  38.319 47.659 1.000 26.000  ? 62  VAL   BBB CG1 1 ? 
ATOM   2474 C  CG2 . VAL   B 1 63  ? 22.832  36.422 48.894 1.000 24.270  ? 62  VAL   BBB CG2 1 ? 
ATOM   2475 N  N   . GLY   B 1 64  ? 20.286  35.393 46.043 1.000 22.558  ? 63  GLY   BBB N   1 ? 
ATOM   2476 C  CA  . GLY   B 1 64  ? 19.782  34.068 45.599 1.000 26.484  ? 63  GLY   BBB CA  1 ? 
ATOM   2477 C  C   . GLY   B 1 64  ? 19.309  33.249 46.767 1.000 21.916  ? 63  GLY   BBB C   1 ? 
ATOM   2478 O  O   . GLY   B 1 64  ? 18.110  32.904 46.766 1.000 28.266  ? 63  GLY   BBB O   1 ? 
ATOM   2479 N  N   . HIS   B 1 65  ? 20.182  32.984 47.743 1.000 22.791  ? 64  HIS   BBB N   1 ? 
ATOM   2480 C  CA  . HIS   B 1 65  ? 19.866  32.235 48.989 1.000 24.376  ? 64  HIS   BBB CA  1 ? 
ATOM   2481 C  C   . HIS   B 1 65  ? 19.493  33.182 50.126 1.000 22.357  ? 64  HIS   BBB C   1 ? 
ATOM   2482 O  O   . HIS   B 1 65  ? 19.017  32.715 51.167 1.000 23.050  ? 64  HIS   BBB O   1 ? 
ATOM   2483 C  CB  . HIS   B 1 65  ? 21.086  31.416 49.381 1.000 25.459  ? 64  HIS   BBB CB  1 ? 
ATOM   2484 C  CG  . HIS   B 1 65  ? 22.275  32.220 49.836 1.000 23.631  ? 64  HIS   BBB CG  1 ? 
ATOM   2485 N  ND1 . HIS   B 1 65  ? 23.287  32.609 48.990 1.000 28.605  ? 64  HIS   BBB ND1 1 ? 
ATOM   2486 C  CD2 . HIS   B 1 65  ? 22.654  32.625 51.065 1.000 20.477  ? 64  HIS   BBB CD2 1 ? 
ATOM   2487 C  CE1 . HIS   B 1 65  ? 24.222  33.268 49.684 1.000 22.068  ? 64  HIS   BBB CE1 1 ? 
ATOM   2488 N  NE2 . HIS   B 1 65  ? 23.865  33.253 50.967 1.000 25.569  ? 64  HIS   BBB NE2 1 ? 
ATOM   2489 N  N   . SER   B 1 66  ? 19.717  34.510 49.950 1.000 21.667  ? 65  SER   BBB N   1 ? 
ATOM   2490 C  CA  . SER   B 1 66  ? 19.504  35.463 51.062 1.000 21.066  ? 65  SER   BBB CA  1 ? 
ATOM   2491 C  C   . SER   B 1 66  ? 19.466  36.872 50.471 1.000 22.058  ? 65  SER   BBB C   1 ? 
ATOM   2492 O  O   . SER   B 1 66  ? 19.512  37.014 49.204 1.000 21.207  ? 65  SER   BBB O   1 ? 
ATOM   2493 C  CB  . SER   B 1 66  ? 20.565  35.340 52.115 1.000 24.696  ? 65  SER   BBB CB  1 ? 
ATOM   2494 O  OG  . SER   B 1 66  ? 20.204  35.977 53.325 1.000 24.587  ? 65  SER   BBB OG  1 ? 
ATOM   2495 N  N   . PHE   B 1 67  ? 19.465  37.860 51.356 1.000 21.400  ? 66  PHE   BBB N   1 ? 
ATOM   2496 C  CA  . PHE   B 1 67  ? 19.735  39.246 50.927 1.000 22.810  ? 66  PHE   BBB CA  1 ? 
ATOM   2497 C  C   . PHE   B 1 67  ? 20.758  39.833 51.901 1.000 20.734  ? 66  PHE   BBB C   1 ? 
ATOM   2498 O  O   . PHE   B 1 67  ? 20.753  39.473 53.097 1.000 19.491  ? 66  PHE   BBB O   1 ? 
ATOM   2499 C  CB  . PHE   B 1 67  ? 18.429  40.033 50.817 1.000 22.175  ? 66  PHE   BBB CB  1 ? 
ATOM   2500 C  CG  . PHE   B 1 67  ? 17.879  40.421 52.151 1.000 21.835  ? 66  PHE   BBB CG  1 ? 
ATOM   2501 C  CD1 . PHE   B 1 67  ? 16.977  39.611 52.793 1.000 22.165  ? 66  PHE   BBB CD1 1 ? 
ATOM   2502 C  CD2 . PHE   B 1 67  ? 18.224  41.634 52.733 1.000 24.498  ? 66  PHE   BBB CD2 1 ? 
ATOM   2503 C  CE1 . PHE   B 1 67  ? 16.487  39.941 54.032 1.000 25.067  ? 66  PHE   BBB CE1 1 ? 
ATOM   2504 C  CE2 . PHE   B 1 67  ? 17.714  41.975 53.974 1.000 22.496  ? 66  PHE   BBB CE2 1 ? 
ATOM   2505 C  CZ  . PHE   B 1 67  ? 16.863  41.131 54.627 1.000 24.489  ? 66  PHE   BBB CZ  1 ? 
ATOM   2506 N  N   . HIS   B 1 68  ? 21.653  40.659 51.362 1.000 20.680  ? 67  HIS   BBB N   1 ? 
ATOM   2507 C  CA  . HIS   B 1 68  ? 22.730  41.306 52.121 1.000 22.430  ? 67  HIS   BBB CA  1 ? 
ATOM   2508 C  C   . HIS   B 1 68  ? 22.512  42.824 52.082 1.000 20.072  ? 67  HIS   BBB C   1 ? 
ATOM   2509 O  O   . HIS   B 1 68  ? 22.158  43.297 51.017 1.000 22.129  ? 67  HIS   BBB O   1 ? 
ATOM   2510 C  CB  . HIS   B 1 68  ? 24.086  40.947 51.538 1.000 22.641  ? 67  HIS   BBB CB  1 ? 
ATOM   2511 C  CG  . HIS   B 1 68  ? 24.384  39.477 51.630 1.000 22.738  ? 67  HIS   BBB CG  1 ? 
ATOM   2512 N  ND1 . HIS   B 1 68  ? 25.411  38.950 50.969 1.000 21.922  ? 67  HIS   BBB ND1 1 ? 
ATOM   2513 C  CD2 . HIS   B 1 68  ? 23.876  38.540 52.455 1.000 23.113  ? 67  HIS   BBB CD2 1 ? 
ATOM   2514 C  CE1 . HIS   B 1 68  ? 25.424  37.606 51.245 1.000 21.954  ? 67  HIS   BBB CE1 1 ? 
ATOM   2515 N  NE2 . HIS   B 1 68  ? 24.525  37.362 52.203 1.000 21.651  ? 67  HIS   BBB NE2 1 ? 
ATOM   2516 N  N   . VAL   B 1 69  ? 22.775  43.495 53.199 1.000 18.358  ? 68  VAL   BBB N   1 ? 
ATOM   2517 C  CA  . VAL   B 1 69  ? 22.861  44.999 53.267 1.000 20.631  ? 68  VAL   BBB CA  1 ? 
ATOM   2518 C  C   . VAL   B 1 69  ? 24.348  45.343 53.466 1.000 20.326  ? 68  VAL   BBB C   1 ? 
ATOM   2519 O  O   . VAL   B 1 69  ? 24.897  45.008 54.555 1.000 20.328  ? 68  VAL   BBB O   1 ? 
ATOM   2520 C  CB  . VAL   B 1 69  ? 21.997  45.523 54.406 1.000 21.001  ? 68  VAL   BBB CB  1 ? 
ATOM   2521 C  CG1 . VAL   B 1 69  ? 22.096  47.055 54.430 1.000 24.271  ? 68  VAL   BBB CG1 1 ? 
ATOM   2522 C  CG2 . VAL   B 1 69  ? 20.554  45.117 54.278 1.000 23.050  ? 68  VAL   BBB CG2 1 ? 
ATOM   2523 N  N   . ASN   B 1 70  ? 24.987  45.919 52.430 1.000 23.119  ? 69  ASN   BBB N   1 ? 
ATOM   2524 C  CA  . ASN   B 1 70  ? 26.430  46.120 52.372 1.000 22.110  ? 69  ASN   BBB CA  1 ? 
ATOM   2525 C  C   . ASN   B 1 70  ? 26.736  47.576 52.731 1.000 19.860  ? 69  ASN   BBB C   1 ? 
ATOM   2526 O  O   . ASN   B 1 70  ? 25.857  48.454 52.457 1.000 22.658  ? 69  ASN   BBB O   1 ? 
ATOM   2527 C  CB  . ASN   B 1 70  ? 26.967  45.790 50.998 1.000 19.962  ? 69  ASN   BBB CB  1 ? 
ATOM   2528 C  CG  . ASN   B 1 70  ? 27.014  44.258 50.845 1.000 20.540  ? 69  ASN   BBB CG  1 ? 
ATOM   2529 O  OD1 . ASN   B 1 70  ? 27.287  43.650 51.827 1.000 29.799  ? 69  ASN   BBB OD1 1 ? 
ATOM   2530 N  ND2 . ASN   B 1 70  ? 26.883  43.761 49.648 1.000 27.941  ? 69  ASN   BBB ND2 1 ? 
ATOM   2531 N  N   . PHE   B 1 71  ? 27.902  47.732 53.347 1.000 21.260  ? 70  PHE   BBB N   1 ? 
ATOM   2532 C  CA  . PHE   B 1 71  ? 28.366  49.032 53.871 1.000 22.918  ? 70  PHE   BBB CA  1 ? 
ATOM   2533 C  C   . PHE   B 1 71  ? 29.646  49.419 53.163 1.000 23.440  ? 70  PHE   BBB C   1 ? 
ATOM   2534 O  O   . PHE   B 1 71  ? 30.442  48.580 52.906 1.000 23.501  ? 70  PHE   BBB O   1 ? 
ATOM   2535 C  CB  . PHE   B 1 71  ? 28.540  48.977 55.384 1.000 23.209  ? 70  PHE   BBB CB  1 ? 
ATOM   2536 C  CG  . PHE   B 1 71  ? 27.219  48.980 56.078 1.000 21.366  ? 70  PHE   BBB CG  1 ? 
ATOM   2537 C  CD1 . PHE   B 1 71  ? 26.446  47.843 56.065 1.000 19.961  ? 70  PHE   BBB CD1 1 ? 
ATOM   2538 C  CD2 . PHE   B 1 71  ? 26.699  50.089 56.751 1.000 21.112  ? 70  PHE   BBB CD2 1 ? 
ATOM   2539 C  CE1 . PHE   B 1 71  ? 25.204  47.781 56.654 1.000 24.121  ? 70  PHE   BBB CE1 1 ? 
ATOM   2540 C  CE2 . PHE   B 1 71  ? 25.441  50.050 57.335 1.000 21.507  ? 70  PHE   BBB CE2 1 ? 
ATOM   2541 C  CZ  . PHE   B 1 71  ? 24.698  48.859 57.313 1.000 23.366  ? 70  PHE   BBB CZ  1 ? 
ATOM   2542 N  N   . GLU   B 1 72  ? 29.836  50.752 52.882 1.000 23.361  ? 71  GLU   BBB N   1 ? 
ATOM   2543 C  CA  . GLU   B 1 72  ? 31.162  51.235 52.442 1.000 24.263  ? 71  GLU   BBB CA  1 ? 
ATOM   2544 C  C   . GLU   B 1 72  ? 32.191  50.784 53.461 1.000 24.292  ? 71  GLU   BBB C   1 ? 
ATOM   2545 O  O   . GLU   B 1 72  ? 31.970  51.047 54.647 1.000 25.718  ? 71  GLU   BBB O   1 ? 
ATOM   2546 C  CB  . GLU   B 1 72  ? 31.203  52.793 52.331 1.000 27.272  ? 71  GLU   BBB CB  1 ? 
ATOM   2547 C  CG  . GLU   B 1 72  ? 30.183  53.309 51.347 1.000 36.711  ? 71  GLU   BBB CG  1 ? 
ATOM   2548 C  CD  . GLU   B 1 72  ? 30.181  54.807 51.117 1.000 42.755  ? 71  GLU   BBB CD  1 ? 
ATOM   2549 O  OE1 . GLU   B 1 72  ? 30.977  55.531 51.781 1.000 46.511  ? 71  GLU   BBB OE1 1 ? 
ATOM   2550 O  OE2 . GLU   B 1 72  ? 29.408  55.238 50.249 1.000 54.109  ? 71  GLU   BBB OE2 1 ? 
ATOM   2551 N  N   . ASP   B 1 73  ? 33.295  50.168 53.017 1.000 24.795  ? 72  ASP   BBB N   1 ? 
ATOM   2552 C  CA  . ASP   B 1 73  ? 34.337  49.636 53.942 1.000 24.277  ? 72  ASP   BBB CA  1 ? 
ATOM   2553 C  C   . ASP   B 1 73  ? 35.738  50.069 53.499 1.000 28.123  ? 72  ASP   BBB C   1 ? 
ATOM   2554 O  O   . ASP   B 1 73  ? 36.724  49.378 53.780 1.000 28.017  ? 72  ASP   BBB O   1 ? 
ATOM   2555 C  CB  . ASP   B 1 73  ? 34.220  48.095 54.051 1.000 24.817  ? 72  ASP   BBB CB  1 ? 
ATOM   2556 C  CG  . ASP   B 1 73  ? 34.616  47.385 52.781 1.000 28.493  ? 72  ASP   BBB CG  1 ? 
ATOM   2557 O  OD1 . ASP   B 1 73  ? 34.609  48.026 51.728 1.000 29.518  ? 72  ASP   BBB OD1 1 ? 
ATOM   2558 O  OD2 . ASP   B 1 73  ? 34.964  46.191 52.852 1.000 28.886  ? 72  ASP   BBB OD2 1 ? 
ATOM   2559 N  N   . ASN   B 1 74  ? 35.826  51.318 53.035 1.000 26.632  ? 73  ASN   BBB N   1 ? 
ATOM   2560 C  CA  . ASN   B 1 74  ? 37.095  51.973 52.597 1.000 32.805  ? 73  ASN   BBB CA  1 ? 
ATOM   2561 C  C   . ASN   B 1 74  ? 37.832  52.541 53.825 1.000 31.053  ? 73  ASN   BBB C   1 ? 
ATOM   2562 O  O   . ASN   B 1 74  ? 39.089  52.753 53.763 1.000 33.343  ? 73  ASN   BBB O   1 ? 
ATOM   2563 C  CB  . ASN   B 1 74  ? 36.868  53.014 51.492 1.000 37.635  ? 73  ASN   BBB CB  1 ? 
ATOM   2564 C  CG  . ASN   B 1 74  ? 35.774  54.012 51.820 1.000 44.540  ? 73  ASN   BBB CG  1 ? 
ATOM   2565 O  OD1 . ASN   B 1 74  ? 34.625  53.624 52.034 1.000 39.630  ? 73  ASN   BBB OD1 1 ? 
ATOM   2566 N  ND2 . ASN   B 1 74  ? 36.095  55.299 51.842 1.000 53.285  ? 73  ASN   BBB ND2 1 ? 
ATOM   2567 N  N   . ASP   B 1 75  ? 37.132  52.756 54.933 1.000 29.978  ? 74  ASP   BBB N   1 ? 
ATOM   2568 C  CA  . ASP   B 1 75  ? 37.786  53.279 56.145 1.000 27.062  ? 74  ASP   BBB CA  1 ? 
ATOM   2569 C  C   . ASP   B 1 75  ? 37.100  52.800 57.417 1.000 30.414  ? 74  ASP   BBB C   1 ? 
ATOM   2570 O  O   . ASP   B 1 75  ? 36.169  51.948 57.327 1.000 30.264  ? 74  ASP   BBB O   1 ? 
ATOM   2571 C  CB  . ASP   B 1 75  ? 37.793  54.818 56.055 1.000 28.437  ? 74  ASP   BBB CB  1 ? 
ATOM   2572 C  CG  . ASP   B 1 75  ? 36.435  55.479 56.106 1.000 34.386  ? 74  ASP   BBB CG  1 ? 
ATOM   2573 O  OD1 . ASP   B 1 75  ? 35.455  54.936 56.621 1.000 31.750  ? 74  ASP   BBB OD1 1 ? 
ATOM   2574 O  OD2 . ASP   B 1 75  ? 36.423  56.671 55.750 1.000 45.640  ? 74  ASP   BBB OD2 1 ? 
ATOM   2575 N  N   . ASN   B 1 76  ? 37.532  53.357 58.555 1.000 30.328  ? 75  ASN   BBB N   1 ? 
ATOM   2576 C  CA  . ASN   B 1 76  ? 37.093  52.913 59.887 1.000 28.113  ? 75  ASN   BBB CA  1 ? 
ATOM   2577 C  C   . ASN   B 1 76  ? 36.007  53.807 60.445 1.000 28.926  ? 75  ASN   BBB C   1 ? 
ATOM   2578 O  O   . ASN   B 1 76  ? 35.957  53.974 61.672 1.000 31.420  ? 75  ASN   BBB O   1 ? 
ATOM   2579 C  CB  . ASN   B 1 76  ? 38.242  52.786 60.861 1.000 33.499  ? 75  ASN   BBB CB  1 ? 
ATOM   2580 C  CG  . ASN   B 1 76  ? 39.041  51.547 60.597 1.000 35.374  ? 75  ASN   BBB CG  1 ? 
ATOM   2581 O  OD1 . ASN   B 1 76  ? 38.530  50.566 60.032 1.000 40.950  ? 75  ASN   BBB OD1 1 ? 
ATOM   2582 N  ND2 . ASN   B 1 76  ? 40.284  51.600 61.022 1.000 49.466  ? 75  ASN   BBB ND2 1 ? 
ATOM   2583 N  N   . ARG   B 1 77  ? 35.126  54.315 59.590 1.000 28.507  ? 76  ARG   BBB N   1 ? 
ATOM   2584 C  CA  . ARG   B 1 77  ? 33.941  55.057 60.096 1.000 28.272  ? 76  ARG   BBB CA  1 ? 
ATOM   2585 C  C   . ARG   B 1 77  ? 33.089  54.161 61.004 1.000 29.838  ? 76  ARG   BBB C   1 ? 
ATOM   2586 O  O   . ARG   B 1 77  ? 32.458  54.691 61.952 1.000 31.170  ? 76  ARG   BBB O   1 ? 
ATOM   2587 C  CB  . ARG   B 1 77  ? 33.170  55.633 58.917 1.000 32.079  ? 76  ARG   BBB CB  1 ? 
ATOM   2588 C  CG  . ARG   B 1 77  ? 33.756  56.994 58.500 1.000 32.604  ? 76  ARG   BBB CG  1 ? 
ATOM   2589 C  CD  . ARG   B 1 77  ? 33.062  57.496 57.245 1.000 36.506  ? 76  ARG   BBB CD  1 ? 
ATOM   2590 N  NE  . ARG   B 1 77  ? 33.213  56.571 56.109 1.000 31.281  ? 76  ARG   BBB NE  1 ? 
ATOM   2591 C  CZ  . ARG   B 1 77  ? 32.476  56.583 54.992 1.000 29.636  ? 76  ARG   BBB CZ  1 ? 
ATOM   2592 N  NH1 . ARG   B 1 77  ? 31.550  57.506 54.825 1.000 35.759  ? 76  ARG   BBB NH1 1 ? 
ATOM   2593 N  NH2 . ARG   B 1 77  ? 32.665  55.686 54.030 1.000 32.573  ? 76  ARG   BBB NH2 1 ? 
ATOM   2594 N  N   . SER   B 1 78  ? 33.029  52.847 60.723 1.000 25.589  ? 77  SER   BBB N   1 ? 
ATOM   2595 C  CA  . SER   B 1 78  ? 32.032  51.963 61.344 1.000 24.832  ? 77  SER   BBB CA  1 ? 
ATOM   2596 C  C   . SER   B 1 78  ? 32.795  50.745 61.869 1.000 23.602  ? 77  SER   BBB C   1 ? 
ATOM   2597 O  O   . SER   B 1 78  ? 33.341  50.067 61.019 1.000 21.616  ? 77  SER   BBB O   1 ? 
ATOM   2598 C  CB  . SER   B 1 78  ? 30.975  51.564 60.340 1.000 21.963  ? 77  SER   BBB CB  1 ? 
ATOM   2599 O  OG  . SER   B 1 78  ? 30.133  52.638 59.982 1.000 22.565  ? 77  SER   BBB OG  1 ? 
ATOM   2600 N  N   . VAL   B 1 79  ? 32.929  50.604 63.194 1.000 23.231  ? 78  VAL   BBB N   1 ? 
ATOM   2601 C  CA  . VAL   B 1 79  ? 33.888  49.649 63.817 1.000 23.601  ? 78  VAL   BBB CA  1 ? 
ATOM   2602 C  C   . VAL   B 1 79  ? 33.331  48.993 65.058 1.000 23.145  ? 78  VAL   BBB C   1 ? 
ATOM   2603 O  O   . VAL   B 1 79  ? 32.504  49.531 65.756 1.000 29.609  ? 78  VAL   BBB O   1 ? 
ATOM   2604 C  CB  . VAL   B 1 79  ? 35.249  50.252 64.147 1.000 26.025  ? 78  VAL   BBB CB  1 ? 
ATOM   2605 C  CG1 . VAL   B 1 79  ? 36.000  50.662 62.874 1.000 35.089  ? 78  VAL   BBB CG1 1 ? 
ATOM   2606 C  CG2 . VAL   B 1 79  ? 35.071  51.402 65.116 1.000 34.328  ? 78  VAL   BBB CG2 1 ? 
ATOM   2607 N  N   . LEU   B 1 80  ? 33.748  47.725 65.188 1.000 21.885  ? 79  LEU   BBB N   1 ? 
ATOM   2608 C  CA  . LEU   B 1 80  ? 33.544  46.908 66.395 1.000 23.973  ? 79  LEU   BBB CA  1 ? 
ATOM   2609 C  C   . LEU   B 1 80  ? 34.883  46.823 67.140 1.000 23.054  ? 79  LEU   BBB C   1 ? 
ATOM   2610 O  O   . LEU   B 1 80  ? 35.927  46.581 66.484 1.000 24.067  ? 79  LEU   BBB O   1 ? 
ATOM   2611 C  CB  . LEU   B 1 80  ? 33.038  45.536 65.927 1.000 21.486  ? 79  LEU   BBB CB  1 ? 
ATOM   2612 C  CG  . LEU   B 1 80  ? 33.101  44.391 66.921 1.000 19.982  ? 79  LEU   BBB CG  1 ? 
ATOM   2613 C  CD1 . LEU   B 1 80  ? 32.224  44.597 68.153 1.000 22.907  ? 79  LEU   BBB CD1 1 ? 
ATOM   2614 C  CD2 . LEU   B 1 80  ? 32.700  43.114 66.194 1.000 23.069  ? 79  LEU   BBB CD2 1 ? 
ATOM   2615 N  N   . LYS   B 1 81  ? 34.875  46.995 68.447 1.000 28.800  ? 80  LYS   BBB N   1 ? 
ATOM   2616 C  CA  . LYS   B 1 81  ? 36.090  46.803 69.272 1.000 28.857  ? 80  LYS   BBB CA  1 ? 
ATOM   2617 C  C   . LYS   B 1 81  ? 35.675  46.152 70.602 1.000 21.548  ? 80  LYS   BBB C   1 ? 
ATOM   2618 O  O   . LYS   B 1 81  ? 34.446  46.052 70.883 1.000 22.709  ? 80  LYS   BBB O   1 ? 
ATOM   2619 C  CB  . LYS   B 1 81  ? 36.909  48.069 69.544 1.000 33.235  ? 80  LYS   BBB CB  1 ? 
ATOM   2620 C  CG  . LYS   B 1 81  ? 36.166  49.352 69.785 1.000 45.253  ? 80  LYS   BBB CG  1 ? 
ATOM   2621 C  CD  . LYS   B 1 81  ? 37.085  50.537 69.553 1.000 58.486  ? 80  LYS   BBB CD  1 ? 
ATOM   2622 C  CE  . LYS   B 1 81  ? 36.342  51.797 69.177 1.000 58.672  ? 80  LYS   BBB CE  1 ? 
ATOM   2623 N  NZ  . LYS   B 1 81  ? 37.147  53.004 69.405 1.000 74.812  ? 80  LYS   BBB NZ  1 ? 
ATOM   2624 N  N   . GLY   B 1 82  ? 36.682  45.753 71.375 1.000 26.874  ? 81  GLY   BBB N   1 ? 
ATOM   2625 C  CA  . GLY   B 1 82  ? 36.514  45.221 72.730 1.000 27.104  ? 81  GLY   BBB CA  1 ? 
ATOM   2626 C  C   . GLY   B 1 82  ? 36.161  43.754 72.663 1.000 24.223  ? 81  GLY   BBB C   1 ? 
ATOM   2627 O  O   . GLY   B 1 82  ? 36.621  43.097 71.730 1.000 24.130  ? 81  GLY   BBB O   1 ? 
ATOM   2628 N  N   . GLY   B 1 83  ? 35.349  43.276 73.579 1.000 23.965  ? 82  GLY   BBB N   1 ? 
ATOM   2629 C  CA  . GLY   B 1 83  ? 35.140  41.815 73.735 1.000 23.234  ? 82  GLY   BBB CA  1 ? 
ATOM   2630 C  C   . GLY   B 1 83  ? 36.454  41.043 73.647 1.000 25.008  ? 82  GLY   BBB C   1 ? 
ATOM   2631 O  O   . GLY   B 1 83  ? 37.387  41.306 74.391 1.000 26.707  ? 82  GLY   BBB O   1 ? 
ATOM   2632 N  N   . PRO   B 1 84  ? 36.575  39.999 72.796 1.000 30.255  ? 83  PRO   BBB N   1 ? 
ATOM   2633 C  CA  . PRO   B 1 84  ? 37.795  39.191 72.761 1.000 29.855  ? 83  PRO   BBB CA  1 ? 
ATOM   2634 C  C   . PRO   B 1 84  ? 38.926  39.847 71.958 1.000 30.659  ? 83  PRO   BBB C   1 ? 
ATOM   2635 O  O   . PRO   B 1 84  ? 39.959  39.266 71.892 1.000 33.297  ? 83  PRO   BBB O   1 ? 
ATOM   2636 C  CB  . PRO   B 1 84  ? 37.386  37.902 72.019 1.000 28.506  ? 83  PRO   BBB CB  1 ? 
ATOM   2637 C  CG  . PRO   B 1 84  ? 36.248  38.361 71.108 1.000 31.994  ? 83  PRO   BBB CG  1 ? 
ATOM   2638 C  CD  . PRO   B 1 84  ? 35.611  39.566 71.789 1.000 28.578  ? 83  PRO   BBB CD  1 ? 
ATOM   2639 N  N   . PHE   B 1 85  ? 38.688  41.007 71.336 1.000 30.792  ? 84  PHE   BBB N   1 ? 
ATOM   2640 C  CA  . PHE   B 1 85  ? 39.554  41.594 70.272 1.000 33.494  ? 84  PHE   BBB CA  1 ? 
ATOM   2641 C  C   . PHE   B 1 85  ? 40.561  42.585 70.862 1.000 32.019  ? 84  PHE   BBB C   1 ? 
ATOM   2642 O  O   . PHE   B 1 85  ? 40.125  43.383 71.735 1.000 37.204  ? 84  PHE   BBB O   1 ? 
ATOM   2643 C  CB  . PHE   B 1 85  ? 38.690  42.302 69.221 1.000 30.619  ? 84  PHE   BBB CB  1 ? 
ATOM   2644 C  CG  . PHE   B 1 85  ? 37.642  41.403 68.624 1.000 27.824  ? 84  PHE   BBB CG  1 ? 
ATOM   2645 C  CD1 . PHE   B 1 85  ? 38.038  40.265 67.946 1.000 30.497  ? 84  PHE   BBB CD1 1 ? 
ATOM   2646 C  CD2 . PHE   B 1 85  ? 36.293  41.666 68.751 1.000 28.716  ? 84  PHE   BBB CD2 1 ? 
ATOM   2647 C  CE1 . PHE   B 1 85  ? 37.099  39.392 67.420 1.000 28.422  ? 84  PHE   BBB CE1 1 ? 
ATOM   2648 C  CE2 . PHE   B 1 85  ? 35.347  40.818 68.184 1.000 33.552  ? 84  PHE   BBB CE2 1 ? 
ATOM   2649 C  CZ  . PHE   B 1 85  ? 35.754  39.668 67.539 1.000 32.652  ? 84  PHE   BBB CZ  1 ? 
ATOM   2650 N  N   . SER   B 1 86  ? 41.814  42.564 70.371 1.000 35.203  ? 85  SER   BBB N   1 ? 
ATOM   2651 C  CA  . SER   B 1 86  ? 42.819  43.665 70.505 1.000 39.660  ? 85  SER   BBB CA  1 ? 
ATOM   2652 C  C   . SER   B 1 86  ? 42.704  44.615 69.316 1.000 39.118  ? 85  SER   BBB C   1 ? 
ATOM   2653 O  O   . SER   B 1 86  ? 43.079  45.762 69.495 1.000 43.415  ? 85  SER   BBB O   1 ? 
ATOM   2654 C  CB  . SER   B 1 86  ? 44.254  43.175 70.592 1.000 47.346  ? 85  SER   BBB CB  1 ? 
ATOM   2655 O  OG  . SER   B 1 86  ? 44.330  41.817 71.017 1.000 62.201  ? 85  SER   BBB OG  1 ? 
ATOM   2656 N  N   . ASP   B 1 87  ? 42.288  44.123 68.143 1.000 46.330  ? 86  ASP   BBB N   1 ? 
ATOM   2657 C  CA  . ASP   B 1 87  ? 42.213  44.871 66.853 1.000 50.003  ? 86  ASP   BBB CA  1 ? 
ATOM   2658 C  C   . ASP   B 1 87  ? 40.813  45.500 66.721 1.000 40.212  ? 86  ASP   BBB C   1 ? 
ATOM   2659 O  O   . ASP   B 1 87  ? 39.868  44.956 67.284 1.000 40.445  ? 86  ASP   BBB O   1 ? 
ATOM   2660 C  CB  . ASP   B 1 87  ? 42.514  43.929 65.665 1.000 59.365  ? 86  ASP   BBB CB  1 ? 
ATOM   2661 C  CG  . ASP   B 1 87  ? 43.904  43.276 65.617 1.000 53.218  ? 86  ASP   BBB CG  1 ? 
ATOM   2662 O  OD1 . ASP   B 1 87  ? 44.888  43.921 66.052 1.000 47.907  ? 86  ASP   BBB OD1 1 ? 
ATOM   2663 O  OD2 . ASP   B 1 87  ? 44.008  42.123 65.109 1.000 44.873  ? 86  ASP   BBB OD2 1 ? 
ATOM   2664 N  N   . SER   B 1 88  ? 40.656  46.608 65.998 1.000 37.812  ? 87  SER   BBB N   1 ? 
ATOM   2665 C  CA  . SER   B 1 88  ? 39.323  47.091 65.548 1.000 30.257  ? 87  SER   BBB CA  1 ? 
ATOM   2666 C  C   . SER   B 1 88  ? 38.912  46.254 64.339 1.000 24.577  ? 87  SER   BBB C   1 ? 
ATOM   2667 O  O   . SER   B 1 88  ? 39.783  46.000 63.502 1.000 32.574  ? 87  SER   BBB O   1 ? 
ATOM   2668 C  CB  . SER   B 1 88  ? 39.322  48.564 65.194 1.000 39.312  ? 87  SER   BBB CB  1 ? 
ATOM   2669 O  OG  . SER   B 1 88  ? 39.223  49.341 66.376 1.000 44.079  ? 87  SER   BBB OG  1 ? 
ATOM   2670 N  N   . TYR   B 1 89  ? 37.628  45.921 64.227 1.000 24.237  ? 88  TYR   BBB N   1 ? 
ATOM   2671 C  CA  . TYR   B 1 89  ? 37.043  45.260 63.044 1.000 24.817  ? 88  TYR   BBB CA  1 ? 
ATOM   2672 C  C   . TYR   B 1 89  ? 36.081  46.216 62.346 1.000 21.806  ? 88  TYR   BBB C   1 ? 
ATOM   2673 O  O   . TYR   B 1 89  ? 35.276  46.875 63.003 1.000 24.833  ? 88  TYR   BBB O   1 ? 
ATOM   2674 C  CB  . TYR   B 1 89  ? 36.363  43.931 63.431 1.000 22.078  ? 88  TYR   BBB CB  1 ? 
ATOM   2675 C  CG  . TYR   B 1 89  ? 37.308  42.816 63.770 1.000 22.899  ? 88  TYR   BBB CG  1 ? 
ATOM   2676 C  CD1 . TYR   B 1 89  ? 38.145  42.877 64.868 1.000 24.626  ? 88  TYR   BBB CD1 1 ? 
ATOM   2677 C  CD2 . TYR   B 1 89  ? 37.357  41.704 62.958 1.000 25.184  ? 88  TYR   BBB CD2 1 ? 
ATOM   2678 C  CE1 . TYR   B 1 89  ? 39.002  41.837 65.185 1.000 28.920  ? 88  TYR   BBB CE1 1 ? 
ATOM   2679 C  CE2 . TYR   B 1 89  ? 38.222  40.668 63.238 1.000 26.523  ? 88  TYR   BBB CE2 1 ? 
ATOM   2680 C  CZ  . TYR   B 1 89  ? 39.031  40.724 64.360 1.000 26.582  ? 88  TYR   BBB CZ  1 ? 
ATOM   2681 O  OH  . TYR   B 1 89  ? 39.896  39.702 64.559 1.000 30.178  ? 88  TYR   BBB OH  1 ? 
ATOM   2682 N  N   . ARG   B 1 90  ? 36.121  46.202 61.019 1.000 22.973  ? 89  ARG   BBB N   1 ? 
ATOM   2683 C  CA  . ARG   B 1 90  ? 35.386  47.160 60.158 1.000 24.069  ? 89  ARG   BBB CA  1 ? 
ATOM   2684 C  C   . ARG   B 1 90  ? 34.055  46.572 59.691 1.000 21.495  ? 89  ARG   BBB C   1 ? 
ATOM   2685 O  O   . ARG   B 1 90  ? 34.073  45.415 59.128 1.000 21.781  ? 89  ARG   BBB O   1 ? 
ATOM   2686 C  CB  . ARG   B 1 90  ? 36.276  47.523 58.976 1.000 23.410  ? 89  ARG   BBB CB  1 ? 
ATOM   2687 C  CG  . ARG   B 1 90  ? 35.642  48.532 58.034 1.000 25.322  ? 89  ARG   BBB CG  1 ? 
ATOM   2688 C  CD  . ARG   B 1 90  ? 36.598  48.953 56.934 1.000 28.245  ? 89  ARG   BBB CD  1 ? 
ATOM   2689 N  NE  . ARG   B 1 90  ? 37.833  49.509 57.471 1.000 29.618  ? 89  ARG   BBB NE  1 ? 
ATOM   2690 C  CZ  . ARG   B 1 90  ? 38.894  49.846 56.740 1.000 29.167  ? 89  ARG   BBB CZ  1 ? 
ATOM   2691 N  NH1 . ARG   B 1 90  ? 38.926  49.624 55.433 1.000 31.630  ? 89  ARG   BBB NH1 1 ? 
ATOM   2692 N  NH2 . ARG   B 1 90  ? 39.941  50.358 57.347 1.000 33.078  ? 89  ARG   BBB NH2 1 ? 
ATOM   2693 N  N   . LEU   B 1 91  ? 32.939  47.202 60.022 1.000 24.097  ? 90  LEU   BBB N   1 ? 
ATOM   2694 C  CA  . LEU   B 1 91  ? 31.602  46.895 59.500 1.000 19.377  ? 90  LEU   BBB CA  1 ? 
ATOM   2695 C  C   . LEU   B 1 91  ? 31.590  46.814 57.975 1.000 18.891  ? 90  LEU   BBB C   1 ? 
ATOM   2696 O  O   . LEU   B 1 91  ? 32.178  47.671 57.286 1.000 23.018  ? 90  LEU   BBB O   1 ? 
ATOM   2697 C  CB  . LEU   B 1 91  ? 30.496  47.809 60.029 1.000 19.882  ? 90  LEU   BBB CB  1 ? 
ATOM   2698 C  CG  . LEU   B 1 91  ? 29.089  47.609 59.479 1.000 19.511  ? 90  LEU   BBB CG  1 ? 
ATOM   2699 C  CD1 . LEU   B 1 91  ? 28.474  46.319 60.009 1.000 17.207  ? 90  LEU   BBB CD1 1 ? 
ATOM   2700 C  CD2 . LEU   B 1 91  ? 28.173  48.781 59.833 1.000 22.839  ? 90  LEU   BBB CD2 1 ? 
ATOM   2701 N  N   . PHE   B 1 92  ? 31.081  45.645 57.427 1.000 20.447  ? 91  PHE   BBB N   1 ? 
ATOM   2702 C  CA  . PHE   B 1 92  ? 30.863  45.592 55.950 1.000 20.103  ? 91  PHE   BBB CA  1 ? 
ATOM   2703 C  C   . PHE   B 1 92  ? 29.451  45.187 55.508 1.000 19.709  ? 91  PHE   BBB C   1 ? 
ATOM   2704 O  O   . PHE   B 1 92  ? 29.129  45.411 54.322 1.000 26.665  ? 91  PHE   BBB O   1 ? 
ATOM   2705 C  CB  . PHE   B 1 92  ? 31.994  44.861 55.211 1.000 20.022  ? 91  PHE   BBB CB  1 ? 
ATOM   2706 C  CG  . PHE   B 1 92  ? 31.957  43.350 55.331 1.000 21.762  ? 91  PHE   BBB CG  1 ? 
ATOM   2707 C  CD1 . PHE   B 1 92  ? 32.479  42.729 56.455 1.000 21.979  ? 91  PHE   BBB CD1 1 ? 
ATOM   2708 C  CD2 . PHE   B 1 92  ? 31.237  42.645 54.396 1.000 21.258  ? 91  PHE   BBB CD2 1 ? 
ATOM   2709 C  CE1 . PHE   B 1 92  ? 32.393  41.322 56.559 1.000 22.693  ? 91  PHE   BBB CE1 1 ? 
ATOM   2710 C  CE2 . PHE   B 1 92  ? 31.167  41.231 54.503 1.000 21.065  ? 91  PHE   BBB CE2 1 ? 
ATOM   2711 C  CZ  . PHE   B 1 92  ? 31.708  40.618 55.595 1.000 24.533  ? 91  PHE   BBB CZ  1 ? 
ATOM   2712 N  N   . GLN   B 1 93  ? 28.695  44.469 56.359 1.000 19.200  ? 92  GLN   BBB N   1 ? 
ATOM   2713 C  CA  . GLN   B 1 93  ? 27.413  43.861 55.956 1.000 18.331  ? 92  GLN   BBB CA  1 ? 
ATOM   2714 C  C   . GLN   B 1 93  ? 26.606  43.459 57.190 1.000 16.898  ? 92  GLN   BBB C   1 ? 
ATOM   2715 O  O   . GLN   B 1 93  ? 27.208  43.191 58.290 1.000 20.674  ? 92  GLN   BBB O   1 ? 
ATOM   2716 C  CB  . GLN   B 1 93  ? 27.719  42.561 55.183 1.000 25.240  ? 92  GLN   BBB CB  1 ? 
ATOM   2717 C  CG  . GLN   B 1 93  ? 26.517  41.773 54.689 1.000 28.880  ? 92  GLN   BBB CG  1 ? 
ATOM   2718 C  CD  . GLN   B 1 93  ? 26.951  40.600 53.838 1.000 22.986  ? 92  GLN   BBB CD  1 ? 
ATOM   2719 O  OE1 . GLN   B 1 93  ? 27.472  40.732 52.701 1.000 25.817  ? 92  GLN   BBB OE1 1 ? 
ATOM   2720 N  NE2 . GLN   B 1 93  ? 26.803  39.425 54.408 1.000 21.501  ? 92  GLN   BBB NE2 1 ? 
ATOM   2721 N  N   . PHE   B 1 94  ? 25.295  43.441 57.026 1.000 18.850  ? 93  PHE   BBB N   1 ? 
ATOM   2722 C  CA  . PHE   B 1 94  ? 24.411  42.609 57.900 1.000 19.338  ? 93  PHE   BBB CA  1 ? 
ATOM   2723 C  C   . PHE   B 1 94  ? 23.390  41.910 57.023 1.000 18.518  ? 93  PHE   BBB C   1 ? 
ATOM   2724 O  O   . PHE   B 1 94  ? 23.136  42.301 55.870 1.000 20.350  ? 93  PHE   BBB O   1 ? 
ATOM   2725 C  CB  . PHE   B 1 94  ? 23.753  43.393 59.034 1.000 19.698  ? 93  PHE   BBB CB  1 ? 
ATOM   2726 C  CG  . PHE   B 1 94  ? 22.646  44.317 58.586 1.000 16.882  ? 93  PHE   BBB CG  1 ? 
ATOM   2727 C  CD1 . PHE   B 1 94  ? 21.363  43.897 58.585 1.000 21.511  ? 93  PHE   BBB CD1 1 ? 
ATOM   2728 C  CD2 . PHE   B 1 94  ? 22.895  45.672 58.315 1.000 19.113  ? 93  PHE   BBB CD2 1 ? 
ATOM   2729 C  CE1 . PHE   B 1 94  ? 20.311  44.672 58.161 1.000 20.412  ? 93  PHE   BBB CE1 1 ? 
ATOM   2730 C  CE2 . PHE   B 1 94  ? 21.843  46.442 57.897 1.000 20.840  ? 93  PHE   BBB CE2 1 ? 
ATOM   2731 C  CZ  . PHE   B 1 94  ? 20.548  46.006 57.915 1.000 20.537  ? 93  PHE   BBB CZ  1 ? 
ATOM   2732 N  N   . HIS   B 1 95  ? 22.972  40.723 57.511 1.000 20.956  ? 94  HIS   BBB N   1 ? 
ATOM   2733 C  CA  . HIS   B 1 95  ? 21.935  39.917 56.854 1.000 22.460  ? 94  HIS   BBB CA  1 ? 
ATOM   2734 C  C   . HIS   B 1 95  ? 21.248  39.062 57.940 1.000 18.909  ? 94  HIS   BBB C   1 ? 
ATOM   2735 O  O   . HIS   B 1 95  ? 21.623  39.123 59.152 1.000 19.133  ? 94  HIS   BBB O   1 ? 
ATOM   2736 C  CB  . HIS   B 1 95  ? 22.579  39.005 55.773 1.000 18.753  ? 94  HIS   BBB CB  1 ? 
ATOM   2737 C  CG  . HIS   B 1 95  ? 23.612  38.097 56.351 1.000 18.684  ? 94  HIS   BBB CG  1 ? 
ATOM   2738 N  ND1 . HIS   B 1 95  ? 24.967  38.244 56.147 1.000 19.014  ? 94  HIS   BBB ND1 1 ? 
ATOM   2739 C  CD2 . HIS   B 1 95  ? 23.472  36.901 57.023 1.000 23.093  ? 94  HIS   BBB CD2 1 ? 
ATOM   2740 C  CE1 . HIS   B 1 95  ? 25.582  37.212 56.706 1.000 21.664  ? 94  HIS   BBB CE1 1 ? 
ATOM   2741 N  NE2 . HIS   B 1 95  ? 24.716  36.563 57.393 1.000 32.921  ? 94  HIS   BBB NE2 1 ? 
ATOM   2742 N  N   . PHE   B 1 96  ? 20.268  38.272 57.484 1.000 19.755  ? 95  PHE   BBB N   1 ? 
ATOM   2743 C  CA  . PHE   B 1 96  ? 19.437  37.445 58.364 1.000 18.710  ? 95  PHE   BBB CA  1 ? 
ATOM   2744 C  C   . PHE   B 1 96  ? 19.523  36.007 57.839 1.000 20.319  ? 95  PHE   BBB C   1 ? 
ATOM   2745 O  O   . PHE   B 1 96  ? 19.820  35.805 56.685 1.000 20.790  ? 95  PHE   BBB O   1 ? 
ATOM   2746 C  CB  . PHE   B 1 96  ? 17.991  37.949 58.407 1.000 18.164  ? 95  PHE   BBB CB  1 ? 
ATOM   2747 C  CG  . PHE   B 1 96  ? 17.886  39.371 58.852 1.000 17.969  ? 95  PHE   BBB CG  1 ? 
ATOM   2748 C  CD1 . PHE   B 1 96  ? 17.956  40.357 57.893 1.000 21.055  ? 95  PHE   BBB CD1 1 ? 
ATOM   2749 C  CD2 . PHE   B 1 96  ? 17.667  39.699 60.173 1.000 19.368  ? 95  PHE   BBB CD2 1 ? 
ATOM   2750 C  CE1 . PHE   B 1 96  ? 17.872  41.677 58.293 1.000 18.840  ? 95  PHE   BBB CE1 1 ? 
ATOM   2751 C  CE2 . PHE   B 1 96  ? 17.527  41.028 60.554 1.000 18.877  ? 95  PHE   BBB CE2 1 ? 
ATOM   2752 C  CZ  . PHE   B 1 96  ? 17.654  42.004 59.603 1.000 24.065  ? 95  PHE   BBB CZ  1 ? 
ATOM   2753 N  N   . HIS   B 1 97  ? 19.236  35.106 58.744 1.000 20.253  ? 96  HIS   BBB N   1 ? 
ATOM   2754 C  CA  . HIS   B 1 97  ? 18.793  33.734 58.413 1.000 18.353  ? 96  HIS   BBB CA  1 ? 
ATOM   2755 C  C   . HIS   B 1 97  ? 17.387  33.503 58.939 1.000 21.185  ? 96  HIS   BBB C   1 ? 
ATOM   2756 O  O   . HIS   B 1 97  ? 17.057  33.993 60.033 1.000 21.641  ? 96  HIS   BBB O   1 ? 
ATOM   2757 C  CB  . HIS   B 1 97  ? 19.813  32.694 58.928 1.000 19.227  ? 96  HIS   BBB CB  1 ? 
ATOM   2758 C  CG  . HIS   B 1 97  ? 21.200  32.855 58.401 1.000 19.774  ? 96  HIS   BBB CG  1 ? 
ATOM   2759 N  ND1 . HIS   B 1 97  ? 21.754  32.176 57.311 1.000 22.574  ? 96  HIS   BBB ND1 1 ? 
ATOM   2760 C  CD2 . HIS   B 1 97  ? 22.133  33.766 58.740 1.000 16.895  ? 96  HIS   BBB CD2 1 ? 
ATOM   2761 C  CE1 . HIS   B 1 97  ? 23.014  32.578 57.118 1.000 19.477  ? 96  HIS   BBB CE1 1 ? 
ATOM   2762 N  NE2 . HIS   B 1 97  ? 23.250  33.617 58.012 1.000 20.827  ? 96  HIS   BBB NE2 1 ? 
ATOM   2763 N  N   . TRP   B 1 98  ? 16.665  32.601 58.269 1.000 23.146  ? 97  TRP   BBB N   1 ? 
ATOM   2764 C  CA  . TRP   B 1 98  ? 15.306  32.230 58.697 1.000 23.281  ? 97  TRP   BBB CA  1 ? 
ATOM   2765 C  C   . TRP   B 1 98  ? 15.061  30.799 58.255 1.000 23.541  ? 97  TRP   BBB C   1 ? 
ATOM   2766 O  O   . TRP   B 1 98  ? 15.906  30.297 57.490 1.000 24.019  ? 97  TRP   BBB O   1 ? 
ATOM   2767 C  CB  . TRP   B 1 98  ? 14.267  33.241 58.182 1.000 21.937  ? 97  TRP   BBB CB  1 ? 
ATOM   2768 C  CG  . TRP   B 1 98  ? 14.232  33.342 56.697 1.000 23.120  ? 97  TRP   BBB CG  1 ? 
ATOM   2769 C  CD1 . TRP   B 1 98  ? 13.535  32.540 55.844 1.000 24.226  ? 97  TRP   BBB CD1 1 ? 
ATOM   2770 C  CD2 . TRP   B 1 98  ? 14.979  34.264 55.879 1.000 23.582  ? 97  TRP   BBB CD2 1 ? 
ATOM   2771 N  NE1 . TRP   B 1 98  ? 13.784  32.884 54.553 1.000 25.132  ? 97  TRP   BBB NE1 1 ? 
ATOM   2772 C  CE2 . TRP   B 1 98  ? 14.595  34.013 54.550 1.000 22.362  ? 97  TRP   BBB CE2 1 ? 
ATOM   2773 C  CE3 . TRP   B 1 98  ? 15.810  35.361 56.136 1.000 24.348  ? 97  TRP   BBB CE3 1 ? 
ATOM   2774 C  CZ2 . TRP   B 1 98  ? 15.153  34.696 53.476 1.000 23.806  ? 97  TRP   BBB CZ2 1 ? 
ATOM   2775 C  CZ3 . TRP   B 1 98  ? 16.342  36.062 55.061 1.000 21.413  ? 97  TRP   BBB CZ3 1 ? 
ATOM   2776 C  CH2 . TRP   B 1 98  ? 15.993  35.754 53.757 1.000 21.376  ? 97  TRP   BBB CH2 1 ? 
ATOM   2777 N  N   . GLY   B 1 99  ? 13.930  30.263 58.668 1.000 22.724  ? 98  GLY   BBB N   1 ? 
ATOM   2778 C  CA  . GLY   B 1 99  ? 13.555  28.849 58.428 1.000 24.403  ? 98  GLY   BBB CA  1 ? 
ATOM   2779 C  C   . GLY   B 1 99  ? 12.182  28.756 57.760 1.000 23.750  ? 98  GLY   BBB C   1 ? 
ATOM   2780 O  O   . GLY   B 1 99  ? 11.430  29.739 57.700 1.000 28.115  ? 98  GLY   BBB O   1 ? 
ATOM   2781 N  N   . SER   B 1 100 ? 11.766  27.572 57.317 1.000 26.382  ? 99  SER   BBB N   1 ? 
ATOM   2782 C  CA  . SER   B 1 100 ? 10.524  27.411 56.529 1.000 28.265  ? 99  SER   BBB CA  1 ? 
ATOM   2783 C  C   . SER   B 1 100 ? 9.303   27.661 57.427 1.000 30.817  ? 99  SER   BBB C   1 ? 
ATOM   2784 O  O   . SER   B 1 100 ? 8.242   28.021 56.859 1.000 36.920  ? 99  SER   BBB O   1 ? 
ATOM   2785 C  CB  . SER   B 1 100 ? 10.533  26.033 55.890 1.000 37.662  ? 99  SER   BBB CB  1 ? 
ATOM   2786 O  OG  . SER   B 1 100 ? 10.554  25.043 56.885 1.000 43.560  ? 99  SER   BBB OG  1 ? 
ATOM   2787 N  N   . THR   B 1 101 ? 9.468   27.521 58.757 1.000 31.689  ? 100 THR   BBB N   1 ? 
ATOM   2788 C  CA  . THR   B 1 101 ? 8.455   27.770 59.823 1.000 34.067  ? 100 THR   BBB CA  1 ? 
ATOM   2789 C  C   . THR   B 1 101 ? 8.999   28.766 60.870 1.000 37.294  ? 100 THR   BBB C   1 ? 
ATOM   2790 O  O   . THR   B 1 101 ? 10.253  28.948 61.001 1.000 34.654  ? 100 THR   BBB O   1 ? 
ATOM   2791 C  CB  . THR   B 1 101 ? 7.999   26.477 60.534 1.000 36.254  ? 100 THR   BBB CB  1 ? 
ATOM   2792 O  OG1 . THR   B 1 101 ? 8.989   26.178 61.515 1.000 44.107  ? 100 THR   BBB OG1 1 ? 
ATOM   2793 C  CG2 . THR   B 1 101 ? 7.780   25.275 59.633 1.000 41.362  ? 100 THR   BBB CG2 1 ? 
ATOM   2794 N  N   . ASN   B 1 102 ? 8.109   29.376 61.661 1.000 39.724  ? 101 ASN   BBB N   1 ? 
ATOM   2795 C  CA  . ASN   B 1 102 ? 8.537   30.297 62.760 1.000 43.688  ? 101 ASN   BBB CA  1 ? 
ATOM   2796 C  C   . ASN   B 1 102 ? 9.182   29.506 63.928 1.000 43.307  ? 101 ASN   BBB C   1 ? 
ATOM   2797 O  O   . ASN   B 1 102 ? 9.800   30.130 64.780 1.000 63.634  ? 101 ASN   BBB O   1 ? 
ATOM   2798 C  CB  . ASN   B 1 102 ? 7.375   31.174 63.232 1.000 44.482  ? 101 ASN   BBB CB  1 ? 
ATOM   2799 C  CG  . ASN   B 1 102 ? 6.689   31.945 62.123 1.000 38.846  ? 101 ASN   BBB CG  1 ? 
ATOM   2800 O  OD1 . ASN   B 1 102 ? 7.258   32.245 61.071 1.000 41.860  ? 101 ASN   BBB OD1 1 ? 
ATOM   2801 N  ND2 . ASN   B 1 102 ? 5.437   32.268 62.347 1.000 41.397  ? 101 ASN   BBB ND2 1 ? 
ATOM   2802 N  N   . GLU   B 1 103 ? 9.117   28.170 63.931 1.000 41.925  ? 102 GLU   BBB N   1 ? 
ATOM   2803 C  CA  . GLU   B 1 103 ? 9.594   27.315 65.074 1.000 56.241  ? 102 GLU   BBB CA  1 ? 
ATOM   2804 C  C   . GLU   B 1 103 ? 11.100  27.003 64.980 1.000 49.403  ? 102 GLU   BBB C   1 ? 
ATOM   2805 O  O   . GLU   B 1 103 ? 11.694  26.563 65.980 1.000 44.771  ? 102 GLU   BBB O   1 ? 
ATOM   2806 C  CB  . GLU   B 1 103 ? 8.784   26.016 65.138 1.000 59.128  ? 102 GLU   BBB CB  1 ? 
ATOM   2807 C  CG  . GLU   B 1 103 ? 7.394   26.203 65.742 1.000 74.745  ? 102 GLU   BBB CG  1 ? 
ATOM   2808 C  CD  . GLU   B 1 103 ? 6.466   27.186 65.034 1.000 71.634  ? 102 GLU   BBB CD  1 ? 
ATOM   2809 O  OE1 . GLU   B 1 103 ? 6.266   27.034 63.804 1.000 78.538  ? 102 GLU   BBB OE1 1 ? 
ATOM   2810 O  OE2 . GLU   B 1 103 ? 5.935   28.103 65.709 1.000 84.219  ? 102 GLU   BBB OE2 1 ? 
ATOM   2811 N  N   . HIS   B 1 104 ? 11.725  27.221 63.831 1.000 41.013  ? 103 HIS   BBB N   1 ? 
ATOM   2812 C  CA  . HIS   B 1 104 ? 13.114  26.761 63.566 1.000 52.643  ? 103 HIS   BBB CA  1 ? 
ATOM   2813 C  C   . HIS   B 1 104 ? 13.697  27.606 62.440 1.000 39.706  ? 103 HIS   BBB C   1 ? 
ATOM   2814 O  O   . HIS   B 1 104 ? 13.632  27.167 61.297 1.000 43.976  ? 103 HIS   BBB O   1 ? 
ATOM   2815 C  CB  . HIS   B 1 104 ? 13.153  25.251 63.220 1.000 69.762  ? 103 HIS   BBB CB  1 ? 
ATOM   2816 C  CG  . HIS   B 1 104 ? 12.980  24.894 61.765 1.000 107.867 ? 103 HIS   BBB CG  1 ? 
ATOM   2817 N  ND1 . HIS   B 1 104 ? 11.942  25.401 60.969 1.000 102.193 ? 103 HIS   BBB ND1 1 ? 
ATOM   2818 C  CD2 . HIS   B 1 104 ? 13.699  24.078 60.952 1.000 123.136 ? 103 HIS   BBB CD2 1 ? 
ATOM   2819 C  CE1 . HIS   B 1 104 ? 12.036  24.905 59.749 1.000 106.638 ? 103 HIS   BBB CE1 1 ? 
ATOM   2820 N  NE2 . HIS   B 1 104 ? 13.112  24.096 59.709 1.000 124.459 ? 103 HIS   BBB NE2 1 ? 
ATOM   2821 N  N   . GLY   B 1 105 ? 14.240  28.777 62.731 1.000 25.567  ? 104 GLY   BBB N   1 ? 
ATOM   2822 C  CA  . GLY   B 1 105 ? 14.882  29.584 61.679 1.000 28.926  ? 104 GLY   BBB CA  1 ? 
ATOM   2823 C  C   . GLY   B 1 105 ? 16.254  30.146 62.079 1.000 24.050  ? 104 GLY   BBB C   1 ? 
ATOM   2824 O  O   . GLY   B 1 105 ? 17.004  30.565 61.141 1.000 23.279  ? 104 GLY   BBB O   1 ? 
ATOM   2825 N  N   . SER   B 1 106 ? 16.618  30.127 63.367 1.000 21.446  ? 105 SER   BBB N   1 ? 
ATOM   2826 C  CA  . SER   B 1 106 ? 17.963  30.571 63.793 1.000 21.177  ? 105 SER   BBB CA  1 ? 
ATOM   2827 C  C   . SER   B 1 106 ? 19.023  29.568 63.319 1.000 22.267  ? 105 SER   BBB C   1 ? 
ATOM   2828 O  O   . SER   B 1 106 ? 18.700  28.380 62.891 1.000 24.623  ? 105 SER   BBB O   1 ? 
ATOM   2829 C  CB  . SER   B 1 106 ? 18.045  30.842 65.262 1.000 24.998  ? 105 SER   BBB CB  1 ? 
ATOM   2830 O  OG  . SER   B 1 106 ? 17.974  29.694 66.095 1.000 24.396  ? 105 SER   BBB OG  1 ? 
ATOM   2831 N  N   . GLU   B 1 107 ? 20.257  29.996 63.416 1.000 19.980  ? 106 GLU   BBB N   1 ? 
ATOM   2832 C  CA  . GLU   B 1 107 ? 21.442  29.155 63.157 1.000 22.365  ? 106 GLU   BBB CA  1 ? 
ATOM   2833 C  C   . GLU   B 1 107 ? 21.962  28.664 64.490 1.000 22.095  ? 106 GLU   BBB C   1 ? 
ATOM   2834 O  O   . GLU   B 1 107 ? 21.973  27.415 64.718 1.000 24.257  ? 106 GLU   BBB O   1 ? 
ATOM   2835 C  CB  . GLU   B 1 107 ? 22.459  29.898 62.303 1.000 21.523  ? 106 GLU   BBB CB  1 ? 
ATOM   2836 C  CG  . GLU   B 1 107 ? 21.948  30.123 60.893 1.000 22.861  ? 106 GLU   BBB CG  1 ? 
ATOM   2837 C  CD  . GLU   B 1 107 ? 22.999  30.192 59.817 1.000 21.900  ? 106 GLU   BBB CD  1 ? 
ATOM   2838 O  OE1 . GLU   B 1 107 ? 22.863  29.364 58.843 1.000 24.242  ? 106 GLU   BBB OE1 1 ? 
ATOM   2839 O  OE2 . GLU   B 1 107 ? 23.923  31.077 59.905 1.000 26.720  ? 106 GLU   BBB OE2 1 ? 
ATOM   2840 N  N   . HIS   B 1 108 ? 22.442  29.507 65.344 1.000 20.090  ? 107 HIS   BBB N   1 ? 
ATOM   2841 C  CA  . HIS   B 1 108 ? 22.862  29.147 66.709 1.000 21.021  ? 107 HIS   BBB CA  1 ? 
ATOM   2842 C  C   . HIS   B 1 108 ? 21.636  28.733 67.521 1.000 20.971  ? 107 HIS   BBB C   1 ? 
ATOM   2843 O  O   . HIS   B 1 108 ? 20.524  29.153 67.200 1.000 22.018  ? 107 HIS   BBB O   1 ? 
ATOM   2844 C  CB  . HIS   B 1 108 ? 23.635  30.287 67.369 1.000 23.430  ? 107 HIS   BBB CB  1 ? 
ATOM   2845 C  CG  . HIS   B 1 108 ? 24.933  30.502 66.732 1.000 20.311  ? 107 HIS   BBB CG  1 ? 
ATOM   2846 N  ND1 . HIS   B 1 108 ? 25.066  31.301 65.618 1.000 19.734  ? 107 HIS   BBB ND1 1 ? 
ATOM   2847 C  CD2 . HIS   B 1 108 ? 26.164  30.088 67.066 1.000 21.088  ? 107 HIS   BBB CD2 1 ? 
ATOM   2848 C  CE1 . HIS   B 1 108 ? 26.323  31.296 65.263 1.000 21.071  ? 107 HIS   BBB CE1 1 ? 
ATOM   2849 N  NE2 . HIS   B 1 108 ? 27.024  30.508 66.114 1.000 21.030  ? 107 HIS   BBB NE2 1 ? 
ATOM   2850 N  N   . THR   B 1 109 ? 21.829  27.798 68.454 1.000 23.480  ? 108 THR   BBB N   1 ? 
ATOM   2851 C  CA  . THR   B 1 109 ? 20.798  27.420 69.448 1.000 24.461  ? 108 THR   BBB CA  1 ? 
ATOM   2852 C  C   . THR   B 1 109 ? 21.407  27.621 70.832 1.000 29.917  ? 108 THR   BBB C   1 ? 
ATOM   2853 O  O   . THR   B 1 109 ? 22.603  27.651 70.927 1.000 31.319  ? 108 THR   BBB O   1 ? 
ATOM   2854 C  CB  . THR   B 1 109 ? 20.328  25.965 69.185 1.000 24.265  ? 108 THR   BBB CB  1 ? 
ATOM   2855 O  OG1 . THR   B 1 109 ? 21.506  25.181 69.408 1.000 27.194  ? 108 THR   BBB OG1 1 ? 
ATOM   2856 C  CG2 . THR   B 1 109 ? 19.742  25.866 67.788 1.000 25.751  ? 108 THR   BBB CG2 1 ? 
ATOM   2857 N  N   . VAL   B 1 110 ? 20.580  27.751 71.862 1.000 27.190  ? 109 VAL   BBB N   1 ? 
ATOM   2858 C  CA  . VAL   B 1 110 ? 20.973  27.907 73.299 1.000 28.545  ? 109 VAL   BBB CA  1 ? 
ATOM   2859 C  C   . VAL   B 1 110 ? 20.255  26.800 74.067 1.000 26.391  ? 109 VAL   BBB C   1 ? 
ATOM   2860 O  O   . VAL   B 1 110 ? 19.009  26.779 74.104 1.000 29.030  ? 109 VAL   BBB O   1 ? 
ATOM   2861 C  CB  . VAL   B 1 110 ? 20.639  29.321 73.847 1.000 27.445  ? 109 VAL   BBB CB  1 ? 
ATOM   2862 C  CG1 . VAL   B 1 110 ? 21.059  29.463 75.284 1.000 28.524  ? 109 VAL   BBB CG1 1 ? 
ATOM   2863 C  CG2 . VAL   B 1 110 ? 21.282  30.411 73.011 1.000 30.614  ? 109 VAL   BBB CG2 1 ? 
ATOM   2864 N  N   . ASP   B 1 111 ? 21.033  25.936 74.680 1.000 26.117  ? 110 ASP   BBB N   1 ? 
ATOM   2865 C  CA  . ASP   B 1 111 ? 20.510  24.709 75.337 1.000 27.251  ? 110 ASP   BBB CA  1 ? 
ATOM   2866 C  C   . ASP   B 1 111 ? 19.459  24.013 74.463 1.000 26.440  ? 110 ASP   BBB C   1 ? 
ATOM   2867 O  O   . ASP   B 1 111 ? 18.448  23.547 74.982 1.000 32.188  ? 110 ASP   BBB O   1 ? 
ATOM   2868 C  CB  . ASP   B 1 111 ? 19.904  25.065 76.685 1.000 30.164  ? 110 ASP   BBB CB  1 ? 
ATOM   2869 C  CG  . ASP   B 1 111 ? 20.928  25.606 77.636 1.000 34.183  ? 110 ASP   BBB CG  1 ? 
ATOM   2870 O  OD1 . ASP   B 1 111 ? 22.049  25.070 77.630 1.000 38.288  ? 110 ASP   BBB OD1 1 ? 
ATOM   2871 O  OD2 . ASP   B 1 111 ? 20.600  26.583 78.325 1.000 31.168  ? 110 ASP   BBB OD2 1 ? 
ATOM   2872 N  N   . GLY   B 1 112 ? 19.748  23.881 73.179 1.000 27.505  ? 111 GLY   BBB N   1 ? 
ATOM   2873 C  CA  . GLY   B 1 112 ? 18.924  23.116 72.227 1.000 32.105  ? 111 GLY   BBB CA  1 ? 
ATOM   2874 C  C   . GLY   B 1 112 ? 17.714  23.889 71.742 1.000 34.833  ? 111 GLY   BBB C   1 ? 
ATOM   2875 O  O   . GLY   B 1 112 ? 17.031  23.345 70.867 1.000 34.889  ? 111 GLY   BBB O   1 ? 
ATOM   2876 N  N   . VAL   B 1 113 ? 17.473  25.123 72.202 1.000 31.742  ? 112 VAL   BBB N   1 ? 
ATOM   2877 C  CA  . VAL   B 1 113 ? 16.265  25.909 71.800 1.000 30.801  ? 112 VAL   BBB CA  1 ? 
ATOM   2878 C  C   . VAL   B 1 113 ? 16.584  26.637 70.498 1.000 27.920  ? 112 VAL   BBB C   1 ? 
ATOM   2879 O  O   . VAL   B 1 113 ? 17.607  27.376 70.444 1.000 29.292  ? 112 VAL   BBB O   1 ? 
ATOM   2880 C  CB  . VAL   B 1 113 ? 15.807  26.868 72.903 1.000 33.936  ? 112 VAL   BBB CB  1 ? 
ATOM   2881 C  CG1 . VAL   B 1 113 ? 14.698  27.805 72.414 1.000 41.589  ? 112 VAL   BBB CG1 1 ? 
ATOM   2882 C  CG2 . VAL   B 1 113 ? 15.374  26.079 74.138 1.000 38.905  ? 112 VAL   BBB CG2 1 ? 
ATOM   2883 N  N   . LYS   B 1 114 ? 15.788  26.370 69.471 1.000 26.479  ? 113 LYS   BBB N   1 ? 
ATOM   2884 C  CA  . LYS   B 1 114 ? 15.914  27.071 68.176 1.000 30.083  ? 113 LYS   BBB CA  1 ? 
ATOM   2885 C  C   . LYS   B 1 114 ? 14.995  28.275 68.259 1.000 31.989  ? 113 LYS   BBB C   1 ? 
ATOM   2886 O  O   . LYS   B 1 114 ? 13.858  28.127 68.788 1.000 36.914  ? 113 LYS   BBB O   1 ? 
ATOM   2887 C  CB  . LYS   B 1 114 ? 15.501  26.210 66.977 1.000 37.237  ? 113 LYS   BBB CB  1 ? 
ATOM   2888 C  CG  . LYS   B 1 114 ? 16.251  24.913 66.868 1.000 39.744  ? 113 LYS   BBB CG  1 ? 
ATOM   2889 C  CD  . LYS   B 1 114 ? 15.398  23.670 66.701 1.000 42.608  ? 113 LYS   BBB CD  1 ? 
ATOM   2890 C  CE  . LYS   B 1 114 ? 16.218  22.413 66.882 1.000 67.487  ? 113 LYS   BBB CE  1 ? 
ATOM   2891 N  NZ  . LYS   B 1 114 ? 15.366  21.199 66.832 1.000 65.317  ? 113 LYS   BBB NZ  1 ? 
ATOM   2892 N  N   . TYR   B 1 115 ? 15.481  29.405 67.732 1.000 27.798  ? 114 TYR   BBB N   1 ? 
ATOM   2893 C  CA  . TYR   B 1 115 ? 14.718  30.667 67.647 1.000 27.291  ? 114 TYR   BBB CA  1 ? 
ATOM   2894 C  C   . TYR   B 1 115 ? 14.168  30.794 66.226 1.000 25.986  ? 114 TYR   BBB C   1 ? 
ATOM   2895 O  O   . TYR   B 1 115 ? 14.448  29.934 65.322 1.000 24.195  ? 114 TYR   BBB O   1 ? 
ATOM   2896 C  CB  . TYR   B 1 115 ? 15.643  31.802 68.121 1.000 25.377  ? 114 TYR   BBB CB  1 ? 
ATOM   2897 C  CG  . TYR   B 1 115 ? 15.719  31.947 69.618 1.000 27.297  ? 114 TYR   BBB CG  1 ? 
ATOM   2898 C  CD1 . TYR   B 1 115 ? 16.351  30.999 70.403 1.000 27.880  ? 114 TYR   BBB CD1 1 ? 
ATOM   2899 C  CD2 . TYR   B 1 115 ? 15.117  33.024 70.262 1.000 29.268  ? 114 TYR   BBB CD2 1 ? 
ATOM   2900 C  CE1 . TYR   B 1 115 ? 16.392  31.078 71.779 1.000 33.063  ? 114 TYR   BBB CE1 1 ? 
ATOM   2901 C  CE2 . TYR   B 1 115 ? 15.163  33.143 71.656 1.000 39.639  ? 114 TYR   BBB CE2 1 ? 
ATOM   2902 C  CZ  . TYR   B 1 115 ? 15.795  32.157 72.418 1.000 35.019  ? 114 TYR   BBB CZ  1 ? 
ATOM   2903 O  OH  . TYR   B 1 115 ? 15.866  32.207 73.777 1.000 34.495  ? 114 TYR   BBB OH  1 ? 
ATOM   2904 N  N   . SER   B 1 116 ? 13.379  31.832 65.990 1.000 24.736  ? 115 SER   BBB N   1 ? 
ATOM   2905 C  CA  . SER   B 1 116 ? 12.651  31.987 64.704 1.000 23.669  ? 115 SER   BBB CA  1 ? 
ATOM   2906 C  C   . SER   B 1 116 ? 13.585  32.495 63.588 1.000 24.344  ? 115 SER   BBB C   1 ? 
ATOM   2907 O  O   . SER   B 1 116 ? 13.290  32.273 62.428 1.000 25.052  ? 115 SER   BBB O   1 ? 
ATOM   2908 C  CB  . SER   B 1 116 ? 11.470  32.882 64.906 1.000 31.292  ? 115 SER   BBB CB  1 ? 
ATOM   2909 O  OG  . SER   B 1 116 ? 10.686  32.434 66.017 1.000 36.881  ? 115 SER   BBB OG  1 ? 
ATOM   2910 N  N   . ALA   B 1 117 ? 14.639  33.240 63.906 1.000 21.800  ? 116 ALA   BBB N   1 ? 
ATOM   2911 C  CA  . ALA   B 1 117 ? 15.518  33.814 62.875 1.000 21.739  ? 116 ALA   BBB CA  1 ? 
ATOM   2912 C  C   . ALA   B 1 117 ? 16.794  34.263 63.581 1.000 18.906  ? 116 ALA   BBB C   1 ? 
ATOM   2913 O  O   . ALA   B 1 117 ? 16.854  34.127 64.832 1.000 20.631  ? 116 ALA   BBB O   1 ? 
ATOM   2914 C  CB  . ALA   B 1 117 ? 14.789  34.926 62.133 1.000 22.848  ? 116 ALA   BBB CB  1 ? 
ATOM   2915 N  N   . GLU   B 1 118 ? 17.775  34.742 62.827 1.000 19.912  ? 117 GLU   BBB N   1 ? 
ATOM   2916 C  CA  . GLU   B 1 118 ? 19.058  35.259 63.389 1.000 17.801  ? 117 GLU   BBB CA  1 ? 
ATOM   2917 C  C   . GLU   B 1 118 ? 19.601  36.398 62.527 1.000 20.595  ? 117 GLU   BBB C   1 ? 
ATOM   2918 O  O   . GLU   B 1 118 ? 19.526  36.315 61.286 1.000 21.782  ? 117 GLU   BBB O   1 ? 
ATOM   2919 C  CB  . GLU   B 1 118 ? 19.988  34.072 63.517 1.000 23.245  ? 117 GLU   BBB CB  1 ? 
ATOM   2920 C  CG  . GLU   B 1 118 ? 21.223  34.316 64.353 1.000 24.008  ? 117 GLU   BBB CG  1 ? 
ATOM   2921 C  CD  . GLU   B 1 118 ? 22.023  33.069 64.588 1.000 19.040  ? 117 GLU   BBB CD  1 ? 
ATOM   2922 O  OE1 . GLU   B 1 118 ? 23.276  33.123 64.539 1.000 19.520  ? 117 GLU   BBB OE1 1 ? 
ATOM   2923 O  OE2 . GLU   B 1 118 ? 21.314  32.131 65.008 1.000 23.210  ? 117 GLU   BBB OE2 1 ? 
ATOM   2924 N  N   . LEU   B 1 119 ? 20.002  37.484 63.223 1.000 19.177  ? 118 LEU   BBB N   1 ? 
ATOM   2925 C  CA  . LEU   B 1 119 ? 20.736  38.582 62.567 1.000 17.651  ? 118 LEU   BBB CA  1 ? 
ATOM   2926 C  C   . LEU   B 1 119 ? 22.224  38.312 62.666 1.000 20.132  ? 118 LEU   BBB C   1 ? 
ATOM   2927 O  O   . LEU   B 1 119 ? 22.666  38.062 63.784 1.000 20.410  ? 118 LEU   BBB O   1 ? 
ATOM   2928 C  CB  . LEU   B 1 119 ? 20.332  39.838 63.349 1.000 18.239  ? 118 LEU   BBB CB  1 ? 
ATOM   2929 C  CG  . LEU   B 1 119 ? 21.154  41.095 63.090 1.000 18.134  ? 118 LEU   BBB CG  1 ? 
ATOM   2930 C  CD1 . LEU   B 1 119 ? 20.987  41.560 61.657 1.000 17.896  ? 118 LEU   BBB CD1 1 ? 
ATOM   2931 C  CD2 . LEU   B 1 119 ? 20.691  42.180 64.064 1.000 20.411  ? 118 LEU   BBB CD2 1 ? 
ATOM   2932 N  N   . HIS   B 1 120 ? 22.945  38.498 61.588 1.000 22.202  ? 119 HIS   BBB N   1 ? 
ATOM   2933 C  CA  . HIS   B 1 120 ? 24.421  38.503 61.528 1.000 17.739  ? 119 HIS   BBB CA  1 ? 
ATOM   2934 C  C   . HIS   B 1 120 ? 24.895  39.925 61.140 1.000 17.562  ? 119 HIS   BBB C   1 ? 
ATOM   2935 O  O   . HIS   B 1 120 ? 24.611  40.296 60.014 1.000 19.133  ? 119 HIS   BBB O   1 ? 
ATOM   2936 C  CB  . HIS   B 1 120 ? 24.948  37.507 60.525 1.000 17.176  ? 119 HIS   BBB CB  1 ? 
ATOM   2937 C  CG  . HIS   B 1 120 ? 24.700  36.127 61.071 1.000 17.921  ? 119 HIS   BBB CG  1 ? 
ATOM   2938 N  ND1 . HIS   B 1 120 ? 24.671  34.926 60.255 1.000 20.133  ? 119 HIS   BBB ND1 1 ? 
ATOM   2939 C  CD2 . HIS   B 1 120 ? 24.428  35.760 62.362 1.000 16.873  ? 119 HIS   BBB CD2 1 ? 
ATOM   2940 C  CE1 . HIS   B 1 120 ? 24.439  33.906 61.106 1.000 18.057  ? 119 HIS   BBB CE1 1 ? 
ATOM   2941 N  NE2 . HIS   B 1 120 ? 24.285  34.332 62.372 1.000 18.260  ? 119 HIS   BBB NE2 1 ? 
ATOM   2942 N  N   . VAL   B 1 121 ? 25.720  40.523 61.983 1.000 17.780  ? 120 VAL   BBB N   1 ? 
ATOM   2943 C  CA  . VAL   B 1 121 ? 26.413  41.815 61.645 1.000 15.771  ? 120 VAL   BBB CA  1 ? 
ATOM   2944 C  C   . VAL   B 1 121 ? 27.891  41.464 61.448 1.000 19.186  ? 120 VAL   BBB C   1 ? 
ATOM   2945 O  O   . VAL   B 1 121 ? 28.564  41.131 62.425 1.000 21.170  ? 120 VAL   BBB O   1 ? 
ATOM   2946 C  CB  . VAL   B 1 121 ? 26.165  42.798 62.770 1.000 18.328  ? 120 VAL   BBB CB  1 ? 
ATOM   2947 C  CG1 . VAL   B 1 121 ? 26.649  44.216 62.371 1.000 23.311  ? 120 VAL   BBB CG1 1 ? 
ATOM   2948 C  CG2 . VAL   B 1 121 ? 24.690  42.830 63.115 1.000 21.145  ? 120 VAL   BBB CG2 1 ? 
ATOM   2949 N  N   . ALA   B 1 122 ? 28.365  41.594 60.208 1.000 20.558  ? 121 ALA   BBB N   1 ? 
ATOM   2950 C  CA  . ALA   B 1 122 ? 29.670  41.067 59.733 1.000 20.277  ? 121 ALA   BBB CA  1 ? 
ATOM   2951 C  C   . ALA   B 1 122 ? 30.740  42.143 59.650 1.000 18.369  ? 121 ALA   BBB C   1 ? 
ATOM   2952 O  O   . ALA   B 1 122 ? 30.425  43.279 59.166 1.000 19.453  ? 121 ALA   BBB O   1 ? 
ATOM   2953 C  CB  . ALA   B 1 122 ? 29.478  40.390 58.389 1.000 22.192  ? 121 ALA   BBB CB  1 ? 
ATOM   2954 N  N   . HIS   B 1 123 ? 31.944  41.822 60.075 1.000 19.372  ? 122 HIS   BBB N   1 ? 
ATOM   2955 C  CA  . HIS   B 1 123 ? 33.092  42.776 60.154 1.000 19.724  ? 122 HIS   BBB CA  1 ? 
ATOM   2956 C  C   . HIS   B 1 123 ? 34.372  42.111 59.712 1.000 20.070  ? 122 HIS   BBB C   1 ? 
ATOM   2957 O  O   . HIS   B 1 123 ? 34.430  40.823 59.799 1.000 21.415  ? 122 HIS   BBB O   1 ? 
ATOM   2958 C  CB  . HIS   B 1 123 ? 33.313  43.254 61.573 1.000 19.103  ? 122 HIS   BBB CB  1 ? 
ATOM   2959 C  CG  . HIS   B 1 123 ? 32.097  43.650 62.300 1.000 19.332  ? 122 HIS   BBB CG  1 ? 
ATOM   2960 N  ND1 . HIS   B 1 123 ? 31.123  42.837 62.766 1.000 21.303  ? 122 HIS   BBB ND1 1 ? 
ATOM   2961 C  CD2 . HIS   B 1 123 ? 31.758  44.913 62.720 1.000 21.037  ? 122 HIS   BBB CD2 1 ? 
ATOM   2962 C  CE1 . HIS   B 1 123 ? 30.197  43.492 63.409 1.000 18.744  ? 122 HIS   BBB CE1 1 ? 
ATOM   2963 N  NE2 . HIS   B 1 123 ? 30.580  44.862 63.392 1.000 18.271  ? 122 HIS   BBB NE2 1 ? 
ATOM   2964 N  N   . TRP   B 1 124 ? 35.352  42.843 59.260 1.000 21.833  ? 123 TRP   BBB N   1 ? 
ATOM   2965 C  CA  . TRP   B 1 124 ? 36.686  42.276 58.892 1.000 22.884  ? 123 TRP   BBB CA  1 ? 
ATOM   2966 C  C   . TRP   B 1 124 ? 37.829  43.050 59.566 1.000 24.577  ? 123 TRP   BBB C   1 ? 
ATOM   2967 O  O   . TRP   B 1 124 ? 37.649  44.270 59.945 1.000 23.844  ? 123 TRP   BBB O   1 ? 
ATOM   2968 C  CB  . TRP   B 1 124 ? 36.872  42.110 57.375 1.000 21.123  ? 123 TRP   BBB CB  1 ? 
ATOM   2969 C  CG  . TRP   B 1 124 ? 36.880  43.377 56.574 1.000 21.952  ? 123 TRP   BBB CG  1 ? 
ATOM   2970 C  CD1 . TRP   B 1 124 ? 35.818  43.915 55.934 1.000 24.068  ? 123 TRP   BBB CD1 1 ? 
ATOM   2971 C  CD2 . TRP   B 1 124 ? 38.020  44.137 56.161 1.000 24.512  ? 123 TRP   BBB CD2 1 ? 
ATOM   2972 N  NE1 . TRP   B 1 124 ? 36.200  45.036 55.242 1.000 25.217  ? 123 TRP   BBB NE1 1 ? 
ATOM   2973 C  CE2 . TRP   B 1 124 ? 37.552  45.170 55.326 1.000 23.593  ? 123 TRP   BBB CE2 1 ? 
ATOM   2974 C  CE3 . TRP   B 1 124 ? 39.390  44.052 56.421 1.000 25.705  ? 123 TRP   BBB CE3 1 ? 
ATOM   2975 C  CZ2 . TRP   B 1 124 ? 38.399  46.147 54.794 1.000 27.496  ? 123 TRP   BBB CZ2 1 ? 
ATOM   2976 C  CZ3 . TRP   B 1 124 ? 40.232  45.004 55.881 1.000 32.981  ? 123 TRP   BBB CZ3 1 ? 
ATOM   2977 C  CH2 . TRP   B 1 124 ? 39.736  46.050 55.084 1.000 27.904  ? 123 TRP   BBB CH2 1 ? 
ATOM   2978 N  N   . ASN   B 1 125 ? 38.952  42.379 59.750 1.000 22.126  ? 124 ASN   BBB N   1 ? 
ATOM   2979 C  CA  . ASN   B 1 125 ? 40.090  42.857 60.560 1.000 25.035  ? 124 ASN   BBB CA  1 ? 
ATOM   2980 C  C   . ASN   B 1 125 ? 40.898  43.823 59.679 1.000 27.449  ? 124 ASN   BBB C   1 ? 
ATOM   2981 O  O   . ASN   B 1 125 ? 41.809  43.341 58.949 1.000 26.617  ? 124 ASN   BBB O   1 ? 
ATOM   2982 C  CB  . ASN   B 1 125 ? 40.913  41.682 61.071 1.000 25.042  ? 124 ASN   BBB CB  1 ? 
ATOM   2983 C  CG  . ASN   B 1 125 ? 41.989  42.043 62.068 1.000 29.753  ? 124 ASN   BBB CG  1 ? 
ATOM   2984 O  OD1 . ASN   B 1 125 ? 42.439  41.178 62.842 1.000 34.094  ? 124 ASN   BBB OD1 1 ? 
ATOM   2985 N  ND2 . ASN   B 1 125 ? 42.422  43.297 62.062 1.000 26.385  ? 124 ASN   BBB ND2 1 ? 
ATOM   2986 N  N   . SER   B 1 126 ? 40.591  45.140 59.745 1.000 28.041  ? 125 SER   BBB N   1 ? 
ATOM   2987 C  CA  . SER   B 1 126 ? 41.267  46.163 58.926 1.000 34.043  ? 125 SER   BBB CA  1 ? 
ATOM   2988 C  C   . SER   B 1 126 ? 42.590  46.565 59.581 1.000 32.793  ? 125 SER   BBB C   1 ? 
ATOM   2989 O  O   . SER   B 1 126 ? 43.366  47.282 58.924 1.000 35.836  ? 125 SER   BBB O   1 ? 
ATOM   2990 C  CB  . SER   B 1 126 ? 40.378  47.358 58.682 1.000 30.206  ? 125 SER   BBB CB  1 ? 
ATOM   2991 O  OG  . SER   B 1 126 ? 39.823  47.830 59.894 1.000 29.564  ? 125 SER   BBB OG  1 ? 
ATOM   2992 N  N   . ALA   B 1 127 ? 42.852  46.165 60.822 1.000 35.352  ? 126 ALA   BBB N   1 ? 
ATOM   2993 C  CA  . ALA   B 1 127 ? 44.162  46.422 61.466 1.000 39.603  ? 126 ALA   BBB CA  1 ? 
ATOM   2994 C  C   . ALA   B 1 127 ? 45.228  45.540 60.803 1.000 38.134  ? 126 ALA   BBB C   1 ? 
ATOM   2995 O  O   . ALA   B 1 127 ? 46.371  45.954 60.781 1.000 43.536  ? 126 ALA   BBB O   1 ? 
ATOM   2996 C  CB  . ALA   B 1 127 ? 44.087  46.174 62.952 1.000 38.435  ? 126 ALA   BBB CB  1 ? 
ATOM   2997 N  N   . LYS   B 1 128 ? 44.859  44.353 60.303 1.000 42.684  ? 127 LYS   BBB N   1 ? 
ATOM   2998 C  CA  . LYS   B 1 128 ? 45.849  43.330 59.849 1.000 46.597  ? 127 LYS   BBB CA  1 ? 
ATOM   2999 C  C   . LYS   B 1 128 ? 45.825  43.149 58.330 1.000 36.821  ? 127 LYS   BBB C   1 ? 
ATOM   3000 O  O   . LYS   B 1 128 ? 46.855  42.856 57.771 1.000 35.237  ? 127 LYS   BBB O   1 ? 
ATOM   3001 C  CB  . LYS   B 1 128 ? 45.572  42.005 60.560 1.000 48.167  ? 127 LYS   BBB CB  1 ? 
ATOM   3002 C  CG  . LYS   B 1 128 ? 45.840  42.065 62.053 1.000 49.140  ? 127 LYS   BBB CG  1 ? 
ATOM   3003 C  CD  . LYS   B 1 128 ? 47.047  41.314 62.436 1.000 56.963  ? 127 LYS   BBB CD  1 ? 
ATOM   3004 C  CE  . LYS   B 1 128 ? 46.937  39.883 61.960 1.000 61.494  ? 127 LYS   BBB CE  1 ? 
ATOM   3005 N  NZ  . LYS   B 1 128 ? 47.481  38.935 62.954 1.000 67.085  ? 127 LYS   BBB NZ  1 ? 
ATOM   3006 N  N   . TYR   B 1 129 ? 44.670  43.271 57.696 1.000 33.159  ? 128 TYR   BBB N   1 ? 
ATOM   3007 C  CA  . TYR   B 1 129 ? 44.481  42.904 56.275 1.000 38.286  ? 128 TYR   BBB CA  1 ? 
ATOM   3008 C  C   . TYR   B 1 129 ? 44.034  44.148 55.519 1.000 36.862  ? 128 TYR   BBB C   1 ? 
ATOM   3009 O  O   . TYR   B 1 129 ? 43.663  45.120 56.198 1.000 35.874  ? 128 TYR   BBB O   1 ? 
ATOM   3010 C  CB  . TYR   B 1 129 ? 43.546  41.703 56.198 1.000 37.600  ? 128 TYR   BBB CB  1 ? 
ATOM   3011 C  CG  . TYR   B 1 129 ? 44.055  40.601 57.091 1.000 35.633  ? 128 TYR   BBB CG  1 ? 
ATOM   3012 C  CD1 . TYR   B 1 129 ? 45.360  40.177 56.992 1.000 43.292  ? 128 TYR   BBB CD1 1 ? 
ATOM   3013 C  CD2 . TYR   B 1 129 ? 43.287  40.092 58.117 1.000 37.079  ? 128 TYR   BBB CD2 1 ? 
ATOM   3014 C  CE1 . TYR   B 1 129 ? 45.869  39.198 57.823 1.000 41.928  ? 128 TYR   BBB CE1 1 ? 
ATOM   3015 C  CE2 . TYR   B 1 129 ? 43.779  39.116 58.962 1.000 41.188  ? 128 TYR   BBB CE2 1 ? 
ATOM   3016 C  CZ  . TYR   B 1 129 ? 45.078  38.673 58.827 1.000 41.462  ? 128 TYR   BBB CZ  1 ? 
ATOM   3017 O  OH  . TYR   B 1 129 ? 45.554  37.693 59.649 1.000 38.992  ? 128 TYR   BBB OH  1 ? 
ATOM   3018 N  N   . SER   B 1 130 ? 44.118  44.113 54.186 1.000 35.655  ? 129 SER   BBB N   1 ? 
ATOM   3019 C  CA  . SER   B 1 130 ? 43.889  45.306 53.328 1.000 39.976  ? 129 SER   BBB CA  1 ? 
ATOM   3020 C  C   . SER   B 1 130 ? 42.464  45.332 52.813 1.000 36.403  ? 129 SER   BBB C   1 ? 
ATOM   3021 O  O   . SER   B 1 130 ? 42.044  46.352 52.355 1.000 35.131  ? 129 SER   BBB O   1 ? 
ATOM   3022 C  CB  . SER   B 1 130 ? 44.841  45.328 52.180 1.000 45.917  ? 129 SER   BBB CB  1 ? 
ATOM   3023 O  OG  . SER   B 1 130 ? 46.131  45.530 52.686 1.000 45.361  ? 129 SER   BBB OG  1 ? 
ATOM   3024 N  N   . SER   B 1 131 ? 41.803  44.183 52.779 1.000 31.988  ? 130 SER   BBB N   1 ? 
ATOM   3025 C  CA  . SER   B 1 131 ? 40.488  44.045 52.130 1.000 28.890  ? 130 SER   BBB CA  1 ? 
ATOM   3026 C  C   . SER   B 1 131 ? 39.733  42.937 52.836 1.000 25.197  ? 130 SER   BBB C   1 ? 
ATOM   3027 O  O   . SER   B 1 131 ? 40.398  42.122 53.528 1.000 31.071  ? 130 SER   BBB O   1 ? 
ATOM   3028 C  CB  . SER   B 1 131 ? 40.652  43.770 50.649 1.000 27.573  ? 130 SER   BBB CB  1 ? 
ATOM   3029 O  OG  . SER   B 1 131 ? 41.170  42.459 50.455 1.000 32.123  ? 130 SER   BBB OG  1 ? 
ATOM   3030 N  N   . LEU   B 1 132 ? 38.425  42.926 52.642 1.000 26.653  ? 131 LEU   BBB N   1 ? 
ATOM   3031 C  CA  . LEU   B 1 132 ? 37.555  41.786 52.999 1.000 24.940  ? 131 LEU   BBB CA  1 ? 
ATOM   3032 C  C   . LEU   B 1 132 ? 38.137  40.534 52.340 1.000 24.501  ? 131 LEU   BBB C   1 ? 
ATOM   3033 O  O   . LEU   B 1 132 ? 38.232  39.461 53.028 1.000 29.084  ? 131 LEU   BBB O   1 ? 
ATOM   3034 C  CB  . LEU   B 1 132 ? 36.123  42.037 52.507 1.000 27.872  ? 131 LEU   BBB CB  1 ? 
ATOM   3035 C  CG  . LEU   B 1 132 ? 35.131  40.889 52.741 1.000 28.240  ? 131 LEU   BBB CG  1 ? 
ATOM   3036 C  CD1 . LEU   B 1 132 ? 35.113  40.414 54.183 1.000 23.954  ? 131 LEU   BBB CD1 1 ? 
ATOM   3037 C  CD2 . LEU   B 1 132 ? 33.734  41.259 52.304 1.000 31.381  ? 131 LEU   BBB CD2 1 ? 
ATOM   3038 N  N   . ALA   B 1 133 ? 38.422  40.641 51.049 1.000 27.067  ? 132 ALA   BBB N   1 ? 
ATOM   3039 C  CA  . ALA   B 1 133 ? 38.819  39.502 50.197 1.000 30.886  ? 132 ALA   BBB CA  1 ? 
ATOM   3040 C  C   . ALA   B 1 133 ? 40.006  38.858 50.896 1.000 28.343  ? 132 ALA   BBB C   1 ? 
ATOM   3041 O  O   . ALA   B 1 133 ? 39.997  37.570 50.970 1.000 30.561  ? 132 ALA   BBB O   1 ? 
ATOM   3042 C  CB  . ALA   B 1 133 ? 39.139  39.907 48.755 1.000 32.941  ? 132 ALA   BBB CB  1 ? 
ATOM   3043 N  N   . GLU   B 1 134 ? 40.986  39.654 51.339 1.000 29.688  ? 133 GLU   BBB N   1 ? 
ATOM   3044 C  CA  . GLU   B 1 134 ? 42.201  39.127 52.012 1.000 32.215  ? 133 GLU   BBB CA  1 ? 
ATOM   3045 C  C   . GLU   B 1 134 ? 41.818  38.497 53.346 1.000 31.132  ? 133 GLU   BBB C   1 ? 
ATOM   3046 O  O   . GLU   B 1 134 ? 42.197  37.298 53.573 1.000 35.099  ? 133 GLU   BBB O   1 ? 
ATOM   3047 C  CB  . GLU   B 1 134 ? 43.252  40.206 52.243 1.000 33.510  ? 133 GLU   BBB CB  1 ? 
ATOM   3048 C  CG  . GLU   B 1 134 ? 44.526  39.651 52.854 1.000 37.802  ? 133 GLU   BBB CG  1 ? 
ATOM   3049 C  CD  . GLU   B 1 134 ? 45.683  40.606 53.068 1.000 39.618  ? 133 GLU   BBB CD  1 ? 
ATOM   3050 O  OE1 . GLU   B 1 134 ? 46.782  40.081 53.372 1.000 36.642  ? 133 GLU   BBB OE1 1 ? 
ATOM   3051 O  OE2 . GLU   B 1 134 ? 45.499  41.858 52.947 1.000 40.544  ? 133 GLU   BBB OE2 1 ? 
ATOM   3052 N  N   . ALA   B 1 135 ? 41.048  39.214 54.157 1.000 28.616  ? 134 ALA   BBB N   1 ? 
ATOM   3053 C  CA  . ALA   B 1 135 ? 40.748  38.875 55.561 1.000 29.422  ? 134 ALA   BBB CA  1 ? 
ATOM   3054 C  C   . ALA   B 1 135 ? 39.920  37.581 55.635 1.000 26.762  ? 134 ALA   BBB C   1 ? 
ATOM   3055 O  O   . ALA   B 1 135 ? 39.998  36.920 56.693 1.000 30.134  ? 134 ALA   BBB O   1 ? 
ATOM   3056 C  CB  . ALA   B 1 135 ? 40.045  40.039 56.234 1.000 30.455  ? 134 ALA   BBB CB  1 ? 
ATOM   3057 N  N   . ALA   B 1 136 ? 39.154  37.232 54.593 1.000 24.246  ? 135 ALA   BBB N   1 ? 
ATOM   3058 C  CA  . ALA   B 1 136 ? 38.025  36.286 54.706 1.000 27.145  ? 135 ALA   BBB CA  1 ? 
ATOM   3059 C  C   . ALA   B 1 136 ? 38.552  34.876 54.977 1.000 27.527  ? 135 ALA   BBB C   1 ? 
ATOM   3060 O  O   . ALA   B 1 136 ? 37.787  34.075 55.533 1.000 28.499  ? 135 ALA   BBB O   1 ? 
ATOM   3061 C  CB  . ALA   B 1 136 ? 37.178  36.306 53.469 1.000 30.677  ? 135 ALA   BBB CB  1 ? 
ATOM   3062 N  N   . SER   B 1 137 ? 39.808  34.619 54.633 1.000 27.364  ? 136 SER   BBB N   1 ? 
ATOM   3063 C  CA  . SER   B 1 137 ? 40.379  33.254 54.706 1.000 30.809  ? 136 SER   BBB CA  1 ? 
ATOM   3064 C  C   . SER   B 1 137 ? 41.319  33.127 55.908 1.000 34.280  ? 136 SER   BBB C   1 ? 
ATOM   3065 O  O   . SER   B 1 137 ? 41.836  32.078 56.080 1.000 34.344  ? 136 SER   BBB O   1 ? 
ATOM   3066 C  CB  . SER   B 1 137 ? 41.067  32.867 53.421 1.000 30.828  ? 136 SER   BBB CB  1 ? 
ATOM   3067 O  OG  . SER   B 1 137 ? 42.117  33.796 53.111 1.000 38.672  ? 136 SER   BBB OG  1 ? 
ATOM   3068 N  N   . LYS   B 1 138 ? 41.422  34.125 56.773 1.000 32.281  ? 137 LYS   BBB N   1 ? 
ATOM   3069 C  CA  . LYS   B 1 138 ? 42.426  34.195 57.873 1.000 33.950  ? 137 LYS   BBB CA  1 ? 
ATOM   3070 C  C   . LYS   B 1 138 ? 41.740  33.881 59.195 1.000 29.707  ? 137 LYS   BBB C   1 ? 
ATOM   3071 O  O   . LYS   B 1 138 ? 40.651  34.355 59.380 1.000 29.139  ? 137 LYS   BBB O   1 ? 
ATOM   3072 C  CB  . LYS   B 1 138 ? 43.031  35.602 57.952 1.000 33.141  ? 137 LYS   BBB CB  1 ? 
ATOM   3073 C  CG  . LYS   B 1 138 ? 43.807  36.062 56.720 1.000 48.006  ? 137 LYS   BBB CG  1 ? 
ATOM   3074 C  CD  . LYS   B 1 138 ? 44.848  35.056 56.212 1.000 54.916  ? 137 LYS   BBB CD  1 ? 
ATOM   3075 C  CE  . LYS   B 1 138 ? 46.042  35.671 55.508 1.000 66.028  ? 137 LYS   BBB CE  1 ? 
ATOM   3076 N  NZ  . LYS   B 1 138 ? 45.627  36.491 54.353 1.000 68.823  ? 137 LYS   BBB NZ  1 ? 
ATOM   3077 N  N   . ALA   B 1 139 ? 42.320  33.009 60.032 1.000 27.428  ? 138 ALA   BBB N   1 ? 
ATOM   3078 C  CA  . ALA   B 1 139 ? 41.745  32.626 61.351 1.000 32.337  ? 138 ALA   BBB CA  1 ? 
ATOM   3079 C  C   . ALA   B 1 139 ? 41.194  33.844 62.111 1.000 26.484  ? 138 ALA   BBB C   1 ? 
ATOM   3080 O  O   . ALA   B 1 139 ? 40.126  33.696 62.707 1.000 27.342  ? 138 ALA   BBB O   1 ? 
ATOM   3081 C  CB  . ALA   B 1 139 ? 42.743  31.877 62.214 1.000 36.471  ? 138 ALA   BBB CB  1 ? 
ATOM   3082 N  N   . ASP   B 1 140 ? 41.904  34.985 62.091 1.000 31.611  ? 139 ASP   BBB N   1 ? 
ATOM   3083 C  CA  . ASP   B 1 140 ? 41.584  36.216 62.870 1.000 28.572  ? 139 ASP   BBB CA  1 ? 
ATOM   3084 C  C   . ASP   B 1 140 ? 40.945  37.282 61.943 1.000 28.648  ? 139 ASP   BBB C   1 ? 
ATOM   3085 O  O   . ASP   B 1 140 ? 40.968  38.518 62.308 1.000 32.034  ? 139 ASP   BBB O   1 ? 
ATOM   3086 C  CB  . ASP   B 1 140 ? 42.849  36.736 63.567 1.000 32.165  ? 139 ASP   BBB CB  1 ? 
ATOM   3087 C  CG  . ASP   B 1 140 ? 44.004  37.124 62.648 1.000 35.180  ? 139 ASP   BBB CG  1 ? 
ATOM   3088 O  OD1 . ASP   B 1 140 ? 43.890  36.875 61.435 1.000 37.360  ? 139 ASP   BBB OD1 1 ? 
ATOM   3089 O  OD2 . ASP   B 1 140 ? 45.045  37.611 63.151 1.000 37.929  ? 139 ASP   BBB OD2 1 ? 
ATOM   3090 N  N   . GLY   B 1 141 ? 40.453  36.867 60.761 1.000 26.656  ? 140 GLY   BBB N   1 ? 
ATOM   3091 C  CA  . GLY   B 1 141 ? 40.031  37.762 59.660 1.000 27.322  ? 140 GLY   BBB CA  1 ? 
ATOM   3092 C  C   . GLY   B 1 141 ? 38.690  38.449 59.892 1.000 25.850  ? 140 GLY   BBB C   1 ? 
ATOM   3093 O  O   . GLY   B 1 141 ? 38.518  39.699 59.483 1.000 26.092  ? 140 GLY   BBB O   1 ? 
ATOM   3094 N  N   . LEU   B 1 142 ? 37.755  37.715 60.497 1.000 22.222  ? 141 LEU   BBB N   1 ? 
ATOM   3095 C  CA  . LEU   B 1 142 ? 36.313  38.029 60.489 1.000 19.999  ? 141 LEU   BBB CA  1 ? 
ATOM   3096 C  C   . LEU   B 1 142 ? 35.738  37.980 61.905 1.000 23.348  ? 141 LEU   BBB C   1 ? 
ATOM   3097 O  O   . LEU   B 1 142 ? 36.269  37.272 62.776 1.000 22.993  ? 141 LEU   BBB O   1 ? 
ATOM   3098 C  CB  . LEU   B 1 142 ? 35.558  37.091 59.562 1.000 23.722  ? 141 LEU   BBB CB  1 ? 
ATOM   3099 C  CG  . LEU   B 1 142 ? 35.960  37.099 58.083 1.000 20.557  ? 141 LEU   BBB CG  1 ? 
ATOM   3100 C  CD1 . LEU   B 1 142 ? 35.034  36.210 57.271 1.000 24.799  ? 141 LEU   BBB CD1 1 ? 
ATOM   3101 C  CD2 . LEU   B 1 142 ? 35.990  38.522 57.522 1.000 22.764  ? 141 LEU   BBB CD2 1 ? 
ATOM   3102 N  N   . ALA   B 1 143 ? 34.668  38.739 62.113 1.000 19.706  ? 142 ALA   BBB N   1 ? 
ATOM   3103 C  CA  . ALA   B 1 143 ? 33.917  38.810 63.369 1.000 18.630  ? 142 ALA   BBB CA  1 ? 
ATOM   3104 C  C   . ALA   B 1 143 ? 32.457  39.009 62.957 1.000 20.395  ? 142 ALA   BBB C   1 ? 
ATOM   3105 O  O   . ALA   B 1 143 ? 32.158  39.872 62.069 1.000 21.186  ? 142 ALA   BBB O   1 ? 
ATOM   3106 C  CB  . ALA   B 1 143 ? 34.412  39.969 64.260 1.000 20.979  ? 142 ALA   BBB CB  1 ? 
ATOM   3107 N  N   . VAL   B 1 144 ? 31.577  38.322 63.649 1.000 19.785  ? 143 VAL   BBB N   1 ? 
ATOM   3108 C  CA  . VAL   B 1 144 ? 30.129  38.360 63.421 1.000 19.094  ? 143 VAL   BBB CA  1 ? 
ATOM   3109 C  C   . VAL   B 1 144 ? 29.442  38.464 64.777 1.000 20.637  ? 143 VAL   BBB C   1 ? 
ATOM   3110 O  O   . VAL   B 1 144 ? 29.771  37.737 65.685 1.000 20.206  ? 143 VAL   BBB O   1 ? 
ATOM   3111 C  CB  . VAL   B 1 144 ? 29.560  37.164 62.658 1.000 19.942  ? 143 VAL   BBB CB  1 ? 
ATOM   3112 C  CG1 . VAL   B 1 144 ? 28.052  37.319 62.545 1.000 24.035  ? 143 VAL   BBB CG1 1 ? 
ATOM   3113 C  CG2 . VAL   B 1 144 ? 30.191  37.032 61.296 1.000 21.894  ? 143 VAL   BBB CG2 1 ? 
ATOM   3114 N  N   . ILE   B 1 145 ? 28.647  39.527 64.967 1.000 24.319  ? 144 ILE   BBB N   1 ? 
ATOM   3115 C  CA  . ILE   B 1 145 ? 27.698  39.626 66.095 1.000 21.434  ? 144 ILE   BBB CA  1 ? 
ATOM   3116 C  C   . ILE   B 1 145 ? 26.399  38.971 65.700 1.000 20.653  ? 144 ILE   BBB C   1 ? 
ATOM   3117 O  O   . ILE   B 1 145 ? 25.839  39.324 64.655 1.000 19.786  ? 144 ILE   BBB O   1 ? 
ATOM   3118 C  CB  . ILE   B 1 145 ? 27.423  41.114 66.449 1.000 19.523  ? 144 ILE   BBB CB  1 ? 
ATOM   3119 C  CG1 . ILE   B 1 145 ? 28.723  41.741 66.854 1.000 19.238  ? 144 ILE   BBB CG1 1 ? 
ATOM   3120 C  CG2 . ILE   B 1 145 ? 26.433  41.205 67.596 1.000 20.700  ? 144 ILE   BBB CG2 1 ? 
ATOM   3121 C  CD1 . ILE   B 1 145 ? 28.534  43.291 66.980 1.000 22.679  ? 144 ILE   BBB CD1 1 ? 
ATOM   3122 N  N   . GLY   B 1 146 ? 26.077  37.814 66.348 1.000 21.856  ? 145 GLY   BBB N   1 ? 
ATOM   3123 C  CA  . GLY   B 1 146 ? 24.752  37.291 66.099 1.000 23.492  ? 145 GLY   BBB CA  1 ? 
ATOM   3124 C  C   . GLY   B 1 146 ? 23.786  37.557 67.193 1.000 23.201  ? 145 GLY   BBB C   1 ? 
ATOM   3125 O  O   . GLY   B 1 146 ? 24.155  37.531 68.346 1.000 20.655  ? 145 GLY   BBB O   1 ? 
ATOM   3126 N  N   . VAL   B 1 147 ? 22.547  37.772 66.771 1.000 20.421  ? 146 VAL   BBB N   1 ? 
ATOM   3127 C  CA  . VAL   B 1 147 ? 21.380  38.039 67.636 1.000 20.441  ? 146 VAL   BBB CA  1 ? 
ATOM   3128 C  C   . VAL   B 1 147 ? 20.234  37.131 67.239 1.000 18.327  ? 146 VAL   BBB C   1 ? 
ATOM   3129 O  O   . VAL   B 1 147 ? 19.827  37.148 66.078 1.000 18.938  ? 146 VAL   BBB O   1 ? 
ATOM   3130 C  CB  . VAL   B 1 147 ? 20.919  39.523 67.502 1.000 20.376  ? 146 VAL   BBB CB  1 ? 
ATOM   3131 C  CG1 . VAL   B 1 147 ? 19.876  39.776 68.531 1.000 23.363  ? 146 VAL   BBB CG1 1 ? 
ATOM   3132 C  CG2 . VAL   B 1 147 ? 22.127  40.445 67.600 1.000 20.434  ? 146 VAL   BBB CG2 1 ? 
ATOM   3133 N  N   . LEU   B 1 148 ? 19.838  36.281 68.194 1.000 18.758  ? 147 LEU   BBB N   1 ? 
ATOM   3134 C  CA  . LEU   B 1 148 ? 18.644  35.451 68.082 1.000 20.437  ? 147 LEU   BBB CA  1 ? 
ATOM   3135 C  C   . LEU   B 1 148 ? 17.388  36.297 68.004 1.000 22.332  ? 147 LEU   BBB C   1 ? 
ATOM   3136 O  O   . LEU   B 1 148 ? 17.259  37.306 68.781 1.000 21.174  ? 147 LEU   BBB O   1 ? 
ATOM   3137 C  CB  . LEU   B 1 148 ? 18.662  34.496 69.277 1.000 22.118  ? 147 LEU   BBB CB  1 ? 
ATOM   3138 C  CG  . LEU   B 1 148 ? 19.924  33.650 69.320 1.000 25.379  ? 147 LEU   BBB CG  1 ? 
ATOM   3139 C  CD1 . LEU   B 1 148 ? 20.048  32.912 70.647 1.000 30.404  ? 147 LEU   BBB CD1 1 ? 
ATOM   3140 C  CD2 . LEU   B 1 148 ? 19.935  32.685 68.149 1.000 23.061  ? 147 LEU   BBB CD2 1 ? 
ATOM   3141 N  N   . MET   B 1 149 ? 16.510  35.915 67.093 1.000 21.283  ? 148 MET   BBB N   1 ? 
ATOM   3142 C  CA  . MET   B 1 149 ? 15.232  36.641 66.853 1.000 21.508  ? 148 MET   BBB CA  1 ? 
ATOM   3143 C  C   . MET   B 1 149 ? 14.069  35.735 67.274 1.000 21.547  ? 148 MET   BBB C   1 ? 
ATOM   3144 O  O   . MET   B 1 149 ? 13.929  34.661 66.694 1.000 23.863  ? 148 MET   BBB O   1 ? 
ATOM   3145 C  CB  . MET   B 1 149 ? 15.133  37.062 65.389 1.000 21.779  ? 148 MET   BBB CB  1 ? 
ATOM   3146 C  CG  . MET   B 1 149 ? 16.254  38.042 65.011 1.000 19.519  ? 148 MET   BBB CG  1 ? 
ATOM   3147 S  SD  . MET   B 1 149 ? 16.350  38.438 63.307 1.000 21.553  ? 148 MET   BBB SD  1 ? 
ATOM   3148 C  CE  . MET   B 1 149 ? 14.871  39.443 63.132 1.000 26.790  ? 148 MET   BBB CE  1 ? 
ATOM   3149 N  N   . LYS   B 1 150 ? 13.265  36.207 68.211 1.000 22.299  ? 149 LYS   BBB N   1 ? 
ATOM   3150 C  CA  . LYS   B 1 150 ? 12.146  35.473 68.847 1.000 21.948  ? 149 LYS   BBB CA  1 ? 
ATOM   3151 C  C   . LYS   B 1 150 ? 10.778  35.886 68.255 1.000 24.153  ? 149 LYS   BBB C   1 ? 
ATOM   3152 O  O   . LYS   B 1 150 ? 10.366  37.059 68.389 1.000 23.673  ? 149 LYS   BBB O   1 ? 
ATOM   3153 C  CB  . LYS   B 1 150 ? 12.211  35.648 70.363 1.000 26.897  ? 149 LYS   BBB CB  1 ? 
ATOM   3154 C  CG  . LYS   B 1 150 ? 11.205  34.799 71.130 1.000 34.111  ? 149 LYS   BBB CG  1 ? 
ATOM   3155 C  CD  . LYS   B 1 150 ? 11.237  34.944 72.627 1.000 37.209  ? 149 LYS   BBB CD  1 ? 
ATOM   3156 C  CE  . LYS   B 1 150 ? 10.009  34.335 73.274 1.000 50.373  ? 149 LYS   BBB CE  1 ? 
ATOM   3157 N  NZ  . LYS   B 1 150 ? 10.267  34.003 74.691 1.000 62.225  ? 149 LYS   BBB NZ  1 ? 
ATOM   3158 N  N   . VAL   B 1 151 ? 10.021  34.972 67.638 1.000 24.658  ? 150 VAL   BBB N   1 ? 
ATOM   3159 C  CA  . VAL   B 1 151 ? 8.692   35.339 67.050 1.000 24.151  ? 150 VAL   BBB CA  1 ? 
ATOM   3160 C  C   . VAL   B 1 151 ? 7.793   35.888 68.172 1.000 27.323  ? 150 VAL   BBB C   1 ? 
ATOM   3161 O  O   . VAL   B 1 151 ? 7.757   35.308 69.297 1.000 26.629  ? 150 VAL   BBB O   1 ? 
ATOM   3162 C  CB  . VAL   B 1 151 ? 8.029   34.211 66.230 1.000 28.513  ? 150 VAL   BBB CB  1 ? 
ATOM   3163 C  CG1 . VAL   B 1 151 ? 7.608   33.035 67.103 1.000 30.833  ? 150 VAL   BBB CG1 1 ? 
ATOM   3164 C  CG2 . VAL   B 1 151 ? 6.856   34.738 65.397 1.000 28.683  ? 150 VAL   BBB CG2 1 ? 
ATOM   3165 N  N   . GLY   B 1 152 ? 7.112   37.011 67.882 1.000 27.808  ? 151 GLY   BBB N   1 ? 
ATOM   3166 C  CA  . GLY   B 1 152 ? 6.237   37.740 68.810 1.000 26.648  ? 151 GLY   BBB CA  1 ? 
ATOM   3167 C  C   . GLY   B 1 152 ? 5.800   39.055 68.181 1.000 25.920  ? 151 GLY   BBB C   1 ? 
ATOM   3168 O  O   . GLY   B 1 152 ? 5.384   39.037 66.995 1.000 25.971  ? 151 GLY   BBB O   1 ? 
ATOM   3169 N  N   . GLU   B 1 153 ? 5.943   40.155 68.913 1.000 26.898  ? 152 GLU   BBB N   1 ? 
ATOM   3170 C  CA  . GLU   B 1 153 ? 5.565   41.524 68.432 1.000 30.597  ? 152 GLU   BBB CA  1 ? 
ATOM   3171 C  C   . GLU   B 1 153 ? 6.356   41.893 67.170 1.000 28.729  ? 152 GLU   BBB C   1 ? 
ATOM   3172 O  O   . GLU   B 1 153 ? 7.549   41.575 67.104 1.000 27.796  ? 152 GLU   BBB O   1 ? 
ATOM   3173 C  CB  . GLU   B 1 153 ? 5.903   42.638 69.437 1.000 37.398  ? 152 GLU   BBB CB  1 ? 
ATOM   3174 C  CG  . GLU   B 1 153 ? 5.533   42.364 70.876 1.000 51.594  ? 152 GLU   BBB CG  1 ? 
ATOM   3175 C  CD  . GLU   B 1 153 ? 4.074   42.542 71.236 1.000 63.097  ? 152 GLU   BBB CD  1 ? 
ATOM   3176 O  OE1 . GLU   B 1 153 ? 3.218   41.967 70.513 1.000 72.215  ? 152 GLU   BBB OE1 1 ? 
ATOM   3177 O  OE2 . GLU   B 1 153 ? 3.807   43.233 72.249 1.000 77.613  ? 152 GLU   BBB OE2 1 ? 
ATOM   3178 N  N   . ALA   B 1 154 ? 5.756   42.666 66.263 1.000 25.198  ? 153 ALA   BBB N   1 ? 
ATOM   3179 C  CA  . ALA   B 1 154 ? 6.492   43.313 65.143 1.000 28.779  ? 153 ALA   BBB CA  1 ? 
ATOM   3180 C  C   . ALA   B 1 154 ? 7.658   44.097 65.739 1.000 25.178  ? 153 ALA   BBB C   1 ? 
ATOM   3181 O  O   . ALA   B 1 154 ? 7.450   44.769 66.757 1.000 29.743  ? 153 ALA   BBB O   1 ? 
ATOM   3182 C  CB  . ALA   B 1 154 ? 5.593   44.241 64.320 1.000 28.476  ? 153 ALA   BBB CB  1 ? 
ATOM   3183 N  N   . ASN   B 1 155 ? 8.786   44.083 65.054 1.000 21.557  ? 154 ASN   BBB N   1 ? 
ATOM   3184 C  CA  . ASN   B 1 155 ? 10.015  44.844 65.388 1.000 25.948  ? 154 ASN   BBB CA  1 ? 
ATOM   3185 C  C   . ASN   B 1 155 ? 10.051  46.041 64.466 1.000 23.538  ? 154 ASN   BBB C   1 ? 
ATOM   3186 O  O   . ASN   B 1 155 ? 10.326  45.935 63.289 1.000 24.897  ? 154 ASN   BBB O   1 ? 
ATOM   3187 C  CB  . ASN   B 1 155 ? 11.297  44.014 65.282 1.000 27.740  ? 154 ASN   BBB CB  1 ? 
ATOM   3188 C  CG  . ASN   B 1 155 ? 12.514  44.700 65.850 1.000 24.391  ? 154 ASN   BBB CG  1 ? 
ATOM   3189 O  OD1 . ASN   B 1 155 ? 12.610  45.954 65.886 1.000 27.432  ? 154 ASN   BBB OD1 1 ? 
ATOM   3190 N  ND2 . ASN   B 1 155 ? 13.498  43.902 66.209 1.000 22.310  ? 154 ASN   BBB ND2 1 ? 
ATOM   3191 N  N   . PRO   B 1 156 ? 9.711   47.224 64.974 1.000 24.969  ? 155 PRO   BBB N   1 ? 
ATOM   3192 C  CA  . PRO   B 1 156 ? 9.702   48.405 64.104 1.000 25.850  ? 155 PRO   BBB CA  1 ? 
ATOM   3193 C  C   . PRO   B 1 156 ? 11.082  48.762 63.527 1.000 23.860  ? 155 PRO   BBB C   1 ? 
ATOM   3194 O  O   . PRO   B 1 156 ? 11.152  49.381 62.460 1.000 27.749  ? 155 PRO   BBB O   1 ? 
ATOM   3195 C  CB  . PRO   B 1 156 ? 9.164   49.502 65.022 1.000 28.556  ? 155 PRO   BBB CB  1 ? 
ATOM   3196 C  CG  . PRO   B 1 156 ? 9.409   49.001 66.445 1.000 31.648  ? 155 PRO   BBB CG  1 ? 
ATOM   3197 C  CD  . PRO   B 1 156 ? 9.392   47.476 66.378 1.000 25.313  ? 155 PRO   BBB CD  1 ? 
ATOM   3198 N  N   . LYS   B 1 157 ? 12.157  48.379 64.219 1.000 26.033  ? 156 LYS   BBB N   1 ? 
ATOM   3199 C  CA  . LYS   B 1 157 ? 13.540  48.688 63.771 1.000 23.276  ? 156 LYS   BBB CA  1 ? 
ATOM   3200 C  C   . LYS   B 1 157 ? 13.829  48.016 62.430 1.000 22.885  ? 156 LYS   BBB C   1 ? 
ATOM   3201 O  O   . LYS   B 1 157 ? 14.815  48.426 61.802 1.000 24.312  ? 156 LYS   BBB O   1 ? 
ATOM   3202 C  CB  . LYS   B 1 157 ? 14.600  48.326 64.809 1.000 28.620  ? 156 LYS   BBB CB  1 ? 
ATOM   3203 C  CG  . LYS   B 1 157 ? 14.380  48.839 66.232 1.000 39.671  ? 156 LYS   BBB CG  1 ? 
ATOM   3204 C  CD  . LYS   B 1 157 ? 14.901  50.220 66.539 1.000 46.402  ? 156 LYS   BBB CD  1 ? 
ATOM   3205 C  CE  . LYS   B 1 157 ? 14.917  50.490 68.037 1.000 54.452  ? 156 LYS   BBB CE  1 ? 
ATOM   3206 N  NZ  . LYS   B 1 157 ? 16.008  49.770 68.751 1.000 49.084  ? 156 LYS   BBB NZ  1 ? 
ATOM   3207 N  N   . LEU   B 1 158 ? 13.065  46.975 62.055 1.000 24.153  ? 157 LEU   BBB N   1 ? 
ATOM   3208 C  CA  . LEU   B 1 158 ? 13.225  46.254 60.764 1.000 23.954  ? 157 LEU   BBB CA  1 ? 
ATOM   3209 C  C   . LEU   B 1 158 ? 12.548  46.933 59.571 1.000 27.713  ? 157 LEU   BBB C   1 ? 
ATOM   3210 O  O   . LEU   B 1 158 ? 12.763  46.445 58.451 1.000 26.418  ? 157 LEU   BBB O   1 ? 
ATOM   3211 C  CB  . LEU   B 1 158 ? 12.662  44.829 60.907 1.000 24.178  ? 157 LEU   BBB CB  1 ? 
ATOM   3212 C  CG  . LEU   B 1 158 ? 13.364  43.912 61.871 1.000 25.275  ? 157 LEU   BBB CG  1 ? 
ATOM   3213 C  CD1 . LEU   B 1 158 ? 12.579  42.617 61.926 1.000 27.751  ? 157 LEU   BBB CD1 1 ? 
ATOM   3214 C  CD2 . LEU   B 1 158 ? 14.801  43.645 61.427 1.000 28.877  ? 157 LEU   BBB CD2 1 ? 
ATOM   3215 N  N   . GLN   B 1 159 ? 11.906  48.084 59.751 1.000 27.667  ? 158 GLN   BBB N   1 ? 
ATOM   3216 C  CA  . GLN   B 1 159 ? 10.918  48.609 58.778 1.000 28.834  ? 158 GLN   BBB CA  1 ? 
ATOM   3217 C  C   . GLN   B 1 159 ? 11.695  49.013 57.534 1.000 29.628  ? 158 GLN   BBB C   1 ? 
ATOM   3218 O  O   . GLN   B 1 159 ? 11.266  48.627 56.461 1.000 33.665  ? 158 GLN   BBB O   1 ? 
ATOM   3219 C  CB  . GLN   B 1 159 ? 10.065  49.708 59.429 1.000 32.953  ? 158 GLN   BBB CB  1 ? 
ATOM   3220 C  CG  . GLN   B 1 159 ? 9.312   50.623 58.474 1.000 42.477  ? 158 GLN   BBB CG  1 ? 
ATOM   3221 C  CD  . GLN   B 1 159 ? 8.092   50.006 57.838 1.000 65.187  ? 158 GLN   BBB CD  1 ? 
ATOM   3222 O  OE1 . GLN   B 1 159 ? 7.887   48.786 57.842 1.000 66.687  ? 158 GLN   BBB OE1 1 ? 
ATOM   3223 N  NE2 . GLN   B 1 159 ? 7.277   50.875 57.258 1.000 76.701  ? 158 GLN   BBB NE2 1 ? 
ATOM   3224 N  N   . LYS   B 1 160 ? 12.821  49.716 57.681 1.000 27.446  ? 159 LYS   BBB N   1 ? 
ATOM   3225 C  CA  . LYS   B 1 160 ? 13.546  50.226 56.503 1.000 28.274  ? 159 LYS   BBB CA  1 ? 
ATOM   3226 C  C   . LYS   B 1 160 ? 14.027  49.028 55.675 1.000 28.175  ? 159 LYS   BBB C   1 ? 
ATOM   3227 O  O   . LYS   B 1 160 ? 13.871  49.085 54.441 1.000 28.064  ? 159 LYS   BBB O   1 ? 
ATOM   3228 C  CB  . LYS   B 1 160 ? 14.680  51.168 56.893 1.000 35.359  ? 159 LYS   BBB CB  1 ? 
ATOM   3229 C  CG  . LYS   B 1 160 ? 15.313  51.905 55.721 1.000 38.775  ? 159 LYS   BBB CG  1 ? 
ATOM   3230 C  CD  . LYS   B 1 160 ? 16.661  52.527 56.081 1.000 43.405  ? 159 LYS   BBB CD  1 ? 
ATOM   3231 C  CE  . LYS   B 1 160 ? 17.516  52.876 54.876 1.000 40.362  ? 159 LYS   BBB CE  1 ? 
ATOM   3232 N  NZ  . LYS   B 1 160 ? 17.111  54.156 54.298 1.000 45.971  ? 159 LYS   BBB NZ  1 ? 
ATOM   3233 N  N   . VAL   B 1 161 ? 14.535  47.971 56.331 1.000 23.159  ? 160 VAL   BBB N   1 ? 
ATOM   3234 C  CA  . VAL   B 1 161 ? 15.038  46.772 55.615 1.000 27.173  ? 160 VAL   BBB CA  1 ? 
ATOM   3235 C  C   . VAL   B 1 161 ? 13.859  46.175 54.859 1.000 25.004  ? 160 VAL   BBB C   1 ? 
ATOM   3236 O  O   . VAL   B 1 161 ? 13.978  45.906 53.654 1.000 26.642  ? 160 VAL   BBB O   1 ? 
ATOM   3237 C  CB  . VAL   B 1 161 ? 15.679  45.770 56.589 1.000 27.146  ? 160 VAL   BBB CB  1 ? 
ATOM   3238 C  CG1 . VAL   B 1 161 ? 16.001  44.483 55.886 1.000 32.075  ? 160 VAL   BBB CG1 1 ? 
ATOM   3239 C  CG2 . VAL   B 1 161 ? 16.911  46.330 57.227 1.000 28.295  ? 160 VAL   BBB CG2 1 ? 
ATOM   3240 N  N   . LEU   B 1 162 ? 12.748  45.963 55.548 1.000 24.614  ? 161 LEU   BBB N   1 ? 
ATOM   3241 C  CA  . LEU   B 1 162 ? 11.599  45.225 54.939 1.000 28.817  ? 161 LEU   BBB CA  1 ? 
ATOM   3242 C  C   . LEU   B 1 162 ? 11.018  46.045 53.772 1.000 25.353  ? 161 LEU   BBB C   1 ? 
ATOM   3243 O  O   . LEU   B 1 162 ? 10.653  45.459 52.762 1.000 28.412  ? 161 LEU   BBB O   1 ? 
ATOM   3244 C  CB  . LEU   B 1 162 ? 10.562  44.911 56.021 1.000 26.367  ? 161 LEU   BBB CB  1 ? 
ATOM   3245 C  CG  . LEU   B 1 162 ? 11.026  43.931 57.097 1.000 29.794  ? 161 LEU   BBB CG  1 ? 
ATOM   3246 C  CD1 . LEU   B 1 162 ? 10.067  43.899 58.287 1.000 34.014  ? 161 LEU   BBB CD1 1 ? 
ATOM   3247 C  CD2 . LEU   B 1 162 ? 11.151  42.553 56.497 1.000 40.123  ? 161 LEU   BBB CD2 1 ? 
ATOM   3248 N  N   . ASP   B 1 163 ? 10.926  47.374 53.922 1.000 26.210  ? 162 ASP   BBB N   1 ? 
ATOM   3249 C  CA  . ASP   B 1 163 ? 10.404  48.304 52.875 1.000 24.725  ? 162 ASP   BBB CA  1 ? 
ATOM   3250 C  C   . ASP   B 1 163 ? 11.264  48.248 51.607 1.000 22.154  ? 162 ASP   BBB C   1 ? 
ATOM   3251 O  O   . ASP   B 1 163 ? 10.726  48.455 50.543 1.000 29.393  ? 162 ASP   BBB O   1 ? 
ATOM   3252 C  CB  . ASP   B 1 163 ? 10.365  49.725 53.439 1.000 28.117  ? 162 ASP   BBB CB  1 ? 
ATOM   3253 C  CG  . ASP   B 1 163 ? 9.200   49.961 54.372 1.000 34.354  ? 162 ASP   BBB CG  1 ? 
ATOM   3254 O  OD1 . ASP   B 1 163 ? 8.330   49.060 54.471 1.000 36.694  ? 162 ASP   BBB OD1 1 ? 
ATOM   3255 O  OD2 . ASP   B 1 163 ? 9.124   51.084 54.935 1.000 35.083  ? 162 ASP   BBB OD2 1 ? 
ATOM   3256 N  N   . ALA   B 1 164 ? 12.558  47.934 51.736 1.000 26.218  ? 163 ALA   BBB N   1 ? 
ATOM   3257 C  CA  . ALA   B 1 164 ? 13.558  47.897 50.641 1.000 24.239  ? 163 ALA   BBB CA  1 ? 
ATOM   3258 C  C   . ALA   B 1 164 ? 13.413  46.602 49.828 1.000 23.089  ? 163 ALA   BBB C   1 ? 
ATOM   3259 O  O   . ALA   B 1 164 ? 13.913  46.588 48.678 1.000 26.864  ? 163 ALA   BBB O   1 ? 
ATOM   3260 C  CB  . ALA   B 1 164 ? 14.971  48.033 51.184 1.000 23.195  ? 163 ALA   BBB CB  1 ? 
ATOM   3261 N  N   . LEU   B 1 165 ? 12.805  45.559 50.406 1.000 24.877  ? 164 LEU   BBB N   1 ? 
ATOM   3262 C  CA  . LEU   B 1 165 ? 12.835  44.234 49.714 1.000 27.863  ? 164 LEU   BBB CA  1 ? 
ATOM   3263 C  C   . LEU   B 1 165 ? 12.080  44.273 48.356 1.000 28.137  ? 164 LEU   BBB C   1 ? 
ATOM   3264 O  O   . LEU   B 1 165 ? 12.442  43.472 47.447 1.000 25.628  ? 164 LEU   BBB O   1 ? 
ATOM   3265 C  CB  . LEU   B 1 165 ? 12.298  43.119 50.620 1.000 28.319  ? 164 LEU   BBB CB  1 ? 
ATOM   3266 C  CG  . LEU   B 1 165 ? 13.053  42.897 51.928 1.000 24.999  ? 164 LEU   BBB CG  1 ? 
ATOM   3267 C  CD1 . LEU   B 1 165 ? 12.448  41.733 52.706 1.000 28.507  ? 164 LEU   BBB CD1 1 ? 
ATOM   3268 C  CD2 . LEU   B 1 165 ? 14.529  42.697 51.676 1.000 25.623  ? 164 LEU   BBB CD2 1 ? 
ATOM   3269 N  N   . GLN   B 1 166 ? 11.069  45.148 48.195 1.000 25.364  ? 165 GLN   BBB N   1 ? 
ATOM   3270 C  CA  . GLN   B 1 166 ? 10.282  45.200 46.936 1.000 29.142  ? 165 GLN   BBB CA  1 ? 
ATOM   3271 C  C   . GLN   B 1 166 ? 11.195  45.594 45.755 1.000 24.608  ? 165 GLN   BBB C   1 ? 
ATOM   3272 O  O   . GLN   B 1 166 ? 10.825  45.298 44.610 1.000 31.435  ? 165 GLN   BBB O   1 ? 
ATOM   3273 C  CB  . GLN   B 1 166 ? 9.044   46.086 47.045 1.000 31.844  ? 165 GLN   BBB CB  1 ? 
ATOM   3274 C  CG  . GLN   B 1 166 ? 9.273   47.438 47.726 1.000 35.879  ? 165 GLN   BBB CG  1 ? 
ATOM   3275 C  CD  . GLN   B 1 166 ? 10.169  48.381 46.966 1.000 37.668  ? 165 GLN   BBB CD  1 ? 
ATOM   3276 O  OE1 . GLN   B 1 166 ? 10.014  48.581 45.746 1.000 34.217  ? 165 GLN   BBB OE1 1 ? 
ATOM   3277 N  NE2 . GLN   B 1 166 ? 11.093  48.987 47.701 1.000 39.836  ? 165 GLN   BBB NE2 1 ? 
ATOM   3278 N  N   . ALA   B 1 167 ? 12.358  46.201 45.986 1.000 26.543  ? 166 ALA   BBB N   1 ? 
ATOM   3279 C  CA  . ALA   B 1 167 ? 13.233  46.663 44.877 1.000 29.496  ? 166 ALA   BBB CA  1 ? 
ATOM   3280 C  C   . ALA   B 1 167 ? 14.227  45.562 44.483 1.000 29.246  ? 166 ALA   BBB C   1 ? 
ATOM   3281 O  O   . ALA   B 1 167 ? 14.922  45.752 43.473 1.000 30.744  ? 166 ALA   BBB O   1 ? 
ATOM   3282 C  CB  . ALA   B 1 167 ? 13.949  47.953 45.232 1.000 31.859  ? 166 ALA   BBB CB  1 ? 
ATOM   3283 N  N   . ILE   B 1 168 ? 14.300  44.477 45.256 1.000 26.823  ? 167 ILE   BBB N   1 ? 
ATOM   3284 C  CA  . ILE   B 1 168 ? 15.319  43.403 45.052 1.000 29.042  ? 167 ILE   BBB CA  1 ? 
ATOM   3285 C  C   . ILE   B 1 168 ? 14.660  42.014 45.143 1.000 28.228  ? 167 ILE   BBB C   1 ? 
ATOM   3286 O  O   . ILE   B 1 168 ? 15.235  41.123 45.799 1.000 27.337  ? 167 ILE   BBB O   1 ? 
ATOM   3287 C  CB  . ILE   B 1 168 ? 16.511  43.535 46.023 1.000 28.554  ? 167 ILE   BBB CB  1 ? 
ATOM   3288 C  CG1 . ILE   B 1 168 ? 16.101  43.402 47.482 1.000 29.188  ? 167 ILE   BBB CG1 1 ? 
ATOM   3289 C  CG2 . ILE   B 1 168 ? 17.269  44.851 45.802 1.000 26.767  ? 167 ILE   BBB CG2 1 ? 
ATOM   3290 C  CD1 . ILE   B 1 168 ? 17.131  42.712 48.317 1.000 32.582  ? 167 ILE   BBB CD1 1 ? 
ATOM   3291 N  N   . LYS   B 1 169 ? 13.557  41.825 44.432 1.000 29.339  ? 168 LYS   BBB N   1 ? 
ATOM   3292 C  CA  . LYS   B 1 169 ? 12.707  40.629 44.572 1.000 26.439  ? 168 LYS   BBB CA  1 ? 
ATOM   3293 C  C   . LYS   B 1 169 ? 13.422  39.361 44.063 1.000 26.824  ? 168 LYS   BBB C   1 ? 
ATOM   3294 O  O   . LYS   B 1 169 ? 13.200  38.317 44.696 1.000 28.693  ? 168 LYS   BBB O   1 ? 
ATOM   3295 C  CB  . LYS   B 1 169 ? 11.347  40.814 43.898 1.000 38.402  ? 168 LYS   BBB CB  1 ? 
ATOM   3296 C  CG  . LYS   B 1 169 ? 10.293  41.348 44.859 1.000 44.267  ? 168 LYS   BBB CG  1 ? 
ATOM   3297 C  CD  . LYS   B 1 169 ? 9.916   40.373 45.989 1.000 47.074  ? 168 LYS   BBB CD  1 ? 
ATOM   3298 C  CE  . LYS   B 1 169 ? 8.882   40.961 46.914 1.000 52.646  ? 168 LYS   BBB CE  1 ? 
ATOM   3299 N  NZ  . LYS   B 1 169 ? 8.578   40.032 48.019 1.000 60.422  ? 168 LYS   BBB NZ  1 ? 
ATOM   3300 N  N   . THR   B 1 170 ? 14.202  39.451 42.989 1.000 26.444  ? 169 THR   BBB N   1 ? 
ATOM   3301 C  CA  . THR   B 1 170 ? 14.841  38.298 42.307 1.000 26.908  ? 169 THR   BBB CA  1 ? 
ATOM   3302 C  C   . THR   B 1 170 ? 16.369  38.304 42.413 1.000 27.849  ? 169 THR   BBB C   1 ? 
ATOM   3303 O  O   . THR   B 1 170 ? 16.960  39.380 42.602 1.000 25.622  ? 169 THR   BBB O   1 ? 
ATOM   3304 C  CB  . THR   B 1 170 ? 14.358  38.254 40.845 1.000 30.434  ? 169 THR   BBB CB  1 ? 
ATOM   3305 O  OG1 . THR   B 1 170 ? 14.513  39.496 40.150 1.000 28.836  ? 169 THR   BBB OG1 1 ? 
ATOM   3306 C  CG2 . THR   B 1 170 ? 12.887  37.913 40.791 1.000 39.658  ? 169 THR   BBB CG2 1 ? 
ATOM   3307 N  N   . LYS   B 1 171 ? 16.988  37.117 42.282 1.000 29.264  ? 170 LYS   BBB N   1 ? 
ATOM   3308 C  CA  . LYS   B 1 171 ? 18.460  36.931 42.359 1.000 24.125  ? 170 LYS   BBB CA  1 ? 
ATOM   3309 C  C   . LYS   B 1 171 ? 19.193  37.977 41.502 1.000 25.243  ? 170 LYS   BBB C   1 ? 
ATOM   3310 O  O   . LYS   B 1 171 ? 18.908  38.124 40.286 1.000 27.037  ? 170 LYS   BBB O   1 ? 
ATOM   3311 C  CB  . LYS   B 1 171 ? 18.902  35.547 41.901 1.000 27.211  ? 170 LYS   BBB CB  1 ? 
ATOM   3312 C  CG  . LYS   B 1 171 ? 20.409  35.327 42.093 1.000 29.485  ? 170 LYS   BBB CG  1 ? 
ATOM   3313 C  CD  . LYS   B 1 171 ? 20.902  33.890 42.067 1.000 33.613  ? 170 LYS   BBB CD  1 ? 
ATOM   3314 C  CE  . LYS   B 1 171 ? 20.388  33.080 40.915 1.000 44.654  ? 170 LYS   BBB CE  1 ? 
ATOM   3315 N  NZ  . LYS   B 1 171 ? 20.793  31.652 41.053 1.000 55.323  ? 170 LYS   BBB NZ  1 ? 
ATOM   3316 N  N   . GLY   B 1 172 ? 20.139  38.672 42.121 1.000 25.003  ? 171 GLY   BBB N   1 ? 
ATOM   3317 C  CA  . GLY   B 1 172 ? 21.027  39.571 41.388 1.000 24.224  ? 171 GLY   BBB CA  1 ? 
ATOM   3318 C  C   . GLY   B 1 172 ? 20.536  41.024 41.433 1.000 27.298  ? 171 GLY   BBB C   1 ? 
ATOM   3319 O  O   . GLY   B 1 172 ? 21.347  41.899 41.153 1.000 29.485  ? 171 GLY   BBB O   1 ? 
ATOM   3320 N  N   . LYS   B 1 173 ? 19.278  41.286 41.744 1.000 26.502  ? 172 LYS   BBB N   1 ? 
ATOM   3321 C  CA  . LYS   B 1 173 ? 18.800  42.682 41.890 1.000 25.069  ? 172 LYS   BBB CA  1 ? 
ATOM   3322 C  C   . LYS   B 1 173 ? 19.477  43.348 43.094 1.000 25.931  ? 172 LYS   BBB C   1 ? 
ATOM   3323 O  O   . LYS   B 1 173 ? 19.804  42.700 44.117 1.000 26.715  ? 172 LYS   BBB O   1 ? 
ATOM   3324 C  CB  . LYS   B 1 173 ? 17.274  42.734 41.954 1.000 28.801  ? 172 LYS   BBB CB  1 ? 
ATOM   3325 C  CG  . LYS   B 1 173 ? 16.591  42.231 40.695 1.000 33.219  ? 172 LYS   BBB CG  1 ? 
ATOM   3326 C  CD  . LYS   B 1 173 ? 15.195  42.729 40.579 1.000 41.024  ? 172 LYS   BBB CD  1 ? 
ATOM   3327 C  CE  . LYS   B 1 173 ? 15.146  44.212 40.317 1.000 40.567  ? 172 LYS   BBB CE  1 ? 
ATOM   3328 N  NZ  . LYS   B 1 173 ? 13.754  44.697 40.377 1.000 48.635  ? 172 LYS   BBB NZ  1 ? 
ATOM   3329 N  N   . ARG   B 1 174 ? 19.725  44.647 42.937 1.000 28.405  ? 173 ARG   BBB N   1 ? 
ATOM   3330 C  CA  . ARG   B 1 174 ? 20.364  45.448 43.984 1.000 27.545  ? 173 ARG   BBB CA  1 ? 
ATOM   3331 C  C   . ARG   B 1 174 ? 19.831  46.881 43.869 1.000 29.565  ? 173 ARG   BBB C   1 ? 
ATOM   3332 O  O   . ARG   B 1 174 ? 19.392  47.324 42.741 1.000 27.439  ? 173 ARG   BBB O   1 ? 
ATOM   3333 C  CB  . ARG   B 1 174 ? 21.878  45.341 43.812 1.000 28.457  ? 173 ARG   BBB CB  1 ? 
ATOM   3334 C  CG  . ARG   B 1 174 ? 22.353  45.598 42.390 1.000 39.977  ? 173 ARG   BBB CG  1 ? 
ATOM   3335 C  CD  . ARG   B 1 174 ? 23.578  44.771 41.998 1.000 42.283  ? 173 ARG   BBB CD  1 ? 
ATOM   3336 N  NE  . ARG   B 1 174 ? 24.698  45.097 42.862 1.000 40.958  ? 173 ARG   BBB NE  1 ? 
ATOM   3337 C  CZ  . ARG   B 1 174 ? 25.770  44.334 43.052 1.000 39.286  ? 173 ARG   BBB CZ  1 ? 
ATOM   3338 N  NH1 . ARG   B 1 174 ? 26.718  44.732 43.885 1.000 47.653  ? 173 ARG   BBB NH1 1 ? 
ATOM   3339 N  NH2 . ARG   B 1 174 ? 25.906  43.187 42.407 1.000 41.369  ? 173 ARG   BBB NH2 1 ? 
ATOM   3340 N  N   . ALA   B 1 175 ? 19.883  47.588 44.988 1.000 21.721  ? 174 ALA   BBB N   1 ? 
ATOM   3341 C  CA  . ALA   B 1 175 ? 19.431  48.991 45.067 1.000 27.170  ? 174 ALA   BBB CA  1 ? 
ATOM   3342 C  C   . ALA   B 1 175 ? 20.259  49.726 46.091 1.000 25.732  ? 174 ALA   BBB C   1 ? 
ATOM   3343 O  O   . ALA   B 1 175 ? 20.707  49.131 47.060 1.000 25.958  ? 174 ALA   BBB O   1 ? 
ATOM   3344 C  CB  . ALA   B 1 175 ? 17.983  48.995 45.462 1.000 30.499  ? 174 ALA   BBB CB  1 ? 
ATOM   3345 N  N   . PRO   B 1 176 ? 20.320  51.094 45.988 1.000 25.091  ? 175 PRO   BBB N   1 ? 
ATOM   3346 C  CA  . PRO   B 1 176 ? 20.934  51.874 47.049 1.000 25.644  ? 175 PRO   BBB CA  1 ? 
ATOM   3347 C  C   . PRO   B 1 176 ? 20.130  51.643 48.331 1.000 24.752  ? 175 PRO   BBB C   1 ? 
ATOM   3348 O  O   . PRO   B 1 176 ? 18.889  51.510 48.260 1.000 28.660  ? 175 PRO   BBB O   1 ? 
ATOM   3349 C  CB  . PRO   B 1 176 ? 20.886  53.336 46.545 1.000 29.020  ? 175 PRO   BBB CB  1 ? 
ATOM   3350 C  CG  . PRO   B 1 176 ? 20.834  53.130 45.034 1.000 34.433  ? 175 PRO   BBB CG  1 ? 
ATOM   3351 C  CD  . PRO   B 1 176 ? 19.976  51.884 44.816 1.000 29.470  ? 175 PRO   BBB CD  1 ? 
ATOM   3352 N  N   . PHE   B 1 177 ? 20.862  51.620 49.448 1.000 24.786  ? 176 PHE   BBB N   1 ? 
ATOM   3353 C  CA  . PHE   B 1 177 ? 20.345  51.506 50.835 1.000 25.043  ? 176 PHE   BBB CA  1 ? 
ATOM   3354 C  C   . PHE   B 1 177 ? 21.232  52.377 51.717 1.000 25.363  ? 176 PHE   BBB C   1 ? 
ATOM   3355 O  O   . PHE   B 1 177 ? 22.423  52.036 51.884 1.000 23.813  ? 176 PHE   BBB O   1 ? 
ATOM   3356 C  CB  . PHE   B 1 177 ? 20.360  50.031 51.255 1.000 27.335  ? 176 PHE   BBB CB  1 ? 
ATOM   3357 C  CG  . PHE   B 1 177 ? 19.691  49.789 52.579 1.000 24.299  ? 176 PHE   BBB CG  1 ? 
ATOM   3358 C  CD1 . PHE   B 1 177 ? 20.397  49.934 53.757 1.000 26.092  ? 176 PHE   BBB CD1 1 ? 
ATOM   3359 C  CD2 . PHE   B 1 177 ? 18.341  49.459 52.636 1.000 25.992  ? 176 PHE   BBB CD2 1 ? 
ATOM   3360 C  CE1 . PHE   B 1 177 ? 19.759  49.759 54.979 1.000 27.566  ? 176 PHE   BBB CE1 1 ? 
ATOM   3361 C  CE2 . PHE   B 1 177 ? 17.712  49.261 53.849 1.000 26.157  ? 176 PHE   BBB CE2 1 ? 
ATOM   3362 C  CZ  . PHE   B 1 177 ? 18.421  49.420 55.025 1.000 25.809  ? 176 PHE   BBB CZ  1 ? 
ATOM   3363 N  N   . THR   B 1 178 ? 20.721  53.554 52.114 1.000 26.543  ? 177 THR   BBB N   1 ? 
ATOM   3364 C  CA  . THR   B 1 178 ? 21.584  54.624 52.682 1.000 28.751  ? 177 THR   BBB CA  1 ? 
ATOM   3365 C  C   . THR   B 1 178 ? 21.067  55.114 54.030 1.000 24.949  ? 177 THR   BBB C   1 ? 
ATOM   3366 O  O   . THR   B 1 178 ? 19.859  54.958 54.334 1.000 26.991  ? 177 THR   BBB O   1 ? 
ATOM   3367 C  CB  . THR   B 1 178 ? 21.736  55.801 51.712 1.000 27.813  ? 177 THR   BBB CB  1 ? 
ATOM   3368 O  OG1 . THR   B 1 178 ? 20.418  56.264 51.432 1.000 30.409  ? 177 THR   BBB OG1 1 ? 
ATOM   3369 C  CG2 . THR   B 1 178 ? 22.445  55.425 50.425 1.000 30.544  ? 177 THR   BBB CG2 1 ? 
ATOM   3370 N  N   . ASN   B 1 179 ? 21.969  55.696 54.801 1.000 29.300  ? 178 ASN   BBB N   1 ? 
ATOM   3371 C  CA  . ASN   B 1 179 ? 21.600  56.405 56.055 1.000 30.256  ? 178 ASN   BBB CA  1 ? 
ATOM   3372 C  C   . ASN   B 1 179 ? 20.947  55.427 57.061 1.000 26.162  ? 178 ASN   BBB C   1 ? 
ATOM   3373 O  O   . ASN   B 1 179 ? 19.745  55.542 57.406 1.000 30.032  ? 178 ASN   BBB O   1 ? 
ATOM   3374 C  CB  . ASN   B 1 179 ? 20.687  57.575 55.702 1.000 36.234  ? 178 ASN   BBB CB  1 ? 
ATOM   3375 C  CG  . ASN   B 1 179 ? 20.550  58.462 56.903 1.000 42.737  ? 178 ASN   BBB CG  1 ? 
ATOM   3376 O  OD1 . ASN   B 1 179 ? 19.494  59.064 57.113 1.000 54.686  ? 178 ASN   BBB OD1 1 ? 
ATOM   3377 N  ND2 . ASN   B 1 179 ? 21.614  58.513 57.696 1.000 46.149  ? 178 ASN   BBB ND2 1 ? 
ATOM   3378 N  N   . PHE   B 1 180 ? 21.674  54.392 57.435 1.000 28.591  ? 179 PHE   BBB N   1 ? 
ATOM   3379 C  CA  . PHE   B 1 180 ? 21.145  53.349 58.339 1.000 28.402  ? 179 PHE   BBB CA  1 ? 
ATOM   3380 C  C   . PHE   B 1 180 ? 22.266  52.859 59.265 1.000 27.306  ? 179 PHE   BBB C   1 ? 
ATOM   3381 O  O   . PHE   B 1 180 ? 23.364  52.541 58.770 1.000 23.865  ? 179 PHE   BBB O   1 ? 
ATOM   3382 C  CB  . PHE   B 1 180 ? 20.545  52.189 57.551 1.000 26.111  ? 179 PHE   BBB CB  1 ? 
ATOM   3383 C  CG  . PHE   B 1 180 ? 19.883  51.236 58.492 1.000 25.376  ? 179 PHE   BBB CG  1 ? 
ATOM   3384 C  CD1 . PHE   B 1 180 ? 18.638  51.505 59.031 1.000 27.193  ? 179 PHE   BBB CD1 1 ? 
ATOM   3385 C  CD2 . PHE   B 1 180 ? 20.487  50.014 58.787 1.000 29.873  ? 179 PHE   BBB CD2 1 ? 
ATOM   3386 C  CE1 . PHE   B 1 180 ? 18.040  50.629 59.928 1.000 28.209  ? 179 PHE   BBB CE1 1 ? 
ATOM   3387 C  CE2 . PHE   B 1 180 ? 19.893  49.120 59.673 1.000 24.733  ? 179 PHE   BBB CE2 1 ? 
ATOM   3388 C  CZ  . PHE   B 1 180 ? 18.644  49.380 60.180 1.000 24.895  ? 179 PHE   BBB CZ  1 ? 
ATOM   3389 N  N   . ASP   B 1 181 ? 22.002  52.865 60.563 1.000 23.002  ? 180 ASP   BBB N   1 ? 
ATOM   3390 C  CA  . ASP   B 1 181 ? 22.956  52.403 61.596 1.000 26.349  ? 180 ASP   BBB CA  1 ? 
ATOM   3391 C  C   . ASP   B 1 181 ? 22.470  51.069 62.136 1.000 21.275  ? 180 ASP   BBB C   1 ? 
ATOM   3392 O  O   . ASP   B 1 181 ? 21.481  51.022 62.881 1.000 23.449  ? 180 ASP   BBB O   1 ? 
ATOM   3393 C  CB  . ASP   B 1 181 ? 23.036  53.379 62.764 1.000 30.500  ? 180 ASP   BBB CB  1 ? 
ATOM   3394 C  CG  . ASP   B 1 181 ? 24.013  53.012 63.864 1.000 26.821  ? 180 ASP   BBB CG  1 ? 
ATOM   3395 O  OD1 . ASP   B 1 181 ? 24.477  51.831 63.890 1.000 28.343  ? 180 ASP   BBB OD1 1 ? 
ATOM   3396 O  OD2 . ASP   B 1 181 ? 24.276  53.836 64.761 1.000 29.958  ? 180 ASP   BBB OD2 1 ? 
ATOM   3397 N  N   . PRO   B 1 182 ? 23.092  49.932 61.739 1.000 21.085  ? 181 PRO   BBB N   1 ? 
ATOM   3398 C  CA  . PRO   B 1 182 ? 22.559  48.638 62.163 1.000 22.818  ? 181 PRO   BBB CA  1 ? 
ATOM   3399 C  C   . PRO   B 1 182 ? 22.754  48.284 63.637 1.000 23.023  ? 181 PRO   BBB C   1 ? 
ATOM   3400 O  O   . PRO   B 1 182 ? 22.143  47.301 64.088 1.000 23.251  ? 181 PRO   BBB O   1 ? 
ATOM   3401 C  CB  . PRO   B 1 182 ? 23.269  47.689 61.202 1.000 24.474  ? 181 PRO   BBB CB  1 ? 
ATOM   3402 C  CG  . PRO   B 1 182 ? 24.608  48.348 60.959 1.000 23.371  ? 181 PRO   BBB CG  1 ? 
ATOM   3403 C  CD  . PRO   B 1 182 ? 24.259  49.832 60.869 1.000 22.239  ? 181 PRO   BBB CD  1 ? 
ATOM   3404 N  N   . SER   B 1 183 ? 23.478  49.095 64.400 1.000 21.237  ? 182 SER   BBB N   1 ? 
ATOM   3405 C  CA  . SER   B 1 183 ? 23.552  48.928 65.869 1.000 21.887  ? 182 SER   BBB CA  1 ? 
ATOM   3406 C  C   . SER   B 1 183 ? 22.161  49.149 66.457 1.000 22.041  ? 182 SER   BBB C   1 ? 
ATOM   3407 O  O   . SER   B 1 183 ? 21.924  48.649 67.553 1.000 23.494  ? 182 SER   BBB O   1 ? 
ATOM   3408 C  CB  . SER   B 1 183 ? 24.586  49.795 66.547 1.000 21.950  ? 182 SER   BBB CB  1 ? 
ATOM   3409 O  OG  . SER   B 1 183 ? 24.154  51.124 66.477 1.000 22.384  ? 182 SER   BBB OG  1 ? 
ATOM   3410 N  N   . THR   B 1 184 ? 21.256  49.834 65.760 1.000 20.603  ? 183 THR   BBB N   1 ? 
ATOM   3411 C  CA  . THR   B 1 184 ? 19.850  50.005 66.227 1.000 21.420  ? 183 THR   BBB CA  1 ? 
ATOM   3412 C  C   . THR   B 1 184 ? 19.095  48.651 66.241 1.000 18.845  ? 183 THR   BBB C   1 ? 
ATOM   3413 O  O   . THR   B 1 184 ? 18.015  48.574 66.886 1.000 22.971  ? 183 THR   BBB O   1 ? 
ATOM   3414 C  CB  . THR   B 1 184 ? 19.085  50.980 65.351 1.000 23.810  ? 183 THR   BBB CB  1 ? 
ATOM   3415 O  OG1 . THR   B 1 184 ? 19.063  50.505 64.015 1.000 30.262  ? 183 THR   BBB OG1 1 ? 
ATOM   3416 C  CG2 . THR   B 1 184 ? 19.671  52.375 65.387 1.000 30.509  ? 183 THR   BBB CG2 1 ? 
ATOM   3417 N  N   . LEU   B 1 185 ? 19.636  47.625 65.582 1.000 20.584  ? 184 LEU   BBB N   1 ? 
ATOM   3418 C  CA  . LEU   B 1 185 ? 18.947  46.309 65.611 1.000 20.932  ? 184 LEU   BBB CA  1 ? 
ATOM   3419 C  C   . LEU   B 1 185 ? 19.352  45.491 66.820 1.000 21.140  ? 184 LEU   BBB C   1 ? 
ATOM   3420 O  O   . LEU   B 1 185 ? 18.713  44.459 67.031 1.000 21.434  ? 184 LEU   BBB O   1 ? 
ATOM   3421 C  CB  . LEU   B 1 185 ? 19.300  45.527 64.348 1.000 22.503  ? 184 LEU   BBB CB  1 ? 
ATOM   3422 C  CG  . LEU   B 1 185 ? 18.827  46.207 63.051 1.000 23.901  ? 184 LEU   BBB CG  1 ? 
ATOM   3423 C  CD1 . LEU   B 1 185 ? 19.434  45.575 61.788 1.000 25.445  ? 184 LEU   BBB CD1 1 ? 
ATOM   3424 C  CD2 . LEU   B 1 185 ? 17.327  46.263 62.963 1.000 25.930  ? 184 LEU   BBB CD2 1 ? 
ATOM   3425 N  N   . LEU   B 1 186 ? 20.409  45.857 67.504 1.000 19.376  ? 185 LEU   BBB N   1 ? 
ATOM   3426 C  CA  . LEU   B 1 186 ? 21.002  45.113 68.627 1.000 19.975  ? 185 LEU   BBB CA  1 ? 
ATOM   3427 C  C   . LEU   B 1 186 ? 20.127  45.196 69.865 1.000 19.977  ? 185 LEU   BBB C   1 ? 
ATOM   3428 O  O   . LEU   B 1 186 ? 19.435  46.192 70.119 1.000 21.738  ? 185 LEU   BBB O   1 ? 
ATOM   3429 C  CB  . LEU   B 1 186 ? 22.420  45.625 68.874 1.000 20.723  ? 185 LEU   BBB CB  1 ? 
ATOM   3430 C  CG  . LEU   B 1 186 ? 23.423  45.373 67.745 1.000 22.303  ? 185 LEU   BBB CG  1 ? 
ATOM   3431 C  CD1 . LEU   B 1 186 ? 24.784  45.837 68.163 1.000 23.615  ? 185 LEU   BBB CD1 1 ? 
ATOM   3432 C  CD2 . LEU   B 1 186 ? 23.526  43.836 67.379 1.000 21.610  ? 185 LEU   BBB CD2 1 ? 
ATOM   3433 N  N   . PRO   B 1 187 ? 20.149  44.185 70.756 1.000 22.473  ? 186 PRO   BBB N   1 ? 
ATOM   3434 C  CA  . PRO   B 1 187 ? 19.427  44.253 72.019 1.000 20.694  ? 186 PRO   BBB CA  1 ? 
ATOM   3435 C  C   . PRO   B 1 187 ? 20.055  45.386 72.897 1.000 20.972  ? 186 PRO   BBB C   1 ? 
ATOM   3436 O  O   . PRO   B 1 187 ? 21.204  45.802 72.599 1.000 22.777  ? 186 PRO   BBB O   1 ? 
ATOM   3437 C  CB  . PRO   B 1 187 ? 19.573  42.801 72.566 1.000 21.447  ? 186 PRO   BBB CB  1 ? 
ATOM   3438 C  CG  . PRO   B 1 187 ? 20.892  42.417 72.028 1.000 20.947  ? 186 PRO   BBB CG  1 ? 
ATOM   3439 C  CD  . PRO   B 1 187 ? 20.823  42.849 70.586 1.000 20.275  ? 186 PRO   BBB CD  1 ? 
ATOM   3440 N  N   . SER   B 1 188 ? 19.360  45.829 73.959 1.000 20.676  ? 187 SER   BBB N   1 ? 
ATOM   3441 C  CA  . SER   B 1 188 ? 19.827  46.887 74.901 1.000 22.201  ? 187 SER   BBB CA  1 ? 
ATOM   3442 C  C   . SER   B 1 188 ? 21.119  46.435 75.573 1.000 24.907  ? 187 SER   BBB C   1 ? 
ATOM   3443 O  O   . SER   B 1 188 ? 22.068  47.184 75.676 1.000 27.944  ? 187 SER   BBB O   1 ? 
ATOM   3444 C  CB  . SER   B 1 188 ? 18.818  47.212 75.974 1.000 30.302  ? 187 SER   BBB CB  1 ? 
ATOM   3445 O  OG  . SER   B 1 188 ? 17.632  47.731 75.415 1.000 39.588  ? 187 SER   BBB OG  1 ? 
ATOM   3446 N  N   . SER   B 1 189 ? 21.103  45.215 76.092 1.000 24.314  ? 188 SER   BBB N   1 ? 
ATOM   3447 C  CA  . SER   B 1 189 ? 22.272  44.597 76.741 1.000 25.976  ? 188 SER   BBB CA  1 ? 
ATOM   3448 C  C   . SER   B 1 189 ? 23.124  43.881 75.682 1.000 24.070  ? 188 SER   BBB C   1 ? 
ATOM   3449 O  O   . SER   B 1 189 ? 22.545  43.103 74.868 1.000 26.442  ? 188 SER   BBB O   1 ? 
ATOM   3450 C  CB  . SER   B 1 189 ? 21.816  43.630 77.813 1.000 29.335  ? 188 SER   BBB CB  1 ? 
ATOM   3451 O  OG  . SER   B 1 189 ? 22.918  42.935 78.345 1.000 30.372  ? 188 SER   BBB OG  1 ? 
ATOM   3452 N  N   . LEU   B 1 190 ? 24.442  44.026 75.780 1.000 23.014  ? 189 LEU   BBB N   1 ? 
ATOM   3453 C  CA  . LEU   B 1 190 ? 25.406  43.342 74.893 1.000 28.348  ? 189 LEU   BBB CA  1 ? 
ATOM   3454 C  C   . LEU   B 1 190 ? 26.199  42.309 75.689 1.000 24.541  ? 189 LEU   BBB C   1 ? 
ATOM   3455 O  O   . LEU   B 1 190 ? 27.306  42.072 75.263 1.000 23.792  ? 189 LEU   BBB O   1 ? 
ATOM   3456 C  CB  . LEU   B 1 190 ? 26.288  44.395 74.207 1.000 28.282  ? 189 LEU   BBB CB  1 ? 
ATOM   3457 C  CG  . LEU   B 1 190 ? 25.528  45.336 73.263 1.000 26.875  ? 189 LEU   BBB CG  1 ? 
ATOM   3458 C  CD1 . LEU   B 1 190 ? 26.517  46.195 72.537 1.000 29.044  ? 189 LEU   BBB CD1 1 ? 
ATOM   3459 C  CD2 . LEU   B 1 190 ? 24.647  44.572 72.248 1.000 27.665  ? 189 LEU   BBB CD2 1 ? 
ATOM   3460 N  N   . ASP   B 1 191 ? 25.624  41.675 76.722 1.000 24.113  ? 190 ASP   BBB N   1 ? 
ATOM   3461 C  CA  . ASP   B 1 191 ? 26.277  40.481 77.313 1.000 26.087  ? 190 ASP   BBB CA  1 ? 
ATOM   3462 C  C   . ASP   B 1 191 ? 26.404  39.455 76.180 1.000 24.262  ? 190 ASP   BBB C   1 ? 
ATOM   3463 O  O   . ASP   B 1 191 ? 25.479  39.392 75.352 1.000 19.066  ? 190 ASP   BBB O   1 ? 
ATOM   3464 C  CB  . ASP   B 1 191 ? 25.490  39.882 78.482 1.000 28.685  ? 190 ASP   BBB CB  1 ? 
ATOM   3465 C  CG  . ASP   B 1 191 ? 25.414  40.766 79.716 1.000 31.548  ? 190 ASP   BBB CG  1 ? 
ATOM   3466 O  OD1 . ASP   B 1 191 ? 26.298  41.622 79.903 1.000 31.247  ? 190 ASP   BBB OD1 1 ? 
ATOM   3467 O  OD2 . ASP   B 1 191 ? 24.485  40.560 80.500 1.000 35.991  ? 190 ASP   BBB OD2 1 ? 
ATOM   3468 N  N   . PHE   B 1 192 ? 27.487  38.679 76.126 1.000 21.780  ? 191 PHE   BBB N   1 ? 
ATOM   3469 C  CA  . PHE   B 1 192 ? 27.740  37.821 74.942 1.000 19.458  ? 191 PHE   BBB CA  1 ? 
ATOM   3470 C  C   . PHE   B 1 192 ? 28.450  36.529 75.353 1.000 19.311  ? 191 PHE   BBB C   1 ? 
ATOM   3471 O  O   . PHE   B 1 192 ? 29.149  36.481 76.373 1.000 20.795  ? 191 PHE   BBB O   1 ? 
ATOM   3472 C  CB  . PHE   B 1 192 ? 28.483  38.537 73.819 1.000 21.037  ? 191 PHE   BBB CB  1 ? 
ATOM   3473 C  CG  . PHE   B 1 192 ? 29.888  38.949 74.180 1.000 18.283  ? 191 PHE   BBB CG  1 ? 
ATOM   3474 C  CD1 . PHE   B 1 192 ? 30.134  40.173 74.849 1.000 19.635  ? 191 PHE   BBB CD1 1 ? 
ATOM   3475 C  CD2 . PHE   B 1 192 ? 30.967  38.134 73.859 1.000 23.559  ? 191 PHE   BBB CD2 1 ? 
ATOM   3476 C  CE1 . PHE   B 1 192 ? 31.433  40.496 75.219 1.000 21.354  ? 191 PHE   BBB CE1 1 ? 
ATOM   3477 C  CE2 . PHE   B 1 192 ? 32.255  38.491 74.195 1.000 20.632  ? 191 PHE   BBB CE2 1 ? 
ATOM   3478 C  CZ  . PHE   B 1 192 ? 32.491  39.670 74.880 1.000 22.171  ? 191 PHE   BBB CZ  1 ? 
ATOM   3479 N  N   . TRP   B 1 193 ? 28.280  35.531 74.487 1.000 21.354  ? 192 TRP   BBB N   1 ? 
ATOM   3480 C  CA  . TRP   B 1 193 ? 29.172  34.366 74.346 1.000 23.783  ? 192 TRP   BBB CA  1 ? 
ATOM   3481 C  C   . TRP   B 1 193 ? 30.091  34.550 73.142 1.000 21.716  ? 192 TRP   BBB C   1 ? 
ATOM   3482 O  O   . TRP   B 1 193 ? 29.659  35.149 72.094 1.000 22.215  ? 192 TRP   BBB O   1 ? 
ATOM   3483 C  CB  . TRP   B 1 193 ? 28.302  33.121 74.144 1.000 23.316  ? 192 TRP   BBB CB  1 ? 
ATOM   3484 C  CG  . TRP   B 1 193 ? 27.369  32.849 75.277 1.000 23.171  ? 192 TRP   BBB CG  1 ? 
ATOM   3485 C  CD1 . TRP   B 1 193 ? 27.725  32.410 76.526 1.000 26.449  ? 192 TRP   BBB CD1 1 ? 
ATOM   3486 C  CD2 . TRP   B 1 193 ? 25.936  32.907 75.267 1.000 21.515  ? 192 TRP   BBB CD2 1 ? 
ATOM   3487 N  NE1 . TRP   B 1 193 ? 26.619  32.237 77.297 1.000 26.539  ? 192 TRP   BBB NE1 1 ? 
ATOM   3488 C  CE2 . TRP   B 1 193 ? 25.499  32.509 76.552 1.000 23.055  ? 192 TRP   BBB CE2 1 ? 
ATOM   3489 C  CE3 . TRP   B 1 193 ? 24.983  33.224 74.305 1.000 23.691  ? 192 TRP   BBB CE3 1 ? 
ATOM   3490 C  CZ2 . TRP   B 1 193 ? 24.155  32.493 76.912 1.000 25.953  ? 192 TRP   BBB CZ2 1 ? 
ATOM   3491 C  CZ3 . TRP   B 1 193 ? 23.653  33.170 74.643 1.000 22.820  ? 192 TRP   BBB CZ3 1 ? 
ATOM   3492 C  CH2 . TRP   B 1 193 ? 23.248  32.805 75.930 1.000 24.937  ? 192 TRP   BBB CH2 1 ? 
ATOM   3493 N  N   . THR   B 1 194 ? 31.288  33.992 73.230 1.000 22.489  ? 193 THR   BBB N   1 ? 
ATOM   3494 C  CA  . THR   B 1 194 ? 32.215  33.972 72.075 1.000 22.823  ? 193 THR   BBB CA  1 ? 
ATOM   3495 C  C   . THR   B 1 194 ? 32.819  32.570 71.869 1.000 21.184  ? 193 THR   BBB C   1 ? 
ATOM   3496 O  O   . THR   B 1 194 ? 33.130  31.893 72.875 1.000 24.149  ? 193 THR   BBB O   1 ? 
ATOM   3497 C  CB  . THR   B 1 194 ? 33.220  35.110 72.179 1.000 23.381  ? 193 THR   BBB CB  1 ? 
ATOM   3498 O  OG1 . THR   B 1 194 ? 33.971  35.054 70.977 1.000 22.629  ? 193 THR   BBB OG1 1 ? 
ATOM   3499 C  CG2 . THR   B 1 194 ? 34.057  35.028 73.439 1.000 24.495  ? 193 THR   BBB CG2 1 ? 
ATOM   3500 N  N   . TYR   B 1 195 ? 33.059  32.243 70.619 1.000 22.773  ? 194 TYR   BBB N   1 ? 
ATOM   3501 C  CA  . TYR   B 1 195 ? 33.780  30.999 70.261 1.000 23.815  ? 194 TYR   BBB CA  1 ? 
ATOM   3502 C  C   . TYR   B 1 195 ? 34.407  31.154 68.877 1.000 26.272  ? 194 TYR   BBB C   1 ? 
ATOM   3503 O  O   . TYR   B 1 195 ? 33.960  31.973 68.055 1.000 22.702  ? 194 TYR   BBB O   1 ? 
ATOM   3504 C  CB  . TYR   B 1 195 ? 32.822  29.811 70.379 1.000 25.214  ? 194 TYR   BBB CB  1 ? 
ATOM   3505 C  CG  . TYR   B 1 195 ? 31.901  29.668 69.200 1.000 22.988  ? 194 TYR   BBB CG  1 ? 
ATOM   3506 C  CD1 . TYR   B 1 195 ? 30.716  30.380 69.129 1.000 24.573  ? 194 TYR   BBB CD1 1 ? 
ATOM   3507 C  CD2 . TYR   B 1 195 ? 32.234  28.882 68.112 1.000 22.069  ? 194 TYR   BBB CD2 1 ? 
ATOM   3508 C  CE1 . TYR   B 1 195 ? 29.874  30.301 68.037 1.000 22.202  ? 194 TYR   BBB CE1 1 ? 
ATOM   3509 C  CE2 . TYR   B 1 195 ? 31.391  28.749 67.027 1.000 23.127  ? 194 TYR   BBB CE2 1 ? 
ATOM   3510 C  CZ  . TYR   B 1 195 ? 30.215  29.492 66.968 1.000 20.892  ? 194 TYR   BBB CZ  1 ? 
ATOM   3511 O  OH  . TYR   B 1 195 ? 29.430  29.431 65.869 1.000 23.456  ? 194 TYR   BBB OH  1 ? 
ATOM   3512 N  N   . PRO   B 1 196 ? 35.496  30.405 68.585 1.000 23.662  ? 195 PRO   BBB N   1 ? 
ATOM   3513 C  CA  . PRO   B 1 196 ? 36.083  30.425 67.250 1.000 23.898  ? 195 PRO   BBB CA  1 ? 
ATOM   3514 C  C   . PRO   B 1 196 ? 35.301  29.548 66.294 1.000 23.606  ? 195 PRO   BBB C   1 ? 
ATOM   3515 O  O   . PRO   B 1 196 ? 35.067  28.290 66.591 1.000 27.960  ? 195 PRO   BBB O   1 ? 
ATOM   3516 C  CB  . PRO   B 1 196 ? 37.522  29.950 67.450 1.000 27.288  ? 195 PRO   BBB CB  1 ? 
ATOM   3517 C  CG  . PRO   B 1 196 ? 37.392  29.015 68.646 1.000 29.955  ? 195 PRO   BBB CG  1 ? 
ATOM   3518 C  CD  . PRO   B 1 196 ? 36.317  29.635 69.532 1.000 27.952  ? 195 PRO   BBB CD  1 ? 
ATOM   3519 N  N   . GLY   B 1 197 ? 34.981  30.062 65.134 1.000 24.859  ? 196 GLY   BBB N   1 ? 
ATOM   3520 C  CA  . GLY   B 1 197 ? 34.174  29.326 64.152 1.000 23.804  ? 196 GLY   BBB CA  1 ? 
ATOM   3521 C  C   . GLY   B 1 197 ? 34.407  29.783 62.743 1.000 23.749  ? 196 GLY   BBB C   1 ? 
ATOM   3522 O  O   . GLY   B 1 197 ? 35.552  30.088 62.356 1.000 26.022  ? 196 GLY   BBB O   1 ? 
ATOM   3523 N  N   . SER   B 1 198 ? 33.349  29.665 61.983 1.000 24.209  ? 197 SER   BBB N   1 ? 
ATOM   3524 C  CA  . SER   B 1 198 ? 33.381  29.629 60.511 1.000 23.581  ? 197 SER   BBB CA  1 ? 
ATOM   3525 C  C   . SER   B 1 198 ? 32.258  30.497 59.935 1.000 23.049  ? 197 SER   BBB C   1 ? 
ATOM   3526 O  O   . SER   B 1 198 ? 31.292  30.814 60.659 1.000 22.186  ? 197 SER   BBB O   1 ? 
ATOM   3527 C  CB  . SER   B 1 198 ? 33.317  28.172 60.016 1.000 25.787  ? 197 SER   BBB CB  1 ? 
ATOM   3528 O  OG  . SER   B 1 198 ? 31.972  27.802 59.928 1.000 27.710  ? 197 SER   BBB OG  1 ? 
ATOM   3529 N  N   . LEU   B 1 199 ? 32.354  30.772 58.635 1.000 23.336  ? 198 LEU   BBB N   1 ? 
ATOM   3530 C  CA  . LEU   B 1 199 ? 31.199  31.156 57.815 1.000 22.551  ? 198 LEU   BBB CA  1 ? 
ATOM   3531 C  C   . LEU   B 1 199 ? 30.149  30.064 57.940 1.000 21.109  ? 198 LEU   BBB C   1 ? 
ATOM   3532 O  O   . LEU   B 1 199 ? 30.572  28.880 57.921 1.000 23.013  ? 198 LEU   BBB O   1 ? 
ATOM   3533 C  CB  . LEU   B 1 199 ? 31.672  31.324 56.386 1.000 22.885  ? 198 LEU   BBB CB  1 ? 
ATOM   3534 C  CG  . LEU   B 1 199 ? 32.691  32.463 56.125 1.000 23.631  ? 198 LEU   BBB CG  1 ? 
ATOM   3535 C  CD1 . LEU   B 1 199 ? 32.973  32.543 54.646 1.000 26.347  ? 198 LEU   BBB CD1 1 ? 
ATOM   3536 C  CD2 . LEU   B 1 199 ? 32.343  33.817 56.727 1.000 24.187  ? 198 LEU   BBB CD2 1 ? 
ATOM   3537 N  N   . THR   B 1 200 ? 28.862  30.396 58.017 1.000 19.497  ? 199 THR   BBB N   1 ? 
ATOM   3538 C  CA  . THR   B 1 200 ? 27.796  29.361 58.144 1.000 21.653  ? 199 THR   BBB CA  1 ? 
ATOM   3539 C  C   . THR   B 1 200 ? 27.318  28.824 56.785 1.000 21.480  ? 199 THR   BBB C   1 ? 
ATOM   3540 O  O   . THR   B 1 200 ? 26.379  27.982 56.757 1.000 22.787  ? 199 THR   BBB O   1 ? 
ATOM   3541 C  CB  . THR   B 1 200 ? 26.595  29.822 58.952 1.000 21.116  ? 199 THR   BBB CB  1 ? 
ATOM   3542 O  OG1 . THR   B 1 200 ? 25.894  30.900 58.309 1.000 27.345  ? 199 THR   BBB OG1 1 ? 
ATOM   3543 C  CG2 . THR   B 1 200 ? 27.027  30.138 60.361 1.000 21.360  ? 199 THR   BBB CG2 1 ? 
ATOM   3544 N  N   . HIS   B 1 201 ? 27.893  29.309 55.698 1.000 23.574  ? 200 HIS   BBB N   1 ? 
ATOM   3545 C  CA  . HIS   B 1 201 ? 27.619  28.790 54.344 1.000 23.932  ? 200 HIS   BBB CA  1 ? 
ATOM   3546 C  C   . HIS   B 1 201 ? 28.876  28.873 53.502 1.000 21.731  ? 200 HIS   BBB C   1 ? 
ATOM   3547 O  O   . HIS   B 1 201 ? 29.885  29.433 53.920 1.000 24.482  ? 200 HIS   BBB O   1 ? 
ATOM   3548 C  CB  . HIS   B 1 201 ? 26.365  29.416 53.740 1.000 23.887  ? 200 HIS   BBB CB  1 ? 
ATOM   3549 C  CG  . HIS   B 1 201 ? 26.552  30.890 53.532 1.000 25.692  ? 200 HIS   BBB CG  1 ? 
ATOM   3550 N  ND1 . HIS   B 1 201 ? 25.786  31.817 54.184 1.000 30.959  ? 200 HIS   BBB ND1 1 ? 
ATOM   3551 C  CD2 . HIS   B 1 201 ? 27.400  31.545 52.725 1.000 23.008  ? 200 HIS   BBB CD2 1 ? 
ATOM   3552 C  CE1 . HIS   B 1 201 ? 26.177  33.045 53.810 1.000 24.764  ? 200 HIS   BBB CE1 1 ? 
ATOM   3553 N  NE2 . HIS   B 1 201 ? 27.152  32.911 52.899 1.000 27.354  ? 200 HIS   BBB NE2 1 ? 
ATOM   3554 N  N   . PRO   B 1 202 ? 28.915  28.153 52.353 1.000 25.288  ? 201 PRO   BBB N   1 ? 
ATOM   3555 C  CA  . PRO   B 1 202 ? 30.099  28.209 51.498 1.000 25.110  ? 201 PRO   BBB CA  1 ? 
ATOM   3556 C  C   . PRO   B 1 202 ? 30.504  29.663 51.248 1.000 23.900  ? 201 PRO   BBB C   1 ? 
ATOM   3557 O  O   . PRO   B 1 202 ? 29.638  30.520 50.970 1.000 26.618  ? 201 PRO   BBB O   1 ? 
ATOM   3558 C  CB  . PRO   B 1 202 ? 29.656  27.423 50.261 1.000 25.070  ? 201 PRO   BBB CB  1 ? 
ATOM   3559 C  CG  . PRO   B 1 202 ? 28.713  26.388 50.869 1.000 26.252  ? 201 PRO   BBB CG  1 ? 
ATOM   3560 C  CD  . PRO   B 1 202 ? 27.893  27.204 51.864 1.000 27.434  ? 201 PRO   BBB CD  1 ? 
ATOM   3561 N  N   . PRO   B 1 203 ? 31.824  29.950 51.279 1.000 24.504  ? 202 PRO   BBB N   1 ? 
ATOM   3562 C  CA  . PRO   B 1 203 ? 32.864  28.905 51.359 1.000 26.854  ? 202 PRO   BBB CA  1 ? 
ATOM   3563 C  C   . PRO   B 1 203 ? 33.344  28.334 52.704 1.000 26.479  ? 202 PRO   BBB C   1 ? 
ATOM   3564 O  O   . PRO   B 1 203 ? 34.335  27.541 52.751 1.000 28.248  ? 202 PRO   BBB O   1 ? 
ATOM   3565 C  CB  . PRO   B 1 203 ? 34.094  29.563 50.763 1.000 25.956  ? 202 PRO   BBB CB  1 ? 
ATOM   3566 C  CG  . PRO   B 1 203 ? 33.879  31.080 51.082 1.000 29.468  ? 202 PRO   BBB CG  1 ? 
ATOM   3567 C  CD  . PRO   B 1 203 ? 32.385  31.301 51.078 1.000 28.991  ? 202 PRO   BBB CD  1 ? 
ATOM   3568 N  N   . LEU   B 1 204 ? 32.616  28.631 53.769 1.000 24.496  ? 203 LEU   BBB N   1 ? 
ATOM   3569 C  CA  . LEU   B 1 204 ? 32.729  27.891 55.071 1.000 25.942  ? 203 LEU   BBB CA  1 ? 
ATOM   3570 C  C   . LEU   B 1 204 ? 34.115  28.080 55.705 1.000 26.707  ? 203 LEU   BBB C   1 ? 
ATOM   3571 O  O   . LEU   B 1 204 ? 34.438  27.343 56.636 1.000 27.283  ? 203 LEU   BBB O   1 ? 
ATOM   3572 C  CB  . LEU   B 1 204 ? 32.407  26.401 54.861 1.000 24.163  ? 203 LEU   BBB CB  1 ? 
ATOM   3573 C  CG  . LEU   B 1 204 ? 30.967  26.088 54.497 1.000 25.453  ? 203 LEU   BBB CG  1 ? 
ATOM   3574 C  CD1 . LEU   B 1 204 ? 30.830  24.555 54.128 1.000 29.184  ? 203 LEU   BBB CD1 1 ? 
ATOM   3575 C  CD2 . LEU   B 1 204 ? 30.079  26.355 55.685 1.000 28.517  ? 203 LEU   BBB CD2 1 ? 
ATOM   3576 N  N   . TYR   B 1 205 ? 34.839  29.162 55.358 1.000 29.112  ? 204 TYR   BBB N   1 ? 
ATOM   3577 C  CA  . TYR   B 1 205 ? 36.179  29.477 55.902 1.000 25.761  ? 204 TYR   BBB CA  1 ? 
ATOM   3578 C  C   . TYR   B 1 205 ? 36.072  29.494 57.417 1.000 23.821  ? 204 TYR   BBB C   1 ? 
ATOM   3579 O  O   . TYR   B 1 205 ? 35.051  29.998 57.959 1.000 25.126  ? 204 TYR   BBB O   1 ? 
ATOM   3580 C  CB  . TYR   B 1 205 ? 36.652  30.836 55.381 1.000 23.729  ? 204 TYR   BBB CB  1 ? 
ATOM   3581 C  CG  . TYR   B 1 205 ? 37.016  30.874 53.910 1.000 23.442  ? 204 TYR   BBB CG  1 ? 
ATOM   3582 C  CD1 . TYR   B 1 205 ? 37.616  29.786 53.259 1.000 32.733  ? 204 TYR   BBB CD1 1 ? 
ATOM   3583 C  CD2 . TYR   B 1 205 ? 36.858  32.031 53.175 1.000 27.763  ? 204 TYR   BBB CD2 1 ? 
ATOM   3584 C  CE1 . TYR   B 1 205 ? 37.983  29.847 51.917 1.000 34.750  ? 204 TYR   BBB CE1 1 ? 
ATOM   3585 C  CE2 . TYR   B 1 205 ? 37.206  32.101 51.838 1.000 30.285  ? 204 TYR   BBB CE2 1 ? 
ATOM   3586 C  CZ  . TYR   B 1 205 ? 37.792  31.022 51.196 1.000 35.238  ? 204 TYR   BBB CZ  1 ? 
ATOM   3587 O  OH  . TYR   B 1 205 ? 38.128  31.179 49.865 1.000 35.592  ? 204 TYR   BBB OH  1 ? 
ATOM   3588 N  N   . GLU   B 1 206 ? 37.109  29.051 58.092 1.000 24.820  ? 205 GLU   BBB N   1 ? 
ATOM   3589 C  CA  . GLU   B 1 206 ? 37.182  29.003 59.584 1.000 25.816  ? 205 GLU   BBB CA  1 ? 
ATOM   3590 C  C   . GLU   B 1 206 ? 37.932  30.227 60.069 1.000 24.721  ? 205 GLU   BBB C   1 ? 
ATOM   3591 O  O   . GLU   B 1 206 ? 39.022  30.110 60.608 1.000 28.221  ? 205 GLU   BBB O   1 ? 
ATOM   3592 C  CB  . GLU   B 1 206 ? 37.841  27.683 60.025 1.000 25.721  ? 205 GLU   BBB CB  1 ? 
ATOM   3593 C  CG  . GLU   B 1 206 ? 36.940  26.473 59.786 1.000 25.883  ? 205 GLU   BBB CG  1 ? 
ATOM   3594 C  CD  . GLU   B 1 206 ? 37.435  25.113 60.266 1.000 28.394  ? 205 GLU   BBB CD  1 ? 
ATOM   3595 O  OE1 . GLU   B 1 206 ? 36.559  24.218 60.349 1.000 31.507  ? 205 GLU   BBB OE1 1 ? 
ATOM   3596 O  OE2 . GLU   B 1 206 ? 38.645  24.964 60.550 1.000 34.633  ? 205 GLU   BBB OE2 1 ? 
ATOM   3597 N  N   . SER   B 1 207 ? 37.313  31.377 59.832 1.000 23.252  ? 206 SER   BBB N   1 ? 
ATOM   3598 C  CA  . SER   B 1 207 ? 37.929  32.734 59.884 1.000 21.127  ? 206 SER   BBB CA  1 ? 
ATOM   3599 C  C   . SER   B 1 207 ? 37.158  33.639 60.831 1.000 23.951  ? 206 SER   BBB C   1 ? 
ATOM   3600 O  O   . SER   B 1 207 ? 37.509  34.865 60.917 1.000 24.824  ? 206 SER   BBB O   1 ? 
ATOM   3601 C  CB  . SER   B 1 207 ? 37.970  33.270 58.501 1.000 23.039  ? 206 SER   BBB CB  1 ? 
ATOM   3602 O  OG  . SER   B 1 207 ? 36.666  33.262 57.918 1.000 24.205  ? 206 SER   BBB OG  1 ? 
ATOM   3603 N  N   . VAL   B 1 208 ? 36.115  33.108 61.467 1.000 23.514  ? 207 VAL   BBB N   1 ? 
ATOM   3604 C  CA  . VAL   B 1 208 ? 35.090  33.905 62.199 1.000 23.493  ? 207 VAL   BBB CA  1 ? 
ATOM   3605 C  C   . VAL   B 1 208 ? 35.236  33.793 63.720 1.000 25.743  ? 207 VAL   BBB C   1 ? 
ATOM   3606 O  O   . VAL   B 1 208 ? 35.148  32.685 64.297 1.000 23.142  ? 207 VAL   BBB O   1 ? 
ATOM   3607 C  CB  . VAL   B 1 208 ? 33.646  33.641 61.753 1.000 20.270  ? 207 VAL   BBB CB  1 ? 
ATOM   3608 C  CG1 . VAL   B 1 208 ? 32.682  34.597 62.460 1.000 23.298  ? 207 VAL   BBB CG1 1 ? 
ATOM   3609 C  CG2 . VAL   B 1 208 ? 33.511  33.829 60.262 1.000 21.776  ? 207 VAL   BBB CG2 1 ? 
ATOM   3610 N  N   . THR   B 1 209 ? 35.416  34.963 64.356 1.000 20.916  ? 208 THR   BBB N   1 ? 
ATOM   3611 C  CA  . THR   B 1 209 ? 35.247  35.070 65.823 1.000 21.436  ? 208 THR   BBB CA  1 ? 
ATOM   3612 C  C   . THR   B 1 209 ? 33.789  35.427 66.084 1.000 23.637  ? 208 THR   BBB C   1 ? 
ATOM   3613 O  O   . THR   B 1 209 ? 33.354  36.504 65.633 1.000 21.077  ? 208 THR   BBB O   1 ? 
ATOM   3614 C  CB  . THR   B 1 209 ? 36.183  36.070 66.499 1.000 24.563  ? 208 THR   BBB CB  1 ? 
ATOM   3615 O  OG1 . THR   B 1 209 ? 37.577  35.788 66.320 1.000 26.368  ? 208 THR   BBB OG1 1 ? 
ATOM   3616 C  CG2 . THR   B 1 209 ? 35.924  36.085 67.984 1.000 24.957  ? 208 THR   BBB CG2 1 ? 
ATOM   3617 N  N   . TRP   B 1 210 ? 33.007  34.491 66.622 1.000 22.572  ? 209 TRP   BBB N   1 ? 
ATOM   3618 C  CA  . TRP   B 1 210 ? 31.549  34.620 66.858 1.000 19.409  ? 209 TRP   BBB CA  1 ? 
ATOM   3619 C  C   . TRP   B 1 210 ? 31.304  35.346 68.168 1.000 21.750  ? 209 TRP   BBB C   1 ? 
ATOM   3620 O  O   . TRP   B 1 210 ? 31.971  34.991 69.151 1.000 22.125  ? 209 TRP   BBB O   1 ? 
ATOM   3621 C  CB  . TRP   B 1 210 ? 30.876  33.246 66.801 1.000 20.874  ? 209 TRP   BBB CB  1 ? 
ATOM   3622 C  CG  . TRP   B 1 210 ? 30.611  32.883 65.383 1.000 18.677  ? 209 TRP   BBB CG  1 ? 
ATOM   3623 C  CD1 . TRP   B 1 210 ? 31.394  32.060 64.599 1.000 22.213  ? 209 TRP   BBB CD1 1 ? 
ATOM   3624 C  CD2 . TRP   B 1 210 ? 29.525  33.341 64.560 1.000 19.683  ? 209 TRP   BBB CD2 1 ? 
ATOM   3625 N  NE1 . TRP   B 1 210 ? 30.880  31.990 63.343 1.000 21.412  ? 209 TRP   BBB NE1 1 ? 
ATOM   3626 C  CE2 . TRP   B 1 210 ? 29.726  32.758 63.291 1.000 21.063  ? 209 TRP   BBB CE2 1 ? 
ATOM   3627 C  CE3 . TRP   B 1 210 ? 28.442  34.214 64.754 1.000 19.162  ? 209 TRP   BBB CE3 1 ? 
ATOM   3628 C  CZ2 . TRP   B 1 210 ? 28.870  33.036 62.228 1.000 22.901  ? 209 TRP   BBB CZ2 1 ? 
ATOM   3629 C  CZ3 . TRP   B 1 210 ? 27.562  34.436 63.718 1.000 21.580  ? 209 TRP   BBB CZ3 1 ? 
ATOM   3630 C  CH2 . TRP   B 1 210 ? 27.766  33.832 62.473 1.000 21.872  ? 209 TRP   BBB CH2 1 ? 
ATOM   3631 N  N   . ILE   B 1 211 ? 30.511  36.430 68.099 1.000 19.591  ? 210 ILE   BBB N   1 ? 
ATOM   3632 C  CA  . ILE   B 1 211 ? 29.928  37.081 69.292 1.000 19.166  ? 210 ILE   BBB CA  1 ? 
ATOM   3633 C  C   . ILE   B 1 211 ? 28.417  36.881 69.309 1.000 19.472  ? 210 ILE   BBB C   1 ? 
ATOM   3634 O  O   . ILE   B 1 211 ? 27.749  37.429 68.415 1.000 20.669  ? 210 ILE   BBB O   1 ? 
ATOM   3635 C  CB  . ILE   B 1 211 ? 30.232  38.605 69.214 1.000 20.637  ? 210 ILE   BBB CB  1 ? 
ATOM   3636 C  CG1 . ILE   B 1 211 ? 31.729  38.899 69.059 1.000 24.579  ? 210 ILE   BBB CG1 1 ? 
ATOM   3637 C  CG2 . ILE   B 1 211 ? 29.575  39.197 70.436 1.000 20.261  ? 210 ILE   BBB CG2 1 ? 
ATOM   3638 C  CD1 . ILE   B 1 211 ? 32.593  38.628 70.243 1.000 29.517  ? 210 ILE   BBB CD1 1 ? 
ATOM   3639 N  N   . ILE   B 1 212 ? 27.907  35.951 70.168 1.000 22.222  ? 211 ILE   BBB N   1 ? 
ATOM   3640 C  CA  . ILE   B 1 212 ? 26.458  35.682 70.253 1.000 19.322  ? 211 ILE   BBB CA  1 ? 
ATOM   3641 C  C   . ILE   B 1 212 ? 25.822  36.405 71.428 1.000 20.060  ? 211 ILE   BBB C   1 ? 
ATOM   3642 O  O   . ILE   B 1 212 ? 26.285  36.186 72.557 1.000 20.916  ? 211 ILE   BBB O   1 ? 
ATOM   3643 C  CB  . ILE   B 1 212 ? 26.210  34.152 70.306 1.000 20.044  ? 211 ILE   BBB CB  1 ? 
ATOM   3644 C  CG1 . ILE   B 1 212 ? 26.975  33.519 69.153 1.000 22.504  ? 211 ILE   BBB CG1 1 ? 
ATOM   3645 C  CG2 . ILE   B 1 212 ? 24.703  33.918 70.306 1.000 20.658  ? 211 ILE   BBB CG2 1 ? 
ATOM   3646 C  CD1 . ILE   B 1 212 ? 26.439  33.780 67.798 1.000 21.530  ? 211 ILE   BBB CD1 1 ? 
ATOM   3647 N  N   . CYS   B 1 213 ? 24.891  37.349 71.155 1.000 19.128  ? 212 CYS   BBB N   1 ? 
ATOM   3648 C  CA  . CYS   B 1 213 ? 24.272  38.125 72.249 1.000 22.214  ? 212 CYS   BBB CA  1 ? 
ATOM   3649 C  C   . CYS   B 1 213 ? 23.430  37.176 73.129 1.000 19.592  ? 212 CYS   BBB C   1 ? 
ATOM   3650 O  O   . CYS   B 1 213 ? 22.693  36.310 72.605 1.000 20.580  ? 212 CYS   BBB O   1 ? 
ATOM   3651 C  CB  . CYS   B 1 213 ? 23.405  39.248 71.676 1.000 22.435  ? 212 CYS   BBB CB  1 ? 
ATOM   3652 S  SG  . CYS   B 1 213 ? 24.358  40.558 70.869 1.000 22.328  ? 212 CYS   BBB SG  1 ? 
ATOM   3653 N  N   . LYS   B 1 214 ? 23.538  37.326 74.424 1.000 19.001  ? 213 LYS   BBB N   1 ? 
ATOM   3654 C  CA  . LYS   B 1 214 ? 22.671  36.690 75.434 1.000 21.135  ? 213 LYS   BBB CA  1 ? 
ATOM   3655 C  C   . LYS   B 1 214 ? 21.205  37.061 75.199 1.000 21.365  ? 213 LYS   BBB C   1 ? 
ATOM   3656 O  O   . LYS   B 1 214 ? 20.327  36.211 75.286 1.000 27.064  ? 213 LYS   BBB O   1 ? 
ATOM   3657 C  CB  . LYS   B 1 214 ? 23.145  37.025 76.849 1.000 26.185  ? 213 LYS   BBB CB  1 ? 
ATOM   3658 C  CG  . LYS   B 1 214 ? 22.402  36.313 77.978 1.000 30.639  ? 213 LYS   BBB CG  1 ? 
ATOM   3659 C  CD  . LYS   B 1 214 ? 22.556  36.925 79.363 1.000 39.561  ? 213 LYS   BBB CD  1 ? 
ATOM   3660 C  CE  . LYS   B 1 214 ? 21.747  38.203 79.490 1.000 48.409  ? 213 LYS   BBB CE  1 ? 
ATOM   3661 N  NZ  . LYS   B 1 214 ? 22.305  39.229 80.418 1.000 55.163  ? 213 LYS   BBB NZ  1 ? 
ATOM   3662 N  N   . GLU   B 1 215 ? 20.901  38.316 74.903 1.000 19.389  ? 214 GLU   BBB N   1 ? 
ATOM   3663 C  CA  . GLU   B 1 215 ? 19.496  38.744 74.781 1.000 20.079  ? 214 GLU   BBB CA  1 ? 
ATOM   3664 C  C   . GLU   B 1 215 ? 19.052  38.624 73.313 1.000 18.963  ? 214 GLU   BBB C   1 ? 
ATOM   3665 O  O   . GLU   B 1 215 ? 19.877  38.902 72.358 1.000 20.105  ? 214 GLU   BBB O   1 ? 
ATOM   3666 C  CB  . GLU   B 1 215 ? 19.367  40.215 75.212 1.000 21.561  ? 214 GLU   BBB CB  1 ? 
ATOM   3667 C  CG  . GLU   B 1 215 ? 19.743  40.464 76.656 1.000 29.556  ? 214 GLU   BBB CG  1 ? 
ATOM   3668 C  CD  . GLU   B 1 215 ? 19.076  39.656 77.783 1.000 42.132  ? 214 GLU   BBB CD  1 ? 
ATOM   3669 O  OE1 . GLU   B 1 215 ? 18.012  39.034 77.569 1.000 52.665  ? 214 GLU   BBB OE1 1 ? 
ATOM   3670 O  OE2 . GLU   B 1 215 ? 19.601  39.695 78.920 1.000 57.346  ? 214 GLU   BBB OE2 1 ? 
ATOM   3671 N  N   . SER   B 1 216 ? 17.784  38.271 73.136 1.000 18.838  ? 215 SER   BBB N   1 ? 
ATOM   3672 C  CA  . SER   B 1 216 ? 17.127  38.123 71.829 1.000 21.490  ? 215 SER   BBB CA  1 ? 
ATOM   3673 C  C   . SER   B 1 216 ? 16.465  39.489 71.454 1.000 20.096  ? 215 SER   BBB C   1 ? 
ATOM   3674 O  O   . SER   B 1 216 ? 16.304  40.362 72.380 1.000 23.583  ? 215 SER   BBB O   1 ? 
ATOM   3675 C  CB  . SER   B 1 216 ? 16.196  36.950 71.830 1.000 23.408  ? 215 SER   BBB CB  1 ? 
ATOM   3676 O  OG  . SER   B 1 216 ? 15.200  37.049 72.811 1.000 26.231  ? 215 SER   BBB OG  1 ? 
ATOM   3677 N  N   . ILE   B 1 217 ? 16.009  39.616 70.209 1.000 19.851  ? 216 ILE   BBB N   1 ? 
ATOM   3678 C  CA  . ILE   B 1 217 ? 15.131  40.741 69.775 1.000 19.779  ? 216 ILE   BBB CA  1 ? 
ATOM   3679 C  C   . ILE   B 1 217 ? 13.870  40.120 69.179 1.000 20.288  ? 216 ILE   BBB C   1 ? 
ATOM   3680 O  O   . ILE   B 1 217 ? 13.906  38.826 68.912 1.000 22.614  ? 216 ILE   BBB O   1 ? 
ATOM   3681 C  CB  . ILE   B 1 217 ? 15.879  41.619 68.754 1.000 21.759  ? 216 ILE   BBB CB  1 ? 
ATOM   3682 C  CG1 . ILE   B 1 217 ? 16.204  40.825 67.477 1.000 20.021  ? 216 ILE   BBB CG1 1 ? 
ATOM   3683 C  CG2 . ILE   B 1 217 ? 17.103  42.276 69.378 1.000 22.122  ? 216 ILE   BBB CG2 1 ? 
ATOM   3684 C  CD1 . ILE   B 1 217 ? 16.889  41.588 66.342 1.000 22.441  ? 216 ILE   BBB CD1 1 ? 
ATOM   3685 N  N   . SER   B 1 218 ? 12.827  40.906 68.959 1.000 22.976  ? 217 SER   BBB N   1 ? 
ATOM   3686 C  CA  A SER   B 1 218 ? 11.523  40.421 68.443 0.500 23.017  ? 217 SER   BBB CA  1 ? 
ATOM   3687 C  CA  B SER   B 1 218 ? 11.534  40.404 68.442 0.500 23.864  ? 217 SER   BBB CA  1 ? 
ATOM   3688 C  C   . SER   B 1 218 ? 11.487  40.424 66.910 1.000 23.083  ? 217 SER   BBB C   1 ? 
ATOM   3689 O  O   . SER   B 1 218 ? 12.372  41.042 66.266 1.000 22.084  ? 217 SER   BBB O   1 ? 
ATOM   3690 C  CB  A SER   B 1 218 ? 10.357  41.181 69.021 0.500 21.454  ? 217 SER   BBB CB  1 ? 
ATOM   3691 C  CB  B SER   B 1 218 ? 10.376  41.139 69.028 0.500 25.391  ? 217 SER   BBB CB  1 ? 
ATOM   3692 O  OG  A SER   B 1 218 ? 10.230  42.479 68.441 0.500 25.030  ? 217 SER   BBB OG  1 ? 
ATOM   3693 O  OG  B SER   B 1 218 ? 9.203   40.354 68.909 0.500 25.837  ? 217 SER   BBB OG  1 ? 
ATOM   3694 N  N   . VAL   B 1 219 ? 10.481  39.745 66.366 1.000 22.478  ? 218 VAL   BBB N   1 ? 
ATOM   3695 C  CA  . VAL   B 1 219 ? 10.103  39.747 64.935 1.000 23.705  ? 218 VAL   BBB CA  1 ? 
ATOM   3696 C  C   . VAL   B 1 219 ? 8.697   39.159 64.902 1.000 24.308  ? 218 VAL   BBB C   1 ? 
ATOM   3697 O  O   . VAL   B 1 219 ? 8.410   38.244 65.763 1.000 25.076  ? 218 VAL   BBB O   1 ? 
ATOM   3698 C  CB  . VAL   B 1 219 ? 11.121  38.974 64.065 1.000 20.508  ? 218 VAL   BBB CB  1 ? 
ATOM   3699 C  CG1 . VAL   B 1 219 ? 11.181  37.496 64.378 1.000 21.883  ? 218 VAL   BBB CG1 1 ? 
ATOM   3700 C  CG2 . VAL   B 1 219 ? 10.927  39.180 62.568 1.000 23.122  ? 218 VAL   BBB CG2 1 ? 
ATOM   3701 N  N   . SER   B 1 220 ? 7.813   39.685 64.057 1.000 23.746  ? 219 SER   BBB N   1 ? 
ATOM   3702 C  CA  . SER   B 1 220 ? 6.441   39.131 63.902 1.000 26.607  ? 219 SER   BBB CA  1 ? 
ATOM   3703 C  C   . SER   B 1 220 ? 6.472   38.010 62.867 1.000 22.713  ? 219 SER   BBB C   1 ? 
ATOM   3704 O  O   . SER   B 1 220 ? 7.362   38.030 61.937 1.000 23.488  ? 219 SER   BBB O   1 ? 
ATOM   3705 C  CB  . SER   B 1 220 ? 5.392   40.146 63.500 1.000 28.811  ? 219 SER   BBB CB  1 ? 
ATOM   3706 O  OG  . SER   B 1 220 ? 5.648   40.645 62.188 1.000 25.942  ? 219 SER   BBB OG  1 ? 
ATOM   3707 N  N   . SER   B 1 221 ? 5.422   37.196 62.908 1.000 28.254  ? 220 SER   BBB N   1 ? 
ATOM   3708 C  CA  . SER   B 1 221 ? 5.113   36.158 61.878 1.000 25.335  ? 220 SER   BBB CA  1 ? 
ATOM   3709 C  C   . SER   B 1 221 ? 5.095   36.822 60.495 1.000 28.977  ? 220 SER   BBB C   1 ? 
ATOM   3710 O  O   . SER   B 1 221 ? 5.652   36.237 59.569 1.000 27.076  ? 220 SER   BBB O   1 ? 
ATOM   3711 C  CB  . SER   B 1 221 ? 3.819   35.481 62.164 1.000 29.364  ? 220 SER   BBB CB  1 ? 
ATOM   3712 O  OG  . SER   B 1 221 ? 3.674   34.291 61.354 1.000 36.828  ? 220 SER   BBB OG  1 ? 
ATOM   3713 N  N   . GLU   B 1 222 ? 4.514   38.034 60.361 1.000 26.114  ? 221 GLU   BBB N   1 ? 
ATOM   3714 C  CA  . GLU   B 1 222 ? 4.330   38.637 59.013 1.000 28.309  ? 221 GLU   BBB CA  1 ? 
ATOM   3715 C  C   . GLU   B 1 222 ? 5.683   39.184 58.539 1.000 26.870  ? 221 GLU   BBB C   1 ? 
ATOM   3716 O  O   . GLU   B 1 222 ? 5.930   39.155 57.340 1.000 26.865  ? 221 GLU   BBB O   1 ? 
ATOM   3717 C  CB  . GLU   B 1 222 ? 3.187   39.666 58.961 1.000 32.159  ? 221 GLU   BBB CB  1 ? 
ATOM   3718 C  CG  . GLU   B 1 222 ? 1.808   39.056 59.273 1.000 31.054  ? 221 GLU   BBB CG  1 ? 
ATOM   3719 C  CD  . GLU   B 1 222 ? 1.661   38.510 60.692 1.000 31.745  ? 221 GLU   BBB CD  1 ? 
ATOM   3720 O  OE1 . GLU   B 1 222 ? 2.080   39.208 61.644 1.000 36.659  ? 221 GLU   BBB OE1 1 ? 
ATOM   3721 O  OE2 . GLU   B 1 222 ? 1.116   37.393 60.858 1.000 34.684  ? 221 GLU   BBB OE2 1 ? 
ATOM   3722 N  N   . GLN   B 1 223 ? 6.548   39.663 59.433 1.000 26.474  ? 222 GLN   BBB N   1 ? 
ATOM   3723 C  CA  . GLN   B 1 223 ? 7.897   40.139 59.034 1.000 23.221  ? 222 GLN   BBB CA  1 ? 
ATOM   3724 C  C   . GLN   B 1 223 ? 8.693   38.924 58.497 1.000 24.437  ? 222 GLN   BBB C   1 ? 
ATOM   3725 O  O   . GLN   B 1 223 ? 9.396   39.026 57.443 1.000 25.829  ? 222 GLN   BBB O   1 ? 
ATOM   3726 C  CB  . GLN   B 1 223 ? 8.529   40.857 60.218 1.000 21.714  ? 222 GLN   BBB CB  1 ? 
ATOM   3727 C  CG  . GLN   B 1 223 ? 7.898   42.216 60.522 1.000 24.596  ? 222 GLN   BBB CG  1 ? 
ATOM   3728 C  CD  . GLN   B 1 223 ? 8.548   42.902 61.696 1.000 21.136  ? 222 GLN   BBB CD  1 ? 
ATOM   3729 O  OE1 . GLN   B 1 223 ? 8.874   42.278 62.707 1.000 22.919  ? 222 GLN   BBB OE1 1 ? 
ATOM   3730 N  NE2 . GLN   B 1 223 ? 8.662   44.242 61.611 1.000 22.901  ? 222 GLN   BBB NE2 1 ? 
ATOM   3731 N  N   . LEU   B 1 224 ? 8.610   37.789 59.162 1.000 23.212  ? 223 LEU   BBB N   1 ? 
ATOM   3732 C  CA  . LEU   B 1 224 ? 9.288   36.585 58.614 1.000 26.213  ? 223 LEU   BBB CA  1 ? 
ATOM   3733 C  C   . LEU   B 1 224 ? 8.726   36.187 57.227 1.000 23.606  ? 223 LEU   BBB C   1 ? 
ATOM   3734 O  O   . LEU   B 1 224 ? 9.538   35.810 56.330 1.000 24.803  ? 223 LEU   BBB O   1 ? 
ATOM   3735 C  CB  . LEU   B 1 224 ? 9.145   35.478 59.652 1.000 24.060  ? 223 LEU   BBB CB  1 ? 
ATOM   3736 C  CG  . LEU   B 1 224 ? 9.934   35.699 60.947 1.000 26.721  ? 223 LEU   BBB CG  1 ? 
ATOM   3737 C  CD1 . LEU   B 1 224 ? 9.612   34.635 61.990 1.000 34.305  ? 223 LEU   BBB CD1 1 ? 
ATOM   3738 C  CD2 . LEU   B 1 224 ? 11.436  35.707 60.686 1.000 27.080  ? 223 LEU   BBB CD2 1 ? 
ATOM   3739 N  N   . ALA   B 1 225 ? 7.407   36.301 57.015 1.000 23.298  ? 224 ALA   BBB N   1 ? 
ATOM   3740 C  CA  . ALA   B 1 225 ? 6.773   36.045 55.708 1.000 24.585  ? 224 ALA   BBB CA  1 ? 
ATOM   3741 C  C   . ALA   B 1 225 ? 7.389   36.947 54.640 1.000 22.774  ? 224 ALA   BBB C   1 ? 
ATOM   3742 O  O   . ALA   B 1 225 ? 7.543   36.508 53.518 1.000 27.496  ? 224 ALA   BBB O   1 ? 
ATOM   3743 C  CB  . ALA   B 1 225 ? 5.289   36.265 55.779 1.000 26.530  ? 224 ALA   BBB CB  1 ? 
ATOM   3744 N  N   . GLN   B 1 226 ? 7.666   38.219 54.960 1.000 24.560  ? 225 GLN   BBB N   1 ? 
ATOM   3745 C  CA  . GLN   B 1 226 ? 8.281   39.125 53.961 1.000 25.284  ? 225 GLN   BBB CA  1 ? 
ATOM   3746 C  C   . GLN   B 1 226 ? 9.654   38.587 53.544 1.000 20.688  ? 225 GLN   BBB C   1 ? 
ATOM   3747 O  O   . GLN   B 1 226 ? 9.917   38.583 52.339 1.000 27.781  ? 225 GLN   BBB O   1 ? 
ATOM   3748 C  CB  . GLN   B 1 226 ? 8.419   40.550 54.491 1.000 27.059  ? 225 GLN   BBB CB  1 ? 
ATOM   3749 C  CG  . GLN   B 1 226 ? 7.108   41.268 54.584 1.000 28.287  ? 225 GLN   BBB CG  1 ? 
ATOM   3750 C  CD  . GLN   B 1 226 ? 7.341   42.718 54.928 1.000 32.158  ? 225 GLN   BBB CD  1 ? 
ATOM   3751 O  OE1 . GLN   B 1 226 ? 7.123   43.133 56.068 1.000 32.013  ? 225 GLN   BBB OE1 1 ? 
ATOM   3752 N  NE2 . GLN   B 1 226 ? 7.817   43.490 53.948 1.000 31.291  ? 225 GLN   BBB NE2 1 ? 
ATOM   3753 N  N   . PHE   B 1 227 ? 10.505  38.147 54.474 1.000 24.335  ? 226 PHE   BBB N   1 ? 
ATOM   3754 C  CA  . PHE   B 1 227 ? 11.788  37.490 54.118 1.000 21.786  ? 226 PHE   BBB CA  1 ? 
ATOM   3755 C  C   . PHE   B 1 227 ? 11.504  36.319 53.155 1.000 25.743  ? 226 PHE   BBB C   1 ? 
ATOM   3756 O  O   . PHE   B 1 227 ? 12.161  36.199 52.106 1.000 26.262  ? 226 PHE   BBB O   1 ? 
ATOM   3757 C  CB  . PHE   B 1 227 ? 12.500  36.930 55.338 1.000 27.944  ? 226 PHE   BBB CB  1 ? 
ATOM   3758 C  CG  . PHE   B 1 227 ? 13.053  37.891 56.347 1.000 26.396  ? 226 PHE   BBB CG  1 ? 
ATOM   3759 C  CD1 . PHE   B 1 227 ? 13.274  39.230 56.058 1.000 30.078  ? 226 PHE   BBB CD1 1 ? 
ATOM   3760 C  CD2 . PHE   B 1 227 ? 13.375  37.435 57.614 1.000 28.094  ? 226 PHE   BBB CD2 1 ? 
ATOM   3761 C  CE1 . PHE   B 1 227 ? 13.778  40.077 57.031 1.000 28.126  ? 226 PHE   BBB CE1 1 ? 
ATOM   3762 C  CE2 . PHE   B 1 227 ? 13.884  38.283 58.578 1.000 28.526  ? 226 PHE   BBB CE2 1 ? 
ATOM   3763 C  CZ  . PHE   B 1 227 ? 14.108  39.604 58.276 1.000 30.007  ? 226 PHE   BBB CZ  1 ? 
ATOM   3764 N  N   . ARG   B 1 228 ? 10.484  35.530 53.451 1.000 24.082  ? 227 ARG   BBB N   1 ? 
ATOM   3765 C  CA  . ARG   B 1 228 ? 10.247  34.290 52.651 1.000 24.831  ? 227 ARG   BBB CA  1 ? 
ATOM   3766 C  C   . ARG   B 1 228 ? 9.570   34.624 51.307 1.000 28.371  ? 227 ARG   BBB C   1 ? 
ATOM   3767 O  O   . ARG   B 1 228 ? 9.456   33.707 50.455 1.000 33.552  ? 227 ARG   BBB O   1 ? 
ATOM   3768 C  CB  . ARG   B 1 228 ? 9.353   33.318 53.416 1.000 27.496  ? 227 ARG   BBB CB  1 ? 
ATOM   3769 C  CG  . ARG   B 1 228 ? 9.965   32.757 54.685 1.000 28.689  ? 227 ARG   BBB CG  1 ? 
ATOM   3770 C  CD  . ARG   B 1 228 ? 9.227   31.493 55.113 1.000 30.518  ? 227 ARG   BBB CD  1 ? 
ATOM   3771 N  NE  . ARG   B 1 228 ? 9.461   31.308 56.522 1.000 34.792  ? 227 ARG   BBB NE  1 ? 
ATOM   3772 C  CZ  . ARG   B 1 228 ? 8.715   31.788 57.512 1.000 29.174  ? 227 ARG   BBB CZ  1 ? 
ATOM   3773 N  NH1 . ARG   B 1 228 ? 9.083   31.541 58.758 1.000 32.160  ? 227 ARG   BBB NH1 1 ? 
ATOM   3774 N  NH2 . ARG   B 1 228 ? 7.593   32.432 57.269 1.000 30.643  ? 227 ARG   BBB NH2 1 ? 
ATOM   3775 N  N   . SER   B 1 229 ? 9.081   35.862 51.127 1.000 23.844  ? 228 SER   BBB N   1 ? 
ATOM   3776 C  CA  . SER   B 1 229 ? 8.483   36.345 49.858 1.000 24.204  ? 228 SER   BBB CA  1 ? 
ATOM   3777 C  C   . SER   B 1 229 ? 9.598   36.776 48.883 1.000 25.724  ? 228 SER   BBB C   1 ? 
ATOM   3778 O  O   . SER   B 1 229 ? 9.278   37.061 47.697 1.000 28.271  ? 228 SER   BBB O   1 ? 
ATOM   3779 C  CB  . SER   B 1 229 ? 7.426   37.403 50.096 1.000 31.683  ? 228 SER   BBB CB  1 ? 
ATOM   3780 O  OG  . SER   B 1 229 ? 8.018   38.670 50.346 1.000 38.827  ? 228 SER   BBB OG  1 ? 
ATOM   3781 N  N   . LEU   B 1 230 ? 10.866  36.798 49.319 1.000 25.975  ? 229 LEU   BBB N   1 ? 
ATOM   3782 C  CA  . LEU   B 1 230 ? 11.996  37.026 48.388 1.000 26.688  ? 229 LEU   BBB CA  1 ? 
ATOM   3783 C  C   . LEU   B 1 230 ? 12.134  35.819 47.455 1.000 28.243  ? 229 LEU   BBB C   1 ? 
ATOM   3784 O  O   . LEU   B 1 230 ? 11.830  34.667 47.911 1.000 28.336  ? 229 LEU   BBB O   1 ? 
ATOM   3785 C  CB  . LEU   B 1 230 ? 13.296  37.275 49.137 1.000 24.962  ? 229 LEU   BBB CB  1 ? 
ATOM   3786 C  CG  . LEU   B 1 230 ? 13.449  38.670 49.728 1.000 28.910  ? 229 LEU   BBB CG  1 ? 
ATOM   3787 C  CD1 . LEU   B 1 230 ? 14.644  38.661 50.679 1.000 28.736  ? 229 LEU   BBB CD1 1 ? 
ATOM   3788 C  CD2 . LEU   B 1 230 ? 13.586  39.741 48.636 1.000 32.035  ? 229 LEU   BBB CD2 1 ? 
ATOM   3789 N  N   . LEU   B 1 231 ? 12.578  36.075 46.224 1.000 31.587  ? 230 LEU   BBB N   1 ? 
ATOM   3790 C  CA  . LEU   B 1 231 ? 12.702  35.005 45.212 1.000 27.719  ? 230 LEU   BBB CA  1 ? 
ATOM   3791 C  C   . LEU   B 1 231 ? 14.171  34.627 44.963 1.000 27.908  ? 230 LEU   BBB C   1 ? 
ATOM   3792 O  O   . LEU   B 1 231 ? 15.026  35.523 44.834 1.000 25.916  ? 230 LEU   BBB O   1 ? 
ATOM   3793 C  CB  . LEU   B 1 231 ? 11.990  35.477 43.944 1.000 31.189  ? 230 LEU   BBB CB  1 ? 
ATOM   3794 C  CG  . LEU   B 1 231 ? 10.510  35.857 44.086 1.000 31.932  ? 230 LEU   BBB CG  1 ? 
ATOM   3795 C  CD1 . LEU   B 1 231 ? 9.901   36.201 42.706 1.000 36.630  ? 230 LEU   BBB CD1 1 ? 
ATOM   3796 C  CD2 . LEU   B 1 231 ? 9.682   34.775 44.799 1.000 36.243  ? 230 LEU   BBB CD2 1 ? 
ATOM   3797 N  N   . SER   B 1 232 ? 14.445  33.304 44.860 1.000 27.588  ? 231 SER   BBB N   1 ? 
ATOM   3798 C  CA  . SER   B 1 232 ? 15.805  32.747 44.655 1.000 30.234  ? 231 SER   BBB CA  1 ? 
ATOM   3799 C  C   . SER   B 1 232 ? 16.152  32.737 43.156 1.000 28.527  ? 231 SER   BBB C   1 ? 
ATOM   3800 O  O   . SER   B 1 232 ? 17.360  32.594 42.794 1.000 30.074  ? 231 SER   BBB O   1 ? 
ATOM   3801 C  CB  . SER   B 1 232 ? 15.934  31.380 45.306 1.000 29.338  ? 231 SER   BBB CB  1 ? 
ATOM   3802 O  OG  . SER   B 1 232 ? 14.971  30.476 44.790 1.000 31.692  ? 231 SER   BBB OG  1 ? 
ATOM   3803 N  N   . ASN   B 1 233 ? 15.140  32.909 42.314 1.000 26.880  ? 232 ASN   BBB N   1 ? 
ATOM   3804 C  CA  . ASN   B 1 233 ? 15.233  32.788 40.839 1.000 29.371  ? 232 ASN   BBB CA  1 ? 
ATOM   3805 C  C   . ASN   B 1 233 ? 15.629  34.158 40.278 1.000 30.208  ? 232 ASN   BBB C   1 ? 
ATOM   3806 O  O   . ASN   B 1 233 ? 15.371  35.218 40.931 1.000 30.968  ? 232 ASN   BBB O   1 ? 
ATOM   3807 C  CB  . ASN   B 1 233 ? 13.930  32.277 40.211 1.000 31.184  ? 232 ASN   BBB CB  1 ? 
ATOM   3808 C  CG  . ASN   B 1 233 ? 12.746  33.166 40.547 1.000 27.035  ? 232 ASN   BBB CG  1 ? 
ATOM   3809 O  OD1 . ASN   B 1 233 ? 12.190  33.057 41.629 1.000 33.961  ? 232 ASN   BBB OD1 1 ? 
ATOM   3810 N  ND2 . ASN   B 1 233 ? 12.360  34.052 39.640 1.000 31.897  ? 232 ASN   BBB ND2 1 ? 
ATOM   3811 N  N   . VAL   B 1 234 ? 16.209  34.132 39.097 1.000 33.626  ? 233 VAL   BBB N   1 ? 
ATOM   3812 C  CA  . VAL   B 1 234 ? 16.412  35.370 38.300 1.000 35.121  ? 233 VAL   BBB CA  1 ? 
ATOM   3813 C  C   . VAL   B 1 234 ? 15.066  35.786 37.698 1.000 31.537  ? 233 VAL   BBB C   1 ? 
ATOM   3814 O  O   . VAL   B 1 234 ? 14.159  34.951 37.531 1.000 37.031  ? 233 VAL   BBB O   1 ? 
ATOM   3815 C  CB  . VAL   B 1 234 ? 17.504  35.194 37.233 1.000 37.850  ? 233 VAL   BBB CB  1 ? 
ATOM   3816 C  CG1 . VAL   B 1 234 ? 18.801  34.663 37.847 1.000 40.001  ? 233 VAL   BBB CG1 1 ? 
ATOM   3817 C  CG2 . VAL   B 1 234 ? 17.040  34.295 36.100 1.000 44.665  ? 233 VAL   BBB CG2 1 ? 
ATOM   3818 N  N   . GLU   B 1 235 ? 14.976  37.074 37.399 1.000 34.754  ? 234 GLU   BBB N   1 ? 
ATOM   3819 C  CA  . GLU   B 1 235 ? 13.776  37.748 36.860 1.000 33.486  ? 234 GLU   BBB CA  1 ? 
ATOM   3820 C  C   . GLU   B 1 235 ? 13.341  36.996 35.612 1.000 38.413  ? 234 GLU   BBB C   1 ? 
ATOM   3821 O  O   . GLU   B 1 235 ? 14.209  36.709 34.788 1.000 42.445  ? 234 GLU   BBB O   1 ? 
ATOM   3822 C  CB  . GLU   B 1 235 ? 14.086  39.207 36.530 1.000 33.266  ? 234 GLU   BBB CB  1 ? 
ATOM   3823 C  CG  . GLU   B 1 235 ? 12.843  39.962 36.165 1.000 38.898  ? 234 GLU   BBB CG  1 ? 
ATOM   3824 C  CD  . GLU   B 1 235 ? 13.053  41.453 35.995 1.000 35.911  ? 234 GLU   BBB CD  1 ? 
ATOM   3825 O  OE1 . GLU   B 1 235 ? 13.228  42.153 37.001 1.000 46.534  ? 234 GLU   BBB OE1 1 ? 
ATOM   3826 O  OE2 . GLU   B 1 235 ? 13.033  41.902 34.856 1.000 55.876  ? 234 GLU   BBB OE2 1 ? 
ATOM   3827 N  N   . GLY   B 1 236 ? 12.066  36.638 35.522 1.000 40.550  ? 235 GLY   BBB N   1 ? 
ATOM   3828 C  CA  . GLY   B 1 236 ? 11.495  36.046 34.301 1.000 43.633  ? 235 GLY   BBB CA  1 ? 
ATOM   3829 C  C   . GLY   B 1 236 ? 11.346  34.543 34.394 1.000 40.709  ? 235 GLY   BBB C   1 ? 
ATOM   3830 O  O   . GLY   B 1 236 ? 10.526  34.004 33.632 1.000 54.511  ? 235 GLY   BBB O   1 ? 
ATOM   3831 N  N   . ASP   B 1 237 ? 12.101  33.880 35.271 1.000 36.540  ? 236 ASP   BBB N   1 ? 
ATOM   3832 C  CA  . ASP   B 1 237 ? 11.929  32.423 35.534 1.000 38.658  ? 236 ASP   BBB CA  1 ? 
ATOM   3833 C  C   . ASP   B 1 237 ? 10.764  32.255 36.509 1.000 41.747  ? 236 ASP   BBB C   1 ? 
ATOM   3834 O  O   . ASP   B 1 237 ? 10.368  33.313 37.117 1.000 43.232  ? 236 ASP   BBB O   1 ? 
ATOM   3835 C  CB  . ASP   B 1 237 ? 13.198  31.794 36.103 1.000 39.994  ? 236 ASP   BBB CB  1 ? 
ATOM   3836 C  CG  . ASP   B 1 237 ? 14.312  31.604 35.085 1.000 46.352  ? 236 ASP   BBB CG  1 ? 
ATOM   3837 O  OD1 . ASP   B 1 237 ? 14.138  32.009 33.913 1.000 47.895  ? 236 ASP   BBB OD1 1 ? 
ATOM   3838 O  OD2 . ASP   B 1 237 ? 15.351  31.044 35.471 1.000 50.387  ? 236 ASP   BBB OD2 1 ? 
ATOM   3839 N  N   . ASN   B 1 238 ? 10.241  31.024 36.687 1.000 41.399  ? 237 ASN   BBB N   1 ? 
ATOM   3840 C  CA  . ASN   B 1 238 ? 9.100   30.809 37.621 1.000 46.235  ? 237 ASN   BBB CA  1 ? 
ATOM   3841 C  C   . ASN   B 1 238 ? 9.594   31.105 39.040 1.000 37.147  ? 237 ASN   BBB C   1 ? 
ATOM   3842 O  O   . ASN   B 1 238 ? 10.759  30.772 39.404 1.000 39.637  ? 237 ASN   BBB O   1 ? 
ATOM   3843 C  CB  . ASN   B 1 238 ? 8.393   29.447 37.569 1.000 59.011  ? 237 ASN   BBB CB  1 ? 
ATOM   3844 C  CG  . ASN   B 1 238 ? 6.898   29.517 37.899 1.000 64.122  ? 237 ASN   BBB CG  1 ? 
ATOM   3845 O  OD1 . ASN   B 1 238 ? 6.441   30.442 38.598 1.000 45.727  ? 237 ASN   BBB OD1 1 ? 
ATOM   3846 N  ND2 . ASN   B 1 238 ? 6.118   28.557 37.380 1.000 49.201  ? 237 ASN   BBB ND2 1 ? 
ATOM   3847 N  N   . ALA   B 1 239 ? 8.736   31.765 39.800 1.000 49.137  ? 238 ALA   BBB N   1 ? 
ATOM   3848 C  CA  . ALA   B 1 239 ? 9.076   32.304 41.122 1.000 40.849  ? 238 ALA   BBB CA  1 ? 
ATOM   3849 C  C   . ALA   B 1 239 ? 9.359   31.132 42.064 1.000 40.728  ? 238 ALA   BBB C   1 ? 
ATOM   3850 O  O   . ALA   B 1 239 ? 8.562   30.181 42.060 1.000 48.190  ? 238 ALA   BBB O   1 ? 
ATOM   3851 C  CB  . ALA   B 1 239 ? 7.953   33.196 41.578 1.000 50.934  ? 238 ALA   BBB CB  1 ? 
ATOM   3852 N  N   . VAL   B 1 240 ? 10.492  31.178 42.781 1.000 39.528  ? 239 VAL   BBB N   1 ? 
ATOM   3853 C  CA  . VAL   B 1 240 ? 10.885  30.175 43.819 1.000 36.562  ? 239 VAL   BBB CA  1 ? 
ATOM   3854 C  C   . VAL   B 1 240 ? 11.154  30.956 45.104 1.000 30.784  ? 239 VAL   BBB C   1 ? 
ATOM   3855 O  O   . VAL   B 1 240 ? 12.173  31.638 45.262 1.000 33.164  ? 239 VAL   BBB O   1 ? 
ATOM   3856 C  CB  . VAL   B 1 240 ? 12.064  29.272 43.381 1.000 36.255  ? 239 VAL   BBB CB  1 ? 
ATOM   3857 C  CG1 . VAL   B 1 240 ? 12.390  28.215 44.449 1.000 42.055  ? 239 VAL   BBB CG1 1 ? 
ATOM   3858 C  CG2 . VAL   B 1 240 ? 11.843  28.650 41.985 1.000 35.055  ? 239 VAL   BBB CG2 1 ? 
ATOM   3859 N  N   . PRO   B 1 241 ? 10.211  30.907 46.057 1.000 36.190  ? 240 PRO   BBB N   1 ? 
ATOM   3860 C  CA  . PRO   B 1 241 ? 10.391  31.615 47.323 1.000 33.351  ? 240 PRO   BBB CA  1 ? 
ATOM   3861 C  C   . PRO   B 1 241 ? 11.610  31.103 48.099 1.000 28.733  ? 240 PRO   BBB C   1 ? 
ATOM   3862 O  O   . PRO   B 1 241 ? 11.872  29.920 48.122 1.000 36.822  ? 240 PRO   BBB O   1 ? 
ATOM   3863 C  CB  . PRO   B 1 241 ? 9.081   31.368 48.075 1.000 40.091  ? 240 PRO   BBB CB  1 ? 
ATOM   3864 C  CG  . PRO   B 1 241 ? 8.088   31.131 46.948 1.000 45.053  ? 240 PRO   BBB CG  1 ? 
ATOM   3865 C  CD  . PRO   B 1 241 ? 8.862   30.314 45.928 1.000 44.620  ? 240 PRO   BBB CD  1 ? 
ATOM   3866 N  N   . MET   B 1 242 ? 12.306  32.052 48.712 1.000 27.185  ? 241 MET   BBB N   1 ? 
ATOM   3867 C  CA  . MET   B 1 242 ? 13.470  31.851 49.615 1.000 30.954  ? 241 MET   BBB CA  1 ? 
ATOM   3868 C  C   . MET   B 1 242 ? 12.960  31.337 50.969 1.000 26.782  ? 241 MET   BBB C   1 ? 
ATOM   3869 O  O   . MET   B 1 242 ? 12.827  32.094 51.904 1.000 26.842  ? 241 MET   BBB O   1 ? 
ATOM   3870 C  CB  . MET   B 1 242 ? 14.151  33.219 49.767 1.000 28.461  ? 241 MET   BBB CB  1 ? 
ATOM   3871 C  CG  . MET   B 1 242 ? 15.623  33.201 49.804 1.000 32.790  ? 241 MET   BBB CG  1 ? 
ATOM   3872 S  SD  . MET   B 1 242 ? 16.214  34.917 49.758 1.000 29.359  ? 241 MET   BBB SD  1 ? 
ATOM   3873 C  CE  . MET   B 1 242 ? 16.380  35.329 48.023 1.000 28.378  ? 241 MET   BBB CE  1 ? 
ATOM   3874 N  N   . GLN   B 1 243 ? 12.563  30.086 51.078 1.000 29.218  ? 242 GLN   BBB N   1 ? 
ATOM   3875 C  CA  . GLN   B 1 243 ? 11.836  29.644 52.295 1.000 29.242  ? 242 GLN   BBB CA  1 ? 
ATOM   3876 C  C   . GLN   B 1 243 ? 12.729  29.496 53.521 1.000 24.743  ? 242 GLN   BBB C   1 ? 
ATOM   3877 O  O   . GLN   B 1 243 ? 12.196  29.587 54.622 1.000 31.682  ? 242 GLN   BBB O   1 ? 
ATOM   3878 C  CB  . GLN   B 1 243 ? 11.188  28.304 52.045 1.000 39.330  ? 242 GLN   BBB CB  1 ? 
ATOM   3879 C  CG  . GLN   B 1 243 ? 9.935   28.502 51.233 1.000 49.617  ? 242 GLN   BBB CG  1 ? 
ATOM   3880 C  CD  . GLN   B 1 243 ? 9.040   27.305 51.261 1.000 48.573  ? 242 GLN   BBB CD  1 ? 
ATOM   3881 O  OE1 . GLN   B 1 243 ? 8.076   27.296 50.523 1.000 58.358  ? 242 GLN   BBB OE1 1 ? 
ATOM   3882 N  NE2 . GLN   B 1 243 ? 9.336   26.338 52.115 1.000 68.185  ? 242 GLN   BBB NE2 1 ? 
ATOM   3883 N  N   . HIS   B 1 244 ? 14.010  29.214 53.347 1.000 24.352  ? 243 HIS   BBB N   1 ? 
ATOM   3884 C  CA  . HIS   B 1 244 ? 14.938  28.962 54.469 1.000 23.375  ? 243 HIS   BBB CA  1 ? 
ATOM   3885 C  C   . HIS   B 1 244 ? 16.397  29.110 54.048 1.000 25.107  ? 243 HIS   BBB C   1 ? 
ATOM   3886 O  O   . HIS   B 1 244 ? 16.728  28.959 52.802 1.000 26.254  ? 243 HIS   BBB O   1 ? 
ATOM   3887 C  CB  . HIS   B 1 244 ? 14.669  27.559 55.074 1.000 27.276  ? 243 HIS   BBB CB  1 ? 
ATOM   3888 C  CG  . HIS   B 1 244 ? 14.817  26.357 54.169 1.000 34.480  ? 243 HIS   BBB CG  1 ? 
ATOM   3889 N  ND1 . HIS   B 1 244 ? 15.861  25.508 54.294 1.000 41.098  ? 243 HIS   BBB ND1 1 ? 
ATOM   3890 C  CD2 . HIS   B 1 244 ? 14.058  25.889 53.142 1.000 44.705  ? 243 HIS   BBB CD2 1 ? 
ATOM   3891 C  CE1 . HIS   B 1 244 ? 15.744  24.507 53.415 1.000 46.053  ? 243 HIS   BBB CE1 1 ? 
ATOM   3892 N  NE2 . HIS   B 1 244 ? 14.620  24.700 52.685 1.000 36.823  ? 243 HIS   BBB NE2 1 ? 
ATOM   3893 N  N   . ASN   B 1 245 ? 17.254  29.369 55.032 1.000 22.734  ? 244 ASN   BBB N   1 ? 
ATOM   3894 C  CA  . ASN   B 1 245 ? 18.710  29.506 54.765 1.000 21.970  ? 244 ASN   BBB CA  1 ? 
ATOM   3895 C  C   . ASN   B 1 245 ? 19.496  29.370 56.068 1.000 25.859  ? 244 ASN   BBB C   1 ? 
ATOM   3896 O  O   . ASN   B 1 245 ? 20.618  29.945 56.126 1.000 24.786  ? 244 ASN   BBB O   1 ? 
ATOM   3897 C  CB  . ASN   B 1 245 ? 18.971  30.816 54.003 1.000 21.481  ? 244 ASN   BBB CB  1 ? 
ATOM   3898 C  CG  . ASN   B 1 245 ? 18.458  32.025 54.747 1.000 21.290  ? 244 ASN   BBB CG  1 ? 
ATOM   3899 O  OD1 . ASN   B 1 245 ? 18.178  31.918 55.941 1.000 20.451  ? 244 ASN   BBB OD1 1 ? 
ATOM   3900 N  ND2 . ASN   B 1 245 ? 18.373  33.160 54.033 1.000 24.350  ? 244 ASN   BBB ND2 1 ? 
ATOM   3901 N  N   . ASN   B 1 246 ? 19.046  28.461 56.961 1.000 22.228  ? 245 ASN   BBB N   1 ? 
ATOM   3902 C  CA  . ASN   B 1 246 ? 19.690  28.233 58.275 1.000 23.988  ? 245 ASN   BBB CA  1 ? 
ATOM   3903 C  C   . ASN   B 1 246 ? 20.417  26.864 58.204 1.000 23.560  ? 245 ASN   BBB C   1 ? 
ATOM   3904 O  O   . ASN   B 1 246 ? 19.784  25.816 57.812 1.000 30.347  ? 245 ASN   BBB O   1 ? 
ATOM   3905 C  CB  . ASN   B 1 246 ? 18.740  28.385 59.473 1.000 23.775  ? 245 ASN   BBB CB  1 ? 
ATOM   3906 C  CG  . ASN   B 1 246 ? 17.572  27.401 59.503 1.000 25.380  ? 245 ASN   BBB CG  1 ? 
ATOM   3907 O  OD1 . ASN   B 1 246 ? 17.388  26.651 60.457 1.000 38.477  ? 245 ASN   BBB OD1 1 ? 
ATOM   3908 N  ND2 . ASN   B 1 246 ? 16.784  27.335 58.461 1.000 28.059  ? 245 ASN   BBB ND2 1 ? 
ATOM   3909 N  N   . ARG   B 1 247 ? 21.715  26.873 58.520 1.000 25.241  ? 246 ARG   BBB N   1 ? 
ATOM   3910 C  CA  . ARG   B 1 247 ? 22.539  25.637 58.607 1.000 24.809  ? 246 ARG   BBB CA  1 ? 
ATOM   3911 C  C   . ARG   B 1 247 ? 22.273  24.965 59.950 1.000 24.146  ? 246 ARG   BBB C   1 ? 
ATOM   3912 O  O   . ARG   B 1 247 ? 22.254  25.553 61.013 1.000 25.804  ? 246 ARG   BBB O   1 ? 
ATOM   3913 C  CB  . ARG   B 1 247 ? 24.039  25.951 58.426 1.000 23.342  ? 246 ARG   BBB CB  1 ? 
ATOM   3914 C  CG  . ARG   B 1 247 ? 24.889  24.687 58.297 1.000 25.692  ? 246 ARG   BBB CG  1 ? 
ATOM   3915 C  CD  . ARG   B 1 247 ? 26.382  24.957 58.446 1.000 24.898  ? 246 ARG   BBB CD  1 ? 
ATOM   3916 N  NE  . ARG   B 1 247 ? 27.219  23.871 57.995 1.000 27.714  ? 246 ARG   BBB NE  1 ? 
ATOM   3917 C  CZ  . ARG   B 1 247 ? 28.554  23.853 58.109 1.000 29.332  ? 246 ARG   BBB CZ  1 ? 
ATOM   3918 N  NH1 . ARG   B 1 247 ? 29.201  24.819 58.734 1.000 28.972  ? 246 ARG   BBB NH1 1 ? 
ATOM   3919 N  NH2 . ARG   B 1 247 ? 29.261  22.820 57.663 1.000 35.325  ? 246 ARG   BBB NH2 1 ? 
ATOM   3920 N  N   . PRO   B 1 248 ? 22.159  23.604 60.003 1.000 26.182  ? 247 PRO   BBB N   1 ? 
ATOM   3921 C  CA  . PRO   B 1 248 ? 22.114  22.944 61.290 1.000 27.672  ? 247 PRO   BBB CA  1 ? 
ATOM   3922 C  C   . PRO   B 1 248 ? 23.357  23.233 62.126 1.000 44.325  ? 247 PRO   BBB C   1 ? 
ATOM   3923 O  O   . PRO   B 1 248 ? 24.401  23.430 61.546 1.000 35.444  ? 247 PRO   BBB O   1 ? 
ATOM   3924 C  CB  . PRO   B 1 248 ? 22.175  21.420 60.906 1.000 29.686  ? 247 PRO   BBB CB  1 ? 
ATOM   3925 C  CG  . PRO   B 1 248 ? 21.695  21.422 59.440 1.000 31.626  ? 247 PRO   BBB CG  1 ? 
ATOM   3926 C  CD  . PRO   B 1 248 ? 22.090  22.779 58.823 1.000 26.692  ? 247 PRO   BBB CD  1 ? 
ATOM   3927 N  N   . THR   B 1 249 ? 23.247  23.102 63.436 1.000 40.182  ? 248 THR   BBB N   1 ? 
ATOM   3928 C  CA  . THR   B 1 249 ? 24.404  23.182 64.360 1.000 31.102  ? 248 THR   BBB CA  1 ? 
ATOM   3929 C  C   . THR   B 1 249 ? 25.414  22.072 64.083 1.000 27.065  ? 248 THR   BBB C   1 ? 
ATOM   3930 O  O   . THR   B 1 249 ? 24.965  20.952 63.728 1.000 31.299  ? 248 THR   BBB O   1 ? 
ATOM   3931 C  CB  . THR   B 1 249 ? 23.995  23.197 65.824 1.000 27.342  ? 248 THR   BBB CB  1 ? 
ATOM   3932 O  OG1 . THR   B 1 249 ? 23.184  22.082 66.157 1.000 30.356  ? 248 THR   BBB OG1 1 ? 
ATOM   3933 C  CG2 . THR   B 1 249 ? 23.251  24.478 66.142 1.000 29.212  ? 248 THR   BBB CG2 1 ? 
ATOM   3934 N  N   . GLN   B 1 250 ? 26.689  22.399 64.257 1.000 27.367  ? 249 GLN   BBB N   1 ? 
ATOM   3935 C  CA  . GLN   B 1 250 ? 27.847  21.534 63.938 1.000 25.004  ? 249 GLN   BBB CA  1 ? 
ATOM   3936 C  C   . GLN   B 1 250 ? 28.557  21.238 65.246 1.000 28.040  ? 249 GLN   BBB C   1 ? 
ATOM   3937 O  O   . GLN   B 1 250 ? 28.312  21.897 66.260 1.000 44.649  ? 249 GLN   BBB O   1 ? 
ATOM   3938 C  CB  . GLN   B 1 250 ? 28.785  22.243 62.958 1.000 27.495  ? 249 GLN   BBB CB  1 ? 
ATOM   3939 C  CG  . GLN   B 1 250 ? 28.098  22.736 61.700 1.000 29.550  ? 249 GLN   BBB CG  1 ? 
ATOM   3940 C  CD  . GLN   B 1 250 ? 27.487  21.615 60.895 1.000 29.653  ? 249 GLN   BBB CD  1 ? 
ATOM   3941 O  OE1 . GLN   B 1 250 ? 26.320  21.653 60.487 1.000 30.516  ? 249 GLN   BBB OE1 1 ? 
ATOM   3942 N  NE2 . GLN   B 1 250 ? 28.289  20.602 60.657 1.000 34.686  ? 249 GLN   BBB NE2 1 ? 
ATOM   3943 N  N   . PRO   B 1 251 ? 29.358  20.143 65.280 1.000 31.168  ? 250 PRO   BBB N   1 ? 
ATOM   3944 C  CA  . PRO   B 1 251 ? 29.951  19.705 66.534 1.000 35.689  ? 250 PRO   BBB CA  1 ? 
ATOM   3945 C  C   . PRO   B 1 251 ? 31.060  20.661 66.984 1.000 31.408  ? 250 PRO   BBB C   1 ? 
ATOM   3946 O  O   . PRO   B 1 251 ? 31.836  21.135 66.134 1.000 29.744  ? 250 PRO   BBB O   1 ? 
ATOM   3947 C  CB  . PRO   B 1 251 ? 30.459  18.281 66.281 1.000 42.884  ? 250 PRO   BBB CB  1 ? 
ATOM   3948 C  CG  . PRO   B 1 251 ? 30.552  18.170 64.778 1.000 39.538  ? 250 PRO   BBB CG  1 ? 
ATOM   3949 C  CD  . PRO   B 1 251 ? 29.665  19.245 64.159 1.000 34.310  ? 250 PRO   BBB CD  1 ? 
ATOM   3950 N  N   . LEU   B 1 252 ? 31.130  20.852 68.308 1.000 33.280  ? 251 LEU   BBB N   1 ? 
ATOM   3951 C  CA  . LEU   B 1 252 ? 32.103  21.752 68.986 1.000 38.703  ? 251 LEU   BBB CA  1 ? 
ATOM   3952 C  C   . LEU   B 1 252 ? 33.521  21.199 68.781 1.000 34.489  ? 251 LEU   BBB C   1 ? 
ATOM   3953 O  O   . LEU   B 1 252 ? 34.485  21.986 68.703 1.000 37.978  ? 251 LEU   BBB O   1 ? 
ATOM   3954 C  CB  . LEU   B 1 252 ? 31.717  21.834 70.469 1.000 42.436  ? 251 LEU   BBB CB  1 ? 
ATOM   3955 C  CG  . LEU   B 1 252 ? 31.836  23.187 71.167 1.000 39.939  ? 251 LEU   BBB CG  1 ? 
ATOM   3956 C  CD1 . LEU   B 1 252 ? 31.380  24.321 70.281 1.000 36.065  ? 251 LEU   BBB CD1 1 ? 
ATOM   3957 C  CD2 . LEU   B 1 252 ? 31.047  23.198 72.472 1.000 43.352  ? 251 LEU   BBB CD2 1 ? 
ATOM   3958 N  N   . LYS   B 1 253 ? 33.693  19.851 68.744 1.000 43.671  ? 252 LYS   BBB N   1 ? 
ATOM   3959 C  CA  . LYS   B 1 253 ? 35.033  19.323 68.439 1.000 43.578  ? 252 LYS   BBB CA  1 ? 
ATOM   3960 C  C   . LYS   B 1 253 ? 36.069  19.915 69.411 1.000 56.193  ? 252 LYS   BBB C   1 ? 
ATOM   3961 O  O   . LYS   B 1 253 ? 37.192  20.180 68.961 1.000 43.344  ? 252 LYS   BBB O   1 ? 
ATOM   3962 C  CB  . LYS   B 1 253 ? 35.439  19.585 66.987 1.000 35.538  ? 252 LYS   BBB CB  1 ? 
ATOM   3963 C  CG  . LYS   B 1 253 ? 34.775  18.673 65.973 1.000 43.686  ? 252 LYS   BBB CG  1 ? 
ATOM   3964 C  CD  . LYS   B 1 253 ? 35.284  17.243 66.034 1.000 56.585  ? 252 LYS   BBB CD  1 ? 
ATOM   3965 C  CE  . LYS   B 1 253 ? 34.233  16.210 65.683 1.000 71.461  ? 252 LYS   BBB CE  1 ? 
ATOM   3966 N  NZ  . LYS   B 1 253 ? 33.691  16.440 64.327 1.000 79.216  ? 252 LYS   BBB NZ  1 ? 
ATOM   3967 N  N   . GLY   B 1 254 ? 35.681  20.041 70.686 1.000 51.538  ? 253 GLY   BBB N   1 ? 
ATOM   3968 C  CA  . GLY   B 1 254 ? 36.595  20.398 71.796 1.000 42.761  ? 253 GLY   BBB CA  1 ? 
ATOM   3969 C  C   . GLY   B 1 254 ? 36.706  21.911 72.002 1.000 38.068  ? 253 GLY   BBB C   1 ? 
ATOM   3970 O  O   . GLY   B 1 254 ? 37.294  22.302 72.977 1.000 40.728  ? 253 GLY   BBB O   1 ? 
ATOM   3971 N  N   . ARG   B 1 255 ? 36.141  22.738 71.140 1.000 37.115  ? 254 ARG   BBB N   1 ? 
ATOM   3972 C  CA  . ARG   B 1 255 ? 36.154  24.213 71.369 1.000 30.022  ? 254 ARG   BBB CA  1 ? 
ATOM   3973 C  C   . ARG   B 1 255 ? 35.450  24.581 72.674 1.000 30.915  ? 254 ARG   BBB C   1 ? 
ATOM   3974 O  O   . ARG   B 1 255 ? 34.488  23.887 73.056 1.000 33.259  ? 254 ARG   BBB O   1 ? 
ATOM   3975 C  CB  . ARG   B 1 255 ? 35.452  24.959 70.231 1.000 28.056  ? 254 ARG   BBB CB  1 ? 
ATOM   3976 C  CG  . ARG   B 1 255 ? 36.249  24.971 68.941 1.000 31.165  ? 254 ARG   BBB CG  1 ? 
ATOM   3977 C  CD  . ARG   B 1 255 ? 35.461  25.523 67.791 1.000 33.028  ? 254 ARG   BBB CD  1 ? 
ATOM   3978 N  NE  . ARG   B 1 255 ? 34.385  24.647 67.428 1.000 31.420  ? 254 ARG   BBB NE  1 ? 
ATOM   3979 C  CZ  . ARG   B 1 255 ? 33.507  24.880 66.497 1.000 27.576  ? 254 ARG   BBB CZ  1 ? 
ATOM   3980 N  NH1 . ARG   B 1 255 ? 33.517  26.048 65.898 1.000 27.801  ? 254 ARG   BBB NH1 1 ? 
ATOM   3981 N  NH2 . ARG   B 1 255 ? 32.578  24.002 66.190 1.000 28.978  ? 254 ARG   BBB NH2 1 ? 
ATOM   3982 N  N   . THR   B 1 256 ? 35.815  25.742 73.234 1.000 28.889  ? 255 THR   BBB N   1 ? 
ATOM   3983 C  CA  . THR   B 1 256 ? 35.238  26.298 74.470 1.000 28.935  ? 255 THR   BBB CA  1 ? 
ATOM   3984 C  C   . THR   B 1 256 ? 34.328  27.472 74.075 1.000 28.178  ? 255 THR   BBB C   1 ? 
ATOM   3985 O  O   . THR   B 1 256 ? 34.809  28.273 73.252 1.000 31.345  ? 255 THR   BBB O   1 ? 
ATOM   3986 C  CB  . THR   B 1 256 ? 36.355  26.865 75.346 1.000 37.305  ? 255 THR   BBB CB  1 ? 
ATOM   3987 O  OG1 . THR   B 1 256 ? 37.171  25.762 75.694 1.000 48.314  ? 255 THR   BBB OG1 1 ? 
ATOM   3988 C  CG2 . THR   B 1 256 ? 35.873  27.547 76.605 1.000 43.174  ? 255 THR   BBB CG2 1 ? 
ATOM   3989 N  N   . VAL   B 1 257 ? 33.067  27.527 74.527 1.000 28.602  ? 256 VAL   BBB N   1 ? 
ATOM   3990 C  CA  . VAL   B 1 257 ? 32.269  28.792 74.409 1.000 24.875  ? 256 VAL   BBB CA  1 ? 
ATOM   3991 C  C   . VAL   B 1 257 ? 32.505  29.600 75.666 1.000 29.520  ? 256 VAL   BBB C   1 ? 
ATOM   3992 O  O   . VAL   B 1 257 ? 32.167  29.101 76.719 1.000 30.832  ? 256 VAL   BBB O   1 ? 
ATOM   3993 C  CB  . VAL   B 1 257 ? 30.762  28.580 74.159 1.000 24.684  ? 256 VAL   BBB CB  1 ? 
ATOM   3994 C  CG1 . VAL   B 1 257 ? 30.031  29.909 74.027 1.000 25.476  ? 256 VAL   BBB CG1 1 ? 
ATOM   3995 C  CG2 . VAL   B 1 257 ? 30.506  27.692 72.946 1.000 29.828  ? 256 VAL   BBB CG2 1 ? 
ATOM   3996 N  N   . ARG   B 1 258 ? 33.005  30.840 75.528 1.000 27.731  ? 257 ARG   BBB N   1 ? 
ATOM   3997 C  CA  . ARG   B 1 258 ? 33.308  31.693 76.699 1.000 27.093  ? 257 ARG   BBB CA  1 ? 
ATOM   3998 C  C   . ARG   B 1 258 ? 32.119  32.617 76.915 1.000 21.933  ? 257 ARG   BBB C   1 ? 
ATOM   3999 O  O   . ARG   B 1 258 ? 31.462  33.020 75.910 1.000 27.651  ? 257 ARG   BBB O   1 ? 
ATOM   4000 C  CB  . ARG   B 1 258 ? 34.615  32.447 76.482 1.000 25.969  ? 257 ARG   BBB CB  1 ? 
ATOM   4001 C  CG  . ARG   B 1 258 ? 35.840  31.558 76.341 1.000 29.535  ? 257 ARG   BBB CG  1 ? 
ATOM   4002 C  CD  . ARG   B 1 258 ? 37.058  32.454 76.147 1.000 31.062  ? 257 ARG   BBB CD  1 ? 
ATOM   4003 N  NE  . ARG   B 1 258 ? 37.153  32.994 74.791 1.000 29.864  ? 257 ARG   BBB NE  1 ? 
ATOM   4004 C  CZ  . ARG   B 1 258 ? 37.904  34.037 74.443 1.000 29.360  ? 257 ARG   BBB CZ  1 ? 
ATOM   4005 N  NH1 . ARG   B 1 258 ? 38.650  34.678 75.319 1.000 33.437  ? 257 ARG   BBB NH1 1 ? 
ATOM   4006 N  NH2 . ARG   B 1 258 ? 37.953  34.404 73.192 1.000 33.795  ? 257 ARG   BBB NH2 1 ? 
ATOM   4007 N  N   . ALA   B 1 259 ? 31.878  32.985 78.163 1.000 25.882  ? 258 ALA   BBB N   1 ? 
ATOM   4008 C  CA  . ALA   B 1 259 ? 30.803  33.942 78.511 1.000 27.109  ? 258 ALA   BBB CA  1 ? 
ATOM   4009 C  C   . ALA   B 1 259 ? 31.438  35.239 79.009 1.000 24.451  ? 258 ALA   BBB C   1 ? 
ATOM   4010 O  O   . ALA   B 1 259 ? 32.408  35.173 79.755 1.000 26.298  ? 258 ALA   BBB O   1 ? 
ATOM   4011 C  CB  . ALA   B 1 259 ? 29.880  33.341 79.546 1.000 29.044  ? 258 ALA   BBB CB  1 ? 
ATOM   4012 N  N   . SER   B 1 260 ? 30.855  36.386 78.608 1.000 24.853  ? 259 SER   BBB N   1 ? 
ATOM   4013 C  CA  . SER   B 1 260 ? 31.238  37.730 79.117 1.000 24.689  ? 259 SER   BBB CA  1 ? 
ATOM   4014 C  C   . SER   B 1 260 ? 30.682  37.995 80.524 1.000 26.518  ? 259 SER   BBB C   1 ? 
ATOM   4015 O  O   . SER   B 1 260 ? 31.081  38.960 81.166 1.000 30.323  ? 259 SER   BBB O   1 ? 
ATOM   4016 C  CB  . SER   B 1 260 ? 30.806  38.797 78.145 1.000 21.729  ? 259 SER   BBB CB  1 ? 
ATOM   4017 O  OG  . SER   B 1 260 ? 29.418  39.095 78.271 1.000 24.648  ? 259 SER   BBB OG  1 ? 
ATOM   4018 N  N   . PHE   B 1 261 ? 29.743  37.191 80.976 1.000 26.185  ? 260 PHE   BBB N   1 ? 
ATOM   4019 C  CA  . PHE   B 1 261 ? 28.799  37.521 82.076 1.000 37.014  ? 260 PHE   BBB CA  1 ? 
ATOM   4020 C  C   . PHE   B 1 261 ? 28.646  36.290 82.968 1.000 36.369  ? 260 PHE   BBB C   1 ? 
ATOM   4021 O  O   . PHE   B 1 261 ? 28.082  36.340 84.022 1.000 42.353  ? 260 PHE   BBB O   1 ? 
ATOM   4022 C  CB  . PHE   B 1 261 ? 27.435  37.932 81.507 1.000 39.175  ? 260 PHE   BBB CB  1 ? 
ATOM   4023 C  CG  . PHE   B 1 261 ? 26.751  36.851 80.713 1.000 35.398  ? 260 PHE   BBB CG  1 ? 
ATOM   4024 C  CD1 . PHE   B 1 261 ? 27.076  36.641 79.373 1.000 26.897  ? 260 PHE   BBB CD1 1 ? 
ATOM   4025 C  CD2 . PHE   B 1 261 ? 25.820  36.021 81.324 1.000 35.331  ? 260 PHE   BBB CD2 1 ? 
ATOM   4026 C  CE1 . PHE   B 1 261 ? 26.440  35.650 78.650 1.000 32.081  ? 260 PHE   BBB CE1 1 ? 
ATOM   4027 C  CE2 . PHE   B 1 261 ? 25.220  34.998 80.606 1.000 31.684  ? 260 PHE   BBB CE2 1 ? 
ATOM   4028 C  CZ  . PHE   B 1 261 ? 25.515  34.840 79.270 1.000 28.050  ? 260 PHE   BBB CZ  1 ? 
ATOM   4029 O  OXT . PHE   B 1 261 ? 29.095  35.224 82.580 1.000 35.320  ? 260 PHE   BBB OXT 1 ? 
HETATM 4030 ZN ZN  . ZN    C 2 .   ? -13.677 35.000 39.789 1.000 21.158  ? 301 ZN    AAA ZN  1 ? 
HETATM 4031 O  O   . A1H1P D 3 .   ? -20.390 38.031 40.832 1.000 22.572  ? 302 A1H1P AAA O   1 ? 
HETATM 4032 C  C1  . A1H1P D 3 .   ? -18.608 36.429 40.340 1.000 22.994  ? 302 A1H1P AAA C1  1 ? 
HETATM 4033 O  O4  . A1H1P D 3 .   ? -17.568 33.537 39.353 1.000 26.363  ? 302 A1H1P AAA O4  1 ? 
HETATM 4034 S  S   . A1H1P D 3 .   ? -16.691 34.667 39.700 1.000 24.378  ? 302 A1H1P AAA S   1 ? 
HETATM 4035 O  O3  . A1H1P D 3 .   ? -16.330 35.601 38.651 1.000 26.152  ? 302 A1H1P AAA O3  1 ? 
HETATM 4036 N  N   . A1H1P D 3 .   ? -15.310 34.189 40.318 1.000 24.599  ? 302 A1H1P AAA N   1 ? 
HETATM 4037 C  C   . A1H1P D 3 .   ? -17.626 35.610 40.876 1.000 25.684  ? 302 A1H1P AAA C   1 ? 
HETATM 4038 C  C16 . A1H1P D 3 .   ? -17.463 35.494 42.247 1.000 25.764  ? 302 A1H1P AAA C16 1 ? 
HETATM 4039 C  C6  . A1H1P D 3 .   ? -18.280 36.206 43.129 1.000 26.020  ? 302 A1H1P AAA C6  1 ? 
HETATM 4040 C  C4  . A1H1P D 3 .   ? -19.229 37.045 42.589 1.000 26.881  ? 302 A1H1P AAA C4  1 ? 
HETATM 4041 O  O1  . A1H1P D 3 .   ? -20.036 37.714 43.453 1.000 24.010  ? 302 A1H1P AAA O1  1 ? 
HETATM 4042 C  C5  . A1H1P D 3 .   ? -21.390 37.257 43.479 1.000 23.250  ? 302 A1H1P AAA C5  1 ? 
HETATM 4043 C  C2  . A1H1P D 3 .   ? -19.398 37.165 41.203 1.000 24.027  ? 302 A1H1P AAA C2  1 ? 
HETATM 4044 C  C3  . A1H1P D 3 .   ? -20.609 38.257 39.440 1.000 21.915  ? 302 A1H1P AAA C3  1 ? 
HETATM 4045 C  C7  . A1H1P D 3 .   ? -18.179 36.016 44.611 1.000 35.289  ? 302 A1H1P AAA C7  1 ? 
HETATM 4046 O  O2  . A1H1P D 3 .   ? -18.866 35.177 45.197 1.000 42.756  ? 302 A1H1P AAA O2  1 ? 
HETATM 4047 N  N1  . A1H1P D 3 .   ? -17.425 36.892 45.276 1.000 52.704  ? 302 A1H1P AAA N1  1 ? 
HETATM 4048 C  C8  . A1H1P D 3 .   ? -17.722 37.260 46.657 1.000 56.657  ? 302 A1H1P AAA C8  1 ? 
HETATM 4049 C  C9  . A1H1P D 3 .   ? -19.135 37.860 46.810 1.000 60.776  ? 302 A1H1P AAA C9  1 ? 
HETATM 4050 N  N2  . A1H1P D 3 .   ? -19.760 37.229 47.994 1.000 65.326  ? 302 A1H1P AAA N2  1 ? 
HETATM 4051 C  C13 . A1H1P D 3 .   ? -21.216 36.984 47.863 1.000 62.411  ? 302 A1H1P AAA C13 1 ? 
HETATM 4052 C  C14 . A1H1P D 3 .   ? -21.615 35.577 47.539 1.000 57.667  ? 302 A1H1P AAA C14 1 ? 
HETATM 4053 C  C15 . A1H1P D 3 .   ? -22.717 35.283 46.842 1.000 60.607  ? 302 A1H1P AAA C15 1 ? 
HETATM 4054 C  C12 . A1H1P D 3 .   ? -19.405 38.117 49.102 1.000 70.106  ? 302 A1H1P AAA C12 1 ? 
HETATM 4055 C  C11 . A1H1P D 3 .   ? -19.561 39.515 48.516 1.000 66.793  ? 302 A1H1P AAA C11 1 ? 
HETATM 4056 C  C10 . A1H1P D 3 .   ? -19.139 39.376 47.077 1.000 46.192  ? 302 A1H1P AAA C10 1 ? 
HETATM 4057 ZN ZN  . ZN    E 2 .   ? 24.933  34.685 58.291 1.000 21.044  ? 301 ZN    BBB ZN  1 ? 
HETATM 4058 O  O   . A1H1P F 3 .   ? 31.672  37.638 57.038 1.000 21.760  ? 302 A1H1P BBB O   1 ? 
HETATM 4059 C  C1  . A1H1P F 3 .   ? 29.856  36.107 57.554 1.000 22.762  ? 302 A1H1P BBB C1  1 ? 
HETATM 4060 O  O4  . A1H1P F 3 .   ? 28.781  33.218 58.555 1.000 24.148  ? 302 A1H1P BBB O4  1 ? 
HETATM 4061 S  S   . A1H1P F 3 .   ? 27.938  34.371 58.221 1.000 21.717  ? 302 A1H1P BBB S   1 ? 
HETATM 4062 O  O3  . A1H1P F 3 .   ? 27.634  35.306 59.301 1.000 20.071  ? 302 A1H1P BBB O3  1 ? 
HETATM 4063 N  N   . A1H1P F 3 .   ? 26.545  33.949 57.629 1.000 22.375  ? 302 A1H1P BBB N   1 ? 
HETATM 4064 C  C   . A1H1P F 3 .   ? 28.872  35.281 57.033 1.000 20.988  ? 302 A1H1P BBB C   1 ? 
HETATM 4065 C  C16 . A1H1P F 3 .   ? 28.650  35.217 55.668 1.000 20.240  ? 302 A1H1P BBB C16 1 ? 
HETATM 4066 C  C6  . A1H1P F 3 .   ? 29.454  35.945 54.780 1.000 23.829  ? 302 A1H1P BBB C6  1 ? 
HETATM 4067 C  C4  . A1H1P F 3 .   ? 30.451  36.737 55.308 1.000 24.342  ? 302 A1H1P BBB C4  1 ? 
HETATM 4068 O  O1  . A1H1P F 3 .   ? 31.270  37.455 54.457 1.000 25.878  ? 302 A1H1P BBB O1  1 ? 
HETATM 4069 C  C5  . A1H1P F 3 .   ? 32.606  36.995 54.255 1.000 26.940  ? 302 A1H1P BBB C5  1 ? 
HETATM 4070 C  C2  . A1H1P F 3 .   ? 30.636  36.832 56.678 1.000 23.446  ? 302 A1H1P BBB C2  1 ? 
HETATM 4071 C  C3  . A1H1P F 3 .   ? 31.916  37.767 58.419 1.000 21.669  ? 302 A1H1P BBB C3  1 ? 
HETATM 4072 C  C7  . A1H1P F 3 .   ? 29.290  35.769 53.312 1.000 30.644  ? 302 A1H1P BBB C7  1 ? 
HETATM 4073 O  O2  . A1H1P F 3 .   ? 29.787  34.805 52.730 1.000 41.941  ? 302 A1H1P BBB O2  1 ? 
HETATM 4074 N  N1  . A1H1P F 3 .   ? 28.675  36.757 52.660 1.000 40.043  ? 302 A1H1P BBB N1  1 ? 
HETATM 4075 C  C8  . A1H1P F 3 .   ? 28.848  36.976 51.232 1.000 34.339  ? 302 A1H1P BBB C8  1 ? 
HETATM 4076 C  C9  . A1H1P F 3 .   ? 30.244  37.511 50.909 1.000 40.344  ? 302 A1H1P BBB C9  1 ? 
HETATM 4077 N  N2  . A1H1P F 3 .   ? 30.541  37.336 49.470 1.000 42.006  ? 302 A1H1P BBB N2  1 ? 
HETATM 4078 C  C13 . A1H1P F 3 .   ? 31.493  36.239 49.178 1.000 47.788  ? 302 A1H1P BBB C13 1 ? 
HETATM 4079 C  C14 . A1H1P F 3 .   ? 32.606  36.084 50.177 1.000 43.831  ? 302 A1H1P BBB C14 1 ? 
HETATM 4080 C  C15 . A1H1P F 3 .   ? 32.922  35.045 50.825 1.000 53.420  ? 302 A1H1P BBB C15 1 ? 
HETATM 4081 C  C12 . A1H1P F 3 .   ? 31.073  38.631 48.984 1.000 45.008  ? 302 A1H1P BBB C12 1 ? 
HETATM 4082 C  C11 . A1H1P F 3 .   ? 30.380  39.678 49.830 1.000 43.987  ? 302 A1H1P BBB C11 1 ? 
HETATM 4083 C  C10 . A1H1P F 3 .   ? 30.330  39.030 51.177 1.000 40.614  ? 302 A1H1P BBB C10 1 ? 
HETATM 4084 O  O   . HOH   G 4 .   ? -3.716  25.812 40.275 1.000 43.398  ? 401 HOH   AAA O   1 ? 
HETATM 4085 O  O   . HOH   G 4 .   ? 0.251   27.872 50.916 1.000 47.792  ? 402 HOH   AAA O   1 ? 
HETATM 4086 O  O   . HOH   G 4 .   ? -7.256  48.956 27.839 1.000 60.771  ? 403 HOH   AAA O   1 ? 
HETATM 4087 O  O   . HOH   G 4 .   ? -16.952 58.209 45.604 1.000 51.445  ? 404 HOH   AAA O   1 ? 
HETATM 4088 O  O   . HOH   G 4 .   ? -13.089 48.201 54.140 0.500 30.064  ? 405 HOH   AAA O   1 ? 
HETATM 4089 O  O   . HOH   G 4 .   ? -12.778 29.412 41.537 1.000 24.208  ? 406 HOH   AAA O   1 ? 
HETATM 4090 O  O   . HOH   G 4 .   ? -13.230 53.712 50.692 1.000 37.443  ? 407 HOH   AAA O   1 ? 
HETATM 4091 O  O   . HOH   G 4 .   ? 3.611   46.782 44.205 1.000 37.734  ? 408 HOH   AAA O   1 ? 
HETATM 4092 O  O   . HOH   G 4 .   ? -10.740 40.931 23.205 1.000 27.089  ? 409 HOH   AAA O   1 ? 
HETATM 4093 O  O   . HOH   G 4 .   ? -19.835 55.729 33.920 1.000 50.383  ? 410 HOH   AAA O   1 ? 
HETATM 4094 O  O   . HOH   G 4 .   ? -22.626 53.454 42.811 1.000 39.706  ? 411 HOH   AAA O   1 ? 
HETATM 4095 O  O   . HOH   G 4 .   ? -15.452 22.644 29.389 1.000 30.580  ? 412 HOH   AAA O   1 ? 
HETATM 4096 O  O   . HOH   G 4 .   ? -4.859  50.909 35.506 1.000 38.557  ? 413 HOH   AAA O   1 ? 
HETATM 4097 O  O   . HOH   G 4 .   ? -5.607  50.493 49.009 1.000 39.997  ? 414 HOH   AAA O   1 ? 
HETATM 4098 O  O   . HOH   G 4 .   ? -14.807 19.052 34.680 1.000 49.986  ? 415 HOH   AAA O   1 ? 
HETATM 4099 O  O   . HOH   G 4 .   ? -8.770  37.397 27.416 1.000 27.163  ? 416 HOH   AAA O   1 ? 
HETATM 4100 O  O   . HOH   G 4 .   ? -4.836  29.566 56.103 1.000 44.070  ? 417 HOH   AAA O   1 ? 
HETATM 4101 O  O   . HOH   G 4 .   ? -7.189  25.413 42.486 1.000 37.001  ? 418 HOH   AAA O   1 ? 
HETATM 4102 O  O   . HOH   G 4 .   ? -0.332  31.187 38.096 1.000 29.275  ? 419 HOH   AAA O   1 ? 
HETATM 4103 O  O   . HOH   G 4 .   ? -16.184 39.629 48.995 1.000 32.778  ? 420 HOH   AAA O   1 ? 
HETATM 4104 O  O   . HOH   G 4 .   ? -27.968 22.930 36.386 1.000 34.681  ? 421 HOH   AAA O   1 ? 
HETATM 4105 O  O   . HOH   G 4 .   ? 9.629   38.656 34.322 1.000 43.458  ? 422 HOH   AAA O   1 ? 
HETATM 4106 O  O   . HOH   G 4 .   ? -4.731  47.780 56.374 1.000 49.442  ? 423 HOH   AAA O   1 ? 
HETATM 4107 O  O   . HOH   G 4 .   ? 2.931   44.238 54.305 1.000 46.228  ? 424 HOH   AAA O   1 ? 
HETATM 4108 O  O   . HOH   G 4 .   ? -19.633 20.268 36.910 1.000 43.676  ? 425 HOH   AAA O   1 ? 
HETATM 4109 O  O   . HOH   G 4 .   ? -26.543 22.701 29.768 0.500 28.886  ? 426 HOH   AAA O   1 ? 
HETATM 4110 O  O   . HOH   G 4 .   ? -1.812  29.217 59.978 1.000 40.755  ? 427 HOH   AAA O   1 ? 
HETATM 4111 O  O   . HOH   G 4 .   ? -12.972 56.185 45.081 1.000 30.282  ? 428 HOH   AAA O   1 ? 
HETATM 4112 O  O   . HOH   G 4 .   ? -26.655 33.966 30.543 1.000 37.245  ? 429 HOH   AAA O   1 ? 
HETATM 4113 O  O   . HOH   G 4 .   ? -5.401  39.180 59.731 1.000 38.452  ? 430 HOH   AAA O   1 ? 
HETATM 4114 O  O   . HOH   G 4 .   ? 1.247   40.494 48.212 1.000 42.819  ? 431 HOH   AAA O   1 ? 
HETATM 4115 O  O   . HOH   G 4 .   ? -13.720 34.452 53.300 1.000 44.314  ? 432 HOH   AAA O   1 ? 
HETATM 4116 O  O   . HOH   G 4 .   ? 1.561   35.157 59.471 1.000 40.925  ? 433 HOH   AAA O   1 ? 
HETATM 4117 O  O   . HOH   G 4 .   ? -33.246 36.551 45.262 1.000 44.310  ? 434 HOH   AAA O   1 ? 
HETATM 4118 O  O   . HOH   G 4 .   ? -11.507 19.824 33.898 0.500 25.740  ? 435 HOH   AAA O   1 ? 
HETATM 4119 O  O   . HOH   G 4 .   ? -10.571 34.871 43.239 1.000 23.925  ? 436 HOH   AAA O   1 ? 
HETATM 4120 O  O   . HOH   G 4 .   ? -37.095 39.038 44.376 1.000 44.883  ? 437 HOH   AAA O   1 ? 
HETATM 4121 O  O   . HOH   G 4 .   ? -4.315  45.229 31.469 1.000 25.912  ? 438 HOH   AAA O   1 ? 
HETATM 4122 O  O   . HOH   G 4 .   ? -26.888 36.547 33.929 1.000 31.082  ? 439 HOH   AAA O   1 ? 
HETATM 4123 O  O   . HOH   G 4 .   ? -3.932  43.195 25.482 1.000 41.301  ? 440 HOH   AAA O   1 ? 
HETATM 4124 O  O   . HOH   G 4 .   ? -15.630 21.797 40.897 1.000 35.613  ? 441 HOH   AAA O   1 ? 
HETATM 4125 O  O   . HOH   G 4 .   ? -30.954 48.948 31.747 1.000 47.050  ? 442 HOH   AAA O   1 ? 
HETATM 4126 O  O   . HOH   G 4 .   ? -20.189 50.730 40.713 1.000 26.607  ? 443 HOH   AAA O   1 ? 
HETATM 4127 O  O   . HOH   G 4 .   ? -10.546 48.404 26.041 1.000 48.008  ? 444 HOH   AAA O   1 ? 
HETATM 4128 O  O   . HOH   G 4 .   ? -2.082  51.191 45.884 1.000 39.101  ? 445 HOH   AAA O   1 ? 
HETATM 4129 O  O   . HOH   G 4 .   ? -26.419 30.343 33.708 1.000 29.882  ? 446 HOH   AAA O   1 ? 
HETATM 4130 O  O   . HOH   G 4 .   ? 2.976   34.994 65.983 1.000 35.050  ? 447 HOH   AAA O   1 ? 
HETATM 4131 O  O   . HOH   G 4 .   ? 1.890   38.310 27.905 1.000 35.537  ? 448 HOH   AAA O   1 ? 
HETATM 4132 O  O   . HOH   G 4 .   ? -11.475 24.139 18.451 1.000 32.802  ? 449 HOH   AAA O   1 ? 
HETATM 4133 O  O   . HOH   G 4 .   ? -9.612  22.985 30.242 1.000 35.082  ? 450 HOH   AAA O   1 ? 
HETATM 4134 O  O   . HOH   G 4 .   ? -22.934 46.883 48.379 1.000 48.463  ? 451 HOH   AAA O   1 ? 
HETATM 4135 O  O   . HOH   G 4 .   ? -15.258 55.373 47.559 1.000 36.171  ? 452 HOH   AAA O   1 ? 
HETATM 4136 O  O   . HOH   G 4 .   ? 6.155   42.498 40.657 1.000 37.440  ? 453 HOH   AAA O   1 ? 
HETATM 4137 O  O   . HOH   G 4 .   ? 4.287   45.789 41.564 1.000 43.380  ? 454 HOH   AAA O   1 ? 
HETATM 4138 O  O   . HOH   G 4 .   ? -22.031 52.555 39.922 1.000 29.020  ? 455 HOH   AAA O   1 ? 
HETATM 4139 O  O   . HOH   G 4 .   ? 4.250   36.723 52.136 1.000 32.045  ? 456 HOH   AAA O   1 ? 
HETATM 4140 O  O   . HOH   G 4 .   ? -28.853 35.319 46.847 1.000 45.799  ? 457 HOH   AAA O   1 ? 
HETATM 4141 O  O   . HOH   G 4 .   ? -17.225 18.974 43.776 1.000 36.822  ? 458 HOH   AAA O   1 ? 
HETATM 4142 O  O   . HOH   G 4 .   ? -9.284  25.777 34.828 1.000 28.984  ? 459 HOH   AAA O   1 ? 
HETATM 4143 O  O   . HOH   G 4 .   ? -25.572 49.140 47.417 1.000 47.300  ? 460 HOH   AAA O   1 ? 
HETATM 4144 O  O   . HOH   G 4 .   ? -24.392 31.755 24.487 1.000 42.897  ? 461 HOH   AAA O   1 ? 
HETATM 4145 O  O   . HOH   G 4 .   ? -6.511  30.549 47.825 1.000 38.988  ? 462 HOH   AAA O   1 ? 
HETATM 4146 O  O   . HOH   G 4 .   ? 4.049   45.959 39.200 1.000 42.454  ? 463 HOH   AAA O   1 ? 
HETATM 4147 O  O   . HOH   G 4 .   ? -26.026 26.607 44.807 1.000 31.235  ? 464 HOH   AAA O   1 ? 
HETATM 4148 O  O   . HOH   G 4 .   ? -30.297 50.213 36.386 1.000 48.139  ? 465 HOH   AAA O   1 ? 
HETATM 4149 O  O   . HOH   G 4 .   ? -7.910  38.368 43.463 1.000 23.603  ? 466 HOH   AAA O   1 ? 
HETATM 4150 O  O   . HOH   G 4 .   ? -1.029  41.192 59.078 1.000 36.174  ? 467 HOH   AAA O   1 ? 
HETATM 4151 O  O   . HOH   G 4 .   ? -14.937 53.731 31.848 1.000 31.543  ? 468 HOH   AAA O   1 ? 
HETATM 4152 O  O   . HOH   G 4 .   ? -9.636  21.831 23.646 1.000 39.847  ? 469 HOH   AAA O   1 ? 
HETATM 4153 O  O   . HOH   G 4 .   ? -26.636 33.929 48.598 1.000 42.281  ? 470 HOH   AAA O   1 ? 
HETATM 4154 O  O   . HOH   G 4 .   ? -14.357 31.677 17.898 1.000 40.970  ? 471 HOH   AAA O   1 ? 
HETATM 4155 O  O   . HOH   G 4 .   ? 7.356   37.070 33.342 1.000 34.179  ? 472 HOH   AAA O   1 ? 
HETATM 4156 O  O   . HOH   G 4 .   ? -20.532 18.248 28.238 1.000 41.922  ? 473 HOH   AAA O   1 ? 
HETATM 4157 O  O   . HOH   G 4 .   ? -17.222 44.240 21.948 1.000 37.684  ? 474 HOH   AAA O   1 ? 
HETATM 4158 O  O   . HOH   G 4 .   ? 2.876   42.491 47.142 0.500 27.271  ? 475 HOH   AAA O   1 ? 
HETATM 4159 O  O   . HOH   G 4 .   ? -13.291 20.885 30.197 1.000 38.166  ? 476 HOH   AAA O   1 ? 
HETATM 4160 O  O   . HOH   G 4 .   ? 4.060   40.043 27.544 1.000 46.759  ? 477 HOH   AAA O   1 ? 
HETATM 4161 O  O   . HOH   G 4 .   ? 0.029   29.745 31.249 1.000 37.224  ? 478 HOH   AAA O   1 ? 
HETATM 4162 O  O   . HOH   G 4 .   ? -5.491  29.749 23.304 1.000 30.614  ? 479 HOH   AAA O   1 ? 
HETATM 4163 O  O   . HOH   G 4 .   ? -28.214 28.227 40.547 1.000 29.493  ? 480 HOH   AAA O   1 ? 
HETATM 4164 O  O   . HOH   G 4 .   ? -1.137  43.685 28.479 1.000 30.156  ? 481 HOH   AAA O   1 ? 
HETATM 4165 O  O   . HOH   G 4 .   ? 5.518   34.411 45.927 1.000 36.606  ? 482 HOH   AAA O   1 ? 
HETATM 4166 O  O   . HOH   G 4 .   ? -0.964  44.024 55.817 1.000 35.350  ? 483 HOH   AAA O   1 ? 
HETATM 4167 O  O   . HOH   G 4 .   ? -26.091 45.615 46.182 1.000 35.985  ? 484 HOH   AAA O   1 ? 
HETATM 4168 O  O   . HOH   G 4 .   ? -24.386 33.962 26.392 1.000 35.405  ? 485 HOH   AAA O   1 ? 
HETATM 4169 O  O   . HOH   G 4 .   ? -0.898  39.431 26.511 1.000 33.675  ? 486 HOH   AAA O   1 ? 
HETATM 4170 O  O   . HOH   G 4 .   ? -17.160 42.165 50.014 1.000 41.191  ? 487 HOH   AAA O   1 ? 
HETATM 4171 O  O   . HOH   G 4 .   ? -20.403 58.131 36.441 1.000 39.067  ? 488 HOH   AAA O   1 ? 
HETATM 4172 O  O   . HOH   G 4 .   ? -27.459 32.513 32.814 1.000 34.589  ? 489 HOH   AAA O   1 ? 
HETATM 4173 O  O   . HOH   G 4 .   ? -22.023 22.374 33.567 1.000 35.202  ? 490 HOH   AAA O   1 ? 
HETATM 4174 O  O   . HOH   G 4 .   ? -13.327 35.410 44.098 1.000 30.411  ? 491 HOH   AAA O   1 ? 
HETATM 4175 O  O   . HOH   G 4 .   ? -1.853  24.816 28.636 1.000 34.000  ? 492 HOH   AAA O   1 ? 
HETATM 4176 O  O   . HOH   G 4 .   ? -35.112 42.649 46.845 0.500 39.587  ? 493 HOH   AAA O   1 ? 
HETATM 4177 O  O   . HOH   G 4 .   ? -2.805  48.606 57.887 1.000 37.858  ? 494 HOH   AAA O   1 ? 
HETATM 4178 O  O   . HOH   G 4 .   ? -33.095 43.367 47.602 1.000 38.029  ? 495 HOH   AAA O   1 ? 
HETATM 4179 O  O   . HOH   G 4 .   ? -7.855  54.422 37.020 1.000 34.905  ? 496 HOH   AAA O   1 ? 
HETATM 4180 O  O   . HOH   G 4 .   ? 7.511   39.750 43.195 1.000 36.459  ? 497 HOH   AAA O   1 ? 
HETATM 4181 O  O   . HOH   G 4 .   ? -10.941 32.574 44.432 1.000 27.425  ? 498 HOH   AAA O   1 ? 
HETATM 4182 O  O   . HOH   G 4 .   ? -19.329 31.151 50.915 1.000 41.313  ? 499 HOH   AAA O   1 ? 
HETATM 4183 O  O   . HOH   G 4 .   ? -14.115 57.340 33.588 1.000 58.432  ? 500 HOH   AAA O   1 ? 
HETATM 4184 O  O   . HOH   G 4 .   ? 0.237   32.319 30.350 1.000 28.251  ? 501 HOH   AAA O   1 ? 
HETATM 4185 O  O   . HOH   G 4 .   ? -6.553  54.233 47.509 1.000 39.021  ? 502 HOH   AAA O   1 ? 
HETATM 4186 O  O   . HOH   G 4 .   ? -4.634  24.927 21.031 1.000 28.817  ? 503 HOH   AAA O   1 ? 
HETATM 4187 O  O   . HOH   G 4 .   ? -26.329 27.737 25.553 1.000 40.883  ? 504 HOH   AAA O   1 ? 
HETATM 4188 O  O   . HOH   G 4 .   ? -18.120 18.489 17.924 1.000 45.886  ? 505 HOH   AAA O   1 ? 
HETATM 4189 O  O   . HOH   G 4 .   ? 8.786   43.116 32.041 1.000 45.637  ? 506 HOH   AAA O   1 ? 
HETATM 4190 O  O   . HOH   G 4 .   ? 6.806   30.939 32.975 0.500 29.065  ? 507 HOH   AAA O   1 ? 
HETATM 4191 O  O   . HOH   G 4 .   ? -27.337 46.512 27.559 1.000 41.985  ? 508 HOH   AAA O   1 ? 
HETATM 4192 O  O   . HOH   G 4 .   ? -19.560 25.980 21.709 1.000 39.588  ? 509 HOH   AAA O   1 ? 
HETATM 4193 O  O   . HOH   G 4 .   ? -17.035 25.945 22.341 1.000 44.791  ? 510 HOH   AAA O   1 ? 
HETATM 4194 O  O   . HOH   G 4 .   ? 5.414   32.534 43.670 1.000 31.145  ? 511 HOH   AAA O   1 ? 
HETATM 4195 O  O   . HOH   G 4 .   ? -15.232 19.102 31.599 1.000 46.544  ? 512 HOH   AAA O   1 ? 
HETATM 4196 O  O   . HOH   G 4 .   ? -9.054  58.870 48.984 1.000 30.070  ? 513 HOH   AAA O   1 ? 
HETATM 4197 O  O   . HOH   G 4 .   ? 4.744   33.127 48.124 1.000 39.278  ? 514 HOH   AAA O   1 ? 
HETATM 4198 O  O   . HOH   G 4 .   ? -26.150 28.606 48.832 0.500 25.862  ? 515 HOH   AAA O   1 ? 
HETATM 4199 O  O   . HOH   G 4 .   ? -11.775 49.569 28.081 1.000 47.600  ? 516 HOH   AAA O   1 ? 
HETATM 4200 O  O   . HOH   G 4 .   ? -25.878 23.960 45.528 1.000 33.557  ? 517 HOH   AAA O   1 ? 
HETATM 4201 O  O   . HOH   G 4 .   ? 7.096   43.399 37.834 1.000 40.770  ? 518 HOH   AAA O   1 ? 
HETATM 4202 O  O   . HOH   G 4 .   ? -8.586  42.667 60.588 1.000 57.907  ? 519 HOH   AAA O   1 ? 
HETATM 4203 O  O   . HOH   G 4 .   ? -11.986 50.534 54.418 1.000 40.653  ? 520 HOH   AAA O   1 ? 
HETATM 4204 O  O   . HOH   G 4 .   ? -26.367 30.354 24.909 1.000 36.992  ? 521 HOH   AAA O   1 ? 
HETATM 4205 O  O   . HOH   G 4 .   ? 4.862   38.894 52.886 1.000 42.890  ? 522 HOH   AAA O   1 ? 
HETATM 4206 O  O   . HOH   G 4 .   ? -15.606 56.121 31.363 1.000 53.353  ? 523 HOH   AAA O   1 ? 
HETATM 4207 O  O   . HOH   G 4 .   ? -18.026 43.304 19.518 1.000 46.969  ? 524 HOH   AAA O   1 ? 
HETATM 4208 O  O   . HOH   G 4 .   ? 4.257   30.073 47.712 1.000 46.818  ? 525 HOH   AAA O   1 ? 
HETATM 4209 O  O   . HOH   G 4 .   ? -32.342 45.367 49.189 1.000 48.455  ? 526 HOH   AAA O   1 ? 
HETATM 4210 O  O   . HOH   G 4 .   ? 3.252   42.945 26.718 1.000 53.229  ? 527 HOH   AAA O   1 ? 
HETATM 4211 O  O   . HOH   G 4 .   ? 1.972   43.052 63.905 1.000 43.838  ? 528 HOH   AAA O   1 ? 
HETATM 4212 O  O   . HOH   G 4 .   ? -26.689 33.772 27.946 1.000 36.083  ? 529 HOH   AAA O   1 ? 
HETATM 4213 O  O   . HOH   G 4 .   ? 8.286   42.134 42.249 1.000 40.906  ? 530 HOH   AAA O   1 ? 
HETATM 4214 O  O   . HOH   G 4 .   ? -30.177 36.373 30.408 1.000 48.920  ? 531 HOH   AAA O   1 ? 
HETATM 4215 O  O   . HOH   G 4 .   ? -6.166  41.392 61.278 1.000 46.685  ? 532 HOH   AAA O   1 ? 
HETATM 4216 O  O   . HOH   G 4 .   ? 0.621   42.680 57.630 1.000 35.756  ? 533 HOH   AAA O   1 ? 
HETATM 4217 O  O   . HOH   G 4 .   ? -27.887 26.953 42.950 1.000 38.492  ? 534 HOH   AAA O   1 ? 
HETATM 4218 O  O   . HOH   H 4 .   ? 32.596  40.527 81.808 0.500 22.959  ? 401 HOH   BBB O   1 ? 
HETATM 4219 O  O   . HOH   H 4 .   ? 27.347  46.164 47.520 1.000 50.819  ? 402 HOH   BBB O   1 ? 
HETATM 4220 O  O   . HOH   H 4 .   ? 44.983  46.262 66.381 1.000 43.406  ? 403 HOH   BBB O   1 ? 
HETATM 4221 O  O   . HOH   H 4 .   ? 23.848  29.075 56.653 1.000 26.923  ? 404 HOH   BBB O   1 ? 
HETATM 4222 O  O   . HOH   H 4 .   ? 8.070   33.138 70.393 1.000 43.364  ? 405 HOH   BBB O   1 ? 
HETATM 4223 O  O   . HOH   H 4 .   ? 1.805   38.917 64.087 1.000 34.673  ? 406 HOH   BBB O   1 ? 
HETATM 4224 O  O   . HOH   H 4 .   ? 28.815  40.945 79.813 1.000 28.306  ? 407 HOH   BBB O   1 ? 
HETATM 4225 O  O   . HOH   H 4 .   ? 10.402  28.122 47.223 0.500 31.343  ? 408 HOH   BBB O   1 ? 
HETATM 4226 O  O   . HOH   H 4 .   ? 12.838  44.471 37.854 0.500 28.159  ? 409 HOH   BBB O   1 ? 
HETATM 4227 O  O   . HOH   H 4 .   ? 16.422  38.110 75.843 1.000 31.666  ? 410 HOH   BBB O   1 ? 
HETATM 4228 O  O   . HOH   H 4 .   ? 10.324  44.937 69.027 1.000 52.314  ? 411 HOH   BBB O   1 ? 
HETATM 4229 O  O   . HOH   H 4 .   ? 28.534  20.005 47.610 1.000 40.554  ? 412 HOH   BBB O   1 ? 
HETATM 4230 O  O   . HOH   H 4 .   ? 47.457  46.234 54.737 1.000 54.959  ? 413 HOH   BBB O   1 ? 
HETATM 4231 O  O   . HOH   H 4 .   ? 28.886  46.721 75.561 1.000 37.819  ? 414 HOH   BBB O   1 ? 
HETATM 4232 O  O   . HOH   H 4 .   ? 7.474   46.670 54.201 1.000 36.521  ? 415 HOH   BBB O   1 ? 
HETATM 4233 O  O   . HOH   H 4 .   ? 18.915  28.479 78.003 1.000 44.393  ? 416 HOH   BBB O   1 ? 
HETATM 4234 O  O   . HOH   H 4 .   ? 22.905  40.552 74.844 1.000 22.176  ? 417 HOH   BBB O   1 ? 
HETATM 4235 O  O   . HOH   H 4 .   ? 17.518  30.342 50.776 1.000 33.291  ? 418 HOH   BBB O   1 ? 
HETATM 4236 O  O   . HOH   H 4 .   ? 34.426  21.413 73.813 1.000 55.079  ? 419 HOH   BBB O   1 ? 
HETATM 4237 O  O   . HOH   H 4 .   ? 38.474  36.303 63.725 1.000 32.130  ? 420 HOH   BBB O   1 ? 
HETATM 4238 O  O   . HOH   H 4 .   ? 40.209  28.353 62.098 1.000 52.324  ? 421 HOH   BBB O   1 ? 
HETATM 4239 O  O   . HOH   H 4 .   ? 8.081   28.097 54.272 1.000 43.096  ? 422 HOH   BBB O   1 ? 
HETATM 4240 O  O   . HOH   H 4 .   ? 41.456  41.108 76.886 1.000 42.620  ? 423 HOH   BBB O   1 ? 
HETATM 4241 O  O   . HOH   H 4 .   ? 26.513  54.904 50.598 1.000 40.292  ? 424 HOH   BBB O   1 ? 
HETATM 4242 O  O   . HOH   H 4 .   ? 15.297  48.403 59.228 1.000 39.293  ? 425 HOH   BBB O   1 ? 
HETATM 4243 O  O   . HOH   H 4 .   ? 33.637  52.076 57.994 1.000 30.715  ? 426 HOH   BBB O   1 ? 
HETATM 4244 O  O   . HOH   H 4 .   ? 23.023  23.834 79.727 1.000 40.651  ? 427 HOH   BBB O   1 ? 
HETATM 4245 O  O   . HOH   H 4 .   ? 5.517   46.331 67.595 1.000 37.558  ? 428 HOH   BBB O   1 ? 
HETATM 4246 O  O   . HOH   H 4 .   ? 9.368   45.470 50.467 1.000 31.011  ? 429 HOH   BBB O   1 ? 
HETATM 4247 O  O   . HOH   H 4 .   ? 43.291  42.904 48.959 1.000 33.521  ? 430 HOH   BBB O   1 ? 
HETATM 4248 O  O   . HOH   H 4 .   ? 17.894  25.519 55.969 1.000 36.937  ? 431 HOH   BBB O   1 ? 
HETATM 4249 O  O   . HOH   H 4 .   ? 39.324  22.405 60.660 1.000 34.940  ? 432 HOH   BBB O   1 ? 
HETATM 4250 O  O   . HOH   H 4 .   ? 15.633  42.890 72.832 1.000 36.069  ? 433 HOH   BBB O   1 ? 
HETATM 4251 O  O   . HOH   H 4 .   ? 20.776  25.447 63.388 1.000 38.261  ? 434 HOH   BBB O   1 ? 
HETATM 4252 O  O   . HOH   H 4 .   ? 9.656   38.106 70.733 1.000 32.101  ? 435 HOH   BBB O   1 ? 
HETATM 4253 O  O   . HOH   H 4 .   ? 26.093  44.268 80.213 1.000 50.871  ? 436 HOH   BBB O   1 ? 
HETATM 4254 O  O   . HOH   H 4 .   ? 32.300  17.638 69.301 1.000 49.680  ? 437 HOH   BBB O   1 ? 
HETATM 4255 O  O   . HOH   H 4 .   ? 5.192   42.387 57.768 1.000 36.259  ? 438 HOH   BBB O   1 ? 
HETATM 4256 O  O   . HOH   H 4 .   ? 21.366  22.653 68.044 1.000 36.867  ? 439 HOH   BBB O   1 ? 
HETATM 4257 O  O   . HOH   H 4 .   ? 38.251  33.226 66.743 1.000 33.119  ? 440 HOH   BBB O   1 ? 
HETATM 4258 O  O   . HOH   H 4 .   ? 21.882  21.497 74.456 1.000 37.575  ? 441 HOH   BBB O   1 ? 
HETATM 4259 O  O   . HOH   H 4 .   ? 26.629  22.317 68.313 1.000 79.741  ? 442 HOH   BBB O   1 ? 
HETATM 4260 O  O   . HOH   H 4 .   ? 12.364  44.074 42.597 1.000 30.456  ? 443 HOH   BBB O   1 ? 
HETATM 4261 O  O   . HOH   H 4 .   ? 34.965  47.915 75.413 1.000 38.011  ? 444 HOH   BBB O   1 ? 
HETATM 4262 O  O   . HOH   H 4 .   ? 6.884   36.652 46.525 1.000 36.733  ? 445 HOH   BBB O   1 ? 
HETATM 4263 O  O   . HOH   H 4 .   ? 24.730  56.029 53.524 1.000 32.257  ? 446 HOH   BBB O   1 ? 
HETATM 4264 O  O   . HOH   H 4 .   ? 16.999  49.050 73.141 1.000 38.252  ? 447 HOH   BBB O   1 ? 
HETATM 4265 O  O   . HOH   H 4 .   ? 12.365  40.990 39.438 1.000 35.309  ? 448 HOH   BBB O   1 ? 
HETATM 4266 O  O   . HOH   H 4 .   ? 38.154  22.211 67.430 1.000 40.445  ? 449 HOH   BBB O   1 ? 
HETATM 4267 O  O   . HOH   H 4 .   ? 11.746  31.235 60.455 1.000 26.353  ? 450 HOH   BBB O   1 ? 
HETATM 4268 O  O   . HOH   H 4 .   ? 20.715  36.841 70.802 1.000 22.017  ? 451 HOH   BBB O   1 ? 
HETATM 4269 O  O   . HOH   H 4 .   ? 19.839  33.707 76.252 1.000 40.718  ? 452 HOH   BBB O   1 ? 
HETATM 4270 O  O   . HOH   H 4 .   ? 36.221  24.274 48.253 1.000 66.000  ? 453 HOH   BBB O   1 ? 
HETATM 4271 O  O   . HOH   H 4 .   ? 31.790  50.385 57.295 1.000 24.003  ? 454 HOH   BBB O   1 ? 
HETATM 4272 O  O   . HOH   H 4 .   ? 11.519  32.100 68.606 1.000 39.770  ? 455 HOH   BBB O   1 ? 
HETATM 4273 O  O   . HOH   H 4 .   ? 19.103  38.208 54.882 1.000 22.692  ? 456 HOH   BBB O   1 ? 
HETATM 4274 O  O   . HOH   H 4 .   ? 23.150  56.283 64.256 1.000 38.890  ? 457 HOH   BBB O   1 ? 
HETATM 4275 O  O   . HOH   H 4 .   ? 21.825  34.546 55.020 1.000 21.171  ? 458 HOH   BBB O   1 ? 
HETATM 4276 O  O   . HOH   H 4 .   ? 26.486  31.274 80.014 1.000 37.074  ? 459 HOH   BBB O   1 ? 
HETATM 4277 O  O   . HOH   H 4 .   ? 16.896  52.544 46.669 1.000 46.905  ? 460 HOH   BBB O   1 ? 
HETATM 4278 O  O   . HOH   H 4 .   ? 3.053   43.157 66.483 1.000 39.418  ? 461 HOH   BBB O   1 ? 
HETATM 4279 O  O   . HOH   H 4 .   ? 7.414   40.098 71.243 1.000 33.852  ? 462 HOH   BBB O   1 ? 
HETATM 4280 O  O   . HOH   H 4 .   ? 16.520  50.450 62.945 1.000 39.137  ? 463 HOH   BBB O   1 ? 
HETATM 4281 O  O   . HOH   H 4 .   ? 16.788  38.935 38.692 1.000 32.495  ? 464 HOH   BBB O   1 ? 
HETATM 4282 O  O   . HOH   H 4 .   ? 3.983   37.346 65.323 1.000 30.725  ? 465 HOH   BBB O   1 ? 
HETATM 4283 O  O   . HOH   H 4 .   ? 31.020  19.986 60.657 0.500 28.592  ? 466 HOH   BBB O   1 ? 
HETATM 4284 O  O   . HOH   H 4 .   ? 37.926  29.647 63.716 1.000 32.030  ? 467 HOH   BBB O   1 ? 
HETATM 4285 O  O   . HOH   H 4 .   ? 13.613  51.158 52.616 1.000 31.185  ? 468 HOH   BBB O   1 ? 
HETATM 4286 O  O   . HOH   H 4 .   ? 17.666  28.581 75.732 1.000 38.333  ? 469 HOH   BBB O   1 ? 
HETATM 4287 O  O   . HOH   H 4 .   ? 39.147  31.789 64.470 1.000 31.037  ? 470 HOH   BBB O   1 ? 
HETATM 4288 O  O   . HOH   H 4 .   ? 26.669  21.384 56.878 1.000 36.705  ? 471 HOH   BBB O   1 ? 
HETATM 4289 O  O   . HOH   H 4 .   ? 33.340  21.847 63.662 1.000 34.189  ? 472 HOH   BBB O   1 ? 
HETATM 4290 O  O   . HOH   H 4 .   ? 43.078  47.840 56.183 1.000 46.526  ? 473 HOH   BBB O   1 ? 
HETATM 4291 O  O   . HOH   H 4 .   ? 32.655  41.610 79.596 1.000 34.377  ? 474 HOH   BBB O   1 ? 
HETATM 4292 O  O   . HOH   H 4 .   ? 34.071  53.170 54.966 1.000 29.303  ? 475 HOH   BBB O   1 ? 
HETATM 4293 O  O   . HOH   H 4 .   ? 27.044  40.705 49.538 1.000 32.574  ? 476 HOH   BBB O   1 ? 
HETATM 4294 O  O   . HOH   H 4 .   ? 32.386  57.485 61.936 1.000 40.661  ? 477 HOH   BBB O   1 ? 
HETATM 4295 O  O   . HOH   H 4 .   ? 28.000  24.456 73.899 1.000 36.779  ? 478 HOH   BBB O   1 ? 
HETATM 4296 O  O   . HOH   H 4 .   ? 28.272  18.495 53.877 1.000 46.311  ? 479 HOH   BBB O   1 ? 
HETATM 4297 O  O   . HOH   H 4 .   ? 30.251  41.376 82.318 1.000 36.394  ? 480 HOH   BBB O   1 ? 
HETATM 4298 O  O   . HOH   H 4 .   ? 29.174  31.077 47.096 0.500 43.553  ? 481 HOH   BBB O   1 ? 
HETATM 4299 O  O   . HOH   H 4 .   ? 36.777  26.837 51.557 1.000 39.450  ? 482 HOH   BBB O   1 ? 
HETATM 4300 O  O   . HOH   H 4 .   ? 29.503  43.647 76.038 1.000 23.356  ? 483 HOH   BBB O   1 ? 
HETATM 4301 O  O   . HOH   H 4 .   ? 26.513  53.304 66.383 1.000 27.612  ? 484 HOH   BBB O   1 ? 
HETATM 4302 O  O   . HOH   H 4 .   ? 36.111  30.743 72.897 1.000 33.608  ? 485 HOH   BBB O   1 ? 
HETATM 4303 O  O   . HOH   H 4 .   ? 24.422  35.226 54.039 1.000 24.741  ? 486 HOH   BBB O   1 ? 
HETATM 4304 O  O   . HOH   H 4 .   ? 16.701  50.292 49.563 1.000 37.935  ? 487 HOH   BBB O   1 ? 
HETATM 4305 O  O   . HOH   H 4 .   ? 15.944  44.994 67.159 1.000 24.847  ? 488 HOH   BBB O   1 ? 
HETATM 4306 O  O   . HOH   H 4 .   ? 34.646  22.754 44.712 1.000 37.904  ? 489 HOH   BBB O   1 ? 
HETATM 4307 O  O   . HOH   H 4 .   ? 5.899   34.421 52.538 1.000 33.080  ? 490 HOH   BBB O   1 ? 
HETATM 4308 O  O   . HOH   H 4 .   ? 28.658  49.652 72.020 1.000 42.410  ? 491 HOH   BBB O   1 ? 
HETATM 4309 O  O   . HOH   H 4 .   ? 11.282  29.304 67.052 0.500 29.819  ? 492 HOH   BBB O   1 ? 
HETATM 4310 O  O   . HOH   H 4 .   ? 25.636  45.581 77.832 1.000 49.614  ? 493 HOH   BBB O   1 ? 
HETATM 4311 O  O   . HOH   H 4 .   ? 33.670  47.005 49.252 1.000 41.698  ? 494 HOH   BBB O   1 ? 
HETATM 4312 O  O   . HOH   H 4 .   ? 31.745  25.476 75.993 1.000 60.782  ? 495 HOH   BBB O   1 ? 
HETATM 4313 O  O   . HOH   H 4 .   ? 16.322  31.400 38.124 1.000 41.674  ? 496 HOH   BBB O   1 ? 
HETATM 4314 O  O   . HOH   H 4 .   ? 32.677  39.882 84.152 0.500 28.379  ? 497 HOH   BBB O   1 ? 
HETATM 4315 O  O   . HOH   H 4 .   ? 34.586  39.419 81.441 1.000 30.340  ? 498 HOH   BBB O   1 ? 
HETATM 4316 O  O   . HOH   H 4 .   ? 8.262   44.119 44.120 1.000 42.193  ? 499 HOH   BBB O   1 ? 
HETATM 4317 O  O   . HOH   H 4 .   ? 4.014   39.759 55.295 1.000 29.769  ? 500 HOH   BBB O   1 ? 
HETATM 4318 O  O   . HOH   H 4 .   ? 13.520  24.685 69.986 1.000 42.862  ? 501 HOH   BBB O   1 ? 
HETATM 4319 O  O   . HOH   H 4 .   ? 39.796  37.463 75.563 1.000 45.748  ? 502 HOH   BBB O   1 ? 
HETATM 4320 O  O   . HOH   H 4 .   ? 37.341  45.339 51.454 1.000 29.803  ? 503 HOH   BBB O   1 ? 
HETATM 4321 O  O   . HOH   H 4 .   ? 43.117  48.115 65.885 1.000 40.451  ? 504 HOH   BBB O   1 ? 
HETATM 4322 O  O   . HOH   H 4 .   ? 36.145  33.152 71.000 1.000 28.563  ? 505 HOH   BBB O   1 ? 
HETATM 4323 O  O   . HOH   H 4 .   ? 37.943  27.030 71.765 1.000 39.731  ? 506 HOH   BBB O   1 ? 
HETATM 4324 O  O   . HOH   H 4 .   ? 9.760   35.260 39.248 1.000 46.873  ? 507 HOH   BBB O   1 ? 
HETATM 4325 O  O   . HOH   H 4 .   ? 26.747  60.544 59.513 1.000 48.456  ? 508 HOH   BBB O   1 ? 
HETATM 4326 O  O   . HOH   H 4 .   ? 34.621  29.990 84.254 1.000 48.388  ? 509 HOH   BBB O   1 ? 
HETATM 4327 O  O   . HOH   H 4 .   ? 39.375  45.910 70.267 1.000 36.710  ? 510 HOH   BBB O   1 ? 
HETATM 4328 O  O   . HOH   H 4 .   ? 7.356   45.905 59.600 1.000 36.443  ? 511 HOH   BBB O   1 ? 
HETATM 4329 O  O   . HOH   H 4 .   ? 25.145  20.586 67.722 1.000 37.701  ? 512 HOH   BBB O   1 ? 
HETATM 4330 O  O   . HOH   H 4 .   ? 6.587   33.176 50.311 1.000 33.745  ? 513 HOH   BBB O   1 ? 
HETATM 4331 O  O   . HOH   H 4 .   ? 16.623  46.430 69.355 1.000 34.528  ? 514 HOH   BBB O   1 ? 
HETATM 4332 O  O   . HOH   H 4 .   ? 39.581  28.099 56.852 1.000 40.220  ? 515 HOH   BBB O   1 ? 
HETATM 4333 O  O   . HOH   H 4 .   ? 7.034   45.970 56.857 1.000 40.739  ? 516 HOH   BBB O   1 ? 
HETATM 4334 O  O   . HOH   H 4 .   ? 12.870  43.552 70.255 1.000 26.346  ? 517 HOH   BBB O   1 ? 
HETATM 4335 O  O   . HOH   H 4 .   ? 19.575  54.202 61.581 1.000 34.117  ? 518 HOH   BBB O   1 ? 
HETATM 4336 O  O   . HOH   H 4 .   ? 23.573  38.699 43.529 1.000 34.972  ? 519 HOH   BBB O   1 ? 
HETATM 4337 O  O   . HOH   H 4 .   ? 6.025   40.753 51.045 1.000 57.632  ? 520 HOH   BBB O   1 ? 
HETATM 4338 O  O   . HOH   H 4 .   ? 17.907  54.074 51.330 1.000 34.745  ? 521 HOH   BBB O   1 ? 
HETATM 4339 O  O   . HOH   H 4 .   ? 32.468  18.906 62.039 1.000 41.646  ? 522 HOH   BBB O   1 ? 
HETATM 4340 O  O   . HOH   H 4 .   ? 3.071   42.078 61.817 1.000 47.855  ? 523 HOH   BBB O   1 ? 
HETATM 4341 O  O   . HOH   H 4 .   ? 22.062  32.249 53.692 1.000 22.959  ? 524 HOH   BBB O   1 ? 
HETATM 4342 O  O   . HOH   H 4 .   ? 39.637  47.783 51.269 1.000 40.145  ? 525 HOH   BBB O   1 ? 
HETATM 4343 O  O   . HOH   H 4 .   ? 17.562  25.636 63.399 1.000 41.390  ? 526 HOH   BBB O   1 ? 
HETATM 4344 O  O   . HOH   H 4 .   ? 30.700  45.829 51.662 1.000 34.997  ? 527 HOH   BBB O   1 ? 
HETATM 4345 O  O   . HOH   H 4 .   ? 38.222  42.545 80.711 1.000 30.020  ? 528 HOH   BBB O   1 ? 
HETATM 4346 O  O   . HOH   H 4 .   ? 27.754  55.633 67.541 1.000 38.981  ? 529 HOH   BBB O   1 ? 
HETATM 4347 O  O   . HOH   H 4 .   ? 16.877  34.968 74.569 1.000 52.507  ? 530 HOH   BBB O   1 ? 
HETATM 4348 O  O   . HOH   H 4 .   ? 14.157  50.926 60.190 1.000 37.341  ? 531 HOH   BBB O   1 ? 
HETATM 4349 O  O   . HOH   H 4 .   ? 19.359  45.394 40.004 1.000 37.444  ? 532 HOH   BBB O   1 ? 
HETATM 4350 O  O   . HOH   H 4 .   ? 33.558  50.959 68.382 1.000 39.116  ? 533 HOH   BBB O   1 ? 
HETATM 4351 O  O   . HOH   H 4 .   ? 18.731  43.189 76.192 1.000 31.418  ? 534 HOH   BBB O   1 ? 
HETATM 4352 O  O   . HOH   H 4 .   ? 5.821   32.619 54.696 1.000 34.204  ? 535 HOH   BBB O   1 ? 
HETATM 4353 O  O   . HOH   H 4 .   ? 41.054  30.059 49.908 1.000 43.926  ? 536 HOH   BBB O   1 ? 
HETATM 4354 O  O   . HOH   H 4 .   ? 29.123  25.704 75.609 1.000 36.005  ? 537 HOH   BBB O   1 ? 
HETATM 4355 O  O   . HOH   H 4 .   ? 25.958  52.280 68.810 1.000 37.843  ? 538 HOH   BBB O   1 ? 
HETATM 4356 O  O   . HOH   H 4 .   ? 41.738  22.058 63.017 1.000 47.438  ? 539 HOH   BBB O   1 ? 
HETATM 4357 O  O   . HOH   H 4 .   ? 14.192  27.878 49.453 1.000 52.507  ? 540 HOH   BBB O   1 ? 
HETATM 4358 O  O   . HOH   H 4 .   ? 6.335   39.197 45.825 1.000 43.000  ? 541 HOH   BBB O   1 ? 
HETATM 4359 O  O   . HOH   H 4 .   ? 33.043  24.833 43.562 1.000 43.752  ? 542 HOH   BBB O   1 ? 
HETATM 4360 O  O   . HOH   H 4 .   ? 36.829  42.770 48.969 1.000 37.290  ? 543 HOH   BBB O   1 ? 
HETATM 4361 O  O   . HOH   H 4 .   ? 12.312  38.980 72.015 1.000 44.053  ? 544 HOH   BBB O   1 ? 
HETATM 4362 O  O   . HOH   H 4 .   ? 6.612   30.449 50.916 1.000 37.746  ? 545 HOH   BBB O   1 ? 
HETATM 4363 O  O   . HOH   H 4 .   ? 26.790  34.376 49.386 1.000 33.636  ? 546 HOH   BBB O   1 ? 
HETATM 4364 O  O   . HOH   H 4 .   ? 41.933  40.393 67.414 0.500 33.004  ? 547 HOH   BBB O   1 ? 
HETATM 4365 O  O   . HOH   H 4 .   ? 39.759  35.338 70.152 1.000 46.941  ? 548 HOH   BBB O   1 ? 
HETATM 4366 O  O   . HOH   H 4 .   ? 36.018  44.039 81.217 1.000 33.918  ? 549 HOH   BBB O   1 ? 
HETATM 4367 O  O   . HOH   H 4 .   ? 36.396  48.885 73.318 1.000 48.799  ? 550 HOH   BBB O   1 ? 
HETATM 4368 O  O   . HOH   H 4 .   ? 10.604  42.616 40.812 1.000 34.364  ? 551 HOH   BBB O   1 ? 
HETATM 4369 O  O   . HOH   H 4 .   ? 30.279  42.789 78.574 1.000 33.280  ? 552 HOH   BBB O   1 ? 
HETATM 4370 O  O   . HOH   H 4 .   ? 38.272  33.057 69.509 1.000 32.545  ? 553 HOH   BBB O   1 ? 
HETATM 4371 O  O   . HOH   H 4 .   ? 3.101   42.158 56.334 1.000 34.404  ? 554 HOH   BBB O   1 ? 
HETATM 4372 O  O   . HOH   H 4 .   ? 15.606  29.371 39.437 0.500 31.583  ? 555 HOH   BBB O   1 ? 
HETATM 4373 O  O   . HOH   H 4 .   ? 15.218  45.014 71.276 1.000 38.021  ? 556 HOH   BBB O   1 ? 
HETATM 4374 O  O   . HOH   H 4 .   ? 17.617  41.037 37.046 1.000 40.055  ? 557 HOH   BBB O   1 ? 
HETATM 4375 O  O   . HOH   H 4 .   ? 27.200  40.105 46.943 0.500 29.566  ? 558 HOH   BBB O   1 ? 
HETATM 4376 O  O   . HOH   H 4 .   ? 5.910   30.196 53.444 0.500 30.847  ? 559 HOH   BBB O   1 ? 
HETATM 4377 O  O   . HOH   H 4 .   ? 40.066  31.067 70.090 1.000 40.674  ? 560 HOH   BBB O   1 ? 
HETATM 4378 O  O   . HOH   H 4 .   ? 41.260  29.705 68.154 1.000 51.324  ? 561 HOH   BBB O   1 ? 
HETATM 4379 O  O   . HOH   H 4 .   ? 33.676  47.280 82.193 1.000 38.921  ? 562 HOH   BBB 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   . TRP   A 6   ? 0.613 0.508 0.587 0.078  0.088  0.008  5   TRP   AAA N   
2    C  CA  . TRP   A 6   ? 0.581 0.400 0.492 0.058  0.058  0.117  5   TRP   AAA CA  
3    C  C   . TRP   A 6   ? 0.605 0.222 0.469 0.093  -0.003 -0.038 5   TRP   AAA C   
4    O  O   . TRP   A 6   ? 0.672 0.302 0.506 0.008  0.004  -0.112 5   TRP   AAA O   
5    C  CB  . TRP   A 6   ? 0.511 0.082 0.585 0.158  0.064  0.071  5   TRP   AAA CB  
6    C  CG  . TRP   A 6   ? 0.503 0.072 0.528 0.106  0.111  0.093  5   TRP   AAA CG  
7    C  CD1 . TRP   A 6   ? 0.813 0.050 0.500 0.182  0.033  -0.027 5   TRP   AAA CD1 
8    C  CD2 . TRP   A 6   ? 0.523 0.127 0.375 0.049  0.048  0.059  5   TRP   AAA CD2 
9    N  NE1 . TRP   A 6   ? 0.606 0.018 0.542 0.046  0.049  0.061  5   TRP   AAA NE1 
10   C  CE2 . TRP   A 6   ? 0.528 0.140 0.478 0.038  0.042  0.030  5   TRP   AAA CE2 
11   C  CE3 . TRP   A 6   ? 0.456 0.319 0.389 0.010  0.024  0.049  5   TRP   AAA CE3 
12   C  CZ2 . TRP   A 6   ? 0.519 0.040 0.449 -0.013 0.034  -0.075 5   TRP   AAA CZ2 
13   C  CZ3 . TRP   A 6   ? 0.583 0.062 0.430 0.086  0.071  -0.081 5   TRP   AAA CZ3 
14   C  CH2 . TRP   A 6   ? 0.470 0.011 0.452 -0.030 0.037  -0.039 5   TRP   AAA CH2 
15   N  N   . GLY   A 7   ? 0.562 0.249 0.512 0.121  0.015  0.014  6   GLY   AAA N   
16   C  CA  . GLY   A 7   ? 0.550 0.223 0.562 0.117  0.041  0.035  6   GLY   AAA CA  
17   C  C   . GLY   A 7   ? 0.576 0.282 0.540 0.033  0.028  0.080  6   GLY   AAA C   
18   O  O   . GLY   A 7   ? 0.634 0.031 0.660 0.111  -0.029 0.011  6   GLY   AAA O   
19   N  N   . TYR   A 8   ? 0.619 0.103 0.598 0.065  0.043  0.119  7   TYR   AAA N   
20   C  CA  . TYR   A 8   ? 0.662 0.187 0.639 0.091  0.086  0.118  7   TYR   AAA CA  
21   C  C   . TYR   A 8   ? 0.993 0.026 0.627 0.108  -0.016 -0.071 7   TYR   AAA C   
22   O  O   . TYR   A 8   ? 0.869 0.197 0.703 0.238  0.044  0.050  7   TYR   AAA O   
23   C  CB  . TYR   A 8   ? 0.641 0.090 0.525 0.099  -0.022 0.100  7   TYR   AAA CB  
24   C  CG  . TYR   A 8   ? 0.561 0.103 0.430 0.075  -0.003 0.049  7   TYR   AAA CG  
25   C  CD1 . TYR   A 8   ? 0.636 0.177 0.438 0.080  -0.010 0.070  7   TYR   AAA CD1 
26   C  CD2 . TYR   A 8   ? 0.517 0.215 0.403 0.072  0.021  -0.027 7   TYR   AAA CD2 
27   C  CE1 . TYR   A 8   ? 0.610 0.049 0.446 0.031  0.006  0.020  7   TYR   AAA CE1 
28   C  CE2 . TYR   A 8   ? 0.510 0.104 0.359 0.004  0.014  0.000  7   TYR   AAA CE2 
29   C  CZ  . TYR   A 8   ? 0.469 0.180 0.344 0.047  0.019  -0.066 7   TYR   AAA CZ  
30   O  OH  . TYR   A 8   ? 0.421 0.166 0.394 -0.015 -0.008 -0.030 7   TYR   AAA OH  
31   N  N   . ASP   A 9   ? 0.957 0.030 0.722 0.149  0.077  0.035  8   ASP   AAA N   
32   C  CA  . ASP   A 9   ? 0.832 0.182 0.802 0.283  0.102  0.068  8   ASP   AAA CA  
33   C  C   . ASP   A 9   ? 0.715 0.357 0.826 0.196  -0.026 0.089  8   ASP   AAA C   
34   O  O   . ASP   A 9   ? 0.724 0.493 0.748 0.079  -0.063 0.229  8   ASP   AAA O   
35   C  CB  . ASP   A 9   ? 0.856 0.671 0.831 0.292  -0.140 0.184  8   ASP   AAA CB  
36   C  CG  . ASP   A 9   ? 1.223 1.007 0.662 0.171  -0.040 0.139  8   ASP   AAA CG  
37   O  OD1 . ASP   A 9   ? 1.628 1.104 0.783 -0.367 -0.304 0.362  8   ASP   AAA OD1 
38   O  OD2 . ASP   A 9   ? 1.152 0.874 0.872 0.233  0.164  0.529  8   ASP   AAA OD2 
39   N  N   . ASP   A 10  ? 0.840 0.331 1.064 0.181  0.053  0.290  9   ASP   AAA N   
40   C  CA  . ASP   A 10  ? 0.709 0.465 1.129 0.194  0.017  0.199  9   ASP   AAA CA  
41   C  C   . ASP   A 10  ? 0.887 0.101 1.061 0.135  0.144  0.135  9   ASP   AAA C   
42   O  O   . ASP   A 10  ? 0.852 0.594 1.320 -0.137 0.272  0.033  9   ASP   AAA O   
43   C  CB  . ASP   A 10  ? 0.775 0.595 1.262 0.310  -0.020 0.460  9   ASP   AAA CB  
44   C  CG  . ASP   A 10  ? 0.867 0.937 1.557 0.454  -0.170 0.237  9   ASP   AAA CG  
45   O  OD1 . ASP   A 10  ? 1.084 1.560 1.570 0.704  -0.208 0.175  9   ASP   AAA OD1 
46   O  OD2 . ASP   A 10  ? 0.836 0.975 1.809 0.191  0.486  0.312  9   ASP   AAA OD2 
47   N  N   . LYS   A 11  ? 0.831 0.372 1.037 0.157  -0.022 0.191  10  LYS   AAA N   
48   C  CA  . LYS   A 11  ? 0.844 0.315 0.797 0.203  -0.026 0.097  10  LYS   AAA CA  
49   C  C   . LYS   A 11  ? 0.785 0.080 0.788 0.098  0.164  0.234  10  LYS   AAA C   
50   O  O   . LYS   A 11  ? 3.272 0.517 3.685 -0.165 0.161  -1.365 10  LYS   AAA O   
51   C  CB  . LYS   A 11  ? 0.817 0.398 0.646 0.189  0.071  -0.048 10  LYS   AAA CB  
52   N  N   . ASN   A 12  ? 1.489 0.065 0.960 0.243  0.077  -0.122 11  ASN   AAA N   
53   C  CA  . ASN   A 12  ? 0.800 0.187 0.711 0.245  0.039  0.008  11  ASN   AAA CA  
54   C  C   . ASN   A 12  ? 0.861 0.053 0.873 0.169  0.007  0.109  11  ASN   AAA C   
55   O  O   . ASN   A 12  ? 0.750 0.083 0.600 0.239  0.022  0.021  11  ASN   AAA O   
56   C  CB  . ASN   A 12  ? 1.016 0.195 0.525 0.222  0.088  0.078  11  ASN   AAA CB  
57   C  CG  . ASN   A 12  ? 1.008 0.620 0.506 0.058  0.058  0.026  11  ASN   AAA CG  
58   O  OD1 . ASN   A 12  ? 0.874 0.149 0.582 0.149  0.074  0.114  11  ASN   AAA OD1 
59   N  ND2 . ASN   A 12  ? 0.858 0.122 0.652 0.100  0.081  0.145  11  ASN   AAA ND2 
60   N  N   . GLY   A 13  ? 0.871 0.089 0.671 -0.022 0.058  0.179  12  GLY   AAA N   
61   C  CA  . GLY   A 13  ? 0.723 0.052 0.547 0.173  0.084  -0.027 12  GLY   AAA CA  
62   C  C   . GLY   A 13  ? 0.581 0.010 0.669 0.043  0.080  0.023  12  GLY   AAA C   
63   O  O   . GLY   A 13  ? 0.709 0.076 0.765 -0.146 0.015  0.031  12  GLY   AAA O   
64   N  N   . PRO   A 14  ? 0.619 0.010 0.629 0.008  0.039  -0.049 13  PRO   AAA N   
65   C  CA  . PRO   A 14  ? 0.601 0.016 0.562 0.017  0.076  -0.067 13  PRO   AAA CA  
66   C  C   . PRO   A 14  ? 0.658 0.018 0.641 0.004  0.126  -0.083 13  PRO   AAA C   
67   O  O   . PRO   A 14  ? 0.672 0.136 0.817 0.056  0.123  -0.044 13  PRO   AAA O   
68   C  CB  . PRO   A 14  ? 0.576 0.082 0.590 -0.005 0.046  0.054  13  PRO   AAA CB  
69   C  CG  . PRO   A 14  ? 0.552 0.117 0.560 0.008  0.056  -0.024 13  PRO   AAA CG  
70   C  CD  . PRO   A 14  ? 0.549 0.219 0.579 0.067  0.109  0.107  13  PRO   AAA CD  
71   N  N   . GLU   A 15  ? 0.737 0.182 0.719 0.169  0.095  -0.055 14  GLU   AAA N   
72   C  CA  . GLU   A 15  ? 0.672 0.180 0.867 0.122  0.069  0.018  14  GLU   AAA CA  
73   C  C   . GLU   A 15  ? 0.607 0.029 0.862 -0.015 0.026  -0.047 14  GLU   AAA C   
74   O  O   . GLU   A 15  ? 1.100 0.022 1.003 0.117  0.059  -0.053 14  GLU   AAA O   
75   C  CB  . GLU   A 15  ? 0.919 0.105 1.125 0.190  0.165  -0.218 14  GLU   AAA CB  
76   C  CG  . GLU   A 15  ? 1.044 0.384 1.050 0.247  0.228  -0.285 14  GLU   AAA CG  
77   C  CD  . GLU   A 15  ? 1.045 0.746 1.123 0.133  0.034  -0.566 14  GLU   AAA CD  
78   O  OE1 . GLU   A 15  ? 1.329 1.091 1.042 0.153  0.188  -0.469 14  GLU   AAA OE1 
79   O  OE2 . GLU   A 15  ? 1.147 1.269 0.943 -0.202 0.118  -0.528 14  GLU   AAA OE2 
80   N  N   . GLN   A 16  ? 0.953 0.055 1.000 0.209  0.054  0.060  15  GLN   AAA N   
81   C  CA  . GLN   A 16  ? 0.779 0.016 0.904 0.032  -0.010 0.088  15  GLN   AAA CA  
82   C  C   . GLN   A 16  ? 0.691 0.185 0.825 0.010  0.071  0.196  15  GLN   AAA C   
83   O  O   . GLN   A 16  ? 0.731 0.009 0.708 0.001  0.049  0.044  15  GLN   AAA O   
84   C  CB  . GLN   A 16  ? 0.845 0.331 0.917 -0.049 -0.044 0.103  15  GLN   AAA CB  
85   C  CG  . GLN   A 16  ? 0.864 0.454 1.108 -0.037 -0.163 -0.031 15  GLN   AAA CG  
86   C  CD  . GLN   A 16  ? 1.118 0.491 1.478 -0.208 -0.043 0.113  15  GLN   AAA CD  
87   O  OE1 . GLN   A 16  ? 0.993 0.164 1.534 -0.039 -0.195 0.377  15  GLN   AAA OE1 
88   N  NE2 . GLN   A 16  ? 1.105 0.813 1.492 -0.129 0.013  0.299  15  GLN   AAA NE2 
89   N  N   . TRP   A 17  ? 0.654 0.007 0.679 -0.019 0.058  -0.019 16  TRP   AAA N   
90   C  CA  . TRP   A 17  ? 0.626 0.210 0.520 0.048  0.015  0.008  16  TRP   AAA CA  
91   C  C   . TRP   A 17  ? 0.646 0.064 0.522 -0.011 0.134  -0.117 16  TRP   AAA C   
92   O  O   . TRP   A 17  ? 0.620 0.110 0.523 0.069  0.115  0.032  16  TRP   AAA O   
93   C  CB  . TRP   A 17  ? 0.587 0.135 0.457 -0.017 0.062  -0.073 16  TRP   AAA CB  
94   C  CG  . TRP   A 17  ? 0.509 0.068 0.430 0.043  0.005  0.035  16  TRP   AAA CG  
95   C  CD1 . TRP   A 17  ? 0.525 0.252 0.416 0.019  0.048  0.023  16  TRP   AAA CD1 
96   C  CD2 . TRP   A 17  ? 0.480 0.179 0.473 0.055  0.047  0.052  16  TRP   AAA CD2 
97   N  NE1 . TRP   A 17  ? 0.529 0.149 0.464 0.088  0.046  0.018  16  TRP   AAA NE1 
98   C  CE2 . TRP   A 17  ? 0.512 0.194 0.425 -0.010 0.100  -0.003 16  TRP   AAA CE2 
99   C  CE3 . TRP   A 17  ? 0.540 0.037 0.436 0.075  0.101  -0.039 16  TRP   AAA CE3 
100  C  CZ2 . TRP   A 17  ? 0.477 0.210 0.413 0.044  0.105  0.038  16  TRP   AAA CZ2 
101  C  CZ3 . TRP   A 17  ? 0.391 0.213 0.471 0.063  0.059  0.038  16  TRP   AAA CZ3 
102  C  CH2 . TRP   A 17  ? 0.430 0.219 0.394 0.090  0.037  -0.042 16  TRP   AAA CH2 
103  N  N   . SER   A 18  ? 0.657 0.054 0.590 0.011  -0.028 -0.111 17  SER   AAA N   
104  C  CA  . SER   A 18  ? 0.656 0.096 0.595 -0.021 0.081  -0.114 17  SER   AAA CA  
105  C  C   . SER   A 18  ? 0.744 0.015 0.614 0.062  0.049  -0.041 17  SER   AAA C   
106  O  O   . SER   A 18  ? 0.765 0.045 0.924 -0.169 0.025  -0.034 17  SER   AAA O   
107  C  CB  . SER   A 18  ? 0.740 0.020 0.750 -0.040 0.123  -0.097 17  SER   AAA CB  
108  O  OG  . SER   A 18  ? 0.690 0.072 0.624 -0.038 0.086  -0.001 17  SER   AAA OG  
109  N  N   . LYS   A 19  ? 0.746 0.007 0.644 0.004  0.046  0.014  18  LYS   AAA N   
110  C  CA  . LYS   A 19  ? 0.719 0.153 0.608 0.030  0.064  0.088  18  LYS   AAA CA  
111  C  C   . LYS   A 19  ? 0.770 0.040 0.679 -0.117 0.091  -0.024 18  LYS   AAA C   
112  O  O   . LYS   A 19  ? 0.941 0.019 0.959 -0.072 0.112  0.071  18  LYS   AAA O   
113  C  CB  . LYS   A 19  ? 0.663 0.432 0.743 0.047  0.160  0.222  18  LYS   AAA CB  
114  C  CG  . LYS   A 19  ? 0.858 0.367 1.005 0.141  0.090  0.194  18  LYS   AAA CG  
115  C  CD  . LYS   A 19  ? 0.808 0.726 1.065 0.179  0.152  0.314  18  LYS   AAA CD  
116  C  CE  . LYS   A 19  ? 0.757 0.759 0.914 0.247  0.225  0.553  18  LYS   AAA CE  
117  N  NZ  . LYS   A 19  ? 0.906 1.158 0.837 0.296  0.093  0.223  18  LYS   AAA NZ  
118  N  N   . LEU   A 20  ? 0.934 0.018 0.822 -0.094 0.033  0.038  19  LEU   AAA N   
119  C  CA  . LEU   A 20  ? 0.789 0.248 0.460 -0.062 0.057  0.063  19  LEU   AAA CA  
120  C  C   . LEU   A 20  ? 0.672 0.075 0.520 -0.044 0.164  0.052  19  LEU   AAA C   
121  O  O   . LEU   A 20  ? 0.736 0.021 0.587 0.035  0.112  0.054  19  LEU   AAA O   
122  C  CB  . LEU   A 20  ? 1.075 0.358 0.692 -0.159 0.007  -0.065 19  LEU   AAA CB  
123  C  CG  . LEU   A 20  ? 1.210 0.853 0.741 0.015  -0.056 -0.121 19  LEU   AAA CG  
124  C  CD1 . LEU   A 20  ? 1.369 1.333 1.050 -0.008 0.085  -0.011 19  LEU   AAA CD1 
125  C  CD2 . LEU   A 20  ? 1.096 0.523 0.671 0.145  -0.015 -0.153 19  LEU   AAA CD2 
126  N  N   . TYR   A 21  ? 0.719 0.012 0.462 -0.002 0.125  0.049  20  TYR   AAA N   
127  C  CA  . TYR   A 21  ? 0.582 0.023 0.463 -0.042 0.168  0.052  20  TYR   AAA CA  
128  C  C   . TYR   A 21  ? 0.852 0.008 0.785 -0.013 0.089  0.033  20  TYR   AAA C   
129  O  O   . TYR   A 21  ? 0.977 0.011 0.866 -0.069 0.179  -0.009 20  TYR   AAA O   
130  C  CB  . TYR   A 21  ? 0.683 0.007 0.581 -0.011 0.149  -0.015 20  TYR   AAA CB  
131  C  CG  . TYR   A 21  ? 0.730 0.127 0.498 -0.023 0.058  -0.037 20  TYR   AAA CG  
132  C  CD1 . TYR   A 21  ? 0.712 0.292 0.583 -0.040 0.163  -0.119 20  TYR   AAA CD1 
133  C  CD2 . TYR   A 21  ? 0.681 0.012 0.556 -0.058 0.045  0.009  20  TYR   AAA CD2 
134  C  CE1 . TYR   A 21  ? 0.779 0.020 0.643 -0.092 0.071  0.034  20  TYR   AAA CE1 
135  C  CE2 . TYR   A 21  ? 0.691 0.213 0.478 -0.089 0.051  -0.019 20  TYR   AAA CE2 
136  C  CZ  . TYR   A 21  ? 0.790 0.037 0.604 -0.155 0.017  -0.001 20  TYR   AAA CZ  
137  O  OH  . TYR   A 21  ? 0.876 0.376 0.607 -0.265 0.081  -0.226 20  TYR   AAA OH  
138  N  N   . PRO   A 22  ? 0.621 0.041 0.562 -0.127 0.117  -0.093 21  PRO   AAA N   
139  C  CA  . PRO   A 22  ? 0.808 0.010 0.801 -0.025 0.177  -0.050 21  PRO   AAA CA  
140  C  C   . PRO   A 22  ? 0.619 0.052 0.616 -0.016 0.117  -0.166 21  PRO   AAA C   
141  O  O   . PRO   A 22  ? 0.898 0.008 0.811 -0.026 0.123  -0.036 21  PRO   AAA O   
142  C  CB  . PRO   A 22  ? 0.706 0.029 0.744 -0.021 0.152  -0.128 21  PRO   AAA CB  
143  C  CG  . PRO   A 22  ? 0.780 0.037 0.798 -0.046 0.077  -0.151 21  PRO   AAA CG  
144  C  CD  . PRO   A 22  ? 0.687 0.009 0.695 -0.035 0.218  -0.026 21  PRO   AAA CD  
145  N  N   . ILE   A 23  ? 0.580 0.045 0.544 0.043  0.077  -0.124 22  ILE   AAA N   
146  C  CA  . ILE   A 23  ? 0.559 0.064 0.538 -0.004 0.091  -0.090 22  ILE   AAA CA  
147  C  C   . ILE   A 23  ? 0.503 0.017 0.532 -0.010 0.003  -0.074 22  ILE   AAA C   
148  O  O   . ILE   A 23  ? 0.578 0.194 0.545 -0.030 0.057  -0.118 22  ILE   AAA O   
149  C  CB  . ILE   A 23  ? 0.414 0.113 0.558 0.042  0.085  -0.070 22  ILE   AAA CB  
150  C  CG1 . ILE   A 23  ? 0.507 0.126 0.592 0.066  0.106  -0.020 22  ILE   AAA CG1 
151  C  CG2 . ILE   A 23  ? 0.471 0.170 0.579 0.019  0.051  -0.068 22  ILE   AAA CG2 
152  C  CD1 . ILE   A 23  ? 0.605 0.314 0.456 0.016  -0.004 0.006  22  ILE   AAA CD1 
153  N  N   . ALA   A 24  ? 0.508 0.083 0.582 -0.083 -0.002 -0.113 23  ALA   AAA N   
154  C  CA  . ALA   A 24  ? 0.535 0.035 0.619 -0.030 0.062  -0.119 23  ALA   AAA CA  
155  C  C   . ALA   A 24  ? 0.515 0.238 0.576 0.015  0.046  -0.153 23  ALA   AAA C   
156  O  O   . ALA   A 24  ? 0.714 0.019 0.676 0.038  0.124  -0.076 23  ALA   AAA O   
157  C  CB  . ALA   A 24  ? 0.525 0.098 0.544 0.032  0.081  -0.118 23  ALA   AAA CB  
158  N  N   . ASN   A 25  ? 0.695 0.184 0.543 -0.061 0.165  -0.077 24  ASN   AAA N   
159  C  CA  . ASN   A 25  ? 0.713 0.010 0.621 0.014  0.095  -0.045 24  ASN   AAA CA  
160  C  C   . ASN   A 25  ? 0.766 0.016 0.615 -0.084 0.050  -0.019 24  ASN   AAA C   
161  O  O   . ASN   A 25  ? 0.541 0.294 0.763 -0.088 0.040  -0.310 24  ASN   AAA O   
162  C  CB  . ASN   A 25  ? 0.722 0.012 0.590 -0.019 0.143  -0.056 24  ASN   AAA CB  
163  C  CG  . ASN   A 25  ? 0.724 0.267 0.624 -0.094 0.107  -0.086 24  ASN   AAA CG  
164  O  OD1 . ASN   A 25  ? 0.793 0.060 0.777 -0.017 -0.009 -0.031 24  ASN   AAA OD1 
165  N  ND2 . ASN   A 25  ? 0.786 0.042 0.869 0.110  0.291  -0.083 24  ASN   AAA ND2 
166  N  N   . GLY   A 26  ? 0.585 0.013 0.636 0.010  0.076  -0.064 25  GLY   AAA N   
167  C  CA  . GLY   A 26  ? 0.662 0.042 0.644 -0.113 0.029  0.096  25  GLY   AAA CA  
168  C  C   . GLY   A 26  ? 0.458 0.019 0.633 -0.038 0.036  -0.079 25  GLY   AAA C   
169  O  O   . GLY   A 26  ? 0.488 0.145 0.619 -0.047 0.099  -0.156 25  GLY   AAA O   
170  N  N   . ASN   A 27  ? 0.578 0.068 0.491 -0.027 -0.043 -0.126 26  ASN   AAA N   
171  C  CA  . ASN   A 27  ? 0.587 0.128 0.493 -0.061 0.020  -0.136 26  ASN   AAA CA  
172  C  C   . ASN   A 27  ? 0.541 0.159 0.447 -0.060 -0.011 -0.150 26  ASN   AAA C   
173  O  O   . ASN   A 27  ? 0.702 0.074 0.504 -0.048 0.039  -0.135 26  ASN   AAA O   
174  C  CB  . ASN   A 27  ? 0.619 0.086 0.573 -0.174 0.048  -0.144 26  ASN   AAA CB  
175  C  CG  . ASN   A 27  ? 0.596 0.201 0.669 -0.302 0.059  -0.022 26  ASN   AAA CG  
176  O  OD1 . ASN   A 27  ? 0.746 0.460 0.749 -0.129 -0.013 -0.303 26  ASN   AAA OD1 
177  N  ND2 . ASN   A 27  ? 0.591 0.355 0.728 -0.270 0.108  -0.046 26  ASN   AAA ND2 
178  N  N   . ASN   A 28  ? 0.536 0.119 0.496 -0.126 0.015  -0.147 27  ASN   AAA N   
179  C  CA  . ASN   A 28  ? 0.537 0.086 0.504 -0.091 -0.024 -0.164 27  ASN   AAA CA  
180  C  C   . ASN   A 28  ? 0.488 0.073 0.442 -0.056 0.038  -0.165 27  ASN   AAA C   
181  O  O   . ASN   A 28  ? 0.506 0.064 0.466 0.001  0.013  -0.163 27  ASN   AAA O   
182  C  CB  . ASN   A 28  ? 0.524 0.094 0.533 -0.058 -0.003 -0.077 27  ASN   AAA CB  
183  C  CG  . ASN   A 28  ? 0.401 0.281 0.506 0.036  0.015  0.023  27  ASN   AAA CG  
184  O  OD1 . ASN   A 28  ? 0.556 0.583 0.518 0.098  -0.057 0.037  27  ASN   AAA OD1 
185  N  ND2 . ASN   A 28  ? 0.468 0.149 0.669 -0.075 0.028  -0.077 27  ASN   AAA ND2 
186  N  N   . GLN   A 29  ? 0.491 0.029 0.511 -0.063 0.016  -0.087 28  GLN   AAA N   
187  C  CA  . GLN   A 29  ? 0.460 0.176 0.439 0.042  0.024  -0.094 28  GLN   AAA CA  
188  C  C   . GLN   A 29  ? 0.461 0.111 0.402 -0.012 0.014  -0.123 28  GLN   AAA C   
189  O  O   . GLN   A 29  ? 0.517 0.082 0.445 -0.072 0.023  -0.173 28  GLN   AAA O   
190  C  CB  . GLN   A 29  ? 0.493 0.067 0.476 0.054  0.030  -0.124 28  GLN   AAA CB  
191  C  CG  . GLN   A 29  ? 0.533 0.091 0.533 -0.046 0.052  -0.189 28  GLN   AAA CG  
192  C  CD  . GLN   A 29  ? 0.438 0.047 0.504 0.018  -0.008 -0.141 28  GLN   AAA CD  
193  O  OE1 . GLN   A 29  ? 0.455 0.142 0.503 -0.024 0.001  -0.146 28  GLN   AAA OE1 
194  N  NE2 . GLN   A 29  ? 0.455 0.014 0.545 0.015  0.032  -0.062 28  GLN   AAA NE2 
195  N  N   . SER   A 30  ? 0.445 0.156 0.425 -0.008 0.011  -0.124 29  SER   AAA N   
196  C  CA  . SER   A 30  ? 0.491 0.012 0.395 0.003  0.042  -0.046 29  SER   AAA CA  
197  C  C   . SER   A 30  ? 0.479 0.011 0.447 0.020  0.052  -0.039 29  SER   AAA C   
198  O  O   . SER   A 30  ? 0.467 0.038 0.457 -0.007 0.035  -0.030 29  SER   AAA O   
199  C  CB  . SER   A 30  ? 0.484 0.024 0.433 -0.006 0.019  -0.087 29  SER   AAA CB  
200  O  OG  . SER   A 30  ? 0.417 0.027 0.460 -0.033 0.016  -0.092 29  SER   AAA OG  
201  N  N   . PRO   A 31  ? 0.479 0.028 0.374 0.025  0.033  -0.084 30  PRO   AAA N   
202  C  CA  . PRO   A 31  ? 0.378 0.171 0.352 0.076  0.029  -0.097 30  PRO   AAA CA  
203  C  C   . PRO   A 31  ? 0.491 0.214 0.357 0.044  0.063  -0.116 30  PRO   AAA C   
204  O  O   . PRO   A 31  ? 0.413 0.160 0.455 -0.018 0.039  -0.134 30  PRO   AAA O   
205  C  CB  . PRO   A 31  ? 0.421 0.212 0.322 0.057  0.023  -0.081 30  PRO   AAA CB  
206  C  CG  . PRO   A 31  ? 0.435 0.141 0.422 0.005  0.049  -0.011 30  PRO   AAA CG  
207  C  CD  . PRO   A 31  ? 0.405 0.192 0.462 0.036  0.050  -0.054 30  PRO   AAA CD  
208  N  N   . VAL   A 32  ? 0.446 0.140 0.344 0.039  0.019  -0.089 31  VAL   AAA N   
209  C  CA  . VAL   A 32  ? 0.481 0.232 0.391 -0.020 0.018  -0.148 31  VAL   AAA CA  
210  C  C   . VAL   A 32  ? 0.436 0.079 0.491 -0.062 0.041  -0.181 31  VAL   AAA C   
211  O  O   . VAL   A 32  ? 0.448 0.045 0.488 -0.069 0.004  -0.072 31  VAL   AAA O   
212  C  CB  . VAL   A 32  ? 0.440 0.104 0.430 0.019  0.036  -0.132 31  VAL   AAA CB  
213  C  CG1 . VAL   A 32  ? 0.380 0.036 0.515 0.027  0.008  -0.105 31  VAL   AAA CG1 
214  C  CG2 . VAL   A 32  ? 0.413 0.217 0.446 0.064  -0.012 -0.093 31  VAL   AAA CG2 
215  N  N   . ASP   A 33  ? 0.477 0.035 0.460 0.025  0.077  -0.106 32  ASP   AAA N   
216  C  CA  . ASP   A 33  ? 0.432 0.032 0.479 0.002  0.096  -0.108 32  ASP   AAA CA  
217  C  C   . ASP   A 33  ? 0.409 0.149 0.475 -0.042 0.050  -0.104 32  ASP   AAA C   
218  O  O   . ASP   A 33  ? 0.485 0.152 0.512 -0.021 0.019  -0.135 32  ASP   AAA O   
219  C  CB  . ASP   A 33  ? 0.586 0.020 0.478 0.014  0.054  -0.077 32  ASP   AAA CB  
220  C  CG  . ASP   A 33  ? 0.502 0.143 0.477 -0.032 0.042  -0.123 32  ASP   AAA CG  
221  O  OD1 . ASP   A 33  ? 0.471 0.209 0.492 -0.038 0.123  -0.117 32  ASP   AAA OD1 
222  O  OD2 . ASP   A 33  ? 0.607 0.201 0.482 -0.135 0.048  -0.157 32  ASP   AAA OD2 
223  N  N   . ILE   A 34  ? 0.454 0.194 0.394 -0.060 0.028  -0.088 33  ILE   AAA N   
224  C  CA  . ILE   A 34  ? 0.477 0.048 0.436 -0.014 0.015  -0.100 33  ILE   AAA CA  
225  C  C   . ILE   A 34  ? 0.401 0.267 0.428 -0.043 0.009  -0.138 33  ILE   AAA C   
226  O  O   . ILE   A 34  ? 0.454 0.199 0.473 -0.070 0.015  -0.205 33  ILE   AAA O   
227  C  CB  . ILE   A 34  ? 0.479 0.060 0.476 -0.044 0.057  -0.069 33  ILE   AAA CB  
228  C  CG1 . ILE   A 34  ? 0.426 0.181 0.441 -0.070 0.009  -0.125 33  ILE   AAA CG1 
229  C  CG2 . ILE   A 34  ? 0.471 0.138 0.480 0.021  0.046  -0.099 33  ILE   AAA CG2 
230  C  CD1 . ILE   A 34  ? 0.596 0.196 0.508 -0.021 0.043  -0.138 33  ILE   AAA CD1 
231  N  N   . LYS   A 35  ? 0.458 0.209 0.475 -0.064 0.035  -0.133 34  LYS   AAA N   
232  C  CA  . LYS   A 35  ? 0.486 0.301 0.456 -0.016 0.007  -0.163 34  LYS   AAA CA  
233  C  C   . LYS   A 35  ? 0.447 0.222 0.407 0.005  0.052  -0.176 34  LYS   AAA C   
234  O  O   . LYS   A 35  ? 0.525 0.331 0.444 0.101  0.009  -0.147 34  LYS   AAA O   
235  C  CB  . LYS   A 35  ? 0.538 0.263 0.513 -0.004 -0.004 -0.173 34  LYS   AAA CB  
236  C  CG  . LYS   A 35  ? 0.560 0.515 0.462 -0.060 -0.032 -0.103 34  LYS   AAA CG  
237  C  CD  . LYS   A 35  ? 0.631 0.552 0.572 -0.161 -0.030 -0.099 34  LYS   AAA CD  
238  C  CE  . LYS   A 35  ? 0.726 0.655 0.634 -0.147 -0.079 -0.051 34  LYS   AAA CE  
239  N  NZ  . LYS   A 35  ? 0.781 0.218 0.748 -0.134 0.105  -0.032 34  LYS   AAA NZ  
240  N  N   . THR   A 36  ? 0.461 0.199 0.384 0.011  0.068  -0.174 35  THR   AAA N   
241  C  CA  . THR   A 36  ? 0.513 0.327 0.383 -0.021 0.008  -0.103 35  THR   AAA CA  
242  C  C   . THR   A 36  ? 0.517 0.249 0.468 0.023  -0.006 -0.143 35  THR   AAA C   
243  O  O   . THR   A 36  ? 0.590 0.310 0.503 -0.099 -0.049 0.037  35  THR   AAA O   
244  C  CB  . THR   A 36  ? 0.431 0.419 0.451 0.006  -0.066 -0.044 35  THR   AAA CB  
245  O  OG1 . THR   A 36  ? 0.523 0.210 0.561 -0.018 -0.033 -0.129 35  THR   AAA OG1 
246  C  CG2 . THR   A 36  ? 0.530 0.257 0.589 -0.019 -0.063 -0.072 35  THR   AAA CG2 
247  N  N   . SER   A 37  ? 0.557 0.259 0.478 0.021  -0.009 -0.196 36  SER   AAA N   
248  C  CA  . SER   A 37  ? 0.563 0.303 0.479 0.110  0.014  -0.205 36  SER   AAA CA  
249  C  C   . SER   A 37  ? 0.511 0.462 0.427 0.078  -0.053 -0.168 36  SER   AAA C   
250  O  O   . SER   A 37  ? 0.566 0.473 0.414 0.001  -0.058 -0.134 36  SER   AAA O   
251  C  CB  . SER   A 37  ? 0.590 0.251 0.479 0.101  0.007  -0.204 36  SER   AAA CB  
252  O  OG  . SER   A 37  ? 0.590 0.454 0.499 0.028  0.043  -0.114 36  SER   AAA OG  
253  N  N   . GLU   A 38  ? 0.568 0.322 0.459 -0.087 0.040  -0.169 37  GLU   AAA N   
254  C  CA  . GLU   A 38  ? 0.603 0.431 0.457 -0.057 0.090  -0.186 37  GLU   AAA CA  
255  C  C   . GLU   A 38  ? 0.486 0.392 0.484 -0.104 0.037  -0.141 37  GLU   AAA C   
256  O  O   . GLU   A 38  ? 0.505 0.499 0.529 -0.030 0.055  -0.189 37  GLU   AAA O   
257  C  CB  . GLU   A 38  ? 0.700 0.273 0.559 -0.048 0.092  -0.181 37  GLU   AAA CB  
258  C  CG  . GLU   A 38  ? 0.640 0.472 0.674 0.096  0.051  -0.221 37  GLU   AAA CG  
259  C  CD  . GLU   A 38  ? 0.826 0.747 0.526 -0.119 0.182  -0.266 37  GLU   AAA CD  
260  O  OE1 . GLU   A 38  ? 0.705 0.857 0.689 -0.214 0.238  -0.301 37  GLU   AAA OE1 
261  O  OE2 . GLU   A 38  ? 1.075 0.585 1.166 0.019  0.110  -0.609 37  GLU   AAA OE2 
262  N  N   . THR   A 39  ? 0.548 0.353 0.411 -0.066 0.040  -0.198 38  THR   AAA N   
263  C  CA  . THR   A 39  ? 0.443 0.424 0.464 -0.064 0.043  -0.281 38  THR   AAA CA  
264  C  C   . THR   A 39  ? 0.493 0.513 0.512 -0.053 0.024  -0.253 38  THR   AAA C   
265  O  O   . THR   A 39  ? 0.671 0.559 0.527 -0.117 0.099  -0.181 38  THR   AAA O   
266  C  CB  . THR   A 39  ? 0.479 0.453 0.480 -0.116 0.001  -0.176 38  THR   AAA CB  
267  O  OG1 . THR   A 39  ? 0.596 0.580 0.379 -0.051 -0.032 -0.148 38  THR   AAA OG1 
268  C  CG2 . THR   A 39  ? 0.488 0.440 0.452 -0.025 0.043  -0.155 38  THR   AAA CG2 
269  N  N   . LYS   A 40  ? 0.592 0.357 0.487 -0.018 -0.032 -0.227 39  LYS   AAA N   
270  C  CA  . LYS   A 40  ? 0.602 0.359 0.478 -0.115 -0.046 -0.152 39  LYS   AAA CA  
271  C  C   . LYS   A 40  ? 0.652 0.358 0.493 -0.036 0.019  -0.149 39  LYS   AAA C   
272  O  O   . LYS   A 40  ? 0.552 0.537 0.443 0.097  -0.103 -0.187 39  LYS   AAA O   
273  C  CB  . LYS   A 40  ? 0.795 0.369 0.622 -0.315 0.090  0.100  39  LYS   AAA CB  
274  C  CG  . LYS   A 40  ? 0.792 0.400 0.840 -0.368 0.005  0.110  39  LYS   AAA CG  
275  C  CD  . LYS   A 40  ? 1.099 0.326 0.984 -0.337 -0.089 -0.058 39  LYS   AAA CD  
276  C  CE  . LYS   A 40  ? 1.715 0.167 1.081 -0.366 -0.114 -0.180 39  LYS   AAA CE  
277  N  NZ  . LYS   A 40  ? 1.308 0.514 1.340 -0.145 -0.269 -0.013 39  LYS   AAA NZ  
278  N  N   . HIS   A 41  ? 0.637 0.241 0.491 0.012  -0.103 -0.073 40  HIS   AAA N   
279  C  CA  . HIS   A 41  ? 0.656 0.205 0.587 -0.132 -0.061 -0.064 40  HIS   AAA CA  
280  C  C   . HIS   A 41  ? 0.694 0.466 0.594 -0.084 -0.161 -0.060 40  HIS   AAA C   
281  O  O   . HIS   A 41  ? 0.946 0.984 0.707 -0.142 -0.321 -0.340 40  HIS   AAA O   
282  C  CB  . HIS   A 41  ? 0.641 0.336 0.543 -0.046 -0.027 -0.147 40  HIS   AAA CB  
283  C  CG  . HIS   A 41  ? 0.710 0.400 0.502 -0.043 -0.063 -0.000 40  HIS   AAA CG  
284  N  ND1 . HIS   A 41  ? 0.728 0.764 0.705 -0.206 -0.133 -0.085 40  HIS   AAA ND1 
285  C  CD2 . HIS   A 41  ? 0.728 0.795 0.471 0.001  -0.231 -0.017 40  HIS   AAA CD2 
286  C  CE1 . HIS   A 41  ? 0.675 0.929 0.434 -0.066 -0.157 -0.052 40  HIS   AAA CE1 
287  N  NE2 . HIS   A 41  ? 0.803 0.763 0.476 -0.016 -0.263 0.117  40  HIS   AAA NE2 
288  N  N   . ASP   A 42  ? 0.573 0.745 0.523 0.052  -0.131 -0.152 41  ASP   AAA N   
289  C  CA  . ASP   A 42  ? 0.631 0.507 0.447 0.053  -0.036 -0.182 41  ASP   AAA CA  
290  C  C   . ASP   A 42  ? 0.662 0.591 0.443 0.033  -0.131 -0.043 41  ASP   AAA C   
291  O  O   . ASP   A 42  ? 0.630 0.588 0.537 -0.013 -0.066 -0.049 41  ASP   AAA O   
292  C  CB  . ASP   A 42  ? 0.612 0.400 0.489 0.034  -0.009 -0.198 41  ASP   AAA CB  
293  C  CG  . ASP   A 42  ? 0.586 0.668 0.519 0.088  -0.000 0.043  41  ASP   AAA CG  
294  O  OD1 . ASP   A 42  ? 0.503 0.778 0.583 0.047  -0.128 0.042  41  ASP   AAA OD1 
295  O  OD2 . ASP   A 42  ? 0.565 0.822 0.567 0.000  0.077  -0.072 41  ASP   AAA OD2 
296  N  N   . THR   A 43  ? 0.785 0.369 0.481 0.063  -0.194 -0.067 42  THR   AAA N   
297  C  CA  . THR   A 43  ? 0.926 0.533 0.456 -0.075 -0.166 0.033  42  THR   AAA CA  
298  C  C   . THR   A 43  ? 0.745 0.529 0.554 -0.167 -0.141 -0.040 42  THR   AAA C   
299  O  O   . THR   A 43  ? 0.623 0.484 0.808 -0.044 -0.120 0.046  42  THR   AAA O   
300  C  CB  . THR   A 43  ? 0.892 0.722 0.429 -0.024 -0.222 0.193  42  THR   AAA CB  
301  O  OG1 . THR   A 43  ? 0.901 1.065 0.501 -0.021 0.000  0.130  42  THR   AAA OG1 
302  C  CG2 . THR   A 43  ? 0.735 0.693 0.460 -0.230 -0.200 0.015  42  THR   AAA CG2 
303  N  N   . SER   A 44  ? 0.777 0.535 0.416 -0.077 -0.165 -0.117 43  SER   AAA N   
304  C  CA  . SER   A 44  ? 0.727 0.633 0.575 -0.052 -0.064 -0.058 43  SER   AAA CA  
305  C  C   . SER   A 44  ? 0.636 0.536 0.660 0.082  -0.046 -0.216 43  SER   AAA C   
306  O  O   . SER   A 44  ? 0.549 0.716 0.696 0.166  0.016  -0.272 43  SER   AAA O   
307  C  CB  . SER   A 44  ? 0.684 0.551 0.637 -0.036 -0.114 0.037  43  SER   AAA CB  
308  O  OG  . SER   A 44  ? 0.561 0.351 0.660 -0.007 -0.071 -0.005 43  SER   AAA OG  
309  N  N   . LEU   A 45  ? 0.716 0.721 0.412 0.145  -0.133 -0.148 44  LEU   AAA N   
310  C  CA  . LEU   A 45  ? 0.593 0.284 0.537 0.042  -0.109 -0.132 44  LEU   AAA CA  
311  C  C   . LEU   A 45  ? 0.519 0.493 0.337 -0.043 -0.009 -0.029 44  LEU   AAA C   
312  O  O   . LEU   A 45  ? 0.656 0.500 0.339 -0.082 0.033  0.002  44  LEU   AAA O   
313  C  CB  . LEU   A 45  ? 0.482 0.597 0.513 0.072  -0.101 -0.044 44  LEU   AAA CB  
314  C  CG  . LEU   A 45  ? 0.536 0.515 0.459 0.016  -0.060 -0.099 44  LEU   AAA CG  
315  C  CD1 . LEU   A 45  ? 0.528 0.426 0.475 -0.026 -0.062 -0.052 44  LEU   AAA CD1 
316  C  CD2 . LEU   A 45  ? 0.458 0.579 0.451 -0.032 -0.062 -0.084 44  LEU   AAA CD2 
317  N  N   . LYS   A 46  ? 0.486 0.323 0.529 0.003  -0.068 -0.037 45  LYS   AAA N   
318  C  CA  . LYS   A 46  ? 0.564 0.378 0.592 -0.064 -0.051 -0.028 45  LYS   AAA CA  
319  C  C   . LYS   A 46  ? 0.518 0.418 0.447 0.058  -0.004 -0.014 45  LYS   AAA C   
320  O  O   . LYS   A 46  ? 0.547 0.359 0.381 0.032  -0.044 -0.050 45  LYS   AAA O   
321  C  CB  . LYS   A 46  ? 0.541 0.458 0.705 0.083  -0.091 0.050  45  LYS   AAA CB  
322  C  CG  . LYS   A 46  ? 0.535 0.541 0.887 0.023  -0.098 0.079  45  LYS   AAA CG  
323  C  CD  . LYS   A 46  ? 0.557 0.716 1.027 -0.012 -0.074 -0.040 45  LYS   AAA CD  
324  C  CE  . LYS   A 46  ? 0.470 1.194 1.002 0.085  -0.153 0.021  45  LYS   AAA CE  
325  N  NZ  . LYS   A 46  ? 0.588 1.263 0.916 0.160  -0.184 -0.015 45  LYS   AAA NZ  
326  N  N   . PRO   A 47  ? 0.484 0.463 0.449 -0.001 -0.031 0.044  46  PRO   AAA N   
327  C  CA  . PRO   A 47  ? 0.520 0.410 0.407 0.052  -0.046 0.005  46  PRO   AAA CA  
328  C  C   . PRO   A 47  ? 0.568 0.281 0.418 0.046  -0.033 -0.016 46  PRO   AAA C   
329  O  O   . PRO   A 47  ? 0.630 0.284 0.484 0.091  -0.020 0.067  46  PRO   AAA O   
330  C  CB  . PRO   A 47  ? 0.513 0.494 0.375 0.058  0.023  0.068  46  PRO   AAA CB  
331  C  CG  . PRO   A 47  ? 0.638 0.447 0.394 -0.016 -0.047 0.119  46  PRO   AAA CG  
332  C  CD  . PRO   A 47  ? 0.619 0.447 0.442 -0.005 -0.078 0.027  46  PRO   AAA CD  
333  N  N   . ILE   A 48  ? 0.630 0.305 0.454 0.090  -0.054 -0.053 47  ILE   AAA N   
334  C  CA  . ILE   A 48  ? 0.541 0.304 0.452 0.009  -0.069 -0.093 47  ILE   AAA CA  
335  C  C   . ILE   A 48  ? 0.443 0.287 0.387 0.033  0.003  -0.011 47  ILE   AAA C   
336  O  O   . ILE   A 48  ? 0.620 0.288 0.413 -0.044 0.049  0.004  47  ILE   AAA O   
337  C  CB  . ILE   A 48  ? 0.713 0.234 0.468 0.027  -0.108 0.013  47  ILE   AAA CB  
338  C  CG1 . ILE   A 48  ? 0.692 0.262 0.422 -0.035 0.016  -0.112 47  ILE   AAA CG1 
339  C  CG2 . ILE   A 48  ? 0.867 0.233 0.444 0.020  -0.095 0.081  47  ILE   AAA CG2 
340  C  CD1 . ILE   A 48  ? 0.661 0.356 0.463 0.019  0.060  -0.045 47  ILE   AAA CD1 
341  N  N   . SER   A 49  ? 0.532 0.237 0.417 -0.019 0.037  -0.049 48  SER   AAA N   
342  C  CA  . SER   A 49  ? 0.550 0.248 0.459 -0.009 -0.012 -0.075 48  SER   AAA CA  
343  C  C   . SER   A 49  ? 0.554 0.232 0.428 -0.018 -0.006 -0.059 48  SER   AAA C   
344  O  O   . SER   A 49  ? 0.574 0.226 0.440 0.010  -0.025 -0.019 48  SER   AAA O   
345  C  CB  . SER   A 49  ? 0.637 0.303 0.524 0.058  0.001  -0.004 48  SER   AAA CB  
346  O  OG  . SER   A 49  ? 0.750 0.229 0.620 0.106  -0.049 0.074  48  SER   AAA OG  
347  N  N   . VAL   A 50  ? 0.542 0.061 0.384 0.073  0.010  -0.025 49  VAL   AAA N   
348  C  CA  . VAL   A 50  ? 0.515 0.014 0.432 -0.031 -0.040 -0.047 49  VAL   AAA CA  
349  C  C   . VAL   A 50  ? 0.579 0.042 0.422 -0.121 0.059  -0.078 49  VAL   AAA C   
350  O  O   . VAL   A 50  ? 0.521 0.208 0.426 0.010  0.035  0.054  49  VAL   AAA O   
351  C  CB  . VAL   A 50  ? 0.516 0.078 0.510 -0.014 0.005  -0.083 49  VAL   AAA CB  
352  C  CG1 . VAL   A 50  ? 0.657 0.059 0.503 -0.014 -0.087 -0.140 49  VAL   AAA CG1 
353  C  CG2 . VAL   A 50  ? 0.549 0.126 0.548 0.099  0.066  0.029  49  VAL   AAA CG2 
354  N  N   . SER   A 51  ? 0.581 0.029 0.456 -0.105 0.076  0.025  50  SER   AAA N   
355  C  CA  . SER   A 51  ? 0.565 0.008 0.419 -0.022 0.043  -0.018 50  SER   AAA CA  
356  C  C   . SER   A 51  ? 0.449 0.014 0.438 0.005  0.016  -0.044 50  SER   AAA C   
357  O  O   . SER   A 51  ? 0.504 0.165 0.464 -0.046 0.076  0.012  50  SER   AAA O   
358  C  CB  . SER   A 51  ? 0.573 0.091 0.563 -0.011 0.053  0.016  50  SER   AAA CB  
359  O  OG  . SER   A 51  ? 0.782 0.110 0.534 0.010  0.017  -0.022 50  SER   AAA OG  
360  N  N   . TYR   A 52  ? 0.459 0.023 0.454 0.010  -0.037 -0.018 51  TYR   AAA N   
361  C  CA  . TYR   A 52  ? 0.453 0.173 0.449 -0.017 -0.017 -0.042 51  TYR   AAA CA  
362  C  C   . TYR   A 52  ? 0.577 0.208 0.514 -0.071 0.072  -0.079 51  TYR   AAA C   
363  O  O   . TYR   A 52  ? 0.729 0.065 0.633 -0.058 0.123  -0.120 51  TYR   AAA O   
364  C  CB  . TYR   A 52  ? 0.392 0.178 0.482 -0.067 -0.054 -0.021 51  TYR   AAA CB  
365  C  CG  . TYR   A 52  ? 0.457 0.141 0.405 -0.073 0.012  0.032  51  TYR   AAA CG  
366  C  CD1 . TYR   A 52  ? 0.455 0.070 0.433 -0.071 0.001  -0.054 51  TYR   AAA CD1 
367  C  CD2 . TYR   A 52  ? 0.444 0.033 0.365 -0.071 -0.019 0.005  51  TYR   AAA CD2 
368  C  CE1 . TYR   A 52  ? 0.430 0.050 0.408 -0.057 0.024  -0.035 51  TYR   AAA CE1 
369  C  CE2 . TYR   A 52  ? 0.427 0.025 0.488 -0.068 0.026  0.057  51  TYR   AAA CE2 
370  C  CZ  . TYR   A 52  ? 0.406 0.052 0.412 -0.059 -0.008 -0.057 51  TYR   AAA CZ  
371  O  OH  . TYR   A 52  ? 0.439 0.009 0.381 0.031  0.019  -0.003 51  TYR   AAA OH  
372  N  N   . ASN   A 53  ? 0.563 0.027 0.490 -0.101 0.068  -0.045 52  ASN   AAA N   
373  C  CA  . ASN   A 53  ? 0.524 0.021 0.511 -0.083 0.030  -0.032 52  ASN   AAA CA  
374  C  C   . ASN   A 53  ? 0.522 0.189 0.362 -0.066 0.080  -0.072 52  ASN   AAA C   
375  O  O   . ASN   A 53  ? 0.605 0.062 0.398 0.013  0.043  -0.053 52  ASN   AAA O   
376  C  CB  . ASN   A 53  ? 0.615 0.009 0.598 -0.041 0.058  -0.011 52  ASN   AAA CB  
377  C  CG  . ASN   A 53  ? 0.694 0.007 0.564 0.013  0.025  0.014  52  ASN   AAA CG  
378  O  OD1 . ASN   A 53  ? 0.766 0.009 0.897 -0.029 0.034  0.039  52  ASN   AAA OD1 
379  N  ND2 . ASN   A 53  ? 0.617 0.085 0.543 0.019  -0.034 0.054  52  ASN   AAA ND2 
380  N  N   . PRO   A 54  ? 0.534 0.097 0.352 -0.071 0.062  -0.027 53  PRO   AAA N   
381  C  CA  . PRO   A 54  ? 0.550 0.119 0.407 -0.049 0.048  0.024  53  PRO   AAA CA  
382  C  C   . PRO   A 54  ? 0.476 0.078 0.383 -0.050 -0.036 -0.073 53  PRO   AAA C   
383  O  O   . PRO   A 54  ? 0.555 0.135 0.380 -0.063 -0.030 -0.042 53  PRO   AAA O   
384  C  CB  . PRO   A 54  ? 0.573 0.101 0.470 -0.001 0.096  -0.023 53  PRO   AAA CB  
385  C  CG  . PRO   A 54  ? 0.572 0.104 0.597 -0.103 0.021  0.092  53  PRO   AAA CG  
386  C  CD  . PRO   A 54  ? 0.557 0.039 0.463 -0.067 0.038  0.015  53  PRO   AAA CD  
387  N  N   . ALA   A 55  ? 0.534 0.109 0.407 -0.044 0.064  -0.051 54  ALA   AAA N   
388  C  CA  . ALA   A 55  ? 0.614 0.039 0.396 -0.059 0.005  -0.104 54  ALA   AAA CA  
389  C  C   . ALA   A 55  ? 0.624 0.245 0.382 -0.097 -0.012 0.033  54  ALA   AAA C   
390  O  O   . ALA   A 55  ? 0.563 0.183 0.435 -0.130 0.067  -0.029 54  ALA   AAA O   
391  C  CB  . ALA   A 55  ? 0.686 0.135 0.474 0.083  0.072  -0.099 54  ALA   AAA CB  
392  N  N   . THR   A 56  ? 0.491 0.220 0.424 -0.025 0.068  -0.032 55  THR   AAA N   
393  C  CA  . THR   A 56  ? 0.412 0.297 0.417 -0.014 0.036  0.018  55  THR   AAA CA  
394  C  C   . THR   A 56  ? 0.408 0.163 0.351 -0.017 0.070  -0.098 55  THR   AAA C   
395  O  O   . THR   A 56  ? 0.428 0.176 0.405 -0.028 0.029  0.003  55  THR   AAA O   
396  C  CB  . THR   A 56  ? 0.460 0.178 0.365 -0.029 0.043  0.011  55  THR   AAA CB  
397  O  OG1 . THR   A 56  ? 0.542 0.014 0.404 -0.064 0.041  -0.015 55  THR   AAA OG1 
398  C  CG2 . THR   A 56  ? 0.481 0.229 0.452 -0.024 0.040  0.062  55  THR   AAA CG2 
399  N  N   . ALA   A 57  ? 0.427 0.034 0.384 -0.032 0.023  -0.073 56  ALA   AAA N   
400  C  CA  . ALA   A 57  ? 0.446 0.162 0.340 0.010  0.012  -0.052 56  ALA   AAA CA  
401  C  C   . ALA   A 57  ? 0.467 0.071 0.349 0.007  0.015  -0.098 56  ALA   AAA C   
402  O  O   . ALA   A 57  ? 0.522 0.058 0.401 -0.034 0.019  -0.098 56  ALA   AAA O   
403  C  CB  . ALA   A 57  ? 0.525 0.057 0.415 -0.061 0.081  -0.069 56  ALA   AAA CB  
404  N  N   . LYS   A 58  ? 0.404 0.109 0.358 0.001  0.017  -0.037 57  LYS   AAA N   
405  C  CA  . LYS   A 58  ? 0.441 0.067 0.405 0.010  0.051  -0.090 57  LYS   AAA CA  
406  C  C   . LYS   A 58  ? 0.464 0.102 0.384 -0.013 0.051  -0.075 57  LYS   AAA C   
407  O  O   . LYS   A 58  ? 0.456 0.188 0.385 -0.025 0.027  -0.089 57  LYS   AAA O   
408  C  CB  . LYS   A 58  ? 0.458 0.153 0.486 -0.024 0.023  0.049  57  LYS   AAA CB  
409  C  CG  . LYS   A 58  ? 0.560 0.260 0.490 0.013  0.033  0.026  57  LYS   AAA CG  
410  C  CD  . LYS   A 58  ? 0.594 0.484 0.637 -0.011 0.049  0.056  57  LYS   AAA CD  
411  C  CE  . LYS   A 58  ? 0.691 0.615 0.512 -0.205 0.068  0.050  57  LYS   AAA CE  
412  N  NZ  . LYS   A 58  ? 0.707 0.827 0.564 -0.252 0.056  -0.188 57  LYS   AAA NZ  
413  N  N   . GLU   A 59  ? 0.431 0.101 0.352 -0.020 0.026  -0.089 58  GLU   AAA N   
414  C  CA  . GLU   A 59  ? 0.379 0.159 0.392 -0.018 0.002  -0.134 58  GLU   AAA CA  
415  C  C   . GLU   A 59  ? 0.388 0.126 0.287 -0.001 0.002  -0.062 58  GLU   AAA C   
416  O  O   . GLU   A 59  ? 0.447 0.065 0.339 -0.036 -0.032 -0.040 58  GLU   AAA O   
417  C  CB  . GLU   A 59  ? 0.375 0.164 0.422 -0.008 0.036  -0.141 58  GLU   AAA CB  
418  C  CG  . GLU   A 59  ? 0.379 0.319 0.454 -0.104 0.036  -0.068 58  GLU   AAA CG  
419  C  CD  . GLU   A 59  ? 0.443 0.348 0.409 -0.026 0.053  -0.081 58  GLU   AAA CD  
420  O  OE1 . GLU   A 59  ? 0.584 0.076 0.419 0.008  0.088  -0.058 58  GLU   AAA OE1 
421  O  OE2 . GLU   A 59  ? 0.598 0.316 0.465 -0.100 0.029  -0.069 58  GLU   AAA OE2 
422  N  N   . ILE   A 60  ? 0.368 0.160 0.366 0.027  0.026  -0.056 59  ILE   AAA N   
423  C  CA  . ILE   A 60  ? 0.361 0.128 0.356 -0.007 -0.009 -0.119 59  ILE   AAA CA  
424  C  C   . ILE   A 60  ? 0.380 0.186 0.359 -0.052 -0.033 -0.061 59  ILE   AAA C   
425  O  O   . ILE   A 60  ? 0.435 0.149 0.370 -0.026 -0.000 -0.057 59  ILE   AAA O   
426  C  CB  . ILE   A 60  ? 0.381 0.192 0.377 0.026  0.020  -0.129 59  ILE   AAA CB  
427  C  CG1 . ILE   A 60  ? 0.359 0.201 0.377 0.076  0.016  -0.090 59  ILE   AAA CG1 
428  C  CG2 . ILE   A 60  ? 0.353 0.213 0.407 -0.027 0.010  -0.065 59  ILE   AAA CG2 
429  C  CD1 . ILE   A 60  ? 0.427 0.091 0.418 0.021  0.020  -0.074 59  ILE   AAA CD1 
430  N  N   . ILE   A 61  ? 0.385 0.170 0.329 0.007  0.028  -0.105 60  ILE   AAA N   
431  C  CA  . ILE   A 61  ? 0.349 0.213 0.327 0.060  0.010  -0.030 60  ILE   AAA CA  
432  C  C   . ILE   A 61  ? 0.303 0.282 0.309 0.083  -0.008 -0.107 60  ILE   AAA C   
433  O  O   . ILE   A 61  ? 0.383 0.268 0.314 -0.002 0.035  -0.088 60  ILE   AAA O   
434  C  CB  . ILE   A 61  ? 0.336 0.160 0.415 0.106  0.017  -0.048 60  ILE   AAA CB  
435  C  CG1 . ILE   A 61  ? 0.428 0.399 0.391 0.087  0.031  -0.065 60  ILE   AAA CG1 
436  C  CG2 . ILE   A 61  ? 0.450 0.058 0.441 0.073  0.046  0.063  60  ILE   AAA CG2 
437  C  CD1 . ILE   A 61  ? 0.447 0.526 0.577 0.020  0.012  -0.110 60  ILE   AAA CD1 
438  N  N   . ASN   A 62  ? 0.374 0.218 0.366 -0.015 -0.039 -0.068 61  ASN   AAA N   
439  C  CA  . ASN   A 62  ? 0.361 0.239 0.329 0.028  0.022  -0.045 61  ASN   AAA CA  
440  C  C   . ASN   A 62  ? 0.351 0.318 0.323 -0.013 0.012  -0.064 61  ASN   AAA C   
441  O  O   . ASN   A 62  ? 0.360 0.194 0.362 0.016  0.060  -0.031 61  ASN   AAA O   
442  C  CB  . ASN   A 62  ? 0.388 0.236 0.368 -0.067 0.018  -0.082 61  ASN   AAA CB  
443  C  CG  . ASN   A 62  ? 0.316 0.307 0.367 -0.013 0.010  -0.014 61  ASN   AAA CG  
444  O  OD1 . ASN   A 62  ? 0.435 0.194 0.382 -0.013 0.023  -0.061 61  ASN   AAA OD1 
445  N  ND2 . ASN   A 62  ? 0.330 0.405 0.367 0.015  0.006  -0.027 61  ASN   AAA ND2 
446  N  N   . VAL   A 63  ? 0.380 0.292 0.380 0.003  -0.061 -0.038 62  VAL   AAA N   
447  C  CA  . VAL   A 63  ? 0.411 0.249 0.415 -0.003 -0.003 -0.029 62  VAL   AAA CA  
448  C  C   . VAL   A 63  ? 0.326 0.248 0.360 0.004  0.032  -0.040 62  VAL   AAA C   
449  O  O   . VAL   A 63  ? 0.471 0.235 0.466 -0.058 0.069  -0.025 62  VAL   AAA O   
450  C  CB  . VAL   A 63  ? 0.428 0.075 0.467 -0.021 -0.014 -0.002 62  VAL   AAA CB  
451  C  CG1 . VAL   A 63  ? 0.431 0.139 0.536 0.067  -0.014 -0.110 62  VAL   AAA CG1 
452  C  CG2 . VAL   A 63  ? 0.420 0.270 0.389 -0.018 -0.033 0.040  62  VAL   AAA CG2 
453  N  N   . GLY   A 64  ? 0.368 0.317 0.411 0.001  0.031  -0.005 63  GLY   AAA N   
454  C  CA  . GLY   A 64  ? 0.430 0.411 0.418 0.061  -0.002 0.041  63  GLY   AAA CA  
455  C  C   . GLY   A 64  ? 0.416 0.336 0.400 0.029  -0.012 0.053  63  GLY   AAA C   
456  O  O   . GLY   A 64  ? 0.486 0.445 0.436 0.109  0.010  -0.062 63  GLY   AAA O   
457  N  N   . HIS   A 65  ? 0.385 0.216 0.415 0.056  0.005  -0.023 64  HIS   AAA N   
458  C  CA  . HIS   A 65  ? 0.434 0.306 0.374 0.069  0.011  -0.020 64  HIS   AAA CA  
459  C  C   . HIS   A 65  ? 0.451 0.126 0.409 0.147  0.022  -0.051 64  HIS   AAA C   
460  O  O   . HIS   A 65  ? 0.454 0.224 0.335 0.067  0.036  -0.008 64  HIS   AAA O   
461  C  CB  . HIS   A 65  ? 0.471 0.247 0.431 0.009  0.014  -0.001 64  HIS   AAA CB  
462  C  CG  . HIS   A 65  ? 0.466 0.166 0.380 -0.040 0.007  0.001  64  HIS   AAA CG  
463  N  ND1 . HIS   A 65  ? 0.492 0.186 0.508 -0.020 0.019  -0.022 64  HIS   AAA ND1 
464  C  CD2 . HIS   A 65  ? 0.479 0.276 0.289 -0.036 0.083  -0.025 64  HIS   AAA CD2 
465  C  CE1 . HIS   A 65  ? 0.386 0.257 0.430 0.035  0.028  -0.103 64  HIS   AAA CE1 
466  N  NE2 . HIS   A 65  ? 0.490 0.280 0.484 -0.099 0.086  -0.198 64  HIS   AAA NE2 
467  N  N   . SER   A 66  ? 0.356 0.107 0.345 0.077  0.002  -0.036 65  SER   AAA N   
468  C  CA  . SER   A 66  ? 0.349 0.138 0.298 0.037  0.002  -0.050 65  SER   AAA CA  
469  C  C   . SER   A 66  ? 0.377 0.109 0.318 -0.006 0.004  -0.018 65  SER   AAA C   
470  O  O   . SER   A 66  ? 0.410 0.117 0.353 0.030  0.003  -0.019 65  SER   AAA O   
471  C  CB  . SER   A 66  ? 0.419 0.111 0.324 0.016  -0.029 -0.034 65  SER   AAA CB  
472  O  OG  . SER   A 66  ? 0.457 0.093 0.351 -0.006 -0.038 -0.049 65  SER   AAA OG  
473  N  N   . PHE   A 67  ? 0.412 0.134 0.305 0.054  0.024  0.000  66  PHE   AAA N   
474  C  CA  . PHE   A 67  ? 0.366 0.191 0.294 0.042  0.012  -0.088 66  PHE   AAA CA  
475  C  C   . PHE   A 67  ? 0.336 0.157 0.282 -0.031 0.021  -0.017 66  PHE   AAA C   
476  O  O   . PHE   A 67  ? 0.377 0.220 0.309 0.019  0.015  -0.042 66  PHE   AAA O   
477  C  CB  . PHE   A 67  ? 0.380 0.218 0.318 0.043  -0.021 -0.050 66  PHE   AAA CB  
478  C  CG  . PHE   A 67  ? 0.362 0.166 0.333 0.019  -0.009 0.001  66  PHE   AAA CG  
479  C  CD1 . PHE   A 67  ? 0.418 0.352 0.301 0.047  -0.009 -0.106 66  PHE   AAA CD1 
480  C  CD2 . PHE   A 67  ? 0.472 0.179 0.344 0.036  -0.017 0.002  66  PHE   AAA CD2 
481  C  CE1 . PHE   A 67  ? 0.394 0.236 0.331 0.037  -0.020 -0.078 66  PHE   AAA CE1 
482  C  CE2 . PHE   A 67  ? 0.448 0.146 0.381 -0.033 0.026  -0.050 66  PHE   AAA CE2 
483  C  CZ  . PHE   A 67  ? 0.356 0.251 0.347 -0.027 -0.035 -0.059 66  PHE   AAA CZ  
484  N  N   . HIS   A 68  ? 0.360 0.082 0.350 -0.055 0.004  -0.026 67  HIS   AAA N   
485  C  CA  . HIS   A 68  ? 0.341 0.067 0.380 -0.029 -0.033 -0.083 67  HIS   AAA CA  
486  C  C   . HIS   A 68  ? 0.347 0.088 0.353 -0.099 -0.026 0.004  67  HIS   AAA C   
487  O  O   . HIS   A 68  ? 0.422 0.120 0.388 -0.000 -0.004 -0.050 67  HIS   AAA O   
488  C  CB  . HIS   A 68  ? 0.412 0.046 0.351 -0.066 -0.006 -0.009 67  HIS   AAA CB  
489  C  CG  . HIS   A 68  ? 0.419 0.069 0.373 -0.110 0.004  -0.044 67  HIS   AAA CG  
490  N  ND1 . HIS   A 68  ? 0.473 0.174 0.403 -0.098 0.017  -0.021 67  HIS   AAA ND1 
491  C  CD2 . HIS   A 68  ? 0.358 0.131 0.483 -0.041 0.021  -0.002 67  HIS   AAA CD2 
492  C  CE1 . HIS   A 68  ? 0.477 0.200 0.434 -0.060 0.014  -0.040 67  HIS   AAA CE1 
493  N  NE2 . HIS   A 68  ? 0.420 0.097 0.470 -0.040 0.033  0.075  67  HIS   AAA NE2 
494  N  N   . VAL   A 69  ? 0.409 0.017 0.301 0.029  -0.034 -0.053 68  VAL   AAA N   
495  C  CA  . VAL   A 69  ? 0.394 0.016 0.331 -0.010 0.002  -0.056 68  VAL   AAA CA  
496  C  C   . VAL   A 69  ? 0.417 0.109 0.278 -0.022 -0.011 -0.035 68  VAL   AAA C   
497  O  O   . VAL   A 69  ? 0.407 0.107 0.301 0.001  -0.013 -0.060 68  VAL   AAA O   
498  C  CB  . VAL   A 69  ? 0.368 0.028 0.368 -0.068 -0.019 -0.052 68  VAL   AAA CB  
499  C  CG1 . VAL   A 69  ? 0.433 0.029 0.459 -0.063 -0.033 -0.074 68  VAL   AAA CG1 
500  C  CG2 . VAL   A 69  ? 0.407 0.225 0.365 -0.039 -0.008 0.014  68  VAL   AAA CG2 
501  N  N   . ASN   A 70  ? 0.396 0.108 0.328 -0.078 0.020  -0.064 69  ASN   AAA N   
502  C  CA  . ASN   A 70  ? 0.396 0.016 0.348 -0.015 0.014  -0.057 69  ASN   AAA CA  
503  C  C   . ASN   A 70  ? 0.324 0.010 0.436 0.036  0.011  0.001  69  ASN   AAA C   
504  O  O   . ASN   A 70  ? 0.382 0.101 0.375 -0.042 0.025  -0.043 69  ASN   AAA O   
505  C  CB  . ASN   A 70  ? 0.415 0.128 0.379 -0.029 0.019  -0.064 69  ASN   AAA CB  
506  C  CG  . ASN   A 70  ? 0.424 0.160 0.329 -0.036 0.022  -0.006 69  ASN   AAA CG  
507  O  OD1 . ASN   A 70  ? 0.428 0.235 0.453 -0.057 0.020  -0.094 69  ASN   AAA OD1 
508  N  ND2 . ASN   A 70  ? 0.520 0.021 0.333 -0.080 0.022  -0.033 69  ASN   AAA ND2 
509  N  N   . PHE   A 71  ? 0.392 0.051 0.389 0.069  0.000  -0.025 70  PHE   AAA N   
510  C  CA  . PHE   A 71  ? 0.418 0.012 0.407 0.038  -0.002 -0.032 70  PHE   AAA CA  
511  C  C   . PHE   A 71  ? 0.387 0.009 0.443 -0.003 0.027  -0.036 70  PHE   AAA C   
512  O  O   . PHE   A 71  ? 0.421 0.085 0.410 -0.065 0.039  -0.022 70  PHE   AAA O   
513  C  CB  . PHE   A 71  ? 0.442 0.013 0.412 -0.042 0.017  -0.035 70  PHE   AAA CB  
514  C  CG  . PHE   A 71  ? 0.401 0.084 0.378 -0.032 0.032  -0.011 70  PHE   AAA CG  
515  C  CD1 . PHE   A 71  ? 0.443 0.151 0.391 0.043  0.055  -0.090 70  PHE   AAA CD1 
516  C  CD2 . PHE   A 71  ? 0.412 0.025 0.409 0.019  0.038  -0.081 70  PHE   AAA CD2 
517  C  CE1 . PHE   A 71  ? 0.447 0.186 0.321 -0.003 0.039  -0.014 70  PHE   AAA CE1 
518  C  CE2 . PHE   A 71  ? 0.407 0.023 0.412 0.017  0.026  -0.079 70  PHE   AAA CE2 
519  C  CZ  . PHE   A 71  ? 0.377 0.075 0.391 0.090  0.050  -0.033 70  PHE   AAA CZ  
520  N  N   . GLU   A 72  ? 0.445 0.028 0.407 -0.030 0.008  -0.089 71  GLU   AAA N   
521  C  CA  . GLU   A 72  ? 0.441 0.032 0.488 -0.029 0.004  0.008  71  GLU   AAA CA  
522  C  C   . GLU   A 72  ? 0.459 0.031 0.523 0.044  0.019  -0.100 71  GLU   AAA C   
523  O  O   . GLU   A 72  ? 0.658 0.016 0.574 0.008  0.044  -0.073 71  GLU   AAA O   
524  C  CB  . GLU   A 72  ? 0.549 0.047 0.503 -0.000 0.001  -0.065 71  GLU   AAA CB  
525  C  CG  . GLU   A 72  ? 0.593 0.023 0.486 -0.006 -0.040 0.043  71  GLU   AAA CG  
526  C  CD  . GLU   A 72  ? 0.673 0.066 0.658 0.024  -0.108 -0.114 71  GLU   AAA CD  
527  O  OE1 . GLU   A 72  ? 0.734 0.087 0.622 -0.011 -0.025 -0.012 71  GLU   AAA OE1 
528  O  OE2 . GLU   A 72  ? 0.665 0.115 0.841 -0.028 -0.092 -0.246 71  GLU   AAA OE2 
529  N  N   . ASP   A 73  ? 0.457 0.124 0.458 0.047  -0.002 -0.062 72  ASP   AAA N   
530  C  CA  . ASP   A 73  ? 0.451 0.016 0.451 0.044  -0.029 0.010  72  ASP   AAA CA  
531  C  C   . ASP   A 73  ? 0.483 0.111 0.538 0.041  0.011  -0.159 72  ASP   AAA C   
532  O  O   . ASP   A 73  ? 0.473 0.151 0.516 0.002  0.093  -0.029 72  ASP   AAA O   
533  C  CB  . ASP   A 73  ? 0.542 0.022 0.462 0.092  -0.028 0.004  72  ASP   AAA CB  
534  C  CG  . ASP   A 73  ? 0.622 0.153 0.374 -0.019 -0.029 -0.068 72  ASP   AAA CG  
535  O  OD1 . ASP   A 73  ? 0.584 0.057 0.427 0.037  0.003  -0.086 72  ASP   AAA OD1 
536  O  OD2 . ASP   A 73  ? 0.508 0.109 0.554 0.044  -0.019 -0.081 72  ASP   AAA OD2 
537  N  N   . ASN   A 74  ? 0.496 0.080 0.578 0.054  0.037  -0.115 73  ASN   AAA N   
538  C  CA  . ASN   A 74  ? 0.459 0.308 0.513 0.059  0.035  -0.141 73  ASN   AAA CA  
539  C  C   . ASN   A 74  ? 0.464 0.184 0.486 0.037  0.063  -0.100 73  ASN   AAA C   
540  O  O   . ASN   A 74  ? 0.466 0.327 0.622 0.043  -0.009 0.021  73  ASN   AAA O   
541  C  CB  . ASN   A 74  ? 0.520 0.243 0.589 0.054  0.037  -0.165 73  ASN   AAA CB  
542  C  CG  . ASN   A 74  ? 0.498 0.436 0.785 -0.012 0.024  -0.157 73  ASN   AAA CG  
543  O  OD1 . ASN   A 74  ? 0.782 0.619 0.991 0.160  0.053  -0.023 73  ASN   AAA OD1 
544  N  ND2 . ASN   A 74  ? 0.510 0.018 0.736 -0.038 0.060  -0.083 73  ASN   AAA ND2 
545  N  N   . ASP   A 75  ? 0.519 0.027 0.560 0.092  0.100  -0.032 74  ASP   AAA N   
546  C  CA  . ASP   A 75  ? 0.531 0.057 0.584 0.044  0.045  -0.058 74  ASP   AAA CA  
547  C  C   . ASP   A 75  ? 0.611 0.197 0.476 0.092  -0.013 -0.058 74  ASP   AAA C   
548  O  O   . ASP   A 75  ? 0.580 0.046 0.623 -0.031 -0.029 -0.052 74  ASP   AAA O   
549  C  CB  . ASP   A 75  ? 0.613 0.061 0.588 -0.030 0.067  -0.067 74  ASP   AAA CB  
550  C  CG  . ASP   A 75  ? 0.651 0.151 0.710 -0.024 0.044  -0.117 74  ASP   AAA CG  
551  O  OD1 . ASP   A 75  ? 0.629 0.041 0.612 -0.092 0.022  -0.058 74  ASP   AAA OD1 
552  O  OD2 . ASP   A 75  ? 0.655 0.129 0.685 0.093  0.049  -0.111 74  ASP   AAA OD2 
553  N  N   . ASN   A 76  ? 0.602 0.145 0.557 0.119  -0.046 -0.034 75  ASN   AAA N   
554  C  CA  . ASN   A 76  ? 0.555 0.292 0.569 0.047  0.012  -0.075 75  ASN   AAA CA  
555  C  C   . ASN   A 76  ? 0.626 0.040 0.518 0.128  -0.040 0.009  75  ASN   AAA C   
556  O  O   . ASN   A 76  ? 0.633 0.107 0.501 0.141  0.032  0.006  75  ASN   AAA O   
557  C  CB  . ASN   A 76  ? 0.530 0.180 0.578 0.186  0.017  -0.082 75  ASN   AAA CB  
558  C  CG  . ASN   A 76  ? 0.581 0.371 0.547 -0.082 -0.049 0.049  75  ASN   AAA CG  
559  O  OD1 . ASN   A 76  ? 0.666 0.199 0.505 0.014  0.028  -0.054 75  ASN   AAA OD1 
560  N  ND2 . ASN   A 76  ? 0.675 0.640 0.705 -0.085 -0.190 0.050  75  ASN   AAA ND2 
561  N  N   . ARG   A 77  ? 0.574 0.188 0.567 0.111  -0.016 -0.028 76  ARG   AAA N   
562  C  CA  . ARG   A 77  ? 0.569 0.022 0.592 0.057  -0.047 -0.079 76  ARG   AAA CA  
563  C  C   . ARG   A 77  ? 0.517 0.188 0.473 0.016  0.052  -0.047 76  ARG   AAA C   
564  O  O   . ARG   A 77  ? 0.635 0.071 0.459 0.007  0.022  0.017  76  ARG   AAA O   
565  C  CB  . ARG   A 77  ? 0.519 0.190 0.525 0.120  -0.032 -0.146 76  ARG   AAA CB  
566  C  CG  . ARG   A 77  ? 0.587 0.042 0.526 0.040  0.024  -0.040 76  ARG   AAA CG  
567  C  CD  . ARG   A 77  ? 0.615 0.121 0.471 0.005  0.079  0.032  76  ARG   AAA CD  
568  N  NE  . ARG   A 77  ? 0.714 0.013 0.593 0.049  -0.015 -0.047 76  ARG   AAA NE  
569  C  CZ  . ARG   A 77  ? 0.594 0.199 0.514 0.014  0.051  -0.125 76  ARG   AAA CZ  
570  N  NH1 . ARG   A 77  ? 0.599 0.181 0.496 -0.016 0.028  -0.003 76  ARG   AAA NH1 
571  N  NH2 . ARG   A 77  ? 0.642 0.246 0.482 0.012  0.013  -0.131 76  ARG   AAA NH2 
572  N  N   . SER   A 78  ? 0.449 0.176 0.491 0.043  -0.015 -0.008 77  SER   AAA N   
573  C  CA  . SER   A 78  ? 0.423 0.283 0.395 -0.031 0.012  -0.070 77  SER   AAA CA  
574  C  C   . SER   A 78  ? 0.431 0.200 0.384 0.007  0.039  -0.053 77  SER   AAA C   
575  O  O   . SER   A 78  ? 0.457 0.083 0.421 0.039  0.023  -0.007 77  SER   AAA O   
576  C  CB  . SER   A 78  ? 0.447 0.126 0.432 -0.042 -0.008 -0.046 77  SER   AAA CB  
577  O  OG  . SER   A 78  ? 0.451 0.090 0.494 -0.019 -0.015 -0.020 77  SER   AAA OG  
578  N  N   . VAL   A 79  ? 0.422 0.129 0.378 0.049  0.006  -0.006 78  VAL   AAA N   
579  C  CA  . VAL   A 79  ? 0.425 0.201 0.473 0.014  -0.019 -0.052 78  VAL   AAA CA  
580  C  C   . VAL   A 79  ? 0.412 0.260 0.394 -0.054 0.027  0.049  78  VAL   AAA C   
581  O  O   . VAL   A 79  ? 0.474 0.121 0.453 -0.078 0.058  -0.024 78  VAL   AAA O   
582  C  CB  . VAL   A 79  ? 0.457 0.247 0.493 -0.006 -0.048 -0.057 78  VAL   AAA CB  
583  C  CG1 . VAL   A 79  ? 0.551 0.344 0.477 0.044  -0.079 -0.077 78  VAL   AAA CG1 
584  C  CG2 . VAL   A 79  ? 0.561 0.377 0.460 0.026  -0.092 0.007  78  VAL   AAA CG2 
585  N  N   . LEU   A 80  ? 0.483 0.193 0.398 0.029  0.019  -0.018 79  LEU   AAA N   
586  C  CA  . LEU   A 80  ? 0.422 0.055 0.402 0.129  0.033  0.032  79  LEU   AAA CA  
587  C  C   . LEU   A 80  ? 0.427 0.080 0.414 0.129  0.015  0.032  79  LEU   AAA C   
588  O  O   . LEU   A 80  ? 0.468 0.153 0.449 0.004  0.003  0.014  79  LEU   AAA O   
589  C  CB  . LEU   A 80  ? 0.502 0.009 0.410 0.033  0.017  -0.005 79  LEU   AAA CB  
590  C  CG  . LEU   A 80  ? 0.579 0.156 0.369 0.017  -0.033 -0.071 79  LEU   AAA CG  
591  C  CD1 . LEU   A 80  ? 0.538 0.108 0.447 0.032  -0.003 -0.133 79  LEU   AAA CD1 
592  C  CD2 . LEU   A 80  ? 0.525 0.171 0.474 -0.024 0.038  0.047  79  LEU   AAA CD2 
593  N  N   . LYS   A 81  ? 0.535 0.130 0.392 0.103  0.017  -0.075 80  LYS   AAA N   
594  C  CA  . LYS   A 81  ? 0.613 0.229 0.447 0.050  -0.083 -0.082 80  LYS   AAA CA  
595  C  C   . LYS   A 81  ? 0.520 0.364 0.466 0.016  -0.037 -0.059 80  LYS   AAA C   
596  O  O   . LYS   A 81  ? 0.493 0.471 0.407 -0.084 0.013  -0.047 80  LYS   AAA O   
597  C  CB  . LYS   A 81  ? 0.586 0.376 0.605 0.195  -0.073 -0.110 80  LYS   AAA CB  
598  C  CG  . LYS   A 81  ? 0.642 0.277 0.651 0.151  -0.097 -0.064 80  LYS   AAA CG  
599  C  CD  . LYS   A 81  ? 0.856 0.314 0.929 0.216  0.044  0.073  80  LYS   AAA CD  
600  C  CE  . LYS   A 81  ? 0.919 0.246 1.190 0.200  0.050  0.135  80  LYS   AAA CE  
601  N  NZ  . LYS   A 81  ? 1.241 0.278 1.522 -0.037 0.040  0.301  80  LYS   AAA NZ  
602  N  N   . GLY   A 82  ? 0.512 0.431 0.446 0.109  -0.065 -0.029 81  GLY   AAA N   
603  C  CA  . GLY   A 82  ? 0.542 0.473 0.444 0.103  -0.089 -0.032 81  GLY   AAA CA  
604  C  C   . GLY   A 82  ? 0.402 0.368 0.424 0.020  -0.015 -0.042 81  GLY   AAA C   
605  O  O   . GLY   A 82  ? 0.471 0.294 0.445 0.020  -0.032 -0.038 81  GLY   AAA O   
606  N  N   . GLY   A 83  ? 0.484 0.366 0.460 0.069  -0.028 -0.059 82  GLY   AAA N   
607  C  CA  . GLY   A 83  ? 0.509 0.341 0.415 0.005  -0.017 -0.005 82  GLY   AAA CA  
608  C  C   . GLY   A 83  ? 0.463 0.467 0.405 -0.021 -0.014 0.016  82  GLY   AAA C   
609  O  O   . GLY   A 83  ? 0.530 0.444 0.535 0.016  -0.096 -0.062 82  GLY   AAA O   
610  N  N   . PRO   A 84  ? 0.465 0.247 0.438 0.072  -0.036 -0.053 83  PRO   AAA N   
611  C  CA  . PRO   A 84  ? 0.502 0.361 0.460 0.029  -0.040 -0.000 83  PRO   AAA CA  
612  C  C   . PRO   A 84  ? 0.445 0.388 0.485 -0.034 -0.051 -0.001 83  PRO   AAA C   
613  O  O   . PRO   A 84  ? 0.475 0.449 0.573 -0.033 -0.042 -0.129 83  PRO   AAA O   
614  C  CB  . PRO   A 84  ? 0.520 0.360 0.401 0.031  -0.039 -0.019 83  PRO   AAA CB  
615  C  CG  . PRO   A 84  ? 0.456 0.378 0.470 -0.042 -0.022 -0.052 83  PRO   AAA CG  
616  C  CD  . PRO   A 84  ? 0.446 0.360 0.435 -0.027 -0.057 -0.065 83  PRO   AAA CD  
617  N  N   . PHE   A 85  ? 0.520 0.448 0.417 0.038  -0.033 -0.069 84  PHE   AAA N   
618  C  CA  . PHE   A 85  ? 0.554 0.418 0.419 0.051  -0.042 -0.066 84  PHE   AAA CA  
619  C  C   . PHE   A 85  ? 0.529 0.571 0.374 0.041  -0.075 0.018  84  PHE   AAA C   
620  O  O   . PHE   A 85  ? 0.557 0.482 0.485 0.111  -0.072 0.103  84  PHE   AAA O   
621  C  CB  . PHE   A 85  ? 0.507 0.332 0.497 0.096  -0.048 -0.119 84  PHE   AAA CB  
622  C  CG  . PHE   A 85  ? 0.541 0.330 0.525 0.091  -0.021 -0.027 84  PHE   AAA CG  
623  C  CD1 . PHE   A 85  ? 0.465 0.481 0.477 -0.011 0.005  -0.031 84  PHE   AAA CD1 
624  C  CD2 . PHE   A 85  ? 0.577 0.405 0.448 0.013  -0.062 -0.033 84  PHE   AAA CD2 
625  C  CE1 . PHE   A 85  ? 0.594 0.389 0.540 0.061  -0.034 -0.131 84  PHE   AAA CE1 
626  C  CE2 . PHE   A 85  ? 0.574 0.461 0.526 0.066  -0.097 -0.056 84  PHE   AAA CE2 
627  C  CZ  . PHE   A 85  ? 0.573 0.491 0.477 0.088  -0.024 -0.092 84  PHE   AAA CZ  
628  N  N   . SER   A 86  ? 0.476 0.543 0.541 0.147  -0.082 -0.181 85  SER   AAA N   
629  C  CA  . SER   A 86  ? 0.470 0.557 0.597 0.117  -0.059 -0.084 85  SER   AAA CA  
630  C  C   . SER   A 86  ? 0.570 0.335 0.622 0.049  -0.131 -0.036 85  SER   AAA C   
631  O  O   . SER   A 86  ? 0.598 0.396 0.602 0.094  -0.001 0.113  85  SER   AAA O   
632  C  CB  . SER   A 86  ? 0.556 0.642 0.829 -0.016 -0.110 -0.193 85  SER   AAA CB  
633  O  OG  . SER   A 86  ? 0.635 0.926 0.961 -0.117 -0.071 -0.309 85  SER   AAA OG  
634  N  N   . ASP   A 87  ? 0.513 0.258 0.567 0.073  -0.047 -0.096 86  ASP   AAA N   
635  C  CA  . ASP   A 87  ? 0.498 0.545 0.584 -0.001 0.062  -0.169 86  ASP   AAA CA  
636  C  C   . ASP   A 87  ? 0.462 0.316 0.509 0.053  0.057  -0.097 86  ASP   AAA C   
637  O  O   . ASP   A 87  ? 0.408 0.531 0.511 0.066  0.060  -0.018 86  ASP   AAA O   
638  C  CB  . ASP   A 87  ? 0.467 0.578 0.646 0.011  0.090  -0.153 86  ASP   AAA CB  
639  C  CG  . ASP   A 87  ? 0.500 0.420 0.643 -0.018 0.029  -0.029 86  ASP   AAA CG  
640  O  OD1 . ASP   A 87  ? 0.541 0.550 1.018 0.167  -0.019 -0.134 86  ASP   AAA OD1 
641  O  OD2 . ASP   A 87  ? 0.694 0.351 0.637 0.032  -0.038 -0.063 86  ASP   AAA OD2 
642  N  N   . SER   A 88  ? 0.529 0.358 0.440 -0.018 -0.037 -0.076 87  SER   AAA N   
643  C  CA  . SER   A 88  ? 0.452 0.290 0.557 0.094  -0.046 0.006  87  SER   AAA CA  
644  C  C   . SER   A 88  ? 0.385 0.115 0.540 0.020  0.036  -0.002 87  SER   AAA C   
645  O  O   . SER   A 88  ? 0.442 0.294 0.501 0.028  0.037  0.011  87  SER   AAA O   
646  C  CB  . SER   A 88  ? 0.480 0.279 0.718 0.109  -0.151 -0.063 87  SER   AAA CB  
647  O  OG  . SER   A 88  ? 0.469 0.382 0.688 0.058  -0.048 0.071  87  SER   AAA OG  
648  N  N   . TYR   A 89  ? 0.392 0.168 0.392 0.016  -0.023 -0.032 88  TYR   AAA N   
649  C  CA  . TYR   A 89  ? 0.363 0.174 0.407 0.042  -0.000 0.003  88  TYR   AAA CA  
650  C  C   . TYR   A 89  ? 0.348 0.200 0.348 0.049  0.017  0.020  88  TYR   AAA C   
651  O  O   . TYR   A 89  ? 0.469 0.063 0.443 -0.016 0.008  -0.038 88  TYR   AAA O   
652  C  CB  . TYR   A 89  ? 0.385 0.120 0.415 0.032  -0.061 -0.013 88  TYR   AAA CB  
653  C  CG  . TYR   A 89  ? 0.415 0.163 0.394 -0.016 -0.014 -0.031 88  TYR   AAA CG  
654  C  CD1 . TYR   A 89  ? 0.448 0.137 0.416 0.013  -0.024 -0.058 88  TYR   AAA CD1 
655  C  CD2 . TYR   A 89  ? 0.385 0.228 0.370 0.013  -0.046 -0.009 88  TYR   AAA CD2 
656  C  CE1 . TYR   A 89  ? 0.458 0.291 0.441 -0.055 -0.012 -0.040 88  TYR   AAA CE1 
657  C  CE2 . TYR   A 89  ? 0.456 0.111 0.520 0.060  -0.052 -0.061 88  TYR   AAA CE2 
658  C  CZ  . TYR   A 89  ? 0.426 0.205 0.439 0.004  0.003  -0.078 88  TYR   AAA CZ  
659  O  OH  . TYR   A 89  ? 0.445 0.241 0.464 -0.018 -0.018 -0.116 88  TYR   AAA OH  
660  N  N   . ARG   A 90  ? 0.396 0.145 0.355 -0.005 0.005  0.015  89  ARG   AAA N   
661  C  CA  . ARG   A 90  ? 0.396 0.175 0.371 -0.005 0.011  -0.046 89  ARG   AAA CA  
662  C  C   . ARG   A 90  ? 0.396 0.122 0.320 -0.026 0.041  0.014  89  ARG   AAA C   
663  O  O   . ARG   A 90  ? 0.441 0.049 0.387 0.022  -0.016 -0.002 89  ARG   AAA O   
664  C  CB  . ARG   A 90  ? 0.393 0.174 0.417 -0.058 0.031  -0.036 89  ARG   AAA CB  
665  C  CG  . ARG   A 90  ? 0.431 0.086 0.465 0.016  0.010  -0.060 89  ARG   AAA CG  
666  C  CD  . ARG   A 90  ? 0.506 0.115 0.481 0.062  0.065  -0.017 89  ARG   AAA CD  
667  N  NE  . ARG   A 90  ? 0.464 0.157 0.557 0.000  0.004  -0.055 89  ARG   AAA NE  
668  C  CZ  . ARG   A 90  ? 0.533 0.007 0.563 0.010  0.002  -0.011 89  ARG   AAA CZ  
669  N  NH1 . ARG   A 90  ? 0.532 0.009 0.520 -0.017 0.061  -0.011 89  ARG   AAA NH1 
670  N  NH2 . ARG   A 90  ? 0.537 0.168 0.697 0.095  -0.038 -0.011 89  ARG   AAA NH2 
671  N  N   . LEU   A 91  ? 0.392 0.008 0.398 -0.008 0.036  -0.027 90  LEU   AAA N   
672  C  CA  . LEU   A 91  ? 0.352 0.111 0.355 -0.001 0.038  -0.060 90  LEU   AAA CA  
673  C  C   . LEU   A 91  ? 0.323 0.131 0.344 0.044  0.045  -0.036 90  LEU   AAA C   
674  O  O   . LEU   A 91  ? 0.473 0.129 0.326 0.091  0.054  -0.038 90  LEU   AAA O   
675  C  CB  . LEU   A 91  ? 0.376 0.017 0.369 0.035  0.037  -0.049 90  LEU   AAA CB  
676  C  CG  . LEU   A 91  ? 0.339 0.138 0.349 0.010  0.059  -0.030 90  LEU   AAA CG  
677  C  CD1 . LEU   A 91  ? 0.368 0.163 0.341 0.092  0.021  0.001  90  LEU   AAA CD1 
678  C  CD2 . LEU   A 91  ? 0.358 0.159 0.388 0.001  0.038  -0.011 90  LEU   AAA CD2 
679  N  N   . PHE   A 92  ? 0.389 0.081 0.365 0.042  0.015  -0.052 91  PHE   AAA N   
680  C  CA  . PHE   A 92  ? 0.397 0.080 0.358 0.032  0.050  -0.062 91  PHE   AAA CA  
681  C  C   . PHE   A 92  ? 0.409 0.038 0.299 0.020  0.037  -0.012 91  PHE   AAA C   
682  O  O   . PHE   A 92  ? 0.455 0.018 0.364 0.004  0.007  -0.065 91  PHE   AAA O   
683  C  CB  . PHE   A 92  ? 0.378 0.021 0.362 0.005  0.014  -0.073 91  PHE   AAA CB  
684  C  CG  . PHE   A 92  ? 0.424 0.015 0.365 0.010  0.023  -0.053 91  PHE   AAA CG  
685  C  CD1 . PHE   A 92  ? 0.391 0.053 0.379 -0.003 0.052  -0.071 91  PHE   AAA CD1 
686  C  CD2 . PHE   A 92  ? 0.454 0.059 0.380 0.049  -0.021 -0.103 91  PHE   AAA CD2 
687  C  CE1 . PHE   A 92  ? 0.397 0.057 0.352 0.035  0.024  -0.070 91  PHE   AAA CE1 
688  C  CE2 . PHE   A 92  ? 0.500 0.044 0.397 0.041  0.042  -0.042 91  PHE   AAA CE2 
689  C  CZ  . PHE   A 92  ? 0.398 0.147 0.385 0.020  0.021  -0.040 91  PHE   AAA CZ  
690  N  N   . GLN   A 93  ? 0.385 0.120 0.333 0.032  0.043  -0.046 92  GLN   AAA N   
691  C  CA  . GLN   A 93  ? 0.330 0.140 0.360 -0.042 0.038  -0.048 92  GLN   AAA CA  
692  C  C   . GLN   A 93  ? 0.327 0.030 0.303 -0.002 -0.009 0.016  92  GLN   AAA C   
693  O  O   . GLN   A 93  ? 0.381 0.016 0.332 0.046  -0.023 -0.039 92  GLN   AAA O   
694  C  CB  . GLN   A 93  ? 0.360 0.229 0.371 -0.038 0.061  0.042  92  GLN   AAA CB  
695  C  CG  . GLN   A 93  ? 0.399 0.229 0.328 -0.030 0.034  -0.071 92  GLN   AAA CG  
696  C  CD  . GLN   A 93  ? 0.455 0.166 0.409 -0.048 0.094  -0.097 92  GLN   AAA CD  
697  O  OE1 . GLN   A 93  ? 0.460 0.280 0.426 -0.067 0.055  -0.029 92  GLN   AAA OE1 
698  N  NE2 . GLN   A 93  ? 0.422 0.128 0.355 0.036  0.017  -0.048 92  GLN   AAA NE2 
699  N  N   . PHE   A 94  ? 0.327 0.096 0.343 -0.022 -0.004 -0.055 93  PHE   AAA N   
700  C  CA  . PHE   A 94  ? 0.358 0.086 0.369 0.006  0.012  -0.055 93  PHE   AAA CA  
701  C  C   . PHE   A 94  ? 0.393 0.123 0.304 0.042  -0.002 -0.098 93  PHE   AAA C   
702  O  O   . PHE   A 94  ? 0.392 0.063 0.329 0.011  0.009  -0.066 93  PHE   AAA O   
703  C  CB  . PHE   A 94  ? 0.425 0.114 0.315 0.013  -0.013 -0.019 93  PHE   AAA CB  
704  C  CG  . PHE   A 94  ? 0.391 0.047 0.309 0.043  0.022  -0.059 93  PHE   AAA CG  
705  C  CD1 . PHE   A 94  ? 0.359 0.284 0.421 0.004  0.002  -0.095 93  PHE   AAA CD1 
706  C  CD2 . PHE   A 94  ? 0.370 0.038 0.372 0.027  -0.013 -0.061 93  PHE   AAA CD2 
707  C  CE1 . PHE   A 94  ? 0.453 0.052 0.365 -0.022 0.005  -0.028 93  PHE   AAA CE1 
708  C  CE2 . PHE   A 94  ? 0.355 0.054 0.394 -0.006 0.006  -0.049 93  PHE   AAA CE2 
709  C  CZ  . PHE   A 94  ? 0.353 0.097 0.385 -0.010 0.009  -0.132 93  PHE   AAA CZ  
710  N  N   . HIS   A 95  ? 0.414 0.069 0.278 0.004  -0.014 -0.083 94  HIS   AAA N   
711  C  CA  . HIS   A 95  ? 0.389 0.217 0.307 0.006  -0.009 -0.056 94  HIS   AAA CA  
712  C  C   . HIS   A 95  ? 0.356 0.185 0.303 0.003  -0.050 -0.072 94  HIS   AAA C   
713  O  O   . HIS   A 95  ? 0.419 0.022 0.332 0.035  -0.004 -0.042 94  HIS   AAA O   
714  C  CB  . HIS   A 95  ? 0.358 0.142 0.302 -0.014 -0.015 -0.067 94  HIS   AAA CB  
715  C  CG  . HIS   A 95  ? 0.344 0.193 0.344 -0.034 -0.001 -0.091 94  HIS   AAA CG  
716  N  ND1 . HIS   A 95  ? 0.339 0.065 0.377 -0.007 -0.006 -0.018 94  HIS   AAA ND1 
717  C  CD2 . HIS   A 95  ? 0.352 0.076 0.366 0.029  0.009  -0.005 94  HIS   AAA CD2 
718  C  CE1 . HIS   A 95  ? 0.365 0.211 0.339 0.014  0.043  -0.130 94  HIS   AAA CE1 
719  N  NE2 . HIS   A 95  ? 0.375 0.012 0.514 0.005  -0.003 -0.052 94  HIS   AAA NE2 
720  N  N   . PHE   A 96  ? 0.352 0.057 0.319 -0.020 0.009  -0.051 95  PHE   AAA N   
721  C  CA  . PHE   A 96  ? 0.303 0.060 0.295 0.042  -0.009 0.024  95  PHE   AAA CA  
722  C  C   . PHE   A 96  ? 0.418 0.044 0.288 0.018  -0.016 0.002  95  PHE   AAA C   
723  O  O   . PHE   A 96  ? 0.397 0.247 0.314 -0.020 0.029  -0.068 95  PHE   AAA O   
724  C  CB  . PHE   A 96  ? 0.300 0.045 0.341 0.052  -0.007 -0.013 95  PHE   AAA CB  
725  C  CG  . PHE   A 96  ? 0.379 0.078 0.362 -0.041 0.009  0.002  95  PHE   AAA CG  
726  C  CD1 . PHE   A 96  ? 0.340 0.143 0.361 -0.038 -0.014 -0.036 95  PHE   AAA CD1 
727  C  CD2 . PHE   A 96  ? 0.370 0.084 0.353 -0.029 0.003  -0.010 95  PHE   AAA CD2 
728  C  CE1 . PHE   A 96  ? 0.381 0.150 0.348 -0.026 -0.017 -0.010 95  PHE   AAA CE1 
729  C  CE2 . PHE   A 96  ? 0.382 0.091 0.372 -0.042 -0.006 -0.025 95  PHE   AAA CE2 
730  C  CZ  . PHE   A 96  ? 0.399 0.051 0.369 -0.023 -0.013 -0.014 95  PHE   AAA CZ  
731  N  N   . HIS   A 97  ? 0.359 0.162 0.300 0.051  -0.018 -0.050 96  HIS   AAA N   
732  C  CA  . HIS   A 97  ? 0.287 0.182 0.363 0.003  -0.059 0.043  96  HIS   AAA CA  
733  C  C   . HIS   A 97  ? 0.317 0.224 0.322 -0.027 -0.007 0.011  96  HIS   AAA C   
734  O  O   . HIS   A 97  ? 0.349 0.092 0.359 0.030  0.023  -0.016 96  HIS   AAA O   
735  C  CB  . HIS   A 97  ? 0.334 0.098 0.408 0.026  -0.029 -0.015 96  HIS   AAA CB  
736  C  CG  . HIS   A 97  ? 0.340 0.112 0.371 0.092  -0.006 -0.016 96  HIS   AAA CG  
737  N  ND1 . HIS   A 97  ? 0.338 0.015 0.400 -0.011 0.008  -0.057 96  HIS   AAA ND1 
738  C  CD2 . HIS   A 97  ? 0.343 0.042 0.344 0.094  0.025  -0.049 96  HIS   AAA CD2 
739  C  CE1 . HIS   A 97  ? 0.280 0.145 0.322 0.002  -0.026 0.061  96  HIS   AAA CE1 
740  N  NE2 . HIS   A 97  ? 0.470 0.053 0.305 0.089  0.031  -0.015 96  HIS   AAA NE2 
741  N  N   . TRP   A 98  ? 0.371 0.182 0.377 0.050  0.001  -0.023 97  TRP   AAA N   
742  C  CA  . TRP   A 98  ? 0.381 0.098 0.419 0.025  -0.012 -0.006 97  TRP   AAA CA  
743  C  C   . TRP   A 98  ? 0.371 0.131 0.428 0.087  -0.006 0.030  97  TRP   AAA C   
744  O  O   . TRP   A 98  ? 0.405 0.158 0.430 0.031  0.018  -0.049 97  TRP   AAA O   
745  C  CB  . TRP   A 98  ? 0.402 0.114 0.375 0.032  -0.049 -0.025 97  TRP   AAA CB  
746  C  CG  . TRP   A 98  ? 0.384 0.196 0.378 0.024  -0.041 -0.071 97  TRP   AAA CG  
747  C  CD1 . TRP   A 98  ? 0.484 0.377 0.334 0.041  -0.031 -0.013 97  TRP   AAA CD1 
748  C  CD2 . TRP   A 98  ? 0.415 0.189 0.359 0.003  -0.004 -0.083 97  TRP   AAA CD2 
749  N  NE1 . TRP   A 98  ? 0.427 0.265 0.349 0.041  -0.007 0.006  97  TRP   AAA NE1 
750  C  CE2 . TRP   A 98  ? 0.380 0.262 0.382 0.009  -0.023 -0.052 97  TRP   AAA CE2 
751  C  CE3 . TRP   A 98  ? 0.419 0.208 0.521 0.053  0.044  -0.118 97  TRP   AAA CE3 
752  C  CZ2 . TRP   A 98  ? 0.395 0.224 0.376 0.075  -0.017 -0.031 97  TRP   AAA CZ2 
753  C  CZ3 . TRP   A 98  ? 0.421 0.118 0.384 0.078  -0.013 -0.017 97  TRP   AAA CZ3 
754  C  CH2 . TRP   A 98  ? 0.379 0.202 0.354 0.068  -0.009 -0.069 97  TRP   AAA CH2 
755  N  N   . GLY   A 99  ? 0.420 0.168 0.437 0.099  -0.028 -0.100 98  GLY   AAA N   
756  C  CA  . GLY   A 99  ? 0.424 0.206 0.515 0.186  0.053  -0.024 98  GLY   AAA CA  
757  C  C   . GLY   A 99  ? 0.406 0.296 0.479 0.004  0.016  -0.101 98  GLY   AAA C   
758  O  O   . GLY   A 99  ? 0.411 0.215 0.449 0.048  0.034  0.074  98  GLY   AAA O   
759  N  N   . SER   A 100 ? 0.520 0.477 0.469 0.141  0.020  0.005  99  SER   AAA N   
760  C  CA  A SER   A 100 ? 0.517 0.488 0.513 0.177  0.002  -0.064 99  SER   AAA CA  
761  C  CA  B SER   A 100 ? 0.516 0.544 0.497 0.171  0.005  -0.057 99  SER   AAA CA  
762  C  C   . SER   A 100 ? 0.518 0.598 0.467 0.195  0.008  -0.126 99  SER   AAA C   
763  O  O   . SER   A 100 ? 0.582 0.706 0.524 0.189  -0.054 -0.076 99  SER   AAA O   
764  C  CB  A SER   A 100 ? 0.655 0.494 0.453 0.170  -0.020 -0.057 99  SER   AAA CB  
765  C  CB  B SER   A 100 ? 0.559 0.580 0.409 0.151  0.047  -0.002 99  SER   AAA CB  
766  O  OG  A SER   A 100 ? 0.717 0.393 0.481 0.163  -0.037 -0.032 99  SER   AAA OG  
767  O  OG  B SER   A 100 ? 0.581 0.733 0.311 0.129  0.043  0.012  99  SER   AAA OG  
768  N  N   . THR   A 101 ? 0.608 0.515 0.431 0.342  0.083  0.005  100 THR   AAA N   
769  C  CA  . THR   A 101 ? 0.513 0.495 0.590 0.309  0.115  0.059  100 THR   AAA CA  
770  C  C   . THR   A 101 ? 0.500 0.421 0.516 0.297  0.064  -0.065 100 THR   AAA C   
771  O  O   . THR   A 101 ? 0.504 0.265 0.512 0.195  0.022  -0.061 100 THR   AAA O   
772  C  CB  . THR   A 101 ? 0.556 0.571 0.566 0.412  0.106  0.026  100 THR   AAA CB  
773  O  OG1 . THR   A 101 ? 0.775 0.533 0.653 0.307  0.034  -0.055 100 THR   AAA OG1 
774  C  CG2 . THR   A 101 ? 0.691 0.695 0.655 0.372  0.223  0.173  100 THR   AAA CG2 
775  N  N   . ASN   A 102 ? 0.505 0.392 0.532 0.265  0.027  -0.034 101 ASN   AAA N   
776  C  CA  . ASN   A 102 ? 0.515 0.358 0.437 0.172  0.048  -0.076 101 ASN   AAA CA  
777  C  C   . ASN   A 102 ? 0.587 0.278 0.500 0.137  0.015  -0.059 101 ASN   AAA C   
778  O  O   . ASN   A 102 ? 0.670 0.306 0.377 0.119  -0.034 -0.123 101 ASN   AAA O   
779  C  CB  . ASN   A 102 ? 0.432 0.459 0.496 0.119  -0.029 -0.104 101 ASN   AAA CB  
780  C  CG  . ASN   A 102 ? 0.467 0.473 0.359 0.088  0.015  -0.056 101 ASN   AAA CG  
781  O  OD1 . ASN   A 102 ? 0.632 0.489 0.397 0.139  0.008  -0.134 101 ASN   AAA OD1 
782  N  ND2 . ASN   A 102 ? 0.404 0.383 0.562 0.094  -0.027 -0.123 101 ASN   AAA ND2 
783  N  N   . GLU   A 103 ? 0.570 0.282 0.487 0.214  0.100  0.024  102 GLU   AAA N   
784  C  CA  . GLU   A 103 ? 0.537 0.317 0.569 0.105  -0.042 0.045  102 GLU   AAA CA  
785  C  C   . GLU   A 103 ? 0.560 0.252 0.431 0.102  -0.023 -0.007 102 GLU   AAA C   
786  O  O   . GLU   A 103 ? 0.613 0.302 0.433 0.092  0.009  -0.082 102 GLU   AAA O   
787  C  CB  . GLU   A 103 ? 0.684 0.372 0.749 0.253  -0.098 0.004  102 GLU   AAA CB  
788  C  CG  . GLU   A 103 ? 0.765 0.359 0.975 0.145  0.040  0.180  102 GLU   AAA CG  
789  C  CD  . GLU   A 103 ? 1.050 0.595 1.101 0.097  -0.096 0.144  102 GLU   AAA CD  
790  O  OE1 . GLU   A 103 ? 1.035 0.296 1.424 0.087  0.317  0.186  102 GLU   AAA OE1 
791  O  OE2 . GLU   A 103 ? 1.317 0.694 1.048 0.695  0.103  0.209  102 GLU   AAA OE2 
792  N  N   . HIS   A 104 ? 0.521 0.336 0.472 0.063  0.024  -0.008 103 HIS   AAA N   
793  C  CA  A HIS   A 104 ? 0.535 0.232 0.543 -0.013 -0.003 -0.110 103 HIS   AAA CA  
794  C  CA  B HIS   A 104 ? 0.524 0.126 0.530 0.027  -0.001 -0.064 103 HIS   AAA CA  
795  C  C   . HIS   A 104 ? 0.465 0.515 0.518 0.105  0.067  -0.220 103 HIS   AAA C   
796  O  O   . HIS   A 104 ? 0.744 0.454 0.700 0.024  -0.067 -0.181 103 HIS   AAA O   
797  C  CB  A HIS   A 104 ? 0.626 0.374 0.519 -0.007 0.012  0.052  103 HIS   AAA CB  
798  C  CB  B HIS   A 104 ? 0.441 0.120 0.419 0.058  0.067  -0.127 103 HIS   AAA CB  
799  C  CG  A HIS   A 104 ? 0.566 0.475 0.518 -0.041 0.021  0.069  103 HIS   AAA CG  
800  C  CG  B HIS   A 104 ? 0.447 0.169 0.428 -0.029 0.025  -0.095 103 HIS   AAA CG  
801  N  ND1 A HIS   A 104 ? 0.594 0.031 0.507 -0.081 -0.033 0.085  103 HIS   AAA ND1 
802  N  ND1 B HIS   A 104 ? 0.498 0.053 0.475 0.049  0.053  -0.073 103 HIS   AAA ND1 
803  C  CD2 A HIS   A 104 ? 0.602 0.441 0.429 -0.021 -0.016 -0.100 103 HIS   AAA CD2 
804  C  CD2 B HIS   A 104 ? 0.460 0.053 0.362 -0.014 0.046  -0.129 103 HIS   AAA CD2 
805  C  CE1 A HIS   A 104 ? 0.444 0.248 0.488 -0.104 -0.041 0.158  103 HIS   AAA CE1 
806  C  CE1 B HIS   A 104 ? 0.477 0.065 0.488 -0.073 0.081  -0.161 103 HIS   AAA CE1 
807  N  NE2 A HIS   A 104 ? 0.493 0.403 0.626 0.024  -0.050 0.037  103 HIS   AAA NE2 
808  N  NE2 B HIS   A 104 ? 0.418 0.235 0.427 0.079  0.014  0.007  103 HIS   AAA NE2 
809  N  N   . GLY   A 105 ? 0.393 0.506 0.465 -0.049 0.056  -0.270 104 GLY   AAA N   
810  C  CA  . GLY   A 105 ? 0.481 0.214 0.432 0.035  -0.036 -0.094 104 GLY   AAA CA  
811  C  C   . GLY   A 105 ? 0.371 0.280 0.331 -0.017 0.018  -0.053 104 GLY   AAA C   
812  O  O   . GLY   A 105 ? 0.411 0.229 0.407 -0.004 0.035  -0.090 104 GLY   AAA O   
813  N  N   . SER   A 106 ? 0.390 0.088 0.378 -0.017 0.005  -0.079 105 SER   AAA N   
814  C  CA  . SER   A 106 ? 0.398 0.216 0.369 -0.004 -0.004 -0.015 105 SER   AAA CA  
815  C  C   . SER   A 106 ? 0.378 0.186 0.328 0.039  -0.028 -0.007 105 SER   AAA C   
816  O  O   . SER   A 106 ? 0.422 0.155 0.360 0.055  0.002  -0.003 105 SER   AAA O   
817  C  CB  . SER   A 106 ? 0.409 0.198 0.324 -0.061 0.024  -0.072 105 SER   AAA CB  
818  O  OG  . SER   A 106 ? 0.413 0.210 0.374 0.023  -0.008 -0.101 105 SER   AAA OG  
819  N  N   . GLU   A 107 ? 0.371 0.211 0.376 0.020  -0.025 -0.057 106 GLU   AAA N   
820  C  CA  . GLU   A 107 ? 0.385 0.201 0.377 0.024  0.016  -0.034 106 GLU   AAA CA  
821  C  C   . GLU   A 107 ? 0.416 0.146 0.347 0.099  0.008  -0.047 106 GLU   AAA C   
822  O  O   . GLU   A 107 ? 0.441 0.145 0.421 0.009  0.023  -0.121 106 GLU   AAA O   
823  C  CB  . GLU   A 107 ? 0.399 0.112 0.360 -0.014 0.022  -0.013 106 GLU   AAA CB  
824  C  CG  . GLU   A 107 ? 0.482 0.133 0.365 -0.015 0.029  -0.060 106 GLU   AAA CG  
825  C  CD  . GLU   A 107 ? 0.474 0.220 0.272 0.064  -0.005 -0.048 106 GLU   AAA CD  
826  O  OE1 . GLU   A 107 ? 0.443 0.016 0.384 -0.025 -0.015 -0.038 106 GLU   AAA OE1 
827  O  OE2 . GLU   A 107 ? 0.442 0.065 0.415 -0.010 0.027  -0.020 106 GLU   AAA OE2 
828  N  N   . HIS   A 108 ? 0.396 0.051 0.356 0.024  0.002  -0.070 107 HIS   AAA N   
829  C  CA  . HIS   A 108 ? 0.443 0.187 0.324 0.020  0.030  -0.091 107 HIS   AAA CA  
830  C  C   . HIS   A 108 ? 0.359 0.259 0.321 -0.005 -0.018 -0.113 107 HIS   AAA C   
831  O  O   . HIS   A 108 ? 0.364 0.166 0.399 0.025  -0.016 -0.084 107 HIS   AAA O   
832  C  CB  . HIS   A 108 ? 0.384 0.172 0.424 -0.030 -0.004 -0.095 107 HIS   AAA CB  
833  C  CG  . HIS   A 108 ? 0.388 0.088 0.363 0.018  0.000  -0.087 107 HIS   AAA CG  
834  N  ND1 . HIS   A 108 ? 0.395 0.056 0.359 0.017  0.020  -0.073 107 HIS   AAA ND1 
835  C  CD2 . HIS   A 108 ? 0.372 0.227 0.429 -0.054 0.047  -0.159 107 HIS   AAA CD2 
836  C  CE1 . HIS   A 108 ? 0.400 0.076 0.390 0.017  -0.012 -0.108 107 HIS   AAA CE1 
837  N  NE2 . HIS   A 108 ? 0.367 0.190 0.378 -0.031 0.006  -0.127 107 HIS   AAA NE2 
838  N  N   . THR   A 109 ? 0.379 0.167 0.430 0.000  -0.010 -0.128 108 THR   AAA N   
839  C  CA  . THR   A 109 ? 0.396 0.054 0.484 0.044  0.022  -0.039 108 THR   AAA CA  
840  C  C   . THR   A 109 ? 0.374 0.018 0.453 -0.047 0.007  -0.051 108 THR   AAA C   
841  O  O   . THR   A 109 ? 0.363 0.276 0.421 -0.011 0.011  -0.134 108 THR   AAA O   
842  C  CB  . THR   A 109 ? 0.401 0.063 0.438 0.059  0.036  -0.013 108 THR   AAA CB  
843  O  OG1 . THR   A 109 ? 0.426 0.238 0.509 0.017  0.001  -0.109 108 THR   AAA OG1 
844  C  CG2 . THR   A 109 ? 0.469 0.142 0.482 0.105  0.028  -0.052 108 THR   AAA CG2 
845  N  N   . VAL   A 110 ? 0.435 0.175 0.398 0.023  0.047  -0.140 109 VAL   AAA N   
846  C  CA  . VAL   A 110 ? 0.420 0.113 0.411 -0.016 0.050  -0.059 109 VAL   AAA CA  
847  C  C   . VAL   A 110 ? 0.383 0.212 0.458 0.027  -0.005 -0.143 109 VAL   AAA C   
848  O  O   . VAL   A 110 ? 0.414 0.137 0.410 0.003  0.054  -0.077 109 VAL   AAA O   
849  C  CB  . VAL   A 110 ? 0.473 0.110 0.423 -0.085 0.019  -0.099 109 VAL   AAA CB  
850  C  CG1 . VAL   A 110 ? 0.543 0.124 0.406 -0.056 0.027  -0.086 109 VAL   AAA CG1 
851  C  CG2 . VAL   A 110 ? 0.459 0.052 0.461 -0.047 0.021  -0.084 109 VAL   AAA CG2 
852  N  N   . ASP   A 111 ? 0.451 0.196 0.434 -0.042 0.049  -0.124 110 ASP   AAA N   
853  C  CA  . ASP   A 111 ? 0.547 0.265 0.491 0.059  0.078  -0.122 110 ASP   AAA CA  
854  C  C   . ASP   A 111 ? 0.434 0.301 0.453 -0.023 0.051  -0.113 110 ASP   AAA C   
855  O  O   . ASP   A 111 ? 0.485 0.142 0.470 0.023  0.045  -0.089 110 ASP   AAA O   
856  C  CB  . ASP   A 111 ? 0.522 0.198 0.439 0.057  0.047  -0.116 110 ASP   AAA CB  
857  C  CG  . ASP   A 111 ? 0.439 0.294 0.363 -0.041 0.057  -0.022 110 ASP   AAA CG  
858  O  OD1 . ASP   A 111 ? 0.501 0.215 0.496 -0.051 0.012  -0.128 110 ASP   AAA OD1 
859  O  OD2 . ASP   A 111 ? 0.654 0.230 0.438 -0.037 0.044  -0.055 110 ASP   AAA OD2 
860  N  N   . GLY   A 112 ? 0.431 0.302 0.443 0.031  0.066  -0.137 111 GLY   AAA N   
861  C  CA  . GLY   A 112 ? 0.532 0.166 0.494 0.060  0.067  -0.075 111 GLY   AAA CA  
862  C  C   . GLY   A 112 ? 0.538 0.039 0.413 0.093  -0.011 -0.034 111 GLY   AAA C   
863  O  O   . GLY   A 112 ? 0.469 0.133 0.487 0.044  -0.014 0.015  111 GLY   AAA O   
864  N  N   . VAL   A 113 ? 0.563 0.133 0.431 -0.031 0.086  -0.012 112 VAL   AAA N   
865  C  CA  . VAL   A 113 ? 0.435 0.124 0.364 0.073  0.081  -0.010 112 VAL   AAA CA  
866  C  C   . VAL   A 113 ? 0.382 0.260 0.338 0.039  0.044  -0.020 112 VAL   AAA C   
867  O  O   . VAL   A 113 ? 0.413 0.266 0.400 0.052  0.050  -0.106 112 VAL   AAA O   
868  C  CB  . VAL   A 113 ? 0.423 0.369 0.293 0.035  0.057  -0.007 112 VAL   AAA CB  
869  C  CG1 . VAL   A 113 ? 0.399 0.355 0.400 0.010  0.052  -0.029 112 VAL   AAA CG1 
870  C  CG2 . VAL   A 113 ? 0.540 0.519 0.326 0.011  0.109  -0.048 112 VAL   AAA CG2 
871  N  N   . LYS   A 114 ? 0.450 0.139 0.379 0.100  0.003  -0.019 113 LYS   AAA N   
872  C  CA  . LYS   A 114 ? 0.427 0.244 0.371 0.012  0.029  -0.026 113 LYS   AAA CA  
873  C  C   . LYS   A 114 ? 0.401 0.185 0.469 0.078  0.080  -0.063 113 LYS   AAA C   
874  O  O   . LYS   A 114 ? 0.414 0.104 0.507 0.005  0.030  -0.092 113 LYS   AAA O   
875  C  CB  . LYS   A 114 ? 0.445 0.282 0.449 0.054  0.048  0.019  113 LYS   AAA CB  
876  C  CG  . LYS   A 114 ? 0.546 0.322 0.473 -0.009 0.008  0.009  113 LYS   AAA CG  
877  C  CD  . LYS   A 114 ? 0.649 0.448 0.456 0.078  0.050  0.098  113 LYS   AAA CD  
878  C  CE  . LYS   A 114 ? 0.996 0.328 0.540 -0.024 0.030  -0.054 113 LYS   AAA CE  
879  N  NZ  . LYS   A 114 ? 1.181 0.383 0.719 -0.172 -0.001 -0.049 113 LYS   AAA NZ  
880  N  N   . TYR   A 115 ? 0.392 0.168 0.420 0.001  0.094  -0.119 114 TYR   AAA N   
881  C  CA  . TYR   A 115 ? 0.364 0.152 0.400 0.000  0.030  -0.018 114 TYR   AAA CA  
882  C  C   . TYR   A 115 ? 0.382 0.191 0.396 0.055  0.046  -0.046 114 TYR   AAA C   
883  O  O   . TYR   A 115 ? 0.387 0.281 0.387 -0.000 0.021  -0.028 114 TYR   AAA O   
884  C  CB  . TYR   A 115 ? 0.398 0.208 0.378 0.049  -0.059 -0.084 114 TYR   AAA CB  
885  C  CG  . TYR   A 115 ? 0.387 0.229 0.353 0.050  0.028  -0.080 114 TYR   AAA CG  
886  C  CD1 . TYR   A 115 ? 0.514 0.219 0.379 0.012  0.042  -0.013 114 TYR   AAA CD1 
887  C  CD2 . TYR   A 115 ? 0.390 0.262 0.366 -0.037 0.020  0.017  114 TYR   AAA CD2 
888  C  CE1 . TYR   A 115 ? 0.481 0.460 0.378 -0.033 -0.002 -0.057 114 TYR   AAA CE1 
889  C  CE2 . TYR   A 115 ? 0.449 0.162 0.408 0.015  0.003  -0.053 114 TYR   AAA CE2 
890  C  CZ  . TYR   A 115 ? 0.451 0.187 0.377 0.028  0.028  -0.077 114 TYR   AAA CZ  
891  O  OH  . TYR   A 115 ? 0.550 0.217 0.404 0.001  0.006  -0.099 114 TYR   AAA OH  
892  N  N   . SER   A 116 ? 0.364 0.278 0.402 0.003  0.032  -0.038 115 SER   AAA N   
893  C  CA  . SER   A 116 ? 0.355 0.198 0.441 0.065  -0.001 -0.035 115 SER   AAA CA  
894  C  C   . SER   A 116 ? 0.356 0.232 0.393 0.030  -0.028 -0.037 115 SER   AAA C   
895  O  O   . SER   A 116 ? 0.424 0.172 0.398 0.016  -0.009 -0.065 115 SER   AAA O   
896  C  CB  . SER   A 116 ? 0.295 0.421 0.454 0.003  0.018  -0.097 115 SER   AAA CB  
897  O  OG  . SER   A 116 ? 0.378 0.465 0.512 0.017  0.087  -0.042 115 SER   AAA OG  
898  N  N   . ALA   A 117 ? 0.348 0.149 0.347 -0.009 -0.000 -0.001 116 ALA   AAA N   
899  C  CA  . ALA   A 117 ? 0.361 0.283 0.344 0.011  0.037  0.024  116 ALA   AAA CA  
900  C  C   . ALA   A 117 ? 0.355 0.142 0.330 -0.015 0.030  -0.013 116 ALA   AAA C   
901  O  O   . ALA   A 117 ? 0.419 0.083 0.364 0.066  0.041  -0.047 116 ALA   AAA O   
902  C  CB  . ALA   A 117 ? 0.374 0.427 0.323 0.017  0.011  -0.051 116 ALA   AAA CB  
903  N  N   . GLU   A 118 ? 0.352 0.207 0.350 0.018  -0.003 -0.067 117 GLU   AAA N   
904  C  CA  . GLU   A 118 ? 0.326 0.209 0.348 0.001  0.004  -0.089 117 GLU   AAA CA  
905  C  C   . GLU   A 118 ? 0.433 0.097 0.297 0.035  -0.026 -0.033 117 GLU   AAA C   
906  O  O   . GLU   A 118 ? 0.415 0.071 0.328 0.016  0.022  -0.048 117 GLU   AAA O   
907  C  CB  . GLU   A 118 ? 0.373 0.146 0.325 -0.016 -0.007 -0.096 117 GLU   AAA CB  
908  C  CG  . GLU   A 118 ? 0.388 0.009 0.347 -0.023 0.002  -0.020 117 GLU   AAA CG  
909  C  CD  . GLU   A 118 ? 0.324 0.077 0.427 -0.083 0.028  -0.095 117 GLU   AAA CD  
910  O  OE1 . GLU   A 118 ? 0.340 0.158 0.351 0.012  0.018  -0.069 117 GLU   AAA OE1 
911  O  OE2 . GLU   A 118 ? 0.420 0.185 0.332 0.060  0.013  -0.063 117 GLU   AAA OE2 
912  N  N   . LEU   A 119 ? 0.381 0.134 0.304 0.012  -0.032 -0.023 118 LEU   AAA N   
913  C  CA  . LEU   A 119 ? 0.363 0.126 0.372 -0.015 0.021  -0.026 118 LEU   AAA CA  
914  C  C   . LEU   A 119 ? 0.365 0.006 0.318 0.006  0.003  0.002  118 LEU   AAA C   
915  O  O   . LEU   A 119 ? 0.380 0.062 0.348 0.026  -0.035 -0.048 118 LEU   AAA O   
916  C  CB  . LEU   A 119 ? 0.342 0.059 0.392 -0.010 -0.025 -0.034 118 LEU   AAA CB  
917  C  CG  . LEU   A 119 ? 0.332 0.090 0.296 0.015  0.026  0.010  118 LEU   AAA CG  
918  C  CD1 . LEU   A 119 ? 0.410 0.042 0.318 -0.013 0.037  -0.003 118 LEU   AAA CD1 
919  C  CD2 . LEU   A 119 ? 0.396 0.097 0.335 0.005  0.027  0.016  118 LEU   AAA CD2 
920  N  N   . HIS   A 120 ? 0.375 0.073 0.305 0.004  0.005  -0.067 119 HIS   AAA N   
921  C  CA  . HIS   A 120 ? 0.392 0.049 0.380 0.042  -0.023 -0.063 119 HIS   AAA CA  
922  C  C   . HIS   A 120 ? 0.398 0.060 0.314 0.053  -0.020 -0.061 119 HIS   AAA C   
923  O  O   . HIS   A 120 ? 0.408 0.092 0.309 -0.005 0.014  -0.027 119 HIS   AAA O   
924  C  CB  . HIS   A 120 ? 0.379 0.175 0.285 0.036  0.020  -0.092 119 HIS   AAA CB  
925  C  CG  . HIS   A 120 ? 0.337 0.113 0.282 -0.017 0.017  -0.035 119 HIS   AAA CG  
926  N  ND1 . HIS   A 120 ? 0.323 0.015 0.434 0.022  -0.041 -0.058 119 HIS   AAA ND1 
927  C  CD2 . HIS   A 120 ? 0.393 0.094 0.310 -0.030 0.037  -0.073 119 HIS   AAA CD2 
928  C  CE1 . HIS   A 120 ? 0.383 0.131 0.269 -0.034 0.052  -0.123 119 HIS   AAA CE1 
929  N  NE2 . HIS   A 120 ? 0.393 0.083 0.302 -0.046 0.021  -0.092 119 HIS   AAA NE2 
930  N  N   . VAL   A 121 ? 0.371 0.071 0.315 0.017  -0.002 -0.097 120 VAL   AAA N   
931  C  CA  . VAL   A 121 ? 0.379 0.069 0.295 0.013  -0.012 -0.108 120 VAL   AAA CA  
932  C  C   . VAL   A 121 ? 0.392 0.084 0.274 0.011  -0.008 -0.001 120 VAL   AAA C   
933  O  O   . VAL   A 121 ? 0.373 0.075 0.322 -0.001 -0.001 -0.044 120 VAL   AAA O   
934  C  CB  . VAL   A 121 ? 0.392 0.057 0.293 0.068  -0.024 -0.076 120 VAL   AAA CB  
935  C  CG1 . VAL   A 121 ? 0.424 0.018 0.400 -0.047 0.017  -0.053 120 VAL   AAA CG1 
936  C  CG2 . VAL   A 121 ? 0.404 0.079 0.328 -0.030 -0.016 -0.009 120 VAL   AAA CG2 
937  N  N   . ALA   A 122 ? 0.407 0.071 0.303 0.012  0.002  -0.046 121 ALA   AAA N   
938  C  CA  . ALA   A 122 ? 0.359 0.143 0.346 0.024  0.003  -0.063 121 ALA   AAA CA  
939  C  C   . ALA   A 122 ? 0.355 0.132 0.334 0.023  -0.059 -0.014 121 ALA   AAA C   
940  O  O   . ALA   A 122 ? 0.358 0.143 0.344 -0.019 0.011  -0.035 121 ALA   AAA O   
941  C  CB  . ALA   A 122 ? 0.458 0.146 0.366 -0.045 0.002  -0.038 121 ALA   AAA CB  
942  N  N   . HIS   A 123 ? 0.360 0.037 0.357 0.026  -0.048 -0.036 122 HIS   AAA N   
943  C  CA  . HIS   A 123 ? 0.336 0.145 0.363 0.038  -0.009 -0.044 122 HIS   AAA CA  
944  C  C   . HIS   A 123 ? 0.389 0.153 0.371 0.005  0.027  -0.111 122 HIS   AAA C   
945  O  O   . HIS   A 123 ? 0.427 0.108 0.352 0.013  -0.030 -0.016 122 HIS   AAA O   
946  C  CB  . HIS   A 123 ? 0.394 0.042 0.365 0.098  0.044  -0.052 122 HIS   AAA CB  
947  C  CG  . HIS   A 123 ? 0.362 0.126 0.370 0.075  0.007  0.029  122 HIS   AAA CG  
948  N  ND1 . HIS   A 123 ? 0.334 0.234 0.359 0.042  0.031  -0.062 122 HIS   AAA ND1 
949  C  CD2 . HIS   A 123 ? 0.406 0.115 0.361 0.022  0.033  -0.075 122 HIS   AAA CD2 
950  C  CE1 . HIS   A 123 ? 0.417 0.129 0.365 0.037  0.034  -0.020 122 HIS   AAA CE1 
951  N  NE2 . HIS   A 123 ? 0.359 0.139 0.330 0.038  0.012  -0.062 122 HIS   AAA NE2 
952  N  N   . TRP   A 124 ? 0.424 0.027 0.377 0.020  0.021  -0.084 123 TRP   AAA N   
953  C  CA  . TRP   A 124 ? 0.404 0.048 0.410 0.070  0.032  -0.074 123 TRP   AAA CA  
954  C  C   . TRP   A 124 ? 0.316 0.197 0.419 -0.011 0.005  -0.006 123 TRP   AAA C   
955  O  O   . TRP   A 124 ? 0.432 0.148 0.476 -0.001 0.032  -0.050 123 TRP   AAA O   
956  C  CB  . TRP   A 124 ? 0.382 0.056 0.431 0.067  0.049  -0.117 123 TRP   AAA CB  
957  C  CG  . TRP   A 124 ? 0.409 0.048 0.381 0.039  0.039  -0.115 123 TRP   AAA CG  
958  C  CD1 . TRP   A 124 ? 0.495 0.073 0.406 -0.027 0.020  -0.062 123 TRP   AAA CD1 
959  C  CD2 . TRP   A 124 ? 0.357 0.133 0.457 0.055  0.054  -0.086 123 TRP   AAA CD2 
960  N  NE1 . TRP   A 124 ? 0.439 0.171 0.426 0.012  0.050  -0.100 123 TRP   AAA NE1 
961  C  CE2 . TRP   A 124 ? 0.423 0.112 0.387 0.037  0.001  0.001  123 TRP   AAA CE2 
962  C  CE3 . TRP   A 124 ? 0.414 0.084 0.531 0.084  -0.012 0.001  123 TRP   AAA CE3 
963  C  CZ2 . TRP   A 124 ? 0.421 0.166 0.442 0.045  0.048  -0.032 123 TRP   AAA CZ2 
964  C  CZ3 . TRP   A 124 ? 0.425 0.180 0.580 0.075  0.047  -0.075 123 TRP   AAA CZ3 
965  C  CH2 . TRP   A 124 ? 0.460 0.041 0.495 0.102  0.059  0.011  123 TRP   AAA CH2 
966  N  N   . ASN   A 125 ? 0.355 0.061 0.486 -0.024 0.019  -0.030 124 ASN   AAA N   
967  C  CA  . ASN   A 125 ? 0.361 0.208 0.458 0.014  -0.005 -0.063 124 ASN   AAA CA  
968  C  C   . ASN   A 125 ? 0.339 0.224 0.441 0.032  0.019  -0.064 124 ASN   AAA C   
969  O  O   . ASN   A 125 ? 0.402 0.169 0.402 0.074  0.060  -0.034 124 ASN   AAA O   
970  C  CB  . ASN   A 125 ? 0.380 0.276 0.423 -0.015 0.001  -0.108 124 ASN   AAA CB  
971  C  CG  . ASN   A 125 ? 0.409 0.189 0.486 0.030  -0.035 -0.131 124 ASN   AAA CG  
972  O  OD1 . ASN   A 125 ? 0.444 0.211 0.531 0.038  -0.042 -0.015 124 ASN   AAA OD1 
973  N  ND2 . ASN   A 125 ? 0.483 0.254 0.577 0.045  -0.028 -0.234 124 ASN   AAA ND2 
974  N  N   . SER   A 126 ? 0.434 0.234 0.447 0.065  0.006  -0.033 125 SER   AAA N   
975  C  CA  . SER   A 126 ? 0.430 0.130 0.550 0.057  0.051  0.014  125 SER   AAA CA  
976  C  C   . SER   A 126 ? 0.430 0.241 0.505 0.035  0.071  -0.014 125 SER   AAA C   
977  O  O   . SER   A 126 ? 0.442 0.242 0.592 0.086  0.061  0.008  125 SER   AAA O   
978  C  CB  . SER   A 126 ? 0.402 0.205 0.501 0.053  0.060  -0.048 125 SER   AAA CB  
979  O  OG  . SER   A 126 ? 0.483 0.121 0.500 0.036  0.064  -0.052 125 SER   AAA OG  
980  N  N   . ALA   A 127 ? 0.464 0.232 0.490 0.019  0.003  -0.000 126 ALA   AAA N   
981  C  CA  . ALA   A 127 ? 0.449 0.341 0.597 0.007  -0.005 0.011  126 ALA   AAA CA  
982  C  C   . ALA   A 127 ? 0.440 0.258 0.604 0.114  -0.008 0.075  126 ALA   AAA C   
983  O  O   . ALA   A 127 ? 0.473 0.179 0.658 0.110  -0.048 -0.093 126 ALA   AAA O   
984  C  CB  . ALA   A 127 ? 0.512 0.420 0.584 0.006  0.049  0.070  126 ALA   AAA CB  
985  N  N   . LYS   A 128 ? 0.457 0.083 0.614 0.015  0.019  -0.068 127 LYS   AAA N   
986  C  CA  . LYS   A 128 ? 0.499 0.137 0.661 0.014  0.040  -0.042 127 LYS   AAA CA  
987  C  C   . LYS   A 128 ? 0.359 0.113 0.660 0.009  0.022  -0.019 127 LYS   AAA C   
988  O  O   . LYS   A 128 ? 0.348 0.384 0.804 -0.079 0.035  0.045  127 LYS   AAA O   
989  C  CB  . LYS   A 128 ? 0.596 0.168 0.680 0.032  -0.077 -0.107 127 LYS   AAA CB  
990  C  CG  . LYS   A 128 ? 0.688 0.187 0.673 0.008  0.011  -0.041 127 LYS   AAA CG  
991  C  CD  . LYS   A 128 ? 0.763 0.377 0.965 -0.030 0.082  -0.262 127 LYS   AAA CD  
992  C  CE  . LYS   A 128 ? 0.586 0.563 0.900 -0.002 0.031  -0.182 127 LYS   AAA CE  
993  N  NZ  . LYS   A 128 ? 0.524 0.609 0.855 0.122  -0.096 -0.175 127 LYS   AAA NZ  
994  N  N   . TYR   A 129 ? 0.398 0.124 0.570 0.028  0.005  -0.047 128 TYR   AAA N   
995  C  CA  . TYR   A 129 ? 0.433 0.260 0.544 0.035  0.021  -0.079 128 TYR   AAA CA  
996  C  C   . TYR   A 129 ? 0.506 0.088 0.487 0.115  0.013  0.013  128 TYR   AAA C   
997  O  O   . TYR   A 129 ? 0.441 0.215 0.536 0.011  0.030  -0.047 128 TYR   AAA O   
998  C  CB  . TYR   A 129 ? 0.414 0.281 0.448 -0.002 -0.007 0.015  128 TYR   AAA CB  
999  C  CG  . TYR   A 129 ? 0.349 0.372 0.468 0.009  0.031  -0.073 128 TYR   AAA CG  
1000 C  CD1 . TYR   A 129 ? 0.375 0.163 0.574 0.022  0.029  -0.146 128 TYR   AAA CD1 
1001 C  CD2 . TYR   A 129 ? 0.379 0.279 0.487 -0.013 0.040  -0.075 128 TYR   AAA CD2 
1002 C  CE1 . TYR   A 129 ? 0.382 0.285 0.546 -0.027 0.017  -0.143 128 TYR   AAA CE1 
1003 C  CE2 . TYR   A 129 ? 0.395 0.293 0.533 0.010  0.008  -0.113 128 TYR   AAA CE2 
1004 C  CZ  . TYR   A 129 ? 0.437 0.226 0.508 -0.023 0.007  -0.110 128 TYR   AAA CZ  
1005 O  OH  . TYR   A 129 ? 0.377 0.111 0.580 -0.012 0.005  -0.082 128 TYR   AAA OH  
1006 N  N   . SER   A 130 ? 0.519 0.107 0.493 0.028  0.050  -0.052 129 SER   AAA N   
1007 C  CA  . SER   A 130 ? 0.498 0.219 0.534 0.017  0.050  -0.116 129 SER   AAA CA  
1008 C  C   . SER   A 130 ? 0.512 0.123 0.505 0.102  0.038  -0.152 129 SER   AAA C   
1009 O  O   . SER   A 130 ? 0.612 0.087 0.551 0.038  0.070  -0.134 129 SER   AAA O   
1010 C  CB  . SER   A 130 ? 0.557 0.230 0.540 0.013  0.113  -0.071 129 SER   AAA CB  
1011 O  OG  . SER   A 130 ? 0.653 0.219 0.647 -0.170 0.096  0.015  129 SER   AAA OG  
1012 N  N   . SER   A 131 ? 0.479 0.021 0.507 0.027  0.038  -0.018 130 SER   AAA N   
1013 C  CA  . SER   A 131 ? 0.507 0.078 0.536 0.029  0.034  -0.061 130 SER   AAA CA  
1014 C  C   . SER   A 131 ? 0.457 0.020 0.479 0.036  -0.011 0.001  130 SER   AAA C   
1015 O  O   . SER   A 131 ? 0.457 0.154 0.385 0.036  -0.001 -0.067 130 SER   AAA O   
1016 C  CB  . SER   A 131 ? 0.585 0.173 0.539 -0.015 0.048  -0.065 130 SER   AAA CB  
1017 O  OG  . SER   A 131 ? 0.575 0.148 0.418 0.042  0.051  -0.058 130 SER   AAA OG  
1018 N  N   . LEU   A 132 ? 0.441 0.020 0.470 0.030  0.014  -0.072 131 LEU   AAA N   
1019 C  CA  . LEU   A 132 ? 0.421 0.033 0.387 0.069  0.005  -0.076 131 LEU   AAA CA  
1020 C  C   . LEU   A 132 ? 0.392 0.162 0.298 -0.040 0.010  -0.089 131 LEU   AAA C   
1021 O  O   . LEU   A 132 ? 0.422 0.105 0.449 -0.028 0.046  -0.113 131 LEU   AAA O   
1022 C  CB  . LEU   A 132 ? 0.444 0.215 0.404 0.013  0.018  0.001  131 LEU   AAA CB  
1023 C  CG  . LEU   A 132 ? 0.374 0.205 0.416 -0.021 0.026  -0.036 131 LEU   AAA CG  
1024 C  CD1 . LEU   A 132 ? 0.394 0.163 0.430 0.023  0.045  -0.052 131 LEU   AAA CD1 
1025 C  CD2 . LEU   A 132 ? 0.435 0.238 0.414 0.016  -0.029 -0.071 131 LEU   AAA CD2 
1026 N  N   . ALA   A 133 ? 0.390 0.109 0.372 0.002  0.080  -0.007 132 ALA   AAA N   
1027 C  CA  . ALA   A 133 ? 0.415 0.167 0.435 -0.074 0.080  0.018  132 ALA   AAA CA  
1028 C  C   . ALA   A 133 ? 0.481 0.024 0.369 -0.013 0.034  -0.063 132 ALA   AAA C   
1029 O  O   . ALA   A 133 ? 0.505 0.043 0.483 -0.095 0.078  -0.087 132 ALA   AAA O   
1030 C  CB  . ALA   A 133 ? 0.483 0.148 0.459 0.009  0.056  -0.022 132 ALA   AAA CB  
1031 N  N   . GLU   A 134 ? 0.402 0.093 0.444 -0.030 0.053  0.030  133 GLU   AAA N   
1032 C  CA  . GLU   A 134 ? 0.405 0.205 0.448 -0.033 0.034  -0.012 133 GLU   AAA CA  
1033 C  C   . GLU   A 134 ? 0.364 0.164 0.461 -0.011 0.053  -0.030 133 GLU   AAA C   
1034 O  O   . GLU   A 134 ? 0.440 0.204 0.444 -0.048 0.032  -0.054 133 GLU   AAA O   
1035 C  CB  . GLU   A 134 ? 0.417 0.212 0.529 -0.011 0.027  0.004  133 GLU   AAA CB  
1036 C  CG  . GLU   A 134 ? 0.487 0.024 0.509 -0.042 0.033  -0.086 133 GLU   AAA CG  
1037 C  CD  . GLU   A 134 ? 0.399 0.141 0.718 -0.018 0.049  -0.115 133 GLU   AAA CD  
1038 O  OE1 . GLU   A 134 ? 0.482 0.070 0.568 0.019  0.069  0.031  133 GLU   AAA OE1 
1039 O  OE2 . GLU   A 134 ? 0.491 0.041 0.863 -0.091 -0.000 -0.063 133 GLU   AAA OE2 
1040 N  N   . ALA   A 135 ? 0.358 0.128 0.427 -0.002 0.020  -0.032 134 ALA   AAA N   
1041 C  CA  . ALA   A 135 ? 0.407 0.116 0.376 0.019  0.016  0.044  134 ALA   AAA CA  
1042 C  C   . ALA   A 135 ? 0.345 0.156 0.398 0.023  -0.014 -0.089 134 ALA   AAA C   
1043 O  O   . ALA   A 135 ? 0.484 0.031 0.453 0.090  0.020  -0.047 134 ALA   AAA O   
1044 C  CB  . ALA   A 135 ? 0.402 0.046 0.439 0.026  0.020  -0.010 134 ALA   AAA CB  
1045 N  N   . ALA   A 136 ? 0.412 0.070 0.408 0.002  0.023  -0.081 135 ALA   AAA N   
1046 C  CA  . ALA   A 136 ? 0.364 0.165 0.449 0.000  0.021  -0.114 135 ALA   AAA CA  
1047 C  C   . ALA   A 136 ? 0.368 0.213 0.389 -0.056 0.054  -0.114 135 ALA   AAA C   
1048 O  O   . ALA   A 136 ? 0.485 0.255 0.419 0.096  0.027  -0.074 135 ALA   AAA O   
1049 C  CB  . ALA   A 136 ? 0.455 0.104 0.476 -0.030 0.011  -0.113 135 ALA   AAA CB  
1050 N  N   . SER   A 137 ? 0.355 0.193 0.459 -0.051 0.053  -0.133 136 SER   AAA N   
1051 C  CA  . SER   A 137 ? 0.514 0.154 0.440 -0.038 0.015  -0.123 136 SER   AAA CA  
1052 C  C   . SER   A 137 ? 0.495 0.083 0.474 -0.052 0.018  -0.061 136 SER   AAA C   
1053 O  O   . SER   A 137 ? 0.490 0.065 0.709 -0.011 -0.025 -0.125 136 SER   AAA O   
1054 C  CB  . SER   A 137 ? 0.502 0.231 0.562 -0.006 0.052  0.026  136 SER   AAA CB  
1055 O  OG  . SER   A 137 ? 0.499 0.125 0.581 -0.090 0.067  -0.047 136 SER   AAA OG  
1056 N  N   . LYS   A 138 ? 0.471 0.075 0.468 -0.031 0.016  -0.047 137 LYS   AAA N   
1057 C  CA  . LYS   A 138 ? 0.436 0.116 0.470 -0.033 0.045  -0.076 137 LYS   AAA CA  
1058 C  C   . LYS   A 138 ? 0.396 0.118 0.492 -0.012 0.028  -0.084 137 LYS   AAA C   
1059 O  O   . LYS   A 138 ? 0.375 0.071 0.470 -0.009 -0.024 -0.116 137 LYS   AAA O   
1060 C  CB  . LYS   A 138 ? 0.448 0.159 0.523 0.029  0.047  -0.022 137 LYS   AAA CB  
1061 C  CG  . LYS   A 138 ? 0.530 0.141 0.501 0.005  0.013  -0.068 137 LYS   AAA CG  
1062 C  CD  . LYS   A 138 ? 0.541 0.405 0.532 -0.031 0.055  -0.138 137 LYS   AAA CD  
1063 C  CE  . LYS   A 138 ? 0.769 0.466 0.503 0.158  0.074  -0.031 137 LYS   AAA CE  
1064 N  NZ  . LYS   A 138 ? 1.014 0.788 0.647 0.166  0.022  0.073  137 LYS   AAA NZ  
1065 N  N   . ALA   A 139 ? 0.475 0.169 0.468 -0.016 -0.011 -0.104 138 ALA   AAA N   
1066 C  CA  . ALA   A 139 ? 0.400 0.193 0.527 0.024  0.032  -0.073 138 ALA   AAA CA  
1067 C  C   . ALA   A 139 ? 0.374 0.203 0.464 0.022  0.004  -0.088 138 ALA   AAA C   
1068 O  O   . ALA   A 139 ? 0.409 0.291 0.475 0.021  0.029  -0.079 138 ALA   AAA O   
1069 C  CB  . ALA   A 139 ? 0.422 0.293 0.487 0.014  0.011  -0.113 138 ALA   AAA CB  
1070 N  N   . ASP   A 140 ? 0.380 0.157 0.517 0.005  -0.013 -0.053 139 ASP   AAA N   
1071 C  CA  . ASP   A 140 ? 0.422 0.233 0.433 -0.024 -0.019 -0.031 139 ASP   AAA CA  
1072 C  C   . ASP   A 140 ? 0.341 0.276 0.395 -0.005 -0.058 -0.047 139 ASP   AAA C   
1073 O  O   . ASP   A 140 ? 0.484 0.334 0.432 -0.007 0.007  0.006  139 ASP   AAA O   
1074 C  CB  . ASP   A 140 ? 0.397 0.226 0.501 -0.035 -0.053 -0.060 139 ASP   AAA CB  
1075 C  CG  . ASP   A 140 ? 0.446 0.297 0.420 -0.026 -0.029 -0.040 139 ASP   AAA CG  
1076 O  OD1 . ASP   A 140 ? 0.420 0.187 0.426 -0.011 -0.010 -0.033 139 ASP   AAA OD1 
1077 O  OD2 . ASP   A 140 ? 0.491 0.383 0.631 0.027  -0.072 -0.071 139 ASP   AAA OD2 
1078 N  N   . GLY   A 141 ? 0.344 0.188 0.399 0.018  -0.023 -0.069 140 GLY   AAA N   
1079 C  CA  . GLY   A 141 ? 0.362 0.177 0.346 0.046  -0.023 -0.034 140 GLY   AAA CA  
1080 C  C   . GLY   A 141 ? 0.353 0.126 0.381 0.024  0.018  -0.057 140 GLY   AAA C   
1081 O  O   . GLY   A 141 ? 0.396 0.218 0.449 0.001  -0.017 -0.155 140 GLY   AAA O   
1082 N  N   . LEU   A 142 ? 0.343 0.102 0.389 -0.017 -0.029 -0.104 141 LEU   AAA N   
1083 C  CA  . LEU   A 142 ? 0.360 0.130 0.379 0.020  -0.010 -0.077 141 LEU   AAA CA  
1084 C  C   . LEU   A 142 ? 0.408 0.158 0.363 0.013  -0.032 -0.054 141 LEU   AAA C   
1085 O  O   . LEU   A 142 ? 0.368 0.279 0.370 -0.025 -0.006 -0.093 141 LEU   AAA O   
1086 C  CB  . LEU   A 142 ? 0.402 0.090 0.373 0.014  -0.019 -0.079 141 LEU   AAA CB  
1087 C  CG  . LEU   A 142 ? 0.325 0.046 0.414 0.010  -0.010 -0.112 141 LEU   AAA CG  
1088 C  CD1 . LEU   A 142 ? 0.433 0.099 0.502 0.091  0.028  -0.064 141 LEU   AAA CD1 
1089 C  CD2 . LEU   A 142 ? 0.404 0.030 0.366 0.019  0.010  -0.084 141 LEU   AAA CD2 
1090 N  N   . ALA   A 143 ? 0.347 0.205 0.369 0.033  0.008  -0.062 142 ALA   AAA N   
1091 C  CA  . ALA   A 143 ? 0.372 0.146 0.344 0.024  -0.004 -0.023 142 ALA   AAA CA  
1092 C  C   . ALA   A 143 ? 0.368 0.206 0.315 0.054  -0.003 -0.074 142 ALA   AAA C   
1093 O  O   . ALA   A 143 ? 0.410 0.170 0.389 0.015  -0.024 -0.078 142 ALA   AAA O   
1094 C  CB  . ALA   A 143 ? 0.381 0.189 0.379 0.056  -0.030 -0.015 142 ALA   AAA CB  
1095 N  N   . VAL   A 144 ? 0.391 0.016 0.341 0.007  0.014  -0.055 143 VAL   AAA N   
1096 C  CA  . VAL   A 144 ? 0.351 0.013 0.345 0.027  0.004  -0.038 143 VAL   AAA CA  
1097 C  C   . VAL   A 144 ? 0.414 0.102 0.291 -0.027 -0.021 -0.019 143 VAL   AAA C   
1098 O  O   . VAL   A 144 ? 0.400 0.186 0.318 -0.007 -0.001 -0.081 143 VAL   AAA O   
1099 C  CB  . VAL   A 144 ? 0.364 0.011 0.362 0.038  0.020  -0.008 143 VAL   AAA CB  
1100 C  CG1 . VAL   A 144 ? 0.388 0.012 0.376 0.027  -0.036 -0.006 143 VAL   AAA CG1 
1101 C  CG2 . VAL   A 144 ? 0.328 0.130 0.356 0.018  0.001  -0.039 143 VAL   AAA CG2 
1102 N  N   . ILE   A 145 ? 0.368 0.051 0.326 -0.000 0.010  -0.041 144 ILE   AAA N   
1103 C  CA  . ILE   A 145 ? 0.361 0.082 0.343 -0.061 0.009  -0.064 144 ILE   AAA CA  
1104 C  C   . ILE   A 145 ? 0.432 0.150 0.279 -0.015 -0.008 -0.071 144 ILE   AAA C   
1105 O  O   . ILE   A 145 ? 0.414 0.172 0.305 0.015  -0.028 -0.056 144 ILE   AAA O   
1106 C  CB  . ILE   A 145 ? 0.389 0.083 0.358 -0.028 -0.022 -0.026 144 ILE   AAA CB  
1107 C  CG1 . ILE   A 145 ? 0.350 0.038 0.367 -0.008 0.014  -0.083 144 ILE   AAA CG1 
1108 C  CG2 . ILE   A 145 ? 0.415 0.218 0.398 -0.041 -0.014 0.003  144 ILE   AAA CG2 
1109 C  CD1 . ILE   A 145 ? 0.398 0.030 0.478 0.000  -0.009 -0.091 144 ILE   AAA CD1 
1110 N  N   . GLY   A 146 ? 0.367 0.206 0.333 -0.021 0.024  -0.113 145 GLY   AAA N   
1111 C  CA  . GLY   A 146 ? 0.392 0.080 0.393 -0.027 0.008  -0.095 145 GLY   AAA CA  
1112 C  C   . GLY   A 146 ? 0.359 0.154 0.301 0.061  -0.030 -0.071 145 GLY   AAA C   
1113 O  O   . GLY   A 146 ? 0.362 0.209 0.294 0.002  0.014  -0.061 145 GLY   AAA O   
1114 N  N   . VAL   A 147 ? 0.358 0.181 0.367 0.062  -0.024 -0.099 146 VAL   AAA N   
1115 C  CA  . VAL   A 147 ? 0.382 0.023 0.340 -0.030 -0.027 -0.055 146 VAL   AAA CA  
1116 C  C   . VAL   A 147 ? 0.370 0.120 0.253 -0.001 -0.049 -0.048 146 VAL   AAA C   
1117 O  O   . VAL   A 147 ? 0.398 0.078 0.289 0.021  -0.035 -0.055 146 VAL   AAA O   
1118 C  CB  . VAL   A 147 ? 0.400 0.040 0.352 -0.023 -0.026 -0.103 146 VAL   AAA CB  
1119 C  CG1 . VAL   A 147 ? 0.398 0.131 0.370 0.019  0.009  -0.083 146 VAL   AAA CG1 
1120 C  CG2 . VAL   A 147 ? 0.408 0.074 0.409 0.011  0.014  -0.035 146 VAL   AAA CG2 
1121 N  N   . LEU   A 148 ? 0.393 0.149 0.301 0.002  -0.026 -0.062 147 LEU   AAA N   
1122 C  CA  . LEU   A 148 ? 0.411 0.235 0.330 0.039  0.012  -0.057 147 LEU   AAA CA  
1123 C  C   . LEU   A 148 ? 0.401 0.135 0.257 0.055  0.011  -0.052 147 LEU   AAA C   
1124 O  O   . LEU   A 148 ? 0.418 0.170 0.317 0.014  0.048  -0.032 147 LEU   AAA O   
1125 C  CB  . LEU   A 148 ? 0.419 0.228 0.349 0.033  0.014  -0.067 147 LEU   AAA CB  
1126 C  CG  . LEU   A 148 ? 0.515 0.262 0.412 -0.047 0.080  -0.064 147 LEU   AAA CG  
1127 C  CD1 . LEU   A 148 ? 0.520 0.214 0.496 -0.043 -0.004 -0.116 147 LEU   AAA CD1 
1128 C  CD2 . LEU   A 148 ? 0.508 0.106 0.401 -0.030 0.056  -0.110 147 LEU   AAA CD2 
1129 N  N   . MET   A 149 ? 0.396 0.147 0.338 0.044  -0.016 -0.039 148 MET   AAA N   
1130 C  CA  . MET   A 149 ? 0.398 0.055 0.337 0.013  -0.014 -0.018 148 MET   AAA CA  
1131 C  C   . MET   A 149 ? 0.345 0.227 0.346 -0.000 0.007  -0.021 148 MET   AAA C   
1132 O  O   . MET   A 149 ? 0.420 0.212 0.351 0.057  -0.016 -0.042 148 MET   AAA O   
1133 C  CB  . MET   A 149 ? 0.417 0.264 0.340 0.020  0.019  -0.089 148 MET   AAA CB  
1134 C  CG  . MET   A 149 ? 0.332 0.197 0.362 -0.019 -0.040 -0.009 148 MET   AAA CG  
1135 S  SD  . MET   A 149 ? 0.405 0.194 0.365 0.006  -0.010 -0.056 148 MET   AAA SD  
1136 C  CE  . MET   A 149 ? 0.406 0.192 0.354 0.040  -0.020 -0.067 148 MET   AAA CE  
1137 N  N   . LYS   A 150 ? 0.368 0.318 0.339 0.001  0.031  -0.037 149 LYS   AAA N   
1138 C  CA  . LYS   A 150 ? 0.338 0.374 0.349 -0.060 0.073  -0.072 149 LYS   AAA CA  
1139 C  C   . LYS   A 150 ? 0.322 0.213 0.369 -0.011 0.032  -0.033 149 LYS   AAA C   
1140 O  O   . LYS   A 150 ? 0.447 0.212 0.413 -0.077 0.023  -0.067 149 LYS   AAA O   
1141 C  CB  . LYS   A 150 ? 0.391 0.330 0.340 -0.049 -0.015 -0.042 149 LYS   AAA CB  
1142 C  CG  . LYS   A 150 ? 0.428 0.274 0.422 -0.043 0.031  -0.088 149 LYS   AAA CG  
1143 C  CD  . LYS   A 150 ? 0.551 0.440 0.437 -0.046 -0.044 0.024  149 LYS   AAA CD  
1144 C  CE  . LYS   A 150 ? 0.647 0.520 0.587 -0.167 0.010  -0.032 149 LYS   AAA CE  
1145 N  NZ  . LYS   A 150 ? 0.594 0.770 0.708 0.010  0.028  -0.380 149 LYS   AAA NZ  
1146 N  N   . VAL   A 151 ? 0.424 0.243 0.387 0.044  -0.008 -0.062 150 VAL   AAA N   
1147 C  CA  . VAL   A 151 ? 0.378 0.307 0.428 0.022  0.008  -0.045 150 VAL   AAA CA  
1148 C  C   . VAL   A 151 ? 0.338 0.346 0.378 -0.038 -0.014 -0.100 150 VAL   AAA C   
1149 O  O   . VAL   A 151 ? 0.427 0.352 0.323 0.012  0.027  -0.023 150 VAL   AAA O   
1150 C  CB  . VAL   A 151 ? 0.451 0.306 0.372 0.042  0.011  -0.050 150 VAL   AAA CB  
1151 C  CG1 . VAL   A 151 ? 0.459 0.288 0.505 0.008  0.054  -0.093 150 VAL   AAA CG1 
1152 C  CG2 . VAL   A 151 ? 0.484 0.210 0.474 -0.032 0.001  -0.058 150 VAL   AAA CG2 
1153 N  N   . GLY   A 152 ? 0.386 0.291 0.423 -0.044 -0.024 -0.038 151 GLY   AAA N   
1154 C  CA  . GLY   A 152 ? 0.329 0.368 0.476 -0.015 0.015  -0.019 151 GLY   AAA CA  
1155 C  C   . GLY   A 152 ? 0.376 0.396 0.420 -0.070 -0.012 0.060  151 GLY   AAA C   
1156 O  O   . GLY   A 152 ? 0.398 0.611 0.462 -0.036 -0.072 -0.030 151 GLY   AAA O   
1157 N  N   . GLU   A 153 ? 0.471 0.298 0.381 0.003  -0.001 -0.040 152 GLU   AAA N   
1158 C  CA  . GLU   A 153 ? 0.464 0.321 0.517 -0.035 0.019  -0.049 152 GLU   AAA CA  
1159 C  C   . GLU   A 153 ? 0.441 0.457 0.381 -0.086 -0.055 -0.071 152 GLU   AAA C   
1160 O  O   . GLU   A 153 ? 0.424 0.447 0.405 -0.008 -0.011 -0.044 152 GLU   AAA O   
1161 C  CB  . GLU   A 153 ? 0.585 0.364 0.517 -0.041 0.056  -0.022 152 GLU   AAA CB  
1162 C  CG  . GLU   A 153 ? 0.689 0.472 0.666 0.019  0.100  -0.250 152 GLU   AAA CG  
1163 C  CD  . GLU   A 153 ? 0.694 0.744 0.962 -0.041 0.086  -0.190 152 GLU   AAA CD  
1164 O  OE1 . GLU   A 153 ? 0.839 0.805 1.123 0.051  -0.048 -0.342 152 GLU   AAA OE1 
1165 O  OE2 . GLU   A 153 ? 0.990 0.750 1.216 -0.142 0.073  -0.001 152 GLU   AAA OE2 
1166 N  N   . ALA   A 154 ? 0.414 0.585 0.373 -0.096 -0.003 -0.131 153 ALA   AAA N   
1167 C  CA  . ALA   A 154 ? 0.402 0.517 0.426 -0.071 0.038  -0.095 153 ALA   AAA CA  
1168 C  C   . ALA   A 154 ? 0.475 0.405 0.299 -0.152 0.012  -0.015 153 ALA   AAA C   
1169 O  O   . ALA   A 154 ? 0.468 0.425 0.328 -0.140 0.037  -0.015 153 ALA   AAA O   
1170 C  CB  . ALA   A 154 ? 0.405 0.577 0.423 -0.105 0.012  -0.066 153 ALA   AAA CB  
1171 N  N   . ASN   A 155 ? 0.423 0.257 0.432 -0.042 0.002  -0.026 154 ASN   AAA N   
1172 C  CA  . ASN   A 155 ? 0.436 0.277 0.429 -0.023 0.015  -0.096 154 ASN   AAA CA  
1173 C  C   . ASN   A 155 ? 0.464 0.236 0.379 -0.057 0.031  -0.054 154 ASN   AAA C   
1174 O  O   . ASN   A 155 ? 0.484 0.387 0.365 -0.123 0.018  -0.069 154 ASN   AAA O   
1175 C  CB  . ASN   A 155 ? 0.506 0.140 0.493 -0.038 -0.031 -0.101 154 ASN   AAA CB  
1176 C  CG  . ASN   A 155 ? 0.481 0.194 0.425 -0.029 0.001  -0.121 154 ASN   AAA CG  
1177 O  OD1 . ASN   A 155 ? 0.508 0.176 0.532 -0.070 -0.052 -0.067 154 ASN   AAA OD1 
1178 N  ND2 . ASN   A 155 ? 0.476 0.157 0.436 -0.062 0.027  -0.110 154 ASN   AAA ND2 
1179 N  N   . PRO   A 156 ? 0.548 0.212 0.524 -0.024 0.067  -0.010 155 PRO   AAA N   
1180 C  CA  . PRO   A 156 ? 0.571 0.300 0.445 -0.037 0.037  -0.036 155 PRO   AAA CA  
1181 C  C   . PRO   A 156 ? 0.549 0.336 0.344 -0.082 0.026  0.016  155 PRO   AAA C   
1182 O  O   . PRO   A 156 ? 0.670 0.269 0.417 -0.098 0.037  -0.051 155 PRO   AAA O   
1183 C  CB  . PRO   A 156 ? 0.519 0.316 0.568 -0.075 0.055  -0.047 155 PRO   AAA CB  
1184 C  CG  . PRO   A 156 ? 0.645 0.203 0.590 -0.148 0.106  -0.002 155 PRO   AAA CG  
1185 C  CD  . PRO   A 156 ? 0.615 0.192 0.493 -0.083 0.043  -0.096 155 PRO   AAA CD  
1186 N  N   . LYS   A 157 ? 0.496 0.128 0.451 -0.018 0.006  -0.014 156 LYS   AAA N   
1187 C  CA  . LYS   A 157 ? 0.472 0.331 0.463 -0.062 0.050  -0.012 156 LYS   AAA CA  
1188 C  C   . LYS   A 157 ? 0.418 0.436 0.440 0.020  0.062  -0.021 156 LYS   AAA C   
1189 O  O   . LYS   A 157 ? 0.443 0.343 0.458 -0.075 0.073  -0.109 156 LYS   AAA O   
1190 C  CB  . LYS   A 157 ? 0.507 0.450 0.486 -0.013 0.002  0.016  156 LYS   AAA CB  
1191 C  CG  . LYS   A 157 ? 0.583 0.570 0.557 0.120  0.035  0.129  156 LYS   AAA CG  
1192 C  CD  . LYS   A 157 ? 0.686 0.497 0.795 0.010  0.051  0.175  156 LYS   AAA CD  
1193 C  CE  . LYS   A 157 ? 0.947 0.757 0.721 0.093  0.161  0.243  156 LYS   AAA CE  
1194 N  NZ  . LYS   A 157 ? 0.938 0.896 1.062 0.140  0.207  0.373  156 LYS   AAA NZ  
1195 N  N   . LEU   A 158 ? 0.420 0.233 0.389 -0.047 0.025  -0.106 157 LEU   AAA N   
1196 C  CA  . LEU   A 158 ? 0.503 0.335 0.390 -0.019 0.089  -0.105 157 LEU   AAA CA  
1197 C  C   . LEU   A 158 ? 0.544 0.265 0.432 -0.049 0.046  -0.056 157 LEU   AAA C   
1198 O  O   . LEU   A 158 ? 0.543 0.335 0.483 -0.120 0.052  -0.009 157 LEU   AAA O   
1199 C  CB  . LEU   A 158 ? 0.462 0.436 0.470 0.059  0.052  -0.093 157 LEU   AAA CB  
1200 C  CG  . LEU   A 158 ? 0.427 0.469 0.473 0.043  0.002  -0.087 157 LEU   AAA CG  
1201 C  CD1 . LEU   A 158 ? 0.467 0.424 0.449 0.042  -0.021 -0.050 157 LEU   AAA CD1 
1202 C  CD2 . LEU   A 158 ? 0.462 0.483 0.599 -0.007 0.038  -0.108 157 LEU   AAA CD2 
1203 N  N   . GLN   A 159 ? 0.467 0.652 0.426 -0.240 0.009  0.027  158 GLN   AAA N   
1204 C  CA  . GLN   A 159 ? 0.485 0.608 0.480 -0.167 0.012  -0.098 158 GLN   AAA CA  
1205 C  C   . GLN   A 159 ? 0.469 0.416 0.488 -0.158 0.043  0.049  158 GLN   AAA C   
1206 O  O   . GLN   A 159 ? 0.557 0.500 0.424 -0.168 0.042  -0.016 158 GLN   AAA O   
1207 C  CB  . GLN   A 159 ? 0.512 0.636 0.563 -0.123 0.014  -0.041 158 GLN   AAA CB  
1208 C  CG  . GLN   A 159 ? 0.423 0.896 0.646 -0.174 0.013  0.030  158 GLN   AAA CG  
1209 C  CD  . GLN   A 159 ? 0.514 0.862 0.665 -0.072 -0.033 -0.048 158 GLN   AAA CD  
1210 O  OE1 . GLN   A 159 ? 0.584 0.502 0.783 -0.103 -0.094 -0.158 158 GLN   AAA OE1 
1211 N  NE2 . GLN   A 159 ? 0.729 0.715 0.560 -0.153 -0.120 -0.267 158 GLN   AAA NE2 
1212 N  N   . LYS   A 160 ? 0.517 0.426 0.406 -0.127 0.009  -0.073 159 LYS   AAA N   
1213 C  CA  . LYS   A 160 ? 0.398 0.374 0.485 -0.136 0.040  -0.058 159 LYS   AAA CA  
1214 C  C   . LYS   A 160 ? 0.508 0.308 0.500 -0.116 -0.020 -0.064 159 LYS   AAA C   
1215 O  O   . LYS   A 160 ? 0.610 0.134 0.542 -0.125 -0.004 0.003  159 LYS   AAA O   
1216 C  CB  . LYS   A 160 ? 0.455 0.549 0.529 -0.063 0.016  -0.046 159 LYS   AAA CB  
1217 C  CG  . LYS   A 160 ? 0.656 0.570 0.621 -0.018 0.059  -0.094 159 LYS   AAA CG  
1218 C  CD  . LYS   A 160 ? 0.714 0.435 0.651 0.048  0.114  -0.101 159 LYS   AAA CD  
1219 C  CE  . LYS   A 160 ? 0.690 0.217 0.652 -0.130 0.068  -0.238 159 LYS   AAA CE  
1220 N  NZ  . LYS   A 160 ? 0.785 0.039 0.573 -0.096 0.049  -0.089 159 LYS   AAA NZ  
1221 N  N   . VAL   A 161 ? 0.456 0.331 0.398 -0.076 -0.004 -0.048 160 VAL   AAA N   
1222 C  CA  . VAL   A 161 ? 0.415 0.229 0.392 -0.066 0.023  -0.073 160 VAL   AAA CA  
1223 C  C   . VAL   A 161 ? 0.370 0.277 0.363 -0.075 0.016  -0.110 160 VAL   AAA C   
1224 O  O   . VAL   A 161 ? 0.410 0.338 0.413 -0.070 0.046  -0.077 160 VAL   AAA O   
1225 C  CB  . VAL   A 161 ? 0.470 0.278 0.336 -0.078 -0.027 -0.041 160 VAL   AAA CB  
1226 C  CG1 . VAL   A 161 ? 0.646 0.247 0.416 -0.167 -0.007 -0.044 160 VAL   AAA CG1 
1227 C  CG2 . VAL   A 161 ? 0.478 0.231 0.430 -0.083 -0.053 -0.081 160 VAL   AAA CG2 
1228 N  N   . LEU   A 162 ? 0.377 0.431 0.419 -0.031 0.010  -0.069 161 LEU   AAA N   
1229 C  CA  . LEU   A 162 ? 0.422 0.386 0.467 0.057  0.034  -0.075 161 LEU   AAA CA  
1230 C  C   . LEU   A 162 ? 0.402 0.354 0.400 0.048  0.030  -0.024 161 LEU   AAA C   
1231 O  O   . LEU   A 162 ? 0.402 0.521 0.356 0.023  0.002  -0.056 161 LEU   AAA O   
1232 C  CB  . LEU   A 162 ? 0.472 0.526 0.398 0.012  0.046  -0.045 161 LEU   AAA CB  
1233 C  CG  . LEU   A 162 ? 0.501 0.583 0.467 0.049  -0.008 -0.082 161 LEU   AAA CG  
1234 C  CD1 . LEU   A 162 ? 0.521 0.749 0.564 0.051  0.060  -0.111 161 LEU   AAA CD1 
1235 C  CD2 . LEU   A 162 ? 0.706 0.543 0.453 0.151  -0.000 -0.038 161 LEU   AAA CD2 
1236 N  N   . ASP   A 163 ? 0.418 0.391 0.388 -0.039 0.013  -0.025 162 ASP   AAA N   
1237 C  CA  . ASP   A 163 ? 0.388 0.383 0.481 -0.059 0.027  -0.088 162 ASP   AAA CA  
1238 C  C   . ASP   A 163 ? 0.418 0.467 0.456 -0.082 -0.033 -0.055 162 ASP   AAA C   
1239 O  O   . ASP   A 163 ? 0.428 0.576 0.469 -0.054 -0.031 -0.100 162 ASP   AAA O   
1240 C  CB  . ASP   A 163 ? 0.495 0.416 0.512 -0.087 0.002  -0.114 162 ASP   AAA CB  
1241 C  CG  . ASP   A 163 ? 0.482 0.466 0.579 -0.104 0.029  -0.046 162 ASP   AAA CG  
1242 O  OD1 . ASP   A 163 ? 0.437 0.535 0.715 -0.107 0.038  -0.045 162 ASP   AAA OD1 
1243 O  OD2 . ASP   A 163 ? 0.612 0.440 0.637 -0.195 0.114  -0.116 162 ASP   AAA OD2 
1244 N  N   . ALA   A 164 ? 0.388 0.360 0.423 -0.055 -0.013 -0.088 163 ALA   AAA N   
1245 C  CA  . ALA   A 164 ? 0.431 0.381 0.421 -0.023 -0.007 -0.105 163 ALA   AAA CA  
1246 C  C   . ALA   A 164 ? 0.347 0.358 0.387 0.022  -0.000 -0.095 163 ALA   AAA C   
1247 O  O   . ALA   A 164 ? 0.465 0.240 0.414 -0.001 0.022  -0.091 163 ALA   AAA O   
1248 C  CB  . ALA   A 164 ? 0.418 0.403 0.349 -0.052 -0.022 -0.085 163 ALA   AAA CB  
1249 N  N   . LEU   A 165 ? 0.409 0.432 0.433 0.070  0.004  -0.113 164 LEU   AAA N   
1250 C  CA  . LEU   A 165 ? 0.394 0.441 0.415 0.039  -0.009 -0.098 164 LEU   AAA CA  
1251 C  C   . LEU   A 165 ? 0.383 0.447 0.382 0.022  0.019  -0.080 164 LEU   AAA C   
1252 O  O   . LEU   A 165 ? 0.424 0.303 0.396 -0.003 -0.018 -0.106 164 LEU   AAA O   
1253 C  CB  . LEU   A 165 ? 0.442 0.330 0.446 0.018  -0.093 -0.135 164 LEU   AAA CB  
1254 C  CG  . LEU   A 165 ? 0.490 0.305 0.393 0.027  -0.059 -0.085 164 LEU   AAA CG  
1255 C  CD1 . LEU   A 165 ? 0.584 0.172 0.467 -0.092 -0.046 -0.132 164 LEU   AAA CD1 
1256 C  CD2 . LEU   A 165 ? 0.540 0.249 0.413 0.030  -0.017 -0.092 164 LEU   AAA CD2 
1257 N  N   . GLN   A 166 ? 0.435 0.352 0.467 0.048  -0.015 -0.125 165 GLN   AAA N   
1258 C  CA  . GLN   A 166 ? 0.416 0.363 0.421 0.001  -0.016 -0.057 165 GLN   AAA CA  
1259 C  C   . GLN   A 166 ? 0.400 0.390 0.420 -0.017 -0.026 -0.094 165 GLN   AAA C   
1260 O  O   . GLN   A 166 ? 0.499 0.230 0.435 0.042  -0.040 -0.024 165 GLN   AAA O   
1261 C  CB  . GLN   A 166 ? 0.478 0.323 0.530 -0.025 -0.057 -0.104 165 GLN   AAA CB  
1262 C  CG  . GLN   A 166 ? 0.542 0.450 0.495 -0.080 -0.125 0.026  165 GLN   AAA CG  
1263 C  CD  . GLN   A 166 ? 0.726 0.518 0.746 0.086  -0.071 -0.017 165 GLN   AAA CD  
1264 O  OE1 . GLN   A 166 ? 0.601 0.534 0.825 0.000  -0.261 -0.056 165 GLN   AAA OE1 
1265 N  NE2 . GLN   A 166 ? 0.777 0.665 0.650 -0.054 0.008  0.336  165 GLN   AAA NE2 
1266 N  N   . ALA   A 167 ? 0.437 0.285 0.496 -0.009 -0.037 -0.104 166 ALA   AAA N   
1267 C  CA  . ALA   A 167 ? 0.404 0.342 0.497 0.071  -0.033 -0.037 166 ALA   AAA CA  
1268 C  C   . ALA   A 167 ? 0.434 0.399 0.327 0.043  -0.006 -0.093 166 ALA   AAA C   
1269 O  O   . ALA   A 167 ? 0.469 0.364 0.370 0.049  0.026  -0.139 166 ALA   AAA O   
1270 C  CB  . ALA   A 167 ? 0.567 0.266 0.454 0.017  0.019  -0.007 166 ALA   AAA CB  
1271 N  N   . ILE   A 168 ? 0.358 0.293 0.410 0.005  0.002  -0.070 167 ILE   AAA N   
1272 C  CA  . ILE   A 168 ? 0.422 0.242 0.460 0.014  -0.014 -0.074 167 ILE   AAA CA  
1273 C  C   . ILE   A 168 ? 0.358 0.254 0.400 0.043  -0.032 -0.019 167 ILE   AAA C   
1274 O  O   . ILE   A 168 ? 0.397 0.511 0.424 -0.048 -0.066 -0.116 167 ILE   AAA O   
1275 C  CB  . ILE   A 168 ? 0.358 0.201 0.427 -0.013 0.023  -0.016 167 ILE   AAA CB  
1276 C  CG1 . ILE   A 168 ? 0.451 0.302 0.382 -0.003 -0.024 -0.100 167 ILE   AAA CG1 
1277 C  CG2 . ILE   A 168 ? 0.440 0.309 0.442 0.068  0.002  -0.055 167 ILE   AAA CG2 
1278 C  CD1 . ILE   A 168 ? 0.438 0.329 0.416 0.014  -0.041 -0.052 167 ILE   AAA CD1 
1279 N  N   . LYS   A 169 ? 0.353 0.379 0.411 -0.033 -0.010 -0.081 168 LYS   AAA N   
1280 C  CA  . LYS   A 169 ? 0.380 0.390 0.373 -0.003 0.043  -0.082 168 LYS   AAA CA  
1281 C  C   . LYS   A 169 ? 0.345 0.341 0.341 0.011  0.001  -0.055 168 LYS   AAA C   
1282 O  O   . LYS   A 169 ? 0.382 0.403 0.415 0.025  0.017  -0.078 168 LYS   AAA O   
1283 C  CB  . LYS   A 169 ? 0.507 0.680 0.391 -0.032 -0.052 -0.121 168 LYS   AAA CB  
1284 C  CG  . LYS   A 169 ? 0.481 0.863 0.658 -0.052 0.015  -0.176 168 LYS   AAA CG  
1285 C  CD  . LYS   A 169 ? 0.629 0.945 0.752 0.055  -0.005 -0.284 168 LYS   AAA CD  
1286 C  CE  . LYS   A 169 ? 0.731 0.773 0.642 0.207  0.000  -0.263 168 LYS   AAA CE  
1287 N  NZ  . LYS   A 169 ? 0.654 0.479 0.766 0.146  -0.192 -0.224 168 LYS   AAA NZ  
1288 N  N   . THR   A 170 ? 0.387 0.139 0.380 0.069  0.002  -0.096 169 THR   AAA N   
1289 C  CA  . THR   A 170 ? 0.380 0.330 0.364 0.011  -0.016 -0.032 169 THR   AAA CA  
1290 C  C   . THR   A 170 ? 0.398 0.347 0.424 0.040  -0.010 -0.085 169 THR   AAA C   
1291 O  O   . THR   A 170 ? 0.372 0.405 0.425 0.045  -0.001 -0.047 169 THR   AAA O   
1292 C  CB  . THR   A 170 ? 0.400 0.342 0.400 0.025  -0.073 -0.043 169 THR   AAA CB  
1293 O  OG1 . THR   A 170 ? 0.401 0.371 0.384 -0.004 -0.005 -0.061 169 THR   AAA OG1 
1294 C  CG2 . THR   A 170 ? 0.398 0.386 0.340 -0.018 -0.056 0.055  169 THR   AAA CG2 
1295 N  N   . LYS   A 171 ? 0.367 0.405 0.405 0.007  0.012  -0.072 170 LYS   AAA N   
1296 C  CA  . LYS   A 171 ? 0.391 0.380 0.403 -0.063 0.023  -0.042 170 LYS   AAA CA  
1297 C  C   . LYS   A 171 ? 0.399 0.430 0.386 0.010  -0.014 -0.034 170 LYS   AAA C   
1298 O  O   . LYS   A 171 ? 0.399 0.591 0.407 -0.002 -0.000 -0.088 170 LYS   AAA O   
1299 C  CB  . LYS   A 171 ? 0.419 0.393 0.436 -0.016 0.049  0.030  170 LYS   AAA CB  
1300 C  CG  . LYS   A 171 ? 0.426 0.409 0.410 -0.093 0.010  -0.063 170 LYS   AAA CG  
1301 C  CD  . LYS   A 171 ? 0.482 0.399 0.496 -0.105 0.006  0.019  170 LYS   AAA CD  
1302 C  CE  . LYS   A 171 ? 0.529 0.483 0.722 -0.130 -0.037 -0.035 170 LYS   AAA CE  
1303 N  NZ  . LYS   A 171 ? 0.663 0.505 0.946 -0.227 0.001  0.122  170 LYS   AAA NZ  
1304 N  N   . GLY   A 172 ? 0.404 0.462 0.362 0.010  0.000  -0.003 171 GLY   AAA N   
1305 C  CA  . GLY   A 172 ? 0.406 0.534 0.405 -0.023 0.038  -0.030 171 GLY   AAA CA  
1306 C  C   . GLY   A 172 ? 0.336 0.468 0.419 0.050  0.014  -0.031 171 GLY   AAA C   
1307 O  O   . GLY   A 172 ? 0.382 0.457 0.526 0.041  0.039  -0.015 171 GLY   AAA O   
1308 N  N   . LYS   A 173 ? 0.362 0.368 0.405 0.013  -0.025 -0.022 172 LYS   AAA N   
1309 C  CA  . LYS   A 173 ? 0.446 0.351 0.394 0.021  -0.020 -0.014 172 LYS   AAA CA  
1310 C  C   . LYS   A 173 ? 0.439 0.449 0.348 0.083  -0.026 -0.117 172 LYS   AAA C   
1311 O  O   . LYS   A 173 ? 0.406 0.461 0.390 -0.002 0.014  -0.146 172 LYS   AAA O   
1312 C  CB  . LYS   A 173 ? 0.446 0.289 0.487 0.004  -0.038 -0.009 172 LYS   AAA CB  
1313 C  CG  . LYS   A 173 ? 0.450 0.494 0.515 -0.007 -0.025 0.017  172 LYS   AAA CG  
1314 C  CD  . LYS   A 173 ? 0.477 0.698 0.622 -0.054 -0.070 -0.195 172 LYS   AAA CD  
1315 C  CE  . LYS   A 173 ? 0.515 0.729 0.760 -0.125 -0.088 -0.081 172 LYS   AAA CE  
1316 N  NZ  . LYS   A 173 ? 0.590 0.649 0.540 -0.164 -0.066 -0.053 172 LYS   AAA NZ  
1317 N  N   . ARG   A 174 ? 0.436 0.357 0.354 0.008  -0.011 -0.097 173 ARG   AAA N   
1318 C  CA  . ARG   A 174 ? 0.507 0.307 0.373 -0.039 -0.098 -0.120 173 ARG   AAA CA  
1319 C  C   . ARG   A 174 ? 0.484 0.405 0.350 -0.172 -0.011 -0.053 173 ARG   AAA C   
1320 O  O   . ARG   A 174 ? 0.522 0.311 0.397 -0.030 -0.025 -0.115 173 ARG   AAA O   
1321 C  CB  . ARG   A 174 ? 0.522 0.573 0.465 -0.050 -0.041 -0.108 173 ARG   AAA CB  
1322 C  CG  . ARG   A 174 ? 0.625 0.885 0.496 -0.023 0.016  -0.090 173 ARG   AAA CG  
1323 C  CD  . ARG   A 174 ? 0.621 0.837 0.576 -0.128 0.075  -0.048 173 ARG   AAA CD  
1324 N  NE  . ARG   A 174 ? 0.608 0.752 0.646 -0.064 0.116  -0.127 173 ARG   AAA NE  
1325 C  CZ  . ARG   A 174 ? 0.451 0.736 0.699 0.075  0.016  0.122  173 ARG   AAA CZ  
1326 N  NH1 . ARG   A 174 ? 0.691 0.678 0.670 0.324  0.291  0.208  173 ARG   AAA NH1 
1327 N  NH2 . ARG   A 174 ? 0.545 0.718 0.683 0.048  0.052  0.252  173 ARG   AAA NH2 
1328 N  N   . ALA   A 175 ? 0.414 0.325 0.367 -0.111 -0.005 -0.074 174 ALA   AAA N   
1329 C  CA  . ALA   A 175 ? 0.407 0.278 0.386 -0.063 0.031  -0.106 174 ALA   AAA CA  
1330 C  C   . ALA   A 175 ? 0.463 0.354 0.414 -0.122 -0.036 -0.095 174 ALA   AAA C   
1331 O  O   . ALA   A 175 ? 0.467 0.271 0.435 -0.086 0.007  -0.150 174 ALA   AAA O   
1332 C  CB  . ALA   A 175 ? 0.417 0.283 0.451 -0.080 -0.008 -0.129 174 ALA   AAA CB  
1333 N  N   . PRO   A 176 ? 0.507 0.344 0.406 -0.069 -0.049 -0.157 175 PRO   AAA N   
1334 C  CA  . PRO   A 176 ? 0.487 0.155 0.424 -0.160 -0.013 -0.172 175 PRO   AAA CA  
1335 C  C   . PRO   A 176 ? 0.419 0.218 0.441 -0.120 -0.013 -0.103 175 PRO   AAA C   
1336 O  O   . PRO   A 176 ? 0.413 0.302 0.475 -0.132 0.003  -0.080 175 PRO   AAA O   
1337 C  CB  . PRO   A 176 ? 0.519 0.172 0.485 -0.089 -0.002 -0.230 175 PRO   AAA CB  
1338 C  CG  . PRO   A 176 ? 0.536 0.454 0.459 -0.044 -0.004 -0.219 175 PRO   AAA CG  
1339 C  CD  . PRO   A 176 ? 0.549 0.364 0.438 -0.066 0.016  -0.216 175 PRO   AAA CD  
1340 N  N   . PHE   A 177 ? 0.456 0.197 0.373 -0.120 0.016  -0.075 176 PHE   AAA N   
1341 C  CA  . PHE   A 177 ? 0.456 0.087 0.401 -0.071 0.001  -0.115 176 PHE   AAA CA  
1342 C  C   . PHE   A 177 ? 0.419 0.160 0.442 -0.078 0.045  -0.060 176 PHE   AAA C   
1343 O  O   . PHE   A 177 ? 0.440 0.035 0.553 -0.051 0.010  -0.101 176 PHE   AAA O   
1344 C  CB  . PHE   A 177 ? 0.413 0.088 0.468 0.008  -0.004 -0.116 176 PHE   AAA CB  
1345 C  CG  . PHE   A 177 ? 0.422 0.135 0.443 -0.027 0.010  -0.072 176 PHE   AAA CG  
1346 C  CD1 . PHE   A 177 ? 0.456 0.128 0.440 -0.068 0.029  -0.071 176 PHE   AAA CD1 
1347 C  CD2 . PHE   A 177 ? 0.415 0.174 0.382 -0.071 0.019  -0.007 176 PHE   AAA CD2 
1348 C  CE1 . PHE   A 177 ? 0.456 0.233 0.451 -0.104 0.003  -0.074 176 PHE   AAA CE1 
1349 C  CE2 . PHE   A 177 ? 0.458 0.274 0.446 0.011  0.064  -0.028 176 PHE   AAA CE2 
1350 C  CZ  . PHE   A 177 ? 0.471 0.048 0.499 -0.061 0.005  -0.010 176 PHE   AAA CZ  
1351 N  N   . THR   A 178 ? 0.442 0.139 0.489 -0.114 0.034  -0.131 177 THR   AAA N   
1352 C  CA  . THR   A 178 ? 0.468 0.165 0.421 -0.045 0.086  -0.127 177 THR   AAA CA  
1353 C  C   . THR   A 178 ? 0.445 0.141 0.382 -0.037 0.036  -0.112 177 THR   AAA C   
1354 O  O   . THR   A 178 ? 0.450 0.330 0.464 -0.080 0.081  -0.135 177 THR   AAA O   
1355 C  CB  . THR   A 178 ? 0.467 0.199 0.443 -0.083 0.070  -0.165 177 THR   AAA CB  
1356 O  OG1 . THR   A 178 ? 0.564 0.368 0.561 -0.209 0.053  -0.147 177 THR   AAA OG1 
1357 C  CG2 . THR   A 178 ? 0.550 0.223 0.452 -0.045 0.080  -0.147 177 THR   AAA CG2 
1358 N  N   . ASN   A 179 ? 0.535 0.217 0.360 -0.115 -0.013 -0.084 178 ASN   AAA N   
1359 C  CA  . ASN   A 179 ? 0.556 0.129 0.392 -0.179 0.033  -0.096 178 ASN   AAA CA  
1360 C  C   . ASN   A 179 ? 0.406 0.242 0.385 -0.133 0.062  -0.074 178 ASN   AAA C   
1361 O  O   . ASN   A 179 ? 0.422 0.165 0.520 -0.100 0.071  -0.094 178 ASN   AAA O   
1362 C  CB  . ASN   A 179 ? 0.685 0.025 0.477 -0.052 0.047  -0.086 178 ASN   AAA CB  
1363 C  CG  . ASN   A 179 ? 0.648 0.287 0.404 -0.171 -0.024 0.035  178 ASN   AAA CG  
1364 O  OD1 . ASN   A 179 ? 0.595 0.150 0.606 -0.184 -0.019 -0.061 178 ASN   AAA OD1 
1365 N  ND2 . ASN   A 179 ? 0.716 0.214 0.492 -0.187 0.118  -0.018 178 ASN   AAA ND2 
1366 N  N   . PHE   A 180 ? 0.543 0.043 0.422 -0.079 0.088  -0.058 179 PHE   AAA N   
1367 C  CA  . PHE   A 180 ? 0.468 0.244 0.362 -0.039 0.078  -0.091 179 PHE   AAA CA  
1368 C  C   . PHE   A 180 ? 0.476 0.031 0.396 -0.012 0.076  -0.098 179 PHE   AAA C   
1369 O  O   . PHE   A 180 ? 0.473 0.140 0.454 -0.040 0.086  -0.087 179 PHE   AAA O   
1370 C  CB  . PHE   A 180 ? 0.490 0.279 0.367 -0.014 0.009  -0.068 179 PHE   AAA CB  
1371 C  CG  . PHE   A 180 ? 0.460 0.248 0.413 -0.085 0.010  -0.139 179 PHE   AAA CG  
1372 C  CD1 . PHE   A 180 ? 0.509 0.213 0.450 -0.052 0.070  -0.080 179 PHE   AAA CD1 
1373 C  CD2 . PHE   A 180 ? 0.406 0.160 0.494 -0.052 0.093  -0.088 179 PHE   AAA CD2 
1374 C  CE1 . PHE   A 180 ? 0.458 0.233 0.570 -0.067 0.083  -0.141 179 PHE   AAA CE1 
1375 C  CE2 . PHE   A 180 ? 0.455 0.187 0.386 -0.048 0.100  -0.060 179 PHE   AAA CE2 
1376 C  CZ  . PHE   A 180 ? 0.481 0.201 0.394 -0.058 0.109  -0.095 179 PHE   AAA CZ  
1377 N  N   . ASP   A 181 ? 0.547 0.069 0.384 -0.038 0.043  -0.041 180 ASP   AAA N   
1378 C  CA  . ASP   A 181 ? 0.502 0.163 0.430 0.016  -0.003 -0.048 180 ASP   AAA CA  
1379 C  C   . ASP   A 181 ? 0.423 0.117 0.538 -0.113 0.097  -0.088 180 ASP   AAA C   
1380 O  O   . ASP   A 181 ? 0.493 0.057 0.447 -0.103 0.077  -0.105 180 ASP   AAA O   
1381 C  CB  . ASP   A 181 ? 0.494 0.093 0.457 -0.019 0.021  -0.059 180 ASP   AAA CB  
1382 C  CG  . ASP   A 181 ? 0.509 0.198 0.387 -0.081 0.037  0.064  180 ASP   AAA CG  
1383 O  OD1 . ASP   A 181 ? 0.504 0.175 0.435 -0.074 0.015  -0.050 180 ASP   AAA OD1 
1384 O  OD2 . ASP   A 181 ? 0.708 0.062 0.476 -0.007 0.040  0.067  180 ASP   AAA OD2 
1385 N  N   . PRO   A 182 ? 0.444 0.065 0.357 -0.044 0.030  -0.039 181 PRO   AAA N   
1386 C  CA  . PRO   A 182 ? 0.433 0.200 0.382 0.095  0.025  -0.067 181 PRO   AAA CA  
1387 C  C   . PRO   A 182 ? 0.407 0.231 0.348 0.020  0.032  -0.025 181 PRO   AAA C   
1388 O  O   . PRO   A 182 ? 0.450 0.196 0.456 0.003  0.051  -0.061 181 PRO   AAA O   
1389 C  CB  . PRO   A 182 ? 0.464 0.229 0.432 -0.013 0.014  -0.071 181 PRO   AAA CB  
1390 C  CG  . PRO   A 182 ? 0.467 0.016 0.434 -0.058 0.045  0.026  181 PRO   AAA CG  
1391 C  CD  . PRO   A 182 ? 0.422 0.013 0.417 -0.053 0.048  0.006  181 PRO   AAA CD  
1392 N  N   . SER   A 183 ? 0.432 0.229 0.363 -0.008 -0.018 -0.054 182 SER   AAA N   
1393 C  CA  . SER   A 183 ? 0.454 0.242 0.371 -0.006 -0.016 -0.036 182 SER   AAA CA  
1394 C  C   . SER   A 183 ? 0.438 0.196 0.318 -0.007 -0.033 -0.012 182 SER   AAA C   
1395 O  O   . SER   A 183 ? 0.508 0.205 0.363 -0.020 0.015  -0.038 182 SER   AAA O   
1396 C  CB  . SER   A 183 ? 0.462 0.094 0.431 -0.017 0.037  -0.049 182 SER   AAA CB  
1397 O  OG  . SER   A 183 ? 0.606 0.060 0.473 -0.016 0.075  -0.020 182 SER   AAA OG  
1398 N  N   . THR   A 184 ? 0.459 0.079 0.362 -0.015 0.014  -0.047 183 THR   AAA N   
1399 C  CA  . THR   A 184 ? 0.451 0.127 0.403 0.002  0.008  -0.023 183 THR   AAA CA  
1400 C  C   . THR   A 184 ? 0.432 0.195 0.374 0.045  0.057  -0.046 183 THR   AAA C   
1401 O  O   . THR   A 184 ? 0.478 0.081 0.426 -0.002 0.064  -0.050 183 THR   AAA O   
1402 C  CB  . THR   A 184 ? 0.473 0.172 0.409 0.069  0.002  -0.069 183 THR   AAA CB  
1403 O  OG1 . THR   A 184 ? 0.527 0.220 0.400 -0.004 0.020  -0.048 183 THR   AAA OG1 
1404 C  CG2 . THR   A 184 ? 0.575 0.038 0.505 -0.038 0.053  -0.045 183 THR   AAA CG2 
1405 N  N   . LEU   A 185 ? 0.418 0.197 0.381 0.024  0.019  -0.035 184 LEU   AAA N   
1406 C  CA  . LEU   A 185 ? 0.429 0.195 0.346 0.047  0.000  -0.052 184 LEU   AAA CA  
1407 C  C   . LEU   A 185 ? 0.339 0.233 0.307 0.041  0.022  -0.043 184 LEU   AAA C   
1408 O  O   . LEU   A 185 ? 0.445 0.147 0.409 0.040  0.017  -0.088 184 LEU   AAA O   
1409 C  CB  . LEU   A 185 ? 0.481 0.292 0.323 0.007  -0.018 -0.048 184 LEU   AAA CB  
1410 C  CG  . LEU   A 185 ? 0.484 0.206 0.351 0.061  -0.022 -0.070 184 LEU   AAA CG  
1411 C  CD1 . LEU   A 185 ? 0.580 0.183 0.355 0.021  -0.007 -0.077 184 LEU   AAA CD1 
1412 C  CD2 . LEU   A 185 ? 0.481 0.344 0.385 0.076  -0.072 -0.096 184 LEU   AAA CD2 
1413 N  N   . LEU   A 186 ? 0.372 0.270 0.382 -0.012 -0.031 -0.063 185 LEU   AAA N   
1414 C  CA  . LEU   A 186 ? 0.366 0.195 0.407 -0.063 -0.011 -0.062 185 LEU   AAA CA  
1415 C  C   . LEU   A 186 ? 0.437 0.190 0.363 -0.055 -0.001 -0.104 185 LEU   AAA C   
1416 O  O   . LEU   A 186 ? 0.477 0.194 0.440 -0.042 0.025  -0.066 185 LEU   AAA O   
1417 C  CB  . LEU   A 186 ? 0.386 0.138 0.467 -0.050 -0.002 -0.041 185 LEU   AAA CB  
1418 C  CG  . LEU   A 186 ? 0.398 0.017 0.439 -0.048 0.006  0.001  185 LEU   AAA CG  
1419 C  CD1 . LEU   A 186 ? 0.441 0.142 0.458 0.033  -0.021 -0.076 185 LEU   AAA CD1 
1420 C  CD2 . LEU   A 186 ? 0.468 0.026 0.366 -0.069 0.030  -0.062 185 LEU   AAA CD2 
1421 N  N   . PRO   A 187 ? 0.421 0.100 0.393 -0.053 0.022  -0.058 186 PRO   AAA N   
1422 C  CA  . PRO   A 187 ? 0.518 0.052 0.400 -0.011 0.049  -0.061 186 PRO   AAA CA  
1423 C  C   . PRO   A 187 ? 0.532 0.312 0.346 0.018  -0.007 0.001  186 PRO   AAA C   
1424 O  O   . PRO   A 187 ? 0.556 0.300 0.435 0.030  -0.023 -0.064 186 PRO   AAA O   
1425 C  CB  . PRO   A 187 ? 0.511 0.064 0.364 0.018  0.070  -0.075 186 PRO   AAA CB  
1426 C  CG  . PRO   A 187 ? 0.484 0.169 0.392 0.039  0.046  -0.062 186 PRO   AAA CG  
1427 C  CD  . PRO   A 187 ? 0.460 0.097 0.334 -0.062 0.014  -0.006 186 PRO   AAA CD  
1428 N  N   . SER   A 188 ? 0.493 0.336 0.351 -0.017 0.001  -0.032 187 SER   AAA N   
1429 C  CA  . SER   A 188 ? 0.635 0.277 0.422 -0.010 0.042  -0.017 187 SER   AAA CA  
1430 C  C   . SER   A 188 ? 0.633 0.229 0.484 0.048  0.035  0.005  187 SER   AAA C   
1431 O  O   . SER   A 188 ? 0.592 0.355 0.593 0.068  -0.014 -0.137 187 SER   AAA O   
1432 C  CB  . SER   A 188 ? 0.549 0.576 0.600 -0.032 0.061  0.048  187 SER   AAA CB  
1433 O  OG  . SER   A 188 ? 0.638 0.663 0.677 0.041  0.096  0.179  187 SER   AAA OG  
1434 N  N   . SER   A 189 ? 0.516 0.287 0.465 -0.063 0.014  -0.114 188 SER   AAA N   
1435 C  CA  . SER   A 189 ? 0.499 0.337 0.433 -0.035 0.000  -0.059 188 SER   AAA CA  
1436 C  C   . SER   A 189 ? 0.501 0.319 0.382 -0.002 -0.044 -0.029 188 SER   AAA C   
1437 O  O   . SER   A 189 ? 0.522 0.176 0.491 0.057  0.008  0.007  188 SER   AAA O   
1438 C  CB  . SER   A 189 ? 0.541 0.434 0.405 -0.013 -0.053 -0.090 188 SER   AAA CB  
1439 O  OG  . SER   A 189 ? 0.515 0.342 0.384 0.011  -0.013 -0.004 188 SER   AAA OG  
1440 N  N   . LEU   A 190 ? 0.539 0.223 0.477 0.021  -0.036 -0.064 189 LEU   AAA N   
1441 C  CA  . LEU   A 190 ? 0.559 0.318 0.447 0.020  -0.018 -0.098 189 LEU   AAA CA  
1442 C  C   . LEU   A 190 ? 0.537 0.159 0.487 0.053  -0.009 -0.057 189 LEU   AAA C   
1443 O  O   . LEU   A 190 ? 0.524 0.190 0.522 0.008  -0.014 -0.075 189 LEU   AAA O   
1444 C  CB  . LEU   A 190 ? 0.608 0.097 0.491 -0.016 -0.002 -0.011 189 LEU   AAA CB  
1445 C  CG  . LEU   A 190 ? 0.560 0.272 0.490 0.113  -0.096 -0.094 189 LEU   AAA CG  
1446 C  CD1 . LEU   A 190 ? 0.581 0.165 0.548 0.089  -0.083 -0.068 189 LEU   AAA CD1 
1447 C  CD2 . LEU   A 190 ? 0.645 0.355 0.485 0.151  -0.068 -0.021 189 LEU   AAA CD2 
1448 N  N   . ASP   A 191 ? 0.529 0.308 0.382 -0.046 -0.025 -0.007 190 ASP   AAA N   
1449 C  CA  . ASP   A 191 ? 0.497 0.266 0.431 -0.023 0.036  -0.066 190 ASP   AAA CA  
1450 C  C   . ASP   A 191 ? 0.372 0.310 0.368 0.016  -0.013 -0.063 190 ASP   AAA C   
1451 O  O   . ASP   A 191 ? 0.427 0.362 0.374 0.083  -0.016 -0.089 190 ASP   AAA O   
1452 C  CB  . ASP   A 191 ? 0.496 0.250 0.371 -0.043 0.016  -0.036 190 ASP   AAA CB  
1453 C  CG  . ASP   A 191 ? 0.517 0.408 0.388 0.010  0.012  0.004  190 ASP   AAA CG  
1454 O  OD1 . ASP   A 191 ? 0.555 0.364 0.413 0.000  -0.012 0.060  190 ASP   AAA OD1 
1455 O  OD2 . ASP   A 191 ? 0.639 0.447 0.369 -0.165 0.051  -0.018 190 ASP   AAA OD2 
1456 N  N   . PHE   A 192 ? 0.432 0.277 0.342 -0.002 -0.014 -0.121 191 PHE   AAA N   
1457 C  CA  . PHE   A 192 ? 0.368 0.256 0.319 0.066  -0.063 -0.053 191 PHE   AAA CA  
1458 C  C   . PHE   A 192 ? 0.484 0.300 0.318 0.002  -0.068 -0.046 191 PHE   AAA C   
1459 O  O   . PHE   A 192 ? 0.467 0.220 0.396 -0.007 -0.049 -0.049 191 PHE   AAA O   
1460 C  CB  . PHE   A 192 ? 0.408 0.374 0.385 0.081  -0.016 -0.080 191 PHE   AAA CB  
1461 C  CG  . PHE   A 192 ? 0.394 0.137 0.341 0.106  -0.006 -0.052 191 PHE   AAA CG  
1462 C  CD1 . PHE   A 192 ? 0.415 0.329 0.379 0.028  -0.032 -0.082 191 PHE   AAA CD1 
1463 C  CD2 . PHE   A 192 ? 0.441 0.226 0.403 0.057  -0.046 0.027  191 PHE   AAA CD2 
1464 C  CE1 . PHE   A 192 ? 0.441 0.169 0.337 0.057  -0.018 -0.091 191 PHE   AAA CE1 
1465 C  CE2 . PHE   A 192 ? 0.475 0.142 0.411 0.080  -0.044 -0.004 191 PHE   AAA CE2 
1466 C  CZ  . PHE   A 192 ? 0.477 0.331 0.380 0.046  -0.017 0.027  191 PHE   AAA CZ  
1467 N  N   . TRP   A 193 ? 0.388 0.203 0.317 0.036  -0.050 -0.083 192 TRP   AAA N   
1468 C  CA  . TRP   A 193 ? 0.407 0.349 0.340 -0.009 -0.029 -0.048 192 TRP   AAA CA  
1469 C  C   . TRP   A 193 ? 0.369 0.369 0.327 -0.056 -0.067 -0.079 192 TRP   AAA C   
1470 O  O   . TRP   A 193 ? 0.479 0.286 0.313 -0.042 0.000  -0.103 192 TRP   AAA O   
1471 C  CB  . TRP   A 193 ? 0.428 0.253 0.344 -0.000 -0.005 -0.147 192 TRP   AAA CB  
1472 C  CG  . TRP   A 193 ? 0.410 0.231 0.414 -0.001 0.024  -0.128 192 TRP   AAA CG  
1473 C  CD1 . TRP   A 193 ? 0.472 0.320 0.419 0.023  -0.000 -0.131 192 TRP   AAA CD1 
1474 C  CD2 . TRP   A 193 ? 0.392 0.201 0.369 0.073  0.021  -0.030 192 TRP   AAA CD2 
1475 N  NE1 . TRP   A 193 ? 0.509 0.339 0.414 -0.031 -0.004 -0.220 192 TRP   AAA NE1 
1476 C  CE2 . TRP   A 193 ? 0.427 0.339 0.407 0.026  -0.007 -0.124 192 TRP   AAA CE2 
1477 C  CE3 . TRP   A 193 ? 0.448 0.392 0.367 0.032  0.047  -0.113 192 TRP   AAA CE3 
1478 C  CZ2 . TRP   A 193 ? 0.438 0.202 0.366 0.036  0.044  -0.106 192 TRP   AAA CZ2 
1479 C  CZ3 . TRP   A 193 ? 0.445 0.347 0.328 0.033  0.047  -0.059 192 TRP   AAA CZ3 
1480 C  CH2 . TRP   A 193 ? 0.442 0.353 0.384 0.054  0.041  -0.094 192 TRP   AAA CH2 
1481 N  N   . THR   A 194 ? 0.380 0.168 0.408 -0.045 -0.018 -0.089 193 THR   AAA N   
1482 C  CA  . THR   A 194 ? 0.401 0.234 0.340 -0.008 -0.032 -0.038 193 THR   AAA CA  
1483 C  C   . THR   A 194 ? 0.423 0.271 0.356 -0.074 -0.022 -0.083 193 THR   AAA C   
1484 O  O   . THR   A 194 ? 0.409 0.385 0.462 -0.001 -0.011 -0.203 193 THR   AAA O   
1485 C  CB  . THR   A 194 ? 0.443 0.112 0.400 -0.036 0.012  -0.036 193 THR   AAA CB  
1486 O  OG1 . THR   A 194 ? 0.433 0.193 0.405 -0.009 0.011  -0.065 193 THR   AAA OG1 
1487 C  CG2 . THR   A 194 ? 0.395 0.223 0.439 0.006  -0.006 -0.051 193 THR   AAA CG2 
1488 N  N   . TYR   A 195 ? 0.462 0.146 0.367 0.005  -0.005 -0.105 194 TYR   AAA N   
1489 C  CA  . TYR   A 195 ? 0.338 0.291 0.416 -0.055 -0.034 -0.108 194 TYR   AAA CA  
1490 C  C   . TYR   A 195 ? 0.351 0.324 0.405 0.005  -0.059 -0.152 194 TYR   AAA C   
1491 O  O   . TYR   A 195 ? 0.397 0.159 0.398 0.006  -0.015 -0.110 194 TYR   AAA O   
1492 C  CB  . TYR   A 195 ? 0.423 0.284 0.413 -0.022 0.004  -0.202 194 TYR   AAA CB  
1493 C  CG  . TYR   A 195 ? 0.400 0.161 0.391 -0.029 0.017  -0.141 194 TYR   AAA CG  
1494 C  CD1 . TYR   A 195 ? 0.397 0.168 0.388 -0.029 -0.021 -0.056 194 TYR   AAA CD1 
1495 C  CD2 . TYR   A 195 ? 0.442 0.096 0.431 -0.003 -0.007 -0.094 194 TYR   AAA CD2 
1496 C  CE1 . TYR   A 195 ? 0.375 0.219 0.433 0.022  -0.007 -0.033 194 TYR   AAA CE1 
1497 C  CE2 . TYR   A 195 ? 0.370 0.116 0.525 0.060  -0.016 -0.079 194 TYR   AAA CE2 
1498 C  CZ  . TYR   A 195 ? 0.348 0.075 0.423 0.047  -0.018 -0.045 194 TYR   AAA CZ  
1499 O  OH  . TYR   A 195 ? 0.396 0.149 0.422 -0.028 0.001  -0.050 194 TYR   AAA OH  
1500 N  N   . PRO   A 196 ? 0.420 0.215 0.428 -0.012 -0.014 -0.141 195 PRO   AAA N   
1501 C  CA  . PRO   A 196 ? 0.443 0.156 0.434 -0.064 0.006  -0.112 195 PRO   AAA CA  
1502 C  C   . PRO   A 196 ? 0.417 0.159 0.443 0.075  0.002  -0.183 195 PRO   AAA C   
1503 O  O   . PRO   A 196 ? 0.505 0.129 0.484 0.015  -0.020 -0.206 195 PRO   AAA O   
1504 C  CB  . PRO   A 196 ? 0.440 0.196 0.453 -0.044 -0.036 -0.102 195 PRO   AAA CB  
1505 C  CG  . PRO   A 196 ? 0.457 0.276 0.424 -0.056 -0.030 -0.120 195 PRO   AAA CG  
1506 C  CD  . PRO   A 196 ? 0.457 0.067 0.528 -0.043 -0.014 -0.149 195 PRO   AAA CD  
1507 N  N   . GLY   A 197 ? 0.412 0.184 0.418 -0.024 -0.009 -0.083 196 GLY   AAA N   
1508 C  CA  . GLY   A 197 ? 0.414 0.071 0.395 -0.041 -0.008 -0.067 196 GLY   AAA CA  
1509 C  C   . GLY   A 197 ? 0.363 0.051 0.412 -0.025 0.009  -0.027 196 GLY   AAA C   
1510 O  O   . GLY   A 197 ? 0.395 0.041 0.462 -0.008 0.016  -0.100 196 GLY   AAA O   
1511 N  N   . SER   A 198 ? 0.391 0.069 0.420 -0.024 -0.021 -0.039 197 SER   AAA N   
1512 C  CA  . SER   A 198 ? 0.375 0.090 0.434 0.042  0.008  -0.004 197 SER   AAA CA  
1513 C  C   . SER   A 198 ? 0.342 0.136 0.349 0.083  0.034  -0.050 197 SER   AAA C   
1514 O  O   . SER   A 198 ? 0.391 0.061 0.362 0.023  0.010  -0.074 197 SER   AAA O   
1515 C  CB  . SER   A 198 ? 0.398 0.073 0.426 -0.015 -0.040 -0.017 197 SER   AAA CB  
1516 O  OG  . SER   A 198 ? 0.420 0.154 0.470 -0.023 0.018  -0.110 197 SER   AAA OG  
1517 N  N   . LEU   A 199 ? 0.417 0.124 0.361 0.004  0.030  -0.039 198 LEU   AAA N   
1518 C  CA  . LEU   A 199 ? 0.375 0.179 0.361 0.054  0.015  -0.018 198 LEU   AAA CA  
1519 C  C   . LEU   A 199 ? 0.337 0.088 0.405 -0.017 -0.026 -0.053 198 LEU   AAA C   
1520 O  O   . LEU   A 199 ? 0.442 0.029 0.418 0.011  0.006  -0.079 198 LEU   AAA O   
1521 C  CB  . LEU   A 199 ? 0.337 0.157 0.396 0.001  0.048  -0.081 198 LEU   AAA CB  
1522 C  CG  . LEU   A 199 ? 0.342 0.079 0.412 -0.019 0.067  -0.047 198 LEU   AAA CG  
1523 C  CD1 . LEU   A 199 ? 0.434 0.238 0.436 0.038  0.024  -0.168 198 LEU   AAA CD1 
1524 C  CD2 . LEU   A 199 ? 0.419 0.071 0.496 -0.062 0.087  -0.077 198 LEU   AAA CD2 
1525 N  N   . THR   A 200 ? 0.288 0.141 0.390 0.011  0.014  -0.095 199 THR   AAA N   
1526 C  CA  . THR   A 200 ? 0.383 0.014 0.439 -0.010 -0.014 -0.055 199 THR   AAA CA  
1527 C  C   . THR   A 200 ? 0.324 0.161 0.426 0.036  0.050  -0.036 199 THR   AAA C   
1528 O  O   . THR   A 200 ? 0.398 0.103 0.494 0.067  0.050  -0.052 199 THR   AAA O   
1529 C  CB  . THR   A 200 ? 0.344 0.236 0.389 -0.063 -0.023 -0.141 199 THR   AAA CB  
1530 O  OG1 . THR   A 200 ? 0.394 0.015 0.393 -0.014 -0.003 -0.057 199 THR   AAA OG1 
1531 C  CG2 . THR   A 200 ? 0.423 0.214 0.393 -0.026 0.046  -0.122 199 THR   AAA CG2 
1532 N  N   . HIS   A 201 ? 0.414 0.019 0.454 0.026  0.035  -0.067 200 HIS   AAA N   
1533 C  CA  . HIS   A 201 ? 0.455 0.043 0.471 -0.030 0.052  0.026  200 HIS   AAA CA  
1534 C  C   . HIS   A 201 ? 0.488 0.095 0.388 0.067  0.052  -0.025 200 HIS   AAA C   
1535 O  O   . HIS   A 201 ? 0.463 0.046 0.441 -0.010 0.017  -0.016 200 HIS   AAA O   
1536 C  CB  . HIS   A 201 ? 0.444 0.035 0.506 0.070  0.004  -0.051 200 HIS   AAA CB  
1537 C  CG  . HIS   A 201 ? 0.510 0.035 0.451 0.014  0.002  -0.091 200 HIS   AAA CG  
1538 N  ND1 . HIS   A 201 ? 0.595 0.125 0.622 0.100  0.028  -0.073 200 HIS   AAA ND1 
1539 C  CD2 . HIS   A 201 ? 0.341 0.112 0.416 -0.053 0.054  -0.027 200 HIS   AAA CD2 
1540 C  CE1 . HIS   A 201 ? 0.471 0.017 0.466 -0.062 0.020  0.028  200 HIS   AAA CE1 
1541 N  NE2 . HIS   A 201 ? 0.523 0.152 0.507 -0.117 0.052  -0.017 200 HIS   AAA NE2 
1542 N  N   . PRO   A 202 ? 0.437 0.051 0.426 0.026  0.057  0.020  201 PRO   AAA N   
1543 C  CA  . PRO   A 202 ? 0.389 0.040 0.476 0.056  0.061  -0.026 201 PRO   AAA CA  
1544 C  C   . PRO   A 202 ? 0.402 0.093 0.415 0.106  0.056  -0.079 201 PRO   AAA C   
1545 O  O   . PRO   A 202 ? 0.455 0.101 0.384 0.040  0.031  0.002  201 PRO   AAA O   
1546 C  CB  . PRO   A 202 ? 0.392 0.051 0.568 0.041  0.039  -0.011 201 PRO   AAA CB  
1547 C  CG  . PRO   A 202 ? 0.519 0.013 0.562 0.057  0.011  0.015  201 PRO   AAA CG  
1548 C  CD  . PRO   A 202 ? 0.480 0.144 0.505 0.063  0.002  0.005  201 PRO   AAA CD  
1549 N  N   . PRO   A 203 ? 0.441 0.075 0.436 0.133  0.025  -0.010 202 PRO   AAA N   
1550 C  CA  . PRO   A 203 ? 0.492 0.155 0.455 0.046  0.012  -0.039 202 PRO   AAA CA  
1551 C  C   . PRO   A 203 ? 0.413 0.192 0.413 0.008  0.067  -0.036 202 PRO   AAA C   
1552 O  O   . PRO   A 203 ? 0.445 0.201 0.500 0.001  0.059  -0.094 202 PRO   AAA O   
1553 C  CB  . PRO   A 203 ? 0.550 0.032 0.423 0.083  0.031  0.005  202 PRO   AAA CB  
1554 C  CG  . PRO   A 203 ? 0.530 0.020 0.495 0.078  0.029  -0.018 202 PRO   AAA CG  
1555 C  CD  . PRO   A 203 ? 0.529 0.033 0.500 0.106  -0.002 -0.045 202 PRO   AAA CD  
1556 N  N   . LEU   A 204 ? 0.449 0.037 0.436 -0.057 0.049  -0.056 203 LEU   AAA N   
1557 C  CA  . LEU   A 204 ? 0.447 0.059 0.459 0.138  0.059  -0.048 203 LEU   AAA CA  
1558 C  C   . LEU   A 204 ? 0.445 0.168 0.456 0.109  0.037  -0.105 203 LEU   AAA C   
1559 O  O   . LEU   A 204 ? 0.466 0.011 0.492 0.016  0.080  -0.039 203 LEU   AAA O   
1560 C  CB  . LEU   A 204 ? 0.458 0.037 0.475 0.092  0.057  -0.062 203 LEU   AAA CB  
1561 C  CG  . LEU   A 204 ? 0.460 0.024 0.469 -0.002 0.008  0.016  203 LEU   AAA CG  
1562 C  CD1 . LEU   A 204 ? 0.517 0.053 0.490 -0.032 0.062  0.091  203 LEU   AAA CD1 
1563 C  CD2 . LEU   A 204 ? 0.469 0.017 0.473 -0.004 0.017  0.010  203 LEU   AAA CD2 
1564 N  N   . TYR   A 205 ? 0.469 0.021 0.453 0.001  0.023  -0.082 204 TYR   AAA N   
1565 C  CA  . TYR   A 205 ? 0.432 0.083 0.406 -0.003 0.048  -0.117 204 TYR   AAA CA  
1566 C  C   . TYR   A 205 ? 0.381 0.127 0.419 0.026  0.059  -0.116 204 TYR   AAA C   
1567 O  O   . TYR   A 205 ? 0.388 0.027 0.419 0.028  0.021  -0.086 204 TYR   AAA O   
1568 C  CB  . TYR   A 205 ? 0.427 0.102 0.390 0.036  0.030  -0.114 204 TYR   AAA CB  
1569 C  CG  . TYR   A 205 ? 0.489 0.159 0.386 0.024  0.017  -0.160 204 TYR   AAA CG  
1570 C  CD1 . TYR   A 205 ? 0.587 0.192 0.521 0.063  0.091  -0.104 204 TYR   AAA CD1 
1571 C  CD2 . TYR   A 205 ? 0.384 0.122 0.446 -0.032 0.007  -0.147 204 TYR   AAA CD2 
1572 C  CE1 . TYR   A 205 ? 0.614 0.244 0.495 -0.059 0.076  -0.201 204 TYR   AAA CE1 
1573 C  CE2 . TYR   A 205 ? 0.441 0.124 0.466 0.065  0.049  -0.014 204 TYR   AAA CE2 
1574 C  CZ  . TYR   A 205 ? 0.593 0.137 0.449 -0.083 0.009  -0.092 204 TYR   AAA CZ  
1575 O  OH  . TYR   A 205 ? 0.512 0.255 0.503 0.023  0.052  -0.044 204 TYR   AAA OH  
1576 N  N   . GLU   A 206 ? 0.404 0.118 0.449 -0.020 0.014  -0.071 205 GLU   AAA N   
1577 C  CA  . GLU   A 206 ? 0.449 0.147 0.421 -0.039 0.034  -0.103 205 GLU   AAA CA  
1578 C  C   . GLU   A 206 ? 0.305 0.202 0.465 -0.092 -0.021 -0.093 205 GLU   AAA C   
1579 O  O   . GLU   A 206 ? 0.389 0.094 0.480 -0.079 -0.028 -0.056 205 GLU   AAA O   
1580 C  CB  . GLU   A 206 ? 0.372 0.196 0.478 -0.053 0.009  -0.127 205 GLU   AAA CB  
1581 C  CG  . GLU   A 206 ? 0.472 0.150 0.542 -0.062 0.034  -0.067 205 GLU   AAA CG  
1582 C  CD  . GLU   A 206 ? 0.371 0.172 0.634 -0.033 -0.005 -0.095 205 GLU   AAA CD  
1583 O  OE1 . GLU   A 206 ? 0.462 0.140 0.490 -0.002 0.037  -0.142 205 GLU   AAA OE1 
1584 O  OE2 . GLU   A 206 ? 0.436 0.161 0.634 -0.020 -0.028 -0.116 205 GLU   AAA OE2 
1585 N  N   . SER   A 207 ? 0.326 0.037 0.467 0.023  -0.012 -0.093 206 SER   AAA N   
1586 C  CA  . SER   A 207 ? 0.348 0.084 0.406 0.082  0.029  -0.079 206 SER   AAA CA  
1587 C  C   . SER   A 207 ? 0.382 0.182 0.388 0.027  0.051  -0.068 206 SER   AAA C   
1588 O  O   . SER   A 207 ? 0.425 0.169 0.461 0.013  -0.014 -0.075 206 SER   AAA O   
1589 C  CB  . SER   A 207 ? 0.429 0.039 0.374 0.019  -0.015 -0.068 206 SER   AAA CB  
1590 O  OG  . SER   A 207 ? 0.455 0.135 0.405 0.012  -0.011 -0.081 206 SER   AAA OG  
1591 N  N   . VAL   A 208 ? 0.346 0.060 0.425 -0.016 0.023  -0.075 207 VAL   AAA N   
1592 C  CA  . VAL   A 208 ? 0.328 0.123 0.393 -0.024 0.035  -0.127 207 VAL   AAA CA  
1593 C  C   . VAL   A 208 ? 0.365 0.101 0.380 0.028  -0.014 -0.135 207 VAL   AAA C   
1594 O  O   . VAL   A 208 ? 0.468 0.046 0.445 -0.012 0.023  -0.112 207 VAL   AAA O   
1595 C  CB  . VAL   A 208 ? 0.351 0.165 0.362 -0.001 0.010  -0.096 207 VAL   AAA CB  
1596 C  CG1 . VAL   A 208 ? 0.372 0.179 0.347 0.008  0.029  -0.113 207 VAL   AAA CG1 
1597 C  CG2 . VAL   A 208 ? 0.406 0.173 0.369 -0.056 0.006  -0.042 207 VAL   AAA CG2 
1598 N  N   . THR   A 209 ? 0.401 0.232 0.414 0.005  -0.038 -0.041 208 THR   AAA N   
1599 C  CA  . THR   A 209 ? 0.407 0.134 0.381 -0.000 -0.022 -0.081 208 THR   AAA CA  
1600 C  C   . THR   A 209 ? 0.386 0.089 0.402 -0.026 -0.011 -0.061 208 THR   AAA C   
1601 O  O   . THR   A 209 ? 0.382 0.142 0.452 -0.094 -0.035 -0.066 208 THR   AAA O   
1602 C  CB  . THR   A 209 ? 0.369 0.251 0.407 -0.011 -0.052 -0.060 208 THR   AAA CB  
1603 O  OG1 . THR   A 209 ? 0.367 0.325 0.430 0.004  0.024  -0.106 208 THR   AAA OG1 
1604 C  CG2 . THR   A 209 ? 0.448 0.309 0.379 -0.073 -0.050 -0.070 208 THR   AAA CG2 
1605 N  N   . TRP   A 210 ? 0.364 0.209 0.352 0.015  0.000  -0.106 209 TRP   AAA N   
1606 C  CA  . TRP   A 210 ? 0.355 0.088 0.359 0.010  0.000  -0.100 209 TRP   AAA CA  
1607 C  C   . TRP   A 210 ? 0.415 0.101 0.378 0.015  -0.053 -0.078 209 TRP   AAA C   
1608 O  O   . TRP   A 210 ? 0.428 0.176 0.329 0.046  -0.025 -0.037 209 TRP   AAA O   
1609 C  CB  . TRP   A 210 ? 0.424 0.105 0.360 0.048  -0.022 -0.152 209 TRP   AAA CB  
1610 C  CG  . TRP   A 210 ? 0.338 0.211 0.359 -0.012 -0.002 -0.102 209 TRP   AAA CG  
1611 C  CD1 . TRP   A 210 ? 0.317 0.131 0.452 -0.043 -0.041 -0.084 209 TRP   AAA CD1 
1612 C  CD2 . TRP   A 210 ? 0.351 0.194 0.329 -0.014 -0.016 -0.094 209 TRP   AAA CD2 
1613 N  NE1 . TRP   A 210 ? 0.357 0.141 0.427 -0.000 0.001  -0.069 209 TRP   AAA NE1 
1614 C  CE2 . TRP   A 210 ? 0.293 0.158 0.387 0.054  0.008  -0.032 209 TRP   AAA CE2 
1615 C  CE3 . TRP   A 210 ? 0.332 0.112 0.344 0.059  -0.019 -0.062 209 TRP   AAA CE3 
1616 C  CZ2 . TRP   A 210 ? 0.384 0.178 0.395 0.017  0.025  -0.043 209 TRP   AAA CZ2 
1617 C  CZ3 . TRP   A 210 ? 0.368 0.189 0.336 0.014  -0.020 -0.083 209 TRP   AAA CZ3 
1618 C  CH2 . TRP   A 210 ? 0.367 0.117 0.372 0.019  0.022  -0.085 209 TRP   AAA CH2 
1619 N  N   . ILE   A 211 ? 0.344 0.218 0.355 -0.037 -0.037 -0.081 210 ILE   AAA N   
1620 C  CA  . ILE   A 211 ? 0.369 0.113 0.365 0.031  -0.014 -0.106 210 ILE   AAA CA  
1621 C  C   . ILE   A 211 ? 0.390 0.210 0.353 0.013  -0.034 -0.090 210 ILE   AAA C   
1622 O  O   . ILE   A 211 ? 0.434 0.188 0.392 0.025  -0.034 -0.142 210 ILE   AAA O   
1623 C  CB  . ILE   A 211 ? 0.419 0.119 0.392 0.046  0.011  -0.098 210 ILE   AAA CB  
1624 C  CG1 . ILE   A 211 ? 0.408 0.174 0.428 0.006  -0.005 -0.052 210 ILE   AAA CG1 
1625 C  CG2 . ILE   A 211 ? 0.420 0.093 0.423 0.059  0.016  -0.029 210 ILE   AAA CG2 
1626 C  CD1 . ILE   A 211 ? 0.462 0.232 0.445 -0.010 -0.011 -0.033 210 ILE   AAA CD1 
1627 N  N   . ILE   A 212 ? 0.445 0.155 0.360 -0.007 0.005  -0.086 211 ILE   AAA N   
1628 C  CA  . ILE   A 212 ? 0.451 0.036 0.322 0.028  0.014  -0.093 211 ILE   AAA CA  
1629 C  C   . ILE   A 212 ? 0.381 0.197 0.317 0.035  -0.058 -0.042 211 ILE   AAA C   
1630 O  O   . ILE   A 212 ? 0.376 0.125 0.324 -0.009 -0.055 -0.080 211 ILE   AAA O   
1631 C  CB  . ILE   A 212 ? 0.459 0.019 0.361 0.013  -0.011 -0.062 211 ILE   AAA CB  
1632 C  CG1 . ILE   A 212 ? 0.447 0.202 0.358 -0.084 0.008  -0.087 211 ILE   AAA CG1 
1633 C  CG2 . ILE   A 212 ? 0.419 0.201 0.321 0.032  0.011  -0.089 211 ILE   AAA CG2 
1634 C  CD1 . ILE   A 212 ? 0.441 0.229 0.332 0.072  0.017  -0.049 211 ILE   AAA CD1 
1635 N  N   . CYS   A 213 ? 0.406 0.187 0.278 0.025  -0.032 -0.079 212 CYS   AAA N   
1636 C  CA  . CYS   A 213 ? 0.379 0.275 0.337 0.010  0.014  -0.065 212 CYS   AAA CA  
1637 C  C   . CYS   A 213 ? 0.335 0.214 0.322 -0.001 -0.032 -0.029 212 CYS   AAA C   
1638 O  O   . CYS   A 213 ? 0.441 0.190 0.331 0.033  -0.018 -0.007 212 CYS   AAA O   
1639 C  CB  . CYS   A 213 ? 0.395 0.289 0.371 0.019  -0.019 -0.107 212 CYS   AAA CB  
1640 S  SG  . CYS   A 213 ? 0.445 0.198 0.388 0.030  -0.014 -0.079 212 CYS   AAA SG  
1641 N  N   . LYS   A 214 ? 0.475 0.152 0.327 -0.021 0.005  -0.029 213 LYS   AAA N   
1642 C  CA  . LYS   A 214 ? 0.473 0.262 0.343 -0.033 0.002  -0.071 213 LYS   AAA CA  
1643 C  C   . LYS   A 214 ? 0.449 0.217 0.337 0.011  -0.026 -0.037 213 LYS   AAA C   
1644 O  O   . LYS   A 214 ? 0.510 0.124 0.358 -0.004 -0.005 -0.067 213 LYS   AAA O   
1645 C  CB  . LYS   A 214 ? 0.479 0.291 0.379 -0.070 -0.071 -0.044 213 LYS   AAA CB  
1646 C  CG  . LYS   A 214 ? 0.515 0.442 0.486 -0.011 -0.046 -0.093 213 LYS   AAA CG  
1647 C  CD  . LYS   A 214 ? 0.551 0.437 0.527 0.004  -0.080 -0.017 213 LYS   AAA CD  
1648 C  CE  . LYS   A 214 ? 0.541 0.467 0.616 -0.031 0.003  -0.114 213 LYS   AAA CE  
1649 N  NZ  . LYS   A 214 ? 0.708 0.315 0.902 -0.071 -0.053 -0.037 213 LYS   AAA NZ  
1650 N  N   . GLU   A 215 ? 0.388 0.215 0.337 0.051  0.005  -0.090 214 GLU   AAA N   
1651 C  CA  . GLU   A 215 ? 0.413 0.041 0.320 0.004  -0.003 -0.081 214 GLU   AAA CA  
1652 C  C   . GLU   A 215 ? 0.351 0.148 0.372 0.006  -0.036 -0.061 214 GLU   AAA C   
1653 O  O   . GLU   A 215 ? 0.463 0.095 0.400 0.026  -0.015 -0.032 214 GLU   AAA O   
1654 C  CB  . GLU   A 215 ? 0.555 0.078 0.373 0.022  0.011  0.035  214 GLU   AAA CB  
1655 C  CG  . GLU   A 215 ? 0.610 0.148 0.506 0.064  0.079  0.033  214 GLU   AAA CG  
1656 C  CD  . GLU   A 215 ? 0.562 0.174 0.520 0.013  0.056  0.035  214 GLU   AAA CD  
1657 O  OE1 . GLU   A 215 ? 0.728 0.383 0.553 -0.002 0.206  -0.153 214 GLU   AAA OE1 
1658 O  OE2 . GLU   A 215 ? 0.988 0.059 0.621 0.162  0.126  0.068  214 GLU   AAA OE2 
1659 N  N   . SER   A 216 ? 0.387 0.127 0.411 0.076  -0.045 -0.080 215 SER   AAA N   
1660 C  CA  . SER   A 216 ? 0.345 0.223 0.351 0.000  -0.021 -0.113 215 SER   AAA CA  
1661 C  C   . SER   A 216 ? 0.389 0.178 0.318 0.009  -0.021 -0.061 215 SER   AAA C   
1662 O  O   . SER   A 216 ? 0.472 0.196 0.357 -0.037 -0.001 -0.074 215 SER   AAA O   
1663 C  CB  . SER   A 216 ? 0.370 0.269 0.382 0.047  -0.033 -0.064 215 SER   AAA CB  
1664 O  OG  . SER   A 216 ? 0.439 0.289 0.372 0.036  0.015  -0.030 215 SER   AAA OG  
1665 N  N   . ILE   A 217 ? 0.431 0.276 0.340 -0.021 -0.011 -0.109 216 ILE   AAA N   
1666 C  CA  . ILE   A 217 ? 0.385 0.249 0.303 -0.021 0.004  -0.029 216 ILE   AAA CA  
1667 C  C   . ILE   A 217 ? 0.372 0.198 0.343 -0.038 0.009  0.045  216 ILE   AAA C   
1668 O  O   . ILE   A 217 ? 0.475 0.111 0.337 -0.020 0.025  -0.030 216 ILE   AAA O   
1669 C  CB  . ILE   A 217 ? 0.344 0.241 0.311 -0.039 0.017  -0.066 216 ILE   AAA CB  
1670 C  CG1 . ILE   A 217 ? 0.377 0.249 0.294 -0.022 0.013  -0.052 216 ILE   AAA CG1 
1671 C  CG2 . ILE   A 217 ? 0.417 0.184 0.272 -0.060 -0.006 -0.028 216 ILE   AAA CG2 
1672 C  CD1 . ILE   A 217 ? 0.397 0.189 0.286 -0.053 0.041  -0.009 216 ILE   AAA CD1 
1673 N  N   . SER   A 218 ? 0.408 0.238 0.439 -0.080 -0.006 -0.075 217 SER   AAA N   
1674 C  CA  . SER   A 218 ? 0.416 0.237 0.407 -0.145 -0.061 -0.064 217 SER   AAA CA  
1675 C  C   . SER   A 218 ? 0.354 0.213 0.401 -0.032 -0.023 -0.042 217 SER   AAA C   
1676 O  O   . SER   A 218 ? 0.379 0.305 0.409 -0.050 0.016  -0.064 217 SER   AAA O   
1677 C  CB  . SER   A 218 ? 0.428 0.364 0.395 -0.178 -0.066 -0.008 217 SER   AAA CB  
1678 O  OG  . SER   A 218 ? 0.646 0.421 0.505 -0.209 -0.011 -0.005 217 SER   AAA OG  
1679 N  N   . VAL   A 219 ? 0.381 0.214 0.399 -0.002 -0.016 -0.032 218 VAL   AAA N   
1680 C  CA  . VAL   A 219 ? 0.416 0.112 0.379 -0.013 -0.004 -0.115 218 VAL   AAA CA  
1681 C  C   . VAL   A 219 ? 0.403 0.391 0.363 0.008  0.028  -0.109 218 VAL   AAA C   
1682 O  O   . VAL   A 219 ? 0.402 0.368 0.421 0.032  -0.009 -0.137 218 VAL   AAA O   
1683 C  CB  . VAL   A 219 ? 0.413 0.250 0.372 -0.014 0.001  -0.097 218 VAL   AAA CB  
1684 C  CG1 . VAL   A 219 ? 0.413 0.246 0.416 0.009  -0.030 -0.114 218 VAL   AAA CG1 
1685 C  CG2 . VAL   A 219 ? 0.391 0.253 0.363 0.035  0.005  -0.080 218 VAL   AAA CG2 
1686 N  N   . SER   A 220 ? 0.443 0.418 0.399 0.007  -0.018 -0.095 219 SER   AAA N   
1687 C  CA  . SER   A 220 ? 0.375 0.498 0.391 -0.020 -0.031 -0.095 219 SER   AAA CA  
1688 C  C   . SER   A 220 ? 0.387 0.508 0.386 0.119  0.035  -0.034 219 SER   AAA C   
1689 O  O   . SER   A 220 ? 0.371 0.349 0.411 -0.006 0.010  -0.082 219 SER   AAA O   
1690 C  CB  . SER   A 220 ? 0.373 0.384 0.419 -0.001 0.029  -0.065 219 SER   AAA CB  
1691 O  OG  . SER   A 220 ? 0.428 0.381 0.398 -0.029 0.000  -0.070 219 SER   AAA OG  
1692 N  N   . SER   A 221 ? 0.398 0.386 0.402 0.058  0.008  -0.096 220 SER   AAA N   
1693 C  CA  . SER   A 221 ? 0.357 0.498 0.435 0.008  0.002  0.005  220 SER   AAA CA  
1694 C  C   . SER   A 221 ? 0.380 0.445 0.440 -0.030 0.031  0.015  220 SER   AAA C   
1695 O  O   . SER   A 221 ? 0.472 0.414 0.400 0.030  0.025  0.029  220 SER   AAA O   
1696 C  CB  . SER   A 221 ? 0.401 0.436 0.641 0.069  -0.125 -0.056 220 SER   AAA CB  
1697 O  OG  . SER   A 221 ? 0.575 0.407 0.652 0.078  -0.104 -0.099 220 SER   AAA OG  
1698 N  N   . GLU   A 222 ? 0.385 0.465 0.409 0.013  0.000  -0.104 221 GLU   AAA N   
1699 C  CA  . GLU   A 222 ? 0.369 0.590 0.367 -0.006 -0.045 -0.038 221 GLU   AAA CA  
1700 C  C   . GLU   A 222 ? 0.418 0.532 0.384 0.002  0.040  0.020  221 GLU   AAA C   
1701 O  O   . GLU   A 222 ? 0.394 0.569 0.352 0.011  -0.001 -0.026 221 GLU   AAA O   
1702 C  CB  . GLU   A 222 ? 0.422 0.590 0.363 -0.032 0.019  -0.063 221 GLU   AAA CB  
1703 C  CG  . GLU   A 222 ? 0.389 0.482 0.422 -0.030 -0.016 -0.039 221 GLU   AAA CG  
1704 C  CD  . GLU   A 222 ? 0.515 0.600 0.376 -0.004 -0.044 -0.009 221 GLU   AAA CD  
1705 O  OE1 . GLU   A 222 ? 0.447 0.544 0.366 0.017  -0.039 -0.003 221 GLU   AAA OE1 
1706 O  OE2 . GLU   A 222 ? 0.524 0.804 0.505 0.031  -0.021 -0.182 221 GLU   AAA OE2 
1707 N  N   . GLN   A 223 ? 0.379 0.511 0.417 0.023  -0.014 -0.088 222 GLN   AAA N   
1708 C  CA  . GLN   A 223 ? 0.310 0.456 0.405 -0.035 -0.064 -0.084 222 GLN   AAA CA  
1709 C  C   . GLN   A 223 ? 0.379 0.373 0.414 0.001  -0.016 -0.064 222 GLN   AAA C   
1710 O  O   . GLN   A 223 ? 0.427 0.457 0.426 -0.026 -0.014 -0.083 222 GLN   AAA O   
1711 C  CB  . GLN   A 223 ? 0.334 0.316 0.461 0.003  -0.027 -0.067 222 GLN   AAA CB  
1712 C  CG  . GLN   A 223 ? 0.418 0.410 0.461 -0.089 -0.056 -0.045 222 GLN   AAA CG  
1713 C  CD  . GLN   A 223 ? 0.467 0.192 0.435 0.064  -0.008 -0.076 222 GLN   AAA CD  
1714 O  OE1 . GLN   A 223 ? 0.444 0.140 0.427 -0.023 0.020  -0.031 222 GLN   AAA OE1 
1715 N  NE2 . GLN   A 223 ? 0.556 0.170 0.464 0.017  0.047  -0.091 222 GLN   AAA NE2 
1716 N  N   . LEU   A 224 ? 0.375 0.450 0.354 -0.015 0.058  -0.085 223 LEU   AAA N   
1717 C  CA  . LEU   A 224 ? 0.376 0.444 0.351 -0.034 -0.012 -0.026 223 LEU   AAA CA  
1718 C  C   . LEU   A 224 ? 0.334 0.492 0.347 0.010  0.002  -0.062 223 LEU   AAA C   
1719 O  O   . LEU   A 224 ? 0.398 0.601 0.391 -0.054 0.058  -0.037 223 LEU   AAA O   
1720 C  CB  . LEU   A 224 ? 0.401 0.500 0.332 -0.034 0.012  -0.054 223 LEU   AAA CB  
1721 C  CG  . LEU   A 224 ? 0.375 0.501 0.410 0.045  -0.069 -0.113 223 LEU   AAA CG  
1722 C  CD1 . LEU   A 224 ? 0.628 0.630 0.481 0.025  0.048  -0.171 223 LEU   AAA CD1 
1723 C  CD2 . LEU   A 224 ? 0.347 0.465 0.361 0.074  -0.080 -0.028 223 LEU   AAA CD2 
1724 N  N   . ALA   A 225 ? 0.361 0.478 0.376 0.002  -0.040 -0.078 224 ALA   AAA N   
1725 C  CA  . ALA   A 225 ? 0.342 0.549 0.398 0.051  -0.044 0.005  224 ALA   AAA CA  
1726 C  C   . ALA   A 225 ? 0.363 0.425 0.375 -0.003 -0.031 0.025  224 ALA   AAA C   
1727 O  O   . ALA   A 225 ? 0.404 0.603 0.338 -0.036 0.043  -0.022 224 ALA   AAA O   
1728 C  CB  . ALA   A 225 ? 0.372 0.544 0.456 -0.026 -0.040 -0.010 224 ALA   AAA CB  
1729 N  N   . GLN   A 226 ? 0.434 0.480 0.373 0.055  0.015  -0.020 225 GLN   AAA N   
1730 C  CA  . GLN   A 226 ? 0.382 0.338 0.397 0.043  -0.016 -0.023 225 GLN   AAA CA  
1731 C  C   . GLN   A 226 ? 0.384 0.330 0.355 0.038  -0.035 -0.046 225 GLN   AAA C   
1732 O  O   . GLN   A 226 ? 0.461 0.472 0.389 0.012  0.033  0.013  225 GLN   AAA O   
1733 C  CB  . GLN   A 226 ? 0.400 0.332 0.441 0.006  0.038  -0.055 225 GLN   AAA CB  
1734 C  CG  . GLN   A 226 ? 0.408 0.288 0.455 -0.009 -0.040 -0.019 225 GLN   AAA CG  
1735 C  CD  . GLN   A 226 ? 0.400 0.316 0.450 0.026  -0.000 -0.026 225 GLN   AAA CD  
1736 O  OE1 . GLN   A 226 ? 0.509 0.456 0.439 -0.055 -0.013 -0.032 225 GLN   AAA OE1 
1737 N  NE2 . GLN   A 226 ? 0.502 0.298 0.483 -0.030 -0.012 -0.084 225 GLN   AAA NE2 
1738 N  N   . PHE   A 227 ? 0.368 0.356 0.358 -0.014 -0.023 -0.062 226 PHE   AAA N   
1739 C  CA  . PHE   A 227 ? 0.376 0.293 0.346 0.027  -0.031 -0.031 226 PHE   AAA CA  
1740 C  C   . PHE   A 227 ? 0.403 0.296 0.335 0.052  -0.009 -0.004 226 PHE   AAA C   
1741 O  O   . PHE   A 227 ? 0.373 0.391 0.391 0.008  -0.012 -0.043 226 PHE   AAA O   
1742 C  CB  . PHE   A 227 ? 0.448 0.265 0.345 -0.004 -0.030 -0.043 226 PHE   AAA CB  
1743 C  CG  . PHE   A 227 ? 0.433 0.279 0.336 0.008  -0.038 -0.041 226 PHE   AAA CG  
1744 C  CD1 . PHE   A 227 ? 0.466 0.317 0.419 0.081  0.032  -0.058 226 PHE   AAA CD1 
1745 C  CD2 . PHE   A 227 ? 0.444 0.516 0.354 -0.040 -0.064 -0.021 226 PHE   AAA CD2 
1746 C  CE1 . PHE   A 227 ? 0.463 0.407 0.412 0.106  0.034  -0.041 226 PHE   AAA CE1 
1747 C  CE2 . PHE   A 227 ? 0.554 0.454 0.318 -0.038 -0.008 -0.041 226 PHE   AAA CE2 
1748 C  CZ  . PHE   A 227 ? 0.514 0.457 0.394 0.079  0.024  0.037  226 PHE   AAA CZ  
1749 N  N   . ARG   A 228 ? 0.368 0.397 0.388 0.056  0.013  -0.043 227 ARG   AAA N   
1750 C  CA  . ARG   A 228 ? 0.440 0.382 0.357 0.049  0.023  -0.019 227 ARG   AAA CA  
1751 C  C   . ARG   A 228 ? 0.459 0.266 0.398 -0.022 0.019  -0.024 227 ARG   AAA C   
1752 O  O   . ARG   A 228 ? 0.475 0.185 0.471 0.017  0.033  -0.047 227 ARG   AAA O   
1753 C  CB  . ARG   A 228 ? 0.443 0.359 0.423 0.018  -0.031 -0.103 227 ARG   AAA CB  
1754 C  CG  . ARG   A 228 ? 0.465 0.431 0.465 0.085  -0.042 -0.196 227 ARG   AAA CG  
1755 C  CD  . ARG   A 228 ? 0.443 0.542 0.557 0.174  -0.060 -0.192 227 ARG   AAA CD  
1756 N  NE  . ARG   A 228 ? 0.495 0.584 0.524 0.109  0.019  -0.184 227 ARG   AAA NE  
1757 C  CZ  . ARG   A 228 ? 0.462 0.421 0.405 0.146  -0.042 -0.172 227 ARG   AAA CZ  
1758 N  NH1 . ARG   A 228 ? 0.583 0.553 0.369 0.203  -0.037 -0.157 227 ARG   AAA NH1 
1759 N  NH2 . ARG   A 228 ? 0.602 0.328 0.484 0.095  -0.116 -0.115 227 ARG   AAA NH2 
1760 N  N   . SER   A 229 ? 0.358 0.315 0.406 -0.036 -0.001 -0.071 228 SER   AAA N   
1761 C  CA  . SER   A 229 ? 0.434 0.387 0.390 0.076  -0.008 -0.087 228 SER   AAA CA  
1762 C  C   . SER   A 229 ? 0.350 0.427 0.379 0.023  0.001  0.008  228 SER   AAA C   
1763 O  O   . SER   A 229 ? 0.461 0.470 0.399 0.042  -0.025 -0.015 228 SER   AAA O   
1764 C  CB  . SER   A 229 ? 0.616 0.291 0.479 -0.004 -0.055 -0.026 228 SER   AAA CB  
1765 O  OG  . SER   A 229 ? 0.727 0.192 0.603 -0.080 0.026  -0.040 228 SER   AAA OG  
1766 N  N   . LEU   A 230 ? 0.373 0.285 0.430 0.010  -0.017 0.045  229 LEU   AAA N   
1767 C  CA  . LEU   A 230 ? 0.440 0.112 0.450 0.018  0.007  -0.048 229 LEU   AAA CA  
1768 C  C   . LEU   A 230 ? 0.423 0.308 0.323 0.016  0.019  0.029  229 LEU   AAA C   
1769 O  O   . LEU   A 230 ? 0.492 0.273 0.431 0.032  -0.038 -0.021 229 LEU   AAA O   
1770 C  CB  . LEU   A 230 ? 0.405 0.275 0.432 -0.004 0.010  -0.033 229 LEU   AAA CB  
1771 C  CG  . LEU   A 230 ? 0.468 0.312 0.498 0.099  -0.040 -0.070 229 LEU   AAA CG  
1772 C  CD1 . LEU   A 230 ? 0.447 0.497 0.511 0.094  -0.034 -0.048 229 LEU   AAA CD1 
1773 C  CD2 . LEU   A 230 ? 0.491 0.405 0.540 0.117  -0.041 -0.164 229 LEU   AAA CD2 
1774 N  N   . LEU   A 231 ? 0.413 0.474 0.341 0.048  0.011  0.019  230 LEU   AAA N   
1775 C  CA  . LEU   A 231 ? 0.393 0.280 0.410 0.021  -0.040 -0.016 230 LEU   AAA CA  
1776 C  C   . LEU   A 231 ? 0.419 0.321 0.386 0.003  -0.005 -0.061 230 LEU   AAA C   
1777 O  O   . LEU   A 231 ? 0.419 0.365 0.442 0.053  -0.023 -0.073 230 LEU   AAA O   
1778 C  CB  . LEU   A 231 ? 0.398 0.548 0.431 -0.045 -0.068 -0.016 230 LEU   AAA CB  
1779 C  CG  . LEU   A 231 ? 0.400 0.573 0.459 -0.015 -0.067 0.027  230 LEU   AAA CG  
1780 C  CD1 . LEU   A 231 ? 0.410 0.654 0.455 0.005  0.003  -0.035 230 LEU   AAA CD1 
1781 C  CD2 . LEU   A 231 ? 0.407 0.546 0.448 -0.013 -0.045 0.035  230 LEU   AAA CD2 
1782 N  N   . SER   A 232 ? 0.483 0.317 0.471 -0.003 0.067  -0.057 231 SER   AAA N   
1783 C  CA  . SER   A 232 ? 0.471 0.223 0.433 0.017  0.025  -0.019 231 SER   AAA CA  
1784 C  C   . SER   A 232 ? 0.434 0.461 0.423 -0.032 0.005  -0.097 231 SER   AAA C   
1785 O  O   . SER   A 232 ? 0.464 0.495 0.425 -0.077 0.056  -0.141 231 SER   AAA O   
1786 C  CB  . SER   A 232 ? 0.443 0.239 0.633 -0.035 0.004  -0.091 231 SER   AAA CB  
1787 O  OG  . SER   A 232 ? 0.516 0.488 0.520 0.017  -0.040 -0.021 231 SER   AAA OG  
1788 N  N   . ASN   A 233 ? 0.404 0.554 0.396 0.036  -0.016 -0.048 232 ASN   AAA N   
1789 C  CA  . ASN   A 233 ? 0.375 0.583 0.422 -0.031 0.006  -0.040 232 ASN   AAA CA  
1790 C  C   . ASN   A 233 ? 0.376 0.542 0.413 -0.042 0.046  0.034  232 ASN   AAA C   
1791 O  O   . ASN   A 233 ? 0.446 0.436 0.446 0.001  0.029  0.006  232 ASN   AAA O   
1792 C  CB  . ASN   A 233 ? 0.476 0.440 0.404 -0.045 -0.041 0.090  232 ASN   AAA CB  
1793 C  CG  . ASN   A 233 ? 0.430 0.569 0.381 -0.053 0.009  -0.008 232 ASN   AAA CG  
1794 O  OD1 . ASN   A 233 ? 0.511 0.509 0.412 0.011  -0.012 -0.042 232 ASN   AAA OD1 
1795 N  ND2 . ASN   A 233 ? 0.392 0.535 0.366 0.011  0.027  0.036  232 ASN   AAA ND2 
1796 N  N   . VAL   A 234 ? 0.431 0.611 0.457 -0.039 0.064  -0.000 233 VAL   AAA N   
1797 C  CA  . VAL   A 234 ? 0.417 0.679 0.402 -0.013 0.029  -0.019 233 VAL   AAA CA  
1798 C  C   . VAL   A 234 ? 0.396 0.491 0.414 0.022  0.050  -0.018 233 VAL   AAA C   
1799 O  O   . VAL   A 234 ? 0.396 0.540 0.391 0.028  0.026  0.004  233 VAL   AAA O   
1800 C  CB  . VAL   A 234 ? 0.386 0.721 0.470 -0.043 0.032  -0.005 233 VAL   AAA CB  
1801 C  CG1 . VAL   A 234 ? 0.397 0.724 0.454 0.006  0.006  -0.022 233 VAL   AAA CG1 
1802 C  CG2 . VAL   A 234 ? 0.446 0.820 0.534 0.003  0.009  0.046  233 VAL   AAA CG2 
1803 N  N   . GLU   A 235 ? 0.423 0.441 0.378 -0.042 0.026  0.046  234 GLU   AAA N   
1804 C  CA  . GLU   A 235 ? 0.481 0.523 0.436 -0.041 -0.053 0.053  234 GLU   AAA CA  
1805 C  C   . GLU   A 235 ? 0.448 0.434 0.424 -0.035 0.019  0.052  234 GLU   AAA C   
1806 O  O   . GLU   A 235 ? 0.515 0.530 0.366 -0.021 0.038  0.049  234 GLU   AAA O   
1807 C  CB  . GLU   A 235 ? 0.452 0.596 0.670 0.064  -0.076 0.022  234 GLU   AAA CB  
1808 C  CG  . GLU   A 235 ? 0.421 0.542 0.471 0.080  -0.016 -0.027 234 GLU   AAA CG  
1809 C  CD  . GLU   A 235 ? 0.680 0.584 0.417 -0.001 -0.002 0.046  234 GLU   AAA CD  
1810 O  OE1 . GLU   A 235 ? 0.583 0.385 0.460 -0.072 -0.021 0.053  234 GLU   AAA OE1 
1811 O  OE2 . GLU   A 235 ? 0.861 0.753 0.473 -0.088 0.096  -0.034 234 GLU   AAA OE2 
1812 N  N   . GLY   A 236 ? 0.509 0.182 0.464 0.043  -0.014 0.066  235 GLY   AAA N   
1813 C  CA  . GLY   A 236 ? 0.587 0.593 0.390 0.024  0.000  0.093  235 GLY   AAA CA  
1814 C  C   . GLY   A 236 ? 0.604 0.567 0.372 -0.081 -0.031 0.045  235 GLY   AAA C   
1815 O  O   . GLY   A 236 ? 0.803 0.808 0.545 -0.057 -0.105 0.189  235 GLY   AAA O   
1816 N  N   . ASP   A 237 ? 0.592 0.662 0.383 -0.028 -0.090 0.063  236 ASP   AAA N   
1817 C  CA  . ASP   A 237 ? 0.656 0.629 0.446 0.030  -0.057 0.106  236 ASP   AAA CA  
1818 C  C   . ASP   A 237 ? 0.601 0.594 0.538 -0.035 -0.039 0.060  236 ASP   AAA C   
1819 O  O   . ASP   A 237 ? 0.608 0.519 0.431 0.022  -0.060 0.063  236 ASP   AAA O   
1820 C  CB  . ASP   A 237 ? 0.671 0.610 0.414 -0.023 -0.032 0.156  236 ASP   AAA CB  
1821 C  CG  . ASP   A 237 ? 0.594 0.585 0.544 -0.074 -0.027 0.187  236 ASP   AAA CG  
1822 O  OD1 . ASP   A 237 ? 0.666 0.877 0.563 0.020  0.023  0.119  236 ASP   AAA OD1 
1823 O  OD2 . ASP   A 237 ? 0.651 0.710 0.544 -0.141 -0.086 0.098  236 ASP   AAA OD2 
1824 N  N   . ASN   A 238 ? 0.622 0.542 0.455 -0.013 -0.028 0.164  237 ASN   AAA N   
1825 C  CA  . ASN   A 238 ? 0.621 0.559 0.450 -0.030 -0.031 0.173  237 ASN   AAA CA  
1826 C  C   . ASN   A 238 ? 0.446 0.651 0.476 -0.046 -0.055 0.181  237 ASN   AAA C   
1827 O  O   . ASN   A 238 ? 0.449 0.526 0.428 -0.011 -0.030 0.082  237 ASN   AAA O   
1828 C  CB  . ASN   A 238 ? 0.816 0.641 0.454 0.095  -0.105 0.289  237 ASN   AAA CB  
1829 C  CG  . ASN   A 238 ? 1.051 0.935 0.503 0.187  -0.239 0.208  237 ASN   AAA CG  
1830 O  OD1 . ASN   A 238 ? 1.188 0.339 0.766 -0.147 -0.240 -0.074 237 ASN   AAA OD1 
1831 N  ND2 . ASN   A 238 ? 0.945 0.918 0.434 0.155  -0.103 0.096  237 ASN   AAA ND2 
1832 N  N   . ALA   A 239 ? 0.436 0.679 0.492 -0.013 -0.017 0.161  238 ALA   AAA N   
1833 C  CA  . ALA   A 239 ? 0.564 0.724 0.502 -0.017 -0.038 0.153  238 ALA   AAA CA  
1834 C  C   . ALA   A 239 ? 0.553 0.631 0.424 0.155  -0.091 0.132  238 ALA   AAA C   
1835 O  O   . ALA   A 239 ? 0.591 0.651 0.509 0.187  0.003  0.124  238 ALA   AAA O   
1836 C  CB  . ALA   A 239 ? 0.415 0.998 0.494 0.042  -0.057 0.210  238 ALA   AAA CB  
1837 N  N   . VAL   A 240 ? 0.503 0.623 0.414 0.118  -0.068 0.139  239 VAL   AAA N   
1838 C  CA  . VAL   A 240 ? 0.543 0.570 0.444 0.121  -0.002 0.087  239 VAL   AAA CA  
1839 C  C   . VAL   A 240 ? 0.522 0.477 0.424 0.119  0.033  0.042  239 VAL   AAA C   
1840 O  O   . VAL   A 240 ? 0.469 0.587 0.383 0.096  -0.058 0.080  239 VAL   AAA O   
1841 C  CB  . VAL   A 240 ? 0.638 0.484 0.523 0.052  -0.077 0.074  239 VAL   AAA CB  
1842 C  CG1 . VAL   A 240 ? 0.600 0.495 0.475 0.158  -0.030 -0.028 239 VAL   AAA CG1 
1843 C  CG2 . VAL   A 240 ? 0.574 0.312 0.518 0.107  -0.071 0.063  239 VAL   AAA CG2 
1844 N  N   . PRO   A 241 ? 0.485 0.403 0.372 0.030  0.010  0.069  240 PRO   AAA N   
1845 C  CA  . PRO   A 241 ? 0.491 0.353 0.388 0.074  0.004  0.054  240 PRO   AAA CA  
1846 C  C   . PRO   A 241 ? 0.490 0.402 0.357 0.063  0.011  0.080  240 PRO   AAA C   
1847 O  O   . PRO   A 241 ? 0.558 0.452 0.455 -0.049 0.037  0.002  240 PRO   AAA O   
1848 C  CB  . PRO   A 241 ? 0.502 0.627 0.494 0.045  0.013  0.084  240 PRO   AAA CB  
1849 C  CG  . PRO   A 241 ? 0.633 0.569 0.512 -0.018 -0.049 0.132  240 PRO   AAA CG  
1850 C  CD  . PRO   A 241 ? 0.566 0.574 0.430 0.126  0.031  0.121  240 PRO   AAA CD  
1851 N  N   . MET   A 242 ? 0.525 0.425 0.384 0.077  -0.005 0.070  241 MET   AAA N   
1852 C  CA  . MET   A 242 ? 0.531 0.366 0.386 0.070  -0.028 -0.007 241 MET   AAA CA  
1853 C  C   . MET   A 242 ? 0.478 0.359 0.376 0.068  0.025  0.075  241 MET   AAA C   
1854 O  O   . MET   A 242 ? 0.463 0.368 0.344 -0.026 -0.009 0.072  241 MET   AAA O   
1855 C  CB  . MET   A 242 ? 0.509 0.353 0.492 0.047  -0.064 0.067  241 MET   AAA CB  
1856 C  CG  . MET   A 242 ? 0.518 0.428 0.482 0.078  0.019  0.141  241 MET   AAA CG  
1857 S  SD  . MET   A 242 ? 0.440 0.376 0.454 0.046  -0.013 -0.069 241 MET   AAA SD  
1858 C  CE  . MET   A 242 ? 0.438 0.381 0.384 0.102  -0.036 -0.004 241 MET   AAA CE  
1859 N  N   . GLN   A 243 ? 0.493 0.288 0.401 -0.053 -0.009 -0.006 242 GLN   AAA N   
1860 C  CA  . GLN   A 243 ? 0.492 0.411 0.452 0.059  0.014  0.054  242 GLN   AAA CA  
1861 C  C   . GLN   A 243 ? 0.444 0.380 0.459 0.051  0.024  0.093  242 GLN   AAA C   
1862 O  O   . GLN   A 243 ? 0.455 0.392 0.433 0.123  0.030  -0.010 242 GLN   AAA O   
1863 C  CB  . GLN   A 243 ? 0.650 0.520 0.516 0.136  -0.192 0.069  242 GLN   AAA CB  
1864 C  CG  . GLN   A 243 ? 0.704 0.355 0.610 0.138  -0.219 -0.015 242 GLN   AAA CG  
1865 C  CD  . GLN   A 243 ? 0.739 0.440 0.689 0.166  -0.082 -0.008 242 GLN   AAA CD  
1866 O  OE1 . GLN   A 243 ? 0.816 0.470 0.894 0.026  0.020  -0.226 242 GLN   AAA OE1 
1867 N  NE2 . GLN   A 243 ? 0.795 0.414 0.696 0.265  -0.076 -0.028 242 GLN   AAA NE2 
1868 N  N   . HIS   A 244 ? 0.415 0.385 0.472 0.073  -0.025 -0.008 243 HIS   AAA N   
1869 C  CA  . HIS   A 244 ? 0.442 0.134 0.508 0.134  -0.076 -0.017 243 HIS   AAA CA  
1870 C  C   . HIS   A 244 ? 0.440 0.184 0.379 0.062  -0.001 0.018  243 HIS   AAA C   
1871 O  O   . HIS   A 244 ? 0.451 0.204 0.392 0.081  -0.013 0.034  243 HIS   AAA O   
1872 C  CB  . HIS   A 244 ? 0.488 0.211 0.488 0.193  0.047  -0.033 243 HIS   AAA CB  
1873 C  CG  . HIS   A 244 ? 0.559 0.177 0.554 0.058  0.020  -0.039 243 HIS   AAA CG  
1874 N  ND1 . HIS   A 244 ? 0.571 0.285 0.522 0.065  0.017  -0.080 243 HIS   AAA ND1 
1875 C  CD2 . HIS   A 244 ? 0.536 0.340 0.588 -0.060 0.017  0.093  243 HIS   AAA CD2 
1876 C  CE1 . HIS   A 244 ? 0.581 0.497 0.461 0.016  -0.021 0.037  243 HIS   AAA CE1 
1877 N  NE2 . HIS   A 244 ? 0.524 0.218 0.518 -0.009 0.002  0.052  243 HIS   AAA NE2 
1878 N  N   . ASN   A 245 ? 0.434 0.342 0.360 0.071  -0.011 -0.051 244 ASN   AAA N   
1879 C  CA  . ASN   A 245 ? 0.433 0.170 0.366 0.093  0.003  -0.086 244 ASN   AAA CA  
1880 C  C   . ASN   A 245 ? 0.416 0.249 0.369 0.034  0.042  -0.101 244 ASN   AAA C   
1881 O  O   . ASN   A 245 ? 0.436 0.069 0.464 -0.026 0.009  -0.036 244 ASN   AAA O   
1882 C  CB  . ASN   A 245 ? 0.443 0.153 0.385 0.123  0.027  -0.068 244 ASN   AAA CB  
1883 C  CG  . ASN   A 245 ? 0.406 0.242 0.373 0.057  0.064  -0.124 244 ASN   AAA CG  
1884 O  OD1 . ASN   A 245 ? 0.467 0.075 0.378 0.056  0.029  -0.056 244 ASN   AAA OD1 
1885 N  ND2 . ASN   A 245 ? 0.443 0.200 0.348 0.073  0.002  -0.096 244 ASN   AAA ND2 
1886 N  N   . ASN   A 246 ? 0.421 0.173 0.333 0.071  0.020  -0.044 245 ASN   AAA N   
1887 C  CA  . ASN   A 246 ? 0.365 0.140 0.392 0.088  -0.007 -0.066 245 ASN   AAA CA  
1888 C  C   . ASN   A 246 ? 0.432 0.195 0.469 0.024  -0.038 -0.031 245 ASN   AAA C   
1889 O  O   . ASN   A 246 ? 0.521 0.217 0.475 0.078  0.004  -0.000 245 ASN   AAA O   
1890 C  CB  . ASN   A 246 ? 0.372 0.184 0.408 0.020  0.019  -0.051 245 ASN   AAA CB  
1891 C  CG  . ASN   A 246 ? 0.508 0.059 0.439 0.052  0.006  -0.030 245 ASN   AAA CG  
1892 O  OD1 . ASN   A 246 ? 0.547 0.175 0.490 0.068  0.063  -0.042 245 ASN   AAA OD1 
1893 N  ND2 . ASN   A 246 ? 0.372 0.141 0.434 0.071  0.003  -0.073 245 ASN   AAA ND2 
1894 N  N   . ARG   A 247 ? 0.357 0.043 0.474 0.005  0.039  -0.020 246 ARG   AAA N   
1895 C  CA  . ARG   A 247 ? 0.432 0.056 0.436 -0.046 0.093  -0.007 246 ARG   AAA CA  
1896 C  C   . ARG   A 247 ? 0.429 0.028 0.454 0.086  0.037  -0.035 246 ARG   AAA C   
1897 O  O   . ARG   A 247 ? 0.416 0.082 0.457 -0.003 0.011  -0.030 246 ARG   AAA O   
1898 C  CB  . ARG   A 247 ? 0.428 0.030 0.414 -0.036 0.064  -0.043 246 ARG   AAA CB  
1899 C  CG  . ARG   A 247 ? 0.413 0.124 0.458 -0.092 0.076  -0.049 246 ARG   AAA CG  
1900 C  CD  . ARG   A 247 ? 0.402 0.206 0.449 -0.085 0.026  -0.040 246 ARG   AAA CD  
1901 N  NE  . ARG   A 247 ? 0.434 0.030 0.474 -0.011 0.079  -0.062 246 ARG   AAA NE  
1902 C  CZ  . ARG   A 247 ? 0.466 0.074 0.493 -0.028 0.029  -0.072 246 ARG   AAA CZ  
1903 N  NH1 . ARG   A 247 ? 0.448 0.165 0.502 0.015  -0.003 -0.116 246 ARG   AAA NH1 
1904 N  NH2 . ARG   A 247 ? 0.596 0.019 0.629 -0.030 0.062  -0.086 246 ARG   AAA NH2 
1905 N  N   . PRO   A 248 ? 0.462 0.017 0.475 0.045  0.036  -0.046 247 PRO   AAA N   
1906 C  CA  . PRO   A 248 ? 0.468 0.006 0.478 0.001  0.053  -0.000 247 PRO   AAA CA  
1907 C  C   . PRO   A 248 ? 0.471 0.092 0.394 -0.022 0.060  -0.058 247 PRO   AAA C   
1908 O  O   . PRO   A 248 ? 0.512 0.038 0.526 -0.026 0.057  -0.080 247 PRO   AAA O   
1909 C  CB  . PRO   A 248 ? 0.541 0.007 0.495 0.009  0.083  0.008  247 PRO   AAA CB  
1910 C  CG  . PRO   A 248 ? 0.499 0.134 0.497 0.019  0.103  -0.024 247 PRO   AAA CG  
1911 C  CD  . PRO   A 248 ? 0.453 0.187 0.407 0.105  0.054  -0.023 247 PRO   AAA CD  
1912 N  N   . THR   A 249 ? 0.443 0.038 0.405 -0.001 0.082  -0.074 248 THR   AAA N   
1913 C  CA  . THR   A 249 ? 0.464 0.023 0.441 -0.030 0.023  -0.082 248 THR   AAA CA  
1914 C  C   . THR   A 249 ? 0.452 0.165 0.487 -0.088 -0.028 0.026  248 THR   AAA C   
1915 O  O   . THR   A 249 ? 0.599 0.205 0.407 0.052  0.020  -0.038 248 THR   AAA O   
1916 C  CB  . THR   A 249 ? 0.485 0.069 0.504 -0.008 0.088  -0.074 248 THR   AAA CB  
1917 O  OG1 . THR   A 249 ? 0.473 0.177 0.494 0.045  0.021  -0.207 248 THR   AAA OG1 
1918 C  CG2 . THR   A 249 ? 0.464 0.083 0.439 -0.012 0.055  -0.132 248 THR   AAA CG2 
1919 N  N   . GLN   A 250 ? 0.422 0.202 0.441 -0.035 0.016  -0.103 249 GLN   AAA N   
1920 C  CA  . GLN   A 250 ? 0.439 0.192 0.455 0.016  0.029  -0.102 249 GLN   AAA CA  
1921 C  C   . GLN   A 250 ? 0.422 0.212 0.417 0.003  0.039  -0.064 249 GLN   AAA C   
1922 O  O   . GLN   A 250 ? 0.559 0.145 0.442 -0.074 0.064  -0.098 249 GLN   AAA O   
1923 C  CB  . GLN   A 250 ? 0.441 0.037 0.534 -0.006 0.037  -0.095 249 GLN   AAA CB  
1924 C  CG  . GLN   A 250 ? 0.458 0.049 0.554 -0.103 0.032  -0.099 249 GLN   AAA CG  
1925 C  CD  . GLN   A 250 ? 0.461 0.222 0.577 -0.020 0.078  -0.004 249 GLN   AAA CD  
1926 O  OE1 . GLN   A 250 ? 0.608 0.280 0.538 -0.152 0.096  -0.083 249 GLN   AAA OE1 
1927 N  NE2 . GLN   A 250 ? 0.543 0.196 0.470 0.049  0.033  -0.139 249 GLN   AAA NE2 
1928 N  N   . PRO   A 251 ? 0.599 0.217 0.562 -0.068 0.022  -0.128 250 PRO   AAA N   
1929 C  CA  . PRO   A 251 ? 0.698 0.136 0.585 -0.101 0.018  -0.175 250 PRO   AAA CA  
1930 C  C   . PRO   A 251 ? 0.551 0.316 0.453 -0.079 0.050  -0.182 250 PRO   AAA C   
1931 O  O   . PRO   A 251 ? 0.630 0.146 0.558 -0.049 0.082  -0.218 250 PRO   AAA O   
1932 C  CB  . PRO   A 251 ? 0.603 0.211 0.665 -0.113 -0.018 -0.060 250 PRO   AAA CB  
1933 C  CG  . PRO   A 251 ? 0.700 0.211 0.675 -0.030 -0.045 -0.147 250 PRO   AAA CG  
1934 C  CD  . PRO   A 251 ? 0.595 0.076 0.683 0.060  0.022  -0.106 250 PRO   AAA CD  
1935 N  N   . LEU   A 252 ? 0.595 0.191 0.455 -0.056 0.018  -0.132 251 LEU   AAA N   
1936 C  CA  . LEU   A 252 ? 0.623 0.089 0.586 -0.105 -0.017 -0.170 251 LEU   AAA CA  
1937 C  C   . LEU   A 252 ? 0.552 0.080 0.619 -0.019 -0.031 -0.134 251 LEU   AAA C   
1938 O  O   . LEU   A 252 ? 0.549 0.142 0.569 0.017  0.018  -0.163 251 LEU   AAA O   
1939 C  CB  . LEU   A 252 ? 0.601 0.425 0.595 -0.122 0.029  -0.225 251 LEU   AAA CB  
1940 C  CG  . LEU   A 252 ? 0.746 0.307 0.649 -0.040 0.115  -0.084 251 LEU   AAA CG  
1941 C  CD1 . LEU   A 252 ? 0.797 0.346 0.691 -0.018 0.161  -0.010 251 LEU   AAA CD1 
1942 C  CD2 . LEU   A 252 ? 0.509 0.297 0.613 -0.124 0.054  -0.113 251 LEU   AAA CD2 
1943 N  N   . LYS   A 253 ? 0.782 0.095 0.662 -0.093 0.055  -0.217 252 LYS   AAA N   
1944 C  CA  . LYS   A 253 ? 0.638 0.353 0.659 -0.021 -0.010 -0.240 252 LYS   AAA CA  
1945 C  C   . LYS   A 253 ? 0.586 0.229 0.545 -0.081 0.083  -0.152 252 LYS   AAA C   
1946 O  O   . LYS   A 253 ? 0.552 0.192 0.610 -0.055 0.014  -0.123 252 LYS   AAA O   
1947 C  CB  . LYS   A 253 ? 0.548 0.095 0.651 -0.146 -0.006 -0.025 252 LYS   AAA CB  
1948 C  CG  . LYS   A 253 ? 0.509 0.536 0.698 -0.012 -0.025 -0.010 252 LYS   AAA CG  
1949 C  CD  . LYS   A 253 ? 0.529 0.292 0.832 0.063  -0.070 0.013  252 LYS   AAA CD  
1950 C  CE  . LYS   A 253 ? 0.558 0.449 0.763 0.180  0.023  0.080  252 LYS   AAA CE  
1951 N  NZ  . LYS   A 253 ? 0.618 1.023 0.887 -0.033 0.007  0.230  252 LYS   AAA NZ  
1952 N  N   . GLY   A 254 ? 0.711 0.300 0.491 -0.191 -0.030 -0.120 253 GLY   AAA N   
1953 C  CA  . GLY   A 254 ? 0.617 0.231 0.582 -0.187 -0.027 -0.102 253 GLY   AAA CA  
1954 C  C   . GLY   A 254 ? 0.639 0.245 0.528 -0.008 -0.117 -0.170 253 GLY   AAA C   
1955 O  O   . GLY   A 254 ? 0.757 0.390 0.432 -0.064 -0.079 -0.127 253 GLY   AAA O   
1956 N  N   . ARG   A 255 ? 0.553 0.243 0.492 -0.057 -0.057 -0.154 254 ARG   AAA N   
1957 C  CA  . ARG   A 255 ? 0.575 0.282 0.453 -0.148 -0.017 -0.139 254 ARG   AAA CA  
1958 C  C   . ARG   A 255 ? 0.473 0.349 0.450 0.009  -0.007 -0.127 254 ARG   AAA C   
1959 O  O   . ARG   A 255 ? 0.577 0.278 0.584 0.000  0.030  -0.211 254 ARG   AAA O   
1960 C  CB  . ARG   A 255 ? 0.574 0.221 0.442 -0.066 -0.004 -0.169 254 ARG   AAA CB  
1961 C  CG  . ARG   A 255 ? 0.535 0.116 0.514 -0.084 0.022  -0.105 254 ARG   AAA CG  
1962 C  CD  . ARG   A 255 ? 0.544 0.318 0.479 -0.090 -0.026 -0.019 254 ARG   AAA CD  
1963 N  NE  . ARG   A 255 ? 0.511 0.113 0.516 -0.113 -0.000 -0.204 254 ARG   AAA NE  
1964 C  CZ  . ARG   A 255 ? 0.434 0.100 0.561 -0.084 0.011  -0.208 254 ARG   AAA CZ  
1965 N  NH1 . ARG   A 255 ? 0.541 0.100 0.485 -0.130 0.060  -0.186 254 ARG   AAA NH1 
1966 N  NH2 . ARG   A 255 ? 0.468 0.132 0.420 -0.084 0.035  -0.095 254 ARG   AAA NH2 
1967 N  N   . THR   A 256 ? 0.583 0.327 0.389 -0.025 -0.024 -0.133 255 THR   AAA N   
1968 C  CA  . THR   A 256 ? 0.585 0.258 0.487 -0.083 0.033  -0.119 255 THR   AAA CA  
1969 C  C   . THR   A 256 ? 0.501 0.331 0.401 -0.099 0.050  -0.125 255 THR   AAA C   
1970 O  O   . THR   A 256 ? 0.548 0.374 0.523 -0.133 0.069  -0.186 255 THR   AAA O   
1971 C  CB  . THR   A 256 ? 0.537 0.370 0.593 -0.112 0.002  -0.058 255 THR   AAA CB  
1972 O  OG1 . THR   A 256 ? 0.595 0.617 0.809 -0.309 -0.029 -0.097 255 THR   AAA OG1 
1973 C  CG2 . THR   A 256 ? 0.629 0.861 0.479 -0.172 0.017  -0.056 255 THR   AAA CG2 
1974 N  N   . VAL   A 257 ? 0.464 0.187 0.522 -0.031 -0.023 -0.193 256 VAL   AAA N   
1975 C  CA  . VAL   A 257 ? 0.500 0.268 0.510 -0.093 0.003  -0.188 256 VAL   AAA CA  
1976 C  C   . VAL   A 257 ? 0.559 0.256 0.490 -0.053 -0.002 -0.219 256 VAL   AAA C   
1977 O  O   . VAL   A 257 ? 0.551 0.276 0.507 0.050  -0.007 -0.184 256 VAL   AAA O   
1978 C  CB  . VAL   A 257 ? 0.522 0.246 0.459 -0.030 0.064  -0.218 256 VAL   AAA CB  
1979 C  CG1 . VAL   A 257 ? 0.593 0.223 0.479 -0.076 0.030  -0.114 256 VAL   AAA CG1 
1980 C  CG2 . VAL   A 257 ? 0.546 0.355 0.450 0.033  -0.060 -0.209 256 VAL   AAA CG2 
1981 N  N   . ARG   A 258 ? 0.505 0.314 0.421 0.017  0.006  -0.210 257 ARG   AAA N   
1982 C  CA  . ARG   A 258 ? 0.489 0.335 0.465 -0.076 -0.057 -0.177 257 ARG   AAA CA  
1983 C  C   . ARG   A 258 ? 0.412 0.397 0.426 -0.024 -0.020 -0.129 257 ARG   AAA C   
1984 O  O   . ARG   A 258 ? 0.471 0.318 0.453 -0.034 -0.034 -0.150 257 ARG   AAA O   
1985 C  CB  . ARG   A 258 ? 0.508 0.352 0.457 -0.056 -0.098 -0.148 257 ARG   AAA CB  
1986 C  CG  . ARG   A 258 ? 0.563 0.304 0.414 -0.050 -0.046 -0.131 257 ARG   AAA CG  
1987 C  CD  . ARG   A 258 ? 0.539 0.331 0.466 -0.053 -0.035 -0.110 257 ARG   AAA CD  
1988 N  NE  . ARG   A 258 ? 0.554 0.508 0.510 0.045  -0.076 -0.182 257 ARG   AAA NE  
1989 C  CZ  . ARG   A 258 ? 0.483 0.470 0.425 0.009  -0.138 -0.168 257 ARG   AAA CZ  
1990 N  NH1 . ARG   A 258 ? 0.678 0.386 0.548 -0.017 -0.116 -0.123 257 ARG   AAA NH1 
1991 N  NH2 . ARG   A 258 ? 0.518 0.737 0.452 -0.017 -0.072 -0.208 257 ARG   AAA NH2 
1992 N  N   . ALA   A 259 ? 0.464 0.339 0.418 -0.028 -0.017 -0.140 258 ALA   AAA N   
1993 C  CA  . ALA   A 259 ? 0.398 0.500 0.408 -0.026 -0.016 -0.047 258 ALA   AAA CA  
1994 C  C   . ALA   A 259 ? 0.434 0.417 0.483 -0.034 -0.017 -0.108 258 ALA   AAA C   
1995 O  O   . ALA   A 259 ? 0.540 0.523 0.437 0.046  0.008  -0.155 258 ALA   AAA O   
1996 C  CB  . ALA   A 259 ? 0.483 0.421 0.433 -0.030 0.001  -0.078 258 ALA   AAA CB  
1997 N  N   . SER   A 260 ? 0.425 0.432 0.403 0.021  -0.111 -0.097 259 SER   AAA N   
1998 C  CA  . SER   A 260 ? 0.466 0.411 0.414 0.024  -0.044 -0.113 259 SER   AAA CA  
1999 C  C   . SER   A 260 ? 0.496 0.521 0.354 0.105  -0.078 -0.064 259 SER   AAA C   
2000 O  O   . SER   A 260 ? 0.603 0.444 0.375 0.057  -0.063 -0.087 259 SER   AAA O   
2001 C  CB  . SER   A 260 ? 0.453 0.396 0.364 0.025  -0.070 -0.088 259 SER   AAA CB  
2002 O  OG  . SER   A 260 ? 0.456 0.250 0.485 0.081  -0.046 -0.147 259 SER   AAA OG  
2003 N  N   . PHE   A 261 ? 0.553 0.462 0.487 0.038  0.016  -0.173 260 PHE   AAA N   
2004 C  CA  . PHE   A 261 ? 0.537 0.569 0.443 0.107  -0.005 -0.195 260 PHE   AAA CA  
2005 C  C   . PHE   A 261 ? 0.652 0.503 0.401 -0.006 -0.020 -0.161 260 PHE   AAA C   
2006 O  O   . PHE   A 261 ? 0.560 0.594 0.492 -0.028 -0.002 -0.164 260 PHE   AAA O   
2007 C  CB  . PHE   A 261 ? 0.465 0.613 0.531 0.070  0.028  -0.077 260 PHE   AAA CB  
2008 C  CG  . PHE   A 261 ? 0.516 0.420 0.544 0.036  0.023  -0.134 260 PHE   AAA CG  
2009 C  CD1 . PHE   A 261 ? 0.440 0.417 0.479 0.077  0.009  -0.148 260 PHE   AAA CD1 
2010 C  CD2 . PHE   A 261 ? 0.513 0.509 0.600 0.109  -0.001 -0.097 260 PHE   AAA CD2 
2011 C  CE1 . PHE   A 261 ? 0.492 0.535 0.397 0.032  0.008  -0.164 260 PHE   AAA CE1 
2012 C  CE2 . PHE   A 261 ? 0.525 0.600 0.532 0.217  0.028  -0.138 260 PHE   AAA CE2 
2013 C  CZ  . PHE   A 261 ? 0.538 0.437 0.539 0.058  0.015  -0.120 260 PHE   AAA CZ  
2014 O  OXT . PHE   A 261 ? 0.585 0.559 0.416 0.024  0.003  -0.062 260 PHE   AAA OXT 
2015 N  N   . ASP   B 5   ? 0.516 0.465 0.552 0.019  -0.009 -0.043 4   ASP   BBB N   
2016 C  CA  . ASP   B 5   ? 0.509 0.357 0.516 -0.033 -0.059 0.043  4   ASP   BBB CA  
2017 C  C   . ASP   B 5   ? 0.610 0.318 0.480 0.048  0.011  -0.045 4   ASP   BBB C   
2018 O  O   . ASP   B 5   ? 0.589 0.301 0.569 0.053  0.024  -0.017 4   ASP   BBB O   
2019 C  CB  . ASP   B 5   ? 0.456 0.540 0.516 -0.001 -0.009 0.021  4   ASP   BBB CB  
2020 C  CG  . ASP   B 5   ? 0.556 0.587 0.485 0.042  -0.059 -0.220 4   ASP   BBB CG  
2021 O  OD1 . ASP   B 5   ? 0.636 0.398 0.598 0.027  0.001  -0.090 4   ASP   BBB OD1 
2022 O  OD2 . ASP   B 5   ? 0.560 0.526 0.588 -0.066 -0.086 -0.037 4   ASP   BBB OD2 
2023 N  N   . TRP   B 6   ? 0.814 0.215 0.637 0.072  0.015  -0.104 5   TRP   BBB N   
2024 C  CA  . TRP   B 6   ? 0.617 0.148 0.580 0.040  -0.032 -0.061 5   TRP   BBB CA  
2025 C  C   . TRP   B 6   ? 0.542 0.301 0.546 0.025  -0.000 -0.025 5   TRP   BBB C   
2026 O  O   . TRP   B 6   ? 0.676 0.192 0.528 0.012  -0.044 -0.129 5   TRP   BBB O   
2027 C  CB  . TRP   B 6   ? 0.591 0.071 0.572 0.018  -0.008 0.001  5   TRP   BBB CB  
2028 C  CG  . TRP   B 6   ? 0.504 0.112 0.489 0.029  0.035  -0.101 5   TRP   BBB CG  
2029 C  CD1 . TRP   B 6   ? 0.534 0.141 0.502 0.027  0.050  -0.134 5   TRP   BBB CD1 
2030 C  CD2 . TRP   B 6   ? 0.499 0.111 0.422 -0.001 0.011  -0.082 5   TRP   BBB CD2 
2031 N  NE1 . TRP   B 6   ? 0.542 0.087 0.522 0.057  -0.019 -0.065 5   TRP   BBB NE1 
2032 C  CE2 . TRP   B 6   ? 0.509 0.153 0.502 -0.032 0.038  -0.102 5   TRP   BBB CE2 
2033 C  CE3 . TRP   B 6   ? 0.555 0.181 0.478 0.007  0.068  -0.101 5   TRP   BBB CE3 
2034 C  CZ2 . TRP   B 6   ? 0.527 0.099 0.469 0.104  -0.008 -0.003 5   TRP   BBB CZ2 
2035 C  CZ3 . TRP   B 6   ? 0.505 0.131 0.536 -0.005 0.025  -0.085 5   TRP   BBB CZ3 
2036 C  CH2 . TRP   B 6   ? 0.496 0.074 0.427 0.037  -0.011 -0.078 5   TRP   BBB CH2 
2037 N  N   . GLY   B 7   ? 0.547 0.051 0.545 -0.010 0.009  -0.141 6   GLY   BBB N   
2038 C  CA  . GLY   B 7   ? 0.529 0.284 0.546 0.058  -0.029 -0.138 6   GLY   BBB CA  
2039 C  C   . GLY   B 7   ? 0.514 0.188 0.590 -0.025 -0.052 -0.176 6   GLY   BBB C   
2040 O  O   . GLY   B 7   ? 0.593 0.154 0.633 0.042  -0.097 -0.163 6   GLY   BBB O   
2041 N  N   . TYR   B 8   ? 0.549 0.137 0.611 -0.032 0.002  -0.146 7   TYR   BBB N   
2042 C  CA  . TYR   B 8   ? 0.554 0.180 0.612 -0.042 0.079  -0.204 7   TYR   BBB CA  
2043 C  C   . TYR   B 8   ? 0.582 0.206 0.615 -0.106 0.091  -0.176 7   TYR   BBB C   
2044 O  O   . TYR   B 8   ? 0.684 0.092 0.617 -0.074 0.104  -0.123 7   TYR   BBB O   
2045 C  CB  . TYR   B 8   ? 0.554 0.105 0.516 0.007  -0.007 -0.136 7   TYR   BBB CB  
2046 C  CG  . TYR   B 8   ? 0.520 0.126 0.451 -0.009 -0.016 -0.072 7   TYR   BBB CG  
2047 C  CD1 . TYR   B 8   ? 0.488 0.085 0.431 0.044  -0.024 -0.091 7   TYR   BBB CD1 
2048 C  CD2 . TYR   B 8   ? 0.528 0.117 0.415 -0.012 -0.029 -0.071 7   TYR   BBB CD2 
2049 C  CE1 . TYR   B 8   ? 0.564 0.009 0.395 -0.011 0.032  -0.031 7   TYR   BBB CE1 
2050 C  CE2 . TYR   B 8   ? 0.494 0.017 0.498 0.029  -0.058 -0.044 7   TYR   BBB CE2 
2051 C  CZ  . TYR   B 8   ? 0.505 0.008 0.421 0.021  -0.019 -0.021 7   TYR   BBB CZ  
2052 O  OH  . TYR   B 8   ? 0.438 0.043 0.485 0.041  -0.009 -0.041 7   TYR   BBB OH  
2053 N  N   . ASP   B 9   ? 0.728 0.163 0.763 -0.012 0.016  -0.329 8   ASP   BBB N   
2054 C  CA  . ASP   B 9   ? 0.580 0.441 0.810 -0.175 -0.065 -0.277 8   ASP   BBB CA  
2055 C  C   . ASP   B 9   ? 0.802 0.256 0.709 -0.346 0.053  -0.106 8   ASP   BBB C   
2056 O  O   . ASP   B 9   ? 0.878 0.268 0.797 -0.186 0.085  -0.180 8   ASP   BBB O   
2057 C  CB  . ASP   B 9   ? 0.763 0.718 0.903 -0.249 -0.241 -0.091 8   ASP   BBB CB  
2058 C  CG  . ASP   B 9   ? 0.903 1.046 1.013 -0.132 -0.389 -0.020 8   ASP   BBB CG  
2059 O  OD1 . ASP   B 9   ? 1.109 1.010 1.208 -0.326 -0.151 -0.232 8   ASP   BBB OD1 
2060 O  OD2 . ASP   B 9   ? 1.260 1.831 0.925 -0.441 0.156  -0.219 8   ASP   BBB OD2 
2061 N  N   . ASP   B 10  ? 0.773 0.347 1.046 -0.370 0.089  -0.282 9   ASP   BBB N   
2062 C  CA  . ASP   B 10  ? 0.763 0.581 0.968 -0.204 0.117  -0.165 9   ASP   BBB CA  
2063 C  C   . ASP   B 10  ? 0.822 0.218 0.785 0.083  -0.056 -0.266 9   ASP   BBB C   
2064 O  O   . ASP   B 10  ? 0.865 0.703 0.825 0.323  0.080  -0.029 9   ASP   BBB O   
2065 C  CB  . ASP   B 10  ? 0.715 0.820 0.989 -0.291 0.053  -0.134 9   ASP   BBB CB  
2066 C  CG  . ASP   B 10  ? 0.865 0.879 1.095 -0.240 0.180  -0.032 9   ASP   BBB CG  
2067 O  OD1 . ASP   B 10  ? 0.946 0.545 1.026 0.120  -0.138 0.176  9   ASP   BBB OD1 
2068 O  OD2 . ASP   B 10  ? 1.221 0.847 1.531 -0.550 0.179  -0.406 9   ASP   BBB OD2 
2069 N  N   . LYS   B 11  ? 0.758 0.290 0.801 -0.090 -0.080 -0.194 10  LYS   BBB N   
2070 C  CA  . LYS   B 11  ? 0.691 0.266 0.862 0.039  -0.059 -0.031 10  LYS   BBB CA  
2071 C  C   . LYS   B 11  ? 0.717 0.255 0.799 0.102  -0.031 -0.435 10  LYS   BBB C   
2072 O  O   . LYS   B 11  ? 0.748 0.121 0.922 0.062  0.201  -0.121 10  LYS   BBB O   
2073 C  CB  . LYS   B 11  ? 0.672 0.042 0.893 -0.121 -0.105 0.079  10  LYS   BBB CB  
2074 N  N   . ASN   B 12  ? 0.903 0.159 1.034 0.110  0.068  -0.369 11  ASN   BBB N   
2075 C  CA  . ASN   B 12  ? 0.995 0.238 0.561 0.011  -0.031 -0.127 11  ASN   BBB CA  
2076 C  C   . ASN   B 12  ? 0.724 0.198 0.580 -0.027 0.021  -0.169 11  ASN   BBB C   
2077 O  O   . ASN   B 12  ? 0.662 0.210 0.522 -0.048 0.061  -0.090 11  ASN   BBB O   
2078 C  CB  . ASN   B 12  ? 1.009 0.146 0.647 0.252  -0.101 -0.130 11  ASN   BBB CB  
2079 C  CG  . ASN   B 12  ? 0.830 0.460 0.498 0.274  -0.132 0.012  11  ASN   BBB CG  
2080 O  OD1 . ASN   B 12  ? 0.810 0.157 0.654 -0.063 -0.041 -0.091 11  ASN   BBB OD1 
2081 N  ND2 . ASN   B 12  ? 1.097 0.238 0.522 0.237  0.087  0.003  11  ASN   BBB ND2 
2082 N  N   . GLY   B 13  ? 0.718 0.248 0.596 -0.013 0.064  -0.118 12  GLY   BBB N   
2083 C  CA  . GLY   B 13  ? 0.609 0.226 0.598 -0.062 0.036  -0.120 12  GLY   BBB CA  
2084 C  C   . GLY   B 13  ? 0.654 0.279 0.613 0.044  0.072  -0.166 12  GLY   BBB C   
2085 O  O   . GLY   B 13  ? 0.680 0.101 0.798 -0.022 0.158  -0.132 12  GLY   BBB O   
2086 N  N   . PRO   B 14  ? 0.648 0.020 0.602 0.029  0.084  -0.082 13  PRO   BBB N   
2087 C  CA  . PRO   B 14  ? 0.596 0.131 0.598 0.002  0.114  -0.009 13  PRO   BBB CA  
2088 C  C   . PRO   B 14  ? 0.474 0.148 0.630 -0.004 0.104  -0.021 13  PRO   BBB C   
2089 O  O   . PRO   B 14  ? 0.506 0.061 0.660 0.012  0.082  -0.077 13  PRO   BBB O   
2090 C  CB  . PRO   B 14  ? 0.632 0.085 0.600 0.083  0.082  -0.059 13  PRO   BBB CB  
2091 C  CG  . PRO   B 14  ? 0.604 0.081 0.607 0.058  0.029  -0.162 13  PRO   BBB CG  
2092 C  CD  . PRO   B 14  ? 0.565 0.283 0.540 0.078  0.082  -0.132 13  PRO   BBB CD  
2093 N  N   . GLU   B 15  ? 0.539 0.237 0.653 -0.087 0.053  -0.022 14  GLU   BBB N   
2094 C  CA  . GLU   B 15  ? 0.614 0.237 0.652 -0.044 0.125  -0.047 14  GLU   BBB CA  
2095 C  C   . GLU   B 15  ? 0.694 0.134 0.697 0.047  0.114  0.006  14  GLU   BBB C   
2096 O  O   . GLU   B 15  ? 0.867 0.050 0.736 0.094  0.206  0.006  14  GLU   BBB O   
2097 C  CB  . GLU   B 15  ? 0.699 0.363 0.728 -0.167 0.063  -0.063 14  GLU   BBB CB  
2098 C  CG  . GLU   B 15  ? 0.936 0.377 0.793 -0.114 0.145  -0.070 14  GLU   BBB CG  
2099 C  CD  . GLU   B 15  ? 0.911 0.395 1.028 -0.306 0.052  0.054  14  GLU   BBB CD  
2100 O  OE1 . GLU   B 15  ? 1.151 0.535 1.175 -0.304 -0.037 -0.353 14  GLU   BBB OE1 
2101 O  OE2 . GLU   B 15  ? 1.000 0.436 0.819 -0.071 0.146  -0.274 14  GLU   BBB OE2 
2102 N  N   . GLN   B 16  ? 0.668 0.077 0.644 -0.088 -0.003 -0.053 15  GLN   BBB N   
2103 C  CA  . GLN   B 16  ? 0.590 0.163 0.783 -0.022 0.100  -0.019 15  GLN   BBB CA  
2104 C  C   . GLN   B 16  ? 0.946 0.014 0.781 -0.049 0.133  -0.066 15  GLN   BBB C   
2105 O  O   . GLN   B 16  ? 0.843 0.011 0.882 -0.032 0.073  -0.058 15  GLN   BBB O   
2106 C  CB  . GLN   B 16  ? 0.724 0.104 0.967 0.027  -0.051 -0.045 15  GLN   BBB CB  
2107 C  CG  . GLN   B 16  ? 0.864 0.029 0.982 0.017  -0.046 -0.147 15  GLN   BBB CG  
2108 C  CD  . GLN   B 16  ? 0.934 0.043 1.036 0.134  -0.071 -0.106 15  GLN   BBB CD  
2109 O  OE1 . GLN   B 16  ? 1.286 0.973 1.050 -0.083 -0.066 0.233  15  GLN   BBB OE1 
2110 N  NE2 . GLN   B 16  ? 0.727 0.156 1.179 -0.103 -0.048 -0.225 15  GLN   BBB NE2 
2111 N  N   . TRP   B 17  ? 0.612 0.079 0.676 0.002  0.111  -0.217 16  TRP   BBB N   
2112 C  CA  . TRP   B 17  ? 0.545 0.110 0.502 0.013  0.021  -0.080 16  TRP   BBB CA  
2113 C  C   . TRP   B 17  ? 0.577 0.072 0.536 0.035  0.135  -0.128 16  TRP   BBB C   
2114 O  O   . TRP   B 17  ? 0.613 0.009 0.645 -0.018 0.096  -0.039 16  TRP   BBB O   
2115 C  CB  . TRP   B 17  ? 0.522 0.063 0.636 0.100  0.034  -0.113 16  TRP   BBB CB  
2116 C  CG  . TRP   B 17  ? 0.463 0.073 0.549 0.043  0.037  -0.085 16  TRP   BBB CG  
2117 C  CD1 . TRP   B 17  ? 0.532 0.024 0.551 -0.040 -0.012 -0.087 16  TRP   BBB CD1 
2118 C  CD2 . TRP   B 17  ? 0.541 0.014 0.460 0.053  0.044  -0.026 16  TRP   BBB CD2 
2119 N  NE1 . TRP   B 17  ? 0.599 0.197 0.513 0.068  0.003  -0.189 16  TRP   BBB NE1 
2120 C  CE2 . TRP   B 17  ? 0.530 0.050 0.485 0.032  -0.000 -0.138 16  TRP   BBB CE2 
2121 C  CE3 . TRP   B 17  ? 0.559 0.019 0.464 0.076  0.047  -0.025 16  TRP   BBB CE3 
2122 C  CZ2 . TRP   B 17  ? 0.535 0.012 0.565 0.040  0.058  -0.036 16  TRP   BBB CZ2 
2123 C  CZ3 . TRP   B 17  ? 0.493 0.016 0.439 -0.051 0.045  -0.050 16  TRP   BBB CZ3 
2124 C  CH2 . TRP   B 17  ? 0.564 0.009 0.654 -0.000 0.012  -0.040 16  TRP   BBB CH2 
2125 N  N   . SER   B 18  ? 0.554 0.103 0.655 -0.032 0.042  -0.062 17  SER   BBB N   
2126 C  CA  . SER   B 18  ? 0.578 0.192 0.618 -0.033 0.032  -0.047 17  SER   BBB CA  
2127 C  C   . SER   B 18  ? 0.892 0.015 0.673 -0.045 0.001  -0.065 17  SER   BBB C   
2128 O  O   . SER   B 18  ? 0.900 0.026 0.871 0.131  0.147  0.037  17  SER   BBB O   
2129 C  CB  . SER   B 18  ? 0.598 0.145 0.649 0.017  0.018  -0.044 17  SER   BBB CB  
2130 O  OG  . SER   B 18  ? 0.705 0.094 0.605 0.034  0.001  -0.095 17  SER   BBB OG  
2131 N  N   . LYS   B 19  ? 0.806 0.038 0.587 0.125  0.151  -0.060 18  LYS   BBB N   
2132 C  CA  . LYS   B 19  ? 0.650 0.093 0.525 -0.003 0.123  -0.138 18  LYS   BBB CA  
2133 C  C   . LYS   B 19  ? 0.717 0.136 0.623 0.018  0.190  -0.057 18  LYS   BBB C   
2134 O  O   . LYS   B 19  ? 0.757 0.025 0.670 0.019  0.126  -0.106 18  LYS   BBB O   
2135 C  CB  . LYS   B 19  ? 0.524 0.020 0.729 -0.022 0.114  -0.081 18  LYS   BBB CB  
2136 C  CG  . LYS   B 19  ? 0.635 0.093 0.782 -0.086 0.148  -0.096 18  LYS   BBB CG  
2137 C  CD  . LYS   B 19  ? 0.883 0.179 1.164 -0.334 0.125  -0.276 18  LYS   BBB CD  
2138 C  CE  . LYS   B 19  ? 0.779 0.146 1.025 -0.203 0.109  0.009  18  LYS   BBB CE  
2139 N  NZ  . LYS   B 19  ? 0.860 0.198 1.016 -0.081 0.045  -0.073 18  LYS   BBB NZ  
2140 N  N   . LEU   B 20  ? 0.749 0.085 0.612 -0.038 0.111  0.030  19  LEU   BBB N   
2141 C  CA  . LEU   B 20  ? 0.683 0.086 0.584 -0.096 0.057  0.002  19  LEU   BBB CA  
2142 C  C   . LEU   B 20  ? 0.667 0.031 0.664 0.093  0.088  -0.073 19  LEU   BBB C   
2143 O  O   . LEU   B 20  ? 0.738 0.016 0.796 0.051  0.188  -0.054 19  LEU   BBB O   
2144 C  CB  . LEU   B 20  ? 0.645 0.321 0.665 -0.006 0.093  0.008  19  LEU   BBB CB  
2145 C  CG  . LEU   B 20  ? 0.855 0.430 0.650 -0.052 0.053  -0.005 19  LEU   BBB CG  
2146 C  CD1 . LEU   B 20  ? 0.906 0.684 0.480 0.057  0.053  -0.064 19  LEU   BBB CD1 
2147 C  CD2 . LEU   B 20  ? 0.796 0.576 0.716 -0.132 0.004  -0.168 19  LEU   BBB CD2 
2148 N  N   . TYR   B 21  ? 0.730 0.017 0.701 0.085  0.112  -0.003 20  TYR   BBB N   
2149 C  CA  . TYR   B 21  ? 0.591 0.086 0.502 0.144  0.070  -0.039 20  TYR   BBB CA  
2150 C  C   . TYR   B 21  ? 0.825 0.024 0.614 0.084  0.117  -0.061 20  TYR   BBB C   
2151 O  O   . TYR   B 21  ? 0.660 0.011 0.620 0.055  0.102  0.006  20  TYR   BBB O   
2152 C  CB  . TYR   B 21  ? 0.658 0.015 0.514 0.047  0.043  -0.047 20  TYR   BBB CB  
2153 C  CG  . TYR   B 21  ? 0.555 0.129 0.471 0.046  0.102  0.013  20  TYR   BBB CG  
2154 C  CD1 . TYR   B 21  ? 0.619 0.017 0.639 0.080  0.034  -0.003 20  TYR   BBB CD1 
2155 C  CD2 . TYR   B 21  ? 0.631 0.007 0.608 -0.001 0.096  -0.020 20  TYR   BBB CD2 
2156 C  CE1 . TYR   B 21  ? 0.570 0.193 0.548 0.141  -0.002 0.009  20  TYR   BBB CE1 
2157 C  CE2 . TYR   B 21  ? 0.684 0.065 0.644 0.128  0.103  0.053  20  TYR   BBB CE2 
2158 C  CZ  . TYR   B 21  ? 0.603 0.150 0.625 0.050  0.032  0.032  20  TYR   BBB CZ  
2159 O  OH  . TYR   B 21  ? 0.817 0.131 0.592 0.077  -0.003 -0.079 20  TYR   BBB OH  
2160 N  N   . PRO   B 22  ? 0.590 0.049 0.528 0.118  0.123  -0.011 21  PRO   BBB N   
2161 C  CA  . PRO   B 22  ? 0.553 0.043 0.583 0.098  0.057  0.028  21  PRO   BBB CA  
2162 C  C   . PRO   B 22  ? 0.479 0.027 0.584 -0.013 0.068  0.032  21  PRO   BBB C   
2163 O  O   . PRO   B 22  ? 0.539 0.054 0.574 0.116  0.089  0.032  21  PRO   BBB O   
2164 C  CB  . PRO   B 22  ? 0.709 0.044 0.586 0.152  0.102  -0.033 21  PRO   BBB CB  
2165 C  CG  . PRO   B 22  ? 0.654 0.033 0.636 0.130  0.064  -0.008 21  PRO   BBB CG  
2166 C  CD  . PRO   B 22  ? 0.585 0.057 0.596 0.121  0.122  -0.095 21  PRO   BBB CD  
2167 N  N   . ILE   B 23  ? 0.529 0.023 0.671 0.038  0.125  -0.085 22  ILE   BBB N   
2168 C  CA  . ILE   B 23  ? 0.499 0.008 0.611 0.028  -0.048 0.009  22  ILE   BBB CA  
2169 C  C   . ILE   B 23  ? 0.756 0.055 0.660 0.174  0.043  0.082  22  ILE   BBB C   
2170 O  O   . ILE   B 23  ? 0.696 0.033 0.606 0.056  0.028  0.118  22  ILE   BBB O   
2171 C  CB  . ILE   B 23  ? 0.474 0.033 0.568 -0.082 0.024  0.048  22  ILE   BBB CB  
2172 C  CG1 . ILE   B 23  ? 0.500 0.170 0.523 0.068  0.021  0.017  22  ILE   BBB CG1 
2173 C  CG2 . ILE   B 23  ? 0.509 0.098 0.634 0.016  0.012  0.006  22  ILE   BBB CG2 
2174 C  CD1 . ILE   B 23  ? 0.564 0.212 0.631 0.051  0.049  0.178  22  ILE   BBB CD1 
2175 N  N   . ALA   B 24  ? 0.700 0.043 0.754 0.154  0.067  0.057  23  ALA   BBB N   
2176 C  CA  . ALA   B 24  ? 0.634 0.036 0.554 0.137  0.022  0.010  23  ALA   BBB CA  
2177 C  C   . ALA   B 24  ? 0.608 0.041 0.515 0.119  0.082  0.069  23  ALA   BBB C   
2178 O  O   . ALA   B 24  ? 0.647 0.008 0.631 -0.013 0.090  -0.028 23  ALA   BBB O   
2179 C  CB  . ALA   B 24  ? 0.614 0.044 0.612 0.136  0.033  0.073  23  ALA   BBB CB  
2180 N  N   . ASN   B 25  ? 0.577 0.046 0.540 0.112  0.027  -0.023 24  ASN   BBB N   
2181 C  CA  . ASN   B 25  ? 0.604 0.012 0.523 -0.058 0.044  -0.019 24  ASN   BBB CA  
2182 C  C   . ASN   B 25  ? 0.646 0.036 0.539 -0.024 -0.052 0.113  24  ASN   BBB C   
2183 O  O   . ASN   B 25  ? 0.618 0.035 0.536 0.103  0.017  0.079  24  ASN   BBB O   
2184 C  CB  . ASN   B 25  ? 0.704 0.039 0.559 0.011  0.031  -0.074 24  ASN   BBB CB  
2185 C  CG  . ASN   B 25  ? 0.749 0.062 0.657 -0.115 0.025  0.080  24  ASN   BBB CG  
2186 O  OD1 . ASN   B 25  ? 1.204 0.009 0.923 0.040  -0.195 0.022  24  ASN   BBB OD1 
2187 N  ND2 . ASN   B 25  ? 0.844 0.050 0.939 -0.129 0.163  0.039  24  ASN   BBB ND2 
2188 N  N   . GLY   B 26  ? 0.509 0.022 0.647 0.085  0.037  0.036  25  GLY   BBB N   
2189 C  CA  . GLY   B 26  ? 0.518 0.046 0.588 0.130  0.012  0.065  25  GLY   BBB CA  
2190 C  C   . GLY   B 26  ? 0.479 0.024 0.576 0.079  0.056  0.063  25  GLY   BBB C   
2191 O  O   . GLY   B 26  ? 0.522 0.036 0.608 0.071  0.101  0.033  25  GLY   BBB O   
2192 N  N   . ASN   B 27  ? 0.532 0.069 0.504 0.160  0.011  0.064  26  ASN   BBB N   
2193 C  CA  . ASN   B 27  ? 0.604 0.085 0.514 0.130  0.019  -0.011 26  ASN   BBB CA  
2194 C  C   . ASN   B 27  ? 0.682 0.055 0.499 0.165  -0.015 0.059  26  ASN   BBB C   
2195 O  O   . ASN   B 27  ? 0.657 0.033 0.555 0.118  0.029  0.060  26  ASN   BBB O   
2196 C  CB  . ASN   B 27  ? 0.546 0.135 0.545 0.112  0.081  0.060  26  ASN   BBB CB  
2197 C  CG  . ASN   B 27  ? 0.755 0.170 0.721 0.210  0.065  0.066  26  ASN   BBB CG  
2198 O  OD1 . ASN   B 27  ? 0.705 0.178 0.697 0.244  0.041  0.129  26  ASN   BBB OD1 
2199 N  ND2 . ASN   B 27  ? 0.836 0.236 0.837 0.327  0.046  0.049  26  ASN   BBB ND2 
2200 N  N   . ASN   B 28  ? 0.492 0.058 0.547 0.130  0.042  0.106  27  ASN   BBB N   
2201 C  CA  . ASN   B 28  ? 0.494 0.075 0.487 0.119  0.019  0.060  27  ASN   BBB CA  
2202 C  C   . ASN   B 28  ? 0.546 0.066 0.493 0.125  0.016  0.125  27  ASN   BBB C   
2203 O  O   . ASN   B 28  ? 0.494 0.042 0.520 0.109  0.023  0.081  27  ASN   BBB O   
2204 C  CB  . ASN   B 28  ? 0.440 0.169 0.537 0.112  0.007  0.101  27  ASN   BBB CB  
2205 C  CG  . ASN   B 28  ? 0.425 0.358 0.487 0.030  0.022  0.054  27  ASN   BBB CG  
2206 O  OD1 . ASN   B 28  ? 0.572 0.160 0.756 0.090  -0.019 0.082  27  ASN   BBB OD1 
2207 N  ND2 . ASN   B 28  ? 0.599 0.506 0.465 0.024  0.007  0.049  27  ASN   BBB ND2 
2208 N  N   . GLN   B 29  ? 0.527 0.040 0.618 0.132  0.027  0.023  28  GLN   BBB N   
2209 C  CA  . GLN   B 29  ? 0.420 0.108 0.425 0.059  0.040  0.017  28  GLN   BBB CA  
2210 C  C   . GLN   B 29  ? 0.490 0.012 0.456 0.049  0.008  -0.022 28  GLN   BBB C   
2211 O  O   . GLN   B 29  ? 0.640 0.008 0.525 0.016  0.026  0.021  28  GLN   BBB O   
2212 C  CB  . GLN   B 29  ? 0.482 0.154 0.451 0.037  -0.015 0.003  28  GLN   BBB CB  
2213 C  CG  . GLN   B 29  ? 0.542 0.169 0.461 0.093  0.011  0.027  28  GLN   BBB CG  
2214 C  CD  . GLN   B 29  ? 0.476 0.052 0.525 0.142  0.008  -0.034 28  GLN   BBB CD  
2215 O  OE1 . GLN   B 29  ? 0.509 0.012 0.507 0.044  0.013  0.034  28  GLN   BBB OE1 
2216 N  NE2 . GLN   B 29  ? 0.523 0.047 0.809 0.144  0.066  0.016  28  GLN   BBB NE2 
2217 N  N   . SER   B 30  ? 0.413 0.039 0.477 0.018  0.010  0.123  29  SER   BBB N   
2218 C  CA  . SER   B 30  ? 0.503 0.017 0.544 0.027  0.067  0.072  29  SER   BBB CA  
2219 C  C   . SER   B 30  ? 0.614 0.018 0.568 -0.019 0.052  0.076  29  SER   BBB C   
2220 O  O   . SER   B 30  ? 0.612 0.013 0.577 0.042  0.052  0.051  29  SER   BBB O   
2221 C  CB  . SER   B 30  ? 0.438 0.023 0.577 0.069  0.018  0.061  29  SER   BBB CB  
2222 O  OG  . SER   B 30  ? 0.496 0.011 0.563 0.049  0.050  -0.001 29  SER   BBB OG  
2223 N  N   . PRO   B 31  ? 0.611 0.023 0.443 -0.012 0.055  0.083  30  PRO   BBB N   
2224 C  CA  . PRO   B 31  ? 0.494 0.058 0.390 -0.001 0.042  0.140  30  PRO   BBB CA  
2225 C  C   . PRO   B 31  ? 0.432 0.015 0.415 0.031  0.023  0.054  30  PRO   BBB C   
2226 O  O   . PRO   B 31  ? 0.507 0.016 0.507 0.070  0.062  0.000  30  PRO   BBB O   
2227 C  CB  . PRO   B 31  ? 0.468 0.014 0.371 -0.042 0.051  -0.041 30  PRO   BBB CB  
2228 C  CG  . PRO   B 31  ? 0.573 0.010 0.522 -0.043 0.028  -0.002 30  PRO   BBB CG  
2229 C  CD  . PRO   B 31  ? 0.573 0.007 0.514 0.020  0.010  -0.005 30  PRO   BBB CD  
2230 N  N   . VAL   B 32  ? 0.497 0.009 0.422 0.006  0.036  0.033  31  VAL   BBB N   
2231 C  CA  . VAL   B 32  ? 0.489 0.023 0.469 -0.037 0.046  0.075  31  VAL   BBB CA  
2232 C  C   . VAL   B 32  ? 0.501 0.060 0.483 0.008  0.054  0.159  31  VAL   BBB C   
2233 O  O   . VAL   B 32  ? 0.543 0.010 0.462 -0.014 0.019  0.041  31  VAL   BBB O   
2234 C  CB  . VAL   B 32  ? 0.517 0.006 0.486 0.004  0.014  0.006  31  VAL   BBB CB  
2235 C  CG1 . VAL   B 32  ? 0.533 0.056 0.588 0.069  0.044  0.103  31  VAL   BBB CG1 
2236 C  CG2 . VAL   B 32  ? 0.493 0.006 0.496 0.004  0.032  -0.007 31  VAL   BBB CG2 
2237 N  N   . ASP   B 33  ? 0.598 0.016 0.527 0.035  0.054  0.066  32  ASP   BBB N   
2238 C  CA  . ASP   B 33  ? 0.499 0.030 0.585 -0.008 0.062  0.114  32  ASP   BBB CA  
2239 C  C   . ASP   B 33  ? 0.490 0.111 0.514 0.035  0.098  0.015  32  ASP   BBB C   
2240 O  O   . ASP   B 33  ? 0.529 0.060 0.605 -0.060 0.026  0.031  32  ASP   BBB O   
2241 C  CB  . ASP   B 33  ? 0.531 0.059 0.488 -0.056 -0.003 0.150  32  ASP   BBB CB  
2242 C  CG  . ASP   B 33  ? 0.564 0.161 0.475 0.069  0.001  0.140  32  ASP   BBB CG  
2243 O  OD1 . ASP   B 33  ? 0.514 0.020 0.488 -0.055 0.054  0.054  32  ASP   BBB OD1 
2244 O  OD2 . ASP   B 33  ? 0.722 0.054 0.554 0.150  -0.057 0.082  32  ASP   BBB OD2 
2245 N  N   . ILE   B 34  ? 0.487 0.031 0.459 0.075  0.026  0.082  33  ILE   BBB N   
2246 C  CA  . ILE   B 34  ? 0.440 0.032 0.442 0.067  0.013  0.083  33  ILE   BBB CA  
2247 C  C   . ILE   B 34  ? 0.433 0.014 0.429 0.024  -0.015 0.048  33  ILE   BBB C   
2248 O  O   . ILE   B 34  ? 0.510 0.027 0.498 0.048  0.028  0.092  33  ILE   BBB O   
2249 C  CB  . ILE   B 34  ? 0.449 0.035 0.446 0.069  0.016  0.029  33  ILE   BBB CB  
2250 C  CG1 . ILE   B 34  ? 0.508 0.062 0.417 0.162  0.018  0.044  33  ILE   BBB CG1 
2251 C  CG2 . ILE   B 34  ? 0.485 0.056 0.440 0.003  0.053  -0.019 33  ILE   BBB CG2 
2252 C  CD1 . ILE   B 34  ? 0.457 0.034 0.427 0.102  0.035  0.054  33  ILE   BBB CD1 
2253 N  N   . LYS   B 35  ? 0.572 0.028 0.485 0.090  -0.002 0.060  34  LYS   BBB N   
2254 C  CA  . LYS   B 35  ? 0.536 0.146 0.451 0.044  -0.027 0.078  34  LYS   BBB CA  
2255 C  C   . LYS   B 35  ? 0.468 0.049 0.443 -0.040 -0.027 0.133  34  LYS   BBB C   
2256 O  O   . LYS   B 35  ? 0.496 0.195 0.485 -0.081 -0.050 0.127  34  LYS   BBB O   
2257 C  CB  . LYS   B 35  ? 0.581 0.140 0.648 0.101  -0.080 0.010  34  LYS   BBB CB  
2258 C  CG  . LYS   B 35  ? 0.897 0.114 0.766 -0.042 -0.174 0.076  34  LYS   BBB CG  
2259 C  CD  . LYS   B 35  ? 1.068 0.335 1.067 0.233  -0.135 -0.088 34  LYS   BBB CD  
2260 C  CE  . LYS   B 35  ? 1.162 0.092 1.247 0.054  -0.479 -0.317 34  LYS   BBB CE  
2261 N  NZ  . LYS   B 35  ? 1.733 0.629 2.414 1.001  -0.106 -0.377 34  LYS   BBB NZ  
2262 N  N   . THR   B 36  ? 0.518 0.225 0.430 -0.060 0.033  0.092  35  THR   BBB N   
2263 C  CA  . THR   B 36  ? 0.476 0.222 0.466 -0.069 0.003  0.083  35  THR   BBB CA  
2264 C  C   . THR   B 36  ? 0.575 0.171 0.476 -0.139 -0.026 0.123  35  THR   BBB C   
2265 O  O   . THR   B 36  ? 0.571 0.389 0.584 -0.154 -0.104 0.103  35  THR   BBB O   
2266 C  CB  . THR   B 36  ? 0.474 0.286 0.465 -0.065 0.018  0.091  35  THR   BBB CB  
2267 O  OG1 . THR   B 36  ? 0.506 0.178 0.492 -0.070 0.034  0.064  35  THR   BBB OG1 
2268 C  CG2 . THR   B 36  ? 0.502 0.018 0.513 -0.023 0.020  0.071  35  THR   BBB CG2 
2269 N  N   . SER   B 37  ? 0.674 0.216 0.498 -0.142 -0.011 0.226  36  SER   BBB N   
2270 C  CA  . SER   B 37  ? 0.696 0.201 0.523 -0.038 -0.004 0.180  36  SER   BBB CA  
2271 C  C   . SER   B 37  ? 0.631 0.299 0.499 -0.246 -0.034 0.211  36  SER   BBB C   
2272 O  O   . SER   B 37  ? 0.699 0.376 0.672 0.075  -0.119 0.189  36  SER   BBB O   
2273 C  CB  . SER   B 37  ? 0.766 0.281 0.525 -0.113 0.023  0.216  36  SER   BBB CB  
2274 O  OG  . SER   B 37  ? 0.709 0.176 0.647 -0.110 -0.066 0.173  36  SER   BBB OG  
2275 N  N   . GLU   B 38  ? 0.688 0.171 0.533 -0.061 -0.018 0.254  37  GLU   BBB N   
2276 C  CA  . GLU   B 38  ? 0.614 0.198 0.733 -0.050 -0.071 0.200  37  GLU   BBB CA  
2277 C  C   . GLU   B 38  ? 0.437 0.083 0.714 0.020  -0.066 0.031  37  GLU   BBB C   
2278 O  O   . GLU   B 38  ? 0.486 0.011 0.715 0.013  -0.043 0.056  37  GLU   BBB O   
2279 C  CB  . GLU   B 38  ? 0.672 0.117 0.680 -0.080 0.006  0.234  37  GLU   BBB CB  
2280 C  CG  . GLU   B 38  ? 0.738 0.153 1.080 -0.032 -0.056 0.393  37  GLU   BBB CG  
2281 C  CD  . GLU   B 38  ? 0.862 0.405 0.927 0.168  -0.063 0.352  37  GLU   BBB CD  
2282 O  OE1 . GLU   B 38  ? 0.732 0.711 1.221 0.244  0.184  0.006  37  GLU   BBB OE1 
2283 O  OE2 . GLU   B 38  ? 1.185 0.926 0.938 -0.009 -0.077 -0.012 37  GLU   BBB OE2 
2284 N  N   . THR   B 39  ? 0.439 0.079 0.507 0.012  -0.038 0.077  38  THR   BBB N   
2285 C  CA  . THR   B 39  ? 0.392 0.166 0.602 -0.072 -0.015 0.038  38  THR   BBB CA  
2286 C  C   . THR   B 39  ? 0.442 0.257 0.527 -0.017 -0.032 0.074  38  THR   BBB C   
2287 O  O   . THR   B 39  ? 0.609 0.151 0.555 -0.037 -0.059 0.095  38  THR   BBB O   
2288 C  CB  . THR   B 39  ? 0.447 0.050 0.602 -0.054 0.057  0.030  38  THR   BBB CB  
2289 O  OG1 . THR   B 39  ? 0.520 0.190 0.497 0.000  0.012  0.081  38  THR   BBB OG1 
2290 C  CG2 . THR   B 39  ? 0.504 0.024 0.732 -0.050 0.003  0.096  38  THR   BBB CG2 
2291 N  N   . LYS   B 40  ? 0.426 0.101 0.568 0.034  0.015  0.028  39  LYS   BBB N   
2292 C  CA  . LYS   B 40  ? 0.531 0.065 0.725 -0.150 -0.025 0.067  39  LYS   BBB CA  
2293 C  C   . LYS   B 40  ? 0.444 0.060 0.422 0.007  0.023  0.066  39  LYS   BBB C   
2294 O  O   . LYS   B 40  ? 0.464 0.099 0.455 0.030  -0.012 0.085  39  LYS   BBB O   
2295 C  CB  . LYS   B 40  ? 0.522 0.113 0.830 -0.143 -0.034 0.159  39  LYS   BBB CB  
2296 C  CG  . LYS   B 40  ? 0.612 0.156 0.630 0.021  -0.156 0.143  39  LYS   BBB CG  
2297 C  CD  . LYS   B 40  ? 0.650 0.069 0.722 0.015  -0.200 0.197  39  LYS   BBB CD  
2298 C  CE  . LYS   B 40  ? 0.837 0.111 0.825 0.042  -0.106 0.282  39  LYS   BBB CE  
2299 N  NZ  . LYS   B 40  ? 0.814 0.173 0.798 0.098  -0.026 0.215  39  LYS   BBB NZ  
2300 N  N   . HIS   B 41  ? 0.533 0.151 0.425 -0.053 -0.011 0.045  40  HIS   BBB N   
2301 C  CA  . HIS   B 41  ? 0.510 0.138 0.381 -0.037 -0.058 0.163  40  HIS   BBB CA  
2302 C  C   . HIS   B 41  ? 0.563 0.253 0.374 -0.063 -0.026 0.097  40  HIS   BBB C   
2303 O  O   . HIS   B 41  ? 0.572 0.115 0.437 -0.028 0.008  0.057  40  HIS   BBB O   
2304 C  CB  . HIS   B 41  ? 0.514 0.313 0.388 0.019  -0.054 0.163  40  HIS   BBB CB  
2305 C  CG  . HIS   B 41  ? 0.488 0.321 0.472 -0.023 -0.049 0.106  40  HIS   BBB CG  
2306 N  ND1 . HIS   B 41  ? 0.498 0.300 0.406 0.057  -0.020 0.081  40  HIS   BBB ND1 
2307 C  CD2 . HIS   B 41  ? 0.518 0.333 0.414 -0.002 -0.092 0.046  40  HIS   BBB CD2 
2308 C  CE1 . HIS   B 41  ? 0.515 0.239 0.428 0.147  -0.022 -0.059 40  HIS   BBB CE1 
2309 N  NE2 . HIS   B 41  ? 0.597 0.204 0.402 0.034  -0.023 0.049  40  HIS   BBB NE2 
2310 N  N   . ASP   B 42  ? 0.512 0.316 0.342 -0.065 -0.079 0.129  41  ASP   BBB N   
2311 C  CA  . ASP   B 42  ? 0.474 0.075 0.396 -0.013 -0.017 0.056  41  ASP   BBB CA  
2312 C  C   . ASP   B 42  ? 0.443 0.100 0.401 -0.060 -0.045 0.018  41  ASP   BBB C   
2313 O  O   . ASP   B 42  ? 0.447 0.227 0.450 -0.053 -0.039 0.069  41  ASP   BBB O   
2314 C  CB  . ASP   B 42  ? 0.498 0.192 0.417 0.024  -0.018 0.064  41  ASP   BBB CB  
2315 C  CG  . ASP   B 42  ? 0.495 0.244 0.378 -0.023 -0.036 0.045  41  ASP   BBB CG  
2316 O  OD1 . ASP   B 42  ? 0.556 0.115 0.416 -0.076 -0.029 -0.002 41  ASP   BBB OD1 
2317 O  OD2 . ASP   B 42  ? 0.731 0.160 0.464 -0.025 0.106  0.037  41  ASP   BBB OD2 
2318 N  N   . THR   B 43  ? 0.495 0.075 0.353 -0.021 -0.040 0.068  42  THR   BBB N   
2319 C  CA  . THR   B 43  ? 0.465 0.085 0.396 -0.037 -0.003 0.034  42  THR   BBB CA  
2320 C  C   . THR   B 43  ? 0.406 0.182 0.348 0.059  -0.002 0.077  42  THR   BBB C   
2321 O  O   . THR   B 43  ? 0.457 0.160 0.401 0.028  -0.024 0.043  42  THR   BBB O   
2322 C  CB  . THR   B 43  ? 0.391 0.268 0.407 -0.044 0.024  0.025  42  THR   BBB CB  
2323 O  OG1 . THR   B 43  ? 0.394 0.307 0.372 -0.008 0.012  0.138  42  THR   BBB OG1 
2324 C  CG2 . THR   B 43  ? 0.450 0.365 0.305 0.044  0.016  0.039  42  THR   BBB CG2 
2325 N  N   . SER   B 44  ? 0.404 0.287 0.321 0.011  0.010  0.088  43  SER   BBB N   
2326 C  CA  . SER   B 44  ? 0.408 0.353 0.302 -0.025 -0.025 0.072  43  SER   BBB CA  
2327 C  C   . SER   B 44  ? 0.419 0.313 0.395 0.001  -0.045 0.096  43  SER   BBB C   
2328 O  O   . SER   B 44  ? 0.524 0.293 0.488 0.038  0.037  0.125  43  SER   BBB O   
2329 C  CB  . SER   B 44  ? 0.422 0.358 0.329 0.021  -0.037 0.052  43  SER   BBB CB  
2330 O  OG  . SER   B 44  ? 0.474 0.387 0.325 0.010  -0.012 0.050  43  SER   BBB OG  
2331 N  N   . LEU   B 45  ? 0.419 0.134 0.405 0.021  -0.022 0.055  44  LEU   BBB N   
2332 C  CA  . LEU   B 45  ? 0.402 0.185 0.340 0.063  0.008  0.033  44  LEU   BBB CA  
2333 C  C   . LEU   B 45  ? 0.443 0.158 0.342 0.039  0.020  0.011  44  LEU   BBB C   
2334 O  O   . LEU   B 45  ? 0.515 0.192 0.316 0.016  0.020  0.127  44  LEU   BBB O   
2335 C  CB  . LEU   B 45  ? 0.403 0.125 0.356 0.051  -0.019 0.052  44  LEU   BBB CB  
2336 C  CG  . LEU   B 45  ? 0.391 0.130 0.395 0.057  -0.010 0.047  44  LEU   BBB CG  
2337 C  CD1 . LEU   B 45  ? 0.458 0.076 0.478 0.050  -0.028 0.056  44  LEU   BBB CD1 
2338 C  CD2 . LEU   B 45  ? 0.485 0.135 0.456 -0.009 0.030  0.053  44  LEU   BBB CD2 
2339 N  N   . LYS   B 46  ? 0.418 0.171 0.431 0.063  -0.024 0.048  45  LYS   BBB N   
2340 C  CA  . LYS   B 46  ? 0.400 0.134 0.362 0.031  -0.000 0.039  45  LYS   BBB CA  
2341 C  C   . LYS   B 46  ? 0.406 0.129 0.368 -0.015 -0.019 0.037  45  LYS   BBB C   
2342 O  O   . LYS   B 46  ? 0.460 0.159 0.373 0.053  -0.048 0.020  45  LYS   BBB O   
2343 C  CB  . LYS   B 46  ? 0.416 0.150 0.427 0.044  -0.015 0.124  45  LYS   BBB CB  
2344 C  CG  . LYS   B 46  ? 0.536 0.021 0.486 0.011  -0.099 0.078  45  LYS   BBB CG  
2345 C  CD  . LYS   B 46  ? 0.629 0.073 0.431 -0.116 -0.070 0.105  45  LYS   BBB CD  
2346 C  CE  . LYS   B 46  ? 0.656 0.341 0.525 -0.109 -0.053 0.063  45  LYS   BBB CE  
2347 N  NZ  . LYS   B 46  ? 0.694 0.390 0.594 -0.161 -0.049 0.070  45  LYS   BBB NZ  
2348 N  N   . PRO   B 47  ? 0.448 0.144 0.371 0.012  -0.049 -0.009 46  PRO   BBB N   
2349 C  CA  . PRO   B 47  ? 0.456 0.063 0.360 -0.051 -0.045 -0.027 46  PRO   BBB CA  
2350 C  C   . PRO   B 47  ? 0.443 0.141 0.357 0.029  -0.035 0.004  46  PRO   BBB C   
2351 O  O   . PRO   B 47  ? 0.465 0.188 0.457 0.044  0.016  0.031  46  PRO   BBB O   
2352 C  CB  . PRO   B 47  ? 0.539 0.160 0.348 0.021  -0.014 -0.044 46  PRO   BBB CB  
2353 C  CG  . PRO   B 47  ? 0.490 0.308 0.401 -0.021 -0.083 0.020  46  PRO   BBB CG  
2354 C  CD  . PRO   B 47  ? 0.504 0.182 0.343 -0.034 -0.068 0.012  46  PRO   BBB CD  
2355 N  N   . ILE   B 48  ? 0.451 0.230 0.343 -0.024 -0.036 0.028  47  ILE   BBB N   
2356 C  CA  . ILE   B 48  ? 0.466 0.141 0.356 0.070  -0.040 0.067  47  ILE   BBB CA  
2357 C  C   . ILE   B 48  ? 0.402 0.122 0.357 0.049  0.003  0.022  47  ILE   BBB C   
2358 O  O   . ILE   B 48  ? 0.523 0.016 0.564 0.069  0.044  0.024  47  ILE   BBB O   
2359 C  CB  . ILE   B 48  ? 0.504 0.312 0.415 0.143  -0.066 -0.052 47  ILE   BBB CB  
2360 C  CG1 . ILE   B 48  ? 0.459 0.474 0.452 0.203  -0.004 -0.024 47  ILE   BBB CG1 
2361 C  CG2 . ILE   B 48  ? 0.679 0.131 0.404 0.044  -0.023 -0.011 47  ILE   BBB CG2 
2362 C  CD1 . ILE   B 48  ? 0.768 0.541 0.474 0.193  -0.038 -0.050 47  ILE   BBB CD1 
2363 N  N   . SER   B 49  ? 0.542 0.030 0.406 0.070  0.014  0.020  48  SER   BBB N   
2364 C  CA  . SER   B 49  ? 0.572 0.040 0.400 0.018  -0.073 0.063  48  SER   BBB CA  
2365 C  C   . SER   B 49  ? 0.456 0.012 0.387 -0.033 0.006  0.033  48  SER   BBB C   
2366 O  O   . SER   B 49  ? 0.483 0.140 0.377 0.030  -0.004 0.031  48  SER   BBB O   
2367 C  CB  . SER   B 49  ? 0.727 0.096 0.525 -0.104 -0.129 0.007  48  SER   BBB CB  
2368 O  OG  . SER   B 49  ? 0.917 0.035 0.609 -0.005 -0.130 -0.037 48  SER   BBB OG  
2369 N  N   . VAL   B 50  ? 0.438 0.012 0.405 -0.028 0.021  0.008  49  VAL   BBB N   
2370 C  CA  . VAL   B 50  ? 0.469 0.009 0.414 0.031  -0.020 0.007  49  VAL   BBB CA  
2371 C  C   . VAL   B 50  ? 0.545 0.029 0.380 0.106  0.029  0.033  49  VAL   BBB C   
2372 O  O   . VAL   B 50  ? 0.638 0.090 0.361 0.044  0.033  -0.019 49  VAL   BBB O   
2373 C  CB  . VAL   B 50  ? 0.491 0.029 0.551 -0.025 -0.015 0.107  49  VAL   BBB CB  
2374 C  CG1 . VAL   B 50  ? 0.577 0.007 0.634 0.010  -0.048 0.021  49  VAL   BBB CG1 
2375 C  CG2 . VAL   B 50  ? 0.540 0.014 0.756 -0.042 0.017  0.056  49  VAL   BBB CG2 
2376 N  N   . SER   B 51  ? 0.582 0.010 0.455 0.034  0.005  0.031  50  SER   BBB N   
2377 C  CA  . SER   B 51  ? 0.658 0.008 0.548 0.032  0.033  0.018  50  SER   BBB CA  
2378 C  C   . SER   B 51  ? 1.041 0.014 0.666 -0.063 0.049  0.048  50  SER   BBB C   
2379 O  O   . SER   B 51  ? 1.034 0.007 0.516 0.013  -0.009 0.019  50  SER   BBB O   
2380 C  CB  . SER   B 51  ? 0.714 0.141 0.384 -0.077 -0.054 0.103  50  SER   BBB CB  
2381 O  OG  . SER   B 51  ? 0.864 0.102 0.515 -0.052 0.041  0.120  50  SER   BBB OG  
2382 N  N   . TYR   B 52  ? 1.036 0.019 0.587 -0.048 0.067  0.075  51  TYR   BBB N   
2383 C  CA  . TYR   B 52  ? 0.648 0.007 0.514 0.022  0.035  0.015  51  TYR   BBB CA  
2384 C  C   . TYR   B 52  ? 0.697 0.019 0.570 0.092  0.078  0.000  51  TYR   BBB C   
2385 O  O   . TYR   B 52  ? 0.743 0.021 0.471 0.084  0.156  0.012  51  TYR   BBB O   
2386 C  CB  . TYR   B 52  ? 0.539 0.009 0.438 0.024  -0.042 -0.029 51  TYR   BBB CB  
2387 C  CG  . TYR   B 52  ? 0.484 0.090 0.384 0.076  0.003  0.051  51  TYR   BBB CG  
2388 C  CD1 . TYR   B 52  ? 0.471 0.013 0.352 0.029  -0.036 0.040  51  TYR   BBB CD1 
2389 C  CD2 . TYR   B 52  ? 0.494 0.034 0.413 0.107  0.024  -0.035 51  TYR   BBB CD2 
2390 C  CE1 . TYR   B 52  ? 0.447 0.042 0.392 0.067  0.014  0.076  51  TYR   BBB CE1 
2391 C  CE2 . TYR   B 52  ? 0.444 0.011 0.388 0.035  -0.027 0.024  51  TYR   BBB CE2 
2392 C  CZ  . TYR   B 52  ? 0.436 0.009 0.313 0.023  -0.010 0.020  51  TYR   BBB CZ  
2393 O  OH  . TYR   B 52  ? 0.445 0.009 0.414 0.030  0.032  0.020  51  TYR   BBB OH  
2394 N  N   . ASN   B 53  ? 0.817 0.015 0.520 0.027  0.036  -0.063 52  ASN   BBB N   
2395 C  CA  . ASN   B 53  ? 0.727 0.027 0.459 0.122  0.003  -0.015 52  ASN   BBB CA  
2396 C  C   . ASN   B 53  ? 0.706 0.126 0.312 0.147  0.044  -0.000 52  ASN   BBB C   
2397 O  O   . ASN   B 53  ? 0.755 0.007 0.425 0.017  -0.019 0.012  52  ASN   BBB O   
2398 C  CB  . ASN   B 53  ? 0.811 0.008 0.443 0.040  0.023  0.001  52  ASN   BBB CB  
2399 C  CG  . ASN   B 53  ? 0.889 0.028 0.582 0.098  0.043  0.084  52  ASN   BBB CG  
2400 O  OD1 . ASN   B 53  ? 1.026 0.006 0.655 -0.009 0.049  0.005  52  ASN   BBB OD1 
2401 N  ND2 . ASN   B 53  ? 0.871 0.067 0.490 0.027  0.046  0.004  52  ASN   BBB ND2 
2402 N  N   . PRO   B 54  ? 0.743 0.021 0.342 0.098  0.039  -0.013 53  PRO   BBB N   
2403 C  CA  . PRO   B 54  ? 0.679 0.015 0.451 0.077  0.001  -0.002 53  PRO   BBB CA  
2404 C  C   . PRO   B 54  ? 0.536 0.056 0.459 0.027  -0.028 0.084  53  PRO   BBB C   
2405 O  O   . PRO   B 54  ? 0.783 0.020 0.475 0.069  -0.041 0.055  53  PRO   BBB O   
2406 C  CB  . PRO   B 54  ? 0.657 0.053 0.496 0.027  0.067  -0.072 53  PRO   BBB CB  
2407 C  CG  . PRO   B 54  ? 0.707 0.069 0.441 0.092  -0.008 -0.092 53  PRO   BBB CG  
2408 C  CD  . PRO   B 54  ? 0.768 0.046 0.472 0.116  -0.013 -0.103 53  PRO   BBB CD  
2409 N  N   . ALA   B 55  ? 0.743 0.010 0.358 -0.045 0.031  -0.019 54  ALA   BBB N   
2410 C  CA  . ALA   B 55  ? 0.677 0.008 0.375 -0.027 0.025  0.010  54  ALA   BBB CA  
2411 C  C   . ALA   B 55  ? 0.656 0.031 0.346 0.027  0.029  0.090  54  ALA   BBB C   
2412 O  O   . ALA   B 55  ? 0.709 0.015 0.367 0.037  0.070  0.053  54  ALA   BBB O   
2413 C  CB  . ALA   B 55  ? 0.826 0.008 0.476 0.014  -0.048 0.021  54  ALA   BBB CB  
2414 N  N   . THR   B 56  ? 0.735 0.009 0.380 -0.038 0.029  0.012  55  THR   BBB N   
2415 C  CA  . THR   B 56  ? 0.573 0.069 0.362 0.084  0.003  -0.052 55  THR   BBB CA  
2416 C  C   . THR   B 56  ? 0.527 0.027 0.280 0.061  0.050  0.055  55  THR   BBB C   
2417 O  O   . THR   B 56  ? 0.543 0.008 0.369 0.023  0.017  -0.016 55  THR   BBB O   
2418 C  CB  . THR   B 56  ? 0.546 0.105 0.345 0.037  0.008  -0.043 55  THR   BBB CB  
2419 O  OG1 . THR   B 56  ? 0.563 0.008 0.335 0.000  0.006  -0.021 55  THR   BBB OG1 
2420 C  CG2 . THR   B 56  ? 0.628 0.046 0.387 -0.014 -0.022 0.007  55  THR   BBB CG2 
2421 N  N   . ALA   B 57  ? 0.580 0.026 0.474 0.084  0.019  0.063  56  ALA   BBB N   
2422 C  CA  . ALA   B 57  ? 0.491 0.135 0.350 0.059  0.006  0.080  56  ALA   BBB CA  
2423 C  C   . ALA   B 57  ? 0.602 0.015 0.335 0.066  0.051  0.023  56  ALA   BBB C   
2424 O  O   . ALA   B 57  ? 0.550 0.025 0.352 0.066  -0.020 0.059  56  ALA   BBB O   
2425 C  CB  . ALA   B 57  ? 0.516 0.110 0.394 0.098  0.047  0.073  56  ALA   BBB CB  
2426 N  N   . LYS   B 58  ? 0.498 0.007 0.355 0.015  0.003  0.010  57  LYS   BBB N   
2427 C  CA  . LYS   B 58  ? 0.506 0.007 0.376 0.016  0.015  -0.005 57  LYS   BBB CA  
2428 C  C   . LYS   B 58  ? 0.533 0.028 0.343 0.047  -0.019 0.031  57  LYS   BBB C   
2429 O  O   . LYS   B 58  ? 0.539 0.012 0.358 0.021  -0.013 0.043  57  LYS   BBB O   
2430 C  CB  . LYS   B 58  ? 0.476 0.146 0.435 -0.030 0.042  0.038  57  LYS   BBB CB  
2431 C  CG  . LYS   B 58  ? 0.495 0.356 0.418 -0.042 0.012  0.052  57  LYS   BBB CG  
2432 C  CD  . LYS   B 58  ? 0.559 0.486 0.627 0.005  0.140  -0.068 57  LYS   BBB CD  
2433 C  CE  . LYS   B 58  ? 0.738 0.636 0.668 0.024  0.199  0.034  57  LYS   BBB CE  
2434 N  NZ  . LYS   B 58  ? 0.954 0.912 0.991 -0.112 0.256  0.164  57  LYS   BBB NZ  
2435 N  N   . GLU   B 59  ? 0.481 0.041 0.365 0.012  -0.014 0.047  58  GLU   BBB N   
2436 C  CA  . GLU   B 59  ? 0.405 0.159 0.356 0.033  -0.036 0.059  58  GLU   BBB CA  
2437 C  C   . GLU   B 59  ? 0.393 0.183 0.280 0.015  -0.021 0.001  58  GLU   BBB C   
2438 O  O   . GLU   B 59  ? 0.476 0.094 0.362 -0.022 -0.061 0.023  58  GLU   BBB O   
2439 C  CB  . GLU   B 59  ? 0.456 0.181 0.352 -0.013 0.016  0.032  58  GLU   BBB CB  
2440 C  CG  . GLU   B 59  ? 0.542 0.341 0.433 -0.022 0.005  -0.006 58  GLU   BBB CG  
2441 C  CD  . GLU   B 59  ? 0.555 0.396 0.367 0.033  0.021  0.038  58  GLU   BBB CD  
2442 O  OE1 . GLU   B 59  ? 0.539 0.239 0.505 0.045  0.112  0.055  58  GLU   BBB OE1 
2443 O  OE2 . GLU   B 59  ? 0.635 0.482 0.443 0.176  0.017  0.075  58  GLU   BBB OE2 
2444 N  N   . ILE   B 60  ? 0.384 0.080 0.327 0.024  -0.029 0.044  59  ILE   BBB N   
2445 C  CA  . ILE   B 60  ? 0.324 0.124 0.319 0.002  -0.030 0.040  59  ILE   BBB CA  
2446 C  C   . ILE   B 60  ? 0.430 0.140 0.312 0.053  0.006  0.018  59  ILE   BBB C   
2447 O  O   . ILE   B 60  ? 0.459 0.102 0.328 0.040  0.005  -0.010 59  ILE   BBB O   
2448 C  CB  . ILE   B 60  ? 0.410 0.174 0.330 0.061  -0.003 -0.011 59  ILE   BBB CB  
2449 C  CG1 . ILE   B 60  ? 0.410 0.155 0.382 0.070  0.005  0.005  59  ILE   BBB CG1 
2450 C  CG2 . ILE   B 60  ? 0.359 0.165 0.342 0.034  -0.021 -0.032 59  ILE   BBB CG2 
2451 C  CD1 . ILE   B 60  ? 0.466 0.091 0.406 0.095  0.005  0.093  59  ILE   BBB CD1 
2452 N  N   . ILE   B 61  ? 0.400 0.127 0.321 0.041  0.017  0.009  60  ILE   BBB N   
2453 C  CA  . ILE   B 61  ? 0.402 0.118 0.279 -0.013 0.037  0.023  60  ILE   BBB CA  
2454 C  C   . ILE   B 61  ? 0.413 0.094 0.294 -0.015 0.001  0.005  60  ILE   BBB C   
2455 O  O   . ILE   B 61  ? 0.392 0.117 0.321 0.025  -0.036 -0.011 60  ILE   BBB O   
2456 C  CB  . ILE   B 61  ? 0.417 0.234 0.438 -0.024 0.133  -0.103 60  ILE   BBB CB  
2457 C  CG1 . ILE   B 61  ? 0.450 0.451 0.562 -0.095 0.099  -0.230 60  ILE   BBB CG1 
2458 C  CG2 . ILE   B 61  ? 0.502 0.327 0.339 0.021  -0.033 -0.053 60  ILE   BBB CG2 
2459 C  CD1 . ILE   B 61  ? 0.455 0.756 0.718 0.080  -0.018 -0.057 60  ILE   BBB CD1 
2460 N  N   . ASN   B 62  ? 0.414 0.087 0.332 -0.005 -0.021 0.004  61  ASN   BBB N   
2461 C  CA  . ASN   B 62  ? 0.340 0.110 0.369 -0.031 0.007  -0.010 61  ASN   BBB CA  
2462 C  C   . ASN   B 62  ? 0.327 0.207 0.374 -0.040 0.011  -0.034 61  ASN   BBB C   
2463 O  O   . ASN   B 62  ? 0.388 0.062 0.404 0.029  0.039  -0.052 61  ASN   BBB O   
2464 C  CB  . ASN   B 62  ? 0.331 0.188 0.401 0.019  0.023  0.011  61  ASN   BBB CB  
2465 C  CG  . ASN   B 62  ? 0.302 0.183 0.350 0.043  0.020  -0.037 61  ASN   BBB CG  
2466 O  OD1 . ASN   B 62  ? 0.360 0.134 0.474 0.043  0.014  -0.055 61  ASN   BBB OD1 
2467 N  ND2 . ASN   B 62  ? 0.317 0.176 0.358 0.014  0.016  -0.059 61  ASN   BBB ND2 
2468 N  N   . VAL   B 63  ? 0.353 0.205 0.369 -0.005 -0.014 -0.055 62  VAL   BBB N   
2469 C  CA  . VAL   B 63  ? 0.354 0.122 0.405 -0.043 0.019  -0.048 62  VAL   BBB CA  
2470 C  C   . VAL   B 63  ? 0.354 0.114 0.409 -0.040 -0.015 -0.001 62  VAL   BBB C   
2471 O  O   . VAL   B 63  ? 0.377 0.164 0.479 0.015  0.015  -0.088 62  VAL   BBB O   
2472 C  CB  . VAL   B 63  ? 0.351 0.163 0.414 -0.037 0.009  -0.024 62  VAL   BBB CB  
2473 C  CG1 . VAL   B 63  ? 0.359 0.217 0.412 -0.051 -0.035 -0.080 62  VAL   BBB CG1 
2474 C  CG2 . VAL   B 63  ? 0.436 0.029 0.457 -0.011 -0.023 -0.056 62  VAL   BBB CG2 
2475 N  N   . GLY   B 64  ? 0.368 0.091 0.398 0.046  -0.015 -0.092 63  GLY   BBB N   
2476 C  CA  . GLY   B 64  ? 0.414 0.147 0.446 -0.027 0.047  -0.109 63  GLY   BBB CA  
2477 C  C   . GLY   B 64  ? 0.360 0.056 0.417 0.041  -0.040 -0.066 63  GLY   BBB C   
2478 O  O   . GLY   B 64  ? 0.433 0.157 0.484 0.019  -0.054 -0.114 63  GLY   BBB O   
2479 N  N   . HIS   B 65  ? 0.348 0.119 0.398 0.029  -0.029 -0.057 64  HIS   BBB N   
2480 C  CA  . HIS   B 65  ? 0.392 0.181 0.353 0.021  -0.042 -0.044 64  HIS   BBB CA  
2481 C  C   . HIS   B 65  ? 0.430 0.035 0.384 0.012  0.007  0.016  64  HIS   BBB C   
2482 O  O   . HIS   B 65  ? 0.488 0.037 0.351 0.051  0.000  -0.053 64  HIS   BBB O   
2483 C  CB  . HIS   B 65  ? 0.484 0.017 0.466 0.054  -0.014 -0.049 64  HIS   BBB CB  
2484 C  CG  . HIS   B 65  ? 0.427 0.092 0.378 0.035  -0.026 -0.016 64  HIS   BBB CG  
2485 N  ND1 . HIS   B 65  ? 0.395 0.202 0.490 0.031  -0.015 -0.090 64  HIS   BBB ND1 
2486 C  CD2 . HIS   B 65  ? 0.415 0.016 0.347 -0.001 0.008  -0.057 64  HIS   BBB CD2 
2487 C  CE1 . HIS   B 65  ? 0.392 0.022 0.424 0.072  -0.006 -0.029 64  HIS   BBB CE1 
2488 N  NE2 . HIS   B 65  ? 0.426 0.090 0.456 0.058  0.032  0.013  64  HIS   BBB NE2 
2489 N  N   . SER   B 66  ? 0.406 0.047 0.370 -0.026 -0.003 0.012  65  SER   BBB N   
2490 C  CA  . SER   B 66  ? 0.341 0.122 0.338 0.035  -0.022 -0.005 65  SER   BBB CA  
2491 C  C   . SER   B 66  ? 0.395 0.139 0.304 0.019  -0.030 -0.014 65  SER   BBB C   
2492 O  O   . SER   B 66  ? 0.400 0.048 0.359 -0.013 -0.017 -0.043 65  SER   BBB O   
2493 C  CB  . SER   B 66  ? 0.447 0.174 0.318 0.031  -0.026 -0.002 65  SER   BBB CB  
2494 O  OG  . SER   B 66  ? 0.480 0.080 0.374 0.063  -0.022 -0.026 65  SER   BBB OG  
2495 N  N   . PHE   B 67  ? 0.371 0.132 0.310 -0.016 0.005  -0.021 66  PHE   BBB N   
2496 C  CA  . PHE   B 67  ? 0.374 0.159 0.334 -0.030 0.002  0.001  66  PHE   BBB CA  
2497 C  C   . PHE   B 67  ? 0.348 0.166 0.274 0.064  0.011  -0.057 66  PHE   BBB C   
2498 O  O   . PHE   B 67  ? 0.406 0.032 0.303 0.007  -0.005 -0.025 66  PHE   BBB O   
2499 C  CB  . PHE   B 67  ? 0.380 0.154 0.309 -0.028 -0.040 -0.040 66  PHE   BBB CB  
2500 C  CG  . PHE   B 67  ? 0.317 0.177 0.336 0.025  -0.002 -0.034 66  PHE   BBB CG  
2501 C  CD1 . PHE   B 67  ? 0.405 0.096 0.341 0.013  -0.003 -0.026 66  PHE   BBB CD1 
2502 C  CD2 . PHE   B 67  ? 0.500 0.090 0.340 0.061  -0.031 -0.005 66  PHE   BBB CD2 
2503 C  CE1 . PHE   B 67  ? 0.476 0.151 0.325 0.030  -0.008 -0.048 66  PHE   BBB CE1 
2504 C  CE2 . PHE   B 67  ? 0.365 0.114 0.376 0.037  -0.009 -0.007 66  PHE   BBB CE2 
2505 C  CZ  . PHE   B 67  ? 0.412 0.188 0.331 -0.018 0.003  -0.033 66  PHE   BBB CZ  
2506 N  N   . HIS   B 68  ? 0.376 0.111 0.299 0.055  -0.020 -0.031 67  HIS   BBB N   
2507 C  CA  . HIS   B 68  ? 0.356 0.052 0.444 -0.000 -0.049 0.016  67  HIS   BBB CA  
2508 C  C   . HIS   B 68  ? 0.365 0.061 0.336 0.036  -0.064 -0.037 67  HIS   BBB C   
2509 O  O   . HIS   B 68  ? 0.442 0.061 0.337 0.015  -0.043 -0.001 67  HIS   BBB O   
2510 C  CB  . HIS   B 68  ? 0.426 0.023 0.411 0.016  -0.028 -0.081 67  HIS   BBB CB  
2511 C  CG  . HIS   B 68  ? 0.398 0.018 0.448 0.042  0.001  -0.057 67  HIS   BBB CG  
2512 N  ND1 . HIS   B 68  ? 0.394 0.008 0.430 -0.010 0.009  -0.028 67  HIS   BBB ND1 
2513 C  CD2 . HIS   B 68  ? 0.400 0.060 0.418 0.048  0.041  -0.096 67  HIS   BBB CD2 
2514 C  CE1 . HIS   B 68  ? 0.363 0.015 0.457 -0.023 0.068  -0.059 67  HIS   BBB CE1 
2515 N  NE2 . HIS   B 68  ? 0.383 0.022 0.417 0.008  0.053  -0.078 67  HIS   BBB NE2 
2516 N  N   . VAL   B 69  ? 0.380 0.010 0.308 -0.009 -0.019 0.010  68  VAL   BBB N   
2517 C  CA  . VAL   B 69  ? 0.408 0.013 0.363 0.040  -0.019 0.029  68  VAL   BBB CA  
2518 C  C   . VAL   B 69  ? 0.452 0.016 0.304 0.038  -0.022 -0.044 68  VAL   BBB C   
2519 O  O   . VAL   B 69  ? 0.420 0.033 0.319 -0.000 -0.020 0.018  68  VAL   BBB O   
2520 C  CB  . VAL   B 69  ? 0.371 0.024 0.403 0.066  -0.007 0.046  68  VAL   BBB CB  
2521 C  CG1 . VAL   B 69  ? 0.498 0.037 0.387 0.106  -0.042 0.044  68  VAL   BBB CG1 
2522 C  CG2 . VAL   B 69  ? 0.398 0.083 0.395 0.062  -0.015 -0.039 68  VAL   BBB CG2 
2523 N  N   . ASN   B 70  ? 0.510 0.010 0.358 0.043  -0.009 0.007  69  ASN   BBB N   
2524 C  CA  . ASN   B 70  ? 0.458 0.016 0.367 0.021  0.011  0.055  69  ASN   BBB CA  
2525 C  C   . ASN   B 70  ? 0.359 0.017 0.379 -0.036 -0.002 -0.051 69  ASN   BBB C   
2526 O  O   . ASN   B 70  ? 0.426 0.043 0.391 0.062  0.010  -0.051 69  ASN   BBB O   
2527 C  CB  . ASN   B 70  ? 0.396 0.007 0.355 0.003  -0.022 0.016  69  ASN   BBB CB  
2528 C  CG  . ASN   B 70  ? 0.385 0.021 0.374 0.006  -0.039 -0.074 69  ASN   BBB CG  
2529 O  OD1 . ASN   B 70  ? 0.651 0.008 0.473 0.008  -0.015 -0.031 69  ASN   BBB OD1 
2530 N  ND2 . ASN   B 70  ? 0.530 0.092 0.439 0.087  -0.086 -0.147 69  ASN   BBB ND2 
2531 N  N   . PHE   B 71  ? 0.435 0.026 0.347 -0.071 -0.005 -0.052 70  PHE   BBB N   
2532 C  CA  . PHE   B 71  ? 0.456 0.009 0.406 -0.033 -0.027 -0.010 70  PHE   BBB CA  
2533 C  C   . PHE   B 71  ? 0.491 0.025 0.374 -0.003 0.011  0.083  70  PHE   BBB C   
2534 O  O   . PHE   B 71  ? 0.471 0.031 0.391 -0.028 0.013  -0.032 70  PHE   BBB O   
2535 C  CB  . PHE   B 71  ? 0.485 0.008 0.388 0.015  0.017  -0.022 70  PHE   BBB CB  
2536 C  CG  . PHE   B 71  ? 0.440 0.025 0.347 -0.044 0.019  -0.028 70  PHE   BBB CG  
2537 C  CD1 . PHE   B 71  ? 0.428 0.007 0.324 0.005  0.039  0.014  70  PHE   BBB CD1 
2538 C  CD2 . PHE   B 71  ? 0.464 0.016 0.322 -0.000 -0.006 0.055  70  PHE   BBB CD2 
2539 C  CE1 . PHE   B 71  ? 0.484 0.108 0.325 -0.006 0.038  0.012  70  PHE   BBB CE1 
2540 C  CE2 . PHE   B 71  ? 0.452 0.013 0.352 -0.005 0.010  0.049  70  PHE   BBB CE2 
2541 C  CZ  . PHE   B 71  ? 0.471 0.061 0.356 -0.121 0.033  -0.023 70  PHE   BBB CZ  
2542 N  N   . GLU   B 72  ? 0.495 0.026 0.367 0.049  0.021  0.074  71  GLU   BBB N   
2543 C  CA  . GLU   B 72  ? 0.505 0.013 0.404 0.040  0.006  -0.036 71  GLU   BBB CA  
2544 C  C   . GLU   B 72  ? 0.529 0.018 0.376 -0.053 0.033  0.045  71  GLU   BBB C   
2545 O  O   . GLU   B 72  ? 0.601 0.008 0.368 0.017  0.037  0.023  71  GLU   BBB O   
2546 C  CB  . GLU   B 72  ? 0.554 0.018 0.464 0.077  0.021  0.027  71  GLU   BBB CB  
2547 C  CG  . GLU   B 72  ? 0.671 0.135 0.589 0.044  -0.056 0.036  71  GLU   BBB CG  
2548 C  CD  . GLU   B 72  ? 0.769 0.151 0.705 0.121  -0.091 0.073  71  GLU   BBB CD  
2549 O  OE1 . GLU   B 72  ? 0.932 0.196 0.639 0.025  -0.079 0.073  71  GLU   BBB OE1 
2550 O  OE2 . GLU   B 72  ? 0.909 0.224 0.923 0.111  -0.192 0.281  71  GLU   BBB OE2 
2551 N  N   . ASP   B 73  ? 0.495 0.029 0.418 -0.089 0.012  0.050  72  ASP   BBB N   
2552 C  CA  . ASP   B 73  ? 0.491 0.007 0.424 -0.015 -0.002 0.002  72  ASP   BBB CA  
2553 C  C   . ASP   B 73  ? 0.532 0.012 0.525 0.024  0.041  0.052  72  ASP   BBB C   
2554 O  O   . ASP   B 73  ? 0.492 0.059 0.514 -0.025 0.050  0.078  72  ASP   BBB O   
2555 C  CB  . ASP   B 73  ? 0.478 0.015 0.451 -0.050 0.069  0.029  72  ASP   BBB CB  
2556 C  CG  . ASP   B 73  ? 0.567 0.105 0.411 0.042  0.039  0.033  72  ASP   BBB CG  
2557 O  OD1 . ASP   B 73  ? 0.651 0.006 0.464 -0.002 -0.037 -0.005 72  ASP   BBB OD1 
2558 O  OD2 . ASP   B 73  ? 0.520 0.063 0.515 -0.037 0.006  0.060  72  ASP   BBB OD2 
2559 N  N   . ASN   B 74  ? 0.564 0.024 0.424 -0.099 -0.030 0.003  73  ASN   BBB N   
2560 C  CA  . ASN   B 74  ? 0.515 0.172 0.560 -0.087 -0.033 0.020  73  ASN   BBB CA  
2561 C  C   . ASN   B 74  ? 0.554 0.126 0.500 -0.129 0.066  0.053  73  ASN   BBB C   
2562 O  O   . ASN   B 74  ? 0.545 0.154 0.568 -0.100 0.004  -0.042 73  ASN   BBB O   
2563 C  CB  . ASN   B 74  ? 0.581 0.286 0.562 -0.181 -0.038 0.114  73  ASN   BBB CB  
2564 C  CG  . ASN   B 74  ? 0.775 0.193 0.725 -0.166 -0.062 0.141  73  ASN   BBB CG  
2565 O  OD1 . ASN   B 74  ? 0.806 0.069 0.631 -0.002 0.052  0.125  73  ASN   BBB OD1 
2566 N  ND2 . ASN   B 74  ? 0.891 0.193 0.941 -0.183 -0.176 0.161  73  ASN   BBB ND2 
2567 N  N   . ASP   B 75  ? 0.598 0.041 0.501 -0.135 0.072  0.025  74  ASP   BBB N   
2568 C  CA  . ASP   B 75  ? 0.539 0.020 0.470 -0.078 0.038  0.025  74  ASP   BBB CA  
2569 C  C   . ASP   B 75  ? 0.593 0.147 0.416 -0.133 0.024  0.017  74  ASP   BBB C   
2570 O  O   . ASP   B 75  ? 0.600 0.089 0.461 -0.079 -0.026 0.073  74  ASP   BBB O   
2571 C  CB  . ASP   B 75  ? 0.614 0.028 0.438 -0.094 0.011  0.055  74  ASP   BBB CB  
2572 C  CG  . ASP   B 75  ? 0.678 0.040 0.589 -0.116 -0.054 0.098  74  ASP   BBB CG  
2573 O  OD1 . ASP   B 75  ? 0.633 0.096 0.477 -0.057 -0.045 0.005  74  ASP   BBB OD1 
2574 O  OD2 . ASP   B 75  ? 0.924 0.113 0.697 -0.218 0.013  0.192  74  ASP   BBB OD2 
2575 N  N   . ASN   B 76  ? 0.616 0.076 0.460 -0.205 0.011  0.018  75  ASN   BBB N   
2576 C  CA  . ASN   B 76  ? 0.563 0.088 0.417 -0.191 -0.042 0.051  75  ASN   BBB CA  
2577 C  C   . ASN   B 76  ? 0.592 0.145 0.362 -0.132 -0.093 -0.002 75  ASN   BBB C   
2578 O  O   . ASN   B 76  ? 0.674 0.186 0.334 -0.175 -0.053 0.076  75  ASN   BBB O   
2579 C  CB  . ASN   B 76  ? 0.572 0.156 0.544 -0.256 -0.067 -0.021 75  ASN   BBB CB  
2580 C  CG  . ASN   B 76  ? 0.495 0.318 0.531 -0.141 -0.110 0.014  75  ASN   BBB CG  
2581 O  OD1 . ASN   B 76  ? 0.667 0.372 0.517 -0.341 -0.086 0.098  75  ASN   BBB OD1 
2582 N  ND2 . ASN   B 76  ? 0.612 0.463 0.805 -0.078 -0.317 -0.090 75  ASN   BBB ND2 
2583 N  N   . ARG   B 77  ? 0.542 0.071 0.469 -0.100 -0.006 0.058  76  ARG   BBB N   
2584 C  CA  . ARG   B 77  ? 0.567 0.057 0.450 -0.087 0.022  0.007  76  ARG   BBB CA  
2585 C  C   . ARG   B 77  ? 0.668 0.042 0.424 -0.011 0.067  0.083  76  ARG   BBB C   
2586 O  O   . ARG   B 77  ? 0.780 0.016 0.388 -0.074 0.032  0.027  76  ARG   BBB O   
2587 C  CB  . ARG   B 77  ? 0.649 0.023 0.546 -0.100 -0.059 0.035  76  ARG   BBB CB  
2588 C  CG  . ARG   B 77  ? 0.700 0.024 0.515 -0.105 -0.031 -0.022 76  ARG   BBB CG  
2589 C  CD  . ARG   B 77  ? 0.836 0.063 0.489 -0.097 0.007  0.096  76  ARG   BBB CD  
2590 N  NE  . ARG   B 77  ? 0.613 0.120 0.455 0.012  -0.014 0.098  76  ARG   BBB NE  
2591 C  CZ  . ARG   B 77  ? 0.504 0.156 0.466 0.001  -0.013 0.110  76  ARG   BBB CZ  
2592 N  NH1 . ARG   B 77  ? 0.594 0.169 0.595 0.081  -0.050 0.042  76  ARG   BBB NH1 
2593 N  NH2 . ARG   B 77  ? 0.620 0.127 0.490 -0.076 -0.002 0.082  76  ARG   BBB NH2 
2594 N  N   . SER   B 78  ? 0.463 0.102 0.407 -0.080 0.005  -0.046 77  SER   BBB N   
2595 C  CA  . SER   B 78  ? 0.464 0.121 0.358 -0.006 0.018  0.034  77  SER   BBB CA  
2596 C  C   . SER   B 78  ? 0.444 0.159 0.294 0.004  0.074  0.052  77  SER   BBB C   
2597 O  O   . SER   B 78  ? 0.454 0.012 0.356 0.024  0.040  0.040  77  SER   BBB O   
2598 C  CB  . SER   B 78  ? 0.474 0.035 0.326 0.048  0.008  0.009  77  SER   BBB CB  
2599 O  OG  . SER   B 78  ? 0.477 0.012 0.369 0.031  -0.018 -0.036 77  SER   BBB OG  
2600 N  N   . VAL   B 79  ? 0.502 0.057 0.324 -0.031 0.006  0.020  78  VAL   BBB N   
2601 C  CA  . VAL   B 79  ? 0.527 0.035 0.335 -0.015 -0.013 -0.007 78  VAL   BBB CA  
2602 C  C   . VAL   B 79  ? 0.439 0.047 0.393 0.002  0.010  0.044  78  VAL   BBB C   
2603 O  O   . VAL   B 79  ? 0.627 0.012 0.486 0.043  -0.003 0.037  78  VAL   BBB O   
2604 C  CB  . VAL   B 79  ? 0.525 0.103 0.361 -0.071 0.028  -0.018 78  VAL   BBB CB  
2605 C  CG1 . VAL   B 79  ? 0.548 0.384 0.402 -0.030 0.048  0.002  78  VAL   BBB CG1 
2606 C  CG2 . VAL   B 79  ? 0.586 0.291 0.427 -0.104 0.004  -0.181 78  VAL   BBB CG2 
2607 N  N   . LEU   B 80  ? 0.492 0.015 0.325 -0.005 -0.010 -0.012 79  LEU   BBB N   
2608 C  CA  . LEU   B 80  ? 0.433 0.169 0.309 -0.077 -0.012 0.002  79  LEU   BBB CA  
2609 C  C   . LEU   B 80  ? 0.404 0.029 0.443 -0.093 -0.005 0.021  79  LEU   BBB C   
2610 O  O   . LEU   B 80  ? 0.421 0.075 0.419 -0.044 -0.016 0.017  79  LEU   BBB O   
2611 C  CB  . LEU   B 80  ? 0.417 0.085 0.314 0.013  -0.049 0.027  79  LEU   BBB CB  
2612 C  CG  . LEU   B 80  ? 0.422 0.008 0.329 -0.016 -0.058 -0.020 79  LEU   BBB CG  
2613 C  CD1 . LEU   B 80  ? 0.479 0.008 0.384 0.001  -0.027 0.021  79  LEU   BBB CD1 
2614 C  CD2 . LEU   B 80  ? 0.452 0.017 0.407 -0.068 -0.023 0.013  79  LEU   BBB CD2 
2615 N  N   . LYS   B 81  ? 0.602 0.026 0.466 -0.103 -0.036 0.036  80  LYS   BBB N   
2616 C  CA  . LYS   B 81  ? 0.618 0.023 0.455 -0.102 -0.072 0.020  80  LYS   BBB CA  
2617 C  C   . LYS   B 81  ? 0.405 0.048 0.366 -0.070 -0.037 -0.007 80  LYS   BBB C   
2618 O  O   . LYS   B 81  ? 0.440 0.077 0.346 -0.047 -0.010 0.068  80  LYS   BBB O   
2619 C  CB  . LYS   B 81  ? 0.669 0.100 0.494 -0.248 -0.141 0.066  80  LYS   BBB CB  
2620 C  CG  . LYS   B 81  ? 0.685 0.308 0.726 -0.070 -0.199 0.028  80  LYS   BBB CG  
2621 C  CD  . LYS   B 81  ? 1.113 0.371 0.738 -0.286 -0.102 0.099  80  LYS   BBB CD  
2622 C  CE  . LYS   B 81  ? 0.817 0.281 1.132 -0.436 -0.047 -0.186 80  LYS   BBB CE  
2623 N  NZ  . LYS   B 81  ? 1.439 0.052 1.352 -0.252 -0.026 -0.033 80  LYS   BBB NZ  
2624 N  N   . GLY   B 82  ? 0.432 0.192 0.397 -0.048 -0.066 0.014  81  GLY   BBB N   
2625 C  CA  . GLY   B 82  ? 0.378 0.269 0.382 -0.043 -0.032 0.009  81  GLY   BBB CA  
2626 C  C   . GLY   B 82  ? 0.368 0.252 0.300 -0.010 0.002  0.013  81  GLY   BBB C   
2627 O  O   . GLY   B 82  ? 0.452 0.128 0.336 -0.037 0.017  0.026  81  GLY   BBB O   
2628 N  N   . GLY   B 83  ? 0.409 0.122 0.379 -0.039 -0.013 0.057  82  GLY   BBB N   
2629 C  CA  . GLY   B 83  ? 0.437 0.124 0.322 -0.033 0.004  0.033  82  GLY   BBB CA  
2630 C  C   . GLY   B 83  ? 0.412 0.125 0.414 -0.040 -0.047 0.079  82  GLY   BBB C   
2631 O  O   . GLY   B 83  ? 0.460 0.068 0.487 -0.049 -0.095 0.106  82  GLY   BBB O   
2632 N  N   . PRO   B 84  ? 0.479 0.310 0.360 0.041  -0.014 0.037  83  PRO   BBB N   
2633 C  CA  . PRO   B 84  ? 0.499 0.158 0.477 -0.007 -0.019 -0.044 83  PRO   BBB CA  
2634 C  C   . PRO   B 84  ? 0.402 0.330 0.434 0.085  -0.040 0.075  83  PRO   BBB C   
2635 O  O   . PRO   B 84  ? 0.453 0.244 0.569 0.098  0.042  0.149  83  PRO   BBB O   
2636 C  CB  . PRO   B 84  ? 0.512 0.057 0.514 -0.020 0.023  0.015  83  PRO   BBB CB  
2637 C  CG  . PRO   B 84  ? 0.476 0.295 0.444 -0.007 0.021  -0.024 83  PRO   BBB CG  
2638 C  CD  . PRO   B 84  ? 0.424 0.220 0.441 0.043  -0.051 0.053  83  PRO   BBB CD  
2639 N  N   . PHE   B 85  ? 0.454 0.248 0.469 0.044  -0.050 0.033  84  PHE   BBB N   
2640 C  CA  . PHE   B 85  ? 0.433 0.352 0.488 -0.014 -0.031 0.001  84  PHE   BBB CA  
2641 C  C   . PHE   B 85  ? 0.455 0.290 0.472 -0.006 -0.064 0.064  84  PHE   BBB C   
2642 O  O   . PHE   B 85  ? 0.599 0.326 0.489 -0.089 -0.054 -0.046 84  PHE   BBB O   
2643 C  CB  . PHE   B 85  ? 0.475 0.221 0.468 -0.086 -0.035 0.003  84  PHE   BBB CB  
2644 C  CG  . PHE   B 85  ? 0.445 0.239 0.373 -0.100 -0.005 0.032  84  PHE   BBB CG  
2645 C  CD1 . PHE   B 85  ? 0.496 0.224 0.438 -0.129 -0.001 0.058  84  PHE   BBB CD1 
2646 C  CD2 . PHE   B 85  ? 0.475 0.221 0.396 -0.063 -0.035 0.133  84  PHE   BBB CD2 
2647 C  CE1 . PHE   B 85  ? 0.455 0.124 0.501 -0.066 0.022  -0.029 84  PHE   BBB CE1 
2648 C  CE2 . PHE   B 85  ? 0.591 0.251 0.433 -0.054 -0.077 0.097  84  PHE   BBB CE2 
2649 C  CZ  . PHE   B 85  ? 0.408 0.360 0.473 -0.087 -0.044 0.020  84  PHE   BBB CZ  
2650 N  N   . SER   B 86  ? 0.473 0.389 0.475 -0.105 -0.049 0.112  85  SER   BBB N   
2651 C  CA  . SER   B 86  ? 0.484 0.467 0.556 -0.161 -0.028 0.096  85  SER   BBB CA  
2652 C  C   . SER   B 86  ? 0.627 0.218 0.642 -0.197 0.020  0.072  85  SER   BBB C   
2653 O  O   . SER   B 86  ? 0.644 0.103 0.903 -0.073 -0.004 0.167  85  SER   BBB O   
2654 C  CB  . SER   B 86  ? 0.456 0.748 0.595 -0.150 -0.063 0.074  85  SER   BBB CB  
2655 O  OG  . SER   B 86  ? 0.618 0.725 1.020 -0.063 -0.045 -0.023 85  SER   BBB OG  
2656 N  N   . ASP   B 87  ? 0.557 0.651 0.553 -0.137 0.000  0.142  86  ASP   BBB N   
2657 C  CA  . ASP   B 87  ? 0.571 0.770 0.558 0.016  0.022  0.144  86  ASP   BBB CA  
2658 C  C   . ASP   B 87  ? 0.550 0.455 0.523 -0.056 0.053  0.208  86  ASP   BBB C   
2659 O  O   . ASP   B 87  ? 0.518 0.458 0.561 -0.095 -0.035 0.233  86  ASP   BBB O   
2660 C  CB  . ASP   B 87  ? 0.621 0.822 0.812 0.009  0.130  -0.010 86  ASP   BBB CB  
2661 C  CG  . ASP   B 87  ? 0.664 0.542 0.816 0.008  -0.137 -0.113 86  ASP   BBB CG  
2662 O  OD1 . ASP   B 87  ? 0.486 0.646 0.688 -0.105 -0.053 0.179  86  ASP   BBB OD1 
2663 O  OD2 . ASP   B 87  ? 0.588 0.383 0.735 0.008  -0.108 0.053  86  ASP   BBB OD2 
2664 N  N   . SER   B 88  ? 0.509 0.380 0.548 -0.148 -0.058 0.154  87  SER   BBB N   
2665 C  CA  . SER   B 88  ? 0.510 0.185 0.455 -0.146 -0.077 0.105  87  SER   BBB CA  
2666 C  C   . SER   B 88  ? 0.390 0.090 0.455 -0.015 -0.018 0.080  87  SER   BBB C   
2667 O  O   . SER   B 88  ? 0.432 0.236 0.570 -0.045 0.008  0.055  87  SER   BBB O   
2668 C  CB  . SER   B 88  ? 0.624 0.106 0.764 -0.174 -0.066 -0.032 87  SER   BBB CB  
2669 O  OG  . SER   B 88  ? 0.683 0.043 0.949 -0.030 -0.039 -0.017 87  SER   BBB OG  
2670 N  N   . TYR   B 89  ? 0.397 0.097 0.428 -0.050 0.002  0.004  88  TYR   BBB N   
2671 C  CA  . TYR   B 89  ? 0.389 0.177 0.377 -0.090 -0.008 0.056  88  TYR   BBB CA  
2672 C  C   . TYR   B 89  ? 0.405 0.082 0.341 -0.049 0.045  -0.001 88  TYR   BBB C   
2673 O  O   . TYR   B 89  ? 0.408 0.164 0.372 0.019  0.029  0.027  88  TYR   BBB O   
2674 C  CB  . TYR   B 89  ? 0.363 0.060 0.416 -0.029 -0.035 0.010  88  TYR   BBB CB  
2675 C  CG  . TYR   B 89  ? 0.366 0.148 0.356 -0.007 0.001  0.038  88  TYR   BBB CG  
2676 C  CD1 . TYR   B 89  ? 0.387 0.109 0.440 -0.015 -0.039 0.053  88  TYR   BBB CD1 
2677 C  CD2 . TYR   B 89  ? 0.442 0.140 0.375 0.018  -0.017 0.035  88  TYR   BBB CD2 
2678 C  CE1 . TYR   B 89  ? 0.408 0.178 0.513 0.008  -0.060 0.067  88  TYR   BBB CE1 
2679 C  CE2 . TYR   B 89  ? 0.392 0.122 0.494 -0.051 -0.067 0.065  88  TYR   BBB CE2 
2680 C  CZ  . TYR   B 89  ? 0.416 0.162 0.432 0.065  -0.020 0.121  88  TYR   BBB CZ  
2681 O  OH  . TYR   B 89  ? 0.465 0.116 0.566 0.076  -0.067 0.126  88  TYR   BBB OH  
2682 N  N   . ARG   B 90  ? 0.439 0.064 0.370 -0.046 -0.011 0.021  89  ARG   BBB N   
2683 C  CA  . ARG   B 90  ? 0.458 0.050 0.406 0.006  0.021  0.041  89  ARG   BBB CA  
2684 C  C   . ARG   B 90  ? 0.443 0.043 0.330 -0.018 0.026  -0.046 89  ARG   BBB C   
2685 O  O   . ARG   B 90  ? 0.449 0.009 0.369 0.026  0.020  -0.021 89  ARG   BBB O   
2686 C  CB  . ARG   B 90  ? 0.470 0.013 0.406 0.020  0.037  -0.004 89  ARG   BBB CB  
2687 C  CG  . ARG   B 90  ? 0.453 0.069 0.441 -0.021 0.022  0.034  89  ARG   BBB CG  
2688 C  CD  . ARG   B 90  ? 0.512 0.123 0.438 -0.020 0.051  0.029  89  ARG   BBB CD  
2689 N  NE  . ARG   B 90  ? 0.515 0.133 0.478 -0.020 0.039  0.073  89  ARG   BBB NE  
2690 C  CZ  . ARG   B 90  ? 0.448 0.193 0.467 0.027  0.039  0.009  89  ARG   BBB CZ  
2691 N  NH1 . ARG   B 90  ? 0.717 0.019 0.466 -0.002 0.117  0.074  89  ARG   BBB NH1 
2692 N  NH2 . ARG   B 90  ? 0.492 0.185 0.579 0.024  -0.048 0.004  89  ARG   BBB NH2 
2693 N  N   . LEU   B 91  ? 0.481 0.010 0.425 -0.009 -0.008 0.038  90  LEU   BBB N   
2694 C  CA  . LEU   B 91  ? 0.383 0.010 0.344 -0.008 0.032  0.033  90  LEU   BBB CA  
2695 C  C   . LEU   B 91  ? 0.357 0.018 0.343 -0.036 0.034  -0.053 90  LEU   BBB C   
2696 O  O   . LEU   B 91  ? 0.449 0.076 0.349 -0.059 0.007  0.041  90  LEU   BBB O   
2697 C  CB  . LEU   B 91  ? 0.369 0.017 0.370 -0.002 0.023  0.052  90  LEU   BBB CB  
2698 C  CG  . LEU   B 91  ? 0.396 0.011 0.335 -0.024 0.029  0.030  90  LEU   BBB CG  
2699 C  CD1 . LEU   B 91  ? 0.344 0.012 0.298 -0.029 0.038  -0.033 90  LEU   BBB CD1 
2700 C  CD2 . LEU   B 91  ? 0.446 0.048 0.374 0.003  0.027  -0.041 90  LEU   BBB CD2 
2701 N  N   . PHE   B 92  ? 0.432 0.008 0.337 -0.025 0.009  0.004  91  PHE   BBB N   
2702 C  CA  . PHE   B 92  ? 0.398 0.007 0.359 -0.003 0.028  0.010  91  PHE   BBB CA  
2703 C  C   . PHE   B 92  ? 0.395 0.011 0.343 0.030  0.067  -0.023 91  PHE   BBB C   
2704 O  O   . PHE   B 92  ? 0.568 0.007 0.438 -0.004 -0.012 -0.012 91  PHE   BBB O   
2705 C  CB  . PHE   B 92  ? 0.394 0.007 0.360 0.011  0.023  0.006  91  PHE   BBB CB  
2706 C  CG  . PHE   B 92  ? 0.453 0.007 0.367 0.013  -0.001 0.014  91  PHE   BBB CG  
2707 C  CD1 . PHE   B 92  ? 0.430 0.015 0.391 0.058  0.012  -0.011 91  PHE   BBB CD1 
2708 C  CD2 . PHE   B 92  ? 0.383 0.012 0.412 0.046  -0.002 0.012  91  PHE   BBB CD2 
2709 C  CE1 . PHE   B 92  ? 0.418 0.008 0.437 0.020  0.013  0.012  91  PHE   BBB CE1 
2710 C  CE2 . PHE   B 92  ? 0.434 0.008 0.359 0.022  0.041  0.011  91  PHE   BBB CE2 
2711 C  CZ  . PHE   B 92  ? 0.390 0.115 0.428 0.008  -0.007 0.010  91  PHE   BBB CZ  
2712 N  N   . GLN   B 93  ? 0.368 0.098 0.263 0.034  0.016  0.047  92  GLN   BBB N   
2713 C  CA  . GLN   B 93  ? 0.327 0.056 0.314 0.061  0.013  0.001  92  GLN   BBB CA  
2714 C  C   . GLN   B 93  ? 0.319 0.022 0.301 -0.005 0.007  -0.069 92  GLN   BBB C   
2715 O  O   . GLN   B 93  ? 0.416 0.006 0.363 -0.001 -0.012 -0.006 92  GLN   BBB O   
2716 C  CB  . GLN   B 93  ? 0.365 0.216 0.377 0.063  0.056  -0.138 92  GLN   BBB CB  
2717 C  CG  . GLN   B 93  ? 0.429 0.326 0.343 0.026  0.015  -0.089 92  GLN   BBB CG  
2718 C  CD  . GLN   B 93  ? 0.438 0.088 0.347 -0.005 0.012  0.043  92  GLN   BBB CD  
2719 O  OE1 . GLN   B 93  ? 0.487 0.096 0.397 0.041  0.012  0.009  92  GLN   BBB OE1 
2720 N  NE2 . GLN   B 93  ? 0.411 0.082 0.324 -0.016 -0.014 0.037  92  GLN   BBB NE2 
2721 N  N   . PHE   B 94  ? 0.326 0.086 0.305 0.007  0.008  0.005  93  PHE   BBB N   
2722 C  CA  . PHE   B 94  ? 0.351 0.053 0.331 -0.011 -0.003 0.027  93  PHE   BBB CA  
2723 C  C   . PHE   B 94  ? 0.361 0.015 0.327 -0.020 0.017  0.049  93  PHE   BBB C   
2724 O  O   . PHE   B 94  ? 0.430 0.006 0.337 -0.000 -0.013 0.006  93  PHE   BBB O   
2725 C  CB  . PHE   B 94  ? 0.358 0.106 0.284 0.027  -0.008 0.057  93  PHE   BBB CB  
2726 C  CG  . PHE   B 94  ? 0.313 0.011 0.317 -0.000 0.026  0.038  93  PHE   BBB CG  
2727 C  CD1 . PHE   B 94  ? 0.348 0.047 0.422 -0.013 -0.032 -0.051 93  PHE   BBB CD1 
2728 C  CD2 . PHE   B 94  ? 0.324 0.024 0.379 -0.071 -0.003 0.025  93  PHE   BBB CD2 
2729 C  CE1 . PHE   B 94  ? 0.372 0.023 0.381 -0.077 -0.021 -0.004 93  PHE   BBB CE1 
2730 C  CE2 . PHE   B 94  ? 0.392 0.036 0.364 0.027  -0.013 -0.001 93  PHE   BBB CE2 
2731 C  CZ  . PHE   B 94  ? 0.421 0.008 0.352 0.022  -0.036 -0.014 93  PHE   BBB CZ  
2732 N  N   . HIS   B 95  ? 0.396 0.021 0.379 -0.002 -0.030 0.074  94  HIS   BBB N   
2733 C  CA  . HIS   B 95  ? 0.360 0.151 0.343 0.016  0.014  -0.016 94  HIS   BBB CA  
2734 C  C   . HIS   B 95  ? 0.353 0.062 0.303 0.040  -0.045 0.017  94  HIS   BBB C   
2735 O  O   . HIS   B 95  ? 0.399 0.009 0.319 -0.014 -0.040 -0.026 94  HIS   BBB O   
2736 C  CB  . HIS   B 95  ? 0.360 0.007 0.346 -0.008 -0.019 -0.008 94  HIS   BBB CB  
2737 C  CG  . HIS   B 95  ? 0.354 0.011 0.345 0.007  -0.017 0.038  94  HIS   BBB CG  
2738 N  ND1 . HIS   B 95  ? 0.368 0.009 0.345 0.030  0.017  -0.007 94  HIS   BBB ND1 
2739 C  CD2 . HIS   B 95  ? 0.480 0.014 0.383 -0.048 0.023  -0.034 94  HIS   BBB CD2 
2740 C  CE1 . HIS   B 95  ? 0.390 0.109 0.325 0.062  -0.009 0.037  94  HIS   BBB CE1 
2741 N  NE2 . HIS   B 95  ? 0.569 0.007 0.674 0.019  0.004  -0.008 94  HIS   BBB NE2 
2742 N  N   . PHE   B 96  ? 0.344 0.073 0.334 0.045  -0.025 0.004  95  PHE   BBB N   
2743 C  CA  . PHE   B 96  ? 0.305 0.075 0.330 -0.043 -0.019 -0.103 95  PHE   BBB CA  
2744 C  C   . PHE   B 96  ? 0.379 0.047 0.345 0.040  -0.001 -0.055 95  PHE   BBB C   
2745 O  O   . PHE   B 96  ? 0.408 0.011 0.372 0.041  0.024  -0.004 95  PHE   BBB O   
2746 C  CB  . PHE   B 96  ? 0.365 0.023 0.303 0.016  0.001  -0.057 95  PHE   BBB CB  
2747 C  CG  . PHE   B 96  ? 0.384 0.017 0.282 -0.023 -0.006 -0.050 95  PHE   BBB CG  
2748 C  CD1 . PHE   B 96  ? 0.439 0.045 0.316 0.035  0.001  -0.025 95  PHE   BBB CD1 
2749 C  CD2 . PHE   B 96  ? 0.431 0.012 0.292 0.049  -0.021 -0.006 95  PHE   BBB CD2 
2750 C  CE1 . PHE   B 96  ? 0.391 0.018 0.308 0.010  -0.013 0.013  95  PHE   BBB CE1 
2751 C  CE2 . PHE   B 96  ? 0.380 0.030 0.307 0.070  -0.028 -0.048 95  PHE   BBB CE2 
2752 C  CZ  . PHE   B 96  ? 0.433 0.159 0.323 0.036  -0.033 0.033  95  PHE   BBB CZ  
2753 N  N   . HIS   B 97  ? 0.351 0.059 0.360 -0.067 -0.029 -0.088 96  HIS   BBB N   
2754 C  CA  . HIS   B 97  ? 0.306 0.011 0.380 -0.025 -0.067 -0.026 96  HIS   BBB CA  
2755 C  C   . HIS   B 97  ? 0.348 0.117 0.339 0.001  -0.013 -0.017 96  HIS   BBB C   
2756 O  O   . HIS   B 97  ? 0.408 0.007 0.407 -0.020 0.038  -0.008 96  HIS   BBB O   
2757 C  CB  . HIS   B 97  ? 0.334 0.016 0.380 0.026  -0.058 -0.058 96  HIS   BBB CB  
2758 C  CG  . HIS   B 97  ? 0.353 0.008 0.391 -0.022 -0.010 -0.005 96  HIS   BBB CG  
2759 N  ND1 . HIS   B 97  ? 0.439 0.017 0.402 -0.056 0.006  -0.038 96  HIS   BBB ND1 
2760 C  CD2 . HIS   B 97  ? 0.295 0.016 0.331 -0.051 0.029  -0.018 96  HIS   BBB CD2 
2761 C  CE1 . HIS   B 97  ? 0.396 0.037 0.307 0.024  0.017  0.043  96  HIS   BBB CE1 
2762 N  NE2 . HIS   B 97  ? 0.339 0.200 0.252 0.072  0.018  -0.010 96  HIS   BBB NE2 
2763 N  N   . TRP   B 98  ? 0.406 0.066 0.408 0.080  -0.022 -0.093 97  TRP   BBB N   
2764 C  CA  . TRP   B 98  ? 0.400 0.063 0.421 0.045  0.006  -0.120 97  TRP   BBB CA  
2765 C  C   . TRP   B 98  ? 0.415 0.059 0.420 -0.049 0.018  -0.060 97  TRP   BBB C   
2766 O  O   . TRP   B 98  ? 0.410 0.069 0.434 -0.055 0.017  -0.034 97  TRP   BBB O   
2767 C  CB  . TRP   B 98  ? 0.344 0.095 0.395 -0.029 -0.012 -0.034 97  TRP   BBB CB  
2768 C  CG  . TRP   B 98  ? 0.388 0.071 0.419 0.013  -0.017 -0.023 97  TRP   BBB CG  
2769 C  CD1 . TRP   B 98  ? 0.473 0.018 0.430 0.008  0.028  -0.064 97  TRP   BBB CD1 
2770 C  CD2 . TRP   B 98  ? 0.455 0.017 0.424 0.003  0.006  -0.065 97  TRP   BBB CD2 
2771 N  NE1 . TRP   B 98  ? 0.494 0.041 0.419 -0.044 -0.035 -0.109 97  TRP   BBB NE1 
2772 C  CE2 . TRP   B 98  ? 0.394 0.014 0.442 -0.032 -0.044 -0.045 97  TRP   BBB CE2 
2773 C  CE3 . TRP   B 98  ? 0.404 0.109 0.412 -0.052 -0.012 -0.094 97  TRP   BBB CE3 
2774 C  CZ2 . TRP   B 98  ? 0.386 0.069 0.450 -0.002 0.044  -0.079 97  TRP   BBB CZ2 
2775 C  CZ3 . TRP   B 98  ? 0.411 0.017 0.385 0.024  -0.047 -0.061 97  TRP   BBB CZ3 
2776 C  CH2 . TRP   B 98  ? 0.380 0.067 0.365 0.006  -0.021 -0.026 97  TRP   BBB CH2 
2777 N  N   . GLY   B 99  ? 0.379 0.020 0.465 -0.020 0.011  -0.075 98  GLY   BBB N   
2778 C  CA  . GLY   B 99  ? 0.447 0.038 0.442 -0.093 0.001  -0.058 98  GLY   BBB CA  
2779 C  C   . GLY   B 99  ? 0.421 0.023 0.458 -0.077 -0.023 -0.030 98  GLY   BBB C   
2780 O  O   . GLY   B 99  ? 0.446 0.124 0.499 0.001  -0.009 -0.058 98  GLY   BBB O   
2781 N  N   . SER   B 100 ? 0.493 0.032 0.477 -0.104 -0.061 -0.030 99  SER   BBB N   
2782 C  CA  . SER   B 100 ? 0.436 0.042 0.595 -0.048 -0.047 -0.062 99  SER   BBB CA  
2783 C  C   . SER   B 100 ? 0.522 0.140 0.509 -0.025 -0.031 -0.048 99  SER   BBB C   
2784 O  O   . SER   B 100 ? 0.588 0.102 0.712 -0.084 -0.076 0.069  99  SER   BBB O   
2785 C  CB  . SER   B 100 ? 0.622 0.035 0.774 -0.130 -0.168 0.003  99  SER   BBB CB  
2786 O  OG  . SER   B 100 ? 0.732 0.235 0.688 -0.067 -0.156 0.058  99  SER   BBB OG  
2787 N  N   . THR   B 101 ? 0.533 0.139 0.531 -0.073 -0.037 0.013  100 THR   BBB N   
2788 C  CA  . THR   B 101 ? 0.575 0.108 0.612 -0.153 0.037  -0.053 100 THR   BBB CA  
2789 C  C   . THR   B 101 ? 0.601 0.355 0.461 -0.179 0.041  -0.082 100 THR   BBB C   
2790 O  O   . THR   B 101 ? 0.593 0.258 0.466 -0.154 0.051  -0.064 100 THR   BBB O   
2791 C  CB  . THR   B 101 ? 0.693 0.100 0.585 -0.124 0.058  -0.043 100 THR   BBB CB  
2792 O  OG1 . THR   B 101 ? 0.946 0.010 0.720 -0.045 -0.019 0.034  100 THR   BBB OG1 
2793 C  CG2 . THR   B 101 ? 0.694 0.256 0.622 -0.202 0.108  -0.133 100 THR   BBB CG2 
2794 N  N   . ASN   B 102 ? 0.606 0.330 0.574 -0.232 0.052  -0.112 101 ASN   BBB N   
2795 C  CA  . ASN   B 102 ? 0.704 0.291 0.666 -0.258 0.063  -0.161 101 ASN   BBB CA  
2796 C  C   . ASN   B 102 ? 0.856 0.181 0.609 -0.296 0.083  -0.160 101 ASN   BBB C   
2797 O  O   . ASN   B 102 ? 0.877 0.897 0.644 -0.607 0.162  -0.274 101 ASN   BBB O   
2798 C  CB  . ASN   B 102 ? 0.666 0.401 0.624 -0.194 0.130  -0.033 101 ASN   BBB CB  
2799 C  CG  . ASN   B 102 ? 0.478 0.309 0.689 -0.122 0.078  -0.130 101 ASN   BBB CG  
2800 O  OD1 . ASN   B 102 ? 0.607 0.242 0.742 -0.154 0.135  -0.144 101 ASN   BBB OD1 
2801 N  ND2 . ASN   B 102 ? 0.536 0.201 0.835 -0.165 0.210  -0.162 101 ASN   BBB ND2 
2802 N  N   . GLU   B 103 ? 0.849 0.195 0.549 -0.341 0.122  -0.099 102 GLU   BBB N   
2803 C  CA  . GLU   B 103 ? 0.731 0.733 0.673 -0.208 -0.018 0.069  102 GLU   BBB CA  
2804 C  C   . GLU   B 103 ? 0.742 0.726 0.409 -0.179 -0.017 0.140  102 GLU   BBB C   
2805 O  O   . GLU   B 103 ? 0.574 0.621 0.506 -0.169 -0.029 0.168  102 GLU   BBB O   
2806 C  CB  . GLU   B 103 ? 0.779 0.762 0.705 -0.226 -0.024 0.297  102 GLU   BBB CB  
2807 C  CG  . GLU   B 103 ? 0.898 1.146 0.796 -0.239 0.077  0.154  102 GLU   BBB CG  
2808 C  CD  . GLU   B 103 ? 0.740 1.096 0.885 -0.104 0.169  -0.060 102 GLU   BBB CD  
2809 O  OE1 . GLU   B 103 ? 1.158 0.895 0.931 -0.749 -0.092 -0.005 102 GLU   BBB OE1 
2810 O  OE2 . GLU   B 103 ? 0.939 1.084 1.176 -0.110 0.084  -0.344 102 GLU   BBB OE2 
2811 N  N   . HIS   B 104 ? 0.739 0.393 0.427 -0.165 0.060  -0.059 103 HIS   BBB N   
2812 C  CA  . HIS   B 104 ? 0.795 0.424 0.781 -0.179 0.013  -0.038 103 HIS   BBB CA  
2813 C  C   . HIS   B 104 ? 0.674 0.139 0.695 -0.107 -0.136 -0.062 103 HIS   BBB C   
2814 O  O   . HIS   B 104 ? 0.838 0.106 0.727 0.048  -0.094 -0.120 103 HIS   BBB O   
2815 C  CB  . HIS   B 104 ? 1.158 0.300 1.193 -0.383 -0.185 0.029  103 HIS   BBB CB  
2816 C  CG  . HIS   B 104 ? 1.583 1.209 1.306 -0.072 -0.070 -0.262 103 HIS   BBB CG  
2817 N  ND1 . HIS   B 104 ? 1.654 0.411 1.818 -0.090 -0.013 -0.735 103 HIS   BBB ND1 
2818 C  CD2 . HIS   B 104 ? 1.916 1.262 1.501 0.148  -0.169 -0.493 103 HIS   BBB CD2 
2819 C  CE1 . HIS   B 104 ? 1.209 1.660 1.183 0.049  -0.799 -0.214 103 HIS   BBB CE1 
2820 N  NE2 . HIS   B 104 ? 1.993 1.560 1.175 0.271  0.115  -0.589 103 HIS   BBB NE2 
2821 N  N   . GLY   B 105 ? 0.465 0.079 0.427 -0.020 -0.008 -0.069 104 GLY   BBB N   
2822 C  CA  . GLY   B 105 ? 0.465 0.145 0.489 0.016  0.015  -0.031 104 GLY   BBB CA  
2823 C  C   . GLY   B 105 ? 0.424 0.111 0.379 0.040  0.019  -0.029 104 GLY   BBB C   
2824 O  O   . GLY   B 105 ? 0.450 0.009 0.425 -0.013 0.024  -0.007 104 GLY   BBB O   
2825 N  N   . SER   B 106 ? 0.372 0.096 0.347 0.022  -0.019 -0.021 105 SER   BBB N   
2826 C  CA  . SER   B 106 ? 0.387 0.071 0.347 0.010  0.003  0.030  105 SER   BBB CA  
2827 C  C   . SER   B 106 ? 0.372 0.123 0.352 -0.012 -0.011 -0.052 105 SER   BBB C   
2828 O  O   . SER   B 106 ? 0.430 0.061 0.445 -0.024 -0.005 -0.021 105 SER   BBB O   
2829 C  CB  . SER   B 106 ? 0.438 0.171 0.341 0.041  0.033  0.034  105 SER   BBB CB  
2830 O  OG  . SER   B 106 ? 0.459 0.086 0.382 -0.047 -0.006 -0.000 105 SER   BBB OG  
2831 N  N   . GLU   B 107 ? 0.368 0.013 0.379 -0.023 0.002  0.014  106 GLU   BBB N   
2832 C  CA  . GLU   B 107 ? 0.421 0.006 0.422 -0.004 0.028  0.004  106 GLU   BBB CA  
2833 C  C   . GLU   B 107 ? 0.413 0.013 0.413 -0.043 -0.008 0.029  106 GLU   BBB C   
2834 O  O   . GLU   B 107 ? 0.409 0.010 0.503 0.034  0.041  0.017  106 GLU   BBB O   
2835 C  CB  . GLU   B 107 ? 0.382 0.013 0.423 -0.009 0.041  -0.051 106 GLU   BBB CB  
2836 C  CG  . GLU   B 107 ? 0.456 0.008 0.405 0.001  0.066  -0.026 106 GLU   BBB CG  
2837 C  CD  . GLU   B 107 ? 0.320 0.129 0.383 -0.056 0.008  -0.043 106 GLU   BBB CD  
2838 O  OE1 . GLU   B 107 ? 0.457 0.008 0.456 -0.023 -0.036 -0.005 106 GLU   BBB OE1 
2839 O  OE2 . GLU   B 107 ? 0.486 0.011 0.518 -0.026 0.051  0.037  106 GLU   BBB OE2 
2840 N  N   . HIS   B 108 ? 0.389 0.009 0.365 -0.015 0.000  0.027  107 HIS   BBB N   
2841 C  CA  . HIS   B 108 ? 0.428 0.008 0.363 -0.008 0.016  -0.021 107 HIS   BBB CA  
2842 C  C   . HIS   B 108 ? 0.348 0.031 0.418 -0.005 -0.009 -0.007 107 HIS   BBB C   
2843 O  O   . HIS   B 108 ? 0.382 0.017 0.438 -0.034 0.025  0.041  107 HIS   BBB O   
2844 C  CB  . HIS   B 108 ? 0.441 0.007 0.442 0.022  0.020  -0.000 107 HIS   BBB CB  
2845 C  CG  . HIS   B 108 ? 0.401 0.007 0.364 0.007  -0.007 -0.009 107 HIS   BBB CG  
2846 N  ND1 . HIS   B 108 ? 0.354 0.017 0.378 -0.038 0.024  0.031  107 HIS   BBB ND1 
2847 C  CD2 . HIS   B 108 ? 0.399 0.012 0.391 -0.018 0.028  0.041  107 HIS   BBB CD2 
2848 C  CE1 . HIS   B 108 ? 0.368 0.047 0.385 -0.031 0.015  0.062  107 HIS   BBB CE1 
2849 N  NE2 . HIS   B 108 ? 0.408 0.008 0.383 -0.001 0.016  0.027  107 HIS   BBB NE2 
2850 N  N   . THR   B 109 ? 0.469 0.030 0.394 -0.024 0.023  -0.005 108 THR   BBB N   
2851 C  CA  . THR   B 109 ? 0.443 0.007 0.479 -0.006 0.058  -0.020 108 THR   BBB CA  
2852 C  C   . THR   B 109 ? 0.562 0.016 0.559 0.042  0.019  0.059  108 THR   BBB C   
2853 O  O   . THR   B 109 ? 0.581 0.025 0.585 -0.023 0.022  0.100  108 THR   BBB O   
2854 C  CB  . THR   B 109 ? 0.410 0.035 0.477 -0.099 0.009  -0.047 108 THR   BBB CB  
2855 O  OG1 . THR   B 109 ? 0.475 0.060 0.498 -0.062 -0.028 0.092  108 THR   BBB OG1 
2856 C  CG2 . THR   B 109 ? 0.496 0.027 0.456 -0.049 0.024  -0.087 108 THR   BBB CG2 
2857 N  N   . VAL   B 110 ? 0.499 0.016 0.518 -0.039 -0.022 0.061  109 VAL   BBB N   
2858 C  CA  . VAL   B 110 ? 0.589 0.016 0.479 0.031  0.030  0.065  109 VAL   BBB CA  
2859 C  C   . VAL   B 110 ? 0.434 0.065 0.503 -0.044 0.007  0.141  109 VAL   BBB C   
2860 O  O   . VAL   B 110 ? 0.440 0.211 0.452 -0.059 0.065  0.047  109 VAL   BBB O   
2861 C  CB  . VAL   B 110 ? 0.572 0.007 0.464 0.010  -0.005 -0.010 109 VAL   BBB CB  
2862 C  CG1 . VAL   B 110 ? 0.490 0.164 0.430 0.008  -0.005 0.037  109 VAL   BBB CG1 
2863 C  CG2 . VAL   B 110 ? 0.512 0.185 0.466 0.098  0.062  0.178  109 VAL   BBB CG2 
2864 N  N   . ASP   B 111 ? 0.477 0.069 0.446 -0.022 0.006  0.105  110 ASP   BBB N   
2865 C  CA  . ASP   B 111 ? 0.529 0.072 0.434 -0.013 0.006  0.128  110 ASP   BBB CA  
2866 C  C   . ASP   B 111 ? 0.456 0.121 0.427 -0.057 0.065  0.104  110 ASP   BBB C   
2867 O  O   . ASP   B 111 ? 0.491 0.162 0.570 -0.073 0.107  0.122  110 ASP   BBB O   
2868 C  CB  . ASP   B 111 ? 0.606 0.021 0.519 -0.069 0.081  0.040  110 ASP   BBB CB  
2869 C  CG  . ASP   B 111 ? 0.586 0.255 0.457 -0.052 0.105  -0.028 110 ASP   BBB CG  
2870 O  OD1 . ASP   B 111 ? 0.576 0.347 0.532 -0.113 0.082  0.068  110 ASP   BBB OD1 
2871 O  OD2 . ASP   B 111 ? 0.666 0.034 0.484 -0.080 0.087  0.057  110 ASP   BBB OD2 
2872 N  N   . GLY   B 112 ? 0.515 0.068 0.462 -0.066 0.045  0.009  111 GLY   BBB N   
2873 C  CA  . GLY   B 112 ? 0.624 0.060 0.536 -0.170 -0.000 0.061  111 GLY   BBB CA  
2874 C  C   . GLY   B 112 ? 0.514 0.272 0.538 -0.129 0.033  -0.044 111 GLY   BBB C   
2875 O  O   . GLY   B 112 ? 0.716 0.032 0.578 -0.135 0.045  -0.000 111 GLY   BBB O   
2876 N  N   . VAL   B 113 ? 0.477 0.217 0.512 -0.117 0.019  0.062  112 VAL   BBB N   
2877 C  CA  . VAL   B 113 ? 0.497 0.206 0.467 -0.101 0.026  0.022  112 VAL   BBB CA  
2878 C  C   . VAL   B 113 ? 0.424 0.158 0.478 -0.038 0.026  0.009  112 VAL   BBB C   
2879 O  O   . VAL   B 113 ? 0.493 0.185 0.435 -0.095 0.056  0.028  112 VAL   BBB O   
2880 C  CB  . VAL   B 113 ? 0.480 0.366 0.444 0.028  0.093  0.111  112 VAL   BBB CB  
2881 C  CG1 . VAL   B 113 ? 0.493 0.622 0.464 0.051  0.009  0.125  112 VAL   BBB CG1 
2882 C  CG2 . VAL   B 113 ? 0.569 0.425 0.484 -0.059 0.017  0.166  112 VAL   BBB CG2 
2883 N  N   . LYS   B 114 ? 0.496 0.048 0.462 -0.046 -0.011 0.056  113 LYS   BBB N   
2884 C  CA  . LYS   B 114 ? 0.507 0.187 0.449 -0.047 -0.035 0.095  113 LYS   BBB CA  
2885 C  C   . LYS   B 114 ? 0.516 0.191 0.509 -0.074 0.096  0.092  113 LYS   BBB C   
2886 O  O   . LYS   B 114 ? 0.557 0.208 0.638 -0.137 0.074  0.083  113 LYS   BBB O   
2887 C  CB  . LYS   B 114 ? 0.544 0.273 0.598 0.038  0.027  -0.097 113 LYS   BBB CB  
2888 C  CG  . LYS   B 114 ? 0.607 0.305 0.598 0.076  0.009  -0.064 113 LYS   BBB CG  
2889 C  CD  . LYS   B 114 ? 0.707 0.315 0.596 0.072  0.082  -0.088 113 LYS   BBB CD  
2890 C  CE  . LYS   B 114 ? 1.609 0.019 0.936 -0.141 -0.091 -0.014 113 LYS   BBB CE  
2891 N  NZ  . LYS   B 114 ? 1.174 0.148 1.160 -0.274 -0.066 -0.272 113 LYS   BBB NZ  
2892 N  N   . TYR   B 115 ? 0.483 0.115 0.458 -0.038 0.051  0.042  114 TYR   BBB N   
2893 C  CA  . TYR   B 115 ? 0.425 0.146 0.466 -0.029 -0.022 -0.036 114 TYR   BBB CA  
2894 C  C   . TYR   B 115 ? 0.389 0.192 0.406 0.032  0.047  0.002  114 TYR   BBB C   
2895 O  O   . TYR   B 115 ? 0.442 0.040 0.438 -0.051 0.009  0.017  114 TYR   BBB O   
2896 C  CB  . TYR   B 115 ? 0.450 0.036 0.478 0.003  0.029  -0.063 114 TYR   BBB CB  
2897 C  CG  . TYR   B 115 ? 0.423 0.175 0.439 0.067  0.061  -0.070 114 TYR   BBB CG  
2898 C  CD1 . TYR   B 115 ? 0.551 0.018 0.491 0.005  0.045  -0.074 114 TYR   BBB CD1 
2899 C  CD2 . TYR   B 115 ? 0.500 0.114 0.498 0.069  0.089  -0.042 114 TYR   BBB CD2 
2900 C  CE1 . TYR   B 115 ? 0.512 0.232 0.512 -0.010 -0.010 -0.076 114 TYR   BBB CE1 
2901 C  CE2 . TYR   B 115 ? 0.604 0.417 0.484 0.013  -0.028 0.076  114 TYR   BBB CE2 
2902 C  CZ  . TYR   B 115 ? 0.641 0.220 0.470 0.031  -0.006 -0.031 114 TYR   BBB CZ  
2903 O  OH  . TYR   B 115 ? 0.630 0.194 0.486 -0.003 0.013  -0.008 114 TYR   BBB OH  
2904 N  N   . SER   B 116 ? 0.448 0.031 0.461 -0.038 -0.012 -0.034 115 SER   BBB N   
2905 C  CA  . SER   B 116 ? 0.396 0.010 0.494 -0.038 0.001  -0.008 115 SER   BBB CA  
2906 C  C   . SER   B 116 ? 0.336 0.184 0.405 0.006  -0.012 -0.049 115 SER   BBB C   
2907 O  O   . SER   B 116 ? 0.424 0.092 0.436 -0.061 0.023  -0.079 115 SER   BBB O   
2908 C  CB  . SER   B 116 ? 0.388 0.327 0.474 0.074  0.059  -0.032 115 SER   BBB CB  
2909 O  OG  . SER   B 116 ? 0.582 0.251 0.568 0.079  0.094  0.063  115 SER   BBB OG  
2910 N  N   . ALA   B 117 ? 0.358 0.071 0.399 0.010  0.021  -0.040 116 ALA   BBB N   
2911 C  CA  . ALA   B 117 ? 0.322 0.165 0.339 0.059  0.010  -0.056 116 ALA   BBB CA  
2912 C  C   . ALA   B 117 ? 0.368 0.028 0.323 0.026  0.029  -0.076 116 ALA   BBB C   
2913 O  O   . ALA   B 117 ? 0.415 0.012 0.357 0.009  0.028  -0.042 116 ALA   BBB O   
2914 C  CB  . ALA   B 117 ? 0.321 0.130 0.417 0.046  -0.028 -0.080 116 ALA   BBB CB  
2915 N  N   . GLU   B 118 ? 0.350 0.050 0.357 0.051  0.018  0.013  117 GLU   BBB N   
2916 C  CA  . GLU   B 118 ? 0.347 0.024 0.306 0.076  0.018  -0.006 117 GLU   BBB CA  
2917 C  C   . GLU   B 118 ? 0.451 0.008 0.324 -0.001 -0.010 -0.023 117 GLU   BBB C   
2918 O  O   . GLU   B 118 ? 0.455 0.011 0.361 0.021  0.034  -0.035 117 GLU   BBB O   
2919 C  CB  . GLU   B 118 ? 0.415 0.007 0.462 0.017  0.019  -0.001 117 GLU   BBB CB  
2920 C  CG  . GLU   B 118 ? 0.441 0.010 0.461 0.039  0.001  0.003  117 GLU   BBB CG  
2921 C  CD  . GLU   B 118 ? 0.301 0.024 0.398 0.064  0.047  0.049  117 GLU   BBB CD  
2922 O  OE1 . GLU   B 118 ? 0.340 0.014 0.388 0.042  0.004  0.030  117 GLU   BBB OE1 
2923 O  OE2 . GLU   B 118 ? 0.471 0.007 0.404 0.000  0.045  0.015  117 GLU   BBB OE2 
2924 N  N   . LEU   B 119 ? 0.383 0.013 0.333 0.043  0.033  -0.018 118 LEU   BBB N   
2925 C  CA  . LEU   B 119 ? 0.367 0.014 0.290 0.012  0.012  0.004  118 LEU   BBB CA  
2926 C  C   . LEU   B 119 ? 0.412 0.020 0.333 0.013  -0.034 -0.066 118 LEU   BBB C   
2927 O  O   . LEU   B 119 ? 0.422 0.006 0.347 0.001  -0.040 -0.005 118 LEU   BBB O   
2928 C  CB  . LEU   B 119 ? 0.340 0.028 0.325 0.014  -0.004 -0.025 118 LEU   BBB CB  
2929 C  CG  . LEU   B 119 ? 0.358 0.037 0.294 0.020  0.038  -0.020 118 LEU   BBB CG  
2930 C  CD1 . LEU   B 119 ? 0.363 0.020 0.297 -0.011 0.020  -0.063 118 LEU   BBB CD1 
2931 C  CD2 . LEU   B 119 ? 0.391 0.011 0.374 0.026  0.020  -0.030 118 LEU   BBB CD2 
2932 N  N   . HIS   B 120 ? 0.430 0.007 0.407 -0.007 -0.008 -0.011 119 HIS   BBB N   
2933 C  CA  . HIS   B 120 ? 0.386 0.014 0.274 -0.048 0.012  0.016  119 HIS   BBB CA  
2934 C  C   . HIS   B 120 ? 0.345 0.018 0.304 -0.023 -0.026 0.056  119 HIS   BBB C   
2935 O  O   . HIS   B 120 ? 0.409 0.007 0.311 -0.010 -0.015 0.013  119 HIS   BBB O   
2936 C  CB  . HIS   B 120 ? 0.333 0.053 0.266 -0.043 0.015  0.003  119 HIS   BBB CB  
2937 C  CG  . HIS   B 120 ? 0.356 0.033 0.292 -0.045 0.020  -0.007 119 HIS   BBB CG  
2938 N  ND1 . HIS   B 120 ? 0.327 0.013 0.425 0.027  -0.047 0.039  119 HIS   BBB ND1 
2939 C  CD2 . HIS   B 120 ? 0.342 0.008 0.291 0.018  0.003  -0.013 119 HIS   BBB CD2 
2940 C  CE1 . HIS   B 120 ? 0.376 0.064 0.246 0.011  -0.033 0.073  119 HIS   BBB CE1 
2941 N  NE2 . HIS   B 120 ? 0.370 0.017 0.307 -0.050 -0.016 0.035  119 HIS   BBB NE2 
2942 N  N   . VAL   B 121 ? 0.364 0.025 0.287 0.008  -0.008 0.071  120 VAL   BBB N   
2943 C  CA  . VAL   B 121 ? 0.341 0.024 0.234 -0.072 0.000  0.025  120 VAL   BBB CA  
2944 C  C   . VAL   B 121 ? 0.371 0.026 0.332 -0.049 -0.013 -0.065 120 VAL   BBB C   
2945 O  O   . VAL   B 121 ? 0.427 0.009 0.368 0.004  -0.044 -0.032 120 VAL   BBB O   
2946 C  CB  . VAL   B 121 ? 0.414 0.012 0.271 -0.012 -0.008 0.037  120 VAL   BBB CB  
2947 C  CG1 . VAL   B 121 ? 0.444 0.029 0.413 -0.006 0.010  0.096  120 VAL   BBB CG1 
2948 C  CG2 . VAL   B 121 ? 0.442 0.011 0.350 -0.035 -0.021 -0.024 120 VAL   BBB CG2 
2949 N  N   . ALA   B 122 ? 0.431 0.007 0.343 -0.015 -0.006 -0.010 121 ALA   BBB N   
2950 C  CA  . ALA   B 122 ? 0.371 0.041 0.358 -0.017 0.027  0.015  121 ALA   BBB CA  
2951 C  C   . ALA   B 122 ? 0.346 0.067 0.285 0.020  -0.039 0.090  121 ALA   BBB C   
2952 O  O   . ALA   B 122 ? 0.369 0.013 0.357 0.018  0.016  0.045  121 ALA   BBB O   
2953 C  CB  . ALA   B 122 ? 0.366 0.139 0.338 0.019  -0.018 0.012  121 ALA   BBB CB  
2954 N  N   . HIS   B 123 ? 0.355 0.014 0.367 0.051  -0.029 -0.019 122 HIS   BBB N   
2955 C  CA  . HIS   B 123 ? 0.380 0.049 0.320 -0.003 -0.033 0.067  122 HIS   BBB CA  
2956 C  C   . HIS   B 123 ? 0.384 0.012 0.367 -0.035 0.016  0.026  122 HIS   BBB C   
2957 O  O   . HIS   B 123 ? 0.386 0.017 0.410 0.025  0.012  0.040  122 HIS   BBB O   
2958 C  CB  . HIS   B 123 ? 0.410 0.012 0.304 -0.006 0.021  0.040  122 HIS   BBB CB  
2959 C  CG  . HIS   B 123 ? 0.370 0.013 0.351 0.027  0.005  -0.041 122 HIS   BBB CG  
2960 N  ND1 . HIS   B 123 ? 0.362 0.083 0.364 -0.033 0.021  0.014  122 HIS   BBB ND1 
2961 C  CD2 . HIS   B 123 ? 0.402 0.007 0.391 0.003  0.029  -0.008 122 HIS   BBB CD2 
2962 C  CE1 . HIS   B 123 ? 0.330 0.047 0.335 -0.096 0.038  0.051  122 HIS   BBB CE1 
2963 N  NE2 . HIS   B 123 ? 0.353 0.011 0.330 -0.038 -0.007 0.018  122 HIS   BBB NE2 
2964 N  N   . TRP   B 124 ? 0.388 0.052 0.389 -0.059 0.019  0.040  123 TRP   BBB N   
2965 C  CA  . TRP   B 124 ? 0.391 0.094 0.385 -0.012 0.016  0.077  123 TRP   BBB CA  
2966 C  C   . TRP   B 124 ? 0.372 0.150 0.411 0.031  -0.004 -0.004 123 TRP   BBB C   
2967 O  O   . TRP   B 124 ? 0.362 0.122 0.422 -0.034 0.002  -0.021 123 TRP   BBB O   
2968 C  CB  . TRP   B 124 ? 0.363 0.060 0.380 0.014  0.049  0.073  123 TRP   BBB CB  
2969 C  CG  . TRP   B 124 ? 0.409 0.060 0.365 -0.012 0.036  0.067  123 TRP   BBB CG  
2970 C  CD1 . TRP   B 124 ? 0.424 0.136 0.355 -0.029 0.039  0.081  123 TRP   BBB CD1 
2971 C  CD2 . TRP   B 124 ? 0.412 0.127 0.392 -0.025 0.009  0.063  123 TRP   BBB CD2 
2972 N  NE1 . TRP   B 124 ? 0.504 0.061 0.393 -0.000 0.028  0.067  123 TRP   BBB NE1 
2973 C  CE2 . TRP   B 124 ? 0.427 0.059 0.411 0.030  0.002  0.018  123 TRP   BBB CE2 
2974 C  CE3 . TRP   B 124 ? 0.428 0.140 0.409 -0.024 -0.014 0.004  123 TRP   BBB CE3 
2975 C  CZ2 . TRP   B 124 ? 0.368 0.283 0.394 -0.001 0.056  0.019  123 TRP   BBB CZ2 
2976 C  CZ3 . TRP   B 124 ? 0.512 0.316 0.425 -0.041 0.073  0.100  123 TRP   BBB CZ3 
2977 C  CH2 . TRP   B 124 ? 0.392 0.247 0.421 -0.096 0.010  0.060  123 TRP   BBB CH2 
2978 N  N   . ASN   B 125 ? 0.334 0.092 0.415 -0.012 0.037  0.031  124 ASN   BBB N   
2979 C  CA  . ASN   B 125 ? 0.333 0.164 0.454 0.021  0.003  0.022  124 ASN   BBB CA  
2980 C  C   . ASN   B 125 ? 0.364 0.223 0.456 0.021  0.011  0.054  124 ASN   BBB C   
2981 O  O   . ASN   B 125 ? 0.485 0.014 0.512 -0.040 0.070  0.042  124 ASN   BBB O   
2982 C  CB  . ASN   B 125 ? 0.350 0.188 0.413 0.032  0.016  0.037  124 ASN   BBB CB  
2983 C  CG  . ASN   B 125 ? 0.436 0.240 0.454 -0.033 -0.028 0.016  124 ASN   BBB CG  
2984 O  OD1 . ASN   B 125 ? 0.447 0.338 0.510 0.056  -0.009 0.059  124 ASN   BBB OD1 
2985 N  ND2 . ASN   B 125 ? 0.374 0.219 0.410 -0.025 -0.049 0.098  124 ASN   BBB ND2 
2986 N  N   . SER   B 126 ? 0.365 0.149 0.551 -0.105 -0.007 0.015  125 SER   BBB N   
2987 C  CA  . SER   B 126 ? 0.412 0.306 0.575 -0.058 0.055  0.107  125 SER   BBB CA  
2988 C  C   . SER   B 126 ? 0.424 0.315 0.508 -0.049 0.068  0.060  125 SER   BBB C   
2989 O  O   . SER   B 126 ? 0.471 0.228 0.663 -0.050 0.070  0.119  125 SER   BBB O   
2990 C  CB  . SER   B 126 ? 0.464 0.205 0.478 -0.093 0.063  0.080  125 SER   BBB CB  
2991 O  OG  . SER   B 126 ? 0.576 0.052 0.496 -0.124 0.010  0.092  125 SER   BBB OG  
2992 N  N   . ALA   B 127 ? 0.495 0.353 0.495 -0.013 0.004  0.004  126 ALA   BBB N   
2993 C  CA  . ALA   B 127 ? 0.518 0.411 0.576 -0.073 -0.014 0.019  126 ALA   BBB CA  
2994 C  C   . ALA   B 127 ? 0.398 0.495 0.557 -0.085 -0.064 0.037  126 ALA   BBB C   
2995 O  O   . ALA   B 127 ? 0.473 0.397 0.784 -0.164 -0.098 0.180  126 ALA   BBB O   
2996 C  CB  . ALA   B 127 ? 0.636 0.249 0.575 0.032  -0.079 -0.020 126 ALA   BBB CB  
2997 N  N   . LYS   B 128 ? 0.544 0.410 0.668 -0.136 0.042  0.098  127 LYS   BBB N   
2998 C  CA  . LYS   B 128 ? 0.589 0.573 0.608 -0.044 0.067  0.156  127 LYS   BBB CA  
2999 C  C   . LYS   B 128 ? 0.383 0.410 0.606 -0.073 0.074  0.136  127 LYS   BBB C   
3000 O  O   . LYS   B 128 ? 0.393 0.367 0.580 -0.022 0.042  0.151  127 LYS   BBB O   
3001 C  CB  . LYS   B 128 ? 0.504 0.662 0.664 -0.085 0.134  0.222  127 LYS   BBB CB  
3002 C  CG  . LYS   B 128 ? 0.593 0.579 0.696 0.091  -0.005 0.274  127 LYS   BBB CG  
3003 C  CD  . LYS   B 128 ? 0.530 0.730 0.904 0.182  0.094  0.178  127 LYS   BBB CD  
3004 C  CE  . LYS   B 128 ? 0.802 0.768 0.767 -0.089 -0.033 0.294  127 LYS   BBB CE  
3005 N  NZ  . LYS   B 128 ? 0.619 1.008 0.921 0.113  -0.016 0.391  127 LYS   BBB NZ  
3006 N  N   . TYR   B 129 ? 0.408 0.325 0.527 -0.001 0.061  0.177  128 TYR   BBB N   
3007 C  CA  . TYR   B 129 ? 0.520 0.416 0.519 -0.009 0.062  0.209  128 TYR   BBB CA  
3008 C  C   . TYR   B 129 ? 0.511 0.319 0.572 0.015  0.065  0.150  128 TYR   BBB C   
3009 O  O   . TYR   B 129 ? 0.430 0.318 0.615 -0.028 0.059  0.122  128 TYR   BBB O   
3010 C  CB  . TYR   B 129 ? 0.422 0.440 0.567 0.001  0.048  0.179  128 TYR   BBB CB  
3011 C  CG  . TYR   B 129 ? 0.433 0.330 0.591 0.066  0.138  0.153  128 TYR   BBB CG  
3012 C  CD1 . TYR   B 129 ? 0.465 0.551 0.629 0.143  0.126  0.279  128 TYR   BBB CD1 
3013 C  CD2 . TYR   B 129 ? 0.439 0.347 0.623 0.050  0.123  0.177  128 TYR   BBB CD2 
3014 C  CE1 . TYR   B 129 ? 0.371 0.547 0.674 0.053  0.061  0.333  128 TYR   BBB CE1 
3015 C  CE2 . TYR   B 129 ? 0.390 0.578 0.597 0.156  0.060  0.178  128 TYR   BBB CE2 
3016 C  CZ  . TYR   B 129 ? 0.337 0.651 0.588 0.134  0.043  0.302  128 TYR   BBB CZ  
3017 O  OH  . TYR   B 129 ? 0.396 0.379 0.706 0.067  -0.026 0.227  128 TYR   BBB OH  
3018 N  N   . SER   B 130 ? 0.491 0.338 0.526 -0.112 0.083  0.186  129 SER   BBB N   
3019 C  CA  . SER   B 130 ? 0.552 0.365 0.603 -0.088 0.087  0.217  129 SER   BBB CA  
3020 C  C   . SER   B 130 ? 0.573 0.168 0.642 -0.054 0.049  0.115  129 SER   BBB C   
3021 O  O   . SER   B 130 ? 0.511 0.196 0.628 -0.050 0.117  0.137  129 SER   BBB O   
3022 C  CB  . SER   B 130 ? 0.395 0.608 0.742 0.037  0.121  0.071  129 SER   BBB CB  
3023 O  OG  . SER   B 130 ? 0.471 0.529 0.723 -0.039 0.081  0.163  129 SER   BBB OG  
3024 N  N   . SER   B 131 ? 0.493 0.217 0.505 -0.061 0.050  0.019  130 SER   BBB N   
3025 C  CA  . SER   B 131 ? 0.541 0.039 0.518 -0.033 0.003  -0.004 130 SER   BBB CA  
3026 C  C   . SER   B 131 ? 0.393 0.220 0.344 -0.020 0.021  0.024  130 SER   BBB C   
3027 O  O   . SER   B 131 ? 0.474 0.327 0.379 0.048  0.037  0.049  130 SER   BBB O   
3028 C  CB  . SER   B 131 ? 0.503 0.032 0.513 0.034  0.084  0.042  130 SER   BBB CB  
3029 O  OG  . SER   B 131 ? 0.671 0.055 0.495 0.066  0.103  -0.017 130 SER   BBB OG  
3030 N  N   . LEU   B 132 ? 0.393 0.212 0.409 0.020  0.052  0.033  131 LEU   BBB N   
3031 C  CA  . LEU   B 132 ? 0.457 0.143 0.348 0.008  0.070  -0.011 131 LEU   BBB CA  
3032 C  C   . LEU   B 132 ? 0.437 0.174 0.319 0.108  0.074  0.064  131 LEU   BBB C   
3033 O  O   . LEU   B 132 ? 0.535 0.063 0.507 0.026  0.107  0.063  131 LEU   BBB O   
3034 C  CB  . LEU   B 132 ? 0.535 0.120 0.405 0.046  0.022  0.009  131 LEU   BBB CB  
3035 C  CG  . LEU   B 132 ? 0.441 0.250 0.382 0.028  0.062  -0.045 131 LEU   BBB CG  
3036 C  CD1 . LEU   B 132 ? 0.430 0.101 0.379 0.044  0.048  -0.055 131 LEU   BBB CD1 
3037 C  CD2 . LEU   B 132 ? 0.449 0.338 0.405 -0.031 0.017  0.022  131 LEU   BBB CD2 
3038 N  N   . ALA   B 133 ? 0.548 0.130 0.351 0.049  0.110  0.006  132 ALA   BBB N   
3039 C  CA  . ALA   B 133 ? 0.569 0.159 0.446 0.072  0.133  -0.027 132 ALA   BBB CA  
3040 C  C   . ALA   B 133 ? 0.581 0.006 0.489 -0.007 0.096  -0.001 132 ALA   BBB C   
3041 O  O   . ALA   B 133 ? 0.657 0.034 0.471 0.124  0.080  -0.028 132 ALA   BBB O   
3042 C  CB  . ALA   B 133 ? 0.696 0.094 0.462 0.054  0.046  0.016  132 ALA   BBB CB  
3043 N  N   . GLU   B 134 ? 0.464 0.223 0.441 0.007  0.102  -0.037 133 GLU   BBB N   
3044 C  CA  . GLU   B 134 ? 0.512 0.272 0.440 0.048  0.077  0.001  133 GLU   BBB CA  
3045 C  C   . GLU   B 134 ? 0.530 0.107 0.545 0.052  0.141  0.056  133 GLU   BBB C   
3046 O  O   . GLU   B 134 ? 0.588 0.151 0.594 0.111  0.081  0.042  133 GLU   BBB O   
3047 C  CB  . GLU   B 134 ? 0.540 0.282 0.451 0.022  0.096  0.075  133 GLU   BBB CB  
3048 C  CG  . GLU   B 134 ? 0.591 0.388 0.458 0.067  0.051  0.057  133 GLU   BBB CG  
3049 C  CD  . GLU   B 134 ? 0.484 0.478 0.543 0.086  0.024  0.118  133 GLU   BBB CD  
3050 O  OE1 . GLU   B 134 ? 0.516 0.185 0.691 0.037  0.030  0.084  133 GLU   BBB OE1 
3051 O  OE2 . GLU   B 134 ? 0.496 0.491 0.554 0.093  0.086  0.146  133 GLU   BBB OE2 
3052 N  N   . ALA   B 135 ? 0.454 0.184 0.450 0.007  0.110  0.067  134 ALA   BBB N   
3053 C  CA  . ALA   B 135 ? 0.468 0.215 0.435 0.045  0.068  0.032  134 ALA   BBB CA  
3054 C  C   . ALA   B 135 ? 0.391 0.212 0.414 0.102  0.006  0.060  134 ALA   BBB C   
3055 O  O   . ALA   B 135 ? 0.526 0.075 0.544 0.046  0.092  0.113  134 ALA   BBB O   
3056 C  CB  . ALA   B 135 ? 0.443 0.287 0.427 0.063  0.028  -0.002 134 ALA   BBB CB  
3057 N  N   . ALA   B 136 ? 0.437 0.081 0.404 0.055  0.020  0.036  135 ALA   BBB N   
3058 C  CA  . ALA   B 136 ? 0.401 0.118 0.513 0.059  0.013  0.041  135 ALA   BBB CA  
3059 C  C   . ALA   B 136 ? 0.434 0.152 0.460 0.085  0.061  0.094  135 ALA   BBB C   
3060 O  O   . ALA   B 136 ? 0.506 0.149 0.429 0.014  0.091  0.026  135 ALA   BBB O   
3061 C  CB  . ALA   B 136 ? 0.525 0.096 0.544 0.058  -0.012 0.170  135 ALA   BBB CB  
3062 N  N   . SER   B 137 ? 0.420 0.076 0.544 0.049  0.071  0.078  136 SER   BBB N   
3063 C  CA  . SER   B 137 ? 0.491 0.155 0.525 0.141  0.126  0.168  136 SER   BBB CA  
3064 C  C   . SER   B 137 ? 0.605 0.138 0.560 0.250  0.051  0.097  136 SER   BBB C   
3065 O  O   . SER   B 137 ? 0.608 0.029 0.668 0.098  0.068  0.077  136 SER   BBB O   
3066 C  CB  . SER   B 137 ? 0.579 0.025 0.568 0.064  0.112  -0.065 136 SER   BBB CB  
3067 O  OG  . SER   B 137 ? 0.586 0.256 0.627 0.005  0.202  0.105  136 SER   BBB OG  
3068 N  N   . LYS   B 138 ? 0.479 0.124 0.624 -0.006 0.097  0.077  137 LYS   BBB N   
3069 C  CA  . LYS   B 138 ? 0.480 0.222 0.588 0.060  0.062  0.179  137 LYS   BBB CA  
3070 C  C   . LYS   B 138 ? 0.379 0.199 0.551 0.106  0.055  0.192  137 LYS   BBB C   
3071 O  O   . LYS   B 138 ? 0.384 0.195 0.528 0.072  0.045  0.070  137 LYS   BBB O   
3072 C  CB  . LYS   B 138 ? 0.405 0.286 0.569 -0.011 0.015  0.159  137 LYS   BBB CB  
3073 C  CG  . LYS   B 138 ? 0.725 0.464 0.635 -0.039 0.116  0.228  137 LYS   BBB CG  
3074 C  CD  . LYS   B 138 ? 0.762 0.640 0.685 0.012  0.118  0.225  137 LYS   BBB CD  
3075 C  CE  . LYS   B 138 ? 0.968 0.756 0.786 -0.178 0.193  0.132  137 LYS   BBB CE  
3076 N  NZ  . LYS   B 138 ? 1.249 0.563 0.802 -0.172 0.069  -0.048 137 LYS   BBB NZ  
3077 N  N   . ALA   B 139 ? 0.452 0.104 0.487 0.118  0.009  0.077  138 ALA   BBB N   
3078 C  CA  . ALA   B 139 ? 0.432 0.251 0.546 0.083  0.054  0.062  138 ALA   BBB CA  
3079 C  C   . ALA   B 139 ? 0.361 0.168 0.477 0.022  0.046  0.080  138 ALA   BBB C   
3080 O  O   . ALA   B 139 ? 0.423 0.066 0.549 -0.005 0.058  0.048  138 ALA   BBB O   
3081 C  CB  . ALA   B 139 ? 0.508 0.192 0.686 0.095  -0.028 0.108  138 ALA   BBB CB  
3082 N  N   . ASP   B 140 ? 0.404 0.178 0.619 0.012  0.006  0.105  139 ASP   BBB N   
3083 C  CA  . ASP   B 140 ? 0.422 0.194 0.469 0.056  -0.010 0.111  139 ASP   BBB CA  
3084 C  C   . ASP   B 140 ? 0.419 0.250 0.419 0.010  -0.052 0.125  139 ASP   BBB C   
3085 O  O   . ASP   B 140 ? 0.423 0.262 0.533 -0.019 0.017  0.049  139 ASP   BBB O   
3086 C  CB  . ASP   B 140 ? 0.430 0.237 0.555 0.095  -0.022 0.090  139 ASP   BBB CB  
3087 C  CG  . ASP   B 140 ? 0.391 0.350 0.595 -0.003 -0.035 0.021  139 ASP   BBB CG  
3088 O  OD1 . ASP   B 140 ? 0.484 0.320 0.615 0.017  0.010  0.115  139 ASP   BBB OD1 
3089 O  OD2 . ASP   B 140 ? 0.496 0.281 0.665 -0.022 -0.085 -0.093 139 ASP   BBB OD2 
3090 N  N   . GLY   B 141 ? 0.382 0.202 0.429 0.003  0.007  0.111  140 GLY   BBB N   
3091 C  CA  . GLY   B 141 ? 0.375 0.193 0.470 -0.008 -0.001 0.132  140 GLY   BBB CA  
3092 C  C   . GLY   B 141 ? 0.393 0.212 0.377 0.028  0.026  0.131  140 GLY   BBB C   
3093 O  O   . GLY   B 141 ? 0.405 0.182 0.405 0.015  0.006  0.105  140 GLY   BBB O   
3094 N  N   . LEU   B 142 ? 0.370 0.053 0.421 0.017  0.028  -0.009 141 LEU   BBB N   
3095 C  CA  . LEU   B 142 ? 0.354 0.018 0.388 -0.048 0.033  0.041  141 LEU   BBB CA  
3096 C  C   . LEU   B 142 ? 0.305 0.184 0.399 0.014  0.015  0.059  141 LEU   BBB C   
3097 O  O   . LEU   B 142 ? 0.374 0.096 0.404 0.018  -0.017 0.039  141 LEU   BBB O   
3098 C  CB  . LEU   B 142 ? 0.367 0.165 0.369 0.026  0.003  -0.031 141 LEU   BBB CB  
3099 C  CG  . LEU   B 142 ? 0.397 0.016 0.367 0.032  -0.009 0.051  141 LEU   BBB CG  
3100 C  CD1 . LEU   B 142 ? 0.438 0.142 0.363 0.017  -0.059 0.035  141 LEU   BBB CD1 
3101 C  CD2 . LEU   B 142 ? 0.388 0.040 0.437 0.066  0.017  0.101  141 LEU   BBB CD2 
3102 N  N   . ALA   B 143 ? 0.384 0.006 0.359 -0.001 0.030  0.007  142 ALA   BBB N   
3103 C  CA  . ALA   B 143 ? 0.367 0.007 0.334 -0.000 0.022  -0.009 142 ALA   BBB CA  
3104 C  C   . ALA   B 143 ? 0.391 0.122 0.262 -0.023 0.003  0.029  142 ALA   BBB C   
3105 O  O   . ALA   B 143 ? 0.369 0.055 0.381 -0.020 -0.001 0.068  142 ALA   BBB O   
3106 C  CB  . ALA   B 143 ? 0.413 0.008 0.377 0.004  -0.035 -0.005 142 ALA   BBB CB  
3107 N  N   . VAL   B 144 ? 0.386 0.009 0.356 0.012  0.008  0.029  143 VAL   BBB N   
3108 C  CA  . VAL   B 144 ? 0.341 0.008 0.377 0.010  0.010  -0.020 143 VAL   BBB CA  
3109 C  C   . VAL   B 144 ? 0.347 0.088 0.350 0.141  -0.010 0.010  143 VAL   BBB C   
3110 O  O   . VAL   B 144 ? 0.415 0.012 0.341 0.048  -0.042 -0.011 143 VAL   BBB O   
3111 C  CB  . VAL   B 144 ? 0.417 0.007 0.333 -0.019 0.007  0.003  143 VAL   BBB CB  
3112 C  CG1 . VAL   B 144 ? 0.466 0.009 0.438 -0.032 -0.027 -0.009 143 VAL   BBB CG1 
3113 C  CG2 . VAL   B 144 ? 0.405 0.053 0.374 -0.035 -0.000 0.029  143 VAL   BBB CG2 
3114 N  N   . ILE   B 145 ? 0.492 0.006 0.425 0.008  0.014  0.002  144 ILE   BBB N   
3115 C  CA  . ILE   B 145 ? 0.425 0.020 0.370 0.060  -0.002 0.042  144 ILE   BBB CA  
3116 C  C   . ILE   B 145 ? 0.408 0.030 0.347 0.066  -0.001 0.066  144 ILE   BBB C   
3117 O  O   . ILE   B 145 ? 0.395 0.009 0.348 -0.007 -0.002 0.032  144 ILE   BBB O   
3118 C  CB  . ILE   B 145 ? 0.364 0.031 0.346 0.092  -0.010 -0.019 144 ILE   BBB CB  
3119 C  CG1 . ILE   B 145 ? 0.388 0.017 0.327 0.055  0.019  0.029  144 ILE   BBB CG1 
3120 C  CG2 . ILE   B 145 ? 0.390 0.069 0.328 0.040  -0.032 -0.020 144 ILE   BBB CG2 
3121 C  CD1 . ILE   B 145 ? 0.460 0.022 0.380 0.061  0.014  0.054  144 ILE   BBB CD1 
3122 N  N   . GLY   B 146 ? 0.398 0.025 0.408 0.056  -0.023 0.062  145 GLY   BBB N   
3123 C  CA  . GLY   B 146 ? 0.381 0.045 0.466 0.064  -0.027 0.108  145 GLY   BBB CA  
3124 C  C   . GLY   B 146 ? 0.467 0.010 0.405 -0.039 -0.056 0.018  145 GLY   BBB C   
3125 O  O   . GLY   B 146 ? 0.397 0.007 0.381 -0.008 -0.019 0.010  145 GLY   BBB O   
3126 N  N   . VAL   B 147 ? 0.424 0.009 0.343 -0.013 -0.001 0.030  146 VAL   BBB N   
3127 C  CA  . VAL   B 147 ? 0.334 0.062 0.381 0.093  -0.040 0.093  146 VAL   BBB CA  
3128 C  C   . VAL   B 147 ? 0.354 0.070 0.272 0.066  -0.031 0.057  146 VAL   BBB C   
3129 O  O   . VAL   B 147 ? 0.390 0.017 0.313 0.042  -0.032 0.038  146 VAL   BBB O   
3130 C  CB  . VAL   B 147 ? 0.384 0.050 0.340 0.045  -0.034 0.109  146 VAL   BBB CB  
3131 C  CG1 . VAL   B 147 ? 0.449 0.009 0.429 -0.004 -0.028 0.036  146 VAL   BBB CG1 
3132 C  CG2 . VAL   B 147 ? 0.327 0.045 0.404 0.074  0.001  0.004  146 VAL   BBB CG2 
3133 N  N   . LEU   B 148 ? 0.369 0.027 0.317 -0.007 -0.011 0.035  147 LEU   BBB N   
3134 C  CA  . LEU   B 148 ? 0.348 0.106 0.322 -0.014 0.012  0.011  147 LEU   BBB CA  
3135 C  C   . LEU   B 148 ? 0.382 0.156 0.310 0.020  -0.017 -0.017 147 LEU   BBB C   
3136 O  O   . LEU   B 148 ? 0.403 0.084 0.318 -0.019 0.009  0.009  147 LEU   BBB O   
3137 C  CB  . LEU   B 148 ? 0.372 0.119 0.349 -0.034 -0.011 0.053  147 LEU   BBB CB  
3138 C  CG  . LEU   B 148 ? 0.381 0.170 0.413 -0.012 0.004  -0.015 147 LEU   BBB CG  
3139 C  CD1 . LEU   B 148 ? 0.471 0.197 0.487 0.049  0.003  0.029  147 LEU   BBB CD1 
3140 C  CD2 . LEU   B 148 ? 0.447 0.015 0.414 -0.051 0.019  0.034  147 LEU   BBB CD2 
3141 N  N   . MET   B 149 ? 0.396 0.047 0.367 0.001  -0.012 -0.014 148 MET   BBB N   
3142 C  CA  . MET   B 149 ? 0.389 0.045 0.383 -0.015 -0.032 -0.042 148 MET   BBB CA  
3143 C  C   . MET   B 149 ? 0.342 0.143 0.333 -0.024 -0.018 -0.059 148 MET   BBB C   
3144 O  O   . MET   B 149 ? 0.387 0.101 0.419 -0.047 0.030  -0.063 148 MET   BBB O   
3145 C  CB  . MET   B 149 ? 0.409 0.008 0.411 0.025  0.021  0.003  148 MET   BBB CB  
3146 C  CG  . MET   B 149 ? 0.348 0.019 0.375 0.022  0.010  -0.063 148 MET   BBB CG  
3147 S  SD  . MET   B 149 ? 0.418 0.037 0.364 0.012  -0.013 -0.012 148 MET   BBB SD  
3148 C  CE  . MET   B 149 ? 0.405 0.187 0.426 0.020  0.028  0.021  148 MET   BBB CE  
3149 N  N   . LYS   B 150 ? 0.357 0.128 0.363 0.032  0.040  0.050  149 LYS   BBB N   
3150 C  CA  . LYS   B 150 ? 0.353 0.082 0.399 -0.015 0.036  -0.050 149 LYS   BBB CA  
3151 C  C   . LYS   B 150 ? 0.353 0.118 0.446 0.006  0.004  -0.000 149 LYS   BBB C   
3152 O  O   . LYS   B 150 ? 0.373 0.118 0.409 0.049  0.010  0.037  149 LYS   BBB O   
3153 C  CB  . LYS   B 150 ? 0.439 0.218 0.365 0.037  -0.004 0.017  149 LYS   BBB CB  
3154 C  CG  . LYS   B 150 ? 0.596 0.251 0.449 -0.031 0.077  -0.010 149 LYS   BBB CG  
3155 C  CD  . LYS   B 150 ? 0.759 0.231 0.424 -0.087 0.048  0.088  149 LYS   BBB CD  
3156 C  CE  . LYS   B 150 ? 0.791 0.600 0.524 -0.066 0.157  0.122  149 LYS   BBB CE  
3157 N  NZ  . LYS   B 150 ? 0.820 0.909 0.636 -0.040 -0.004 0.076  149 LYS   BBB NZ  
3158 N  N   . VAL   B 151 ? 0.407 0.126 0.404 0.011  -0.000 -0.036 150 VAL   BBB N   
3159 C  CA  . VAL   B 151 ? 0.412 0.163 0.343 -0.060 0.000  0.020  150 VAL   BBB CA  
3160 C  C   . VAL   B 151 ? 0.408 0.262 0.369 0.014  -0.006 0.020  150 VAL   BBB C   
3161 O  O   . VAL   B 151 ? 0.409 0.220 0.382 0.014  0.032  0.008  150 VAL   BBB O   
3162 C  CB  . VAL   B 151 ? 0.438 0.227 0.418 -0.063 -0.023 -0.025 150 VAL   BBB CB  
3163 C  CG1 . VAL   B 151 ? 0.408 0.281 0.482 -0.082 0.013  0.036  150 VAL   BBB CG1 
3164 C  CG2 . VAL   B 151 ? 0.536 0.124 0.430 -0.070 -0.060 -0.004 150 VAL   BBB CG2 
3165 N  N   . GLY   B 152 ? 0.419 0.247 0.391 0.006  0.020  -0.017 151 GLY   BBB N   
3166 C  CA  . GLY   B 152 ? 0.415 0.231 0.367 0.048  0.011  0.012  151 GLY   BBB CA  
3167 C  C   . GLY   B 152 ? 0.391 0.213 0.380 0.022  -0.036 0.019  151 GLY   BBB C   
3168 O  O   . GLY   B 152 ? 0.433 0.121 0.433 0.089  -0.025 0.040  151 GLY   BBB O   
3169 N  N   . GLU   B 153 ? 0.448 0.227 0.347 0.075  0.018  -0.025 152 GLU   BBB N   
3170 C  CA  . GLU   B 153 ? 0.449 0.329 0.385 0.101  0.002  0.074  152 GLU   BBB CA  
3171 C  C   . GLU   B 153 ? 0.415 0.271 0.406 0.082  -0.008 0.075  152 GLU   BBB C   
3172 O  O   . GLU   B 153 ? 0.421 0.221 0.415 0.075  -0.017 0.008  152 GLU   BBB O   
3173 C  CB  . GLU   B 153 ? 0.608 0.316 0.498 0.093  0.006  -0.003 152 GLU   BBB CB  
3174 C  CG  . GLU   B 153 ? 0.761 0.623 0.576 0.108  0.053  0.025  152 GLU   BBB CG  
3175 C  CD  . GLU   B 153 ? 0.869 0.819 0.709 0.255  0.187  -0.091 152 GLU   BBB CD  
3176 O  OE1 . GLU   B 153 ? 0.751 1.164 0.829 -0.011 0.276  0.042  152 GLU   BBB OE1 
3177 O  OE2 . GLU   B 153 ? 1.130 1.094 0.726 0.361  -0.067 -0.382 152 GLU   BBB OE2 
3178 N  N   . ALA   B 154 ? 0.523 0.028 0.406 0.101  -0.022 -0.032 153 ALA   BBB N   
3179 C  CA  . ALA   B 154 ? 0.438 0.245 0.411 0.084  -0.016 -0.021 153 ALA   BBB CA  
3180 C  C   . ALA   B 154 ? 0.403 0.202 0.351 0.095  0.011  -0.035 153 ALA   BBB C   
3181 O  O   . ALA   B 154 ? 0.477 0.274 0.379 0.095  0.064  -0.063 153 ALA   BBB O   
3182 C  CB  . ALA   B 154 ? 0.406 0.234 0.442 0.105  0.029  0.018  153 ALA   BBB CB  
3183 N  N   . ASN   B 155 ? 0.388 0.052 0.380 0.081  0.001  -0.006 154 ASN   BBB N   
3184 C  CA  . ASN   B 155 ? 0.363 0.243 0.380 0.053  -0.005 0.039  154 ASN   BBB CA  
3185 C  C   . ASN   B 155 ? 0.396 0.157 0.341 0.103  0.012  -0.005 154 ASN   BBB C   
3186 O  O   . ASN   B 155 ? 0.462 0.121 0.363 0.077  0.007  0.014  154 ASN   BBB O   
3187 C  CB  . ASN   B 155 ? 0.408 0.169 0.477 0.073  0.006  0.011  154 ASN   BBB CB  
3188 C  CG  . ASN   B 155 ? 0.397 0.066 0.464 0.084  0.003  -0.006 154 ASN   BBB CG  
3189 O  OD1 . ASN   B 155 ? 0.543 0.064 0.435 0.044  -0.057 -0.039 154 ASN   BBB OD1 
3190 N  ND2 . ASN   B 155 ? 0.468 0.054 0.326 0.097  0.010  0.015  154 ASN   BBB ND2 
3191 N  N   . PRO   B 156 ? 0.455 0.155 0.338 0.044  -0.012 -0.036 155 PRO   BBB N   
3192 C  CA  . PRO   B 156 ? 0.459 0.150 0.373 0.119  -0.015 -0.021 155 PRO   BBB CA  
3193 C  C   . PRO   B 156 ? 0.469 0.117 0.321 0.109  -0.017 -0.022 155 PRO   BBB C   
3194 O  O   . PRO   B 156 ? 0.492 0.171 0.392 0.122  0.027  0.060  155 PRO   BBB O   
3195 C  CB  . PRO   B 156 ? 0.534 0.036 0.515 0.072  0.005  -0.054 155 PRO   BBB CB  
3196 C  CG  . PRO   B 156 ? 0.664 0.059 0.479 0.081  0.007  -0.141 155 PRO   BBB CG  
3197 C  CD  . PRO   B 156 ? 0.524 0.032 0.406 0.067  0.039  -0.077 155 PRO   BBB CD  
3198 N  N   . LYS   B 157 ? 0.444 0.139 0.406 0.042  -0.042 -0.049 156 LYS   BBB N   
3199 C  CA  . LYS   B 157 ? 0.454 0.023 0.408 0.033  -0.005 -0.043 156 LYS   BBB CA  
3200 C  C   . LYS   B 157 ? 0.367 0.150 0.352 0.027  -0.006 -0.027 156 LYS   BBB C   
3201 O  O   . LYS   B 157 ? 0.491 0.023 0.410 0.040  0.017  0.010  156 LYS   BBB O   
3202 C  CB  . LYS   B 157 ? 0.512 0.130 0.446 0.018  -0.035 -0.063 156 LYS   BBB CB  
3203 C  CG  . LYS   B 157 ? 0.565 0.442 0.500 -0.029 0.044  -0.165 156 LYS   BBB CG  
3204 C  CD  . LYS   B 157 ? 0.652 0.415 0.696 -0.043 0.060  -0.210 156 LYS   BBB CD  
3205 C  CE  . LYS   B 157 ? 0.685 0.692 0.692 -0.067 0.012  -0.175 156 LYS   BBB CE  
3206 N  NZ  . LYS   B 157 ? 0.718 0.573 0.574 -0.041 0.073  -0.282 156 LYS   BBB NZ  
3207 N  N   . LEU   B 158 ? 0.406 0.129 0.383 0.021  -0.002 0.035  157 LEU   BBB N   
3208 C  CA  . LEU   B 158 ? 0.429 0.069 0.412 0.007  0.011  0.003  157 LEU   BBB CA  
3209 C  C   . LEU   B 158 ? 0.454 0.185 0.413 0.153  -0.035 -0.118 157 LEU   BBB C   
3210 O  O   . LEU   B 158 ? 0.523 0.048 0.433 0.006  0.044  -0.071 157 LEU   BBB O   
3211 C  CB  . LEU   B 158 ? 0.428 0.026 0.465 0.059  0.033  -0.067 157 LEU   BBB CB  
3212 C  CG  . LEU   B 158 ? 0.406 0.199 0.356 -0.028 0.026  0.027  157 LEU   BBB CG  
3213 C  CD1 . LEU   B 158 ? 0.458 0.162 0.434 -0.023 -0.020 -0.060 157 LEU   BBB CD1 
3214 C  CD2 . LEU   B 158 ? 0.449 0.159 0.489 -0.019 0.039  0.064  157 LEU   BBB CD2 
3215 N  N   . GLN   B 159 ? 0.444 0.191 0.417 0.160  -0.057 -0.111 158 GLN   BBB N   
3216 C  CA  . GLN   B 159 ? 0.423 0.291 0.381 0.103  -0.022 -0.053 158 GLN   BBB CA  
3217 C  C   . GLN   B 159 ? 0.446 0.299 0.380 0.133  0.015  -0.111 158 GLN   BBB C   
3218 O  O   . GLN   B 159 ? 0.518 0.393 0.368 0.128  -0.014 -0.061 158 GLN   BBB O   
3219 C  CB  . GLN   B 159 ? 0.571 0.271 0.410 0.169  -0.011 -0.061 158 GLN   BBB CB  
3220 C  CG  . GLN   B 159 ? 0.531 0.651 0.432 0.108  -0.124 0.029  158 GLN   BBB CG  
3221 C  CD  . GLN   B 159 ? 0.523 1.066 0.888 0.059  -0.187 0.004  158 GLN   BBB CD  
3222 O  OE1 . GLN   B 159 ? 0.447 1.026 1.061 0.186  -0.003 0.205  158 GLN   BBB OE1 
3223 N  NE2 . GLN   B 159 ? 0.722 0.960 1.232 0.546  0.155  0.006  158 GLN   BBB NE2 
3224 N  N   . LYS   B 160 ? 0.466 0.234 0.344 0.121  -0.032 -0.010 159 LYS   BBB N   
3225 C  CA  . LYS   B 160 ? 0.471 0.241 0.362 0.156  -0.015 0.002  159 LYS   BBB CA  
3226 C  C   . LYS   B 160 ? 0.547 0.166 0.357 0.160  -0.109 0.038  159 LYS   BBB C   
3227 O  O   . LYS   B 160 ? 0.504 0.191 0.371 0.064  -0.073 0.050  159 LYS   BBB O   
3228 C  CB  . LYS   B 160 ? 0.566 0.339 0.438 0.048  -0.071 0.022  159 LYS   BBB CB  
3229 C  CG  . LYS   B 160 ? 0.617 0.387 0.469 0.053  -0.045 0.063  159 LYS   BBB CG  
3230 C  CD  . LYS   B 160 ? 0.756 0.394 0.499 -0.067 -0.116 0.069  159 LYS   BBB CD  
3231 C  CE  . LYS   B 160 ? 0.739 0.190 0.604 0.148  -0.092 0.113  159 LYS   BBB CE  
3232 N  NZ  . LYS   B 160 ? 0.828 0.235 0.684 0.244  -0.125 0.116  159 LYS   BBB NZ  
3233 N  N   . VAL   B 161 ? 0.502 0.017 0.361 0.053  -0.009 0.039  160 VAL   BBB N   
3234 C  CA  . VAL   B 161 ? 0.445 0.165 0.422 0.076  0.011  -0.053 160 VAL   BBB CA  
3235 C  C   . VAL   B 161 ? 0.399 0.177 0.374 0.056  0.012  0.034  160 VAL   BBB C   
3236 O  O   . VAL   B 161 ? 0.468 0.143 0.402 0.048  0.035  0.026  160 VAL   BBB O   
3237 C  CB  . VAL   B 161 ? 0.398 0.222 0.411 0.027  -0.023 -0.020 160 VAL   BBB CB  
3238 C  CG1 . VAL   B 161 ? 0.490 0.261 0.468 0.107  0.040  -0.018 160 VAL   BBB CG1 
3239 C  CG2 . VAL   B 161 ? 0.402 0.197 0.476 0.005  -0.044 0.093  160 VAL   BBB CG2 
3240 N  N   . LEU   B 162 ? 0.400 0.131 0.404 0.053  -0.003 0.060  161 LEU   BBB N   
3241 C  CA  . LEU   B 162 ? 0.423 0.307 0.364 0.013  -0.012 0.005  161 LEU   BBB CA  
3242 C  C   . LEU   B 162 ? 0.450 0.174 0.339 0.008  -0.014 -0.022 161 LEU   BBB C   
3243 O  O   . LEU   B 162 ? 0.461 0.269 0.349 -0.001 -0.027 -0.026 161 LEU   BBB O   
3244 C  CB  . LEU   B 162 ? 0.456 0.178 0.368 -0.006 0.003  0.020  161 LEU   BBB CB  
3245 C  CG  . LEU   B 162 ? 0.486 0.252 0.394 -0.003 -0.013 0.055  161 LEU   BBB CG  
3246 C  CD1 . LEU   B 162 ? 0.469 0.420 0.404 -0.063 -0.038 -0.058 161 LEU   BBB CD1 
3247 C  CD2 . LEU   B 162 ? 0.646 0.366 0.513 0.029  0.040  -0.085 161 LEU   BBB CD2 
3248 N  N   . ASP   B 163 ? 0.439 0.189 0.368 0.080  0.031  -0.023 162 ASP   BBB N   
3249 C  CA  . ASP   B 163 ? 0.405 0.106 0.429 0.081  -0.000 -0.047 162 ASP   BBB CA  
3250 C  C   . ASP   B 163 ? 0.412 0.060 0.370 0.061  -0.068 0.020  162 ASP   BBB C   
3251 O  O   . ASP   B 163 ? 0.451 0.261 0.405 0.120  -0.065 0.037  162 ASP   BBB O   
3252 C  CB  . ASP   B 163 ? 0.492 0.166 0.410 0.095  -0.028 -0.116 162 ASP   BBB CB  
3253 C  CG  . ASP   B 163 ? 0.498 0.307 0.500 0.114  0.017  -0.089 162 ASP   BBB CG  
3254 O  OD1 . ASP   B 163 ? 0.511 0.316 0.568 0.145  0.028  -0.056 162 ASP   BBB OD1 
3255 O  OD2 . ASP   B 163 ? 0.544 0.238 0.551 0.042  0.073  -0.043 162 ASP   BBB OD2 
3256 N  N   . ALA   B 164 ? 0.371 0.232 0.393 0.008  -0.007 0.015  163 ALA   BBB N   
3257 C  CA  . ALA   B 164 ? 0.423 0.110 0.388 0.044  -0.002 -0.028 163 ALA   BBB CA  
3258 C  C   . ALA   B 164 ? 0.332 0.186 0.359 0.049  0.042  -0.078 163 ALA   BBB C   
3259 O  O   . ALA   B 164 ? 0.409 0.302 0.310 0.083  -0.011 -0.045 163 ALA   BBB O   
3260 C  CB  . ALA   B 164 ? 0.424 0.049 0.408 -0.003 0.022  0.005  163 ALA   BBB CB  
3261 N  N   . LEU   B 165 ? 0.335 0.236 0.374 0.030  0.004  -0.013 164 LEU   BBB N   
3262 C  CA  . LEU   B 165 ? 0.422 0.313 0.324 0.032  -0.004 -0.060 164 LEU   BBB CA  
3263 C  C   . LEU   B 165 ? 0.400 0.345 0.324 0.143  -0.001 -0.028 164 LEU   BBB C   
3264 O  O   . LEU   B 165 ? 0.410 0.186 0.378 0.095  -0.023 -0.047 164 LEU   BBB O   
3265 C  CB  . LEU   B 165 ? 0.392 0.321 0.363 0.051  -0.003 -0.012 164 LEU   BBB CB  
3266 C  CG  . LEU   B 165 ? 0.420 0.154 0.375 -0.028 -0.014 -0.034 164 LEU   BBB CG  
3267 C  CD1 . LEU   B 165 ? 0.501 0.200 0.381 -0.020 0.046  -0.020 164 LEU   BBB CD1 
3268 C  CD2 . LEU   B 165 ? 0.411 0.224 0.339 -0.036 -0.042 -0.028 164 LEU   BBB CD2 
3269 N  N   . GLN   B 166 ? 0.381 0.234 0.349 0.090  -0.045 -0.015 165 GLN   BBB N   
3270 C  CA  . GLN   B 166 ? 0.433 0.307 0.367 0.071  -0.042 0.003  165 GLN   BBB CA  
3271 C  C   . GLN   B 166 ? 0.376 0.134 0.425 0.090  -0.048 0.028  165 GLN   BBB C   
3272 O  O   . GLN   B 166 ? 0.495 0.267 0.433 0.053  -0.058 0.009  165 GLN   BBB O   
3273 C  CB  . GLN   B 166 ? 0.464 0.268 0.478 0.083  -0.025 0.043  165 GLN   BBB CB  
3274 C  CG  . GLN   B 166 ? 0.542 0.375 0.446 0.136  -0.053 -0.008 165 GLN   BBB CG  
3275 C  CD  . GLN   B 166 ? 0.532 0.451 0.448 0.081  0.009  -0.060 165 GLN   BBB CD  
3276 O  OE1 . GLN   B 166 ? 0.586 0.239 0.476 0.013  -0.051 -0.004 165 GLN   BBB OE1 
3277 N  NE2 . GLN   B 166 ? 0.566 0.540 0.408 0.089  -0.026 -0.069 165 GLN   BBB NE2 
3278 N  N   . ALA   B 167 ? 0.382 0.215 0.412 0.049  -0.029 0.029  166 ALA   BBB N   
3279 C  CA  . ALA   B 167 ? 0.414 0.344 0.362 0.087  -0.000 -0.009 166 ALA   BBB CA  
3280 C  C   . ALA   B 167 ? 0.473 0.317 0.321 0.080  0.058  -0.020 166 ALA   BBB C   
3281 O  O   . ALA   B 167 ? 0.441 0.351 0.376 0.065  0.041  0.056  166 ALA   BBB O   
3282 C  CB  . ALA   B 167 ? 0.530 0.296 0.385 0.059  -0.026 0.029  166 ALA   BBB CB  
3283 N  N   . ILE   B 168 ? 0.366 0.292 0.362 -0.006 0.022  -0.001 167 ILE   BBB N   
3284 C  CA  . ILE   B 168 ? 0.358 0.340 0.405 0.003  0.056  -0.071 167 ILE   BBB CA  
3285 C  C   . ILE   B 168 ? 0.348 0.367 0.357 0.016  -0.020 0.001  167 ILE   BBB C   
3286 O  O   . ILE   B 168 ? 0.424 0.232 0.383 0.035  -0.037 -0.047 167 ILE   BBB O   
3287 C  CB  . ILE   B 168 ? 0.469 0.261 0.355 0.017  -0.012 -0.001 167 ILE   BBB CB  
3288 C  CG1 . ILE   B 168 ? 0.508 0.299 0.302 0.055  -0.077 -0.058 167 ILE   BBB CG1 
3289 C  CG2 . ILE   B 168 ? 0.375 0.273 0.368 0.058  0.001  -0.046 167 ILE   BBB CG2 
3290 C  CD1 . ILE   B 168 ? 0.518 0.370 0.350 0.114  -0.065 -0.030 167 ILE   BBB CD1 
3291 N  N   . LYS   B 169 ? 0.357 0.385 0.373 0.025  -0.013 -0.017 168 LYS   BBB N   
3292 C  CA  . LYS   B 169 ? 0.355 0.299 0.351 0.064  0.034  0.018  168 LYS   BBB CA  
3293 C  C   . LYS   B 169 ? 0.371 0.307 0.341 0.048  0.042  -0.032 168 LYS   BBB C   
3294 O  O   . LYS   B 169 ? 0.423 0.322 0.346 0.007  -0.013 0.007  168 LYS   BBB O   
3295 C  CB  . LYS   B 169 ? 0.444 0.550 0.465 0.094  -0.046 0.052  168 LYS   BBB CB  
3296 C  CG  . LYS   B 169 ? 0.441 0.722 0.519 0.055  -0.013 0.115  168 LYS   BBB CG  
3297 C  CD  . LYS   B 169 ? 0.536 0.711 0.543 -0.058 0.057  0.123  168 LYS   BBB CD  
3298 C  CE  . LYS   B 169 ? 0.624 0.737 0.639 -0.089 0.086  0.076  168 LYS   BBB CE  
3299 N  NZ  . LYS   B 169 ? 0.801 0.809 0.686 -0.032 -0.052 0.142  168 LYS   BBB NZ  
3300 N  N   . THR   B 170 ? 0.338 0.345 0.322 0.021  -0.011 -0.095 169 THR   BBB N   
3301 C  CA  . THR   B 170 ? 0.364 0.308 0.351 0.013  -0.034 -0.103 169 THR   BBB CA  
3302 C  C   . THR   B 170 ? 0.377 0.311 0.370 -0.011 -0.087 -0.110 169 THR   BBB C   
3303 O  O   . THR   B 170 ? 0.354 0.270 0.349 -0.003 0.004  -0.031 169 THR   BBB O   
3304 C  CB  . THR   B 170 ? 0.428 0.389 0.339 -0.041 -0.048 -0.011 169 THR   BBB CB  
3305 O  OG1 . THR   B 170 ? 0.407 0.339 0.350 0.009  -0.015 -0.023 169 THR   BBB OG1 
3306 C  CG2 . THR   B 170 ? 0.470 0.610 0.427 -0.071 -0.077 -0.104 169 THR   BBB CG2 
3307 N  N   . LYS   B 171 ? 0.374 0.338 0.400 0.024  0.020  -0.066 170 LYS   BBB N   
3308 C  CA  . LYS   B 171 ? 0.384 0.164 0.368 0.033  0.019  -0.118 170 LYS   BBB CA  
3309 C  C   . LYS   B 171 ? 0.414 0.264 0.281 0.025  -0.033 -0.072 170 LYS   BBB C   
3310 O  O   . LYS   B 171 ? 0.415 0.279 0.334 0.046  -0.025 -0.040 170 LYS   BBB O   
3311 C  CB  . LYS   B 171 ? 0.485 0.135 0.413 -0.029 0.008  -0.166 170 LYS   BBB CB  
3312 C  CG  . LYS   B 171 ? 0.461 0.154 0.505 0.015  -0.008 -0.096 170 LYS   BBB CG  
3313 C  CD  . LYS   B 171 ? 0.580 0.146 0.552 0.016  0.030  -0.033 170 LYS   BBB CD  
3314 C  CE  . LYS   B 171 ? 0.560 0.358 0.779 0.071  -0.107 -0.079 170 LYS   BBB CE  
3315 N  NZ  . LYS   B 171 ? 0.697 0.328 1.078 -0.001 -0.125 0.178  170 LYS   BBB NZ  
3316 N  N   . GLY   B 172 ? 0.398 0.230 0.323 0.004  -0.019 -0.027 171 GLY   BBB N   
3317 C  CA  . GLY   B 172 ? 0.323 0.252 0.345 0.018  -0.004 -0.087 171 GLY   BBB CA  
3318 C  C   . GLY   B 172 ? 0.344 0.259 0.434 0.044  0.018  -0.046 171 GLY   BBB C   
3319 O  O   . GLY   B 172 ? 0.396 0.311 0.413 0.006  0.039  -0.050 171 GLY   BBB O   
3320 N  N   . LYS   B 173 ? 0.356 0.279 0.373 0.044  -0.002 -0.048 172 LYS   BBB N   
3321 C  CA  . LYS   B 173 ? 0.369 0.273 0.311 0.043  0.004  0.033  172 LYS   BBB CA  
3322 C  C   . LYS   B 173 ? 0.412 0.256 0.317 0.013  -0.028 0.043  172 LYS   BBB C   
3323 O  O   . LYS   B 173 ? 0.413 0.310 0.292 0.006  -0.034 0.029  172 LYS   BBB O   
3324 C  CB  . LYS   B 173 ? 0.379 0.280 0.435 0.092  -0.066 -0.005 172 LYS   BBB CB  
3325 C  CG  . LYS   B 173 ? 0.368 0.417 0.477 0.058  -0.077 -0.049 172 LYS   BBB CG  
3326 C  CD  . LYS   B 173 ? 0.414 0.554 0.591 0.076  -0.093 -0.024 172 LYS   BBB CD  
3327 C  CE  . LYS   B 173 ? 0.487 0.534 0.521 0.072  -0.121 -0.014 172 LYS   BBB CE  
3328 N  NZ  . LYS   B 173 ? 0.594 0.532 0.723 0.155  -0.125 -0.084 172 LYS   BBB NZ  
3329 N  N   . ARG   B 174 ? 0.453 0.287 0.339 -0.011 -0.035 0.013  173 ARG   BBB N   
3330 C  CA  . ARG   B 174 ? 0.447 0.233 0.366 0.011  -0.058 0.032  173 ARG   BBB CA  
3331 C  C   . ARG   B 174 ? 0.518 0.295 0.311 0.097  -0.007 -0.020 173 ARG   BBB C   
3332 O  O   . ARG   B 174 ? 0.469 0.177 0.396 0.080  -0.033 0.061  173 ARG   BBB O   
3333 C  CB  . ARG   B 174 ? 0.443 0.219 0.419 0.022  -0.033 -0.061 173 ARG   BBB CB  
3334 C  CG  . ARG   B 174 ? 0.485 0.578 0.457 0.079  -0.003 0.001  173 ARG   BBB CG  
3335 C  CD  . ARG   B 174 ? 0.540 0.582 0.484 0.155  -0.069 -0.005 173 ARG   BBB CD  
3336 N  NE  . ARG   B 174 ? 0.412 0.553 0.592 0.010  0.024  0.069  173 ARG   BBB NE  
3337 C  CZ  . ARG   B 174 ? 0.446 0.509 0.538 0.067  0.102  -0.053 173 ARG   BBB CZ  
3338 N  NH1 . ARG   B 174 ? 0.510 0.596 0.705 0.200  -0.059 -0.076 173 ARG   BBB NH1 
3339 N  NH2 . ARG   B 174 ? 0.472 0.456 0.644 0.108  0.073  -0.086 173 ARG   BBB NH2 
3340 N  N   . ALA   B 175 ? 0.465 0.032 0.329 0.032  -0.037 0.020  174 ALA   BBB N   
3341 C  CA  . ALA   B 175 ? 0.541 0.059 0.432 0.103  -0.009 0.089  174 ALA   BBB CA  
3342 C  C   . ALA   B 175 ? 0.478 0.068 0.432 0.044  0.011  0.151  174 ALA   BBB C   
3343 O  O   . ALA   B 175 ? 0.491 0.100 0.395 0.079  -0.003 0.062  174 ALA   BBB O   
3344 C  CB  . ALA   B 175 ? 0.556 0.180 0.423 0.074  -0.017 0.003  174 ALA   BBB CB  
3345 N  N   . PRO   B 176 ? 0.526 0.046 0.382 0.085  0.004  0.019  175 PRO   BBB N   
3346 C  CA  . PRO   B 176 ? 0.579 0.035 0.361 0.084  -0.006 0.069  175 PRO   BBB CA  
3347 C  C   . PRO   B 176 ? 0.476 0.013 0.451 0.016  0.002  0.054  175 PRO   BBB C   
3348 O  O   . PRO   B 176 ? 0.468 0.130 0.491 0.097  0.050  0.079  175 PRO   BBB O   
3349 C  CB  . PRO   B 176 ? 0.589 0.076 0.438 0.070  0.001  0.144  175 PRO   BBB CB  
3350 C  CG  . PRO   B 176 ? 0.566 0.283 0.460 0.020  -0.072 0.074  175 PRO   BBB CG  
3351 C  CD  . PRO   B 176 ? 0.530 0.208 0.381 0.038  -0.061 0.078  175 PRO   BBB CD  
3352 N  N   . PHE   B 177 ? 0.514 0.020 0.407 0.069  0.017  0.045  176 PHE   BBB N   
3353 C  CA  . PHE   B 177 ? 0.498 0.060 0.394 0.043  0.023  0.033  176 PHE   BBB CA  
3354 C  C   . PHE   B 177 ? 0.445 0.125 0.393 0.088  0.008  0.010  176 PHE   BBB C   
3355 O  O   . PHE   B 177 ? 0.444 0.011 0.449 0.016  0.016  0.033  176 PHE   BBB O   
3356 C  CB  . PHE   B 177 ? 0.560 0.064 0.415 0.073  0.004  0.039  176 PHE   BBB CB  
3357 C  CG  . PHE   B 177 ? 0.496 0.011 0.416 0.031  0.007  0.035  176 PHE   BBB CG  
3358 C  CD1 . PHE   B 177 ? 0.534 0.012 0.446 0.034  -0.018 0.037  176 PHE   BBB CD1 
3359 C  CD2 . PHE   B 177 ? 0.520 0.087 0.381 0.032  -0.019 0.013  176 PHE   BBB CD2 
3360 C  CE1 . PHE   B 177 ? 0.555 0.019 0.474 0.083  0.020  -0.003 176 PHE   BBB CE1 
3361 C  CE2 . PHE   B 177 ? 0.562 0.013 0.419 0.041  0.006  0.039  176 PHE   BBB CE2 
3362 C  CZ  . PHE   B 177 ? 0.542 0.010 0.428 0.025  -0.004 0.032  176 PHE   BBB CZ  
3363 N  N   . THR   B 178 ? 0.529 0.091 0.388 0.112  -0.012 0.066  177 THR   BBB N   
3364 C  CA  . THR   B 178 ? 0.544 0.220 0.329 0.065  0.013  0.085  177 THR   BBB CA  
3365 C  C   . THR   B 178 ? 0.449 0.145 0.354 0.185  0.000  0.060  177 THR   BBB C   
3366 O  O   . THR   B 178 ? 0.531 0.040 0.455 0.128  0.038  0.038  177 THR   BBB O   
3367 C  CB  . THR   B 178 ? 0.558 0.087 0.411 0.038  0.004  0.048  177 THR   BBB CB  
3368 O  OG1 . THR   B 178 ? 0.596 0.091 0.469 0.093  0.009  -0.030 177 THR   BBB OG1 
3369 C  CG2 . THR   B 178 ? 0.721 0.028 0.412 -0.029 0.052  0.088  177 THR   BBB CG2 
3370 N  N   . ASN   B 179 ? 0.600 0.071 0.443 0.163  -0.032 0.084  178 ASN   BBB N   
3371 C  CA  . ASN   B 179 ? 0.641 0.065 0.443 0.159  0.104  0.100  178 ASN   BBB CA  
3372 C  C   . ASN   B 179 ? 0.521 0.056 0.417 0.138  0.078  0.049  178 ASN   BBB C   
3373 O  O   . ASN   B 179 ? 0.590 0.126 0.425 0.107  0.066  -0.004 178 ASN   BBB O   
3374 C  CB  . ASN   B 179 ? 0.741 0.148 0.488 0.249  0.015  0.038  178 ASN   BBB CB  
3375 C  CG  . ASN   B 179 ? 0.980 0.094 0.550 0.197  -0.007 0.006  178 ASN   BBB CG  
3376 O  OD1 . ASN   B 179 ? 1.125 0.391 0.562 0.208  0.205  0.039  178 ASN   BBB OD1 
3377 N  ND2 . ASN   B 179 ? 1.125 0.160 0.469 0.400  -0.138 -0.017 178 ASN   BBB ND2 
3378 N  N   . PHE   B 180 ? 0.558 0.041 0.487 0.138  0.032  0.001  179 PHE   BBB N   
3379 C  CA  . PHE   B 180 ? 0.488 0.182 0.409 0.057  0.038  -0.025 179 PHE   BBB CA  
3380 C  C   . PHE   B 180 ? 0.484 0.128 0.426 0.049  0.035  0.062  179 PHE   BBB C   
3381 O  O   . PHE   B 180 ? 0.446 0.026 0.435 0.022  -0.007 0.088  179 PHE   BBB O   
3382 C  CB  . PHE   B 180 ? 0.560 0.029 0.403 0.111  0.026  0.011  179 PHE   BBB CB  
3383 C  CG  . PHE   B 180 ? 0.521 0.033 0.410 0.103  0.039  0.004  179 PHE   BBB CG  
3384 C  CD1 . PHE   B 180 ? 0.530 0.042 0.461 0.137  0.022  0.007  179 PHE   BBB CD1 
3385 C  CD2 . PHE   B 180 ? 0.587 0.102 0.446 0.182  0.082  0.045  179 PHE   BBB CD2 
3386 C  CE1 . PHE   B 180 ? 0.496 0.031 0.544 0.110  0.037  0.007  179 PHE   BBB CE1 
3387 C  CE2 . PHE   B 180 ? 0.517 0.030 0.393 0.027  0.032  -0.066 179 PHE   BBB CE2 
3388 C  CZ  . PHE   B 180 ? 0.524 0.013 0.410 0.050  0.037  0.026  179 PHE   BBB CZ  
3389 N  N   . ASP   B 181 ? 0.435 0.043 0.396 0.043  -0.000 0.026  180 ASP   BBB N   
3390 C  CA  . ASP   B 181 ? 0.514 0.166 0.321 -0.029 -0.032 0.051  180 ASP   BBB CA  
3391 C  C   . ASP   B 181 ? 0.401 0.055 0.352 0.103  0.025  -0.001 180 ASP   BBB C   
3392 O  O   . ASP   B 181 ? 0.437 0.096 0.357 0.080  0.007  -0.014 180 ASP   BBB O   
3393 C  CB  . ASP   B 181 ? 0.612 0.026 0.521 0.106  0.001  0.025  180 ASP   BBB CB  
3394 C  CG  . ASP   B 181 ? 0.554 0.070 0.395 0.160  0.039  -0.071 180 ASP   BBB CG  
3395 O  OD1 . ASP   B 181 ? 0.615 0.010 0.452 0.046  -0.012 -0.010 180 ASP   BBB OD1 
3396 O  OD2 . ASP   B 181 ? 0.710 0.015 0.413 0.050  0.046  -0.042 180 ASP   BBB OD2 
3397 N  N   . PRO   B 182 ? 0.438 0.022 0.341 0.080  0.019  0.021  181 PRO   BBB N   
3398 C  CA  . PRO   B 182 ? 0.431 0.106 0.330 -0.008 0.037  0.031  181 PRO   BBB CA  
3399 C  C   . PRO   B 182 ? 0.377 0.214 0.284 -0.024 0.021  -0.037 181 PRO   BBB C   
3400 O  O   . PRO   B 182 ? 0.406 0.133 0.344 0.014  0.018  -0.032 181 PRO   BBB O   
3401 C  CB  . PRO   B 182 ? 0.450 0.184 0.295 0.048  0.015  0.015  181 PRO   BBB CB  
3402 C  CG  . PRO   B 182 ? 0.462 0.026 0.399 0.095  -0.005 -0.002 181 PRO   BBB CG  
3403 C  CD  . PRO   B 182 ? 0.447 0.035 0.363 0.113  0.003  0.000  181 PRO   BBB CD  
3404 N  N   . SER   B 183 ? 0.423 0.059 0.325 0.009  -0.016 -0.002 182 SER   BBB N   
3405 C  CA  . SER   B 183 ? 0.420 0.076 0.335 0.042  -0.021 0.011  182 SER   BBB CA  
3406 C  C   . SER   B 183 ? 0.411 0.159 0.267 0.003  -0.029 -0.023 182 SER   BBB C   
3407 O  O   . SER   B 183 ? 0.505 0.033 0.354 0.090  0.024  0.013  182 SER   BBB O   
3408 C  CB  . SER   B 183 ? 0.420 0.062 0.352 0.091  -0.009 -0.003 182 SER   BBB CB  
3409 O  OG  . SER   B 183 ? 0.420 0.020 0.411 0.028  0.014  -0.016 182 SER   BBB OG  
3410 N  N   . THR   B 184 ? 0.411 0.033 0.339 -0.014 -0.027 -0.026 183 THR   BBB N   
3411 C  CA  . THR   B 184 ? 0.410 0.026 0.378 -0.080 -0.025 0.009  183 THR   BBB CA  
3412 C  C   . THR   B 184 ? 0.309 0.007 0.399 0.006  0.009  0.018  183 THR   BBB C   
3413 O  O   . THR   B 184 ? 0.426 0.006 0.440 -0.000 0.043  -0.004 183 THR   BBB O   
3414 C  CB  . THR   B 184 ? 0.447 0.055 0.403 -0.029 0.017  0.044  183 THR   BBB CB  
3415 O  OG1 . THR   B 184 ? 0.685 0.015 0.451 0.074  -0.044 0.005  183 THR   BBB OG1 
3416 C  CG2 . THR   B 184 ? 0.603 0.051 0.505 -0.062 0.077  -0.020 183 THR   BBB CG2 
3417 N  N   . LEU   B 185 ? 0.372 0.054 0.356 0.046  0.052  0.005  184 LEU   BBB N   
3418 C  CA  . LEU   B 185 ? 0.370 0.109 0.316 -0.029 0.011  -0.005 184 LEU   BBB CA  
3419 C  C   . LEU   B 185 ? 0.332 0.122 0.349 -0.063 -0.023 0.002  184 LEU   BBB C   
3420 O  O   . LEU   B 185 ? 0.389 0.019 0.407 -0.022 -0.001 -0.033 184 LEU   BBB O   
3421 C  CB  . LEU   B 185 ? 0.444 0.014 0.397 0.058  0.003  -0.010 184 LEU   BBB CB  
3422 C  CG  . LEU   B 185 ? 0.471 0.063 0.374 -0.028 -0.014 0.008  184 LEU   BBB CG  
3423 C  CD1 . LEU   B 185 ? 0.565 0.045 0.357 0.014  -0.044 -0.008 184 LEU   BBB CD1 
3424 C  CD2 . LEU   B 185 ? 0.480 0.085 0.420 0.018  -0.071 -0.075 184 LEU   BBB CD2 
3425 N  N   . LEU   B 186 ? 0.351 0.019 0.366 0.024  -0.023 0.000  185 LEU   BBB N   
3426 C  CA  . LEU   B 186 ? 0.347 0.037 0.375 0.101  0.007  -0.007 185 LEU   BBB CA  
3427 C  C   . LEU   B 186 ? 0.337 0.099 0.323 0.134  -0.003 0.012  185 LEU   BBB C   
3428 O  O   . LEU   B 186 ? 0.411 0.008 0.406 0.027  0.001  0.000  185 LEU   BBB O   
3429 C  CB  . LEU   B 186 ? 0.393 0.026 0.368 0.082  -0.016 0.027  185 LEU   BBB CB  
3430 C  CG  . LEU   B 186 ? 0.374 0.032 0.441 0.098  0.013  0.005  185 LEU   BBB CG  
3431 C  CD1 . LEU   B 186 ? 0.441 0.044 0.412 0.046  -0.030 0.007  185 LEU   BBB CD1 
3432 C  CD2 . LEU   B 186 ? 0.410 0.021 0.391 0.064  0.031  -0.034 185 LEU   BBB CD2 
3433 N  N   . PRO   B 187 ? 0.429 0.013 0.412 0.044  -0.002 -0.029 186 PRO   BBB N   
3434 C  CA  . PRO   B 187 ? 0.402 0.009 0.375 0.029  -0.013 0.006  186 PRO   BBB CA  
3435 C  C   . PRO   B 187 ? 0.398 0.058 0.341 -0.007 -0.013 -0.046 186 PRO   BBB C   
3436 O  O   . PRO   B 187 ? 0.433 0.024 0.408 0.022  -0.001 -0.005 186 PRO   BBB O   
3437 C  CB  . PRO   B 187 ? 0.435 0.039 0.341 -0.013 -0.009 0.104  186 PRO   BBB CB  
3438 C  CG  . PRO   B 187 ? 0.413 0.015 0.368 -0.053 0.005  0.025  186 PRO   BBB CG  
3439 C  CD  . PRO   B 187 ? 0.397 0.036 0.337 0.077  0.006  -0.069 186 PRO   BBB CD  
3440 N  N   . SER   B 188 ? 0.389 0.051 0.347 -0.059 -0.005 -0.009 187 SER   BBB N   
3441 C  CA  . SER   B 188 ? 0.432 0.011 0.401 -0.034 -0.007 -0.024 187 SER   BBB CA  
3442 C  C   . SER   B 188 ? 0.431 0.133 0.383 -0.031 -0.010 -0.008 187 SER   BBB C   
3443 O  O   . SER   B 188 ? 0.426 0.206 0.430 -0.039 0.002  -0.038 187 SER   BBB O   
3444 C  CB  . SER   B 188 ? 0.418 0.215 0.518 -0.027 0.053  0.041  187 SER   BBB CB  
3445 O  OG  . SER   B 188 ? 0.536 0.474 0.494 -0.010 0.002  0.035  187 SER   BBB OG  
3446 N  N   . SER   B 189 ? 0.442 0.109 0.373 0.004  -0.001 -0.017 188 SER   BBB N   
3447 C  CA  . SER   B 189 ? 0.421 0.171 0.394 -0.040 -0.030 -0.073 188 SER   BBB CA  
3448 C  C   . SER   B 189 ? 0.388 0.183 0.344 0.024  -0.041 0.012  188 SER   BBB C   
3449 O  O   . SER   B 189 ? 0.448 0.142 0.414 0.045  -0.044 -0.038 188 SER   BBB O   
3450 C  CB  . SER   B 189 ? 0.439 0.311 0.364 0.018  -0.012 -0.015 188 SER   BBB CB  
3451 O  OG  . SER   B 189 ? 0.512 0.178 0.465 0.001  -0.082 0.093  188 SER   BBB OG  
3452 N  N   . LEU   B 190 ? 0.431 0.044 0.399 -0.017 -0.020 -0.012 189 LEU   BBB N   
3453 C  CA  . LEU   B 190 ? 0.371 0.268 0.438 0.035  -0.017 0.011  189 LEU   BBB CA  
3454 C  C   . LEU   B 190 ? 0.350 0.176 0.406 0.011  0.011  0.014  189 LEU   BBB C   
3455 O  O   . LEU   B 190 ? 0.379 0.088 0.438 0.004  -0.011 0.015  189 LEU   BBB O   
3456 C  CB  . LEU   B 190 ? 0.463 0.192 0.419 0.080  -0.009 0.009  189 LEU   BBB CB  
3457 C  CG  . LEU   B 190 ? 0.416 0.202 0.404 0.049  -0.001 0.042  189 LEU   BBB CG  
3458 C  CD1 . LEU   B 190 ? 0.475 0.233 0.396 0.041  -0.037 0.076  189 LEU   BBB CD1 
3459 C  CD2 . LEU   B 190 ? 0.392 0.331 0.328 0.099  -0.009 0.087  189 LEU   BBB CD2 
3460 N  N   . ASP   B 191 ? 0.378 0.149 0.390 0.009  -0.002 -0.006 190 ASP   BBB N   
3461 C  CA  . ASP   B 191 ? 0.399 0.261 0.331 0.049  -0.012 0.009  190 ASP   BBB CA  
3462 C  C   . ASP   B 191 ? 0.394 0.193 0.335 -0.008 -0.042 0.025  190 ASP   BBB C   
3463 O  O   . ASP   B 191 ? 0.320 0.007 0.397 -0.007 -0.015 0.008  190 ASP   BBB O   
3464 C  CB  . ASP   B 191 ? 0.450 0.291 0.349 0.081  0.043  -0.031 190 ASP   BBB CB  
3465 C  CG  . ASP   B 191 ? 0.481 0.265 0.453 0.029  0.025  -0.111 190 ASP   BBB CG  
3466 O  OD1 . ASP   B 191 ? 0.481 0.253 0.453 -0.007 -0.052 -0.118 190 ASP   BBB OD1 
3467 O  OD2 . ASP   B 191 ? 0.542 0.400 0.426 0.103  -0.005 -0.049 190 ASP   BBB OD2 
3468 N  N   . PHE   B 192 ? 0.398 0.087 0.342 -0.079 -0.017 0.026  191 PHE   BBB N   
3469 C  CA  . PHE   B 192 ? 0.331 0.064 0.344 0.058  -0.033 0.060  191 PHE   BBB CA  
3470 C  C   . PHE   B 192 ? 0.390 0.010 0.334 0.009  -0.063 0.029  191 PHE   BBB C   
3471 O  O   . PHE   B 192 ? 0.426 0.026 0.338 0.045  -0.038 0.037  191 PHE   BBB O   
3472 C  CB  . PHE   B 192 ? 0.335 0.126 0.338 0.004  0.001  -0.002 191 PHE   BBB CB  
3473 C  CG  . PHE   B 192 ? 0.323 0.011 0.360 -0.024 -0.001 0.007  191 PHE   BBB CG  
3474 C  CD1 . PHE   B 192 ? 0.356 0.014 0.376 -0.007 -0.002 -0.005 191 PHE   BBB CD1 
3475 C  CD2 . PHE   B 192 ? 0.312 0.182 0.402 0.039  -0.033 0.038  191 PHE   BBB CD2 
3476 C  CE1 . PHE   B 192 ? 0.358 0.028 0.425 -0.033 0.008  0.050  191 PHE   BBB CE1 
3477 C  CE2 . PHE   B 192 ? 0.334 0.067 0.383 0.037  -0.044 0.063  191 PHE   BBB CE2 
3478 C  CZ  . PHE   B 192 ? 0.340 0.193 0.310 -0.011 -0.018 -0.015 191 PHE   BBB CZ  
3479 N  N   . TRP   B 193 ? 0.426 0.088 0.297 -0.020 0.006  0.005  192 TRP   BBB N   
3480 C  CA  . TRP   B 193 ? 0.381 0.119 0.404 -0.019 -0.019 0.040  192 TRP   BBB CA  
3481 C  C   . TRP   B 193 ? 0.354 0.154 0.317 0.005  -0.062 0.027  192 TRP   BBB C   
3482 O  O   . TRP   B 193 ? 0.403 0.131 0.310 0.042  -0.022 0.061  192 TRP   BBB O   
3483 C  CB  . TRP   B 193 ? 0.458 0.012 0.415 0.044  0.037  0.031  192 TRP   BBB CB  
3484 C  CG  . TRP   B 193 ? 0.432 0.008 0.440 0.020  0.017  0.019  192 TRP   BBB CG  
3485 C  CD1 . TRP   B 193 ? 0.454 0.108 0.442 0.014  0.011  0.048  192 TRP   BBB CD1 
3486 C  CD2 . TRP   B 193 ? 0.432 0.007 0.379 0.000  -0.003 -0.012 192 TRP   BBB CD2 
3487 N  NE1 . TRP   B 193 ? 0.494 0.112 0.403 0.007  0.015  0.094  192 TRP   BBB NE1 
3488 C  CE2 . TRP   B 193 ? 0.479 0.007 0.390 -0.006 0.006  0.013  192 TRP   BBB CE2 
3489 C  CE3 . TRP   B 193 ? 0.444 0.013 0.443 0.010  -0.005 -0.053 192 TRP   BBB CE3 
3490 C  CZ2 . TRP   B 193 ? 0.490 0.016 0.480 -0.031 -0.016 0.063  192 TRP   BBB CZ2 
3491 C  CZ3 . TRP   B 193 ? 0.444 0.007 0.416 0.015  0.006  0.013  192 TRP   BBB CZ3 
3492 C  CH2 . TRP   B 193 ? 0.422 0.077 0.449 -0.041 0.048  0.044  192 TRP   BBB CH2 
3493 N  N   . THR   B 194 ? 0.446 0.027 0.382 0.052  -0.018 0.071  193 THR   BBB N   
3494 C  CA  . THR   B 194 ? 0.405 0.067 0.396 0.079  -0.004 0.008  193 THR   BBB CA  
3495 C  C   . THR   B 194 ? 0.431 0.034 0.340 0.042  -0.011 -0.015 193 THR   BBB C   
3496 O  O   . THR   B 194 ? 0.397 0.095 0.425 0.002  -0.026 0.060  193 THR   BBB O   
3497 C  CB  . THR   B 194 ? 0.405 0.113 0.370 0.031  -0.007 0.010  193 THR   BBB CB  
3498 O  OG1 . THR   B 194 ? 0.440 0.010 0.410 0.003  0.006  0.036  193 THR   BBB OG1 
3499 C  CG2 . THR   B 194 ? 0.452 0.053 0.425 0.014  -0.029 0.060  193 THR   BBB CG2 
3500 N  N   . TYR   B 195 ? 0.429 0.102 0.335 0.066  0.024  0.053  194 TYR   BBB N   
3501 C  CA  . TYR   B 195 ? 0.360 0.115 0.430 0.038  0.028  0.022  194 TYR   BBB CA  
3502 C  C   . TYR   B 195 ? 0.402 0.210 0.385 0.070  -0.021 0.086  194 TYR   BBB C   
3503 O  O   . TYR   B 195 ? 0.418 0.058 0.387 0.043  -0.000 0.047  194 TYR   BBB O   
3504 C  CB  . TYR   B 195 ? 0.424 0.047 0.486 0.043  -0.032 0.104  194 TYR   BBB CB  
3505 C  CG  . TYR   B 195 ? 0.396 0.090 0.387 0.055  0.024  0.056  194 TYR   BBB CG  
3506 C  CD1 . TYR   B 195 ? 0.398 0.074 0.462 0.050  -0.020 0.027  194 TYR   BBB CD1 
3507 C  CD2 . TYR   B 195 ? 0.417 0.025 0.397 0.034  0.021  0.080  194 TYR   BBB CD2 
3508 C  CE1 . TYR   B 195 ? 0.375 0.020 0.448 0.061  -0.022 0.038  194 TYR   BBB CE1 
3509 C  CE2 . TYR   B 195 ? 0.418 0.017 0.444 0.030  -0.020 0.060  194 TYR   BBB CE2 
3510 C  CZ  . TYR   B 195 ? 0.349 0.012 0.433 0.010  -0.006 0.046  194 TYR   BBB CZ  
3511 O  OH  . TYR   B 195 ? 0.411 0.014 0.467 -0.016 -0.034 0.057  194 TYR   BBB OH  
3512 N  N   . PRO   B 196 ? 0.413 0.036 0.450 0.051  0.015  0.103  195 PRO   BBB N   
3513 C  CA  . PRO   B 196 ? 0.458 0.028 0.422 0.071  -0.000 0.067  195 PRO   BBB CA  
3514 C  C   . PRO   B 196 ? 0.489 0.017 0.391 0.012  0.046  0.063  195 PRO   BBB C   
3515 O  O   . PRO   B 196 ? 0.528 0.040 0.494 0.064  0.046  0.118  195 PRO   BBB O   
3516 C  CB  . PRO   B 196 ? 0.449 0.135 0.452 0.091  0.003  0.023  195 PRO   BBB CB  
3517 C  CG  . PRO   B 196 ? 0.395 0.291 0.452 0.041  0.024  0.090  195 PRO   BBB CG  
3518 C  CD  . PRO   B 196 ? 0.443 0.155 0.464 0.093  0.040  0.173  195 PRO   BBB CD  
3519 N  N   . GLY   B 197 ? 0.492 0.016 0.436 0.052  0.010  0.044  196 GLY   BBB N   
3520 C  CA  . GLY   B 197 ? 0.441 0.069 0.395 0.090  0.015  0.047  196 GLY   BBB CA  
3521 C  C   . GLY   B 197 ? 0.438 0.022 0.442 0.083  0.024  0.006  196 GLY   BBB C   
3522 O  O   . GLY   B 197 ? 0.446 0.014 0.528 0.054  0.026  0.031  196 GLY   BBB O   
3523 N  N   . SER   B 198 ? 0.437 0.018 0.464 0.060  0.024  0.045  197 SER   BBB N   
3524 C  CA  . SER   B 198 ? 0.449 0.010 0.436 0.035  0.061  -0.016 197 SER   BBB CA  
3525 C  C   . SER   B 198 ? 0.381 0.075 0.419 0.029  0.060  0.034  197 SER   BBB C   
3526 O  O   . SER   B 198 ? 0.410 0.016 0.416 0.054  0.009  0.035  197 SER   BBB O   
3527 C  CB  . SER   B 198 ? 0.467 0.037 0.477 0.111  0.068  -0.023 197 SER   BBB CB  
3528 O  OG  . SER   B 198 ? 0.528 0.016 0.509 0.071  0.048  0.007  197 SER   BBB OG  
3529 N  N   . LEU   B 199 ? 0.436 0.006 0.444 0.004  0.023  -0.005 198 LEU   BBB N   
3530 C  CA  . LEU   B 199 ? 0.439 0.009 0.408 0.036  0.015  -0.001 198 LEU   BBB CA  
3531 C  C   . LEU   B 199 ? 0.353 0.063 0.387 0.076  0.029  -0.010 198 LEU   BBB C   
3532 O  O   . LEU   B 199 ? 0.432 0.038 0.404 0.074  0.023  0.031  198 LEU   BBB O   
3533 C  CB  . LEU   B 199 ? 0.440 0.012 0.417 -0.025 0.038  -0.043 198 LEU   BBB CB  
3534 C  CG  . LEU   B 199 ? 0.457 0.021 0.419 0.007  -0.007 0.079  198 LEU   BBB CG  
3535 C  CD1 . LEU   B 199 ? 0.521 0.016 0.463 0.045  0.063  0.058  198 LEU   BBB CD1 
3536 C  CD2 . LEU   B 199 ? 0.454 0.046 0.419 0.044  0.027  0.052  198 LEU   BBB CD2 
3537 N  N   . THR   B 200 ? 0.322 0.038 0.381 0.086  0.040  0.009  199 THR   BBB N   
3538 C  CA  . THR   B 200 ? 0.319 0.080 0.424 0.034  -0.009 0.064  199 THR   BBB CA  
3539 C  C   . THR   B 200 ? 0.349 0.079 0.388 0.026  0.039  -0.017 199 THR   BBB C   
3540 O  O   . THR   B 200 ? 0.435 0.008 0.423 0.016  0.031  -0.017 199 THR   BBB O   
3541 C  CB  . THR   B 200 ? 0.394 0.029 0.379 0.069  -0.023 0.059  199 THR   BBB CB  
3542 O  OG1 . THR   B 200 ? 0.528 0.009 0.502 0.026  0.023  0.028  199 THR   BBB OG1 
3543 C  CG2 . THR   B 200 ? 0.428 0.016 0.368 -0.022 -0.013 0.055  199 THR   BBB CG2 
3544 N  N   . HIS   B 201 ? 0.466 0.011 0.419 0.045  0.033  -0.006 200 HIS   BBB N   
3545 C  CA  . HIS   B 201 ? 0.463 0.035 0.412 -0.042 0.013  0.015  200 HIS   BBB CA  
3546 C  C   . HIS   B 201 ? 0.418 0.026 0.382 0.057  -0.015 -0.014 200 HIS   BBB C   
3547 O  O   . HIS   B 201 ? 0.416 0.014 0.500 0.051  -0.029 0.025  200 HIS   BBB O   
3548 C  CB  . HIS   B 201 ? 0.445 0.031 0.431 -0.097 0.003  -0.037 200 HIS   BBB CB  
3549 C  CG  . HIS   B 201 ? 0.462 0.029 0.486 -0.086 -0.039 -0.048 200 HIS   BBB CG  
3550 N  ND1 . HIS   B 201 ? 0.553 0.130 0.494 0.014  0.004  -0.013 200 HIS   BBB ND1 
3551 C  CD2 . HIS   B 201 ? 0.411 0.045 0.418 0.022  0.018  -0.077 200 HIS   BBB CD2 
3552 C  CE1 . HIS   B 201 ? 0.429 0.038 0.473 0.046  -0.005 -0.113 200 HIS   BBB CE1 
3553 N  NE2 . HIS   B 201 ? 0.540 0.041 0.459 0.049  0.012  -0.048 200 HIS   BBB NE2 
3554 N  N   . PRO   B 202 ? 0.497 0.074 0.389 0.023  0.018  -0.035 201 PRO   BBB N   
3555 C  CA  . PRO   B 202 ? 0.524 0.034 0.395 0.045  0.048  -0.054 201 PRO   BBB CA  
3556 C  C   . PRO   B 202 ? 0.389 0.073 0.446 0.042  0.032  0.010  201 PRO   BBB C   
3557 O  O   . PRO   B 202 ? 0.493 0.018 0.500 0.052  0.035  -0.052 201 PRO   BBB O   
3558 C  CB  . PRO   B 202 ? 0.505 0.040 0.407 -0.016 0.066  -0.051 201 PRO   BBB CB  
3559 C  CG  . PRO   B 202 ? 0.549 0.008 0.441 0.026  0.066  0.006  201 PRO   BBB CG  
3560 C  CD  . PRO   B 202 ? 0.499 0.077 0.466 0.060  0.015  -0.058 201 PRO   BBB CD  
3561 N  N   . PRO   B 203 ? 0.427 0.094 0.409 -0.019 0.014  0.039  202 PRO   BBB N   
3562 C  CA  . PRO   B 203 ? 0.488 0.098 0.434 0.034  0.050  -0.028 202 PRO   BBB CA  
3563 C  C   . PRO   B 203 ? 0.366 0.228 0.412 0.025  0.055  -0.037 202 PRO   BBB C   
3564 O  O   . PRO   B 203 ? 0.418 0.113 0.542 0.044  0.088  -0.027 202 PRO   BBB O   
3565 C  CB  . PRO   B 203 ? 0.537 0.017 0.432 0.041  0.067  0.061  202 PRO   BBB CB  
3566 C  CG  . PRO   B 203 ? 0.587 0.009 0.523 -0.027 0.057  -0.033 202 PRO   BBB CG  
3567 C  CD  . PRO   B 203 ? 0.526 0.093 0.483 -0.063 0.040  -0.018 202 PRO   BBB CD  
3568 N  N   . LEU   B 204 ? 0.459 0.067 0.405 0.061  0.086  -0.009 203 LEU   BBB N   
3569 C  CA  . LEU   B 204 ? 0.490 0.020 0.476 -0.069 0.044  0.036  203 LEU   BBB CA  
3570 C  C   . LEU   B 204 ? 0.466 0.070 0.478 -0.090 0.063  0.083  203 LEU   BBB C   
3571 O  O   . LEU   B 204 ? 0.495 0.015 0.526 0.065  0.080  0.020  203 LEU   BBB O   
3572 C  CB  . LEU   B 204 ? 0.435 0.007 0.476 0.007  0.075  -0.016 203 LEU   BBB CB  
3573 C  CG  . LEU   B 204 ? 0.431 0.007 0.530 -0.005 -0.003 -0.009 203 LEU   BBB CG  
3574 C  CD1 . LEU   B 204 ? 0.556 0.017 0.536 -0.032 -0.001 -0.068 203 LEU   BBB CD1 
3575 C  CD2 . LEU   B 204 ? 0.445 0.010 0.628 -0.020 0.006  0.042  203 LEU   BBB CD2 
3576 N  N   . TYR   B 205 ? 0.501 0.019 0.586 0.057  0.049  0.063  204 TYR   BBB N   
3577 C  CA  . TYR   B 205 ? 0.517 0.011 0.451 0.044  0.029  0.021  204 TYR   BBB CA  
3578 C  C   . TYR   B 205 ? 0.370 0.081 0.453 0.027  -0.010 0.006  204 TYR   BBB C   
3579 O  O   . TYR   B 205 ? 0.383 0.087 0.485 0.041  0.039  0.105  204 TYR   BBB O   
3580 C  CB  . TYR   B 205 ? 0.466 0.028 0.408 -0.020 0.045  0.088  204 TYR   BBB CB  
3581 C  CG  . TYR   B 205 ? 0.459 0.054 0.378 0.004  0.027  0.082  204 TYR   BBB CG  
3582 C  CD1 . TYR   B 205 ? 0.508 0.263 0.472 0.035  0.042  -0.087 204 TYR   BBB CD1 
3583 C  CD2 . TYR   B 205 ? 0.497 0.102 0.455 0.057  0.002  0.124  204 TYR   BBB CD2 
3584 C  CE1 . TYR   B 205 ? 0.541 0.259 0.520 0.144  0.101  0.016  204 TYR   BBB CE1 
3585 C  CE2 . TYR   B 205 ? 0.552 0.139 0.459 -0.034 0.085  0.057  204 TYR   BBB CE2 
3586 C  CZ  . TYR   B 205 ? 0.524 0.282 0.533 0.091  0.101  0.067  204 TYR   BBB CZ  
3587 O  OH  . TYR   B 205 ? 0.695 0.084 0.574 -0.042 0.117  0.084  204 TYR   BBB OH  
3588 N  N   . GLU   B 206 ? 0.447 0.036 0.460 0.100  0.015  0.060  205 GLU   BBB N   
3589 C  CA  . GLU   B 206 ? 0.434 0.117 0.431 0.111  0.014  0.115  205 GLU   BBB CA  
3590 C  C   . GLU   B 206 ? 0.348 0.157 0.433 0.162  0.008  0.083  205 GLU   BBB C   
3591 O  O   . GLU   B 206 ? 0.391 0.138 0.543 0.091  -0.026 0.103  205 GLU   BBB O   
3592 C  CB  . GLU   B 206 ? 0.499 0.017 0.462 0.044  0.008  0.056  205 GLU   BBB CB  
3593 C  CG  . GLU   B 206 ? 0.392 0.042 0.550 0.097  0.044  -0.003 205 GLU   BBB CG  
3594 C  CD  . GLU   B 206 ? 0.419 0.081 0.578 0.081  -0.022 0.046  205 GLU   BBB CD  
3595 O  OE1 . GLU   B 206 ? 0.540 0.020 0.638 0.077  0.052  0.045  205 GLU   BBB OE1 
3596 O  OE2 . GLU   B 206 ? 0.510 0.032 0.774 0.103  -0.106 0.033  205 GLU   BBB OE2 
3597 N  N   . SER   B 207 ? 0.343 0.015 0.525 0.028  0.012  0.060  206 SER   BBB N   
3598 C  CA  . SER   B 207 ? 0.374 0.058 0.371 -0.032 -0.026 0.028  206 SER   BBB CA  
3599 C  C   . SER   B 207 ? 0.398 0.116 0.396 -0.036 0.007  0.010  206 SER   BBB C   
3600 O  O   . SER   B 207 ? 0.421 0.065 0.457 0.022  0.020  0.056  206 SER   BBB O   
3601 C  CB  . SER   B 207 ? 0.466 0.008 0.401 0.009  -0.026 0.026  206 SER   BBB CB  
3602 O  OG  . SER   B 207 ? 0.465 0.017 0.438 0.052  0.021  0.010  206 SER   BBB OG  
3603 N  N   . VAL   B 208 ? 0.389 0.096 0.408 0.020  0.002  0.014  207 VAL   BBB N   
3604 C  CA  . VAL   B 208 ? 0.392 0.092 0.408 0.081  0.002  0.055  207 VAL   BBB CA  
3605 C  C   . VAL   B 208 ? 0.471 0.105 0.401 0.035  -0.027 0.020  207 VAL   BBB C   
3606 O  O   . VAL   B 208 ? 0.420 0.078 0.382 0.017  0.016  0.023  207 VAL   BBB O   
3607 C  CB  . VAL   B 208 ? 0.382 0.014 0.375 0.048  0.002  0.023  207 VAL   BBB CB  
3608 C  CG1 . VAL   B 208 ? 0.435 0.033 0.417 0.083  0.033  0.071  207 VAL   BBB CG1 
3609 C  CG2 . VAL   B 208 ? 0.421 0.047 0.360 0.050  -0.003 -0.057 207 VAL   BBB CG2 
3610 N  N   . THR   B 209 ? 0.342 0.064 0.389 0.041  -0.023 0.007  208 THR   BBB N   
3611 C  CA  . THR   B 209 ? 0.388 0.041 0.386 0.004  -0.055 0.053  208 THR   BBB CA  
3612 C  C   . THR   B 209 ? 0.376 0.123 0.399 -0.023 -0.052 0.104  208 THR   BBB C   
3613 O  O   . THR   B 209 ? 0.352 0.065 0.384 0.011  -0.011 0.032  208 THR   BBB O   
3614 C  CB  . THR   B 209 ? 0.342 0.162 0.429 -0.042 -0.043 0.059  208 THR   BBB CB  
3615 O  OG1 . THR   B 209 ? 0.350 0.215 0.438 -0.025 0.012  0.077  208 THR   BBB OG1 
3616 C  CG2 . THR   B 209 ? 0.485 0.024 0.439 0.046  0.013  0.031  208 THR   BBB CG2 
3617 N  N   . TRP   B 210 ? 0.383 0.011 0.464 0.012  -0.033 0.043  209 TRP   BBB N   
3618 C  CA  . TRP   B 210 ? 0.349 0.012 0.377 0.008  -0.023 0.043  209 TRP   BBB CA  
3619 C  C   . TRP   B 210 ? 0.370 0.092 0.364 0.071  0.000  0.074  209 TRP   BBB C   
3620 O  O   . TRP   B 210 ? 0.426 0.028 0.387 -0.002 -0.020 0.034  209 TRP   BBB O   
3621 C  CB  . TRP   B 210 ? 0.348 0.024 0.421 -0.048 0.011  0.018  209 TRP   BBB CB  
3622 C  CG  . TRP   B 210 ? 0.315 0.030 0.364 -0.014 0.003  0.027  209 TRP   BBB CG  
3623 C  CD1 . TRP   B 210 ? 0.414 0.008 0.422 0.012  -0.025 0.025  209 TRP   BBB CD1 
3624 C  CD2 . TRP   B 210 ? 0.337 0.041 0.370 0.031  -0.013 -0.001 209 TRP   BBB CD2 
3625 N  NE1 . TRP   B 210 ? 0.442 0.009 0.362 0.008  -0.002 0.031  209 TRP   BBB NE1 
3626 C  CE2 . TRP   B 210 ? 0.302 0.132 0.367 -0.035 -0.004 0.010  209 TRP   BBB CE2 
3627 C  CE3 . TRP   B 210 ? 0.349 0.013 0.366 0.011  0.006  0.049  209 TRP   BBB CE3 
3628 C  CZ2 . TRP   B 210 ? 0.372 0.099 0.400 -0.046 -0.029 0.024  209 TRP   BBB CZ2 
3629 C  CZ3 . TRP   B 210 ? 0.412 0.009 0.399 0.032  -0.011 0.004  209 TRP   BBB CZ3 
3630 C  CH2 . TRP   B 210 ? 0.433 0.031 0.366 -0.063 0.020  0.029  209 TRP   BBB CH2 
3631 N  N   . ILE   B 211 ? 0.401 0.024 0.320 0.014  0.008  0.074  210 ILE   BBB N   
3632 C  CA  . ILE   B 211 ? 0.353 0.038 0.337 -0.046 0.029  0.088  210 ILE   BBB CA  
3633 C  C   . ILE   B 211 ? 0.376 0.024 0.340 -0.030 -0.005 0.067  210 ILE   BBB C   
3634 O  O   . ILE   B 211 ? 0.382 0.083 0.320 -0.016 -0.021 0.039  210 ILE   BBB O   
3635 C  CB  . ILE   B 211 ? 0.373 0.044 0.368 -0.047 0.017  0.104  210 ILE   BBB CB  
3636 C  CG1 . ILE   B 211 ? 0.415 0.097 0.423 0.016  0.033  0.010  210 ILE   BBB CG1 
3637 C  CG2 . ILE   B 211 ? 0.367 0.022 0.381 -0.009 -0.002 0.076  210 ILE   BBB CG2 
3638 C  CD1 . ILE   B 211 ? 0.503 0.130 0.489 0.024  -0.004 0.109  210 ILE   BBB CD1 
3639 N  N   . ILE   B 212 ? 0.394 0.022 0.429 0.029  -0.011 0.074  211 ILE   BBB N   
3640 C  CA  . ILE   B 212 ? 0.374 0.018 0.343 0.023  -0.021 0.056  211 ILE   BBB CA  
3641 C  C   . ILE   B 212 ? 0.290 0.115 0.357 0.049  -0.035 0.020  211 ILE   BBB C   
3642 O  O   . ILE   B 212 ? 0.396 0.010 0.389 0.018  -0.046 0.031  211 ILE   BBB O   
3643 C  CB  . ILE   B 212 ? 0.411 0.014 0.337 -0.027 -0.011 0.044  211 ILE   BBB CB  
3644 C  CG1 . ILE   B 212 ? 0.442 0.009 0.404 -0.018 -0.009 -0.030 211 ILE   BBB CG1 
3645 C  CG2 . ILE   B 212 ? 0.421 0.009 0.356 0.030  0.021  0.009  211 ILE   BBB CG2 
3646 C  CD1 . ILE   B 212 ? 0.386 0.007 0.425 -0.013 -0.009 0.002  211 ILE   BBB CD1 
3647 N  N   . CYS   B 213 ? 0.389 0.012 0.326 0.018  -0.061 0.035  212 CYS   BBB N   
3648 C  CA  . CYS   B 213 ? 0.386 0.115 0.344 0.001  -0.018 -0.006 212 CYS   BBB CA  
3649 C  C   . CYS   B 213 ? 0.339 0.126 0.279 0.037  -0.026 -0.008 212 CYS   BBB C   
3650 O  O   . CYS   B 213 ? 0.390 0.047 0.345 0.024  -0.028 0.038  212 CYS   BBB O   
3651 C  CB  . CYS   B 213 ? 0.444 0.078 0.331 -0.031 -0.036 0.016  212 CYS   BBB CB  
3652 S  SG  . CYS   B 213 ? 0.442 0.010 0.396 0.007  -0.018 0.038  212 CYS   BBB SG  
3653 N  N   . LYS   B 214 ? 0.406 0.007 0.309 0.011  -0.032 -0.003 213 LYS   BBB N   
3654 C  CA  . LYS   B 214 ? 0.383 0.054 0.366 0.034  0.017  0.020  213 LYS   BBB CA  
3655 C  C   . LYS   B 214 ? 0.382 0.071 0.358 0.004  -0.032 0.052  213 LYS   BBB C   
3656 O  O   . LYS   B 214 ? 0.546 0.009 0.473 -0.001 -0.010 0.035  213 LYS   BBB O   
3657 C  CB  . LYS   B 214 ? 0.408 0.209 0.377 -0.017 -0.019 0.013  213 LYS   BBB CB  
3658 C  CG  . LYS   B 214 ? 0.469 0.233 0.462 -0.036 0.012  0.050  213 LYS   BBB CG  
3659 C  CD  . LYS   B 214 ? 0.581 0.362 0.560 -0.032 0.022  -0.087 213 LYS   BBB CD  
3660 C  CE  . LYS   B 214 ? 0.612 0.610 0.617 0.074  0.038  -0.233 213 LYS   BBB CE  
3661 N  NZ  . LYS   B 214 ? 0.695 0.597 0.804 -0.126 0.200  -0.327 213 LYS   BBB NZ  
3662 N  N   . GLU   B 215 ? 0.345 0.047 0.344 -0.014 -0.007 0.053  214 GLU   BBB N   
3663 C  CA  . GLU   B 215 ? 0.359 0.051 0.352 -0.042 -0.009 -0.032 214 GLU   BBB CA  
3664 C  C   . GLU   B 215 ? 0.339 0.035 0.347 0.020  0.030  -0.027 214 GLU   BBB C   
3665 O  O   . GLU   B 215 ? 0.405 0.008 0.351 -0.027 0.033  -0.007 214 GLU   BBB O   
3666 C  CB  . GLU   B 215 ? 0.422 0.019 0.379 -0.012 -0.019 0.020  214 GLU   BBB CB  
3667 C  CG  . GLU   B 215 ? 0.502 0.208 0.412 -0.002 -0.036 -0.056 214 GLU   BBB CG  
3668 C  CD  . GLU   B 215 ? 0.627 0.541 0.433 -0.088 0.028  -0.037 214 GLU   BBB CD  
3669 O  OE1 . GLU   B 215 ? 0.613 0.825 0.563 -0.117 0.046  -0.103 214 GLU   BBB OE1 
3670 O  OE2 . GLU   B 215 ? 0.810 0.931 0.437 0.038  -0.002 -0.008 214 GLU   BBB OE2 
3671 N  N   . SER   B 216 ? 0.378 0.010 0.328 -0.004 0.014  0.032  215 SER   BBB N   
3672 C  CA  . SER   B 216 ? 0.448 0.031 0.337 0.008  -0.006 0.090  215 SER   BBB CA  
3673 C  C   . SER   B 216 ? 0.431 0.041 0.291 0.064  0.001  0.085  215 SER   BBB C   
3674 O  O   . SER   B 216 ? 0.424 0.115 0.357 -0.009 0.022  0.011  215 SER   BBB O   
3675 C  CB  . SER   B 216 ? 0.425 0.101 0.363 -0.081 0.031  -0.062 215 SER   BBB CB  
3676 O  OG  . SER   B 216 ? 0.481 0.141 0.374 -0.066 0.060  -0.012 215 SER   BBB OG  
3677 N  N   . ILE   B 217 ? 0.374 0.071 0.309 0.039  -0.023 0.026  216 ILE   BBB N   
3678 C  CA  . ILE   B 217 ? 0.383 0.059 0.309 0.017  -0.043 0.028  216 ILE   BBB CA  
3679 C  C   . ILE   B 217 ? 0.377 0.063 0.331 0.025  -0.011 0.018  216 ILE   BBB C   
3680 O  O   . ILE   B 217 ? 0.410 0.057 0.393 0.032  -0.000 -0.018 216 ILE   BBB O   
3681 C  CB  . ILE   B 217 ? 0.379 0.153 0.295 0.038  0.007  0.028  216 ILE   BBB CB  
3682 C  CG1 . ILE   B 217 ? 0.379 0.070 0.311 0.020  0.008  -0.011 216 ILE   BBB CG1 
3683 C  CG2 . ILE   B 217 ? 0.469 0.015 0.357 0.031  0.002  -0.049 216 ILE   BBB CG2 
3684 C  CD1 . ILE   B 217 ? 0.425 0.127 0.300 0.075  0.045  -0.021 216 ILE   BBB CD1 
3685 N  N   . SER   B 218 ? 0.397 0.070 0.406 0.061  0.004  0.002  217 SER   BBB N   
3686 C  CA  A SER   B 218 ? 0.412 0.059 0.403 0.057  0.003  0.009  217 SER   BBB CA  
3687 C  CA  B SER   B 218 ? 0.411 0.093 0.403 0.047  0.012  -0.002 217 SER   BBB CA  
3688 C  C   . SER   B 218 ? 0.303 0.179 0.395 0.032  0.039  -0.024 217 SER   BBB C   
3689 O  O   . SER   B 218 ? 0.379 0.096 0.365 0.008  0.003  -0.045 217 SER   BBB O   
3690 C  CB  A SER   B 218 ? 0.395 0.035 0.384 0.035  0.002  0.024  217 SER   BBB CB  
3691 C  CB  B SER   B 218 ? 0.410 0.160 0.395 0.033  0.021  -0.043 217 SER   BBB CB  
3692 O  OG  A SER   B 218 ? 0.520 0.031 0.400 0.112  -0.001 -0.008 217 SER   BBB OG  
3693 O  OG  B SER   B 218 ? 0.465 0.119 0.397 0.021  0.031  -0.028 217 SER   BBB OG  
3694 N  N   . VAL   B 219 ? 0.352 0.135 0.366 -0.016 0.007  0.053  218 VAL   BBB N   
3695 C  CA  . VAL   B 219 ? 0.360 0.175 0.366 -0.007 0.016  -0.014 218 VAL   BBB CA  
3696 C  C   . VAL   B 219 ? 0.337 0.252 0.335 0.006  -0.000 0.024  218 VAL   BBB C   
3697 O  O   . VAL   B 219 ? 0.394 0.151 0.407 -0.029 0.019  -0.007 218 VAL   BBB O   
3698 C  CB  . VAL   B 219 ? 0.345 0.069 0.365 -0.012 -0.003 -0.011 218 VAL   BBB CB  
3699 C  CG1 . VAL   B 219 ? 0.371 0.078 0.383 -0.009 -0.024 0.011  218 VAL   BBB CG1 
3700 C  CG2 . VAL   B 219 ? 0.366 0.142 0.371 0.012  0.004  -0.067 218 VAL   BBB CG2 
3701 N  N   . SER   B 220 ? 0.431 0.075 0.397 0.079  -0.019 -0.038 219 SER   BBB N   
3702 C  CA  . SER   B 220 ? 0.415 0.237 0.359 0.029  -0.003 -0.076 219 SER   BBB CA  
3703 C  C   . SER   B 220 ? 0.332 0.160 0.370 -0.015 0.015  -0.057 219 SER   BBB C   
3704 O  O   . SER   B 220 ? 0.374 0.146 0.372 -0.005 0.003  -0.022 219 SER   BBB O   
3705 C  CB  . SER   B 220 ? 0.369 0.338 0.387 0.022  0.013  -0.017 219 SER   BBB CB  
3706 O  OG  . SER   B 220 ? 0.430 0.195 0.361 0.019  -0.017 -0.030 219 SER   BBB OG  
3707 N  N   . SER   B 221 ? 0.417 0.270 0.386 -0.112 0.025  -0.036 220 SER   BBB N   
3708 C  CA  . SER   B 221 ? 0.340 0.181 0.442 -0.005 -0.046 -0.042 220 SER   BBB CA  
3709 C  C   . SER   B 221 ? 0.392 0.333 0.376 0.081  -0.028 -0.074 220 SER   BBB C   
3710 O  O   . SER   B 221 ? 0.454 0.163 0.413 0.050  -0.003 -0.050 220 SER   BBB O   
3711 C  CB  . SER   B 221 ? 0.407 0.238 0.471 -0.102 -0.039 -0.038 220 SER   BBB CB  
3712 O  OG  . SER   B 221 ? 0.557 0.274 0.568 -0.057 0.016  -0.081 220 SER   BBB OG  
3713 N  N   . GLU   B 222 ? 0.387 0.220 0.386 -0.019 -0.015 -0.037 221 GLU   BBB N   
3714 C  CA  . GLU   B 222 ? 0.415 0.287 0.374 0.045  0.001  -0.048 221 GLU   BBB CA  
3715 C  C   . GLU   B 222 ? 0.384 0.291 0.346 0.046  -0.015 -0.039 221 GLU   BBB C   
3716 O  O   . GLU   B 222 ? 0.407 0.259 0.355 0.020  -0.020 -0.092 221 GLU   BBB O   
3717 C  CB  . GLU   B 222 ? 0.403 0.445 0.374 0.083  0.063  -0.056 221 GLU   BBB CB  
3718 C  CG  . GLU   B 222 ? 0.361 0.463 0.355 0.072  0.024  -0.002 221 GLU   BBB CG  
3719 C  CD  . GLU   B 222 ? 0.416 0.410 0.380 0.004  0.023  0.044  221 GLU   BBB CD  
3720 O  OE1 . GLU   B 222 ? 0.535 0.494 0.364 0.102  0.017  -0.007 221 GLU   BBB OE1 
3721 O  OE2 . GLU   B 222 ? 0.482 0.416 0.419 -0.049 -0.025 -0.068 221 GLU   BBB OE2 
3722 N  N   . GLN   B 223 ? 0.390 0.248 0.368 0.065  -0.011 -0.012 222 GLN   BBB N   
3723 C  CA  . GLN   B 223 ? 0.387 0.158 0.338 0.066  -0.008 -0.017 222 GLN   BBB CA  
3724 C  C   . GLN   B 223 ? 0.397 0.178 0.354 0.058  0.005  -0.031 222 GLN   BBB C   
3725 O  O   . GLN   B 223 ? 0.432 0.153 0.396 0.039  -0.011 0.005  222 GLN   BBB O   
3726 C  CB  . GLN   B 223 ? 0.398 0.099 0.328 0.038  -0.011 0.016  222 GLN   BBB CB  
3727 C  CG  . GLN   B 223 ? 0.401 0.168 0.365 0.083  0.012  -0.021 222 GLN   BBB CG  
3728 C  CD  . GLN   B 223 ? 0.426 0.026 0.351 0.033  0.005  -0.004 222 GLN   BBB CD  
3729 O  OE1 . GLN   B 223 ? 0.453 0.058 0.360 0.043  -0.002 -0.010 222 GLN   BBB OE1 
3730 N  NE2 . GLN   B 223 ? 0.458 0.017 0.395 0.034  0.033  -0.044 222 GLN   BBB NE2 
3731 N  N   . LEU   B 224 ? 0.347 0.224 0.311 -0.022 -0.001 -0.026 223 LEU   BBB N   
3732 C  CA  . LEU   B 224 ? 0.404 0.226 0.366 0.033  -0.030 -0.003 223 LEU   BBB CA  
3733 C  C   . LEU   B 224 ? 0.344 0.205 0.348 0.025  -0.010 0.059  223 LEU   BBB C   
3734 O  O   . LEU   B 224 ? 0.389 0.182 0.371 0.038  -0.011 -0.030 223 LEU   BBB O   
3735 C  CB  . LEU   B 224 ? 0.438 0.094 0.383 0.043  -0.036 -0.027 223 LEU   BBB CB  
3736 C  CG  . LEU   B 224 ? 0.390 0.190 0.434 -0.020 -0.049 -0.033 223 LEU   BBB CG  
3737 C  CD1 . LEU   B 224 ? 0.551 0.291 0.461 0.052  0.047  0.025  223 LEU   BBB CD1 
3738 C  CD2 . LEU   B 224 ? 0.394 0.186 0.448 -0.053 0.002  -0.097 223 LEU   BBB CD2 
3739 N  N   . ALA   B 225 ? 0.350 0.157 0.379 -0.016 -0.039 -0.025 224 ALA   BBB N   
3740 C  CA  . ALA   B 225 ? 0.329 0.242 0.363 -0.016 -0.027 -0.011 224 ALA   BBB CA  
3741 C  C   . ALA   B 225 ? 0.347 0.148 0.369 -0.018 -0.010 -0.050 224 ALA   BBB C   
3742 O  O   . ALA   B 225 ? 0.441 0.231 0.373 0.043  0.016  -0.024 224 ALA   BBB O   
3743 C  CB  . ALA   B 225 ? 0.362 0.231 0.415 -0.017 0.032  0.036  224 ALA   BBB CB  
3744 N  N   . GLN   B 226 ? 0.366 0.169 0.398 -0.009 0.009  -0.091 225 GLN   BBB N   
3745 C  CA  . GLN   B 226 ? 0.392 0.177 0.391 -0.023 -0.004 -0.060 225 GLN   BBB CA  
3746 C  C   . GLN   B 226 ? 0.384 0.041 0.361 -0.056 -0.033 -0.037 225 GLN   BBB C   
3747 O  O   . GLN   B 226 ? 0.460 0.231 0.364 0.021  -0.009 -0.011 225 GLN   BBB O   
3748 C  CB  . GLN   B 226 ? 0.412 0.221 0.395 0.014  -0.003 -0.131 225 GLN   BBB CB  
3749 C  CG  . GLN   B 226 ? 0.426 0.221 0.428 0.066  -0.005 -0.128 225 GLN   BBB CG  
3750 C  CD  . GLN   B 226 ? 0.460 0.244 0.518 -0.040 -0.032 -0.092 225 GLN   BBB CD  
3751 O  OE1 . GLN   B 226 ? 0.507 0.180 0.529 0.098  -0.078 -0.050 225 GLN   BBB OE1 
3752 N  NE2 . GLN   B 226 ? 0.449 0.223 0.518 0.075  -0.027 -0.082 225 GLN   BBB NE2 
3753 N  N   . PHE   B 227 ? 0.360 0.200 0.364 0.005  -0.015 0.014  226 PHE   BBB N   
3754 C  CA  . PHE   B 227 ? 0.350 0.072 0.406 -0.037 -0.023 -0.013 226 PHE   BBB CA  
3755 C  C   . PHE   B 227 ? 0.396 0.205 0.378 0.001  -0.023 -0.088 226 PHE   BBB C   
3756 O  O   . PHE   B 227 ? 0.377 0.232 0.388 -0.002 -0.002 -0.072 226 PHE   BBB O   
3757 C  CB  . PHE   B 227 ? 0.428 0.262 0.371 0.005  -0.016 -0.014 226 PHE   BBB CB  
3758 C  CG  . PHE   B 227 ? 0.431 0.220 0.352 0.030  0.016  -0.033 226 PHE   BBB CG  
3759 C  CD1 . PHE   B 227 ? 0.430 0.283 0.430 -0.087 -0.006 -0.021 226 PHE   BBB CD1 
3760 C  CD2 . PHE   B 227 ? 0.440 0.217 0.409 0.050  0.017  -0.017 226 PHE   BBB CD2 
3761 C  CE1 . PHE   B 227 ? 0.415 0.223 0.430 -0.057 0.033  -0.046 226 PHE   BBB CE1 
3762 C  CE2 . PHE   B 227 ? 0.440 0.243 0.402 0.105  -0.004 -0.063 226 PHE   BBB CE2 
3763 C  CZ  . PHE   B 227 ? 0.430 0.286 0.424 -0.109 -0.002 -0.038 226 PHE   BBB CZ  
3764 N  N   . ARG   B 228 ? 0.436 0.100 0.378 0.009  -0.015 -0.084 227 ARG   BBB N   
3765 C  CA  . ARG   B 228 ? 0.402 0.154 0.388 -0.016 -0.006 -0.122 227 ARG   BBB CA  
3766 C  C   . ARG   B 228 ? 0.451 0.230 0.396 0.044  -0.025 -0.084 227 ARG   BBB C   
3767 O  O   . ARG   B 228 ? 0.514 0.314 0.446 -0.043 0.015  -0.134 227 ARG   BBB O   
3768 C  CB  . ARG   B 228 ? 0.447 0.104 0.494 0.031  0.009  -0.068 227 ARG   BBB CB  
3769 C  CG  . ARG   B 228 ? 0.455 0.127 0.508 -0.034 0.036  0.040  227 ARG   BBB CG  
3770 C  CD  . ARG   B 228 ? 0.545 0.064 0.550 -0.089 -0.072 -0.031 227 ARG   BBB CD  
3771 N  NE  . ARG   B 228 ? 0.483 0.301 0.538 -0.014 -0.015 -0.009 227 ARG   BBB NE  
3772 C  CZ  . ARG   B 228 ? 0.538 0.015 0.556 -0.062 0.004  -0.027 227 ARG   BBB CZ  
3773 N  NH1 . ARG   B 228 ? 0.520 0.191 0.510 -0.010 -0.002 -0.105 227 ARG   BBB NH1 
3774 N  NH2 . ARG   B 228 ? 0.497 0.230 0.437 -0.044 -0.071 -0.031 227 ARG   BBB NH2 
3775 N  N   . SER   B 229 ? 0.410 0.188 0.308 0.008  -0.017 -0.069 228 SER   BBB N   
3776 C  CA  . SER   B 229 ? 0.448 0.130 0.342 -0.016 -0.021 -0.113 228 SER   BBB CA  
3777 C  C   . SER   B 229 ? 0.391 0.222 0.364 0.070  -0.022 -0.078 228 SER   BBB C   
3778 O  O   . SER   B 229 ? 0.367 0.338 0.369 0.051  -0.047 -0.072 228 SER   BBB O   
3779 C  CB  . SER   B 229 ? 0.476 0.311 0.417 0.031  0.006  -0.213 228 SER   BBB CB  
3780 O  OG  . SER   B 229 ? 0.552 0.371 0.552 -0.073 0.022  -0.084 228 SER   BBB OG  
3781 N  N   . LEU   B 230 ? 0.391 0.240 0.356 -0.006 0.015  -0.055 229 LEU   BBB N   
3782 C  CA  . LEU   B 230 ? 0.345 0.306 0.362 0.033  -0.000 -0.089 229 LEU   BBB CA  
3783 C  C   . LEU   B 230 ? 0.401 0.296 0.376 0.050  0.045  -0.090 229 LEU   BBB C   
3784 O  O   . LEU   B 230 ? 0.401 0.271 0.405 -0.010 -0.021 -0.082 229 LEU   BBB O   
3785 C  CB  . LEU   B 230 ? 0.381 0.258 0.310 0.021  -0.030 -0.068 229 LEU   BBB CB  
3786 C  CG  . LEU   B 230 ? 0.406 0.268 0.424 -0.014 -0.001 -0.072 229 LEU   BBB CG  
3787 C  CD1 . LEU   B 230 ? 0.416 0.231 0.445 -0.026 -0.011 -0.121 229 LEU   BBB CD1 
3788 C  CD2 . LEU   B 230 ? 0.459 0.246 0.513 -0.052 -0.013 0.001  229 LEU   BBB CD2 
3789 N  N   . LEU   B 231 ? 0.389 0.473 0.338 0.041  0.002  -0.136 230 LEU   BBB N   
3790 C  CA  . LEU   B 231 ? 0.370 0.309 0.373 0.017  -0.030 -0.085 230 LEU   BBB CA  
3791 C  C   . LEU   B 231 ? 0.391 0.260 0.409 -0.026 0.017  -0.066 230 LEU   BBB C   
3792 O  O   . LEU   B 231 ? 0.397 0.176 0.412 -0.014 0.007  -0.009 230 LEU   BBB O   
3793 C  CB  . LEU   B 231 ? 0.369 0.428 0.389 0.044  -0.051 -0.081 230 LEU   BBB CB  
3794 C  CG  . LEU   B 231 ? 0.361 0.412 0.440 0.063  -0.060 -0.063 230 LEU   BBB CG  
3795 C  CD1 . LEU   B 231 ? 0.367 0.566 0.459 0.141  0.004  -0.049 230 LEU   BBB CD1 
3796 C  CD2 . LEU   B 231 ? 0.377 0.587 0.413 0.057  0.001  -0.014 230 LEU   BBB CD2 
3797 N  N   . SER   B 232 ? 0.408 0.228 0.412 0.006  -0.017 0.005  231 SER   BBB N   
3798 C  CA  . SER   B 232 ? 0.433 0.287 0.429 0.020  -0.035 -0.046 231 SER   BBB CA  
3799 C  C   . SER   B 232 ? 0.376 0.250 0.457 0.049  -0.004 -0.054 231 SER   BBB C   
3800 O  O   . SER   B 232 ? 0.446 0.217 0.480 0.101  0.018  -0.158 231 SER   BBB O   
3801 C  CB  . SER   B 232 ? 0.404 0.261 0.450 -0.022 -0.032 -0.036 231 SER   BBB CB  
3802 O  OG  . SER   B 232 ? 0.480 0.295 0.429 -0.059 -0.023 -0.090 231 SER   BBB OG  
3803 N  N   . ASN   B 233 ? 0.398 0.229 0.394 0.048  -0.016 -0.118 232 ASN   BBB N   
3804 C  CA  . ASN   B 233 ? 0.392 0.322 0.402 0.044  -0.031 -0.032 232 ASN   BBB CA  
3805 C  C   . ASN   B 233 ? 0.405 0.388 0.355 -0.028 0.009  -0.066 232 ASN   BBB C   
3806 O  O   . ASN   B 233 ? 0.434 0.316 0.427 -0.022 -0.042 -0.088 232 ASN   BBB O   
3807 C  CB  . ASN   B 233 ? 0.454 0.342 0.389 0.041  -0.056 -0.128 232 ASN   BBB CB  
3808 C  CG  . ASN   B 233 ? 0.340 0.348 0.339 -0.026 0.008  -0.037 232 ASN   BBB CG  
3809 O  OD1 . ASN   B 233 ? 0.410 0.482 0.398 -0.087 0.066  -0.134 232 ASN   BBB OD1 
3810 N  ND2 . ASN   B 233 ? 0.515 0.319 0.377 0.008  -0.095 -0.075 232 ASN   BBB ND2 
3811 N  N   . VAL   B 234 ? 0.474 0.456 0.348 -0.054 0.048  -0.119 233 VAL   BBB N   
3812 C  CA  . VAL   B 234 ? 0.418 0.492 0.424 0.003  0.008  -0.069 233 VAL   BBB CA  
3813 C  C   . VAL   B 234 ? 0.386 0.402 0.410 -0.025 0.026  -0.039 233 VAL   BBB C   
3814 O  O   . VAL   B 234 ? 0.369 0.556 0.482 -0.035 0.029  -0.156 233 VAL   BBB O   
3815 C  CB  . VAL   B 234 ? 0.379 0.608 0.452 0.005  -0.006 -0.142 233 VAL   BBB CB  
3816 C  CG1 . VAL   B 234 ? 0.488 0.580 0.453 0.059  -0.024 -0.136 233 VAL   BBB CG1 
3817 C  CG2 . VAL   B 234 ? 0.467 0.658 0.572 -0.052 0.019  -0.232 233 VAL   BBB CG2 
3818 N  N   . GLU   B 235 ? 0.451 0.403 0.466 0.013  -0.022 -0.057 234 GLU   BBB N   
3819 C  CA  . GLU   B 235 ? 0.399 0.455 0.418 -0.015 0.013  -0.082 234 GLU   BBB CA  
3820 C  C   . GLU   B 235 ? 0.448 0.662 0.350 -0.003 0.037  -0.115 234 GLU   BBB C   
3821 O  O   . GLU   B 235 ? 0.478 0.794 0.340 -0.042 0.058  -0.106 234 GLU   BBB O   
3822 C  CB  . GLU   B 235 ? 0.496 0.409 0.359 0.041  -0.028 0.004  234 GLU   BBB CB  
3823 C  CG  . GLU   B 235 ? 0.493 0.420 0.565 0.045  -0.019 -0.029 234 GLU   BBB CG  
3824 C  CD  . GLU   B 235 ? 0.546 0.424 0.395 0.098  -0.029 0.047  234 GLU   BBB CD  
3825 O  OE1 . GLU   B 235 ? 0.644 0.723 0.401 0.024  -0.124 -0.002 234 GLU   BBB OE1 
3826 O  OE2 . GLU   B 235 ? 0.913 0.856 0.353 0.111  0.077  0.035  234 GLU   BBB OE2 
3827 N  N   . GLY   B 236 ? 0.436 0.652 0.452 0.025  0.012  -0.172 235 GLY   BBB N   
3828 C  CA  . GLY   B 236 ? 0.540 0.640 0.478 -0.007 -0.063 -0.090 235 GLY   BBB CA  
3829 C  C   . GLY   B 236 ? 0.565 0.589 0.392 0.020  -0.003 -0.134 235 GLY   BBB C   
3830 O  O   . GLY   B 236 ? 0.733 0.746 0.592 0.031  -0.075 -0.275 235 GLY   BBB O   
3831 N  N   . ASP   B 237 ? 0.479 0.495 0.415 -0.068 -0.031 -0.082 236 ASP   BBB N   
3832 C  CA  . ASP   B 237 ? 0.600 0.495 0.373 -0.135 -0.007 -0.122 236 ASP   BBB CA  
3833 C  C   . ASP   B 237 ? 0.590 0.572 0.425 -0.154 -0.022 -0.183 236 ASP   BBB C   
3834 O  O   . ASP   B 237 ? 0.592 0.573 0.477 -0.028 -0.013 -0.081 236 ASP   BBB O   
3835 C  CB  . ASP   B 237 ? 0.631 0.479 0.410 -0.057 -0.024 -0.219 236 ASP   BBB CB  
3836 C  CG  . ASP   B 237 ? 0.710 0.669 0.381 0.068  -0.012 -0.146 236 ASP   BBB CG  
3837 O  OD1 . ASP   B 237 ? 0.648 0.748 0.424 0.030  -0.023 -0.111 236 ASP   BBB OD1 
3838 O  OD2 . ASP   B 237 ? 0.575 0.682 0.657 -0.007 -0.039 -0.235 236 ASP   BBB OD2 
3839 N  N   . ASN   B 238 ? 0.721 0.465 0.387 -0.086 0.010  -0.139 237 ASN   BBB N   
3840 C  CA  . ASN   B 238 ? 0.697 0.609 0.450 -0.129 -0.026 -0.147 237 ASN   BBB CA  
3841 C  C   . ASN   B 238 ? 0.599 0.298 0.515 -0.067 -0.096 -0.183 237 ASN   BBB C   
3842 O  O   . ASN   B 238 ? 0.532 0.512 0.462 -0.052 -0.005 -0.229 237 ASN   BBB O   
3843 C  CB  . ASN   B 238 ? 1.014 0.615 0.613 -0.206 -0.074 -0.350 237 ASN   BBB CB  
3844 C  CG  . ASN   B 238 ? 1.001 0.539 0.897 -0.225 -0.031 -0.341 237 ASN   BBB CG  
3845 O  OD1 . ASN   B 238 ? 0.668 0.514 0.555 -0.086 -0.030 -0.033 237 ASN   BBB OD1 
3846 N  ND2 . ASN   B 238 ? 0.923 0.252 0.695 -0.036 -0.288 -0.087 237 ASN   BBB ND2 
3847 N  N   . ALA   B 239 ? 0.620 0.774 0.474 -0.075 -0.029 -0.298 238 ALA   BBB N   
3848 C  CA  . ALA   B 239 ? 0.529 0.579 0.444 -0.091 -0.020 -0.225 238 ALA   BBB CA  
3849 C  C   . ALA   B 239 ? 0.376 0.605 0.567 -0.197 0.020  -0.159 238 ALA   BBB C   
3850 O  O   . ALA   B 239 ? 0.519 0.737 0.575 -0.346 -0.005 -0.118 238 ALA   BBB O   
3851 C  CB  . ALA   B 239 ? 0.413 0.981 0.541 -0.091 0.080  -0.275 238 ALA   BBB CB  
3852 N  N   . VAL   B 240 ? 0.530 0.451 0.521 -0.109 -0.072 -0.208 239 VAL   BBB N   
3853 C  CA  . VAL   B 240 ? 0.444 0.513 0.432 -0.033 -0.011 -0.215 239 VAL   BBB CA  
3854 C  C   . VAL   B 240 ? 0.449 0.237 0.483 -0.038 0.037  -0.196 239 VAL   BBB C   
3855 O  O   . VAL   B 240 ? 0.446 0.396 0.418 -0.079 0.012  -0.097 239 VAL   BBB O   
3856 C  CB  . VAL   B 240 ? 0.598 0.225 0.555 0.018  -0.028 -0.199 239 VAL   BBB CB  
3857 C  CG1 . VAL   B 240 ? 0.663 0.468 0.466 -0.173 -0.084 -0.081 239 VAL   BBB CG1 
3858 C  CG2 . VAL   B 240 ? 0.578 0.217 0.537 -0.140 0.060  -0.191 239 VAL   BBB CG2 
3859 N  N   . PRO   B 241 ? 0.466 0.467 0.442 -0.039 0.006  -0.215 240 PRO   BBB N   
3860 C  CA  . PRO   B 241 ? 0.400 0.425 0.443 -0.073 -0.047 -0.185 240 PRO   BBB CA  
3861 C  C   . PRO   B 241 ? 0.410 0.295 0.386 -0.092 -0.046 -0.157 240 PRO   BBB C   
3862 O  O   . PRO   B 241 ? 0.541 0.328 0.530 0.094  0.018  -0.120 240 PRO   BBB O   
3863 C  CB  . PRO   B 241 ? 0.444 0.501 0.578 -0.144 -0.031 -0.185 240 PRO   BBB CB  
3864 C  CG  . PRO   B 241 ? 0.561 0.733 0.417 -0.053 -0.012 -0.173 240 PRO   BBB CG  
3865 C  CD  . PRO   B 241 ? 0.545 0.654 0.496 -0.130 -0.006 -0.266 240 PRO   BBB CD  
3866 N  N   . MET   B 242 ? 0.450 0.119 0.464 -0.066 0.014  -0.145 241 MET   BBB N   
3867 C  CA  . MET   B 242 ? 0.434 0.273 0.469 -0.128 -0.008 -0.088 241 MET   BBB CA  
3868 C  C   . MET   B 242 ? 0.462 0.200 0.355 -0.025 -0.072 -0.111 241 MET   BBB C   
3869 O  O   . MET   B 242 ? 0.470 0.147 0.403 0.014  -0.043 -0.117 241 MET   BBB O   
3870 C  CB  . MET   B 242 ? 0.425 0.212 0.445 -0.069 -0.003 -0.092 241 MET   BBB CB  
3871 C  CG  . MET   B 242 ? 0.449 0.170 0.627 0.010  0.063  -0.042 241 MET   BBB CG  
3872 S  SD  . MET   B 242 ? 0.445 0.171 0.499 -0.011 0.007  -0.025 241 MET   BBB SD  
3873 C  CE  . MET   B 242 ? 0.535 0.039 0.504 0.080  -0.008 -0.103 241 MET   BBB CE  
3874 N  N   . GLN   B 243 ? 0.448 0.180 0.482 0.015  0.009  -0.143 242 GLN   BBB N   
3875 C  CA  . GLN   B 243 ? 0.525 0.129 0.458 0.002  -0.013 -0.096 242 GLN   BBB CA  
3876 C  C   . GLN   B 243 ? 0.421 0.075 0.445 -0.049 0.053  -0.090 242 GLN   BBB C   
3877 O  O   . GLN   B 243 ? 0.475 0.319 0.410 -0.060 0.015  -0.074 242 GLN   BBB O   
3878 C  CB  . GLN   B 243 ? 0.625 0.229 0.641 -0.070 -0.083 -0.187 242 GLN   BBB CB  
3879 C  CG  . GLN   B 243 ? 0.745 0.229 0.911 -0.254 -0.221 -0.137 242 GLN   BBB CG  
3880 C  CD  . GLN   B 243 ? 0.683 0.221 0.941 -0.230 -0.107 -0.130 242 GLN   BBB CD  
3881 O  OE1 . GLN   B 243 ? 0.747 0.414 1.056 -0.303 -0.151 0.039  242 GLN   BBB OE1 
3882 N  NE2 . GLN   B 243 ? 0.821 0.721 1.048 -0.008 -0.182 0.127  242 GLN   BBB NE2 
3883 N  N   . HIS   B 244 ? 0.443 0.098 0.385 -0.017 0.038  -0.036 243 HIS   BBB N   
3884 C  CA  . HIS   B 244 ? 0.466 0.013 0.409 -0.055 0.018  0.006  243 HIS   BBB CA  
3885 C  C   . HIS   B 244 ? 0.427 0.134 0.394 -0.007 -0.007 -0.021 243 HIS   BBB C   
3886 O  O   . HIS   B 244 ? 0.497 0.067 0.434 0.041  -0.059 -0.092 243 HIS   BBB O   
3887 C  CB  . HIS   B 244 ? 0.510 0.009 0.518 -0.029 -0.041 -0.016 243 HIS   BBB CB  
3888 C  CG  . HIS   B 244 ? 0.586 0.028 0.696 -0.029 0.017  -0.119 243 HIS   BBB CG  
3889 N  ND1 . HIS   B 244 ? 0.560 0.192 0.809 0.028  -0.022 -0.095 243 HIS   BBB ND1 
3890 C  CD2 . HIS   B 244 ? 0.898 0.019 0.782 -0.042 -0.010 -0.091 243 HIS   BBB CD2 
3891 C  CE1 . HIS   B 244 ? 0.617 0.348 0.785 -0.009 -0.127 -0.159 243 HIS   BBB CE1 
3892 N  NE2 . HIS   B 244 ? 0.664 0.061 0.674 0.079  -0.102 -0.184 243 HIS   BBB NE2 
3893 N  N   . ASN   B 245 ? 0.439 0.012 0.414 0.009  -0.028 -0.035 244 ASN   BBB N   
3894 C  CA  . ASN   B 245 ? 0.421 0.009 0.405 -0.033 -0.017 0.014  244 ASN   BBB CA  
3895 C  C   . ASN   B 245 ? 0.455 0.129 0.399 -0.003 0.011  -0.000 244 ASN   BBB C   
3896 O  O   . ASN   B 245 ? 0.474 0.022 0.446 0.041  -0.013 -0.016 244 ASN   BBB O   
3897 C  CB  . ASN   B 245 ? 0.441 0.018 0.357 -0.016 -0.003 0.030  244 ASN   BBB CB  
3898 C  CG  . ASN   B 245 ? 0.416 0.111 0.282 -0.024 0.001  -0.029 244 ASN   BBB CG  
3899 O  OD1 . ASN   B 245 ? 0.424 0.009 0.345 -0.029 0.002  -0.011 244 ASN   BBB OD1 
3900 N  ND2 . ASN   B 245 ? 0.417 0.131 0.377 -0.048 -0.012 0.012  244 ASN   BBB ND2 
3901 N  N   . ASN   B 246 ? 0.433 0.016 0.395 -0.012 0.005  -0.061 245 ASN   BBB N   
3902 C  CA  . ASN   B 246 ? 0.417 0.016 0.479 0.044  -0.007 0.045  245 ASN   BBB CA  
3903 C  C   . ASN   B 246 ? 0.443 0.008 0.444 0.024  -0.061 -0.020 245 ASN   BBB C   
3904 O  O   . ASN   B 246 ? 0.568 0.024 0.561 -0.064 0.000  -0.075 245 ASN   BBB O   
3905 C  CB  . ASN   B 246 ? 0.436 0.013 0.454 -0.040 0.009  -0.037 245 ASN   BBB CB  
3906 C  CG  . ASN   B 246 ? 0.413 0.007 0.544 -0.012 -0.031 -0.014 245 ASN   BBB CG  
3907 O  OD1 . ASN   B 246 ? 0.612 0.283 0.567 -0.177 -0.004 0.067  245 ASN   BBB OD1 
3908 N  ND2 . ASN   B 246 ? 0.471 0.015 0.581 -0.062 -0.075 -0.005 245 ASN   BBB ND2 
3909 N  N   . ARG   B 247 ? 0.427 0.011 0.520 0.045  0.037  -0.008 246 ARG   BBB N   
3910 C  CA  . ARG   B 247 ? 0.456 0.035 0.451 0.098  0.053  -0.046 246 ARG   BBB CA  
3911 C  C   . ARG   B 247 ? 0.447 0.031 0.440 -0.102 0.014  -0.024 246 ARG   BBB C   
3912 O  O   . ARG   B 247 ? 0.485 0.018 0.477 -0.015 0.021  -0.074 246 ARG   BBB O   
3913 C  CB  . ARG   B 247 ? 0.442 0.026 0.419 0.079  0.052  -0.036 246 ARG   BBB CB  
3914 C  CG  . ARG   B 247 ? 0.527 0.022 0.427 0.074  0.015  -0.044 246 ARG   BBB CG  
3915 C  CD  . ARG   B 247 ? 0.488 0.043 0.415 0.132  0.041  -0.003 246 ARG   BBB CD  
3916 N  NE  . ARG   B 247 ? 0.507 0.040 0.505 0.088  0.033  -0.091 246 ARG   BBB NE  
3917 C  CZ  . ARG   B 247 ? 0.490 0.047 0.577 0.115  -0.024 -0.092 246 ARG   BBB CZ  
3918 N  NH1 . ARG   B 247 ? 0.550 0.008 0.543 -0.010 0.004  0.025  246 ARG   BBB NH1 
3919 N  NH2 . ARG   B 247 ? 0.642 0.007 0.693 0.022  0.130  0.006  246 ARG   BBB NH2 
3920 N  N   . PRO   B 248 ? 0.498 0.015 0.482 -0.040 0.040  -0.054 247 PRO   BBB N   
3921 C  CA  . PRO   B 248 ? 0.523 0.028 0.501 0.097  0.051  -0.030 247 PRO   BBB CA  
3922 C  C   . PRO   B 248 ? 0.779 0.024 0.881 0.037  0.035  -0.116 247 PRO   BBB C   
3923 O  O   . PRO   B 248 ? 0.677 0.017 0.652 0.054  -0.027 -0.067 247 PRO   BBB O   
3924 C  CB  . PRO   B 248 ? 0.543 0.012 0.573 -0.010 0.014  -0.054 247 PRO   BBB CB  
3925 C  CG  . PRO   B 248 ? 0.670 0.022 0.509 -0.092 0.091  -0.051 247 PRO   BBB CG  
3926 C  CD  . PRO   B 248 ? 0.558 0.018 0.437 -0.079 0.024  0.016  247 PRO   BBB CD  
3927 N  N   . THR   B 249 ? 0.702 0.008 0.816 -0.012 0.091  -0.041 248 THR   BBB N   
3928 C  CA  . THR   B 249 ? 0.568 0.013 0.601 -0.001 0.161  0.061  248 THR   BBB CA  
3929 C  C   . THR   B 249 ? 0.437 0.009 0.582 0.023  0.035  0.027  248 THR   BBB C   
3930 O  O   . THR   B 249 ? 0.643 0.008 0.538 -0.034 0.067  0.003  248 THR   BBB O   
3931 C  CB  . THR   B 249 ? 0.522 0.011 0.506 0.019  0.031  -0.042 248 THR   BBB CB  
3932 O  OG1 . THR   B 249 ? 0.548 0.112 0.493 -0.025 0.059  0.080  248 THR   BBB OG1 
3933 C  CG2 . THR   B 249 ? 0.511 0.021 0.579 0.005  0.024  0.091  248 THR   BBB CG2 
3934 N  N   . GLN   B 250 ? 0.447 0.034 0.559 0.087  0.052  0.087  249 GLN   BBB N   
3935 C  CA  . GLN   B 250 ? 0.405 0.014 0.532 0.043  0.028  0.040  249 GLN   BBB CA  
3936 C  C   . GLN   B 250 ? 0.465 0.056 0.545 0.090  0.083  0.137  249 GLN   BBB C   
3937 O  O   . GLN   B 250 ? 0.960 0.016 0.720 0.030  0.069  0.079  249 GLN   BBB O   
3938 C  CB  . GLN   B 250 ? 0.473 0.032 0.540 0.066  0.038  0.098  249 GLN   BBB CB  
3939 C  CG  . GLN   B 250 ? 0.572 0.027 0.525 0.050  -0.032 0.064  249 GLN   BBB CG  
3940 C  CD  . GLN   B 250 ? 0.521 0.144 0.462 0.038  -0.011 0.015  249 GLN   BBB CD  
3941 O  OE1 . GLN   B 250 ? 0.573 0.007 0.580 0.015  -0.025 0.009  249 GLN   BBB OE1 
3942 N  NE2 . GLN   B 250 ? 0.663 0.150 0.506 0.055  0.107  -0.105 249 GLN   BBB NE2 
3943 N  N   . PRO   B 251 ? 0.639 0.019 0.527 0.084  0.057  0.030  250 PRO   BBB N   
3944 C  CA  . PRO   B 251 ? 0.656 0.191 0.509 0.037  0.036  -0.001 250 PRO   BBB CA  
3945 C  C   . PRO   B 251 ? 0.624 0.031 0.538 0.100  0.055  0.066  250 PRO   BBB C   
3946 O  O   . PRO   B 251 ? 0.570 0.075 0.486 0.092  0.005  0.042  250 PRO   BBB O   
3947 C  CB  . PRO   B 251 ? 0.834 0.224 0.572 0.168  -0.009 0.062  250 PRO   BBB CB  
3948 C  CG  . PRO   B 251 ? 0.889 0.044 0.569 0.168  0.016  0.060  250 PRO   BBB CG  
3949 C  CD  . PRO   B 251 ? 0.756 0.016 0.532 0.077  0.018  0.029  250 PRO   BBB CD  
3950 N  N   . LEU   B 252 ? 0.615 0.131 0.518 0.063  0.091  0.103  251 LEU   BBB N   
3951 C  CA  . LEU   B 252 ? 0.657 0.197 0.617 0.134  -0.024 0.088  251 LEU   BBB CA  
3952 C  C   . LEU   B 252 ? 0.672 0.061 0.578 0.140  -0.014 0.117  251 LEU   BBB C   
3953 O  O   . LEU   B 252 ? 0.820 0.007 0.616 0.020  -0.030 -0.007 251 LEU   BBB O   
3954 C  CB  . LEU   B 252 ? 0.800 0.177 0.636 0.180  0.004  0.067  251 LEU   BBB CB  
3955 C  CG  . LEU   B 252 ? 0.752 0.160 0.605 0.035  0.016  0.139  251 LEU   BBB CG  
3956 C  CD1 . LEU   B 252 ? 0.610 0.142 0.619 0.162  -0.009 0.058  251 LEU   BBB CD1 
3957 C  CD2 . LEU   B 252 ? 0.659 0.329 0.659 0.080  0.044  0.061  251 LEU   BBB CD2 
3958 N  N   . LYS   B 253 ? 0.882 0.118 0.660 0.110  0.028  0.256  252 LYS   BBB N   
3959 C  CA  . LYS   B 253 ? 0.788 0.140 0.728 0.138  -0.027 0.276  252 LYS   BBB CA  
3960 C  C   . LYS   B 253 ? 1.033 0.049 1.053 0.132  0.007  0.164  252 LYS   BBB C   
3961 O  O   . LYS   B 253 ? 0.775 0.080 0.792 0.170  -0.085 0.047  252 LYS   BBB O   
3962 C  CB  . LYS   B 253 ? 0.621 0.082 0.648 0.104  -0.074 0.087  252 LYS   BBB CB  
3963 C  CG  . LYS   B 253 ? 0.793 0.009 0.858 -0.046 0.048  -0.005 252 LYS   BBB CG  
3964 C  CD  . LYS   B 253 ? 1.092 0.037 1.021 0.109  0.157  -0.124 252 LYS   BBB CD  
3965 C  CE  . LYS   B 253 ? 1.141 0.718 0.856 -0.078 -0.054 -0.284 252 LYS   BBB CE  
3966 N  NZ  . LYS   B 253 ? 1.282 0.976 0.752 0.067  -0.071 -0.482 252 LYS   BBB NZ  
3967 N  N   . GLY   B 254 ? 0.856 0.044 1.059 0.107  0.041  0.165  253 GLY   BBB N   
3968 C  CA  . GLY   B 254 ? 0.700 0.052 0.873 0.147  0.043  0.120  253 GLY   BBB CA  
3969 C  C   . GLY   B 254 ? 0.708 0.028 0.711 0.122  -0.137 -0.044 253 GLY   BBB C   
3970 O  O   . GLY   B 254 ? 0.814 0.015 0.719 0.032  -0.153 0.065  253 GLY   BBB O   
3971 N  N   . ARG   B 255 ? 0.686 0.115 0.609 0.163  -0.046 -0.014 254 ARG   BBB N   
3972 C  CA  . ARG   B 255 ? 0.529 0.104 0.507 0.046  -0.032 0.037  254 ARG   BBB CA  
3973 C  C   . ARG   B 255 ? 0.530 0.151 0.494 -0.010 -0.027 0.054  254 ARG   BBB C   
3974 O  O   . ARG   B 255 ? 0.619 0.084 0.561 0.022  0.005  0.136  254 ARG   BBB O   
3975 C  CB  . ARG   B 255 ? 0.562 0.024 0.480 0.080  0.013  0.057  254 ARG   BBB CB  
3976 C  CG  . ARG   B 255 ? 0.595 0.052 0.538 0.086  0.043  0.031  254 ARG   BBB CG  
3977 C  CD  . ARG   B 255 ? 0.591 0.152 0.513 0.062  -0.012 0.024  254 ARG   BBB CD  
3978 N  NE  . ARG   B 255 ? 0.608 0.051 0.535 0.125  -0.020 0.095  254 ARG   BBB NE  
3979 C  CZ  . ARG   B 255 ? 0.458 0.119 0.470 0.027  0.029  0.187  254 ARG   BBB CZ  
3980 N  NH1 . ARG   B 255 ? 0.528 0.062 0.467 0.073  0.001  0.134  254 ARG   BBB NH1 
3981 N  NH2 . ARG   B 255 ? 0.518 0.048 0.536 0.104  0.041  0.111  254 ARG   BBB NH2 
3982 N  N   . THR   B 256 ? 0.541 0.104 0.453 0.075  -0.038 0.046  255 THR   BBB N   
3983 C  CA  . THR   B 256 ? 0.572 0.029 0.498 0.084  0.003  0.072  255 THR   BBB CA  
3984 C  C   . THR   B 256 ? 0.502 0.101 0.468 0.124  0.014  0.070  255 THR   BBB C   
3985 O  O   . THR   B 256 ? 0.571 0.090 0.530 0.042  -0.007 0.057  255 THR   BBB O   
3986 C  CB  . THR   B 256 ? 0.529 0.369 0.520 0.072  -0.110 0.165  255 THR   BBB CB  
3987 O  OG1 . THR   B 256 ? 0.847 0.488 0.501 0.317  -0.003 0.048  255 THR   BBB OG1 
3988 C  CG2 . THR   B 256 ? 0.563 0.472 0.605 0.083  -0.124 0.130  255 THR   BBB CG2 
3989 N  N   . VAL   B 257 ? 0.464 0.040 0.583 0.117  -0.032 0.036  256 VAL   BBB N   
3990 C  CA  . VAL   B 257 ? 0.420 0.044 0.481 0.107  0.085  0.090  256 VAL   BBB CA  
3991 C  C   . VAL   B 257 ? 0.426 0.229 0.466 -0.053 0.024  0.090  256 VAL   BBB C   
3992 O  O   . VAL   B 257 ? 0.614 0.011 0.546 0.005  0.000  0.051  256 VAL   BBB O   
3993 C  CB  . VAL   B 257 ? 0.449 0.042 0.446 0.057  0.016  0.093  256 VAL   BBB CB  
3994 C  CG1 . VAL   B 257 ? 0.452 0.036 0.480 0.036  -0.004 0.113  256 VAL   BBB CG1 
3995 C  CG2 . VAL   B 257 ? 0.471 0.263 0.400 0.030  -0.041 0.084  256 VAL   BBB CG2 
3996 N  N   . ARG   B 258 ? 0.432 0.191 0.431 -0.006 -0.032 0.122  257 ARG   BBB N   
3997 C  CA  . ARG   B 258 ? 0.412 0.194 0.424 0.038  -0.040 0.090  257 ARG   BBB CA  
3998 C  C   . ARG   B 258 ? 0.420 0.087 0.326 -0.022 -0.017 0.089  257 ARG   BBB C   
3999 O  O   . ARG   B 258 ? 0.442 0.253 0.356 0.034  -0.052 0.098  257 ARG   BBB O   
4000 C  CB  . ARG   B 258 ? 0.414 0.168 0.405 0.053  -0.033 0.087  257 ARG   BBB CB  
4001 C  CG  . ARG   B 258 ? 0.378 0.327 0.418 0.046  -0.095 0.031  257 ARG   BBB CG  
4002 C  CD  . ARG   B 258 ? 0.419 0.296 0.466 0.053  -0.039 0.058  257 ARG   BBB CD  
4003 N  NE  . ARG   B 258 ? 0.444 0.167 0.523 0.032  0.047  0.094  257 ARG   BBB NE  
4004 C  CZ  . ARG   B 258 ? 0.369 0.280 0.467 -0.020 -0.031 0.098  257 ARG   BBB CZ  
4005 N  NH1 . ARG   B 258 ? 0.521 0.259 0.490 -0.008 -0.048 0.073  257 ARG   BBB NH1 
4006 N  NH2 . ARG   B 258 ? 0.514 0.232 0.538 0.041  -0.035 0.150  257 ARG   BBB NH2 
4007 N  N   . ALA   B 259 ? 0.416 0.194 0.374 -0.021 0.016  0.029  258 ALA   BBB N   
4008 C  CA  . ALA   B 259 ? 0.429 0.186 0.415 0.008  -0.019 0.019  258 ALA   BBB CA  
4009 C  C   . ALA   B 259 ? 0.387 0.148 0.394 0.013  -0.038 0.047  258 ALA   BBB C   
4010 O  O   . ALA   B 259 ? 0.457 0.135 0.408 -0.005 -0.030 0.058  258 ALA   BBB O   
4011 C  CB  . ALA   B 259 ? 0.394 0.244 0.466 0.059  0.016  -0.002 258 ALA   BBB CB  
4012 N  N   . SER   B 260 ? 0.378 0.215 0.351 0.034  -0.065 0.056  259 SER   BBB N   
4013 C  CA  . SER   B 260 ? 0.406 0.217 0.314 0.006  -0.054 0.057  259 SER   BBB CA  
4014 C  C   . SER   B 260 ? 0.398 0.279 0.330 -0.036 -0.068 0.051  259 SER   BBB C   
4015 O  O   . SER   B 260 ? 0.491 0.218 0.443 -0.017 -0.089 0.033  259 SER   BBB O   
4016 C  CB  . SER   B 260 ? 0.411 0.081 0.334 -0.046 -0.036 0.031  259 SER   BBB CB  
4017 O  OG  . SER   B 260 ? 0.446 0.077 0.413 0.036  -0.070 0.004  259 SER   BBB OG  
4018 N  N   . PHE   B 261 ? 0.432 0.135 0.428 -0.047 -0.084 0.016  260 PHE   BBB N   
4019 C  CA  . PHE   B 261 ? 0.567 0.389 0.451 -0.037 -0.041 0.053  260 PHE   BBB CA  
4020 C  C   . PHE   B 261 ? 0.551 0.450 0.381 0.054  0.050  0.079  260 PHE   BBB C   
4021 O  O   . PHE   B 261 ? 0.722 0.523 0.364 -0.095 0.104  0.044  260 PHE   BBB O   
4022 C  CB  . PHE   B 261 ? 0.589 0.431 0.468 -0.063 -0.040 0.040  260 PHE   BBB CB  
4023 C  CG  . PHE   B 261 ? 0.487 0.402 0.457 -0.062 -0.043 0.098  260 PHE   BBB CG  
4024 C  CD1 . PHE   B 261 ? 0.502 0.073 0.447 -0.004 -0.046 0.106  260 PHE   BBB CD1 
4025 C  CD2 . PHE   B 261 ? 0.565 0.336 0.441 -0.086 0.012  -0.012 260 PHE   BBB CD2 
4026 C  CE1 . PHE   B 261 ? 0.507 0.260 0.452 -0.019 -0.044 0.033  260 PHE   BBB CE1 
4027 C  CE2 . PHE   B 261 ? 0.499 0.325 0.379 -0.063 -0.020 0.008  260 PHE   BBB CE2 
4028 C  CZ  . PHE   B 261 ? 0.513 0.128 0.425 0.062  0.026  -0.030 260 PHE   BBB CZ  
4029 O  OXT . PHE   B 261 ? 0.611 0.276 0.455 -0.056 -0.045 0.162  260 PHE   BBB OXT 
4030 ZN ZN  . ZN    C .   ? 0.383 0.043 0.377 0.009  0.002  -0.051 301 ZN    AAA ZN  
4031 O  O   . A1H1P D .   ? 0.376 0.110 0.371 -0.004 -0.008 -0.053 302 A1H1P AAA O   
4032 C  C1  . A1H1P D .   ? 0.404 0.057 0.412 0.007  0.044  -0.075 302 A1H1P AAA C1  
4033 O  O4  . A1H1P D .   ? 0.381 0.106 0.515 -0.007 -0.012 -0.084 302 A1H1P AAA O4  
4034 S  S   . A1H1P D .   ? 0.369 0.192 0.365 -0.035 0.018  -0.071 302 A1H1P AAA S   
4035 O  O3  . A1H1P D .   ? 0.367 0.305 0.321 0.033  0.052  -0.053 302 A1H1P AAA O3  
4036 N  N   . A1H1P D .   ? 0.378 0.219 0.337 -0.000 -0.027 -0.177 302 A1H1P AAA N   
4037 C  C   . A1H1P D .   ? 0.474 0.138 0.364 -0.011 -0.010 -0.080 302 A1H1P AAA C   
4038 C  C16 . A1H1P D .   ? 0.385 0.264 0.330 0.059  0.026  -0.060 302 A1H1P AAA C16 
4039 C  C6  . A1H1P D .   ? 0.422 0.191 0.375 0.058  0.053  -0.025 302 A1H1P AAA C6  
4040 C  C4  . A1H1P D .   ? 0.377 0.291 0.353 0.049  0.046  -0.024 302 A1H1P AAA C4  
4041 O  O1  . A1H1P D .   ? 0.423 0.118 0.372 0.044  0.029  -0.016 302 A1H1P AAA O1  
4042 C  C5  . A1H1P D .   ? 0.418 0.096 0.370 0.046  0.059  -0.000 302 A1H1P AAA C5  
4043 C  C2  . A1H1P D .   ? 0.379 0.185 0.348 0.062  0.061  -0.018 302 A1H1P AAA C2  
4044 C  C3  . A1H1P D .   ? 0.384 0.084 0.365 -0.062 -0.012 -0.098 302 A1H1P AAA C3  
4045 C  C7  . A1H1P D .   ? 0.501 0.424 0.415 0.100  -0.014 -0.058 302 A1H1P AAA C7  
4046 O  O2  . A1H1P D .   ? 0.563 0.499 0.562 0.197  0.099  0.057  302 A1H1P AAA O2  
4047 N  N1  . A1H1P D .   ? 0.810 0.669 0.524 0.168  -0.265 -0.214 302 A1H1P AAA N1  
4048 C  C8  . A1H1P D .   ? 0.897 0.690 0.566 0.204  -0.116 -0.203 302 A1H1P AAA C8  
4049 C  C9  . A1H1P D .   ? 0.948 0.675 0.686 0.145  0.166  -0.173 302 A1H1P AAA C9  
4050 N  N2  . A1H1P D .   ? 0.984 0.825 0.673 0.118  0.273  -0.240 302 A1H1P AAA N2  
4051 C  C13 . A1H1P D .   ? 1.109 0.209 1.053 0.080  0.278  -0.383 302 A1H1P AAA C13 
4052 C  C14 . A1H1P D .   ? 1.204 0.222 0.764 -0.234 0.199  -0.001 302 A1H1P AAA C14 
4053 C  C15 . A1H1P D .   ? 1.226 0.287 0.789 -0.013 0.030  0.304  302 A1H1P AAA C15 
4054 C  C12 . A1H1P D .   ? 1.080 0.769 0.814 -0.058 0.272  -0.281 302 A1H1P AAA C12 
4055 C  C11 . A1H1P D .   ? 1.015 0.937 0.586 0.091  0.201  -0.129 302 A1H1P AAA C11 
4056 C  C10 . A1H1P D .   ? 0.837 0.475 0.443 -0.139 0.085  0.128  302 A1H1P AAA C10 
4057 ZN ZN  . ZN    E .   ? 0.398 0.006 0.395 0.005  -0.003 0.002  301 ZN    BBB ZN  
4058 O  O   . A1H1P F .   ? 0.439 0.009 0.379 -0.021 -0.011 0.024  302 A1H1P BBB O   
4059 C  C1  . A1H1P F .   ? 0.409 0.100 0.356 -0.003 0.039  -0.035 302 A1H1P BBB C1  
4060 O  O4  . A1H1P F .   ? 0.357 0.087 0.473 0.096  -0.025 -0.028 302 A1H1P BBB O4  
4061 S  S   . A1H1P F .   ? 0.341 0.104 0.380 0.080  0.020  -0.005 302 A1H1P BBB S   
4062 O  O3  . A1H1P F .   ? 0.345 0.097 0.321 -0.021 0.018  -0.011 302 A1H1P BBB O3  
4063 N  N   . A1H1P F .   ? 0.298 0.169 0.383 -0.041 -0.001 0.173  302 A1H1P BBB N   
4064 C  C   . A1H1P F .   ? 0.414 0.053 0.331 0.061  0.027  -0.033 302 A1H1P BBB C   
4065 C  C16 . A1H1P F .   ? 0.412 0.006 0.350 -0.007 0.055  -0.004 302 A1H1P BBB C16 
4066 C  C6  . A1H1P F .   ? 0.446 0.096 0.363 -0.032 0.081  0.017  302 A1H1P BBB C6  
4067 C  C4  . A1H1P F .   ? 0.438 0.137 0.350 -0.041 0.009  0.056  302 A1H1P BBB C4  
4068 O  O1  . A1H1P F .   ? 0.482 0.025 0.477 -0.045 0.062  0.032  302 A1H1P BBB O1  
4069 C  C5  . A1H1P F .   ? 0.407 0.196 0.421 -0.074 0.021  0.006  302 A1H1P BBB C5  
4070 C  C2  . A1H1P F .   ? 0.389 0.122 0.380 -0.036 0.039  -0.010 302 A1H1P BBB C2  
4071 C  C3  . A1H1P F .   ? 0.433 0.015 0.376 -0.059 -0.048 0.009  302 A1H1P BBB C3  
4072 C  C7  . A1H1P F .   ? 0.608 0.209 0.347 -0.078 0.022  0.094  302 A1H1P BBB C7  
4073 O  O2  . A1H1P F .   ? 0.682 0.457 0.455 -0.083 0.028  -0.150 302 A1H1P BBB O2  
4074 N  N1  . A1H1P F .   ? 0.628 0.480 0.413 0.127  -0.015 0.075  302 A1H1P BBB N1  
4075 C  C8  . A1H1P F .   ? 0.582 0.338 0.384 -0.034 -0.040 0.083  302 A1H1P BBB C8  
4076 C  C9  . A1H1P F .   ? 0.677 0.387 0.469 -0.061 0.025  0.125  302 A1H1P BBB C9  
4077 N  N2  . A1H1P F .   ? 0.648 0.410 0.538 -0.011 0.101  -0.003 302 A1H1P BBB N2  
4078 C  C13 . A1H1P F .   ? 0.764 0.310 0.741 0.022  -0.031 -0.024 302 A1H1P BBB C13 
4079 C  C14 . A1H1P F .   ? 0.795 0.146 0.724 -0.126 -0.046 0.016  302 A1H1P BBB C14 
4080 C  C15 . A1H1P F .   ? 1.072 0.229 0.729 0.068  0.048  0.048  302 A1H1P BBB C15 
4081 C  C12 . A1H1P F .   ? 0.563 0.565 0.582 -0.096 0.081  0.068  302 A1H1P BBB C12 
4082 C  C11 . A1H1P F .   ? 0.628 0.556 0.487 -0.052 0.023  0.102  302 A1H1P BBB C11 
4083 C  C10 . A1H1P F .   ? 0.619 0.424 0.500 -0.035 0.060  0.050  302 A1H1P BBB C10 
4084 O  O   . HOH   G .   ? 0.686 0.424 0.539 0.085  -0.029 -0.091 401 HOH   AAA O   
4085 O  O   . HOH   G .   ? 0.665 0.571 0.580 0.273  -0.019 0.048  402 HOH   AAA O   
4086 O  O   . HOH   G .   ? 1.019 0.211 1.079 0.114  0.095  0.223  403 HOH   AAA O   
4087 O  O   . HOH   G .   ? 1.277 0.068 0.610 0.136  -0.022 -0.082 404 HOH   AAA O   
4088 O  O   . HOH   G .   ? 0.428 0.368 0.346 0.081  0.044  0.014  405 HOH   AAA O   
4089 O  O   . HOH   G .   ? 0.439 0.015 0.465 0.034  0.000  -0.053 406 HOH   AAA O   
4090 O  O   . HOH   G .   ? 0.646 0.105 0.672 -0.023 0.002  -0.195 407 HOH   AAA O   
4091 O  O   . HOH   G .   ? 0.528 0.272 0.634 -0.119 0.010  -0.114 408 HOH   AAA O   
4092 O  O   . HOH   G .   ? 0.481 0.145 0.403 0.067  0.004  -0.035 409 HOH   AAA O   
4093 O  O   . HOH   G .   ? 1.044 0.257 0.613 0.232  0.338  0.140  410 HOH   AAA O   
4094 O  O   . HOH   G .   ? 0.801 0.009 0.699 -0.026 0.025  -0.033 411 HOH   AAA O   
4095 O  O   . HOH   G .   ? 0.482 0.160 0.519 -0.087 0.075  -0.151 412 HOH   AAA O   
4096 O  O   . HOH   G .   ? 0.525 0.425 0.515 -0.125 0.056  -0.093 413 HOH   AAA O   
4097 O  O   . HOH   G .   ? 0.676 0.315 0.529 0.087  0.021  -0.017 414 HOH   AAA O   
4098 O  O   . HOH   G .   ? 0.826 0.235 0.838 0.211  -0.068 -0.062 415 HOH   AAA O   
4099 O  O   . HOH   G .   ? 0.437 0.204 0.391 0.030  0.008  -0.047 416 HOH   AAA O   
4100 O  O   . HOH   G .   ? 0.603 0.438 0.633 0.036  0.009  0.114  417 HOH   AAA O   
4101 O  O   . HOH   G .   ? 0.616 0.208 0.581 0.060  -0.047 0.044  418 HOH   AAA O   
4102 O  O   . HOH   G .   ? 0.464 0.181 0.468 0.066  0.037  0.002  419 HOH   AAA O   
4103 O  O   . HOH   G .   ? 0.466 0.311 0.469 0.087  0.000  0.011  420 HOH   AAA O   
4104 O  O   . HOH   G .   ? 0.500 0.177 0.641 0.025  0.032  -0.187 421 HOH   AAA O   
4105 O  O   . HOH   G .   ? 0.408 0.751 0.493 0.047  -0.057 -0.059 422 HOH   AAA O   
4106 O  O   . HOH   G .   ? 0.835 0.424 0.619 -0.069 0.161  -0.166 423 HOH   AAA O   
4107 O  O   . HOH   G .   ? 0.493 0.622 0.641 -0.053 -0.050 -0.025 424 HOH   AAA O   
4108 O  O   . HOH   G .   ? 0.777 0.076 0.806 -0.091 0.123  -0.229 425 HOH   AAA O   
4109 O  O   . HOH   G .   ? 0.421 0.206 0.471 -0.074 -0.024 -0.192 426 HOH   AAA O   
4110 O  O   . HOH   G .   ? 0.668 0.423 0.457 0.074  0.068  0.077  427 HOH   AAA O   
4111 O  O   . HOH   G .   ? 0.608 0.051 0.491 -0.011 0.006  -0.054 428 HOH   AAA O   
4112 O  O   . HOH   G .   ? 0.564 0.405 0.446 0.021  -0.025 -0.108 429 HOH   AAA O   
4113 O  O   . HOH   G .   ? 0.386 0.633 0.442 -0.023 -0.034 -0.039 430 HOH   AAA O   
4114 O  O   . HOH   G .   ? 0.639 0.453 0.534 0.001  -0.131 -0.121 431 HOH   AAA O   
4115 O  O   . HOH   G .   ? 0.617 0.140 0.927 0.009  0.007  -0.155 432 HOH   AAA O   
4116 O  O   . HOH   G .   ? 0.422 0.657 0.476 0.011  -0.023 -0.100 433 HOH   AAA O   
4117 O  O   . HOH   G .   ? 0.465 0.479 0.740 -0.003 0.151  -0.221 434 HOH   AAA O   
4118 O  O   . HOH   G .   ? 0.570 0.024 0.384 0.100  0.024  -0.001 435 HOH   AAA O   
4119 O  O   . HOH   G .   ? 0.413 0.157 0.339 -0.019 -0.036 -0.013 436 HOH   AAA O   
4120 O  O   . HOH   G .   ? 0.586 0.466 0.653 -0.020 -0.048 0.098  437 HOH   AAA O   
4121 O  O   . HOH   G .   ? 0.494 0.070 0.420 0.007  -0.011 -0.071 438 HOH   AAA O   
4122 O  O   . HOH   G .   ? 0.397 0.302 0.482 0.014  -0.030 -0.138 439 HOH   AAA O   
4123 O  O   . HOH   G .   ? 0.695 0.137 0.737 0.027  0.028  0.151  440 HOH   AAA O   
4124 O  O   . HOH   G .   ? 0.704 0.123 0.526 0.084  0.135  -0.026 441 HOH   AAA O   
4125 O  O   . HOH   G .   ? 0.646 0.571 0.571 0.169  -0.055 0.038  442 HOH   AAA O   
4126 O  O   . HOH   G .   ? 0.518 0.098 0.395 0.005  0.005  -0.005 443 HOH   AAA O   
4127 O  O   . HOH   G .   ? 1.130 0.014 0.681 0.075  0.044  0.042  444 HOH   AAA O   
4128 O  O   . HOH   G .   ? 0.616 0.205 0.664 -0.136 0.039  -0.079 445 HOH   AAA O   
4129 O  O   . HOH   G .   ? 0.491 0.157 0.488 -0.035 0.025  -0.074 446 HOH   AAA O   
4130 O  O   . HOH   G .   ? 0.616 0.164 0.552 0.002  -0.017 -0.045 447 HOH   AAA O   
4131 O  O   . HOH   G .   ? 0.540 0.417 0.393 -0.134 0.086  -0.071 448 HOH   AAA O   
4132 O  O   . HOH   G .   ? 0.638 0.089 0.519 -0.049 0.018  -0.113 449 HOH   AAA O   
4133 O  O   . HOH   G .   ? 0.540 0.204 0.589 -0.035 0.139  -0.157 450 HOH   AAA O   
4134 O  O   . HOH   G .   ? 0.888 0.462 0.491 -0.121 0.014  -0.112 451 HOH   AAA O   
4135 O  O   . HOH   G .   ? 0.599 0.200 0.576 -0.006 0.098  -0.120 452 HOH   AAA O   
4136 O  O   . HOH   G .   ? 0.491 0.460 0.471 0.024  -0.053 -0.100 453 HOH   AAA O   
4137 O  O   . HOH   G .   ? 0.686 0.387 0.575 -0.038 0.014  -0.120 454 HOH   AAA O   
4138 O  O   . HOH   G .   ? 0.519 0.147 0.436 0.040  0.049  -0.018 455 HOH   AAA O   
4139 O  O   . HOH   G .   ? 0.452 0.303 0.463 0.097  -0.040 -0.010 456 HOH   AAA O   
4140 O  O   . HOH   G .   ? 0.821 0.261 0.658 -0.244 0.132  0.002  457 HOH   AAA O   
4141 O  O   . HOH   G .   ? 0.666 0.179 0.554 0.119  0.037  -0.001 458 HOH   AAA O   
4142 O  O   . HOH   G .   ? 0.495 0.154 0.452 0.082  0.002  -0.023 459 HOH   AAA O   
4143 O  O   . HOH   G .   ? 0.559 0.659 0.579 0.009  0.101  -0.017 460 HOH   AAA O   
4144 O  O   . HOH   G .   ? 0.444 0.623 0.563 -0.052 0.008  -0.196 461 HOH   AAA O   
4145 O  O   . HOH   G .   ? 0.658 0.368 0.455 0.138  -0.054 0.021  462 HOH   AAA O   
4146 O  O   . HOH   G .   ? 0.594 0.361 0.658 0.056  -0.177 -0.076 463 HOH   AAA O   
4147 O  O   . HOH   G .   ? 0.514 0.048 0.625 -0.043 0.029  0.051  464 HOH   AAA O   
4148 O  O   . HOH   G .   ? 0.655 0.476 0.697 -0.122 -0.016 0.157  465 HOH   AAA O   
4149 O  O   . HOH   G .   ? 0.402 0.132 0.363 0.027  -0.011 -0.021 466 HOH   AAA O   
4150 O  O   . HOH   G .   ? 0.527 0.422 0.426 0.019  -0.041 -0.129 467 HOH   AAA O   
4151 O  O   . HOH   G .   ? 0.607 0.142 0.449 0.024  0.085  0.029  468 HOH   AAA O   
4152 O  O   . HOH   G .   ? 0.619 0.306 0.590 0.037  0.077  -0.242 469 HOH   AAA O   
4153 O  O   . HOH   G .   ? 1.024 0.019 0.564 0.049  0.296  -0.055 470 HOH   AAA O   
4154 O  O   . HOH   G .   ? 0.623 0.418 0.516 0.009  -0.011 -0.302 471 HOH   AAA O   
4155 O  O   . HOH   G .   ? 0.455 0.384 0.460 0.011  0.090  -0.099 472 HOH   AAA O   
4156 O  O   . HOH   G .   ? 0.731 0.060 0.802 0.024  0.066  -0.198 473 HOH   AAA O   
4157 O  O   . HOH   G .   ? 0.558 0.383 0.490 0.145  0.030  -0.035 474 HOH   AAA O   
4158 O  O   . HOH   G .   ? 0.353 0.203 0.480 0.093  -0.059 -0.042 475 HOH   AAA O   
4159 O  O   . HOH   G .   ? 0.608 0.174 0.668 0.016  -0.001 -0.236 476 HOH   AAA O   
4160 O  O   . HOH   G .   ? 0.531 0.784 0.462 -0.131 0.008  -0.188 477 HOH   AAA O   
4161 O  O   . HOH   G .   ? 0.534 0.324 0.556 -0.020 -0.038 -0.177 478 HOH   AAA O   
4162 O  O   . HOH   G .   ? 0.524 0.300 0.339 0.048  0.022  -0.037 479 HOH   AAA O   
4163 O  O   . HOH   G .   ? 0.521 0.050 0.550 -0.096 0.075  -0.076 480 HOH   AAA O   
4164 O  O   . HOH   G .   ? 0.520 0.032 0.594 -0.044 0.009  0.046  481 HOH   AAA O   
4165 O  O   . HOH   G .   ? 0.605 0.327 0.458 0.050  -0.032 -0.024 482 HOH   AAA O   
4166 O  O   . HOH   G .   ? 0.489 0.440 0.414 0.086  -0.042 -0.183 483 HOH   AAA O   
4167 O  O   . HOH   G .   ? 0.537 0.188 0.642 -0.063 0.082  -0.218 484 HOH   AAA O   
4168 O  O   . HOH   G .   ? 0.441 0.360 0.544 0.020  -0.043 -0.120 485 HOH   AAA O   
4169 O  O   . HOH   G .   ? 0.671 0.146 0.462 -0.109 0.067  -0.071 486 HOH   AAA O   
4170 O  O   . HOH   G .   ? 0.691 0.342 0.531 -0.148 0.063  0.129  487 HOH   AAA O   
4171 O  O   . HOH   G .   ? 0.602 0.338 0.545 -0.033 -0.011 0.056  488 HOH   AAA O   
4172 O  O   . HOH   G .   ? 0.675 0.110 0.529 0.026  -0.001 -0.135 489 HOH   AAA O   
4173 O  O   . HOH   G .   ? 0.577 0.168 0.593 -0.040 0.133  -0.176 490 HOH   AAA O   
4174 O  O   . HOH   G .   ? 0.521 0.161 0.473 0.060  0.013  -0.047 491 HOH   AAA O   
4175 O  O   . HOH   G .   ? 0.674 0.105 0.513 0.084  0.028  -0.077 492 HOH   AAA O   
4176 O  O   . HOH   G .   ? 0.548 0.456 0.501 0.112  0.112  -0.269 493 HOH   AAA O   
4177 O  O   . HOH   G .   ? 0.728 0.195 0.516 0.056  -0.005 -0.104 494 HOH   AAA O   
4178 O  O   . HOH   G .   ? 0.559 0.267 0.619 0.094  0.067  -0.118 495 HOH   AAA O   
4179 O  O   . HOH   G .   ? 0.607 0.264 0.455 -0.192 0.080  -0.097 496 HOH   AAA O   
4180 O  O   . HOH   G .   ? 0.515 0.397 0.473 -0.020 -0.046 -0.004 497 HOH   AAA O   
4181 O  O   . HOH   G .   ? 0.462 0.161 0.419 0.049  -0.057 -0.068 498 HOH   AAA O   
4182 O  O   . HOH   G .   ? 0.756 0.144 0.669 0.131  0.161  0.068  499 HOH   AAA O   
4183 O  O   . HOH   G .   ? 0.941 0.762 0.517 0.170  0.217  0.009  500 HOH   AAA O   
4184 O  O   . HOH   G .   ? 0.436 0.210 0.427 0.071  0.042  -0.036 501 HOH   AAA O   
4185 O  O   . HOH   G .   ? 0.455 0.371 0.657 -0.098 -0.002 -0.013 502 HOH   AAA O   
4186 O  O   . HOH   G .   ? 0.513 0.109 0.473 -0.001 0.055  -0.125 503 HOH   AAA O   
4187 O  O   . HOH   G .   ? 0.648 0.366 0.539 0.098  -0.028 -0.106 504 HOH   AAA O   
4188 O  O   . HOH   G .   ? 0.844 0.184 0.716 -0.064 -0.049 0.000  505 HOH   AAA O   
4189 O  O   . HOH   G .   ? 0.445 0.816 0.473 0.015  0.010  -0.148 506 HOH   AAA O   
4190 O  O   . HOH   G .   ? 0.334 0.291 0.479 0.012  -0.029 -0.131 507 HOH   AAA O   
4191 O  O   . HOH   G .   ? 0.541 0.224 0.830 0.173  -0.024 -0.092 508 HOH   AAA O   
4192 O  O   . HOH   G .   ? 0.659 0.233 0.612 -0.144 -0.020 -0.163 509 HOH   AAA O   
4193 O  O   . HOH   G .   ? 0.584 0.297 0.821 -0.139 0.240  -0.276 510 HOH   AAA O   
4194 O  O   . HOH   G .   ? 0.442 0.275 0.466 0.006  -0.039 0.018  511 HOH   AAA O   
4195 O  O   . HOH   G .   ? 0.767 0.212 0.790 0.040  -0.005 -0.269 512 HOH   AAA O   
4196 O  O   . HOH   G .   ? 0.670 0.033 0.440 -0.031 -0.020 0.001  513 HOH   AAA O   
4197 O  O   . HOH   G .   ? 0.451 0.585 0.457 0.162  -0.038 -0.027 514 HOH   AAA O   
4198 O  O   . HOH   G .   ? 0.422 0.168 0.393 0.020  0.088  -0.075 515 HOH   AAA O   
4199 O  O   . HOH   G .   ? 0.793 0.409 0.607 -0.058 0.041  0.061  516 HOH   AAA O   
4200 O  O   . HOH   G .   ? 0.532 0.194 0.549 -0.064 0.062  0.032  517 HOH   AAA O   
4201 O  O   . HOH   G .   ? 0.517 0.458 0.574 0.038  0.001  0.116  518 HOH   AAA O   
4202 O  O   . HOH   G .   ? 0.628 0.928 0.644 -0.059 -0.117 0.109  519 HOH   AAA O   
4203 O  O   . HOH   G .   ? 0.726 0.231 0.588 0.044  0.018  0.019  520 HOH   AAA O   
4204 O  O   . HOH   G .   ? 0.649 0.264 0.493 -0.061 -0.043 -0.069 521 HOH   AAA O   
4205 O  O   . HOH   G .   ? 0.558 0.561 0.511 0.006  -0.134 -0.066 522 HOH   AAA O   
4206 O  O   . HOH   G .   ? 1.060 0.232 0.735 -0.038 0.176  0.069  523 HOH   AAA O   
4207 O  O   . HOH   G .   ? 0.615 0.740 0.430 -0.160 0.075  -0.064 524 HOH   AAA O   
4208 O  O   . HOH   G .   ? 0.584 0.528 0.667 -0.071 0.067  -0.153 525 HOH   AAA O   
4209 O  O   . HOH   G .   ? 0.998 0.071 0.772 -0.163 0.085  -0.184 526 HOH   AAA O   
4210 O  O   . HOH   G .   ? 0.722 0.636 0.665 0.021  -0.005 0.223  527 HOH   AAA O   
4211 O  O   . HOH   G .   ? 0.845 0.062 0.758 -0.070 -0.024 0.011  528 HOH   AAA O   
4212 O  O   . HOH   G .   ? 0.553 0.335 0.483 -0.015 0.059  -0.164 529 HOH   AAA O   
4213 O  O   . HOH   G .   ? 0.582 0.433 0.539 0.175  -0.003 0.094  530 HOH   AAA O   
4214 O  O   . HOH   G .   ? 0.759 0.481 0.619 0.167  -0.101 -0.195 531 HOH   AAA O   
4215 O  O   . HOH   G .   ? 0.607 0.726 0.440 0.026  0.048  -0.124 532 HOH   AAA O   
4216 O  O   . HOH   G .   ? 0.534 0.382 0.442 0.017  -0.013 -0.042 533 HOH   AAA O   
4217 O  O   . HOH   G .   ? 0.475 0.320 0.667 -0.009 0.037  0.062  534 HOH   AAA O   
4218 O  O   . HOH   H .   ? 0.515 0.028 0.329 -0.104 -0.052 -0.005 401 HOH   BBB O   
4219 O  O   . HOH   H .   ? 0.786 0.731 0.414 0.370  0.157  0.105  402 HOH   BBB O   
4220 O  O   . HOH   H .   ? 0.673 0.252 0.724 -0.013 -0.038 0.018  403 HOH   BBB O   
4221 O  O   . HOH   H .   ? 0.461 0.007 0.555 0.010  -0.005 -0.009 404 HOH   BBB O   
4222 O  O   . HOH   H .   ? 0.602 0.175 0.871 -0.080 0.058  -0.123 405 HOH   BBB O   
4223 O  O   . HOH   H .   ? 0.461 0.453 0.403 0.050  -0.024 0.037  406 HOH   BBB O   
4224 O  O   . HOH   H .   ? 0.475 0.126 0.475 -0.031 -0.046 0.058  407 HOH   BBB O   
4225 O  O   . HOH   H .   ? 0.505 0.141 0.545 -0.160 0.062  -0.197 408 HOH   BBB O   
4226 O  O   . HOH   H .   ? 0.632 0.068 0.370 0.012  0.029  -0.021 409 HOH   BBB O   
4227 O  O   . HOH   H .   ? 0.462 0.325 0.416 -0.013 0.017  0.106  410 HOH   BBB O   
4228 O  O   . HOH   H .   ? 1.143 0.342 0.503 0.192  -0.172 0.022  411 HOH   BBB O   
4229 O  O   . HOH   H .   ? 0.715 0.156 0.670 0.118  0.107  -0.213 412 HOH   BBB O   
4230 O  O   . HOH   H .   ? 0.826 0.443 0.820 0.299  0.129  0.176  413 HOH   BBB O   
4231 O  O   . HOH   H .   ? 0.612 0.346 0.480 0.004  0.026  0.043  414 HOH   BBB O   
4232 O  O   . HOH   H .   ? 0.637 0.153 0.598 0.056  0.096  0.028  415 HOH   BBB O   
4233 O  O   . HOH   H .   ? 0.726 0.477 0.484 0.038  0.037  -0.092 416 HOH   BBB O   
4234 O  O   . HOH   H .   ? 0.419 0.014 0.410 -0.020 -0.023 0.005  417 HOH   BBB O   
4235 O  O   . HOH   H .   ? 0.641 0.190 0.434 -0.165 0.004  -0.072 418 HOH   BBB O   
4236 O  O   . HOH   H .   ? 0.924 0.479 0.690 0.175  -0.208 0.127  419 HOH   BBB O   
4237 O  O   . HOH   H .   ? 0.443 0.216 0.561 0.013  -0.038 0.171  420 HOH   BBB O   
4238 O  O   . HOH   H .   ? 0.902 0.207 0.879 0.315  -0.024 0.036  421 HOH   BBB O   
4239 O  O   . HOH   H .   ? 0.622 0.357 0.659 -0.010 -0.005 -0.276 422 HOH   BBB O   
4240 O  O   . HOH   H .   ? 0.494 0.468 0.658 -0.106 0.024  0.102  423 HOH   BBB O   
4241 O  O   . HOH   H .   ? 0.574 0.367 0.590 0.029  0.037  0.184  424 HOH   BBB O   
4242 O  O   . HOH   H .   ? 0.683 0.246 0.564 -0.010 -0.037 -0.026 425 HOH   BBB O   
4243 O  O   . HOH   H .   ? 0.709 0.009 0.448 -0.019 0.041  0.030  426 HOH   BBB O   
4244 O  O   . HOH   H .   ? 0.691 0.026 0.828 -0.028 0.036  0.122  427 HOH   BBB O   
4245 O  O   . HOH   H .   ? 0.695 0.155 0.577 0.170  0.104  0.043  428 HOH   BBB O   
4246 O  O   . HOH   H .   ? 0.469 0.231 0.478 0.066  -0.040 -0.004 429 HOH   BBB O   
4247 O  O   . HOH   H .   ? 0.514 0.013 0.747 -0.001 0.102  -0.067 430 HOH   BBB O   
4248 O  O   . HOH   H .   ? 0.617 0.263 0.523 -0.095 -0.041 -0.071 431 HOH   BBB O   
4249 O  O   . HOH   H .   ? 0.604 0.088 0.635 0.128  0.030  0.078  432 HOH   BBB O   
4250 O  O   . HOH   H .   ? 0.539 0.104 0.727 -0.025 -0.022 -0.151 433 HOH   BBB O   
4251 O  O   . HOH   H .   ? 0.785 0.010 0.658 -0.055 0.021  -0.009 434 HOH   BBB O   
4252 O  O   . HOH   H .   ? 0.646 0.128 0.446 0.075  0.016  0.030  435 HOH   BBB O   
4253 O  O   . HOH   H .   ? 0.709 0.172 1.052 0.094  -0.129 -0.300 436 HOH   BBB O   
4254 O  O   . HOH   H .   ? 0.762 0.087 1.039 -0.051 -0.160 0.289  437 HOH   BBB O   
4255 O  O   . HOH   H .   ? 0.524 0.303 0.551 0.024  -0.090 -0.037 438 HOH   BBB O   
4256 O  O   . HOH   H .   ? 0.759 0.016 0.626 -0.083 -0.029 0.020  439 HOH   BBB O   
4257 O  O   . HOH   H .   ? 0.538 0.230 0.490 0.085  -0.008 0.091  440 HOH   BBB O   
4258 O  O   . HOH   H .   ? 0.805 0.032 0.591 -0.053 0.009  0.112  441 HOH   BBB O   
4259 O  O   . HOH   H .   ? 1.283 0.072 1.675 -0.112 -0.192 0.319  442 HOH   BBB O   
4260 O  O   . HOH   H .   ? 0.435 0.286 0.437 0.040  -0.049 -0.018 443 HOH   BBB O   
4261 O  O   . HOH   H .   ? 0.637 0.151 0.656 -0.038 0.107  0.036  444 HOH   BBB O   
4262 O  O   . HOH   H .   ? 0.415 0.568 0.413 -0.099 -0.021 -0.069 445 HOH   BBB O   
4263 O  O   . HOH   H .   ? 0.695 0.016 0.515 0.055  -0.043 0.048  446 HOH   BBB O   
4264 O  O   . HOH   H .   ? 0.707 0.241 0.505 0.118  0.018  -0.013 447 HOH   BBB O   
4265 O  O   . HOH   H .   ? 0.473 0.375 0.494 0.103  -0.008 -0.078 448 HOH   BBB O   
4266 O  O   . HOH   H .   ? 0.721 0.191 0.625 0.253  0.067  0.106  449 HOH   BBB O   
4267 O  O   . HOH   H .   ? 0.416 0.157 0.428 -0.047 0.026  -0.043 450 HOH   BBB O   
4268 O  O   . HOH   H .   ? 0.428 0.053 0.356 -0.005 0.015  0.056  451 HOH   BBB O   
4269 O  O   . HOH   H .   ? 0.622 0.271 0.653 -0.025 -0.022 0.240  452 HOH   BBB O   
4270 O  O   . HOH   H .   ? 1.059 0.014 1.436 -0.034 0.119  0.090  453 HOH   BBB O   
4271 O  O   . HOH   H .   ? 0.512 0.012 0.388 -0.054 -0.022 0.003  454 HOH   BBB O   
4272 O  O   . HOH   H .   ? 0.722 0.022 0.768 -0.063 -0.011 -0.085 455 HOH   BBB O   
4273 O  O   . HOH   H .   ? 0.438 0.008 0.416 -0.024 -0.014 0.018  456 HOH   BBB O   
4274 O  O   . HOH   H .   ? 0.853 0.115 0.509 0.108  0.032  -0.035 457 HOH   BBB O   
4275 O  O   . HOH   H .   ? 0.390 0.024 0.391 0.082  0.002  -0.012 458 HOH   BBB O   
4276 O  O   . HOH   H .   ? 0.722 0.135 0.552 -0.023 0.102  0.159  459 HOH   BBB O   
4277 O  O   . HOH   H .   ? 0.717 0.503 0.562 0.319  0.069  0.214  460 HOH   BBB O   
4278 O  O   . HOH   H .   ? 0.485 0.504 0.508 0.064  0.064  0.078  461 HOH   BBB O   
4279 O  O   . HOH   H .   ? 0.658 0.162 0.466 0.090  -0.001 -0.065 462 HOH   BBB O   
4280 O  O   . HOH   H .   ? 0.636 0.179 0.672 -0.016 0.133  -0.035 463 HOH   BBB O   
4281 O  O   . HOH   H .   ? 0.412 0.373 0.450 0.099  -0.048 -0.120 464 HOH   BBB O   
4282 O  O   . HOH   H .   ? 0.401 0.404 0.362 0.042  0.014  -0.026 465 HOH   BBB O   
4283 O  O   . HOH   H .   ? 0.523 0.112 0.451 0.127  0.158  0.176  466 HOH   BBB O   
4284 O  O   . HOH   H .   ? 0.517 0.165 0.536 0.076  -0.020 0.076  467 HOH   BBB O   
4285 O  O   . HOH   H .   ? 0.535 0.198 0.452 0.094  -0.080 0.011  468 HOH   BBB O   
4286 O  O   . HOH   H .   ? 0.555 0.380 0.521 0.037  0.062  0.118  469 HOH   BBB O   
4287 O  O   . HOH   H .   ? 0.505 0.194 0.480 0.009  0.015  0.121  470 HOH   BBB O   
4288 O  O   . HOH   H .   ? 0.708 0.017 0.669 -0.044 0.034  0.072  471 HOH   BBB O   
4289 O  O   . HOH   H .   ? 0.683 0.039 0.577 0.138  0.064  0.062  472 HOH   BBB O   
4290 O  O   . HOH   H .   ? 0.628 0.531 0.609 -0.181 0.064  0.039  473 HOH   BBB O   
4291 O  O   . HOH   H .   ? 0.547 0.232 0.526 -0.093 -0.060 0.055  474 HOH   BBB O   
4292 O  O   . HOH   H .   ? 0.631 0.007 0.475 0.007  -0.014 -0.016 475 HOH   BBB O   
4293 O  O   . HOH   H .   ? 0.587 0.147 0.503 0.041  -0.005 -0.015 476 HOH   BBB O   
4294 O  O   . HOH   H .   ? 0.723 0.346 0.475 -0.113 0.033  -0.101 477 HOH   BBB O   
4295 O  O   . HOH   H .   ? 0.544 0.167 0.686 0.025  -0.029 0.186  478 HOH   BBB O   
4296 O  O   . HOH   H .   ? 0.890 0.045 0.825 0.185  0.118  0.016  479 HOH   BBB O   
4297 O  O   . HOH   H .   ? 0.556 0.374 0.453 -0.009 -0.064 -0.019 480 HOH   BBB O   
4298 O  O   . HOH   H .   ? 0.996 0.020 0.639 0.043  -0.017 -0.086 481 HOH   BBB O   
4299 O  O   . HOH   H .   ? 0.549 0.201 0.750 0.067  0.106  -0.141 482 HOH   BBB O   
4300 O  O   . HOH   H .   ? 0.441 0.022 0.424 -0.013 0.025  0.018  483 HOH   BBB O   
4301 O  O   . HOH   H .   ? 0.646 0.026 0.377 -0.028 -0.019 -0.033 484 HOH   BBB O   
4302 O  O   . HOH   H .   ? 0.481 0.226 0.570 -0.010 -0.080 0.105  485 HOH   BBB O   
4303 O  O   . HOH   H .   ? 0.488 0.009 0.443 -0.023 -0.037 -0.026 486 HOH   BBB O   
4304 O  O   . HOH   H .   ? 0.656 0.341 0.445 -0.046 -0.005 0.041  487 HOH   BBB O   
4305 O  O   . HOH   H .   ? 0.437 0.073 0.434 0.062  -0.024 -0.027 488 HOH   BBB O   
4306 O  O   . HOH   H .   ? 0.724 0.011 0.705 0.023  0.123  -0.050 489 HOH   BBB O   
4307 O  O   . HOH   H .   ? 0.534 0.317 0.406 0.030  -0.022 -0.046 490 HOH   BBB O   
4308 O  O   . HOH   H .   ? 0.670 0.581 0.360 0.043  0.009  -0.042 491 HOH   BBB O   
4309 O  O   . HOH   H .   ? 0.466 0.055 0.613 -0.044 0.034  0.160  492 HOH   BBB O   
4310 O  O   . HOH   H .   ? 0.747 0.544 0.594 -0.084 0.010  -0.193 493 HOH   BBB O   
4311 O  O   . HOH   H .   ? 0.786 0.164 0.635 0.087  -0.137 -0.044 494 HOH   BBB O   
4312 O  O   . HOH   H .   ? 1.175 0.068 1.067 -0.067 -0.057 0.250  495 HOH   BBB O   
4313 O  O   . HOH   H .   ? 0.576 0.377 0.631 -0.040 0.028  -0.206 496 HOH   BBB O   
4314 O  O   . HOH   H .   ? 0.384 0.173 0.521 -0.005 -0.013 0.137  497 HOH   BBB O   
4315 O  O   . HOH   H .   ? 0.492 0.240 0.421 0.010  0.013  0.142  498 HOH   BBB O   
4316 O  O   . HOH   H .   ? 0.449 0.564 0.591 -0.068 0.012  -0.107 499 HOH   BBB O   
4317 O  O   . HOH   H .   ? 0.457 0.212 0.461 0.018  -0.082 -0.027 500 HOH   BBB O   
4318 O  O   . HOH   H .   ? 0.636 0.361 0.632 -0.183 -0.097 0.289  501 HOH   BBB O   
4319 O  O   . HOH   H .   ? 0.573 0.428 0.737 0.137  0.006  0.097  502 HOH   BBB O   
4320 O  O   . HOH   H .   ? 0.656 0.070 0.406 -0.091 0.028  0.036  503 HOH   BBB O   
4321 O  O   . HOH   H .   ? 0.626 0.269 0.641 -0.120 -0.114 0.017  504 HOH   BBB O   
4322 O  O   . HOH   H .   ? 0.451 0.131 0.503 0.057  -0.075 0.056  505 HOH   BBB O   
4323 O  O   . HOH   H .   ? 0.798 0.015 0.697 0.030  0.012  0.071  506 HOH   BBB O   
4324 O  O   . HOH   H .   ? 0.381 0.797 0.603 0.043  -0.027 0.034  507 HOH   BBB O   
4325 O  O   . HOH   H .   ? 1.046 0.015 0.780 -0.079 0.014  -0.047 508 HOH   BBB O   
4326 O  O   . HOH   H .   ? 1.176 0.196 0.467 -0.038 -0.198 0.081  509 HOH   BBB O   
4327 O  O   . HOH   H .   ? 0.582 0.119 0.693 -0.005 0.089  -0.017 510 HOH   BBB O   
4328 O  O   . HOH   H .   ? 0.663 0.172 0.549 0.121  -0.065 0.002  511 HOH   BBB O   
4329 O  O   . HOH   H .   ? 0.664 0.132 0.637 -0.002 0.039  0.095  512 HOH   BBB O   
4330 O  O   . HOH   H .   ? 0.531 0.363 0.388 -0.035 0.015  -0.086 513 HOH   BBB O   
4331 O  O   . HOH   H .   ? 0.453 0.153 0.706 0.052  -0.058 -0.098 514 HOH   BBB O   
4332 O  O   . HOH   H .   ? 0.506 0.412 0.610 0.242  0.085  0.087  515 HOH   BBB O   
4333 O  O   . HOH   H .   ? 0.600 0.332 0.616 0.102  0.031  0.045  516 HOH   BBB O   
4334 O  O   . HOH   H .   ? 0.489 0.099 0.413 0.069  -0.020 -0.061 517 HOH   BBB O   
4335 O  O   . HOH   H .   ? 0.717 0.161 0.418 0.160  0.008  -0.011 518 HOH   BBB O   
4336 O  O   . HOH   H .   ? 0.595 0.231 0.502 0.019  0.001  -0.108 519 HOH   BBB O   
4337 O  O   . HOH   H .   ? 1.000 0.674 0.515 -0.032 -0.159 0.006  520 HOH   BBB O   
4338 O  O   . HOH   H .   ? 0.575 0.158 0.587 0.136  -0.036 -0.025 521 HOH   BBB O   
4339 O  O   . HOH   H .   ? 0.751 0.184 0.647 -0.045 0.097  0.011  522 HOH   BBB O   
4340 O  O   . HOH   H .   ? 1.148 0.207 0.463 0.283  -0.038 -0.028 523 HOH   BBB O   
4341 O  O   . HOH   H .   ? 0.433 0.011 0.428 -0.019 -0.024 -0.037 524 HOH   BBB O   
4342 O  O   . HOH   H .   ? 0.701 0.242 0.582 0.069  0.042  0.141  525 HOH   BBB O   
4343 O  O   . HOH   H .   ? 0.821 0.111 0.641 -0.154 -0.072 0.019  526 HOH   BBB O   
4344 O  O   . HOH   H .   ? 0.593 0.180 0.557 0.026  -0.048 -0.062 527 HOH   BBB O   
4345 O  O   . HOH   H .   ? 0.491 0.162 0.488 0.021  -0.011 0.120  528 HOH   BBB O   
4346 O  O   . HOH   H .   ? 0.544 0.114 0.824 0.070  0.016  0.112  529 HOH   BBB O   
4347 O  O   . HOH   H .   ? 0.829 0.593 0.573 0.048  0.077  0.285  530 HOH   BBB O   
4348 O  O   . HOH   H .   ? 0.779 0.077 0.563 0.063  0.056  0.011  531 HOH   BBB O   
4349 O  O   . HOH   H .   ? 0.723 0.330 0.370 -0.049 -0.057 0.082  532 HOH   BBB O   
4350 O  O   . HOH   H .   ? 0.783 0.185 0.518 -0.161 -0.046 0.089  533 HOH   BBB O   
4351 O  O   . HOH   H .   ? 0.502 0.288 0.404 0.011  0.041  0.016  534 HOH   BBB O   
4352 O  O   . HOH   H .   ? 0.409 0.431 0.460 -0.065 -0.013 -0.036 535 HOH   BBB O   
4353 O  O   . HOH   H .   ? 0.850 0.180 0.639 -0.043 -0.039 0.011  536 HOH   BBB O   
4354 O  O   . HOH   H .   ? 0.572 0.134 0.662 -0.004 -0.009 0.156  537 HOH   BBB O   
4355 O  O   . HOH   H .   ? 0.607 0.317 0.513 0.094  -0.048 -0.075 538 HOH   BBB O   
4356 O  O   . HOH   H .   ? 0.648 0.426 0.729 0.209  0.069  -0.014 539 HOH   BBB O   
4357 O  O   . HOH   H .   ? 0.858 0.117 1.020 -0.002 0.056  -0.280 540 HOH   BBB O   
4358 O  O   . HOH   H .   ? 0.700 0.339 0.594 0.000  0.148  -0.139 541 HOH   BBB O   
4359 O  O   . HOH   H .   ? 0.604 0.352 0.707 -0.027 -0.048 0.058  542 HOH   BBB O   
4360 O  O   . HOH   H .   ? 0.647 0.386 0.384 0.031  0.125  -0.011 543 HOH   BBB O   
4361 O  O   . HOH   H .   ? 0.939 0.133 0.602 -0.050 -0.060 0.102  544 HOH   BBB O   
4362 O  O   . HOH   H .   ? 0.591 0.298 0.546 0.054  0.069  -0.120 545 HOH   BBB O   
4363 O  O   . HOH   H .   ? 0.400 0.240 0.638 -0.035 -0.005 -0.005 546 HOH   BBB O   
4364 O  O   . HOH   H .   ? 0.393 0.283 0.577 0.055  0.154  0.205  547 HOH   BBB O   
4365 O  O   . HOH   H .   ? 0.809 0.214 0.760 0.005  -0.082 -0.040 548 HOH   BBB O   
4366 O  O   . HOH   H .   ? 0.529 0.241 0.520 0.061  -0.010 0.133  549 HOH   BBB O   
4367 O  O   . HOH   H .   ? 1.039 0.071 0.745 -0.186 -0.028 0.068  550 HOH   BBB O   
4368 O  O   . HOH   H .   ? 0.499 0.431 0.376 0.084  -0.084 -0.033 551 HOH   BBB O   
4369 O  O   . HOH   H .   ? 0.569 0.298 0.397 0.081  -0.045 0.039  552 HOH   BBB O   
4370 O  O   . HOH   H .   ? 0.508 0.274 0.454 0.020  0.007  -0.000 553 HOH   BBB O   
4371 O  O   . HOH   H .   ? 0.448 0.424 0.435 0.029  -0.058 -0.097 554 HOH   BBB O   
4372 O  O   . HOH   H .   ? 0.616 0.098 0.486 0.143  -0.013 -0.170 555 HOH   BBB O   
4373 O  O   . HOH   H .   ? 0.640 0.202 0.603 0.194  0.001  -0.092 556 HOH   BBB O   
4374 O  O   . HOH   H .   ? 0.462 0.538 0.523 -0.108 -0.006 -0.035 557 HOH   BBB O   
4375 O  O   . HOH   H .   ? 0.531 0.059 0.533 0.031  0.138  -0.151 558 HOH   BBB O   
4376 O  O   . HOH   H .   ? 0.544 0.027 0.601 0.106  -0.034 -0.001 559 HOH   BBB O   
4377 O  O   . HOH   H .   ? 0.606 0.243 0.696 0.058  0.003  0.101  560 HOH   BBB O   
4378 O  O   . HOH   H .   ? 0.563 0.428 0.960 0.177  -0.078 0.064  561 HOH   BBB O   
4379 O  O   . HOH   H .   ? 0.512 0.450 0.517 0.112  -0.050 0.027  562 HOH   BBB O   
# 
