data_9BCJ
# 
_entry.id   9BCJ 
# 
_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   9BCJ         pdb_00009bcj 10.2210/pdb9bcj/pdb 
WWPDB D_1000270652 ?            ?                   
# 
_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       2025-01-08 
# 
_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                        9BCJ 
_pdbx_database_status.recvd_initial_deposition_date   2024-04-09 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        '9BCH is the solution structure of apo form of HbpA' 
_pdbx_database_related.db_id          9BCH 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rclubb@mbi.ucla.edu 
_pdbx_contact_author.name_first         Robert 
_pdbx_contact_author.name_last          Clubb 
_pdbx_contact_author.name_mi            T 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-5718-3985 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mahoney, B.J.' 1 0000-0003-4323-9276 
'Cascio, D.'    2 0000-0002-3877-6803 
'Clubb, R.T.'   3 0000-0001-5718-3985 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_id_ASTM           PNASA6 
_citation.journal_id_CSD            0040 
_citation.journal_id_ISSN           1091-6490 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            122 
_citation.language                  ? 
_citation.page_first                e2411833122 
_citation.page_last                 e2411833122 
_citation.title                     'Molecular basis of hemoglobin binding and heme removal in Corynebacterium diphtheriae.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1073/pnas.2411833122 
_citation.pdbx_database_id_PubMed   39739808 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mahoney, B.J.'       1  0000-0003-4323-9276 
primary 'Lyman, L.R.'         2  ?                   
primary 'Ford, J.'            3  0000-0001-9501-551X 
primary 'Soule, J.'           4  0000-0002-6159-4354 
primary 'Cheung, N.A.'        5  ?                   
primary 'Goring, A.K.'        6  0000-0003-4220-6472 
primary 'Ellis-Guardiola, K.' 7  0000-0001-7966-1052 
primary 'Collazo, M.J.'       8  ?                   
primary 'Cascio, D.'          9  0000-0001-8285-754X 
primary 'Ton-That, H.'        10 0000-0003-1611-0469 
primary 'Schmitt, M.P.'       11 ?                   
primary 'Clubb, R.T.'         12 0000-0001-5718-3985 
# 
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     nat 'Hemoglobin subunit alpha'        15150.353 1   ? ? ? ?                         
2 polymer     nat 'Hemoglobin subunit beta'         15890.198 1   ? ? ? ?                         
3 polymer     man 'Membrane protein'                21918.514 1   ? ? ? 'A31S, TEV cleavage scar' 
4 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   2   ? ? ? ?                         
5 non-polymer syn GLYCEROL                          92.094    3   ? ? ? ?                         
6 non-polymer syn 'PHOSPHATE ION'                   94.971    1   ? ? ? ?                         
7 water       nat water                             18.015    269 ? ? ? ?                         
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'Alpha-globin,Hemoglobin alpha chain' 
2 'Beta-globin,Hemoglobin beta chain'   
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
;
;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
;
A ? 
2 'polypeptide(L)' no no 
;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
;
;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
;
B ? 
3 'polypeptide(L)' no no 
;SEEVKNADLYWGFSGSSHHKYDHNGPKFEKAGKGAELTNIDAASAYAETFKKGVFPNNKREKSDILVFHNGEVKTETNHS
SYQINWPGEVTMKLGYGDGLVIKDLNLMLKNGNMGELKATVGENSNITLFDVQEYSVSDNTITVTPKIPPCTTGTWKPWH
NDLTSKLGSLKSVFFESYTCNNDDIAKKPLPLTVVLNG
;
;SEEVKNADLYWGFSGSSHHKYDHNGPKFEKAGKGAELTNIDAASAYAETFKKGVFPNNKREKSDILVFHNGEVKTETNHS
SYQINWPGEVTMKLGYGDGLVIKDLNLMLKNGNMGELKATVGENSNITLFDVQEYSVSDNTITVTPKIPPCTTGTWKPWH
NDLTSKLGSLKSVFFESYTCNNDDIAKKPLPLTVVLNG
;
C ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
5 GLYCEROL                          GOL 
6 'PHOSPHATE ION'                   PO4 
7 water                             HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   VAL n 
1 2   LEU n 
1 3   SER n 
1 4   PRO n 
1 5   ALA n 
1 6   ASP n 
1 7   LYS n 
1 8   THR n 
1 9   ASN n 
1 10  VAL n 
1 11  LYS n 
1 12  ALA n 
1 13  ALA n 
1 14  TRP n 
1 15  GLY n 
1 16  LYS n 
1 17  VAL n 
1 18  GLY n 
1 19  ALA n 
1 20  HIS n 
1 21  ALA n 
1 22  GLY n 
1 23  GLU n 
1 24  TYR n 
1 25  GLY n 
1 26  ALA n 
1 27  GLU n 
1 28  ALA n 
1 29  LEU n 
1 30  GLU n 
1 31  ARG n 
1 32  MET n 
1 33  PHE n 
1 34  LEU n 
1 35  SER n 
1 36  PHE n 
1 37  PRO n 
1 38  THR n 
1 39  THR n 
1 40  LYS n 
1 41  THR n 
1 42  TYR n 
1 43  PHE n 
1 44  PRO n 
1 45  HIS n 
1 46  PHE n 
1 47  ASP n 
1 48  LEU n 
1 49  SER n 
1 50  HIS n 
1 51  GLY n 
1 52  SER n 
1 53  ALA n 
1 54  GLN n 
1 55  VAL n 
1 56  LYS n 
1 57  GLY n 
1 58  HIS n 
1 59  GLY n 
1 60  LYS n 
1 61  LYS n 
1 62  VAL n 
1 63  ALA n 
1 64  ASP n 
1 65  ALA n 
1 66  LEU n 
1 67  THR n 
1 68  ASN n 
1 69  ALA n 
1 70  VAL n 
1 71  ALA n 
1 72  HIS n 
1 73  VAL n 
1 74  ASP n 
1 75  ASP n 
1 76  MET n 
1 77  PRO n 
1 78  ASN n 
1 79  ALA n 
1 80  LEU n 
1 81  SER n 
1 82  ALA n 
1 83  LEU n 
1 84  SER n 
1 85  ASP n 
1 86  LEU n 
1 87  HIS n 
1 88  ALA n 
1 89  HIS n 
1 90  LYS n 
1 91  LEU n 
1 92  ARG n 
1 93  VAL n 
1 94  ASP n 
1 95  PRO n 
1 96  VAL n 
1 97  ASN n 
1 98  PHE n 
1 99  LYS n 
1 100 LEU n 
1 101 LEU n 
1 102 SER n 
1 103 HIS n 
1 104 CYS n 
1 105 LEU n 
1 106 LEU n 
1 107 VAL n 
1 108 THR n 
1 109 LEU n 
1 110 ALA n 
1 111 ALA n 
1 112 HIS n 
1 113 LEU n 
1 114 PRO n 
1 115 ALA n 
1 116 GLU n 
1 117 PHE n 
1 118 THR n 
1 119 PRO n 
1 120 ALA n 
1 121 VAL n 
1 122 HIS n 
1 123 ALA n 
1 124 SER n 
1 125 LEU n 
1 126 ASP n 
1 127 LYS n 
1 128 PHE n 
1 129 LEU n 
1 130 ALA n 
1 131 SER n 
1 132 VAL n 
1 133 SER n 
1 134 THR n 
1 135 VAL n 
1 136 LEU n 
1 137 THR n 
1 138 SER n 
1 139 LYS n 
1 140 TYR n 
1 141 ARG n 
2 1   VAL n 
2 2   HIS n 
2 3   LEU n 
2 4   THR n 
2 5   PRO n 
2 6   GLU n 
2 7   GLU n 
2 8   LYS n 
2 9   SER n 
2 10  ALA n 
2 11  VAL n 
2 12  THR n 
2 13  ALA n 
2 14  LEU n 
2 15  TRP n 
2 16  GLY n 
2 17  LYS n 
2 18  VAL n 
2 19  ASN n 
2 20  VAL n 
2 21  ASP n 
2 22  GLU n 
2 23  VAL n 
2 24  GLY n 
2 25  GLY n 
2 26  GLU n 
2 27  ALA n 
2 28  LEU n 
2 29  GLY n 
2 30  ARG n 
2 31  LEU n 
2 32  LEU n 
2 33  VAL n 
2 34  VAL n 
2 35  TYR n 
2 36  PRO n 
2 37  TRP n 
2 38  THR n 
2 39  GLN n 
2 40  ARG n 
2 41  PHE n 
2 42  PHE n 
2 43  GLU n 
2 44  SER n 
2 45  PHE n 
2 46  GLY n 
2 47  ASP n 
2 48  LEU n 
2 49  SER n 
2 50  THR n 
2 51  PRO n 
2 52  ASP n 
2 53  ALA n 
2 54  VAL n 
2 55  MET n 
2 56  GLY n 
2 57  ASN n 
2 58  PRO n 
2 59  LYS n 
2 60  VAL n 
2 61  LYS n 
2 62  ALA n 
2 63  HIS n 
2 64  GLY n 
2 65  LYS n 
2 66  LYS n 
2 67  VAL n 
2 68  LEU n 
2 69  GLY n 
2 70  ALA n 
2 71  PHE n 
2 72  SER n 
2 73  ASP n 
2 74  GLY n 
2 75  LEU n 
2 76  ALA n 
2 77  HIS n 
2 78  LEU n 
2 79  ASP n 
2 80  ASN n 
2 81  LEU n 
2 82  LYS n 
2 83  GLY n 
2 84  THR n 
2 85  PHE n 
2 86  ALA n 
2 87  THR n 
2 88  LEU n 
2 89  SER n 
2 90  GLU n 
2 91  LEU n 
2 92  HIS n 
2 93  CYS n 
2 94  ASP n 
2 95  LYS n 
2 96  LEU n 
2 97  HIS n 
2 98  VAL n 
2 99  ASP n 
2 100 PRO n 
2 101 GLU n 
2 102 ASN n 
2 103 PHE n 
2 104 ARG n 
2 105 LEU n 
2 106 LEU n 
2 107 GLY n 
2 108 ASN n 
2 109 VAL n 
2 110 LEU n 
2 111 VAL n 
2 112 CYS n 
2 113 VAL n 
2 114 LEU n 
2 115 ALA n 
2 116 HIS n 
2 117 HIS n 
2 118 PHE n 
2 119 GLY n 
2 120 LYS n 
2 121 GLU n 
2 122 PHE n 
2 123 THR n 
2 124 PRO n 
2 125 PRO n 
2 126 VAL n 
2 127 GLN n 
2 128 ALA n 
2 129 ALA n 
2 130 TYR n 
2 131 GLN n 
2 132 LYS n 
2 133 VAL n 
2 134 VAL n 
2 135 ALA n 
2 136 GLY n 
2 137 VAL n 
2 138 ALA n 
2 139 ASN n 
2 140 ALA n 
2 141 LEU n 
2 142 ALA n 
2 143 HIS n 
2 144 LYS n 
2 145 TYR n 
2 146 HIS n 
3 1   SER n 
3 2   GLU n 
3 3   GLU n 
3 4   VAL n 
3 5   LYS n 
3 6   ASN n 
3 7   ALA n 
3 8   ASP n 
3 9   LEU n 
3 10  TYR n 
3 11  TRP n 
3 12  GLY n 
3 13  PHE n 
3 14  SER n 
3 15  GLY n 
3 16  SER n 
3 17  SER n 
3 18  HIS n 
3 19  HIS n 
3 20  LYS n 
3 21  TYR n 
3 22  ASP n 
3 23  HIS n 
3 24  ASN n 
3 25  GLY n 
3 26  PRO n 
3 27  LYS n 
3 28  PHE n 
3 29  GLU n 
3 30  LYS n 
3 31  ALA n 
3 32  GLY n 
3 33  LYS n 
3 34  GLY n 
3 35  ALA n 
3 36  GLU n 
3 37  LEU n 
3 38  THR n 
3 39  ASN n 
3 40  ILE n 
3 41  ASP n 
3 42  ALA n 
3 43  ALA n 
3 44  SER n 
3 45  ALA n 
3 46  TYR n 
3 47  ALA n 
3 48  GLU n 
3 49  THR n 
3 50  PHE n 
3 51  LYS n 
3 52  LYS n 
3 53  GLY n 
3 54  VAL n 
3 55  PHE n 
3 56  PRO n 
3 57  ASN n 
3 58  ASN n 
3 59  LYS n 
3 60  ARG n 
3 61  GLU n 
3 62  LYS n 
3 63  SER n 
3 64  ASP n 
3 65  ILE n 
3 66  LEU n 
3 67  VAL n 
3 68  PHE n 
3 69  HIS n 
3 70  ASN n 
3 71  GLY n 
3 72  GLU n 
3 73  VAL n 
3 74  LYS n 
3 75  THR n 
3 76  GLU n 
3 77  THR n 
3 78  ASN n 
3 79  HIS n 
3 80  SER n 
3 81  SER n 
3 82  TYR n 
3 83  GLN n 
3 84  ILE n 
3 85  ASN n 
3 86  TRP n 
3 87  PRO n 
3 88  GLY n 
3 89  GLU n 
3 90  VAL n 
3 91  THR n 
3 92  MET n 
3 93  LYS n 
3 94  LEU n 
3 95  GLY n 
3 96  TYR n 
3 97  GLY n 
3 98  ASP n 
3 99  GLY n 
3 100 LEU n 
3 101 VAL n 
3 102 ILE n 
3 103 LYS n 
3 104 ASP n 
3 105 LEU n 
3 106 ASN n 
3 107 LEU n 
3 108 MET n 
3 109 LEU n 
3 110 LYS n 
3 111 ASN n 
3 112 GLY n 
3 113 ASN n 
3 114 MET n 
3 115 GLY n 
3 116 GLU n 
3 117 LEU n 
3 118 LYS n 
3 119 ALA n 
3 120 THR n 
3 121 VAL n 
3 122 GLY n 
3 123 GLU n 
3 124 ASN n 
3 125 SER n 
3 126 ASN n 
3 127 ILE n 
3 128 THR n 
3 129 LEU n 
3 130 PHE n 
3 131 ASP n 
3 132 VAL n 
3 133 GLN n 
3 134 GLU n 
3 135 TYR n 
3 136 SER n 
3 137 VAL n 
3 138 SER n 
3 139 ASP n 
3 140 ASN n 
3 141 THR n 
3 142 ILE n 
3 143 THR n 
3 144 VAL n 
3 145 THR n 
3 146 PRO n 
3 147 LYS n 
3 148 ILE n 
3 149 PRO n 
3 150 PRO n 
3 151 CYS n 
3 152 THR n 
3 153 THR n 
3 154 GLY n 
3 155 THR n 
3 156 TRP n 
3 157 LYS n 
3 158 PRO n 
3 159 TRP n 
3 160 HIS n 
3 161 ASN n 
3 162 ASP n 
3 163 LEU n 
3 164 THR n 
3 165 SER n 
3 166 LYS n 
3 167 LEU n 
3 168 GLY n 
3 169 SER n 
3 170 LEU n 
3 171 LYS n 
3 172 SER n 
3 173 VAL n 
3 174 PHE n 
3 175 PHE n 
3 176 GLU n 
3 177 SER n 
3 178 TYR n 
3 179 THR n 
3 180 CYS n 
3 181 ASN n 
3 182 ASN n 
3 183 ASP n 
3 184 ASP n 
3 185 ILE n 
3 186 ALA n 
3 187 LYS n 
3 188 LYS n 
3 189 PRO n 
3 190 LEU n 
3 191 PRO n 
3 192 LEU n 
3 193 THR n 
3 194 VAL n 
3 195 VAL n 
3 196 LEU n 
3 197 ASN n 
3 198 GLY n 
# 
_entity_src_gen.entity_id                          3 
_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                   198 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 DIP2330 
_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      'Corynebacterium diphtheriae NCTC 13129' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     257309 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 700971 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pMAPLe4 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_entity_src_nat.entity_id 
_entity_src_nat.pdbx_src_id 
_entity_src_nat.pdbx_alt_source_flag 
_entity_src_nat.pdbx_beg_seq_num 
_entity_src_nat.pdbx_end_seq_num 
_entity_src_nat.common_name 
_entity_src_nat.pdbx_organism_scientific 
_entity_src_nat.pdbx_ncbi_taxonomy_id 
_entity_src_nat.genus 
_entity_src_nat.species 
_entity_src_nat.strain 
_entity_src_nat.tissue 
_entity_src_nat.tissue_fraction 
_entity_src_nat.pdbx_secretion 
_entity_src_nat.pdbx_fragment 
_entity_src_nat.pdbx_variant 
_entity_src_nat.pdbx_cell_line 
_entity_src_nat.pdbx_atcc 
_entity_src_nat.pdbx_cellular_location 
_entity_src_nat.pdbx_organ 
_entity_src_nat.pdbx_organelle 
_entity_src_nat.pdbx_cell 
_entity_src_nat.pdbx_plasmid_name 
_entity_src_nat.pdbx_plasmid_details 
_entity_src_nat.details 
1 1 sample 1 141 human 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 1 146 human 'Homo sapiens' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                           ?                               'C3 H7 N O2'       89.093  
ARG 'L-peptide linking' y ARGININE                          ?                               'C6 H15 N4 O2 1'   175.209 
ASN 'L-peptide linking' y ASPARAGINE                        ?                               'C4 H8 N2 O3'      132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                   ?                               'C4 H7 N O4'       133.103 
CYS 'L-peptide linking' y CYSTEINE                          ?                               'C3 H7 N O2 S'     121.158 
GLN 'L-peptide linking' y GLUTAMINE                         ?                               'C5 H10 N2 O3'     146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                   ?                               'C5 H9 N O4'       147.129 
GLY 'peptide linking'   y GLYCINE                           ?                               'C2 H5 N O2'       75.067  
GOL non-polymer         . GLYCEROL                          'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME                            'C34 H32 Fe N4 O4' 616.487 
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 
PO4 non-polymer         . 'PHOSPHATE ION'                   ?                               'O4 P -3'          94.971  
PRO 'L-peptide linking' y PROLINE                           ?                               'C5 H9 N O2'       115.130 
SER 'L-peptide linking' y SERINE                            ?                               'C3 H7 N O3'       105.093 
THR 'L-peptide linking' y THREONINE                         ?                               'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?                               'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?                               'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?                               'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   VAL 1   1   1   VAL VAL A . n 
A 1 2   LEU 2   2   2   LEU LEU A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   PRO 4   4   4   PRO PRO A . n 
A 1 5   ALA 5   5   5   ALA ALA A . n 
A 1 6   ASP 6   6   6   ASP ASP A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   ASN 9   9   9   ASN ASN A . n 
A 1 10  VAL 10  10  10  VAL VAL A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  ALA 12  12  12  ALA ALA A . n 
A 1 13  ALA 13  13  13  ALA ALA A . n 
A 1 14  TRP 14  14  14  TRP TRP A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  LYS 16  16  16  LYS LYS A . n 
A 1 17  VAL 17  17  17  VAL VAL A . n 
A 1 18  GLY 18  18  18  GLY GLY A . n 
A 1 19  ALA 19  19  19  ALA ALA A . n 
A 1 20  HIS 20  20  20  HIS HIS A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  GLY 22  22  22  GLY GLY A . n 
A 1 23  GLU 23  23  23  GLU GLU A . n 
A 1 24  TYR 24  24  24  TYR TYR A . n 
A 1 25  GLY 25  25  25  GLY GLY A . n 
A 1 26  ALA 26  26  26  ALA ALA A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  ALA 28  28  28  ALA ALA A . n 
A 1 29  LEU 29  29  29  LEU LEU A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  ARG 31  31  31  ARG ARG A . n 
A 1 32  MET 32  32  32  MET MET A . n 
A 1 33  PHE 33  33  33  PHE PHE A . n 
A 1 34  LEU 34  34  34  LEU LEU A . n 
A 1 35  SER 35  35  35  SER SER A . n 
A 1 36  PHE 36  36  36  PHE PHE A . n 
A 1 37  PRO 37  37  37  PRO PRO A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  LYS 40  40  40  LYS LYS A . n 
A 1 41  THR 41  41  41  THR THR A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  PHE 43  43  43  PHE PHE A . n 
A 1 44  PRO 44  44  44  PRO PRO A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  PHE 46  46  46  PHE PHE A . n 
A 1 47  ASP 47  47  47  ASP ASP A . n 
A 1 48  LEU 48  48  48  LEU LEU A . n 
A 1 49  SER 49  49  49  SER SER A . n 
A 1 50  HIS 50  50  50  HIS HIS A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  ALA 53  53  53  ALA ALA A . n 
A 1 54  GLN 54  54  54  GLN GLN A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  LYS 56  56  56  LYS LYS A . n 
A 1 57  GLY 57  57  57  GLY GLY A . n 
A 1 58  HIS 58  58  58  HIS HIS A . n 
A 1 59  GLY 59  59  59  GLY GLY A . n 
A 1 60  LYS 60  60  60  LYS LYS A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  VAL 62  62  62  VAL VAL A . n 
A 1 63  ALA 63  63  63  ALA ALA A . n 
A 1 64  ASP 64  64  64  ASP ASP A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  LEU 66  66  66  LEU LEU A . n 
A 1 67  THR 67  67  67  THR THR A . n 
A 1 68  ASN 68  68  68  ASN ASN A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  VAL 70  70  70  VAL VAL A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  HIS 72  72  72  HIS HIS A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  ASP 74  74  74  ASP ASP A . n 
A 1 75  ASP 75  75  75  ASP ASP A . n 
A 1 76  MET 76  76  76  MET MET A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  LEU 80  80  80  LEU LEU A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ALA 82  82  82  ALA ALA A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  LEU 86  86  86  LEU LEU A . n 
A 1 87  HIS 87  87  87  HIS HIS A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  HIS 89  89  89  HIS HIS A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  LEU 91  91  91  LEU LEU A . n 
A 1 92  ARG 92  92  92  ARG ARG A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  ASP 94  94  94  ASP ASP A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  ASN 97  97  97  ASN ASN A . n 
A 1 98  PHE 98  98  98  PHE PHE A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 LEU 100 100 100 LEU LEU A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 HIS 103 103 103 HIS HIS A . n 
A 1 104 CYS 104 104 104 CYS CYS A . n 
A 1 105 LEU 105 105 105 LEU LEU A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 VAL 107 107 107 VAL VAL A . n 
A 1 108 THR 108 108 108 THR THR A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 ALA 110 110 110 ALA ALA A . n 
A 1 111 ALA 111 111 111 ALA ALA A . n 
A 1 112 HIS 112 112 112 HIS HIS A . n 
A 1 113 LEU 113 113 113 LEU LEU A . n 
A 1 114 PRO 114 114 114 PRO PRO A . n 
A 1 115 ALA 115 115 115 ALA ALA A . n 
A 1 116 GLU 116 116 116 GLU GLU A . n 
A 1 117 PHE 117 117 117 PHE PHE A . n 
A 1 118 THR 118 118 118 THR THR A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 ALA 120 120 120 ALA ALA A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 SER 124 124 124 SER SER A . n 
A 1 125 LEU 125 125 125 LEU LEU A . n 
A 1 126 ASP 126 126 126 ASP ASP A . n 
A 1 127 LYS 127 127 127 LYS LYS A . n 
A 1 128 PHE 128 128 128 PHE PHE A . n 
A 1 129 LEU 129 129 129 LEU LEU A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 SER 131 131 131 SER SER A . n 
A 1 132 VAL 132 132 132 VAL VAL A . n 
A 1 133 SER 133 133 133 SER SER A . n 
A 1 134 THR 134 134 134 THR THR A . n 
A 1 135 VAL 135 135 135 VAL VAL A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 SER 138 138 138 SER SER A . n 
A 1 139 LYS 139 139 139 LYS LYS A . n 
A 1 140 TYR 140 140 140 TYR TYR A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
B 2 1   VAL 1   1   1   VAL VAL B . n 
B 2 2   HIS 2   2   2   HIS HIS B . n 
B 2 3   LEU 3   3   3   LEU LEU B . n 
B 2 4   THR 4   4   4   THR THR B . n 
B 2 5   PRO 5   5   5   PRO PRO B . n 
B 2 6   GLU 6   6   6   GLU GLU B . n 
B 2 7   GLU 7   7   7   GLU GLU B . n 
B 2 8   LYS 8   8   8   LYS LYS B . n 
B 2 9   SER 9   9   9   SER SER B . n 
B 2 10  ALA 10  10  10  ALA ALA B . n 
B 2 11  VAL 11  11  11  VAL VAL B . n 
B 2 12  THR 12  12  12  THR THR B . n 
B 2 13  ALA 13  13  13  ALA ALA B . n 
B 2 14  LEU 14  14  14  LEU LEU B . n 
B 2 15  TRP 15  15  15  TRP TRP B . n 
B 2 16  GLY 16  16  16  GLY GLY B . n 
B 2 17  LYS 17  17  17  LYS LYS B . n 
B 2 18  VAL 18  18  18  VAL VAL B . n 
B 2 19  ASN 19  19  19  ASN ASN B . n 
B 2 20  VAL 20  20  20  VAL VAL B . n 
B 2 21  ASP 21  21  21  ASP ASP B . n 
B 2 22  GLU 22  22  22  GLU GLU B . n 
B 2 23  VAL 23  23  23  VAL VAL B . n 
B 2 24  GLY 24  24  24  GLY GLY B . n 
B 2 25  GLY 25  25  25  GLY GLY B . n 
B 2 26  GLU 26  26  26  GLU GLU B . n 
B 2 27  ALA 27  27  27  ALA ALA B . n 
B 2 28  LEU 28  28  28  LEU LEU B . n 
B 2 29  GLY 29  29  29  GLY GLY B . n 
B 2 30  ARG 30  30  30  ARG ARG B . n 
B 2 31  LEU 31  31  31  LEU LEU B . n 
B 2 32  LEU 32  32  32  LEU LEU B . n 
B 2 33  VAL 33  33  33  VAL VAL B . n 
B 2 34  VAL 34  34  34  VAL VAL B . n 
B 2 35  TYR 35  35  35  TYR TYR B . n 
B 2 36  PRO 36  36  36  PRO PRO B . n 
B 2 37  TRP 37  37  37  TRP TRP B . n 
B 2 38  THR 38  38  38  THR THR B . n 
B 2 39  GLN 39  39  39  GLN GLN B . n 
B 2 40  ARG 40  40  40  ARG ARG B . n 
B 2 41  PHE 41  41  41  PHE PHE B . n 
B 2 42  PHE 42  42  42  PHE PHE B . n 
B 2 43  GLU 43  43  43  GLU GLU B . n 
B 2 44  SER 44  44  44  SER SER B . n 
B 2 45  PHE 45  45  45  PHE PHE B . n 
B 2 46  GLY 46  46  46  GLY GLY B . n 
B 2 47  ASP 47  47  47  ASP ASP B . n 
B 2 48  LEU 48  48  48  LEU LEU B . n 
B 2 49  SER 49  49  49  SER SER B . n 
B 2 50  THR 50  50  50  THR THR B . n 
B 2 51  PRO 51  51  51  PRO PRO B . n 
B 2 52  ASP 52  52  52  ASP ASP B . n 
B 2 53  ALA 53  53  53  ALA ALA B . n 
B 2 54  VAL 54  54  54  VAL VAL B . n 
B 2 55  MET 55  55  55  MET MET B . n 
B 2 56  GLY 56  56  56  GLY GLY B . n 
B 2 57  ASN 57  57  57  ASN ASN B . n 
B 2 58  PRO 58  58  58  PRO PRO B . n 
B 2 59  LYS 59  59  59  LYS LYS B . n 
B 2 60  VAL 60  60  60  VAL VAL B . n 
B 2 61  LYS 61  61  61  LYS LYS B . n 
B 2 62  ALA 62  62  62  ALA ALA B . n 
B 2 63  HIS 63  63  63  HIS HIS B . n 
B 2 64  GLY 64  64  64  GLY GLY B . n 
B 2 65  LYS 65  65  65  LYS LYS B . n 
B 2 66  LYS 66  66  66  LYS LYS B . n 
B 2 67  VAL 67  67  67  VAL VAL B . n 
B 2 68  LEU 68  68  68  LEU LEU B . n 
B 2 69  GLY 69  69  69  GLY GLY B . n 
B 2 70  ALA 70  70  70  ALA ALA B . n 
B 2 71  PHE 71  71  71  PHE PHE B . n 
B 2 72  SER 72  72  72  SER SER B . n 
B 2 73  ASP 73  73  73  ASP ASP B . n 
B 2 74  GLY 74  74  74  GLY GLY B . n 
B 2 75  LEU 75  75  75  LEU LEU B . n 
B 2 76  ALA 76  76  76  ALA ALA B . n 
B 2 77  HIS 77  77  77  HIS HIS B . n 
B 2 78  LEU 78  78  78  LEU LEU B . n 
B 2 79  ASP 79  79  79  ASP ASP B . n 
B 2 80  ASN 80  80  80  ASN ASN B . n 
B 2 81  LEU 81  81  81  LEU LEU B . n 
B 2 82  LYS 82  82  82  LYS LYS B . n 
B 2 83  GLY 83  83  83  GLY GLY B . n 
B 2 84  THR 84  84  84  THR THR B . n 
B 2 85  PHE 85  85  85  PHE PHE B . n 
B 2 86  ALA 86  86  86  ALA ALA B . n 
B 2 87  THR 87  87  87  THR THR B . n 
B 2 88  LEU 88  88  88  LEU LEU B . n 
B 2 89  SER 89  89  89  SER SER B . n 
B 2 90  GLU 90  90  90  GLU GLU B . n 
B 2 91  LEU 91  91  91  LEU LEU B . n 
B 2 92  HIS 92  92  92  HIS HIS B . n 
B 2 93  CYS 93  93  93  CYS CYS B . n 
B 2 94  ASP 94  94  94  ASP ASP B . n 
B 2 95  LYS 95  95  95  LYS LYS B . n 
B 2 96  LEU 96  96  96  LEU LEU B . n 
B 2 97  HIS 97  97  97  HIS HIS B . n 
B 2 98  VAL 98  98  98  VAL VAL B . n 
B 2 99  ASP 99  99  99  ASP ASP B . n 
B 2 100 PRO 100 100 100 PRO PRO B . n 
B 2 101 GLU 101 101 101 GLU GLU B . n 
B 2 102 ASN 102 102 102 ASN ASN B . n 
B 2 103 PHE 103 103 103 PHE PHE B . n 
B 2 104 ARG 104 104 104 ARG ARG B . n 
B 2 105 LEU 105 105 105 LEU LEU B . n 
B 2 106 LEU 106 106 106 LEU LEU B . n 
B 2 107 GLY 107 107 107 GLY GLY B . n 
B 2 108 ASN 108 108 108 ASN ASN B . n 
B 2 109 VAL 109 109 109 VAL VAL B . n 
B 2 110 LEU 110 110 110 LEU LEU B . n 
B 2 111 VAL 111 111 111 VAL VAL B . n 
B 2 112 CYS 112 112 112 CYS CYS B . n 
B 2 113 VAL 113 113 113 VAL VAL B . n 
B 2 114 LEU 114 114 114 LEU LEU B . n 
B 2 115 ALA 115 115 115 ALA ALA B . n 
B 2 116 HIS 116 116 116 HIS HIS B . n 
B 2 117 HIS 117 117 117 HIS HIS B . n 
B 2 118 PHE 118 118 118 PHE PHE B . n 
B 2 119 GLY 119 119 119 GLY GLY B . n 
B 2 120 LYS 120 120 120 LYS LYS B . n 
B 2 121 GLU 121 121 121 GLU GLU B . n 
B 2 122 PHE 122 122 122 PHE PHE B . n 
B 2 123 THR 123 123 123 THR THR B . n 
B 2 124 PRO 124 124 124 PRO PRO B . n 
B 2 125 PRO 125 125 125 PRO PRO B . n 
B 2 126 VAL 126 126 126 VAL VAL B . n 
B 2 127 GLN 127 127 127 GLN GLN B . n 
B 2 128 ALA 128 128 128 ALA ALA B . n 
B 2 129 ALA 129 129 129 ALA ALA B . n 
B 2 130 TYR 130 130 130 TYR TYR B . n 
B 2 131 GLN 131 131 131 GLN GLN B . n 
B 2 132 LYS 132 132 132 LYS LYS B . n 
B 2 133 VAL 133 133 133 VAL VAL B . n 
B 2 134 VAL 134 134 134 VAL VAL B . n 
B 2 135 ALA 135 135 135 ALA ALA B . n 
B 2 136 GLY 136 136 136 GLY GLY B . n 
B 2 137 VAL 137 137 137 VAL VAL B . n 
B 2 138 ALA 138 138 138 ALA ALA B . n 
B 2 139 ASN 139 139 139 ASN ASN B . n 
B 2 140 ALA 140 140 140 ALA ALA B . n 
B 2 141 LEU 141 141 141 LEU LEU B . n 
B 2 142 ALA 142 142 142 ALA ALA B . n 
B 2 143 HIS 143 143 ?   ?   ?   B . n 
B 2 144 LYS 144 144 ?   ?   ?   B . n 
B 2 145 TYR 145 145 ?   ?   ?   B . n 
B 2 146 HIS 146 146 ?   ?   ?   B . n 
C 3 1   SER 1   32  ?   ?   ?   C . n 
C 3 2   GLU 2   33  ?   ?   ?   C . n 
C 3 3   GLU 3   34  ?   ?   ?   C . n 
C 3 4   VAL 4   35  ?   ?   ?   C . n 
C 3 5   LYS 5   36  36  LYS LYS C . n 
C 3 6   ASN 6   37  37  ASN ASN C . n 
C 3 7   ALA 7   38  38  ALA ALA C . n 
C 3 8   ASP 8   39  39  ASP ASP C . n 
C 3 9   LEU 9   40  40  LEU LEU C . n 
C 3 10  TYR 10  41  41  TYR TYR C . n 
C 3 11  TRP 11  42  42  TRP TRP C . n 
C 3 12  GLY 12  43  43  GLY GLY C . n 
C 3 13  PHE 13  44  44  PHE PHE C . n 
C 3 14  SER 14  45  45  SER SER C . n 
C 3 15  GLY 15  46  46  GLY GLY C . n 
C 3 16  SER 16  47  47  SER SER C . n 
C 3 17  SER 17  48  48  SER SER C . n 
C 3 18  HIS 18  49  49  HIS HIS C . n 
C 3 19  HIS 19  50  50  HIS HIS C . n 
C 3 20  LYS 20  51  51  LYS LYS C . n 
C 3 21  TYR 21  52  52  TYR TYR C . n 
C 3 22  ASP 22  53  53  ASP ASP C . n 
C 3 23  HIS 23  54  54  HIS HIS C . n 
C 3 24  ASN 24  55  55  ASN ASN C . n 
C 3 25  GLY 25  56  56  GLY GLY C . n 
C 3 26  PRO 26  57  57  PRO PRO C . n 
C 3 27  LYS 27  58  58  LYS LYS C . n 
C 3 28  PHE 28  59  59  PHE PHE C . n 
C 3 29  GLU 29  60  60  GLU GLU C . n 
C 3 30  LYS 30  61  61  LYS LYS C . n 
C 3 31  ALA 31  62  62  ALA ALA C . n 
C 3 32  GLY 32  63  63  GLY GLY C . n 
C 3 33  LYS 33  64  64  LYS LYS C . n 
C 3 34  GLY 34  65  65  GLY GLY C . n 
C 3 35  ALA 35  66  66  ALA ALA C . n 
C 3 36  GLU 36  67  67  GLU GLU C . n 
C 3 37  LEU 37  68  68  LEU LEU C . n 
C 3 38  THR 38  69  69  THR THR C . n 
C 3 39  ASN 39  70  70  ASN ASN C . n 
C 3 40  ILE 40  71  71  ILE ILE C . n 
C 3 41  ASP 41  72  72  ASP ASP C . n 
C 3 42  ALA 42  73  73  ALA ALA C . n 
C 3 43  ALA 43  74  74  ALA ALA C . n 
C 3 44  SER 44  75  75  SER SER C . n 
C 3 45  ALA 45  76  76  ALA ALA C . n 
C 3 46  TYR 46  77  77  TYR TYR C . n 
C 3 47  ALA 47  78  78  ALA ALA C . n 
C 3 48  GLU 48  79  79  GLU GLU C . n 
C 3 49  THR 49  80  80  THR THR C . n 
C 3 50  PHE 50  81  81  PHE PHE C . n 
C 3 51  LYS 51  82  82  LYS LYS C . n 
C 3 52  LYS 52  83  83  LYS LYS C . n 
C 3 53  GLY 53  84  84  GLY GLY C . n 
C 3 54  VAL 54  85  85  VAL VAL C . n 
C 3 55  PHE 55  86  86  PHE PHE C . n 
C 3 56  PRO 56  87  87  PRO PRO C . n 
C 3 57  ASN 57  88  88  ASN ASN C . n 
C 3 58  ASN 58  89  89  ASN ASN C . n 
C 3 59  LYS 59  90  90  LYS LYS C . n 
C 3 60  ARG 60  91  91  ARG ARG C . n 
C 3 61  GLU 61  92  92  GLU GLU C . n 
C 3 62  LYS 62  93  93  LYS LYS C . n 
C 3 63  SER 63  94  94  SER SER C . n 
C 3 64  ASP 64  95  95  ASP ASP C . n 
C 3 65  ILE 65  96  96  ILE ILE C . n 
C 3 66  LEU 66  97  97  LEU LEU C . n 
C 3 67  VAL 67  98  98  VAL VAL C . n 
C 3 68  PHE 68  99  99  PHE PHE C . n 
C 3 69  HIS 69  100 100 HIS HIS C . n 
C 3 70  ASN 70  101 101 ASN ASN C . n 
C 3 71  GLY 71  102 102 GLY GLY C . n 
C 3 72  GLU 72  103 103 GLU GLU C . n 
C 3 73  VAL 73  104 104 VAL VAL C . n 
C 3 74  LYS 74  105 105 LYS LYS C . n 
C 3 75  THR 75  106 106 THR THR C . n 
C 3 76  GLU 76  107 ?   ?   ?   C . n 
C 3 77  THR 77  108 ?   ?   ?   C . n 
C 3 78  ASN 78  109 ?   ?   ?   C . n 
C 3 79  HIS 79  110 ?   ?   ?   C . n 
C 3 80  SER 80  111 ?   ?   ?   C . n 
C 3 81  SER 81  112 112 SER SER C . n 
C 3 82  TYR 82  113 113 TYR TYR C . n 
C 3 83  GLN 83  114 114 GLN GLN C . n 
C 3 84  ILE 84  115 115 ILE ILE C . n 
C 3 85  ASN 85  116 116 ASN ASN C . n 
C 3 86  TRP 86  117 117 TRP TRP C . n 
C 3 87  PRO 87  118 118 PRO PRO C . n 
C 3 88  GLY 88  119 119 GLY GLY C . n 
C 3 89  GLU 89  120 120 GLU GLU C . n 
C 3 90  VAL 90  121 121 VAL VAL C . n 
C 3 91  THR 91  122 122 THR THR C . n 
C 3 92  MET 92  123 123 MET MET C . n 
C 3 93  LYS 93  124 124 LYS LYS C . n 
C 3 94  LEU 94  125 125 LEU LEU C . n 
C 3 95  GLY 95  126 126 GLY GLY C . n 
C 3 96  TYR 96  127 127 TYR TYR C . n 
C 3 97  GLY 97  128 128 GLY GLY C . n 
C 3 98  ASP 98  129 129 ASP ASP C . n 
C 3 99  GLY 99  130 130 GLY GLY C . n 
C 3 100 LEU 100 131 131 LEU LEU C . n 
C 3 101 VAL 101 132 132 VAL VAL C . n 
C 3 102 ILE 102 133 133 ILE ILE C . n 
C 3 103 LYS 103 134 134 LYS LYS C . n 
C 3 104 ASP 104 135 135 ASP ASP C . n 
C 3 105 LEU 105 136 136 LEU LEU C . n 
C 3 106 ASN 106 137 137 ASN ASN C . n 
C 3 107 LEU 107 138 138 LEU LEU C . n 
C 3 108 MET 108 139 139 MET MET C . n 
C 3 109 LEU 109 140 140 LEU LEU C . n 
C 3 110 LYS 110 141 141 LYS LYS C . n 
C 3 111 ASN 111 142 142 ASN ASN C . n 
C 3 112 GLY 112 143 143 GLY GLY C . n 
C 3 113 ASN 113 144 144 ASN ASN C . n 
C 3 114 MET 114 145 145 MET MET C . n 
C 3 115 GLY 115 146 146 GLY GLY C . n 
C 3 116 GLU 116 147 147 GLU GLU C . n 
C 3 117 LEU 117 148 148 LEU LEU C . n 
C 3 118 LYS 118 149 149 LYS LYS C . n 
C 3 119 ALA 119 150 150 ALA ALA C . n 
C 3 120 THR 120 151 151 THR THR C . n 
C 3 121 VAL 121 152 152 VAL VAL C . n 
C 3 122 GLY 122 153 153 GLY GLY C . n 
C 3 123 GLU 123 154 154 GLU GLU C . n 
C 3 124 ASN 124 155 155 ASN ASN C . n 
C 3 125 SER 125 156 156 SER SER C . n 
C 3 126 ASN 126 157 157 ASN ASN C . n 
C 3 127 ILE 127 158 158 ILE ILE C . n 
C 3 128 THR 128 159 159 THR THR C . n 
C 3 129 LEU 129 160 160 LEU LEU C . n 
C 3 130 PHE 130 161 161 PHE PHE C . n 
C 3 131 ASP 131 162 162 ASP ASP C . n 
C 3 132 VAL 132 163 163 VAL VAL C . n 
C 3 133 GLN 133 164 164 GLN GLN C . n 
C 3 134 GLU 134 165 165 GLU GLU C . n 
C 3 135 TYR 135 166 166 TYR TYR C . n 
C 3 136 SER 136 167 167 SER SER C . n 
C 3 137 VAL 137 168 168 VAL VAL C . n 
C 3 138 SER 138 169 169 SER SER C . n 
C 3 139 ASP 139 170 170 ASP ASP C . n 
C 3 140 ASN 140 171 171 ASN ASN C . n 
C 3 141 THR 141 172 172 THR THR C . n 
C 3 142 ILE 142 173 173 ILE ILE C . n 
C 3 143 THR 143 174 174 THR THR C . n 
C 3 144 VAL 144 175 175 VAL VAL C . n 
C 3 145 THR 145 176 176 THR THR C . n 
C 3 146 PRO 146 177 177 PRO PRO C . n 
C 3 147 LYS 147 178 178 LYS LYS C . n 
C 3 148 ILE 148 179 179 ILE ILE C . n 
C 3 149 PRO 149 180 180 PRO PRO C . n 
C 3 150 PRO 150 181 181 PRO PRO C . n 
C 3 151 CYS 151 182 182 CYS CYS C . n 
C 3 152 THR 152 183 183 THR THR C . n 
C 3 153 THR 153 184 184 THR THR C . n 
C 3 154 GLY 154 185 185 GLY GLY C . n 
C 3 155 THR 155 186 186 THR THR C . n 
C 3 156 TRP 156 187 187 TRP TRP C . n 
C 3 157 LYS 157 188 188 LYS LYS C . n 
C 3 158 PRO 158 189 189 PRO PRO C . n 
C 3 159 TRP 159 190 190 TRP TRP C . n 
C 3 160 HIS 160 191 191 HIS HIS C . n 
C 3 161 ASN 161 192 192 ASN ASN C . n 
C 3 162 ASP 162 193 193 ASP ASP C . n 
C 3 163 LEU 163 194 194 LEU LEU C . n 
C 3 164 THR 164 195 195 THR THR C . n 
C 3 165 SER 165 196 196 SER SER C . n 
C 3 166 LYS 166 197 197 LYS LYS C . n 
C 3 167 LEU 167 198 198 LEU LEU C . n 
C 3 168 GLY 168 199 199 GLY GLY C . n 
C 3 169 SER 169 200 200 SER SER C . n 
C 3 170 LEU 170 201 201 LEU LEU C . n 
C 3 171 LYS 171 202 202 LYS LYS C . n 
C 3 172 SER 172 203 203 SER SER C . n 
C 3 173 VAL 173 204 204 VAL VAL C . n 
C 3 174 PHE 174 205 205 PHE PHE C . n 
C 3 175 PHE 175 206 206 PHE PHE C . n 
C 3 176 GLU 176 207 207 GLU GLU C . n 
C 3 177 SER 177 208 208 SER SER C . n 
C 3 178 TYR 178 209 209 TYR TYR C . n 
C 3 179 THR 179 210 210 THR THR C . n 
C 3 180 CYS 180 211 211 CYS CYS C . n 
C 3 181 ASN 181 212 212 ASN ASN C . n 
C 3 182 ASN 182 213 213 ASN ASN C . n 
C 3 183 ASP 183 214 214 ASP ASP C . n 
C 3 184 ASP 184 215 215 ASP ASP C . n 
C 3 185 ILE 185 216 216 ILE ILE C . n 
C 3 186 ALA 186 217 217 ALA ALA C . n 
C 3 187 LYS 187 218 218 LYS LYS C . n 
C 3 188 LYS 188 219 219 LYS LYS C . n 
C 3 189 PRO 189 220 220 PRO PRO C . n 
C 3 190 LEU 190 221 221 LEU LEU C . n 
C 3 191 PRO 191 222 222 PRO PRO C . n 
C 3 192 LEU 192 223 223 LEU LEU C . n 
C 3 193 THR 193 224 224 THR THR C . n 
C 3 194 VAL 194 225 225 VAL VAL C . n 
C 3 195 VAL 195 226 226 VAL VAL C . n 
C 3 196 LEU 196 227 227 LEU LEU C . n 
C 3 197 ASN 197 228 228 ASN ASN C . n 
C 3 198 GLY 198 229 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        HEM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   HEM 
_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 
D 4 HEM 1   201 201 HEM HEM A . 
E 5 GOL 1   202 3   GOL GOL A . 
F 4 HEM 1   201 201 HEM HEM B . 
G 5 GOL 1   202 2   GOL GOL B . 
H 6 PO4 1   203 1   PO4 PO4 B . 
I 5 GOL 1   301 1   GOL GOL C . 
J 7 HOH 1   301 358 HOH HOH A . 
J 7 HOH 2   302 192 HOH HOH A . 
J 7 HOH 3   303 234 HOH HOH A . 
J 7 HOH 4   304 4   HOH HOH A . 
J 7 HOH 5   305 34  HOH HOH A . 
J 7 HOH 6   306 184 HOH HOH A . 
J 7 HOH 7   307 341 HOH HOH A . 
J 7 HOH 8   308 256 HOH HOH A . 
J 7 HOH 9   309 6   HOH HOH A . 
J 7 HOH 10  310 97  HOH HOH A . 
J 7 HOH 11  311 33  HOH HOH A . 
J 7 HOH 12  312 185 HOH HOH A . 
J 7 HOH 13  313 58  HOH HOH A . 
J 7 HOH 14  314 361 HOH HOH A . 
J 7 HOH 15  315 136 HOH HOH A . 
J 7 HOH 16  316 363 HOH HOH A . 
J 7 HOH 17  317 198 HOH HOH A . 
J 7 HOH 18  318 53  HOH HOH A . 
J 7 HOH 19  319 173 HOH HOH A . 
J 7 HOH 20  320 317 HOH HOH A . 
J 7 HOH 21  321 48  HOH HOH A . 
J 7 HOH 22  322 30  HOH HOH A . 
J 7 HOH 23  323 274 HOH HOH A . 
J 7 HOH 24  324 103 HOH HOH A . 
J 7 HOH 25  325 7   HOH HOH A . 
J 7 HOH 26  326 213 HOH HOH A . 
J 7 HOH 27  327 335 HOH HOH A . 
J 7 HOH 28  328 333 HOH HOH A . 
J 7 HOH 29  329 261 HOH HOH A . 
J 7 HOH 30  330 324 HOH HOH A . 
J 7 HOH 31  331 133 HOH HOH A . 
J 7 HOH 32  332 212 HOH HOH A . 
J 7 HOH 33  333 368 HOH HOH A . 
J 7 HOH 34  334 128 HOH HOH A . 
J 7 HOH 35  335 131 HOH HOH A . 
J 7 HOH 36  336 137 HOH HOH A . 
J 7 HOH 37  337 98  HOH HOH A . 
J 7 HOH 38  338 45  HOH HOH A . 
J 7 HOH 39  339 225 HOH HOH A . 
J 7 HOH 40  340 186 HOH HOH A . 
J 7 HOH 41  341 116 HOH HOH A . 
J 7 HOH 42  342 44  HOH HOH A . 
J 7 HOH 43  343 63  HOH HOH A . 
J 7 HOH 44  344 9   HOH HOH A . 
J 7 HOH 45  345 229 HOH HOH A . 
J 7 HOH 46  346 18  HOH HOH A . 
J 7 HOH 47  347 196 HOH HOH A . 
J 7 HOH 48  348 43  HOH HOH A . 
J 7 HOH 49  349 235 HOH HOH A . 
J 7 HOH 50  350 340 HOH HOH A . 
J 7 HOH 51  351 90  HOH HOH A . 
J 7 HOH 52  352 2   HOH HOH A . 
J 7 HOH 53  353 55  HOH HOH A . 
J 7 HOH 54  354 32  HOH HOH A . 
J 7 HOH 55  355 263 HOH HOH A . 
J 7 HOH 56  356 347 HOH HOH A . 
J 7 HOH 57  357 227 HOH HOH A . 
J 7 HOH 58  358 20  HOH HOH A . 
J 7 HOH 59  359 295 HOH HOH A . 
J 7 HOH 60  360 11  HOH HOH A . 
J 7 HOH 61  361 24  HOH HOH A . 
J 7 HOH 62  362 208 HOH HOH A . 
J 7 HOH 63  363 117 HOH HOH A . 
J 7 HOH 64  364 129 HOH HOH A . 
J 7 HOH 65  365 104 HOH HOH A . 
J 7 HOH 66  366 81  HOH HOH A . 
J 7 HOH 67  367 69  HOH HOH A . 
J 7 HOH 68  368 132 HOH HOH A . 
J 7 HOH 69  369 310 HOH HOH A . 
J 7 HOH 70  370 193 HOH HOH A . 
J 7 HOH 71  371 336 HOH HOH A . 
J 7 HOH 72  372 66  HOH HOH A . 
J 7 HOH 73  373 269 HOH HOH A . 
J 7 HOH 74  374 157 HOH HOH A . 
J 7 HOH 75  375 346 HOH HOH A . 
J 7 HOH 76  376 41  HOH HOH A . 
J 7 HOH 77  377 216 HOH HOH A . 
J 7 HOH 78  378 158 HOH HOH A . 
J 7 HOH 79  379 91  HOH HOH A . 
J 7 HOH 80  380 319 HOH HOH A . 
J 7 HOH 81  381 26  HOH HOH A . 
J 7 HOH 82  382 64  HOH HOH A . 
J 7 HOH 83  383 222 HOH HOH A . 
J 7 HOH 84  384 258 HOH HOH A . 
J 7 HOH 85  385 221 HOH HOH A . 
J 7 HOH 86  386 236 HOH HOH A . 
J 7 HOH 87  387 93  HOH HOH A . 
J 7 HOH 88  388 296 HOH HOH A . 
J 7 HOH 89  389 217 HOH HOH A . 
J 7 HOH 90  390 72  HOH HOH A . 
J 7 HOH 91  391 350 HOH HOH A . 
J 7 HOH 92  392 299 HOH HOH A . 
J 7 HOH 93  393 87  HOH HOH A . 
J 7 HOH 94  394 331 HOH HOH A . 
J 7 HOH 95  395 226 HOH HOH A . 
J 7 HOH 96  396 183 HOH HOH A . 
J 7 HOH 97  397 82  HOH HOH A . 
J 7 HOH 98  398 360 HOH HOH A . 
J 7 HOH 99  399 214 HOH HOH A . 
J 7 HOH 100 400 106 HOH HOH A . 
J 7 HOH 101 401 356 HOH HOH A . 
J 7 HOH 102 402 115 HOH HOH A . 
J 7 HOH 103 403 366 HOH HOH A . 
J 7 HOH 104 404 215 HOH HOH A . 
J 7 HOH 105 405 359 HOH HOH A . 
J 7 HOH 106 406 275 HOH HOH A . 
J 7 HOH 107 407 345 HOH HOH A . 
K 7 HOH 1   301 70  HOH HOH B . 
K 7 HOH 2   302 84  HOH HOH B . 
K 7 HOH 3   303 135 HOH HOH B . 
K 7 HOH 4   304 203 HOH HOH B . 
K 7 HOH 5   305 339 HOH HOH B . 
K 7 HOH 6   306 327 HOH HOH B . 
K 7 HOH 7   307 96  HOH HOH B . 
K 7 HOH 8   308 308 HOH HOH B . 
K 7 HOH 9   309 187 HOH HOH B . 
K 7 HOH 10  310 376 HOH HOH B . 
K 7 HOH 11  311 78  HOH HOH B . 
K 7 HOH 12  312 5   HOH HOH B . 
K 7 HOH 13  313 378 HOH HOH B . 
K 7 HOH 14  314 199 HOH HOH B . 
K 7 HOH 15  315 61  HOH HOH B . 
K 7 HOH 16  316 25  HOH HOH B . 
K 7 HOH 17  317 290 HOH HOH B . 
K 7 HOH 18  318 342 HOH HOH B . 
K 7 HOH 19  319 134 HOH HOH B . 
K 7 HOH 20  320 362 HOH HOH B . 
K 7 HOH 21  321 113 HOH HOH B . 
K 7 HOH 22  322 372 HOH HOH B . 
K 7 HOH 23  323 121 HOH HOH B . 
K 7 HOH 24  324 68  HOH HOH B . 
K 7 HOH 25  325 375 HOH HOH B . 
K 7 HOH 26  326 145 HOH HOH B . 
K 7 HOH 27  327 313 HOH HOH B . 
K 7 HOH 28  328 88  HOH HOH B . 
K 7 HOH 29  329 351 HOH HOH B . 
K 7 HOH 30  330 102 HOH HOH B . 
K 7 HOH 31  331 301 HOH HOH B . 
K 7 HOH 32  332 354 HOH HOH B . 
K 7 HOH 33  333 169 HOH HOH B . 
K 7 HOH 34  334 294 HOH HOH B . 
K 7 HOH 35  335 231 HOH HOH B . 
K 7 HOH 36  336 207 HOH HOH B . 
K 7 HOH 37  337 312 HOH HOH B . 
K 7 HOH 38  338 144 HOH HOH B . 
K 7 HOH 39  339 50  HOH HOH B . 
K 7 HOH 40  340 189 HOH HOH B . 
K 7 HOH 41  341 40  HOH HOH B . 
K 7 HOH 42  342 364 HOH HOH B . 
K 7 HOH 43  343 251 HOH HOH B . 
K 7 HOH 44  344 381 HOH HOH B . 
K 7 HOH 45  345 262 HOH HOH B . 
K 7 HOH 46  346 371 HOH HOH B . 
K 7 HOH 47  347 223 HOH HOH B . 
K 7 HOH 48  348 80  HOH HOH B . 
K 7 HOH 49  349 365 HOH HOH B . 
K 7 HOH 50  350 252 HOH HOH B . 
K 7 HOH 51  351 357 HOH HOH B . 
K 7 HOH 52  352 367 HOH HOH B . 
K 7 HOH 53  353 271 HOH HOH B . 
K 7 HOH 54  354 140 HOH HOH B . 
K 7 HOH 55  355 352 HOH HOH B . 
K 7 HOH 56  356 204 HOH HOH B . 
K 7 HOH 57  357 42  HOH HOH B . 
K 7 HOH 58  358 374 HOH HOH B . 
K 7 HOH 59  359 250 HOH HOH B . 
L 7 HOH 1   401 23  HOH HOH C . 
L 7 HOH 2   402 323 HOH HOH C . 
L 7 HOH 3   403 3   HOH HOH C . 
L 7 HOH 4   404 322 HOH HOH C . 
L 7 HOH 5   405 328 HOH HOH C . 
L 7 HOH 6   406 338 HOH HOH C . 
L 7 HOH 7   407 28  HOH HOH C . 
L 7 HOH 8   408 35  HOH HOH C . 
L 7 HOH 9   409 188 HOH HOH C . 
L 7 HOH 10  410 180 HOH HOH C . 
L 7 HOH 11  411 73  HOH HOH C . 
L 7 HOH 12  412 8   HOH HOH C . 
L 7 HOH 13  413 107 HOH HOH C . 
L 7 HOH 14  414 202 HOH HOH C . 
L 7 HOH 15  415 309 HOH HOH C . 
L 7 HOH 16  416 75  HOH HOH C . 
L 7 HOH 17  417 182 HOH HOH C . 
L 7 HOH 18  418 159 HOH HOH C . 
L 7 HOH 19  419 1   HOH HOH C . 
L 7 HOH 20  420 74  HOH HOH C . 
L 7 HOH 21  421 311 HOH HOH C . 
L 7 HOH 22  422 273 HOH HOH C . 
L 7 HOH 23  423 10  HOH HOH C . 
L 7 HOH 24  424 16  HOH HOH C . 
L 7 HOH 25  425 17  HOH HOH C . 
L 7 HOH 26  426 195 HOH HOH C . 
L 7 HOH 27  427 51  HOH HOH C . 
L 7 HOH 28  428 242 HOH HOH C . 
L 7 HOH 29  429 326 HOH HOH C . 
L 7 HOH 30  430 12  HOH HOH C . 
L 7 HOH 31  431 49  HOH HOH C . 
L 7 HOH 32  432 14  HOH HOH C . 
L 7 HOH 33  433 369 HOH HOH C . 
L 7 HOH 34  434 31  HOH HOH C . 
L 7 HOH 35  435 15  HOH HOH C . 
L 7 HOH 36  436 318 HOH HOH C . 
L 7 HOH 37  437 348 HOH HOH C . 
L 7 HOH 38  438 259 HOH HOH C . 
L 7 HOH 39  439 52  HOH HOH C . 
L 7 HOH 40  440 355 HOH HOH C . 
L 7 HOH 41  441 79  HOH HOH C . 
L 7 HOH 42  442 37  HOH HOH C . 
L 7 HOH 43  443 240 HOH HOH C . 
L 7 HOH 44  444 377 HOH HOH C . 
L 7 HOH 45  445 239 HOH HOH C . 
L 7 HOH 46  446 160 HOH HOH C . 
L 7 HOH 47  447 218 HOH HOH C . 
L 7 HOH 48  448 57  HOH HOH C . 
L 7 HOH 49  449 177 HOH HOH C . 
L 7 HOH 50  450 39  HOH HOH C . 
L 7 HOH 51  451 29  HOH HOH C . 
L 7 HOH 52  452 325 HOH HOH C . 
L 7 HOH 53  453 147 HOH HOH C . 
L 7 HOH 54  454 344 HOH HOH C . 
L 7 HOH 55  455 22  HOH HOH C . 
L 7 HOH 56  456 154 HOH HOH C . 
L 7 HOH 57  457 138 HOH HOH C . 
L 7 HOH 58  458 278 HOH HOH C . 
L 7 HOH 59  459 89  HOH HOH C . 
L 7 HOH 60  460 36  HOH HOH C . 
L 7 HOH 61  461 60  HOH HOH C . 
L 7 HOH 62  462 190 HOH HOH C . 
L 7 HOH 63  463 152 HOH HOH C . 
L 7 HOH 64  464 237 HOH HOH C . 
L 7 HOH 65  465 130 HOH HOH C . 
L 7 HOH 66  466 304 HOH HOH C . 
L 7 HOH 67  467 246 HOH HOH C . 
L 7 HOH 68  468 21  HOH HOH C . 
L 7 HOH 69  469 332 HOH HOH C . 
L 7 HOH 70  470 349 HOH HOH C . 
L 7 HOH 71  471 86  HOH HOH C . 
L 7 HOH 72  472 337 HOH HOH C . 
L 7 HOH 73  473 85  HOH HOH C . 
L 7 HOH 74  474 329 HOH HOH C . 
L 7 HOH 75  475 47  HOH HOH C . 
L 7 HOH 76  476 65  HOH HOH C . 
L 7 HOH 77  477 334 HOH HOH C . 
L 7 HOH 78  478 76  HOH HOH C . 
L 7 HOH 79  479 56  HOH HOH C . 
L 7 HOH 80  480 146 HOH HOH C . 
L 7 HOH 81  481 99  HOH HOH C . 
L 7 HOH 82  482 249 HOH HOH C . 
L 7 HOH 83  483 305 HOH HOH C . 
L 7 HOH 84  484 201 HOH HOH C . 
L 7 HOH 85  485 247 HOH HOH C . 
L 7 HOH 86  486 379 HOH HOH C . 
L 7 HOH 87  487 380 HOH HOH C . 
L 7 HOH 88  488 77  HOH HOH C . 
L 7 HOH 89  489 306 HOH HOH C . 
L 7 HOH 90  490 92  HOH HOH C . 
L 7 HOH 91  491 260 HOH HOH C . 
L 7 HOH 92  492 373 HOH HOH C . 
L 7 HOH 93  493 255 HOH HOH C . 
L 7 HOH 94  494 219 HOH HOH C . 
L 7 HOH 95  495 303 HOH HOH C . 
L 7 HOH 96  496 343 HOH HOH C . 
L 7 HOH 97  497 62  HOH HOH C . 
L 7 HOH 98  498 162 HOH HOH C . 
L 7 HOH 99  499 238 HOH HOH C . 
L 7 HOH 100 500 100 HOH HOH C . 
L 7 HOH 101 501 194 HOH HOH C . 
L 7 HOH 102 502 243 HOH HOH C . 
L 7 HOH 103 503 370 HOH HOH C . 
# 
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 B VAL 1   ? CG1 ? B VAL 1   CG1 
2  1 Y 1 B VAL 1   ? CG2 ? B VAL 1   CG2 
3  1 Y 1 B HIS 2   ? CG  ? B HIS 2   CG  
4  1 Y 1 B HIS 2   ? ND1 ? B HIS 2   ND1 
5  1 Y 1 B HIS 2   ? CD2 ? B HIS 2   CD2 
6  1 Y 1 B HIS 2   ? CE1 ? B HIS 2   CE1 
7  1 Y 1 B HIS 2   ? NE2 ? B HIS 2   NE2 
8  1 Y 1 B LYS 82  ? CG  ? B LYS 82  CG  
9  1 Y 1 B LYS 82  ? CD  ? B LYS 82  CD  
10 1 Y 1 B LYS 82  ? CE  ? B LYS 82  CE  
11 1 Y 1 B LYS 82  ? NZ  ? B LYS 82  NZ  
12 1 Y 1 B GLU 90  ? CG  ? B GLU 90  CG  
13 1 Y 1 B GLU 90  ? CD  ? B GLU 90  CD  
14 1 Y 1 B GLU 90  ? OE1 ? B GLU 90  OE1 
15 1 Y 1 B GLU 90  ? OE2 ? B GLU 90  OE2 
16 1 Y 1 C LYS 36  ? CG  ? C LYS 5   CG  
17 1 Y 1 C LYS 36  ? CD  ? C LYS 5   CD  
18 1 Y 1 C LYS 36  ? CE  ? C LYS 5   CE  
19 1 Y 1 C LYS 36  ? NZ  ? C LYS 5   NZ  
20 1 Y 1 C LYS 82  ? CD  ? C LYS 51  CD  
21 1 Y 1 C LYS 82  ? CE  ? C LYS 51  CE  
22 1 Y 1 C LYS 82  ? NZ  ? C LYS 51  NZ  
23 1 Y 1 C LYS 93  ? CG  ? C LYS 62  CG  
24 1 Y 1 C LYS 93  ? CD  ? C LYS 62  CD  
25 1 Y 1 C LYS 93  ? CE  ? C LYS 62  CE  
26 1 Y 1 C LYS 93  ? NZ  ? C LYS 62  NZ  
27 1 Y 1 C LYS 105 ? CD  ? C LYS 74  CD  
28 1 Y 1 C LYS 105 ? CE  ? C LYS 74  CE  
29 1 Y 1 C LYS 105 ? NZ  ? C LYS 74  NZ  
30 1 Y 1 C LYS 141 ? CD  ? C LYS 110 CD  
31 1 Y 1 C LYS 141 ? CE  ? C LYS 110 CE  
32 1 Y 1 C LYS 141 ? NZ  ? C LYS 110 NZ  
33 1 Y 1 C GLU 154 ? CG  ? C GLU 123 CG  
34 1 Y 1 C GLU 154 ? CD  ? C GLU 123 CD  
35 1 Y 1 C GLU 154 ? OE1 ? C GLU 123 OE1 
36 1 Y 1 C GLU 154 ? OE2 ? C GLU 123 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS       ? ? ? BUILT=20220820 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? XSCALE    ? ? ? .              2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .              3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER    ? ? ? 2.8.3          4 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? BUCCANEER ? ? ? 1.6.5          5 
? 'model building' ? ? ? ? ? ? ? ? ? ? ? Coot      ? ? ? 0.9.3          6 
? refinement       ? ? ? ? ? ? ? ? ? ? ? BUSTER    ? ? ? 2.10.4         7 
# 
_cell.angle_alpha                  90 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BCJ 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     58.925 
_cell.length_a_esd                 ? 
_cell.length_b                     58.925 
_cell.length_b_esd                 ? 
_cell.length_c                     286.146 
_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                         9BCJ 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                92 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 41 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BCJ 
_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             2.26 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.6 
_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              8.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '20% PEG-2000 MME, 100 mM Tris, 240 mM TMAO' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-02-28 
_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   0.97903 
_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                        'APS BEAMLINE 24-ID-C' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97903 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   24-ID-C 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9BCJ 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.691 
_reflns.d_resolution_low                               19.596 
_reflns.details                                        
;Some remarks regarding the mmCIF items written, the PDB Exchange Dictionary (PDBx/mmCIF) Version 5.0 supporting the data files in the current PDB archive (dictionary version 5.325, last updated 2020-04-13: http://mmcif.wwpdb.org/dictionaries/mmcif_pdbx_v50.dic/Index/) and the actual quantities provided by MRFANA (https://github.com/githubgphl/MRFANA) from the autoPROC package (https://www.globalphasing.com/autoproc/). In general, the mmCIF categories here should provide items that are currently used in the PDB archive. If there are alternatives, the one recommended by the PDB developers has been selected.

The distinction between *_all and *_obs quantities is not always clear: often only one version is actively used within the PDB archive (or is the one recommended by PDB developers). The intention of distinguishing between classes of reflections before and after some kind of observation criterion was applied, can in principle be useful - but such criteria change in various ways throughout the data processing steps (rejection of overloaded or too partial reflections, outlier/misfit rejections during scaling etc) and there is no retrospect computation of data scaling/merging statistics for the reflections used in the final refinement (where another observation criterion might have been applied). Typical data processing will usually only provide one version of statistics at various stages and these are given in the recommended item here, irrespective of the "_all" and "_obs" connotation, see e.g. the use of _reflns.pdbx_Rmerge_I_obs, _reflns.pdbx_Rrim_I_all and _reflns.pdbx_Rpim_I_all.

Please note that all statistics related to "merged intensities" (or "merging") are based on inverse-variance weighting of the individual measurements making up a symmetry-unique reflection. This is standard for several decades now, even if some of the dictionary definitions seem to suggest that a simple "mean" or "average" intensity is being used instead.

R-values are always given for all symmetry-equivalent reflections following Friedel's law, i.e. Bijvoet pairs are not treated separately (since we want to describe the overall mean intensity and not the mean I(+) and I(-) here).

The Rrim metric is identical to the Rmeas R-value and only differs in name.

_reflns.pdbx_number_measured_all is the number of measured intensities just before the final merging step (at which point no additional rejection takes place).

_reflns.number_obs is the number of symmetry-unique observations, i.e. the result of merging those measurements via inverse-variance weighting.

_reflns.pdbx_netI_over_sigmaI is based on the merged intensities (_reflns.number_obs) as expected.

_reflns.pdbx_redundancy is synonymous with "multiplicity".

The per-shell item _reflns_shell.number_measured_all corresponds to the overall value _reflns.pdbx_number_measured_all.

The per-shell item _reflns_shell.number_unique_all corresponds to the overall value _reflns.number_obs.

The per-shell item _reflns_shell.percent_possible_all corresponds to the overall value _reflns.percent_possible_obs.

The per-shell item _reflns_shell.meanI_over_sigI_obs corresponds to the overall value given as _reflns.pdbx_netI_over_sigmaI. But be aware of the incorrect definition of the former in the current dictionary!
;
_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                                     43427 
_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                           94.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                11.33 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.86 
_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                                0.0955 
_reflns.pdbx_Rpim_I_all                                0.0284 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       492180 
_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                              0.0910 
_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              94.5 
_reflns.pdbx_percent_possible_spherical                75.1 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    94.6 
_reflns.pdbx_percent_possible_spherical_anomalous      73.8 
_reflns.pdbx_redundancy_anomalous                      6.18 
_reflns.pdbx_CC_half_anomalous                         -0.198 
_reflns.pdbx_absDiff_over_sigma_anomalous              0.749 
_reflns.pdbx_percent_possible_anomalous                94.6 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
5.227 19.596 ? 31.81 21425 21425 ? 2170 2170 ? ? ? ? ? ? ? ? ? ? ? 9.87  ? ? ? 0.0639 0.0200 ? 1  ? 0.999 ? ? 99.6  ? 0.0605 ? 
99.6  99.6  99.1  99.1  6.03 -0.091 0.697 99.1  
4.116 5.227  ? 33.12 23533 23533 ? 2172 2172 ? ? ? ? ? ? ? ? ? ? ? 10.83 ? ? ? 0.0653 0.0195 ? 2  ? 0.998 ? ? 99.8  ? 0.0622 ? 
99.8  99.8  100.0 100.0 6.21 -0.299 0.659 100.0 
3.579 4.116  ? 31.93 24847 24847 ? 2172 2172 ? ? ? ? ? ? ? ? ? ? ? 11.44 ? ? ? 0.0706 0.0207 ? 3  ? 0.998 ? ? 100.0 ? 0.0674 ? 
100.0 100.0 100.0 100.0 6.41 -0.305 0.676 100.0 
3.240 3.579  ? 26.91 24439 24439 ? 2170 2170 ? ? ? ? ? ? ? ? ? ? ? 11.26 ? ? ? 0.0787 0.0234 ? 4  ? 0.992 ? ? 100.0 ? 0.0749 ? 
100.0 100.0 100.0 100.0 6.23 -0.214 0.687 100.0 
2.998 3.240  ? 21.14 22718 22718 ? 2171 2171 ? ? ? ? ? ? ? ? ? ? ? 10.46 ? ? ? 0.0930 0.0285 ? 5  ? 0.997 ? ? 99.5  ? 0.0883 ? 
99.5  99.5  99.5  99.5  5.74 -0.168 0.713 99.5  
2.816 2.998  ? 17.86 24975 24975 ? 2172 2172 ? ? ? ? ? ? ? ? ? ? ? 11.50 ? ? ? 0.1102 0.0328 ? 6  ? 0.998 ? ? 100.0 ? 0.1051 ? 
100.0 100.0 100.0 100.0 6.27 -0.087 0.723 100.0 
2.671 2.816  ? 15.58 25516 25516 ? 2172 2172 ? ? ? ? ? ? ? ? ? ? ? 11.75 ? ? ? 0.1327 0.0386 ? 7  ? 0.997 ? ? 100.0 ? 0.1268 ? 
100.0 100.0 100.0 100.0 6.41 -0.100 0.731 100.0 
2.552 2.671  ? 12.43 25946 25946 ? 2170 2170 ? ? ? ? ? ? ? ? ? ? ? 11.96 ? ? ? 0.1660 0.0479 ? 8  ? 0.996 ? ? 100.0 ? 0.1587 ? 
100.0 100.0 100.0 100.0 6.49 -0.148 0.732 100.0 
2.450 2.552  ? 11.16 26466 26466 ? 2173 2173 ? ? ? ? ? ? ? ? ? ? ? 12.18 ? ? ? 0.1948 0.0555 ? 9  ? 0.994 ? ? 100.0 ? 0.1865 ? 
100.0 100.0 100.0 100.0 6.57 -0.069 0.759 100.0 
2.363 2.450  ? 9.61  26755 26755 ? 2171 2171 ? ? ? ? ? ? ? ? ? ? ? 12.32 ? ? ? 0.2316 0.0657 ? 10 ? 0.993 ? ? 100.0 ? 0.2218 ? 
100.0 100.0 100.0 100.0 6.64 -0.122 0.725 100.0 
2.288 2.363  ? 8.30  26727 26727 ? 2173 2173 ? ? ? ? ? ? ? ? ? ? ? 12.30 ? ? ? 0.2791 0.0788 ? 11 ? 0.992 ? ? 100.0 ? 0.2675 ? 
100.0 100.0 100.0 100.0 6.63 -0.040 0.774 100.0 
2.221 2.288  ? 6.82  22822 22822 ? 2170 2170 ? ? ? ? ? ? ? ? ? ? ? 10.52 ? ? ? 0.3089 0.0939 ? 12 ? 0.986 ? ? 100.0 ? 0.2937 ? 
100.0 100.0 99.9  99.9  5.62 -0.027 0.772 99.9  
2.160 2.221  ? 6.16  24492 24492 ? 2171 2171 ? ? ? ? ? ? ? ? ? ? ? 11.28 ? ? ? 0.3678 0.1086 ? 13 ? 0.988 ? ? 100.0 ? 0.3510 ? 
100.0 100.0 100.0 100.0 6.04 -0.048 0.766 100.0 
2.106 2.160  ? 5.14  25459 25459 ? 2170 2170 ? ? ? ? ? ? ? ? ? ? ? 11.73 ? ? ? 0.4763 0.1377 ? 14 ? 0.979 ? ? 99.9  ? 0.4555 ? 
99.9  99.9  100.0 100.0 6.23 -0.052 0.770 100.0 
2.057 2.106  ? 4.47  25775 25775 ? 2172 2172 ? ? ? ? ? ? ? ? ? ? ? 11.87 ? ? ? 0.5740 0.1646 ? 15 ? 0.974 ? ? 100.0 ? 0.5495 ? 
100.0 100.0 100.0 100.0 6.35 -0.033 0.791 100.0 
2.012 2.057  ? 3.85  26075 26075 ? 2172 2172 ? ? ? ? ? ? ? ? ? ? ? 12.01 ? ? ? 0.6907 0.1966 ? 16 ? 0.960 ? ? 98.4  ? 0.6616 ? 
98.4  98.4  98.5  98.5  6.39 -0.006 0.785 98.5  
1.967 2.012  ? 3.15  26170 26170 ? 2171 2171 ? ? ? ? ? ? ? ? ? ? ? 12.05 ? ? ? 0.9009 0.2553 ? 17 ? 0.939 ? ? 92.4  ? 0.8633 ? 
92.4  92.4  92.9  92.9  6.40 0.016  0.807 92.9  
1.910 1.967  ? 3.15  25719 25719 ? 2172 2172 ? ? ? ? ? ? ? ? ? ? ? 11.84 ? ? ? 0.9019 0.2574 ? 18 ? 0.932 ? ? 72.8  ? 0.8636 ? 
72.8  65.9  72.6  65.2  6.33 -0.008 0.801 72.6  
1.835 1.910  ? 2.86  24166 24166 ? 2172 2172 ? ? ? ? ? ? ? ? ? ? ? 11.13 ? ? ? 0.9435 0.2765 ? 19 ? 0.918 ? ? 79.2  ? 0.9009 ? 
79.2  43.0  79.2  42.0  6.01 -0.071 0.777 79.2  
1.691 1.835  ? 1.81  18155 18155 ? 2171 2171 ? ? ? ? ? ? ? ? ? ? ? 8.36  ? ? ? 1.2663 0.4220 ? 20 ? 0.695 ? ? 70.4  ? 1.1894 ? 
70.4  17.6  73.2  17.0  4.54 -0.058 0.799 73.2  
# 
_refine.aniso_B[1][1]                            0.3796 
_refine.aniso_B[1][2]                            0 
_refine.aniso_B[1][3]                            0 
_refine.aniso_B[2][2]                            0.3796 
_refine.aniso_B[2][3]                            0 
_refine.aniso_B[3][3]                            -0.7592 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               32.82 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.955 
_refine.correlation_coeff_Fo_to_Fc_free          0.95 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9BCJ 
_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                            1.691 
_refine.ls_d_res_low                             19.6 
_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                     43427 
_refine.ls_number_reflns_R_free                  2174 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    75.1 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1898 
_refine.ls_R_factor_R_free                       0.2147 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1885 
_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                    ? 
_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               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_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   0.121 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.123 
_refine.pdbx_overall_SU_R_Blow_DPI               0.14 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_R_Cruickshank_DPI             0.133 
_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_analyze.entry_id                        9BCJ 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_sigma_a_free_details    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_sigma_a_obs_details     ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.RG_d_res_high                   ? 
_refine_analyze.RG_d_res_low                    ? 
_refine_analyze.RG_free                         ? 
_refine_analyze.RG_work                         ? 
_refine_analyze.RG_free_work_ratio              ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.691 
_refine_hist.d_res_low                        19.6 
_refine_hist.number_atoms_solvent             269 
_refine_hist.number_atoms_total               3960 
_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        3582 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         109 
_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' ? 0.009 ? 3805 ? t_bond_d                  2  HARMONIC     
'X-RAY DIFFRACTION' ? 0.91  ? 5182 ? t_angle_deg               2  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 1258 ? t_dihedral_angle_d        2  SINUSOIDAL   
'X-RAY DIFFRACTION' ? ?     ? 696  ? t_gen_planes              5  HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 3805 ? t_it                      10 HARMONIC     
'X-RAY DIFFRACTION' ? ?     ? 475  ? t_chiral_improper_torsion 5  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? ?     ? 3383 ? t_ideal_dist_contact      4  SEMIHARMONIC 
'X-RAY DIFFRACTION' ? 3.45  ? ?    ? t_omega_torsion           ?  ?            
'X-RAY DIFFRACTION' ? 15.3  ? ?    ? t_other_torsion           ?  ?            
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.691 
_refine_ls_shell.d_res_low                        1.78 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             42 
_refine_ls_shell.number_reflns_R_work             ? 
_refine_ls_shell.percent_reflns_obs               11.35 
_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                  0.274 
_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                  0.2632 
# 
_struct.entry_id                     9BCJ 
_struct.title                        
'Crystal structure of human hemoglobin in complex with the HbpA receptor from Corynebacterium diphtheriae' 
_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        9BCJ 
_struct_keywords.text            'Complex, Hemoglobin, heme, beta-sandwich, PROTEIN BINDING' 
_struct_keywords.pdbx_keywords   'PROTEIN BINDING' 
# 
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 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 5 ? 
J N N 7 ? 
K N N 7 ? 
L N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP HBA_HUMAN    P69905 ? 1 
;VLSPADKTNVKAAWGKVGAHAGEYGAEALERMFLSFPTTKTYFPHFDLSHGSAQVKGHGKKVADALTNAVAHVDDMPNAL
SALSDLHAHKLRVDPVNFKLLSHCLLVTLAAHLPAEFTPAVHASLDKFLASVSTVLTSKYR
;
2  
2 UNP HBB_HUMAN    P68871 ? 2 
;VHLTPEEKSAVTALWGKVNVDEVGGEALGRLLVVYPWTQRFFESFGDLSTPDAVMGNPKVKAHGKKVLGAFSDGLAHLDN
LKGTFATLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGKEFTPPVQAAYQKVVAGVANALAHKYH
;
2  
3 UNP Q6NEE5_CORDI Q6NEE5 ? 3 
;AEEVKNADLYWGFSGSSHHKYDHNGPKFEKAGKGAELTNIDAASAYAETFKKGVFPNNKREKSDILVFHNGEVKTETNHS
SYQINWPGEVTMKLGYGDGLVIKDLNLMLKNGNMGELKATVGENSNITLFDVQEYSVSDNTITVTPKIPPCTTGTWKPWH
NDLTSKLGSLKSVFFESYTCNNDDIAKKPLPLTVVLNG
;
32 
# 
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 9BCJ A 1 ? 141 ? P69905 2  ? 142 ? 1  141 
2 2 9BCJ B 1 ? 146 ? P68871 2  ? 147 ? 1  146 
3 3 9BCJ C 1 ? 198 ? Q6NEE5 32 ? 229 ? 32 229 
# 
_struct_ref_seq_dif.align_id                     3 
_struct_ref_seq_dif.pdbx_pdb_id_code             9BCJ 
_struct_ref_seq_dif.mon_id                       SER 
_struct_ref_seq_dif.pdbx_pdb_strand_id           C 
_struct_ref_seq_dif.seq_num                      1 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   Q6NEE5 
_struct_ref_seq_dif.db_mon_id                    ALA 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          32 
_struct_ref_seq_dif.details                      conflict 
_struct_ref_seq_dif.pdbx_auth_seq_num            32 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 17660 ? 
1 MORE         -153  ? 
1 'SSA (A^2)'  36630 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z  1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000 
2 'crystal symmetry operation' 7_555 y,x,-z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 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 SER A 3   ? LYS A 16  ? SER A 3   LYS A 16  1 ? 14 
HELX_P HELX_P2  AA2 VAL A 17  ? ALA A 19  ? VAL A 17  ALA A 19  5 ? 3  
HELX_P HELX_P3  AA3 HIS A 20  ? PHE A 36  ? HIS A 20  PHE A 36  1 ? 17 
HELX_P HELX_P4  AA4 PRO A 37  ? PHE A 43  ? PRO A 37  PHE A 43  5 ? 7  
HELX_P HELX_P5  AA5 SER A 52  ? HIS A 72  ? SER A 52  HIS A 72  1 ? 21 
HELX_P HELX_P6  AA6 ASP A 75  ? LEU A 80  ? ASP A 75  LEU A 80  1 ? 6  
HELX_P HELX_P7  AA7 LEU A 80  ? HIS A 89  ? LEU A 80  HIS A 89  1 ? 10 
HELX_P HELX_P8  AA8 ASP A 94  ? LEU A 113 ? ASP A 94  LEU A 113 1 ? 20 
HELX_P HELX_P9  AA9 THR A 118 ? SER A 138 ? THR A 118 SER A 138 1 ? 21 
HELX_P HELX_P10 AB1 THR B 4   ? GLY B 16  ? THR B 4   GLY B 16  1 ? 13 
HELX_P HELX_P11 AB2 GLU B 22  ? TYR B 35  ? GLU B 22  TYR B 35  1 ? 14 
HELX_P HELX_P12 AB3 PRO B 36  ? GLY B 46  ? PRO B 36  GLY B 46  5 ? 11 
HELX_P HELX_P13 AB4 THR B 50  ? ASN B 57  ? THR B 50  ASN B 57  1 ? 8  
HELX_P HELX_P14 AB5 ASN B 57  ? HIS B 77  ? ASN B 57  HIS B 77  1 ? 21 
HELX_P HELX_P15 AB6 ASN B 80  ? PHE B 85  ? ASN B 80  PHE B 85  1 ? 6  
HELX_P HELX_P16 AB7 PHE B 85  ? LYS B 95  ? PHE B 85  LYS B 95  1 ? 11 
HELX_P HELX_P17 AB8 PRO B 100 ? GLY B 119 ? PRO B 100 GLY B 119 1 ? 20 
HELX_P HELX_P18 AB9 LYS B 120 ? PHE B 122 ? LYS B 120 PHE B 122 5 ? 3  
HELX_P HELX_P19 AC1 THR B 123 ? ALA B 142 ? THR B 123 ALA B 142 1 ? 20 
HELX_P HELX_P20 AC2 SER C 14  ? HIS C 19  ? SER C 45  HIS C 50  5 ? 6  
HELX_P HELX_P21 AC3 TYR C 21  ? GLY C 25  ? TYR C 52  GLY C 56  5 ? 5  
HELX_P HELX_P22 AC4 ASP C 41  ? ALA C 45  ? ASP C 72  ALA C 76  5 ? 5  
HELX_P HELX_P23 AC5 TYR C 46  ? LYS C 52  ? TYR C 77  LYS C 83  1 ? 7  
HELX_P HELX_P24 AC6 HIS C 160 ? GLY C 168 ? HIS C 191 GLY C 199 1 ? 9  
HELX_P HELX_P25 AC7 LEU C 170 ? PHE C 175 ? LEU C 201 PHE C 206 5 ? 6  
HELX_P HELX_P26 AC8 ASN C 181 ? ALA C 186 ? ASN C 212 ALA C 217 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1 disulf ? ? C CYS 151 SG  ? ? ? 1_555 C CYS 180 SG ? ? C CYS 182 C CYS 211 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
metalc1 metalc ? ? A HIS 87  NE2 ? ? ? 1_555 D HEM .   FE ? ? A HIS 87  A HEM 201 1_555 ? ? ? ? ? ? ? 2.105 ? ? 
metalc2 metalc ? ? D HEM .   FE  ? ? ? 1_555 J HOH .   O  ? ? A HEM 201 A HOH 330 1_555 ? ? ? ? ? ? ? 2.166 ? ? 
metalc3 metalc ? ? B HIS 92  NE2 ? ? ? 1_555 F HEM .   FE ? ? B HIS 92  B HEM 201 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc4 metalc ? ? F HEM .   FE  ? ? ? 1_555 K HOH .   O  ? ? B HEM 201 B HOH 317 1_555 ? ? ? ? ? ? ? 2.279 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 NA ? D HEM . ? A HEM 201 ? 1_555 88.9  ? 
2  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 NB ? D HEM . ? A HEM 201 ? 1_555 89.4  ? 
3  NA  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 NB ? D HEM . ? A HEM 201 ? 1_555 88.6  ? 
4  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 NC ? D HEM . ? A HEM 201 ? 1_555 94.3  ? 
5  NA  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 NC ? D HEM . ? A HEM 201 ? 1_555 176.8 ? 
6  NB  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 NC ? D HEM . ? A HEM 201 ? 1_555 91.1  ? 
7  NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 ND ? D HEM . ? A HEM 201 ? 1_555 91.0  ? 
8  NA  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 ND ? D HEM . ? A HEM 201 ? 1_555 90.9  ? 
9  NB  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 ND ? D HEM . ? A HEM 201 ? 1_555 179.4 ? 
10 NC  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 ND ? D HEM . ? A HEM 201 ? 1_555 89.4  ? 
11 NE2 ? A HIS 87 ? A HIS 87  ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 O  ? J HOH . ? A HOH 330 ? 1_555 176.1 ? 
12 NA  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 O  ? J HOH . ? A HOH 330 ? 1_555 93.2  ? 
13 NB  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 O  ? J HOH . ? A HOH 330 ? 1_555 87.4  ? 
14 NC  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 O  ? J HOH . ? A HOH 330 ? 1_555 83.6  ? 
15 ND  ? D HEM .  ? A HEM 201 ? 1_555 FE ? D HEM . ? A HEM 201 ? 1_555 O  ? J HOH . ? A HOH 330 ? 1_555 92.3  ? 
16 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NA ? F HEM . ? B HEM 201 ? 1_555 87.9  ? 
17 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NB ? F HEM . ? B HEM 201 ? 1_555 88.6  ? 
18 NA  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NB ? F HEM . ? B HEM 201 ? 1_555 88.5  ? 
19 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NC ? F HEM . ? B HEM 201 ? 1_555 93.6  ? 
20 NA  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NC ? F HEM . ? B HEM 201 ? 1_555 178.4 ? 
21 NB  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 NC ? F HEM . ? B HEM 201 ? 1_555 91.1  ? 
22 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 ND ? F HEM . ? B HEM 201 ? 1_555 92.3  ? 
23 NA  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 ND ? F HEM . ? B HEM 201 ? 1_555 91.1  ? 
24 NB  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 ND ? F HEM . ? B HEM 201 ? 1_555 179.0 ? 
25 NC  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 ND ? F HEM . ? B HEM 201 ? 1_555 89.3  ? 
26 NE2 ? B HIS 92 ? B HIS 92  ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 O  ? K HOH . ? B HOH 317 ? 1_555 174.9 ? 
27 NA  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 O  ? K HOH . ? B HOH 317 ? 1_555 97.1  ? 
28 NB  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 O  ? K HOH . ? B HOH 317 ? 1_555 91.9  ? 
29 NC  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 O  ? K HOH . ? B HOH 317 ? 1_555 81.3  ? 
30 ND  ? F HEM .  ? B HEM 201 ? 1_555 FE ? F HEM . ? B HEM 201 ? 1_555 O  ? K HOH . ? B HOH 317 ? 1_555 87.4  ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      C 
_pdbx_modification_feature.label_seq_id                       151 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     C 
_pdbx_modification_feature.modified_residue_label_seq_id      180 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       C 
_pdbx_modification_feature.auth_seq_id                        182 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      C 
_pdbx_modification_feature.modified_residue_auth_seq_id       211 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6  ? 
AA2 ? 10 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2  ? anti-parallel 
AA1 2 3  ? anti-parallel 
AA1 3 4  ? anti-parallel 
AA1 4 5  ? anti-parallel 
AA1 5 6  ? anti-parallel 
AA2 1 2  ? anti-parallel 
AA2 2 3  ? anti-parallel 
AA2 3 4  ? anti-parallel 
AA2 4 5  ? anti-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 
# 
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  LYS C 27  ? GLY C 32  ? LYS C 58  GLY C 63  
AA1 2  GLU C 89  ? LYS C 93  ? GLU C 120 LYS C 124 
AA1 3  LEU C 100 ? LYS C 110 ? LEU C 131 LYS C 141 
AA1 4  TYR C 82  ? ASN C 85  ? TYR C 113 ASN C 116 
AA1 5  ASP C 64  ? LYS C 74  ? ASP C 95  LYS C 105 
AA1 6  ALA C 35  ? ASN C 39  ? ALA C 66  ASN C 70  
AA2 1  LYS C 27  ? GLY C 32  ? LYS C 58  GLY C 63  
AA2 2  GLU C 89  ? LYS C 93  ? GLU C 120 LYS C 124 
AA2 3  LEU C 100 ? LYS C 110 ? LEU C 131 LYS C 141 
AA2 4  MET C 114 ? VAL C 121 ? MET C 145 VAL C 152 
AA2 5  ASN C 124 ? SER C 138 ? ASN C 155 SER C 169 
AA2 6  THR C 141 ? PRO C 146 ? THR C 172 PRO C 177 
AA2 7  LEU C 192 ? ASN C 197 ? LEU C 223 ASN C 228 
AA2 8  ASN C 6   ? TRP C 11  ? ASN C 37  TRP C 42  
AA2 9  ASP C 64  ? LYS C 74  ? ASP C 95  LYS C 105 
AA2 10 ALA C 35  ? ASN C 39  ? ALA C 66  ASN C 70  
# 
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 LYS C 27  ? N LYS C 58  O LYS C 93  ? O LYS C 124 
AA1 2 3  N VAL C 90  ? N VAL C 121 O ILE C 102 ? O ILE C 133 
AA1 3 4  O LEU C 107 ? O LEU C 138 N ILE C 84  ? N ILE C 115 
AA1 4 5  O ASN C 85  ? O ASN C 116 N GLU C 72  ? N GLU C 103 
AA1 5 6  O ILE C 65  ? O ILE C 96  N THR C 38  ? N THR C 69  
AA2 1 2  N LYS C 27  ? N LYS C 58  O LYS C 93  ? O LYS C 124 
AA2 2 3  N VAL C 90  ? N VAL C 121 O ILE C 102 ? O ILE C 133 
AA2 3 4  N LYS C 103 ? N LYS C 134 O THR C 120 ? O THR C 151 
AA2 4 5  N LEU C 117 ? N LEU C 148 O LEU C 129 ? O LEU C 160 
AA2 5 6  N GLU C 134 ? N GLU C 165 O THR C 145 ? O THR C 176 
AA2 6 7  N ILE C 142 ? N ILE C 173 O VAL C 194 ? O VAL C 225 
AA2 7 8  O ASN C 197 ? O ASN C 228 N ASN C 6   ? N ASN C 37  
AA2 8 9  N LEU C 9   ? N LEU C 40  O PHE C 68  ? O PHE C 99  
AA2 9 10 O ILE C 65  ? O ILE C 96  N THR C 38  ? N THR C 69  
# 
_pdbx_entry_details.entry_id                   9BCJ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 75  ? ? -147.21 37.75   
2 1 LYS A 90  ? ? -94.83  -63.99  
3 1 ASN B 80  ? ? -156.57 52.57   
4 1 CYS B 93  ? ? -93.37  -67.91  
5 1 PHE C 44  ? ? 69.90   -70.50  
6 1 ASP C 170 ? ? 67.19   -122.27 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? ? -32.8658 -45.8685 12.3822 0.0071  ? 0.0295 ? -0.0045 ? -0.0196 ? 0.0074  ? -0.0289 ? 1.0356 ? -0.2933 ? 
-0.3313 ? 0.7193 ? 0.3398  ? 1.8537 ? 0.0125  ? 0.0584 ? 0.2375  ? 0.0584 ? 0.0491  ? 0.0938  ? 0.2375  ? 0.0938  ? -0.0616 ? 
2 'X-RAY DIFFRACTION' ? ? -39.3228 -15.7814 3.2935  0.0942  ? 0.0501 ? 0.0178  ? -0.1114 ? -0.0233 ? -0.0401 ? 0.7076 ? 0.3296  ? 
-0.3456 ? 2.1749 ? -0.7825 ? 2.9881 ? 0.0676  ? 0.1641 ? -0.6076 ? 0.1641 ? -0.0167 ? -0.1467 ? -0.6076 ? -0.1467 ? -0.0509 ? 
3 'X-RAY DIFFRACTION' ? ? -59.1084 -47.2901 31.3708 -0.1039 ? 0.0094 ? 0.0082  ? 0.0894  ? 0.0576  ? -0.0727 ? 1.3571 ? 0.0205  ? 
-0.5272 ? 1.2499 ? -1.1418 ? 3.6231 ? -0.0274 ? 0.0749 ? -0.0298 ? 0.0749 ? 0.1992  ? -0.4559 ? -0.0298 ? -0.4559 ? -0.1719 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 1   ? ? ? A 141 ? ? '{ A|* }' 
2 'X-RAY DIFFRACTION' 1 ? ? A 201 ? ? ? A 201 ? ? '{ A|* }' 
3 'X-RAY DIFFRACTION' 2 ? ? B 1   ? ? ? B 142 ? ? '{ B|* }' 
4 'X-RAY DIFFRACTION' 2 ? ? B 201 ? ? ? B 201 ? ? '{ B|* }' 
5 'X-RAY DIFFRACTION' 3 ? ? C 36  ? ? ? C 228 ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 B HIS 143 ? B HIS 143 
2  1 Y 1 B LYS 144 ? B LYS 144 
3  1 Y 1 B TYR 145 ? B TYR 145 
4  1 Y 1 B HIS 146 ? B HIS 146 
5  1 Y 1 C SER 32  ? C SER 1   
6  1 Y 1 C GLU 33  ? C GLU 2   
7  1 Y 1 C GLU 34  ? C GLU 3   
8  1 Y 1 C VAL 35  ? C VAL 4   
9  1 Y 1 C GLU 107 ? C GLU 76  
10 1 Y 1 C THR 108 ? C THR 77  
11 1 Y 1 C ASN 109 ? C ASN 78  
12 1 Y 1 C HIS 110 ? C HIS 79  
13 1 Y 1 C SER 111 ? C SER 80  
14 1 Y 1 C GLY 229 ? C GLY 198 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
GOL C1   C  N N 137 
GOL O1   O  N N 138 
GOL C2   C  N N 139 
GOL O2   O  N N 140 
GOL C3   C  N N 141 
GOL O3   O  N N 142 
GOL H11  H  N N 143 
GOL H12  H  N N 144 
GOL HO1  H  N N 145 
GOL H2   H  N N 146 
GOL HO2  H  N N 147 
GOL H31  H  N N 148 
GOL H32  H  N N 149 
GOL HO3  H  N N 150 
HEM CHA  C  N N 151 
HEM CHB  C  N N 152 
HEM CHC  C  N N 153 
HEM CHD  C  N N 154 
HEM C1A  C  Y N 155 
HEM C2A  C  Y N 156 
HEM C3A  C  Y N 157 
HEM C4A  C  Y N 158 
HEM CMA  C  N N 159 
HEM CAA  C  N N 160 
HEM CBA  C  N N 161 
HEM CGA  C  N N 162 
HEM O1A  O  N N 163 
HEM O2A  O  N N 164 
HEM C1B  C  N N 165 
HEM C2B  C  N N 166 
HEM C3B  C  N N 167 
HEM C4B  C  N N 168 
HEM CMB  C  N N 169 
HEM CAB  C  N N 170 
HEM CBB  C  N N 171 
HEM C1C  C  Y N 172 
HEM C2C  C  Y N 173 
HEM C3C  C  Y N 174 
HEM C4C  C  Y N 175 
HEM CMC  C  N N 176 
HEM CAC  C  N N 177 
HEM CBC  C  N N 178 
HEM C1D  C  N N 179 
HEM C2D  C  N N 180 
HEM C3D  C  N N 181 
HEM C4D  C  N N 182 
HEM CMD  C  N N 183 
HEM CAD  C  N N 184 
HEM CBD  C  N N 185 
HEM CGD  C  N N 186 
HEM O1D  O  N N 187 
HEM O2D  O  N N 188 
HEM NA   N  Y N 189 
HEM NB   N  N N 190 
HEM NC   N  Y N 191 
HEM ND   N  N N 192 
HEM FE   FE N N 193 
HEM HHB  H  N N 194 
HEM HHC  H  N N 195 
HEM HHD  H  N N 196 
HEM HMA  H  N N 197 
HEM HMAA H  N N 198 
HEM HMAB H  N N 199 
HEM HAA  H  N N 200 
HEM HAAA H  N N 201 
HEM HBA  H  N N 202 
HEM HBAA H  N N 203 
HEM HMB  H  N N 204 
HEM HMBA H  N N 205 
HEM HMBB H  N N 206 
HEM HAB  H  N N 207 
HEM HBB  H  N N 208 
HEM HBBA H  N N 209 
HEM HMC  H  N N 210 
HEM HMCA H  N N 211 
HEM HMCB H  N N 212 
HEM HAC  H  N N 213 
HEM HBC  H  N N 214 
HEM HBCA H  N N 215 
HEM HMD  H  N N 216 
HEM HMDA H  N N 217 
HEM HMDB H  N N 218 
HEM HAD  H  N N 219 
HEM HADA H  N N 220 
HEM HBD  H  N N 221 
HEM HBDA H  N N 222 
HEM H2A  H  N N 223 
HEM H2D  H  N N 224 
HEM HHA  H  N N 225 
HIS N    N  N N 226 
HIS CA   C  N S 227 
HIS C    C  N N 228 
HIS O    O  N N 229 
HIS CB   C  N N 230 
HIS CG   C  Y N 231 
HIS ND1  N  Y N 232 
HIS CD2  C  Y N 233 
HIS CE1  C  Y N 234 
HIS NE2  N  Y N 235 
HIS OXT  O  N N 236 
HIS H    H  N N 237 
HIS H2   H  N N 238 
HIS HA   H  N N 239 
HIS HB2  H  N N 240 
HIS HB3  H  N N 241 
HIS HD1  H  N N 242 
HIS HD2  H  N N 243 
HIS HE1  H  N N 244 
HIS HE2  H  N N 245 
HIS HXT  H  N N 246 
HOH O    O  N N 247 
HOH H1   H  N N 248 
HOH H2   H  N N 249 
ILE N    N  N N 250 
ILE CA   C  N S 251 
ILE C    C  N N 252 
ILE O    O  N N 253 
ILE CB   C  N S 254 
ILE CG1  C  N N 255 
ILE CG2  C  N N 256 
ILE CD1  C  N N 257 
ILE OXT  O  N N 258 
ILE H    H  N N 259 
ILE H2   H  N N 260 
ILE HA   H  N N 261 
ILE HB   H  N N 262 
ILE HG12 H  N N 263 
ILE HG13 H  N N 264 
ILE HG21 H  N N 265 
ILE HG22 H  N N 266 
ILE HG23 H  N N 267 
ILE HD11 H  N N 268 
ILE HD12 H  N N 269 
ILE HD13 H  N N 270 
ILE HXT  H  N N 271 
LEU N    N  N N 272 
LEU CA   C  N S 273 
LEU C    C  N N 274 
LEU O    O  N N 275 
LEU CB   C  N N 276 
LEU CG   C  N N 277 
LEU CD1  C  N N 278 
LEU CD2  C  N N 279 
LEU OXT  O  N N 280 
LEU H    H  N N 281 
LEU H2   H  N N 282 
LEU HA   H  N N 283 
LEU HB2  H  N N 284 
LEU HB3  H  N N 285 
LEU HG   H  N N 286 
LEU HD11 H  N N 287 
LEU HD12 H  N N 288 
LEU HD13 H  N N 289 
LEU HD21 H  N N 290 
LEU HD22 H  N N 291 
LEU HD23 H  N N 292 
LEU HXT  H  N N 293 
LYS N    N  N N 294 
LYS CA   C  N S 295 
LYS C    C  N N 296 
LYS O    O  N N 297 
LYS CB   C  N N 298 
LYS CG   C  N N 299 
LYS CD   C  N N 300 
LYS CE   C  N N 301 
LYS NZ   N  N N 302 
LYS OXT  O  N N 303 
LYS H    H  N N 304 
LYS H2   H  N N 305 
LYS HA   H  N N 306 
LYS HB2  H  N N 307 
LYS HB3  H  N N 308 
LYS HG2  H  N N 309 
LYS HG3  H  N N 310 
LYS HD2  H  N N 311 
LYS HD3  H  N N 312 
LYS HE2  H  N N 313 
LYS HE3  H  N N 314 
LYS HZ1  H  N N 315 
LYS HZ2  H  N N 316 
LYS HZ3  H  N N 317 
LYS HXT  H  N N 318 
MET N    N  N N 319 
MET CA   C  N S 320 
MET C    C  N N 321 
MET O    O  N N 322 
MET CB   C  N N 323 
MET CG   C  N N 324 
MET SD   S  N N 325 
MET CE   C  N N 326 
MET OXT  O  N N 327 
MET H    H  N N 328 
MET H2   H  N N 329 
MET HA   H  N N 330 
MET HB2  H  N N 331 
MET HB3  H  N N 332 
MET HG2  H  N N 333 
MET HG3  H  N N 334 
MET HE1  H  N N 335 
MET HE2  H  N N 336 
MET HE3  H  N N 337 
MET HXT  H  N N 338 
PHE N    N  N N 339 
PHE CA   C  N S 340 
PHE C    C  N N 341 
PHE O    O  N N 342 
PHE CB   C  N N 343 
PHE CG   C  Y N 344 
PHE CD1  C  Y N 345 
PHE CD2  C  Y N 346 
PHE CE1  C  Y N 347 
PHE CE2  C  Y N 348 
PHE CZ   C  Y N 349 
PHE OXT  O  N N 350 
PHE H    H  N N 351 
PHE H2   H  N N 352 
PHE HA   H  N N 353 
PHE HB2  H  N N 354 
PHE HB3  H  N N 355 
PHE HD1  H  N N 356 
PHE HD2  H  N N 357 
PHE HE1  H  N N 358 
PHE HE2  H  N N 359 
PHE HZ   H  N N 360 
PHE HXT  H  N N 361 
PO4 P    P  N N 362 
PO4 O1   O  N N 363 
PO4 O2   O  N N 364 
PO4 O3   O  N N 365 
PO4 O4   O  N N 366 
PRO N    N  N N 367 
PRO CA   C  N S 368 
PRO C    C  N N 369 
PRO O    O  N N 370 
PRO CB   C  N N 371 
PRO CG   C  N N 372 
PRO CD   C  N N 373 
PRO OXT  O  N N 374 
PRO H    H  N N 375 
PRO HA   H  N N 376 
PRO HB2  H  N N 377 
PRO HB3  H  N N 378 
PRO HG2  H  N N 379 
PRO HG3  H  N N 380 
PRO HD2  H  N N 381 
PRO HD3  H  N N 382 
PRO HXT  H  N N 383 
SER N    N  N N 384 
SER CA   C  N S 385 
SER C    C  N N 386 
SER O    O  N N 387 
SER CB   C  N N 388 
SER OG   O  N N 389 
SER OXT  O  N N 390 
SER H    H  N N 391 
SER H2   H  N N 392 
SER HA   H  N N 393 
SER HB2  H  N N 394 
SER HB3  H  N N 395 
SER HG   H  N N 396 
SER HXT  H  N N 397 
THR N    N  N N 398 
THR CA   C  N S 399 
THR C    C  N N 400 
THR O    O  N N 401 
THR CB   C  N R 402 
THR OG1  O  N N 403 
THR CG2  C  N N 404 
THR OXT  O  N N 405 
THR H    H  N N 406 
THR H2   H  N N 407 
THR HA   H  N N 408 
THR HB   H  N N 409 
THR HG1  H  N N 410 
THR HG21 H  N N 411 
THR HG22 H  N N 412 
THR HG23 H  N N 413 
THR HXT  H  N N 414 
TRP N    N  N N 415 
TRP CA   C  N S 416 
TRP C    C  N N 417 
TRP O    O  N N 418 
TRP CB   C  N N 419 
TRP CG   C  Y N 420 
TRP CD1  C  Y N 421 
TRP CD2  C  Y N 422 
TRP NE1  N  Y N 423 
TRP CE2  C  Y N 424 
TRP CE3  C  Y N 425 
TRP CZ2  C  Y N 426 
TRP CZ3  C  Y N 427 
TRP CH2  C  Y N 428 
TRP OXT  O  N N 429 
TRP H    H  N N 430 
TRP H2   H  N N 431 
TRP HA   H  N N 432 
TRP HB2  H  N N 433 
TRP HB3  H  N N 434 
TRP HD1  H  N N 435 
TRP HE1  H  N N 436 
TRP HE3  H  N N 437 
TRP HZ2  H  N N 438 
TRP HZ3  H  N N 439 
TRP HH2  H  N N 440 
TRP HXT  H  N N 441 
TYR N    N  N N 442 
TYR CA   C  N S 443 
TYR C    C  N N 444 
TYR O    O  N N 445 
TYR CB   C  N N 446 
TYR CG   C  Y N 447 
TYR CD1  C  Y N 448 
TYR CD2  C  Y N 449 
TYR CE1  C  Y N 450 
TYR CE2  C  Y N 451 
TYR CZ   C  Y N 452 
TYR OH   O  N N 453 
TYR OXT  O  N N 454 
TYR H    H  N N 455 
TYR H2   H  N N 456 
TYR HA   H  N N 457 
TYR HB2  H  N N 458 
TYR HB3  H  N N 459 
TYR HD1  H  N N 460 
TYR HD2  H  N N 461 
TYR HE1  H  N N 462 
TYR HE2  H  N N 463 
TYR HH   H  N N 464 
TYR HXT  H  N N 465 
VAL N    N  N N 466 
VAL CA   C  N S 467 
VAL C    C  N N 468 
VAL O    O  N N 469 
VAL CB   C  N N 470 
VAL CG1  C  N N 471 
VAL CG2  C  N N 472 
VAL OXT  O  N N 473 
VAL H    H  N N 474 
VAL H2   H  N N 475 
VAL HA   H  N N 476 
VAL HB   H  N N 477 
VAL HG11 H  N N 478 
VAL HG12 H  N N 479 
VAL HG13 H  N N 480 
VAL HG21 H  N N 481 
VAL HG22 H  N N 482 
VAL HG23 H  N N 483 
VAL HXT  H  N N 484 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HEM CHA C1A  sing N N 142 
HEM CHA C4D  doub N N 143 
HEM CHA HHA  sing N N 144 
HEM CHB C4A  sing N N 145 
HEM CHB C1B  doub N N 146 
HEM CHB HHB  sing N N 147 
HEM CHC C4B  sing N N 148 
HEM CHC C1C  doub N N 149 
HEM CHC HHC  sing N N 150 
HEM CHD C4C  doub N N 151 
HEM CHD C1D  sing N N 152 
HEM CHD HHD  sing N N 153 
HEM C1A C2A  doub Y N 154 
HEM C1A NA   sing Y N 155 
HEM C2A C3A  sing Y N 156 
HEM C2A CAA  sing N N 157 
HEM C3A C4A  doub Y N 158 
HEM C3A CMA  sing N N 159 
HEM C4A NA   sing Y N 160 
HEM CMA HMA  sing N N 161 
HEM CMA HMAA sing N N 162 
HEM CMA HMAB sing N N 163 
HEM CAA CBA  sing N N 164 
HEM CAA HAA  sing N N 165 
HEM CAA HAAA sing N N 166 
HEM CBA CGA  sing N N 167 
HEM CBA HBA  sing N N 168 
HEM CBA HBAA sing N N 169 
HEM CGA O1A  doub N N 170 
HEM CGA O2A  sing N N 171 
HEM C1B C2B  sing N N 172 
HEM C1B NB   sing N N 173 
HEM C2B C3B  doub N N 174 
HEM C2B CMB  sing N N 175 
HEM C3B C4B  sing N N 176 
HEM C3B CAB  sing N N 177 
HEM C4B NB   doub N N 178 
HEM CMB HMB  sing N N 179 
HEM CMB HMBA sing N N 180 
HEM CMB HMBB sing N N 181 
HEM CAB CBB  doub N N 182 
HEM CAB HAB  sing N N 183 
HEM CBB HBB  sing N N 184 
HEM CBB HBBA sing N N 185 
HEM C1C C2C  sing Y N 186 
HEM C1C NC   sing Y N 187 
HEM C2C C3C  doub Y N 188 
HEM C2C CMC  sing N N 189 
HEM C3C C4C  sing Y N 190 
HEM C3C CAC  sing N N 191 
HEM C4C NC   sing Y N 192 
HEM CMC HMC  sing N N 193 
HEM CMC HMCA sing N N 194 
HEM CMC HMCB sing N N 195 
HEM CAC CBC  doub N N 196 
HEM CAC HAC  sing N N 197 
HEM CBC HBC  sing N N 198 
HEM CBC HBCA sing N N 199 
HEM C1D C2D  sing N N 200 
HEM C1D ND   doub N N 201 
HEM C2D C3D  doub N N 202 
HEM C2D CMD  sing N N 203 
HEM C3D C4D  sing N N 204 
HEM C3D CAD  sing N N 205 
HEM C4D ND   sing N N 206 
HEM CMD HMD  sing N N 207 
HEM CMD HMDA sing N N 208 
HEM CMD HMDB sing N N 209 
HEM CAD CBD  sing N N 210 
HEM CAD HAD  sing N N 211 
HEM CAD HADA sing N N 212 
HEM CBD CGD  sing N N 213 
HEM CBD HBD  sing N N 214 
HEM CBD HBDA sing N N 215 
HEM CGD O1D  doub N N 216 
HEM CGD O2D  sing N N 217 
HEM O2A H2A  sing N N 218 
HEM O2D H2D  sing N N 219 
HEM FE  NA   sing N N 220 
HEM FE  NB   sing N N 221 
HEM FE  NC   sing N N 222 
HEM FE  ND   sing N N 223 
HIS N   CA   sing N N 224 
HIS N   H    sing N N 225 
HIS N   H2   sing N N 226 
HIS CA  C    sing N N 227 
HIS CA  CB   sing N N 228 
HIS CA  HA   sing N N 229 
HIS C   O    doub N N 230 
HIS C   OXT  sing N N 231 
HIS CB  CG   sing N N 232 
HIS CB  HB2  sing N N 233 
HIS CB  HB3  sing N N 234 
HIS CG  ND1  sing Y N 235 
HIS CG  CD2  doub Y N 236 
HIS ND1 CE1  doub Y N 237 
HIS ND1 HD1  sing N N 238 
HIS CD2 NE2  sing Y N 239 
HIS CD2 HD2  sing N N 240 
HIS CE1 NE2  sing Y N 241 
HIS CE1 HE1  sing N N 242 
HIS NE2 HE2  sing N N 243 
HIS OXT HXT  sing N N 244 
HOH O   H1   sing N N 245 
HOH O   H2   sing N N 246 
ILE N   CA   sing N N 247 
ILE N   H    sing N N 248 
ILE N   H2   sing N N 249 
ILE CA  C    sing N N 250 
ILE CA  CB   sing N N 251 
ILE CA  HA   sing N N 252 
ILE C   O    doub N N 253 
ILE C   OXT  sing N N 254 
ILE CB  CG1  sing N N 255 
ILE CB  CG2  sing N N 256 
ILE CB  HB   sing N N 257 
ILE CG1 CD1  sing N N 258 
ILE CG1 HG12 sing N N 259 
ILE CG1 HG13 sing N N 260 
ILE CG2 HG21 sing N N 261 
ILE CG2 HG22 sing N N 262 
ILE CG2 HG23 sing N N 263 
ILE CD1 HD11 sing N N 264 
ILE CD1 HD12 sing N N 265 
ILE CD1 HD13 sing N N 266 
ILE OXT HXT  sing N N 267 
LEU N   CA   sing N N 268 
LEU N   H    sing N N 269 
LEU N   H2   sing N N 270 
LEU CA  C    sing N N 271 
LEU CA  CB   sing N N 272 
LEU CA  HA   sing N N 273 
LEU C   O    doub N N 274 
LEU C   OXT  sing N N 275 
LEU CB  CG   sing N N 276 
LEU CB  HB2  sing N N 277 
LEU CB  HB3  sing N N 278 
LEU CG  CD1  sing N N 279 
LEU CG  CD2  sing N N 280 
LEU CG  HG   sing N N 281 
LEU CD1 HD11 sing N N 282 
LEU CD1 HD12 sing N N 283 
LEU CD1 HD13 sing N N 284 
LEU CD2 HD21 sing N N 285 
LEU CD2 HD22 sing N N 286 
LEU CD2 HD23 sing N N 287 
LEU OXT HXT  sing N N 288 
LYS N   CA   sing N N 289 
LYS N   H    sing N N 290 
LYS N   H2   sing N N 291 
LYS CA  C    sing N N 292 
LYS CA  CB   sing N N 293 
LYS CA  HA   sing N N 294 
LYS C   O    doub N N 295 
LYS C   OXT  sing N N 296 
LYS CB  CG   sing N N 297 
LYS CB  HB2  sing N N 298 
LYS CB  HB3  sing N N 299 
LYS CG  CD   sing N N 300 
LYS CG  HG2  sing N N 301 
LYS CG  HG3  sing N N 302 
LYS CD  CE   sing N N 303 
LYS CD  HD2  sing N N 304 
LYS CD  HD3  sing N N 305 
LYS CE  NZ   sing N N 306 
LYS CE  HE2  sing N N 307 
LYS CE  HE3  sing N N 308 
LYS NZ  HZ1  sing N N 309 
LYS NZ  HZ2  sing N N 310 
LYS NZ  HZ3  sing N N 311 
LYS OXT HXT  sing N N 312 
MET N   CA   sing N N 313 
MET N   H    sing N N 314 
MET N   H2   sing N N 315 
MET CA  C    sing N N 316 
MET CA  CB   sing N N 317 
MET CA  HA   sing N N 318 
MET C   O    doub N N 319 
MET C   OXT  sing N N 320 
MET CB  CG   sing N N 321 
MET CB  HB2  sing N N 322 
MET CB  HB3  sing N N 323 
MET CG  SD   sing N N 324 
MET CG  HG2  sing N N 325 
MET CG  HG3  sing N N 326 
MET SD  CE   sing N N 327 
MET CE  HE1  sing N N 328 
MET CE  HE2  sing N N 329 
MET CE  HE3  sing N N 330 
MET OXT HXT  sing N N 331 
PHE N   CA   sing N N 332 
PHE N   H    sing N N 333 
PHE N   H2   sing N N 334 
PHE CA  C    sing N N 335 
PHE CA  CB   sing N N 336 
PHE CA  HA   sing N N 337 
PHE C   O    doub N N 338 
PHE C   OXT  sing N N 339 
PHE CB  CG   sing N N 340 
PHE CB  HB2  sing N N 341 
PHE CB  HB3  sing N N 342 
PHE CG  CD1  doub Y N 343 
PHE CG  CD2  sing Y N 344 
PHE CD1 CE1  sing Y N 345 
PHE CD1 HD1  sing N N 346 
PHE CD2 CE2  doub Y N 347 
PHE CD2 HD2  sing N N 348 
PHE CE1 CZ   doub Y N 349 
PHE CE1 HE1  sing N N 350 
PHE CE2 CZ   sing Y N 351 
PHE CE2 HE2  sing N N 352 
PHE CZ  HZ   sing N N 353 
PHE OXT HXT  sing N N 354 
PO4 P   O1   doub N N 355 
PO4 P   O2   sing N N 356 
PO4 P   O3   sing N N 357 
PO4 P   O4   sing N N 358 
PRO N   CA   sing N N 359 
PRO N   CD   sing N N 360 
PRO N   H    sing N N 361 
PRO CA  C    sing N N 362 
PRO CA  CB   sing N N 363 
PRO CA  HA   sing N N 364 
PRO C   O    doub N N 365 
PRO C   OXT  sing N N 366 
PRO CB  CG   sing N N 367 
PRO CB  HB2  sing N N 368 
PRO CB  HB3  sing N N 369 
PRO CG  CD   sing N N 370 
PRO CG  HG2  sing N N 371 
PRO CG  HG3  sing N N 372 
PRO CD  HD2  sing N N 373 
PRO CD  HD3  sing N N 374 
PRO OXT HXT  sing N N 375 
SER N   CA   sing N N 376 
SER N   H    sing N N 377 
SER N   H2   sing N N 378 
SER CA  C    sing N N 379 
SER CA  CB   sing N N 380 
SER CA  HA   sing N N 381 
SER C   O    doub N N 382 
SER C   OXT  sing N N 383 
SER CB  OG   sing N N 384 
SER CB  HB2  sing N N 385 
SER CB  HB3  sing N N 386 
SER OG  HG   sing N N 387 
SER OXT HXT  sing N N 388 
THR N   CA   sing N N 389 
THR N   H    sing N N 390 
THR N   H2   sing N N 391 
THR CA  C    sing N N 392 
THR CA  CB   sing N N 393 
THR CA  HA   sing N N 394 
THR C   O    doub N N 395 
THR C   OXT  sing N N 396 
THR CB  OG1  sing N N 397 
THR CB  CG2  sing N N 398 
THR CB  HB   sing N N 399 
THR OG1 HG1  sing N N 400 
THR CG2 HG21 sing N N 401 
THR CG2 HG22 sing N N 402 
THR CG2 HG23 sing N N 403 
THR OXT HXT  sing N N 404 
TRP N   CA   sing N N 405 
TRP N   H    sing N N 406 
TRP N   H2   sing N N 407 
TRP CA  C    sing N N 408 
TRP CA  CB   sing N N 409 
TRP CA  HA   sing N N 410 
TRP C   O    doub N N 411 
TRP C   OXT  sing N N 412 
TRP CB  CG   sing N N 413 
TRP CB  HB2  sing N N 414 
TRP CB  HB3  sing N N 415 
TRP CG  CD1  doub Y N 416 
TRP CG  CD2  sing Y N 417 
TRP CD1 NE1  sing Y N 418 
TRP CD1 HD1  sing N N 419 
TRP CD2 CE2  doub Y N 420 
TRP CD2 CE3  sing Y N 421 
TRP NE1 CE2  sing Y N 422 
TRP NE1 HE1  sing N N 423 
TRP CE2 CZ2  sing Y N 424 
TRP CE3 CZ3  doub Y N 425 
TRP CE3 HE3  sing N N 426 
TRP CZ2 CH2  doub Y N 427 
TRP CZ2 HZ2  sing N N 428 
TRP CZ3 CH2  sing Y N 429 
TRP CZ3 HZ3  sing N N 430 
TRP CH2 HH2  sing N N 431 
TRP OXT HXT  sing N N 432 
TYR N   CA   sing N N 433 
TYR N   H    sing N N 434 
TYR N   H2   sing N N 435 
TYR CA  C    sing N N 436 
TYR CA  CB   sing N N 437 
TYR CA  HA   sing N N 438 
TYR C   O    doub N N 439 
TYR C   OXT  sing N N 440 
TYR CB  CG   sing N N 441 
TYR CB  HB2  sing N N 442 
TYR CB  HB3  sing N N 443 
TYR CG  CD1  doub Y N 444 
TYR CG  CD2  sing Y N 445 
TYR CD1 CE1  sing Y N 446 
TYR CD1 HD1  sing N N 447 
TYR CD2 CE2  doub Y N 448 
TYR CD2 HD2  sing N N 449 
TYR CE1 CZ   doub Y N 450 
TYR CE1 HE1  sing N N 451 
TYR CE2 CZ   sing Y N 452 
TYR CE2 HE2  sing N N 453 
TYR CZ  OH   sing N N 454 
TYR OH  HH   sing N N 455 
TYR OXT HXT  sing N N 456 
VAL N   CA   sing N N 457 
VAL N   H    sing N N 458 
VAL N   H2   sing N N 459 
VAL CA  C    sing N N 460 
VAL CA  CB   sing N N 461 
VAL CA  HA   sing N N 462 
VAL C   O    doub N N 463 
VAL C   OXT  sing N N 464 
VAL CB  CG1  sing N N 465 
VAL CB  CG2  sing N N 466 
VAL CB  HB   sing N N 467 
VAL CG1 HG11 sing N N 468 
VAL CG1 HG12 sing N N 469 
VAL CG1 HG13 sing N N 470 
VAL CG2 HG21 sing N N 471 
VAL CG2 HG22 sing N N 472 
VAL CG2 HG23 sing N N 473 
VAL OXT HXT  sing N N 474 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' R01-AI161828 1 
'Department of Energy (DOE, United States)'                                                       'United States' 
DE-FC02-02ER63421 2 
# 
_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   2DN3 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BCJ 
_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]   0.016971 
_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]   0.016971 
_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]   0.003495 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
FE 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . VAL A 1 1   ? -39.925 -46.09  -3.221  1   20.53 ? 1   VAL A N   1 
ATOM   2    C  CA  . VAL A 1 1   ? -40.608 -47.354 -3.56   1   20.88 ? 1   VAL A CA  1 
ATOM   3    C  C   . VAL A 1 1   ? -39.592 -48.493 -3.593  1   21.63 ? 1   VAL A C   1 
ATOM   4    O  O   . VAL A 1 1   ? -38.706 -48.505 -4.456  1   21.36 ? 1   VAL A O   1 
ATOM   5    C  CB  . VAL A 1 1   ? -41.403 -47.336 -4.899  1   20.62 ? 1   VAL A CB  1 
ATOM   6    C  CG1 . VAL A 1 1   ? -42.292 -48.583 -4.999  1   20.45 ? 1   VAL A CG1 1 
ATOM   7    C  CG2 . VAL A 1 1   ? -42.257 -46.061 -5.035  1   21.02 ? 1   VAL A CG2 1 
ATOM   8    N  N   . LEU A 1 2   ? -39.731 -49.45  -2.676  1   21.41 ? 2   LEU A N   1 
ATOM   9    C  CA  . LEU A 1 2   ? -38.845 -50.614 -2.666  1   22.4  ? 2   LEU A CA  1 
ATOM   10   C  C   . LEU A 1 2   ? -39.234 -51.635 -3.711  1   22.71 ? 2   LEU A C   1 
ATOM   11   O  O   . LEU A 1 2   ? -40.411 -51.97  -3.851  1   22.93 ? 2   LEU A O   1 
ATOM   12   C  CB  . LEU A 1 2   ? -38.903 -51.294 -1.289  1   23.1  ? 2   LEU A CB  1 
ATOM   13   C  CG  . LEU A 1 2   ? -38.5   -50.406 -0.131  1   26.46 ? 2   LEU A CG  1 
ATOM   14   C  CD1 . LEU A 1 2   ? -38.707 -51.147 1.174   1   27.33 ? 2   LEU A CD1 1 
ATOM   15   C  CD2 . LEU A 1 2   ? -37.056 -50.045 -0.247  1   27.17 ? 2   LEU A CD2 1 
ATOM   16   N  N   . SER A 1 3   ? -38.252 -52.191 -4.394  1   23.63 ? 3   SER A N   1 
ATOM   17   C  CA  . SER A 1 3   ? -38.503 -53.295 -5.344  1   24.7  ? 3   SER A CA  1 
ATOM   18   C  C   . SER A 1 3   ? -38.652 -54.608 -4.514  1   26.77 ? 3   SER A C   1 
ATOM   19   O  O   . SER A 1 3   ? -38.235 -54.642 -3.346  1   26.85 ? 3   SER A O   1 
ATOM   20   C  CB  . SER A 1 3   ? -37.301 -53.436 -6.284  1   26.48 ? 3   SER A CB  1 
ATOM   21   O  OG  . SER A 1 3   ? -36.179 -53.982 -5.601  1   26.69 ? 3   SER A OG  1 
ATOM   22   N  N   . PRO A 1 4   ? -39.137 -55.728 -5.112  1   27.76 ? 4   PRO A N   1 
ATOM   23   C  CA  . PRO A 1 4   ? -39.152 -56.997 -4.388  1   27.39 ? 4   PRO A CA  1 
ATOM   24   C  C   . PRO A 1 4   ? -37.748 -57.405 -3.946  1   26.89 ? 4   PRO A C   1 
ATOM   25   O  O   . PRO A 1 4   ? -37.594 -57.814 -2.796  1   27.81 ? 4   PRO A O   1 
ATOM   26   C  CB  . PRO A 1 4   ? -39.729 -57.987 -5.413  1   28.77 ? 4   PRO A CB  1 
ATOM   27   C  CG  . PRO A 1 4   ? -40.495 -57.14  -6.37   1   30.09 ? 4   PRO A CG  1 
ATOM   28   C  CD  . PRO A 1 4   ? -39.715 -55.873 -6.464  1   28.12 ? 4   PRO A CD  1 
ATOM   29   N  N   . ALA A 1 5   ? -36.729 -57.241 -4.809  1   26.15 ? 5   ALA A N   1 
ATOM   30   C  CA  . ALA A 1 5   ? -35.343 -57.552 -4.432  1   26.68 ? 5   ALA A CA  1 
ATOM   31   C  C   . ALA A 1 5   ? -34.838 -56.67  -3.278  1   25.42 ? 5   ALA A C   1 
ATOM   32   O  O   . ALA A 1 5   ? -34.103 -57.174 -2.435  1   25.9  ? 5   ALA A O   1 
ATOM   33   C  CB  . ALA A 1 5   ? -34.405 -57.449 -5.63   1   27.34 ? 5   ALA A CB  1 
ATOM   34   N  N   . ASP A 1 6   ? -35.243 -55.377 -3.203  1   23.11 ? 6   ASP A N   1 
ATOM   35   C  CA  . ASP A 1 6   ? -34.832 -54.495 -2.08   1   21.86 ? 6   ASP A CA  1 
ATOM   36   C  C   . ASP A 1 6   ? -35.347 -55.088 -0.763  1   23.12 ? 6   ASP A C   1 
ATOM   37   O  O   . ASP A 1 6   ? -34.612 -55.135 0.231   1   23.09 ? 6   ASP A O   1 
ATOM   38   C  CB  . ASP A 1 6   ? -35.428 -53.079 -2.202  1   21.59 ? 6   ASP A CB  1 
ATOM   39   C  CG  . ASP A 1 6   ? -34.822 -52.22  -3.28   1   25.49 ? 6   ASP A CG  1 
ATOM   40   O  OD1 . ASP A 1 6   ? -33.631 -52.375 -3.548  1   26.4  ? 6   ASP A OD1 1 
ATOM   41   O  OD2 . ASP A 1 6   ? -35.562 -51.397 -3.869  1   27.18 ? 6   ASP A OD2 1 
ATOM   42   N  N   . LYS A 1 7   ? -36.601 -55.542 -0.76   1   22.82 ? 7   LYS A N   1 
ATOM   43   C  CA  . LYS A 1 7   ? -37.209 -56.097 0.442   1   22.91 ? 7   LYS A CA  1 
ATOM   44   C  C   . LYS A 1 7   ? -36.48  -57.354 0.899   1   23.46 ? 7   LYS A C   1 
ATOM   45   O  O   . LYS A 1 7   ? -36.17  -57.468 2.092   1   22.91 ? 7   LYS A O   1 
ATOM   46   C  CB  . LYS A 1 7   ? -38.7   -56.406 0.186   1   24.28 ? 7   LYS A CB  1 
ATOM   47   C  CG  . LYS A 1 7   ? -39.526 -55.152 -0.072  1   27.16 ? 7   LYS A CG  1 
ATOM   48   C  CD  . LYS A 1 7   ? -40.931 -55.491 -0.562  1   31.02 ? 7   LYS A CD  1 
ATOM   49   C  CE  . LYS A 1 7   ? -41.479 -54.288 -1.303  1   35.38 ? 7   LYS A CE  1 
ATOM   50   N  NZ  . LYS A 1 7   ? -42.87  -54.504 -1.794  1   36.32 ? 7   LYS A NZ  1 
ATOM   51   N  N   . THR A 1 8   ? -36.178 -58.274 -0.016  1   24.53 ? 8   THR A N   1 
ATOM   52   C  CA  . THR A 1 8   ? -35.473 -59.51  0.35    1   26.4  ? 8   THR A CA  1 
ATOM   53   C  C   . THR A 1 8   ? -34.046 -59.183 0.799   1   24.53 ? 8   THR A C   1 
ATOM   54   O  O   . THR A 1 8   ? -33.581 -59.776 1.779   1   23.62 ? 8   THR A O   1 
ATOM   55   C  CB  . THR A 1 8   ? -35.569 -60.604 -0.742  1   31.11 ? 8   THR A CB  1 
ATOM   56   O  OG1 . THR A 1 8   ? -35.015 -60.141 -1.952  1   34.4  ? 8   THR A OG1 1 
ATOM   57   C  CG2 . THR A 1 8   ? -36.979 -61.035 -1.005  1   31.82 ? 8   THR A CG2 1 
ATOM   58   N  N   . ASN A 1 9   ? -33.39  -58.169 0.158   1   22.43 ? 9   ASN A N   1 
ATOM   59   C  CA  . ASN A 1 9   ? -32.041 -57.709 0.558   1   21.48 ? 9   ASN A CA  1 
ATOM   60   C  C   . ASN A 1 9   ? -32.037 -57.166 2.013   1   21.22 ? 9   ASN A C   1 
ATOM   61   O  O   . ASN A 1 9   ? -31.15  -57.492 2.802   1   21.03 ? 9   ASN A O   1 
ATOM   62   C  CB  . ASN A 1 9   ? -31.535 -56.6   -0.393  1   21.47 ? 9   ASN A CB  1 
ATOM   63   C  CG  . ASN A 1 9   ? -31.013 -57.129 -1.717  1   23.95 ? 9   ASN A CG  1 
ATOM   64   O  OD1 . ASN A 1 9   ? -30.689 -58.312 -1.856  1   23.17 ? 9   ASN A OD1 1 
ATOM   65   N  ND2 . ASN A 1 9   ? -30.936 -56.26  -2.719  1   25.2  ? 9   ASN A ND2 1 
ATOM   66   N  N   . VAL A 1 10  ? -32.987 -56.295 2.343   1   20.7  ? 10  VAL A N   1 
ATOM   67   C  CA  . VAL A 1 10  ? -33.054 -55.684 3.685   1   21.85 ? 10  VAL A CA  1 
ATOM   68   C  C   . VAL A 1 10  ? -33.341 -56.741 4.756   1   22.96 ? 10  VAL A C   1 
ATOM   69   O  O   . VAL A 1 10  ? -32.714 -56.744 5.819   1   23.42 ? 10  VAL A O   1 
ATOM   70   C  CB  . VAL A 1 10  ? -34.118 -54.567 3.673   1   22.51 ? 10  VAL A CB  1 
ATOM   71   C  CG1 . VAL A 1 10  ? -34.433 -54.084 5.089   1   23.97 ? 10  VAL A CG1 1 
ATOM   72   C  CG2 . VAL A 1 10  ? -33.636 -53.398 2.791   1   21.89 ? 10  VAL A CG2 1 
ATOM   73   N  N   . LYS A 1 11  ? -34.267 -57.658 4.47    1   23.07 ? 11  LYS A N   1 
ATOM   74   C  CA  . LYS A 1 11  ? -34.614 -58.71  5.421   1   24.13 ? 11  LYS A CA  1 
ATOM   75   C  C   . LYS A 1 11  ? -33.407 -59.616 5.675   1   24.12 ? 11  LYS A C   1 
ATOM   76   O  O   . LYS A 1 11  ? -33.144 -59.976 6.82    1   24.17 ? 11  LYS A O   1 
ATOM   77   C  CB  . LYS A 1 11  ? -35.807 -59.53  4.894   1   25.83 ? 11  LYS A CB  1 
ATOM   78   C  CG  . LYS A 1 11  ? -37.127 -58.758 4.919   1   30.99 ? 11  LYS A CG  1 
ATOM   79   C  CD  . LYS A 1 11  ? -38.261 -59.501 4.149   1   36.2  ? 11  LYS A CD  1 
ATOM   80   C  CE  . LYS A 1 11  ? -39.579 -58.741 4.225   1   39.08 ? 11  LYS A CE  1 
ATOM   81   N  NZ  . LYS A 1 11  ? -40.123 -58.652 5.626   1   38.32 ? 11  LYS A NZ  1 
ATOM   82   N  N   . ALA A 1 12  ? -32.675 -59.984 4.615   1   23.73 ? 12  ALA A N   1 
ATOM   83   C  CA  . ALA A 1 12  ? -31.486 -60.849 4.775   1   24.1  ? 12  ALA A CA  1 
ATOM   84   C  C   . ALA A 1 12  ? -30.387 -60.138 5.577   1   24.7  ? 12  ALA A C   1 
ATOM   85   O  O   . ALA A 1 12  ? -29.872 -60.721 6.523   1   25.18 ? 12  ALA A O   1 
ATOM   86   C  CB  . ALA A 1 12  ? -30.946 -61.277 3.409   1   23.19 ? 12  ALA A CB  1 
ATOM   87   N  N   . ALA A 1 13  ? -30.06  -58.855 5.237   1   23.88 ? 13  ALA A N   1 
ATOM   88   C  CA  . ALA A 1 13  ? -29.011 -58.114 5.928   1   24.62 ? 13  ALA A CA  1 
ATOM   89   C  C   . ALA A 1 13  ? -29.37  -57.813 7.398   1   25.73 ? 13  ALA A C   1 
ATOM   90   O  O   . ALA A 1 13  ? -28.566 -58.093 8.287   1   25.42 ? 13  ALA A O   1 
ATOM   91   C  CB  . ALA A 1 13  ? -28.695 -56.825 5.192   1   24.64 ? 13  ALA A CB  1 
ATOM   92   N  N   . TRP A 1 14  ? -30.593 -57.294 7.658   1   26    ? 14  TRP A N   1 
ATOM   93   C  CA  . TRP A 1 14  ? -31.027 -57.028 9.016   1   27.21 ? 14  TRP A CA  1 
ATOM   94   C  C   . TRP A 1 14  ? -31.164 -58.292 9.849   1   29.29 ? 14  TRP A C   1 
ATOM   95   O  O   . TRP A 1 14  ? -30.903 -58.243 11.055  1   29.59 ? 14  TRP A O   1 
ATOM   96   C  CB  . TRP A 1 14  ? -32.301 -56.18  9.065   1   26.82 ? 14  TRP A CB  1 
ATOM   97   C  CG  . TRP A 1 14  ? -32.494 -55.559 10.415  1   26.74 ? 14  TRP A CG  1 
ATOM   98   C  CD1 . TRP A 1 14  ? -33.344 -55.973 11.393  1   27.32 ? 14  TRP A CD1 1 
ATOM   99   C  CD2 . TRP A 1 14  ? -31.74  -54.466 10.97   1   26.34 ? 14  TRP A CD2 1 
ATOM   100  N  NE1 . TRP A 1 14  ? -33.193 -55.181 12.515  1   27.26 ? 14  TRP A NE1 1 
ATOM   101  C  CE2 . TRP A 1 14  ? -32.205 -54.261 12.285  1   26.63 ? 14  TRP A CE2 1 
ATOM   102  C  CE3 . TRP A 1 14  ? -30.735 -53.625 10.469  1   26.75 ? 14  TRP A CE3 1 
ATOM   103  C  CZ2 . TRP A 1 14  ? -31.66  -53.286 13.128  1   27.47 ? 14  TRP A CZ2 1 
ATOM   104  C  CZ3 . TRP A 1 14  ? -30.216 -52.645 11.296  1   27.58 ? 14  TRP A CZ3 1 
ATOM   105  C  CH2 . TRP A 1 14  ? -30.66  -52.503 12.62   1   27.75 ? 14  TRP A CH2 1 
ATOM   106  N  N   . GLY A 1 15  ? -31.465 -59.426 9.211   1   30.55 ? 15  GLY A N   1 
ATOM   107  C  CA  . GLY A 1 15  ? -31.522 -60.714 9.896   1   32.92 ? 15  GLY A CA  1 
ATOM   108  C  C   . GLY A 1 15  ? -30.168 -61.159 10.431  1   35.9  ? 15  GLY A C   1 
ATOM   109  O  O   . GLY A 1 15  ? -30.091 -61.918 11.398  1   36.2  ? 15  GLY A O   1 
ATOM   110  N  N   . LYS A 1 16  ? -29.076 -60.694 9.818   1   36.94 ? 16  LYS A N   1 
ATOM   111  C  CA  . LYS A 1 16  ? -27.726 -61.018 10.271  1   38.4  ? 16  LYS A CA  1 
ATOM   112  C  C   . LYS A 1 16  ? -27.283 -60.215 11.498  1   39.88 ? 16  LYS A C   1 
ATOM   113  O  O   . LYS A 1 16  ? -26.265 -60.551 12.096  1   40.14 ? 16  LYS A O   1 
ATOM   114  C  CB  . LYS A 1 16  ? -26.731 -60.832 9.133   1   41.01 ? 16  LYS A CB  1 
ATOM   115  C  CG  . LYS A 1 16  ? -26.962 -61.812 8.01    1   47.66 ? 16  LYS A CG  1 
ATOM   116  C  CD  . LYS A 1 16  ? -26.595 -63.229 8.434   1   53.52 ? 16  LYS A CD  1 
ATOM   117  C  CE  . LYS A 1 16  ? -26.956 -64.209 7.344   1   59.46 ? 16  LYS A CE  1 
ATOM   118  N  NZ  . LYS A 1 16  ? -27.27  -65.539 7.913   1   63.43 ? 16  LYS A NZ  1 
ATOM   119  N  N   . VAL A 1 17  ? -28.028 -59.155 11.867  1   40.1  ? 17  VAL A N   1 
ATOM   120  C  CA  . VAL A 1 17  ? -27.736 -58.327 13.026  1   40.79 ? 17  VAL A CA  1 
ATOM   121  C  C   . VAL A 1 17  ? -27.969 -59.116 14.312  1   42.12 ? 17  VAL A C   1 
ATOM   122  O  O   . VAL A 1 17  ? -27.096 -59.133 15.172  1   42.81 ? 17  VAL A O   1 
ATOM   123  C  CB  . VAL A 1 17  ? -28.546 -57.007 12.979  1   40.75 ? 17  VAL A CB  1 
ATOM   124  C  CG1 . VAL A 1 17  ? -28.45  -56.258 14.282  1   41.01 ? 17  VAL A CG1 1 
ATOM   125  C  CG2 . VAL A 1 17  ? -28.084 -56.122 11.823  1   40.81 ? 17  VAL A CG2 1 
ATOM   126  N  N   . GLY A 1 18  ? -29.141 -59.744 14.422  1   42.45 ? 18  GLY A N   1 
ATOM   127  C  CA  . GLY A 1 18  ? -29.545 -60.601 15.536  1   42.97 ? 18  GLY A CA  1 
ATOM   128  C  C   . GLY A 1 18  ? -29.366 -60.058 16.935  1   43.26 ? 18  GLY A C   1 
ATOM   129  O  O   . GLY A 1 18  ? -29.918 -59.011 17.286  1   44.2  ? 18  GLY A O   1 
ATOM   130  N  N   . ALA A 1 19  ? -28.59  -60.771 17.748  1   42.63 ? 19  ALA A N   1 
ATOM   131  C  CA  . ALA A 1 19  ? -28.329 -60.365 19.128  1   42.55 ? 19  ALA A CA  1 
ATOM   132  C  C   . ALA A 1 19  ? -27.566 -59.037 19.234  1   42.06 ? 19  ALA A C   1 
ATOM   133  O  O   . ALA A 1 19  ? -27.556 -58.434 20.302  1   43.3  ? 19  ALA A O   1 
ATOM   134  C  CB  . ALA A 1 19  ? -27.554 -61.455 19.841  1   42.85 ? 19  ALA A CB  1 
ATOM   135  N  N   . HIS A 1 20  ? -26.903 -58.603 18.158  1   40.4  ? 20  HIS A N   1 
ATOM   136  C  CA  . HIS A 1 20  ? -26.14  -57.363 18.172  1   39.96 ? 20  HIS A CA  1 
ATOM   137  C  C   . HIS A 1 20  ? -26.971 -56.121 17.857  1   39.06 ? 20  HIS A C   1 
ATOM   138  O  O   . HIS A 1 20  ? -26.398 -55.043 17.705  1   38    ? 20  HIS A O   1 
ATOM   139  C  CB  . HIS A 1 20  ? -24.937 -57.466 17.228  1   41.2  ? 20  HIS A CB  1 
ATOM   140  C  CG  . HIS A 1 20  ? -24.074 -58.657 17.522  1   44.76 ? 20  HIS A CG  1 
ATOM   141  N  ND1 . HIS A 1 20  ? -23.329 -58.733 18.678  1   47.3  ? 20  HIS A ND1 1 
ATOM   142  C  CD2 . HIS A 1 20  ? -23.909 -59.802 16.821  1   46.37 ? 20  HIS A CD2 1 
ATOM   143  C  CE1 . HIS A 1 20  ? -22.714 -59.904 18.637  1   48    ? 20  HIS A CE1 1 
ATOM   144  N  NE2 . HIS A 1 20  ? -23.028 -60.58  17.537  1   47.78 ? 20  HIS A NE2 1 
ATOM   145  N  N   . ALA A 1 21  ? -28.314 -56.253 17.812  1   39.11 ? 21  ALA A N   1 
ATOM   146  C  CA  . ALA A 1 21  ? -29.22  -55.159 17.477  1   39.54 ? 21  ALA A CA  1 
ATOM   147  C  C   . ALA A 1 21  ? -28.968 -53.899 18.307  1   38.46 ? 21  ALA A C   1 
ATOM   148  O  O   . ALA A 1 21  ? -28.607 -52.886 17.713  1   39.21 ? 21  ALA A O   1 
ATOM   149  C  CB  . ALA A 1 21  ? -30.688 -55.613 17.539  1   40.09 ? 21  ALA A CB  1 
ATOM   150  N  N   . GLY A 1 22  ? -29.023 -54.01  19.631  1   36.96 ? 22  GLY A N   1 
ATOM   151  C  CA  . GLY A 1 22  ? -28.801 -52.913 20.556  1   35.56 ? 22  GLY A CA  1 
ATOM   152  C  C   . GLY A 1 22  ? -27.429 -52.301 20.389  1   33.47 ? 22  GLY A C   1 
ATOM   153  O  O   . GLY A 1 22  ? -27.292 -51.079 20.411  1   32.47 ? 22  GLY A O   1 
ATOM   154  N  N   . GLU A 1 23  ? -26.412 -53.154 20.226  1   31.51 ? 23  GLU A N   1 
ATOM   155  C  CA  . GLU A 1 23  ? -25.031 -52.721 20.044  1   30.8  ? 23  GLU A CA  1 
ATOM   156  C  C   . GLU A 1 23  ? -24.893 -51.854 18.775  1   28.97 ? 23  GLU A C   1 
ATOM   157  O  O   . GLU A 1 23  ? -24.335 -50.755 18.835  1   28.39 ? 23  GLU A O   1 
ATOM   158  C  CB  . GLU A 1 23  ? -24.11  -53.946 19.959  1   33.84 ? 23  GLU A CB  1 
ATOM   159  C  CG  . GLU A 1 23  ? -22.653 -53.568 19.809  1   42.43 ? 23  GLU A CG  1 
ATOM   160  C  CD  . GLU A 1 23  ? -21.73  -54.735 19.523  1   51.82 ? 23  GLU A CD  1 
ATOM   161  O  OE1 . GLU A 1 23  ? -22.046 -55.861 19.973  1   54.76 ? 23  GLU A OE1 1 
ATOM   162  O  OE2 . GLU A 1 23  ? -20.698 -54.525 18.844  1   52.95 ? 23  GLU A OE2 1 
ATOM   163  N  N   . TYR A 1 24  ? -25.469 -52.311 17.663  1   27.5  ? 24  TYR A N   1 
ATOM   164  C  CA  . TYR A 1 24  ? -25.411 -51.554 16.419  1   27.69 ? 24  TYR A CA  1 
ATOM   165  C  C   . TYR A 1 24  ? -26.22  -50.262 16.499  1   25.85 ? 24  TYR A C   1 
ATOM   166  O  O   . TYR A 1 24  ? -25.738 -49.215 16.061  1   25.07 ? 24  TYR A O   1 
ATOM   167  C  CB  . TYR A 1 24  ? -25.832 -52.41  15.22   1   29.93 ? 24  TYR A CB  1 
ATOM   168  C  CG  . TYR A 1 24  ? -24.965 -53.628 14.932  1   33.06 ? 24  TYR A CG  1 
ATOM   169  C  CD1 . TYR A 1 24  ? -23.767 -53.838 15.608  1   35.09 ? 24  TYR A CD1 1 
ATOM   170  C  CD2 . TYR A 1 24  ? -25.309 -54.529 13.935  1   35.19 ? 24  TYR A CD2 1 
ATOM   171  C  CE1 . TYR A 1 24  ? -22.982 -54.965 15.359  1   36.34 ? 24  TYR A CE1 1 
ATOM   172  C  CE2 . TYR A 1 24  ? -24.539 -55.659 13.683  1   36.4  ? 24  TYR A CE2 1 
ATOM   173  C  CZ  . TYR A 1 24  ? -23.36  -55.856 14.373  1   37.65 ? 24  TYR A CZ  1 
ATOM   174  O  OH  . TYR A 1 24  ? -22.591 -56.954 14.078  1   41    ? 24  TYR A OH  1 
ATOM   175  N  N   . GLY A 1 25  ? -27.409 -50.314 17.104  1   25.38 ? 25  GLY A N   1 
ATOM   176  C  CA  . GLY A 1 25  ? -28.216 -49.102 17.279  1   25.47 ? 25  GLY A CA  1 
ATOM   177  C  C   . GLY A 1 25  ? -27.5   -48.074 18.15   1   24.62 ? 25  GLY A C   1 
ATOM   178  O  O   . GLY A 1 25  ? -27.485 -46.89  17.826  1   24.12 ? 25  GLY A O   1 
ATOM   179  N  N   . ALA A 1 26  ? -26.876 -48.526 19.246  1   24.68 ? 26  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 26  ? -26.132 -47.642 20.151  1   24.76 ? 26  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 26  ? -24.93  -47.024 19.438  1   24.18 ? 26  ALA A C   1 
ATOM   182  O  O   . ALA A 1 26  ? -24.687 -45.822 19.573  1   24.77 ? 26  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 26  ? -25.678 -48.386 21.408  1   25.01 ? 26  ALA A CB  1 
ATOM   184  N  N   . GLU A 1 27  ? -24.198 -47.829 18.667  1   23.69 ? 27  GLU A N   1 
ATOM   185  C  CA  . GLU A 1 27  ? -23.046 -47.325 17.933  1   23.55 ? 27  GLU A CA  1 
ATOM   186  C  C   . GLU A 1 27  ? -23.497 -46.294 16.88   1   23.34 ? 27  GLU A C   1 
ATOM   187  O  O   . GLU A 1 27  ? -22.876 -45.243 16.763  1   23.83 ? 27  GLU A O   1 
ATOM   188  C  CB  . GLU A 1 27  ? -22.269 -48.47  17.273  1   26.29 ? 27  GLU A CB  1 
ATOM   189  C  CG  . GLU A 1 27  ? -21.103 -47.966 16.435  1   29.66 ? 27  GLU A CG  1 
ATOM   190  C  CD  . GLU A 1 27  ? -20.126 -49.022 15.969  1   34.73 ? 27  GLU A CD  1 
ATOM   191  O  OE1 . GLU A 1 27  ? -19.85  -49.969 16.742  1   36.14 ? 27  GLU A OE1 1 
ATOM   192  O  OE2 . GLU A 1 27  ? -19.638 -48.907 14.824  1   35.73 ? 27  GLU A OE2 1 
ATOM   193  N  N   . ALA A 1 28  ? -24.604 -46.559 16.152  1   22.4  ? 28  ALA A N   1 
ATOM   194  C  CA  . ALA A 1 28  ? -25.09  -45.605 15.141  1   22.27 ? 28  ALA A CA  1 
ATOM   195  C  C   . ALA A 1 28  ? -25.451 -44.259 15.793  1   20.91 ? 28  ALA A C   1 
ATOM   196  O  O   . ALA A 1 28  ? -25.144 -43.206 15.242  1   20.11 ? 28  ALA A O   1 
ATOM   197  C  CB  . ALA A 1 28  ? -26.321 -46.172 14.444  1   22.59 ? 28  ALA A CB  1 
ATOM   198  N  N   . LEU A 1 29  ? -26.078 -44.298 16.978  1   20.79 ? 29  LEU A N   1 
ATOM   199  C  CA  . LEU A 1 29  ? -26.437 -43.06  17.692  1   21.06 ? 29  LEU A CA  1 
ATOM   200  C  C   . LEU A 1 29  ? -25.166 -42.322 18.108  1   21.89 ? 29  LEU A C   1 
ATOM   201  O  O   . LEU A 1 29  ? -25.081 -41.107 17.938  1   22.1  ? 29  LEU A O   1 
ATOM   202  C  CB  . LEU A 1 29  ? -27.219 -43.43  18.97   1   20.58 ? 29  LEU A CB  1 
ATOM   203  C  CG  . LEU A 1 29  ? -28.66  -43.856 18.734  1   22.29 ? 29  LEU A CG  1 
ATOM   204  C  CD1 . LEU A 1 29  ? -29.276 -44.259 20.053  1   23.77 ? 29  LEU A CD1 1 
ATOM   205  C  CD2 . LEU A 1 29  ? -29.476 -42.686 18.137  1   21.59 ? 29  LEU A CD2 1 
ATOM   206  N  N   . GLU A 1 30  ? -24.166 -43.058 18.64   1   22.01 ? 30  GLU A N   1 
ATOM   207  C  CA  . GLU A 1 30  ? -22.906 -42.464 19.076  1   23.46 ? 30  GLU A CA  1 
ATOM   208  C  C   . GLU A 1 30  ? -22.209 -41.772 17.891  1   22.67 ? 30  GLU A C   1 
ATOM   209  O  O   . GLU A 1 30  ? -21.699 -40.643 18.022  1   23.15 ? 30  GLU A O   1 
ATOM   210  C  CB  . GLU A 1 30  ? -21.992 -43.549 19.672  1   28.45 ? 30  GLU A CB  1 
ATOM   211  C  CG  . GLU A 1 30  ? -20.578 -43.076 19.963  1   38.73 ? 30  GLU A CG  1 
ATOM   212  C  CD  . GLU A 1 30  ? -19.618 -44.133 20.474  1   49.48 ? 30  GLU A CD  1 
ATOM   213  O  OE1 . GLU A 1 30  ? -18.55  -43.74  20.994  1   53.35 ? 30  GLU A OE1 1 
ATOM   214  O  OE2 . GLU A 1 30  ? -19.918 -45.344 20.345  1   51.77 ? 30  GLU A OE2 1 
ATOM   215  N  N   . ARG A 1 31  ? -22.181 -42.461 16.739  1   21.09 ? 31  ARG A N   1 
ATOM   216  C  CA  . ARG A 1 31  ? -21.581 -41.914 15.523  1   20.95 ? 31  ARG A CA  1 
ATOM   217  C  C   . ARG A 1 31  ? -22.327 -40.644 15.104  1   21.91 ? 31  ARG A C   1 
ATOM   218  O  O   . ARG A 1 31  ? -21.693 -39.65  14.757  1   22.36 ? 31  ARG A O   1 
ATOM   219  C  CB  . ARG A 1 31  ? -21.602 -42.941 14.384  1   20.75 ? 31  ARG A CB  1 
ATOM   220  C  CG  . ARG A 1 31  ? -20.595 -44.093 14.593  1   22.13 ? 31  ARG A CG  1 
ATOM   221  C  CD  . ARG A 1 31  ? -20.707 -45.145 13.467  1   23.61 ? 31  ARG A CD  1 
ATOM   222  N  NE  . ARG A 1 31  ? -19.752 -46.239 13.66   1   25.55 ? 31  ARG A NE  1 
ATOM   223  C  CZ  . ARG A 1 31  ? -18.452 -46.165 13.393  1   26.3  ? 31  ARG A CZ  1 
ATOM   224  N  NH1 . ARG A 1 31  ? -17.944 -45.075 12.826  1   22.69 ? 31  ARG A NH1 1 
ATOM   225  N  NH2 . ARG A 1 31  ? -17.653 -47.187 13.673  1   25.97 ? 31  ARG A NH2 1 
ATOM   226  N  N   . MET A 1 32  ? -23.672 -40.666 15.188  1   20.49 ? 32  MET A N   1 
ATOM   227  C  CA  . MET A 1 32  ? -24.457 -39.493 14.859  1   20.04 ? 32  MET A CA  1 
ATOM   228  C  C   . MET A 1 32  ? -24.17  -38.301 15.768  1   20.73 ? 32  MET A C   1 
ATOM   229  O  O   . MET A 1 32  ? -23.954 -37.207 15.273  1   22.05 ? 32  MET A O   1 
ATOM   230  C  CB  . MET A 1 32  ? -25.966 -39.819 14.88   1   19.1  ? 32  MET A CB  1 
ATOM   231  C  CG  . MET A 1 32  ? -26.78  -38.655 14.468  1   21.22 ? 32  MET A CG  1 
ATOM   232  S  SD  . MET A 1 32  ? -28.554 -38.975 14.596  1   24.18 ? 32  MET A SD  1 
ATOM   233  C  CE  . MET A 1 32  ? -28.756 -39.057 16.375  1   21.01 ? 32  MET A CE  1 
ATOM   234  N  N   . PHE A 1 33  ? -24.25  -38.488 17.084  1   20.47 ? 33  PHE A N   1 
ATOM   235  C  CA  . PHE A 1 33  ? -24.016 -37.406 18.048  1   20.87 ? 33  PHE A CA  1 
ATOM   236  C  C   . PHE A 1 33  ? -22.594 -36.828 17.909  1   22.28 ? 33  PHE A C   1 
ATOM   237  O  O   . PHE A 1 33  ? -22.384 -35.644 18.134  1   22    ? 33  PHE A O   1 
ATOM   238  C  CB  . PHE A 1 33  ? -24.195 -37.965 19.478  1   20.09 ? 33  PHE A CB  1 
ATOM   239  C  CG  . PHE A 1 33  ? -25.621 -38.35  19.797  1   20.05 ? 33  PHE A CG  1 
ATOM   240  C  CD1 . PHE A 1 33  ? -26.686 -37.607 19.304  1   20.51 ? 33  PHE A CD1 1 
ATOM   241  C  CD2 . PHE A 1 33  ? -25.894 -39.415 20.648  1   20.9  ? 33  PHE A CD2 1 
ATOM   242  C  CE1 . PHE A 1 33  ? -28.007 -37.938 19.644  1   21.4  ? 33  PHE A CE1 1 
ATOM   243  C  CE2 . PHE A 1 33  ? -27.213 -39.754 20.973  1   21.49 ? 33  PHE A CE2 1 
ATOM   244  C  CZ  . PHE A 1 33  ? -28.255 -39     20.491  1   21.37 ? 33  PHE A CZ  1 
ATOM   245  N  N   . LEU A 1 34  ? -21.627 -37.675 17.562  1   23.11 ? 34  LEU A N   1 
ATOM   246  C  CA  . LEU A 1 34  ? -20.24  -37.222 17.475  1   25.19 ? 34  LEU A CA  1 
ATOM   247  C  C   . LEU A 1 34  ? -19.991 -36.536 16.116  1   24.85 ? 34  LEU A C   1 
ATOM   248  O  O   . LEU A 1 34  ? -19.395 -35.483 16.083  1   25.94 ? 34  LEU A O   1 
ATOM   249  C  CB  . LEU A 1 34  ? -19.309 -38.427 17.695  1   27.41 ? 34  LEU A CB  1 
ATOM   250  C  CG  . LEU A 1 34  ? -17.908 -38.146 18.109  1   32.48 ? 34  LEU A CG  1 
ATOM   251  C  CD1 . LEU A 1 34  ? -17.865 -37.359 19.415  1   33.81 ? 34  LEU A CD1 1 
ATOM   252  C  CD2 . LEU A 1 34  ? -17.127 -39.45  18.256  1   34.5  ? 34  LEU A CD2 1 
ATOM   253  N  N   . SER A 1 35  ? -20.447 -37.112 15.027  1   24.66 ? 35  SER A N   1 
ATOM   254  C  CA  . SER A 1 35  ? -20.243 -36.559 13.672  1   24.37 ? 35  SER A CA  1 
ATOM   255  C  C   . SER A 1 35  ? -21.082 -35.341 13.385  1   24.26 ? 35  SER A C   1 
ATOM   256  O  O   . SER A 1 35  ? -20.634 -34.449 12.679  1   24.76 ? 35  SER A O   1 
ATOM   257  C  CB  . SER A 1 35  ? -20.558 -37.603 12.612  1   25.19 ? 35  SER A CB  1 
ATOM   258  O  OG  . SER A 1 35  ? -19.62  -38.663 12.672  1   26.71 ? 35  SER A OG  1 
ATOM   259  N  N   . PHE A 1 36  ? -22.322 -35.318 13.895  1   23.3  ? 36  PHE A N   1 
ATOM   260  C  CA  . PHE A 1 36  ? -23.284 -34.257 13.607  1   21.92 ? 36  PHE A CA  1 
ATOM   261  C  C   . PHE A 1 36  ? -23.819 -33.757 14.958  1   22.31 ? 36  PHE A C   1 
ATOM   262  O  O   . PHE A 1 36  ? -24.936 -34.105 15.347  1   20.94 ? 36  PHE A O   1 
ATOM   263  C  CB  . PHE A 1 36  ? -24.425 -34.875 12.763  1   20.92 ? 36  PHE A CB  1 
ATOM   264  C  CG  . PHE A 1 36  ? -23.914 -35.599 11.523  1   20.83 ? 36  PHE A CG  1 
ATOM   265  C  CD1 . PHE A 1 36  ? -23.313 -34.893 10.481  1   21.45 ? 36  PHE A CD1 1 
ATOM   266  C  CD2 . PHE A 1 36  ? -23.991 -36.979 11.426  1   20.86 ? 36  PHE A CD2 1 
ATOM   267  C  CE1 . PHE A 1 36  ? -22.811 -35.561 9.363   1   22.25 ? 36  PHE A CE1 1 
ATOM   268  C  CE2 . PHE A 1 36  ? -23.49  -37.645 10.3    1   21.37 ? 36  PHE A CE2 1 
ATOM   269  C  CZ  . PHE A 1 36  ? -22.926 -36.934 9.27    1   21.33 ? 36  PHE A CZ  1 
ATOM   270  N  N   . PRO A 1 37  ? -23.018 -32.948 15.681  1   23.38 ? 37  PRO A N   1 
ATOM   271  C  CA  . PRO A 1 37  ? -23.41  -32.542 17.041  1   23.72 ? 37  PRO A CA  1 
ATOM   272  C  C   . PRO A 1 37  ? -24.762 -31.843 17.195  1   23.6  ? 37  PRO A C   1 
ATOM   273  O  O   . PRO A 1 37  ? -25.31  -31.871 18.293  1   22.92 ? 37  PRO A O   1 
ATOM   274  C  CB  . PRO A 1 37  ? -22.262 -31.617 17.49   1   24.68 ? 37  PRO A CB  1 
ATOM   275  C  CG  . PRO A 1 37  ? -21.132 -31.908 16.597  1   25.36 ? 37  PRO A CG  1 
ATOM   276  C  CD  . PRO A 1 37  ? -21.673 -32.441 15.319  1   23.67 ? 37  PRO A CD  1 
ATOM   277  N  N   . THR A 1 38  ? -25.306 -31.226 16.121  1   23.36 ? 38  THR A N   1 
ATOM   278  C  CA  . THR A 1 38  ? -26.623 -30.58  16.225  1   24.42 ? 38  THR A CA  1 
ATOM   279  C  C   . THR A 1 38  ? -27.722 -31.589 16.594  1   22.34 ? 38  THR A C   1 
ATOM   280  O  O   . THR A 1 38  ? -28.709 -31.198 17.209  1   22.69 ? 38  THR A O   1 
ATOM   281  C  CB  . THR A 1 38  ? -26.986 -29.855 14.913  1   27.9  ? 38  THR A CB  1 
ATOM   282  O  OG1 . THR A 1 38  ? -26.788 -30.771 13.825  1   31.46 ? 38  THR A OG1 1 
ATOM   283  C  CG2 . THR A 1 38  ? -26.11  -28.649 14.68   1   28.35 ? 38  THR A CG2 1 
ATOM   284  N  N   . THR A 1 39  ? -27.556 -32.881 16.224  1   20    ? 39  THR A N   1 
ATOM   285  C  CA  . THR A 1 39  ? -28.548 -33.923 16.542  1   19.03 ? 39  THR A CA  1 
ATOM   286  C  C   . THR A 1 39  ? -28.68  -34.116 18.055  1   19.91 ? 39  THR A C   1 
ATOM   287  O  O   . THR A 1 39  ? -29.745 -34.499 18.504  1   20.78 ? 39  THR A O   1 
ATOM   288  C  CB  . THR A 1 39  ? -28.17  -35.248 15.898  1   19.22 ? 39  THR A CB  1 
ATOM   289  O  OG1 . THR A 1 39  ? -26.901 -35.667 16.43   1   19.99 ? 39  THR A OG1 1 
ATOM   290  C  CG2 . THR A 1 39  ? -28.122 -35.16  14.336  1   18.63 ? 39  THR A CG2 1 
ATOM   291  N  N   . LYS A 1 40  ? -27.644 -33.786 18.835  1   19.22 ? 40  LYS A N   1 
ATOM   292  C  CA  . LYS A 1 40  ? -27.716 -33.868 20.305  1   19.49 ? 40  LYS A CA  1 
ATOM   293  C  C   . LYS A 1 40  ? -28.8   -32.967 20.882  1   20.86 ? 40  LYS A C   1 
ATOM   294  O  O   . LYS A 1 40  ? -29.259 -33.22  21.997  1   21.82 ? 40  LYS A O   1 
ATOM   295  C  CB  . LYS A 1 40  ? -26.361 -33.502 20.945  1   21.03 ? 40  LYS A CB  1 
ATOM   296  C  CG  . LYS A 1 40  ? -25.247 -34.499 20.632  1   23.4  ? 40  LYS A CG  1 
ATOM   297  C  CD  . LYS A 1 40  ? -23.988 -34.226 21.438  1   30.95 ? 40  LYS A CD  1 
ATOM   298  C  CE  . LYS A 1 40  ? -23.396 -32.863 21.147  1   36.88 ? 40  LYS A CE  1 
ATOM   299  N  NZ  . LYS A 1 40  ? -22.011 -32.715 21.697  1   39.05 ? 40  LYS A NZ  1 
ATOM   300  N  N   . THR A 1 41  ? -29.205 -31.912 20.154  1   21.02 ? 41  THR A N   1 
ATOM   301  C  CA  . THR A 1 41  ? -30.201 -30.98  20.667  1   22.11 ? 41  THR A CA  1 
ATOM   302  C  C   . THR A 1 41  ? -31.597 -31.624 20.765  1   21.58 ? 41  THR A C   1 
ATOM   303  O  O   . THR A 1 41  ? -32.459 -31.054 21.421  1   21.82 ? 41  THR A O   1 
ATOM   304  C  CB  . THR A 1 41  ? -30.191 -29.664 19.882  1   24.28 ? 41  THR A CB  1 
ATOM   305  O  OG1 . THR A 1 41  ? -30.7   -29.917 18.576  1   25.65 ? 41  THR A OG1 1 
ATOM   306  C  CG2 . THR A 1 41  ? -28.792 -29.038 19.813  1   25.33 ? 41  THR A CG2 1 
ATOM   307  N  N   . TYR A 1 42  ? -31.818 -32.804 20.149  1   19.24 ? 42  TYR A N   1 
ATOM   308  C  CA  . TYR A 1 42  ? -33.096 -33.508 20.351  1   19.59 ? 42  TYR A CA  1 
ATOM   309  C  C   . TYR A 1 42  ? -33.094 -34.302 21.679  1   19.73 ? 42  TYR A C   1 
ATOM   310  O  O   . TYR A 1 42  ? -34.166 -34.725 22.145  1   19.18 ? 42  TYR A O   1 
ATOM   311  C  CB  . TYR A 1 42  ? -33.386 -34.472 19.181  1   18.61 ? 42  TYR A CB  1 
ATOM   312  C  CG  . TYR A 1 42  ? -33.822 -33.72  17.949  1   19.18 ? 42  TYR A CG  1 
ATOM   313  C  CD1 . TYR A 1 42  ? -35.148 -33.322 17.788  1   19.88 ? 42  TYR A CD1 1 
ATOM   314  C  CD2 . TYR A 1 42  ? -32.891 -33.254 17.036  1   19.82 ? 42  TYR A CD2 1 
ATOM   315  C  CE1 . TYR A 1 42  ? -35.552 -32.608 16.662  1   20.26 ? 42  TYR A CE1 1 
ATOM   316  C  CE2 . TYR A 1 42  ? -33.275 -32.5   15.929  1   21.04 ? 42  TYR A CE2 1 
ATOM   317  C  CZ  . TYR A 1 42  ? -34.606 -32.178 15.75   1   21.74 ? 42  TYR A CZ  1 
ATOM   318  O  OH  . TYR A 1 42  ? -34.978 -31.503 14.62   1   24.44 ? 42  TYR A OH  1 
ATOM   319  N  N   . PHE A 1 43  ? -31.908 -34.482 22.328  1   18.85 ? 43  PHE A N   1 
ATOM   320  C  CA  . PHE A 1 43  ? -31.807 -35.309 23.545  1   20.05 ? 43  PHE A CA  1 
ATOM   321  C  C   . PHE A 1 43  ? -31.193 -34.522 24.71   1   21.81 ? 43  PHE A C   1 
ATOM   322  O  O   . PHE A 1 43  ? -30.203 -34.952 25.325  1   22.78 ? 43  PHE A O   1 
ATOM   323  C  CB  . PHE A 1 43  ? -30.933 -36.545 23.231  1   19.47 ? 43  PHE A CB  1 
ATOM   324  C  CG  . PHE A 1 43  ? -31.463 -37.455 22.143  1   19.47 ? 43  PHE A CG  1 
ATOM   325  C  CD1 . PHE A 1 43  ? -31.284 -37.137 20.795  1   19.88 ? 43  PHE A CD1 1 
ATOM   326  C  CD2 . PHE A 1 43  ? -32.125 -38.64  22.463  1   20.39 ? 43  PHE A CD2 1 
ATOM   327  C  CE1 . PHE A 1 43  ? -31.747 -37.989 19.787  1   19.39 ? 43  PHE A CE1 1 
ATOM   328  C  CE2 . PHE A 1 43  ? -32.585 -39.5   21.451  1   19.89 ? 43  PHE A CE2 1 
ATOM   329  C  CZ  . PHE A 1 43  ? -32.407 -39.16  20.124  1   19.62 ? 43  PHE A CZ  1 
ATOM   330  N  N   . PRO A 1 44  ? -31.766 -33.349 25.047  1   21.97 ? 44  PRO A N   1 
ATOM   331  C  CA  . PRO A 1 44  ? -31.164 -32.535 26.113  1   22.91 ? 44  PRO A CA  1 
ATOM   332  C  C   . PRO A 1 44  ? -31.221 -33.203 27.482  1   24.25 ? 44  PRO A C   1 
ATOM   333  O  O   . PRO A 1 44  ? -30.386 -32.904 28.34   1   24.31 ? 44  PRO A O   1 
ATOM   334  C  CB  . PRO A 1 44  ? -31.995 -31.252 26.063  1   23    ? 44  PRO A CB  1 
ATOM   335  C  CG  . PRO A 1 44  ? -33.364 -31.716 25.646  1   22.6  ? 44  PRO A CG  1 
ATOM   336  C  CD  . PRO A 1 44  ? -33.007 -32.728 24.541  1   21.01 ? 44  PRO A CD  1 
ATOM   337  N  N   . HIS A 1 45  ? -32.175 -34.127 27.665  1   24.8  ? 45  HIS A N   1 
ATOM   338  C  CA  . HIS A 1 45  ? -32.371 -34.863 28.917  1   25.89 ? 45  HIS A CA  1 
ATOM   339  C  C   . HIS A 1 45  ? -31.47  -36.113 29.034  1   26.79 ? 45  HIS A C   1 
ATOM   340  O  O   . HIS A 1 45  ? -31.522 -36.817 30.051  1   27.89 ? 45  HIS A O   1 
ATOM   341  C  CB  . HIS A 1 45  ? -33.863 -35.267 29.026  1   25.97 ? 45  HIS A CB  1 
ATOM   342  C  CG  . HIS A 1 45  ? -34.368 -36.086 27.877  1   26.93 ? 45  HIS A CG  1 
ATOM   343  N  ND1 . HIS A 1 45  ? -34.399 -35.583 26.571  1   28.1  ? 45  HIS A ND1 1 
ATOM   344  C  CD2 . HIS A 1 45  ? -34.87  -37.343 27.868  1   27.31 ? 45  HIS A CD2 1 
ATOM   345  C  CE1 . HIS A 1 45  ? -34.918 -36.547 25.828  1   28.47 ? 45  HIS A CE1 1 
ATOM   346  N  NE2 . HIS A 1 45  ? -35.207 -37.627 26.565  1   28.33 ? 45  HIS A NE2 1 
ATOM   347  N  N   . PHE A 1 46  ? -30.665 -36.41  28.01   1   26.03 ? 46  PHE A N   1 
ATOM   348  C  CA  . PHE A 1 46  ? -29.811 -37.584 28.043  1   25.67 ? 46  PHE A CA  1 
ATOM   349  C  C   . PHE A 1 46  ? -28.436 -37.294 28.586  1   26.97 ? 46  PHE A C   1 
ATOM   350  O  O   . PHE A 1 46  ? -27.892 -36.198 28.407  1   27.5  ? 46  PHE A O   1 
ATOM   351  C  CB  . PHE A 1 46  ? -29.622 -38.142 26.611  1   24.66 ? 46  PHE A CB  1 
ATOM   352  C  CG  . PHE A 1 46  ? -30.608 -39.2   26.175  1   24.76 ? 46  PHE A CG  1 
ATOM   353  C  CD1 . PHE A 1 46  ? -31.933 -39.138 26.571  1   25.03 ? 46  PHE A CD1 1 
ATOM   354  C  CD2 . PHE A 1 46  ? -30.249 -40.158 25.233  1   25.65 ? 46  PHE A CD2 1 
ATOM   355  C  CE1 . PHE A 1 46  ? -32.838 -40.116 26.175  1   26.44 ? 46  PHE A CE1 1 
ATOM   356  C  CE2 . PHE A 1 46  ? -31.166 -41.116 24.806  1   26.45 ? 46  PHE A CE2 1 
ATOM   357  C  CZ  . PHE A 1 46  ? -32.453 -41.092 25.277  1   25.87 ? 46  PHE A CZ  1 
ATOM   358  N  N   . ASP A 1 47  ? -27.818 -38.33  29.145  1   26.76 ? 47  ASP A N   1 
ATOM   359  C  CA  . ASP A 1 47  ? -26.402 -38.337 29.424  1   27.26 ? 47  ASP A CA  1 
ATOM   360  C  C   . ASP A 1 47  ? -25.847 -38.749 28.054  1   26.77 ? 47  ASP A C   1 
ATOM   361  O  O   . ASP A 1 47  ? -26.126 -39.858 27.575  1   25.35 ? 47  ASP A O   1 
ATOM   362  C  CB  . ASP A 1 47  ? -26.066 -39.414 30.471  1   30.23 ? 47  ASP A CB  1 
ATOM   363  C  CG  . ASP A 1 47  ? -24.602 -39.757 30.602  1   37.55 ? 47  ASP A CG  1 
ATOM   364  O  OD1 . ASP A 1 47  ? -23.778 -39.108 29.939  1   38.3  ? 47  ASP A OD1 1 
ATOM   365  O  OD2 . ASP A 1 47  ? -24.277 -40.674 31.382  1   42.86 ? 47  ASP A OD2 1 
ATOM   366  N  N   . LEU A 1 48  ? -25.141 -37.836 27.387  1   27.79 ? 48  LEU A N   1 
ATOM   367  C  CA  . LEU A 1 48  ? -24.624 -38.08  26.055  1   30.12 ? 48  LEU A CA  1 
ATOM   368  C  C   . LEU A 1 48  ? -23.124 -38.414 26.011  1   32.53 ? 48  LEU A C   1 
ATOM   369  O  O   . LEU A 1 48  ? -22.567 -38.481 24.925  1   33.04 ? 48  LEU A O   1 
ATOM   370  C  CB  . LEU A 1 48  ? -24.954 -36.918 25.113  1   29.39 ? 48  LEU A CB  1 
ATOM   371  C  CG  . LEU A 1 48  ? -26.453 -36.722 24.884  1   29.97 ? 48  LEU A CG  1 
ATOM   372  C  CD1 . LEU A 1 48  ? -26.758 -35.35  24.275  1   29.98 ? 48  LEU A CD1 1 
ATOM   373  C  CD2 . LEU A 1 48  ? -27.014 -37.824 24.023  1   29.9  ? 48  LEU A CD2 1 
ATOM   374  N  N   . SER A 1 49  ? -22.511 -38.699 27.16   1   33.68 ? 49  SER A N   1 
ATOM   375  C  CA  . SER A 1 49  ? -21.098 -39.098 27.226  1   35.78 ? 49  SER A CA  1 
ATOM   376  C  C   . SER A 1 49  ? -20.911 -40.47  26.553  1   37.14 ? 49  SER A C   1 
ATOM   377  O  O   . SER A 1 49  ? -21.874 -41.232 26.432  1   36.36 ? 49  SER A O   1 
ATOM   378  C  CB  . SER A 1 49  ? -20.635 -39.157 28.679  1   38.02 ? 49  SER A CB  1 
ATOM   379  O  OG  . SER A 1 49  ? -21.418 -40.061 29.443  1   40.74 ? 49  SER A OG  1 
ATOM   380  N  N   . HIS A 1 50  ? -19.68  -40.795 26.102  1   38.59 ? 50  HIS A N   1 
ATOM   381  C  CA  . HIS A 1 50  ? -19.44  -42.082 25.435  1   40.06 ? 50  HIS A CA  1 
ATOM   382  C  C   . HIS A 1 50  ? -19.744 -43.239 26.397  1   39.83 ? 50  HIS A C   1 
ATOM   383  O  O   . HIS A 1 50  ? -19.449 -43.139 27.578  1   39.83 ? 50  HIS A O   1 
ATOM   384  C  CB  . HIS A 1 50  ? -17.997 -42.176 24.903  1   42.62 ? 50  HIS A CB  1 
ATOM   385  C  CG  . HIS A 1 50  ? -17.549 -43.578 24.614  1   46.41 ? 50  HIS A CG  1 
ATOM   386  N  ND1 . HIS A 1 50  ? -17.912 -44.227 23.442  1   48.83 ? 50  HIS A ND1 1 
ATOM   387  C  CD2 . HIS A 1 50  ? -16.834 -44.431 25.388  1   48.35 ? 50  HIS A CD2 1 
ATOM   388  C  CE1 . HIS A 1 50  ? -17.384 -45.439 23.525  1   50.03 ? 50  HIS A CE1 1 
ATOM   389  N  NE2 . HIS A 1 50  ? -16.729 -45.61  24.686  1   49.93 ? 50  HIS A NE2 1 
ATOM   390  N  N   . GLY A 1 51  ? -20.35  -44.303 25.879  1   39.64 ? 51  GLY A N   1 
ATOM   391  C  CA  . GLY A 1 51  ? -20.674 -45.453 26.714  1   39.12 ? 51  GLY A CA  1 
ATOM   392  C  C   . GLY A 1 51  ? -21.801 -45.198 27.695  1   37.79 ? 51  GLY A C   1 
ATOM   393  O  O   . GLY A 1 51  ? -22.054 -46.014 28.577  1   38.55 ? 51  GLY A O   1 
ATOM   394  N  N   . SER A 1 52  ? -22.532 -44.081 27.536  1   35.49 ? 52  SER A N   1 
ATOM   395  C  CA  . SER A 1 52  ? -23.689 -43.74  28.351  1   34.13 ? 52  SER A CA  1 
ATOM   396  C  C   . SER A 1 52  ? -24.707 -44.894 28.285  1   33.27 ? 52  SER A C   1 
ATOM   397  O  O   . SER A 1 52  ? -25.018 -45.349 27.187  1   32.76 ? 52  SER A O   1 
ATOM   398  C  CB  . SER A 1 52  ? -24.335 -42.476 27.776  1   34.14 ? 52  SER A CB  1 
ATOM   399  O  OG  . SER A 1 52  ? -25.736 -42.409 27.961  1   34.59 ? 52  SER A OG  1 
ATOM   400  N  N   . ALA A 1 53  ? -25.201 -45.348 29.443  1   32.96 ? 53  ALA A N   1 
ATOM   401  C  CA  . ALA A 1 53  ? -26.22  -46.398 29.536  1   32.26 ? 53  ALA A CA  1 
ATOM   402  C  C   . ALA A 1 53  ? -27.545 -45.939 28.874  1   30.24 ? 53  ALA A C   1 
ATOM   403  O  O   . ALA A 1 53  ? -28.26  -46.744 28.279  1   29.8  ? 53  ALA A O   1 
ATOM   404  C  CB  . ALA A 1 53  ? -26.452 -46.759 31.01   1   32.99 ? 53  ALA A CB  1 
ATOM   405  N  N   . GLN A 1 54  ? -27.837 -44.638 28.931  1   28.04 ? 54  GLN A N   1 
ATOM   406  C  CA  . GLN A 1 54  ? -29.026 -44.083 28.332  1   27.16 ? 54  GLN A CA  1 
ATOM   407  C  C   . GLN A 1 54  ? -28.957 -44.203 26.805  1   25.52 ? 54  GLN A C   1 
ATOM   408  O  O   . GLN A 1 54  ? -29.946 -44.565 26.161  1   24.55 ? 54  GLN A O   1 
ATOM   409  C  CB  . GLN A 1 54  ? -29.112 -42.628 28.721  1   29.54 ? 54  GLN A CB  1 
ATOM   410  C  CG  . GLN A 1 54  ? -30.542 -42.196 28.868  1   33.5  ? 54  GLN A CG  1 
ATOM   411  C  CD  . GLN A 1 54  ? -30.686 -40.948 29.676  1   34.59 ? 54  GLN A CD  1 
ATOM   412  O  OE1 . GLN A 1 54  ? -29.711 -40.302 30.093  1   32.41 ? 54  GLN A OE1 1 
ATOM   413  N  NE2 . GLN A 1 54  ? -31.924 -40.554 29.841  1   36.5  ? 54  GLN A NE2 1 
ATOM   414  N  N   . VAL A 1 55  ? -27.785 -43.88  26.234  1   24.6  ? 55  VAL A N   1 
ATOM   415  C  CA  . VAL A 1 55  ? -27.578 -44.008 24.78   1   24.65 ? 55  VAL A CA  1 
ATOM   416  C  C   . VAL A 1 55  ? -27.645 -45.49  24.394  1   25.61 ? 55  VAL A C   1 
ATOM   417  O  O   . VAL A 1 55  ? -28.281 -45.834 23.394  1   26.01 ? 55  VAL A O   1 
ATOM   418  C  CB  . VAL A 1 55  ? -26.26  -43.331 24.331  1   24.02 ? 55  VAL A CB  1 
ATOM   419  C  CG1 . VAL A 1 55  ? -25.912 -43.707 22.888  1   24.24 ? 55  VAL A CG1 1 
ATOM   420  C  CG2 . VAL A 1 55  ? -26.383 -41.807 24.465  1   23.76 ? 55  VAL A CG2 1 
ATOM   421  N  N   . LYS A 1 56  ? -27.035 -46.37  25.214  1   25.48 ? 56  LYS A N   1 
ATOM   422  C  CA  . LYS A 1 56  ? -27.099 -47.81  24.934  1   26.74 ? 56  LYS A CA  1 
ATOM   423  C  C   . LYS A 1 56  ? -28.545 -48.339 24.914  1   26.14 ? 56  LYS A C   1 
ATOM   424  O  O   . LYS A 1 56  ? -28.906 -49.048 23.983  1   26.7  ? 56  LYS A O   1 
ATOM   425  C  CB  . LYS A 1 56  ? -26.259 -48.604 25.933  1   29.13 ? 56  LYS A CB  1 
ATOM   426  C  CG  . LYS A 1 56  ? -24.776 -48.435 25.722  1   35.91 ? 56  LYS A CG  1 
ATOM   427  C  CD  . LYS A 1 56  ? -24.018 -49.421 26.617  1   41.7  ? 56  LYS A CD  1 
ATOM   428  C  CE  . LYS A 1 56  ? -22.527 -49.225 26.583  1   46.97 ? 56  LYS A CE  1 
ATOM   429  N  NZ  . LYS A 1 56  ? -21.875 -49.923 27.738  1   51.15 ? 56  LYS A NZ  1 
ATOM   430  N  N   . GLY A 1 57  ? -29.339 -47.989 25.92   1   25.38 ? 57  GLY A N   1 
ATOM   431  C  CA  . GLY A 1 57  ? -30.729 -48.414 26.002  1   25.32 ? 57  GLY A CA  1 
ATOM   432  C  C   . GLY A 1 57  ? -31.558 -47.835 24.864  1   25.02 ? 57  GLY A C   1 
ATOM   433  O  O   . GLY A 1 57  ? -32.421 -48.52  24.313  1   24.05 ? 57  GLY A O   1 
ATOM   434  N  N   . HIS A 1 58  ? -31.296 -46.571 24.5    1   24.27 ? 58  HIS A N   1 
ATOM   435  C  CA  . HIS A 1 58  ? -32.015 -45.949 23.389  1   23.34 ? 58  HIS A CA  1 
ATOM   436  C  C   . HIS A 1 58  ? -31.707 -46.665 22.065  1   23.1  ? 58  HIS A C   1 
ATOM   437  O  O   . HIS A 1 58  ? -32.614 -46.907 21.268  1   22.21 ? 58  HIS A O   1 
ATOM   438  C  CB  . HIS A 1 58  ? -31.739 -44.431 23.28   1   23.16 ? 58  HIS A CB  1 
ATOM   439  C  CG  . HIS A 1 58  ? -32.693 -43.771 22.333  1   24.9  ? 58  HIS A CG  1 
ATOM   440  N  ND1 . HIS A 1 58  ? -34.058 -43.764 22.581  1   26.74 ? 58  HIS A ND1 1 
ATOM   441  C  CD2 . HIS A 1 58  ? -32.47  -43.209 21.119  1   26.34 ? 58  HIS A CD2 1 
ATOM   442  C  CE1 . HIS A 1 58  ? -34.614 -43.209 21.506  1   27.38 ? 58  HIS A CE1 1 
ATOM   443  N  NE2 . HIS A 1 58  ? -33.701 -42.865 20.602  1   26.54 ? 58  HIS A NE2 1 
ATOM   444  N  N   . GLY A 1 59  ? -30.44  -47.065 21.882  1   22.78 ? 59  GLY A N   1 
ATOM   445  C  CA  . GLY A 1 59  ? -30.005 -47.767 20.682  1   23.58 ? 59  GLY A CA  1 
ATOM   446  C  C   . GLY A 1 59  ? -30.708 -49.099 20.498  1   23.28 ? 59  GLY A C   1 
ATOM   447  O  O   . GLY A 1 59  ? -31.053 -49.467 19.379  1   22.91 ? 59  GLY A O   1 
ATOM   448  N  N   . LYS A 1 60  ? -30.998 -49.78  21.593  1   22.62 ? 60  LYS A N   1 
ATOM   449  C  CA  . LYS A 1 60  ? -31.731 -51.038 21.578  1   23.25 ? 60  LYS A CA  1 
ATOM   450  C  C   . LYS A 1 60  ? -33.196 -50.79  21.123  1   23.23 ? 60  LYS A C   1 
ATOM   451  O  O   . LYS A 1 60  ? -33.733 -51.566 20.313  1   22.96 ? 60  LYS A O   1 
ATOM   452  C  CB  . LYS A 1 60  ? -31.685 -51.689 22.985  1   26.82 ? 60  LYS A CB  1 
ATOM   453  C  CG  . LYS A 1 60  ? -32.559 -52.917 23.124  1   31.62 ? 60  LYS A CG  1 
ATOM   454  C  CD  . LYS A 1 60  ? -32.149 -54.035 22.183  1   38.37 ? 60  LYS A CD  1 
ATOM   455  C  CE  . LYS A 1 60  ? -32.797 -55.346 22.599  1   43.81 ? 60  LYS A CE  1 
ATOM   456  N  NZ  . LYS A 1 60  ? -33.082 -56.195 21.4    1   46.03 ? 60  LYS A NZ  1 
ATOM   457  N  N   . LYS A 1 61  ? -33.807 -49.673 21.555  1   22.01 ? 61  LYS A N   1 
ATOM   458  C  CA  . LYS A 1 61  ? -35.189 -49.341 21.115  1   21.28 ? 61  LYS A CA  1 
ATOM   459  C  C   . LYS A 1 61  ? -35.199 -49.001 19.621  1   21.08 ? 61  LYS A C   1 
ATOM   460  O  O   . LYS A 1 61  ? -36.074 -49.46  18.887  1   20.05 ? 61  LYS A O   1 
ATOM   461  C  CB  . LYS A 1 61  ? -35.723 -48.137 21.903  1   21.33 ? 61  LYS A CB  1 
ATOM   462  C  CG  . LYS A 1 61  ? -35.921 -48.466 23.399  1   24.9  ? 61  LYS A CG  1 
ATOM   463  C  CD  . LYS A 1 61  ? -36.322 -47.266 24.154  1   30.12 ? 61  LYS A CD  1 
ATOM   464  C  CE  . LYS A 1 61  ? -36.426 -47.577 25.631  1   36.95 ? 61  LYS A CE  1 
ATOM   465  N  NZ  . LYS A 1 61  ? -36.893 -46.371 26.364  1   42.17 ? 61  LYS A NZ  1 
ATOM   466  N  N   . VAL A 1 62  ? -34.215 -48.188 19.152  1   20.58 ? 62  VAL A N   1 
ATOM   467  C  CA  . VAL A 1 62  ? -34.131 -47.847 17.74   1   20.4  ? 62  VAL A CA  1 
ATOM   468  C  C   . VAL A 1 62  ? -33.974 -49.122 16.879  1   21.15 ? 62  VAL A C   1 
ATOM   469  O  O   . VAL A 1 62  ? -34.669 -49.289 15.871  1   21.26 ? 62  VAL A O   1 
ATOM   470  C  CB  . VAL A 1 62  ? -32.974 -46.85  17.495  1   20.62 ? 62  VAL A CB  1 
ATOM   471  C  CG1 . VAL A 1 62  ? -32.731 -46.644 15.98   1   20.22 ? 62  VAL A CG1 1 
ATOM   472  C  CG2 . VAL A 1 62  ? -33.28  -45.503 18.168  1   20.74 ? 62  VAL A CG2 1 
ATOM   473  N  N   . ALA A 1 63  ? -33.064 -50.013 17.278  1   21.43 ? 63  ALA A N   1 
ATOM   474  C  CA  . ALA A 1 63  ? -32.821 -51.259 16.539  1   21.76 ? 63  ALA A CA  1 
ATOM   475  C  C   . ALA A 1 63  ? -34.074 -52.158 16.526  1   21.21 ? 63  ALA A C   1 
ATOM   476  O  O   . ALA A 1 63  ? -34.413 -52.72  15.48   1   21.76 ? 63  ALA A O   1 
ATOM   477  C  CB  . ALA A 1 63  ? -31.659 -51.996 17.161  1   22.73 ? 63  ALA A CB  1 
ATOM   478  N  N   . ASP A 1 64  ? -34.763 -52.282 17.672  1   20.87 ? 64  ASP A N   1 
ATOM   479  C  CA  . ASP A 1 64  ? -36.01  -53.07  17.771  1   20.75 ? 64  ASP A CA  1 
ATOM   480  C  C   . ASP A 1 64  ? -37.099 -52.474 16.889  1   19.51 ? 64  ASP A C   1 
ATOM   481  O  O   . ASP A 1 64  ? -37.869 -53.221 16.285  1   19.47 ? 64  ASP A O   1 
ATOM   482  C  CB  . ASP A 1 64  ? -36.511 -53.133 19.23   1   21.92 ? 64  ASP A CB  1 
ATOM   483  C  CG  . ASP A 1 64  ? -35.694 -54.034 20.134  1   26.97 ? 64  ASP A CG  1 
ATOM   484  O  OD1 . ASP A 1 64  ? -34.807 -54.755 19.615  1   27.87 ? 64  ASP A OD1 1 
ATOM   485  O  OD2 . ASP A 1 64  ? -35.942 -54.019 21.361  1   27.44 ? 64  ASP A OD2 1 
ATOM   486  N  N   . ALA A 1 65  ? -37.166 -51.135 16.795  1   18.25 ? 65  ALA A N   1 
ATOM   487  C  CA  . ALA A 1 65  ? -38.157 -50.499 15.912  1   19.83 ? 65  ALA A CA  1 
ATOM   488  C  C   . ALA A 1 65  ? -37.821 -50.837 14.452  1   20.24 ? 65  ALA A C   1 
ATOM   489  O  O   . ALA A 1 65  ? -38.725 -51.088 13.666  1   20.6  ? 65  ALA A O   1 
ATOM   490  C  CB  . ALA A 1 65  ? -38.15  -48.969 16.104  1   20.39 ? 65  ALA A CB  1 
ATOM   491  N  N   . LEU A 1 66  ? -36.536 -50.857 14.094  1   20.08 ? 66  LEU A N   1 
ATOM   492  C  CA  . LEU A 1 66  ? -36.132 -51.192 12.716  1   21.08 ? 66  LEU A CA  1 
ATOM   493  C  C   . LEU A 1 66  ? -36.45  -52.657 12.422  1   21.8  ? 66  LEU A C   1 
ATOM   494  O  O   . LEU A 1 66  ? -36.873 -52.962 11.312  1   21.1  ? 66  LEU A O   1 
ATOM   495  C  CB  . LEU A 1 66  ? -34.65  -50.875 12.472  1   20.82 ? 66  LEU A CB  1 
ATOM   496  C  CG  . LEU A 1 66  ? -34.313 -49.354 12.424  1   22.48 ? 66  LEU A CG  1 
ATOM   497  C  CD1 . LEU A 1 66  ? -32.788 -49.135 12.333  1   23.09 ? 66  LEU A CD1 1 
ATOM   498  C  CD2 . LEU A 1 66  ? -34.995 -48.674 11.208  1   22.37 ? 66  LEU A CD2 1 
ATOM   499  N  N   . THR A 1 67  ? -36.32  -53.554 13.423  1   21.4  ? 67  THR A N   1 
ATOM   500  C  CA  . THR A 1 67  ? -36.662 -54.976 13.251  1   21.99 ? 67  THR A CA  1 
ATOM   501  C  C   . THR A 1 67  ? -38.155 -55.091 12.916  1   21.38 ? 67  THR A C   1 
ATOM   502  O  O   . THR A 1 67  ? -38.534 -55.839 12.013  1   22.59 ? 67  THR A O   1 
ATOM   503  C  CB  . THR A 1 67  ? -36.354 -55.763 14.56   1   24.15 ? 67  THR A CB  1 
ATOM   504  O  OG1 . THR A 1 67  ? -34.943 -55.723 14.781  1   24.93 ? 67  THR A OG1 1 
ATOM   505  C  CG2 . THR A 1 67  ? -36.815 -57.25  14.496  1   24.62 ? 67  THR A CG2 1 
ATOM   506  N  N   . ASN A 1 68  ? -38.994 -54.313 13.601  1   20.21 ? 68  ASN A N   1 
ATOM   507  C  CA  . ASN A 1 68  ? -40.439 -54.31  13.351  1   21.16 ? 68  ASN A CA  1 
ATOM   508  C  C   . ASN A 1 68  ? -40.774 -53.738 11.988  1   21.44 ? 68  ASN A C   1 
ATOM   509  O  O   . ASN A 1 68  ? -41.64  -54.284 11.304  1   22.64 ? 68  ASN A O   1 
ATOM   510  C  CB  . ASN A 1 68  ? -41.183 -53.548 14.46   1   23.63 ? 68  ASN A CB  1 
ATOM   511  C  CG  . ASN A 1 68  ? -41.266 -54.352 15.733  1   30.46 ? 68  ASN A CG  1 
ATOM   512  O  OD1 . ASN A 1 68  ? -41.223 -55.595 15.716  1   33.5  ? 68  ASN A OD1 1 
ATOM   513  N  ND2 . ASN A 1 68  ? -41.37  -53.677 16.875  1   31.19 ? 68  ASN A ND2 1 
ATOM   514  N  N   . ALA A 1 69  ? -40.074 -52.661 11.573  1   19.62 ? 69  ALA A N   1 
ATOM   515  C  CA  . ALA A 1 69  ? -40.286 -52.02  10.279  1   20.69 ? 69  ALA A CA  1 
ATOM   516  C  C   . ALA A 1 69  ? -39.899 -53.014 9.152   1   22.24 ? 69  ALA A C   1 
ATOM   517  O  O   . ALA A 1 69  ? -40.633 -53.141 8.177   1   22.99 ? 69  ALA A O   1 
ATOM   518  C  CB  . ALA A 1 69  ? -39.426 -50.749 10.178  1   20.04 ? 69  ALA A CB  1 
ATOM   519  N  N   . VAL A 1 70  ? -38.773 -53.724 9.3     1   22.57 ? 70  VAL A N   1 
ATOM   520  C  CA  . VAL A 1 70  ? -38.318 -54.781 8.362   1   23.82 ? 70  VAL A CA  1 
ATOM   521  C  C   . VAL A 1 70  ? -39.38  -55.887 8.248   1   25.21 ? 70  VAL A C   1 
ATOM   522  O  O   . VAL A 1 70  ? -39.699 -56.339 7.14    1   25.98 ? 70  VAL A O   1 
ATOM   523  C  CB  . VAL A 1 70  ? -36.952 -55.416 8.81    1   25.16 ? 70  VAL A CB  1 
ATOM   524  C  CG1 . VAL A 1 70  ? -36.647 -56.698 8.029   1   27.07 ? 70  VAL A CG1 1 
ATOM   525  C  CG2 . VAL A 1 70  ? -35.795 -54.434 8.68    1   25.5  ? 70  VAL A CG2 1 
ATOM   526  N  N   . ALA A 1 71  ? -39.907 -56.348 9.378   1   25.21 ? 71  ALA A N   1 
ATOM   527  C  CA  . ALA A 1 71  ? -40.92  -57.401 9.388   1   26.48 ? 71  ALA A CA  1 
ATOM   528  C  C   . ALA A 1 71  ? -42.218 -56.958 8.704   1   26.91 ? 71  ALA A C   1 
ATOM   529  O  O   . ALA A 1 71  ? -42.888 -57.776 8.087   1   27.84 ? 71  ALA A O   1 
ATOM   530  C  CB  . ALA A 1 71  ? -41.216 -57.856 10.825  1   26.58 ? 71  ALA A CB  1 
ATOM   531  N  N   . HIS A 1 72  ? -42.549 -55.672 8.768   1   25.79 ? 72  HIS A N   1 
ATOM   532  C  CA  . HIS A 1 72  ? -43.801 -55.165 8.204   1   25.06 ? 72  HIS A CA  1 
ATOM   533  C  C   . HIS A 1 72  ? -43.522 -54.125 7.128   1   24.52 ? 72  HIS A C   1 
ATOM   534  O  O   . HIS A 1 72  ? -44.199 -53.11  7.05    1   23.96 ? 72  HIS A O   1 
ATOM   535  C  CB  . HIS A 1 72  ? -44.664 -54.58  9.356   1   24.59 ? 72  HIS A CB  1 
ATOM   536  C  CG  . HIS A 1 72  ? -44.927 -55.585 10.431  1   28.03 ? 72  HIS A CG  1 
ATOM   537  N  ND1 . HIS A 1 72  ? -45.721 -56.706 10.199  1   30.13 ? 72  HIS A ND1 1 
ATOM   538  C  CD2 . HIS A 1 72  ? -44.515 -55.602 11.718  1   29.12 ? 72  HIS A CD2 1 
ATOM   539  C  CE1 . HIS A 1 72  ? -45.726 -57.381 11.341  1   30.07 ? 72  HIS A CE1 1 
ATOM   540  N  NE2 . HIS A 1 72  ? -45.02  -56.749 12.284  1   29.62 ? 72  HIS A NE2 1 
ATOM   541  N  N   . VAL A 1 73  ? -42.526 -54.389 6.294   1   24.76 ? 73  VAL A N   1 
ATOM   542  C  CA  . VAL A 1 73  ? -42.047 -53.473 5.275   1   25.79 ? 73  VAL A CA  1 
ATOM   543  C  C   . VAL A 1 73  ? -43.126 -53.071 4.253   1   26.05 ? 73  VAL A C   1 
ATOM   544  O  O   . VAL A 1 73  ? -43.055 -51.958 3.716   1   26    ? 73  VAL A O   1 
ATOM   545  C  CB  . VAL A 1 73  ? -40.777 -54.062 4.614   1   27.61 ? 73  VAL A CB  1 
ATOM   546  C  CG1 . VAL A 1 73  ? -41.128 -55.252 3.726   1   27.88 ? 73  VAL A CG1 1 
ATOM   547  C  CG2 . VAL A 1 73  ? -40.017 -52.998 3.837   1   28.35 ? 73  VAL A CG2 1 
ATOM   548  N  N   . ASP A 1 74  ? -44.154 -53.899 4.057   1   26.26 ? 74  ASP A N   1 
ATOM   549  C  CA  . ASP A 1 74  ? -45.251 -53.546 3.143   1   28.11 ? 74  ASP A CA  1 
ATOM   550  C  C   . ASP A 1 74  ? -46.477 -52.903 3.851   1   27.53 ? 74  ASP A C   1 
ATOM   551  O  O   . ASP A 1 74  ? -47.532 -52.715 3.229   1   27.92 ? 74  ASP A O   1 
ATOM   552  C  CB  . ASP A 1 74  ? -45.699 -54.758 2.313   1   32.24 ? 74  ASP A CB  1 
ATOM   553  C  CG  . ASP A 1 74  ? -44.664 -55.164 1.285   1   39.31 ? 74  ASP A CG  1 
ATOM   554  O  OD1 . ASP A 1 74  ? -44.07  -54.267 0.657   1   39.32 ? 74  ASP A OD1 1 
ATOM   555  O  OD2 . ASP A 1 74  ? -44.418 -56.372 1.144   1   44.69 ? 74  ASP A OD2 1 
ATOM   556  N  N   . ASP A 1 75  ? -46.34  -52.577 5.139   1   25.23 ? 75  ASP A N   1 
ATOM   557  C  CA  . ASP A 1 75  ? -47.433 -51.947 5.886   1   23.95 ? 75  ASP A CA  1 
ATOM   558  C  C   . ASP A 1 75  ? -46.837 -50.983 6.943   1   22.19 ? 75  ASP A C   1 
ATOM   559  O  O   . ASP A 1 75  ? -47.329 -50.889 8.095   1   21.37 ? 75  ASP A O   1 
ATOM   560  C  CB  . ASP A 1 75  ? -48.248 -53.054 6.554   1   24.76 ? 75  ASP A CB  1 
ATOM   561  C  CG  . ASP A 1 75  ? -49.61  -52.635 7.081   1   29.05 ? 75  ASP A CG  1 
ATOM   562  O  OD1 . ASP A 1 75  ? -50.226 -51.725 6.487   1   28.21 ? 75  ASP A OD1 1 
ATOM   563  O  OD2 . ASP A 1 75  ? -50.056 -53.217 8.083   1   30.8  ? 75  ASP A OD2 1 
ATOM   564  N  N   . MET A 1 76  ? -45.756 -50.294 6.576   1   21.07 ? 76  MET A N   1 
ATOM   565  C  CA  . MET A 1 76  ? -45.037 -49.44  7.53    1   21.3  ? 76  MET A CA  1 
ATOM   566  C  C   . MET A 1 76  ? -45.858 -48.271 8.112   1   21.08 ? 76  MET A C   1 
ATOM   567  O  O   . MET A 1 76  ? -45.779 -48.089 9.327   1   20.73 ? 76  MET A O   1 
ATOM   568  C  CB  . MET A 1 76  ? -43.705 -48.958 6.961   1   22.22 ? 76  MET A CB  1 
ATOM   569  C  CG  . MET A 1 76  ? -42.724 -50.105 6.831   1   26.36 ? 76  MET A CG  1 
ATOM   570  S  SD  . MET A 1 76  ? -41.022 -49.536 6.614   1   29.42 ? 76  MET A SD  1 
ATOM   571  C  CE  . MET A 1 76  ? -41.044 -49.097 4.916   1   28.54 ? 76  MET A CE  1 
ATOM   572  N  N   . PRO A 1 77  ? -46.687 -47.512 7.358   1   21.31 ? 77  PRO A N   1 
ATOM   573  C  CA  . PRO A 1 77  ? -47.486 -46.44  8.011   1   21.03 ? 77  PRO A CA  1 
ATOM   574  C  C   . PRO A 1 77  ? -48.347 -46.987 9.167   1   20.64 ? 77  PRO A C   1 
ATOM   575  O  O   . PRO A 1 77  ? -48.364 -46.398 10.251  1   19.7  ? 77  PRO A O   1 
ATOM   576  C  CB  . PRO A 1 77  ? -48.343 -45.891 6.858   1   21.65 ? 77  PRO A CB  1 
ATOM   577  C  CG  . PRO A 1 77  ? -47.454 -46.098 5.623   1   22.02 ? 77  PRO A CG  1 
ATOM   578  C  CD  . PRO A 1 77  ? -46.871 -47.501 5.883   1   20.57 ? 77  PRO A CD  1 
ATOM   579  N  N   . ASN A 1 78  ? -48.991 -48.14  8.968   1   20.83 ? 78  ASN A N   1 
ATOM   580  C  CA  . ASN A 1 78  ? -49.781 -48.753 10.048  1   21.83 ? 78  ASN A CA  1 
ATOM   581  C  C   . ASN A 1 78  ? -48.881 -49.284 11.171  1   22.15 ? 78  ASN A C   1 
ATOM   582  O  O   . ASN A 1 78  ? -49.148 -49.022 12.337  1   22.63 ? 78  ASN A O   1 
ATOM   583  C  CB  . ASN A 1 78  ? -50.662 -49.879 9.494   1   23.14 ? 78  ASN A CB  1 
ATOM   584  C  CG  . ASN A 1 78  ? -51.869 -49.35  8.754   1   27.96 ? 78  ASN A CG  1 
ATOM   585  O  OD1 . ASN A 1 78  ? -52.432 -48.308 9.115   1   28.71 ? 78  ASN A OD1 1 
ATOM   586  N  ND2 . ASN A 1 78  ? -52.287 -50.05  7.705   1   28.02 ? 78  ASN A ND2 1 
ATOM   587  N  N   . ALA A 1 79  ? -47.843 -50.058 10.838  1   21.29 ? 79  ALA A N   1 
ATOM   588  C  CA  . ALA A 1 79  ? -46.964 -50.654 11.849  1   20.76 ? 79  ALA A CA  1 
ATOM   589  C  C   . ALA A 1 79  ? -46.239 -49.632 12.698  1   20.9  ? 79  ALA A C   1 
ATOM   590  O  O   . ALA A 1 79  ? -46.018 -49.885 13.884  1   20.99 ? 79  ALA A O   1 
ATOM   591  C  CB  . ALA A 1 79  ? -45.947 -51.594 11.183  1   20.06 ? 79  ALA A CB  1 
ATOM   592  N  N   . LEU A 1 80  ? -45.902 -48.464 12.134  1   19.71 ? 80  LEU A N   1 
ATOM   593  C  CA  . LEU A 1 80  ? -45.111 -47.474 12.877  1   19.28 ? 80  LEU A CA  1 
ATOM   594  C  C   . LEU A 1 80  ? -45.865 -46.202 13.277  1   18.67 ? 80  LEU A C   1 
ATOM   595  O  O   . LEU A 1 80  ? -45.224 -45.173 13.515  1   17.96 ? 80  LEU A O   1 
ATOM   596  C  CB  . LEU A 1 80  ? -43.936 -47.054 11.982  1   19.88 ? 80  LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 80  ? -43.08  -48.178 11.382  1   21.66 ? 80  LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 80  ? -41.91  -47.592 10.582  1   21.76 ? 80  LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 80  ? -42.579 -49.157 12.477  1   20.9  ? 80  LEU A CD2 1 
ATOM   600  N  N   . SER A 1 81  ? -47.204 -46.241 13.289  1   18.84 ? 81  SER A N   1 
ATOM   601  C  CA  . SER A 1 81  ? -47.983 -45.028 13.521  1   19.52 ? 81  SER A CA  1 
ATOM   602  C  C   . SER A 1 81  ? -47.653 -44.282 14.815  1   18.6  ? 81  SER A C   1 
ATOM   603  O  O   . SER A 1 81  ? -47.608 -43.052 14.789  1   17.3  ? 81  SER A O   1 
ATOM   604  C  CB  . SER A 1 81  ? -49.487 -45.296 13.425  1   20.93 ? 81  SER A CB  1 
ATOM   605  O  OG  . SER A 1 81  ? -49.921 -46.069 14.522  1   25.01 ? 81  SER A OG  1 
ATOM   606  N  N   . ALA A 1 82  ? -47.431 -44.991 15.947  1   18.22 ? 82  ALA A N   1 
ATOM   607  C  CA  . ALA A 1 82  ? -47.121 -44.312 17.217  1   18.13 ? 82  ALA A CA  1 
ATOM   608  C  C   . ALA A 1 82  ? -45.698 -43.679 17.167  1   18.55 ? 82  ALA A C   1 
ATOM   609  O  O   . ALA A 1 82  ? -45.468 -42.635 17.786  1   17.79 ? 82  ALA A O   1 
ATOM   610  C  CB  . ALA A 1 82  ? -47.232 -45.299 18.383  1   18.55 ? 82  ALA A CB  1 
ATOM   611  N  N   . LEU A 1 83  ? -44.774 -44.262 16.359  1   17.67 ? 83  LEU A N   1 
ATOM   612  C  CA  . LEU A 1 83  ? -43.456 -43.65  16.178  1   17.57 ? 83  LEU A CA  1 
ATOM   613  C  C   . LEU A 1 83  ? -43.583 -42.393 15.33   1   17.69 ? 83  LEU A C   1 
ATOM   614  O  O   . LEU A 1 83  ? -42.87  -41.423 15.585  1   18.09 ? 83  LEU A O   1 
ATOM   615  C  CB  . LEU A 1 83  ? -42.459 -44.637 15.541  1   17.79 ? 83  LEU A CB  1 
ATOM   616  C  CG  . LEU A 1 83  ? -42.006 -45.752 16.499  1   19.5  ? 83  LEU A CG  1 
ATOM   617  C  CD1 . LEU A 1 83  ? -41.038 -46.711 15.797  1   20.22 ? 83  LEU A CD1 1 
ATOM   618  C  CD2 . LEU A 1 83  ? -41.286 -45.15  17.729  1   20.17 ? 83  LEU A CD2 1 
ATOM   619  N  N   . SER A 1 84  ? -44.523 -42.386 14.34   1   17.43 ? 84  SER A N   1 
ATOM   620  C  CA  . SER A 1 84  ? -44.803 -41.191 13.541  1   17.61 ? 84  SER A CA  1 
ATOM   621  C  C   . SER A 1 84  ? -45.446 -40.132 14.463  1   18.76 ? 84  SER A C   1 
ATOM   622  O  O   . SER A 1 84  ? -45.029 -38.973 14.467  1   18.77 ? 84  SER A O   1 
ATOM   623  C  CB  . SER A 1 84  ? -45.723 -41.512 12.372  1   19.07 ? 84  SER A CB  1 
ATOM   624  O  OG  . SER A 1 84  ? -46.043 -40.298 11.696  1   22.41 ? 84  SER A OG  1 
ATOM   625  N  N   . ASP A 1 85  ? -46.381 -40.536 15.326  1   19.18 ? 85  ASP A N   1 
ATOM   626  C  CA  . ASP A 1 85  ? -46.973 -39.626 16.322  1   18.89 ? 85  ASP A CA  1 
ATOM   627  C  C   . ASP A 1 85  ? -45.859 -38.938 17.165  1   19.67 ? 85  ASP A C   1 
ATOM   628  O  O   . ASP A 1 85  ? -45.845 -37.706 17.318  1   20.21 ? 85  ASP A O   1 
ATOM   629  C  CB  . ASP A 1 85  ? -47.929 -40.425 17.229  1   19.45 ? 85  ASP A CB  1 
ATOM   630  C  CG  . ASP A 1 85  ? -48.939 -39.584 17.988  1   26.07 ? 85  ASP A CG  1 
ATOM   631  O  OD1 . ASP A 1 85  ? -48.875 -38.312 17.882  1   25    ? 85  ASP A OD1 1 
ATOM   632  O  OD2 . ASP A 1 85  ? -49.8   -40.181 18.684  1   27.66 ? 85  ASP A OD2 1 
ATOM   633  N  N   . LEU A 1 86  ? -44.926 -39.726 17.691  1   19.21 ? 86  LEU A N   1 
ATOM   634  C  CA  . LEU A 1 86  ? -43.822 -39.169 18.5    1   19.56 ? 86  LEU A CA  1 
ATOM   635  C  C   . LEU A 1 86  ? -42.875 -38.285 17.642  1   19.31 ? 86  LEU A C   1 
ATOM   636  O  O   . LEU A 1 86  ? -42.593 -37.156 18.033  1   19.64 ? 86  LEU A O   1 
ATOM   637  C  CB  . LEU A 1 86  ? -43.01  -40.33  19.108  1   19.72 ? 86  LEU A CB  1 
ATOM   638  C  CG  . LEU A 1 86  ? -41.728 -39.94  19.841  1   19.87 ? 86  LEU A CG  1 
ATOM   639  C  CD1 . LEU A 1 86  ? -42.066 -39.033 21.058  1   18.95 ? 86  LEU A CD1 1 
ATOM   640  C  CD2 . LEU A 1 86  ? -40.93  -41.208 20.248  1   20.13 ? 86  LEU A CD2 1 
ATOM   641  N  N   . HIS A 1 87  ? -42.351 -38.8   16.513  1   18.24 ? 87  HIS A N   1 
ATOM   642  C  CA  . HIS A 1 87  ? -41.326 -38.067 15.752  1   18.7  ? 87  HIS A CA  1 
ATOM   643  C  C   . HIS A 1 87  ? -41.865 -36.905 14.937  1   19.26 ? 87  HIS A C   1 
ATOM   644  O  O   . HIS A 1 87  ? -41.191 -35.876 14.842  1   20.34 ? 87  HIS A O   1 
ATOM   645  C  CB  . HIS A 1 87  ? -40.494 -39.014 14.853  1   17.8  ? 87  HIS A CB  1 
ATOM   646  C  CG  . HIS A 1 87  ? -39.667 -39.998 15.654  1   17.06 ? 87  HIS A CG  1 
ATOM   647  N  ND1 . HIS A 1 87  ? -40.222 -41.147 16.163  1   18.79 ? 87  HIS A ND1 1 
ATOM   648  C  CD2 . HIS A 1 87  ? -38.367 -39.949 16.016  1   17.59 ? 87  HIS A CD2 1 
ATOM   649  C  CE1 . HIS A 1 87  ? -39.235 -41.793 16.777  1   19.6  ? 87  HIS A CE1 1 
ATOM   650  N  NE2 . HIS A 1 87  ? -38.108 -41.104 16.737  1   19.01 ? 87  HIS A NE2 1 
ATOM   651  N  N   . ALA A 1 88  ? -43.064 -37.061 14.349  1   17.79 ? 88  ALA A N   1 
ATOM   652  C  CA  . ALA A 1 88  ? -43.616 -36.01  13.507  1   18.77 ? 88  ALA A CA  1 
ATOM   653  C  C   . ALA A 1 88  ? -44.539 -35.062 14.249  1   20.75 ? 88  ALA A C   1 
ATOM   654  O  O   . ALA A 1 88  ? -44.52  -33.851 13.969  1   23.47 ? 88  ALA A O   1 
ATOM   655  C  CB  . ALA A 1 88  ? -44.353 -36.621 12.282  1   18.92 ? 88  ALA A CB  1 
ATOM   656  N  N   . HIS A 1 89  ? -45.389 -35.579 15.144  1   20.34 ? 89  HIS A N   1 
ATOM   657  C  CA  . HIS A 1 89  ? -46.374 -34.715 15.81   1   20.8  ? 89  HIS A CA  1 
ATOM   658  C  C   . HIS A 1 89  ? -45.868 -34.108 17.107  1   20.78 ? 89  HIS A C   1 
ATOM   659  O  O   . HIS A 1 89  ? -46.228 -32.969 17.411  1   22.29 ? 89  HIS A O   1 
ATOM   660  C  CB  . HIS A 1 89  ? -47.71  -35.458 16.059  1   21.17 ? 89  HIS A CB  1 
ATOM   661  C  CG  . HIS A 1 89  ? -48.374 -35.944 14.808  1   21.16 ? 89  HIS A CG  1 
ATOM   662  N  ND1 . HIS A 1 89  ? -49.51  -35.324 14.31   1   21.7  ? 89  HIS A ND1 1 
ATOM   663  C  CD2 . HIS A 1 89  ? -48.014 -36.949 13.963  1   21.8  ? 89  HIS A CD2 1 
ATOM   664  C  CE1 . HIS A 1 89  ? -49.82  -35.968 13.189  1   21.71 ? 89  HIS A CE1 1 
ATOM   665  N  NE2 . HIS A 1 89  ? -48.956 -36.966 12.944  1   22.33 ? 89  HIS A NE2 1 
ATOM   666  N  N   . LYS A 1 90  ? -45.068 -34.854 17.878  1   19.53 ? 90  LYS A N   1 
ATOM   667  C  CA  . LYS A 1 90  ? -44.577 -34.351 19.154  1   19.55 ? 90  LYS A CA  1 
ATOM   668  C  C   . LYS A 1 90  ? -43.186 -33.703 19.055  1   19.61 ? 90  LYS A C   1 
ATOM   669  O  O   . LYS A 1 90  ? -43.067 -32.524 19.373  1   20.37 ? 90  LYS A O   1 
ATOM   670  C  CB  . LYS A 1 90  ? -44.615 -35.471 20.248  1   19.77 ? 90  LYS A CB  1 
ATOM   671  C  CG  . LYS A 1 90  ? -44.17  -35.012 21.633  1   22.29 ? 90  LYS A CG  1 
ATOM   672  C  CD  . LYS A 1 90  ? -45.183 -33.997 22.162  1   26.93 ? 90  LYS A CD  1 
ATOM   673  C  CE  . LYS A 1 90  ? -44.935 -33.652 23.623  1   32.64 ? 90  LYS A CE  1 
ATOM   674  N  NZ  . LYS A 1 90  ? -45.915 -32.619 24.087  1   33.96 ? 90  LYS A NZ  1 
ATOM   675  N  N   . LEU A 1 91  ? -42.145 -34.473 18.703  1   17.91 ? 91  LEU A N   1 
ATOM   676  C  CA  . LEU A 1 91  ? -40.754 -33.995 18.638  1   18.67 ? 91  LEU A CA  1 
ATOM   677  C  C   . LEU A 1 91  ? -40.541 -33.045 17.46   1   20.23 ? 91  LEU A C   1 
ATOM   678  O  O   . LEU A 1 91  ? -39.677 -32.169 17.532  1   22.01 ? 91  LEU A O   1 
ATOM   679  C  CB  . LEU A 1 91  ? -39.797 -35.192 18.485  1   18.66 ? 91  LEU A CB  1 
ATOM   680  C  CG  . LEU A 1 91  ? -39.783 -36.173 19.668  1   20.66 ? 91  LEU A CG  1 
ATOM   681  C  CD1 . LEU A 1 91  ? -38.935 -37.407 19.35   1   21.31 ? 91  LEU A CD1 1 
ATOM   682  C  CD2 . LEU A 1 91  ? -39.279 -35.467 20.954  1   22.35 ? 91  LEU A CD2 1 
ATOM   683  N  N   . ARG A 1 92  ? -41.251 -33.289 16.359  1   18.7  ? 92  ARG A N   1 
ATOM   684  C  CA  . ARG A 1 92  ? -41.139 -32.522 15.104  1   18.27 ? 92  ARG A CA  1 
ATOM   685  C  C   . ARG A 1 92  ? -39.692 -32.521 14.609  1   18.05 ? 92  ARG A C   1 
ATOM   686  O  O   . ARG A 1 92  ? -39.099 -31.463 14.377  1   17.88 ? 92  ARG A O   1 
ATOM   687  C  CB  . ARG A 1 92  ? -41.653 -31.102 15.317  1   19.44 ? 92  ARG A CB  1 
ATOM   688  C  CG  . ARG A 1 92  ? -43.139 -31.064 15.62   1   23.62 ? 92  ARG A CG  1 
ATOM   689  C  CD  . ARG A 1 92  ? -43.45  -29.625 15.872  1   30.44 ? 92  ARG A CD  1 
ATOM   690  N  NE  . ARG A 1 92  ? -44.84  -29.371 16.197  1   35.16 ? 92  ARG A NE  1 
ATOM   691  C  CZ  . ARG A 1 92  ? -45.244 -28.693 17.266  1   39.96 ? 92  ARG A CZ  1 
ATOM   692  N  NH1 . ARG A 1 92  ? -44.361 -28.26  18.16   1   41.38 ? 92  ARG A NH1 1 
ATOM   693  N  NH2 . ARG A 1 92  ? -46.537 -28.459 17.462  1   40.5  ? 92  ARG A NH2 1 
ATOM   694  N  N   . VAL A 1 93  ? -39.109 -33.726 14.514  1   17.04 ? 93  VAL A N   1 
ATOM   695  C  CA  . VAL A 1 93  ? -37.721 -33.862 14.095  1   16.35 ? 93  VAL A CA  1 
ATOM   696  C  C   . VAL A 1 93  ? -37.586 -33.433 12.632  1   17.45 ? 93  VAL A C   1 
ATOM   697  O  O   . VAL A 1 93  ? -38.372 -33.847 11.778  1   17.54 ? 93  VAL A O   1 
ATOM   698  C  CB  . VAL A 1 93  ? -37.258 -35.341 14.29   1   15.57 ? 93  VAL A CB  1 
ATOM   699  C  CG1 . VAL A 1 93  ? -35.828 -35.546 13.789  1   15.97 ? 93  VAL A CG1 1 
ATOM   700  C  CG2 . VAL A 1 93  ? -37.426 -35.794 15.763  1   15.48 ? 93  VAL A CG2 1 
ATOM   701  N  N   . ASP A 1 94  ? -36.589 -32.568 12.336  1   18.06 ? 94  ASP A N   1 
ATOM   702  C  CA  . ASP A 1 94  ? -36.335 -32.151 10.969  1   17.84 ? 94  ASP A CA  1 
ATOM   703  C  C   . ASP A 1 94  ? -35.85  -33.391 10.188  1   18.87 ? 94  ASP A C   1 
ATOM   704  O  O   . ASP A 1 94  ? -34.934 -34.085 10.619  1   19.5  ? 94  ASP A O   1 
ATOM   705  C  CB  . ASP A 1 94  ? -35.261 -31.061 10.976  1   18.84 ? 94  ASP A CB  1 
ATOM   706  C  CG  . ASP A 1 94  ? -34.994 -30.437 9.622   1   20.62 ? 94  ASP A CG  1 
ATOM   707  O  OD1 . ASP A 1 94  ? -34.822 -31.179 8.663   1   20.64 ? 94  ASP A OD1 1 
ATOM   708  O  OD2 . ASP A 1 94  ? -34.915 -29.213 9.552   1   21.9  ? 94  ASP A OD2 1 
ATOM   709  N  N   . PRO A 1 95  ? -36.444 -33.638 9.002   1   18.86 ? 95  PRO A N   1 
ATOM   710  C  CA  . PRO A 1 95  ? -36.061 -34.788 8.187   1   18.72 ? 95  PRO A CA  1 
ATOM   711  C  C   . PRO A 1 95  ? -34.573 -34.937 7.902   1   18.23 ? 95  PRO A C   1 
ATOM   712  O  O   . PRO A 1 95  ? -34.126 -36.058 7.688   1   17.26 ? 95  PRO A O   1 
ATOM   713  C  CB  . PRO A 1 95  ? -36.818 -34.539 6.871   1   20.44 ? 95  PRO A CB  1 
ATOM   714  C  CG  . PRO A 1 95  ? -37.997 -33.799 7.26    1   21.24 ? 95  PRO A CG  1 
ATOM   715  C  CD  . PRO A 1 95  ? -37.576 -32.914 8.403   1   19.37 ? 95  PRO A CD  1 
ATOM   716  N  N   . VAL A 1 96  ? -33.781 -33.839 7.911   1   18.81 ? 96  VAL A N   1 
ATOM   717  C  CA  . VAL A 1 96  ? -32.329 -33.954 7.693   1   19.61 ? 96  VAL A CA  1 
ATOM   718  C  C   . VAL A 1 96  ? -31.706 -34.886 8.739   1   18.78 ? 96  VAL A C   1 
ATOM   719  O  O   . VAL A 1 96  ? -30.856 -35.692 8.403   1   19.48 ? 96  VAL A O   1 
ATOM   720  C  CB  . VAL A 1 96  ? -31.589 -32.582 7.662   1   21.62 ? 96  VAL A CB  1 
ATOM   721  C  CG1 . VAL A 1 96  ? -31.574 -31.921 9.066   1   22.46 ? 96  VAL A CG1 1 
ATOM   722  C  CG2 . VAL A 1 96  ? -30.161 -32.765 7.15    1   23.25 ? 96  VAL A CG2 1 
ATOM   723  N  N   . ASN A 1 97  ? -32.21  -34.858 9.98    1   17.34 ? 97  ASN A N   1 
ATOM   724  C  CA  . ASN A 1 97  ? -31.665 -35.7   11.05   1   17.36 ? 97  ASN A CA  1 
ATOM   725  C  C   . ASN A 1 97  ? -31.824 -37.192 10.777  1   17.26 ? 97  ASN A C   1 
ATOM   726  O  O   . ASN A 1 97  ? -30.939 -37.967 11.129  1   17.33 ? 97  ASN A O   1 
ATOM   727  C  CB  . ASN A 1 97  ? -32.282 -35.29  12.386  1   17.72 ? 97  ASN A CB  1 
ATOM   728  C  CG  . ASN A 1 97  ? -31.897 -33.852 12.668  1   22.05 ? 97  ASN A CG  1 
ATOM   729  O  OD1 . ASN A 1 97  ? -30.716 -33.535 12.773  1   23.41 ? 97  ASN A OD1 1 
ATOM   730  N  ND2 . ASN A 1 97  ? -32.851 -32.959 12.645  1   19.85 ? 97  ASN A ND2 1 
ATOM   731  N  N   . PHE A 1 98  ? -32.91  -37.581 10.092  1   17.07 ? 98  PHE A N   1 
ATOM   732  C  CA  . PHE A 1 98  ? -33.135 -38.973 9.683   1   17.67 ? 98  PHE A CA  1 
ATOM   733  C  C   . PHE A 1 98  ? -32.108 -39.389 8.628   1   18    ? 98  PHE A C   1 
ATOM   734  O  O   . PHE A 1 98  ? -31.66  -40.532 8.657   1   18    ? 98  PHE A O   1 
ATOM   735  C  CB  . PHE A 1 98  ? -34.56  -39.146 9.126   1   18.1  ? 98  PHE A CB  1 
ATOM   736  C  CG  . PHE A 1 98  ? -35.562 -39.267 10.251  1   19.75 ? 98  PHE A CG  1 
ATOM   737  C  CD1 . PHE A 1 98  ? -36.069 -38.135 10.872  1   20.94 ? 98  PHE A CD1 1 
ATOM   738  C  CD2 . PHE A 1 98  ? -35.974 -40.512 10.707  1   20.24 ? 98  PHE A CD2 1 
ATOM   739  C  CE1 . PHE A 1 98  ? -36.933 -38.244 11.977  1   20.65 ? 98  PHE A CE1 1 
ATOM   740  C  CE2 . PHE A 1 98  ? -36.868 -40.617 11.796  1   20.96 ? 98  PHE A CE2 1 
ATOM   741  C  CZ  . PHE A 1 98  ? -37.346 -39.483 12.405  1   20.86 ? 98  PHE A CZ  1 
ATOM   742  N  N   . LYS A 1 99  ? -31.712 -38.478 7.723   1   17.33 ? 99  LYS A N   1 
ATOM   743  C  CA  . LYS A 1 99  ? -30.647 -38.808 6.749   1   17.9  ? 99  LYS A CA  1 
ATOM   744  C  C   . LYS A 1 99  ? -29.32  -39.029 7.501   1   17.3  ? 99  LYS A C   1 
ATOM   745  O  O   . LYS A 1 99  ? -28.536 -39.9   7.129   1   17.18 ? 99  LYS A O   1 
ATOM   746  C  CB  . LYS A 1 99  ? -30.46  -37.652 5.752   1   20.62 ? 99  LYS A CB  1 
ATOM   747  C  CG  . LYS A 1 99  ? -31.719 -37.394 4.924   1   24.13 ? 99  LYS A CG  1 
ATOM   748  C  CD  . LYS A 1 99  ? -31.434 -36.409 3.795   1   27.95 ? 99  LYS A CD  1 
ATOM   749  C  CE  . LYS A 1 99  ? -32.709 -35.986 3.114   1   33.8  ? 99  LYS A CE  1 
ATOM   750  N  NZ  . LYS A 1 99  ? -33.166 -37.037 2.168   1   38.65 ? 99  LYS A NZ  1 
ATOM   751  N  N   . LEU A 1 100 ? -29.095 -38.258 8.574   1   16.44 ? 100 LEU A N   1 
ATOM   752  C  CA  . LEU A 1 100 ? -27.861 -38.384 9.345   1   17.52 ? 100 LEU A CA  1 
ATOM   753  C  C   . LEU A 1 100 ? -27.802 -39.693 10.096  1   18.46 ? 100 LEU A C   1 
ATOM   754  O  O   . LEU A 1 100 ? -26.769 -40.375 10.036  1   19.92 ? 100 LEU A O   1 
ATOM   755  C  CB  . LEU A 1 100 ? -27.681 -37.191 10.279  1   17.54 ? 100 LEU A CB  1 
ATOM   756  C  CG  . LEU A 1 100 ? -27.702 -35.837 9.583   1   18.63 ? 100 LEU A CG  1 
ATOM   757  C  CD1 . LEU A 1 100 ? -27.608 -34.687 10.624  1   19.46 ? 100 LEU A CD1 1 
ATOM   758  C  CD2 . LEU A 1 100 ? -26.606 -35.739 8.507   1   19.97 ? 100 LEU A CD2 1 
ATOM   759  N  N   . LEU A 1 101 ? -28.902 -40.069 10.747  1   18.11 ? 101 LEU A N   1 
ATOM   760  C  CA  . LEU A 1 101 ? -28.935 -41.337 11.491  1   18.9  ? 101 LEU A CA  1 
ATOM   761  C  C   . LEU A 1 101 ? -28.865 -42.519 10.514  1   18.45 ? 101 LEU A C   1 
ATOM   762  O  O   . LEU A 1 101 ? -28.177 -43.504 10.8    1   18.71 ? 101 LEU A O   1 
ATOM   763  C  CB  . LEU A 1 101 ? -30.177 -41.475 12.38   1   19.18 ? 101 LEU A CB  1 
ATOM   764  C  CG  . LEU A 1 101 ? -30.252 -42.761 13.242  1   21.05 ? 101 LEU A CG  1 
ATOM   765  C  CD1 . LEU A 1 101 ? -28.99  -42.966 14.104  1   21.94 ? 101 LEU A CD1 1 
ATOM   766  C  CD2 . LEU A 1 101 ? -31.503 -42.764 14.125  1   21.44 ? 101 LEU A CD2 1 
ATOM   767  N  N   . SER A 1 102 ? -29.549 -42.418 9.365   1   17.62 ? 102 SER A N   1 
ATOM   768  C  CA  . SER A 1 102 ? -29.551 -43.502 8.378   1   17.32 ? 102 SER A CA  1 
ATOM   769  C  C   . SER A 1 102 ? -28.131 -43.747 7.86    1   18.23 ? 102 SER A C   1 
ATOM   770  O  O   . SER A 1 102 ? -27.675 -44.906 7.801   1   18.18 ? 102 SER A O   1 
ATOM   771  C  CB  . SER A 1 102 ? -30.512 -43.167 7.243   1   18.5  ? 102 SER A CB  1 
ATOM   772  O  OG  . SER A 1 102 ? -31.841 -43.016 7.728   1   19.85 ? 102 SER A OG  1 
ATOM   773  N  N   . HIS A 1 103 ? -27.398 -42.652 7.592   1   17.98 ? 103 HIS A N   1 
ATOM   774  C  CA  . HIS A 1 103 ? -25.991 -42.738 7.155   1   19.21 ? 103 HIS A CA  1 
ATOM   775  C  C   . HIS A 1 103 ? -25.142 -43.412 8.238   1   19.65 ? 103 HIS A C   1 
ATOM   776  O  O   . HIS A 1 103 ? -24.353 -44.305 7.942   1   20.66 ? 103 HIS A O   1 
ATOM   777  C  CB  . HIS A 1 103 ? -25.445 -41.343 6.829   1   19.67 ? 103 HIS A CB  1 
ATOM   778  C  CG  . HIS A 1 103 ? -23.958 -41.305 6.579   1   20.97 ? 103 HIS A CG  1 
ATOM   779  N  ND1 . HIS A 1 103 ? -23.398 -41.907 5.468   1   21.74 ? 103 HIS A ND1 1 
ATOM   780  C  CD2 . HIS A 1 103 ? -22.979 -40.677 7.281   1   21.83 ? 103 HIS A CD2 1 
ATOM   781  C  CE1 . HIS A 1 103 ? -22.092 -41.663 5.541   1   22.63 ? 103 HIS A CE1 1 
ATOM   782  N  NE2 . HIS A 1 103 ? -21.794 -40.925 6.62    1   23.31 ? 103 HIS A NE2 1 
ATOM   783  N  N   . CYS A 1 104 ? -25.306 -43.006 9.496   1   19.64 ? 104 CYS A N   1 
ATOM   784  C  CA  . CYS A 1 104 ? -24.554 -43.641 10.594  1   20.45 ? 104 CYS A CA  1 
ATOM   785  C  C   . CYS A 1 104 ? -24.922 -45.12  10.808  1   20.56 ? 104 CYS A C   1 
ATOM   786  O  O   . CYS A 1 104 ? -24.048 -45.882 11.164  1   20.62 ? 104 CYS A O   1 
ATOM   787  C  CB  . CYS A 1 104 ? -24.668 -42.826 11.871  1   20.31 ? 104 CYS A CB  1 
ATOM   788  S  SG  . CYS A 1 104 ? -23.942 -41.17  11.719  1   23.94 ? 104 CYS A SG  1 
ATOM   789  N  N   . LEU A 1 105 ? -26.174 -45.534 10.553  1   20.48 ? 105 LEU A N   1 
ATOM   790  C  CA  . LEU A 1 105 ? -26.576 -46.948 10.622  1   21.44 ? 105 LEU A CA  1 
ATOM   791  C  C   . LEU A 1 105 ? -25.863 -47.709 9.463   1   21.04 ? 105 LEU A C   1 
ATOM   792  O  O   . LEU A 1 105 ? -25.285 -48.793 9.665   1   21.23 ? 105 LEU A O   1 
ATOM   793  C  CB  . LEU A 1 105 ? -28.114 -47.064 10.449  1   23    ? 105 LEU A CB  1 
ATOM   794  C  CG  . LEU A 1 105 ? -28.961 -46.744 11.698  1   27.13 ? 105 LEU A CG  1 
ATOM   795  C  CD1 . LEU A 1 105 ? -30.411 -46.398 11.337  1   27.89 ? 105 LEU A CD1 1 
ATOM   796  C  CD2 . LEU A 1 105 ? -28.95  -47.926 12.707  1   29.23 ? 105 LEU A CD2 1 
ATOM   797  N  N   . LEU A 1 106 ? -25.845 -47.113 8.255   1   20.29 ? 106 LEU A N   1 
ATOM   798  C  CA  . LEU A 1 106 ? -25.117 -47.726 7.124   1   20.66 ? 106 LEU A CA  1 
ATOM   799  C  C   . LEU A 1 106 ? -23.633 -47.9   7.454   1   21.41 ? 106 LEU A C   1 
ATOM   800  O  O   . LEU A 1 106 ? -23.067 -48.953 7.198   1   22.02 ? 106 LEU A O   1 
ATOM   801  C  CB  . LEU A 1 106 ? -25.275 -46.865 5.85    1   20.44 ? 106 LEU A CB  1 
ATOM   802  C  CG  . LEU A 1 106 ? -26.691 -46.829 5.261   1   22.02 ? 106 LEU A CG  1 
ATOM   803  C  CD1 . LEU A 1 106 ? -26.692 -46.074 3.971   1   22.78 ? 106 LEU A CD1 1 
ATOM   804  C  CD2 . LEU A 1 106 ? -27.197 -48.274 4.91    1   23.36 ? 106 LEU A CD2 1 
ATOM   805  N  N   . VAL A 1 107 ? -23.003 -46.868 8.022   1   21.31 ? 107 VAL A N   1 
ATOM   806  C  CA  . VAL A 1 107 ? -21.587 -46.912 8.389   1   21.88 ? 107 VAL A CA  1 
ATOM   807  C  C   . VAL A 1 107 ? -21.319 -48.033 9.411   1   22.52 ? 107 VAL A C   1 
ATOM   808  O  O   . VAL A 1 107 ? -20.343 -48.773 9.279   1   23.37 ? 107 VAL A O   1 
ATOM   809  C  CB  . VAL A 1 107 ? -21.123 -45.518 8.938   1   22.72 ? 107 VAL A CB  1 
ATOM   810  C  CG1 . VAL A 1 107 ? -19.743 -45.634 9.621   1   23.33 ? 107 VAL A CG1 1 
ATOM   811  C  CG2 . VAL A 1 107 ? -21.068 -44.484 7.81    1   22.37 ? 107 VAL A CG2 1 
ATOM   812  N  N   . THR A 1 108 ? -22.204 -48.176 10.396  1   22.25 ? 108 THR A N   1 
ATOM   813  C  CA  . THR A 1 108 ? -22.077 -49.207 11.424  1   22.51 ? 108 THR A CA  1 
ATOM   814  C  C   . THR A 1 108 ? -22.198 -50.591 10.776  1   24.05 ? 108 THR A C   1 
ATOM   815  O  O   . THR A 1 108 ? -21.392 -51.478 11.056  1   24.63 ? 108 THR A O   1 
ATOM   816  C  CB  . THR A 1 108 ? -23.173 -48.991 12.485  1   22.06 ? 108 THR A CB  1 
ATOM   817  O  OG1 . THR A 1 108 ? -23.043 -47.661 13.006  1   21.19 ? 108 THR A OG1 1 
ATOM   818  C  CG2 . THR A 1 108 ? -23.103 -50.039 13.636  1   21.78 ? 108 THR A CG2 1 
ATOM   819  N  N   . LEU A 1 109 ? -23.183 -50.774 9.893   1   24.55 ? 109 LEU A N   1 
ATOM   820  C  CA  . LEU A 1 109 ? -23.372 -52.061 9.209   1   25.37 ? 109 LEU A CA  1 
ATOM   821  C  C   . LEU A 1 109 ? -22.158 -52.401 8.316   1   26.35 ? 109 LEU A C   1 
ATOM   822  O  O   . LEU A 1 109 ? -21.689 -53.54  8.318   1   26.9  ? 109 LEU A O   1 
ATOM   823  C  CB  . LEU A 1 109 ? -24.69  -52.058 8.412   1   25.39 ? 109 LEU A CB  1 
ATOM   824  C  CG  . LEU A 1 109 ? -25.982 -51.973 9.266   1   26.76 ? 109 LEU A CG  1 
ATOM   825  C  CD1 . LEU A 1 109 ? -27.207 -51.799 8.392   1   27.13 ? 109 LEU A CD1 1 
ATOM   826  C  CD2 . LEU A 1 109 ? -26.168 -53.218 10.133  1   27.94 ? 109 LEU A CD2 1 
ATOM   827  N  N   . ALA A 1 110 ? -21.607 -51.403 7.619   1   25.93 ? 110 ALA A N   1 
ATOM   828  C  CA  . ALA A 1 110 ? -20.436 -51.587 6.777   1   26.94 ? 110 ALA A CA  1 
ATOM   829  C  C   . ALA A 1 110 ? -19.21  -51.987 7.618   1   27.79 ? 110 ALA A C   1 
ATOM   830  O  O   . ALA A 1 110 ? -18.398 -52.815 7.193   1   27.17 ? 110 ALA A O   1 
ATOM   831  C  CB  . ALA A 1 110 ? -20.142 -50.296 6.025   1   27.21 ? 110 ALA A CB  1 
ATOM   832  N  N   . ALA A 1 111 ? -19.061 -51.369 8.8     1   28.09 ? 111 ALA A N   1 
ATOM   833  C  CA  . ALA A 1 111 ? -17.929 -51.655 9.671   1   29.55 ? 111 ALA A CA  1 
ATOM   834  C  C   . ALA A 1 111 ? -18.044 -53.049 10.299  1   31.61 ? 111 ALA A C   1 
ATOM   835  O  O   . ALA A 1 111 ? -17.036 -53.736 10.428  1   32.27 ? 111 ALA A O   1 
ATOM   836  C  CB  . ALA A 1 111 ? -17.842 -50.6   10.781  1   29.57 ? 111 ALA A CB  1 
ATOM   837  N  N   . HIS A 1 112 ? -19.244 -53.441 10.745  1   32.09 ? 112 HIS A N   1 
ATOM   838  C  CA  . HIS A 1 112 ? -19.415 -54.713 11.46   1   33.85 ? 112 HIS A CA  1 
ATOM   839  C  C   . HIS A 1 112 ? -19.715 -55.908 10.596  1   34.56 ? 112 HIS A C   1 
ATOM   840  O  O   . HIS A 1 112 ? -19.327 -57.006 10.94   1   34.93 ? 112 HIS A O   1 
ATOM   841  C  CB  . HIS A 1 112 ? -20.532 -54.581 12.508  1   35.3  ? 112 HIS A CB  1 
ATOM   842  C  CG  . HIS A 1 112 ? -20.13  -53.773 13.689  1   38.85 ? 112 HIS A CG  1 
ATOM   843  N  ND1 . HIS A 1 112 ? -19.551 -54.363 14.802  1   41.24 ? 112 HIS A ND1 1 
ATOM   844  C  CD2 . HIS A 1 112 ? -20.223 -52.439 13.894  1   40.09 ? 112 HIS A CD2 1 
ATOM   845  C  CE1 . HIS A 1 112 ? -19.322 -53.373 15.652  1   42.07 ? 112 HIS A CE1 1 
ATOM   846  N  NE2 . HIS A 1 112 ? -19.708 -52.194 15.148  1   41.3  ? 112 HIS A NE2 1 
ATOM   847  N  N   . LEU A 1 113 ? -20.445 -55.718 9.49    1   34.17 ? 113 LEU A N   1 
ATOM   848  C  CA  . LEU A 1 113 ? -20.837 -56.829 8.62    1   33.7  ? 113 LEU A CA  1 
ATOM   849  C  C   . LEU A 1 113 ? -20.364 -56.614 7.169   1   34.3  ? 113 LEU A C   1 
ATOM   850  O  O   . LEU A 1 113 ? -21.19  -56.466 6.26    1   34.05 ? 113 LEU A O   1 
ATOM   851  C  CB  . LEU A 1 113 ? -22.366 -56.976 8.69    1   33.22 ? 113 LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 113 ? -22.951 -57.379 10.057  1   35.01 ? 113 LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 113 ? -24.47  -57.232 10.083  1   35.7  ? 113 LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 113 ? -22.564 -58.813 10.433  1   35.8  ? 113 LEU A CD2 1 
ATOM   855  N  N   . PRO A 1 114 ? -19.036 -56.584 6.919   1   34.89 ? 114 PRO A N   1 
ATOM   856  C  CA  . PRO A 1 114 ? -18.561 -56.317 5.551   1   35.72 ? 114 PRO A CA  1 
ATOM   857  C  C   . PRO A 1 114 ? -19.011 -57.335 4.503   1   36.83 ? 114 PRO A C   1 
ATOM   858  O  O   . PRO A 1 114 ? -19.172 -56.968 3.333   1   37.28 ? 114 PRO A O   1 
ATOM   859  C  CB  . PRO A 1 114 ? -17.036 -56.322 5.7     1   36.4  ? 114 PRO A CB  1 
ATOM   860  C  CG  . PRO A 1 114 ? -16.774 -57.099 6.987   1   36.39 ? 114 PRO A CG  1 
ATOM   861  C  CD  . PRO A 1 114 ? -17.907 -56.723 7.861   1   34.12 ? 114 PRO A CD  1 
ATOM   862  N  N   . ALA A 1 115 ? -19.195 -58.607 4.898   1   36.07 ? 115 ALA A N   1 
ATOM   863  C  CA  . ALA A 1 115 ? -19.654 -59.622 3.947   1   36.03 ? 115 ALA A CA  1 
ATOM   864  C  C   . ALA A 1 115 ? -21.087 -59.333 3.482   1   34.99 ? 115 ALA A C   1 
ATOM   865  O  O   . ALA A 1 115 ? -21.406 -59.558 2.314   1   35.64 ? 115 ALA A O   1 
ATOM   866  C  CB  . ALA A 1 115 ? -19.573 -61.004 4.569   1   36.62 ? 115 ALA A CB  1 
ATOM   867  N  N   . GLU A 1 116 ? -21.932 -58.795 4.365   1   33.17 ? 116 GLU A N   1 
ATOM   868  C  CA  . GLU A 1 116 ? -23.319 -58.491 4.013   1   33.3  ? 116 GLU A CA  1 
ATOM   869  C  C   . GLU A 1 116 ? -23.464 -57.151 3.248   1   31.99 ? 116 GLU A C   1 
ATOM   870  O  O   . GLU A 1 116 ? -24.414 -56.989 2.482   1   32.46 ? 116 GLU A O   1 
ATOM   871  C  CB  . GLU A 1 116 ? -24.183 -58.426 5.291   1   36.43 ? 116 GLU A CB  1 
ATOM   872  C  CG  . GLU A 1 116 ? -24.03  -59.641 6.193   1   42.46 ? 116 GLU A CG  1 
ATOM   873  C  CD  . GLU A 1 116 ? -24.499 -60.939 5.566   1   50.75 ? 116 GLU A CD  1 
ATOM   874  O  OE1 . GLU A 1 116 ? -23.82  -61.972 5.768   1   52.81 ? 116 GLU A OE1 1 
ATOM   875  O  OE2 . GLU A 1 116 ? -25.55  -60.927 4.881   1   53.08 ? 116 GLU A OE2 1 
ATOM   876  N  N   . PHE A 1 117 ? -22.563 -56.184 3.499   1   29.86 ? 117 PHE A N   1 
ATOM   877  C  CA  . PHE A 1 117 ? -22.655 -54.846 2.92    1   27.89 ? 117 PHE A CA  1 
ATOM   878  C  C   . PHE A 1 117 ? -22.2   -54.782 1.468   1   27.14 ? 117 PHE A C   1 
ATOM   879  O  O   . PHE A 1 117 ? -21.245 -54.073 1.145   1   28.03 ? 117 PHE A O   1 
ATOM   880  C  CB  . PHE A 1 117 ? -21.912 -53.819 3.796   1   27.21 ? 117 PHE A CB  1 
ATOM   881  C  CG  . PHE A 1 117 ? -22.389 -52.39  3.643   1   26.54 ? 117 PHE A CG  1 
ATOM   882  C  CD1 . PHE A 1 117 ? -23.626 -51.997 4.129   1   27.05 ? 117 PHE A CD1 1 
ATOM   883  C  CD2 . PHE A 1 117 ? -21.595 -51.438 3.024   1   27.03 ? 117 PHE A CD2 1 
ATOM   884  C  CE1 . PHE A 1 117 ? -24.051 -50.678 4.006   1   26.74 ? 117 PHE A CE1 1 
ATOM   885  C  CE2 . PHE A 1 117 ? -22.041 -50.131 2.868   1   27.05 ? 117 PHE A CE2 1 
ATOM   886  C  CZ  . PHE A 1 117 ? -23.259 -49.759 3.372   1   26.33 ? 117 PHE A CZ  1 
ATOM   887  N  N   . THR A 1 118 ? -22.865 -55.532 0.591   1   25.05 ? 118 THR A N   1 
ATOM   888  C  CA  . THR A 1 118 ? -22.552 -55.473 -0.833  1   25.17 ? 118 THR A CA  1 
ATOM   889  C  C   . THR A 1 118 ? -23.133 -54.172 -1.414  1   24.93 ? 118 THR A C   1 
ATOM   890  O  O   . THR A 1 118 ? -24.049 -53.573 -0.837  1   24.37 ? 118 THR A O   1 
ATOM   891  C  CB  . THR A 1 118 ? -23.167 -56.67  -1.563  1   26.81 ? 118 THR A CB  1 
ATOM   892  O  OG1 . THR A 1 118 ? -24.583 -56.599 -1.456  1   27.93 ? 118 THR A OG1 1 
ATOM   893  C  CG2 . THR A 1 118 ? -22.628 -58.049 -1.062  1   27.2  ? 118 THR A CG2 1 
ATOM   894  N  N   . PRO A 1 119 ? -22.692 -53.759 -2.611  1   25.34 ? 119 PRO A N   1 
ATOM   895  C  CA  . PRO A 1 119 ? -23.307 -52.556 -3.227  1   24.95 ? 119 PRO A CA  1 
ATOM   896  C  C   . PRO A 1 119 ? -24.838 -52.697 -3.372  1   24.41 ? 119 PRO A C   1 
ATOM   897  O  O   . PRO A 1 119 ? -25.552 -51.741 -3.1    1   23.8  ? 119 PRO A O   1 
ATOM   898  C  CB  . PRO A 1 119 ? -22.609 -52.457 -4.579  1   25.96 ? 119 PRO A CB  1 
ATOM   899  C  CG  . PRO A 1 119 ? -21.251 -53.137 -4.35   1   26.38 ? 119 PRO A CG  1 
ATOM   900  C  CD  . PRO A 1 119 ? -21.563 -54.282 -3.411  1   24.9  ? 119 PRO A CD  1 
ATOM   901  N  N   . ALA A 1 120 ? -25.345 -53.884 -3.776  1   24.38 ? 120 ALA A N   1 
ATOM   902  C  CA  . ALA A 1 120 ? -26.805 -54.068 -3.922  1   24.65 ? 120 ALA A CA  1 
ATOM   903  C  C   . ALA A 1 120 ? -27.523 -53.922 -2.577  1   22.46 ? 120 ALA A C   1 
ATOM   904  O  O   . ALA A 1 120 ? -28.591 -53.326 -2.51   1   22.09 ? 120 ALA A O   1 
ATOM   905  C  CB  . ALA A 1 120 ? -27.112 -55.45  -4.513  1   25.89 ? 120 ALA A CB  1 
ATOM   906  N  N   . VAL A 1 121 ? -26.95  -54.487 -1.513  1   21.85 ? 121 VAL A N   1 
ATOM   907  C  CA  . VAL A 1 121 ? -27.56  -54.438 -0.192  1   22.2  ? 121 VAL A CA  1 
ATOM   908  C  C   . VAL A 1 121 ? -27.498 -53.031 0.372   1   21.44 ? 121 VAL A C   1 
ATOM   909  O  O   . VAL A 1 121 ? -28.485 -52.547 0.889   1   20.99 ? 121 VAL A O   1 
ATOM   910  C  CB  . VAL A 1 121 ? -26.986 -55.517 0.739   1   23.21 ? 121 VAL A CB  1 
ATOM   911  C  CG1 . VAL A 1 121 ? -27.355 -55.253 2.196   1   23.83 ? 121 VAL A CG1 1 
ATOM   912  C  CG2 . VAL A 1 121 ? -27.485 -56.906 0.288   1   24.03 ? 121 VAL A CG2 1 
ATOM   913  N  N   . HIS A 1 122 ? -26.391 -52.317 0.15    1   21.03 ? 122 HIS A N   1 
ATOM   914  C  CA  . HIS A 1 122 ? -26.24  -50.92  0.571   1   20.72 ? 122 HIS A CA  1 
ATOM   915  C  C   . HIS A 1 122 ? -27.355 -50.071 -0.074  1   20.86 ? 122 HIS A C   1 
ATOM   916  O  O   . HIS A 1 122 ? -28.031 -49.292 0.62    1   22.07 ? 122 HIS A O   1 
ATOM   917  C  CB  . HIS A 1 122 ? -24.827 -50.449 0.145   1   21.14 ? 122 HIS A CB  1 
ATOM   918  C  CG  . HIS A 1 122 ? -24.492 -49.004 0.4     1   19.85 ? 122 HIS A CG  1 
ATOM   919  N  ND1 . HIS A 1 122 ? -23.235 -48.502 0.093   1   20.47 ? 122 HIS A ND1 1 
ATOM   920  C  CD2 . HIS A 1 122 ? -25.278 -47.985 0.822   1   19.32 ? 122 HIS A CD2 1 
ATOM   921  C  CE1 . HIS A 1 122 ? -23.286 -47.214 0.377   1   20.85 ? 122 HIS A CE1 1 
ATOM   922  N  NE2 . HIS A 1 122 ? -24.498 -46.856 0.825   1   20.07 ? 122 HIS A NE2 1 
ATOM   923  N  N   . ALA A 1 123 ? -27.589 -50.265 -1.39   1   19.57 ? 123 ALA A N   1 
ATOM   924  C  CA  . ALA A 1 123 ? -28.641 -49.56  -2.113  1   18.4  ? 123 ALA A CA  1 
ATOM   925  C  C   . ALA A 1 123 ? -30.035 -49.838 -1.516  1   18.25 ? 123 ALA A C   1 
ATOM   926  O  O   . ALA A 1 123 ? -30.818 -48.904 -1.323  1   18.17 ? 123 ALA A O   1 
ATOM   927  C  CB  . ALA A 1 123 ? -28.605 -49.968 -3.596  1   17.2  ? 123 ALA A CB  1 
ATOM   928  N  N   . SER A 1 124 ? -30.348 -51.113 -1.229  1   18.18 ? 124 SER A N   1 
ATOM   929  C  CA  . SER A 1 124 ? -31.662 -51.507 -0.695  1   19.1  ? 124 SER A CA  1 
ATOM   930  C  C   . SER A 1 124 ? -31.868 -50.966 0.744   1   18.89 ? 124 SER A C   1 
ATOM   931  O  O   . SER A 1 124 ? -32.946 -50.475 1.073   1   18.34 ? 124 SER A O   1 
ATOM   932  C  CB  . SER A 1 124 ? -31.81  -53.036 -0.718  1   18.92 ? 124 SER A CB  1 
ATOM   933  O  OG  . SER A 1 124 ? -31.607 -53.543 -2.032  1   21.31 ? 124 SER A OG  1 
ATOM   934  N  N   . LEU A 1 125 ? -30.8   -50.979 1.573   1   18.43 ? 125 LEU A N   1 
ATOM   935  C  CA  . LEU A 1 125 ? -30.85  -50.437 2.934   1   18.11 ? 125 LEU A CA  1 
ATOM   936  C  C   . LEU A 1 125 ? -31.041 -48.93  2.92    1   18.38 ? 125 LEU A C   1 
ATOM   937  O  O   . LEU A 1 125 ? -31.797 -48.404 3.734   1   17.95 ? 125 LEU A O   1 
ATOM   938  C  CB  . LEU A 1 125 ? -29.539 -50.754 3.628   1   17.81 ? 125 LEU A CB  1 
ATOM   939  C  CG  . LEU A 1 125 ? -29.414 -52.198 4.082   1   19.68 ? 125 LEU A CG  1 
ATOM   940  C  CD1 . LEU A 1 125 ? -28.003 -52.462 4.513   1   20.91 ? 125 LEU A CD1 1 
ATOM   941  C  CD2 . LEU A 1 125 ? -30.393 -52.48  5.226   1   20.51 ? 125 LEU A CD2 1 
ATOM   942  N  N   . ASP A 1 126 ? -30.412 -48.235 1.955   1   18.94 ? 126 ASP A N   1 
ATOM   943  C  CA  . ASP A 1 126 ? -30.565 -46.802 1.847   1   18.45 ? 126 ASP A CA  1 
ATOM   944  C  C   . ASP A 1 126 ? -32.034 -46.428 1.543   1   18.07 ? 126 ASP A C   1 
ATOM   945  O  O   . ASP A 1 126 ? -32.611 -45.57  2.217   1   16.65 ? 126 ASP A O   1 
ATOM   946  C  CB  . ASP A 1 126 ? -29.556 -46.204 0.857   1   21.45 ? 126 ASP A CB  1 
ATOM   947  C  CG  . ASP A 1 126 ? -29.521 -44.673 0.961   1   28.93 ? 126 ASP A CG  1 
ATOM   948  O  OD1 . ASP A 1 126 ? -28.896 -44.158 1.898   1   31.28 ? 126 ASP A OD1 1 
ATOM   949  O  OD2 . ASP A 1 126 ? -30.183 -44.024 0.173   1   30.19 ? 126 ASP A OD2 1 
ATOM   950  N  N   . LYS A 1 127 ? -32.659 -47.112 0.578   1   18.13 ? 127 LYS A N   1 
ATOM   951  C  CA  . LYS A 1 127 ? -34.071 -46.872 0.254   1   18.06 ? 127 LYS A CA  1 
ATOM   952  C  C   . LYS A 1 127 ? -34.998 -47.233 1.4     1   18.43 ? 127 LYS A C   1 
ATOM   953  O  O   . LYS A 1 127 ? -35.934 -46.486 1.689   1   18.35 ? 127 LYS A O   1 
ATOM   954  C  CB  . LYS A 1 127 ? -34.47  -47.708 -0.978  1   18.32 ? 127 LYS A CB  1 
ATOM   955  C  CG  . LYS A 1 127 ? -33.782 -47.248 -2.251  1   17.91 ? 127 LYS A CG  1 
ATOM   956  C  CD  . LYS A 1 127 ? -34.177 -48.174 -3.409  1   21.3  ? 127 LYS A CD  1 
ATOM   957  C  CE  . LYS A 1 127 ? -35.634 -48.014 -3.801  1   22.19 ? 127 LYS A CE  1 
ATOM   958  N  NZ  . LYS A 1 127 ? -35.986 -48.943 -4.943  1   21.87 ? 127 LYS A NZ  1 
ATOM   959  N  N   . PHE A 1 128 ? -34.737 -48.368 2.068   1   18.16 ? 128 PHE A N   1 
ATOM   960  C  CA  . PHE A 1 128 ? -35.533 -48.817 3.215   1   17.7  ? 128 PHE A CA  1 
ATOM   961  C  C   . PHE A 1 128 ? -35.478 -47.754 4.333   1   17.46 ? 128 PHE A C   1 
ATOM   962  O  O   . PHE A 1 128 ? -36.525 -47.389 4.87    1   17.81 ? 128 PHE A O   1 
ATOM   963  C  CB  . PHE A 1 128 ? -34.994 -50.156 3.76    1   17.67 ? 128 PHE A CB  1 
ATOM   964  C  CG  . PHE A 1 128 ? -35.593 -50.554 5.089   1   18.54 ? 128 PHE A CG  1 
ATOM   965  C  CD1 . PHE A 1 128 ? -36.916 -50.961 5.175   1   20.2  ? 128 PHE A CD1 1 
ATOM   966  C  CD2 . PHE A 1 128 ? -34.826 -50.559 6.242   1   20.12 ? 128 PHE A CD2 1 
ATOM   967  C  CE1 . PHE A 1 128 ? -37.477 -51.316 6.394   1   20.78 ? 128 PHE A CE1 1 
ATOM   968  C  CE2 . PHE A 1 128 ? -35.396 -50.885 7.472   1   20.79 ? 128 PHE A CE2 1 
ATOM   969  C  CZ  . PHE A 1 128 ? -36.722 -51.258 7.535   1   20.06 ? 128 PHE A CZ  1 
ATOM   970  N  N   . LEU A 1 129 ? -34.276 -47.281 4.695   1   15.98 ? 129 LEU A N   1 
ATOM   971  C  CA  . LEU A 1 129 ? -34.153 -46.281 5.769   1   16.5  ? 129 LEU A CA  1 
ATOM   972  C  C   . LEU A 1 129 ? -34.797 -44.956 5.34    1   17.38 ? 129 LEU A C   1 
ATOM   973  O  O   . LEU A 1 129 ? -35.407 -44.287 6.166   1   17.37 ? 129 LEU A O   1 
ATOM   974  C  CB  . LEU A 1 129 ? -32.693 -46.1   6.18    1   16.24 ? 129 LEU A CB  1 
ATOM   975  C  CG  . LEU A 1 129 ? -32.081 -47.342 6.854   1   18.16 ? 129 LEU A CG  1 
ATOM   976  C  CD1 . LEU A 1 129 ? -30.56  -47.215 6.968   1   19.54 ? 129 LEU A CD1 1 
ATOM   977  C  CD2 . LEU A 1 129 ? -32.695 -47.595 8.223   1   19.86 ? 129 LEU A CD2 1 
ATOM   978  N  N   . ALA A 1 130 ? -34.756 -44.629 4.022   1   17.23 ? 130 ALA A N   1 
ATOM   979  C  CA  . ALA A 1 130 ? -35.446 -43.433 3.516   1   17.86 ? 130 ALA A CA  1 
ATOM   980  C  C   . ALA A 1 130 ? -36.997 -43.601 3.663   1   17.16 ? 130 ALA A C   1 
ATOM   981  O  O   . ALA A 1 130 ? -37.687 -42.64  4.005   1   16.01 ? 130 ALA A O   1 
ATOM   982  C  CB  . ALA A 1 130 ? -35.061 -43.156 2.054   1   19.42 ? 130 ALA A CB  1 
ATOM   983  N  N   . SER A 1 131 ? -37.539 -44.807 3.402   1   16.72 ? 131 SER A N   1 
ATOM   984  C  CA  . SER A 1 131 ? -38.989 -45.039 3.531   1   17.84 ? 131 SER A CA  1 
ATOM   985  C  C   . SER A 1 131 ? -39.393 -44.995 5.027   1   18.45 ? 131 SER A C   1 
ATOM   986  O  O   . SER A 1 131 ? -40.436 -44.417 5.354   1   20.28 ? 131 SER A O   1 
ATOM   987  C  CB  . SER A 1 131 ? -39.374 -46.409 2.961   1   20.32 ? 131 SER A CB  1 
ATOM   988  O  OG  . SER A 1 131 ? -39.31  -46.365 1.552   1   23.75 ? 131 SER A OG  1 
ATOM   989  N  N   . VAL A 1 132 ? -38.579 -45.566 5.921   1   17.01 ? 132 VAL A N   1 
ATOM   990  C  CA  . VAL A 1 132 ? -38.858 -45.507 7.391   1   16.84 ? 132 VAL A CA  1 
ATOM   991  C  C   . VAL A 1 132 ? -38.85  -44.006 7.825   1   16.92 ? 132 VAL A C   1 
ATOM   992  O  O   . VAL A 1 132 ? -39.767 -43.547 8.499   1   17.53 ? 132 VAL A O   1 
ATOM   993  C  CB  . VAL A 1 132 ? -37.797 -46.28  8.203   1   18.36 ? 132 VAL A CB  1 
ATOM   994  C  CG1 . VAL A 1 132 ? -37.951 -45.99  9.729   1   18.38 ? 132 VAL A CG1 1 
ATOM   995  C  CG2 . VAL A 1 132 ? -37.909 -47.784 7.945   1   18.97 ? 132 VAL A CG2 1 
ATOM   996  N  N   . SER A 1 133 ? -37.868 -43.242 7.333   1   16.06 ? 133 SER A N   1 
ATOM   997  C  CA  . SER A 1 133 ? -37.746 -41.804 7.611   1   16.74 ? 133 SER A CA  1 
ATOM   998  C  C   . SER A 1 133 ? -38.949 -41.011 7.119   1   16.54 ? 133 SER A C   1 
ATOM   999  O  O   . SER A 1 133 ? -39.449 -40.125 7.831   1   15.35 ? 133 SER A O   1 
ATOM   1000 C  CB  . SER A 1 133 ? -36.471 -41.248 6.968   1   18.02 ? 133 SER A CB  1 
ATOM   1001 O  OG  . SER A 1 133 ? -35.332 -41.891 7.527   1   20.5  ? 133 SER A OG  1 
ATOM   1002 N  N   . THR A 1 134 ? -39.462 -41.345 5.925   1   16.31 ? 134 THR A N   1 
ATOM   1003 C  CA  . THR A 1 134 ? -40.656 -40.648 5.415   1   16.4  ? 134 THR A CA  1 
ATOM   1004 C  C   . THR A 1 134 ? -41.857 -40.939 6.319   1   16.97 ? 134 THR A C   1 
ATOM   1005 O  O   . THR A 1 134 ? -42.615 -40.022 6.647   1   18.03 ? 134 THR A O   1 
ATOM   1006 C  CB  . THR A 1 134 ? -40.963 -41.073 3.963   1   17.66 ? 134 THR A CB  1 
ATOM   1007 O  OG1 . THR A 1 134 ? -39.899 -40.552 3.148   1   19.09 ? 134 THR A OG1 1 
ATOM   1008 C  CG2 . THR A 1 134 ? -42.341 -40.497 3.485   1   17.72 ? 134 THR A CG2 1 
ATOM   1009 N  N   . VAL A 1 135 ? -42.017 -42.198 6.765   1   16.32 ? 135 VAL A N   1 
ATOM   1010 C  CA  . VAL A 1 135 ? -43.126 -42.55  7.645   1   16.87 ? 135 VAL A CA  1 
ATOM   1011 C  C   . VAL A 1 135 ? -43.03  -41.767 8.975   1   17.91 ? 135 VAL A C   1 
ATOM   1012 O  O   . VAL A 1 135 ? -44.005 -41.167 9.425   1   18.37 ? 135 VAL A O   1 
ATOM   1013 C  CB  . VAL A 1 135 ? -43.159 -44.092 7.94    1   17.64 ? 135 VAL A CB  1 
ATOM   1014 C  CG1 . VAL A 1 135 ? -44.224 -44.411 8.998   1   18.28 ? 135 VAL A CG1 1 
ATOM   1015 C  CG2 . VAL A 1 135 ? -43.459 -44.878 6.666   1   18.38 ? 135 VAL A CG2 1 
ATOM   1016 N  N   . LEU A 1 136 ? -41.84  -41.741 9.565   1   17.55 ? 136 LEU A N   1 
ATOM   1017 C  CA  . LEU A 1 136 ? -41.666 -41.151 10.903  1   18.82 ? 136 LEU A CA  1 
ATOM   1018 C  C   . LEU A 1 136 ? -41.721 -39.621 10.881  1   19.31 ? 136 LEU A C   1 
ATOM   1019 O  O   . LEU A 1 136 ? -42.014 -39.025 11.906  1   20.18 ? 136 LEU A O   1 
ATOM   1020 C  CB  . LEU A 1 136 ? -40.388 -41.672 11.552  1   19.34 ? 136 LEU A CB  1 
ATOM   1021 C  CG  . LEU A 1 136 ? -40.568 -42.899 12.513  1   22.36 ? 136 LEU A CG  1 
ATOM   1022 C  CD1 . LEU A 1 136 ? -41.211 -44.121 11.802  1   22.19 ? 136 LEU A CD1 1 
ATOM   1023 C  CD2 . LEU A 1 136 ? -39.213 -43.307 13.146  1   23.74 ? 136 LEU A CD2 1 
ATOM   1024 N  N   . THR A 1 137 ? -41.517 -38.994 9.7     1   18.46 ? 137 THR A N   1 
ATOM   1025 C  CA  . THR A 1 137 ? -41.6   -37.549 9.552   1   18.51 ? 137 THR A CA  1 
ATOM   1026 C  C   . THR A 1 137 ? -42.881 -37.056 8.889   1   20    ? 137 THR A C   1 
ATOM   1027 O  O   . THR A 1 137 ? -43.031 -35.838 8.712   1   21.29 ? 137 THR A O   1 
ATOM   1028 C  CB  . THR A 1 137 ? -40.394 -37.035 8.775   1   19.89 ? 137 THR A CB  1 
ATOM   1029 O  OG1 . THR A 1 137 ? -40.35  -37.619 7.461   1   19.41 ? 137 THR A OG1 1 
ATOM   1030 C  CG2 . THR A 1 137 ? -39.097 -37.258 9.542   1   20.66 ? 137 THR A CG2 1 
ATOM   1031 N  N   . SER A 1 138 ? -43.809 -37.956 8.535   1   18.04 ? 138 SER A N   1 
ATOM   1032 C  CA  . SER A 1 138 ? -45.067 -37.526 7.892   1   19.44 ? 138 SER A CA  1 
ATOM   1033 C  C   . SER A 1 138 ? -46.203 -37.518 8.905   1   20.87 ? 138 SER A C   1 
ATOM   1034 O  O   . SER A 1 138 ? -46.195 -38.319 9.859   1   20.62 ? 138 SER A O   1 
ATOM   1035 C  CB  . SER A 1 138 ? -45.447 -38.48  6.752   1   19.66 ? 138 SER A CB  1 
ATOM   1036 O  OG  . SER A 1 138 ? -44.546 -38.488 5.652   1   20.12 ? 138 SER A OG  1 
ATOM   1037 N  N   . LYS A 1 139 ? -47.172 -36.615 8.712   1   20.8  ? 139 LYS A N   1 
ATOM   1038 C  CA  . LYS A 1 139 ? -48.364 -36.5   9.547   1   22.17 ? 139 LYS A CA  1 
ATOM   1039 C  C   . LYS A 1 139 ? -49.495 -37.09  8.724   1   23.57 ? 139 LYS A C   1 
ATOM   1040 O  O   . LYS A 1 139 ? -49.953 -36.455 7.771   1   24.13 ? 139 LYS A O   1 
ATOM   1041 C  CB  . LYS A 1 139 ? -48.631 -35.011 9.898   1   23.31 ? 139 LYS A CB  1 
ATOM   1042 C  CG  . LYS A 1 139 ? -47.532 -34.463 10.83   1   26.5  ? 139 LYS A CG  1 
ATOM   1043 C  CD  . LYS A 1 139 ? -47.574 -32.937 11.074  1   29.77 ? 139 LYS A CD  1 
ATOM   1044 C  CE  . LYS A 1 139 ? -48.334 -32.528 12.281  1   32.56 ? 139 LYS A CE  1 
ATOM   1045 N  NZ  . LYS A 1 139 ? -48.167 -31.073 12.601  1   32.06 ? 139 LYS A NZ  1 
ATOM   1046 N  N   . TYR A 1 140 ? -49.812 -38.364 8.953   1   22.94 ? 140 TYR A N   1 
ATOM   1047 C  CA  . TYR A 1 140 ? -50.85  -39.047 8.171   1   23.47 ? 140 TYR A CA  1 
ATOM   1048 C  C   . TYR A 1 140 ? -52.065 -39.501 8.988   1   26.08 ? 140 TYR A C   1 
ATOM   1049 O  O   . TYR A 1 140 ? -52.911 -40.252 8.473   1   26.73 ? 140 TYR A O   1 
ATOM   1050 C  CB  . TYR A 1 140 ? -50.256 -40.218 7.385   1   22.67 ? 140 TYR A CB  1 
ATOM   1051 C  CG  . TYR A 1 140 ? -49.478 -41.192 8.249   1   21.04 ? 140 TYR A CG  1 
ATOM   1052 C  CD1 . TYR A 1 140 ? -48.111 -41.041 8.441   1   20.5  ? 140 TYR A CD1 1 
ATOM   1053 C  CD2 . TYR A 1 140 ? -50.078 -42.339 8.753   1   21.17 ? 140 TYR A CD2 1 
ATOM   1054 C  CE1 . TYR A 1 140 ? -47.378 -41.96  9.181   1   20.17 ? 140 TYR A CE1 1 
ATOM   1055 C  CE2 . TYR A 1 140 ? -49.354 -43.269 9.496   1   20.9  ? 140 TYR A CE2 1 
ATOM   1056 C  CZ  . TYR A 1 140 ? -47.994 -43.1   9.665   1   20.56 ? 140 TYR A CZ  1 
ATOM   1057 O  OH  . TYR A 1 140 ? -47.282 -44.007 10.422  1   20.82 ? 140 TYR A OH  1 
ATOM   1058 N  N   . ARG A 1 141 ? -52.158 -39.044 10.253  1   27.5  ? 141 ARG A N   1 
ATOM   1059 C  CA  . ARG A 1 141 ? -53.299 -39.302 11.126  1   30.19 ? 141 ARG A CA  1 
ATOM   1060 C  C   . ARG A 1 141 ? -54.532 -38.531 10.614  1   33.81 ? 141 ARG A C   1 
ATOM   1061 O  O   . ARG A 1 141 ? -54.373 -37.517 9.869   1   35.57 ? 141 ARG A O   1 
ATOM   1062 C  CB  . ARG A 1 141 ? -52.986 -38.82  12.545  1   30.42 ? 141 ARG A CB  1 
ATOM   1063 C  CG  . ARG A 1 141 ? -51.746 -39.442 13.088  1   31.07 ? 141 ARG A CG  1 
ATOM   1064 C  CD  . ARG A 1 141 ? -51.342 -38.91  14.464  1   31.79 ? 141 ARG A CD  1 
ATOM   1065 N  NE  . ARG A 1 141 ? -52.108 -39.468 15.584  1   29.25 ? 141 ARG A NE  1 
ATOM   1066 C  CZ  . ARG A 1 141 ? -51.983 -40.713 16.037  1   28.98 ? 141 ARG A CZ  1 
ATOM   1067 N  NH1 . ARG A 1 141 ? -51.199 -41.58  15.406  1   28.42 ? 141 ARG A NH1 1 
ATOM   1068 N  NH2 . ARG A 1 141 ? -52.691 -41.12  17.091  1   28.29 ? 141 ARG A NH2 1 
ATOM   1069 O  OXT . ARG A 1 141 ? -55.657 -38.942 10.955  1   36.18 ? 141 ARG A OXT 1 
ATOM   1070 N  N   . VAL B 2 1   ? -25.963 -12.519 -6.011  1   49.12 ? 1   VAL B N   1 
ATOM   1071 C  CA  . VAL B 2 1   ? -26.922 -12.841 -7.065  1   49.72 ? 1   VAL B CA  1 
ATOM   1072 C  C   . VAL B 2 1   ? -26.7   -11.926 -8.267  1   49.89 ? 1   VAL B C   1 
ATOM   1073 O  O   . VAL B 2 1   ? -26.497 -10.724 -8.091  1   50.03 ? 1   VAL B O   1 
ATOM   1074 C  CB  . VAL B 2 1   ? -28.382 -12.751 -6.556  1   50.49 ? 1   VAL B CB  1 
ATOM   1075 N  N   . HIS B 2 2   ? -26.73  -12.495 -9.485  1   49.32 ? 2   HIS B N   1 
ATOM   1076 C  CA  . HIS B 2 2   ? -26.555 -11.724 -10.714 1   49.07 ? 2   HIS B CA  1 
ATOM   1077 C  C   . HIS B 2 2   ? -27.86  -11.624 -11.482 1   47.59 ? 2   HIS B C   1 
ATOM   1078 O  O   . HIS B 2 2   ? -28.258 -12.552 -12.194 1   48.18 ? 2   HIS B O   1 
ATOM   1079 C  CB  . HIS B 2 2   ? -25.476 -12.346 -11.616 1   50.75 ? 2   HIS B CB  1 
ATOM   1080 N  N   . LEU B 2 3   ? -28.501 -10.48  -11.376 1   45.55 ? 3   LEU B N   1 
ATOM   1081 C  CA  . LEU B 2 3   ? -29.75  -10.221 -12.087 1   43.55 ? 3   LEU B CA  1 
ATOM   1082 C  C   . LEU B 2 3   ? -29.46  -9.2    -13.169 1   41.63 ? 3   LEU B C   1 
ATOM   1083 O  O   . LEU B 2 3   ? -28.712 -8.266  -12.916 1   42.48 ? 3   LEU B O   1 
ATOM   1084 C  CB  . LEU B 2 3   ? -30.776 -9.611  -11.115 1   43.26 ? 3   LEU B CB  1 
ATOM   1085 C  CG  . LEU B 2 3   ? -31.649 -10.577 -10.35  1   43.95 ? 3   LEU B CG  1 
ATOM   1086 C  CD1 . LEU B 2 3   ? -30.846 -11.336 -9.332  1   44.6  ? 3   LEU B CD1 1 
ATOM   1087 C  CD2 . LEU B 2 3   ? -32.762 -9.83   -9.654  1   45.01 ? 3   LEU B CD2 1 
ATOM   1088 N  N   . THR B 2 4   ? -30.079 -9.327  -14.34  1   39.81 ? 4   THR B N   1 
ATOM   1089 C  CA  . THR B 2 4   ? -29.94  -8.321  -15.392 1   39.42 ? 4   THR B CA  1 
ATOM   1090 C  C   . THR B 2 4   ? -30.718 -7.051  -14.948 1   38.81 ? 4   THR B C   1 
ATOM   1091 O  O   . THR B 2 4   ? -31.621 -7.149  -14.108 1   38.26 ? 4   THR B O   1 
ATOM   1092 C  CB  . THR B 2 4   ? -30.56  -8.847  -16.703 1   40.37 ? 4   THR B CB  1 
ATOM   1093 O  OG1 . THR B 2 4   ? -31.976 -8.987  -16.528 1   40.09 ? 4   THR B OG1 1 
ATOM   1094 C  CG2 . THR B 2 4   ? -29.934 -10.167 -17.172 1   41.32 ? 4   THR B CG2 1 
ATOM   1095 N  N   . PRO B 2 5   ? -30.472 -5.869  -15.55  1   39.12 ? 5   PRO B N   1 
ATOM   1096 C  CA  . PRO B 2 5   ? -31.26  -4.687  -15.166 1   38.56 ? 5   PRO B CA  1 
ATOM   1097 C  C   . PRO B 2 5   ? -32.768 -4.922  -15.341 1   37.22 ? 5   PRO B C   1 
ATOM   1098 O  O   . PRO B 2 5   ? -33.533 -4.527  -14.478 1   36.83 ? 5   PRO B O   1 
ATOM   1099 C  CB  . PRO B 2 5   ? -30.714 -3.594  -16.077 1   39.98 ? 5   PRO B CB  1 
ATOM   1100 C  CG  . PRO B 2 5   ? -29.348 -4.048  -16.409 1   40.47 ? 5   PRO B CG  1 
ATOM   1101 C  CD  . PRO B 2 5   ? -29.439 -5.519  -16.54  1   38.73 ? 5   PRO B CD  1 
ATOM   1102 N  N   . GLU B 2 6   ? -33.188 -5.665  -16.396 1   36.47 ? 6   GLU B N   1 
ATOM   1103 C  CA  . GLU B 2 6   ? -34.61  -5.953  -16.586 1   35.82 ? 6   GLU B CA  1 
ATOM   1104 C  C   . GLU B 2 6   ? -35.183 -6.843  -15.515 1   34.65 ? 6   GLU B C   1 
ATOM   1105 O  O   . GLU B 2 6   ? -36.324 -6.627  -15.094 1   35.56 ? 6   GLU B O   1 
ATOM   1106 C  CB  . GLU B 2 6   ? -34.899 -6.505  -17.978 1   38.17 ? 6   GLU B CB  1 
ATOM   1107 C  CG  . GLU B 2 6   ? -34.748 -5.419  -19.019 1   41.35 ? 6   GLU B CG  1 
ATOM   1108 C  CD  . GLU B 2 6   ? -35.035 -5.914  -20.413 1   50.45 ? 6   GLU B CD  1 
ATOM   1109 O  OE1 . GLU B 2 6   ? -35.903 -6.806  -20.552 1   53.25 ? 6   GLU B OE1 1 
ATOM   1110 O  OE2 . GLU B 2 6   ? -34.41  -5.403  -21.369 1   54.04 ? 6   GLU B OE2 1 
ATOM   1111 N  N   . GLU B 2 7   ? -34.411 -7.825  -15.047 1   32.63 ? 7   GLU B N   1 
ATOM   1112 C  CA  . GLU B 2 7   ? -34.863 -8.681  -13.967 1   31.91 ? 7   GLU B CA  1 
ATOM   1113 C  C   . GLU B 2 7   ? -34.925 -7.884  -12.663 1   31.48 ? 7   GLU B C   1 
ATOM   1114 O  O   . GLU B 2 7   ? -35.854 -8.064  -11.896 1   30.89 ? 7   GLU B O   1 
ATOM   1115 C  CB  . GLU B 2 7   ? -33.917 -9.869  -13.801 1   33.12 ? 7   GLU B CB  1 
ATOM   1116 C  CG  . GLU B 2 7   ? -34.115 -10.906 -14.884 1   37.16 ? 7   GLU B CG  1 
ATOM   1117 C  CD  . GLU B 2 7   ? -33.134 -12.052 -14.752 1   43.08 ? 7   GLU B CD  1 
ATOM   1118 O  OE1 . GLU B 2 7   ? -31.943 -11.781 -14.47  1   40.17 ? 7   GLU B OE1 1 
ATOM   1119 O  OE2 . GLU B 2 7   ? -33.564 -13.218 -14.916 1   47.35 ? 7   GLU B OE2 1 
ATOM   1120 N  N   . LYS B 2 8   ? -33.943 -7.009  -12.412 1   32.07 ? 8   LYS B N   1 
ATOM   1121 C  CA  . LYS B 2 8   ? -33.939 -6.193  -11.178 1   33.4  ? 8   LYS B CA  1 
ATOM   1122 C  C   . LYS B 2 8   ? -35.155 -5.232  -11.189 1   34.07 ? 8   LYS B C   1 
ATOM   1123 O  O   . LYS B 2 8   ? -35.841 -5.057  -10.185 1   34.36 ? 8   LYS B O   1 
ATOM   1124 C  CB  . LYS B 2 8   ? -32.632 -5.394  -11.048 1   36.25 ? 8   LYS B CB  1 
ATOM   1125 C  CG  . LYS B 2 8   ? -32.423 -4.926  -9.616  1   44.68 ? 8   LYS B CG  1 
ATOM   1126 C  CD  . LYS B 2 8   ? -31.32  -3.89   -9.475  1   51.73 ? 8   LYS B CD  1 
ATOM   1127 C  CE  . LYS B 2 8   ? -31.353 -3.274  -8.1    1   56.8  ? 8   LYS B CE  1 
ATOM   1128 N  NZ  . LYS B 2 8   ? -31.602 -4.308  -7.048  1   60.53 ? 8   LYS B NZ  1 
ATOM   1129 N  N   . SER B 2 9   ? -35.469 -4.724  -12.366 1   33.82 ? 9   SER B N   1 
ATOM   1130 C  CA  . SER B 2 9   ? -36.596 -3.865  -12.617 1   34.54 ? 9   SER B CA  1 
ATOM   1131 C  C   . SER B 2 9   ? -37.91  -4.584  -12.273 1   34.05 ? 9   SER B C   1 
ATOM   1132 O  O   . SER B 2 9   ? -38.718 -4.032  -11.538 1   34.52 ? 9   SER B O   1 
ATOM   1133 C  CB  . SER B 2 9   ? -36.592 -3.506  -14.094 1   36.25 ? 9   SER B CB  1 
ATOM   1134 O  OG  . SER B 2 9   ? -37.286 -2.297  -14.257 1   39.4  ? 9   SER B OG  1 
ATOM   1135 N  N   . ALA B 2 10  ? -38.096 -5.819  -12.766 1   33.58 ? 10  ALA B N   1 
ATOM   1136 C  CA  . ALA B 2 10  ? -39.296 -6.611  -12.533 1   34.42 ? 10  ALA B CA  1 
ATOM   1137 C  C   . ALA B 2 10  ? -39.453 -6.947  -11.057 1   34.46 ? 10  ALA B C   1 
ATOM   1138 O  O   . ALA B 2 10  ? -40.563 -6.897  -10.532 1   35.42 ? 10  ALA B O   1 
ATOM   1139 C  CB  . ALA B 2 10  ? -39.25  -7.894  -13.353 1   34.89 ? 10  ALA B CB  1 
ATOM   1140 N  N   . VAL B 2 11  ? -38.341 -7.275  -10.389 1   32.98 ? 11  VAL B N   1 
ATOM   1141 C  CA  . VAL B 2 11  ? -38.359 -7.579  -8.97   1   32.24 ? 11  VAL B CA  1 
ATOM   1142 C  C   . VAL B 2 11  ? -38.768 -6.351  -8.166  1   32.92 ? 11  VAL B C   1 
ATOM   1143 O  O   . VAL B 2 11  ? -39.638 -6.457  -7.302  1   33.39 ? 11  VAL B O   1 
ATOM   1144 C  CB  . VAL B 2 11  ? -36.989 -8.169  -8.513  1   32.21 ? 11  VAL B CB  1 
ATOM   1145 C  CG1 . VAL B 2 11  ? -36.823 -8.106  -6.996  1   32.58 ? 11  VAL B CG1 1 
ATOM   1146 C  CG2 . VAL B 2 11  ? -36.83  -9.611  -9.009  1   31.13 ? 11  VAL B CG2 1 
ATOM   1147 N  N   . THR B 2 12  ? -38.143 -5.199  -8.44   1   32.85 ? 12  THR B N   1 
ATOM   1148 C  CA  . THR B 2 12  ? -38.391 -3.949  -7.712  1   33.68 ? 12  THR B CA  1 
ATOM   1149 C  C   . THR B 2 12  ? -39.825 -3.461  -7.903  1   34.22 ? 12  THR B C   1 
ATOM   1150 O  O   . THR B 2 12  ? -40.421 -2.906  -6.971  1   34.08 ? 12  THR B O   1 
ATOM   1151 C  CB  . THR B 2 12  ? -37.419 -2.862  -8.216  1   36.38 ? 12  THR B CB  1 
ATOM   1152 O  OG1 . THR B 2 12  ? -36.073 -3.315  -8.082  1   37.82 ? 12  THR B OG1 1 
ATOM   1153 C  CG2 . THR B 2 12  ? -37.602 -1.521  -7.493  1   37.08 ? 12  THR B CG2 1 
ATOM   1154 N  N   . ALA B 2 13  ? -40.35  -3.579  -9.135  1   33.9  ? 13  ALA B N   1 
ATOM   1155 C  CA  . ALA B 2 13  ? -41.711 -3.135  -9.427  1   34.31 ? 13  ALA B CA  1 
ATOM   1156 C  C   . ALA B 2 13  ? -42.749 -3.973  -8.67   1   34.5  ? 13  ALA B C   1 
ATOM   1157 O  O   . ALA B 2 13  ? -43.653 -3.397  -8.063  1   35.3  ? 13  ALA B O   1 
ATOM   1158 C  CB  . ALA B 2 13  ? -41.984 -3.183  -10.922 1   34.38 ? 13  ALA B CB  1 
ATOM   1159 N  N   . LEU B 2 14  ? -42.602 -5.307  -8.656  1   33.47 ? 14  LEU B N   1 
ATOM   1160 C  CA  . LEU B 2 14  ? -43.55  -6.149  -7.947  1   34.16 ? 14  LEU B CA  1 
ATOM   1161 C  C   . LEU B 2 14  ? -43.398 -5.926  -6.422  1   33.65 ? 14  LEU B C   1 
ATOM   1162 O  O   . LEU B 2 14  ? -44.406 -5.794  -5.727  1   32.94 ? 14  LEU B O   1 
ATOM   1163 C  CB  . LEU B 2 14  ? -43.341 -7.638  -8.281  1   35.95 ? 14  LEU B CB  1 
ATOM   1164 C  CG  . LEU B 2 14  ? -44.466 -8.574  -7.824  1   39.63 ? 14  LEU B CG  1 
ATOM   1165 C  CD1 . LEU B 2 14  ? -45.406 -8.88   -8.954  1   41.42 ? 14  LEU B CD1 1 
ATOM   1166 C  CD2 . LEU B 2 14  ? -43.927 -9.897  -7.33   1   41.27 ? 14  LEU B CD2 1 
ATOM   1167 N  N   . TRP B 2 15  ? -42.155 -5.864  -5.917  1   33.88 ? 15  TRP B N   1 
ATOM   1168 C  CA  . TRP B 2 15  ? -41.918 -5.653  -4.464  1   35.02 ? 15  TRP B CA  1 
ATOM   1169 C  C   . TRP B 2 15  ? -42.577 -4.401  -3.899  1   36.88 ? 15  TRP B C   1 
ATOM   1170 O  O   . TRP B 2 15  ? -42.917 -4.351  -2.706  1   37.03 ? 15  TRP B O   1 
ATOM   1171 C  CB  . TRP B 2 15  ? -40.42  -5.626  -4.13   1   34.55 ? 15  TRP B CB  1 
ATOM   1172 C  CG  . TRP B 2 15  ? -40.136 -5.908  -2.683  1   34.86 ? 15  TRP B CG  1 
ATOM   1173 C  CD1 . TRP B 2 15  ? -39.737 -5.018  -1.734  1   36.09 ? 15  TRP B CD1 1 
ATOM   1174 C  CD2 . TRP B 2 15  ? -40.27  -7.174  -2.02   1   34.6  ? 15  TRP B CD2 1 
ATOM   1175 N  NE1 . TRP B 2 15  ? -39.566 -5.661  -0.526  1   36.23 ? 15  TRP B NE1 1 
ATOM   1176 C  CE2 . TRP B 2 15  ? -39.885 -6.987  -0.677  1   35.4  ? 15  TRP B CE2 1 
ATOM   1177 C  CE3 . TRP B 2 15  ? -40.622 -8.461  -2.444  1   34.62 ? 15  TRP B CE3 1 
ATOM   1178 C  CZ2 . TRP B 2 15  ? -39.846 -8.037  0.238   1   35.99 ? 15  TRP B CZ2 1 
ATOM   1179 C  CZ3 . TRP B 2 15  ? -40.59  -9.499  -1.533  1   35.63 ? 15  TRP B CZ3 1 
ATOM   1180 C  CH2 . TRP B 2 15  ? -40.207 -9.285  -0.211  1   35.53 ? 15  TRP B CH2 1 
ATOM   1181 N  N   . GLY B 2 16  ? -42.717 -3.385  -4.739  1   37.69 ? 16  GLY B N   1 
ATOM   1182 C  CA  . GLY B 2 16  ? -43.346 -2.124  -4.356  1   38.37 ? 16  GLY B CA  1 
ATOM   1183 C  C   . GLY B 2 16  ? -44.832 -2.252  -4.083  1   39.45 ? 16  GLY B C   1 
ATOM   1184 O  O   . GLY B 2 16  ? -45.4   -1.448  -3.34   1   41.3  ? 16  GLY B O   1 
ATOM   1185 N  N   . LYS B 2 17  ? -45.482 -3.273  -4.652  1   38.37 ? 17  LYS B N   1 
ATOM   1186 C  CA  . LYS B 2 17  ? -46.915 -3.487  -4.442  1   38.62 ? 17  LYS B CA  1 
ATOM   1187 C  C   . LYS B 2 17  ? -47.224 -4.518  -3.345  1   38.52 ? 17  LYS B C   1 
ATOM   1188 O  O   . LYS B 2 17  ? -48.397 -4.786  -3.099  1   38.42 ? 17  LYS B O   1 
ATOM   1189 C  CB  . LYS B 2 17  ? -47.562 -3.961  -5.744  1   40.61 ? 17  LYS B CB  1 
ATOM   1190 C  CG  . LYS B 2 17  ? -47.433 -2.961  -6.856  1   44.26 ? 17  LYS B CG  1 
ATOM   1191 C  CD  . LYS B 2 17  ? -48.08  -3.513  -8.103  1   49.98 ? 17  LYS B CD  1 
ATOM   1192 C  CE  . LYS B 2 17  ? -48.26  -2.427  -9.136  1   53.7  ? 17  LYS B CE  1 
ATOM   1193 N  NZ  . LYS B 2 17  ? -47.662 -2.868  -10.42  1   58.47 ? 17  LYS B NZ  1 
ATOM   1194 N  N   . VAL B 2 18  ? -46.199 -5.133  -2.75   1   37.98 ? 18  VAL B N   1 
ATOM   1195 C  CA  . VAL B 2 18  ? -46.368 -6.139  -1.71   1   38.78 ? 18  VAL B CA  1 
ATOM   1196 C  C   . VAL B 2 18  ? -46.981 -5.523  -0.468  1   41.27 ? 18  VAL B C   1 
ATOM   1197 O  O   . VAL B 2 18  ? -46.523 -4.479  0.004   1   41.93 ? 18  VAL B O   1 
ATOM   1198 C  CB  . VAL B 2 18  ? -45.019 -6.836  -1.399  1   38.09 ? 18  VAL B CB  1 
ATOM   1199 C  CG1 . VAL B 2 18  ? -45.06  -7.608  -0.073  1   38.16 ? 18  VAL B CG1 1 
ATOM   1200 C  CG2 . VAL B 2 18  ? -44.609 -7.755  -2.549  1   38.08 ? 18  VAL B CG2 1 
ATOM   1201 N  N   . ASN B 2 19  ? -48.02  -6.173  0.067   1   42.45 ? 19  ASN B N   1 
ATOM   1202 C  CA  . ASN B 2 19  ? -48.61  -5.736  1.325   1   43.17 ? 19  ASN B CA  1 
ATOM   1203 C  C   . ASN B 2 19  ? -47.651 -6.257  2.416   1   43.46 ? 19  ASN B C   1 
ATOM   1204 O  O   . ASN B 2 19  ? -47.624 -7.458  2.72    1   42.38 ? 19  ASN B O   1 
ATOM   1205 C  CB  . ASN B 2 19  ? -50.009 -6.328  1.486   1   44.78 ? 19  ASN B CB  1 
ATOM   1206 C  CG  . ASN B 2 19  ? -50.697 -5.92   2.765   1   48.84 ? 19  ASN B CG  1 
ATOM   1207 O  OD1 . ASN B 2 19  ? -50.097 -5.851  3.836   1   49.33 ? 19  ASN B OD1 1 
ATOM   1208 N  ND2 . ASN B 2 19  ? -51.982 -5.629  2.68    1   50.75 ? 19  ASN B ND2 1 
ATOM   1209 N  N   . VAL B 2 20  ? -46.844 -5.352  2.971   1   44.01 ? 20  VAL B N   1 
ATOM   1210 C  CA  . VAL B 2 20  ? -45.853 -5.669  4.004   1   45.17 ? 20  VAL B CA  1 
ATOM   1211 C  C   . VAL B 2 20  ? -46.463 -6.132  5.344   1   45.13 ? 20  VAL B C   1 
ATOM   1212 O  O   . VAL B 2 20  ? -45.755 -6.715  6.17    1   44.4  ? 20  VAL B O   1 
ATOM   1213 C  CB  . VAL B 2 20  ? -44.876 -4.496  4.222   1   46.93 ? 20  VAL B CB  1 
ATOM   1214 C  CG1 . VAL B 2 20  ? -44.252 -4.061  2.899   1   48.27 ? 20  VAL B CG1 1 
ATOM   1215 C  CG2 . VAL B 2 20  ? -45.58  -3.325  4.899   1   47.42 ? 20  VAL B CG2 1 
ATOM   1216 N  N   . ASP B 2 21  ? -47.766 -5.907  5.548   1   45.51 ? 21  ASP B N   1 
ATOM   1217 C  CA  . ASP B 2 21  ? -48.427 -6.37   6.773   1   45.84 ? 21  ASP B CA  1 
ATOM   1218 C  C   . ASP B 2 21  ? -48.892 -7.83   6.67    1   44.33 ? 21  ASP B C   1 
ATOM   1219 O  O   . ASP B 2 21  ? -49.174 -8.43   7.706   1   45.53 ? 21  ASP B O   1 
ATOM   1220 C  CB  . ASP B 2 21  ? -49.639 -5.496  7.079   1   49.13 ? 21  ASP B CB  1 
ATOM   1221 C  CG  . ASP B 2 21  ? -49.295 -4.067  7.441   1   56.13 ? 21  ASP B CG  1 
ATOM   1222 O  OD1 . ASP B 2 21  ? -48.151 -3.829  7.903   1   57.47 ? 21  ASP B OD1 1 
ATOM   1223 O  OD2 . ASP B 2 21  ? -50.174 -3.192  7.289   1   58.91 ? 21  ASP B OD2 1 
ATOM   1224 N  N   . GLU B 2 22  ? -49.037 -8.385  5.456   1   41.23 ? 22  GLU B N   1 
ATOM   1225 C  CA  . GLU B 2 22  ? -49.59  -9.734  5.318   1   39.45 ? 22  GLU B CA  1 
ATOM   1226 C  C   . GLU B 2 22  ? -48.688 -10.771 4.676   1   36.19 ? 22  GLU B C   1 
ATOM   1227 O  O   . GLU B 2 22  ? -48.677 -11.917 5.13    1   36.78 ? 22  GLU B O   1 
ATOM   1228 C  CB  . GLU B 2 22  ? -50.93  -9.698  4.546   1   42.5  ? 22  GLU B CB  1 
ATOM   1229 C  CG  . GLU B 2 22  ? -51.915 -8.63   5.025   1   50.64 ? 22  GLU B CG  1 
ATOM   1230 C  CD  . GLU B 2 22  ? -52.835 -8.977  6.184   1   60.95 ? 22  GLU B CD  1 
ATOM   1231 O  OE1 . GLU B 2 22  ? -53.878 -8.296  6.331   1   64.17 ? 22  GLU B OE1 1 
ATOM   1232 O  OE2 . GLU B 2 22  ? -52.517 -9.918  6.948   1   63.14 ? 22  GLU B OE2 1 
ATOM   1233 N  N   . VAL B 2 23  ? -48.015 -10.422 3.572   1   33.24 ? 23  VAL B N   1 
ATOM   1234 C  CA  . VAL B 2 23  ? -47.223 -11.382 2.802   1   31.61 ? 23  VAL B CA  1 
ATOM   1235 C  C   . VAL B 2 23  ? -46.205 -12.17  3.653   1   29.92 ? 23  VAL B C   1 
ATOM   1236 O  O   . VAL B 2 23  ? -46.082 -13.384 3.457   1   29.31 ? 23  VAL B O   1 
ATOM   1237 C  CB  . VAL B 2 23  ? -46.58  -10.727 1.567   1   31.75 ? 23  VAL B CB  1 
ATOM   1238 C  CG1 . VAL B 2 23  ? -45.535 -11.637 0.917   1   31.67 ? 23  VAL B CG1 1 
ATOM   1239 C  CG2 . VAL B 2 23  ? -47.665 -10.361 0.565   1   32.91 ? 23  VAL B CG2 1 
ATOM   1240 N  N   . GLY B 2 24  ? -45.52  -11.495 4.576   1   29.36 ? 24  GLY B N   1 
ATOM   1241 C  CA  . GLY B 2 24  ? -44.532 -12.144 5.433   1   29.23 ? 24  GLY B CA  1 
ATOM   1242 C  C   . GLY B 2 24  ? -45.174 -13.16  6.352   1   29.76 ? 24  GLY B C   1 
ATOM   1243 O  O   . GLY B 2 24  ? -44.707 -14.298 6.451   1   29.6  ? 24  GLY B O   1 
ATOM   1244 N  N   . GLY B 2 25  ? -46.284 -12.761 6.981   1   29.36 ? 25  GLY B N   1 
ATOM   1245 C  CA  . GLY B 2 25  ? -47.038 -13.648 7.857   1   29.1  ? 25  GLY B CA  1 
ATOM   1246 C  C   . GLY B 2 25  ? -47.568 -14.853 7.107   1   28.57 ? 25  GLY B C   1 
ATOM   1247 O  O   . GLY B 2 25  ? -47.541 -15.961 7.631   1   29.14 ? 25  GLY B O   1 
ATOM   1248 N  N   . GLU B 2 26  ? -48.004 -14.656 5.853   1   27.78 ? 26  GLU B N   1 
ATOM   1249 C  CA  . GLU B 2 26  ? -48.511 -15.757 5.021   1   27.01 ? 26  GLU B CA  1 
ATOM   1250 C  C   . GLU B 2 26  ? -47.404 -16.695 4.63    1   25.23 ? 26  GLU B C   1 
ATOM   1251 O  O   . GLU B 2 26  ? -47.614 -17.902 4.672   1   25.23 ? 26  GLU B O   1 
ATOM   1252 C  CB  . GLU B 2 26  ? -49.273 -15.236 3.769   1   30.01 ? 26  GLU B CB  1 
ATOM   1253 C  CG  . GLU B 2 26  ? -50.699 -14.837 4.12    1   37.67 ? 26  GLU B CG  1 
ATOM   1254 C  CD  . GLU B 2 26  ? -51.393 -14.048 3.03    1   44.41 ? 26  GLU B CD  1 
ATOM   1255 O  OE1 . GLU B 2 26  ? -51.183 -14.376 1.84    1   44.79 ? 26  GLU B OE1 1 
ATOM   1256 O  OE2 . GLU B 2 26  ? -52.141 -13.1   3.366   1   46.16 ? 26  GLU B OE2 1 
ATOM   1257 N  N   . ALA B 2 27  ? -46.205 -16.169 4.293   1   24.26 ? 27  ALA B N   1 
ATOM   1258 C  CA  . ALA B 2 27  ? -45.089 -17.048 3.937   1   24.47 ? 27  ALA B CA  1 
ATOM   1259 C  C   . ALA B 2 27  ? -44.629 -17.876 5.14    1   24.21 ? 27  ALA B C   1 
ATOM   1260 O  O   . ALA B 2 27  ? -44.441 -19.098 5.022   1   24.14 ? 27  ALA B O   1 
ATOM   1261 C  CB  . ALA B 2 27  ? -43.93  -16.255 3.31    1   24.57 ? 27  ALA B CB  1 
ATOM   1262 N  N   . LEU B 2 28  ? -44.451 -17.242 6.272   1   24.05 ? 28  LEU B N   1 
ATOM   1263 C  CA  . LEU B 2 28  ? -44.044 -17.97  7.497   1   24.67 ? 28  LEU B CA  1 
ATOM   1264 C  C   . LEU B 2 28  ? -45.125 -18.988 7.914   1   22.87 ? 28  LEU B C   1 
ATOM   1265 O  O   . LEU B 2 28  ? -44.819 -20.136 8.204   1   22.36 ? 28  LEU B O   1 
ATOM   1266 C  CB  . LEU B 2 28  ? -43.766 -16.997 8.656   1   25.36 ? 28  LEU B CB  1 
ATOM   1267 C  CG  . LEU B 2 28  ? -43.279 -17.683 9.951   1   27.73 ? 28  LEU B CG  1 
ATOM   1268 C  CD1 . LEU B 2 28  ? -41.934 -18.393 9.718   1   27.95 ? 28  LEU B CD1 1 
ATOM   1269 C  CD2 . LEU B 2 28  ? -43.182 -16.677 11.136  1   29.27 ? 28  LEU B CD2 1 
ATOM   1270 N  N   . GLY B 2 29  ? -46.384 -18.574 7.894   1   22.86 ? 29  GLY B N   1 
ATOM   1271 C  CA  . GLY B 2 29  ? -47.502 -19.452 8.252   1   22.79 ? 29  GLY B CA  1 
ATOM   1272 C  C   . GLY B 2 29  ? -47.565 -20.671 7.34    1   22.63 ? 29  GLY B C   1 
ATOM   1273 O  O   . GLY B 2 29  ? -47.65  -21.808 7.812   1   22.23 ? 29  GLY B O   1 
ATOM   1274 N  N   . ARG B 2 30  ? -47.415 -20.445 6.024   1   22.11 ? 30  ARG B N   1 
ATOM   1275 C  CA  . ARG B 2 30  ? -47.417 -21.545 5.064   1   21.11 ? 30  ARG B CA  1 
ATOM   1276 C  C   . ARG B 2 30  ? -46.202 -22.414 5.243   1   20.07 ? 30  ARG B C   1 
ATOM   1277 O  O   . ARG B 2 30  ? -46.331 -23.626 5.143   1   20.07 ? 30  ARG B O   1 
ATOM   1278 C  CB  . ARG B 2 30  ? -47.552 -21.046 3.614   1   21.75 ? 30  ARG B CB  1 
ATOM   1279 C  CG  . ARG B 2 30  ? -49     -20.629 3.252   1   22.55 ? 30  ARG B CG  1 
ATOM   1280 C  CD  . ARG B 2 30  ? -49.066 -20.078 1.816   1   24.3  ? 30  ARG B CD  1 
ATOM   1281 N  NE  . ARG B 2 30  ? -50.42  -19.589 1.55    1   24.92 ? 30  ARG B NE  1 
ATOM   1282 C  CZ  . ARG B 2 30  ? -51.362 -20.285 0.932   1   26.31 ? 30  ARG B CZ  1 
ATOM   1283 N  NH1 . ARG B 2 30  ? -51.09  -21.481 0.433   1   24.45 ? 30  ARG B NH1 1 
ATOM   1284 N  NH2 . ARG B 2 30  ? -52.577 -19.774 0.773   1   27.48 ? 30  ARG B NH2 1 
ATOM   1285 N  N   . LEU B 2 31  ? -45.044 -21.855 5.646   1   19.43 ? 31  LEU B N   1 
ATOM   1286 C  CA  . LEU B 2 31  ? -43.855 -22.698 5.92    1   19.99 ? 31  LEU B CA  1 
ATOM   1287 C  C   . LEU B 2 31  ? -44.214 -23.682 7.072   1   20.4  ? 31  LEU B C   1 
ATOM   1288 O  O   . LEU B 2 31  ? -43.946 -24.87  6.989   1   20.04 ? 31  LEU B O   1 
ATOM   1289 C  CB  . LEU B 2 31  ? -42.657 -21.815 6.384   1   19.71 ? 31  LEU B CB  1 
ATOM   1290 C  CG  . LEU B 2 31  ? -41.361 -22.61  6.788   1   21.57 ? 31  LEU B CG  1 
ATOM   1291 C  CD1 . LEU B 2 31  ? -40.638 -23.207 5.517   1   21.49 ? 31  LEU B CD1 1 
ATOM   1292 C  CD2 . LEU B 2 31  ? -40.418 -21.735 7.682   1   22.45 ? 31  LEU B CD2 1 
ATOM   1293 N  N   . LEU B 2 32  ? -44.854 -23.161 8.133   1   20.75 ? 32  LEU B N   1 
ATOM   1294 C  CA  . LEU B 2 32  ? -45.212 -23.96  9.296   1   21.47 ? 32  LEU B CA  1 
ATOM   1295 C  C   . LEU B 2 32  ? -46.262 -25.021 8.969   1   21.97 ? 32  LEU B C   1 
ATOM   1296 O  O   . LEU B 2 32  ? -46.286 -26.056 9.627   1   21.99 ? 32  LEU B O   1 
ATOM   1297 C  CB  . LEU B 2 32  ? -45.722 -23.047 10.43   1   23.51 ? 32  LEU B CB  1 
ATOM   1298 C  CG  . LEU B 2 32  ? -44.717 -22.01  10.966  1   27.35 ? 32  LEU B CG  1 
ATOM   1299 C  CD1 . LEU B 2 32  ? -45.288 -21.258 12.165  1   28.77 ? 32  LEU B CD1 1 
ATOM   1300 C  CD2 . LEU B 2 32  ? -43.471 -22.659 11.444  1   29.17 ? 32  LEU B CD2 1 
ATOM   1301 N  N   . VAL B 2 33  ? -47.149 -24.759 7.973   1   20.89 ? 33  VAL B N   1 
ATOM   1302 C  CA  . VAL B 2 33  ? -48.204 -25.711 7.639   1   21    ? 33  VAL B CA  1 
ATOM   1303 C  C   . VAL B 2 33  ? -47.689 -26.757 6.643   1   20.64 ? 33  VAL B C   1 
ATOM   1304 O  O   . VAL B 2 33  ? -47.984 -27.94  6.766   1   20.68 ? 33  VAL B O   1 
ATOM   1305 C  CB  . VAL B 2 33  ? -49.464 -24.972 7.094   1   21.95 ? 33  VAL B CB  1 
ATOM   1306 C  CG1 . VAL B 2 33  ? -50.478 -25.945 6.492   1   22.87 ? 33  VAL B CG1 1 
ATOM   1307 C  CG2 . VAL B 2 33  ? -50.126 -24.116 8.188   1   21.79 ? 33  VAL B CG2 1 
ATOM   1308 N  N   . VAL B 2 34  ? -46.945 -26.307 5.641   1   19.69 ? 34  VAL B N   1 
ATOM   1309 C  CA  . VAL B 2 34  ? -46.476 -27.179 4.575   1   18.98 ? 34  VAL B CA  1 
ATOM   1310 C  C   . VAL B 2 34  ? -45.301 -28.056 4.985   1   18.42 ? 34  VAL B C   1 
ATOM   1311 O  O   . VAL B 2 34  ? -45.231 -29.204 4.513   1   18.6  ? 34  VAL B O   1 
ATOM   1312 C  CB  . VAL B 2 34  ? -46.169 -26.369 3.285   1   19.45 ? 34  VAL B CB  1 
ATOM   1313 C  CG1 . VAL B 2 34  ? -45.677 -27.286 2.155   1   19.45 ? 34  VAL B CG1 1 
ATOM   1314 C  CG2 . VAL B 2 34  ? -47.396 -25.568 2.822   1   20.27 ? 34  VAL B CG2 1 
ATOM   1315 N  N   . TYR B 2 35  ? -44.359 -27.508 5.797   1   18.17 ? 35  TYR B N   1 
ATOM   1316 C  CA  . TYR B 2 35  ? -43.14  -28.207 6.24    1   19.06 ? 35  TYR B CA  1 
ATOM   1317 C  C   . TYR B 2 35  ? -43.242 -28.182 7.737   1   19.81 ? 35  TYR B C   1 
ATOM   1318 O  O   . TYR B 2 35  ? -42.659 -27.307 8.401   1   20    ? 35  TYR B O   1 
ATOM   1319 C  CB  . TYR B 2 35  ? -41.889 -27.469 5.734   1   18.38 ? 35  TYR B CB  1 
ATOM   1320 C  CG  . TYR B 2 35  ? -41.945 -27.358 4.222   1   19.19 ? 35  TYR B CG  1 
ATOM   1321 C  CD1 . TYR B 2 35  ? -41.882 -28.49  3.42    1   20.5  ? 35  TYR B CD1 1 
ATOM   1322 C  CD2 . TYR B 2 35  ? -42.181 -26.138 3.605   1   20.25 ? 35  TYR B CD2 1 
ATOM   1323 C  CE1 . TYR B 2 35  ? -41.971 -28.399 2.027   1   21.37 ? 35  TYR B CE1 1 
ATOM   1324 C  CE2 . TYR B 2 35  ? -42.243 -26.026 2.218   1   20.97 ? 35  TYR B CE2 1 
ATOM   1325 C  CZ  . TYR B 2 35  ? -42.143 -27.161 1.433   1   22.49 ? 35  TYR B CZ  1 
ATOM   1326 O  OH  . TYR B 2 35  ? -42.21  -27.045 0.063   1   25.39 ? 35  TYR B OH  1 
ATOM   1327 N  N   . PRO B 2 36  ? -44.082 -29.089 8.282   1   20.21 ? 36  PRO B N   1 
ATOM   1328 C  CA  . PRO B 2 36  ? -44.516 -28.907 9.681   1   19.94 ? 36  PRO B CA  1 
ATOM   1329 C  C   . PRO B 2 36  ? -43.462 -29.071 10.749  1   19.91 ? 36  PRO B C   1 
ATOM   1330 O  O   . PRO B 2 36  ? -43.675 -28.572 11.854  1   21.17 ? 36  PRO B O   1 
ATOM   1331 C  CB  . PRO B 2 36  ? -45.688 -29.88  9.845   1   21.32 ? 36  PRO B CB  1 
ATOM   1332 C  CG  . PRO B 2 36  ? -45.628 -30.791 8.698   1   22.13 ? 36  PRO B CG  1 
ATOM   1333 C  CD  . PRO B 2 36  ? -44.865 -30.143 7.596   1   20.54 ? 36  PRO B CD  1 
ATOM   1334 N  N   . TRP B 2 37  ? -42.321 -29.719 10.453  1   18.7  ? 37  TRP B N   1 
ATOM   1335 C  CA  . TRP B 2 37  ? -41.245 -29.8   11.446  1   18.23 ? 37  TRP B CA  1 
ATOM   1336 C  C   . TRP B 2 37  ? -40.686 -28.398 11.756  1   18.66 ? 37  TRP B C   1 
ATOM   1337 O  O   . TRP B 2 37  ? -40.008 -28.236 12.781  1   18.16 ? 37  TRP B O   1 
ATOM   1338 C  CB  . TRP B 2 37  ? -40.105 -30.704 10.942  1   17.59 ? 37  TRP B CB  1 
ATOM   1339 C  CG  . TRP B 2 37  ? -39.524 -30.209 9.647   1   16.84 ? 37  TRP B CG  1 
ATOM   1340 C  CD1 . TRP B 2 37  ? -38.45  -29.384 9.487   1   17.56 ? 37  TRP B CD1 1 
ATOM   1341 C  CD2 . TRP B 2 37  ? -39.951 -30.577 8.327   1   17.1  ? 37  TRP B CD2 1 
ATOM   1342 N  NE1 . TRP B 2 37  ? -38.213 -29.166 8.143   1   17.18 ? 37  TRP B NE1 1 
ATOM   1343 C  CE2 . TRP B 2 37  ? -39.116 -29.902 7.41    1   17.8  ? 37  TRP B CE2 1 
ATOM   1344 C  CE3 . TRP B 2 37  ? -40.968 -31.417 7.832   1   17.37 ? 37  TRP B CE3 1 
ATOM   1345 C  CZ2 . TRP B 2 37  ? -39.277 -30.021 6.022   1   17.83 ? 37  TRP B CZ2 1 
ATOM   1346 C  CZ3 . TRP B 2 37  ? -41.116 -31.548 6.452   1   17.98 ? 37  TRP B CZ3 1 
ATOM   1347 C  CH2 . TRP B 2 37  ? -40.274 -30.864 5.568   1   18    ? 37  TRP B CH2 1 
ATOM   1348 N  N   . THR B 2 38  ? -40.91  -27.397 10.87   1   19.44 ? 38  THR B N   1 
ATOM   1349 C  CA  . THR B 2 38  ? -40.427 -26.026 11.151  1   20.65 ? 38  THR B CA  1 
ATOM   1350 C  C   . THR B 2 38  ? -41.107 -25.428 12.385  1   22.28 ? 38  THR B C   1 
ATOM   1351 O  O   . THR B 2 38  ? -40.544 -24.528 12.999  1   23.19 ? 38  THR B O   1 
ATOM   1352 C  CB  . THR B 2 38  ? -40.512 -25.125 9.922   1   20.76 ? 38  THR B CB  1 
ATOM   1353 O  OG1 . THR B 2 38  ? -41.892 -24.958 9.581   1   21.93 ? 38  THR B OG1 1 
ATOM   1354 C  CG2 . THR B 2 38  ? -39.718 -25.704 8.716   1   20.12 ? 38  THR B CG2 1 
ATOM   1355 N  N   . GLN B 2 39  ? -42.29  -25.96  12.789  1   22.91 ? 39  GLN B N   1 
ATOM   1356 C  CA  . GLN B 2 39  ? -42.978 -25.508 14.013  1   22.82 ? 39  GLN B CA  1 
ATOM   1357 C  C   . GLN B 2 39  ? -42.103 -25.728 15.25   1   23.49 ? 39  GLN B C   1 
ATOM   1358 O  O   . GLN B 2 39  ? -42.328 -25.052 16.256  1   24.1  ? 39  GLN B O   1 
ATOM   1359 C  CB  . GLN B 2 39  ? -44.3   -26.263 14.215  1   22.73 ? 39  GLN B CB  1 
ATOM   1360 C  CG  . GLN B 2 39  ? -45.362 -25.944 13.152  1   23.15 ? 39  GLN B CG  1 
ATOM   1361 C  CD  . GLN B 2 39  ? -46.541 -26.88  13.221  1   26.32 ? 39  GLN B CD  1 
ATOM   1362 O  OE1 . GLN B 2 39  ? -46.832 -27.472 14.274  1   28.91 ? 39  GLN B OE1 1 
ATOM   1363 N  NE2 . GLN B 2 39  ? -47.254 -27.044 12.109  1   25.38 ? 39  GLN B NE2 1 
ATOM   1364 N  N   . ARG B 2 40  ? -41.093 -26.632 15.186  1   22.89 ? 40  ARG B N   1 
ATOM   1365 C  CA  . ARG B 2 40  ? -40.23  -26.887 16.346  1   24.59 ? 40  ARG B CA  1 
ATOM   1366 C  C   . ARG B 2 40  ? -39.488 -25.618 16.774  1   26.29 ? 40  ARG B C   1 
ATOM   1367 O  O   . ARG B 2 40  ? -39.332 -25.36  17.959  1   25.92 ? 40  ARG B O   1 
ATOM   1368 C  CB  . ARG B 2 40  ? -39.207 -27.997 16.039  1   24.08 ? 40  ARG B CB  1 
ATOM   1369 C  CG  . ARG B 2 40  ? -38.35  -28.361 17.264  1   26.99 ? 40  ARG B CG  1 
ATOM   1370 C  CD  . ARG B 2 40  ? -37.495 -29.601 17.023  1   28.68 ? 40  ARG B CD  1 
ATOM   1371 N  NE  . ARG B 2 40  ? -36.446 -29.703 18.048  1   29.01 ? 40  ARG B NE  1 
ATOM   1372 C  CZ  . ARG B 2 40  ? -36.526 -30.48  19.119  1   31.42 ? 40  ARG B CZ  1 
ATOM   1373 N  NH1 . ARG B 2 40  ? -37.57  -31.302 19.285  1   30.1  ? 40  ARG B NH1 1 
ATOM   1374 N  NH2 . ARG B 2 40  ? -35.535 -30.505 19.999  1   31.48 ? 40  ARG B NH2 1 
ATOM   1375 N  N   . PHE B 2 41  ? -39.049 -24.825 15.804  1   28.25 ? 41  PHE B N   1 
ATOM   1376 C  CA  . PHE B 2 41  ? -38.336 -23.581 16.096  1   30.88 ? 41  PHE B CA  1 
ATOM   1377 C  C   . PHE B 2 41  ? -39.231 -22.476 16.678  1   31.97 ? 41  PHE B C   1 
ATOM   1378 O  O   . PHE B 2 41  ? -38.715 -21.484 17.186  1   32.55 ? 41  PHE B O   1 
ATOM   1379 C  CB  . PHE B 2 41  ? -37.67  -23.07  14.814  1   31.22 ? 41  PHE B CB  1 
ATOM   1380 C  CG  . PHE B 2 41  ? -36.673 -24.061 14.275  1   32.68 ? 41  PHE B CG  1 
ATOM   1381 C  CD1 . PHE B 2 41  ? -35.397 -24.143 14.808  1   33.83 ? 41  PHE B CD1 1 
ATOM   1382 C  CD2 . PHE B 2 41  ? -37.023 -24.944 13.268  1   33.52 ? 41  PHE B CD2 1 
ATOM   1383 C  CE1 . PHE B 2 41  ? -34.493 -25.076 14.331  1   34.13 ? 41  PHE B CE1 1 
ATOM   1384 C  CE2 . PHE B 2 41  ? -36.109 -25.874 12.793  1   34.16 ? 41  PHE B CE2 1 
ATOM   1385 C  CZ  . PHE B 2 41  ? -34.845 -25.911 13.309  1   33.45 ? 41  PHE B CZ  1 
ATOM   1386 N  N   . PHE B 2 42  ? -40.559 -22.602 16.545  1   32.22 ? 42  PHE B N   1 
ATOM   1387 C  CA  . PHE B 2 42  ? -41.491 -21.565 16.995  1   33.21 ? 42  PHE B CA  1 
ATOM   1388 C  C   . PHE B 2 42  ? -42.487 -22.069 18.046  1   36.36 ? 42  PHE B C   1 
ATOM   1389 O  O   . PHE B 2 42  ? -43.593 -21.534 18.16   1   36.52 ? 42  PHE B O   1 
ATOM   1390 C  CB  . PHE B 2 42  ? -42.242 -21.01  15.774  1   32.42 ? 42  PHE B CB  1 
ATOM   1391 C  CG  . PHE B 2 42  ? -41.331 -20.447 14.706  1   32.55 ? 42  PHE B CG  1 
ATOM   1392 C  CD1 . PHE B 2 42  ? -40.873 -19.144 14.779  1   33.3  ? 42  PHE B CD1 1 
ATOM   1393 C  CD2 . PHE B 2 42  ? -40.965 -21.208 13.61   1   32.89 ? 42  PHE B CD2 1 
ATOM   1394 C  CE1 . PHE B 2 42  ? -40.044 -18.622 13.791  1   33.21 ? 42  PHE B CE1 1 
ATOM   1395 C  CE2 . PHE B 2 42  ? -40.146 -20.681 12.618  1   33.47 ? 42  PHE B CE2 1 
ATOM   1396 C  CZ  . PHE B 2 42  ? -39.702 -19.387 12.707  1   32.93 ? 42  PHE B CZ  1 
ATOM   1397 N  N   . GLU B 2 43  ? -42.092 -23.087 18.822  1   38.54 ? 43  GLU B N   1 
ATOM   1398 C  CA  . GLU B 2 43  ? -42.91  -23.688 19.879  1   41.44 ? 43  GLU B CA  1 
ATOM   1399 C  C   . GLU B 2 43  ? -43.51  -22.689 20.831  1   42.3  ? 43  GLU B C   1 
ATOM   1400 O  O   . GLU B 2 43  ? -44.626 -22.906 21.307  1   43.78 ? 43  GLU B O   1 
ATOM   1401 C  CB  . GLU B 2 43  ? -42.093 -24.707 20.686  1   45.95 ? 43  GLU B CB  1 
ATOM   1402 C  CG  . GLU B 2 43  ? -41.863 -25.995 19.921  1   54.57 ? 43  GLU B CG  1 
ATOM   1403 C  CD  . GLU B 2 43  ? -41.103 -27.042 20.709  1   64.17 ? 43  GLU B CD  1 
ATOM   1404 O  OE1 . GLU B 2 43  ? -40.265 -26.66  21.559  1   66.63 ? 43  GLU B OE1 1 
ATOM   1405 O  OE2 . GLU B 2 43  ? -41.349 -28.247 20.479  1   65.99 ? 43  GLU B OE2 1 
ATOM   1406 N  N   . SER B 2 44  ? -42.781 -21.603 21.138  1   41.18 ? 44  SER B N   1 
ATOM   1407 C  CA  . SER B 2 44  ? -43.262 -20.589 22.071  1   40.53 ? 44  SER B CA  1 
ATOM   1408 C  C   . SER B 2 44  ? -44.346 -19.659 21.503  1   39.59 ? 44  SER B C   1 
ATOM   1409 O  O   . SER B 2 44  ? -44.906 -18.865 22.261  1   40.05 ? 44  SER B O   1 
ATOM   1410 C  CB  . SER B 2 44  ? -42.1   -19.767 22.615  1   41.79 ? 44  SER B CB  1 
ATOM   1411 O  OG  . SER B 2 44  ? -41.623 -18.852 21.64   1   44.75 ? 44  SER B OG  1 
ATOM   1412 N  N   . PHE B 2 45  ? -44.632 -19.735 20.191  1   38.43 ? 45  PHE B N   1 
ATOM   1413 C  CA  . PHE B 2 45  ? -45.637 -18.891 19.547  1   38.25 ? 45  PHE B CA  1 
ATOM   1414 C  C   . PHE B 2 45  ? -47.084 -19.269 19.887  1   39    ? 45  PHE B C   1 
ATOM   1415 O  O   . PHE B 2 45  ? -47.993 -18.54  19.521  1   39.81 ? 45  PHE B O   1 
ATOM   1416 C  CB  . PHE B 2 45  ? -45.427 -18.837 18.015  1   37.85 ? 45  PHE B CB  1 
ATOM   1417 C  CG  . PHE B 2 45  ? -44.311 -17.93  17.539  1   37.56 ? 45  PHE B CG  1 
ATOM   1418 C  CD1 . PHE B 2 45  ? -43.305 -17.521 18.403  1   38.14 ? 45  PHE B CD1 1 
ATOM   1419 C  CD2 . PHE B 2 45  ? -44.275 -17.478 16.232  1   38.13 ? 45  PHE B CD2 1 
ATOM   1420 C  CE1 . PHE B 2 45  ? -42.296 -16.666 17.968  1   38.71 ? 45  PHE B CE1 1 
ATOM   1421 C  CE2 . PHE B 2 45  ? -43.253 -16.643 15.798  1   38.56 ? 45  PHE B CE2 1 
ATOM   1422 C  CZ  . PHE B 2 45  ? -42.267 -16.251 16.665  1   38.19 ? 45  PHE B CZ  1 
ATOM   1423 N  N   . GLY B 2 46  ? -47.293 -20.38  20.583  1   38.63 ? 46  GLY B N   1 
ATOM   1424 C  CA  . GLY B 2 46  ? -48.624 -20.786 20.998  1   38.53 ? 46  GLY B CA  1 
ATOM   1425 C  C   . GLY B 2 46  ? -49.296 -21.824 20.122  1   37.29 ? 46  GLY B C   1 
ATOM   1426 O  O   . GLY B 2 46  ? -48.687 -22.819 19.74   1   37.11 ? 46  GLY B O   1 
ATOM   1427 N  N   . ASP B 2 47  ? -50.579 -21.617 19.843  1   36    ? 47  ASP B N   1 
ATOM   1428 C  CA  . ASP B 2 47  ? -51.39  -22.563 19.089  1   35.49 ? 47  ASP B CA  1 
ATOM   1429 C  C   . ASP B 2 47  ? -51.006 -22.626 17.611  1   34.02 ? 47  ASP B C   1 
ATOM   1430 O  O   . ASP B 2 47  ? -51.225 -21.675 16.874  1   34.59 ? 47  ASP B O   1 
ATOM   1431 C  CB  . ASP B 2 47  ? -52.877 -22.216 19.252  1   37.85 ? 47  ASP B CB  1 
ATOM   1432 C  CG  . ASP B 2 47  ? -53.859 -23.263 18.767  1   42.3  ? 47  ASP B CG  1 
ATOM   1433 O  OD1 . ASP B 2 47  ? -53.408 -24.339 18.301  1   41.06 ? 47  ASP B OD1 1 
ATOM   1434 O  OD2 . ASP B 2 47  ? -55.086 -23.007 18.849  1   45.24 ? 47  ASP B OD2 1 
ATOM   1435 N  N   . LEU B 2 48  ? -50.428 -23.754 17.202  1   32.41 ? 48  LEU B N   1 
ATOM   1436 C  CA  . LEU B 2 48  ? -50.059 -24.075 15.82   1   31.75 ? 48  LEU B CA  1 
ATOM   1437 C  C   . LEU B 2 48  ? -50.667 -25.449 15.432  1   32.15 ? 48  LEU B C   1 
ATOM   1438 O  O   . LEU B 2 48  ? -50.15  -26.106 14.543  1   31.57 ? 48  LEU B O   1 
ATOM   1439 C  CB  . LEU B 2 48  ? -48.526 -24.155 15.692  1   31.64 ? 48  LEU B CB  1 
ATOM   1440 C  CG  . LEU B 2 48  ? -47.704 -22.975 16.246  1   32.6  ? 48  LEU B CG  1 
ATOM   1441 C  CD1 . LEU B 2 48  ? -46.214 -23.289 16.227  1   33.11 ? 48  LEU B CD1 1 
ATOM   1442 C  CD2 . LEU B 2 48  ? -47.964 -21.701 15.451  1   32.54 ? 48  LEU B CD2 1 
ATOM   1443 N  N   . SER B 2 49  ? -51.79  -25.86  16.079  1   33    ? 49  SER B N   1 
ATOM   1444 C  CA  . SER B 2 49  ? -52.362 -27.188 15.904  1   33.68 ? 49  SER B CA  1 
ATOM   1445 C  C   . SER B 2 49  ? -53.09  -27.41  14.598  1   33.54 ? 49  SER B C   1 
ATOM   1446 O  O   . SER B 2 49  ? -53.185 -28.557 14.137  1   34.42 ? 49  SER B O   1 
ATOM   1447 C  CB  . SER B 2 49  ? -53.263 -27.527 17.081  1   35.4  ? 49  SER B CB  1 
ATOM   1448 O  OG  . SER B 2 49  ? -54.262 -26.542 17.234  1   38.88 ? 49  SER B OG  1 
ATOM   1449 N  N   . THR B 2 50  ? -53.59  -26.331 13.983  1   31.51 ? 50  THR B N   1 
ATOM   1450 C  CA  . THR B 2 50  ? -54.285 -26.446 12.707  1   30.67 ? 50  THR B CA  1 
ATOM   1451 C  C   . THR B 2 50  ? -53.767 -25.357 11.756  1   30.11 ? 50  THR B C   1 
ATOM   1452 O  O   . THR B 2 50  ? -53.319 -24.3   12.216  1   30.72 ? 50  THR B O   1 
ATOM   1453 C  CB  . THR B 2 50  ? -55.817 -26.243 12.906  1   32.89 ? 50  THR B CB  1 
ATOM   1454 O  OG1 . THR B 2 50  ? -56.096 -24.893 13.29   1   34.58 ? 50  THR B OG1 1 
ATOM   1455 C  CG2 . THR B 2 50  ? -56.441 -27.207 13.928  1   33.25 ? 50  THR B CG2 1 
ATOM   1456 N  N   . PRO B 2 51  ? -54.02  -25.486 10.45   1   29.14 ? 51  PRO B N   1 
ATOM   1457 C  CA  . PRO B 2 51  ? -53.628 -24.411 9.522   1   29.1  ? 51  PRO B CA  1 
ATOM   1458 C  C   . PRO B 2 51  ? -54.256 -23.068 9.912   1   30.45 ? 51  PRO B C   1 
ATOM   1459 O  O   . PRO B 2 51  ? -53.558 -22.064 9.951   1   30.64 ? 51  PRO B O   1 
ATOM   1460 C  CB  . PRO B 2 51  ? -54.117 -24.925 8.164   1   29.83 ? 51  PRO B CB  1 
ATOM   1461 C  CG  . PRO B 2 51  ? -54.127 -26.417 8.31    1   29.98 ? 51  PRO B CG  1 
ATOM   1462 C  CD  . PRO B 2 51  ? -54.537 -26.667 9.734   1   28.62 ? 51  PRO B CD  1 
ATOM   1463 N  N   . ASP B 2 52  ? -55.552 -23.05  10.28   1   31.92 ? 52  ASP B N   1 
ATOM   1464 C  CA  . ASP B 2 52  ? -56.207 -21.807 10.703  1   33.08 ? 52  ASP B CA  1 
ATOM   1465 C  C   . ASP B 2 52  ? -55.551 -21.208 11.963  1   33.59 ? 52  ASP B C   1 
ATOM   1466 O  O   . ASP B 2 52  ? -55.409 -19.984 12.036  1   33.94 ? 52  ASP B O   1 
ATOM   1467 C  CB  . ASP B 2 52  ? -57.719 -21.999 10.933  1   35.15 ? 52  ASP B CB  1 
ATOM   1468 C  CG  . ASP B 2 52  ? -58.54  -22.191 9.666   1   39.89 ? 52  ASP B CG  1 
ATOM   1469 O  OD1 . ASP B 2 52  ? -57.981 -22.031 8.561   1   39.49 ? 52  ASP B OD1 1 
ATOM   1470 O  OD2 . ASP B 2 52  ? -59.732 -22.525 9.783   1   42.45 ? 52  ASP B OD2 1 
ATOM   1471 N  N   . ALA B 2 53  ? -55.187 -22.044 12.958  1   33.18 ? 53  ALA B N   1 
ATOM   1472 C  CA  . ALA B 2 53  ? -54.543 -21.523 14.172  1   33.22 ? 53  ALA B CA  1 
ATOM   1473 C  C   . ALA B 2 53  ? -53.167 -20.929 13.817  1   32.66 ? 53  ALA B C   1 
ATOM   1474 O  O   . ALA B 2 53  ? -52.814 -19.867 14.328  1   33.15 ? 53  ALA B O   1 
ATOM   1475 C  CB  . ALA B 2 53  ? -54.387 -22.623 15.218  1   33.26 ? 53  ALA B CB  1 
ATOM   1476 N  N   . VAL B 2 54  ? -52.414 -21.6   12.933  1   30.98 ? 54  VAL B N   1 
ATOM   1477 C  CA  . VAL B 2 54  ? -51.12  -21.106 12.474  1   30.87 ? 54  VAL B CA  1 
ATOM   1478 C  C   . VAL B 2 54  ? -51.274 -19.721 11.763  1   32.04 ? 54  VAL B C   1 
ATOM   1479 O  O   . VAL B 2 54  ? -50.662 -18.744 12.195  1   31.86 ? 54  VAL B O   1 
ATOM   1480 C  CB  . VAL B 2 54  ? -50.411 -22.14  11.54   1   30.43 ? 54  VAL B CB  1 
ATOM   1481 C  CG1 . VAL B 2 54  ? -49.177 -21.53  10.889  1   30.2  ? 54  VAL B CG1 1 
ATOM   1482 C  CG2 . VAL B 2 54  ? -50.059 -23.423 12.292  1   30.41 ? 54  VAL B CG2 1 
ATOM   1483 N  N   . MET B 2 55  ? -52.099 -19.645 10.695  1   32.44 ? 55  MET B N   1 
ATOM   1484 C  CA  . MET B 2 55  ? -52.271 -18.43  9.893   1   33.54 ? 55  MET B CA  1 
ATOM   1485 C  C   . MET B 2 55  ? -52.801 -17.243 10.664  1   36.09 ? 55  MET B C   1 
ATOM   1486 O  O   . MET B 2 55  ? -52.489 -16.096 10.334  1   36.41 ? 55  MET B O   1 
ATOM   1487 C  CB  . MET B 2 55  ? -53.178 -18.685 8.675   1   32.23 ? 55  MET B CB  1 
ATOM   1488 C  CG  . MET B 2 55  ? -52.756 -19.886 7.812   1   30.91 ? 55  MET B CG  1 
ATOM   1489 S  SD  . MET B 2 55  ? -51.04  -19.921 7.274   1   30.7  ? 55  MET B SD  1 
ATOM   1490 C  CE  . MET B 2 55  ? -51.017 -18.527 6.179   1   28.14 ? 55  MET B CE  1 
ATOM   1491 N  N   . GLY B 2 56  ? -53.656 -17.517 11.635  1   36.95 ? 56  GLY B N   1 
ATOM   1492 C  CA  . GLY B 2 56  ? -54.258 -16.469 12.441  1   37.78 ? 56  GLY B CA  1 
ATOM   1493 C  C   . GLY B 2 56  ? -53.477 -16.107 13.69   1   38.01 ? 56  GLY B C   1 
ATOM   1494 O  O   . GLY B 2 56  ? -53.865 -15.186 14.392  1   38.42 ? 56  GLY B O   1 
ATOM   1495 N  N   . ASN B 2 57  ? -52.364 -16.798 13.966  1   37.63 ? 57  ASN B N   1 
ATOM   1496 C  CA  . ASN B 2 57  ? -51.558 -16.559 15.163  1   37.77 ? 57  ASN B CA  1 
ATOM   1497 C  C   . ASN B 2 57  ? -50.873 -15.186 15.088  1   38.17 ? 57  ASN B C   1 
ATOM   1498 O  O   . ASN B 2 57  ? -50.101 -14.931 14.167  1   37.55 ? 57  ASN B O   1 
ATOM   1499 C  CB  . ASN B 2 57  ? -50.523 -17.697 15.316  1   37.96 ? 57  ASN B CB  1 
ATOM   1500 C  CG  . ASN B 2 57  ? -49.8   -17.731 16.641  1   40.27 ? 57  ASN B CG  1 
ATOM   1501 O  OD1 . ASN B 2 57  ? -49.187 -16.751 17.059  1   41.5  ? 57  ASN B OD1 1 
ATOM   1502 N  ND2 . ASN B 2 57  ? -49.837 -18.868 17.317  1   39.43 ? 57  ASN B ND2 1 
ATOM   1503 N  N   . PRO B 2 58  ? -51.117 -14.298 16.079  1   38.74 ? 58  PRO B N   1 
ATOM   1504 C  CA  . PRO B 2 58  ? -50.497 -12.959 16.034  1   38.66 ? 58  PRO B CA  1 
ATOM   1505 C  C   . PRO B 2 58  ? -48.972 -12.971 16.031  1   38.4  ? 58  PRO B C   1 
ATOM   1506 O  O   . PRO B 2 58  ? -48.373 -12.133 15.372  1   39.55 ? 58  PRO B O   1 
ATOM   1507 C  CB  . PRO B 2 58  ? -51.039 -12.264 17.287  1   39.66 ? 58  PRO B CB  1 
ATOM   1508 C  CG  . PRO B 2 58  ? -52.268 -13.024 17.645  1   40.68 ? 58  PRO B CG  1 
ATOM   1509 C  CD  . PRO B 2 58  ? -52.044 -14.438 17.217  1   38.75 ? 58  PRO B CD  1 
ATOM   1510 N  N   . LYS B 2 59  ? -48.343 -13.922 16.728  1   36.98 ? 59  LYS B N   1 
ATOM   1511 C  CA  . LYS B 2 59  ? -46.88  -14.026 16.729  1   36.66 ? 59  LYS B CA  1 
ATOM   1512 C  C   . LYS B 2 59  ? -46.315 -14.466 15.378  1   35.88 ? 59  LYS B C   1 
ATOM   1513 O  O   . LYS B 2 59  ? -45.25  -13.988 14.967  1   35.66 ? 59  LYS B O   1 
ATOM   1514 C  CB  . LYS B 2 59  ? -46.398 -14.926 17.88   1   38.21 ? 59  LYS B CB  1 
ATOM   1515 C  CG  . LYS B 2 59  ? -46.616 -14.272 19.248  1   40.5  ? 59  LYS B CG  1 
ATOM   1516 C  CD  . LYS B 2 59  ? -46.162 -15.18  20.382  1   43.54 ? 59  LYS B CD  1 
ATOM   1517 C  CE  . LYS B 2 59  ? -46.261 -14.497 21.731  1   46.92 ? 59  LYS B CE  1 
ATOM   1518 N  NZ  . LYS B 2 59  ? -45.961 -15.433 22.842  1   48.82 ? 59  LYS B NZ  1 
ATOM   1519 N  N   . VAL B 2 60  ? -47.065 -15.303 14.642  1   35.12 ? 60  VAL B N   1 
ATOM   1520 C  CA  . VAL B 2 60  ? -46.659 -15.739 13.295  1   34.42 ? 60  VAL B CA  1 
ATOM   1521 C  C   . VAL B 2 60  ? -46.693 -14.523 12.36   1   35.3  ? 60  VAL B C   1 
ATOM   1522 O  O   . VAL B 2 60  ? -45.733 -14.277 11.638  1   35.4  ? 60  VAL B O   1 
ATOM   1523 C  CB  . VAL B 2 60  ? -47.545 -16.896 12.774  1   34.53 ? 60  VAL B CB  1 
ATOM   1524 C  CG1 . VAL B 2 60  ? -47.341 -17.126 11.265  1   35.02 ? 60  VAL B CG1 1 
ATOM   1525 C  CG2 . VAL B 2 60  ? -47.274 -18.178 13.557  1   34.96 ? 60  VAL B CG2 1 
ATOM   1526 N  N   . LYS B 2 61  ? -47.762 -13.726 12.419  1   36.34 ? 61  LYS B N   1 
ATOM   1527 C  CA  . LYS B 2 61  ? -47.869 -12.519 11.604  1   37.66 ? 61  LYS B CA  1 
ATOM   1528 C  C   . LYS B 2 61  ? -46.734 -11.51  11.917  1   38.5  ? 61  LYS B C   1 
ATOM   1529 O  O   . LYS B 2 61  ? -46.102 -11.004 10.988  1   38.91 ? 61  LYS B O   1 
ATOM   1530 C  CB  . LYS B 2 61  ? -49.249 -11.853 11.786  1   40.28 ? 61  LYS B CB  1 
ATOM   1531 C  CG  . LYS B 2 61  ? -50.418 -12.762 11.405  1   45.82 ? 61  LYS B CG  1 
ATOM   1532 C  CD  . LYS B 2 61  ? -51.658 -12.464 12.244  1   52.88 ? 61  LYS B CD  1 
ATOM   1533 C  CE  . LYS B 2 61  ? -52.826 -12.009 11.408  1   58.14 ? 61  LYS B CE  1 
ATOM   1534 N  NZ  . LYS B 2 61  ? -53.162 -12.997 10.353  1   61.21 ? 61  LYS B NZ  1 
ATOM   1535 N  N   . ALA B 2 62  ? -46.483 -11.218 13.209  1   38.38 ? 62  ALA B N   1 
ATOM   1536 C  CA  . ALA B 2 62  ? -45.431 -10.27  13.61   1   38.43 ? 62  ALA B CA  1 
ATOM   1537 C  C   . ALA B 2 62  ? -44.026 -10.759 13.177  1   37.56 ? 62  ALA B C   1 
ATOM   1538 O  O   . ALA B 2 62  ? -43.246 -9.972  12.644  1   38.42 ? 62  ALA B O   1 
ATOM   1539 C  CB  . ALA B 2 62  ? -45.472 -10.042 15.116  1   38.89 ? 62  ALA B CB  1 
ATOM   1540 N  N   . HIS B 2 63  ? -43.715 -12.043 13.378  1   35.64 ? 63  HIS B N   1 
ATOM   1541 C  CA  . HIS B 2 63  ? -42.417 -12.574 12.961  1   35.4  ? 63  HIS B CA  1 
ATOM   1542 C  C   . HIS B 2 63  ? -42.273 -12.593 11.431  1   35.82 ? 63  HIS B C   1 
ATOM   1543 O  O   . HIS B 2 63  ? -41.187 -12.332 10.896  1   35.67 ? 63  HIS B O   1 
ATOM   1544 C  CB  . HIS B 2 63  ? -42.173 -13.987 13.506  1   35.04 ? 63  HIS B CB  1 
ATOM   1545 C  CG  . HIS B 2 63  ? -40.767 -14.408 13.276  1   35.7  ? 63  HIS B CG  1 
ATOM   1546 N  ND1 . HIS B 2 63  ? -39.725 -13.796 13.942  1   36.67 ? 63  HIS B ND1 1 
ATOM   1547 C  CD2 . HIS B 2 63  ? -40.263 -15.312 12.402  1   37.31 ? 63  HIS B CD2 1 
ATOM   1548 C  CE1 . HIS B 2 63  ? -38.623 -14.358 13.474  1   37.98 ? 63  HIS B CE1 1 
ATOM   1549 N  NE2 . HIS B 2 63  ? -38.895 -15.27  12.538  1   38.07 ? 63  HIS B NE2 1 
ATOM   1550 N  N   . GLY B 2 64  ? -43.367 -12.885 10.731  1   35.68 ? 64  GLY B N   1 
ATOM   1551 C  CA  . GLY B 2 64  ? -43.364 -12.89  9.272   1   35.69 ? 64  GLY B CA  1 
ATOM   1552 C  C   . GLY B 2 64  ? -42.995 -11.526 8.696   1   36    ? 64  GLY B C   1 
ATOM   1553 O  O   . GLY B 2 64  ? -42.288 -11.441 7.683   1   35.76 ? 64  GLY B O   1 
ATOM   1554 N  N   . LYS B 2 65  ? -43.389 -10.447 9.394   1   36.45 ? 65  LYS B N   1 
ATOM   1555 C  CA  . LYS B 2 65  ? -43.034 -9.091  8.983   1   37.46 ? 65  LYS B CA  1 
ATOM   1556 C  C   . LYS B 2 65  ? -41.519 -8.91   9.017   1   37.32 ? 65  LYS B C   1 
ATOM   1557 O  O   . LYS B 2 65  ? -40.965 -8.324  8.088   1   37.66 ? 65  LYS B O   1 
ATOM   1558 C  CB  . LYS B 2 65  ? -43.687 -8.038  9.893   1   40.23 ? 65  LYS B CB  1 
ATOM   1559 C  CG  . LYS B 2 65  ? -45.159 -7.799  9.651   1   46.13 ? 65  LYS B CG  1 
ATOM   1560 C  CD  . LYS B 2 65  ? -45.588 -6.458  10.28   1   50.7  ? 65  LYS B CD  1 
ATOM   1561 C  CE  . LYS B 2 65  ? -47.082 -6.344  10.458  1   55.64 ? 65  LYS B CE  1 
ATOM   1562 N  NZ  . LYS B 2 65  ? -47.466 -5.007  11.01   1   59.25 ? 65  LYS B NZ  1 
ATOM   1563 N  N   . LYS B 2 66  ? -40.863 -9.392  10.104  1   36.27 ? 66  LYS B N   1 
ATOM   1564 C  CA  . LYS B 2 66  ? -39.413 -9.345  10.265  1   36.16 ? 66  LYS B CA  1 
ATOM   1565 C  C   . LYS B 2 66  ? -38.717 -10.119 9.146   1   36.05 ? 66  LYS B C   1 
ATOM   1566 O  O   . LYS B 2 66  ? -37.775 -9.602  8.556   1   36.16 ? 66  LYS B O   1 
ATOM   1567 C  CB  . LYS B 2 66  ? -38.989 -9.875  11.636  1   38.26 ? 66  LYS B CB  1 
ATOM   1568 C  CG  . LYS B 2 66  ? -39.398 -8.972  12.801  1   43.69 ? 66  LYS B CG  1 
ATOM   1569 C  CD  . LYS B 2 66  ? -39.191 -9.717  14.129  1   50.24 ? 66  LYS B CD  1 
ATOM   1570 C  CE  . LYS B 2 66  ? -39.042 -8.825  15.332  1   56.07 ? 66  LYS B CE  1 
ATOM   1571 N  NZ  . LYS B 2 66  ? -38.234 -9.49   16.394  1   59.71 ? 66  LYS B NZ  1 
ATOM   1572 N  N   . VAL B 2 67  ? -39.184 -11.34  8.834   1   35.11 ? 67  VAL B N   1 
ATOM   1573 C  CA  . VAL B 2 67  ? -38.625 -12.131 7.726   1   34.65 ? 67  VAL B CA  1 
ATOM   1574 C  C   . VAL B 2 67  ? -38.711 -11.372 6.384   1   34.35 ? 67  VAL B C   1 
ATOM   1575 O  O   . VAL B 2 67  ? -37.714 -11.245 5.674   1   34.35 ? 67  VAL B O   1 
ATOM   1576 C  CB  . VAL B 2 67  ? -39.332 -13.502 7.636   1   34.74 ? 67  VAL B CB  1 
ATOM   1577 C  CG1 . VAL B 2 67  ? -38.835 -14.291 6.441   1   35.62 ? 67  VAL B CG1 1 
ATOM   1578 C  CG2 . VAL B 2 67  ? -39.156 -14.288 8.921   1   34.36 ? 67  VAL B CG2 1 
ATOM   1579 N  N   . LEU B 2 68  ? -39.877 -10.836 6.055   1   34.08 ? 68  LEU B N   1 
ATOM   1580 C  CA  . LEU B 2 68  ? -40.074 -10.066 4.816   1   35.06 ? 68  LEU B CA  1 
ATOM   1581 C  C   . LEU B 2 68  ? -39.121 -8.849  4.763   1   35.8  ? 68  LEU B C   1 
ATOM   1582 O  O   . LEU B 2 68  ? -38.565 -8.535  3.699   1   35.73 ? 68  LEU B O   1 
ATOM   1583 C  CB  . LEU B 2 68  ? -41.536 -9.579  4.737   1   35.37 ? 68  LEU B CB  1 
ATOM   1584 C  CG  . LEU B 2 68  ? -41.978 -9.059  3.381   1   37.63 ? 68  LEU B CG  1 
ATOM   1585 C  CD1 . LEU B 2 68  ? -42.352 -10.21  2.472   1   37.91 ? 68  LEU B CD1 1 
ATOM   1586 C  CD2 . LEU B 2 68  ? -43.158 -8.133  3.525   1   38.6  ? 68  LEU B CD2 1 
ATOM   1587 N  N   . GLY B 2 69  ? -38.907 -8.216  5.918   1   35.91 ? 69  GLY B N   1 
ATOM   1588 C  CA  . GLY B 2 69  ? -37.995 -7.082  6.056   1   37.43 ? 69  GLY B CA  1 
ATOM   1589 C  C   . GLY B 2 69  ? -36.575 -7.479  5.68    1   38.97 ? 69  GLY B C   1 
ATOM   1590 O  O   . GLY B 2 69  ? -35.884 -6.728  4.981   1   39.67 ? 69  GLY B O   1 
ATOM   1591 N  N   . ALA B 2 70  ? -36.155 -8.703  6.069   1   38.32 ? 70  ALA B N   1 
ATOM   1592 C  CA  . ALA B 2 70  ? -34.833 -9.207  5.716   1   38.86 ? 70  ALA B CA  1 
ATOM   1593 C  C   . ALA B 2 70  ? -34.716 -9.502  4.241   1   39.16 ? 70  ALA B C   1 
ATOM   1594 O  O   . ALA B 2 70  ? -33.697 -9.142  3.659   1   40.51 ? 70  ALA B O   1 
ATOM   1595 C  CB  . ALA B 2 70  ? -34.482 -10.44  6.531   1   39.08 ? 70  ALA B CB  1 
ATOM   1596 N  N   . PHE B 2 71  ? -35.749 -10.098 3.6     1   37.71 ? 71  PHE B N   1 
ATOM   1597 C  CA  . PHE B 2 71  ? -35.699 -10.32  2.144   1   37.35 ? 71  PHE B CA  1 
ATOM   1598 C  C   . PHE B 2 71  ? -35.59  -8.982  1.399   1   37.59 ? 71  PHE B C   1 
ATOM   1599 O  O   . PHE B 2 71  ? -34.892 -8.892  0.392   1   37.26 ? 71  PHE B O   1 
ATOM   1600 C  CB  . PHE B 2 71  ? -36.93  -11.094 1.639   1   36.64 ? 71  PHE B CB  1 
ATOM   1601 C  CG  . PHE B 2 71  ? -36.819 -12.599 1.703   1   35.93 ? 71  PHE B CG  1 
ATOM   1602 C  CD1 . PHE B 2 71  ? -36.181 -13.308 0.697   1   35.97 ? 71  PHE B CD1 1 
ATOM   1603 C  CD2 . PHE B 2 71  ? -37.387 -13.309 2.747   1   36.18 ? 71  PHE B CD2 1 
ATOM   1604 C  CE1 . PHE B 2 71  ? -36.099 -14.695 0.748   1   35.99 ? 71  PHE B CE1 1 
ATOM   1605 C  CE2 . PHE B 2 71  ? -37.324 -14.703 2.78    1   36.13 ? 71  PHE B CE2 1 
ATOM   1606 C  CZ  . PHE B 2 71  ? -36.68  -15.382 1.785   1   35.37 ? 71  PHE B CZ  1 
ATOM   1607 N  N   . SER B 2 72  ? -36.267 -7.947  1.903   1   38.02 ? 72  SER B N   1 
ATOM   1608 C  CA  . SER B 2 72  ? -36.215 -6.603  1.334   1   39.15 ? 72  SER B CA  1 
ATOM   1609 C  C   . SER B 2 72  ? -34.782 -6.066  1.468   1   40.06 ? 72  SER B C   1 
ATOM   1610 O  O   . SER B 2 72  ? -34.293 -5.431  0.549   1   39.98 ? 72  SER B O   1 
ATOM   1611 C  CB  . SER B 2 72  ? -37.196 -5.678  2.063   1   40.31 ? 72  SER B CB  1 
ATOM   1612 O  OG  . SER B 2 72  ? -36.977 -4.321  1.713   1   44.45 ? 72  SER B OG  1 
ATOM   1613 N  N   . ASP B 2 73  ? -34.123 -6.295  2.616   1   40.48 ? 73  ASP B N   1 
ATOM   1614 C  CA  . ASP B 2 73  ? -32.734 -5.872  2.839   1   41.36 ? 73  ASP B CA  1 
ATOM   1615 C  C   . ASP B 2 73  ? -31.783 -6.552  1.806   1   41.85 ? 73  ASP B C   1 
ATOM   1616 O  O   . ASP B 2 73  ? -30.852 -5.915  1.314   1   42.39 ? 73  ASP B O   1 
ATOM   1617 C  CB  . ASP B 2 73  ? -32.305 -6.081  4.319   1   42.45 ? 73  ASP B CB  1 
ATOM   1618 C  CG  . ASP B 2 73  ? -33.085 -5.239  5.335   1   48.85 ? 73  ASP B CG  1 
ATOM   1619 O  OD1 . ASP B 2 73  ? -33.894 -4.38   4.912   1   49.73 ? 73  ASP B OD1 1 
ATOM   1620 O  OD2 . ASP B 2 73  ? -32.89  -5.439  6.561   1   52.19 ? 73  ASP B OD2 1 
ATOM   1621 N  N   . GLY B 2 74  ? -32.101 -7.783  1.406   1   41.12 ? 74  GLY B N   1 
ATOM   1622 C  CA  . GLY B 2 74  ? -31.374 -8.508  0.369   1   40.98 ? 74  GLY B CA  1 
ATOM   1623 C  C   . GLY B 2 74  ? -31.499 -7.85   -0.994  1   40.76 ? 74  GLY B C   1 
ATOM   1624 O  O   . GLY B 2 74  ? -30.538 -7.822  -1.767  1   40.67 ? 74  GLY B O   1 
ATOM   1625 N  N   . LEU B 2 75  ? -32.675 -7.277  -1.297  1   40.32 ? 75  LEU B N   1 
ATOM   1626 C  CA  . LEU B 2 75  ? -32.885 -6.531  -2.542  1   40.57 ? 75  LEU B CA  1 
ATOM   1627 C  C   . LEU B 2 75  ? -31.999 -5.282  -2.642  1   40.26 ? 75  LEU B C   1 
ATOM   1628 O  O   . LEU B 2 75  ? -31.729 -4.814  -3.745  1   40.68 ? 75  LEU B O   1 
ATOM   1629 C  CB  . LEU B 2 75  ? -34.357 -6.113  -2.706  1   41.44 ? 75  LEU B CB  1 
ATOM   1630 C  CG  . LEU B 2 75  ? -35.378 -7.238  -2.767  1   44.16 ? 75  LEU B CG  1 
ATOM   1631 C  CD1 . LEU B 2 75  ? -36.777 -6.689  -2.899  1   45.04 ? 75  LEU B CD1 1 
ATOM   1632 C  CD2 . LEU B 2 75  ? -35.076 -8.171  -3.911  1   45.51 ? 75  LEU B CD2 1 
ATOM   1633 N  N   . ALA B 2 76  ? -31.587 -4.715  -1.508  1   40.05 ? 76  ALA B N   1 
ATOM   1634 C  CA  . ALA B 2 76  ? -30.719 -3.54   -1.506  1   40.61 ? 76  ALA B CA  1 
ATOM   1635 C  C   . ALA B 2 76  ? -29.238 -3.908  -1.719  1   41.48 ? 76  ALA B C   1 
ATOM   1636 O  O   . ALA B 2 76  ? -28.475 -3.08   -2.194  1   40.52 ? 76  ALA B O   1 
ATOM   1637 C  CB  . ALA B 2 76  ? -30.877 -2.772  -0.201  1   40.14 ? 76  ALA B CB  1 
ATOM   1638 N  N   . HIS B 2 77  ? -28.835 -5.143  -1.383  1   42.94 ? 77  HIS B N   1 
ATOM   1639 C  CA  . HIS B 2 77  ? -27.434 -5.551  -1.495  1   44.51 ? 77  HIS B CA  1 
ATOM   1640 C  C   . HIS B 2 77  ? -27.267 -6.867  -2.251  1   44.4  ? 77  HIS B C   1 
ATOM   1641 O  O   . HIS B 2 77  ? -26.625 -7.785  -1.752  1   43.69 ? 77  HIS B O   1 
ATOM   1642 C  CB  . HIS B 2 77  ? -26.811 -5.64   -0.087  1   46.87 ? 77  HIS B CB  1 
ATOM   1643 C  CG  . HIS B 2 77  ? -26.866 -4.35   0.665   1   51.26 ? 77  HIS B CG  1 
ATOM   1644 N  ND1 . HIS B 2 77  ? -26.316 -3.183  0.142   1   54.04 ? 77  HIS B ND1 1 
ATOM   1645 C  CD2 . HIS B 2 77  ? -27.433 -4.069  1.863   1   52.99 ? 77  HIS B CD2 1 
ATOM   1646 C  CE1 . HIS B 2 77  ? -26.552 -2.236  1.04    1   54.39 ? 77  HIS B CE1 1 
ATOM   1647 N  NE2 . HIS B 2 77  ? -27.217 -2.721  2.095   1   54.45 ? 77  HIS B NE2 1 
ATOM   1648 N  N   . LEU B 2 78  ? -27.807 -6.949  -3.477  1   45.05 ? 78  LEU B N   1 
ATOM   1649 C  CA  . LEU B 2 78  ? -27.732 -8.183  -4.263  1   46.17 ? 78  LEU B CA  1 
ATOM   1650 C  C   . LEU B 2 78  ? -26.297 -8.649  -4.58   1   47.47 ? 78  LEU B C   1 
ATOM   1651 O  O   . LEU B 2 78  ? -26.058 -9.848  -4.687  1   47.82 ? 78  LEU B O   1 
ATOM   1652 C  CB  . LEU B 2 78  ? -28.57  -8.075  -5.536  1   46.38 ? 78  LEU B CB  1 
ATOM   1653 C  CG  . LEU B 2 78  ? -30.081 -8.112  -5.317  1   47.8  ? 78  LEU B CG  1 
ATOM   1654 C  CD1 . LEU B 2 78  ? -30.826 -7.779  -6.595  1   48.22 ? 78  LEU B CD1 1 
ATOM   1655 C  CD2 . LEU B 2 78  ? -30.525 -9.452  -4.75   1   48.22 ? 78  LEU B CD2 1 
ATOM   1656 N  N   . ASP B 2 79  ? -25.349 -7.722  -4.663  1   48.25 ? 79  ASP B N   1 
ATOM   1657 C  CA  . ASP B 2 79  ? -23.956 -8.058  -4.948  1   49.81 ? 79  ASP B CA  1 
ATOM   1658 C  C   . ASP B 2 79  ? -23.109 -8.358  -3.684  1   50.02 ? 79  ASP B C   1 
ATOM   1659 O  O   . ASP B 2 79  ? -21.896 -8.547  -3.796  1   50.83 ? 79  ASP B O   1 
ATOM   1660 C  CB  . ASP B 2 79  ? -23.3   -6.967  -5.816  1   52.81 ? 79  ASP B CB  1 
ATOM   1661 C  CG  . ASP B 2 79  ? -24.039 -6.683  -7.119  1   59.59 ? 79  ASP B CG  1 
ATOM   1662 O  OD1 . ASP B 2 79  ? -24.761 -7.586  -7.606  1   61.01 ? 79  ASP B OD1 1 
ATOM   1663 O  OD2 . ASP B 2 79  ? -23.892 -5.562  -7.653  1   62.2  ? 79  ASP B OD2 1 
ATOM   1664 N  N   . ASN B 2 80  ? -23.731 -8.408  -2.498  1   49.03 ? 80  ASN B N   1 
ATOM   1665 C  CA  . ASN B 2 80  ? -23.014 -8.742  -1.265  1   48.92 ? 80  ASN B CA  1 
ATOM   1666 C  C   . ASN B 2 80  ? -23.969 -9.285  -0.217  1   48.13 ? 80  ASN B C   1 
ATOM   1667 O  O   . ASN B 2 80  ? -24.025 -8.795  0.916   1   47.22 ? 80  ASN B O   1 
ATOM   1668 C  CB  . ASN B 2 80  ? -22.173 -7.588  -0.707  1   50.47 ? 80  ASN B CB  1 
ATOM   1669 C  CG  . ASN B 2 80  ? -21.103 -8.066  0.256   1   53.97 ? 80  ASN B CG  1 
ATOM   1670 O  OD1 . ASN B 2 80  ? -21.07  -9.23   0.687   1   55.29 ? 80  ASN B OD1 1 
ATOM   1671 N  ND2 . ASN B 2 80  ? -20.199 -7.183  0.617   1   55.1  ? 80  ASN B ND2 1 
ATOM   1672 N  N   . LEU B 2 81  ? -24.736 -10.294 -0.616  1   47.96 ? 81  LEU B N   1 
ATOM   1673 C  CA  . LEU B 2 81  ? -25.681 -10.945 0.27    1   48.79 ? 81  LEU B CA  1 
ATOM   1674 C  C   . LEU B 2 81  ? -24.974 -11.63  1.432   1   49.37 ? 81  LEU B C   1 
ATOM   1675 O  O   . LEU B 2 81  ? -25.463 -11.564 2.555   1   49.47 ? 81  LEU B O   1 
ATOM   1676 C  CB  . LEU B 2 81  ? -26.54  -11.934 -0.52   1   48.86 ? 81  LEU B CB  1 
ATOM   1677 C  CG  . LEU B 2 81  ? -27.441 -11.265 -1.546  1   50.38 ? 81  LEU B CG  1 
ATOM   1678 C  CD1 . LEU B 2 81  ? -28.092 -12.281 -2.451  1   51.23 ? 81  LEU B CD1 1 
ATOM   1679 C  CD2 . LEU B 2 81  ? -28.489 -10.409 -0.876  1   50.45 ? 81  LEU B CD2 1 
ATOM   1680 N  N   . LYS B 2 82  ? -23.8   -12.23  1.185   1   49.78 ? 82  LYS B N   1 
ATOM   1681 C  CA  . LYS B 2 82  ? -23.046 -12.91  2.241   1   50.87 ? 82  LYS B CA  1 
ATOM   1682 C  C   . LYS B 2 82  ? -22.692 -11.965 3.383   1   51.34 ? 82  LYS B C   1 
ATOM   1683 O  O   . LYS B 2 82  ? -22.941 -12.29  4.538   1   51.45 ? 82  LYS B O   1 
ATOM   1684 C  CB  . LYS B 2 82  ? -21.786 -13.603 1.686   1   53.13 ? 82  LYS B CB  1 
ATOM   1685 N  N   . GLY B 2 83  ? -22.17  -10.792 3.051   1   51.42 ? 83  GLY B N   1 
ATOM   1686 C  CA  . GLY B 2 83  ? -21.818 -9.798  4.052   1   51.96 ? 83  GLY B CA  1 
ATOM   1687 C  C   . GLY B 2 83  ? -23.026 -9.19   4.734   1   52.12 ? 83  GLY B C   1 
ATOM   1688 O  O   . GLY B 2 83  ? -22.999 -8.952  5.939   1   52.8  ? 83  GLY B O   1 
ATOM   1689 N  N   . THR B 2 84  ? -24.095 -8.94   3.978   1   51.5  ? 84  THR B N   1 
ATOM   1690 C  CA  . THR B 2 84  ? -25.308 -8.341  4.527   1   51.87 ? 84  THR B CA  1 
ATOM   1691 C  C   . THR B 2 84  ? -25.999 -9.275  5.535   1   51.17 ? 84  THR B C   1 
ATOM   1692 O  O   . THR B 2 84  ? -26.361 -8.848  6.629   1   51.59 ? 84  THR B O   1 
ATOM   1693 C  CB  . THR B 2 84  ? -26.24  -7.926  3.391   1   54.54 ? 84  THR B CB  1 
ATOM   1694 O  OG1 . THR B 2 84  ? -25.516 -7.078  2.493   1   56.46 ? 84  THR B OG1 1 
ATOM   1695 C  CG2 . THR B 2 84  ? -27.477 -7.199  3.891   1   55.56 ? 84  THR B CG2 1 
ATOM   1696 N  N   . PHE B 2 85  ? -26.124 -10.555 5.19    1   49.9  ? 85  PHE B N   1 
ATOM   1697 C  CA  . PHE B 2 85  ? -26.774 -11.53  6.058   1   49.11 ? 85  PHE B CA  1 
ATOM   1698 C  C   . PHE B 2 85  ? -25.842 -12.2   7.089   1   48.59 ? 85  PHE B C   1 
ATOM   1699 O  O   . PHE B 2 85  ? -26.276 -13.147 7.734   1   48.2  ? 85  PHE B O   1 
ATOM   1700 C  CB  . PHE B 2 85  ? -27.505 -12.591 5.224   1   48.3  ? 85  PHE B CB  1 
ATOM   1701 C  CG  . PHE B 2 85  ? -28.724 -12.055 4.517   1   48.64 ? 85  PHE B CG  1 
ATOM   1702 C  CD1 . PHE B 2 85  ? -29.884 -11.776 5.215   1   49.7  ? 85  PHE B CD1 1 
ATOM   1703 C  CD2 . PHE B 2 85  ? -28.711 -11.83  3.15    1   48.91 ? 85  PHE B CD2 1 
ATOM   1704 C  CE1 . PHE B 2 85  ? -31.011 -11.287 4.556   1   50.45 ? 85  PHE B CE1 1 
ATOM   1705 C  CE2 . PHE B 2 85  ? -29.824 -11.313 2.503   1   49.56 ? 85  PHE B CE2 1 
ATOM   1706 C  CZ  . PHE B 2 85  ? -30.967 -11.047 3.207   1   49.63 ? 85  PHE B CZ  1 
ATOM   1707 N  N   . ALA B 2 86  ? -24.598 -11.709 7.263   1   48.07 ? 86  ALA B N   1 
ATOM   1708 C  CA  . ALA B 2 86  ? -23.635 -12.295 8.205   1   48.78 ? 86  ALA B CA  1 
ATOM   1709 C  C   . ALA B 2 86  ? -24.181 -12.525 9.629   1   49.13 ? 86  ALA B C   1 
ATOM   1710 O  O   . ALA B 2 86  ? -24.065 -13.638 10.137  1   49.32 ? 86  ALA B O   1 
ATOM   1711 C  CB  . ALA B 2 86  ? -22.349 -11.46  8.257   1   49.08 ? 86  ALA B CB  1 
ATOM   1712 N  N   . THR B 2 87  ? -24.789 -11.497 10.258  1   48.86 ? 87  THR B N   1 
ATOM   1713 C  CA  . THR B 2 87  ? -25.332 -11.607 11.617  1   48.77 ? 87  THR B CA  1 
ATOM   1714 C  C   . THR B 2 87  ? -26.462 -12.638 11.692  1   47.11 ? 87  THR B C   1 
ATOM   1715 O  O   . THR B 2 87  ? -26.447 -13.467 12.602  1   47.02 ? 87  THR B O   1 
ATOM   1716 C  CB  . THR B 2 87  ? -25.731 -10.224 12.169  1   51.16 ? 87  THR B CB  1 
ATOM   1717 O  OG1 . THR B 2 87  ? -24.546 -9.491  12.493  1   53.22 ? 87  THR B OG1 1 
ATOM   1718 C  CG2 . THR B 2 87  ? -26.621 -10.311 13.411  1   51.91 ? 87  THR B CG2 1 
ATOM   1719 N  N   . LEU B 2 88  ? -27.421 -12.597 10.736  1   45.56 ? 88  LEU B N   1 
ATOM   1720 C  CA  . LEU B 2 88  ? -28.541 -13.55  10.686  1   45.02 ? 88  LEU B CA  1 
ATOM   1721 C  C   . LEU B 2 88  ? -28.058 -14.962 10.452  1   43.78 ? 88  LEU B C   1 
ATOM   1722 O  O   . LEU B 2 88  ? -28.636 -15.896 10.988  1   43.74 ? 88  LEU B O   1 
ATOM   1723 C  CB  . LEU B 2 88  ? -29.561 -13.209 9.581   1   45.56 ? 88  LEU B CB  1 
ATOM   1724 C  CG  . LEU B 2 88  ? -30.574 -12.11  9.87    1   47.65 ? 88  LEU B CG  1 
ATOM   1725 C  CD1 . LEU B 2 88  ? -31.578 -11.998 8.714   1   48.44 ? 88  LEU B CD1 1 
ATOM   1726 C  CD2 . LEU B 2 88  ? -31.311 -12.352 11.209  1   47.41 ? 88  LEU B CD2 1 
ATOM   1727 N  N   . SER B 2 89  ? -27.012 -15.128 9.637   1   43.01 ? 89  SER B N   1 
ATOM   1728 C  CA  . SER B 2 89  ? -26.438 -16.434 9.338   1   43.18 ? 89  SER B CA  1 
ATOM   1729 C  C   . SER B 2 89  ? -25.904 -17.06  10.628  1   42.08 ? 89  SER B C   1 
ATOM   1730 O  O   . SER B 2 89  ? -26.199 -18.223 10.927  1   41.18 ? 89  SER B O   1 
ATOM   1731 C  CB  . SER B 2 89  ? -25.323 -16.301 8.305   1   45.54 ? 89  SER B CB  1 
ATOM   1732 O  OG  . SER B 2 89  ? -24.769 -17.579 8.044   1   50.18 ? 89  SER B OG  1 
ATOM   1733 N  N   . GLU B 2 90  ? -25.194 -16.25  11.425  1   41.75 ? 90  GLU B N   1 
ATOM   1734 C  CA  . GLU B 2 90  ? -24.668 -16.669 12.718  1   42.3  ? 90  GLU B CA  1 
ATOM   1735 C  C   . GLU B 2 90  ? -25.815 -17.028 13.67   1   42.06 ? 90  GLU B C   1 
ATOM   1736 O  O   . GLU B 2 90  ? -25.77  -18.071 14.316  1   42.11 ? 90  GLU B O   1 
ATOM   1737 C  CB  . GLU B 2 90  ? -23.768 -15.574 13.315  1   44.02 ? 90  GLU B CB  1 
ATOM   1738 N  N   . LEU B 2 91  ? -26.864 -16.2   13.708  1   41.67 ? 91  LEU B N   1 
ATOM   1739 C  CA  . LEU B 2 91  ? -28.033 -16.467 14.547  1   41.97 ? 91  LEU B CA  1 
ATOM   1740 C  C   . LEU B 2 91  ? -28.723 -17.804 14.181  1   40.75 ? 91  LEU B C   1 
ATOM   1741 O  O   . LEU B 2 91  ? -28.911 -18.649 15.052  1   40.38 ? 91  LEU B O   1 
ATOM   1742 C  CB  . LEU B 2 91  ? -29.037 -15.295 14.46   1   43.14 ? 91  LEU B CB  1 
ATOM   1743 C  CG  . LEU B 2 91  ? -30.382 -15.525 15.174  1   45.63 ? 91  LEU B CG  1 
ATOM   1744 C  CD1 . LEU B 2 91  ? -30.188 -15.594 16.687  1   46.85 ? 91  LEU B CD1 1 
ATOM   1745 C  CD2 . LEU B 2 91  ? -31.382 -14.448 14.824  1   46.17 ? 91  LEU B CD2 1 
ATOM   1746 N  N   . HIS B 2 92  ? -29.103 -17.992 12.905  1   39.81 ? 92  HIS B N   1 
ATOM   1747 C  CA  . HIS B 2 92  ? -29.805 -19.212 12.479  1   39.43 ? 92  HIS B CA  1 
ATOM   1748 C  C   . HIS B 2 92  ? -28.953 -20.492 12.533  1   41.29 ? 92  HIS B C   1 
ATOM   1749 O  O   . HIS B 2 92  ? -29.515 -21.569 12.674  1   41.09 ? 92  HIS B O   1 
ATOM   1750 C  CB  . HIS B 2 92  ? -30.42  -19.037 11.078  1   38.14 ? 92  HIS B CB  1 
ATOM   1751 C  CG  . HIS B 2 92  ? -31.543 -18.045 11.009  1   37.79 ? 92  HIS B CG  1 
ATOM   1752 N  ND1 . HIS B 2 92  ? -31.303 -16.675 10.979  1   38.73 ? 92  HIS B ND1 1 
ATOM   1753 C  CD2 . HIS B 2 92  ? -32.88  -18.255 10.913  1   38.21 ? 92  HIS B CD2 1 
ATOM   1754 C  CE1 . HIS B 2 92  ? -32.494 -16.103 10.906  1   38.87 ? 92  HIS B CE1 1 
ATOM   1755 N  NE2 . HIS B 2 92  ? -33.474 -17.008 10.876  1   39.05 ? 92  HIS B NE2 1 
ATOM   1756 N  N   . CYS B 2 93  ? -27.615 -20.394 12.41   1   43.28 ? 93  CYS B N   1 
ATOM   1757 C  CA  . CYS B 2 93  ? -26.755 -21.581 12.461  1   45.66 ? 93  CYS B CA  1 
ATOM   1758 C  C   . CYS B 2 93  ? -26.232 -21.855 13.867  1   46.65 ? 93  CYS B C   1 
ATOM   1759 O  O   . CYS B 2 93  ? -26.602 -22.861 14.469  1   46.4  ? 93  CYS B O   1 
ATOM   1760 C  CB  . CYS B 2 93  ? -25.62  -21.515 11.429  1   48.15 ? 93  CYS B CB  1 
ATOM   1761 S  SG  . CYS B 2 93  ? -24.336 -22.799 11.623  1   56.8  ? 93  CYS B SG  1 
ATOM   1762 N  N   . ASP B 2 94  ? -25.357 -20.975 14.384  1   47.54 ? 94  ASP B N   1 
ATOM   1763 C  CA  . ASP B 2 94  ? -24.737 -21.185 15.678  1   49.21 ? 94  ASP B CA  1 
ATOM   1764 C  C   . ASP B 2 94  ? -25.729 -21.205 16.824  1   49.47 ? 94  ASP B C   1 
ATOM   1765 O  O   . ASP B 2 94  ? -25.525 -21.968 17.77   1   49.82 ? 94  ASP B O   1 
ATOM   1766 C  CB  . ASP B 2 94  ? -23.62  -20.151 15.946  1   52.41 ? 94  ASP B CB  1 
ATOM   1767 C  CG  . ASP B 2 94  ? -22.621 -19.972 14.81   1   60.02 ? 94  ASP B CG  1 
ATOM   1768 O  OD1 . ASP B 2 94  ? -22.666 -20.765 13.842  1   61.36 ? 94  ASP B OD1 1 
ATOM   1769 O  OD2 . ASP B 2 94  ? -21.788 -19.039 14.894  1   63.94 ? 94  ASP B OD2 1 
ATOM   1770 N  N   . LYS B 2 95  ? -26.788 -20.371 16.769  1   48.88 ? 95  LYS B N   1 
ATOM   1771 C  CA  . LYS B 2 95  ? -27.733 -20.329 17.888  1   48.82 ? 95  LYS B CA  1 
ATOM   1772 C  C   . LYS B 2 95  ? -28.98  -21.165 17.68   1   47.57 ? 95  LYS B C   1 
ATOM   1773 O  O   . LYS B 2 95  ? -29.366 -21.911 18.585  1   47.84 ? 95  LYS B O   1 
ATOM   1774 C  CB  . LYS B 2 95  ? -28.109 -18.889 18.272  1   51.33 ? 95  LYS B CB  1 
ATOM   1775 C  CG  . LYS B 2 95  ? -28.934 -18.829 19.552  1   56.33 ? 95  LYS B CG  1 
ATOM   1776 C  CD  . LYS B 2 95  ? -29.703 -17.532 19.692  1   61.21 ? 95  LYS B CD  1 
ATOM   1777 C  CE  . LYS B 2 95  ? -30.579 -17.554 20.919  1   65.01 ? 95  LYS B CE  1 
ATOM   1778 N  NZ  . LYS B 2 95  ? -29.781 -17.781 22.153  1   66.52 ? 95  LYS B NZ  1 
ATOM   1779 N  N   . LEU B 2 96  ? -29.618 -21.048 16.503  1   45.91 ? 96  LEU B N   1 
ATOM   1780 C  CA  . LEU B 2 96  ? -30.881 -21.748 16.272  1   44.54 ? 96  LEU B CA  1 
ATOM   1781 C  C   . LEU B 2 96  ? -30.765 -23.153 15.666  1   42.75 ? 96  LEU B C   1 
ATOM   1782 O  O   . LEU B 2 96  ? -31.723 -23.917 15.762  1   43.23 ? 96  LEU B O   1 
ATOM   1783 C  CB  . LEU B 2 96  ? -31.806 -20.88  15.424  1   44.71 ? 96  LEU B CB  1 
ATOM   1784 C  CG  . LEU B 2 96  ? -32.094 -19.502 16.003  1   46.92 ? 96  LEU B CG  1 
ATOM   1785 C  CD1 . LEU B 2 96  ? -32.717 -18.585 14.959  1   47.89 ? 96  LEU B CD1 1 
ATOM   1786 C  CD2 . LEU B 2 96  ? -32.934 -19.602 17.277  1   47.57 ? 96  LEU B CD2 1 
ATOM   1787 N  N   . HIS B 2 97  ? -29.632 -23.488 15.036  1   40.48 ? 97  HIS B N   1 
ATOM   1788 C  CA  . HIS B 2 97  ? -29.419 -24.793 14.407  1   39.25 ? 97  HIS B CA  1 
ATOM   1789 C  C   . HIS B 2 97  ? -30.459 -25.118 13.326  1   36.6  ? 97  HIS B C   1 
ATOM   1790 O  O   . HIS B 2 97  ? -30.929 -26.255 13.233  1   36.17 ? 97  HIS B O   1 
ATOM   1791 C  CB  . HIS B 2 97  ? -29.31  -25.922 15.446  1   40.93 ? 97  HIS B CB  1 
ATOM   1792 C  CG  . HIS B 2 97  ? -28.238 -25.66  16.456  1   43.95 ? 97  HIS B CG  1 
ATOM   1793 N  ND1 . HIS B 2 97  ? -26.947 -25.347 16.065  1   46.58 ? 97  HIS B ND1 1 
ATOM   1794 C  CD2 . HIS B 2 97  ? -28.309 -25.622 17.808  1   45.49 ? 97  HIS B CD2 1 
ATOM   1795 C  CE1 . HIS B 2 97  ? -26.276 -25.12  17.188  1   47.23 ? 97  HIS B CE1 1 
ATOM   1796 N  NE2 . HIS B 2 97  ? -27.051 -25.286 18.262  1   46.74 ? 97  HIS B NE2 1 
ATOM   1797 N  N   . VAL B 2 98  ? -30.807 -24.117 12.513  1   34.08 ? 98  VAL B N   1 
ATOM   1798 C  CA  . VAL B 2 98  ? -31.755 -24.343 11.434  1   31.96 ? 98  VAL B CA  1 
ATOM   1799 C  C   . VAL B 2 98  ? -31.01  -24.97  10.275  1   31.41 ? 98  VAL B C   1 
ATOM   1800 O  O   . VAL B 2 98  ? -30.092 -24.35  9.715   1   31.27 ? 98  VAL B O   1 
ATOM   1801 C  CB  . VAL B 2 98  ? -32.463 -23.054 10.991  1   31.22 ? 98  VAL B CB  1 
ATOM   1802 C  CG1 . VAL B 2 98  ? -33.475 -23.368 9.879   1   30.54 ? 98  VAL B CG1 1 
ATOM   1803 C  CG2 . VAL B 2 98  ? -33.14  -22.37  12.184  1   31.26 ? 98  VAL B CG2 1 
ATOM   1804 N  N   . ASP B 2 99  ? -31.39  -26.198 9.877   1   30.63 ? 99  ASP B N   1 
ATOM   1805 C  CA  . ASP B 2 99  ? -30.761 -26.819 8.711   1   30.16 ? 99  ASP B CA  1 
ATOM   1806 C  C   . ASP B 2 99  ? -30.985 -25.92  7.471   1   29.71 ? 99  ASP B C   1 
ATOM   1807 O  O   . ASP B 2 99  ? -32.096 -25.437 7.266   1   29.04 ? 99  ASP B O   1 
ATOM   1808 C  CB  . ASP B 2 99  ? -31.312 -28.203 8.438   1   30.63 ? 99  ASP B CB  1 
ATOM   1809 C  CG  . ASP B 2 99  ? -30.486 -28.85  7.362   1   34.34 ? 99  ASP B CG  1 
ATOM   1810 O  OD1 . ASP B 2 99  ? -29.38  -29.321 7.673   1   35.64 ? 99  ASP B OD1 1 
ATOM   1811 O  OD2 . ASP B 2 99  ? -30.916 -28.825 6.201   1   36.25 ? 99  ASP B OD2 1 
ATOM   1812 N  N   . PRO B 2 100 ? -29.924 -25.623 6.707   1   30.18 ? 100 PRO B N   1 
ATOM   1813 C  CA  . PRO B 2 100 ? -30.073 -24.683 5.583   1   29.85 ? 100 PRO B CA  1 
ATOM   1814 C  C   . PRO B 2 100 ? -31.091 -25.049 4.487   1   28.29 ? 100 PRO B C   1 
ATOM   1815 O  O   . PRO B 2 100 ? -31.549 -24.158 3.764   1   27.7  ? 100 PRO B O   1 
ATOM   1816 C  CB  . PRO B 2 100 ? -28.651 -24.547 5.015   1   31.58 ? 100 PRO B CB  1 
ATOM   1817 C  CG  . PRO B 2 100 ? -27.86  -25.641 5.615   1   31.9  ? 100 PRO B CG  1 
ATOM   1818 C  CD  . PRO B 2 100 ? -28.523 -26.048 6.899   1   30.13 ? 100 PRO B CD  1 
ATOM   1819 N  N   . GLU B 2 101 ? -31.505 -26.32  4.391   1   27    ? 101 GLU B N   1 
ATOM   1820 C  CA  . GLU B 2 101 ? -32.537 -26.723 3.441   1   27.06 ? 101 GLU B CA  1 
ATOM   1821 C  C   . GLU B 2 101 ? -33.856 -25.97  3.739   1   25.78 ? 101 GLU B C   1 
ATOM   1822 O  O   . GLU B 2 101 ? -34.562 -25.608 2.818   1   25.7  ? 101 GLU B O   1 
ATOM   1823 C  CB  . GLU B 2 101 ? -32.73  -28.268 3.474   1   29.76 ? 101 GLU B CB  1 
ATOM   1824 C  CG  . GLU B 2 101 ? -33.866 -28.794 2.608   1   34.46 ? 101 GLU B CG  1 
ATOM   1825 C  CD  . GLU B 2 101 ? -33.707 -28.564 1.117   1   41.32 ? 101 GLU B CD  1 
ATOM   1826 O  OE1 . GLU B 2 101 ? -32.581 -28.226 0.684   1   42.92 ? 101 GLU B OE1 1 
ATOM   1827 O  OE2 . GLU B 2 101 ? -34.704 -28.733 0.379   1   43.11 ? 101 GLU B OE2 1 
ATOM   1828 N  N   . ASN B 2 102 ? -34.125 -25.635 5.018   1   24.22 ? 102 ASN B N   1 
ATOM   1829 C  CA  . ASN B 2 102 ? -35.322 -24.866 5.383   1   23.35 ? 102 ASN B CA  1 
ATOM   1830 C  C   . ASN B 2 102 ? -35.332 -23.438 4.818   1   23.92 ? 102 ASN B C   1 
ATOM   1831 O  O   . ASN B 2 102 ? -36.414 -22.886 4.564   1   23.99 ? 102 ASN B O   1 
ATOM   1832 C  CB  . ASN B 2 102 ? -35.499 -24.851 6.91    1   22.22 ? 102 ASN B CB  1 
ATOM   1833 C  CG  . ASN B 2 102 ? -35.676 -26.283 7.397   1   24.58 ? 102 ASN B CG  1 
ATOM   1834 O  OD1 . ASN B 2 102 ? -36.617 -26.989 6.991   1   22.79 ? 102 ASN B OD1 1 
ATOM   1835 N  ND2 . ASN B 2 102 ? -34.734 -26.743 8.202   1   24.57 ? 102 ASN B ND2 1 
ATOM   1836 N  N   . PHE B 2 103 ? -34.139 -22.843 4.59    1   23.72 ? 103 PHE B N   1 
ATOM   1837 C  CA  . PHE B 2 103 ? -34.047 -21.496 3.987   1   24.18 ? 103 PHE B CA  1 
ATOM   1838 C  C   . PHE B 2 103 ? -34.546 -21.547 2.531   1   24.17 ? 103 PHE B C   1 
ATOM   1839 O  O   . PHE B 2 103 ? -35.242 -20.625 2.066   1   24.34 ? 103 PHE B O   1 
ATOM   1840 C  CB  . PHE B 2 103 ? -32.581 -21.022 3.979   1   25.15 ? 103 PHE B CB  1 
ATOM   1841 C  CG  . PHE B 2 103 ? -31.937 -20.984 5.341   1   27.22 ? 103 PHE B CG  1 
ATOM   1842 C  CD1 . PHE B 2 103 ? -32.651 -20.571 6.449   1   29.2  ? 103 PHE B CD1 1 
ATOM   1843 C  CD2 . PHE B 2 103 ? -30.58  -21.237 5.492   1   28.19 ? 103 PHE B CD2 1 
ATOM   1844 C  CE1 . PHE B 2 103 ? -32.043 -20.512 7.71    1   30.37 ? 103 PHE B CE1 1 
ATOM   1845 C  CE2 . PHE B 2 103 ? -29.974 -21.152 6.737   1   29.51 ? 103 PHE B CE2 1 
ATOM   1846 C  CZ  . PHE B 2 103 ? -30.712 -20.806 7.843   1   29.72 ? 103 PHE B CZ  1 
ATOM   1847 N  N   . ARG B 2 104 ? -34.174 -22.615 1.806   1   23.42 ? 104 ARG B N   1 
ATOM   1848 C  CA  . ARG B 2 104 ? -34.645 -22.811 0.431   1   24.28 ? 104 ARG B CA  1 
ATOM   1849 C  C   . ARG B 2 104 ? -36.181 -23.002 0.433   1   23.72 ? 104 ARG B C   1 
ATOM   1850 O  O   . ARG B 2 104 ? -36.886 -22.489 -0.452  1   23.49 ? 104 ARG B O   1 
ATOM   1851 C  CB  . ARG B 2 104 ? -33.975 -24.054 -0.183  1   26.46 ? 104 ARG B CB  1 
ATOM   1852 C  CG  . ARG B 2 104 ? -34.156 -24.13  -1.713  1   33.31 ? 104 ARG B CG  1 
ATOM   1853 C  CD  . ARG B 2 104 ? -33.676 -25.442 -2.361  1   37.74 ? 104 ARG B CD  1 
ATOM   1854 N  NE  . ARG B 2 104 ? -34.455 -26.588 -1.888  1   43.17 ? 104 ARG B NE  1 
ATOM   1855 C  CZ  . ARG B 2 104 ? -35.581 -27.019 -2.457  1   45.76 ? 104 ARG B CZ  1 
ATOM   1856 N  NH1 . ARG B 2 104 ? -36.055 -26.422 -3.546  1   46.96 ? 104 ARG B NH1 1 
ATOM   1857 N  NH2 . ARG B 2 104 ? -36.234 -28.054 -1.948  1   43.8  ? 104 ARG B NH2 1 
ATOM   1858 N  N   . LEU B 2 105 ? -36.694 -23.771 1.402   1   22.96 ? 105 LEU B N   1 
ATOM   1859 C  CA  . LEU B 2 105 ? -38.143 -24.032 1.5     1   23    ? 105 LEU B CA  1 
ATOM   1860 C  C   . LEU B 2 105 ? -38.909 -22.738 1.774   1   22.72 ? 105 LEU B C   1 
ATOM   1861 O  O   . LEU B 2 105 ? -39.898 -22.465 1.089   1   23.33 ? 105 LEU B O   1 
ATOM   1862 C  CB  . LEU B 2 105 ? -38.445 -25.098 2.578   1   22.81 ? 105 LEU B CB  1 
ATOM   1863 C  CG  . LEU B 2 105 ? -37.818 -26.487 2.306   1   23.03 ? 105 LEU B CG  1 
ATOM   1864 C  CD1 . LEU B 2 105 ? -38.135 -27.458 3.426   1   23.74 ? 105 LEU B CD1 1 
ATOM   1865 C  CD2 . LEU B 2 105 ? -38.33  -27.07  0.98    1   24.1  ? 105 LEU B CD2 1 
ATOM   1866 N  N   . LEU B 2 106 ? -38.422 -21.911 2.709   1   21.77 ? 106 LEU B N   1 
ATOM   1867 C  CA  . LEU B 2 106 ? -39.051 -20.631 2.985   1   21.66 ? 106 LEU B CA  1 
ATOM   1868 C  C   . LEU B 2 106 ? -39.038 -19.698 1.745   1   21.96 ? 106 LEU B C   1 
ATOM   1869 O  O   . LEU B 2 106 ? -40.052 -19.051 1.455   1   22.09 ? 106 LEU B O   1 
ATOM   1870 C  CB  . LEU B 2 106 ? -38.398 -19.956 4.205   1   22.2  ? 106 LEU B CB  1 
ATOM   1871 C  CG  . LEU B 2 106 ? -38.896 -18.576 4.582   1   24.54 ? 106 LEU B CG  1 
ATOM   1872 C  CD1 . LEU B 2 106 ? -40.42  -18.561 4.772   1   25.11 ? 106 LEU B CD1 1 
ATOM   1873 C  CD2 . LEU B 2 106 ? -38.296 -18.181 5.936   1   25.84 ? 106 LEU B CD2 1 
ATOM   1874 N  N   . GLY B 2 107 ? -37.946 -19.686 0.989   1   21.65 ? 107 GLY B N   1 
ATOM   1875 C  CA  . GLY B 2 107 ? -37.884 -18.866 -0.226  1   22.08 ? 107 GLY B CA  1 
ATOM   1876 C  C   . GLY B 2 107 ? -38.913 -19.322 -1.25   1   22.93 ? 107 GLY B C   1 
ATOM   1877 O  O   . GLY B 2 107 ? -39.558 -18.495 -1.903  1   24.71 ? 107 GLY B O   1 
ATOM   1878 N  N   . ASN B 2 108 ? -39.129 -20.64  -1.36   1   21.49 ? 108 ASN B N   1 
ATOM   1879 C  CA  . ASN B 2 108 ? -40.088 -21.17  -2.323  1   22.91 ? 108 ASN B CA  1 
ATOM   1880 C  C   . ASN B 2 108 ? -41.543 -20.948 -1.872  1   22.07 ? 108 ASN B C   1 
ATOM   1881 O  O   . ASN B 2 108 ? -42.417 -20.645 -2.693  1   22.21 ? 108 ASN B O   1 
ATOM   1882 C  CB  . ASN B 2 108 ? -39.767 -22.626 -2.654  1   25.69 ? 108 ASN B CB  1 
ATOM   1883 C  CG  . ASN B 2 108 ? -38.599 -22.736 -3.621  1   31.69 ? 108 ASN B CG  1 
ATOM   1884 O  OD1 . ASN B 2 108 ? -38.148 -21.744 -4.25   1   31.38 ? 108 ASN B OD1 1 
ATOM   1885 N  ND2 . ASN B 2 108 ? -38.093 -23.951 -3.76   1   34.69 ? 108 ASN B ND2 1 
ATOM   1886 N  N   . VAL B 2 109 ? -41.791 -20.999 -0.572  1   21    ? 109 VAL B N   1 
ATOM   1887 C  CA  . VAL B 2 109 ? -43.114 -20.678 -0.039  1   20.96 ? 109 VAL B CA  1 
ATOM   1888 C  C   . VAL B 2 109 ? -43.379 -19.183 -0.285  1   20.77 ? 109 VAL B C   1 
ATOM   1889 O  O   . VAL B 2 109 ? -44.488 -18.821 -0.69   1   21.29 ? 109 VAL B O   1 
ATOM   1890 C  CB  . VAL B 2 109 ? -43.242 -21.028 1.462   1   23.2  ? 109 VAL B CB  1 
ATOM   1891 C  CG1 . VAL B 2 109 ? -44.55  -20.484 1.997   1   24.41 ? 109 VAL B CG1 1 
ATOM   1892 C  CG2 . VAL B 2 109 ? -43.178 -22.544 1.665   1   24.11 ? 109 VAL B CG2 1 
ATOM   1893 N  N   . LEU B 2 110 ? -42.359 -18.318 -0.097  1   20.06 ? 110 LEU B N   1 
ATOM   1894 C  CA  . LEU B 2 110 ? -42.544 -16.878 -0.378  1   21.47 ? 110 LEU B CA  1 
ATOM   1895 C  C   . LEU B 2 110 ? -42.897 -16.675 -1.891  1   22.17 ? 110 LEU B C   1 
ATOM   1896 O  O   . LEU B 2 110 ? -43.805 -15.919 -2.2    1   22.24 ? 110 LEU B O   1 
ATOM   1897 C  CB  . LEU B 2 110 ? -41.288 -16.087 -0.013  1   22.5  ? 110 LEU B CB  1 
ATOM   1898 C  CG  . LEU B 2 110 ? -41.331 -14.588 -0.422  1   24.91 ? 110 LEU B CG  1 
ATOM   1899 C  CD1 . LEU B 2 110 ? -42.466 -13.853 0.288   1   24.04 ? 110 LEU B CD1 1 
ATOM   1900 C  CD2 . LEU B 2 110 ? -39.982 -13.9   -0.183  1   27.03 ? 110 LEU B CD2 1 
ATOM   1901 N  N   . VAL B 2 111 ? -42.244 -17.427 -2.807  1   21.66 ? 111 VAL B N   1 
ATOM   1902 C  CA  . VAL B 2 111 ? -42.585 -17.337 -4.238  1   22.41 ? 111 VAL B CA  1 
ATOM   1903 C  C   . VAL B 2 111 ? -44.05  -17.75  -4.452  1   22.58 ? 111 VAL B C   1 
ATOM   1904 O  O   . VAL B 2 111 ? -44.764 -17.071 -5.169  1   23.79 ? 111 VAL B O   1 
ATOM   1905 C  CB  . VAL B 2 111 ? -41.615 -18.148 -5.111  1   23.17 ? 111 VAL B CB  1 
ATOM   1906 C  CG1 . VAL B 2 111 ? -42.15  -18.266 -6.549  1   24.12 ? 111 VAL B CG1 1 
ATOM   1907 C  CG2 . VAL B 2 111 ? -40.228 -17.501 -5.1    1   24.1  ? 111 VAL B CG2 1 
ATOM   1908 N  N   . CYS B 2 112 ? -44.508 -18.828 -3.792  1   22.29 ? 112 CYS B N   1 
ATOM   1909 C  CA  . CYS B 2 112 ? -45.912 -19.265 -3.885  1   22.1  ? 112 CYS B CA  1 
ATOM   1910 C  C   . CYS B 2 112 ? -46.881 -18.178 -3.387  1   22.22 ? 112 CYS B C   1 
ATOM   1911 O  O   . CYS B 2 112 ? -47.961 -18.035 -3.948  1   22.56 ? 112 CYS B O   1 
ATOM   1912 C  CB  . CYS B 2 112 ? -46.138 -20.565 -3.122  1   22.18 ? 112 CYS B CB  1 
ATOM   1913 S  SG  . CYS B 2 112 ? -45.341 -22.029 -3.853  1   24.39 ? 112 CYS B SG  1 
ATOM   1914 N  N   . VAL B 2 113 ? -46.547 -17.506 -2.289  1   22.32 ? 113 VAL B N   1 
ATOM   1915 C  CA  . VAL B 2 113 ? -47.396 -16.459 -1.703  1   23.37 ? 113 VAL B CA  1 
ATOM   1916 C  C   . VAL B 2 113 ? -47.449 -15.278 -2.682  1   24.07 ? 113 VAL B C   1 
ATOM   1917 O  O   . VAL B 2 113 ? -48.518 -14.707 -2.879  1   24.87 ? 113 VAL B O   1 
ATOM   1918 C  CB  . VAL B 2 113 ? -46.916 -16.041 -0.286  1   24.3  ? 113 VAL B CB  1 
ATOM   1919 C  CG1 . VAL B 2 113 ? -47.598 -14.746 0.199   1   26.26 ? 113 VAL B CG1 1 
ATOM   1920 C  CG2 . VAL B 2 113 ? -47.146 -17.172 0.715   1   23.26 ? 113 VAL B CG2 1 
ATOM   1921 N  N   . LEU B 2 114 ? -46.322 -14.923 -3.304  1   24.06 ? 114 LEU B N   1 
ATOM   1922 C  CA  . LEU B 2 114 ? -46.308 -13.823 -4.295  1   25.43 ? 114 LEU B CA  1 
ATOM   1923 C  C   . LEU B 2 114 ? -47.195 -14.177 -5.481  1   26.51 ? 114 LEU B C   1 
ATOM   1924 O  O   . LEU B 2 114 ? -47.981 -13.342 -5.924  1   28.1  ? 114 LEU B O   1 
ATOM   1925 C  CB  . LEU B 2 114 ? -44.874 -13.533 -4.774  1   25.62 ? 114 LEU B CB  1 
ATOM   1926 C  CG  . LEU B 2 114 ? -43.956 -12.899 -3.737  1   27.07 ? 114 LEU B CG  1 
ATOM   1927 C  CD1 . LEU B 2 114 ? -42.563 -12.752 -4.284  1   27.14 ? 114 LEU B CD1 1 
ATOM   1928 C  CD2 . LEU B 2 114 ? -44.508 -11.547 -3.27   1   28.59 ? 114 LEU B CD2 1 
ATOM   1929 N  N   . ALA B 2 115 ? -47.138 -15.447 -5.932  1   25.88 ? 115 ALA B N   1 
ATOM   1930 C  CA  . ALA B 2 115 ? -47.962 -15.952 -7.034  1   26.89 ? 115 ALA B CA  1 
ATOM   1931 C  C   . ALA B 2 115 ? -49.462 -15.905 -6.627  1   27.47 ? 115 ALA B C   1 
ATOM   1932 O  O   . ALA B 2 115 ? -50.32  -15.527 -7.419  1   27.93 ? 115 ALA B O   1 
ATOM   1933 C  CB  . ALA B 2 115 ? -47.551 -17.393 -7.356  1   27    ? 115 ALA B CB  1 
ATOM   1934 N  N   . HIS B 2 116 ? -49.766 -16.302 -5.399  1   26.78 ? 116 HIS B N   1 
ATOM   1935 C  CA  . HIS B 2 116 ? -51.118 -16.318 -4.885  1   27.64 ? 116 HIS B CA  1 
ATOM   1936 C  C   . HIS B 2 116 ? -51.693 -14.9   -4.803  1   29.35 ? 116 HIS B C   1 
ATOM   1937 O  O   . HIS B 2 116 ? -52.846 -14.696 -5.148  1   30    ? 116 HIS B O   1 
ATOM   1938 C  CB  . HIS B 2 116 ? -51.108 -16.992 -3.497  1   28.3  ? 116 HIS B CB  1 
ATOM   1939 C  CG  . HIS B 2 116 ? -52.458 -17.378 -3.005  1   29.34 ? 116 HIS B CG  1 
ATOM   1940 N  ND1 . HIS B 2 116 ? -52.788 -17.268 -1.681  1   31.5  ? 116 HIS B ND1 1 
ATOM   1941 C  CD2 . HIS B 2 116 ? -53.492 -17.935 -3.667  1   30.77 ? 116 HIS B CD2 1 
ATOM   1942 C  CE1 . HIS B 2 116 ? -54.03  -17.706 -1.582  1   31.99 ? 116 HIS B CE1 1 
ATOM   1943 N  NE2 . HIS B 2 116 ? -54.491 -18.122 -2.75   1   31.64 ? 116 HIS B NE2 1 
ATOM   1944 N  N   . HIS B 2 117 ? -50.877 -13.917 -4.436  1   30.89 ? 117 HIS B N   1 
ATOM   1945 C  CA  . HIS B 2 117 ? -51.33  -12.531 -4.299  1   32.61 ? 117 HIS B CA  1 
ATOM   1946 C  C   . HIS B 2 117 ? -51.438 -11.814 -5.645  1   34.13 ? 117 HIS B C   1 
ATOM   1947 O  O   . HIS B 2 117 ? -52.382 -11.06  -5.865  1   34.28 ? 117 HIS B O   1 
ATOM   1948 C  CB  . HIS B 2 117 ? -50.349 -11.747 -3.411  1   34.23 ? 117 HIS B CB  1 
ATOM   1949 C  CG  . HIS B 2 117 ? -50.613 -11.867 -1.94   1   38.95 ? 117 HIS B CG  1 
ATOM   1950 N  ND1 . HIS B 2 117 ? -51.148 -10.807 -1.211  1   41.83 ? 117 HIS B ND1 1 
ATOM   1951 C  CD2 . HIS B 2 117 ? -50.456 -12.928 -1.116  1   39.98 ? 117 HIS B CD2 1 
ATOM   1952 C  CE1 . HIS B 2 117 ? -51.27  -11.255 0.032   1   42.54 ? 117 HIS B CE1 1 
ATOM   1953 N  NE2 . HIS B 2 117 ? -50.86  -12.524 0.136   1   41.63 ? 117 HIS B NE2 1 
ATOM   1954 N  N   . PHE B 2 118 ? -50.474 -12.045 -6.545  1   34.27 ? 118 PHE B N   1 
ATOM   1955 C  CA  . PHE B 2 118 ? -50.408 -11.309 -7.8    1   34.52 ? 118 PHE B CA  1 
ATOM   1956 C  C   . PHE B 2 118 ? -51.062 -11.998 -9.011  1   34.67 ? 118 PHE B C   1 
ATOM   1957 O  O   . PHE B 2 118 ? -51.274 -11.346 -10.024 1   34.62 ? 118 PHE B O   1 
ATOM   1958 C  CB  . PHE B 2 118 ? -48.95  -10.933 -8.099  1   34.09 ? 118 PHE B CB  1 
ATOM   1959 C  CG  . PHE B 2 118 ? -48.456 -9.842  -7.179  1   34.76 ? 118 PHE B CG  1 
ATOM   1960 C  CD1 . PHE B 2 118 ? -48.806 -8.519  -7.396  1   36.69 ? 118 PHE B CD1 1 
ATOM   1961 C  CD2 . PHE B 2 118 ? -47.665 -10.141 -6.08   1   35.34 ? 118 PHE B CD2 1 
ATOM   1962 C  CE1 . PHE B 2 118 ? -48.365 -7.517  -6.54   1   37.79 ? 118 PHE B CE1 1 
ATOM   1963 C  CE2 . PHE B 2 118 ? -47.238 -9.14   -5.219  1   36.47 ? 118 PHE B CE2 1 
ATOM   1964 C  CZ  . PHE B 2 118 ? -47.603 -7.831  -5.447  1   37.14 ? 118 PHE B CZ  1 
ATOM   1965 N  N   . GLY B 2 119 ? -51.384 -13.284 -8.906  1   35.03 ? 119 GLY B N   1 
ATOM   1966 C  CA  . GLY B 2 119 ? -52.024 -14.004 -10.006 1   35.67 ? 119 GLY B CA  1 
ATOM   1967 C  C   . GLY B 2 119 ? -51.303 -13.927 -11.335 1   36.35 ? 119 GLY B C   1 
ATOM   1968 O  O   . GLY B 2 119 ? -50.091 -14.147 -11.408 1   36.08 ? 119 GLY B O   1 
ATOM   1969 N  N   . LYS B 2 120 ? -52.035 -13.537 -12.387 1   37.17 ? 120 LYS B N   1 
ATOM   1970 C  CA  . LYS B 2 120 ? -51.51  -13.414 -13.742 1   38.52 ? 120 LYS B CA  1 
ATOM   1971 C  C   . LYS B 2 120 ? -50.341 -12.444 -13.866 1   38.2  ? 120 LYS B C   1 
ATOM   1972 O  O   . LYS B 2 120 ? -49.594 -12.515 -14.837 1   38.51 ? 120 LYS B O   1 
ATOM   1973 C  CB  . LYS B 2 120 ? -52.625 -12.985 -14.708 1   42.53 ? 120 LYS B CB  1 
ATOM   1974 C  CG  . LYS B 2 120 ? -53.898 -13.825 -14.623 1   49.58 ? 120 LYS B CG  1 
ATOM   1975 C  CD  . LYS B 2 120 ? -53.69  -15.322 -14.827 1   55.94 ? 120 LYS B CD  1 
ATOM   1976 C  CE  . LYS B 2 120 ? -55.01  -16.003 -15.131 1   61.2  ? 120 LYS B CE  1 
ATOM   1977 N  NZ  . LYS B 2 120 ? -55.863 -16.146 -13.914 1   64.39 ? 120 LYS B NZ  1 
ATOM   1978 N  N   . GLU B 2 121 ? -50.211 -11.503 -12.927 1   36.58 ? 121 GLU B N   1 
ATOM   1979 C  CA  . GLU B 2 121 ? -49.107 -10.547 -12.931 1   36.1  ? 121 GLU B CA  1 
ATOM   1980 C  C   . GLU B 2 121 ? -47.778 -11.227 -12.515 1   34.06 ? 121 GLU B C   1 
ATOM   1981 O  O   . GLU B 2 121 ? -46.704 -10.753 -12.873 1   34.49 ? 121 GLU B O   1 
ATOM   1982 C  CB  . GLU B 2 121 ? -49.452 -9.34   -12.036 1   39.75 ? 121 GLU B CB  1 
ATOM   1983 C  CG  . GLU B 2 121 ? -48.427 -8.22   -12.05  1   48.08 ? 121 GLU B CG  1 
ATOM   1984 C  CD  . GLU B 2 121 ? -48.838 -6.96   -11.306 1   57.49 ? 121 GLU B CD  1 
ATOM   1985 O  OE1 . GLU B 2 121 ? -50.047 -6.806  -11.017 1   56.62 ? 121 GLU B OE1 1 
ATOM   1986 O  OE2 . GLU B 2 121 ? -47.946 -6.13   -11.007 1   61.99 ? 121 GLU B OE2 1 
ATOM   1987 N  N   . PHE B 2 122 ? -47.84  -12.357 -11.797 1   32.44 ? 122 PHE B N   1 
ATOM   1988 C  CA  . PHE B 2 122 ? -46.635 -13.092 -11.416 1   30.63 ? 122 PHE B CA  1 
ATOM   1989 C  C   . PHE B 2 122 ? -46.285 -13.994 -12.594 1   29.9  ? 122 PHE B C   1 
ATOM   1990 O  O   . PHE B 2 122 ? -46.434 -15.205 -12.526 1   29.88 ? 122 PHE B O   1 
ATOM   1991 C  CB  . PHE B 2 122 ? -46.874 -13.909 -10.137 1   29.12 ? 122 PHE B CB  1 
ATOM   1992 C  CG  . PHE B 2 122 ? -45.579 -14.298 -9.47   1   27.77 ? 122 PHE B CG  1 
ATOM   1993 C  CD1 . PHE B 2 122 ? -44.789 -13.347 -8.848  1   27.91 ? 122 PHE B CD1 1 
ATOM   1994 C  CD2 . PHE B 2 122 ? -45.157 -15.621 -9.454  1   27.1  ? 122 PHE B CD2 1 
ATOM   1995 C  CE1 . PHE B 2 122 ? -43.607 -13.711 -8.208  1   28.22 ? 122 PHE B CE1 1 
ATOM   1996 C  CE2 . PHE B 2 122 ? -43.968 -15.979 -8.833  1   26.61 ? 122 PHE B CE2 1 
ATOM   1997 C  CZ  . PHE B 2 122 ? -43.191 -15.021 -8.236  1   27.26 ? 122 PHE B CZ  1 
ATOM   1998 N  N   . THR B 2 123 ? -45.877 -13.391 -13.688 1   29.76 ? 123 THR B N   1 
ATOM   1999 C  CA  . THR B 2 123 ? -45.584 -14.073 -14.951 1   29.8  ? 123 THR B CA  1 
ATOM   2000 C  C   . THR B 2 123 ? -44.34  -14.955 -14.841 1   30.21 ? 123 THR B C   1 
ATOM   2001 O  O   . THR B 2 123 ? -43.5   -14.723 -13.97  1   30.38 ? 123 THR B O   1 
ATOM   2002 C  CB  . THR B 2 123 ? -45.364 -13.013 -16.049 1   30.66 ? 123 THR B CB  1 
ATOM   2003 O  OG1 . THR B 2 123 ? -44.173 -12.294 -15.735 1   30.98 ? 123 THR B OG1 1 
ATOM   2004 C  CG2 . THR B 2 123 ? -46.533 -12.043 -16.166 1   31.29 ? 123 THR B CG2 1 
ATOM   2005 N  N   . PRO B 2 124 ? -44.173 -15.944 -15.739 1   30.15 ? 124 PRO B N   1 
ATOM   2006 C  CA  . PRO B 2 124 ? -42.943 -16.757 -15.71  1   30.12 ? 124 PRO B CA  1 
ATOM   2007 C  C   . PRO B 2 124 ? -41.64  -15.924 -15.691 1   29.65 ? 124 PRO B C   1 
ATOM   2008 O  O   . PRO B 2 124 ? -40.827 -16.236 -14.822 1   28.93 ? 124 PRO B O   1 
ATOM   2009 C  CB  . PRO B 2 124 ? -43.091 -17.658 -16.945 1   30.63 ? 124 PRO B CB  1 
ATOM   2010 C  CG  . PRO B 2 124 ? -44.596 -17.809 -17.085 1   31.31 ? 124 PRO B CG  1 
ATOM   2011 C  CD  . PRO B 2 124 ? -45.09  -16.398 -16.808 1   30.09 ? 124 PRO B CD  1 
ATOM   2012 N  N   . PRO B 2 125 ? -41.462 -14.797 -16.445 1   29.61 ? 125 PRO B N   1 
ATOM   2013 C  CA  . PRO B 2 125 ? -40.213 -14.019 -16.291 1   29.71 ? 125 PRO B CA  1 
ATOM   2014 C  C   . PRO B 2 125 ? -40.063 -13.402 -14.898 1   29.33 ? 125 PRO B C   1 
ATOM   2015 O  O   . PRO B 2 125 ? -38.954 -13.355 -14.37  1   29.97 ? 125 PRO B O   1 
ATOM   2016 C  CB  . PRO B 2 125 ? -40.342 -12.914 -17.354 1   30.82 ? 125 PRO B CB  1 
ATOM   2017 C  CG  . PRO B 2 125 ? -41.248 -13.525 -18.412 1   32.37 ? 125 PRO B CG  1 
ATOM   2018 C  CD  . PRO B 2 125 ? -42.266 -14.271 -17.578 1   29.89 ? 125 PRO B CD  1 
ATOM   2019 N  N   . VAL B 2 126 ? -41.158 -12.894 -14.321 1   28.25 ? 126 VAL B N   1 
ATOM   2020 C  CA  . VAL B 2 126 ? -41.127 -12.276 -12.985 1   28.96 ? 126 VAL B CA  1 
ATOM   2021 C  C   . VAL B 2 126 ? -40.753 -13.354 -11.953 1   28.03 ? 126 VAL B C   1 
ATOM   2022 O  O   . VAL B 2 126 ? -39.883 -13.113 -11.119 1   28.8  ? 126 VAL B O   1 
ATOM   2023 C  CB  . VAL B 2 126 ? -42.448 -11.565 -12.631 1   30.25 ? 126 VAL B CB  1 
ATOM   2024 C  CG1 . VAL B 2 126 ? -42.48  -11.165 -11.158 1   31.12 ? 126 VAL B CG1 1 
ATOM   2025 C  CG2 . VAL B 2 126 ? -42.672 -10.337 -13.53  1   32.03 ? 126 VAL B CG2 1 
ATOM   2026 N  N   . GLN B 2 127 ? -41.328 -14.568 -12.066 1   25.74 ? 127 GLN B N   1 
ATOM   2027 C  CA  . GLN B 2 127 ? -40.952 -15.656 -11.136 1   24.73 ? 127 GLN B CA  1 
ATOM   2028 C  C   . GLN B 2 127 ? -39.458 -15.981 -11.299 1   24.53 ? 127 GLN B C   1 
ATOM   2029 O  O   . GLN B 2 127 ? -38.768 -16.135 -10.297 1   23.88 ? 127 GLN B O   1 
ATOM   2030 C  CB  . GLN B 2 127 ? -41.752 -16.948 -11.424 1   24.12 ? 127 GLN B CB  1 
ATOM   2031 C  CG  . GLN B 2 127 ? -41.323 -18.109 -10.498 1   23.63 ? 127 GLN B CG  1 
ATOM   2032 C  CD  . GLN B 2 127 ? -41.883 -19.446 -10.872 1   23.6  ? 127 GLN B CD  1 
ATOM   2033 O  OE1 . GLN B 2 127 ? -42.7   -19.554 -11.782 1   25.18 ? 127 GLN B OE1 1 
ATOM   2034 N  NE2 . GLN B 2 127 ? -41.436 -20.509 -10.176 1   22.25 ? 127 GLN B NE2 1 
ATOM   2035 N  N   . ALA B 2 128 ? -38.955 -16.091 -12.557 1   24.48 ? 128 ALA B N   1 
ATOM   2036 C  CA  . ALA B 2 128 ? -37.549 -16.462 -12.758 1   25.16 ? 128 ALA B CA  1 
ATOM   2037 C  C   . ALA B 2 128 ? -36.593 -15.503 -12.058 1   25.8  ? 128 ALA B C   1 
ATOM   2038 O  O   . ALA B 2 128 ? -35.594 -15.938 -11.478 1   26.07 ? 128 ALA B O   1 
ATOM   2039 C  CB  . ALA B 2 128 ? -37.22  -16.556 -14.248 1   24.97 ? 128 ALA B CB  1 
ATOM   2040 N  N   . ALA B 2 129 ? -36.94  -14.203 -12.06  1   25.15 ? 129 ALA B N   1 
ATOM   2041 C  CA  . ALA B 2 129 ? -36.112 -13.198 -11.413 1   26.02 ? 129 ALA B CA  1 
ATOM   2042 C  C   . ALA B 2 129 ? -36.171 -13.389 -9.883  1   26.22 ? 129 ALA B C   1 
ATOM   2043 O  O   . ALA B 2 129 ? -35.127 -13.388 -9.224  1   26.48 ? 129 ALA B O   1 
ATOM   2044 C  CB  . ALA B 2 129 ? -36.573 -11.804 -11.822 1   26    ? 129 ALA B CB  1 
ATOM   2045 N  N   . TYR B 2 130 ? -37.376 -13.594 -9.327  1   24.88 ? 130 TYR B N   1 
ATOM   2046 C  CA  . TYR B 2 130 ? -37.506 -13.853 -7.889  1   25.13 ? 130 TYR B CA  1 
ATOM   2047 C  C   . TYR B 2 130 ? -36.786 -15.138 -7.465  1   25.54 ? 130 TYR B C   1 
ATOM   2048 O  O   . TYR B 2 130 ? -36.302 -15.216 -6.328  1   26.53 ? 130 TYR B O   1 
ATOM   2049 C  CB  . TYR B 2 130 ? -38.986 -13.894 -7.47   1   24.77 ? 130 TYR B CB  1 
ATOM   2050 C  CG  . TYR B 2 130 ? -39.464 -12.521 -7.056  1   25.92 ? 130 TYR B CG  1 
ATOM   2051 C  CD1 . TYR B 2 130 ? -39.25  -12.049 -5.766  1   26.83 ? 130 TYR B CD1 1 
ATOM   2052 C  CD2 . TYR B 2 130 ? -40.065 -11.667 -7.97   1   26.7  ? 130 TYR B CD2 1 
ATOM   2053 C  CE1 . TYR B 2 130 ? -39.64  -10.769 -5.389  1   28.17 ? 130 TYR B CE1 1 
ATOM   2054 C  CE2 . TYR B 2 130 ? -40.468 -10.385 -7.603  1   28.14 ? 130 TYR B CE2 1 
ATOM   2055 C  CZ  . TYR B 2 130 ? -40.248 -9.941  -6.312  1   29.36 ? 130 TYR B CZ  1 
ATOM   2056 O  OH  . TYR B 2 130 ? -40.625 -8.673  -5.94   1   32.07 ? 130 TYR B OH  1 
ATOM   2057 N  N   . GLN B 2 131 ? -36.688 -16.128 -8.356  1   24.83 ? 131 GLN B N   1 
ATOM   2058 C  CA  . GLN B 2 131 ? -35.98  -17.363 -8.014  1   25.45 ? 131 GLN B CA  1 
ATOM   2059 C  C   . GLN B 2 131 ? -34.49  -17.081 -7.776  1   26.09 ? 131 GLN B C   1 
ATOM   2060 O  O   . GLN B 2 131 ? -33.912 -17.652 -6.845  1   26.79 ? 131 GLN B O   1 
ATOM   2061 C  CB  . GLN B 2 131 ? -36.199 -18.503 -9.039  1   25.02 ? 131 GLN B CB  1 
ATOM   2062 C  CG  . GLN B 2 131 ? -37.667 -18.939 -9.154  1   24.9  ? 131 GLN B CG  1 
ATOM   2063 C  CD  . GLN B 2 131 ? -38.26  -19.747 -7.984  1   25.96 ? 131 GLN B CD  1 
ATOM   2064 O  OE1 . GLN B 2 131 ? -39.474 -19.98  -7.954  1   26.72 ? 131 GLN B OE1 1 
ATOM   2065 N  NE2 . GLN B 2 131 ? -37.446 -20.22  -7.016  1   20.5  ? 131 GLN B NE2 1 
ATOM   2066 N  N   . LYS B 2 132 ? -33.895 -16.173 -8.563  1   25.65 ? 132 LYS B N   1 
ATOM   2067 C  CA  . LYS B 2 132 ? -32.485 -15.807 -8.354  1   26.83 ? 132 LYS B CA  1 
ATOM   2068 C  C   . LYS B 2 132 ? -32.32  -15.117 -6.991  1   27.1  ? 132 LYS B C   1 
ATOM   2069 O  O   . LYS B 2 132 ? -31.388 -15.418 -6.253  1   26.93 ? 132 LYS B O   1 
ATOM   2070 C  CB  . LYS B 2 132 ? -31.968 -14.893 -9.491  1   28.38 ? 132 LYS B CB  1 
ATOM   2071 C  CG  . LYS B 2 132 ? -31.869 -15.599 -10.849 1   31.36 ? 132 LYS B CG  1 
ATOM   2072 C  CD  . LYS B 2 132 ? -31.51  -14.59  -11.953 1   35.31 ? 132 LYS B CD  1 
ATOM   2073 C  CE  . LYS B 2 132 ? -31.034 -15.242 -13.222 1   41.16 ? 132 LYS B CE  1 
ATOM   2074 N  NZ  . LYS B 2 132 ? -30.77  -14.196 -14.259 1   42.83 ? 132 LYS B NZ  1 
ATOM   2075 N  N   . VAL B 2 133 ? -33.258 -14.231 -6.64   1   27.07 ? 133 VAL B N   1 
ATOM   2076 C  CA  . VAL B 2 133 ? -33.208 -13.526 -5.367  1   28.13 ? 133 VAL B CA  1 
ATOM   2077 C  C   . VAL B 2 133 ? -33.341 -14.484 -4.175  1   28.47 ? 133 VAL B C   1 
ATOM   2078 O  O   . VAL B 2 133 ? -32.491 -14.449 -3.277  1   28.76 ? 133 VAL B O   1 
ATOM   2079 C  CB  . VAL B 2 133 ? -34.296 -12.432 -5.306  1   28.91 ? 133 VAL B CB  1 
ATOM   2080 C  CG1 . VAL B 2 133 ? -34.271 -11.709 -3.967  1   29.67 ? 133 VAL B CG1 1 
ATOM   2081 C  CG2 . VAL B 2 133 ? -34.149 -11.451 -6.465  1   29.97 ? 133 VAL B CG2 1 
ATOM   2082 N  N   . VAL B 2 134 ? -34.362 -15.376 -4.185  1   27.84 ? 134 VAL B N   1 
ATOM   2083 C  CA  . VAL B 2 134 ? -34.566 -16.249 -3.031  1   28.49 ? 134 VAL B CA  1 
ATOM   2084 C  C   . VAL B 2 134 ? -33.449 -17.279 -2.901  1   29.27 ? 134 VAL B C   1 
ATOM   2085 O  O   . VAL B 2 134 ? -33.106 -17.622 -1.762  1   29.33 ? 134 VAL B O   1 
ATOM   2086 C  CB  . VAL B 2 134 ? -35.971 -16.89  -2.913  1   29.04 ? 134 VAL B CB  1 
ATOM   2087 C  CG1 . VAL B 2 134 ? -37.056 -15.818 -2.813  1   29.39 ? 134 VAL B CG1 1 
ATOM   2088 C  CG2 . VAL B 2 134 ? -36.244 -17.874 -4.052  1   29.12 ? 134 VAL B CG2 1 
ATOM   2089 N  N   . ALA B 2 135 ? -32.824 -17.709 -4.014  1   29.19 ? 135 ALA B N   1 
ATOM   2090 C  CA  . ALA B 2 135 ? -31.692 -18.632 -3.921  1   30.4  ? 135 ALA B CA  1 
ATOM   2091 C  C   . ALA B 2 135 ? -30.493 -17.916 -3.289  1   31.27 ? 135 ALA B C   1 
ATOM   2092 O  O   . ALA B 2 135 ? -29.807 -18.514 -2.462  1   32.02 ? 135 ALA B O   1 
ATOM   2093 C  CB  . ALA B 2 135 ? -31.309 -19.168 -5.297  1   30.94 ? 135 ALA B CB  1 
ATOM   2094 N  N   . GLY B 2 136 ? -30.263 -16.658 -3.682  1   30.98 ? 136 GLY B N   1 
ATOM   2095 C  CA  . GLY B 2 136 ? -29.188 -15.824 -3.154  1   31.7  ? 136 GLY B CA  1 
ATOM   2096 C  C   . GLY B 2 136 ? -29.34  -15.58  -1.658  1   32.43 ? 136 GLY B C   1 
ATOM   2097 O  O   . GLY B 2 136 ? -28.363 -15.686 -0.916  1   32.61 ? 136 GLY B O   1 
ATOM   2098 N  N   . VAL B 2 137 ? -30.573 -15.286 -1.193  1   32.1  ? 137 VAL B N   1 
ATOM   2099 C  CA  . VAL B 2 137 ? -30.837 -15.065 0.235   1   32.32 ? 137 VAL B CA  1 
ATOM   2100 C  C   . VAL B 2 137 ? -30.617 -16.372 1.015   1   32.67 ? 137 VAL B C   1 
ATOM   2101 O  O   . VAL B 2 137 ? -29.931 -16.358 2.031   1   32.39 ? 137 VAL B O   1 
ATOM   2102 C  CB  . VAL B 2 137 ? -32.27  -14.519 0.463   1   32.74 ? 137 VAL B CB  1 
ATOM   2103 C  CG1 . VAL B 2 137 ? -32.644 -14.541 1.947   1   32.87 ? 137 VAL B CG1 1 
ATOM   2104 C  CG2 . VAL B 2 137 ? -32.423 -13.105 -0.115  1   32.68 ? 137 VAL B CG2 1 
ATOM   2105 N  N   . ALA B 2 138 ? -31.147 -17.505 0.519   1   32.17 ? 138 ALA B N   1 
ATOM   2106 C  CA  . ALA B 2 138 ? -30.973 -18.79  1.203   1   32.66 ? 138 ALA B CA  1 
ATOM   2107 C  C   . ALA B 2 138 ? -29.5   -19.239 1.26    1   34.17 ? 138 ALA B C   1 
ATOM   2108 O  O   . ALA B 2 138 ? -29.072 -19.793 2.272   1   33.86 ? 138 ALA B O   1 
ATOM   2109 C  CB  . ALA B 2 138 ? -31.83  -19.863 0.546   1   32.36 ? 138 ALA B CB  1 
ATOM   2110 N  N   . ASN B 2 139 ? -28.725 -18.981 0.196   1   35.4  ? 139 ASN B N   1 
ATOM   2111 C  CA  . ASN B 2 139 ? -27.306 -19.314 0.183   1   37.38 ? 139 ASN B CA  1 
ATOM   2112 C  C   . ASN B 2 139 ? -26.541 -18.41  1.163   1   38.38 ? 139 ASN B C   1 
ATOM   2113 O  O   . ASN B 2 139 ? -25.664 -18.884 1.887   1   38.66 ? 139 ASN B O   1 
ATOM   2114 C  CB  . ASN B 2 139 ? -26.728 -19.181 -1.223  1   40.37 ? 139 ASN B CB  1 
ATOM   2115 C  CG  . ASN B 2 139 ? -27.022 -20.341 -2.158  1   47.12 ? 139 ASN B CG  1 
ATOM   2116 O  OD1 . ASN B 2 139 ? -27.034 -20.18  -3.388  1   49.95 ? 139 ASN B OD1 1 
ATOM   2117 N  ND2 . ASN B 2 139 ? -27.261 -21.535 -1.622  1   48.37 ? 139 ASN B ND2 1 
ATOM   2118 N  N   . ALA B 2 140 ? -26.892 -17.118 1.204   1   38.69 ? 140 ALA B N   1 
ATOM   2119 C  CA  . ALA B 2 140 ? -26.264 -16.15  2.106   1   39.44 ? 140 ALA B CA  1 
ATOM   2120 C  C   . ALA B 2 140 ? -26.505 -16.533 3.551   1   41.2  ? 140 ALA B C   1 
ATOM   2121 O  O   . ALA B 2 140 ? -25.607 -16.375 4.374   1   41.72 ? 140 ALA B O   1 
ATOM   2122 C  CB  . ALA B 2 140 ? -26.816 -14.753 1.848   1   38.8  ? 140 ALA B CB  1 
ATOM   2123 N  N   . LEU B 2 141 ? -27.721 -17.015 3.875   1   41.72 ? 141 LEU B N   1 
ATOM   2124 C  CA  . LEU B 2 141 ? -28.05  -17.433 5.238   1   43.09 ? 141 LEU B CA  1 
ATOM   2125 C  C   . LEU B 2 141 ? -27.318 -18.734 5.612   1   43.9  ? 141 LEU B C   1 
ATOM   2126 O  O   . LEU B 2 141 ? -26.952 -18.923 6.77    1   43.9  ? 141 LEU B O   1 
ATOM   2127 C  CB  . LEU B 2 141 ? -29.56  -17.657 5.359   1   44.02 ? 141 LEU B CB  1 
ATOM   2128 C  CG  . LEU B 2 141 ? -30.375 -16.546 5.997   1   46.21 ? 141 LEU B CG  1 
ATOM   2129 C  CD1 . LEU B 2 141 ? -30.288 -15.291 5.204   1   47.15 ? 141 LEU B CD1 1 
ATOM   2130 C  CD2 . LEU B 2 141 ? -31.806 -16.937 6.06    1   46.92 ? 141 LEU B CD2 1 
ATOM   2131 N  N   . ALA B 2 142 ? -27.119 -19.636 4.634   1   44.56 ? 142 ALA B N   1 
ATOM   2132 C  CA  . ALA B 2 142 ? -26.44  -20.921 4.854   1   46.18 ? 142 ALA B CA  1 
ATOM   2133 C  C   . ALA B 2 142 ? -24.942 -20.774 5.145   1   47.5  ? 142 ALA B C   1 
ATOM   2134 O  O   . ALA B 2 142 ? -24.374 -19.698 4.962   1   48.27 ? 142 ALA B O   1 
ATOM   2135 C  CB  . ALA B 2 142 ? -26.645 -21.837 3.657   1   46.38 ? 142 ALA B CB  1 
ATOM   2136 N  N   . LYS C 3 5   ? -71.084 -59.004 47.895  1   47.85 ? 36  LYS C N   1 
ATOM   2137 C  CA  . LYS C 3 5   ? -69.881 -59.731 48.314  1   48.68 ? 36  LYS C CA  1 
ATOM   2138 C  C   . LYS C 3 5   ? -68.645 -59.347 47.511  1   47.87 ? 36  LYS C C   1 
ATOM   2139 O  O   . LYS C 3 5   ? -67.529 -59.449 48.026  1   48.81 ? 36  LYS C O   1 
ATOM   2140 C  CB  . LYS C 3 5   ? -70.107 -61.249 48.286  1   51.97 ? 36  LYS C CB  1 
ATOM   2141 N  N   . ASN C 3 6   ? -68.833 -58.893 46.255  1   45.51 ? 37  ASN C N   1 
ATOM   2142 C  CA  . ASN C 3 6   ? -67.718 -58.484 45.447  1   43.83 ? 37  ASN C CA  1 
ATOM   2143 C  C   . ASN C 3 6   ? -68.166 -57.728 44.187  1   40.85 ? 37  ASN C C   1 
ATOM   2144 O  O   . ASN C 3 6   ? -69.363 -57.558 43.921  1   40.62 ? 37  ASN C O   1 
ATOM   2145 C  CB  . ASN C 3 6   ? -66.762 -59.673 45.14   1   46.16 ? 37  ASN C CB  1 
ATOM   2146 C  CG  . ASN C 3 6   ? -67.309 -60.757 44.25   1   51.32 ? 37  ASN C CG  1 
ATOM   2147 O  OD1 . ASN C 3 6   ? -67.314 -60.632 43.019  1   53.24 ? 37  ASN C OD1 1 
ATOM   2148 N  ND2 . ASN C 3 6   ? -67.759 -61.858 44.855  1   52.91 ? 37  ASN C ND2 1 
ATOM   2149 N  N   . ALA C 3 7   ? -67.201 -57.208 43.472  1   37.75 ? 38  ALA C N   1 
ATOM   2150 C  CA  . ALA C 3 7   ? -67.45  -56.483 42.235  1   36.31 ? 38  ALA C CA  1 
ATOM   2151 C  C   . ALA C 3 7   ? -66.405 -56.878 41.251  1   35.68 ? 38  ALA C C   1 
ATOM   2152 O  O   . ALA C 3 7   ? -65.237 -57.022 41.619  1   35.19 ? 38  ALA C O   1 
ATOM   2153 C  CB  . ALA C 3 7   ? -67.333 -54.995 42.471  1   36.27 ? 38  ALA C CB  1 
ATOM   2154 N  N   . ASP C 3 8   ? -66.802 -56.998 39.979  1   35.12 ? 39  ASP C N   1 
ATOM   2155 C  CA  . ASP C 3 8   ? -65.859 -57.237 38.892  1   34.31 ? 39  ASP C CA  1 
ATOM   2156 C  C   . ASP C 3 8   ? -65.822 -55.962 38.09   1   33    ? 39  ASP C C   1 
ATOM   2157 O  O   . ASP C 3 8   ? -66.878 -55.387 37.813  1   32.52 ? 39  ASP C O   1 
ATOM   2158 C  CB  . ASP C 3 8   ? -66.328 -58.363 37.955  1   36.48 ? 39  ASP C CB  1 
ATOM   2159 C  CG  . ASP C 3 8   ? -66.362 -59.725 38.614  1   41.89 ? 39  ASP C CG  1 
ATOM   2160 O  OD1 . ASP C 3 8   ? -65.395 -60.059 39.331  1   42.59 ? 39  ASP C OD1 1 
ATOM   2161 O  OD2 . ASP C 3 8   ? -67.351 -60.453 38.411  1   43.43 ? 39  ASP C OD2 1 
ATOM   2162 N  N   . LEU C 3 9   ? -64.62  -55.524 37.696  1   31.63 ? 40  LEU C N   1 
ATOM   2163 C  CA  . LEU C 3 9   ? -64.476 -54.351 36.852  1   31.16 ? 40  LEU C CA  1 
ATOM   2164 C  C   . LEU C 3 9   ? -64.089 -54.817 35.466  1   30.84 ? 40  LEU C C   1 
ATOM   2165 O  O   . LEU C 3 9   ? -63.151 -55.604 35.322  1   30.84 ? 40  LEU C O   1 
ATOM   2166 C  CB  . LEU C 3 9   ? -63.391 -53.396 37.392  1   30.94 ? 40  LEU C CB  1 
ATOM   2167 C  CG  . LEU C 3 9   ? -62.932 -52.258 36.441  1   32    ? 40  LEU C CG  1 
ATOM   2168 C  CD1 . LEU C 3 9   ? -64.008 -51.202 36.288  1   31.82 ? 40  LEU C CD1 1 
ATOM   2169 C  CD2 . LEU C 3 9   ? -61.677 -51.619 36.964  1   33.47 ? 40  LEU C CD2 1 
ATOM   2170 N  N   . TYR C 3 10  ? -64.756 -54.276 34.443  1   29.64 ? 41  TYR C N   1 
ATOM   2171 C  CA  . TYR C 3 10  ? -64.44  -54.555 33.044  1   28.98 ? 41  TYR C CA  1 
ATOM   2172 C  C   . TYR C 3 10  ? -64     -53.237 32.422  1   27.55 ? 41  TYR C C   1 
ATOM   2173 O  O   . TYR C 3 10  ? -64.725 -52.242 32.533  1   26.71 ? 41  TYR C O   1 
ATOM   2174 C  CB  . TYR C 3 10  ? -65.686 -55.053 32.307  1   29.51 ? 41  TYR C CB  1 
ATOM   2175 C  CG  . TYR C 3 10  ? -66.168 -56.415 32.768  1   30.65 ? 41  TYR C CG  1 
ATOM   2176 C  CD1 . TYR C 3 10  ? -66.982 -56.548 33.886  1   32.11 ? 41  TYR C CD1 1 
ATOM   2177 C  CD2 . TYR C 3 10  ? -65.845 -57.562 32.058  1   31.73 ? 41  TYR C CD2 1 
ATOM   2178 C  CE1 . TYR C 3 10  ? -67.42  -57.793 34.313  1   33.54 ? 41  TYR C CE1 1 
ATOM   2179 C  CE2 . TYR C 3 10  ? -66.295 -58.81  32.46   1   33.51 ? 41  TYR C CE2 1 
ATOM   2180 C  CZ  . TYR C 3 10  ? -67.077 -58.925 33.593  1   34.92 ? 41  TYR C CZ  1 
ATOM   2181 O  OH  . TYR C 3 10  ? -67.529 -60.169 33.981  1   37.5  ? 41  TYR C OH  1 
ATOM   2182 N  N   . TRP C 3 11  ? -62.819 -53.209 31.78   1   26.53 ? 42  TRP C N   1 
ATOM   2183 C  CA  . TRP C 3 11  ? -62.337 -51.974 31.164  1   25.92 ? 42  TRP C CA  1 
ATOM   2184 C  C   . TRP C 3 11  ? -61.433 -52.283 29.975  1   25.35 ? 42  TRP C C   1 
ATOM   2185 O  O   . TRP C 3 11  ? -60.478 -53.048 30.112  1   25.34 ? 42  TRP C O   1 
ATOM   2186 C  CB  . TRP C 3 11  ? -61.54  -51.169 32.214  1   25.18 ? 42  TRP C CB  1 
ATOM   2187 C  CG  . TRP C 3 11  ? -61.195 -49.747 31.841  1   25.15 ? 42  TRP C CG  1 
ATOM   2188 C  CD1 . TRP C 3 11  ? -61.888 -48.914 30.998  1   25.27 ? 42  TRP C CD1 1 
ATOM   2189 C  CD2 . TRP C 3 11  ? -60.142 -48.958 32.409  1   25.01 ? 42  TRP C CD2 1 
ATOM   2190 N  NE1 . TRP C 3 11  ? -61.323 -47.659 31.006  1   24.89 ? 42  TRP C NE1 1 
ATOM   2191 C  CE2 . TRP C 3 11  ? -60.238 -47.663 31.853  1   25.44 ? 42  TRP C CE2 1 
ATOM   2192 C  CE3 . TRP C 3 11  ? -59.159 -49.206 33.387  1   25.67 ? 42  TRP C CE3 1 
ATOM   2193 C  CZ2 . TRP C 3 11  ? -59.358 -46.637 32.205  1   25.97 ? 42  TRP C CZ2 1 
ATOM   2194 C  CZ3 . TRP C 3 11  ? -58.287 -48.188 33.732  1   26.14 ? 42  TRP C CZ3 1 
ATOM   2195 C  CH2 . TRP C 3 11  ? -58.389 -46.922 33.143  1   25.75 ? 42  TRP C CH2 1 
ATOM   2196 N  N   . GLY C 3 12  ? -61.691 -51.645 28.843  1   24.55 ? 43  GLY C N   1 
ATOM   2197 C  CA  . GLY C 3 12  ? -60.848 -51.804 27.67   1   24    ? 43  GLY C CA  1 
ATOM   2198 C  C   . GLY C 3 12  ? -59.695 -50.808 27.637  1   23.83 ? 43  GLY C C   1 
ATOM   2199 O  O   . GLY C 3 12  ? -58.929 -50.775 26.656  1   24.79 ? 43  GLY C O   1 
ATOM   2200 N  N   . PHE C 3 13  ? -59.576 -49.972 28.704  1   22.19 ? 44  PHE C N   1 
ATOM   2201 C  CA  . PHE C 3 13  ? -58.578 -48.939 28.934  1   22.08 ? 44  PHE C CA  1 
ATOM   2202 C  C   . PHE C 3 13  ? -58.787 -47.768 27.971  1   21.84 ? 44  PHE C C   1 
ATOM   2203 O  O   . PHE C 3 13  ? -59.299 -46.737 28.388  1   22.17 ? 44  PHE C O   1 
ATOM   2204 C  CB  . PHE C 3 13  ? -57.155 -49.51  28.931  1   21.97 ? 44  PHE C CB  1 
ATOM   2205 C  CG  . PHE C 3 13  ? -56.152 -48.572 29.556  1   22.67 ? 44  PHE C CG  1 
ATOM   2206 C  CD1 . PHE C 3 13  ? -56.072 -48.439 30.926  1   23.11 ? 44  PHE C CD1 1 
ATOM   2207 C  CD2 . PHE C 3 13  ? -55.322 -47.793 28.768  1   23.58 ? 44  PHE C CD2 1 
ATOM   2208 C  CE1 . PHE C 3 13  ? -55.181 -47.543 31.502  1   24.11 ? 44  PHE C CE1 1 
ATOM   2209 C  CE2 . PHE C 3 13  ? -54.421 -46.92  29.343  1   24.38 ? 44  PHE C CE2 1 
ATOM   2210 C  CZ  . PHE C 3 13  ? -54.352 -46.803 30.711  1   23.82 ? 44  PHE C CZ  1 
ATOM   2211 N  N   . SER C 3 14  ? -58.509 -47.96  26.688  1   21.3  ? 45  SER C N   1 
ATOM   2212 C  CA  . SER C 3 14  ? -58.728 -46.941 25.654  1   21.39 ? 45  SER C CA  1 
ATOM   2213 C  C   . SER C 3 14  ? -58.879 -47.648 24.315  1   22.02 ? 45  SER C C   1 
ATOM   2214 O  O   . SER C 3 14  ? -58.386 -48.769 24.134  1   21.93 ? 45  SER C O   1 
ATOM   2215 C  CB  . SER C 3 14  ? -57.546 -45.978 25.591  1   22.18 ? 45  SER C CB  1 
ATOM   2216 O  OG  . SER C 3 14  ? -56.345 -46.588 25.145  1   23.44 ? 45  SER C OG  1 
ATOM   2217 N  N   . GLY C 3 15  ? -59.563 -47.016 23.374  1   21.96 ? 46  GLY C N   1 
ATOM   2218 C  CA  . GLY C 3 15  ? -59.669 -47.548 22.013  1   21.56 ? 46  GLY C CA  1 
ATOM   2219 C  C   . GLY C 3 15  ? -58.291 -47.742 21.385  1   21.44 ? 46  GLY C C   1 
ATOM   2220 O  O   . GLY C 3 15  ? -58.027 -48.755 20.733  1   22.43 ? 46  GLY C O   1 
ATOM   2221 N  N   . SER C 3 16  ? -57.363 -46.84  21.702  1   19.88 ? 47  SER C N   1 
ATOM   2222 C  CA  . SER C 3 16  ? -55.988 -46.939 21.214  1   20.38 ? 47  SER C CA  1 
ATOM   2223 C  C   . SER C 3 16  ? -55.214 -48.116 21.806  1   21.78 ? 47  SER C C   1 
ATOM   2224 O  O   . SER C 3 16  ? -54.169 -48.472 21.255  1   22.25 ? 47  SER C O   1 
ATOM   2225 C  CB  . SER C 3 16  ? -55.234 -45.625 21.407  1   20.24 ? 47  SER C CB  1 
ATOM   2226 O  OG  . SER C 3 16  ? -55.046 -45.366 22.788  1   22.24 ? 47  SER C OG  1 
ATOM   2227 N  N   . SER C 3 17  ? -55.727 -48.769 22.89   1   21.38 ? 48  SER C N   1 
ATOM   2228 C  CA  . SER C 3 17  ? -55.105 -50.004 23.367  1   21.97 ? 48  SER C CA  1 
ATOM   2229 C  C   . SER C 3 17  ? -55.483 -51.204 22.473  1   23.69 ? 48  SER C C   1 
ATOM   2230 O  O   . SER C 3 17  ? -55.09  -52.33  22.781  1   24.12 ? 48  SER C O   1 
ATOM   2231 C  CB  . SER C 3 17  ? -55.52  -50.324 24.815  1   21.64 ? 48  SER C CB  1 
ATOM   2232 O  OG  . SER C 3 17  ? -55.368 -49.172 25.619  1   21.97 ? 48  SER C OG  1 
ATOM   2233 N  N   . HIS C 3 18  ? -56.235 -50.987 21.386  1   24.19 ? 49  HIS C N   1 
ATOM   2234 C  CA  . HIS C 3 18  ? -56.712 -52.05  20.521  1   24.34 ? 49  HIS C CA  1 
ATOM   2235 C  C   . HIS C 3 18  ? -56.254 -51.872 19.08   1   24.35 ? 49  HIS C C   1 
ATOM   2236 O  O   . HIS C 3 18  ? -56.953 -52.253 18.144  1   24.97 ? 49  HIS C O   1 
ATOM   2237 C  CB  . HIS C 3 18  ? -58.241 -52.181 20.643  1   24.58 ? 49  HIS C CB  1 
ATOM   2238 C  CG  . HIS C 3 18  ? -58.627 -52.449 22.064  1   25.32 ? 49  HIS C CG  1 
ATOM   2239 N  ND1 . HIS C 3 18  ? -58.646 -53.733 22.569  1   26.38 ? 49  HIS C ND1 1 
ATOM   2240 C  CD2 . HIS C 3 18  ? -58.865 -51.58  23.07   1   26.27 ? 49  HIS C CD2 1 
ATOM   2241 C  CE1 . HIS C 3 18  ? -58.94  -53.612 23.862  1   26.89 ? 49  HIS C CE1 1 
ATOM   2242 N  NE2 . HIS C 3 18  ? -59.071 -52.332 24.212  1   27    ? 49  HIS C NE2 1 
ATOM   2243 N  N   . HIS C 3 19  ? -55.039 -51.35  18.913  1   22.82 ? 50  HIS C N   1 
ATOM   2244 C  CA  . HIS C 3 19  ? -54.439 -51.214 17.593  1   23.06 ? 50  HIS C CA  1 
ATOM   2245 C  C   . HIS C 3 19  ? -54.047 -52.604 17.119  1   23.04 ? 50  HIS C C   1 
ATOM   2246 O  O   . HIS C 3 19  ? -53.709 -53.45  17.947  1   22.94 ? 50  HIS C O   1 
ATOM   2247 C  CB  . HIS C 3 19  ? -53.158 -50.38  17.735  1   22.97 ? 50  HIS C CB  1 
ATOM   2248 C  CG  . HIS C 3 19  ? -53.292 -48.938 17.36   1   24.8  ? 50  HIS C CG  1 
ATOM   2249 N  ND1 . HIS C 3 19  ? -53.218 -48.529 16.032  1   26.08 ? 50  HIS C ND1 1 
ATOM   2250 C  CD2 . HIS C 3 19  ? -53.356 -47.839 18.155  1   26.3  ? 50  HIS C CD2 1 
ATOM   2251 C  CE1 . HIS C 3 19  ? -53.279 -47.199 16.065  1   27.01 ? 50  HIS C CE1 1 
ATOM   2252 N  NE2 . HIS C 3 19  ? -53.342 -46.738 17.324  1   27.32 ? 50  HIS C NE2 1 
ATOM   2253 N  N   . LYS C 3 20  ? -54.05  -52.832 15.793  1   23.97 ? 51  LYS C N   1 
ATOM   2254 C  CA  . LYS C 3 20  ? -53.597 -54.092 15.186  1   25.03 ? 51  LYS C CA  1 
ATOM   2255 C  C   . LYS C 3 20  ? -52.122 -54.368 15.588  1   25.75 ? 51  LYS C C   1 
ATOM   2256 O  O   . LYS C 3 20  ? -51.788 -55.489 15.966  1   27.02 ? 51  LYS C O   1 
ATOM   2257 C  CB  . LYS C 3 20  ? -53.711 -53.997 13.647  1   26.02 ? 51  LYS C CB  1 
ATOM   2258 C  CG  . LYS C 3 20  ? -53.198 -55.234 12.919  1   30.29 ? 51  LYS C CG  1 
ATOM   2259 C  CD  . LYS C 3 20  ? -53.387 -55.124 11.412  1   34.34 ? 51  LYS C CD  1 
ATOM   2260 C  CE  . LYS C 3 20  ? -52.644 -56.198 10.653  1   39.3  ? 51  LYS C CE  1 
ATOM   2261 N  NZ  . LYS C 3 20  ? -53     -56.209 9.204   1   43.86 ? 51  LYS C NZ  1 
ATOM   2262 N  N   . TYR C 3 21  ? -51.267 -53.323 15.585  1   24.95 ? 52  TYR C N   1 
ATOM   2263 C  CA  . TYR C 3 21  ? -49.874 -53.468 16.05   1   24.96 ? 52  TYR C CA  1 
ATOM   2264 C  C   . TYR C 3 21  ? -49.829 -52.949 17.46   1   25.05 ? 52  TYR C C   1 
ATOM   2265 O  O   . TYR C 3 21  ? -50.12  -51.759 17.727  1   24.72 ? 52  TYR C O   1 
ATOM   2266 C  CB  . TYR C 3 21  ? -48.896 -52.713 15.15   1   24.99 ? 52  TYR C CB  1 
ATOM   2267 C  CG  . TYR C 3 21  ? -48.877 -53.249 13.74   1   25.82 ? 52  TYR C CG  1 
ATOM   2268 C  CD1 . TYR C 3 21  ? -48.018 -54.276 13.377  1   27.26 ? 52  TYR C CD1 1 
ATOM   2269 C  CD2 . TYR C 3 21  ? -49.74  -52.749 12.774  1   26.31 ? 52  TYR C CD2 1 
ATOM   2270 C  CE1 . TYR C 3 21  ? -47.984 -54.763 12.078  1   27.88 ? 52  TYR C CE1 1 
ATOM   2271 C  CE2 . TYR C 3 21  ? -49.699 -53.207 11.461  1   27.97 ? 52  TYR C CE2 1 
ATOM   2272 C  CZ  . TYR C 3 21  ? -48.849 -54.243 11.125  1   29.19 ? 52  TYR C CZ  1 
ATOM   2273 O  OH  . TYR C 3 21  ? -48.803 -54.698 9.836   1   30.6  ? 52  TYR C OH  1 
ATOM   2274 N  N   . ASP C 3 22  ? -49.544 -53.846 18.385  1   24.64 ? 53  ASP C N   1 
ATOM   2275 C  CA  . ASP C 3 22  ? -49.655 -53.497 19.794  1   25.8  ? 53  ASP C CA  1 
ATOM   2276 C  C   . ASP C 3 22  ? -48.644 -52.448 20.318  1   25.39 ? 53  ASP C C   1 
ATOM   2277 O  O   . ASP C 3 22  ? -48.912 -51.884 21.374  1   26.58 ? 53  ASP C O   1 
ATOM   2278 C  CB  . ASP C 3 22  ? -49.684 -54.726 20.69   1   29.88 ? 53  ASP C CB  1 
ATOM   2279 C  CG  . ASP C 3 22  ? -48.497 -55.605 20.559  1   35.18 ? 53  ASP C CG  1 
ATOM   2280 O  OD1 . ASP C 3 22  ? -47.414 -55.084 20.284  1   36.18 ? 53  ASP C OD1 1 
ATOM   2281 O  OD2 . ASP C 3 22  ? -48.642 -56.804 20.773  1   39.49 ? 53  ASP C OD2 1 
ATOM   2282 N  N   . HIS C 3 23  ? -47.568 -52.123 19.59   1   24.95 ? 54  HIS C N   1 
ATOM   2283 C  CA  . HIS C 3 23  ? -46.665 -51.03  20.004  1   25.14 ? 54  HIS C CA  1 
ATOM   2284 C  C   . HIS C 3 23  ? -47.334 -49.641 19.814  1   23    ? 54  HIS C C   1 
ATOM   2285 O  O   . HIS C 3 23  ? -46.784 -48.622 20.241  1   22.67 ? 54  HIS C O   1 
ATOM   2286 C  CB  . HIS C 3 23  ? -45.367 -51.05  19.157  1   27.77 ? 54  HIS C CB  1 
ATOM   2287 C  CG  . HIS C 3 23  ? -44.404 -52.127 19.546  1   32.93 ? 54  HIS C CG  1 
ATOM   2288 N  ND1 . HIS C 3 23  ? -44.525 -53.421 19.047  1   35.77 ? 54  HIS C ND1 1 
ATOM   2289 C  CD2 . HIS C 3 23  ? -43.337 -52.077 20.378  1   34.99 ? 54  HIS C CD2 1 
ATOM   2290 C  CE1 . HIS C 3 23  ? -43.53  -54.113 19.587  1   36.29 ? 54  HIS C CE1 1 
ATOM   2291 N  NE2 . HIS C 3 23  ? -42.801 -53.359 20.412  1   36.51 ? 54  HIS C NE2 1 
ATOM   2292 N  N   . ASN C 3 24  ? -48.463 -49.581 19.096  1   21.46 ? 55  ASN C N   1 
ATOM   2293 C  CA  . ASN C 3 24  ? -49.117 -48.316 18.746  1   20.46 ? 55  ASN C CA  1 
ATOM   2294 C  C   . ASN C 3 24  ? -50.098 -47.754 19.776  1   20.82 ? 55  ASN C C   1 
ATOM   2295 O  O   . ASN C 3 24  ? -50.66  -46.68  19.591  1   21.59 ? 55  ASN C O   1 
ATOM   2296 C  CB  . ASN C 3 24  ? -49.788 -48.453 17.387  1   19.62 ? 55  ASN C CB  1 
ATOM   2297 C  CG  . ASN C 3 24  ? -48.773 -48.545 16.284  1   22.6  ? 55  ASN C CG  1 
ATOM   2298 O  OD1 . ASN C 3 24  ? -47.675 -47.977 16.365  1   22.81 ? 55  ASN C OD1 1 
ATOM   2299 N  ND2 . ASN C 3 24  ? -49.135 -49.184 15.17   1   23.33 ? 55  ASN C ND2 1 
ATOM   2300 N  N   . GLY C 3 25  ? -50.285 -48.468 20.864  1   20.72 ? 56  GLY C N   1 
ATOM   2301 C  CA  . GLY C 3 25  ? -51.139 -48.039 21.95   1   20.6  ? 56  GLY C CA  1 
ATOM   2302 C  C   . GLY C 3 25  ? -50.774 -48.772 23.225  1   20.4  ? 56  GLY C C   1 
ATOM   2303 O  O   . GLY C 3 25  ? -49.953 -49.714 23.22   1   19.51 ? 56  GLY C O   1 
ATOM   2304 N  N   . PRO C 3 26  ? -51.402 -48.411 24.353  1   20.08 ? 57  PRO C N   1 
ATOM   2305 C  CA  . PRO C 3 26  ? -51.066 -49.115 25.616  1   20.1  ? 57  PRO C CA  1 
ATOM   2306 C  C   . PRO C 3 26  ? -51.232 -50.637 25.478  1   21.68 ? 57  PRO C C   1 
ATOM   2307 O  O   . PRO C 3 26  ? -52.197 -51.111 24.84   1   21.14 ? 57  PRO C O   1 
ATOM   2308 C  CB  . PRO C 3 26  ? -52.058 -48.526 26.632  1   20.36 ? 57  PRO C CB  1 
ATOM   2309 C  CG  . PRO C 3 26  ? -52.317 -47.101 26.107  1   20.45 ? 57  PRO C CG  1 
ATOM   2310 C  CD  . PRO C 3 26  ? -52.372 -47.315 24.571  1   18.71 ? 57  PRO C CD  1 
ATOM   2311 N  N   . LYS C 3 27  ? -50.249 -51.396 25.984  1   21.33 ? 58  LYS C N   1 
ATOM   2312 C  CA  . LYS C 3 27  ? -50.281 -52.858 25.931  1   22.3  ? 58  LYS C CA  1 
ATOM   2313 C  C   . LYS C 3 27  ? -50.179 -53.375 27.353  1   23.69 ? 58  LYS C C   1 
ATOM   2314 O  O   . LYS C 3 27  ? -49.371 -52.867 28.119  1   24.57 ? 58  LYS C O   1 
ATOM   2315 C  CB  . LYS C 3 27  ? -49.091 -53.356 25.111  1   25.48 ? 58  LYS C CB  1 
ATOM   2316 C  CG  . LYS C 3 27  ? -48.945 -54.856 25.062  1   31.29 ? 58  LYS C CG  1 
ATOM   2317 C  CD  . LYS C 3 27  ? -47.506 -55.176 24.673  1   39.82 ? 58  LYS C CD  1 
ATOM   2318 C  CE  . LYS C 3 27  ? -47.205 -56.652 24.727  1   46.94 ? 58  LYS C CE  1 
ATOM   2319 N  NZ  . LYS C 3 27  ? -45.974 -56.966 23.952  1   51.05 ? 58  LYS C NZ  1 
ATOM   2320 N  N   . PHE C 3 28  ? -50.971 -54.384 27.712  1   23.73 ? 59  PHE C N   1 
ATOM   2321 C  CA  . PHE C 3 28  ? -50.982 -54.891 29.089  1   23.99 ? 59  PHE C CA  1 
ATOM   2322 C  C   . PHE C 3 28  ? -50.503 -56.321 29.123  1   24.7  ? 59  PHE C C   1 
ATOM   2323 O  O   . PHE C 3 28  ? -50.781 -57.086 28.201  1   24.92 ? 59  PHE C O   1 
ATOM   2324 C  CB  . PHE C 3 28  ? -52.403 -54.761 29.682  1   23.73 ? 59  PHE C CB  1 
ATOM   2325 C  CG  . PHE C 3 28  ? -52.826 -53.31  29.764  1   23.26 ? 59  PHE C CG  1 
ATOM   2326 C  CD1 . PHE C 3 28  ? -53.438 -52.69  28.691  1   23.94 ? 59  PHE C CD1 1 
ATOM   2327 C  CD2 . PHE C 3 28  ? -52.548 -52.555 30.893  1   23.63 ? 59  PHE C CD2 1 
ATOM   2328 C  CE1 . PHE C 3 28  ? -53.742 -51.335 28.731  1   24.84 ? 59  PHE C CE1 1 
ATOM   2329 C  CE2 . PHE C 3 28  ? -52.929 -51.229 30.965  1   24.46 ? 59  PHE C CE2 1 
ATOM   2330 C  CZ  . PHE C 3 28  ? -53.474 -50.614 29.865  1   24.39 ? 59  PHE C CZ  1 
ATOM   2331 N  N   . GLU C 3 29  ? -49.815 -56.68  30.2    1   25.26 ? 60  GLU C N   1 
ATOM   2332 C  CA  . GLU C 3 29  ? -49.278 -58.013 30.403  1   26.13 ? 60  GLU C CA  1 
ATOM   2333 C  C   . GLU C 3 29  ? -49.032 -58.254 31.896  1   26.19 ? 60  GLU C C   1 
ATOM   2334 O  O   . GLU C 3 29  ? -49.086 -57.321 32.686  1   26.53 ? 60  GLU C O   1 
ATOM   2335 C  CB  . GLU C 3 29  ? -47.966 -58.161 29.646  1   29.07 ? 60  GLU C CB  1 
ATOM   2336 C  CG  . GLU C 3 29  ? -46.914 -57.151 30.035  1   34.29 ? 60  GLU C CG  1 
ATOM   2337 C  CD  . GLU C 3 29  ? -45.614 -57.444 29.309  1   43.65 ? 60  GLU C CD  1 
ATOM   2338 O  OE1 . GLU C 3 29  ? -45.659 -57.678 28.078  1   44.44 ? 60  GLU C OE1 1 
ATOM   2339 O  OE2 . GLU C 3 29  ? -44.555 -57.46  29.973  1   47.59 ? 60  GLU C OE2 1 
ATOM   2340 N  N   . LYS C 3 30  ? -48.753 -59.495 32.267  1   26.49 ? 61  LYS C N   1 
ATOM   2341 C  CA  . LYS C 3 30  ? -48.434 -59.844 33.647  1   27.54 ? 61  LYS C CA  1 
ATOM   2342 C  C   . LYS C 3 30  ? -49.529 -59.465 34.649  1   27.88 ? 61  LYS C C   1 
ATOM   2343 O  O   . LYS C 3 30  ? -49.232 -59.034 35.78   1   28.69 ? 61  LYS C O   1 
ATOM   2344 C  CB  . LYS C 3 30  ? -47.065 -59.252 34.029  1   30.03 ? 61  LYS C CB  1 
ATOM   2345 C  CG  . LYS C 3 30  ? -45.938 -59.783 33.14   1   36.83 ? 61  LYS C CG  1 
ATOM   2346 C  CD  . LYS C 3 30  ? -44.582 -59.142 33.462  1   42.94 ? 61  LYS C CD  1 
ATOM   2347 C  CE  . LYS C 3 30  ? -43.428 -59.777 32.706  1   47.01 ? 61  LYS C CE  1 
ATOM   2348 N  NZ  . LYS C 3 30  ? -43.608 -59.692 31.224  1   49.95 ? 61  LYS C NZ  1 
ATOM   2349 N  N   . ALA C 3 31  ? -50.794 -59.674 34.26   1   27.32 ? 62  ALA C N   1 
ATOM   2350 C  CA  . ALA C 3 31  ? -51.932 -59.431 35.155  1   27.6  ? 62  ALA C CA  1 
ATOM   2351 C  C   . ALA C 3 31  ? -51.876 -60.433 36.3    1   28.11 ? 62  ALA C C   1 
ATOM   2352 O  O   . ALA C 3 31  ? -51.541 -61.603 36.083  1   28.92 ? 62  ALA C O   1 
ATOM   2353 C  CB  . ALA C 3 31  ? -53.239 -59.595 34.396  1   27.6  ? 62  ALA C CB  1 
ATOM   2354 N  N   . GLY C 3 32  ? -52.118 -59.95  37.519  1   27.22 ? 63  GLY C N   1 
ATOM   2355 C  CA  . GLY C 3 32  ? -52.088 -60.755 38.733  1   26.36 ? 63  GLY C CA  1 
ATOM   2356 C  C   . GLY C 3 32  ? -52.978 -60.179 39.822  1   25.9  ? 63  GLY C C   1 
ATOM   2357 O  O   . GLY C 3 32  ? -53.592 -59.116 39.644  1   24.84 ? 63  GLY C O   1 
ATOM   2358 N  N   . LYS C 3 33  ? -53.093 -60.908 40.94   1   25.49 ? 64  LYS C N   1 
ATOM   2359 C  CA  . LYS C 3 33  ? -53.877 -60.515 42.108  1   26.93 ? 64  LYS C CA  1 
ATOM   2360 C  C   . LYS C 3 33  ? -55.332 -60.237 41.783  1   27.53 ? 64  LYS C C   1 
ATOM   2361 O  O   . LYS C 3 33  ? -55.906 -59.268 42.283  1   27.36 ? 64  LYS C O   1 
ATOM   2362 C  CB  . LYS C 3 33  ? -53.228 -59.337 42.848  1   28.64 ? 64  LYS C CB  1 
ATOM   2363 C  CG  . LYS C 3 33  ? -51.755 -59.581 43.2    1   34.14 ? 64  LYS C CG  1 
ATOM   2364 C  CD  . LYS C 3 33  ? -51.265 -58.567 44.24   1   39.73 ? 64  LYS C CD  1 
ATOM   2365 C  CE  . LYS C 3 33  ? -49.764 -58.621 44.412  1   45.82 ? 64  LYS C CE  1 
ATOM   2366 N  NZ  . LYS C 3 33  ? -49.33  -58.01  45.704  1   49.42 ? 64  LYS C NZ  1 
ATOM   2367 N  N   . GLY C 3 34  ? -55.912 -61.046 40.901  1   28.04 ? 65  GLY C N   1 
ATOM   2368 C  CA  . GLY C 3 34  ? -57.318 -60.873 40.543  1   27.92 ? 65  GLY C CA  1 
ATOM   2369 C  C   . GLY C 3 34  ? -57.537 -60.189 39.208  1   27.63 ? 65  GLY C C   1 
ATOM   2370 O  O   . GLY C 3 34  ? -58.627 -60.285 38.643  1   27.43 ? 65  GLY C O   1 
ATOM   2371 N  N   . ALA C 3 35  ? -56.507 -59.502 38.676  1   26.55 ? 66  ALA C N   1 
ATOM   2372 C  CA  . ALA C 3 35  ? -56.619 -58.914 37.336  1   26.2  ? 66  ALA C CA  1 
ATOM   2373 C  C   . ALA C 3 35  ? -56.385 -60.03  36.317  1   27.57 ? 66  ALA C C   1 
ATOM   2374 O  O   . ALA C 3 35  ? -55.595 -60.955 36.558  1   28.23 ? 66  ALA C O   1 
ATOM   2375 C  CB  . ALA C 3 35  ? -55.597 -57.815 37.137  1   24.95 ? 66  ALA C CB  1 
ATOM   2376 N  N   . GLU C 3 36  ? -57.084 -59.959 35.204  1   28.09 ? 67  GLU C N   1 
ATOM   2377 C  CA  . GLU C 3 36  ? -56.982 -60.959 34.154  1   29.48 ? 67  GLU C CA  1 
ATOM   2378 C  C   . GLU C 3 36  ? -57.208 -60.297 32.808  1   30.34 ? 67  GLU C C   1 
ATOM   2379 O  O   . GLU C 3 36  ? -58.137 -59.509 32.677  1   30.66 ? 67  GLU C O   1 
ATOM   2380 C  CB  . GLU C 3 36  ? -58.094 -61.988 34.345  1   34.32 ? 67  GLU C CB  1 
ATOM   2381 C  CG  . GLU C 3 36  ? -57.62  -63.425 34.271  1   44.85 ? 67  GLU C CG  1 
ATOM   2382 C  CD  . GLU C 3 36  ? -58.741 -64.387 33.937  1   57.32 ? 67  GLU C CD  1 
ATOM   2383 O  OE1 . GLU C 3 36  ? -59.61  -64.615 34.809  1   59.39 ? 67  GLU C OE1 1 
ATOM   2384 O  OE2 . GLU C 3 36  ? -58.761 -64.898 32.794  1   62.7  ? 67  GLU C OE2 1 
ATOM   2385 N  N   . LEU C 3 37  ? -56.418 -60.655 31.806  1   30.3  ? 68  LEU C N   1 
ATOM   2386 C  CA  . LEU C 3 37  ? -56.656 -60.179 30.435  1   31.74 ? 68  LEU C CA  1 
ATOM   2387 C  C   . LEU C 3 37  ? -57.601 -61.204 29.805  1   32.99 ? 68  LEU C C   1 
ATOM   2388 O  O   . LEU C 3 37  ? -57.283 -62.395 29.748  1   33.32 ? 68  LEU C O   1 
ATOM   2389 C  CB  . LEU C 3 37  ? -55.34  -60.092 29.688  1   32.48 ? 68  LEU C CB  1 
ATOM   2390 C  CG  . LEU C 3 37  ? -54.564 -58.866 30.052  1   34.48 ? 68  LEU C CG  1 
ATOM   2391 C  CD1 . LEU C 3 37  ? -53.126 -59.025 29.667  1   36.5  ? 68  LEU C CD1 1 
ATOM   2392 C  CD2 . LEU C 3 37  ? -55.162 -57.663 29.389  1   34.94 ? 68  LEU C CD2 1 
ATOM   2393 N  N   . THR C 3 38  ? -58.816 -60.772 29.466  1   33.43 ? 69  THR C N   1 
ATOM   2394 C  CA  . THR C 3 38  ? -59.859 -61.684 29.01   1   34.34 ? 69  THR C CA  1 
ATOM   2395 C  C   . THR C 3 38  ? -60.336 -61.37  27.605  1   35.45 ? 69  THR C C   1 
ATOM   2396 O  O   . THR C 3 38  ? -60.633 -60.215 27.32   1   34.52 ? 69  THR C O   1 
ATOM   2397 C  CB  . THR C 3 38  ? -61.048 -61.58  29.986  1   35.6  ? 69  THR C CB  1 
ATOM   2398 O  OG1 . THR C 3 38  ? -60.577 -61.728 31.332  1   36.99 ? 69  THR C OG1 1 
ATOM   2399 C  CG2 . THR C 3 38  ? -62.13  -62.593 29.705  1   35.98 ? 69  THR C CG2 1 
ATOM   2400 N  N   . ASN C 3 39  ? -60.504 -62.383 26.75   1   37.26 ? 70  ASN C N   1 
ATOM   2401 C  CA  . ASN C 3 39  ? -61.029 -62.16  25.408  1   39.63 ? 70  ASN C CA  1 
ATOM   2402 C  C   . ASN C 3 39  ? -62.442 -61.568 25.487  1   41.3  ? 70  ASN C C   1 
ATOM   2403 O  O   . ASN C 3 39  ? -63.214 -61.983 26.348  1   42.41 ? 70  ASN C O   1 
ATOM   2404 C  CB  . ASN C 3 39  ? -60.999 -63.448 24.591  1   42.51 ? 70  ASN C CB  1 
ATOM   2405 C  CG  . ASN C 3 39  ? -61.496 -63.249 23.183  1   47.67 ? 70  ASN C CG  1 
ATOM   2406 O  OD1 . ASN C 3 39  ? -62.647 -63.528 22.884  1   49.98 ? 70  ASN C OD1 1 
ATOM   2407 N  ND2 . ASN C 3 39  ? -60.663 -62.719 22.303  1   48.93 ? 70  ASN C ND2 1 
ATOM   2408 N  N   . ILE C 3 40  ? -62.761 -60.571 24.653  1   41.9  ? 71  ILE C N   1 
ATOM   2409 C  CA  . ILE C 3 40  ? -64.077 -59.914 24.671  1   43.2  ? 71  ILE C CA  1 
ATOM   2410 C  C   . ILE C 3 40  ? -65.249 -60.902 24.581  1   44.89 ? 71  ILE C C   1 
ATOM   2411 O  O   . ILE C 3 40  ? -66.219 -60.73  25.322  1   45.84 ? 71  ILE C O   1 
ATOM   2412 C  CB  . ILE C 3 40  ? -64.176 -58.802 23.599  1   43.6  ? 71  ILE C CB  1 
ATOM   2413 C  CG1 . ILE C 3 40  ? -65.486 -57.99  23.741  1   44.39 ? 71  ILE C CG1 1 
ATOM   2414 C  CG2 . ILE C 3 40  ? -64.038 -59.388 22.196  1   43.76 ? 71  ILE C CG2 1 
ATOM   2415 C  CD1 . ILE C 3 40  ? -65.734 -57.362 25.151  1   44.83 ? 71  ILE C CD1 1 
ATOM   2416 N  N   . ASP C 3 41  ? -65.135 -61.99  23.788  1   45.51 ? 72  ASP C N   1 
ATOM   2417 C  CA  . ASP C 3 41  ? -66.207 -63.004 23.708  1   46.8  ? 72  ASP C CA  1 
ATOM   2418 C  C   . ASP C 3 41  ? -66.487 -63.701 25.056  1   46.74 ? 72  ASP C C   1 
ATOM   2419 O  O   . ASP C 3 41  ? -67.513 -64.366 25.208  1   47.75 ? 72  ASP C O   1 
ATOM   2420 C  CB  . ASP C 3 41  ? -65.863 -64.083 22.678  1   49.85 ? 72  ASP C CB  1 
ATOM   2421 C  CG  . ASP C 3 41  ? -65.573 -63.567 21.298  1   57.37 ? 72  ASP C CG  1 
ATOM   2422 O  OD1 . ASP C 3 41  ? -66.128 -62.504 20.933  1   59.45 ? 72  ASP C OD1 1 
ATOM   2423 O  OD2 . ASP C 3 41  ? -64.791 -64.225 20.573  1   60.33 ? 72  ASP C OD2 1 
ATOM   2424 N  N   . ALA C 3 42  ? -65.558 -63.608 26.012  1   46.07 ? 73  ALA C N   1 
ATOM   2425 C  CA  . ALA C 3 42  ? -65.741 -64.205 27.337  1   45.73 ? 73  ALA C CA  1 
ATOM   2426 C  C   . ALA C 3 42  ? -65.987 -63.157 28.443  1   45.61 ? 73  ALA C C   1 
ATOM   2427 O  O   . ALA C 3 42  ? -65.979 -63.492 29.63   1   46.14 ? 73  ALA C O   1 
ATOM   2428 C  CB  . ALA C 3 42  ? -64.551 -65.082 27.69   1   45.85 ? 73  ALA C CB  1 
ATOM   2429 N  N   . ALA C 3 43  ? -66.207 -61.894 28.052  1   44.78 ? 74  ALA C N   1 
ATOM   2430 C  CA  . ALA C 3 43  ? -66.462 -60.773 28.946  1   44.37 ? 74  ALA C CA  1 
ATOM   2431 C  C   . ALA C 3 43  ? -67.692 -60.04  28.402  1   44.4  ? 74  ALA C C   1 
ATOM   2432 O  O   . ALA C 3 43  ? -67.678 -58.822 28.223  1   43.6  ? 74  ALA C O   1 
ATOM   2433 C  CB  . ALA C 3 43  ? -65.252 -59.852 28.973  1   43.89 ? 74  ALA C CB  1 
ATOM   2434 N  N   . SER C 3 44  ? -68.777 -60.81  28.176  1   45.26 ? 75  SER C N   1 
ATOM   2435 C  CA  . SER C 3 44  ? -70.049 -60.357 27.609  1   45.7  ? 75  SER C CA  1 
ATOM   2436 C  C   . SER C 3 44  ? -70.683 -59.171 28.321  1   44.68 ? 75  SER C C   1 
ATOM   2437 O  O   . SER C 3 44  ? -71.386 -58.388 27.675  1   45.85 ? 75  SER C O   1 
ATOM   2438 C  CB  . SER C 3 44  ? -71.047 -61.513 27.523  1   47.59 ? 75  SER C CB  1 
ATOM   2439 O  OG  . SER C 3 44  ? -71.304 -62.045 28.81   1   52.44 ? 75  SER C OG  1 
ATOM   2440 N  N   . ALA C 3 45  ? -70.438 -59.018 29.624  1   42.64 ? 76  ALA C N   1 
ATOM   2441 C  CA  . ALA C 3 45  ? -70.968 -57.872 30.361  1   41.42 ? 76  ALA C CA  1 
ATOM   2442 C  C   . ALA C 3 45  ? -70.42  -56.543 29.811  1   40.03 ? 76  ALA C C   1 
ATOM   2443 O  O   . ALA C 3 45  ? -71.093 -55.52  29.923  1   40.91 ? 76  ALA C O   1 
ATOM   2444 C  CB  . ALA C 3 45  ? -70.668 -58.001 31.853  1   41.33 ? 76  ALA C CB  1 
ATOM   2445 N  N   . TYR C 3 46  ? -69.235 -56.559 29.171  1   37.7  ? 77  TYR C N   1 
ATOM   2446 C  CA  . TYR C 3 46  ? -68.651 -55.356 28.577  1   36.4  ? 77  TYR C CA  1 
ATOM   2447 C  C   . TYR C 3 46  ? -68.949 -55.205 27.076  1   38.21 ? 77  TYR C C   1 
ATOM   2448 O  O   . TYR C 3 46  ? -68.584 -54.183 26.5    1   38.75 ? 77  TYR C O   1 
ATOM   2449 C  CB  . TYR C 3 46  ? -67.126 -55.374 28.782  1   34.2  ? 77  TYR C CB  1 
ATOM   2450 C  CG  . TYR C 3 46  ? -66.455 -54.029 28.641  1   32.53 ? 77  TYR C CG  1 
ATOM   2451 C  CD1 . TYR C 3 46  ? -66.818 -52.963 29.449  1   32.39 ? 77  TYR C CD1 1 
ATOM   2452 C  CD2 . TYR C 3 46  ? -65.379 -53.853 27.779  1   32.86 ? 77  TYR C CD2 1 
ATOM   2453 C  CE1 . TYR C 3 46  ? -66.147 -51.745 29.387  1   32.48 ? 77  TYR C CE1 1 
ATOM   2454 C  CE2 . TYR C 3 46  ? -64.698 -52.642 27.709  1   32.86 ? 77  TYR C CE2 1 
ATOM   2455 C  CZ  . TYR C 3 46  ? -65.077 -51.591 28.524  1   32.69 ? 77  TYR C CZ  1 
ATOM   2456 O  OH  . TYR C 3 46  ? -64.411 -50.389 28.454  1   32.3  ? 77  TYR C OH  1 
ATOM   2457 N  N   . ALA C 3 47  ? -69.572 -56.203 26.438  1   39.04 ? 78  ALA C N   1 
ATOM   2458 C  CA  . ALA C 3 47  ? -69.838 -56.192 24.996  1   40.72 ? 78  ALA C CA  1 
ATOM   2459 C  C   . ALA C 3 47  ? -70.439 -54.892 24.431  1   42    ? 78  ALA C C   1 
ATOM   2460 O  O   . ALA C 3 47  ? -69.897 -54.364 23.468  1   42.85 ? 78  ALA C O   1 
ATOM   2461 C  CB  . ALA C 3 47  ? -70.709 -57.384 24.6    1   41.16 ? 78  ALA C CB  1 
ATOM   2462 N  N   . GLU C 3 48  ? -71.529 -54.37  25.01   1   42.02 ? 79  GLU C N   1 
ATOM   2463 C  CA  . GLU C 3 48  ? -72.166 -53.163 24.484  1   42.07 ? 79  GLU C CA  1 
ATOM   2464 C  C   . GLU C 3 48  ? -71.343 -51.888 24.725  1   41.27 ? 79  GLU C C   1 
ATOM   2465 O  O   . GLU C 3 48  ? -71.232 -51.063 23.806  1   40.54 ? 79  GLU C O   1 
ATOM   2466 C  CB  . GLU C 3 48  ? -73.605 -53.042 24.993  1   45.92 ? 79  GLU C CB  1 
ATOM   2467 C  CG  . GLU C 3 48  ? -74.505 -54.102 24.368  1   55.89 ? 79  GLU C CG  1 
ATOM   2468 C  CD  . GLU C 3 48  ? -74.541 -54.099 22.846  1   68.62 ? 79  GLU C CD  1 
ATOM   2469 O  OE1 . GLU C 3 48  ? -75.161 -53.176 22.268  1   71.84 ? 79  GLU C OE1 1 
ATOM   2470 O  OE2 . GLU C 3 48  ? -73.948 -55.016 22.231  1   72.23 ? 79  GLU C OE2 1 
ATOM   2471 N  N   . THR C 3 49  ? -70.687 -51.756 25.902  1   41.39 ? 80  THR C N   1 
ATOM   2472 C  CA  . THR C 3 49  ? -69.831 -50.582 26.143  1   42.9  ? 80  THR C CA  1 
ATOM   2473 C  C   . THR C 3 49  ? -68.661 -50.588 25.161  1   43.38 ? 80  THR C C   1 
ATOM   2474 O  O   . THR C 3 49  ? -68.4   -49.568 24.519  1   44.21 ? 80  THR C O   1 
ATOM   2475 C  CB  . THR C 3 49  ? -69.297 -50.547 27.591  1   44.61 ? 80  THR C CB  1 
ATOM   2476 O  OG1 . THR C 3 49  ? -70.377 -50.301 28.475  1   45.97 ? 80  THR C OG1 1 
ATOM   2477 C  CG2 . THR C 3 49  ? -68.211 -49.485 27.784  1   45.39 ? 80  THR C CG2 1 
ATOM   2478 N  N   . PHE C 3 50  ? -67.985 -51.747 25.015  1   43.15 ? 81  PHE C N   1 
ATOM   2479 C  CA  . PHE C 3 50  ? -66.858 -51.886 24.093  1   44.11 ? 81  PHE C CA  1 
ATOM   2480 C  C   . PHE C 3 50  ? -67.223 -51.486 22.65   1   45.71 ? 81  PHE C C   1 
ATOM   2481 O  O   . PHE C 3 50  ? -66.493 -50.713 22.042  1   47.21 ? 81  PHE C O   1 
ATOM   2482 C  CB  . PHE C 3 50  ? -66.278 -53.312 24.149  1   43.38 ? 81  PHE C CB  1 
ATOM   2483 C  CG  . PHE C 3 50  ? -64.877 -53.432 23.599  1   43.15 ? 81  PHE C CG  1 
ATOM   2484 C  CD1 . PHE C 3 50  ? -63.833 -52.718 24.159  1   43.19 ? 81  PHE C CD1 1 
ATOM   2485 C  CD2 . PHE C 3 50  ? -64.606 -54.252 22.518  1   43.96 ? 81  PHE C CD2 1 
ATOM   2486 C  CE1 . PHE C 3 50  ? -62.545 -52.81  23.638  1   43.65 ? 81  PHE C CE1 1 
ATOM   2487 C  CE2 . PHE C 3 50  ? -63.317 -54.333 21.991  1   44.35 ? 81  PHE C CE2 1 
ATOM   2488 C  CZ  . PHE C 3 50  ? -62.291 -53.636 22.577  1   43.68 ? 81  PHE C CZ  1 
ATOM   2489 N  N   . LYS C 3 51  ? -68.374 -51.932 22.12   1   45.17 ? 82  LYS C N   1 
ATOM   2490 C  CA  . LYS C 3 51  ? -68.789 -51.61  20.749  1   45.16 ? 82  LYS C CA  1 
ATOM   2491 C  C   . LYS C 3 51  ? -69.016 -50.11  20.458  1   44.63 ? 82  LYS C C   1 
ATOM   2492 O  O   . LYS C 3 51  ? -69.051 -49.712 19.289  1   45.05 ? 82  LYS C O   1 
ATOM   2493 C  CB  . LYS C 3 51  ? -70.054 -52.384 20.37   1   47.59 ? 82  LYS C CB  1 
ATOM   2494 C  CG  . LYS C 3 51  ? -69.822 -53.875 20.192  1   53.42 ? 82  LYS C CG  1 
ATOM   2495 N  N   . LYS C 3 52  ? -69.224 -49.3   21.501  1   43    ? 83  LYS C N   1 
ATOM   2496 C  CA  . LYS C 3 52  ? -69.466 -47.871 21.336  1   41.54 ? 83  LYS C CA  1 
ATOM   2497 C  C   . LYS C 3 52  ? -68.213 -47     21.433  1   39.21 ? 83  LYS C C   1 
ATOM   2498 O  O   . LYS C 3 52  ? -68.314 -45.784 21.3    1   39.25 ? 83  LYS C O   1 
ATOM   2499 C  CB  . LYS C 3 52  ? -70.51  -47.39  22.347  1   44.47 ? 83  LYS C CB  1 
ATOM   2500 C  CG  . LYS C 3 52  ? -71.91  -47.928 22.054  1   48.27 ? 83  LYS C CG  1 
ATOM   2501 C  CD  . LYS C 3 52  ? -72.972 -47.33  22.959  1   53.56 ? 83  LYS C CD  1 
ATOM   2502 C  CE  . LYS C 3 52  ? -72.821 -47.739 24.406  1   58.2  ? 83  LYS C CE  1 
ATOM   2503 N  NZ  . LYS C 3 52  ? -74.021 -47.348 25.202  1   60.77 ? 83  LYS C NZ  1 
ATOM   2504 N  N   . GLY C 3 53  ? -67.055 -47.6   21.694  1   36.79 ? 84  GLY C N   1 
ATOM   2505 C  CA  . GLY C 3 53  ? -65.81  -46.845 21.799  1   34.66 ? 84  GLY C CA  1 
ATOM   2506 C  C   . GLY C 3 53  ? -65.3   -46.285 20.487  1   31.93 ? 84  GLY C C   1 
ATOM   2507 O  O   . GLY C 3 53  ? -65.76  -46.67  19.407  1   30.95 ? 84  GLY C O   1 
ATOM   2508 N  N   . VAL C 3 54  ? -64.343 -45.334 20.574  1   29.9  ? 85  VAL C N   1 
ATOM   2509 C  CA  . VAL C 3 54  ? -63.71  -44.749 19.411  1   28.84 ? 85  VAL C CA  1 
ATOM   2510 C  C   . VAL C 3 54  ? -62.39  -45.507 19.285  1   28.14 ? 85  VAL C C   1 
ATOM   2511 O  O   . VAL C 3 54  ? -61.598 -45.492 20.206  1   26.87 ? 85  VAL C O   1 
ATOM   2512 C  CB  . VAL C 3 54  ? -63.501 -43.213 19.518  1   28.76 ? 85  VAL C CB  1 
ATOM   2513 C  CG1 . VAL C 3 54  ? -62.681 -42.701 18.316  1   28.57 ? 85  VAL C CG1 1 
ATOM   2514 C  CG2 . VAL C 3 54  ? -64.856 -42.481 19.603  1   29.54 ? 85  VAL C CG2 1 
ATOM   2515 N  N   . PHE C 3 55  ? -62.21  -46.234 18.18   1   28.14 ? 86  PHE C N   1 
ATOM   2516 C  CA  . PHE C 3 55  ? -61.029 -47.069 17.995  1   28.37 ? 86  PHE C CA  1 
ATOM   2517 C  C   . PHE C 3 55  ? -60.185 -46.563 16.851  1   27.64 ? 86  PHE C C   1 
ATOM   2518 O  O   . PHE C 3 55  ? -60.713 -45.9   15.962  1   27.72 ? 86  PHE C O   1 
ATOM   2519 C  CB  . PHE C 3 55  ? -61.48  -48.51  17.673  1   28.59 ? 86  PHE C CB  1 
ATOM   2520 C  CG  . PHE C 3 55  ? -62.17  -49.167 18.827  1   29.28 ? 86  PHE C CG  1 
ATOM   2521 C  CD1 . PHE C 3 55  ? -61.436 -49.768 19.842  1   29.66 ? 86  PHE C CD1 1 
ATOM   2522 C  CD2 . PHE C 3 55  ? -63.555 -49.205 18.899  1   29.89 ? 86  PHE C CD2 1 
ATOM   2523 C  CE1 . PHE C 3 55  ? -62.066 -50.355 20.925  1   30.4  ? 86  PHE C CE1 1 
ATOM   2524 C  CE2 . PHE C 3 55  ? -64.188 -49.791 19.996  1   30.38 ? 86  PHE C CE2 1 
ATOM   2525 C  CZ  . PHE C 3 55  ? -63.437 -50.376 20.993  1   30.42 ? 86  PHE C CZ  1 
ATOM   2526 N  N   . PRO C 3 56  ? -58.869 -46.887 16.816  1   27.2  ? 87  PRO C N   1 
ATOM   2527 C  CA  . PRO C 3 56  ? -58.073 -46.479 15.658  1   27.49 ? 87  PRO C CA  1 
ATOM   2528 C  C   . PRO C 3 56  ? -58.559 -47.146 14.378  1   26.51 ? 87  PRO C C   1 
ATOM   2529 O  O   . PRO C 3 56  ? -59.196 -48.216 14.41   1   25.39 ? 87  PRO C O   1 
ATOM   2530 C  CB  . PRO C 3 56  ? -56.653 -46.947 16.005  1   28    ? 87  PRO C CB  1 
ATOM   2531 C  CG  . PRO C 3 56  ? -56.847 -48.061 16.986  1   28.36 ? 87  PRO C CG  1 
ATOM   2532 C  CD  . PRO C 3 56  ? -58.078 -47.695 17.766  1   26.74 ? 87  PRO C CD  1 
ATOM   2533 N  N   . ASN C 3 57  ? -58.232 -46.537 13.235  1   27.47 ? 88  ASN C N   1 
ATOM   2534 C  CA  . ASN C 3 57  ? -58.6   -47.119 11.956  1   28.73 ? 88  ASN C CA  1 
ATOM   2535 C  C   . ASN C 3 57  ? -58.015 -48.537 11.757  1   28.17 ? 88  ASN C C   1 
ATOM   2536 O  O   . ASN C 3 57  ? -58.686 -49.412 11.211  1   28.85 ? 88  ASN C O   1 
ATOM   2537 C  CB  . ASN C 3 57  ? -58.17  -46.188 10.818  1   31.86 ? 88  ASN C CB  1 
ATOM   2538 C  CG  . ASN C 3 57  ? -58.978 -44.91  10.806  1   36.97 ? 88  ASN C CG  1 
ATOM   2539 O  OD1 . ASN C 3 57  ? -60.22  -44.94  10.772  1   36.72 ? 88  ASN C OD1 1 
ATOM   2540 N  ND2 . ASN C 3 57  ? -58.28  -43.764 10.834  1   37.82 ? 88  ASN C ND2 1 
ATOM   2541 N  N   . ASN C 3 58  ? -56.783 -48.757 12.21   1   26.81 ? 89  ASN C N   1 
ATOM   2542 C  CA  . ASN C 3 58  ? -56.077 -50.04  12.066  1   27.83 ? 89  ASN C CA  1 
ATOM   2543 C  C   . ASN C 3 58  ? -56.287 -50.762 13.395  1   28.36 ? 89  ASN C C   1 
ATOM   2544 O  O   . ASN C 3 58  ? -55.434 -50.729 14.262  1   28    ? 89  ASN C O   1 
ATOM   2545 C  CB  . ASN C 3 58  ? -54.576 -49.752 11.846  1   28.61 ? 89  ASN C CB  1 
ATOM   2546 C  CG  . ASN C 3 58  ? -53.709 -50.896 11.359  1   30.42 ? 89  ASN C CG  1 
ATOM   2547 O  OD1 . ASN C 3 58  ? -52.612 -51.119 11.874  1   31.4  ? 89  ASN C OD1 1 
ATOM   2548 N  ND2 . ASN C 3 58  ? -54.138 -51.588 10.322  1   28.74 ? 89  ASN C ND2 1 
ATOM   2549 N  N   . LYS C 3 59  ? -57.475 -51.342 13.567  1   29.17 ? 90  LYS C N   1 
ATOM   2550 C  CA  . LYS C 3 59  ? -57.921 -51.97  14.802  1   30.34 ? 90  LYS C CA  1 
ATOM   2551 C  C   . LYS C 3 59  ? -57.66  -53.479 14.806  1   29.78 ? 90  LYS C C   1 
ATOM   2552 O  O   . LYS C 3 59  ? -57.746 -54.132 13.776  1   29.36 ? 90  LYS C O   1 
ATOM   2553 C  CB  . LYS C 3 59  ? -59.428 -51.665 14.965  1   34.59 ? 90  LYS C CB  1 
ATOM   2554 C  CG  . LYS C 3 59  ? -60.12  -52.33  16.14   1   40.68 ? 90  LYS C CG  1 
ATOM   2555 C  CD  . LYS C 3 59  ? -61.586 -51.898 16.26   1   47.13 ? 90  LYS C CD  1 
ATOM   2556 C  CE  . LYS C 3 59  ? -62.403 -52.109 15.006  1   51.35 ? 90  LYS C CE  1 
ATOM   2557 N  NZ  . LYS C 3 59  ? -63.855 -51.8   15.218  1   54.24 ? 90  LYS C NZ  1 
ATOM   2558 N  N   . ARG C 3 60  ? -57.343 -54.02  15.974  1   29.38 ? 91  ARG C N   1 
ATOM   2559 C  CA  . ARG C 3 60  ? -57.071 -55.427 16.231  1   31.34 ? 91  ARG C CA  1 
ATOM   2560 C  C   . ARG C 3 60  ? -58.35  -56.237 15.95   1   33.26 ? 91  ARG C C   1 
ATOM   2561 O  O   . ARG C 3 60  ? -59.447 -55.778 16.278  1   33.02 ? 91  ARG C O   1 
ATOM   2562 C  CB  . ARG C 3 60  ? -56.717 -55.53  17.741  1   32.64 ? 91  ARG C CB  1 
ATOM   2563 C  CG  . ARG C 3 60  ? -56.153 -56.837 18.234  1   35.92 ? 91  ARG C CG  1 
ATOM   2564 C  CD  . ARG C 3 60  ? -55.663 -56.671 19.684  1   35.69 ? 91  ARG C CD  1 
ATOM   2565 N  NE  . ARG C 3 60  ? -54.589 -55.688 19.735  1   38.01 ? 91  ARG C NE  1 
ATOM   2566 C  CZ  . ARG C 3 60  ? -54.236 -54.983 20.807  1   37.2  ? 91  ARG C CZ  1 
ATOM   2567 N  NH1 . ARG C 3 60  ? -54.839 -55.185 21.972  1   38.16 ? 91  ARG C NH1 1 
ATOM   2568 N  NH2 . ARG C 3 60  ? -53.263 -54.082 20.723  1   32.05 ? 91  ARG C NH2 1 
ATOM   2569 N  N   . GLU C 3 61  ? -58.213 -57.434 15.38   1   35.28 ? 92  GLU C N   1 
ATOM   2570 C  CA  . GLU C 3 61  ? -59.368 -58.276 15.074  1   38.21 ? 92  GLU C CA  1 
ATOM   2571 C  C   . GLU C 3 61  ? -59.984 -58.859 16.351  1   39.96 ? 92  GLU C C   1 
ATOM   2572 O  O   . GLU C 3 61  ? -61.197 -58.78  16.538  1   41.56 ? 92  GLU C O   1 
ATOM   2573 C  CB  . GLU C 3 61  ? -58.99  -59.423 14.103  1   42.28 ? 92  GLU C CB  1 
ATOM   2574 C  CG  . GLU C 3 61  ? -60.21  -60.188 13.613  1   50.98 ? 92  GLU C CG  1 
ATOM   2575 C  CD  . GLU C 3 61  ? -60.081 -61.69  13.437  1   63.17 ? 92  GLU C CD  1 
ATOM   2576 O  OE1 . GLU C 3 61  ? -60.29  -62.168 12.299  1   66.28 ? 92  GLU C OE1 1 
ATOM   2577 O  OE2 . GLU C 3 61  ? -59.812 -62.396 14.437  1   67.17 ? 92  GLU C OE2 1 
ATOM   2578 N  N   . LYS C 3 62  ? -59.157 -59.443 17.226  1   39.4  ? 93  LYS C N   1 
ATOM   2579 C  CA  . LYS C 3 62  ? -59.655 -60.071 18.441  1   39.49 ? 93  LYS C CA  1 
ATOM   2580 C  C   . LYS C 3 62  ? -59.051 -59.38  19.634  1   38.69 ? 93  LYS C C   1 
ATOM   2581 O  O   . LYS C 3 62  ? -57.835 -59.377 19.79   1   40.17 ? 93  LYS C O   1 
ATOM   2582 C  CB  . LYS C 3 62  ? -59.34  -61.576 18.456  1   41.99 ? 93  LYS C CB  1 
ATOM   2583 N  N   . SER C 3 63  ? -59.889 -58.756 20.448  1   36.47 ? 94  SER C N   1 
ATOM   2584 C  CA  . SER C 3 63  ? -59.407 -58.003 21.592  1   35.59 ? 94  SER C CA  1 
ATOM   2585 C  C   . SER C 3 63  ? -59.595 -58.661 22.947  1   34.02 ? 94  SER C C   1 
ATOM   2586 O  O   . SER C 3 63  ? -60.571 -59.372 23.166  1   32.86 ? 94  SER C O   1 
ATOM   2587 C  CB  . SER C 3 63  ? -60.089 -56.642 21.623  1   37.32 ? 94  SER C CB  1 
ATOM   2588 O  OG  . SER C 3 63  ? -59.438 -55.734 20.754  1   38.46 ? 94  SER C OG  1 
ATOM   2589 N  N   . ASP C 3 64  ? -58.654 -58.364 23.858  1   33.06 ? 95  ASP C N   1 
ATOM   2590 C  CA  . ASP C 3 64  ? -58.668 -58.7   25.278  1   33.96 ? 95  ASP C CA  1 
ATOM   2591 C  C   . ASP C 3 64  ? -59.096 -57.432 26.02   1   33.66 ? 95  ASP C C   1 
ATOM   2592 O  O   . ASP C 3 64  ? -58.761 -56.307 25.639  1   34.83 ? 95  ASP C O   1 
ATOM   2593 C  CB  . ASP C 3 64  ? -57.266 -59.089 25.788  1   36.31 ? 95  ASP C CB  1 
ATOM   2594 C  CG  . ASP C 3 64  ? -56.88  -60.536 25.565  1   43.67 ? 95  ASP C CG  1 
ATOM   2595 O  OD1 . ASP C 3 64  ? -57.727 -61.31  25.084  1   44.1  ? 95  ASP C OD1 1 
ATOM   2596 O  OD2 . ASP C 3 64  ? -55.724 -60.892 25.869  1   48.35 ? 95  ASP C OD2 1 
ATOM   2597 N  N   . ILE C 3 65  ? -59.757 -57.634 27.126  1   31.97 ? 96  ILE C N   1 
ATOM   2598 C  CA  . ILE C 3 65  ? -60.287 -56.619 27.995  1   31.25 ? 96  ILE C CA  1 
ATOM   2599 C  C   . ILE C 3 65  ? -59.661 -56.833 29.379  1   29.14 ? 96  ILE C C   1 
ATOM   2600 O  O   . ILE C 3 65  ? -59.363 -57.98  29.751  1   30.32 ? 96  ILE C O   1 
ATOM   2601 C  CB  . ILE C 3 65  ? -61.826 -56.926 27.986  1   33.07 ? 96  ILE C CB  1 
ATOM   2602 C  CG1 . ILE C 3 65  ? -62.46  -56.507 26.62   1   34.89 ? 96  ILE C CG1 1 
ATOM   2603 C  CG2 . ILE C 3 65  ? -62.591 -56.344 29.151  1   34.04 ? 96  ILE C CG2 1 
ATOM   2604 C  CD1 . ILE C 3 65  ? -62.232 -55.113 26.314  1   35.16 ? 96  ILE C CD1 1 
ATOM   2605 N  N   . LEU C 3 66  ? -59.444 -55.751 30.135  1   26.08 ? 97  LEU C N   1 
ATOM   2606 C  CA  . LEU C 3 66  ? -58.944 -55.915 31.505  1   25.31 ? 97  LEU C CA  1 
ATOM   2607 C  C   . LEU C 3 66  ? -60.136 -56.307 32.344  1   25.72 ? 97  LEU C C   1 
ATOM   2608 O  O   . LEU C 3 66  ? -61.151 -55.619 32.291  1   26.44 ? 97  LEU C O   1 
ATOM   2609 C  CB  . LEU C 3 66  ? -58.41  -54.591 32.036  1   24.85 ? 97  LEU C CB  1 
ATOM   2610 C  CG  . LEU C 3 66  ? -57.103 -54.142 31.393  1   27.11 ? 97  LEU C CG  1 
ATOM   2611 C  CD1 . LEU C 3 66  ? -56.81  -52.703 31.748  1   26.92 ? 97  LEU C CD1 1 
ATOM   2612 C  CD2 . LEU C 3 66  ? -55.965 -55.029 31.865  1   28.53 ? 97  LEU C CD2 1 
ATOM   2613 N  N   . VAL C 3 67  ? -60.023 -57.371 33.151  1   25.71 ? 98  VAL C N   1 
ATOM   2614 C  CA  . VAL C 3 67  ? -61.078 -57.726 34.091  1   26.26 ? 98  VAL C CA  1 
ATOM   2615 C  C   . VAL C 3 67  ? -60.469 -57.843 35.48   1   26.81 ? 98  VAL C C   1 
ATOM   2616 O  O   . VAL C 3 67  ? -59.531 -58.611 35.667  1   27.34 ? 98  VAL C O   1 
ATOM   2617 C  CB  . VAL C 3 67  ? -61.916 -58.97  33.715  1   27.38 ? 98  VAL C CB  1 
ATOM   2618 C  CG1 . VAL C 3 67  ? -63.055 -59.166 34.722  1   27.67 ? 98  VAL C CG1 1 
ATOM   2619 C  CG2 . VAL C 3 67  ? -62.462 -58.851 32.285  1   28.05 ? 98  VAL C CG2 1 
ATOM   2620 N  N   . PHE C 3 68  ? -60.933 -57.033 36.429  1   25.88 ? 99  PHE C N   1 
ATOM   2621 C  CA  . PHE C 3 68  ? -60.4   -57.07  37.794  1   26.36 ? 99  PHE C CA  1 
ATOM   2622 C  C   . PHE C 3 68  ? -61.425 -57.744 38.693  1   27.14 ? 99  PHE C C   1 
ATOM   2623 O  O   . PHE C 3 68  ? -62.557 -57.264 38.845  1   26.79 ? 99  PHE C O   1 
ATOM   2624 C  CB  . PHE C 3 68  ? -60.061 -55.656 38.292  1   26.22 ? 99  PHE C CB  1 
ATOM   2625 C  CG  . PHE C 3 68  ? -58.822 -55.023 37.679  1   26.74 ? 99  PHE C CG  1 
ATOM   2626 C  CD1 . PHE C 3 68  ? -58.795 -54.656 36.34   1   28.84 ? 99  PHE C CD1 1 
ATOM   2627 C  CD2 . PHE C 3 68  ? -57.706 -54.756 38.454  1   27.8  ? 99  PHE C CD2 1 
ATOM   2628 C  CE1 . PHE C 3 68  ? -57.681 -54.022 35.796  1   29.35 ? 99  PHE C CE1 1 
ATOM   2629 C  CE2 . PHE C 3 68  ? -56.57  -54.18  37.893  1   28.75 ? 99  PHE C CE2 1 
ATOM   2630 C  CZ  . PHE C 3 68  ? -56.571 -53.802 36.572  1   29.05 ? 99  PHE C CZ  1 
ATOM   2631 N  N   . HIS C 3 69  ? -61.053 -58.883 39.252  1   27.96 ? 100 HIS C N   1 
ATOM   2632 C  CA  . HIS C 3 69  ? -61.924 -59.664 40.112  1   28.13 ? 100 HIS C CA  1 
ATOM   2633 C  C   . HIS C 3 69  ? -61.758 -59.297 41.583  1   28.68 ? 100 HIS C C   1 
ATOM   2634 O  O   . HIS C 3 69  ? -60.771 -58.653 41.97   1   28.43 ? 100 HIS C O   1 
ATOM   2635 C  CB  . HIS C 3 69  ? -61.644 -61.186 39.925  1   29.43 ? 100 HIS C CB  1 
ATOM   2636 C  CG  . HIS C 3 69  ? -62.005 -61.678 38.55   1   33.99 ? 100 HIS C CG  1 
ATOM   2637 N  ND1 . HIS C 3 69  ? -61.077 -61.702 37.531  1   36.9  ? 100 HIS C ND1 1 
ATOM   2638 C  CD2 . HIS C 3 69  ? -63.193 -62.114 38.076  1   35.66 ? 100 HIS C CD2 1 
ATOM   2639 C  CE1 . HIS C 3 69  ? -61.722 -62.147 36.46   1   37.78 ? 100 HIS C CE1 1 
ATOM   2640 N  NE2 . HIS C 3 69  ? -63.004 -62.394 36.734  1   38.11 ? 100 HIS C NE2 1 
ATOM   2641 N  N   . ASN C 3 70  ? -62.71  -59.766 42.405  1   28.27 ? 101 ASN C N   1 
ATOM   2642 C  CA  . ASN C 3 70  ? -62.638 -59.66  43.861  1   28.83 ? 101 ASN C CA  1 
ATOM   2643 C  C   . ASN C 3 70  ? -62.517 -58.233 44.38   1   29.95 ? 101 ASN C C   1 
ATOM   2644 O  O   . ASN C 3 70  ? -61.802 -57.988 45.35   1   30.12 ? 101 ASN C O   1 
ATOM   2645 C  CB  . ASN C 3 70  ? -61.496 -60.545 44.377  1   30.33 ? 101 ASN C CB  1 
ATOM   2646 C  CG  . ASN C 3 70  ? -61.789 -62.002 44.135  1   34.7  ? 101 ASN C CG  1 
ATOM   2647 O  OD1 . ASN C 3 70  ? -62.942 -62.425 44.222  1   36.84 ? 101 ASN C OD1 1 
ATOM   2648 N  ND2 . ASN C 3 70  ? -60.784 -62.802 43.794  1   34.54 ? 101 ASN C ND2 1 
ATOM   2649 N  N   . GLY C 3 71  ? -63.234 -57.311 43.751  1   30.81 ? 102 GLY C N   1 
ATOM   2650 C  CA  . GLY C 3 71  ? -63.308 -55.949 44.248  1   32.09 ? 102 GLY C CA  1 
ATOM   2651 C  C   . GLY C 3 71  ? -64.152 -55.888 45.518  1   33.41 ? 102 GLY C C   1 
ATOM   2652 O  O   . GLY C 3 71  ? -65.077 -56.689 45.712  1   32.69 ? 102 GLY C O   1 
ATOM   2653 N  N   . GLU C 3 72  ? -63.843 -54.935 46.39   1   34.97 ? 103 GLU C N   1 
ATOM   2654 C  CA  . GLU C 3 72  ? -64.569 -54.733 47.646  1   37.99 ? 103 GLU C CA  1 
ATOM   2655 C  C   . GLU C 3 72  ? -65.439 -53.5   47.477  1   40.22 ? 103 GLU C C   1 
ATOM   2656 O  O   . GLU C 3 72  ? -64.931 -52.438 47.141  1   39.67 ? 103 GLU C O   1 
ATOM   2657 C  CB  . GLU C 3 72  ? -63.597 -54.457 48.784  1   41.48 ? 103 GLU C CB  1 
ATOM   2658 C  CG  . GLU C 3 72  ? -62.37  -55.343 48.832  1   50.38 ? 103 GLU C CG  1 
ATOM   2659 C  CD  . GLU C 3 72  ? -61.468 -54.997 50.005  1   57.8  ? 103 GLU C CD  1 
ATOM   2660 O  OE1 . GLU C 3 72  ? -62     -54.515 51.032  1   60.55 ? 103 GLU C OE1 1 
ATOM   2661 O  OE2 . GLU C 3 72  ? -60.233 -55.186 49.894  1   58.88 ? 103 GLU C OE2 1 
ATOM   2662 N  N   . VAL C 3 73  ? -66.721 -53.622 47.754  1   42.33 ? 104 VAL C N   1 
ATOM   2663 C  CA  . VAL C 3 73  ? -67.682 -52.538 47.563  1   44.69 ? 104 VAL C CA  1 
ATOM   2664 C  C   . VAL C 3 73  ? -68.205 -52.03  48.893  1   47.29 ? 104 VAL C C   1 
ATOM   2665 O  O   . VAL C 3 73  ? -68.598 -52.828 49.761  1   47.81 ? 104 VAL C O   1 
ATOM   2666 C  CB  . VAL C 3 73  ? -68.893 -52.999 46.717  1   45.76 ? 104 VAL C CB  1 
ATOM   2667 C  CG1 . VAL C 3 73  ? -69.753 -51.811 46.288  1   46.34 ? 104 VAL C CG1 1 
ATOM   2668 C  CG2 . VAL C 3 73  ? -68.469 -53.823 45.509  1   46.56 ? 104 VAL C CG2 1 
ATOM   2669 N  N   . LYS C 3 74  ? -68.255 -50.704 49.039  1   48.54 ? 105 LYS C N   1 
ATOM   2670 C  CA  . LYS C 3 74  ? -68.833 -50.051 50.21   1   50.46 ? 105 LYS C CA  1 
ATOM   2671 C  C   . LYS C 3 74  ? -69.94  -49.163 49.631  1   52.57 ? 105 LYS C C   1 
ATOM   2672 O  O   . LYS C 3 74  ? -69.651 -48.318 48.782  1   51.68 ? 105 LYS C O   1 
ATOM   2673 C  CB  . LYS C 3 74  ? -67.767 -49.219 50.939  1   52.07 ? 105 LYS C CB  1 
ATOM   2674 C  CG  . LYS C 3 74  ? -68.311 -48.388 52.088  1   56.25 ? 105 LYS C CG  1 
ATOM   2675 N  N   . THR C 3 75  ? -71.207 -49.423 49.995  1   54.46 ? 106 THR C N   1 
ATOM   2676 C  CA  . THR C 3 75  ? -72.34  -48.664 49.463  1   57.13 ? 106 THR C CA  1 
ATOM   2677 C  C   . THR C 3 75  ? -72.919 -47.719 50.52   1   58.31 ? 106 THR C C   1 
ATOM   2678 O  O   . THR C 3 75  ? -73.152 -48.137 51.66   1   58.89 ? 106 THR C O   1 
ATOM   2679 C  CB  . THR C 3 75  ? -73.432 -49.616 48.963  1   59.26 ? 106 THR C CB  1 
ATOM   2680 O  OG1 . THR C 3 75  ? -73.805 -50.484 50.035  1   61.29 ? 106 THR C OG1 1 
ATOM   2681 C  CG2 . THR C 3 75  ? -72.997 -50.436 47.762  1   59.89 ? 106 THR C CG2 1 
ATOM   2682 N  N   . SER C 3 81  ? -73.94  -43.422 46.497  1   54.32 ? 112 SER C N   1 
ATOM   2683 C  CA  . SER C 3 81  ? -72.494 -43.454 46.709  1   54.47 ? 112 SER C CA  1 
ATOM   2684 C  C   . SER C 3 81  ? -71.92  -44.877 46.685  1   53.2  ? 112 SER C C   1 
ATOM   2685 O  O   . SER C 3 81  ? -72.521 -45.802 47.23   1   54.15 ? 112 SER C O   1 
ATOM   2686 C  CB  . SER C 3 81  ? -72.129 -42.714 47.996  1   57.6  ? 112 SER C CB  1 
ATOM   2687 O  OG  . SER C 3 81  ? -70.93  -43.131 48.635  1   61.76 ? 112 SER C OG  1 
ATOM   2688 N  N   . TYR C 3 82  ? -70.75  -45.039 46.055  1   51    ? 113 TYR C N   1 
ATOM   2689 C  CA  . TYR C 3 82  ? -70.023 -46.308 45.989  1   49.17 ? 113 TYR C CA  1 
ATOM   2690 C  C   . TYR C 3 82  ? -68.54  -46.01  46.149  1   46.66 ? 113 TYR C C   1 
ATOM   2691 O  O   . TYR C 3 82  ? -68.043 -45.002 45.639  1   46.02 ? 113 TYR C O   1 
ATOM   2692 C  CB  . TYR C 3 82  ? -70.212 -47.029 44.635  1   49.54 ? 113 TYR C CB  1 
ATOM   2693 C  CG  . TYR C 3 82  ? -71.632 -47.444 44.323  1   51.02 ? 113 TYR C CG  1 
ATOM   2694 C  CD1 . TYR C 3 82  ? -72.506 -46.579 43.675  1   51.98 ? 113 TYR C CD1 1 
ATOM   2695 C  CD2 . TYR C 3 82  ? -72.082 -48.726 44.606  1   52.17 ? 113 TYR C CD2 1 
ATOM   2696 C  CE1 . TYR C 3 82  ? -73.802 -46.961 43.363  1   53.11 ? 113 TYR C CE1 1 
ATOM   2697 C  CE2 . TYR C 3 82  ? -73.387 -49.114 44.315  1   53.36 ? 113 TYR C CE2 1 
ATOM   2698 C  CZ  . TYR C 3 82  ? -74.24  -48.231 43.68   1   54.67 ? 113 TYR C CZ  1 
ATOM   2699 O  OH  . TYR C 3 82  ? -75.544 -48.585 43.397  1   57.7  ? 113 TYR C OH  1 
ATOM   2700 N  N   . GLN C 3 83  ? -67.832 -46.903 46.834  1   44.41 ? 114 GLN C N   1 
ATOM   2701 C  CA  . GLN C 3 83  ? -66.392 -46.833 47.007  1   43    ? 114 GLN C CA  1 
ATOM   2702 C  C   . GLN C 3 83  ? -65.951 -48.268 46.765  1   40.4  ? 114 GLN C C   1 
ATOM   2703 O  O   . GLN C 3 83  ? -66.325 -49.157 47.525  1   40.24 ? 114 GLN C O   1 
ATOM   2704 C  CB  . GLN C 3 83  ? -66.037 -46.376 48.441  1   46.34 ? 114 GLN C CB  1 
ATOM   2705 C  CG  . GLN C 3 83  ? -64.535 -46.302 48.708  1   53.32 ? 114 GLN C CG  1 
ATOM   2706 C  CD  . GLN C 3 83  ? -63.816 -45.392 47.738  1   60.87 ? 114 GLN C CD  1 
ATOM   2707 O  OE1 . GLN C 3 83  ? -62.947 -45.824 46.974  1   64.2  ? 114 GLN C OE1 1 
ATOM   2708 N  NE2 . GLN C 3 83  ? -64.169 -44.117 47.728  1   61.69 ? 114 GLN C NE2 1 
ATOM   2709 N  N   . ILE C 3 84  ? -65.257 -48.52  45.656  1   38.21 ? 115 ILE C N   1 
ATOM   2710 C  CA  . ILE C 3 84  ? -64.856 -49.868 45.282  1   36.47 ? 115 ILE C CA  1 
ATOM   2711 C  C   . ILE C 3 84  ? -63.362 -49.924 45.082  1   35.68 ? 115 ILE C C   1 
ATOM   2712 O  O   . ILE C 3 84  ? -62.812 -49.066 44.393  1   35.53 ? 115 ILE C O   1 
ATOM   2713 C  CB  . ILE C 3 84  ? -65.6   -50.355 44.01   1   36.24 ? 115 ILE C CB  1 
ATOM   2714 C  CG1 . ILE C 3 84  ? -67.126 -50.007 44.044  1   36.14 ? 115 ILE C CG1 1 
ATOM   2715 C  CG2 . ILE C 3 84  ? -65.391 -51.855 43.821  1   36.73 ? 115 ILE C CG2 1 
ATOM   2716 C  CD1 . ILE C 3 84  ? -67.868 -50.297 42.749  1   36.24 ? 115 ILE C CD1 1 
ATOM   2717 N  N   . ASN C 3 85  ? -62.703 -50.947 45.645  1   34.75 ? 116 ASN C N   1 
ATOM   2718 C  CA  . ASN C 3 85  ? -61.254 -51.122 45.56   1   34.45 ? 116 ASN C CA  1 
ATOM   2719 C  C   . ASN C 3 85  ? -60.949 -52.511 45.026  1   32.48 ? 116 ASN C C   1 
ATOM   2720 O  O   . ASN C 3 85  ? -61.554 -53.488 45.475  1   33.31 ? 116 ASN C O   1 
ATOM   2721 C  CB  . ASN C 3 85  ? -60.652 -51.021 46.962  1   38.94 ? 116 ASN C CB  1 
ATOM   2722 C  CG  . ASN C 3 85  ? -60.681 -49.635 47.532  1   46.27 ? 116 ASN C CG  1 
ATOM   2723 O  OD1 . ASN C 3 85  ? -59.926 -48.759 47.1    1   49.3  ? 116 ASN C OD1 1 
ATOM   2724 N  ND2 . ASN C 3 85  ? -61.546 -49.405 48.512  1   47.05 ? 116 ASN C ND2 1 
ATOM   2725 N  N   . TRP C 3 86  ? -59.982 -52.618 44.138  1   30.34 ? 117 TRP C N   1 
ATOM   2726 C  CA  . TRP C 3 86  ? -59.581 -53.901 43.591  1   29.21 ? 117 TRP C CA  1 
ATOM   2727 C  C   . TRP C 3 86  ? -58.14  -54.208 43.961  1   29    ? 117 TRP C C   1 
ATOM   2728 O  O   . TRP C 3 86  ? -57.273 -53.331 43.935  1   28.99 ? 117 TRP C O   1 
ATOM   2729 C  CB  . TRP C 3 86  ? -59.745 -53.925 42.049  1   28.55 ? 117 TRP C CB  1 
ATOM   2730 C  CG  . TRP C 3 86  ? -61.18  -53.988 41.611  1   28.24 ? 117 TRP C CG  1 
ATOM   2731 C  CD1 . TRP C 3 86  ? -61.908 -55.11  41.355  1   28.75 ? 117 TRP C CD1 1 
ATOM   2732 C  CD2 . TRP C 3 86  ? -62.057 -52.875 41.365  1   28.58 ? 117 TRP C CD2 1 
ATOM   2733 N  NE1 . TRP C 3 86  ? -63.214 -54.769 41.052  1   28.96 ? 117 TRP C NE1 1 
ATOM   2734 C  CE2 . TRP C 3 86  ? -63.319 -53.403 41.008  1   29.35 ? 117 TRP C CE2 1 
ATOM   2735 C  CE3 . TRP C 3 86  ? -61.888 -51.485 41.372  1   29.32 ? 117 TRP C CE3 1 
ATOM   2736 C  CZ2 . TRP C 3 86  ? -64.397 -52.587 40.637  1   30.63 ? 117 TRP C CZ2 1 
ATOM   2737 C  CZ3 . TRP C 3 86  ? -62.964 -50.678 41.03   1   30.48 ? 117 TRP C CZ3 1 
ATOM   2738 C  CH2 . TRP C 3 86  ? -64.198 -51.229 40.664  1   30.98 ? 117 TRP C CH2 1 
ATOM   2739 N  N   . PRO C 3 87  ? -57.838 -55.486 44.204  1   28.66 ? 118 PRO C N   1 
ATOM   2740 C  CA  . PRO C 3 87  ? -56.451 -55.849 44.534  1   28.42 ? 118 PRO C CA  1 
ATOM   2741 C  C   . PRO C 3 87  ? -55.524 -56.084 43.341  1   28.54 ? 118 PRO C C   1 
ATOM   2742 O  O   . PRO C 3 87  ? -54.31  -56.168 43.535  1   28.65 ? 118 PRO C O   1 
ATOM   2743 C  CB  . PRO C 3 87  ? -56.627 -57.11  45.361  1   29.48 ? 118 PRO C CB  1 
ATOM   2744 C  CG  . PRO C 3 87  ? -57.87  -57.747 44.735  1   29.82 ? 118 PRO C CG  1 
ATOM   2745 C  CD  . PRO C 3 87  ? -58.757 -56.641 44.3    1   27.7  ? 118 PRO C CD  1 
ATOM   2746 N  N   . GLY C 3 88  ? -56.093 -56.191 42.142  1   28.23 ? 119 GLY C N   1 
ATOM   2747 C  CA  . GLY C 3 88  ? -55.389 -56.524 40.916  1   27.92 ? 119 GLY C CA  1 
ATOM   2748 C  C   . GLY C 3 88  ? -54.236 -55.632 40.535  1   27.46 ? 119 GLY C C   1 
ATOM   2749 O  O   . GLY C 3 88  ? -54.213 -54.445 40.874  1   27.43 ? 119 GLY C O   1 
ATOM   2750 N  N   . GLU C 3 89  ? -53.269 -56.216 39.838  1   26.52 ? 120 GLU C N   1 
ATOM   2751 C  CA  . GLU C 3 89  ? -52.148 -55.463 39.314  1   26.35 ? 120 GLU C CA  1 
ATOM   2752 C  C   . GLU C 3 89  ? -51.906 -55.891 37.871  1   26.47 ? 120 GLU C C   1 
ATOM   2753 O  O   . GLU C 3 89  ? -52.175 -57.042 37.493  1   27    ? 120 GLU C O   1 
ATOM   2754 C  CB  . GLU C 3 89  ? -50.896 -55.65  40.181  1   28.93 ? 120 GLU C CB  1 
ATOM   2755 C  CG  . GLU C 3 89  ? -50.309 -57.039 40.103  1   34.37 ? 120 GLU C CG  1 
ATOM   2756 C  CD  . GLU C 3 89  ? -49.195 -57.326 41.09   1   42.85 ? 120 GLU C CD  1 
ATOM   2757 O  OE1 . GLU C 3 89  ? -48.877 -56.443 41.922  1   40.91 ? 120 GLU C OE1 1 
ATOM   2758 O  OE2 . GLU C 3 89  ? -48.642 -58.448 41.024  1   46.13 ? 120 GLU C OE2 1 
ATOM   2759 N  N   . VAL C 3 90  ? -51.438 -54.951 37.051  1   25.39 ? 121 VAL C N   1 
ATOM   2760 C  CA  . VAL C 3 90  ? -51.116 -55.261 35.666  1   25.21 ? 121 VAL C CA  1 
ATOM   2761 C  C   . VAL C 3 90  ? -49.937 -54.409 35.201  1   25.2  ? 121 VAL C C   1 
ATOM   2762 O  O   . VAL C 3 90  ? -49.713 -53.333 35.748  1   25.76 ? 121 VAL C O   1 
ATOM   2763 C  CB  . VAL C 3 90  ? -52.372 -55.089 34.754  1   25.83 ? 121 VAL C CB  1 
ATOM   2764 C  CG1 . VAL C 3 90  ? -52.81  -53.622 34.664  1   25.7  ? 121 VAL C CG1 1 
ATOM   2765 C  CG2 . VAL C 3 90  ? -52.139 -55.677 33.361  1   27.23 ? 121 VAL C CG2 1 
ATOM   2766 N  N   . THR C 3 91  ? -49.158 -54.903 34.227  1   23.84 ? 122 THR C N   1 
ATOM   2767 C  CA  . THR C 3 91  ? -48.06  -54.13  33.669  1   22.97 ? 122 THR C CA  1 
ATOM   2768 C  C   . THR C 3 91  ? -48.506 -53.474 32.363  1   23.15 ? 122 THR C C   1 
ATOM   2769 O  O   . THR C 3 91  ? -49.081 -54.143 31.509  1   22.88 ? 122 THR C O   1 
ATOM   2770 C  CB  . THR C 3 91  ? -46.838 -55.018 33.516  1   23.75 ? 122 THR C CB  1 
ATOM   2771 O  OG1 . THR C 3 91  ? -46.438 -55.368 34.834  1   25.4  ? 122 THR C OG1 1 
ATOM   2772 C  CG2 . THR C 3 91  ? -45.682 -54.333 32.749  1   24.82 ? 122 THR C CG2 1 
ATOM   2773 N  N   . MET C 3 92  ? -48.291 -52.157 32.227  1   21.95 ? 123 MET C N   1 
ATOM   2774 C  CA  . MET C 3 92  ? -48.649 -51.433 31.008  1   21.84 ? 123 MET C CA  1 
ATOM   2775 C  C   . MET C 3 92  ? -47.347 -51.057 30.323  1   22.69 ? 123 MET C C   1 
ATOM   2776 O  O   . MET C 3 92  ? -46.477 -50.481 30.969  1   22.46 ? 123 MET C O   1 
ATOM   2777 C  CB  . MET C 3 92  ? -49.42  -50.145 31.337  1   21.91 ? 123 MET C CB  1 
ATOM   2778 C  CG  . MET C 3 92  ? -49.725 -49.266 30.107  1   24.24 ? 123 MET C CG  1 
ATOM   2779 S  SD  . MET C 3 92  ? -50.723 -47.822 30.527  1   24.48 ? 123 MET C SD  1 
ATOM   2780 C  CE  . MET C 3 92  ? -49.468 -46.707 31.218  1   25.62 ? 123 MET C CE  1 
ATOM   2781 N  N   . LYS C 3 93  ? -47.212 -51.405 29.034  1   22.45 ? 124 LYS C N   1 
ATOM   2782 C  CA  . LYS C 3 93  ? -46.035 -51.046 28.233  1   22.95 ? 124 LYS C CA  1 
ATOM   2783 C  C   . LYS C 3 93  ? -46.543 -50.034 27.191  1   22.28 ? 124 LYS C C   1 
ATOM   2784 O  O   . LYS C 3 93  ? -47.574 -50.269 26.536  1   21.82 ? 124 LYS C O   1 
ATOM   2785 C  CB  . LYS C 3 93  ? -45.463 -52.288 27.522  1   26.61 ? 124 LYS C CB  1 
ATOM   2786 C  CG  . LYS C 3 93  ? -44.938 -53.376 28.489  1   34.06 ? 124 LYS C CG  1 
ATOM   2787 C  CD  . LYS C 3 93  ? -43.426 -53.625 28.355  1   41.98 ? 124 LYS C CD  1 
ATOM   2788 C  CE  . LYS C 3 93  ? -42.922 -54.614 29.39   1   48.63 ? 124 LYS C CE  1 
ATOM   2789 N  NZ  . LYS C 3 93  ? -42.455 -55.901 28.774  1   51.99 ? 124 LYS C NZ  1 
ATOM   2790 N  N   . LEU C 3 94  ? -45.785 -48.944 27      1   21.9  ? 125 LEU C N   1 
ATOM   2791 C  CA  . LEU C 3 94  ? -46.107 -47.901 26.038  1   21.65 ? 125 LEU C CA  1 
ATOM   2792 C  C   . LEU C 3 94  ? -45.025 -47.897 24.99   1   22.12 ? 125 LEU C C   1 
ATOM   2793 O  O   . LEU C 3 94  ? -43.9   -47.467 25.269  1   23.03 ? 125 LEU C O   1 
ATOM   2794 C  CB  . LEU C 3 94  ? -46.127 -46.523 26.743  1   21.69 ? 125 LEU C CB  1 
ATOM   2795 C  CG  . LEU C 3 94  ? -47.146 -46.407 27.875  1   22.54 ? 125 LEU C CG  1 
ATOM   2796 C  CD1 . LEU C 3 94  ? -46.979 -45.104 28.605  1   23.5  ? 125 LEU C CD1 1 
ATOM   2797 C  CD2 . LEU C 3 94  ? -48.578 -46.559 27.34   1   22.52 ? 125 LEU C CD2 1 
ATOM   2798 N  N   . GLY C 3 95  ? -45.337 -48.446 23.833  1   21.95 ? 126 GLY C N   1 
ATOM   2799 C  CA  . GLY C 3 95  ? -44.388 -48.478 22.725  1   21.28 ? 126 GLY C CA  1 
ATOM   2800 C  C   . GLY C 3 95  ? -43.218 -49.371 23.011  1   21.6  ? 126 GLY C C   1 
ATOM   2801 O  O   . GLY C 3 95  ? -43.368 -50.568 23.285  1   21.81 ? 126 GLY C O   1 
ATOM   2802 N  N   . TYR C 3 96  ? -42.039 -48.787 22.961  1   21.63 ? 127 TYR C N   1 
ATOM   2803 C  CA  . TYR C 3 96  ? -40.786 -49.491 23.223  1   22.34 ? 127 TYR C CA  1 
ATOM   2804 C  C   . TYR C 3 96  ? -40.268 -49.285 24.669  1   24.62 ? 127 TYR C C   1 
ATOM   2805 O  O   . TYR C 3 96  ? -39.167 -49.718 24.99   1   24.65 ? 127 TYR C O   1 
ATOM   2806 C  CB  . TYR C 3 96  ? -39.737 -49.037 22.19   1   21.74 ? 127 TYR C CB  1 
ATOM   2807 C  CG  . TYR C 3 96  ? -40.121 -49.49  20.796  1   22.06 ? 127 TYR C CG  1 
ATOM   2808 C  CD1 . TYR C 3 96  ? -41.097 -48.818 20.064  1   21.85 ? 127 TYR C CD1 1 
ATOM   2809 C  CD2 . TYR C 3 96  ? -39.568 -50.631 20.243  1   22.23 ? 127 TYR C CD2 1 
ATOM   2810 C  CE1 . TYR C 3 96  ? -41.496 -49.266 18.811  1   22.37 ? 127 TYR C CE1 1 
ATOM   2811 C  CE2 . TYR C 3 96  ? -39.932 -51.062 18.971  1   22.74 ? 127 TYR C CE2 1 
ATOM   2812 C  CZ  . TYR C 3 96  ? -40.947 -50.419 18.291  1   22.79 ? 127 TYR C CZ  1 
ATOM   2813 O  OH  . TYR C 3 96  ? -41.305 -50.87  17.044  1   22.85 ? 127 TYR C OH  1 
ATOM   2814 N  N   . GLY C 3 97  ? -41.073 -48.676 25.524  1   27.06 ? 128 GLY C N   1 
ATOM   2815 C  CA  . GLY C 3 97  ? -40.673 -48.404 26.903  1   28.66 ? 128 GLY C CA  1 
ATOM   2816 C  C   . GLY C 3 97  ? -40.627 -49.613 27.812  1   30.45 ? 128 GLY C C   1 
ATOM   2817 O  O   . GLY C 3 97  ? -41.1   -50.698 27.457  1   31.31 ? 128 GLY C O   1 
ATOM   2818 N  N   . ASP C 3 98  ? -40.051 -49.428 28.992  1   30.42 ? 129 ASP C N   1 
ATOM   2819 C  CA  . ASP C 3 98  ? -40.043 -50.471 29.996  1   32.83 ? 129 ASP C CA  1 
ATOM   2820 C  C   . ASP C 3 98  ? -41.471 -50.404 30.616  1   33.89 ? 129 ASP C C   1 
ATOM   2821 O  O   . ASP C 3 98  ? -42.118 -49.341 30.617  1   34.03 ? 129 ASP C O   1 
ATOM   2822 C  CB  . ASP C 3 98  ? -38.954 -50.18  31.053  1   36.31 ? 129 ASP C CB  1 
ATOM   2823 C  CG  . ASP C 3 98  ? -37.532 -50.137 30.503  1   45.14 ? 129 ASP C CG  1 
ATOM   2824 O  OD1 . ASP C 3 98  ? -37.365 -50.207 29.262  1   45.28 ? 129 ASP C OD1 1 
ATOM   2825 O  OD2 . ASP C 3 98  ? -36.588 -50.018 31.31   1   50.34 ? 129 ASP C OD2 1 
ATOM   2826 N  N   . GLY C 3 99  ? -41.976 -51.528 31.081  1   34.6  ? 130 GLY C N   1 
ATOM   2827 C  CA  . GLY C 3 99  ? -43.329 -51.558 31.643  1   34.22 ? 130 GLY C CA  1 
ATOM   2828 C  C   . GLY C 3 99  ? -43.467 -50.707 32.899  1   33.57 ? 130 GLY C C   1 
ATOM   2829 O  O   . GLY C 3 99  ? -42.47  -50.374 33.554  1   34.26 ? 130 GLY C O   1 
ATOM   2830 N  N   . LEU C 3 100 ? -44.701 -50.329 33.221  1   31.69 ? 131 LEU C N   1 
ATOM   2831 C  CA  . LEU C 3 100 ? -45.079 -49.603 34.439  1   31.65 ? 131 LEU C CA  1 
ATOM   2832 C  C   . LEU C 3 100 ? -46.178 -50.428 35.082  1   29.04 ? 131 LEU C C   1 
ATOM   2833 O  O   . LEU C 3 100 ? -47.161 -50.714 34.4    1   28.66 ? 131 LEU C O   1 
ATOM   2834 C  CB  . LEU C 3 100 ? -45.683 -48.232 34.097  1   33.66 ? 131 LEU C CB  1 
ATOM   2835 C  CG  . LEU C 3 100 ? -44.703 -47.071 34.066  1   38.27 ? 131 LEU C CG  1 
ATOM   2836 C  CD1 . LEU C 3 100 ? -45.344 -45.856 33.456  1   39.83 ? 131 LEU C CD1 1 
ATOM   2837 C  CD2 . LEU C 3 100 ? -44.194 -46.745 35.469  1   39.79 ? 131 LEU C CD2 1 
ATOM   2838 N  N   . VAL C 3 101 ? -46.069 -50.77  36.387  1   28.17 ? 132 VAL C N   1 
ATOM   2839 C  CA  . VAL C 3 101 ? -47.147 -51.512 37.028  1   27.99 ? 132 VAL C CA  1 
ATOM   2840 C  C   . VAL C 3 101 ? -48.26  -50.547 37.431  1   27.99 ? 132 VAL C C   1 
ATOM   2841 O  O   . VAL C 3 101 ? -47.983 -49.521 38.058  1   28.66 ? 132 VAL C O   1 
ATOM   2842 C  CB  . VAL C 3 101 ? -46.664 -52.312 38.257  1   28.91 ? 132 VAL C CB  1 
ATOM   2843 C  CG1 . VAL C 3 101 ? -47.84  -53.047 38.929  1   28.86 ? 132 VAL C CG1 1 
ATOM   2844 C  CG2 . VAL C 3 101 ? -45.552 -53.285 37.862  1   30.19 ? 132 VAL C CG2 1 
ATOM   2845 N  N   . ILE C 3 102 ? -49.516 -50.891 37.11   1   26.7  ? 133 ILE C N   1 
ATOM   2846 C  CA  . ILE C 3 102 ? -50.692 -50.142 37.54   1   25.8  ? 133 ILE C CA  1 
ATOM   2847 C  C   . ILE C 3 102 ? -51.41  -51.077 38.549  1   26.05 ? 133 ILE C C   1 
ATOM   2848 O  O   . ILE C 3 102 ? -51.634 -52.248 38.24   1   26.68 ? 133 ILE C O   1 
ATOM   2849 C  CB  . ILE C 3 102 ? -51.619 -49.809 36.352  1   26.41 ? 133 ILE C CB  1 
ATOM   2850 C  CG1 . ILE C 3 102 ? -50.851 -48.97  35.273  1   28.27 ? 133 ILE C CG1 1 
ATOM   2851 C  CG2 . ILE C 3 102 ? -52.884 -49.076 36.838  1   26.63 ? 133 ILE C CG2 1 
ATOM   2852 C  CD1 . ILE C 3 102 ? -51.784 -48.499 34.07   1   30.67 ? 133 ILE C CD1 1 
ATOM   2853 N  N   . LYS C 3 103 ? -51.724 -50.579 39.723  1   25.63 ? 134 LYS C N   1 
ATOM   2854 C  CA  . LYS C 3 103 ? -52.375 -51.383 40.757  1   26.89 ? 134 LYS C CA  1 
ATOM   2855 C  C   . LYS C 3 103 ? -53.215 -50.506 41.693  1   27.13 ? 134 LYS C C   1 
ATOM   2856 O  O   . LYS C 3 103 ? -53.311 -49.305 41.477  1   26.67 ? 134 LYS C O   1 
ATOM   2857 C  CB  . LYS C 3 103 ? -51.299 -52.179 41.538  1   29.01 ? 134 LYS C CB  1 
ATOM   2858 C  CG  . LYS C 3 103 ? -50.35  -51.31  42.332  1   33.19 ? 134 LYS C CG  1 
ATOM   2859 C  CD  . LYS C 3 103 ? -49.249 -52.179 42.948  1   39.74 ? 134 LYS C CD  1 
ATOM   2860 C  CE  . LYS C 3 103 ? -48.34  -51.349 43.81   1   44.73 ? 134 LYS C CE  1 
ATOM   2861 N  NZ  . LYS C 3 103 ? -47.417 -52.202 44.594  1   49.14 ? 134 LYS C NZ  1 
ATOM   2862 N  N   . ASP C 3 104 ? -53.83  -51.103 42.725  1   27.81 ? 135 ASP C N   1 
ATOM   2863 C  CA  . ASP C 3 104 ? -54.645 -50.39  43.711  1   29.38 ? 135 ASP C CA  1 
ATOM   2864 C  C   . ASP C 3 104 ? -55.736 -49.521 43.064  1   28.78 ? 135 ASP C C   1 
ATOM   2865 O  O   . ASP C 3 104 ? -55.944 -48.387 43.486  1   29    ? 135 ASP C O   1 
ATOM   2866 C  CB  . ASP C 3 104 ? -53.766 -49.53  44.657  1   32.98 ? 135 ASP C CB  1 
ATOM   2867 C  CG  . ASP C 3 104 ? -52.607 -50.239 45.317  1   41.35 ? 135 ASP C CG  1 
ATOM   2868 O  OD1 . ASP C 3 104 ? -52.755 -51.434 45.649  1   42.69 ? 135 ASP C OD1 1 
ATOM   2869 O  OD2 . ASP C 3 104 ? -51.557 -49.586 45.53   1   44.93 ? 135 ASP C OD2 1 
ATOM   2870 N  N   . LEU C 3 105 ? -56.433 -50.021 42.026  1   28.82 ? 136 LEU C N   1 
ATOM   2871 C  CA  . LEU C 3 105 ? -57.544 -49.276 41.409  1   29.25 ? 136 LEU C CA  1 
ATOM   2872 C  C   . LEU C 3 105 ? -58.607 -48.97  42.479  1   31.08 ? 136 LEU C C   1 
ATOM   2873 O  O   . LEU C 3 105 ? -58.93  -49.854 43.267  1   31.69 ? 136 LEU C O   1 
ATOM   2874 C  CB  . LEU C 3 105 ? -58.173 -50.079 40.262  1   28.74 ? 136 LEU C CB  1 
ATOM   2875 C  CG  . LEU C 3 105 ? -57.599 -49.783 38.896  1   30.85 ? 136 LEU C CG  1 
ATOM   2876 C  CD1 . LEU C 3 105 ? -56.142 -50.19  38.813  1   31.93 ? 136 LEU C CD1 1 
ATOM   2877 C  CD2 . LEU C 3 105 ? -58.396 -50.485 37.805  1   30.68 ? 136 LEU C CD2 1 
ATOM   2878 N  N   . ASN C 3 106 ? -59.008 -47.695 42.595  1   31.87 ? 137 ASN C N   1 
ATOM   2879 C  CA  . ASN C 3 106 ? -59.946 -47.209 43.602  1   33.34 ? 137 ASN C CA  1 
ATOM   2880 C  C   . ASN C 3 106 ? -60.952 -46.342 42.88   1   33.72 ? 137 ASN C C   1 
ATOM   2881 O  O   . ASN C 3 106 ? -60.585 -45.303 42.331  1   33.34 ? 137 ASN C O   1 
ATOM   2882 C  CB  . ASN C 3 106 ? -59.192 -46.349 44.619  1   36.61 ? 137 ASN C CB  1 
ATOM   2883 C  CG  . ASN C 3 106 ? -60.031 -45.772 45.729  1   45.6  ? 137 ASN C CG  1 
ATOM   2884 O  OD1 . ASN C 3 106 ? -61.103 -45.173 45.529  1   48.25 ? 137 ASN C OD1 1 
ATOM   2885 N  ND2 . ASN C 3 106 ? -59.545 -45.934 46.95   1   47.93 ? 137 ASN C ND2 1 
ATOM   2886 N  N   . LEU C 3 107 ? -62.21  -46.763 42.875  1   33.6  ? 138 LEU C N   1 
ATOM   2887 C  CA  . LEU C 3 107 ? -63.258 -46.022 42.215  1   34.85 ? 138 LEU C CA  1 
ATOM   2888 C  C   . LEU C 3 107 ? -64.22  -45.44  43.245  1   36.48 ? 138 LEU C C   1 
ATOM   2889 O  O   . LEU C 3 107 ? -64.735 -46.163 44.103  1   36.26 ? 138 LEU C O   1 
ATOM   2890 C  CB  . LEU C 3 107 ? -64.005 -46.94  41.245  1   34.93 ? 138 LEU C CB  1 
ATOM   2891 C  CG  . LEU C 3 107 ? -65.219 -46.334 40.539  1   36.08 ? 138 LEU C CG  1 
ATOM   2892 C  CD1 . LEU C 3 107 ? -64.783 -45.29  39.492  1   36.41 ? 138 LEU C CD1 1 
ATOM   2893 C  CD2 . LEU C 3 107 ? -66.042 -47.421 39.877  1   36.77 ? 138 LEU C CD2 1 
ATOM   2894 N  N   . MET C 3 108 ? -64.419 -44.121 43.187  1   37.76 ? 139 MET C N   1 
ATOM   2895 C  CA  . MET C 3 108 ? -65.364 -43.42  44.06   1   39.89 ? 139 MET C CA  1 
ATOM   2896 C  C   . MET C 3 108 ? -66.437 -42.889 43.134  1   40.82 ? 139 MET C C   1 
ATOM   2897 O  O   . MET C 3 108 ? -66.11  -42.348 42.075  1   40.45 ? 139 MET C O   1 
ATOM   2898 C  CB  . MET C 3 108 ? -64.696 -42.24  44.806  1   42.02 ? 139 MET C CB  1 
ATOM   2899 C  CG  . MET C 3 108 ? -65.628 -41.543 45.81   1   49.54 ? 139 MET C CG  1 
ATOM   2900 S  SD  . MET C 3 108 ? -66.685 -40.217 45.129  1   65.4  ? 139 MET C SD  1 
ATOM   2901 C  CE  . MET C 3 108 ? -65.431 -38.904 44.866  1   65.53 ? 139 MET C CE  1 
ATOM   2902 N  N   . LEU C 3 109 ? -67.712 -43.061 43.508  1   41.59 ? 140 LEU C N   1 
ATOM   2903 C  CA  . LEU C 3 109 ? -68.863 -42.583 42.731  1   43.23 ? 140 LEU C CA  1 
ATOM   2904 C  C   . LEU C 3 109 ? -69.806 -41.87  43.688  1   45.76 ? 140 LEU C C   1 
ATOM   2905 O  O   . LEU C 3 109 ? -70.077 -42.399 44.773  1   45.19 ? 140 LEU C O   1 
ATOM   2906 C  CB  . LEU C 3 109 ? -69.599 -43.762 42.082  1   42.99 ? 140 LEU C CB  1 
ATOM   2907 C  CG  . LEU C 3 109 ? -68.801 -44.601 41.103  1   43.15 ? 140 LEU C CG  1 
ATOM   2908 C  CD1 . LEU C 3 109 ? -69.572 -45.82  40.696  1   43.16 ? 140 LEU C CD1 1 
ATOM   2909 C  CD2 . LEU C 3 109 ? -68.427 -43.789 39.873  1   44.12 ? 140 LEU C CD2 1 
ATOM   2910 N  N   . LYS C 3 110 ? -70.316 -40.677 43.31   1   47.93 ? 141 LYS C N   1 
ATOM   2911 C  CA  . LYS C 3 110 ? -71.199 -39.94  44.223  1   50.09 ? 141 LYS C CA  1 
ATOM   2912 C  C   . LYS C 3 110 ? -72.214 -39.088 43.479  1   51.69 ? 141 LYS C C   1 
ATOM   2913 O  O   . LYS C 3 110 ? -71.901 -38.528 42.435  1   51.36 ? 141 LYS C O   1 
ATOM   2914 C  CB  . LYS C 3 110 ? -70.351 -39.075 45.184  1   51.98 ? 141 LYS C CB  1 
ATOM   2915 C  CG  . LYS C 3 110 ? -71.06  -38.648 46.456  1   57.11 ? 141 LYS C CG  1 
ATOM   2916 N  N   . ASN C 3 111 ? -73.456 -39.032 43.995  1   53.52 ? 142 ASN C N   1 
ATOM   2917 C  CA  . ASN C 3 111 ? -74.545 -38.21  43.458  1   55.54 ? 142 ASN C CA  1 
ATOM   2918 C  C   . ASN C 3 111 ? -74.904 -38.43  41.982  1   55.39 ? 142 ASN C C   1 
ATOM   2919 O  O   . ASN C 3 111 ? -75.457 -37.531 41.356  1   55.65 ? 142 ASN C O   1 
ATOM   2920 C  CB  . ASN C 3 111 ? -74.25  -36.729 43.688  1   58.96 ? 142 ASN C CB  1 
ATOM   2921 C  CG  . ASN C 3 111 ? -74.292 -36.328 45.136  1   65.19 ? 142 ASN C CG  1 
ATOM   2922 O  OD1 . ASN C 3 111 ? -74.83  -37.043 45.991  1   67.51 ? 142 ASN C OD1 1 
ATOM   2923 N  ND2 . ASN C 3 111 ? -73.742 -35.16  45.44   1   66.67 ? 142 ASN C ND2 1 
ATOM   2924 N  N   . GLY C 3 112 ? -74.569 -39.588 41.425  1   54.88 ? 143 GLY C N   1 
ATOM   2925 C  CA  . GLY C 3 112 ? -74.866 -39.879 40.025  1   54.4  ? 143 GLY C CA  1 
ATOM   2926 C  C   . GLY C 3 112 ? -74.022 -39.144 38.996  1   54.41 ? 143 GLY C C   1 
ATOM   2927 O  O   . GLY C 3 112 ? -74.039 -39.515 37.816  1   54.2  ? 143 GLY C O   1 
ATOM   2928 N  N   . ASN C 3 113 ? -73.282 -38.094 39.41   1   54.2  ? 144 ASN C N   1 
ATOM   2929 C  CA  . ASN C 3 113 ? -72.516 -37.304 38.451  1   54.6  ? 144 ASN C CA  1 
ATOM   2930 C  C   . ASN C 3 113 ? -71.124 -36.88  38.896  1   54.15 ? 144 ASN C C   1 
ATOM   2931 O  O   . ASN C 3 113 ? -70.54  -36.017 38.234  1   54.91 ? 144 ASN C O   1 
ATOM   2932 C  CB  . ASN C 3 113 ? -73.304 -36.078 38.004  1   56.74 ? 144 ASN C CB  1 
ATOM   2933 C  CG  . ASN C 3 113 ? -73.5   -35.035 39.07   1   61.37 ? 144 ASN C CG  1 
ATOM   2934 O  OD1 . ASN C 3 113 ? -73.435 -35.308 40.27   1   62.9  ? 144 ASN C OD1 1 
ATOM   2935 N  ND2 . ASN C 3 113 ? -73.76  -33.806 38.642  1   63.35 ? 144 ASN C ND2 1 
ATOM   2936 N  N   . MET C 3 114 ? -70.58  -37.463 39.972  1   52.69 ? 145 MET C N   1 
ATOM   2937 C  CA  . MET C 3 114 ? -69.204 -37.13  40.344  1   52.14 ? 145 MET C CA  1 
ATOM   2938 C  C   . MET C 3 114 ? -68.411 -38.369 40.802  1   49.36 ? 145 MET C C   1 
ATOM   2939 O  O   . MET C 3 114 ? -68.967 -39.46  40.939  1   50.02 ? 145 MET C O   1 
ATOM   2940 C  CB  . MET C 3 114 ? -69.135 -35.959 41.338  1   54.57 ? 145 MET C CB  1 
ATOM   2941 C  CG  . MET C 3 114 ? -69.436 -36.321 42.746  1   59.69 ? 145 MET C CG  1 
ATOM   2942 S  SD  . MET C 3 114 ? -69.841 -34.825 43.692  1   72.57 ? 145 MET C SD  1 
ATOM   2943 C  CE  . MET C 3 114 ? -71.362 -34.362 42.906  1   74.36 ? 145 MET C CE  1 
ATOM   2944 N  N   . GLY C 3 115 ? -67.112 -38.197 40.978  1   45.94 ? 146 GLY C N   1 
ATOM   2945 C  CA  . GLY C 3 115 ? -66.248 -39.281 41.4    1   43.39 ? 146 GLY C CA  1 
ATOM   2946 C  C   . GLY C 3 115 ? -65.025 -39.403 40.521  1   40.25 ? 146 GLY C C   1 
ATOM   2947 O  O   . GLY C 3 115 ? -64.797 -38.555 39.65   1   39.97 ? 146 GLY C O   1 
ATOM   2948 N  N   . GLU C 3 116 ? -64.234 -40.454 40.735  1   37.9  ? 147 GLU C N   1 
ATOM   2949 C  CA  . GLU C 3 116 ? -63.02  -40.645 39.949  1   36.6  ? 147 GLU C CA  1 
ATOM   2950 C  C   . GLU C 3 116 ? -62.437 -42.044 40.085  1   34.11 ? 147 GLU C C   1 
ATOM   2951 O  O   . GLU C 3 116 ? -62.696 -42.744 41.075  1   33.99 ? 147 GLU C O   1 
ATOM   2952 C  CB  . GLU C 3 116 ? -61.954 -39.588 40.328  1   39.13 ? 147 GLU C CB  1 
ATOM   2953 C  CG  . GLU C 3 116 ? -61.261 -39.832 41.66   1   44.52 ? 147 GLU C CG  1 
ATOM   2954 C  CD  . GLU C 3 116 ? -61.991 -39.257 42.853  1   52.38 ? 147 GLU C CD  1 
ATOM   2955 O  OE1 . GLU C 3 116 ? -62.569 -38.152 42.722  1   53.19 ? 147 GLU C OE1 1 
ATOM   2956 O  OE2 . GLU C 3 116 ? -61.977 -39.906 43.924  1   55.94 ? 147 GLU C OE2 1 
ATOM   2957 N  N   . LEU C 3 117 ? -61.632 -42.444 39.089  1   31.16 ? 148 LEU C N   1 
ATOM   2958 C  CA  . LEU C 3 117 ? -60.907 -43.702 39.154  1   29.78 ? 148 LEU C CA  1 
ATOM   2959 C  C   . LEU C 3 117 ? -59.448 -43.321 39.427  1   30.08 ? 148 LEU C C   1 
ATOM   2960 O  O   . LEU C 3 117 ? -58.877 -42.518 38.676  1   30.41 ? 148 LEU C O   1 
ATOM   2961 C  CB  . LEU C 3 117 ? -61.001 -44.494 37.844  1   28.78 ? 148 LEU C CB  1 
ATOM   2962 C  CG  . LEU C 3 117 ? -60.182 -45.8   37.795  1   28.53 ? 148 LEU C CG  1 
ATOM   2963 C  CD1 . LEU C 3 117 ? -60.661 -46.79  38.904  1   28.32 ? 148 LEU C CD1 1 
ATOM   2964 C  CD2 . LEU C 3 117 ? -60.293 -46.476 36.426  1   28.1  ? 148 LEU C CD2 1 
ATOM   2965 N  N   . LYS C 3 118 ? -58.883 -43.831 40.527  1   29.25 ? 149 LYS C N   1 
ATOM   2966 C  CA  . LYS C 3 118 ? -57.492 -43.597 40.9    1   29.11 ? 149 LYS C CA  1 
ATOM   2967 C  C   . LYS C 3 118 ? -56.734 -44.932 40.88   1   28.17 ? 149 LYS C C   1 
ATOM   2968 O  O   . LYS C 3 118 ? -57.341 -45.998 40.954  1   28.39 ? 149 LYS C O   1 
ATOM   2969 C  CB  . LYS C 3 118 ? -57.392 -43.001 42.324  1   31.96 ? 149 LYS C CB  1 
ATOM   2970 C  CG  . LYS C 3 118 ? -57.926 -41.591 42.482  1   37.05 ? 149 LYS C CG  1 
ATOM   2971 C  CD  . LYS C 3 118 ? -57.683 -41.116 43.904  1   40.58 ? 149 LYS C CD  1 
ATOM   2972 C  CE  . LYS C 3 118 ? -57.876 -39.632 44.092  1   45.24 ? 149 LYS C CE  1 
ATOM   2973 N  NZ  . LYS C 3 118 ? -57.7   -39.232 45.532  1   48.11 ? 149 LYS C NZ  1 
ATOM   2974 N  N   . ALA C 3 119 ? -55.41  -44.869 40.857  1   27.25 ? 150 ALA C N   1 
ATOM   2975 C  CA  . ALA C 3 119 ? -54.552 -46.052 40.857  1   27.38 ? 150 ALA C CA  1 
ATOM   2976 C  C   . ALA C 3 119 ? -53.137 -45.657 41.361  1   28.32 ? 150 ALA C C   1 
ATOM   2977 O  O   . ALA C 3 119 ? -52.808 -44.474 41.453  1   29.3  ? 150 ALA C O   1 
ATOM   2978 C  CB  . ALA C 3 119 ? -54.439 -46.585 39.407  1   26.13 ? 150 ALA C CB  1 
ATOM   2979 N  N   . THR C 3 120 ? -52.311 -46.65  41.676  1   28.04 ? 151 THR C N   1 
ATOM   2980 C  CA  . THR C 3 120 ? -50.893 -46.505 41.888  1   27.9  ? 151 THR C CA  1 
ATOM   2981 C  C   . THR C 3 120 ? -50.283 -46.798 40.49   1   27.8  ? 151 THR C C   1 
ATOM   2982 O  O   . THR C 3 120 ? -50.647 -47.787 39.836  1   27.7  ? 151 THR C O   1 
ATOM   2983 C  CB  . THR C 3 120 ? -50.407 -47.487 42.944  1   30.14 ? 151 THR C CB  1 
ATOM   2984 O  OG1 . THR C 3 120 ? -50.953 -47.102 44.213  1   31.76 ? 151 THR C OG1 1 
ATOM   2985 C  CG2 . THR C 3 120 ? -48.886 -47.536 43.025  1   30.79 ? 151 THR C CG2 1 
ATOM   2986 N  N   . VAL C 3 121 ? -49.451 -45.886 39.981  1   27.46 ? 152 VAL C N   1 
ATOM   2987 C  CA  . VAL C 3 121 ? -48.843 -46.039 38.666  1   28.75 ? 152 VAL C CA  1 
ATOM   2988 C  C   . VAL C 3 121 ? -47.377 -45.977 38.912  1   31.08 ? 152 VAL C C   1 
ATOM   2989 O  O   . VAL C 3 121 ? -46.898 -44.955 39.416  1   32.05 ? 152 VAL C O   1 
ATOM   2990 C  CB  . VAL C 3 121 ? -49.294 -44.919 37.709  1   29.15 ? 152 VAL C CB  1 
ATOM   2991 C  CG1 . VAL C 3 121 ? -48.541 -45.032 36.386  1   28.94 ? 152 VAL C CG1 1 
ATOM   2992 C  CG2 . VAL C 3 121 ? -50.812 -44.976 37.479  1   29.23 ? 152 VAL C CG2 1 
ATOM   2993 N  N   . GLY C 3 122 ? -46.684 -47.097 38.715  1   31.51 ? 153 GLY C N   1 
ATOM   2994 C  CA  . GLY C 3 122 ? -45.268 -47.177 39.051  1   33.04 ? 153 GLY C CA  1 
ATOM   2995 C  C   . GLY C 3 122 ? -45.056 -47.004 40.54   1   35.3  ? 153 GLY C C   1 
ATOM   2996 O  O   . GLY C 3 122 ? -45.778 -47.596 41.359  1   35.01 ? 153 GLY C O   1 
ATOM   2997 N  N   . GLU C 3 123 ? -44.12  -46.133 40.908  1   37.18 ? 154 GLU C N   1 
ATOM   2998 C  CA  . GLU C 3 123 ? -43.845 -45.874 42.32   1   39.01 ? 154 GLU C CA  1 
ATOM   2999 C  C   . GLU C 3 123 ? -44.767 -44.786 42.917  1   39.77 ? 154 GLU C C   1 
ATOM   3000 O  O   . GLU C 3 123 ? -44.575 -44.416 44.069  1   40.03 ? 154 GLU C O   1 
ATOM   3001 C  CB  . GLU C 3 123 ? -42.369 -45.457 42.486  1   43.1  ? 154 GLU C CB  1 
ATOM   3002 N  N   . ASN C 3 124 ? -45.745 -44.261 42.149  1   39.29 ? 155 ASN C N   1 
ATOM   3003 C  CA  . ASN C 3 124 ? -46.594 -43.178 42.631  1   39.49 ? 155 ASN C CA  1 
ATOM   3004 C  C   . ASN C 3 124 ? -48.013 -43.585 42.937  1   38.03 ? 155 ASN C C   1 
ATOM   3005 O  O   . ASN C 3 124 ? -48.705 -44.074 42.071  1   37.75 ? 155 ASN C O   1 
ATOM   3006 C  CB  . ASN C 3 124 ? -46.571 -42.016 41.656  1   42.15 ? 155 ASN C CB  1 
ATOM   3007 C  CG  . ASN C 3 124 ? -45.276 -41.27  41.767  1   48.19 ? 155 ASN C CG  1 
ATOM   3008 O  OD1 . ASN C 3 124 ? -44.388 -41.39  40.921  1   51.24 ? 155 ASN C OD1 1 
ATOM   3009 N  ND2 . ASN C 3 124 ? -45.124 -40.528 42.848  1   49.73 ? 155 ASN C ND2 1 
ATOM   3010 N  N   . SER C 3 125 ? -48.442 -43.387 44.178  1   36.69 ? 156 SER C N   1 
ATOM   3011 C  CA  . SER C 3 125 ? -49.791 -43.743 44.585  1   36.67 ? 156 SER C CA  1 
ATOM   3012 C  C   . SER C 3 125 ? -50.736 -42.534 44.389  1   36.33 ? 156 SER C C   1 
ATOM   3013 O  O   . SER C 3 125 ? -50.263 -41.425 44.114  1   36.11 ? 156 SER C O   1 
ATOM   3014 C  CB  . SER C 3 125 ? -49.771 -44.191 46.049  1   38.49 ? 156 SER C CB  1 
ATOM   3015 O  OG  . SER C 3 125 ? -49.474 -43.08  46.873  1   41.69 ? 156 SER C OG  1 
ATOM   3016 N  N   . ASN C 3 126 ? -52.064 -42.744 44.551  1   36.03 ? 157 ASN C N   1 
ATOM   3017 C  CA  . ASN C 3 126 ? -53.077 -41.686 44.483  1   36.14 ? 157 ASN C CA  1 
ATOM   3018 C  C   . ASN C 3 126 ? -53.059 -40.918 43.156  1   34.63 ? 157 ASN C C   1 
ATOM   3019 O  O   . ASN C 3 126 ? -53.188 -39.688 43.151  1   35.15 ? 157 ASN C O   1 
ATOM   3020 C  CB  . ASN C 3 126 ? -52.911 -40.716 45.675  1   39.41 ? 157 ASN C CB  1 
ATOM   3021 C  CG  . ASN C 3 126 ? -54.122 -39.871 45.933  1   47.36 ? 157 ASN C CG  1 
ATOM   3022 O  OD1 . ASN C 3 126 ? -55.23  -40.384 46.092  1   50.47 ? 157 ASN C OD1 1 
ATOM   3023 N  ND2 . ASN C 3 126 ? -53.939 -38.552 45.999  1   49.58 ? 157 ASN C ND2 1 
ATOM   3024 N  N   . ILE C 3 127 ? -52.852 -41.622 42.034  1   32.29 ? 158 ILE C N   1 
ATOM   3025 C  CA  . ILE C 3 127 ? -52.845 -40.967 40.716  1   31.45 ? 158 ILE C CA  1 
ATOM   3026 C  C   . ILE C 3 127 ? -54.259 -41.06  40.166  1   30.99 ? 158 ILE C C   1 
ATOM   3027 O  O   . ILE C 3 127 ? -54.724 -42.177 39.916  1   30.88 ? 158 ILE C O   1 
ATOM   3028 C  CB  . ILE C 3 127 ? -51.882 -41.687 39.718  1   31.6  ? 158 ILE C CB  1 
ATOM   3029 C  CG1 . ILE C 3 127 ? -50.411 -41.641 40.181  1   33.28 ? 158 ILE C CG1 1 
ATOM   3030 C  CG2 . ILE C 3 127 ? -52.022 -41.136 38.296  1   31.1  ? 158 ILE C CG2 1 
ATOM   3031 C  CD1 . ILE C 3 127 ? -49.874 -40.278 40.462  1   35.3  ? 158 ILE C CD1 1 
ATOM   3032 N  N   . THR C 3 128 ? -54.94  -39.924 39.967  1   29.85 ? 159 THR C N   1 
ATOM   3033 C  CA  . THR C 3 128 ? -56.259 -39.958 39.344  1   28.9  ? 159 THR C CA  1 
ATOM   3034 C  C   . THR C 3 128 ? -56.037 -40.245 37.853  1   27.19 ? 159 THR C C   1 
ATOM   3035 O  O   . THR C 3 128 ? -55.207 -39.599 37.208  1   26.75 ? 159 THR C O   1 
ATOM   3036 C  CB  . THR C 3 128 ? -57.045 -38.647 39.561  1   30.74 ? 159 THR C CB  1 
ATOM   3037 O  OG1 . THR C 3 128 ? -57.222 -38.441 40.957  1   32.36 ? 159 THR C OG1 1 
ATOM   3038 C  CG2 . THR C 3 128 ? -58.415 -38.691 38.918  1   31.3  ? 159 THR C CG2 1 
ATOM   3039 N  N   . LEU C 3 129 ? -56.728 -41.255 37.335  1   25.37 ? 160 LEU C N   1 
ATOM   3040 C  CA  . LEU C 3 129 ? -56.652 -41.607 35.92   1   25.14 ? 160 LEU C CA  1 
ATOM   3041 C  C   . LEU C 3 129 ? -57.694 -40.771 35.167  1   26.05 ? 160 LEU C C   1 
ATOM   3042 O  O   . LEU C 3 129 ? -57.395 -40.209 34.104  1   26.23 ? 160 LEU C O   1 
ATOM   3043 C  CB  . LEU C 3 129 ? -56.925 -43.107 35.736  1   24.64 ? 160 LEU C CB  1 
ATOM   3044 C  CG  . LEU C 3 129 ? -56.001 -44.061 36.484  1   25.55 ? 160 LEU C CG  1 
ATOM   3045 C  CD1 . LEU C 3 129 ? -56.327 -45.493 36.129  1   26.37 ? 160 LEU C CD1 1 
ATOM   3046 C  CD2 . LEU C 3 129 ? -54.507 -43.741 36.212  1   27.07 ? 160 LEU C CD2 1 
ATOM   3047 N  N   . PHE C 3 130 ? -58.919 -40.714 35.698  1   26.38 ? 161 PHE C N   1 
ATOM   3048 C  CA  . PHE C 3 130 ? -59.958 -39.873 35.12   1   28.86 ? 161 PHE C CA  1 
ATOM   3049 C  C   . PHE C 3 130 ? -61.024 -39.495 36.148  1   30.13 ? 161 PHE C C   1 
ATOM   3050 O  O   . PHE C 3 130 ? -61.285 -40.249 37.093  1   30    ? 161 PHE C O   1 
ATOM   3051 C  CB  . PHE C 3 130 ? -60.605 -40.503 33.86   1   29.32 ? 161 PHE C CB  1 
ATOM   3052 C  CG  . PHE C 3 130 ? -61.347 -41.808 34.075  1   30.05 ? 161 PHE C CG  1 
ATOM   3053 C  CD1 . PHE C 3 130 ? -62.649 -41.815 34.559  1   30.8  ? 161 PHE C CD1 1 
ATOM   3054 C  CD2 . PHE C 3 130 ? -60.773 -43.02  33.714  1   29.79 ? 161 PHE C CD2 1 
ATOM   3055 C  CE1 . PHE C 3 130 ? -63.334 -43.012 34.742  1   31.01 ? 161 PHE C CE1 1 
ATOM   3056 C  CE2 . PHE C 3 130 ? -61.467 -44.209 33.883  1   30.07 ? 161 PHE C CE2 1 
ATOM   3057 C  CZ  . PHE C 3 130 ? -62.741 -44.199 34.393  1   30.49 ? 161 PHE C CZ  1 
ATOM   3058 N  N   . ASP C 3 131 ? -61.64  -38.326 35.956  1   31.63 ? 162 ASP C N   1 
ATOM   3059 C  CA  . ASP C 3 131 ? -62.774 -37.895 36.758  1   34.04 ? 162 ASP C CA  1 
ATOM   3060 C  C   . ASP C 3 131 ? -64.02  -38.503 36.099  1   35.07 ? 162 ASP C C   1 
ATOM   3061 O  O   . ASP C 3 131 ? -64.02  -38.784 34.9    1   34.93 ? 162 ASP C O   1 
ATOM   3062 C  CB  . ASP C 3 131 ? -62.889 -36.36  36.766  1   37.11 ? 162 ASP C CB  1 
ATOM   3063 C  CG  . ASP C 3 131 ? -61.813 -35.682 37.592  1   42.3  ? 162 ASP C CG  1 
ATOM   3064 O  OD1 . ASP C 3 131 ? -61.505 -36.185 38.682  1   41.57 ? 162 ASP C OD1 1 
ATOM   3065 O  OD2 . ASP C 3 131 ? -61.286 -34.643 37.142  1   46.1  ? 162 ASP C OD2 1 
ATOM   3066 N  N   . VAL C 3 132 ? -65.093 -38.666 36.866  1   36.06 ? 163 VAL C N   1 
ATOM   3067 C  CA  . VAL C 3 132 ? -66.327 -39.255 36.397  1   37.35 ? 163 VAL C CA  1 
ATOM   3068 C  C   . VAL C 3 132 ? -67.3   -38.161 35.985  1   39.11 ? 163 VAL C C   1 
ATOM   3069 O  O   . VAL C 3 132 ? -67.481 -37.19  36.712  1   39.45 ? 163 VAL C O   1 
ATOM   3070 C  CB  . VAL C 3 132 ? -66.91  -40.214 37.469  1   38.44 ? 163 VAL C CB  1 
ATOM   3071 C  CG1 . VAL C 3 132 ? -68.347 -40.607 37.158  1   39.12 ? 163 VAL C CG1 1 
ATOM   3072 C  CG2 . VAL C 3 132 ? -66.024 -41.454 37.641  1   38.93 ? 163 VAL C CG2 1 
ATOM   3073 N  N   . GLN C 3 133 ? -67.856 -38.275 34.78   1   40.09 ? 164 GLN C N   1 
ATOM   3074 C  CA  . GLN C 3 133 ? -68.839 -37.319 34.297  1   42.41 ? 164 GLN C CA  1 
ATOM   3075 C  C   . GLN C 3 133 ? -70.198 -37.741 34.866  1   43.91 ? 164 GLN C C   1 
ATOM   3076 O  O   . GLN C 3 133 ? -70.929 -36.905 35.398  1   45.08 ? 164 GLN C O   1 
ATOM   3077 C  CB  . GLN C 3 133 ? -68.889 -37.323 32.759  1   44.57 ? 164 GLN C CB  1 
ATOM   3078 C  CG  . GLN C 3 133 ? -70.076 -36.54  32.182  1   51.34 ? 164 GLN C CG  1 
ATOM   3079 C  CD  . GLN C 3 133 ? -69.874 -35.042 32.24   1   59.16 ? 164 GLN C CD  1 
ATOM   3080 O  OE1 . GLN C 3 133 ? -68.774 -34.531 32.013  1   61.88 ? 164 GLN C OE1 1 
ATOM   3081 N  NE2 . GLN C 3 133 ? -70.939 -34.299 32.521  1   60.62 ? 164 GLN C NE2 1 
ATOM   3082 N  N   . GLU C 3 134 ? -70.514 -39.045 34.775  1   43.99 ? 165 GLU C N   1 
ATOM   3083 C  CA  . GLU C 3 134 ? -71.754 -39.616 35.278  1   44.84 ? 165 GLU C CA  1 
ATOM   3084 C  C   . GLU C 3 134 ? -71.658 -41.144 35.352  1   44.27 ? 165 GLU C C   1 
ATOM   3085 O  O   . GLU C 3 134 ? -70.761 -41.753 34.784  1   43.1  ? 165 GLU C O   1 
ATOM   3086 C  CB  . GLU C 3 134 ? -72.929 -39.21  34.371  1   47.71 ? 165 GLU C CB  1 
ATOM   3087 C  CG  . GLU C 3 134 ? -72.864 -39.82  32.986  1   54.96 ? 165 GLU C CG  1 
ATOM   3088 C  CD  . GLU C 3 134 ? -74.084 -39.503 32.149  1   65.94 ? 165 GLU C CD  1 
ATOM   3089 O  OE1 . GLU C 3 134 ? -75.214 -39.695 32.659  1   69.31 ? 165 GLU C OE1 1 
ATOM   3090 O  OE2 . GLU C 3 134 ? -73.914 -39.057 30.989  1   68.47 ? 165 GLU C OE2 1 
ATOM   3091 N  N   . TYR C 3 135 ? -72.615 -41.757 36.039  1   44.91 ? 166 TYR C N   1 
ATOM   3092 C  CA  . TYR C 3 135 ? -72.725 -43.2   36.154  1   46.5  ? 166 TYR C CA  1 
ATOM   3093 C  C   . TYR C 3 135 ? -74.181 -43.569 36.402  1   48.03 ? 166 TYR C C   1 
ATOM   3094 O  O   . TYR C 3 135 ? -74.926 -42.784 36.979  1   48.14 ? 166 TYR C O   1 
ATOM   3095 C  CB  . TYR C 3 135 ? -71.81  -43.78  37.272  1   46.45 ? 166 TYR C CB  1 
ATOM   3096 C  CG  . TYR C 3 135 ? -72.191 -43.358 38.675  1   47.02 ? 166 TYR C CG  1 
ATOM   3097 C  CD1 . TYR C 3 135 ? -71.672 -42.204 39.239  1   47.62 ? 166 TYR C CD1 1 
ATOM   3098 C  CD2 . TYR C 3 135 ? -73.087 -44.108 39.431  1   47.71 ? 166 TYR C CD2 1 
ATOM   3099 C  CE1 . TYR C 3 135 ? -72.046 -41.794 40.513  1   48.62 ? 166 TYR C CE1 1 
ATOM   3100 C  CE2 . TYR C 3 135 ? -73.476 -43.702 40.7    1   48.74 ? 166 TYR C CE2 1 
ATOM   3101 C  CZ  . TYR C 3 135 ? -72.947 -42.549 41.242  1   49.91 ? 166 TYR C CZ  1 
ATOM   3102 O  OH  . TYR C 3 135 ? -73.327 -42.157 42.505  1   52.52 ? 166 TYR C OH  1 
ATOM   3103 N  N   . SER C 3 136 ? -74.595 -44.743 35.935  1   49.08 ? 167 SER C N   1 
ATOM   3104 C  CA  . SER C 3 136 ? -75.944 -45.239 36.185  1   50.46 ? 167 SER C CA  1 
ATOM   3105 C  C   . SER C 3 136 ? -75.87  -46.704 36.601  1   51.6  ? 167 SER C C   1 
ATOM   3106 O  O   . SER C 3 136 ? -74.909 -47.409 36.278  1   51.13 ? 167 SER C O   1 
ATOM   3107 C  CB  . SER C 3 136 ? -76.847 -45.055 34.97   1   52.12 ? 167 SER C CB  1 
ATOM   3108 O  OG  . SER C 3 136 ? -76.425 -45.834 33.862  1   54.75 ? 167 SER C OG  1 
ATOM   3109 N  N   . VAL C 3 137 ? -76.867 -47.146 37.36   1   52.82 ? 168 VAL C N   1 
ATOM   3110 C  CA  . VAL C 3 137 ? -76.941 -48.503 37.866  1   54.67 ? 168 VAL C CA  1 
ATOM   3111 C  C   . VAL C 3 137 ? -78.221 -49.137 37.331  1   56.54 ? 168 VAL C C   1 
ATOM   3112 O  O   . VAL C 3 137 ? -79.305 -48.58  37.504  1   56.31 ? 168 VAL C O   1 
ATOM   3113 C  CB  . VAL C 3 137 ? -76.956 -48.501 39.417  1   55.34 ? 168 VAL C CB  1 
ATOM   3114 C  CG1 . VAL C 3 137 ? -77.242 -49.892 39.978  1   55.78 ? 168 VAL C CG1 1 
ATOM   3115 C  CG2 . VAL C 3 137 ? -75.669 -47.926 39.988  1   55.81 ? 168 VAL C CG2 1 
ATOM   3116 N  N   . SER C 3 138 ? -78.097 -50.29  36.673  1   57.56 ? 169 SER C N   1 
ATOM   3117 C  CA  . SER C 3 138 ? -79.26  -51.012 36.175  1   58.56 ? 169 SER C CA  1 
ATOM   3118 C  C   . SER C 3 138 ? -79.032 -52.451 36.565  1   58.86 ? 169 SER C C   1 
ATOM   3119 O  O   . SER C 3 138 ? -78.019 -53.034 36.175  1   58.62 ? 169 SER C O   1 
ATOM   3120 C  CB  . SER C 3 138 ? -79.372 -50.888 34.656  1   60.58 ? 169 SER C CB  1 
ATOM   3121 O  OG  . SER C 3 138 ? -80.519 -51.588 34.194  1   63.44 ? 169 SER C OG  1 
ATOM   3122 N  N   . ASP C 3 139 ? -79.928 -52.993 37.385  1   59.31 ? 170 ASP C N   1 
ATOM   3123 C  CA  . ASP C 3 139 ? -79.859 -54.354 37.903  1   60.28 ? 170 ASP C CA  1 
ATOM   3124 C  C   . ASP C 3 139 ? -78.63  -54.411 38.851  1   59.62 ? 170 ASP C C   1 
ATOM   3125 O  O   . ASP C 3 139 ? -78.577 -53.615 39.801  1   61.08 ? 170 ASP C O   1 
ATOM   3126 C  CB  . ASP C 3 139 ? -79.869 -55.395 36.74   1   63.95 ? 170 ASP C CB  1 
ATOM   3127 C  CG  . ASP C 3 139 ? -80.319 -56.793 37.131  1   72.08 ? 170 ASP C CG  1 
ATOM   3128 O  OD1 . ASP C 3 139 ? -80.65  -57     38.313  1   73.9  ? 170 ASP C OD1 1 
ATOM   3129 O  OD2 . ASP C 3 139 ? -80.342 -57.678 36.248  1   75.67 ? 170 ASP C OD2 1 
ATOM   3130 N  N   . ASN C 3 140 ? -77.657 -55.293 38.61   1   56.79 ? 171 ASN C N   1 
ATOM   3131 C  CA  . ASN C 3 140 ? -76.472 -55.339 39.452  1   54.69 ? 171 ASN C CA  1 
ATOM   3132 C  C   . ASN C 3 140 ? -75.259 -54.731 38.707  1   51.07 ? 171 ASN C C   1 
ATOM   3133 O  O   . ASN C 3 140 ? -74.133 -55.035 39.066  1   50.89 ? 171 ASN C O   1 
ATOM   3134 C  CB  . ASN C 3 140 ? -76.207 -56.78  39.922  1   57.09 ? 171 ASN C CB  1 
ATOM   3135 C  CG  . ASN C 3 140 ? -75.741 -57.776 38.86   1   62.5  ? 171 ASN C CG  1 
ATOM   3136 O  OD1 . ASN C 3 140 ? -75.823 -57.547 37.636  1   64.64 ? 171 ASN C OD1 1 
ATOM   3137 N  ND2 . ASN C 3 140 ? -75.23  -58.921 39.325  1   63.49 ? 171 ASN C ND2 1 
ATOM   3138 N  N   . THR C 3 141 ? -75.486 -53.869 37.68   1   48.48 ? 172 THR C N   1 
ATOM   3139 C  CA  . THR C 3 141 ? -74.394 -53.341 36.872  1   46.66 ? 172 THR C CA  1 
ATOM   3140 C  C   . THR C 3 141 ? -74.288 -51.809 36.858  1   44.55 ? 172 THR C C   1 
ATOM   3141 O  O   . THR C 3 141 ? -75.275 -51.118 36.619  1   44.46 ? 172 THR C O   1 
ATOM   3142 C  CB  . THR C 3 141 ? -74.528 -53.907 35.451  1   48.18 ? 172 THR C CB  1 
ATOM   3143 O  OG1 . THR C 3 141 ? -74.519 -55.335 35.519  1   49.47 ? 172 THR C OG1 1 
ATOM   3144 C  CG2 . THR C 3 141 ? -73.435 -53.43  34.52   1   48.13 ? 172 THR C CG2 1 
ATOM   3145 N  N   . ILE C 3 142 ? -73.081 -51.284 37.096  1   42.32 ? 173 ILE C N   1 
ATOM   3146 C  CA  . ILE C 3 142 ? -72.826 -49.85  37.062  1   41.57 ? 173 ILE C CA  1 
ATOM   3147 C  C   . ILE C 3 142 ? -72.102 -49.532 35.766  1   40.34 ? 173 ILE C C   1 
ATOM   3148 O  O   . ILE C 3 142 ? -71.1   -50.17  35.461  1   40.04 ? 173 ILE C O   1 
ATOM   3149 C  CB  . ILE C 3 142 ? -71.95  -49.387 38.257  1   42.65 ? 173 ILE C CB  1 
ATOM   3150 C  CG1 . ILE C 3 142 ? -72.449 -49.957 39.607  1   44.19 ? 173 ILE C CG1 1 
ATOM   3151 C  CG2 . ILE C 3 142 ? -71.825 -47.864 38.292  1   42.95 ? 173 ILE C CG2 1 
ATOM   3152 C  CD1 . ILE C 3 142 ? -71.501 -49.654 40.77   1   46.05 ? 173 ILE C CD1 1 
ATOM   3153 N  N   . THR C 3 143 ? -72.567 -48.522 35.029  1   39.46 ? 174 THR C N   1 
ATOM   3154 C  CA  . THR C 3 143 ? -71.906 -48.062 33.825  1   39    ? 174 THR C CA  1 
ATOM   3155 C  C   . THR C 3 143 ? -71.289 -46.723 34.19   1   37.88 ? 174 THR C C   1 
ATOM   3156 O  O   . THR C 3 143 ? -72.008 -45.826 34.618  1   38.35 ? 174 THR C O   1 
ATOM   3157 C  CB  . THR C 3 143 ? -72.898 -47.887 32.683  1   41.16 ? 174 THR C CB  1 
ATOM   3158 O  OG1 . THR C 3 143 ? -73.495 -49.148 32.377  1   42.93 ? 174 THR C OG1 1 
ATOM   3159 C  CG2 . THR C 3 143 ? -72.239 -47.3   31.45   1   41.27 ? 174 THR C CG2 1 
ATOM   3160 N  N   . VAL C 3 144 ? -69.979 -46.584 34.054  1   36.02 ? 175 VAL C N   1 
ATOM   3161 C  CA  . VAL C 3 144 ? -69.277 -45.37  34.458  1   35.82 ? 175 VAL C CA  1 
ATOM   3162 C  C   . VAL C 3 144 ? -68.698 -44.642 33.27   1   35.8  ? 175 VAL C C   1 
ATOM   3163 O  O   . VAL C 3 144 ? -67.856 -45.2   32.56   1   35.37 ? 175 VAL C O   1 
ATOM   3164 C  CB  . VAL C 3 144 ? -68.145 -45.711 35.457  1   36.38 ? 175 VAL C CB  1 
ATOM   3165 C  CG1 . VAL C 3 144 ? -67.376 -44.458 35.856  1   37.36 ? 175 VAL C CG1 1 
ATOM   3166 C  CG2 . VAL C 3 144 ? -68.7   -46.433 36.69   1   35.95 ? 175 VAL C CG2 1 
ATOM   3167 N  N   . THR C 3 145 ? -69.117 -43.387 33.079  1   35.76 ? 176 THR C N   1 
ATOM   3168 C  CA  . THR C 3 145 ? -68.659 -42.563 31.976  1   36.31 ? 176 THR C CA  1 
ATOM   3169 C  C   . THR C 3 145 ? -67.601 -41.557 32.417  1   34.9  ? 176 THR C C   1 
ATOM   3170 O  O   . THR C 3 145 ? -67.863 -40.719 33.285  1   34.75 ? 176 THR C O   1 
ATOM   3171 C  CB  . THR C 3 145 ? -69.857 -41.837 31.351  1   39.55 ? 176 THR C CB  1 
ATOM   3172 O  OG1 . THR C 3 145 ? -70.816 -42.798 30.91   1   41.97 ? 176 THR C OG1 1 
ATOM   3173 C  CG2 . THR C 3 145 ? -69.447 -40.941 30.189  1   38.91 ? 176 THR C CG2 1 
ATOM   3174 N  N   . PRO C 3 146 ? -66.41  -41.604 31.79   1   33.99 ? 177 PRO C N   1 
ATOM   3175 C  CA  . PRO C 3 146 ? -65.359 -40.635 32.132  1   33.85 ? 177 PRO C CA  1 
ATOM   3176 C  C   . PRO C 3 146 ? -65.707 -39.216 31.652  1   34.56 ? 177 PRO C C   1 
ATOM   3177 O  O   . PRO C 3 146 ? -66.41  -39.041 30.655  1   33.82 ? 177 PRO C O   1 
ATOM   3178 C  CB  . PRO C 3 146 ? -64.119 -41.161 31.366  1   34.13 ? 177 PRO C CB  1 
ATOM   3179 C  CG  . PRO C 3 146 ? -64.448 -42.565 30.98   1   34.87 ? 177 PRO C CG  1 
ATOM   3180 C  CD  . PRO C 3 146 ? -65.95  -42.567 30.778  1   33.33 ? 177 PRO C CD  1 
ATOM   3181 N  N   . LYS C 3 147 ? -65.205 -38.203 32.366  1   35.38 ? 178 LYS C N   1 
ATOM   3182 C  CA  . LYS C 3 147 ? -65.399 -36.801 32.01   1   36.32 ? 178 LYS C CA  1 
ATOM   3183 C  C   . LYS C 3 147 ? -64.303 -36.454 31.002  1   36.3  ? 178 LYS C C   1 
ATOM   3184 O  O   . LYS C 3 147 ? -63.121 -36.483 31.35   1   37.12 ? 178 LYS C O   1 
ATOM   3185 C  CB  . LYS C 3 147 ? -65.279 -35.919 33.263  1   39.05 ? 178 LYS C CB  1 
ATOM   3186 C  CG  . LYS C 3 147 ? -65.499 -34.444 32.999  1   45.46 ? 178 LYS C CG  1 
ATOM   3187 C  CD  . LYS C 3 147 ? -65.407 -33.623 34.294  1   51.9  ? 178 LYS C CD  1 
ATOM   3188 C  CE  . LYS C 3 147 ? -66.511 -33.95  35.267  1   57.69 ? 178 LYS C CE  1 
ATOM   3189 N  NZ  . LYS C 3 147 ? -66.46  -33.1   36.495  1   61.05 ? 178 LYS C NZ  1 
ATOM   3190 N  N   . ILE C 3 148 ? -64.675 -36.216 29.729  1   34.57 ? 179 ILE C N   1 
ATOM   3191 C  CA  . ILE C 3 148 ? -63.687 -35.955 28.686  1   34.29 ? 179 ILE C CA  1 
ATOM   3192 C  C   . ILE C 3 148 ? -63.985 -34.624 28.021  1   34.99 ? 179 ILE C C   1 
ATOM   3193 O  O   . ILE C 3 148 ? -65.105 -34.391 27.572  1   34.88 ? 179 ILE C O   1 
ATOM   3194 C  CB  . ILE C 3 148 ? -63.645 -37.132 27.674  1   34.5  ? 179 ILE C CB  1 
ATOM   3195 C  CG1 . ILE C 3 148 ? -63.414 -38.479 28.407  1   35.87 ? 179 ILE C CG1 1 
ATOM   3196 C  CG2 . ILE C 3 148 ? -62.578 -36.907 26.566  1   34.3  ? 179 ILE C CG2 1 
ATOM   3197 C  CD1 . ILE C 3 148 ? -63.688 -39.745 27.566  1   37.05 ? 179 ILE C CD1 1 
ATOM   3198 N  N   . PRO C 3 149 ? -63.005 -33.712 27.991  1   35.24 ? 180 PRO C N   1 
ATOM   3199 C  CA  . PRO C 3 149 ? -63.257 -32.4   27.381  1   35.55 ? 180 PRO C CA  1 
ATOM   3200 C  C   . PRO C 3 149 ? -63.454 -32.542 25.87   1   36.44 ? 180 PRO C C   1 
ATOM   3201 O  O   . PRO C 3 149 ? -62.903 -33.461 25.254  1   36.09 ? 180 PRO C O   1 
ATOM   3202 C  CB  . PRO C 3 149 ? -61.964 -31.621 27.684  1   36.35 ? 180 PRO C CB  1 
ATOM   3203 C  CG  . PRO C 3 149 ? -60.912 -32.682 27.833  1   37.08 ? 180 PRO C CG  1 
ATOM   3204 C  CD  . PRO C 3 149 ? -61.619 -33.835 28.489  1   34.89 ? 180 PRO C CD  1 
ATOM   3205 N  N   . PRO C 3 150 ? -64.209 -31.635 25.247  1   36.84 ? 181 PRO C N   1 
ATOM   3206 C  CA  . PRO C 3 150 ? -64.33  -31.703 23.781  1   37.31 ? 181 PRO C CA  1 
ATOM   3207 C  C   . PRO C 3 150 ? -62.968 -31.42  23.137  1   37.33 ? 181 PRO C C   1 
ATOM   3208 O  O   . PRO C 3 150 ? -62.187 -30.636 23.674  1   36.24 ? 181 PRO C O   1 
ATOM   3209 C  CB  . PRO C 3 150 ? -65.369 -30.623 23.445  1   38.31 ? 181 PRO C CB  1 
ATOM   3210 C  CG  . PRO C 3 150 ? -65.352 -29.684 24.605  1   39.25 ? 181 PRO C CG  1 
ATOM   3211 C  CD  . PRO C 3 150 ? -64.919 -30.472 25.817  1   37.38 ? 181 PRO C CD  1 
ATOM   3212 N  N   . CYS C 3 151 ? -62.66  -32.09  22.021  1   38.14 ? 182 CYS C N   1 
ATOM   3213 C  CA  . CYS C 3 151 ? -61.408 -31.824 21.309  1   39.6  ? 182 CYS C CA  1 
ATOM   3214 C  C   . CYS C 3 151 ? -61.736 -30.648 20.417  1   42.24 ? 182 CYS C C   1 
ATOM   3215 O  O   . CYS C 3 151 ? -62.576 -30.792 19.531  1   43.11 ? 182 CYS C O   1 
ATOM   3216 C  CB  . CYS C 3 151 ? -60.959 -33.038 20.497  1   38.7  ? 182 CYS C CB  1 
ATOM   3217 S  SG  . CYS C 3 151 ? -59.257 -32.924 19.876  1   38.62 ? 182 CYS C SG  1 
ATOM   3218 N  N   . THR C 3 152 ? -61.148 -29.466 20.684  1   43.56 ? 183 THR C N   1 
ATOM   3219 C  CA  . THR C 3 152 ? -61.443 -28.236 19.946  1   45.23 ? 183 THR C CA  1 
ATOM   3220 C  C   . THR C 3 152 ? -60.219 -27.734 19.13   1   45.68 ? 183 THR C C   1 
ATOM   3221 O  O   . THR C 3 152 ? -60.26  -27.796 17.904  1   46.3  ? 183 THR C O   1 
ATOM   3222 C  CB  . THR C 3 152 ? -61.993 -27.175 20.916  1   48.1  ? 183 THR C CB  1 
ATOM   3223 O  OG1 . THR C 3 152 ? -60.98  -26.978 21.908  1   49.99 ? 183 THR C OG1 1 
ATOM   3224 C  CG2 . THR C 3 152 ? -63.315 -27.599 21.591  1   49.01 ? 183 THR C CG2 1 
ATOM   3225 N  N   . THR C 3 153 ? -59.14  -27.249 19.811  1   45.09 ? 184 THR C N   1 
ATOM   3226 C  CA  . THR C 3 153 ? -57.859 -26.761 19.267  1   44.53 ? 184 THR C CA  1 
ATOM   3227 C  C   . THR C 3 153 ? -56.791 -26.805 20.39   1   43    ? 184 THR C C   1 
ATOM   3228 O  O   . THR C 3 153 ? -57.136 -26.969 21.564  1   43.8  ? 184 THR C O   1 
ATOM   3229 C  CB  . THR C 3 153 ? -58.015 -25.364 18.632  1   46.72 ? 184 THR C CB  1 
ATOM   3230 O  OG1 . THR C 3 153 ? -56.871 -25.069 17.807  1   47.78 ? 184 THR C OG1 1 
ATOM   3231 C  CG2 . THR C 3 153 ? -58.24  -24.27  19.665  1   47.46 ? 184 THR C CG2 1 
ATOM   3232 N  N   . GLY C 3 154 ? -55.516 -26.695 20.031  1   40.67 ? 185 GLY C N   1 
ATOM   3233 C  CA  . GLY C 3 154 ? -54.443 -26.739 21.018  1   39.15 ? 185 GLY C CA  1 
ATOM   3234 C  C   . GLY C 3 154 ? -54.221 -28.131 21.584  1   36.62 ? 185 GLY C C   1 
ATOM   3235 O  O   . GLY C 3 154 ? -54.486 -29.127 20.903  1   36.12 ? 185 GLY C O   1 
ATOM   3236 N  N   . THR C 3 155 ? -53.735 -28.223 22.835  1   34.8  ? 186 THR C N   1 
ATOM   3237 C  CA  . THR C 3 155 ? -53.486 -29.529 23.439  1   34.06 ? 186 THR C CA  1 
ATOM   3238 C  C   . THR C 3 155 ? -54.775 -30.128 23.971  1   32.6  ? 186 THR C C   1 
ATOM   3239 O  O   . THR C 3 155 ? -55.492 -29.48  24.742  1   33.75 ? 186 THR C O   1 
ATOM   3240 C  CB  . THR C 3 155 ? -52.378 -29.463 24.503  1   36.27 ? 186 THR C CB  1 
ATOM   3241 O  OG1 . THR C 3 155 ? -51.218 -28.868 23.913  1   37.45 ? 186 THR C OG1 1 
ATOM   3242 C  CG2 . THR C 3 155 ? -52     -30.848 25.012  1   37.58 ? 186 THR C CG2 1 
ATOM   3243 N  N   . TRP C 3 156 ? -55.078 -31.361 23.56   1   29.72 ? 187 TRP C N   1 
ATOM   3244 C  CA  . TRP C 3 156 ? -56.279 -32.042 24.006  1   28.28 ? 187 TRP C CA  1 
ATOM   3245 C  C   . TRP C 3 156 ? -55.84  -33.09  25.015  1   26.53 ? 187 TRP C C   1 
ATOM   3246 O  O   . TRP C 3 156 ? -54.937 -33.881 24.737  1   25.52 ? 187 TRP C O   1 
ATOM   3247 C  CB  . TRP C 3 156 ? -56.989 -32.689 22.823  1   28.68 ? 187 TRP C CB  1 
ATOM   3248 C  CG  . TRP C 3 156 ? -58.274 -33.361 23.207  1   29.53 ? 187 TRP C CG  1 
ATOM   3249 C  CD1 . TRP C 3 156 ? -59.368 -32.784 23.788  1   30.36 ? 187 TRP C CD1 1 
ATOM   3250 C  CD2 . TRP C 3 156 ? -58.599 -34.739 23.011  1   29.47 ? 187 TRP C CD2 1 
ATOM   3251 N  NE1 . TRP C 3 156 ? -60.355 -33.729 23.977  1   30.64 ? 187 TRP C NE1 1 
ATOM   3252 C  CE2 . TRP C 3 156 ? -59.907 -34.938 23.504  1   30.71 ? 187 TRP C CE2 1 
ATOM   3253 C  CE3 . TRP C 3 156 ? -57.898 -35.833 22.508  1   29.62 ? 187 TRP C CE3 1 
ATOM   3254 C  CZ2 . TRP C 3 156 ? -60.541 -36.18  23.45   1   31.13 ? 187 TRP C CZ2 1 
ATOM   3255 C  CZ3 . TRP C 3 156 ? -58.508 -37.067 22.511  1   30.43 ? 187 TRP C CZ3 1 
ATOM   3256 C  CH2 . TRP C 3 156 ? -59.832 -37.22  22.923  1   30.62 ? 187 TRP C CH2 1 
ATOM   3257 N  N   . LYS C 3 157 ? -56.391 -33.018 26.218  1   25.1  ? 188 LYS C N   1 
ATOM   3258 C  CA  . LYS C 3 157 ? -55.995 -33.913 27.293  1   26.21 ? 188 LYS C CA  1 
ATOM   3259 C  C   . LYS C 3 157 ? -57.197 -34.667 27.872  1   26    ? 188 LYS C C   1 
ATOM   3260 O  O   . LYS C 3 157 ? -57.818 -34.195 28.833  1   26.54 ? 188 LYS C O   1 
ATOM   3261 C  CB  . LYS C 3 157 ? -55.277 -33.101 28.383  1   29.74 ? 188 LYS C CB  1 
ATOM   3262 C  CG  . LYS C 3 157 ? -53.982 -32.467 27.857  1   35.05 ? 188 LYS C CG  1 
ATOM   3263 C  CD  . LYS C 3 157 ? -53.659 -31.175 28.587  1   41.85 ? 188 LYS C CD  1 
ATOM   3264 C  CE  . LYS C 3 157 ? -52.281 -31.206 29.21   1   47.94 ? 188 LYS C CE  1 
ATOM   3265 N  NZ  . LYS C 3 157 ? -51.588 -29.888 29.074  1   50.75 ? 188 LYS C NZ  1 
ATOM   3266 N  N   . PRO C 3 158 ? -57.491 -35.867 27.318  1   25.11 ? 189 PRO C N   1 
ATOM   3267 C  CA  . PRO C 3 158 ? -58.668 -36.632 27.774  1   24.71 ? 189 PRO C CA  1 
ATOM   3268 C  C   . PRO C 3 158 ? -58.496 -37.443 29.054  1   24.48 ? 189 PRO C C   1 
ATOM   3269 O  O   . PRO C 3 158 ? -59.48  -37.999 29.521  1   24.52 ? 189 PRO C O   1 
ATOM   3270 C  CB  . PRO C 3 158 ? -58.933 -37.571 26.609  1   25.39 ? 189 PRO C CB  1 
ATOM   3271 C  CG  . PRO C 3 158 ? -57.513 -37.853 26.059  1   25.91 ? 189 PRO C CG  1 
ATOM   3272 C  CD  . PRO C 3 158 ? -56.868 -36.488 26.124  1   24.68 ? 189 PRO C CD  1 
ATOM   3273 N  N   . TRP C 3 159 ? -57.268 -37.518 29.623  1   24.08 ? 190 TRP C N   1 
ATOM   3274 C  CA  . TRP C 3 159 ? -57.006 -38.197 30.905  1   24.74 ? 190 TRP C CA  1 
ATOM   3275 C  C   . TRP C 3 159 ? -56.657 -37.14  31.986  1   26.04 ? 190 TRP C C   1 
ATOM   3276 O  O   . TRP C 3 159 ? -56.352 -35.981 31.643  1   26.34 ? 190 TRP C O   1 
ATOM   3277 C  CB  . TRP C 3 159 ? -55.828 -39.181 30.762  1   23.66 ? 190 TRP C CB  1 
ATOM   3278 C  CG  . TRP C 3 159 ? -56.118 -40.341 29.859  1   22.17 ? 190 TRP C CG  1 
ATOM   3279 C  CD1 . TRP C 3 159 ? -56.057 -40.357 28.496  1   21.92 ? 190 TRP C CD1 1 
ATOM   3280 C  CD2 . TRP C 3 159 ? -56.437 -41.681 30.267  1   21.16 ? 190 TRP C CD2 1 
ATOM   3281 N  NE1 . TRP C 3 159 ? -56.34  -41.621 28.025  1   21.7  ? 190 TRP C NE1 1 
ATOM   3282 C  CE2 . TRP C 3 159 ? -56.553 -42.458 29.095  1   21.66 ? 190 TRP C CE2 1 
ATOM   3283 C  CE3 . TRP C 3 159 ? -56.629 -42.3   31.509  1   22.28 ? 190 TRP C CE3 1 
ATOM   3284 C  CZ2 . TRP C 3 159 ? -56.854 -43.815 29.128  1   22.54 ? 190 TRP C CZ2 1 
ATOM   3285 C  CZ3 . TRP C 3 159 ? -56.929 -43.653 31.542  1   22.93 ? 190 TRP C CZ3 1 
ATOM   3286 C  CH2 . TRP C 3 159 ? -57.035 -44.393 30.358  1   22.35 ? 190 TRP C CH2 1 
ATOM   3287 N  N   . HIS C 3 160 ? -56.724 -37.515 33.276  1   25.91 ? 191 HIS C N   1 
ATOM   3288 C  CA  . HIS C 3 160 ? -56.385 -36.563 34.342  1   26.66 ? 191 HIS C CA  1 
ATOM   3289 C  C   . HIS C 3 160 ? -54.882 -36.186 34.273  1   27.68 ? 191 HIS C C   1 
ATOM   3290 O  O   . HIS C 3 160 ? -54.034 -37.015 33.923  1   27.94 ? 191 HIS C O   1 
ATOM   3291 C  CB  . HIS C 3 160 ? -56.727 -37.142 35.727  1   26.72 ? 191 HIS C CB  1 
ATOM   3292 C  CG  . HIS C 3 160 ? -56.817 -36.127 36.828  1   28.95 ? 191 HIS C CG  1 
ATOM   3293 N  ND1 . HIS C 3 160 ? -55.688 -35.696 37.506  1   30.74 ? 191 HIS C ND1 1 
ATOM   3294 C  CD2 . HIS C 3 160 ? -57.909 -35.557 37.4    1   29.9  ? 191 HIS C CD2 1 
ATOM   3295 C  CE1 . HIS C 3 160 ? -56.118 -34.841 38.42   1   31    ? 191 HIS C CE1 1 
ATOM   3296 N  NE2 . HIS C 3 160 ? -57.447 -34.721 38.389  1   31.23 ? 191 HIS C NE2 1 
ATOM   3297 N  N   . ASN C 3 161 ? -54.574 -34.949 34.606  1   28.16 ? 192 ASN C N   1 
ATOM   3298 C  CA  . ASN C 3 161 ? -53.226 -34.396 34.644  1   30.21 ? 192 ASN C CA  1 
ATOM   3299 C  C   . ASN C 3 161 ? -52.287 -35.199 35.553  1   31.27 ? 192 ASN C C   1 
ATOM   3300 O  O   . ASN C 3 161 ? -51.094 -35.225 35.291  1   32.19 ? 192 ASN C O   1 
ATOM   3301 C  CB  . ASN C 3 161 ? -53.284 -32.944 35.119  1   34    ? 192 ASN C CB  1 
ATOM   3302 C  CG  . ASN C 3 161 ? -51.951 -32.245 35      1   42.07 ? 192 ASN C CG  1 
ATOM   3303 O  OD1 . ASN C 3 161 ? -51.51  -31.879 33.902  1   44.56 ? 192 ASN C OD1 1 
ATOM   3304 N  ND2 . ASN C 3 161 ? -51.252 -32.101 36.124  1   43.93 ? 192 ASN C ND2 1 
ATOM   3305 N  N   . ASP C 3 162 ? -52.805 -35.841 36.639  1   30.51 ? 193 ASP C N   1 
ATOM   3306 C  CA  . ASP C 3 162 ? -51.984 -36.664 37.543  1   30.01 ? 193 ASP C CA  1 
ATOM   3307 C  C   . ASP C 3 162 ? -51.263 -37.757 36.746  1   30.19 ? 193 ASP C C   1 
ATOM   3308 O  O   . ASP C 3 162 ? -50.082 -38.027 36.983  1   31.37 ? 193 ASP C O   1 
ATOM   3309 C  CB  . ASP C 3 162 ? -52.859 -37.373 38.595  1   29.92 ? 193 ASP C CB  1 
ATOM   3310 C  CG  . ASP C 3 162 ? -53.354 -36.528 39.734  1   32.07 ? 193 ASP C CG  1 
ATOM   3311 O  OD1 . ASP C 3 162 ? -53.086 -35.299 39.728  1   30.86 ? 193 ASP C OD1 1 
ATOM   3312 O  OD2 . ASP C 3 162 ? -54.027 -37.085 40.629  1   33.62 ? 193 ASP C OD2 1 
ATOM   3313 N  N   . LEU C 3 163 ? -51.993 -38.397 35.833  1   28.75 ? 194 LEU C N   1 
ATOM   3314 C  CA  . LEU C 3 163 ? -51.443 -39.472 35.012  1   28.07 ? 194 LEU C CA  1 
ATOM   3315 C  C   . LEU C 3 163 ? -50.341 -38.991 34.066  1   27.99 ? 194 LEU C C   1 
ATOM   3316 O  O   . LEU C 3 163 ? -49.243 -39.551 34.086  1   27.61 ? 194 LEU C O   1 
ATOM   3317 C  CB  . LEU C 3 163 ? -52.568 -40.192 34.221  1   27.29 ? 194 LEU C CB  1 
ATOM   3318 C  CG  . LEU C 3 163 ? -52.094 -41.334 33.299  1   27.82 ? 194 LEU C CG  1 
ATOM   3319 C  CD1 . LEU C 3 163 ? -51.243 -42.39  34.087  1   27.3  ? 194 LEU C CD1 1 
ATOM   3320 C  CD2 . LEU C 3 163 ? -53.27  -42.004 32.634  1   28.2  ? 194 LEU C CD2 1 
ATOM   3321 N  N   . THR C 3 164 ? -50.626 -37.965 33.238  1   28.3  ? 195 THR C N   1 
ATOM   3322 C  CA  . THR C 3 164 ? -49.663 -37.459 32.261  1   28.63 ? 195 THR C CA  1 
ATOM   3323 C  C   . THR C 3 164 ? -48.465 -36.758 32.914  1   30.14 ? 195 THR C C   1 
ATOM   3324 O  O   . THR C 3 164 ? -47.344 -36.828 32.386  1   30.14 ? 195 THR C O   1 
ATOM   3325 C  CB  . THR C 3 164 ? -50.371 -36.596 31.222  1   29.14 ? 195 THR C CB  1 
ATOM   3326 O  OG1 . THR C 3 164 ? -51.118 -35.559 31.888  1   29.47 ? 195 THR C OG1 1 
ATOM   3327 C  CG2 . THR C 3 164 ? -51.283 -37.441 30.309  1   28.52 ? 195 THR C CG2 1 
ATOM   3328 N  N   . SER C 3 165 ? -48.682 -36.101 34.062  1   30.83 ? 196 SER C N   1 
ATOM   3329 C  CA  . SER C 3 165 ? -47.558 -35.468 34.752  1   32.41 ? 196 SER C CA  1 
ATOM   3330 C  C   . SER C 3 165 ? -46.635 -36.568 35.321  1   32.97 ? 196 SER C C   1 
ATOM   3331 O  O   . SER C 3 165 ? -45.431 -36.392 35.305  1   34.07 ? 196 SER C O   1 
ATOM   3332 C  CB  . SER C 3 165 ? -48.027 -34.476 35.811  1   35.91 ? 196 SER C CB  1 
ATOM   3333 O  OG  . SER C 3 165 ? -48.826 -35.13  36.777  1   41.22 ? 196 SER C OG  1 
ATOM   3334 N  N   . LYS C 3 166 ? -47.178 -37.726 35.732  1   32.66 ? 197 LYS C N   1 
ATOM   3335 C  CA  . LYS C 3 166 ? -46.362 -38.84  36.224  1   33.51 ? 197 LYS C CA  1 
ATOM   3336 C  C   . LYS C 3 166 ? -45.589 -39.458 35.038  1   32.96 ? 197 LYS C C   1 
ATOM   3337 O  O   . LYS C 3 166 ? -44.391 -39.746 35.152  1   33.16 ? 197 LYS C O   1 
ATOM   3338 C  CB  . LYS C 3 166 ? -47.271 -39.904 36.895  1   35.96 ? 197 LYS C CB  1 
ATOM   3339 C  CG  . LYS C 3 166 ? -46.707 -41.342 36.952  1   40.95 ? 197 LYS C CG  1 
ATOM   3340 C  CD  . LYS C 3 166 ? -45.575 -41.47  37.936  1   47.61 ? 197 LYS C CD  1 
ATOM   3341 C  CE  . LYS C 3 166 ? -44.938 -42.845 37.929  1   52.52 ? 197 LYS C CE  1 
ATOM   3342 N  NZ  . LYS C 3 166 ? -44.319 -43.175 36.621  1   55.37 ? 197 LYS C NZ  1 
ATOM   3343 N  N   . LEU C 3 167 ? -46.288 -39.676 33.919  1   31.32 ? 198 LEU C N   1 
ATOM   3344 C  CA  . LEU C 3 167 ? -45.69  -40.293 32.737  1   31.29 ? 198 LEU C CA  1 
ATOM   3345 C  C   . LEU C 3 167 ? -44.617 -39.468 32.049  1   32.02 ? 198 LEU C C   1 
ATOM   3346 O  O   . LEU C 3 167 ? -43.699 -40.04  31.463  1   33.44 ? 198 LEU C O   1 
ATOM   3347 C  CB  . LEU C 3 167 ? -46.765 -40.643 31.721  1   30.22 ? 198 LEU C CB  1 
ATOM   3348 C  CG  . LEU C 3 167 ? -47.8   -41.638 32.146  1   30.2  ? 198 LEU C CG  1 
ATOM   3349 C  CD1 . LEU C 3 167 ? -48.827 -41.838 31.038  1   29.64 ? 198 LEU C CD1 1 
ATOM   3350 C  CD2 . LEU C 3 167 ? -47.168 -42.976 32.479  1   30.77 ? 198 LEU C CD2 1 
ATOM   3351 N  N   . GLY C 3 168 ? -44.762 -38.152 32.057  1   31.11 ? 199 GLY C N   1 
ATOM   3352 C  CA  . GLY C 3 168 ? -43.828 -37.28  31.351  1   31.4  ? 199 GLY C CA  1 
ATOM   3353 C  C   . GLY C 3 168 ? -44.272 -36.991 29.923  1   31.95 ? 199 GLY C C   1 
ATOM   3354 O  O   . GLY C 3 168 ? -45.176 -37.639 29.391  1   30.74 ? 199 GLY C O   1 
ATOM   3355 N  N   . SER C 3 169 ? -43.652 -36     29.301  1   32.57 ? 200 SER C N   1 
ATOM   3356 C  CA  . SER C 3 169 ? -43.981 -35.512 27.963  1   33.77 ? 200 SER C CA  1 
ATOM   3357 C  C   . SER C 3 169 ? -44.112 -36.551 26.827  1   32.91 ? 200 SER C C   1 
ATOM   3358 O  O   . SER C 3 169 ? -45.081 -36.511 26.061  1   32.76 ? 200 SER C O   1 
ATOM   3359 C  CB  . SER C 3 169 ? -42.942 -34.469 27.538  1   37.08 ? 200 SER C CB  1 
ATOM   3360 O  OG  . SER C 3 169 ? -43.577 -33.291 27.078  1   42.36 ? 200 SER C OG  1 
ATOM   3361 N  N   . LEU C 3 170 ? -43.124 -37.434 26.695  1   31.8  ? 201 LEU C N   1 
ATOM   3362 C  CA  . LEU C 3 170 ? -43.048 -38.325 25.553  1   31.6  ? 201 LEU C CA  1 
ATOM   3363 C  C   . LEU C 3 170 ? -43.882 -39.588 25.766  1   30.6  ? 201 LEU C C   1 
ATOM   3364 O  O   . LEU C 3 170 ? -44.6   -39.973 24.834  1   30.45 ? 201 LEU C O   1 
ATOM   3365 C  CB  . LEU C 3 170 ? -41.576 -38.579 25.185  1   32.54 ? 201 LEU C CB  1 
ATOM   3366 C  CG  . LEU C 3 170 ? -40.72  -37.274 25.043  1   34.27 ? 201 LEU C CG  1 
ATOM   3367 C  CD1 . LEU C 3 170 ? -39.257 -37.568 24.692  1   34.89 ? 201 LEU C CD1 1 
ATOM   3368 C  CD2 . LEU C 3 170 ? -41.316 -36.303 24.008  1   35.05 ? 201 LEU C CD2 1 
ATOM   3369 N  N   . LYS C 3 171 ? -43.934 -40.141 27.005  1   28.95 ? 202 LYS C N   1 
ATOM   3370 C  CA  . LYS C 3 171 ? -44.877 -41.244 27.245  1   28.21 ? 202 LYS C CA  1 
ATOM   3371 C  C   . LYS C 3 171 ? -46.316 -40.705 27.214  1   25.72 ? 202 LYS C C   1 
ATOM   3372 O  O   . LYS C 3 171 ? -47.213 -41.458 26.881  1   25.76 ? 202 LYS C O   1 
ATOM   3373 C  CB  . LYS C 3 171 ? -44.578 -42.016 28.54   1   31.72 ? 202 LYS C CB  1 
ATOM   3374 C  CG  . LYS C 3 171 ? -43.255 -42.759 28.423  1   37.95 ? 202 LYS C CG  1 
ATOM   3375 C  CD  . LYS C 3 171 ? -43.034 -43.636 29.627  1   46.03 ? 202 LYS C CD  1 
ATOM   3376 C  CE  . LYS C 3 171 ? -42.165 -44.823 29.291  1   52.09 ? 202 LYS C CE  1 
ATOM   3377 N  NZ  . LYS C 3 171 ? -42.366 -45.911 30.292  1   56.58 ? 202 LYS C NZ  1 
ATOM   3378 N  N   . SER C 3 172 ? -46.539 -39.394 27.485  1   24.4  ? 203 SER C N   1 
ATOM   3379 C  CA  . SER C 3 172 ? -47.9   -38.822 27.394  1   24.35 ? 203 SER C CA  1 
ATOM   3380 C  C   . SER C 3 172 ? -48.374 -38.662 25.953  1   23.96 ? 203 SER C C   1 
ATOM   3381 O  O   . SER C 3 172 ? -49.566 -38.419 25.734  1   24.71 ? 203 SER C O   1 
ATOM   3382 C  CB  . SER C 3 172 ? -48.03  -37.516 28.167  1   25.35 ? 203 SER C CB  1 
ATOM   3383 O  OG  . SER C 3 172 ? -47.776 -37.778 29.541  1   26.45 ? 203 SER C OG  1 
ATOM   3384 N  N   . VAL C 3 173 ? -47.509 -38.925 24.94   1   22.41 ? 204 VAL C N   1 
ATOM   3385 C  CA  . VAL C 3 173 ? -47.974 -38.95  23.547  1   21.43 ? 204 VAL C CA  1 
ATOM   3386 C  C   . VAL C 3 173 ? -49.082 -40.044 23.393  1   21.07 ? 204 VAL C C   1 
ATOM   3387 O  O   . VAL C 3 173 ? -50.012 -39.86  22.621  1   20.97 ? 204 VAL C O   1 
ATOM   3388 C  CB  . VAL C 3 173 ? -46.789 -39.185 22.584  1   22.6  ? 204 VAL C CB  1 
ATOM   3389 C  CG1 . VAL C 3 173 ? -47.263 -39.476 21.154  1   22.86 ? 204 VAL C CG1 1 
ATOM   3390 C  CG2 . VAL C 3 173 ? -45.851 -37.981 22.598  1   23.61 ? 204 VAL C CG2 1 
ATOM   3391 N  N   . PHE C 3 174 ? -49.051 -41.12  24.231  1   20.25 ? 205 PHE C N   1 
ATOM   3392 C  CA  . PHE C 3 174 ? -50.093 -42.148 24.183  1   20.11 ? 205 PHE C CA  1 
ATOM   3393 C  C   . PHE C 3 174 ? -51.443 -41.7   24.819  1   20.5  ? 205 PHE C C   1 
ATOM   3394 O  O   . PHE C 3 174 ? -52.449 -42.411 24.698  1   20.82 ? 205 PHE C O   1 
ATOM   3395 C  CB  . PHE C 3 174 ? -49.591 -43.42  24.913  1   20.17 ? 205 PHE C CB  1 
ATOM   3396 C  CG  . PHE C 3 174 ? -48.546 -44.181 24.135  1   20.51 ? 205 PHE C CG  1 
ATOM   3397 C  CD1 . PHE C 3 174 ? -47.204 -43.853 24.241  1   21.56 ? 205 PHE C CD1 1 
ATOM   3398 C  CD2 . PHE C 3 174 ? -48.909 -45.187 23.264  1   20.89 ? 205 PHE C CD2 1 
ATOM   3399 C  CE1 . PHE C 3 174 ? -46.253 -44.516 23.466  1   22.61 ? 205 PHE C CE1 1 
ATOM   3400 C  CE2 . PHE C 3 174 ? -47.964 -45.863 22.518  1   21.44 ? 205 PHE C CE2 1 
ATOM   3401 C  CZ  . PHE C 3 174 ? -46.642 -45.521 22.613  1   21.75 ? 205 PHE C CZ  1 
ATOM   3402 N  N   . PHE C 3 175 ? -51.457 -40.549 25.545  1   20.76 ? 206 PHE C N   1 
ATOM   3403 C  CA  . PHE C 3 175 ? -52.586 -40.071 26.347  1   21.19 ? 206 PHE C CA  1 
ATOM   3404 C  C   . PHE C 3 175 ? -53.069 -38.64  26.014  1   23.07 ? 206 PHE C C   1 
ATOM   3405 O  O   . PHE C 3 175 ? -54.005 -38.135 26.65   1   23.46 ? 206 PHE C O   1 
ATOM   3406 C  CB  . PHE C 3 175 ? -52.187 -40.136 27.848  1   20.89 ? 206 PHE C CB  1 
ATOM   3407 C  CG  . PHE C 3 175 ? -51.997 -41.567 28.296  1   21.53 ? 206 PHE C CG  1 
ATOM   3408 C  CD1 . PHE C 3 175 ? -50.763 -42.2   28.167  1   21.93 ? 206 PHE C CD1 1 
ATOM   3409 C  CD2 . PHE C 3 175 ? -53.06  -42.295 28.816  1   21.81 ? 206 PHE C CD2 1 
ATOM   3410 C  CE1 . PHE C 3 175 ? -50.606 -43.543 28.538  1   21.62 ? 206 PHE C CE1 1 
ATOM   3411 C  CE2 . PHE C 3 175 ? -52.905 -43.637 29.156  1   21.6  ? 206 PHE C CE2 1 
ATOM   3412 C  CZ  . PHE C 3 175 ? -51.675 -44.245 29.032  1   20.9  ? 206 PHE C CZ  1 
ATOM   3413 N  N   . GLU C 3 176 ? -52.437 -37.995 25.029  1   22.96 ? 207 GLU C N   1 
ATOM   3414 C  CA  . GLU C 3 176 ? -52.834 -36.653 24.64   1   24.01 ? 207 GLU C CA  1 
ATOM   3415 C  C   . GLU C 3 176 ? -52.436 -36.373 23.215  1   24.8  ? 207 GLU C C   1 
ATOM   3416 O  O   . GLU C 3 176 ? -51.631 -37.115 22.64   1   24.79 ? 207 GLU C O   1 
ATOM   3417 C  CB  . GLU C 3 176 ? -52.267 -35.61  25.602  1   27.45 ? 207 GLU C CB  1 
ATOM   3418 C  CG  . GLU C 3 176 ? -50.775 -35.413 25.534  1   33.41 ? 207 GLU C CG  1 
ATOM   3419 C  CD  . GLU C 3 176 ? -50.225 -34.619 26.711  1   38.37 ? 207 GLU C CD  1 
ATOM   3420 O  OE1 . GLU C 3 176 ? -50.914 -34.506 27.749  1   40.17 ? 207 GLU C OE1 1 
ATOM   3421 O  OE2 . GLU C 3 176 ? -49.089 -34.112 26.593  1   38.62 ? 207 GLU C OE2 1 
ATOM   3422 N  N   . SER C 3 177 ? -52.964 -35.277 22.651  1   25.22 ? 208 SER C N   1 
ATOM   3423 C  CA  . SER C 3 177 ? -52.63  -34.917 21.281  1   26.55 ? 208 SER C CA  1 
ATOM   3424 C  C   . SER C 3 177 ? -52.788 -33.422 21.039  1   27.58 ? 208 SER C C   1 
ATOM   3425 O  O   . SER C 3 177 ? -53.48  -32.736 21.79   1   28.95 ? 208 SER C O   1 
ATOM   3426 C  CB  . SER C 3 177 ? -53.566 -35.662 20.338  1   28.68 ? 208 SER C CB  1 
ATOM   3427 O  OG  . SER C 3 177 ? -54.884 -35.177 20.532  1   32.65 ? 208 SER C OG  1 
ATOM   3428 N  N   A TYR C 3 178 ? -52.155 -32.906 19.999  0.5 27.31 ? 209 TYR C N   1 
ATOM   3429 N  N   B TYR C 3 178 ? -52.134 -32.93  19.989  0.5 27.35 ? 209 TYR C N   1 
ATOM   3430 C  CA  A TYR C 3 178 ? -52.354 -31.517 19.593  0.5 27.95 ? 209 TYR C CA  1 
ATOM   3431 C  CA  B TYR C 3 178 ? -52.209 -31.554 19.505  0.5 28.02 ? 209 TYR C CA  1 
ATOM   3432 C  C   A TYR C 3 178 ? -53.576 -31.446 18.626  0.5 29.46 ? 209 TYR C C   1 
ATOM   3433 C  C   B TYR C 3 178 ? -53.129 -31.467 18.245  0.5 29.35 ? 209 TYR C C   1 
ATOM   3434 O  O   A TYR C 3 178 ? -54.237 -30.408 18.541  0.5 29.64 ? 209 TYR C O   1 
ATOM   3435 O  O   B TYR C 3 178 ? -53.136 -30.435 17.574  0.5 29.19 ? 209 TYR C O   1 
ATOM   3436 C  CB  A TYR C 3 178 ? -51.098 -30.973 18.88   0.5 27.73 ? 209 TYR C CB  1 
ATOM   3437 C  CB  B TYR C 3 178 ? -50.795 -31.033 19.204  0.5 27.83 ? 209 TYR C CB  1 
ATOM   3438 C  CG  A TYR C 3 178 ? -49.863 -30.857 19.751  0.5 27.81 ? 209 TYR C CG  1 
ATOM   3439 C  CG  B TYR C 3 178 ? -50.608 -29.529 19.263  0.5 28.07 ? 209 TYR C CG  1 
ATOM   3440 C  CD1 A TYR C 3 178 ? -49.919 -30.24  20.99   0.5 28.53 ? 209 TYR C CD1 1 
ATOM   3441 C  CD1 B TYR C 3 178 ? -50.965 -28.807 20.395  0.5 29.21 ? 209 TYR C CD1 1 
ATOM   3442 C  CD2 A TYR C 3 178 ? -48.61  -31.226 19.268  0.5 28.18 ? 209 TYR C CD2 1 
ATOM   3443 C  CD2 B TYR C 3 178 ? -49.933 -28.856 18.256  0.5 28.63 ? 209 TYR C CD2 1 
ATOM   3444 C  CE1 A TYR C 3 178 ? -48.781 -30.086 21.774  0.5 29.54 ? 209 TYR C CE1 1 
ATOM   3445 C  CE1 B TYR C 3 178 ? -50.741 -27.436 20.478  0.5 29.86 ? 209 TYR C CE1 1 
ATOM   3446 C  CE2 A TYR C 3 178 ? -47.463 -31.066 20.033  0.5 28.83 ? 209 TYR C CE2 1 
ATOM   3447 C  CE2 B TYR C 3 178 ? -49.664 -27.495 18.347  0.5 29.14 ? 209 TYR C CE2 1 
ATOM   3448 C  CZ  A TYR C 3 178 ? -47.552 -30.505 21.293  0.5 30.38 ? 209 TYR C CZ  1 
ATOM   3449 C  CZ  B TYR C 3 178 ? -50.091 -26.783 19.451  0.5 30.22 ? 209 TYR C CZ  1 
ATOM   3450 O  OH  A TYR C 3 178 ? -46.427 -30.366 22.072  0.5 31.66 ? 209 TYR C OH  1 
ATOM   3451 O  OH  B TYR C 3 178 ? -49.84  -25.436 19.532  0.5 31.97 ? 209 TYR C OH  1 
ATOM   3452 N  N   . THR C 3 179 ? -53.885 -32.553 17.917  1   30.04 ? 210 THR C N   1 
ATOM   3453 C  CA  . THR C 3 179 ? -54.923 -32.611 16.873  1   32.42 ? 210 THR C CA  1 
ATOM   3454 C  C   . THR C 3 179 ? -56.101 -33.495 17.303  1   32.55 ? 210 THR C C   1 
ATOM   3455 O  O   . THR C 3 179 ? -56.011 -34.244 18.287  1   32.77 ? 210 THR C O   1 
ATOM   3456 C  CB  . THR C 3 179 ? -54.369 -33.02  15.488  1   36.4  ? 210 THR C CB  1 
ATOM   3457 O  OG1 . THR C 3 179 ? -53.547 -34.164 15.621  1   39.42 ? 210 THR C OG1 1 
ATOM   3458 C  CG2 . THR C 3 179 ? -53.638 -31.917 14.791  1   38.54 ? 210 THR C CG2 1 
ATOM   3459 N  N   . CYS C 3 180 ? -57.226 -33.37  16.568  1   32.05 ? 211 CYS C N   1 
ATOM   3460 C  CA  . CYS C 3 180 ? -58.454 -34.081 16.851  1   32.6  ? 211 CYS C CA  1 
ATOM   3461 C  C   . CYS C 3 180 ? -58.742 -35.217 15.893  1   31.61 ? 211 CYS C C   1 
ATOM   3462 O  O   . CYS C 3 180 ? -59.905 -35.564 15.72   1   32.72 ? 211 CYS C O   1 
ATOM   3463 C  CB  . CYS C 3 180 ? -59.602 -33.086 16.891  1   34.91 ? 211 CYS C CB  1 
ATOM   3464 S  SG  . CYS C 3 180 ? -59.394 -31.821 18.168  1   40.42 ? 211 CYS C SG  1 
ATOM   3465 N  N   . ASN C 3 181 ? -57.718 -35.813 15.303  1   28.91 ? 212 ASN C N   1 
ATOM   3466 C  CA  . ASN C 3 181 ? -57.901 -36.899 14.349  1   28.78 ? 212 ASN C CA  1 
ATOM   3467 C  C   . ASN C 3 181 ? -58.406 -38.148 15.015  1   28.07 ? 212 ASN C C   1 
ATOM   3468 O  O   . ASN C 3 181 ? -58.231 -38.308 16.239  1   27.62 ? 212 ASN C O   1 
ATOM   3469 C  CB  . ASN C 3 181 ? -56.607 -37.174 13.588  1   31.25 ? 212 ASN C CB  1 
ATOM   3470 C  CG  . ASN C 3 181 ? -56.066 -35.956 12.888  1   37.82 ? 212 ASN C CG  1 
ATOM   3471 O  OD1 . ASN C 3 181 ? -56.767 -35.28  12.131  1   40.18 ? 212 ASN C OD1 1 
ATOM   3472 N  ND2 . ASN C 3 181 ? -54.808 -35.651 13.133  1   39.14 ? 212 ASN C ND2 1 
ATOM   3473 N  N   . ASN C 3 182 ? -59.036 -39.057 14.23   1   26.96 ? 213 ASN C N   1 
ATOM   3474 C  CA  . ASN C 3 182 ? -59.631 -40.289 14.795  1   27.06 ? 213 ASN C CA  1 
ATOM   3475 C  C   . ASN C 3 182 ? -58.71  -41.065 15.727  1   25.79 ? 213 ASN C C   1 
ATOM   3476 O  O   . ASN C 3 182 ? -59.125 -41.461 16.817  1   24.89 ? 213 ASN C O   1 
ATOM   3477 C  CB  . ASN C 3 182 ? -60.153 -41.217 13.681  1   28.27 ? 213 ASN C CB  1 
ATOM   3478 C  CG  . ASN C 3 182 ? -60.726 -42.515 14.235  1   29.91 ? 213 ASN C CG  1 
ATOM   3479 O  OD1 . ASN C 3 182 ? -61.894 -42.578 14.65   1   30.86 ? 213 ASN C OD1 1 
ATOM   3480 N  ND2 . ASN C 3 182 ? -59.898 -43.557 14.327  1   28.16 ? 213 ASN C ND2 1 
ATOM   3481 N  N   . ASP C 3 183 ? -57.477 -41.318 15.278  1   25.22 ? 214 ASP C N   1 
ATOM   3482 C  CA  . ASP C 3 183 ? -56.538 -42.078 16.096  1   24.74 ? 214 ASP C CA  1 
ATOM   3483 C  C   . ASP C 3 183 ? -56.139 -41.371 17.388  1   22.92 ? 214 ASP C C   1 
ATOM   3484 O  O   . ASP C 3 183 ? -55.682 -42.029 18.318  1   22.44 ? 214 ASP C O   1 
ATOM   3485 C  CB  . ASP C 3 183 ? -55.315 -42.483 15.27   1   28.14 ? 214 ASP C CB  1 
ATOM   3486 C  CG  . ASP C 3 183 ? -55.6   -43.62  14.301  1   35.64 ? 214 ASP C CG  1 
ATOM   3487 O  OD1 . ASP C 3 183 ? -56.793 -43.996 14.143  1   37.17 ? 214 ASP C OD1 1 
ATOM   3488 O  OD2 . ASP C 3 183 ? -54.654 -44.099 13.671  1   39.21 ? 214 ASP C OD2 1 
ATOM   3489 N  N   . ASP C 3 184 ? -56.283 -40.032 17.437  1   21.94 ? 215 ASP C N   1 
ATOM   3490 C  CA  . ASP C 3 184 ? -56.018 -39.245 18.638  1   21.88 ? 215 ASP C CA  1 
ATOM   3491 C  C   . ASP C 3 184 ? -57.218 -39.296 19.541  1   22.59 ? 215 ASP C C   1 
ATOM   3492 O  O   . ASP C 3 184 ? -57.058 -39.476 20.751  1   22.71 ? 215 ASP C O   1 
ATOM   3493 C  CB  . ASP C 3 184 ? -55.698 -37.801 18.277  1   24.44 ? 215 ASP C CB  1 
ATOM   3494 C  CG  . ASP C 3 184 ? -54.359 -37.775 17.576  1   31.55 ? 215 ASP C CG  1 
ATOM   3495 O  OD1 . ASP C 3 184 ? -53.408 -38.361 18.114  1   32.98 ? 215 ASP C OD1 1 
ATOM   3496 O  OD2 . ASP C 3 184 ? -54.276 -37.195 16.489  1   36.2  ? 215 ASP C OD2 1 
ATOM   3497 N  N   . ILE C 3 185 ? -58.432 -39.168 18.988  1   22.49 ? 216 ILE C N   1 
ATOM   3498 C  CA  . ILE C 3 185 ? -59.659 -39.294 19.81   1   23.94 ? 216 ILE C CA  1 
ATOM   3499 C  C   . ILE C 3 185 ? -59.688 -40.679 20.488  1   23.3  ? 216 ILE C C   1 
ATOM   3500 O  O   . ILE C 3 185 ? -60.041 -40.799 21.676  1   23.25 ? 216 ILE C O   1 
ATOM   3501 C  CB  . ILE C 3 185 ? -60.931 -39.059 18.949  1   25.47 ? 216 ILE C CB  1 
ATOM   3502 C  CG1 . ILE C 3 185 ? -60.925 -37.675 18.263  1   27.88 ? 216 ILE C CG1 1 
ATOM   3503 C  CG2 . ILE C 3 185 ? -62.22  -39.243 19.792  1   26.59 ? 216 ILE C CG2 1 
ATOM   3504 C  CD1 . ILE C 3 185 ? -60.714 -36.52  19.221  1   29.53 ? 216 ILE C CD1 1 
ATOM   3505 N  N   . ALA C 3 186 ? -59.213 -41.711 19.76   1   22.67 ? 217 ALA C N   1 
ATOM   3506 C  CA  . ALA C 3 186 ? -59.158 -43.077 20.276  1   21.99 ? 217 ALA C CA  1 
ATOM   3507 C  C   . ALA C 3 186 ? -58.313 -43.207 21.558  1   21.88 ? 217 ALA C C   1 
ATOM   3508 O  O   . ALA C 3 186 ? -58.45  -44.218 22.25   1   22    ? 217 ALA C O   1 
ATOM   3509 C  CB  . ALA C 3 186 ? -58.628 -44.023 19.216  1   21.42 ? 217 ALA C CB  1 
ATOM   3510 N  N   . LYS C 3 187 ? -57.407 -42.241 21.851  1   20.85 ? 218 LYS C N   1 
ATOM   3511 C  CA  . LYS C 3 187 ? -56.574 -42.309 23.07   1   20.77 ? 218 LYS C CA  1 
ATOM   3512 C  C   . LYS C 3 187 ? -57.378 -42.109 24.354  1   23.13 ? 218 LYS C C   1 
ATOM   3513 O  O   . LYS C 3 187 ? -56.879 -42.426 25.433  1   24.1  ? 218 LYS C O   1 
ATOM   3514 C  CB  . LYS C 3 187 ? -55.425 -41.277 23.041  1   18.33 ? 218 LYS C CB  1 
ATOM   3515 C  CG  . LYS C 3 187 ? -54.509 -41.392 21.8    1   21.14 ? 218 LYS C CG  1 
ATOM   3516 C  CD  . LYS C 3 187 ? -53.476 -40.25  21.791  1   23.82 ? 218 LYS C CD  1 
ATOM   3517 C  CE  . LYS C 3 187 ? -52.478 -40.439 20.68   1   23.19 ? 218 LYS C CE  1 
ATOM   3518 N  NZ  . LYS C 3 187 ? -51.608 -39.254 20.493  1   22.25 ? 218 LYS C NZ  1 
ATOM   3519 N  N   . LYS C 3 188 ? -58.6   -41.548 24.262  1   23.36 ? 219 LYS C N   1 
ATOM   3520 C  CA  . LYS C 3 188 ? -59.38  -41.244 25.475  1   23.44 ? 219 LYS C CA  1 
ATOM   3521 C  C   . LYS C 3 188 ? -59.789 -42.488 26.278  1   23.88 ? 219 LYS C C   1 
ATOM   3522 O  O   . LYS C 3 188 ? -59.921 -43.573 25.717  1   23.82 ? 219 LYS C O   1 
ATOM   3523 C  CB  . LYS C 3 188 ? -60.607 -40.37  25.123  1   25.03 ? 219 LYS C CB  1 
ATOM   3524 C  CG  . LYS C 3 188 ? -61.716 -41.059 24.343  1   27.28 ? 219 LYS C CG  1 
ATOM   3525 C  CD  . LYS C 3 188 ? -62.62  -39.989 23.708  1   30.91 ? 219 LYS C CD  1 
ATOM   3526 C  CE  . LYS C 3 188 ? -63.733 -40.547 22.859  1   35.83 ? 219 LYS C CE  1 
ATOM   3527 N  NZ  . LYS C 3 188 ? -64.776 -41.16  23.707  1   39.29 ? 219 LYS C NZ  1 
ATOM   3528 N  N   . PRO C 3 189 ? -59.962 -42.349 27.609  1   24.02 ? 220 PRO C N   1 
ATOM   3529 C  CA  . PRO C 3 189 ? -60.353 -43.518 28.412  1   24.16 ? 220 PRO C CA  1 
ATOM   3530 C  C   . PRO C 3 189 ? -61.703 -44.06  27.981  1   25.63 ? 220 PRO C C   1 
ATOM   3531 O  O   . PRO C 3 189 ? -62.632 -43.286 27.674  1   25.27 ? 220 PRO C O   1 
ATOM   3532 C  CB  . PRO C 3 189 ? -60.413 -42.97  29.857  1   24.85 ? 220 PRO C CB  1 
ATOM   3533 C  CG  . PRO C 3 189 ? -60.622 -41.466 29.699  1   25.27 ? 220 PRO C CG  1 
ATOM   3534 C  CD  . PRO C 3 189 ? -59.821 -41.13  28.436  1   23.36 ? 220 PRO C CD  1 
ATOM   3535 N  N   . LEU C 3 190 ? -61.807 -45.385 27.908  1   25.42 ? 221 LEU C N   1 
ATOM   3536 C  CA  . LEU C 3 190 ? -63.094 -46.02  27.61   1   26.16 ? 221 LEU C CA  1 
ATOM   3537 C  C   . LEU C 3 190 ? -63.952 -46.057 28.915  1   27.94 ? 221 LEU C C   1 
ATOM   3538 O  O   . LEU C 3 190 ? -63.407 -45.977 30.024  1   28.03 ? 221 LEU C O   1 
ATOM   3539 C  CB  . LEU C 3 190 ? -62.827 -47.466 27.136  1   26.02 ? 221 LEU C CB  1 
ATOM   3540 C  CG  . LEU C 3 190 ? -62.431 -47.609 25.665  1   27.43 ? 221 LEU C CG  1 
ATOM   3541 C  CD1 . LEU C 3 190 ? -61.831 -48.993 25.397  1   28.15 ? 221 LEU C CD1 1 
ATOM   3542 C  CD2 . LEU C 3 190 ? -63.639 -47.37  24.748  1   27.96 ? 221 LEU C CD2 1 
ATOM   3543 N  N   . PRO C 3 191 ? -65.288 -46.205 28.81   1   29.12 ? 222 PRO C N   1 
ATOM   3544 C  CA  . PRO C 3 191 ? -66.107 -46.295 30.021  1   30.13 ? 222 PRO C CA  1 
ATOM   3545 C  C   . PRO C 3 191 ? -65.855 -47.593 30.809  1   30.45 ? 222 PRO C C   1 
ATOM   3546 O  O   . PRO C 3 191 ? -65.299 -48.56  30.276  1   30.69 ? 222 PRO C O   1 
ATOM   3547 C  CB  . PRO C 3 191 ? -67.559 -46.246 29.485  1   30.89 ? 222 PRO C CB  1 
ATOM   3548 C  CG  . PRO C 3 191 ? -67.468 -45.817 28.078  1   31.5  ? 222 PRO C CG  1 
ATOM   3549 C  CD  . PRO C 3 191 ? -66.114 -46.295 27.592  1   29.67 ? 222 PRO C CD  1 
ATOM   3550 N  N   . LEU C 3 192 ? -66.292 -47.625 32.068  1   30.9  ? 223 LEU C N   1 
ATOM   3551 C  CA  . LEU C 3 192 ? -66.133 -48.835 32.878  1   31.61 ? 223 LEU C CA  1 
ATOM   3552 C  C   . LEU C 3 192 ? -67.492 -49.56  32.993  1   32.35 ? 223 LEU C C   1 
ATOM   3553 O  O   . LEU C 3 192 ? -68.546 -48.921 33.011  1   33.17 ? 223 LEU C O   1 
ATOM   3554 C  CB  . LEU C 3 192 ? -65.672 -48.484 34.307  1   31.74 ? 223 LEU C CB  1 
ATOM   3555 C  CG  . LEU C 3 192 ? -64.593 -47.443 34.502  1   32.91 ? 223 LEU C CG  1 
ATOM   3556 C  CD1 . LEU C 3 192 ? -64.458 -47.104 36.006  1   33.17 ? 223 LEU C CD1 1 
ATOM   3557 C  CD2 . LEU C 3 192 ? -63.234 -47.955 33.986  1   33.24 ? 223 LEU C CD2 1 
ATOM   3558 N  N   . THR C 3 193 ? -67.46  -50.881 33.148  1   32.29 ? 224 THR C N   1 
ATOM   3559 C  CA  . THR C 3 193 ? -68.652 -51.648 33.503  1   32.84 ? 224 THR C CA  1 
ATOM   3560 C  C   . THR C 3 193 ? -68.29  -52.336 34.834  1   32.47 ? 224 THR C C   1 
ATOM   3561 O  O   . THR C 3 193 ? -67.25  -52.984 34.909  1   31.6  ? 224 THR C O   1 
ATOM   3562 C  CB  . THR C 3 193 ? -69.013 -52.66  32.425  1   35.28 ? 224 THR C CB  1 
ATOM   3563 O  OG1 . THR C 3 193 ? -69.446 -51.939 31.275  1   36    ? 224 THR C OG1 1 
ATOM   3564 C  CG2 . THR C 3 193 ? -70.13  -53.614 32.864  1   36.51 ? 224 THR C CG2 1 
ATOM   3565 N  N   . VAL C 3 194 ? -69.077 -52.128 35.899  1   33.41 ? 225 VAL C N   1 
ATOM   3566 C  CA  . VAL C 3 194 ? -68.791 -52.764 37.186  1   34.21 ? 225 VAL C CA  1 
ATOM   3567 C  C   . VAL C 3 194 ? -69.953 -53.697 37.488  1   35.39 ? 225 VAL C C   1 
ATOM   3568 O  O   . VAL C 3 194 ? -71.095 -53.245 37.509  1   35.53 ? 225 VAL C O   1 
ATOM   3569 C  CB  . VAL C 3 194 ? -68.597 -51.728 38.319  1   34.86 ? 225 VAL C CB  1 
ATOM   3570 C  CG1 . VAL C 3 194 ? -68.399 -52.416 39.678  1   35.4  ? 225 VAL C CG1 1 
ATOM   3571 C  CG2 . VAL C 3 194 ? -67.435 -50.797 38.007  1   34.7  ? 225 VAL C CG2 1 
ATOM   3572 N  N   . VAL C 3 195 ? -69.684 -54.992 37.671  1   35.72 ? 226 VAL C N   1 
ATOM   3573 C  CA  . VAL C 3 195 ? -70.74  -55.948 37.954  1   37.31 ? 226 VAL C CA  1 
ATOM   3574 C  C   . VAL C 3 195 ? -70.694 -56.297 39.449  1   39.13 ? 226 VAL C C   1 
ATOM   3575 O  O   . VAL C 3 195 ? -69.692 -56.809 39.923  1   39.09 ? 226 VAL C O   1 
ATOM   3576 C  CB  . VAL C 3 195 ? -70.649 -57.219 37.072  1   37.27 ? 226 VAL C CB  1 
ATOM   3577 C  CG1 . VAL C 3 195 ? -71.7   -58.243 37.498  1   38.04 ? 226 VAL C CG1 1 
ATOM   3578 C  CG2 . VAL C 3 195 ? -70.762 -56.877 35.579  1   37.2  ? 226 VAL C CG2 1 
ATOM   3579 N  N   . LEU C 3 196 ? -71.747 -55.983 40.186  1   41.03 ? 227 LEU C N   1 
ATOM   3580 C  CA  . LEU C 3 196 ? -71.835 -56.27  41.626  1   43.37 ? 227 LEU C CA  1 
ATOM   3581 C  C   . LEU C 3 196 ? -72.402 -57.668 41.85   1   46.19 ? 227 LEU C C   1 
ATOM   3582 O  O   . LEU C 3 196 ? -73.494 -57.97  41.383  1   45.88 ? 227 LEU C O   1 
ATOM   3583 C  CB  . LEU C 3 196 ? -72.751 -55.251 42.315  1   43.92 ? 227 LEU C CB  1 
ATOM   3584 C  CG  . LEU C 3 196 ? -72.479 -53.783 42.017  1   46.34 ? 227 LEU C CG  1 
ATOM   3585 C  CD1 . LEU C 3 196 ? -73.606 -52.899 42.567  1   47.48 ? 227 LEU C CD1 1 
ATOM   3586 C  CD2 . LEU C 3 196 ? -71.114 -53.368 42.53   1   46.99 ? 227 LEU C CD2 1 
ATOM   3587 N  N   . ASN C 3 197 ? -71.715 -58.497 42.644  1   48.44 ? 228 ASN C N   1 
ATOM   3588 C  CA  . ASN C 3 197 ? -72.171 -59.866 42.908  1   50.24 ? 228 ASN C CA  1 
ATOM   3589 C  C   . ASN C 3 197 ? -72.454 -60.047 44.384  1   51.41 ? 228 ASN C C   1 
ATOM   3590 O  O   . ASN C 3 197 ? -71.573 -59.792 45.208  1   51.8  ? 228 ASN C O   1 
ATOM   3591 C  CB  . ASN C 3 197 ? -71.096 -60.874 42.431  1   52.53 ? 228 ASN C CB  1 
ATOM   3592 C  CG  . ASN C 3 197 ? -70.655 -60.667 40.984  1   56.53 ? 228 ASN C CG  1 
ATOM   3593 O  OD1 . ASN C 3 197 ? -71.459 -60.75  40.047  1   58.62 ? 228 ASN C OD1 1 
ATOM   3594 N  ND2 . ASN C 3 197 ? -69.369 -60.388 40.764  1   55.63 ? 228 ASN C ND2 1 
HETATM 3595 C  CHA . HEM D 4 .   ? -37.52  -42.029 20.564  1   19.37 ? 201 HEM A CHA 1 
HETATM 3596 C  CHB . HEM D 4 .   ? -37.006 -44.951 16.756  1   18.1  ? 201 HEM A CHB 1 
HETATM 3597 C  CHC . HEM D 4 .   ? -34.824 -41.402 14.345  1   17.9  ? 201 HEM A CHC 1 
HETATM 3598 C  CHD . HEM D 4 .   ? -35.125 -38.511 18.234  1   17    ? 201 HEM A CHD 1 
HETATM 3599 C  C1A . HEM D 4 .   ? -37.533 -43.169 19.735  1   19.28 ? 201 HEM A C1A 1 
HETATM 3600 C  C2A . HEM D 4 .   ? -38.017 -44.476 20.157  1   20.28 ? 201 HEM A C2A 1 
HETATM 3601 C  C3A . HEM D 4 .   ? -37.857 -45.319 19.085  1   18.78 ? 201 HEM A C3A 1 
HETATM 3602 C  C4A . HEM D 4 .   ? -37.268 -44.518 18.017  1   18.46 ? 201 HEM A C4A 1 
HETATM 3603 C  CMA . HEM D 4 .   ? -38.213 -46.772 18.992  1   18.7  ? 201 HEM A CMA 1 
HETATM 3604 C  CAA . HEM D 4 .   ? -38.601 -44.84  21.499  1   22.23 ? 201 HEM A CAA 1 
HETATM 3605 C  CBA . HEM D 4 .   ? -40.12  -44.786 21.493  1   24.19 ? 201 HEM A CBA 1 
HETATM 3606 C  CGA . HEM D 4 .   ? -40.75  -45.461 22.679  1   25.62 ? 201 HEM A CGA 1 
HETATM 3607 O  O1A . HEM D 4 .   ? -40.188 -45.604 23.713  1   25.47 ? 201 HEM A O1A 1 
HETATM 3608 O  O2A . HEM D 4 .   ? -41.939 -45.912 22.473  1   26.47 ? 201 HEM A O2A 1 
HETATM 3609 C  C1B . HEM D 4 .   ? -36.413 -44.234 15.718  1   18.51 ? 201 HEM A C1B 1 
HETATM 3610 C  C2B . HEM D 4 .   ? -36.102 -44.8   14.417  1   18.41 ? 201 HEM A C2B 1 
HETATM 3611 C  C3B . HEM D 4 .   ? -35.479 -43.768 13.741  1   18.81 ? 201 HEM A C3B 1 
HETATM 3612 C  C4B . HEM D 4 .   ? -35.423 -42.62  14.608  1   18.62 ? 201 HEM A C4B 1 
HETATM 3613 C  CMB . HEM D 4 .   ? -36.433 -46.202 13.991  1   18.08 ? 201 HEM A CMB 1 
HETATM 3614 C  CAB . HEM D 4 .   ? -34.972 -43.751 12.362  1   20.72 ? 201 HEM A CAB 1 
HETATM 3615 C  CBB . HEM D 4 .   ? -34.454 -44.779 11.705  1   22.74 ? 201 HEM A CBB 1 
HETATM 3616 C  C1C . HEM D 4 .   ? -34.699 -40.275 15.184  1   17.81 ? 201 HEM A C1C 1 
HETATM 3617 C  C2C . HEM D 4 .   ? -33.913 -39.098 14.848  1   17.31 ? 201 HEM A C2C 1 
HETATM 3618 C  C3C . HEM D 4 .   ? -33.996 -38.282 15.967  1   18    ? 201 HEM A C3C 1 
HETATM 3619 C  C4C . HEM D 4 .   ? -34.811 -38.967 16.95   1   17.79 ? 201 HEM A C4C 1 
HETATM 3620 C  CMC . HEM D 4 .   ? -33.206 -38.874 13.543  1   15.7  ? 201 HEM A CMC 1 
HETATM 3621 C  CAC . HEM D 4 .   ? -33.377 -36.967 16.168  1   18.53 ? 201 HEM A CAC 1 
HETATM 3622 C  CBC . HEM D 4 .   ? -32.128 -36.588 15.796  1   19.14 ? 201 HEM A CBC 1 
HETATM 3623 C  C1D . HEM D 4 .   ? -35.858 -39.209 19.219  1   17.77 ? 201 HEM A C1D 1 
HETATM 3624 C  C2D . HEM D 4 .   ? -36.076 -38.73  20.581  1   18.27 ? 201 HEM A C2D 1 
HETATM 3625 C  C3D . HEM D 4 .   ? -36.748 -39.735 21.242  1   19.31 ? 201 HEM A C3D 1 
HETATM 3626 C  C4D . HEM D 4 .   ? -36.935 -40.807 20.282  1   18.84 ? 201 HEM A C4D 1 
HETATM 3627 C  CMD . HEM D 4 .   ? -35.628 -37.406 21.114  1   18.43 ? 201 HEM A CMD 1 
HETATM 3628 C  CAD . HEM D 4 .   ? -37.105 -39.765 22.706  1   21.34 ? 201 HEM A CAD 1 
HETATM 3629 C  CBD . HEM D 4 .   ? -36.033 -40.481 23.523  1   23.92 ? 201 HEM A CBD 1 
HETATM 3630 C  CGD . HEM D 4 .   ? -36.323 -40.522 25      1   26.54 ? 201 HEM A CGD 1 
HETATM 3631 O  O1D . HEM D 4 .   ? -36.734 -39.589 25.619  1   25.6  ? 201 HEM A O1D 1 
HETATM 3632 O  O2D . HEM D 4 .   ? -36.047 -41.654 25.557  1   28.85 ? 201 HEM A O2D 1 
HETATM 3633 N  NA  . HEM D 4 .   ? -37.083 -43.213 18.451  1   19.38 ? 201 HEM A NA  1 
HETATM 3634 N  NB  . HEM D 4 .   ? -36.016 -42.932 15.804  1   18.59 ? 201 HEM A NB  1 
HETATM 3635 N  NC  . HEM D 4 .   ? -35.22  -40.178 16.435  1   18.1  ? 201 HEM A NC  1 
HETATM 3636 N  ND  . HEM D 4 .   ? -36.386 -40.45  19.054  1   18.09 ? 201 HEM A ND  1 
HETATM 3637 FE FE  . HEM D 4 .   ? -36.204 -41.677 17.429  1   19.12 ? 201 HEM A FE  1 
HETATM 3638 C  C1  . GOL E 5 .   ? -40.848 -35.03  5.192   1   41.91 ? 202 GOL A C1  1 
HETATM 3639 O  O1  . GOL E 5 .   ? -39.557 -35.551 4.866   1   42.86 ? 202 GOL A O1  1 
HETATM 3640 C  C2  . GOL E 5 .   ? -41.914 -35.916 4.602   1   40.64 ? 202 GOL A C2  1 
HETATM 3641 O  O2  . GOL E 5 .   ? -41.661 -37.256 5.019   1   41.2  ? 202 GOL A O2  1 
HETATM 3642 C  C3  . GOL E 5 .   ? -43.327 -35.483 4.94    1   38.58 ? 202 GOL A C3  1 
HETATM 3643 O  O3  . GOL E 5 .   ? -44.287 -36.281 4.242   1   36.18 ? 202 GOL A O3  1 
HETATM 3644 C  CHA . HEM F 4 .   ? -35.431 -15.014 13.632  1   34.78 ? 201 HEM B CHA 1 
HETATM 3645 C  CHB . HEM F 4 .   ? -34.967 -13.849 8.934   1   32.76 ? 201 HEM B CHB 1 
HETATM 3646 C  CHC . HEM F 4 .   ? -35.497 -18.495 7.785   1   31.85 ? 201 HEM B CHC 1 
HETATM 3647 C  CHD . HEM F 4 .   ? -36.345 -19.636 12.41   1   32.33 ? 201 HEM B CHD 1 
HETATM 3648 C  C1A . HEM F 4 .   ? -35.253 -14.279 12.442  1   34.91 ? 201 HEM B C1A 1 
HETATM 3649 C  C2A . HEM F 4 .   ? -35.137 -12.833 12.387  1   36.17 ? 201 HEM B C2A 1 
HETATM 3650 C  C3A . HEM F 4 .   ? -35.034 -12.497 11.046  1   34.92 ? 201 HEM B C3A 1 
HETATM 3651 C  C4A . HEM F 4 .   ? -35.067 -13.744 10.31   1   33.71 ? 201 HEM B C4A 1 
HETATM 3652 C  CMA . HEM F 4 .   ? -34.948 -11.133 10.428  1   35.31 ? 201 HEM B CMA 1 
HETATM 3653 C  CAA . HEM F 4 .   ? -35.077 -11.918 13.581  1   38.23 ? 201 HEM B CAA 1 
HETATM 3654 C  CBA . HEM F 4 .   ? -33.64  -11.622 13.977  1   41.1  ? 201 HEM B CBA 1 
HETATM 3655 C  CGA . HEM F 4 .   ? -33.484 -10.75  15.191  1   44.22 ? 201 HEM B CGA 1 
HETATM 3656 O  O1A . HEM F 4 .   ? -32.8   -11.068 16.14   1   45.55 ? 201 HEM B O1A 1 
HETATM 3657 O  O2A . HEM F 4 .   ? -34.102 -9.604  15.115  1   45.58 ? 201 HEM B O2A 1 
HETATM 3658 C  C1B . HEM F 4 .   ? -35.019 -15.026 8.19    1   32.21 ? 201 HEM B C1B 1 
HETATM 3659 C  C2B . HEM F 4 .   ? -34.941 -15.093 6.74    1   32.16 ? 201 HEM B C2B 1 
HETATM 3660 C  C3B . HEM F 4 .   ? -35.093 -16.408 6.421   1   31.95 ? 201 HEM B C3B 1 
HETATM 3661 C  C4B . HEM F 4 .   ? -35.261 -17.137 7.659   1   31.99 ? 201 HEM B C4B 1 
HETATM 3662 C  CMB . HEM F 4 .   ? -34.747 -13.926 5.82    1   32.12 ? 201 HEM B CMB 1 
HETATM 3663 C  CAB . HEM F 4 .   ? -35.051 -16.909 5.045   1   32.73 ? 201 HEM B CAB 1 
HETATM 3664 C  CBB . HEM F 4 .   ? -34.726 -18.079 4.599   1   33.37 ? 201 HEM B CBB 1 
HETATM 3665 C  C1C . HEM F 4 .   ? -35.791 -19.236 8.94    1   31.54 ? 201 HEM B C1C 1 
HETATM 3666 C  C2C . HEM F 4 .   ? -36.16  -20.642 8.934   1   31.01 ? 201 HEM B C2C 1 
HETATM 3667 C  C3C . HEM F 4 .   ? -36.408 -20.955 10.255  1   31.5  ? 201 HEM B C3C 1 
HETATM 3668 C  C4C . HEM F 4 .   ? -36.193 -19.76  11.035  1   31.88 ? 201 HEM B C4C 1 
HETATM 3669 C  CMC . HEM F 4 .   ? -36.275 -21.498 7.707   1   30.6  ? 201 HEM B CMC 1 
HETATM 3670 C  CAC . HEM F 4 .   ? -36.845 -22.233 10.824  1   32.11 ? 201 HEM B CAC 1 
HETATM 3671 C  CBC . HEM F 4 .   ? -37.384 -23.306 10.212  1   32.62 ? 201 HEM B CBC 1 
HETATM 3672 C  C1D . HEM F 4 .   ? -36.124 -18.454 13.178  1   33.66 ? 201 HEM B C1D 1 
HETATM 3673 C  C2D . HEM F 4 .   ? -36.255 -18.38  14.619  1   34.69 ? 201 HEM B C2D 1 
HETATM 3674 C  C3D . HEM F 4 .   ? -36.012 -17.073 14.962  1   35.99 ? 201 HEM B C3D 1 
HETATM 3675 C  C4D . HEM F 4 .   ? -35.709 -16.368 13.726  1   34.99 ? 201 HEM B C4D 1 
HETATM 3676 C  CMD . HEM F 4 .   ? -36.561 -19.532 15.527  1   35.23 ? 201 HEM B CMD 1 
HETATM 3677 C  CAD . HEM F 4 .   ? -36.156 -16.478 16.335  1   37.74 ? 201 HEM B CAD 1 
HETATM 3678 C  CBD . HEM F 4 .   ? -37.583 -16.042 16.587  1   40.32 ? 201 HEM B CBD 1 
HETATM 3679 C  CGD . HEM F 4 .   ? -37.885 -15.779 18.032  1   42.94 ? 201 HEM B CGD 1 
HETATM 3680 O  O1D . HEM F 4 .   ? -37.871 -16.645 18.891  1   43.73 ? 201 HEM B O1D 1 
HETATM 3681 O  O2D . HEM F 4 .   ? -38.163 -14.527 18.265  1   44.16 ? 201 HEM B O2D 1 
HETATM 3682 N  NA  . HEM F 4 .   ? -35.205 -14.802 11.187  1   33.56 ? 201 HEM B NA  1 
HETATM 3683 N  NB  . HEM F 4 .   ? -35.197 -16.258 8.726   1   31.9  ? 201 HEM B NB  1 
HETATM 3684 N  NC  . HEM F 4 .   ? -35.809 -18.728 10.2    1   31.68 ? 201 HEM B NC  1 
HETATM 3685 N  ND  . HEM F 4 .   ? -35.784 -17.238 12.659  1   33.33 ? 201 HEM B ND  1 
HETATM 3686 FE FE  . HEM F 4 .   ? -35.479 -16.762 10.706  1   32.69 ? 201 HEM B FE  1 
HETATM 3687 C  C1  . GOL G 5 .   ? -31.374 -21.085 -8.39   1   67.69 ? 202 GOL B C1  1 
HETATM 3688 O  O1  . GOL G 5 .   ? -32.726 -21.423 -8.135  1   67.3  ? 202 GOL B O1  1 
HETATM 3689 C  C2  . GOL G 5 .   ? -31.273 -19.728 -9.049  1   67.87 ? 202 GOL B C2  1 
HETATM 3690 O  O2  . GOL G 5 .   ? -29.907 -19.297 -9.115  1   67.99 ? 202 GOL B O2  1 
HETATM 3691 C  C3  . GOL G 5 .   ? -31.92  -19.699 -10.414 1   67.7  ? 202 GOL B C3  1 
HETATM 3692 O  O3  . GOL G 5 .   ? -31.683 -20.907 -11.13  1   67.58 ? 202 GOL B O3  1 
HETATM 3693 P  P   . PO4 H 6 .   ? -50.24  -28.546 11.556  1   58.27 ? 203 PO4 B P   1 
HETATM 3694 O  O1  . PO4 H 6 .   ? -49.345 -29.23  10.508  1   57.02 ? 203 PO4 B O1  1 
HETATM 3695 O  O2  . PO4 H 6 .   ? -49.455 -28.352 12.869  1   57.48 ? 203 PO4 B O2  1 
HETATM 3696 O  O3  . PO4 H 6 .   ? -50.735 -27.164 11.074  1   57.87 ? 203 PO4 B O3  1 
HETATM 3697 O  O4  . PO4 H 6 .   ? -51.472 -29.445 11.828  1   58.76 ? 203 PO4 B O4  1 
HETATM 3698 C  C1  . GOL I 5 .   ? -54.243 -54.046 25.459  1   41.43 ? 301 GOL C C1  1 
HETATM 3699 O  O1  . GOL I 5 .   ? -53.314 -55.078 25.828  1   41.22 ? 301 GOL C O1  1 
HETATM 3700 C  C2  . GOL I 5 .   ? -55.698 -54.446 25.645  1   41.52 ? 301 GOL C C2  1 
HETATM 3701 O  O2  . GOL I 5 .   ? -55.844 -55.854 25.868  1   41.96 ? 301 GOL C O2  1 
HETATM 3702 C  C3  . GOL I 5 .   ? -56.374 -53.696 26.771  1   41.43 ? 301 GOL C C3  1 
HETATM 3703 O  O3  . GOL I 5 .   ? -57.696 -54.171 26.99   1   41.27 ? 301 GOL C O3  1 
HETATM 3704 O  O   . HOH J 7 .   ? -18.934 -40.465 14.14   1   40.85 ? 301 HOH A O   1 
HETATM 3705 O  O   . HOH J 7 .   ? -38.466 -44.82  25.289  1   46.2  ? 302 HOH A O   1 
HETATM 3706 O  O   . HOH J 7 .   ? -35.21  -29.025 14.193  1   36    ? 303 HOH A O   1 
HETATM 3707 O  O   . HOH J 7 .   ? -43.717 -32.159 12.274  1   24.19 ? 304 HOH A O   1 
HETATM 3708 O  O   . HOH J 7 .   ? -40.67  -34.912 11.84   1   22.9  ? 305 HOH A O   1 
HETATM 3709 O  O   . HOH J 7 .   ? -37.064 -52.167 22.734  1   29.37 ? 306 HOH A O   1 
HETATM 3710 O  O   . HOH J 7 .   ? -28.526 -59.337 -2.776  1   44.89 ? 307 HOH A O   1 
HETATM 3711 O  O   . HOH J 7 .   ? -32.409 -51.116 -5.442  1   38.36 ? 308 HOH A O   1 
HETATM 3712 O  O   . HOH J 7 .   ? -45.778 -30.361 13.352  1   22.41 ? 309 HOH A O   1 
HETATM 3713 O  O   . HOH J 7 .   ? -49.838 -42.791 18.913  1   28.53 ? 310 HOH A O   1 
HETATM 3714 O  O   . HOH J 7 .   ? -49.572 -49.183 6.252   1   25.09 ? 311 HOH A O   1 
HETATM 3715 O  O   . HOH J 7 .   ? -34.205 -56.291 17.255  1   30.95 ? 312 HOH A O   1 
HETATM 3716 O  O   . HOH J 7 .   ? -56.498 -40.875 12.551  1   26.84 ? 313 HOH A O   1 
HETATM 3717 O  O   . HOH J 7 .   ? -27.883 -51.463 23.595  1   46.64 ? 314 HOH A O   1 
HETATM 3718 O  O   . HOH J 7 .   ? -35.177 -44.121 25.116  1   36.46 ? 315 HOH A O   1 
HETATM 3719 O  O   . HOH J 7 .   ? -58.027 -38.926 9.75    1   52.13 ? 316 HOH A O   1 
HETATM 3720 O  O   . HOH J 7 .   ? -24.221 -31.121 13.209  1   31.83 ? 317 HOH A O   1 
HETATM 3721 O  O   . HOH J 7 .   ? -40.044 -37.914 2.802   1   26.73 ? 318 HOH A O   1 
HETATM 3722 O  O   . HOH J 7 .   ? -21.888 -33.599 24.21   1   39.46 ? 319 HOH A O   1 
HETATM 3723 O  O   . HOH J 7 .   ? -45.069 -52.033 15.16   1   35.88 ? 320 HOH A O   1 
HETATM 3724 O  O   . HOH J 7 .   ? -52.702 -53.524 8.398   1   32.34 ? 321 HOH A O   1 
HETATM 3725 O  O   . HOH J 7 .   ? -28.414 -31.81  24.118  1   27.52 ? 322 HOH A O   1 
HETATM 3726 O  O   . HOH J 7 .   ? -18.005 -34.000 12.365  1   33.28 ? 323 HOH A O   1 
HETATM 3727 O  O   . HOH J 7 .   ? -32.219 -28.864 22.98   1   31.37 ? 324 HOH A O   1 
HETATM 3728 O  O   . HOH J 7 .   ? -39.8   -41.764 0.736   1   22.69 ? 325 HOH A O   1 
HETATM 3729 O  O   . HOH J 7 .   ? -34.932 -60.321 8.816   1   33.85 ? 326 HOH A O   1 
HETATM 3730 O  O   . HOH J 7 .   ? -27.887 -42.806 4.012   1   40.64 ? 327 HOH A O   1 
HETATM 3731 O  O   . HOH J 7 .   ? -55.037 -41.866 8.928   1   35.96 ? 328 HOH A O   1 
HETATM 3732 O  O   . HOH J 7 .   ? -52.261 -35.921 10.462  1   38.9  ? 329 HOH A O   1 
HETATM 3733 O  O   . HOH J 7 .   ? -34.203 -42.28  18      1   22.86 ? 330 HOH A O   1 
HETATM 3734 O  O   . HOH J 7 .   ? -43.967 -36.167 1.544   1   28.59 ? 331 HOH A O   1 
HETATM 3735 O  O   . HOH J 7 .   ? -32.051 -58.967 13.427  1   38.05 ? 332 HOH A O   1 
HETATM 3736 O  O   . HOH J 7 .   ? -18.602 -57.404 0.694   1   45.88 ? 333 HOH A O   1 
HETATM 3737 O  O   . HOH J 7 .   ? -52.714 -46.693 11.317  1   35.15 ? 334 HOH A O   1 
HETATM 3738 O  O   . HOH J 7 .   ? -25.888 -58.74  -2.58   1   36.28 ? 335 HOH A O   1 
HETATM 3739 O  O   . HOH J 7 .   ? -47.711 -31.383 15.726  1   36.66 ? 336 HOH A O   1 
HETATM 3740 O  O   . HOH J 7 .   ? -33.636 -50.402 25.916  1   27.56 ? 337 HOH A O   1 
HETATM 3741 O  O   . HOH J 7 .   ? -43.793 -45.147 20.572  1   25.65 ? 338 HOH A O   1 
HETATM 3742 O  O   . HOH J 7 .   ? -20.612 -34.348 19.817  1   37.39 ? 339 HOH A O   1 
HETATM 3743 O  O   . HOH J 7 .   ? -50.527 -33.276 15.879  1   41.15 ? 340 HOH A O   1 
HETATM 3744 O  O   . HOH J 7 .   ? -51.57  -47.946 13.188  1   38.41 ? 341 HOH A O   1 
HETATM 3745 O  O   . HOH J 7 .   ? -35.447 -37.703 5.858   1   20.63 ? 342 HOH A O   1 
HETATM 3746 O  O   . HOH J 7 .   ? -25.02  -42.678 3.329   1   23.6  ? 343 HOH A O   1 
HETATM 3747 O  O   . HOH J 7 .   ? -33.224 -28.052 11.449  1   27.52 ? 344 HOH A O   1 
HETATM 3748 O  O   . HOH J 7 .   ? -26.605 -56.031 21.368  1   43.92 ? 345 HOH A O   1 
HETATM 3749 O  O   . HOH J 7 .   ? -37.655 -58.384 11.247  1   23.37 ? 346 HOH A O   1 
HETATM 3750 O  O   . HOH J 7 .   ? -36.455 -33.181 21.674  1   32.28 ? 347 HOH A O   1 
HETATM 3751 O  O   . HOH J 7 .   ? -25.033 -44.119 1.103   1   24.76 ? 348 HOH A O   1 
HETATM 3752 O  O   . HOH J 7 .   ? -42.553 -51.357 1.025   1   39.31 ? 349 HOH A O   1 
HETATM 3753 O  O   . HOH J 7 .   ? -43.081 -51.872 -2.992  1   48.12 ? 350 HOH A O   1 
HETATM 3754 O  O   . HOH J 7 .   ? -31.387 -43.524 3.707   1   25.86 ? 351 HOH A O   1 
HETATM 3755 O  O   . HOH J 7 .   ? -48.686 -39.37  11.42   1   19.16 ? 352 HOH A O   1 
HETATM 3756 O  O   . HOH J 7 .   ? -50.743 -44.426 16.684  1   32.49 ? 353 HOH A O   1 
HETATM 3757 O  O   . HOH J 7 .   ? -44.835 -49.75  3.797   1   23.53 ? 354 HOH A O   1 
HETATM 3758 O  O   . HOH J 7 .   ? -36.239 -61.328 -4.229  1   43.48 ? 355 HOH A O   1 
HETATM 3759 O  O   . HOH J 7 .   ? -38.82  -44.883 27.841  1   58.54 ? 356 HOH A O   1 
HETATM 3760 O  O   . HOH J 7 .   ? -21.075 -39.744 20.662  1   31.85 ? 357 HOH A O   1 
HETATM 3761 O  O   . HOH J 7 .   ? -45.401 -42.856 20.639  1   24.17 ? 358 HOH A O   1 
HETATM 3762 O  O   . HOH J 7 .   ? -30.385 -57.254 -5.358  1   35.37 ? 359 HOH A O   1 
HETATM 3763 O  O   . HOH J 7 .   ? -36.832 -39.967 3.378   1   23.08 ? 360 HOH A O   1 
HETATM 3764 O  O   . HOH J 7 .   ? -49.47  -41.587 13.104  1   24.45 ? 361 HOH A O   1 
HETATM 3765 O  O   . HOH J 7 .   ? -28.698 -40.655 4.354   1   37.04 ? 362 HOH A O   1 
HETATM 3766 O  O   . HOH J 7 .   ? -22.207 -50.331 20.744  1   34.81 ? 363 HOH A O   1 
HETATM 3767 O  O   . HOH J 7 .   ? -42.496 -33.567 10.429  1   27.58 ? 364 HOH A O   1 
HETATM 3768 O  O   . HOH J 7 .   ? -30.162 -52.964 -4.942  1   29.29 ? 365 HOH A O   1 
HETATM 3769 O  O   . HOH J 7 .   ? -23.971 -56.059 -5.165  1   27.6  ? 366 HOH A O   1 
HETATM 3770 O  O   . HOH J 7 .   ? -42.03  -44.907 -1.571  1   24.92 ? 367 HOH A O   1 
HETATM 3771 O  O   . HOH J 7 .   ? -42.027 -49.487 -0.857  1   29.9  ? 368 HOH A O   1 
HETATM 3772 O  O   . HOH J 7 .   ? -32.137 -27.647 17.387  1   48.57 ? 369 HOH A O   1 
HETATM 3773 O  O   . HOH J 7 .   ? -41.089 -58.278 14.514  1   43.16 ? 370 HOH A O   1 
HETATM 3774 O  O   . HOH J 7 .   ? -39.775 -59.718 -2.253  1   40.93 ? 371 HOH A O   1 
HETATM 3775 O  O   . HOH J 7 .   ? -47.02  -34.436 6.727   1   24.65 ? 372 HOH A O   1 
HETATM 3776 O  O   . HOH J 7 .   ? -48.322 -35.965 19.613  1   33.37 ? 373 HOH A O   1 
HETATM 3777 O  O   . HOH J 7 .   ? -32.704 -44.752 27.265  1   45.21 ? 374 HOH A O   1 
HETATM 3778 O  O   . HOH J 7 .   ? -47.157 -56.848 7.557   1   53.43 ? 375 HOH A O   1 
HETATM 3779 O  O   . HOH J 7 .   ? -41.026 -44.055 0.642   1   26.08 ? 376 HOH A O   1 
HETATM 3780 O  O   . HOH J 7 .   ? -38.619 -55.925 17.426  1   45.66 ? 377 HOH A O   1 
HETATM 3781 O  O   . HOH J 7 .   ? -32.16  -30.01  12.81   1   43    ? 378 HOH A O   1 
HETATM 3782 O  O   . HOH J 7 .   ? -32.833 -41.721 5.16    1   26.98 ? 379 HOH A O   1 
HETATM 3783 O  O   . HOH J 7 .   ? -44.676 -56.151 15.257  1   60.94 ? 380 HOH A O   1 
HETATM 3784 O  O   . HOH J 7 .   ? -37.716 -46.144 -1.042  1   30.74 ? 381 HOH A O   1 
HETATM 3785 O  O   . HOH J 7 .   ? -26.749 -43.053 31.305  1   37.36 ? 382 HOH A O   1 
HETATM 3786 O  O   . HOH J 7 .   ? -56.681 -36.752 7.974   1   31.89 ? 383 HOH A O   1 
HETATM 3787 O  O   . HOH J 7 .   ? -37.87  -38.112 5.379   1   33.93 ? 384 HOH A O   1 
HETATM 3788 O  O   . HOH J 7 .   ? -42.795 -53.503 -5.133  1   44.08 ? 385 HOH A O   1 
HETATM 3789 O  O   . HOH J 7 .   ? -45.225 -56.541 5.318   1   38.37 ? 386 HOH A O   1 
HETATM 3790 O  O   . HOH J 7 .   ? -29.835 -56.561 21.359  1   55.02 ? 387 HOH A O   1 
HETATM 3791 O  O   . HOH J 7 .   ? -23.965 -44.281 32.121  1   44.36 ? 388 HOH A O   1 
HETATM 3792 O  O   . HOH J 7 .   ? -40.535 -55.599 19.334  1   50.06 ? 389 HOH A O   1 
HETATM 3793 O  O   . HOH J 7 .   ? -42.724 -44.246 3.022   1   33.01 ? 390 HOH A O   1 
HETATM 3794 O  O   . HOH J 7 .   ? -30.559 -34.788 32.472  1   56.82 ? 391 HOH A O   1 
HETATM 3795 O  O   . HOH J 7 .   ? -30.637 -39.073 0.817   1   44.02 ? 392 HOH A O   1 
HETATM 3796 O  O   . HOH J 7 .   ? -34.448 -39.789 4.342   1   30.45 ? 393 HOH A O   1 
HETATM 3797 O  O   . HOH J 7 .   ? -52.554 -44.573 10.241  1   47.6  ? 394 HOH A O   1 
HETATM 3798 O  O   . HOH J 7 .   ? -21.094 -37.168 21.506  1   51.84 ? 395 HOH A O   1 
HETATM 3799 O  O   . HOH J 7 .   ? -40.085 -41.843 25.633  1   45.33 ? 396 HOH A O   1 
HETATM 3800 O  O   . HOH J 7 .   ? -32.230 -48.572 -6.527  1   32.38 ? 397 HOH A O   1 
HETATM 3801 O  O   . HOH J 7 .   ? -25.052 -51.786 23.84   1   43.68 ? 398 HOH A O   1 
HETATM 3802 O  O   . HOH J 7 .   ? -35.208 -59.042 11.073  1   34.41 ? 399 HOH A O   1 
HETATM 3803 O  O   . HOH J 7 .   ? -41.846 -37.554 0.714   1   31.77 ? 400 HOH A O   1 
HETATM 3804 O  O   . HOH J 7 .   ? -31.759 -51.835 27.041  1   44.05 ? 401 HOH A O   1 
HETATM 3805 O  O   . HOH J 7 .   ? -38.931 -60.068 13.049  1   40.82 ? 402 HOH A O   1 
HETATM 3806 O  O   . HOH J 7 .   ? -44.662 -51.536 -5.085  1   51.04 ? 403 HOH A O   1 
HETATM 3807 O  O   . HOH J 7 .   ? -34.135 -60.324 13.304  1   42.43 ? 404 HOH A O   1 
HETATM 3808 O  O   . HOH J 7 .   ? -22.824 -50.681 23.237  1   41.08 ? 405 HOH A O   1 
HETATM 3809 O  O   . HOH J 7 .   ? -44.226 -46.353 3.246   1   47.19 ? 406 HOH A O   1 
HETATM 3810 O  O   . HOH J 7 .   ? -19.686 -57.554 -3.792  1   38.62 ? 407 HOH A O   1 
HETATM 3811 O  O   . HOH K 7 .   ? -41.652 -29.816 18.694  1   35.18 ? 301 HOH B O   1 
HETATM 3812 O  O   . HOH K 7 .   ? -45.311 -9.139  6.299   1   43.7  ? 302 HOH B O   1 
HETATM 3813 O  O   . HOH K 7 .   ? -24.52  -11.47  -3.478  1   40.59 ? 303 HOH B O   1 
HETATM 3814 O  O   . HOH K 7 .   ? -49.408 -29.715 7.939   1   36.64 ? 304 HOH B O   1 
HETATM 3815 O  O   . HOH K 7 .   ? -23.87  -14.516 5.425   1   47.11 ? 305 HOH B O   1 
HETATM 3816 O  O   . HOH K 7 .   ? -28.155 -22.646 9.483   1   38.63 ? 306 HOH B O   1 
HETATM 3817 O  O   . HOH K 7 .   ? -48.631 -29.048 15.347  1   30.74 ? 307 HOH B O   1 
HETATM 3818 O  O   . HOH K 7 .   ? -45.943 -3.403  -12.338 1   45.55 ? 308 HOH B O   1 
HETATM 3819 O  O   . HOH K 7 .   ? -34.715 -3.09   2.724   1   31.72 ? 309 HOH B O   1 
HETATM 3820 O  O   . HOH K 7 .   ? -36.164 -7.698  9.542   1   42.59 ? 310 HOH B O   1 
HETATM 3821 O  O   . HOH K 7 .   ? -53.817 -15.454 -7.546  1   30.97 ? 311 HOH B O   1 
HETATM 3822 O  O   . HOH K 7 .   ? -34.626 -20.312 -6.575  1   24.04 ? 312 HOH B O   1 
HETATM 3823 O  O   . HOH K 7 .   ? -35.628 -5.234  -23.777 1   48.89 ? 313 HOH B O   1 
HETATM 3824 O  O   . HOH K 7 .   ? -47.259 -30.865 3.787   1   31.54 ? 314 HOH B O   1 
HETATM 3825 O  O   . HOH K 7 .   ? -35.885 -21.024 -2.524  1   32.13 ? 315 HOH B O   1 
HETATM 3826 O  O   . HOH K 7 .   ? -37.552 -29.354 13.261  1   20.07 ? 316 HOH B O   1 
HETATM 3827 O  O   . HOH K 7 .   ? -37.745 -16.684 10.48   1   33.34 ? 317 HOH B O   1 
HETATM 3828 O  O   . HOH K 7 .   ? -50.924 -15.414 8.174   1   39.09 ? 318 HOH B O   1 
HETATM 3829 O  O   . HOH K 7 .   ? -39.613 -12.447 16.342  1   52.6  ? 319 HOH B O   1 
HETATM 3830 O  O   . HOH K 7 .   ? -57.88  -24.347 15.324  1   46.66 ? 320 HOH B O   1 
HETATM 3831 O  O   . HOH K 7 .   ? -55.666 -21.936 7.061   1   31.16 ? 321 HOH B O   1 
HETATM 3832 O  O   . HOH K 7 .   ? -40.446 -25.665 -1.577  1   43.16 ? 322 HOH B O   1 
HETATM 3833 O  O   . HOH K 7 .   ? -36.454 -3.995  5.931   1   50.16 ? 323 HOH B O   1 
HETATM 3834 O  O   . HOH K 7 .   ? -36.647 -13.165 -15.92  1   30.93 ? 324 HOH B O   1 
HETATM 3835 O  O   . HOH K 7 .   ? -27.669 -19.965 9.256   1   50.7  ? 325 HOH B O   1 
HETATM 3836 O  O   . HOH K 7 .   ? -43.469 -10.234 -17.479 1   35.59 ? 326 HOH B O   1 
HETATM 3837 O  O   . HOH K 7 .   ? -33.413 -29.071 18.881  1   59.53 ? 327 HOH B O   1 
HETATM 3838 O  O   . HOH K 7 .   ? -47.162 -10.374 8.465   1   38.29 ? 328 HOH B O   1 
HETATM 3839 O  O   . HOH K 7 .   ? -43.658 -2.935  -0.381  1   55.88 ? 329 HOH B O   1 
HETATM 3840 O  O   . HOH K 7 .   ? -50.987 -16.933 0.661   1   36.67 ? 330 HOH B O   1 
HETATM 3841 O  O   . HOH K 7 .   ? -32.132 -28.282 14.893  1   43.19 ? 331 HOH B O   1 
HETATM 3842 O  O   . HOH K 7 .   ? -42.906 -6.772  -12.226 1   35.88 ? 332 HOH B O   1 
HETATM 3843 O  O   . HOH K 7 .   ? -56.77  -17.996 10.42   1   43.16 ? 333 HOH B O   1 
HETATM 3844 O  O   . HOH K 7 .   ? -33.562 -10.302 -18.579 1   44.97 ? 334 HOH B O   1 
HETATM 3845 O  O   . HOH K 7 .   ? -38.958 -28.913 -2.507  1   46.14 ? 335 HOH B O   1 
HETATM 3846 O  O   . HOH K 7 .   ? -28.915 -4.688  -4.941  1   42.27 ? 336 HOH B O   1 
HETATM 3847 O  O   . HOH K 7 .   ? -34.554 -28.017 16.604  1   40.24 ? 337 HOH B O   1 
HETATM 3848 O  O   . HOH K 7 .   ? -49.359 -8.231  -1.518  1   41.14 ? 338 HOH B O   1 
HETATM 3849 O  O   . HOH K 7 .   ? -27.319 -9.977  9.169   1   38.89 ? 339 HOH B O   1 
HETATM 3850 O  O   . HOH K 7 .   ? -50.901 -30.209 14.995  1   40.62 ? 340 HOH B O   1 
HETATM 3851 O  O   . HOH K 7 .   ? -35.496 -24.23  -5.452  1   42.94 ? 341 HOH B O   1 
HETATM 3852 O  O   . HOH K 7 .   ? -32.621 -2.17   -12.92  1   55.72 ? 342 HOH B O   1 
HETATM 3853 O  O   . HOH K 7 .   ? -54.025 -17.514 2.088   1   45.97 ? 343 HOH B O   1 
HETATM 3854 O  O   . HOH K 7 .   ? -41.024 -30.899 21.859  1   62.38 ? 344 HOH B O   1 
HETATM 3855 O  O   . HOH K 7 .   ? -38.969 -2.444  -4.33   1   37.48 ? 345 HOH B O   1 
HETATM 3856 O  O   . HOH K 7 .   ? -55.037 -12.927 -11.934 1   42.48 ? 346 HOH B O   1 
HETATM 3857 O  O   . HOH K 7 .   ? -57.668 -25.305 9.825   1   33.15 ? 347 HOH B O   1 
HETATM 3858 O  O   . HOH K 7 .   ? -48.877 -15.473 -15.634 1   41.11 ? 348 HOH B O   1 
HETATM 3859 O  O   . HOH K 7 .   ? -42.774 -0.419  -7.366  1   41.9  ? 349 HOH B O   1 
HETATM 3860 O  O   . HOH K 7 .   ? -55.857 -19.022 1.367   1   34.99 ? 350 HOH B O   1 
HETATM 3861 O  O   . HOH K 7 .   ? -22.4   -12.496 -2.101  1   64.61 ? 351 HOH B O   1 
HETATM 3862 O  O   . HOH K 7 .   ? -57.642 -18.412 7.832   1   56.88 ? 352 HOH B O   1 
HETATM 3863 O  O   . HOH K 7 .   ? -52.164 -33.221 11.526  1   47.68 ? 353 HOH B O   1 
HETATM 3864 O  O   . HOH K 7 .   ? -34.153 -21.859 -4.314  1   41.41 ? 354 HOH B O   1 
HETATM 3865 O  O   . HOH K 7 .   ? -35.141 -28.935 23.863  1   45.82 ? 355 HOH B O   1 
HETATM 3866 O  O   . HOH K 7 .   ? -52.165 -29.29  7.355   1   37.65 ? 356 HOH B O   1 
HETATM 3867 O  O   . HOH K 7 .   ? -55.917 -19.366 5.848   1   38.23 ? 357 HOH B O   1 
HETATM 3868 O  O   . HOH K 7 .   ? -25.877 -23.283 8.292   1   59.4  ? 358 HOH B O   1 
HETATM 3869 O  O   . HOH K 7 .   ? -54.127 -17.497 4.939   1   44.57 ? 359 HOH B O   1 
HETATM 3870 O  O   . HOH L 7 .   ? -43.61  -48.02  29.075  1   22.54 ? 401 HOH C O   1 
HETATM 3871 O  O   . HOH L 7 .   ? -47.387 -33.65  28.402  1   40.64 ? 402 HOH C O   1 
HETATM 3872 O  O   . HOH L 7 .   ? -43.285 -49.85  15.832  1   23.78 ? 403 HOH C O   1 
HETATM 3873 O  O   . HOH L 7 .   ? -42.314 -45.501 25.629  1   35.19 ? 404 HOH C O   1 
HETATM 3874 O  O   . HOH L 7 .   ? -60.995 -37.934 31.576  1   33.1  ? 405 HOH C O   1 
HETATM 3875 O  O   . HOH L 7 .   ? -63.303 -44.662 14.2    1   51.62 ? 406 HOH C O   1 
HETATM 3876 O  O   . HOH L 7 .   ? -63.92  -64.634 43.335  1   34.39 ? 407 HOH C O   1 
HETATM 3877 O  O   . HOH L 7 .   ? -47.588 -35.182 24.783  1   35.07 ? 408 HOH C O   1 
HETATM 3878 O  O   . HOH L 7 .   ? -64.757 -42.868 26.257  1   30.75 ? 409 HOH C O   1 
HETATM 3879 O  O   . HOH L 7 .   ? -47.157 -49.726 40.849  1   29.82 ? 410 HOH C O   1 
HETATM 3880 O  O   . HOH L 7 .   ? -56.681 -30.17  19.377  1   51.85 ? 411 HOH C O   1 
HETATM 3881 O  O   . HOH L 7 .   ? -64.896 -61.434 41.479  1   27.95 ? 412 HOH C O   1 
HETATM 3882 O  O   . HOH L 7 .   ? -45.392 -52.206 23.253  1   26.51 ? 413 HOH C O   1 
HETATM 3883 O  O   . HOH L 7 .   ? -60.753 -55.348 18.497  1   42.04 ? 414 HOH C O   1 
HETATM 3884 O  O   . HOH L 7 .   ? -48.467 -60.107 38.054  1   46.77 ? 415 HOH C O   1 
HETATM 3885 O  O   . HOH L 7 .   ? -51.193 -36.947 18.034  1   38.24 ? 416 HOH C O   1 
HETATM 3886 O  O   . HOH L 7 .   ? -52.894 -45.43  44.868  1   37.03 ? 417 HOH C O   1 
HETATM 3887 O  O   . HOH L 7 .   ? -59.2   -35.661 11.159  1   47.59 ? 418 HOH C O   1 
HETATM 3888 O  O   . HOH L 7 .   ? -52.555 -44.45  22.95   1   18.83 ? 419 HOH C O   1 
HETATM 3889 O  O   . HOH L 7 .   ? -54.557 -36.585 28.741  1   25.5  ? 420 HOH C O   1 
HETATM 3890 O  O   . HOH L 7 .   ? -43.988 -30.497 21.016  1   38.48 ? 421 HOH C O   1 
HETATM 3891 O  O   . HOH L 7 .   ? -67.565 -48.033 17.853  1   50.58 ? 422 HOH C O   1 
HETATM 3892 O  O   . HOH L 7 .   ? -55.016 -46.601 12.829  1   25.1  ? 423 HOH C O   1 
HETATM 3893 O  O   . HOH L 7 .   ? -47.442 -50.434 23.763  1   21.28 ? 424 HOH C O   1 
HETATM 3894 O  O   . HOH L 7 .   ? -56.37  -52.864 41.461  1   25.7  ? 425 HOH C O   1 
HETATM 3895 O  O   . HOH L 7 .   ? -37.746 -51.25  26.663  1   38.43 ? 426 HOH C O   1 
HETATM 3896 O  O   . HOH L 7 .   ? -68.964 -60.311 36.244  1   41.83 ? 427 HOH C O   1 
HETATM 3897 O  O   . HOH L 7 .   ? -77.378 -48.323 33.48   1   47.4  ? 428 HOH C O   1 
HETATM 3898 O  O   . HOH L 7 .   ? -61.892 -62.689 33.482  1   46.68 ? 429 HOH C O   1 
HETATM 3899 O  O   . HOH L 7 .   ? -47.915 -56.654 36.695  1   28.45 ? 430 HOH C O   1 
HETATM 3900 O  O   . HOH L 7 .   ? -72.036 -51.139 31.22   1   37.25 ? 431 HOH C O   1 
HETATM 3901 O  O   . HOH L 7 .   ? -61.055 -44.604 23.478  1   19.78 ? 432 HOH C O   1 
HETATM 3902 O  O   . HOH L 7 .   ? -73.801 -57.016 33.51   1   48.73 ? 433 HOH C O   1 
HETATM 3903 O  O   . HOH L 7 .   ? -58.442 -57.533 41.12   1   24.59 ? 434 HOH C O   1 
HETATM 3904 O  O   . HOH L 7 .   ? -44.977 -47.614 16.315  1   18.78 ? 435 HOH C O   1 
HETATM 3905 O  O   . HOH L 7 .   ? -46.029 -53.846 16.816  1   36.27 ? 436 HOH C O   1 
HETATM 3906 O  O   . HOH L 7 .   ? -52.544 -56.812 18.225  1   48.28 ? 437 HOH C O   1 
HETATM 3907 O  O   . HOH L 7 .   ? -61.654 -48.775 13.368  1   35.88 ? 438 HOH C O   1 
HETATM 3908 O  O   . HOH L 7 .   ? -51.595 -44.216 20.314  1   23.01 ? 439 HOH C O   1 
HETATM 3909 O  O   . HOH L 7 .   ? -64.437 -61.797 46.428  1   42.19 ? 440 HOH C O   1 
HETATM 3910 O  O   . HOH L 7 .   ? -42.053 -52.128 25.325  1   38.77 ? 441 HOH C O   1 
HETATM 3911 O  O   . HOH L 7 .   ? -51.617 -52.317 22.446  1   28.47 ? 442 HOH C O   1 
HETATM 3912 O  O   . HOH L 7 .   ? -75.511 -50.251 33.903  1   42.9  ? 443 HOH C O   1 
HETATM 3913 O  O   . HOH L 7 .   ? -53.234 -53.657 43.939  1   42.13 ? 444 HOH C O   1 
HETATM 3914 O  O   . HOH L 7 .   ? -73.596 -55.545 31.091  1   41.43 ? 445 HOH C O   1 
HETATM 3915 O  O   . HOH L 7 .   ? -42.114 -39.493 29.263  1   39.49 ? 446 HOH C O   1 
HETATM 3916 O  O   . HOH L 7 .   ? -40.492 -54.283 21.637  1   43.55 ? 447 HOH C O   1 
HETATM 3917 O  O   . HOH L 7 .   ? -44.071 -41.712 22.731  1   24.86 ? 448 HOH C O   1 
HETATM 3918 O  O   . HOH L 7 .   ? -53.684 -43.964 18.314  1   29.05 ? 449 HOH C O   1 
HETATM 3919 O  O   . HOH L 7 .   ? -53.626 -34.951 30.847  1   39.25 ? 450 HOH C O   1 
HETATM 3920 O  O   . HOH L 7 .   ? -51.871 -50.555 14.508  1   25.98 ? 451 HOH C O   1 
HETATM 3921 O  O   . HOH L 7 .   ? -52.727 -50.81  20.74   1   38.91 ? 452 HOH C O   1 
HETATM 3922 O  O   . HOH L 7 .   ? -56.022 -57.438 23.143  1   38.49 ? 453 HOH C O   1 
HETATM 3923 O  O   . HOH L 7 .   ? -63.226 -35.66  40.845  1   47.23 ? 454 HOH C O   1 
HETATM 3924 O  O   . HOH L 7 .   ? -44.505 -47.439 19.084  1   21.18 ? 455 HOH C O   1 
HETATM 3925 O  O   . HOH L 7 .   ? -49.606 -33.181 32.11   1   44.64 ? 456 HOH C O   1 
HETATM 3926 O  O   . HOH L 7 .   ? -50.383 -34.503 18.417  1   33.16 ? 457 HOH C O   1 
HETATM 3927 O  O   . HOH L 7 .   ? -48.829 -36.865 39.25   1   34.14 ? 458 HOH C O   1 
HETATM 3928 O  O   . HOH L 7 .   ? -55.382 -45.729 44.325  1   39.29 ? 459 HOH C O   1 
HETATM 3929 O  O   . HOH L 7 .   ? -63.743 -44.222 23.132  1   27.2  ? 460 HOH C O   1 
HETATM 3930 O  O   . HOH L 7 .   ? -49.108 -35.85  22.19   1   29.8  ? 461 HOH C O   1 
HETATM 3931 O  O   . HOH L 7 .   ? -61.201 -42.897 43.747  1   36.48 ? 462 HOH C O   1 
HETATM 3932 O  O   . HOH L 7 .   ? -51.39  -63.18  41.276  1   38.97 ? 463 HOH C O   1 
HETATM 3933 O  O   . HOH L 7 .   ? -71.424 -53.169 28.281  1   39.48 ? 464 HOH C O   1 
HETATM 3934 O  O   . HOH L 7 .   ? -45.225 -54.783 22.249  1   44.54 ? 465 HOH C O   1 
HETATM 3935 O  O   . HOH L 7 .   ? -46.613 -34.617 30.698  1   48.17 ? 466 HOH C O   1 
HETATM 3936 O  O   . HOH L 7 .   ? -65.259 -31.663 18.961  1   39.12 ? 467 HOH C O   1 
HETATM 3937 O  O   . HOH L 7 .   ? -54.665 -44.265 25.623  1   24.03 ? 468 HOH C O   1 
HETATM 3938 O  O   . HOH L 7 .   ? -55.21  -43.386 10.93   1   38.13 ? 469 HOH C O   1 
HETATM 3939 O  O   . HOH L 7 .   ? -56.389 -59.931 16.518  1   44.41 ? 470 HOH C O   1 
HETATM 3940 O  O   . HOH L 7 .   ? -54.245 -62.49  32.387  1   32.56 ? 471 HOH C O   1 
HETATM 3941 O  O   . HOH L 7 .   ? -58.11  -30.773 26.876  1   36.29 ? 472 HOH C O   1 
HETATM 3942 O  O   . HOH L 7 .   ? -43.636 -50.085 37.819  1   30.16 ? 473 HOH C O   1 
HETATM 3943 O  O   . HOH L 7 .   ? -60.455 -36.604 33.933  1   33.54 ? 474 HOH C O   1 
HETATM 3944 O  O   . HOH L 7 .   ? -64.075 -46.095 15.934  1   35.27 ? 475 HOH C O   1 
HETATM 3945 O  O   . HOH L 7 .   ? -51.437 -61.458 32.036  1   35.9  ? 476 HOH C O   1 
HETATM 3946 O  O   . HOH L 7 .   ? -58.695 -29.6   22.268  1   42.85 ? 477 HOH C O   1 
HETATM 3947 O  O   . HOH L 7 .   ? -57.523 -31.157 14.681  1   44.75 ? 478 HOH C O   1 
HETATM 3948 O  O   . HOH L 7 .   ? -59.868 -38.362 11.515  1   28.65 ? 479 HOH C O   1 
HETATM 3949 O  O   . HOH L 7 .   ? -48.112 -61.862 30.663  1   41.99 ? 480 HOH C O   1 
HETATM 3950 O  O   . HOH L 7 .   ? -54.954 -62.852 38.779  1   34.2  ? 481 HOH C O   1 
HETATM 3951 O  O   . HOH L 7 .   ? -39.268 -46.648 29.593  1   43.33 ? 482 HOH C O   1 
HETATM 3952 O  O   . HOH L 7 .   ? -50.443 -59.884 27.326  1   47.64 ? 483 HOH C O   1 
HETATM 3953 O  O   . HOH L 7 .   ? -62.512 -57.989 19.326  1   46.1  ? 484 HOH C O   1 
HETATM 3954 O  O   . HOH L 7 .   ? -56.294 -28.939 16.956  1   41.34 ? 485 HOH C O   1 
HETATM 3955 O  O   . HOH L 7 .   ? -69.021 -61.021 31.389  1   49.1  ? 486 HOH C O   1 
HETATM 3956 O  O   . HOH L 7 .   ? -55.465 -58.186 14.343  1   48.02 ? 487 HOH C O   1 
HETATM 3957 O  O   . HOH L 7 .   ? -56.866 -32.96  34.966  1   35.42 ? 488 HOH C O   1 
HETATM 3958 O  O   . HOH L 7 .   ? -50.427 -63.142 33.561  1   53.48 ? 489 HOH C O   1 
HETATM 3959 O  O   . HOH L 7 .   ? -46.543 -57.097 39.047  1   50.4  ? 490 HOH C O   1 
HETATM 3960 O  O   . HOH L 7 .   ? -64.072 -48.583 14.837  1   44.8  ? 491 HOH C O   1 
HETATM 3961 O  O   . HOH L 7 .   ? -49.522 -33.428 22.202  1   45.1  ? 492 HOH C O   1 
HETATM 3962 O  O   . HOH L 7 .   ? -54.163 -63.761 35.082  1   48.78 ? 493 HOH C O   1 
HETATM 3963 O  O   . HOH L 7 .   ? -39.556 -52.947 23.438  1   35.92 ? 494 HOH C O   1 
HETATM 3964 O  O   . HOH L 7 .   ? -50.121 -61.623 29.63   1   42.03 ? 495 HOH C O   1 
HETATM 3965 O  O   . HOH L 7 .   ? -65.923 -44.515 24.597  1   37.66 ? 496 HOH C O   1 
HETATM 3966 O  O   . HOH L 7 .   ? -48.203 -42.767 20.941  1   31.11 ? 497 HOH C O   1 
HETATM 3967 O  O   . HOH L 7 .   ? -58.973 -58.651 47.885  1   39.58 ? 498 HOH C O   1 
HETATM 3968 O  O   . HOH L 7 .   ? -74.051 -53.103 31.036  1   42.02 ? 499 HOH C O   1 
HETATM 3969 O  O   . HOH L 7 .   ? -64.897 -63.989 41.033  1   46.33 ? 500 HOH C O   1 
HETATM 3970 O  O   . HOH L 7 .   ? -35.755 -51.902 25.187  1   32.55 ? 501 HOH C O   1 
HETATM 3971 O  O   . HOH L 7 .   ? -67.122 -41.321 27.353  1   44.73 ? 502 HOH C O   1 
HETATM 3972 O  O   . HOH L 7 .   ? -76.375 -52.201 32.422  1   56.96 ? 503 HOH C 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   . VAL A 1   ? 0.286  0.2651 0.229  0.0226  -0.0107 -0.0163 1   VAL A N   
2    C  CA  . VAL A 1   ? 0.2914 0.2693 0.2325 0.0163  -0.0149 -0.022  1   VAL A CA  
3    C  C   . VAL A 1   ? 0.308  0.2694 0.2446 0.0155  -0.0144 -0.0247 1   VAL A C   
4    O  O   . VAL A 1   ? 0.3079 0.2648 0.2389 0.0212  -0.0132 -0.0261 1   VAL A O   
5    C  CB  . VAL A 1   ? 0.2862 0.2747 0.2227 0.0178  -0.0184 -0.0265 1   VAL A CB  
6    C  CG1 . VAL A 1   ? 0.2837 0.2729 0.2205 0.0085  -0.0227 -0.0332 1   VAL A CG1 
7    C  CG2 . VAL A 1   ? 0.2849 0.2898 0.2238 0.0225  -0.0187 -0.0231 1   VAL A CG2 
8    N  N   . LEU A 2   ? 0.3078 0.2599 0.2459 0.0089  -0.015  -0.0252 2   LEU A N   
9    C  CA  . LEU A 2   ? 0.3281 0.2626 0.2605 0.0092  -0.0147 -0.0276 2   LEU A CA  
10   C  C   . LEU A 2   ? 0.3362 0.2647 0.2617 0.0059  -0.0176 -0.035  2   LEU A C   
11   O  O   . LEU A 2   ? 0.3368 0.271  0.2636 -0.0019 -0.0203 -0.0385 2   LEU A O   
12   C  CB  . LEU A 2   ? 0.3397 0.2639 0.2739 0.0039  -0.014  -0.0246 2   LEU A CB  
13   C  CG  . LEU A 2   ? 0.3785 0.3081 0.3188 0.0067  -0.0115 -0.0182 2   LEU A CG  
14   C  CD1 . LEU A 2   ? 0.3928 0.3129 0.3329 0.0014  -0.011  -0.0153 2   LEU A CD1 
15   C  CD2 . LEU A 2   ? 0.3888 0.3155 0.3282 0.0155  -0.0094 -0.0169 2   LEU A CD2 
16   N  N   . SER A 3   ? 0.354  0.2714 0.2724 0.0114  -0.0169 -0.0381 3   SER A N   
17   C  CA  . SER A 3   ? 0.3735 0.2815 0.2836 0.0085  -0.0195 -0.0463 3   SER A CA  
18   C  C   . SER A 3   ? 0.4072 0.2954 0.3145 0.0012  -0.0195 -0.0476 3   SER A C   
19   O  O   . SER A 3   ? 0.4097 0.2909 0.3196 0.0019  -0.0173 -0.0416 3   SER A O   
20   C  CB  . SER A 3   ? 0.4004 0.3024 0.3033 0.0181  -0.0179 -0.049  3   SER A CB  
21   O  OG  . SER A 3   ? 0.4086 0.2958 0.3099 0.0227  -0.0154 -0.0467 3   SER A OG  
22   N  N   . PRO A 4   ? 0.4259 0.3025 0.3262 -0.0051 -0.0216 -0.0554 4   PRO A N   
23   C  CA  . PRO A 4   ? 0.4309 0.2837 0.3259 -0.0113 -0.0205 -0.0562 4   PRO A CA  
24   C  C   . PRO A 4   ? 0.4324 0.2674 0.3217 -0.001  -0.0178 -0.0526 4   PRO A C   
25   O  O   . PRO A 4   ? 0.4485 0.271  0.3372 -0.0024 -0.016  -0.0472 4   PRO A O   
26   C  CB  . PRO A 4   ? 0.4539 0.2979 0.3413 -0.0182 -0.0231 -0.0669 4   PRO A CB  
27   C  CG  . PRO A 4   ? 0.4603 0.3303 0.3526 -0.0193 -0.0264 -0.0707 4   PRO A CG  
28   C  CD  . PRO A 4   ? 0.4293 0.3137 0.3255 -0.0071 -0.0249 -0.0641 4   PRO A CD  
29   N  N   . ALA A 5   ? 0.4241 0.2601 0.3095 0.0099  -0.0174 -0.055  5   ALA A N   
30   C  CA  . ALA A 5   ? 0.4361 0.26   0.3176 0.0211  -0.015  -0.0521 5   ALA A CA  
31   C  C   . ALA A 5   ? 0.4136 0.2482 0.3039 0.0251  -0.0132 -0.043  5   ALA A C   
32   O  O   . ALA A 5   ? 0.4248 0.247  0.3123 0.0302  -0.0119 -0.0395 5   ALA A O   
33   C  CB  . ALA A 5   ? 0.4448 0.2722 0.3217 0.0314  -0.0144 -0.0569 5   ALA A CB  
34   N  N   . ASP A 6   ? 0.3738 0.2305 0.2739 0.0231  -0.0131 -0.0395 6   ASP A N   
35   C  CA  . ASP A 6   ? 0.3519 0.2186 0.2603 0.0257  -0.0114 -0.032  6   ASP A CA  
36   C  C   . ASP A 6   ? 0.3717 0.2274 0.2795 0.0196  -0.0115 -0.0278 6   ASP A C   
37   O  O   . ASP A 6   ? 0.3725 0.2242 0.2807 0.0246  -0.0104 -0.023  6   ASP A O   
38   C  CB  . ASP A 6   ? 0.3383 0.2267 0.2555 0.0232  -0.0112 -0.0295 6   ASP A CB  
39   C  CG  . ASP A 6   ? 0.3835 0.2837 0.3015 0.0298  -0.0098 -0.0309 6   ASP A CG  
40   O  OD1 . ASP A 6   ? 0.3968 0.2938 0.3126 0.0375  -0.0079 -0.0318 6   ASP A OD1 
41   O  OD2 . ASP A 6   ? 0.4    0.3128 0.3201 0.0277  -0.0103 -0.031  6   ASP A OD2 
42   N  N   . LYS A 7   ? 0.3694 0.2213 0.2761 0.0088  -0.0128 -0.0298 7   LYS A N   
43   C  CA  . LYS A 7   ? 0.3743 0.2161 0.28   0.0013  -0.0119 -0.0256 7   LYS A CA  
44   C  C   . LYS A 7   ? 0.3938 0.2091 0.2884 0.0054  -0.0107 -0.0246 7   LYS A C   
45   O  O   . LYS A 7   ? 0.3893 0.1987 0.2827 0.0076  -0.0094 -0.0181 7   LYS A O   
46   C  CB  . LYS A 7   ? 0.3903 0.2348 0.2975 -0.0122 -0.013  -0.0294 7   LYS A CB  
47   C  CG  . LYS A 7   ? 0.4141 0.2857 0.332  -0.015  -0.0142 -0.0293 7   LYS A CG  
48   C  CD  . LYS A 7   ? 0.4601 0.3384 0.38   -0.027  -0.0161 -0.0349 7   LYS A CD  
49   C  CE  . LYS A 7   ? 0.5041 0.4086 0.4315 -0.0248 -0.0183 -0.0364 7   LYS A CE  
50   N  NZ  . LYS A 7   ? 0.5107 0.4276 0.4417 -0.0353 -0.0209 -0.0424 7   LYS A NZ  
51   N  N   . THR A 8   ? 0.4158 0.2149 0.3014 0.0075  -0.0113 -0.0309 8   THR A N   
52   C  CA  . THR A 8   ? 0.4529 0.2239 0.3261 0.0129  -0.01   -0.0301 8   THR A CA  
53   C  C   . THR A 8   ? 0.4278 0.2027 0.3017 0.028   -0.0095 -0.0258 8   THR A C   
54   O  O   . THR A 8   ? 0.4234 0.1833 0.2908 0.0329  -0.0085 -0.0205 8   THR A O   
55   C  CB  . THR A 8   ? 0.523  0.2738 0.3854 0.0111  -0.0105 -0.0389 8   THR A CB  
56   O  OG1 . THR A 8   ? 0.5597 0.3234 0.4241 0.0184  -0.0118 -0.0446 8   THR A OG1 
57   C  CG2 . THR A 8   ? 0.5335 0.2802 0.3954 -0.0053 -0.0109 -0.0435 8   THR A CG2 
58   N  N   . ASN A 9   ? 0.3911 0.188  0.2733 0.0349  -0.0101 -0.0275 9   ASN A N   
59   C  CA  . ASN A 9   ? 0.3747 0.181  0.2604 0.0476  -0.0095 -0.0243 9   ASN A CA  
60   C  C   . ASN A 9   ? 0.3669 0.1813 0.2582 0.047   -0.0092 -0.0166 9   ASN A C   
61   O  O   . ASN A 9   ? 0.367  0.1767 0.2552 0.0561  -0.0092 -0.013  9   ASN A O   
62   C  CB  . ASN A 9   ? 0.364  0.1935 0.2584 0.0515  -0.009  -0.0274 9   ASN A CB  
63   C  CG  . ASN A 9   ? 0.3995 0.223  0.2874 0.0575  -0.0087 -0.0345 9   ASN A CG  
64   O  OD1 . ASN A 9   ? 0.4002 0.2027 0.2774 0.0622  -0.0089 -0.0373 9   ASN A OD1 
65   N  ND2 . ASN A 9   ? 0.4079 0.2488 0.3009 0.0578  -0.0079 -0.0374 9   ASN A ND2 
66   N  N   . VAL A 10  ? 0.3528 0.1813 0.2522 0.0375  -0.0092 -0.0143 10  VAL A N   
67   C  CA  . VAL A 10  ? 0.3626 0.2004 0.2672 0.0365  -0.0089 -0.0078 10  VAL A CA  
68   C  C   . VAL A 10  ? 0.3868 0.2039 0.2816 0.0348  -0.0084 -0.003  10  VAL A C   
69   O  O   . VAL A 10  ? 0.3931 0.2103 0.2863 0.0412  -0.0084 0.002   10  VAL A O   
70   C  CB  . VAL A 10  ? 0.3616 0.2176 0.276  0.0271  -0.0087 -0.0074 10  VAL A CB  
71   C  CG1 . VAL A 10  ? 0.3766 0.2393 0.2947 0.0245  -0.008  -0.0013 10  VAL A CG1 
72   C  CG2 . VAL A 10  ? 0.3447 0.2198 0.2674 0.031   -0.0084 -0.0103 10  VAL A CG2 
73   N  N   . LYS A 11  ? 0.3967 0.1957 0.2841 0.026   -0.0077 -0.0046 11  LYS A N   
74   C  CA  . LYS A 11  ? 0.4216 0.1974 0.2978 0.0227  -0.0061 0.0003  11  LYS A CA  
75   C  C   . LYS A 11  ? 0.4319 0.1883 0.2964 0.0364  -0.0061 0.0022  11  LYS A C   
76   O  O   . LYS A 11  ? 0.4379 0.185  0.2956 0.0407  -0.0054 0.009   11  LYS A O   
77   C  CB  . LYS A 11  ? 0.4501 0.21   0.3212 0.0092  -0.0048 -0.0035 11  LYS A CB  
78   C  CG  . LYS A 11  ? 0.5053 0.285  0.3873 -0.0042 -0.0046 -0.0042 11  LYS A CG  
79   C  CD  . LYS A 11  ? 0.5755 0.3452 0.4548 -0.018  -0.0041 -0.0104 11  LYS A CD  
80   C  CE  . LYS A 11  ? 0.6004 0.3931 0.4915 -0.0302 -0.0042 -0.0112 11  LYS A CE  
81   N  NZ  . LYS A 11  ? 0.5899 0.3842 0.482  -0.0359 -0.0012 -0.0035 11  LYS A NZ  
82   N  N   . ALA A 12  ? 0.4298 0.1806 0.2913 0.0442  -0.0071 -0.0038 12  ALA A N   
83   C  CA  . ALA A 12  ? 0.4438 0.1776 0.2943 0.0592  -0.0072 -0.0027 12  ALA A CA  
84   C  C   . ALA A 12  ? 0.4427 0.1964 0.2995 0.0714  -0.0087 0.0015  12  ALA A C   
85   O  O   . ALA A 12  ? 0.4557 0.1975 0.3034 0.0801  -0.0089 0.0071  12  ALA A O   
86   C  CB  . ALA A 12  ? 0.4354 0.163  0.2827 0.0651  -0.0077 -0.011  12  ALA A CB  
87   N  N   . ALA A 13  ? 0.4171 0.2012 0.2892 0.0716  -0.0097 -0.0011 13  ALA A N   
88   C  CA  . ALA A 13  ? 0.4167 0.2221 0.2965 0.0813  -0.011  0.0011  13  ALA A CA  
89   C  C   . ALA A 13  ? 0.4295 0.2388 0.3093 0.0784  -0.0114 0.0083  13  ALA A C   
90   O  O   . ALA A 13  ? 0.4272 0.2362 0.3023 0.089   -0.0128 0.0121  13  ALA A O   
91   C  CB  . ALA A 13  ? 0.4028 0.236  0.2976 0.0795  -0.0109 -0.0035 13  ALA A CB  
92   N  N   . TRP A 14  ? 0.4303 0.2434 0.3143 0.0647  -0.0102 0.0101  14  TRP A N   
93   C  CA  . TRP A 14  ? 0.4447 0.2613 0.3279 0.0615  -0.01   0.0166  14  TRP A CA  
94   C  C   . TRP A 14  ? 0.4856 0.2751 0.3521 0.0642  -0.009  0.0229  14  TRP A C   
95   O  O   . TRP A 14  ? 0.4899 0.282  0.3524 0.069   -0.0095 0.0288  14  TRP A O   
96   C  CB  . TRP A 14  ? 0.433  0.2613 0.3249 0.0473  -0.0086 0.0166  14  TRP A CB  
97   C  CG  . TRP A 14  ? 0.4273 0.2672 0.3214 0.0461  -0.0085 0.0218  14  TRP A CG  
98   C  CD1 . TRP A 14  ? 0.4404 0.2703 0.3273 0.0399  -0.0066 0.0277  14  TRP A CD1 
99   C  CD2 . TRP A 14  ? 0.4115 0.2746 0.3147 0.0516  -0.0101 0.0212  14  TRP A CD2 
100  N  NE1 . TRP A 14  ? 0.433  0.2792 0.3236 0.0419  -0.0071 0.0308  14  TRP A NE1 
101  C  CE2 . TRP A 14  ? 0.415  0.2812 0.3156 0.049   -0.0095 0.0265  14  TRP A CE2 
102  C  CE3 . TRP A 14  ? 0.4071 0.2889 0.3205 0.0576  -0.0114 0.0162  14  TRP A CE3 
103  C  CZ2 . TRP A 14  ? 0.4166 0.3033 0.3237 0.0529  -0.011  0.0264  14  TRP A CZ2 
104  C  CZ3 . TRP A 14  ? 0.4084 0.3102 0.3292 0.0601  -0.0125 0.0162  14  TRP A CZ3 
105  C  CH2 . TRP A 14  ? 0.4111 0.3149 0.3283 0.0582  -0.0126 0.0209  14  TRP A CH2 
106  N  N   . GLY A 15  ? 0.5142 0.2771 0.3697 0.0623  -0.0075 0.0216  15  GLY A N   
107  C  CA  . GLY A 15  ? 0.5606 0.2923 0.3978 0.0656  -0.0057 0.0277  15  GLY A CA  
108  C  C   . GLY A 15  ? 0.6026 0.3301 0.4313 0.0846  -0.0078 0.0309  15  GLY A C   
109  O  O   . GLY A 15  ? 0.6177 0.326  0.4317 0.09    -0.0068 0.0384  15  GLY A O   
110  N  N   . LYS A 16  ? 0.6067 0.3528 0.4442 0.0953  -0.0106 0.0254  16  LYS A N   
111  C  CA  . LYS A 16  ? 0.6259 0.3747 0.4583 0.1143  -0.0132 0.0272  16  LYS A CA  
112  C  C   . LYS A 16  ? 0.6346 0.4078 0.4728 0.1191  -0.0157 0.0314  16  LYS A C   
113  O  O   . LYS A 16  ? 0.639  0.4147 0.4713 0.1349  -0.0183 0.0338  16  LYS A O   
114  C  CB  . LYS A 16  ? 0.6518 0.4139 0.4924 0.1232  -0.0147 0.019   16  LYS A CB  
115  C  CG  . LYS A 16  ? 0.7481 0.4835 0.5792 0.1225  -0.0127 0.0147  16  LYS A CG  
116  C  CD  . LYS A 16  ? 0.8406 0.5422 0.6506 0.1348  -0.0121 0.0193  16  LYS A CD  
117  C  CE  . LYS A 16  ? 0.9293 0.6011 0.7288 0.1319  -0.0097 0.0142  16  LYS A CE  
118  N  NZ  . LYS A 16  ? 1.0009 0.6312 0.778  0.1346  -0.0072 0.0203  16  LYS A NZ  
119  N  N   . VAL A 17  ? 0.6273 0.4193 0.4769 0.1064  -0.0152 0.0316  17  VAL A N   
120  C  CA  . VAL A 17  ? 0.6266 0.4414 0.4817 0.1089  -0.0173 0.0344  17  VAL A CA  
121  C  C   . VAL A 17  ? 0.6555 0.4518 0.4932 0.1133  -0.0168 0.0439  17  VAL A C   
122  O  O   . VAL A 17  ? 0.6623 0.4682 0.4961 0.1263  -0.0199 0.0467  17  VAL A O   
123  C  CB  . VAL A 17  ? 0.6138 0.4502 0.4844 0.0942  -0.0162 0.0316  17  VAL A CB  
124  C  CG1 . VAL A 17  ? 0.61   0.4649 0.4834 0.0952  -0.0177 0.0347  17  VAL A CG1 
125  C  CG2 . VAL A 17  ? 0.6025 0.4591 0.489  0.0926  -0.0166 0.0232  17  VAL A CG2 
126  N  N   . GLY A 18  ? 0.6714 0.4427 0.499  0.1022  -0.0128 0.0486  18  GLY A N   
127  C  CA  . GLY A 18  ? 0.692  0.44   0.5008 0.1037  -0.0105 0.0585  18  GLY A CA  
128  C  C   . GLY A 18  ? 0.6906 0.4555 0.4977 0.1082  -0.0122 0.0639  18  GLY A C   
129  O  O   . GLY A 18  ? 0.6911 0.478  0.5101 0.0984  -0.012  0.0623  18  GLY A O   
130  N  N   . ALA A 19  ? 0.6913 0.4458 0.4826 0.1241  -0.014  0.0703  19  ALA A N   
131  C  CA  . ALA A 19  ? 0.6866 0.4567 0.4734 0.1306  -0.0163 0.0756  19  ALA A CA  
132  C  C   . ALA A 19  ? 0.66   0.4718 0.4664 0.1339  -0.0215 0.0678  19  ALA A C   
133  O  O   . ALA A 19  ? 0.6697 0.499  0.4763 0.1349  -0.0231 0.0699  19  ALA A O   
134  C  CB  . ALA A 19  ? 0.7043 0.4547 0.4692 0.1494  -0.0178 0.0837  19  ALA A CB  
135  N  N   . HIS A 20  ? 0.6288 0.4557 0.4506 0.1356  -0.0237 0.0588  20  HIS A N   
136  C  CA  . HIS A 20  ? 0.6045 0.4689 0.4449 0.1373  -0.0276 0.0508  20  HIS A CA  
137  C  C   . HIS A 20  ? 0.582  0.463  0.4391 0.1201  -0.0254 0.0457  20  HIS A C   
138  O  O   . HIS A 20  ? 0.554  0.463  0.427  0.1193  -0.0276 0.0384  20  HIS A O   
139  C  CB  . HIS A 20  ? 0.6141 0.4887 0.4626 0.1482  -0.0304 0.0439  20  HIS A CB  
140  C  CG  . HIS A 20  ? 0.6695 0.5293 0.5017 0.1673  -0.0329 0.0485  20  HIS A CG  
141  N  ND1 . HIS A 20  ? 0.6998 0.5723 0.5249 0.1814  -0.0373 0.0519  20  HIS A ND1 
142  C  CD2 . HIS A 20  ? 0.7029 0.5352 0.5235 0.1749  -0.0313 0.0502  20  HIS A CD2 
143  C  CE1 . HIS A 20  ? 0.7203 0.5734 0.5299 0.198   -0.0384 0.0561  20  HIS A CE1 
144  N  NE2 . HIS A 20  ? 0.7273 0.5547 0.5335 0.1947  -0.0347 0.0551  20  HIS A NE2 
145  N  N   . ALA A 21  ? 0.5896 0.4538 0.4428 0.1065  -0.0209 0.0494  21  ALA A N   
146  C  CA  . ALA A 21  ? 0.5858 0.4634 0.4532 0.0912  -0.0185 0.0452  21  ALA A CA  
147  C  C   . ALA A 21  ? 0.5592 0.4657 0.4365 0.0906  -0.0207 0.042   21  ALA A C   
148  O  O   . ALA A 21  ? 0.557  0.483  0.4499 0.0876  -0.0215 0.0344  21  ALA A O   
149  C  CB  . ALA A 21  ? 0.6018 0.4594 0.462  0.0784  -0.0136 0.0504  21  ALA A CB  
150  N  N   . GLY A 22  ? 0.5431 0.4511 0.4103 0.0946  -0.0215 0.0474  22  GLY A N   
151  C  CA  . GLY A 22  ? 0.5146 0.4482 0.3885 0.0945  -0.0237 0.0442  22  GLY A CA  
152  C  C   . GLY A 22  ? 0.4763 0.4341 0.3614 0.1029  -0.0285 0.0363  22  GLY A C   
153  O  O   . GLY A 22  ? 0.4517 0.4313 0.3506 0.0973  -0.029  0.0292  22  GLY A O   
154  N  N   . GLU A 23  ? 0.4548 0.4086 0.334  0.1163  -0.0316 0.0373  23  GLU A N   
155  C  CA  . GLU A 23  ? 0.4339 0.4125 0.3241 0.1252  -0.0361 0.0297  23  GLU A CA  
156  C  C   . GLU A 23  ? 0.4007 0.3903 0.3096 0.1162  -0.034  0.021   23  GLU A C   
157  O  O   . GLU A 23  ? 0.3803 0.3953 0.3033 0.1132  -0.0353 0.0133  23  GLU A O   
158  C  CB  . GLU A 23  ? 0.4793 0.4482 0.3585 0.142   -0.0391 0.033   23  GLU A CB  
159  C  CG  . GLU A 23  ? 0.5743 0.5722 0.4654 0.1522  -0.0439 0.0249  23  GLU A CG  
160  C  CD  . GLU A 23  ? 0.699  0.6887 0.5811 0.1697  -0.0465 0.0272  23  GLU A CD  
161  O  OE1 . GLU A 23  ? 0.7517 0.715  0.6137 0.1779  -0.0462 0.0365  23  GLU A OE1 
162  O  OE2 . GLU A 23  ? 0.7027 0.7117 0.5974 0.1753  -0.0483 0.0197  23  GLU A OE2 
163  N  N   . TYR A 24  ? 0.3889 0.3587 0.2971 0.111   -0.0304 0.0224  24  TYR A N   
164  C  CA  . TYR A 24  ? 0.3836 0.3615 0.3069 0.1031  -0.028  0.0154  24  TYR A CA  
165  C  C   . TYR A 24  ? 0.3539 0.3414 0.2869 0.0896  -0.0254 0.0125  24  TYR A C   
166  O  O   . TYR A 24  ? 0.3334 0.3389 0.2802 0.0855  -0.0247 0.0055  24  TYR A O   
167  C  CB  . TYR A 24  ? 0.4214 0.3761 0.3399 0.1019  -0.0253 0.0171  24  TYR A CB  
168  C  CG  . TYR A 24  ? 0.4676 0.4114 0.3771 0.1159  -0.0273 0.0186  24  TYR A CG  
169  C  CD1 . TYR A 24  ? 0.4888 0.4473 0.397  0.1299  -0.0316 0.0178  24  TYR A CD1 
170  C  CD2 . TYR A 24  ? 0.5047 0.425  0.4074 0.1158  -0.0251 0.0198  24  TYR A CD2 
171  C  CE1 . TYR A 24  ? 0.5111 0.4593 0.4102 0.1446  -0.0335 0.0193  24  TYR A CE1 
172  C  CE2 . TYR A 24  ? 0.5275 0.4352 0.4204 0.1295  -0.0266 0.0209  24  TYR A CE2 
173  C  CZ  . TYR A 24  ? 0.5391 0.4611 0.4305 0.1445  -0.0307 0.0207  24  TYR A CZ  
174  O  OH  . TYR A 24  ? 0.5887 0.4986 0.4704 0.1596  -0.0321 0.0216  24  TYR A OH  
175  N  N   . GLY A 25  ? 0.3542 0.3304 0.2799 0.0829  -0.0235 0.0178  25  GLY A N   
176  C  CA  . GLY A 25  ? 0.3495 0.3348 0.2833 0.0718  -0.021  0.0152  25  GLY A CA  
177  C  C   . GLY A 25  ? 0.3285 0.3375 0.2693 0.0732  -0.0234 0.0098  25  GLY A C   
178  O  O   . GLY A 25  ? 0.3143 0.3353 0.2667 0.0663  -0.0216 0.0037  25  GLY A O   
179  N  N   . ALA A 26  ? 0.3297 0.3451 0.2628 0.0824  -0.0273 0.0117  26  ALA A N   
180  C  CA  . ALA A 26  ? 0.3206 0.3604 0.2596 0.0842  -0.0304 0.0056  26  ALA A CA  
181  C  C   . ALA A 26  ? 0.3021 0.3607 0.2559 0.0851  -0.0315 -0.0034 26  ALA A C   
182  O  O   . ALA A 26  ? 0.3004 0.3756 0.2652 0.0784  -0.0308 -0.0109 26  ALA A O   
183  C  CB  . ALA A 26  ? 0.3271 0.3702 0.2531 0.0957  -0.035  0.0099  26  ALA A CB  
184  N  N   . GLU A 27  ? 0.2969 0.3524 0.2509 0.0927  -0.0326 -0.003  27  GLU A N   
185  C  CA  . GLU A 27  ? 0.284  0.3584 0.2523 0.0935  -0.0329 -0.0113 27  GLU A CA  
186  C  C   . GLU A 27  ? 0.2782 0.3508 0.2578 0.0806  -0.0273 -0.0153 27  GLU A C   
187  O  O   . GLU A 27  ? 0.2742 0.365  0.2663 0.0752  -0.0262 -0.0231 27  GLU A O   
188  C  CB  . GLU A 27  ? 0.3213 0.3912 0.2863 0.1052  -0.0346 -0.0095 27  GLU A CB  
189  C  CG  . GLU A 27  ? 0.3519 0.4427 0.3324 0.1055  -0.0339 -0.0181 27  GLU A CG  
190  C  CD  . GLU A 27  ? 0.416  0.5091 0.3943 0.1195  -0.0363 -0.0179 27  GLU A CD  
191  O  OE1 . GLU A 27  ? 0.4389 0.5288 0.4056 0.1325  -0.0409 -0.0134 27  GLU A OE1 
192  O  OE2 . GLU A 27  ? 0.4243 0.5217 0.4115 0.1182  -0.0333 -0.0221 27  GLU A OE2 
193  N  N   . ALA A 28  ? 0.2753 0.3259 0.2498 0.0753  -0.0237 -0.0102 28  ALA A N   
194  C  CA  . ALA A 28  ? 0.2717 0.3197 0.2548 0.0648  -0.0186 -0.0131 28  ALA A CA  
195  C  C   . ALA A 28  ? 0.2495 0.3069 0.2382 0.0562  -0.017  -0.017  28  ALA A C   
196  O  O   . ALA A 28  ? 0.2335 0.2986 0.2322 0.0497  -0.0137 -0.0227 28  ALA A O   
197  C  CB  . ALA A 28  ? 0.2859 0.3111 0.2614 0.0614  -0.0162 -0.007  28  ALA A CB  
198  N  N   . LEU A 29  ? 0.251  0.3068 0.2323 0.0564  -0.0188 -0.0141 29  LEU A N   
199  C  CA  . LEU A 29  ? 0.2504 0.3144 0.2355 0.0493  -0.0174 -0.0184 29  LEU A CA  
200  C  C   . LEU A 29  ? 0.2501 0.3367 0.2449 0.0493  -0.0193 -0.0274 29  LEU A C   
201  O  O   . LEU A 29  ? 0.248  0.3404 0.2511 0.0412  -0.016  -0.0337 29  LEU A O   
202  C  CB  . LEU A 29  ? 0.2493 0.3094 0.2232 0.0515  -0.0194 -0.0134 29  LEU A CB  
203  C  CG  . LEU A 29  ? 0.2798 0.321  0.2462 0.048   -0.0165 -0.006  29  LEU A CG  
204  C  CD1 . LEU A 29  ? 0.3028 0.3423 0.2582 0.0503  -0.0179 -0.0012 29  LEU A CD1 
205  C  CD2 . LEU A 29  ? 0.2695 0.3081 0.2427 0.0391  -0.0118 -0.0088 29  LEU A CD2 
206  N  N   . GLU A 30  ? 0.2478 0.3471 0.2411 0.0585  -0.0244 -0.0283 30  GLU A N   
207  C  CA  . GLU A 30  ? 0.2544 0.3792 0.2577 0.059   -0.027  -0.0377 30  GLU A CA  
208  C  C   . GLU A 30  ? 0.2375 0.3692 0.2548 0.0524  -0.0227 -0.044  30  GLU A C   
209  O  O   . GLU A 30  ? 0.2354 0.3812 0.2629 0.0443  -0.0208 -0.0528 30  GLU A O   
210  C  CB  . GLU A 30  ? 0.3152 0.4521 0.3137 0.0725  -0.0335 -0.0364 30  GLU A CB  
211  C  CG  . GLU A 30  ? 0.4312 0.5987 0.4419 0.074   -0.0368 -0.0467 30  GLU A CG  
212  C  CD  . GLU A 30  ? 0.5639 0.7459 0.5704 0.0893  -0.0436 -0.0457 30  GLU A CD  
213  O  OE1 . GLU A 30  ? 0.6002 0.8111 0.6157 0.0912  -0.0476 -0.0546 30  GLU A OE1 
214  O  OE2 . GLU A 30  ? 0.6027 0.7674 0.5968 0.0995  -0.045  -0.0365 30  GLU A OE2 
215  N  N   . ARG A 31  ? 0.2212 0.3422 0.238  0.0555  -0.0207 -0.0398 31  ARG A N   
216  C  CA  . ARG A 31  ? 0.2142 0.3397 0.2422 0.0499  -0.0158 -0.0444 31  ARG A CA  
217  C  C   . ARG A 31  ? 0.2286 0.3441 0.2598 0.0375  -0.0096 -0.046  31  ARG A C   
218  O  O   . ARG A 31  ? 0.2275 0.3531 0.2689 0.0297  -0.0056 -0.0529 31  ARG A O   
219  C  CB  . ARG A 31  ? 0.2171 0.3301 0.2412 0.0562  -0.0148 -0.039  31  ARG A CB  
220  C  CG  . ARG A 31  ? 0.2312 0.3556 0.254  0.0695  -0.02   -0.039  31  ARG A CG  
221  C  CD  . ARG A 31  ? 0.2572 0.3655 0.2742 0.0759  -0.0188 -0.034  31  ARG A CD  
222  N  NE  . ARG A 31  ? 0.2798 0.397  0.2942 0.09    -0.0234 -0.034  31  ARG A NE  
223  C  CZ  . ARG A 31  ? 0.2776 0.4186 0.303  0.0945  -0.0239 -0.0406 31  ARG A CZ  
224  N  NH1 . ARG A 31  ? 0.2219 0.3787 0.2616 0.0844  -0.0192 -0.0477 31  ARG A NH1 
225  N  NH2 . ARG A 31  ? 0.2719 0.4211 0.2938 0.1093  -0.0287 -0.0402 31  ARG A NH2 
226  N  N   . MET A 32  ? 0.2203 0.3161 0.2421 0.0358  -0.0084 -0.0396 32  MET A N   
227  C  CA  . MET A 32  ? 0.2176 0.3032 0.2407 0.0264  -0.0029 -0.0405 32  MET A CA  
228  C  C   . MET A 32  ? 0.2209 0.3176 0.2491 0.0197  -0.0022 -0.0482 32  MET A C   
229  O  O   . MET A 32  ? 0.2357 0.3317 0.2703 0.0114  0.0032  -0.053  32  MET A O   
230  C  CB  . MET A 32  ? 0.2155 0.282  0.2283 0.0271  -0.0026 -0.0326 32  MET A CB  
231  C  CG  . MET A 32  ? 0.2454 0.3019 0.2589 0.0197  0.0028  -0.0331 32  MET A CG  
232  S  SD  . MET A 32  ? 0.2918 0.3318 0.2952 0.0206  0.0028  -0.0252 32  MET A SD  
233  C  CE  . MET A 32  ? 0.2504 0.2986 0.2491 0.0225  -0.0012 -0.0262 32  MET A CE  
234  N  N   . PHE A 33  ? 0.2165 0.321  0.2404 0.0229  -0.007  -0.0493 33  PHE A N   
235  C  CA  . PHE A 33  ? 0.2167 0.3319 0.2442 0.0169  -0.007  -0.0576 33  PHE A CA  
236  C  C   . PHE A 33  ? 0.2235 0.3591 0.264  0.012   -0.0063 -0.0678 33  PHE A C   
237  O  O   . PHE A 33  ? 0.217  0.3561 0.2629 0.0027  -0.0029 -0.0758 33  PHE A O   
238  C  CB  . PHE A 33  ? 0.2069 0.33   0.2263 0.0236  -0.0133 -0.0566 33  PHE A CB  
239  C  CG  . PHE A 33  ? 0.2163 0.3218 0.2238 0.0261  -0.0129 -0.0479 33  PHE A CG  
240  C  CD1 . PHE A 33  ? 0.2278 0.3173 0.234  0.0202  -0.0074 -0.046  33  PHE A CD1 
241  C  CD2 . PHE A 33  ? 0.2303 0.3363 0.2275 0.0344  -0.0177 -0.0418 33  PHE A CD2 
242  C  CE1 . PHE A 33  ? 0.2464 0.3236 0.2432 0.0221  -0.007  -0.0388 33  PHE A CE1 
243  C  CE2 . PHE A 33  ? 0.2461 0.3373 0.233  0.0353  -0.0165 -0.0342 33  PHE A CE2 
244  C  CZ  . PHE A 33  ? 0.2485 0.3273 0.2362 0.0288  -0.0113 -0.0333 33  PHE A CZ  
245  N  N   . LEU A 34  ? 0.228  0.377  0.2731 0.0182  -0.0093 -0.068  34  LEU A N   
246  C  CA  . LEU A 34  ? 0.2418 0.4148 0.3006 0.0139  -0.009  -0.0781 34  LEU A CA  
247  C  C   . LEU A 34  ? 0.2371 0.4031 0.3038 0.0049  -0.0007 -0.0795 34  LEU A C   
248  O  O   . LEU A 34  ? 0.245  0.4197 0.3209 -0.0058 0.0035  -0.0882 34  LEU A O   
249  C  CB  . LEU A 34  ? 0.263  0.4552 0.3232 0.026   -0.0158 -0.0776 34  LEU A CB  
250  C  CG  . LEU A 34  ? 0.3121 0.5367 0.3853 0.0247  -0.0186 -0.0887 34  LEU A CG  
251  C  CD1 . LEU A 34  ? 0.3245 0.5618 0.3983 0.0195  -0.0218 -0.097  34  LEU A CD1 
252  C  CD2 . LEU A 34  ? 0.3326 0.5735 0.4049 0.0398  -0.0255 -0.0864 34  LEU A CD2 
253  N  N   . SER A 35  ? 0.2417 0.3915 0.3039 0.0086  0.002   -0.0713 35  SER A N   
254  C  CA  . SER A 35  ? 0.2387 0.3811 0.306  0.0017  0.01    -0.0714 35  SER A CA  
255  C  C   . SER A 35  ? 0.2451 0.3675 0.309  -0.008  0.0168  -0.0708 35  SER A C   
256  O  O   . SER A 35  ? 0.2499 0.371  0.3198 -0.0171 0.0241  -0.0745 35  SER A O   
257  C  CB  . SER A 35  ? 0.255  0.3856 0.3165 0.0098  0.0101  -0.0629 35  SER A CB  
258  O  OG  . SER A 35  ? 0.2672 0.4154 0.3324 0.0191  0.0052  -0.0641 35  SER A OG  
259  N  N   . PHE A 36  ? 0.2418 0.348  0.2954 -0.0056 0.0151  -0.0656 36  PHE A N   
260  C  CA  . PHE A 36  ? 0.233  0.3185 0.2814 -0.0119 0.0211  -0.0638 36  PHE A CA  
261  C  C   . PHE A 36  ? 0.2391 0.3248 0.2837 -0.0132 0.0183  -0.0673 36  PHE A C   
262  O  O   . PHE A 36  ? 0.2283 0.3035 0.2639 -0.0079 0.0158  -0.0614 36  PHE A O   
263  C  CB  . PHE A 36  ? 0.2298 0.2965 0.2688 -0.0057 0.0215  -0.0534 36  PHE A CB  
264  C  CG  . PHE A 36  ? 0.2276 0.2953 0.2686 -0.0025 0.0229  -0.0501 36  PHE A CG  
265  C  CD1 . PHE A 36  ? 0.2344 0.3005 0.2802 -0.0087 0.0301  -0.0521 36  PHE A CD1 
266  C  CD2 . PHE A 36  ? 0.2284 0.2982 0.2659 0.0067  0.0174  -0.0453 36  PHE A CD2 
267  C  CE1 . PHE A 36  ? 0.2432 0.3118 0.2904 -0.0053 0.0316  -0.0496 36  PHE A CE1 
268  C  CE2 . PHE A 36  ? 0.2342 0.3049 0.273  0.0102  0.0187  -0.0433 36  PHE A CE2 
269  C  CZ  . PHE A 36  ? 0.232  0.3028 0.2757 0.0044  0.0256  -0.0454 36  PHE A CZ  
270  N  N   . PRO A 37  ? 0.246  0.3448 0.2976 -0.0205 0.0189  -0.0776 37  PRO A N   
271  C  CA  . PRO A 37  ? 0.2506 0.3524 0.2982 -0.021  0.0155  -0.0822 37  PRO A CA  
272  C  C   . PRO A 37  ? 0.2598 0.3394 0.2977 -0.0217 0.019   -0.0786 37  PRO A C   
273  O  O   . PRO A 37  ? 0.2523 0.334  0.2845 -0.0186 0.0152  -0.0796 37  PRO A O   
274  C  CB  . PRO A 37  ? 0.254  0.3718 0.3119 -0.0313 0.0172  -0.0952 37  PRO A CB  
275  C  CG  . PRO A 37  ? 0.2547 0.3855 0.3232 -0.0337 0.0191  -0.097  37  PRO A CG  
276  C  CD  . PRO A 37  ? 0.2405 0.3545 0.3044 -0.0288 0.0224  -0.0862 37  PRO A CD  
277  N  N   . THR A 38  ? 0.2642 0.3237 0.2995 -0.0246 0.026   -0.0744 38  THR A N   
278  C  CA  . THR A 38  ? 0.2874 0.3271 0.3133 -0.0232 0.0291  -0.0707 38  THR A CA  
279  C  C   . THR A 38  ? 0.264  0.3026 0.2823 -0.0136 0.0237  -0.0624 38  THR A C   
280  O  O   . THR A 38  ? 0.273  0.3042 0.2848 -0.0116 0.0241  -0.0616 38  THR A O   
281  C  CB  . THR A 38  ? 0.3393 0.3584 0.3625 -0.0258 0.0371  -0.0664 38  THR A CB  
282  O  OG1 . THR A 38  ? 0.3831 0.4042 0.4081 -0.022  0.0364  -0.0597 38  THR A OG1 
283  C  CG2 . THR A 38  ? 0.3448 0.3596 0.3729 -0.0368 0.0442  -0.0745 38  THR A CG2 
284  N  N   . THR A 39  ? 0.2318 0.2774 0.2509 -0.0078 0.0193  -0.0564 39  THR A N   
285  C  CA  . THR A 39  ? 0.2224 0.2661 0.2344 -0.0002 0.0149  -0.0486 39  THR A CA  
286  C  C   . THR A 39  ? 0.2315 0.2854 0.2398 0.0021  0.0102  -0.0513 39  THR A C   
287  O  O   . THR A 39  ? 0.2463 0.2956 0.2476 0.006   0.0089  -0.046  39  THR A O   
288  C  CB  . THR A 39  ? 0.2233 0.2708 0.2362 0.0047  0.0115  -0.0431 39  THR A CB  
289  O  OG1 . THR A 39  ? 0.2254 0.2905 0.2438 0.0056  0.0075  -0.0483 39  THR A OG1 
290  C  CG2 . THR A 39  ? 0.2185 0.2561 0.2334 0.0034  0.016   -0.0399 39  THR A CG2 
291  N  N   . LYS A 40  ? 0.2163 0.2848 0.2293 -0.0008 0.0081  -0.0598 40  LYS A N   
292  C  CA  . LYS A 40  ? 0.2175 0.297  0.226  0.0016  0.0036  -0.0633 40  LYS A CA  
293  C  C   . LYS A 40  ? 0.2403 0.3097 0.2425 0       0.0068  -0.0647 40  LYS A C   
294  O  O   . LYS A 40  ? 0.2528 0.3278 0.2484 0.0037  0.0037  -0.0643 40  LYS A O   
295  C  CB  . LYS A 40  ? 0.2282 0.3271 0.2438 -0.0021 0.0008  -0.0742 40  LYS A CB  
296  C  CG  . LYS A 40  ? 0.2512 0.3652 0.2726 0.002   -0.0036 -0.0734 40  LYS A CG  
297  C  CD  . LYS A 40  ? 0.3365 0.4746 0.3649 -0.0003 -0.0077 -0.0845 40  LYS A CD  
298  C  CE  . LYS A 40  ? 0.408  0.5475 0.4458 -0.0125 -0.0022 -0.0954 40  LYS A CE  
299  N  NZ  . LYS A 40  ? 0.423  0.5899 0.4708 -0.0158 -0.0061 -0.1068 40  LYS A NZ  
300  N  N   . THR A 41  ? 0.247  0.3014 0.2503 -0.0046 0.0132  -0.066  41  THR A N   
301  C  CA  . THR A 41  ? 0.2663 0.3105 0.2635 -0.0049 0.0167  -0.068  41  THR A CA  
302  C  C   . THR A 41  ? 0.2637 0.3027 0.2535 0.0019  0.0159  -0.0586 41  THR A C   
303  O  O   . THR A 41  ? 0.2698 0.3051 0.2541 0.0035  0.0177  -0.06   41  THR A O   
304  C  CB  . THR A 41  ? 0.2987 0.3265 0.2975 -0.0108 0.0241  -0.0719 41  THR A CB  
305  O  OG1 . THR A 41  ? 0.3201 0.3359 0.3186 -0.0083 0.027   -0.0632 41  THR A OG1 
306  C  CG2 . THR A 41  ? 0.3073 0.341  0.3141 -0.0197 0.0256  -0.0818 41  THR A CG2 
307  N  N   . TYR A 42  ? 0.234  0.2734 0.2238 0.0057  0.0135  -0.0498 42  TYR A N   
308  C  CA  . TYR A 42  ? 0.2411 0.2784 0.2248 0.0106  0.0127  -0.0417 42  TYR A CA  
309  C  C   . TYR A 42  ? 0.2408 0.2899 0.219  0.0137  0.0081  -0.0408 42  TYR A C   
310  O  O   . TYR A 42  ? 0.2359 0.2846 0.2082 0.0165  0.0083  -0.0355 42  TYR A O   
311  C  CB  . TYR A 42  ? 0.2301 0.2618 0.215  0.0123  0.0122  -0.0334 42  TYR A CB  
312  C  CG  . TYR A 42  ? 0.2407 0.2602 0.2277 0.0112  0.017   -0.0323 42  TYR A CG  
313  C  CD1 . TYR A 42  ? 0.2528 0.2662 0.2363 0.0136  0.0197  -0.0291 42  TYR A CD1 
314  C  CD2 . TYR A 42  ? 0.2487 0.2639 0.2406 0.0079  0.0193  -0.0352 42  TYR A CD2 
315  C  CE1 . TYR A 42  ? 0.2612 0.2636 0.245  0.0142  0.0238  -0.0276 42  TYR A CE1 
316  C  CE2 . TYR A 42  ? 0.2684 0.271  0.26   0.0075  0.0242  -0.0336 42  TYR A CE2 
317  C  CZ  . TYR A 42  ? 0.2811 0.2769 0.2682 0.0113  0.0262  -0.0297 42  TYR A CZ  
318  O  OH  . TYR A 42  ? 0.3198 0.3037 0.3053 0.0125  0.0304  -0.0273 42  TYR A OH  
319  N  N   . PHE A 43  ? 0.2252 0.2861 0.2048 0.0134  0.0041  -0.0461 43  PHE A N   
320  C  CA  . PHE A 43  ? 0.2391 0.3111 0.2118 0.0179  -0.0007 -0.0443 43  PHE A CA  
321  C  C   . PHE A 43  ? 0.2577 0.3417 0.2292 0.0166  -0.0024 -0.0544 43  PHE A C   
322  O  O   . PHE A 43  ? 0.2654 0.3632 0.2368 0.0188  -0.0075 -0.0576 43  PHE A O   
323  C  CB  . PHE A 43  ? 0.2298 0.3066 0.2035 0.0215  -0.0052 -0.0399 43  PHE A CB  
324  C  CG  . PHE A 43  ? 0.2337 0.2988 0.2074 0.0228  -0.004  -0.0307 43  PHE A CG  
325  C  CD1 . PHE A 43  ? 0.2389 0.2964 0.22   0.0197  -0.0012 -0.0312 43  PHE A CD1 
326  C  CD2 . PHE A 43  ? 0.2495 0.3105 0.2148 0.0267  -0.0055 -0.0219 43  PHE A CD2 
327  C  CE1 . PHE A 43  ? 0.2361 0.2838 0.2167 0.0209  -0.0006 -0.0238 43  PHE A CE1 
328  C  CE2 . PHE A 43  ? 0.2468 0.2968 0.2121 0.0268  -0.0045 -0.0147 43  PHE A CE2 
329  C  CZ  . PHE A 43  ? 0.2428 0.2868 0.2158 0.0241  -0.0024 -0.0161 43  PHE A CZ  
330  N  N   . PRO A 44  ? 0.2617 0.3412 0.232  0.0137  0.0015  -0.0603 44  PRO A N   
331  C  CA  . PRO A 44  ? 0.2705 0.3604 0.2397 0.0115  0       -0.0716 44  PRO A CA  
332  C  C   . PRO A 44  ? 0.2861 0.3895 0.2456 0.0171  -0.0048 -0.0705 44  PRO A C   
333  O  O   . PRO A 44  ? 0.2825 0.4    0.2414 0.0166  -0.0086 -0.0794 44  PRO A O   
334  C  CB  . PRO A 44  ? 0.2764 0.3536 0.2441 0.0085  0.0061  -0.0763 44  PRO A CB  
335  C  CG  . PRO A 44  ? 0.2758 0.3435 0.2395 0.0128  0.0089  -0.0655 44  PRO A CG  
336  C  CD  . PRO A 44  ? 0.2547 0.32   0.2237 0.0132  0.0072  -0.0574 44  PRO A CD  
337  N  N   . HIS A 45  ? 0.2968 0.3967 0.2487 0.0222  -0.0046 -0.0597 45  HIS A N   
338  C  CA  . HIS A 45  ? 0.3111 0.421  0.2516 0.028   -0.0079 -0.0561 45  HIS A CA  
339  C  C   . HIS A 45  ? 0.3207 0.4385 0.2587 0.0331  -0.0138 -0.0508 45  HIS A C   
340  O  O   . HIS A 45  ? 0.336  0.461  0.2628 0.0389  -0.0168 -0.0467 45  HIS A O   
341  C  CB  . HIS A 45  ? 0.3173 0.4188 0.2507 0.0299  -0.0036 -0.0466 45  HIS A CB  
342  C  CG  . HIS A 45  ? 0.332  0.4219 0.2692 0.0292  -0.0017 -0.0365 45  HIS A CG  
343  N  ND1 . HIS A 45  ? 0.3469 0.4269 0.294  0.0253  0.001   -0.0377 45  HIS A ND1 
344  C  CD2 . HIS A 45  ? 0.3401 0.4263 0.2714 0.0317  -0.002  -0.0255 45  HIS A CD2 
345  C  CE1 . HIS A 45  ? 0.3539 0.4265 0.3012 0.0258  0.0016  -0.0282 45  HIS A CE1 
346  N  NE2 . HIS A 45  ? 0.3543 0.4296 0.2926 0.029   0.0001  -0.021  45  HIS A NE2 
347  N  N   . PHE A 46  ? 0.3086 0.4245 0.2557 0.0319  -0.0153 -0.0505 46  PHE A N   
348  C  CA  . PHE A 46  ? 0.3027 0.4252 0.2475 0.0381  -0.0207 -0.0456 46  PHE A CA  
349  C  C   . PHE A 46  ? 0.3113 0.4536 0.26   0.0396  -0.0263 -0.0556 46  PHE A C   
350  O  O   . PHE A 46  ? 0.3125 0.4612 0.271  0.033   -0.0255 -0.0669 46  PHE A O   
351  C  CB  . PHE A 46  ? 0.2909 0.4025 0.2436 0.037   -0.0193 -0.0403 46  PHE A CB  
352  C  CG  . PHE A 46  ? 0.2996 0.3956 0.2457 0.0392  -0.0171 -0.0279 46  PHE A CG  
353  C  CD1 . PHE A 46  ? 0.3077 0.3963 0.247  0.0376  -0.0131 -0.0231 46  PHE A CD1 
354  C  CD2 . PHE A 46  ? 0.3127 0.4012 0.2608 0.0416  -0.0181 -0.0221 46  PHE A CD2 
355  C  CE1 . PHE A 46  ? 0.3315 0.4073 0.2657 0.038   -0.0108 -0.0126 46  PHE A CE1 
356  C  CE2 . PHE A 46  ? 0.3298 0.4031 0.2721 0.0422  -0.0158 -0.0119 46  PHE A CE2 
357  C  CZ  . PHE A 46  ? 0.3266 0.3941 0.2624 0.0397  -0.0122 -0.0073 46  PHE A CZ  
358  N  N   . ASP A 47  ? 0.3078 0.4596 0.2493 0.0484  -0.0321 -0.0513 47  ASP A N   
359  C  CA  . ASP A 47  ? 0.3053 0.4783 0.2521 0.0518  -0.0384 -0.0593 47  ASP A CA  
360  C  C   . ASP A 47  ? 0.2973 0.4647 0.2552 0.0508  -0.0375 -0.0569 47  ASP A C   
361  O  O   . ASP A 47  ? 0.2853 0.4401 0.2377 0.0565  -0.0372 -0.0459 47  ASP A O   
362  C  CB  . ASP A 47  ? 0.3444 0.5272 0.277  0.0641  -0.0447 -0.0534 47  ASP A CB  
363  C  CG  . ASP A 47  ? 0.4281 0.633  0.3656 0.0709  -0.052  -0.0589 47  ASP A CG  
364  O  OD1 . ASP A 47  ? 0.4288 0.6443 0.3821 0.0647  -0.0522 -0.0687 47  ASP A OD1 
365  O  OD2 . ASP A 47  ? 0.497  0.7093 0.4221 0.0828  -0.0574 -0.0534 47  ASP A OD2 
366  N  N   . LEU A 48  ? 0.303  0.4775 0.2756 0.0429  -0.036  -0.067  48  LEU A N   
367  C  CA  . LEU A 48  ? 0.3304 0.5004 0.3137 0.0411  -0.0341 -0.0656 48  LEU A CA  
368  C  C   . LEU A 48  ? 0.3504 0.5435 0.342  0.0455  -0.0396 -0.0717 48  LEU A C   
369  O  O   . LEU A 48  ? 0.3535 0.5464 0.3554 0.0433  -0.0377 -0.0725 48  LEU A O   
370  C  CB  . LEU A 48  ? 0.3216 0.4803 0.3149 0.0292  -0.027  -0.0705 48  LEU A CB  
371  C  CG  . LEU A 48  ? 0.3388 0.4749 0.3252 0.0267  -0.0215 -0.0633 48  LEU A CG  
372  C  CD1 . LEU A 48  ? 0.3396 0.4662 0.3332 0.0165  -0.0149 -0.0697 48  LEU A CD1 
373  C  CD2 . LEU A 48  ? 0.3442 0.4649 0.3268 0.0312  -0.0203 -0.0512 48  LEU A CD2 
374  N  N   . SER A 49  ? 0.36   0.5734 0.3464 0.0529  -0.0465 -0.0752 49  SER A N   
375  C  CA  . SER A 49  ? 0.3755 0.6146 0.3692 0.0593  -0.0528 -0.0809 49  SER A CA  
376  C  C   . SER A 49  ? 0.397  0.6275 0.3865 0.0706  -0.0542 -0.0698 49  SER A C   
377  O  O   . SER A 49  ? 0.3992 0.606  0.3763 0.0748  -0.052  -0.0577 49  SER A O   
378  C  CB  . SER A 49  ? 0.3988 0.6609 0.3848 0.0666  -0.0604 -0.086  49  SER A CB  
379  O  OG  . SER A 49  ? 0.4439 0.6935 0.4106 0.0771  -0.0622 -0.0742 49  SER A OG  
380  N  N   . HIS A 50  ? 0.4056 0.6553 0.4054 0.0754  -0.0576 -0.0743 50  HIS A N   
381  C  CA  . HIS A 50  ? 0.4286 0.6695 0.424  0.087   -0.0588 -0.0647 50  HIS A CA  
382  C  C   . HIS A 50  ? 0.4345 0.6688 0.4101 0.102   -0.0638 -0.0543 50  HIS A C   
383  O  O   . HIS A 50  ? 0.4307 0.6825 0.4001 0.1073  -0.0694 -0.0578 50  HIS A O   
384  C  CB  . HIS A 50  ? 0.4473 0.7144 0.4576 0.0907  -0.0617 -0.0726 50  HIS A CB  
385  C  CG  . HIS A 50  ? 0.4987 0.7629 0.5017 0.1072  -0.0653 -0.0642 50  HIS A CG  
386  N  ND1 . HIS A 50  ? 0.5377 0.7783 0.5394 0.1082  -0.0606 -0.0563 50  HIS A ND1 
387  C  CD2 . HIS A 50  ? 0.5206 0.8009 0.5157 0.1237  -0.0731 -0.0625 50  HIS A CD2 
388  C  CE1 . HIS A 50  ? 0.5552 0.797  0.5486 0.1248  -0.0652 -0.0506 50  HIS A CE1 
389  N  NE2 . HIS A 50  ? 0.5478 0.8128 0.5365 0.1353  -0.0728 -0.0535 50  HIS A NE2 
390  N  N   . GLY A 51  ? 0.4444 0.6526 0.4092 0.108   -0.0615 -0.0419 51  GLY A N   
391  C  CA  . GLY A 51  ? 0.4484 0.6453 0.3926 0.1215  -0.0649 -0.0308 51  GLY A CA  
392  C  C   . GLY A 51  ? 0.4396 0.6254 0.3708 0.1173  -0.0631 -0.0263 51  GLY A C   
393  O  O   . GLY A 51  ? 0.4576 0.6366 0.3707 0.1276  -0.0656 -0.0176 51  GLY A O   
394  N  N   . SER A 52  ? 0.4091 0.5913 0.3481 0.1027  -0.0581 -0.0314 52  SER A N   
395  C  CA  . SER A 52  ? 0.3988 0.5707 0.3272 0.0978  -0.0552 -0.0279 52  SER A CA  
396  C  C   . SER A 52  ? 0.4028 0.5462 0.315  0.1019  -0.0519 -0.0129 52  SER A C   
397  O  O   . SER A 52  ? 0.4012 0.5267 0.3169 0.0992  -0.0481 -0.0082 52  SER A O   
398  C  CB  . SER A 52  ? 0.3965 0.5637 0.3372 0.0823  -0.0491 -0.0347 52  SER A CB  
399  O  OG  . SER A 52  ? 0.4114 0.5592 0.3436 0.0772  -0.0438 -0.0279 52  SER A OG  
400  N  N   . ALA A 53  ? 0.4059 0.5457 0.3006 0.1077  -0.0529 -0.0061 53  ALA A N   
401  C  CA  . ALA A 53  ? 0.4116 0.5245 0.2898 0.1099  -0.0488 0.008   53  ALA A CA  
402  C  C   . ALA A 53  ? 0.3897 0.4857 0.2737 0.0959  -0.041  0.0097  53  ALA A C   
403  O  O   . ALA A 53  ? 0.3933 0.4667 0.2722 0.094   -0.0369 0.0186  53  ALA A O   
404  C  CB  . ALA A 53  ? 0.4263 0.5422 0.2849 0.1177  -0.0507 0.0138  53  ALA A CB  
405  N  N   . GLN A 54  ? 0.3545 0.4616 0.2493 0.0865  -0.0392 0.0004  54  GLN A N   
406  C  CA  . GLN A 54  ? 0.3455 0.4402 0.2463 0.075   -0.0325 0.001   54  GLN A CA  
407  C  C   . GLN A 54  ? 0.3243 0.4081 0.237  0.0705  -0.0302 0.0009  54  GLN A C   
408  O  O   . GLN A 54  ? 0.3184 0.3846 0.23   0.0655  -0.0255 0.0071  54  GLN A O   
409  C  CB  . GLN A 54  ? 0.3679 0.4772 0.2771 0.0682  -0.0317 -0.01   54  GLN A CB  
410  C  CG  . GLN A 54  ? 0.4223 0.5217 0.3287 0.061   -0.0255 -0.0072 54  GLN A CG  
411  C  CD  . GLN A 54  ? 0.4311 0.5438 0.3392 0.0575  -0.0251 -0.0166 54  GLN A CD  
412  O  OE1 . GLN A 54  ? 0.3965 0.5259 0.309  0.0587  -0.0293 -0.0266 54  GLN A OE1 
413  N  NE2 . GLN A 54  ? 0.4585 0.5643 0.3641 0.0526  -0.0196 -0.0145 54  GLN A NE2 
414  N  N   . VAL A 55  ? 0.3049 0.4009 0.2291 0.0721  -0.0335 -0.0068 55  VAL A N   
415  C  CA  . VAL A 55  ? 0.3048 0.3922 0.2395 0.0689  -0.0314 -0.0072 55  VAL A CA  
416  C  C   . VAL A 55  ? 0.3262 0.3961 0.2509 0.076   -0.0319 0.0029  55  VAL A C   
417  O  O   . VAL A 55  ? 0.3362 0.3894 0.2627 0.0714  -0.0281 0.0069  55  VAL A O   
418  C  CB  . VAL A 55  ? 0.2857 0.3921 0.2348 0.0688  -0.0341 -0.0178 55  VAL A CB  
419  C  CG1 . VAL A 55  ? 0.2885 0.3866 0.2457 0.0682  -0.0323 -0.017  55  VAL A CG1 
420  C  CG2 . VAL A 55  ? 0.2757 0.3921 0.2348 0.0588  -0.0317 -0.0278 55  VAL A CG2 
421  N  N   . LYS A 56  ? 0.3274 0.4003 0.2404 0.0875  -0.0364 0.0072  56  LYS A N   
422  C  CA  . LYS A 56  ? 0.3542 0.4068 0.255  0.095   -0.0364 0.0172  56  LYS A CA  
423  C  C   . LYS A 56  ? 0.3578 0.3866 0.2487 0.0883  -0.0307 0.0264  56  LYS A C   
424  O  O   . LYS A 56  ? 0.3714 0.3815 0.2614 0.0862  -0.028  0.0306  56  LYS A O   
425  C  CB  . LYS A 56  ? 0.387  0.4457 0.2743 0.1097  -0.0419 0.021   56  LYS A CB  
426  C  CG  . LYS A 56  ? 0.4621 0.5431 0.3593 0.118   -0.0477 0.0129  56  LYS A CG  
427  C  CD  . LYS A 56  ? 0.5395 0.6238 0.4211 0.1351  -0.0534 0.0183  56  LYS A CD  
428  C  CE  . LYS A 56  ? 0.5936 0.7058 0.4852 0.1446  -0.0599 0.0095  56  LYS A CE  
429  N  NZ  . LYS A 56  ? 0.6487 0.7701 0.5246 0.1615  -0.0663 0.0137  56  LYS A NZ  
430  N  N   . GLY A 57  ? 0.3498 0.3808 0.2337 0.0847  -0.0288 0.0286  57  GLY A N   
431  C  CA  . GLY A 57  ? 0.3577 0.3706 0.2336 0.0774  -0.0229 0.0366  57  GLY A CA  
432  C  C   . GLY A 57  ? 0.3511 0.3593 0.2404 0.0657  -0.0186 0.0332  57  GLY A C   
433  O  O   . GLY A 57  ? 0.3458 0.3363 0.2318 0.0605  -0.0147 0.039   57  GLY A O   
434  N  N   . HIS A 58  ? 0.3314 0.3553 0.2354 0.0615  -0.0192 0.0236  58  HIS A N   
435  C  CA  . HIS A 58  ? 0.317  0.337  0.2328 0.0521  -0.0153 0.0205  58  HIS A CA  
436  C  C   . HIS A 58  ? 0.3169 0.3246 0.2363 0.0527  -0.0155 0.0218  58  HIS A C   
437  O  O   . HIS A 58  ? 0.309  0.3049 0.23   0.0463  -0.0121 0.0244  58  HIS A O   
438  C  CB  . HIS A 58  ? 0.305  0.3411 0.2337 0.0482  -0.0153 0.0104  58  HIS A CB  
439  C  CG  . HIS A 58  ? 0.3261 0.3569 0.2633 0.0399  -0.0109 0.0089  58  HIS A CG  
440  N  ND1 . HIS A 58  ? 0.3523 0.378  0.2858 0.0349  -0.007  0.0131  58  HIS A ND1 
441  C  CD2 . HIS A 58  ? 0.341  0.371  0.289  0.0366  -0.0098 0.0045  58  HIS A CD2 
442  C  CE1 . HIS A 58  ? 0.3584 0.3811 0.3009 0.0297  -0.0043 0.0108  58  HIS A CE1 
443  N  NE2 . HIS A 58  ? 0.3446 0.3686 0.2951 0.0307  -0.0057 0.0061  58  HIS A NE2 
444  N  N   . GLY A 59  ? 0.3115 0.3229 0.2313 0.0608  -0.0195 0.0199  59  GLY A N   
445  C  CA  . GLY A 59  ? 0.3243 0.3252 0.2466 0.0631  -0.0198 0.0205  59  GLY A CA  
446  C  C   . GLY A 59  ? 0.3323 0.3098 0.2423 0.0632  -0.0179 0.0292  59  GLY A C   
447  O  O   . GLY A 59  ? 0.3307 0.2963 0.2436 0.0593  -0.0159 0.0294  59  GLY A O   
448  N  N   . LYS A 60  ? 0.331  0.3013 0.227  0.0667  -0.0178 0.0362  60  LYS A N   
449  C  CA  . LYS A 60  ? 0.3516 0.2975 0.2342 0.0653  -0.0149 0.0449  60  LYS A CA  
450  C  C   . LYS A 60  ? 0.3518 0.2919 0.239  0.0517  -0.0097 0.0456  60  LYS A C   
451  O  O   . LYS A 60  ? 0.3549 0.2777 0.2399 0.047   -0.0074 0.0481  60  LYS A O   
452  C  CB  . LYS A 60  ? 0.4044 0.3452 0.2695 0.0722  -0.0154 0.0527  60  LYS A CB  
453  C  CG  . LYS A 60  ? 0.4791 0.3932 0.3291 0.0687  -0.0108 0.0625  60  LYS A CG  
454  C  CD  . LYS A 60  ? 0.5737 0.4658 0.4185 0.0728  -0.0111 0.0645  60  LYS A CD  
455  C  CE  . LYS A 60  ? 0.6586 0.5216 0.4842 0.0714  -0.0067 0.0748  60  LYS A CE  
456  N  NZ  . LYS A 60  ? 0.6946 0.5348 0.5196 0.0665  -0.0044 0.0746  60  LYS A NZ  
457  N  N   . LYS A 61  ? 0.3286 0.2845 0.2232 0.0458  -0.0082 0.0424  61  LYS A N   
458  C  CA  . LYS A 61  ? 0.3179 0.2725 0.2183 0.0344  -0.0037 0.0423  61  LYS A CA  
459  C  C   . LYS A 61  ? 0.3114 0.2658 0.2239 0.0307  -0.0039 0.0368  61  LYS A C   
460  O  O   . LYS A 61  ? 0.3012 0.2459 0.2145 0.0237  -0.0014 0.0383  61  LYS A O   
461  C  CB  . LYS A 61  ? 0.311  0.2832 0.2163 0.0313  -0.0023 0.0393  61  LYS A CB  
462  C  CG  . LYS A 61  ? 0.3603 0.3334 0.2525 0.0339  -0.0012 0.0451  61  LYS A CG  
463  C  CD  . LYS A 61  ? 0.419  0.4097 0.3156 0.0321  -0.0001 0.0408  61  LYS A CD  
464  C  CE  . LYS A 61  ? 0.5096 0.5024 0.3921 0.0357  0.0007  0.0461  61  LYS A CE  
465  N  NZ  . LYS A 61  ? 0.5686 0.5787 0.4552 0.0338  0.0021  0.0411  61  LYS A NZ  
466  N  N   . VAL A 62  ? 0.2981 0.2639 0.2199 0.035   -0.0067 0.0302  62  VAL A N   
467  C  CA  . VAL A 62  ? 0.2925 0.2581 0.2242 0.0325  -0.0065 0.0255  62  VAL A CA  
468  C  C   . VAL A 62  ? 0.3099 0.2578 0.236  0.0339  -0.007  0.0282  62  VAL A C   
469  O  O   . VAL A 62  ? 0.3123 0.2538 0.2416 0.028   -0.0053 0.0273  62  VAL A O   
470  C  CB  . VAL A 62  ? 0.2876 0.2675 0.2286 0.0367  -0.0087 0.0186  62  VAL A CB  
471  C  CG1 . VAL A 62  ? 0.2805 0.2583 0.2295 0.0352  -0.0081 0.0148  62  VAL A CG1 
472  C  CG2 . VAL A 62  ? 0.2824 0.2767 0.2291 0.0335  -0.0074 0.0148  62  VAL A CG2 
473  N  N   . ALA A 63  ? 0.319  0.2592 0.2363 0.0422  -0.0093 0.0309  63  ALA A N   
474  C  CA  . ALA A 63  ? 0.3319 0.253  0.2421 0.0452  -0.0096 0.0331  63  ALA A CA  
475  C  C   . ALA A 63  ? 0.3338 0.2363 0.2356 0.0368  -0.0062 0.0384  63  ALA A C   
476  O  O   . ALA A 63  ? 0.3448 0.2353 0.2467 0.0328  -0.0052 0.037   63  ALA A O   
477  C  CB  . ALA A 63  ? 0.3487 0.2654 0.2495 0.0574  -0.0127 0.0358  63  ALA A CB  
478  N  N   . ASP A 64  ? 0.3323 0.2335 0.227  0.0336  -0.004  0.0439  64  ASP A N   
479  C  CA  . ASP A 64  ? 0.3382 0.2242 0.2259 0.0237  0.0003  0.0488  64  ASP A CA  
480  C  C   . ASP A 64  ? 0.3157 0.2104 0.2154 0.0127  0.0022  0.0442  64  ASP A C   
481  O  O   . ASP A 64  ? 0.32   0.2021 0.2176 0.0048  0.0044  0.0447  64  ASP A O   
482  C  CB  . ASP A 64  ? 0.3557 0.2429 0.2343 0.0224  0.0029  0.0553  64  ASP A CB  
483  C  CG  . ASP A 64  ? 0.4298 0.303  0.2919 0.0326  0.0018  0.0621  64  ASP A CG  
484  O  OD1 . ASP A 64  ? 0.4473 0.3073 0.3042 0.0406  -0.0006 0.062   64  ASP A OD1 
485  O  OD2 . ASP A 64  ? 0.4378 0.3135 0.2913 0.0334  0.0035  0.0675  64  ASP A OD2 
486  N  N   . ALA A 65  ? 0.2885 0.2044 0.2004 0.0125  0.0013  0.0393  65  ALA A N   
487  C  CA  . ALA A 65  ? 0.3018 0.227  0.2246 0.0044  0.0026  0.0351  65  ALA A CA  
488  C  C   . ALA A 65  ? 0.3085 0.2263 0.2343 0.0049  0.0008  0.0309  65  ALA A C   
489  O  O   . ALA A 65  ? 0.3127 0.2284 0.2414 -0.0026 0.0019  0.0292  65  ALA A O   
490  C  CB  . ALA A 65  ? 0.2986 0.2446 0.2316 0.0062  0.0022  0.0311  65  ALA A CB  
491  N  N   . LEU A 66  ? 0.3074 0.2229 0.2327 0.0137  -0.0019 0.0289  66  LEU A N   
492  C  CA  . LEU A 66  ? 0.3216 0.2305 0.2489 0.0152  -0.0033 0.0248  66  LEU A CA  
493  C  C   . LEU A 66  ? 0.3416 0.2281 0.2586 0.0121  -0.0025 0.0271  66  LEU A C   
494  O  O   . LEU A 66  ? 0.3339 0.2154 0.2526 0.0076  -0.0024 0.0235  66  LEU A O   
495  C  CB  . LEU A 66  ? 0.3159 0.2296 0.2455 0.0254  -0.0057 0.022   66  LEU A CB  
496  C  CG  . LEU A 66  ? 0.3264 0.2604 0.2673 0.0264  -0.0058 0.018   66  LEU A CG  
497  C  CD1 . LEU A 66  ? 0.3312 0.2715 0.2747 0.0353  -0.0078 0.015   66  LEU A CD1 
498  C  CD2 . LEU A 66  ? 0.3208 0.26   0.2692 0.0212  -0.0046 0.0143  66  LEU A CD2 
499  N  N   . THR A 67  ? 0.3452 0.2175 0.2505 0.014   -0.0015 0.033   67  THR A N   
500  C  CA  . THR A 67  ? 0.3651 0.2119 0.2585 0.0103  0.0003  0.0357  67  THR A CA  
501  C  C   . THR A 67  ? 0.356  0.2032 0.253  -0.0043 0.0032  0.0346  67  THR A C   
502  O  O   . THR A 67  ? 0.3765 0.2107 0.2712 -0.0099 0.0037  0.0315  67  THR A O   
503  C  CB  . THR A 67  ? 0.4023 0.2342 0.2812 0.015   0.0017  0.0438  67  THR A CB  
504  O  OG1 . THR A 67  ? 0.4125 0.2463 0.2885 0.0294  -0.0017 0.0439  67  THR A OG1 
505  C  CG2 . THR A 67  ? 0.4233 0.2246 0.2877 0.0097  0.005   0.0476  67  THR A CG2 
506  N  N   . ASN A 68  ? 0.3335 0.1976 0.2369 -0.0101 0.005   0.0361  68  ASN A N   
507  C  CA  . ASN A 68  ? 0.3415 0.2118 0.2505 -0.0234 0.0077  0.0346  68  ASN A CA  
508  C  C   . ASN A 68  ? 0.3373 0.2199 0.2573 -0.0257 0.0054  0.0271  68  ASN A C   
509  O  O   . ASN A 68  ? 0.3533 0.2324 0.2745 -0.0353 0.0062  0.0241  68  ASN A O   
510  C  CB  . ASN A 68  ? 0.3657 0.2533 0.2788 -0.0269 0.0103  0.0379  68  ASN A CB  
511  C  CG  . ASN A 68  ? 0.4612 0.3347 0.3615 -0.0285 0.014   0.0457  68  ASN A CG  
512  O  OD1 . ASN A 68  ? 0.5117 0.361  0.4003 -0.0316 0.016   0.0489  68  ASN A OD1 
513  N  ND2 . ASN A 68  ? 0.466  0.3527 0.3664 -0.0262 0.0154  0.0492  68  ASN A ND2 
514  N  N   . ALA A 69  ? 0.3071 0.2038 0.2346 -0.0173 0.0026  0.024   69  ALA A N   
515  C  CA  . ALA A 69  ? 0.314  0.2221 0.2502 -0.0176 0.0006  0.0179  69  ALA A CA  
516  C  C   . ALA A 69  ? 0.341  0.2324 0.2717 -0.0174 -0.001  0.0143  69  ALA A C   
517  O  O   . ALA A 69  ? 0.3484 0.2429 0.2823 -0.0235 -0.0017 0.0096  69  ALA A O   
518  C  CB  . ALA A 69  ? 0.2991 0.2207 0.2417 -0.0083 -0.001  0.0164  69  ALA A CB  
519  N  N   . VAL A 70  ? 0.3537 0.2283 0.2756 -0.01   -0.0016 0.016   70  VAL A N   
520  C  CA  . VAL A 70  ? 0.3783 0.2339 0.2928 -0.0084 -0.0026 0.0127  70  VAL A CA  
521  C  C   . VAL A 70  ? 0.403  0.2432 0.3116 -0.0205 -0.0006 0.012   70  VAL A C   
522  O  O   . VAL A 70  ? 0.4147 0.2497 0.3228 -0.0248 -0.0016 0.0061  70  VAL A O   
523  C  CB  . VAL A 70  ? 0.4037 0.2436 0.3086 0.0031  -0.0032 0.0157  70  VAL A CB  
524  C  CG1 . VAL A 70  ? 0.4395 0.2551 0.334  0.0043  -0.0033 0.0129  70  VAL A CG1 
525  C  CG2 . VAL A 70  ? 0.4005 0.2562 0.3122 0.014   -0.0052 0.0142  70  VAL A CG2 
526  N  N   . ALA A 71  ? 0.4073 0.2399 0.3108 -0.0263 0.0025  0.0178  71  ALA A N   
527  C  CA  . ALA A 71  ? 0.4303 0.2476 0.3281 -0.0395 0.0056  0.0175  71  ALA A CA  
528  C  C   . ALA A 71  ? 0.4253 0.2623 0.3347 -0.0513 0.0053  0.0117  71  ALA A C   
529  O  O   . ALA A 71  ? 0.4411 0.2685 0.3483 -0.0617 0.006   0.0072  71  ALA A O   
530  C  CB  . ALA A 71  ? 0.4377 0.2448 0.3275 -0.0433 0.01    0.026   71  ALA A CB  
531  N  N   . HIS A 72  ? 0.398  0.2624 0.3194 -0.0493 0.0039  0.0112  72  HIS A N   
532  C  CA  . HIS A 72  ? 0.3778 0.2641 0.3104 -0.0583 0.0033  0.0062  72  HIS A CA  
533  C  C   . HIS A 72  ? 0.3624 0.2662 0.3029 -0.0503 -0.0007 0.0013  72  HIS A C   
534  O  O   . HIS A 72  ? 0.3444 0.2715 0.2946 -0.0504 -0.0014 0.0002  72  HIS A O   
535  C  CB  . HIS A 72  ? 0.3642 0.2674 0.3028 -0.0632 0.0065  0.0108  72  HIS A CB  
536  C  CG  . HIS A 72  ? 0.4167 0.3023 0.3462 -0.0711 0.0114  0.0165  72  HIS A CG  
537  N  ND1 . HIS A 72  ? 0.4486 0.3218 0.3745 -0.0851 0.0141  0.0143  72  HIS A ND1 
538  C  CD2 . HIS A 72  ? 0.4351 0.3137 0.3576 -0.0671 0.0143  0.0243  72  HIS A CD2 
539  C  CE1 . HIS A 72  ? 0.4567 0.3133 0.3727 -0.0889 0.0191  0.0216  72  HIS A CE1 
540  N  NE2 . HIS A 72  ? 0.4507 0.3107 0.3641 -0.0778 0.0191  0.0279  72  HIS A NE2 
541  N  N   . VAL A 73  ? 0.3713 0.2631 0.3065 -0.0428 -0.003  -0.0014 73  VAL A N   
542  C  CA  . VAL A 73  ? 0.3785 0.2829 0.3185 -0.0342 -0.006  -0.005  73  VAL A CA  
543  C  C   . VAL A 73  ? 0.3733 0.296  0.3205 -0.0395 -0.0082 -0.0109 73  VAL A C   
544  O  O   . VAL A 73  ? 0.3655 0.3043 0.318  -0.0328 -0.0097 -0.0118 73  VAL A O   
545  C  CB  . VAL A 73  ? 0.4103 0.2968 0.3421 -0.0261 -0.0072 -0.0069 73  VAL A CB  
546  C  CG1 . VAL A 73  ? 0.4209 0.2924 0.3462 -0.0328 -0.0081 -0.0129 73  VAL A CG1 
547  C  CG2 . VAL A 73  ? 0.4141 0.313  0.3502 -0.016  -0.0088 -0.0085 73  VAL A CG2 
548  N  N   . ASP A 74  ? 0.3763 0.2978 0.3235 -0.0515 -0.0081 -0.0148 74  ASP A N   
549  C  CA  . ASP A 74  ? 0.3903 0.3328 0.3449 -0.0565 -0.0108 -0.021  74  ASP A CA  
550  C  C   . ASP A 74  ? 0.3716 0.3377 0.3366 -0.0624 -0.0096 -0.0193 74  ASP A C   
551  O  O   . ASP A 74  ? 0.3677 0.3536 0.3396 -0.0676 -0.0118 -0.0246 74  ASP A O   
552  C  CB  . ASP A 74  ? 0.4476 0.3797 0.3978 -0.0666 -0.0123 -0.0286 74  ASP A CB  
553  C  CG  . ASP A 74  ? 0.5455 0.4614 0.4868 -0.059  -0.0144 -0.0324 74  ASP A CG  
554  O  OD1 . ASP A 74  ? 0.542  0.4673 0.4845 -0.0478 -0.0163 -0.0322 74  ASP A OD1 
555  O  OD2 . ASP A 74  ? 0.6242 0.517  0.5568 -0.064  -0.0136 -0.0354 74  ASP A OD2 
556  N  N   . ASP A 75  ? 0.3426 0.3077 0.3083 -0.0611 -0.0061 -0.0124 75  ASP A N   
557  C  CA  . ASP A 75  ? 0.316  0.3033 0.2909 -0.0655 -0.0043 -0.0106 75  ASP A CA  
558  C  C   . ASP A 75  ? 0.2929 0.2822 0.2681 -0.0561 -0.0021 -0.0038 75  ASP A C   
559  O  O   . ASP A 75  ? 0.2799 0.2748 0.2572 -0.0601 0.0013  0.0002  75  ASP A O   
560  C  CB  . ASP A 75  ? 0.3284 0.3099 0.3025 -0.0805 -0.0007 -0.0105 75  ASP A CB  
561  C  CG  . ASP A 75  ? 0.3702 0.3782 0.3552 -0.0881 0.0013  -0.011  75  ASP A CG  
562  O  OD1 . ASP A 75  ? 0.3482 0.3815 0.3422 -0.0838 -0.0017 -0.0146 75  ASP A OD1 
563  O  OD2 . ASP A 75  ? 0.3943 0.3979 0.3782 -0.0977 0.0061  -0.0075 75  ASP A OD2 
564  N  N   . MET A 76  ? 0.2812 0.2657 0.2538 -0.0444 -0.0038 -0.0028 76  MET A N   
565  C  CA  . MET A 76  ? 0.2842 0.2686 0.2565 -0.0363 -0.002  0.0023  76  MET A CA  
566  C  C   . MET A 76  ? 0.2716 0.2776 0.2518 -0.0344 -0.0006 0.0035  76  MET A C   
567  O  O   . MET A 76  ? 0.2676 0.2732 0.2469 -0.0343 0.0022  0.0076  76  MET A O   
568  C  CB  . MET A 76  ? 0.2998 0.2759 0.2687 -0.0257 -0.0035 0.0022  76  MET A CB  
569  C  CG  . MET A 76  ? 0.3624 0.3164 0.3227 -0.0255 -0.004  0.0024  76  MET A CG  
570  S  SD  . MET A 76  ? 0.4044 0.3515 0.362  -0.0131 -0.0046 0.0032  76  MET A SD  
571  C  CE  . MET A 76  ? 0.3906 0.3439 0.3498 -0.0099 -0.0068 -0.002  76  MET A CE  
572  N  N   . PRO A 77  ? 0.2661 0.2909 0.2529 -0.0325 -0.0023 0.0002  77  PRO A N   
573  C  CA  . PRO A 77  ? 0.2538 0.298  0.2473 -0.0296 -0.0006 0.0015  77  PRO A CA  
574  C  C   . PRO A 77  ? 0.2459 0.2966 0.2419 -0.0389 0.0028  0.0034  77  PRO A C   
575  O  O   . PRO A 77  ? 0.2323 0.2873 0.2289 -0.0361 0.0056  0.0066  77  PRO A O   
576  C  CB  . PRO A 77  ? 0.2538 0.3162 0.2527 -0.0268 -0.0035 -0.0028 77  PRO A CB  
577  C  CG  . PRO A 77  ? 0.2647 0.3141 0.2579 -0.0226 -0.0065 -0.0049 77  PRO A CG  
578  C  CD  . PRO A 77  ? 0.2549 0.2844 0.2424 -0.0308 -0.006  -0.0047 77  PRO A CD  
579  N  N   . ASN A 78  ? 0.2484 0.2982 0.245  -0.0505 0.003   0.0013  78  ASN A N   
580  C  CA  . ASN A 78  ? 0.259  0.3132 0.2572 -0.061  0.0073  0.0036  78  ASN A CA  
581  C  C   . ASN A 78  ? 0.2736 0.3059 0.262  -0.0612 0.0105  0.0098  78  ASN A C   
582  O  O   . ASN A 78  ? 0.2779 0.3159 0.2662 -0.0618 0.0142  0.0136  78  ASN A O   
583  C  CB  . ASN A 78  ? 0.2737 0.3307 0.2747 -0.0749 0.0072  -0.0008 78  ASN A CB  
584  C  CG  . ASN A 78  ? 0.3209 0.4078 0.3336 -0.0762 0.0048  -0.0067 78  ASN A CG  
585  O  OD1 . ASN A 78  ? 0.321  0.4292 0.3405 -0.0699 0.0054  -0.0061 78  ASN A OD1 
586  N  ND2 . ASN A 78  ? 0.3202 0.4096 0.3349 -0.0836 0.0017  -0.013  78  ASN A ND2 
587  N  N   . ALA A 79  ? 0.2738 0.2819 0.2532 -0.0602 0.009   0.0106  79  ALA A N   
588  C  CA  . ALA A 79  ? 0.2775 0.2648 0.2464 -0.059  0.0115  0.0166  79  ALA A CA  
589  C  C   . ALA A 79  ? 0.2785 0.2695 0.2463 -0.0483 0.0117  0.0199  79  ALA A C   
590  O  O   . ALA A 79  ? 0.2838 0.2685 0.2454 -0.0485 0.0146  0.025   79  ALA A O   
591  C  CB  . ALA A 79  ? 0.28   0.2424 0.2399 -0.0573 0.0093  0.016   79  ALA A CB  
592  N  N   . LEU A 80  ? 0.2582 0.2595 0.2314 -0.0392 0.009   0.017   80  LEU A N   
593  C  CA  . LEU A 80  ? 0.2525 0.2556 0.2246 -0.0299 0.0092  0.0189  80  LEU A CA  
594  C  C   . LEU A 80  ? 0.2355 0.259  0.2148 -0.0268 0.0107  0.0177  80  LEU A C   
595  O  O   . LEU A 80  ? 0.2259 0.2511 0.2055 -0.0187 0.0103  0.0172  80  LEU A O   
596  C  CB  . LEU A 80  ? 0.2629 0.2584 0.2342 -0.0217 0.006   0.0165  80  LEU A CB  
597  C  CG  . LEU A 80  ? 0.2939 0.2704 0.2586 -0.0221 0.0041  0.0165  80  LEU A CG  
598  C  CD1 . LEU A 80  ? 0.2961 0.2692 0.2613 -0.0134 0.0018  0.014   80  LEU A CD1 
599  C  CD2 . LEU A 80  ? 0.2924 0.2538 0.2478 -0.0234 0.0057  0.0214  80  LEU A CD2 
600  N  N   . SER A 81  ? 0.2305 0.2696 0.2158 -0.033  0.0124  0.0167  81  SER A N   
601  C  CA  . SER A 81  ? 0.23   0.2894 0.2222 -0.0284 0.0136  0.015   81  SER A CA  
602  C  C   . SER A 81  ? 0.2188 0.2797 0.208  -0.0231 0.0162  0.0172  81  SER A C   
603  O  O   . SER A 81  ? 0.1991 0.2673 0.1911 -0.0151 0.0161  0.0151  81  SER A O   
604  C  CB  . SER A 81  ? 0.2388 0.3178 0.2387 -0.036  0.0152  0.0133  81  SER A CB  
605  O  OG  . SER A 81  ? 0.2914 0.3703 0.2888 -0.0447 0.0195  0.0167  81  SER A OG  
606  N  N   . ALA A 82  ? 0.2186 0.2722 0.2013 -0.0274 0.0188  0.0213  82  ALA A N   
607  C  CA  . ALA A 82  ? 0.2179 0.2742 0.1967 -0.0223 0.0209  0.0228  82  ALA A CA  
608  C  C   . ALA A 82  ? 0.2283 0.2734 0.2033 -0.0137 0.0181  0.0214  82  ALA A C   
609  O  O   . ALA A 82  ? 0.2168 0.2672 0.1918 -0.0078 0.0188  0.0196  82  ALA A O   
610  C  CB  . ALA A 82  ? 0.2276 0.2786 0.1985 -0.0286 0.0243  0.0281  82  ALA A CB  
611  N  N   . LEU A 83  ? 0.2227 0.2534 0.1954 -0.0133 0.0149  0.0214  83  LEU A N   
612  C  CA  . LEU A 83  ? 0.2244 0.2476 0.1955 -0.006  0.0125  0.0194  83  LEU A CA  
613  C  C   . LEU A 83  ? 0.2215 0.2514 0.1991 -0.0012 0.0121  0.0152  83  LEU A C   
614  O  O   . LEU A 83  ? 0.2269 0.2561 0.2044 0.0041  0.0123  0.0129  83  LEU A O   
615  C  CB  . LEU A 83  ? 0.2338 0.2414 0.2007 -0.0062 0.0098  0.0204  83  LEU A CB  
616  C  CG  . LEU A 83  ? 0.262  0.2591 0.2197 -0.0077 0.0101  0.0251  83  LEU A CG  
617  C  CD1 . LEU A 83  ? 0.278  0.2592 0.2312 -0.0062 0.0074  0.0257  83  LEU A CD1 
618  C  CD2 . LEU A 83  ? 0.2705 0.2713 0.2244 -0.0022 0.0101  0.0254  83  LEU A CD2 
619  N  N   . SER A 84  ? 0.2143 0.2508 0.197  -0.003  0.0119  0.0141  84  SER A N   
620  C  CA  . SER A 84  ? 0.2131 0.2559 0.2002 0.0028  0.0118  0.0111  84  SER A CA  
621  C  C   . SER A 84  ? 0.2234 0.2773 0.212  0.0065  0.0147  0.0101  84  SER A C   
622  O  O   . SER A 84  ? 0.2245 0.2759 0.2126 0.0128  0.0157  0.0079  84  SER A O   
623  C  CB  . SER A 84  ? 0.2278 0.2777 0.219  0.0007  0.0103  0.0102  84  SER A CB  
624  O  OG  . SER A 84  ? 0.2673 0.3233 0.261  0.0082  0.0105  0.0082  84  SER A OG  
625  N  N   . ASP A 85  ? 0.2249 0.2895 0.2144 0.0024  0.0168  0.0116  85  ASP A N   
626  C  CA  . ASP A 85  ? 0.2174 0.293  0.2075 0.0062  0.0199  0.0105  85  ASP A CA  
627  C  C   . ASP A 85  ? 0.2321 0.2984 0.2169 0.0105  0.0204  0.009   85  ASP A C   
628  O  O   . ASP A 85  ? 0.2385 0.3061 0.2234 0.0168  0.0219  0.0058  85  ASP A O   
629  C  CB  . ASP A 85  ? 0.2204 0.3075 0.2111 -0.0006 0.0225  0.013   85  ASP A CB  
630  C  CG  . ASP A 85  ? 0.2976 0.4018 0.2911 0.0032  0.0261  0.0113  85  ASP A CG  
631  O  OD1 . ASP A 85  ? 0.2836 0.3887 0.2775 0.012   0.0264  0.008   85  ASP A OD1 
632  O  OD2 . ASP A 85  ? 0.3134 0.4294 0.308  -0.0027 0.0291  0.0133  85  ASP A OD2 
633  N  N   . LEU A 86  ? 0.231  0.288  0.2107 0.0073  0.0192  0.011   86  LEU A N   
634  C  CA  . LEU A 86  ? 0.239  0.2901 0.2142 0.0108  0.0189  0.0088  86  LEU A CA  
635  C  C   . LEU A 86  ? 0.2381 0.2805 0.2152 0.0148  0.0176  0.005   86  LEU A C   
636  O  O   . LEU A 86  ? 0.2425 0.2847 0.2191 0.0186  0.0191  0.001   86  LEU A O   
637  C  CB  . LEU A 86  ? 0.2454 0.2893 0.2145 0.0076  0.0171  0.0122  86  LEU A CB  
638  C  CG  . LEU A 86  ? 0.2501 0.29   0.215  0.0112  0.0155  0.0096  86  LEU A CG  
639  C  CD1 . LEU A 86  ? 0.2362 0.2852 0.1986 0.0137  0.0179  0.0066  86  LEU A CD1 
640  C  CD2 . LEU A 86  ? 0.2579 0.2906 0.2162 0.01    0.013   0.0137  86  LEU A CD2 
641  N  N   . HIS A 87  ? 0.2265 0.2613 0.2052 0.0137  0.0154  0.006   87  HIS A N   
642  C  CA  . HIS A 87  ? 0.2347 0.2612 0.2145 0.0165  0.015   0.003   87  HIS A CA  
643  C  C   . HIS A 87  ? 0.2411 0.2674 0.2232 0.0206  0.0172  0.0012  87  HIS A C   
644  O  O   . HIS A 87  ? 0.2571 0.2771 0.2386 0.0231  0.0189  -0.002  87  HIS A O   
645  C  CB  . HIS A 87  ? 0.226  0.2446 0.2058 0.0147  0.0123  0.0045  87  HIS A CB  
646  C  CG  . HIS A 87  ? 0.2187 0.2347 0.1948 0.0131  0.0102  0.006   87  HIS A CG  
647  N  ND1 . HIS A 87  ? 0.2417 0.2581 0.2143 0.0099  0.0095  0.0101  87  HIS A ND1 
648  C  CD2 . HIS A 87  ? 0.2266 0.2401 0.2017 0.0147  0.0088  0.0038  87  HIS A CD2 
649  C  CE1 . HIS A 87  ? 0.2549 0.2668 0.2229 0.0109  0.0076  0.0112  87  HIS A CE1 
650  N  NE2 . HIS A 87  ? 0.2467 0.2587 0.2167 0.0141  0.0067  0.0072  87  HIS A NE2 
651  N  N   . ALA A 88  ? 0.2195 0.2527 0.2037 0.0213  0.0172  0.0031  88  ALA A N   
652  C  CA  . ALA A 88  ? 0.2316 0.2649 0.2166 0.0271  0.0189  0.0021  88  ALA A CA  
653  C  C   . ALA A 88  ? 0.2542 0.2952 0.239  0.0319  0.0217  0.0006  88  ALA A C   
654  O  O   . ALA A 88  ? 0.2914 0.3262 0.274  0.038   0.0242  -0.0013 88  ALA A O   
655  C  CB  . ALA A 88  ? 0.2311 0.2694 0.2184 0.0269  0.0167  0.0043  88  ALA A CB  
656  N  N   . HIS A 89  ? 0.2442 0.2979 0.2307 0.0295  0.0219  0.0014  89  HIS A N   
657  C  CA  . HIS A 89  ? 0.2467 0.3102 0.2334 0.0349  0.0249  -0.0004 89  HIS A CA  
658  C  C   . HIS A 89  ? 0.249  0.309  0.2316 0.0358  0.0272  -0.0036 89  HIS A C   
659  O  O   . HIS A 89  ? 0.2689 0.3286 0.2495 0.0423  0.03    -0.0066 89  HIS A O   
660  C  CB  . HIS A 89  ? 0.2435 0.3262 0.2349 0.0323  0.0249  0.0015  89  HIS A CB  
661  C  CG  . HIS A 89  ? 0.2394 0.3291 0.2355 0.0317  0.0225  0.0031  89  HIS A CG  
662  N  ND1 . HIS A 89  ? 0.2405 0.3439 0.2401 0.0386  0.023   0.0022  89  HIS A ND1 
663  C  CD2 . HIS A 89  ? 0.2487 0.3338 0.2458 0.0258  0.0193  0.0048  89  HIS A CD2 
664  C  CE1 . HIS A 89  ? 0.238  0.346  0.2409 0.0362  0.0198  0.0032  89  HIS A CE1 
665  N  NE2 . HIS A 89  ? 0.2501 0.3468 0.2515 0.0281  0.0177  0.0046  89  HIS A NE2 
666  N  N   . LYS A 90  ? 0.2347 0.2922 0.2152 0.03    0.0258  -0.0031 90  LYS A N   
667  C  CA  . LYS A 90  ? 0.2368 0.2932 0.2129 0.0306  0.0273  -0.0066 90  LYS A CA  
668  C  C   . LYS A 90  ? 0.2428 0.2856 0.2168 0.0306  0.0267  -0.0107 90  LYS A C   
669  O  O   . LYS A 90  ? 0.2548 0.2927 0.2264 0.0343  0.0293  -0.0156 90  LYS A O   
670  C  CB  . LYS A 90  ? 0.2378 0.302  0.2113 0.0255  0.0265  -0.0037 90  LYS A CB  
671  C  CG  . LYS A 90  ? 0.2712 0.3369 0.2389 0.0268  0.0275  -0.0075 90  LYS A CG  
672  C  CD  . LYS A 90  ? 0.3275 0.4013 0.2946 0.0322  0.0315  -0.0108 90  LYS A CD  
673  C  CE  . LYS A 90  ? 0.4007 0.4784 0.3611 0.0333  0.0328  -0.0147 90  LYS A CE  
674  N  NZ  . LYS A 90  ? 0.4153 0.5    0.3748 0.0396  0.037   -0.0188 90  LYS A NZ  
675  N  N   . LEU A 91  ? 0.2229 0.2602 0.1975 0.0264  0.0237  -0.0093 91  LEU A N   
676  C  CA  . LEU A 91  ? 0.2357 0.2638 0.2099 0.0252  0.0231  -0.0135 91  LEU A CA  
677  C  C   . LEU A 91  ? 0.2586 0.2757 0.2343 0.0272  0.0254  -0.015  91  LEU A C   
678  O  O   . LEU A 91  ? 0.284  0.2933 0.259  0.0265  0.0271  -0.02   91  LEU A O   
679  C  CB  . LEU A 91  ? 0.2355 0.263  0.2104 0.0214  0.0193  -0.0109 91  LEU A CB  
680  C  CG  . LEU A 91  ? 0.2598 0.2947 0.2307 0.0199  0.0171  -0.0086 91  LEU A CG  
681  C  CD1 . LEU A 91  ? 0.2692 0.301  0.2397 0.018   0.0135  -0.0052 91  LEU A CD1 
682  C  CD2 . LEU A 91  ? 0.281  0.3201 0.2483 0.0209  0.0174  -0.0143 91  LEU A CD2 
683  N  N   . ARG A 92  ? 0.2387 0.2555 0.2162 0.0292  0.0253  -0.0108 92  ARG A N   
684  C  CA  . ARG A 92  ? 0.237  0.2432 0.2141 0.0321  0.0274  -0.0106 92  ARG A CA  
685  C  C   . ARG A 92  ? 0.2368 0.2339 0.2149 0.0281  0.0273  -0.0123 92  ARG A C   
686  O  O   . ARG A 92  ? 0.2388 0.2253 0.2153 0.0282  0.0308  -0.0156 92  ARG A O   
687  C  CB  . ARG A 92  ? 0.2549 0.2552 0.2285 0.0378  0.0318  -0.0136 92  ARG A CB  
688  C  CG  . ARG A 92  ? 0.3042 0.3157 0.2777 0.0433  0.0321  -0.0119 92  ARG A CG  
689  C  CD  . ARG A 92  ? 0.3951 0.3979 0.3637 0.0499  0.0366  -0.0155 92  ARG A CD  
690  N  NE  . ARG A 92  ? 0.4512 0.4652 0.4196 0.0571  0.0377  -0.0148 92  ARG A NE  
691  C  CZ  . ARG A 92  ? 0.5123 0.5285 0.4777 0.0607  0.0403  -0.019  92  ARG A CZ  
692  N  NH1 . ARG A 92  ? 0.5339 0.5421 0.4962 0.0569  0.0416  -0.0245 92  ARG A NH1 
693  N  NH2 . ARG A 92  ? 0.515  0.5432 0.4808 0.0682  0.0415  -0.0183 92  ARG A NH2 
694  N  N   . VAL A 93  ? 0.2218 0.2232 0.2023 0.0244  0.0236  -0.0104 93  VAL A N   
695  C  CA  . VAL A 93  ? 0.2142 0.2107 0.1965 0.0211  0.0232  -0.0122 93  VAL A CA  
696  C  C   . VAL A 93  ? 0.2312 0.2185 0.2132 0.0225  0.0257  -0.0105 93  VAL A C   
697  O  O   . VAL A 93  ? 0.2325 0.2205 0.2136 0.0251  0.0247  -0.0064 93  VAL A O   
698  C  CB  . VAL A 93  ? 0.2018 0.2044 0.1855 0.0188  0.0186  -0.0099 93  VAL A CB  
699  C  CG1 . VAL A 93  ? 0.2068 0.207  0.1932 0.0168  0.018   -0.012  93  VAL A CG1 
700  C  CG2 . VAL A 93  ? 0.1985 0.2094 0.1804 0.0182  0.0165  -0.0104 93  VAL A CG2 
701  N  N   . ASP A 94  ? 0.2416 0.2207 0.2238 0.0203  0.0292  -0.014  94  ASP A N   
702  C  CA  . ASP A 94  ? 0.2427 0.2121 0.2232 0.0213  0.0325  -0.0119 94  ASP A CA  
703  C  C   . ASP A 94  ? 0.2533 0.2274 0.2363 0.0202  0.0291  -0.0092 94  ASP A C   
704  O  O   . ASP A 94  ? 0.258  0.238  0.2448 0.0171  0.0266  -0.0113 94  ASP A O   
705  C  CB  . ASP A 94  ? 0.2583 0.2185 0.2391 0.0171  0.0376  -0.0165 94  ASP A CB  
706  C  CG  . ASP A 94  ? 0.2861 0.2338 0.2633 0.0178  0.0427  -0.0139 94  ASP A CG  
707  O  OD1 . ASP A 94  ? 0.2856 0.2356 0.2631 0.0187  0.0412  -0.0105 94  ASP A OD1 
708  O  OD2 . ASP A 94  ? 0.3082 0.2428 0.2812 0.0173  0.0485  -0.0155 94  ASP A OD2 
709  N  N   . PRO A 95  ? 0.2551 0.2263 0.2351 0.0237  0.029   -0.0049 95  PRO A N   
710  C  CA  . PRO A 95  ? 0.2521 0.2262 0.2331 0.0231  0.026   -0.0031 95  PRO A CA  
711  C  C   . PRO A 95  ? 0.2451 0.2184 0.2292 0.0198  0.0274  -0.0056 95  PRO A C   
712  O  O   . PRO A 95  ? 0.2307 0.2084 0.2165 0.0195  0.0241  -0.0054 95  PRO A O   
713  C  CB  . PRO A 95  ? 0.277  0.2466 0.2531 0.0276  0.0272  0.0006  95  PRO A CB  
714  C  CG  . PRO A 95  ? 0.2878 0.2576 0.2615 0.0315  0.028   0.0017  95  PRO A CG  
715  C  CD  . PRO A 95  ? 0.2648 0.2313 0.2398 0.0293  0.031   -0.0019 95  PRO A CD  
716  N  N   . VAL A 96  ? 0.2539 0.2218 0.2388 0.017   0.0325  -0.0085 96  VAL A N   
717  C  CA  . VAL A 96  ? 0.2615 0.2322 0.2511 0.013   0.0342  -0.0118 96  VAL A CA  
718  C  C   . VAL A 96  ? 0.2452 0.228  0.2404 0.0116  0.0291  -0.0149 96  VAL A C   
719  O  O   . VAL A 96  ? 0.2513 0.2397 0.2494 0.0118  0.0274  -0.0156 96  VAL A O   
720  C  CB  . VAL A 96  ? 0.2891 0.2527 0.2796 0.0082  0.0412  -0.0153 96  VAL A CB  
721  C  CG1 . VAL A 96  ? 0.2983 0.2639 0.2911 0.005   0.0411  -0.0205 96  VAL A CG1 
722  C  CG2 . VAL A 96  ? 0.3062 0.2751 0.3021 0.0038  0.0436  -0.0183 96  VAL A CG2 
723  N  N   . ASN A 97  ? 0.2258 0.2123 0.2209 0.0116  0.0264  -0.0162 97  ASN A N   
724  C  CA  . ASN A 97  ? 0.2214 0.2186 0.2195 0.0115  0.0216  -0.0184 97  ASN A CA  
725  C  C   . ASN A 97  ? 0.2201 0.2193 0.2164 0.015   0.0169  -0.0144 97  ASN A C   
726  O  O   . ASN A 97  ? 0.218  0.224  0.2166 0.0161  0.0139  -0.0158 97  ASN A O   
727  C  CB  . ASN A 97  ? 0.2256 0.2255 0.2222 0.0111  0.0205  -0.02   97  ASN A CB  
728  C  CG  . ASN A 97  ? 0.281  0.2777 0.2792 0.0072  0.0252  -0.0256 97  ASN A CG  
729  O  OD1 . ASN A 97  ? 0.2949 0.2965 0.2982 0.0031  0.0264  -0.0308 97  ASN A OD1 
730  N  ND2 . ASN A 97  ? 0.2575 0.2452 0.2515 0.0082  0.0285  -0.0246 97  ASN A ND2 
731  N  N   . PHE A 98  ? 0.2211 0.2143 0.2132 0.0169  0.0164  -0.0098 98  PHE A N   
732  C  CA  . PHE A 98  ? 0.2298 0.222  0.2194 0.0191  0.0127  -0.0066 98  PHE A CA  
733  C  C   . PHE A 98  ? 0.2339 0.2252 0.2249 0.0203  0.0133  -0.0076 98  PHE A C   
734  O  O   . PHE A 98  ? 0.2339 0.226  0.224  0.0226  0.0101  -0.0072 98  PHE A O   
735  C  CB  . PHE A 98  ? 0.2379 0.226  0.2238 0.0196  0.0123  -0.0029 98  PHE A CB  
736  C  CG  . PHE A 98  ? 0.2582 0.2496 0.2428 0.0187  0.0108  -0.0014 98  PHE A CG  
737  C  CD1 . PHE A 98  ? 0.2723 0.2658 0.2575 0.0185  0.0133  -0.0026 98  PHE A CD1 
738  C  CD2 . PHE A 98  ? 0.2651 0.2566 0.2472 0.0179  0.0076  0.0011  98  PHE A CD2 
739  C  CE1 . PHE A 98  ? 0.2674 0.2656 0.2514 0.0179  0.0123  -0.0015 98  PHE A CE1 
740  C  CE2 . PHE A 98  ? 0.2735 0.2689 0.2542 0.0164  0.0071  0.0028  98  PHE A CE2 
741  C  CZ  . PHE A 98  ? 0.2702 0.2701 0.2522 0.0166  0.0094  0.0014  98  PHE A CZ  
742  N  N   . LYS A 99  ? 0.2257 0.2148 0.2181 0.0193  0.0178  -0.0089 99  LYS A N   
743  C  CA  . LYS A 99  ? 0.232  0.2222 0.2259 0.0203  0.0193  -0.0102 99  LYS A CA  
744  C  C   . LYS A 99  ? 0.2189 0.2193 0.219  0.0199  0.0182  -0.0145 99  LYS A C   
745  O  O   . LYS A 99  ? 0.2158 0.2201 0.217  0.023   0.0166  -0.0153 99  LYS A O   
746  C  CB  . LYS A 99  ? 0.2681 0.2537 0.2616 0.0184  0.0256  -0.0103 99  LYS A CB  
747  C  CG  . LYS A 99  ? 0.3177 0.2948 0.3042 0.0206  0.0264  -0.0061 99  LYS A CG  
748  C  CD  . LYS A 99  ? 0.3692 0.34   0.3527 0.0204  0.0328  -0.005  99  LYS A CD  
749  C  CE  . LYS A 99  ? 0.4482 0.4119 0.4241 0.024   0.0332  -0.0008 99  LYS A CE  
750  N  NZ  . LYS A 99  ? 0.5106 0.4756 0.4824 0.0275  0.0295  0.0009  99  LYS A NZ  
751  N  N   . LEU A 100 ? 0.2049 0.2108 0.2088 0.0168  0.0187  -0.0175 100 LEU A N   
752  C  CA  . LEU A 100 ? 0.2121 0.231  0.2224 0.0165  0.0171  -0.0225 100 LEU A CA  
753  C  C   . LEU A 100 ? 0.2236 0.2464 0.2313 0.022   0.0108  -0.0209 100 LEU A C   
754  O  O   . LEU A 100 ? 0.2383 0.2695 0.249  0.0257  0.0088  -0.0228 100 LEU A O   
755  C  CB  . LEU A 100 ? 0.2096 0.233  0.2237 0.0112  0.0192  -0.0272 100 LEU A CB  
756  C  CG  . LEU A 100 ? 0.2257 0.2414 0.2407 0.0055  0.0264  -0.0286 100 LEU A CG  
757  C  CD1 . LEU A 100 ? 0.2347 0.2523 0.2523 0       0.0283  -0.034  100 LEU A CD1 
758  C  CD2 . LEU A 100 ? 0.2398 0.2593 0.2596 0.0034  0.0307  -0.0305 100 LEU A CD2 
759  N  N   . LEU A 101 ? 0.2233 0.2399 0.225  0.023   0.0081  -0.017  101 LEU A N   
760  C  CA  . LEU A 101 ? 0.2348 0.2516 0.2317 0.0279  0.003   -0.0142 101 LEU A CA  
761  C  C   . LEU A 101 ? 0.2329 0.242  0.226  0.032   0.0018  -0.0114 101 LEU A C   
762  O  O   . LEU A 101 ? 0.2363 0.2473 0.2274 0.0377  -0.0014 -0.0112 101 LEU A O   
763  C  CB  . LEU A 101 ? 0.242  0.2536 0.233  0.0268  0.0016  -0.0104 101 LEU A CB  
764  C  CG  . LEU A 101 ? 0.2687 0.2782 0.2528 0.0313  -0.0027 -0.0066 101 LEU A CG  
765  C  CD1 . LEU A 101 ? 0.2755 0.2968 0.2612 0.036   -0.0058 -0.0096 101 LEU A CD1 
766  C  CD2 . LEU A 101 ? 0.2766 0.2825 0.2554 0.0288  -0.0027 -0.0029 101 LEU A CD2 
767  N  N   . SER A 102 ? 0.2259 0.2264 0.2172 0.0301  0.0042  -0.0097 102 SER A N   
768  C  CA  . SER A 102 ? 0.2263 0.2187 0.2132 0.0334  0.0031  -0.0081 102 SER A CA  
769  C  C   . SER A 102 ? 0.2341 0.2336 0.225  0.0377  0.0037  -0.0116 102 SER A C   
770  O  O   . SER A 102 ? 0.2357 0.2321 0.2229 0.0436  0.0009  -0.0111 102 SER A O   
771  C  CB  . SER A 102 ? 0.2444 0.2296 0.2291 0.0305  0.0055  -0.0066 102 SER A CB  
772  O  OG  . SER A 102 ? 0.2636 0.2452 0.2455 0.0273  0.0048  -0.0038 102 SER A OG  
773  N  N   . HIS A 103 ? 0.2252 0.2344 0.2235 0.0348  0.0075  -0.0153 103 HIS A N   
774  C  CA  . HIS A 103 ? 0.2351 0.2554 0.2393 0.0378  0.0088  -0.0194 103 HIS A CA  
775  C  C   . HIS A 103 ? 0.2365 0.2672 0.2427 0.0434  0.0042  -0.0213 103 HIS A C   
776  O  O   . HIS A 103 ? 0.2484 0.2824 0.2542 0.0505  0.0025  -0.0223 103 HIS A O   
777  C  CB  . HIS A 103 ? 0.2356 0.2642 0.2476 0.0314  0.0145  -0.0231 103 HIS A CB  
778  C  CG  . HIS A 103 ? 0.2439 0.2883 0.2643 0.0327  0.0164  -0.0283 103 HIS A CG  
779  N  ND1 . HIS A 103 ? 0.2536 0.2988 0.2734 0.037   0.0182  -0.0287 103 HIS A ND1 
780  C  CD2 . HIS A 103 ? 0.2461 0.3073 0.2761 0.0295  0.0172  -0.0338 103 HIS A CD2 
781  C  CE1 . HIS A 103 ? 0.2556 0.3191 0.2852 0.0368  0.02    -0.034  103 HIS A CE1 
782  N  NE2 . HIS A 103 ? 0.2584 0.3326 0.2947 0.032   0.0194  -0.0375 103 HIS A NE2 
783  N  N   . CYS A 104 ? 0.2343 0.2703 0.2416 0.0414  0.0021  -0.0217 104 CYS A N   
784  C  CA  . CYS A 104 ? 0.2409 0.2875 0.2485 0.0479  -0.0028 -0.023  104 CYS A CA  
785  C  C   . CYS A 104 ? 0.2502 0.284  0.2469 0.0559  -0.007  -0.0176 104 CYS A C   
786  O  O   . CYS A 104 ? 0.2491 0.2896 0.2449 0.0644  -0.0103 -0.0184 104 CYS A O   
787  C  CB  . CYS A 104 ? 0.2354 0.2909 0.2455 0.0439  -0.004  -0.0252 104 CYS A CB  
788  S  SG  . CYS A 104 ? 0.2721 0.3424 0.2949 0.0345  0.0011  -0.0331 104 CYS A SG  
789  N  N   . LEU A 105 ? 0.258  0.2737 0.2465 0.0534  -0.0066 -0.0125 105 LEU A N   
790  C  CA  . LEU A 105 ? 0.279  0.2791 0.2565 0.059   -0.0094 -0.0076 105 LEU A CA  
791  C  C   . LEU A 105 ? 0.2755 0.2718 0.2522 0.0651  -0.0089 -0.0094 105 LEU A C   
792  O  O   . LEU A 105 ? 0.2813 0.2733 0.2521 0.0742  -0.0117 -0.0083 105 LEU A O   
793  C  CB  . LEU A 105 ? 0.306  0.2905 0.2774 0.0523  -0.0082 -0.0033 105 LEU A CB  
794  C  CG  . LEU A 105 ? 0.3591 0.3438 0.3279 0.0483  -0.0089 -0.0002 105 LEU A CG  
795  C  CD1 . LEU A 105 ? 0.3717 0.3486 0.3393 0.0404  -0.0066 0.002   105 LEU A CD1 
796  C  CD2 . LEU A 105 ? 0.392  0.3683 0.3503 0.0541  -0.012  0.0045  105 LEU A CD2 
797  N  N   . LEU A 106 ? 0.2637 0.2618 0.2455 0.061   -0.0052 -0.0121 106 LEU A N   
798  C  CA  . LEU A 106 ? 0.2689 0.2659 0.2502 0.0667  -0.0041 -0.0146 106 LEU A CA  
799  C  C   . LEU A 106 ? 0.2708 0.2847 0.2579 0.075   -0.0055 -0.0184 106 LEU A C   
800  O  O   . LEU A 106 ? 0.2815 0.2913 0.2638 0.0845  -0.0073 -0.0187 106 LEU A O   
801  C  CB  . LEU A 106 ? 0.2639 0.2629 0.2497 0.0607  0.0007  -0.0168 106 LEU A CB  
802  C  CG  . LEU A 106 ? 0.2911 0.2751 0.2705 0.0548  0.0015  -0.0137 106 LEU A CG  
803  C  CD1 . LEU A 106 ? 0.2991 0.2856 0.281  0.0516  0.006   -0.0154 106 LEU A CD1 
804  C  CD2 . LEU A 106 ? 0.3175 0.2839 0.2862 0.0587  -0.0012 -0.0119 106 LEU A CD2 
805  N  N   . VAL A 107 ? 0.2595 0.293  0.257  0.0716  -0.0046 -0.0219 107 VAL A N   
806  C  CA  . VAL A 107 ? 0.257  0.3119 0.2624 0.0784  -0.0061 -0.0267 107 VAL A CA  
807  C  C   . VAL A 107 ? 0.2684 0.3211 0.266  0.0898  -0.0121 -0.0241 107 VAL A C   
808  O  O   . VAL A 107 ? 0.2767 0.337  0.2745 0.1007  -0.014  -0.026  107 VAL A O   
809  C  CB  . VAL A 107 ? 0.2566 0.3321 0.2745 0.0701  -0.0042 -0.0316 107 VAL A CB  
810  C  CG1 . VAL A 107 ? 0.2531 0.3541 0.2793 0.077   -0.0073 -0.0371 107 VAL A CG1 
811  C  CG2 . VAL A 107 ? 0.249  0.3269 0.274  0.0609  0.0028  -0.0344 107 VAL A CG2 
812  N  N   . THR A 108 ? 0.2712 0.313  0.2611 0.0878  -0.0147 -0.0192 108 THR A N   
813  C  CA  . THR A 108 ? 0.2797 0.3161 0.2594 0.0981  -0.0198 -0.0152 108 THR A CA  
814  C  C   . THR A 108 ? 0.3105 0.3251 0.2784 0.1066  -0.0202 -0.0116 108 THR A C   
815  O  O   . THR A 108 ? 0.319  0.3348 0.2818 0.1196  -0.0233 -0.0112 108 THR A O   
816  C  CB  . THR A 108 ? 0.2793 0.3064 0.2524 0.0921  -0.0209 -0.0103 108 THR A CB  
817  O  OG1 . THR A 108 ? 0.2584 0.3044 0.2422 0.0843  -0.02   -0.0148 108 THR A OG1 
818  C  CG2 . THR A 108 ? 0.2825 0.3022 0.2427 0.1026  -0.0254 -0.0049 108 THR A CG2 
819  N  N   . LEU A 109 ? 0.3249 0.3198 0.288  0.0997  -0.0172 -0.0095 109 LEU A N   
820  C  CA  . LEU A 109 ? 0.3468 0.3191 0.2982 0.106   -0.0173 -0.0073 109 LEU A CA  
821  C  C   . LEU A 109 ? 0.3547 0.3364 0.3101 0.1158  -0.0167 -0.0124 109 LEU A C   
822  O  O   . LEU A 109 ? 0.3683 0.3394 0.3145 0.1279  -0.0187 -0.0113 109 LEU A O   
823  C  CB  . LEU A 109 ? 0.3545 0.3082 0.3018 0.0952  -0.0145 -0.0056 109 LEU A CB  
824  C  CG  . LEU A 109 ? 0.3774 0.3201 0.3193 0.0866  -0.0148 -0.0002 109 LEU A CG  
825  C  CD1 . LEU A 109 ? 0.3861 0.3176 0.3272 0.0758  -0.0122 -0.0001 109 LEU A CD1 
826  C  CD2 . LEU A 109 ? 0.4035 0.3271 0.331  0.0929  -0.0171 0.0055  109 LEU A CD2 
827  N  N   . ALA A 110 ? 0.3382 0.3402 0.3069 0.1112  -0.0137 -0.0179 110 ALA A N   
828  C  CA  . ALA A 110 ? 0.3447 0.3599 0.3191 0.1194  -0.0122 -0.0233 110 ALA A CA  
829  C  C   . ALA A 110 ? 0.3485 0.3817 0.3257 0.1327  -0.0162 -0.0251 110 ALA A C   
830  O  O   . ALA A 110 ? 0.3412 0.3756 0.3156 0.1453  -0.0168 -0.0272 110 ALA A O   
831  C  CB  . ALA A 110 ? 0.3371 0.3713 0.3253 0.1097  -0.0073 -0.028  110 ALA A CB  
832  N  N   . ALA A 111 ? 0.3454 0.3941 0.328  0.1304  -0.0189 -0.0248 111 ALA A N   
833  C  CA  . ALA A 111 ? 0.3559 0.4254 0.3416 0.1429  -0.0234 -0.0269 111 ALA A CA  
834  C  C   . ALA A 111 ? 0.3947 0.4433 0.3629 0.1572  -0.0278 -0.0207 111 ALA A C   
835  O  O   . ALA A 111 ? 0.4004 0.4586 0.3672 0.1727  -0.0307 -0.0223 111 ALA A O   
836  C  CB  . ALA A 111 ? 0.346  0.4365 0.3408 0.1357  -0.0253 -0.0289 111 ALA A CB  
837  N  N   . HIS A 112 ? 0.4144 0.4356 0.3693 0.1523  -0.0281 -0.0136 112 HIS A N   
838  C  CA  . HIS A 112 ? 0.4502 0.4489 0.3869 0.1643  -0.0314 -0.0067 112 HIS A CA  
839  C  C   . HIS A 112 ? 0.4739 0.442  0.3971 0.1699  -0.0296 -0.0044 112 HIS A C   
840  O  O   . HIS A 112 ? 0.4877 0.4419 0.3976 0.1847  -0.0319 -0.0009 112 HIS A O   
841  C  CB  . HIS A 112 ? 0.4761 0.461  0.4044 0.156   -0.0322 0.0001  112 HIS A CB  
842  C  CG  . HIS A 112 ? 0.51   0.5207 0.4453 0.1559  -0.0355 -0.0012 112 HIS A CG  
843  N  ND1 . HIS A 112 ? 0.5418 0.5572 0.4681 0.17    -0.0405 0.0022  112 HIS A ND1 
844  C  CD2 . HIS A 112 ? 0.5137 0.546  0.4633 0.1437  -0.0345 -0.0058 112 HIS A CD2 
845  C  CE1 . HIS A 112 ? 0.5404 0.5816 0.4763 0.1655  -0.0427 -0.0011 112 HIS A CE1 
846  N  NE2 . HIS A 112 ? 0.5226 0.5739 0.4726 0.1494  -0.0391 -0.0062 112 HIS A NE2 
847  N  N   . LEU A 113 ? 0.4724 0.4283 0.3975 0.1586  -0.0254 -0.0062 113 LEU A N   
848  C  CA  . LEU A 113 ? 0.4808 0.4067 0.3928 0.1618  -0.0236 -0.0052 113 LEU A CA  
849  C  C   . LEU A 113 ? 0.4828 0.4174 0.403  0.1615  -0.0204 -0.0125 113 LEU A C   
850  O  O   . LEU A 113 ? 0.4838 0.4064 0.4034 0.1507  -0.0174 -0.0137 113 LEU A O   
851  C  CB  . LEU A 113 ? 0.4864 0.3862 0.3897 0.1478  -0.0217 -0.0003 113 LEU A CB  
852  C  CG  . LEU A 113 ? 0.5175 0.4034 0.4094 0.1478  -0.0236 0.0078  113 LEU A CG  
853  C  CD1 . LEU A 113 ? 0.533  0.402  0.4214 0.1312  -0.0211 0.0113  113 LEU A CD1 
854  C  CD2 . LEU A 113 ? 0.5419 0.403  0.4152 0.1632  -0.0251 0.0124  113 LEU A CD2 
855  N  N   . PRO A 114 ? 0.4801 0.4374 0.4083 0.1736  -0.021  -0.0175 114 PRO A N   
856  C  CA  . PRO A 114 ? 0.4844 0.4522 0.4206 0.1728  -0.0171 -0.0243 114 PRO A CA  
857  C  C   . PRO A 114 ? 0.5128 0.4511 0.4354 0.1755  -0.0152 -0.0251 114 PRO A C   
858  O  O   . PRO A 114 ? 0.5163 0.4571 0.4432 0.1689  -0.0115 -0.0294 114 PRO A O   
859  C  CB  . PRO A 114 ? 0.4803 0.4772 0.4256 0.1874  -0.0186 -0.029  114 PRO A CB  
860  C  CG  . PRO A 114 ? 0.4857 0.4763 0.4209 0.2007  -0.024  -0.0239 114 PRO A CG  
861  C  CD  . PRO A 114 ? 0.4625 0.4404 0.3935 0.188   -0.0251 -0.0177 114 PRO A CD  
862  N  N   . ALA A 115 ? 0.5184 0.4283 0.4238 0.1854  -0.0173 -0.0213 115 ALA A N   
863  C  CA  . ALA A 115 ? 0.533  0.412  0.4242 0.1871  -0.0154 -0.0229 115 ALA A CA  
864  C  C   . ALA A 115 ? 0.526  0.3885 0.415  0.1684  -0.0134 -0.0219 115 ALA A C   
865  O  O   . ALA A 115 ? 0.5387 0.3912 0.4244 0.1648  -0.0111 -0.0265 115 ALA A O   
866  C  CB  . ALA A 115 ? 0.5567 0.4059 0.4288 0.2008  -0.0176 -0.0185 115 ALA A CB  
867  N  N   . GLU A 116 ? 0.5022 0.3648 0.3935 0.1569  -0.0145 -0.0165 116 GLU A N   
868  C  CA  . GLU A 116 ? 0.5081 0.3586 0.3984 0.1398  -0.0129 -0.0156 116 GLU A CA  
869  C  C   . GLU A 116 ? 0.4783 0.3534 0.3839 0.1292  -0.0107 -0.0194 116 GLU A C   
870  O  O   . GLU A 116 ? 0.4873 0.3542 0.3916 0.1185  -0.0092 -0.0209 116 GLU A O   
871  C  CB  . GLU A 116 ? 0.5518 0.3939 0.4385 0.1322  -0.0144 -0.0082 116 GLU A CB  
872  C  CG  . GLU A 116 ? 0.6416 0.4596 0.5122 0.1426  -0.016  -0.0028 116 GLU A CG  
873  C  CD  . GLU A 116 ? 0.764  0.5462 0.618  0.1436  -0.0145 -0.0036 116 GLU A CD  
874  O  OE1 . GLU A 116 ? 0.8001 0.5649 0.6414 0.1584  -0.0151 -0.0023 116 GLU A OE1 
875  O  OE2 . GLU A 116 ? 0.7975 0.5687 0.6507 0.1299  -0.0127 -0.0059 116 GLU A OE2 
876  N  N   . PHE A 117 ? 0.4369 0.3414 0.3562 0.1318  -0.0104 -0.0209 117 PHE A N   
877  C  CA  . PHE A 117 ? 0.4003 0.3262 0.333  0.1217  -0.0075 -0.0234 117 PHE A CA  
878  C  C   . PHE A 117 ? 0.3886 0.3198 0.323  0.1238  -0.0041 -0.0292 117 PHE A C   
879  O  O   . PHE A 117 ? 0.3882 0.3432 0.3337 0.1263  -0.0016 -0.0326 117 PHE A O   
880  C  CB  . PHE A 117 ? 0.378  0.3315 0.3243 0.1216  -0.008  -0.0232 117 PHE A CB  
881  C  CG  . PHE A 117 ? 0.3612 0.3289 0.3183 0.1082  -0.0052 -0.0235 117 PHE A CG  
882  C  CD1 . PHE A 117 ? 0.3715 0.3298 0.3265 0.0977  -0.0058 -0.0193 117 PHE A CD1 
883  C  CD2 . PHE A 117 ? 0.356  0.3459 0.3249 0.1065  -0.0014 -0.0277 117 PHE A CD2 
884  C  CE1 . PHE A 117 ? 0.3608 0.3306 0.3246 0.0871  -0.0032 -0.0195 117 PHE A CE1 
885  C  CE2 . PHE A 117 ? 0.3507 0.3496 0.3275 0.0947  0.0017  -0.0275 117 PHE A CE2 
886  C  CZ  . PHE A 117 ? 0.3461 0.3345 0.3199 0.0858  0.0006  -0.0234 117 PHE A CZ  
887  N  N   . THR A 118 ? 0.3728 0.2826 0.2963 0.1226  -0.0037 -0.0309 118 THR A N   
888  C  CA  . THR A 118 ? 0.373  0.287  0.2963 0.1242  -0.0004 -0.0365 118 THR A CA  
889  C  C   . THR A 118 ? 0.3629 0.2901 0.2942 0.1118  0.0025  -0.0362 118 THR A C   
890  O  O   . THR A 118 ? 0.3554 0.2814 0.2893 0.1019  0.0014  -0.0322 118 THR A O   
891  C  CB  . THR A 118 ? 0.4081 0.2944 0.3161 0.1258  -0.0013 -0.0391 118 THR A CB  
892  O  OG1 . THR A 118 ? 0.4283 0.3007 0.3323 0.113   -0.0027 -0.0366 118 THR A OG1 
893  C  CG2 . THR A 118 ? 0.4232 0.2903 0.32   0.1391  -0.0035 -0.0392 118 THR A CG2 
894  N  N   . PRO A 119 ? 0.3638 0.3016 0.2974 0.1127  0.0065  -0.0402 119 PRO A N   
895  C  CA  . PRO A 119 ? 0.3543 0.301  0.2925 0.102   0.0095  -0.0391 119 PRO A CA  
896  C  C   . PRO A 119 ? 0.3559 0.2854 0.2864 0.0931  0.0069  -0.0372 119 PRO A C   
897  O  O   . PRO A 119 ? 0.3446 0.2796 0.28   0.0843  0.0072  -0.0337 119 PRO A O   
898  C  CB  . PRO A 119 ? 0.3646 0.3199 0.3017 0.1066  0.0142  -0.0438 119 PRO A CB  
899  C  CG  . PRO A 119 ? 0.3663 0.3298 0.3061 0.1192  0.0145  -0.0471 119 PRO A CG  
900  C  CD  . PRO A 119 ? 0.3567 0.3006 0.2888 0.1242  0.0089  -0.0456 119 PRO A CD  
901  N  N   . ALA A 120 ? 0.3662 0.2754 0.2848 0.0952  0.0043  -0.0399 120 ALA A N   
902  C  CA  . ALA A 120 ? 0.3762 0.2718 0.2887 0.0858  0.0017  -0.0392 120 ALA A CA  
903  C  C   . ALA A 120 ? 0.3484 0.2404 0.2644 0.0792  -0.0008 -0.0336 120 ALA A C   
904  O  O   . ALA A 120 ? 0.3423 0.2364 0.2605 0.07    -0.0015 -0.0315 120 ALA A O   
905  C  CB  . ALA A 120 ? 0.4036 0.2772 0.3028 0.0885  -0.0003 -0.0442 120 ALA A CB  
906  N  N   . VAL A 121 ? 0.3426 0.2295 0.2583 0.0847  -0.0022 -0.0313 121 VAL A N   
907  C  CA  . VAL A 121 ? 0.3478 0.2307 0.2651 0.0795  -0.0043 -0.0259 121 VAL A CA  
908  C  C   . VAL A 121 ? 0.3271 0.2309 0.2566 0.0751  -0.003  -0.0228 121 VAL A C   
909  O  O   . VAL A 121 ? 0.3205 0.2247 0.2522 0.0666  -0.0038 -0.0196 121 VAL A O   
910  C  CB  . VAL A 121 ? 0.3673 0.2366 0.2779 0.088   -0.0062 -0.0239 121 VAL A CB  
911  C  CG1 . VAL A 121 ? 0.3737 0.2446 0.2871 0.0843  -0.0077 -0.0177 121 VAL A CG1 
912  C  CG2 . VAL A 121 ? 0.3916 0.2333 0.288  0.0886  -0.0071 -0.0264 121 VAL A CG2 
913  N  N   . HIS A 122 ? 0.3133 0.235  0.2508 0.0799  -0.0005 -0.0244 122 HIS A N   
914  C  CA  . HIS A 122 ? 0.2993 0.2397 0.2481 0.075   0.0016  -0.0225 122 HIS A CA  
915  C  C   . HIS A 122 ? 0.301  0.2417 0.25   0.0659  0.0031  -0.0215 122 HIS A C   
916  O  O   . HIS A 122 ? 0.3136 0.2581 0.2668 0.0594  0.0029  -0.0183 122 HIS A O   
917  C  CB  . HIS A 122 ? 0.2963 0.2544 0.2526 0.0809  0.005   -0.0259 122 HIS A CB  
918  C  CG  . HIS A 122 ? 0.27   0.2466 0.2377 0.0752  0.0084  -0.0253 122 HIS A CG  
919  N  ND1 . HIS A 122 ? 0.2691 0.2634 0.2451 0.0782  0.0122  -0.0285 122 HIS A ND1 
920  C  CD2 . HIS A 122 ? 0.2615 0.2399 0.2327 0.0665  0.0091  -0.0224 122 HIS A CD2 
921  C  CE1 . HIS A 122 ? 0.2678 0.2725 0.2517 0.0704  0.0152  -0.0275 122 HIS A CE1 
922  N  NE2 . HIS A 122 ? 0.2622 0.2571 0.2431 0.0639  0.0133  -0.0238 122 HIS A NE2 
923  N  N   . ALA A 123 ? 0.2878 0.2243 0.2313 0.0662  0.0043  -0.0244 123 ALA A N   
924  C  CA  . ALA A 123 ? 0.2733 0.2105 0.2153 0.0597  0.0052  -0.0236 123 ALA A CA  
925  C  C   . ALA A 123 ? 0.2752 0.2037 0.2146 0.0529  0.0015  -0.0213 123 ALA A C   
926  O  O   . ALA A 123 ? 0.2708 0.2055 0.2139 0.0474  0.002   -0.0186 123 ALA A O   
927  C  CB  . ALA A 123 ? 0.2618 0.1955 0.1961 0.0627  0.0062  -0.0277 123 ALA A CB  
928  N  N   . SER A 124 ? 0.2815 0.1951 0.2142 0.0531  -0.0016 -0.0224 124 SER A N   
929  C  CA  . SER A 124 ? 0.2967 0.202  0.227  0.0454  -0.0043 -0.0207 124 SER A CA  
930  C  C   . SER A 124 ? 0.2903 0.2008 0.2267 0.0424  -0.0045 -0.0156 124 SER A C   
931  O  O   . SER A 124 ? 0.2812 0.1956 0.2202 0.0356  -0.005  -0.0135 124 SER A O   
932  C  CB  . SER A 124 ? 0.3043 0.1897 0.2249 0.046   -0.0065 -0.0232 124 SER A CB  
933  O  OG  . SER A 124 ? 0.3384 0.2187 0.2526 0.0491  -0.0064 -0.0289 124 SER A OG  
934  N  N   . LEU A 125 ? 0.2827 0.1959 0.2218 0.0481  -0.004  -0.014  125 LEU A N   
935  C  CA  . LEU A 125 ? 0.2746 0.1944 0.219  0.0462  -0.0043 -0.01   125 LEU A CA  
936  C  C   . LEU A 125 ? 0.2702 0.2053 0.223  0.0425  -0.002  -0.0092 125 LEU A C   
937  O  O   . LEU A 125 ? 0.2627 0.2012 0.2182 0.0376  -0.0023 -0.0065 125 LEU A O   
938  C  CB  . LEU A 125 ? 0.2697 0.1919 0.215  0.0544  -0.0047 -0.0098 125 LEU A CB  
939  C  CG  . LEU A 125 ? 0.3025 0.2072 0.238  0.0591  -0.0069 -0.0085 125 LEU A CG  
940  C  CD1 . LEU A 125 ? 0.3159 0.2262 0.2523 0.0699  -0.0076 -0.0091 125 LEU A CD1 
941  C  CD2 . LEU A 125 ? 0.3171 0.2135 0.2488 0.0533  -0.0081 -0.0036 125 LEU A CD2 
942  N  N   . ASP A 126 ? 0.2736 0.2167 0.2295 0.0448  0.0007  -0.0116 126 ASP A N   
943  C  CA  . ASP A 126 ? 0.2617 0.2156 0.2237 0.0415  0.0038  -0.0107 126 ASP A CA  
944  C  C   . ASP A 126 ? 0.2583 0.2103 0.2181 0.0362  0.0031  -0.009  126 ASP A C   
945  O  O   . ASP A 126 ? 0.2374 0.1943 0.2009 0.0328  0.0037  -0.0067 126 ASP A O   
946  C  CB  . ASP A 126 ? 0.2966 0.2577 0.2609 0.0446  0.0078  -0.013  126 ASP A CB  
947  C  CG  . ASP A 126 ? 0.3865 0.3561 0.3566 0.041   0.0119  -0.0116 126 ASP A CG  
948  O  OD1 . ASP A 126 ? 0.4116 0.3884 0.3883 0.04    0.0129  -0.0119 126 ASP A OD1 
949  O  OD2 . ASP A 126 ? 0.4038 0.3722 0.3711 0.0392  0.0139  -0.0104 126 ASP A OD2 
950  N  N   . LYS A 127 ? 0.2631 0.2088 0.2167 0.0357  0.0014  -0.0108 127 LYS A N   
951  C  CA  . LYS A 127 ? 0.2624 0.2093 0.2144 0.0312  0       -0.0101 127 LYS A CA  
952  C  C   . LYS A 127 ? 0.2671 0.2123 0.2207 0.026   -0.0022 -0.008  127 LYS A C   
953  O  O   . LYS A 127 ? 0.2628 0.2151 0.2194 0.0229  -0.0021 -0.0062 127 LYS A O   
954  C  CB  . LYS A 127 ? 0.2698 0.2113 0.2149 0.0314  -0.002  -0.0138 127 LYS A CB  
955  C  CG  . LYS A 127 ? 0.2645 0.2093 0.2067 0.0364  0.0007  -0.0156 127 LYS A CG  
956  C  CD  . LYS A 127 ? 0.3119 0.2513 0.246  0.0368  -0.0018 -0.0202 127 LYS A CD  
957  C  CE  . LYS A 127 ? 0.3221 0.2664 0.2547 0.0324  -0.0047 -0.0208 127 LYS A CE  
958  N  NZ  . LYS A 127 ? 0.3221 0.2622 0.2468 0.0322  -0.0076 -0.0268 127 LYS A NZ  
959  N  N   . PHE A 128 ? 0.2679 0.2034 0.2186 0.0255  -0.0039 -0.0079 128 PHE A N   
960  C  CA  . PHE A 128 ? 0.2632 0.1954 0.2138 0.0203  -0.0051 -0.0053 128 PHE A CA  
961  C  C   . PHE A 128 ? 0.2549 0.197  0.2117 0.0203  -0.0036 -0.002  128 PHE A C   
962  O  O   . PHE A 128 ? 0.2567 0.204  0.2158 0.0156  -0.0036 -0.0003 128 PHE A O   
963  C  CB  . PHE A 128 ? 0.27   0.1873 0.2143 0.0219  -0.0063 -0.0048 128 PHE A CB  
964  C  CG  . PHE A 128 ? 0.2827 0.1958 0.2257 0.0174  -0.0065 -0.0007 128 PHE A CG  
965  C  CD1 . PHE A 128 ? 0.305  0.2157 0.2468 0.0088  -0.0068 -0.0004 128 PHE A CD1 
966  C  CD2 . PHE A 128 ? 0.3031 0.2156 0.2456 0.0217  -0.0062 0.0025  128 PHE A CD2 
967  C  CE1 . PHE A 128 ? 0.314  0.2213 0.2542 0.0041  -0.006  0.0037  128 PHE A CE1 
968  C  CE2 . PHE A 128 ? 0.3137 0.2227 0.2537 0.0179  -0.006  0.0068  128 PHE A CE2 
969  C  CZ  . PHE A 128 ? 0.306  0.2118 0.2446 0.0089  -0.0054 0.0076  128 PHE A CZ  
970  N  N   . LEU A 129 ? 0.2341 0.1796 0.1935 0.0253  -0.0024 -0.0019 129 LEU A N   
971  C  CA  . LEU A 129 ? 0.2359 0.1904 0.2007 0.0249  -0.0011 -0.0001 129 LEU A CA  
972  C  C   . LEU A 129 ? 0.243  0.2057 0.2118 0.023   0.0012  -0.0003 129 LEU A C   
973  O  O   . LEU A 129 ? 0.2403 0.2081 0.2117 0.0208  0.0018  0.0013  129 LEU A O   
974  C  CB  . LEU A 129 ? 0.2304 0.1887 0.1979 0.0299  -0.0005 -0.0013 129 LEU A CB  
975  C  CG  . LEU A 129 ? 0.2588 0.2098 0.2214 0.0338  -0.003  -0.0004 129 LEU A CG  
976  C  CD1 . LEU A 129 ? 0.2726 0.2309 0.2388 0.0402  -0.0028 -0.0027 129 LEU A CD1 
977  C  CD2 . LEU A 129 ? 0.2817 0.231  0.2419 0.0313  -0.0042 0.0033  129 LEU A CD2 
978  N  N   . ALA A 130 ? 0.2414 0.2043 0.2091 0.0246  0.0024  -0.0018 130 ALA A N   
979  C  CA  . ALA A 130 ? 0.2471 0.2155 0.2162 0.0243  0.0045  -0.0011 130 ALA A CA  
980  C  C   . ALA A 130 ? 0.2373 0.2087 0.2058 0.0209  0.0023  0       130 ALA A C   
981  O  O   . ALA A 130 ? 0.2201 0.1974 0.1908 0.0209  0.0036  0.0014  130 ALA A O   
982  C  CB  . ALA A 130 ? 0.2683 0.2355 0.2342 0.0275  0.0063  -0.0023 130 ALA A CB  
983  N  N   . SER A 131 ? 0.234  0.2016 0.1995 0.018   -0.0007 -0.0011 131 SER A N   
984  C  CA  . SER A 131 ? 0.2462 0.2192 0.2125 0.0134  -0.0026 -0.001  131 SER A CA  
985  C  C   . SER A 131 ? 0.252  0.2277 0.2214 0.01    -0.0019 0.0016  131 SER A C   
986  O  O   . SER A 131 ? 0.2708 0.2562 0.2435 0.0084  -0.0016 0.0024  131 SER A O   
987  C  CB  . SER A 131 ? 0.2809 0.2477 0.2433 0.0092  -0.0054 -0.0036 131 SER A CB  
988  O  OG  . SER A 131 ? 0.3253 0.2928 0.2844 0.0121  -0.0063 -0.0065 131 SER A OG  
989  N  N   . VAL A 132 ? 0.2366 0.205  0.2045 0.0099  -0.0018 0.0028  132 VAL A N   
990  C  CA  . VAL A 132 ? 0.2333 0.2042 0.2025 0.0076  -0.001  0.0056  132 VAL A CA  
991  C  C   . VAL A 132 ? 0.2297 0.21   0.2034 0.0106  0.0012  0.0058  132 VAL A C   
992  O  O   . VAL A 132 ? 0.2341 0.222  0.21   0.0087  0.0021  0.0068  132 VAL A O   
993  C  CB  . VAL A 132 ? 0.2568 0.2187 0.2222 0.0095  -0.0015 0.007   132 VAL A CB  
994  C  CG1 . VAL A 132 ? 0.2554 0.2217 0.2212 0.0086  -0.0005 0.0098  132 VAL A CG1 
995  C  CG2 . VAL A 132 ? 0.2709 0.2198 0.23   0.0067  -0.003  0.0073  132 VAL A CG2 
996  N  N   . SER A 133 ? 0.2187 0.1982 0.1934 0.0149  0.0026  0.0043  133 SER A N   
997  C  CA  . SER A 133 ? 0.2245 0.2092 0.2023 0.0172  0.0054  0.0039  133 SER A CA  
998  C  C   . SER A 133 ? 0.2199 0.2102 0.1984 0.0181  0.0063  0.0044  133 SER A C   
999  O  O   . SER A 133 ? 0.2027 0.1977 0.1829 0.0189  0.0081  0.0048  133 SER A O   
1000 C  CB  . SER A 133 ? 0.2416 0.2231 0.22   0.0201  0.0074  0.0021  133 SER A CB  
1001 O  OG  . SER A 133 ? 0.2734 0.2532 0.2523 0.0205  0.0063  0.0012  133 SER A OG  
1002 N  N   . THR A 134 ? 0.2175 0.2082 0.1942 0.0186  0.0049  0.0041  134 THR A N   
1003 C  CA  . THR A 134 ? 0.2159 0.2144 0.1929 0.0208  0.005   0.0046  134 THR A CA  
1004 C  C   . THR A 134 ? 0.2188 0.2268 0.1991 0.0173  0.0039  0.0051  134 THR A C   
1005 O  O   . THR A 134 ? 0.2291 0.2448 0.2112 0.0202  0.0054  0.0056  134 THR A O   
1006 C  CB  . THR A 134 ? 0.2327 0.2319 0.2066 0.0221  0.0029  0.0035  134 THR A CB  
1007 O  OG1 . THR A 134 ? 0.2544 0.246  0.2248 0.0262  0.0053  0.0036  134 THR A OG1 
1008 C  CG2 . THR A 134 ? 0.2293 0.2403 0.2037 0.0251  0.0019  0.0037  134 THR A CG2 
1009 N  N   . VAL A 135 ? 0.2109 0.2177 0.1914 0.0112  0.002   0.005   135 VAL A N   
1010 C  CA  . VAL A 135 ? 0.2139 0.2298 0.1974 0.0064  0.0019  0.0057  135 VAL A CA  
1011 C  C   . VAL A 135 ? 0.2258 0.2443 0.2104 0.0081  0.0046  0.0072  135 VAL A C   
1012 O  O   . VAL A 135 ? 0.2269 0.2566 0.2145 0.0089  0.0058  0.0073  135 VAL A O   
1013 C  CB  . VAL A 135 ? 0.2265 0.2359 0.2079 -0.0013 0.0005  0.0061  135 VAL A CB  
1014 C  CG1 . VAL A 135 ? 0.2308 0.249  0.2148 -0.0073 0.0019  0.0075  135 VAL A CG1 
1015 C  CG2 . VAL A 135 ? 0.2368 0.2446 0.2169 -0.004  -0.0021 0.0033  135 VAL A CG2 
1016 N  N   . LEU A 136 ? 0.225  0.2346 0.2074 0.0092  0.0054  0.0076  136 LEU A N   
1017 C  CA  . LEU A 136 ? 0.2401 0.2521 0.2227 0.0101  0.0073  0.0081  136 LEU A CA  
1018 C  C   . LEU A 136 ? 0.2448 0.2599 0.2289 0.0154  0.0098  0.0065  136 LEU A C   
1019 O  O   . LEU A 136 ? 0.2542 0.2739 0.2386 0.0162  0.0116  0.0061  136 LEU A O   
1020 C  CB  . LEU A 136 ? 0.2505 0.2542 0.2301 0.0098  0.0066  0.0085  136 LEU A CB  
1021 C  CG  . LEU A 136 ? 0.2908 0.2922 0.2667 0.0056  0.0058  0.0114  136 LEU A CG  
1022 C  CD1 . LEU A 136 ? 0.2905 0.2877 0.265  0.0006  0.0045  0.0126  136 LEU A CD1 
1023 C  CD2 . LEU A 136 ? 0.3118 0.3062 0.2839 0.008   0.0046  0.0118  136 LEU A CD2 
1024 N  N   . THR A 137 ? 0.2354 0.2469 0.2191 0.0192  0.0103  0.0057  137 THR A N   
1025 C  CA  . THR A 137 ? 0.2366 0.2472 0.2197 0.0246  0.0133  0.0048  137 THR A CA  
1026 C  C   . THR A 137 ? 0.2528 0.2712 0.2361 0.029   0.0134  0.0057  137 THR A C   
1027 O  O   . THR A 137 ? 0.2707 0.2863 0.2519 0.035   0.0161  0.0055  137 THR A O   
1028 C  CB  . THR A 137 ? 0.2582 0.2581 0.2393 0.0263  0.015   0.004   137 THR A CB  
1029 O  OG1 . THR A 137 ? 0.2533 0.2513 0.2328 0.0268  0.0133  0.005   137 THR A OG1 
1030 C  CG2 . THR A 137 ? 0.2691 0.2647 0.2511 0.0231  0.0152  0.0022  137 THR A CG2 
1031 N  N   . SER A 138 ? 0.2239 0.2521 0.2095 0.0264  0.0105  0.0062  138 SER A N   
1032 C  CA  . SER A 138 ? 0.2373 0.2772 0.2241 0.0312  0.0097  0.0063  138 SER A CA  
1033 C  C   . SER A 138 ? 0.2491 0.3037 0.2403 0.03    0.0103  0.006   138 SER A C   
1034 O  O   . SER A 138 ? 0.2446 0.3013 0.2378 0.0231  0.0103  0.0061  138 SER A O   
1035 C  CB  . SER A 138 ? 0.2383 0.2831 0.2255 0.0285  0.006   0.0058  138 SER A CB  
1036 O  OG  . SER A 138 ? 0.2494 0.283  0.2319 0.0306  0.0055  0.006   138 SER A OG  
1037 N  N   . LYS A 139 ? 0.2444 0.3094 0.2365 0.0375  0.0111  0.0057  139 LYS A N   
1038 C  CA  . LYS A 139 ? 0.2543 0.3368 0.2513 0.0381  0.012   0.005   139 LYS A CA  
1039 C  C   . LYS A 139 ? 0.2643 0.3652 0.2662 0.037   0.0086  0.004   139 LYS A C   
1040 O  O   . LYS A 139 ? 0.2701 0.3763 0.2706 0.0456  0.0073  0.0039  139 LYS A O   
1041 C  CB  . LYS A 139 ? 0.27   0.3514 0.2641 0.0488  0.0154  0.0047  139 LYS A CB  
1042 C  CG  . LYS A 139 ? 0.3175 0.3821 0.3073 0.0479  0.0187  0.0041  139 LYS A CG  
1043 C  CD  . LYS A 139 ? 0.363  0.4199 0.348  0.0578  0.0226  0.0031  139 LYS A CD  
1044 C  CE  . LYS A 139 ? 0.3943 0.4619 0.381  0.0603  0.0249  0.0012  139 LYS A CE  
1045 N  NZ  . LYS A 139 ? 0.3942 0.4493 0.3746 0.0692  0.0291  -0.0007 139 LYS A NZ  
1046 N  N   . TYR A 140 ? 0.2523 0.3606 0.2588 0.0263  0.007   0.0032  140 TYR A N   
1047 C  CA  . TYR A 140 ? 0.251  0.3775 0.2631 0.0227  0.0036  0.001   140 TYR A CA  
1048 C  C   . TYR A 140 ? 0.2739 0.4226 0.2944 0.0163  0.0048  -0.0005 140 TYR A C   
1049 O  O   . TYR A 140 ? 0.2746 0.4397 0.3012 0.01    0.0023  -0.0032 140 TYR A O   
1050 C  CB  . TYR A 140 ? 0.2451 0.3611 0.2551 0.0146  0.0006  0.0001  140 TYR A CB  
1051 C  CG  . TYR A 140 ? 0.2302 0.3312 0.2381 0.0048  0.0023  0.0017  140 TYR A CG  
1052 C  CD1 . TYR A 140 ? 0.2324 0.3125 0.234  0.007   0.0033  0.0037  140 TYR A CD1 
1053 C  CD2 . TYR A 140 ? 0.2283 0.3358 0.24   -0.0067 0.0026  0.001   140 TYR A CD2 
1054 C  CE1 . TYR A 140 ? 0.2335 0.3007 0.2322 -0.0001 0.0042  0.0052  140 TYR A CE1 
1055 C  CE2 . TYR A 140 ? 0.2317 0.323  0.2393 -0.0143 0.0042  0.0032  140 TYR A CE2 
1056 C  CZ  . TYR A 140 ? 0.2364 0.3078 0.2371 -0.0101 0.0045  0.0054  140 TYR A CZ  
1057 O  OH  . TYR A 140 ? 0.2462 0.3029 0.2421 -0.0158 0.0057  0.0078  140 TYR A OH  
1058 N  N   . ARG A 141 ? 0.2912 0.4415 0.3121 0.0175  0.0088  0.0008  141 ARG A N   
1059 C  CA  . ARG A 141 ? 0.3155 0.4878 0.3438 0.0127  0.0113  -0.0002 141 ARG A CA  
1060 C  C   . ARG A 141 ? 0.3505 0.5487 0.3853 0.0219  0.01    -0.0029 141 ARG A C   
1061 O  O   . ARG A 141 ? 0.3756 0.5696 0.4063 0.0348  0.0085  -0.0027 141 ARG A O   
1062 C  CB  . ARG A 141 ? 0.3215 0.4879 0.3465 0.0143  0.0159  0.0017  141 ARG A CB  
1063 C  CG  . ARG A 141 ? 0.3398 0.4827 0.3578 0.0079  0.0166  0.0044  141 ARG A CG  
1064 C  CD  . ARG A 141 ? 0.3524 0.4897 0.366  0.0104  0.0205  0.0056  141 ARG A CD  
1065 N  NE  . ARG A 141 ? 0.3147 0.4657 0.3309 0.0033  0.0241  0.0066  141 ARG A NE  
1066 C  CZ  . ARG A 141 ? 0.3136 0.4596 0.3281 -0.0081 0.0251  0.0093  141 ARG A CZ  
1067 N  NH1 . ARG A 141 ? 0.3133 0.4423 0.3243 -0.0134 0.0222  0.0106  141 ARG A NH1 
1068 N  NH2 . ARG A 141 ? 0.3004 0.4584 0.3161 -0.0142 0.0294  0.0108  141 ARG A NH2 
1069 O  OXT . ARG A 141 ? 0.3693 0.5923 0.4131 0.0165  0.0109  -0.005  141 ARG A OXT 
1070 N  N   . VAL B 1   ? 0.7048 0.4913 0.6703 -0.0851 0.0723  0.0112  1   VAL B N   
1071 C  CA  . VAL B 1   ? 0.7238 0.4945 0.6707 -0.0688 0.0804  0.0084  1   VAL B CA  
1072 C  C   . VAL B 1   ? 0.7423 0.4867 0.6666 -0.0751 0.0917  0.0103  1   VAL B C   
1073 O  O   . VAL B 1   ? 0.7589 0.4792 0.6629 -0.0874 0.0893  0.0105  1   VAL B O   
1074 C  CB  . VAL B 1   ? 0.7483 0.5002 0.6698 -0.0548 0.0711  0.0025  1   VAL B CB  
1075 N  N   . HIS B 2   ? 0.7347 0.4802 0.659  -0.0675 0.1042  0.0116  2   HIS B N   
1076 C  CA  . HIS B 2   ? 0.7483 0.4677 0.6485 -0.0725 0.1159  0.0137  2   HIS B CA  
1077 C  C   . HIS B 2   ? 0.7506 0.4416 0.6159 -0.0575 0.1155  0.0105  2   HIS B C   
1078 O  O   . HIS B 2   ? 0.7557 0.4531 0.6218 -0.0467 0.1205  0.0096  2   HIS B O   
1079 C  CB  . HIS B 2   ? 0.755  0.4949 0.6785 -0.077  0.1324  0.0187  2   HIS B CB  
1080 N  N   . LEU B 3   ? 0.7466 0.4048 0.5793 -0.0573 0.1096  0.0092  3   LEU B N   
1081 C  CA  . LEU B 3   ? 0.7411 0.3731 0.5405 -0.0427 0.1079  0.008   3   LEU B CA  
1082 C  C   . LEU B 3   ? 0.7382 0.3364 0.5073 -0.0496 0.1173  0.0116  3   LEU B C   
1083 O  O   . LEU B 3   ? 0.7556 0.3395 0.5189 -0.0645 0.1195  0.0135  3   LEU B O   
1084 C  CB  . LEU B 3   ? 0.7476 0.3653 0.5306 -0.0337 0.095   0.0049  3   LEU B CB  
1085 C  CG  . LEU B 3   ? 0.7427 0.3851 0.5421 -0.0205 0.0856  0.0015  3   LEU B CG  
1086 C  CD1 . LEU B 3   ? 0.7285 0.4028 0.5633 -0.0287 0.0828  0.0004  3   LEU B CD1 
1087 C  CD2 . LEU B 3   ? 0.7698 0.3934 0.547  -0.0092 0.0766  -0.0004 3   LEU B CD2 
1088 N  N   . THR B 4   ? 0.7278 0.3107 0.4742 -0.0402 0.1217  0.0129  4   THR B N   
1089 C  CA  . THR B 4   ? 0.7466 0.2927 0.4583 -0.0451 0.1298  0.0169  4   THR B CA  
1090 C  C   . THR B 4   ? 0.7615 0.2725 0.4408 -0.0396 0.1207  0.0172  4   THR B C   
1091 O  O   . THR B 4   ? 0.7515 0.2688 0.4333 -0.027  0.1092  0.0142  4   THR B O   
1092 C  CB  . THR B 4   ? 0.7679 0.3059 0.4601 -0.0347 0.1342  0.0183  4   THR B CB  
1093 O  OG1 . THR B 4   ? 0.769  0.3051 0.449  -0.0172 0.1208  0.0169  4   THR B OG1 
1094 C  CG2 . THR B 4   ? 0.7621 0.3283 0.4797 -0.0371 0.1442  0.0172  4   THR B CG2 
1095 N  N   . PRO B 5   ? 0.7897 0.2611 0.4354 -0.0467 0.1265  0.021   5   PRO B N   
1096 C  CA  . PRO B 5   ? 0.807  0.2402 0.4181 -0.0384 0.1191  0.0215  5   PRO B CA  
1097 C  C   . PRO B 5   ? 0.7943 0.227  0.3927 -0.0134 0.1096  0.0218  5   PRO B C   
1098 O  O   . PRO B 5   ? 0.7936 0.2198 0.386  -0.0018 0.1009  0.0201  5   PRO B O   
1099 C  CB  . PRO B 5   ? 0.8507 0.2415 0.4267 -0.05   0.1291  0.0266  5   PRO B CB  
1100 C  CG  . PRO B 5   ? 0.841  0.254  0.4427 -0.071  0.141   0.0277  5   PRO B CG  
1101 C  CD  . PRO B 5   ? 0.7925 0.25   0.429  -0.0629 0.1412  0.0253  5   PRO B CD  
1102 N  N   . GLU B 6   ? 0.7816 0.2253 0.3788 -0.0057 0.111   0.024   6   GLU B N   
1103 C  CA  . GLU B 6   ? 0.7743 0.2236 0.363  0.0156  0.1004  0.0254  6   GLU B CA  
1104 C  C   . GLU B 6   ? 0.736  0.2235 0.3572 0.0238  0.0911  0.0207  6   GLU B C   
1105 O  O   . GLU B 6   ? 0.7492 0.2376 0.3644 0.0407  0.0817  0.0218  6   GLU B O   
1106 C  CB  . GLU B 6   ? 0.8087 0.2578 0.3839 0.0186  0.1027  0.0289  6   GLU B CB  
1107 C  CG  . GLU B 6   ? 0.8779 0.2822 0.4109 0.0165  0.1089  0.0351  6   GLU B CG  
1108 C  CD  . GLU B 6   ? 1.0009 0.4008 0.515  0.0187  0.1107  0.0388  6   GLU B CD  
1109 O  OE1 . GLU B 6   ? 1.025  0.4497 0.5486 0.0288  0.1013  0.0381  6   GLU B OE1 
1110 O  OE2 . GLU B 6   ? 1.0652 0.4354 0.5525 0.0092  0.1214  0.0425  6   GLU B OE2 
1111 N  N   . GLU B 7   ? 0.6884 0.2074 0.3438 0.0129  0.0941  0.0163  7   GLU B N   
1112 C  CA  . GLU B 7   ? 0.6581 0.2111 0.3432 0.0189  0.0859  0.0121  7   GLU B CA  
1113 C  C   . GLU B 7   ? 0.6561 0.1998 0.3403 0.02    0.0811  0.0099  7   GLU B C   
1114 O  O   . GLU B 7   ? 0.6424 0.1985 0.3326 0.0328  0.073   0.0084  7   GLU B O   
1115 C  CB  . GLU B 7   ? 0.6516 0.2361 0.3708 0.0073  0.0911  0.0089  7   GLU B CB  
1116 C  CG  . GLU B 7   ? 0.6988 0.2944 0.4187 0.0097  0.0945  0.0095  7   GLU B CG  
1117 C  CD  . GLU B 7   ? 0.7547 0.3766 0.5054 0.0006  0.102   0.0069  7   GLU B CD  
1118 O  OE1 . GLU B 7   ? 0.7124 0.3367 0.4772 -0.0116 0.1099  0.0074  7   GLU B OE1 
1119 O  OE2 . GLU B 7   ? 0.7993 0.4397 0.5601 0.0056  0.0999  0.005   7   GLU B OE2 
1120 N  N   . LYS B 8   ? 0.6742 0.1951 0.3491 0.0055  0.0865  0.0098  8   LYS B N   
1121 C  CA  . LYS B 8   ? 0.699  0.2039 0.3661 0.004   0.0822  0.007   8   LYS B CA  
1122 C  C   . LYS B 8   ? 0.7297 0.2025 0.3622 0.0236  0.0785  0.0093  8   LYS B C   
1123 O  O   . LYS B 8   ? 0.7337 0.2067 0.365  0.0347  0.073   0.0068  8   LYS B O   
1124 C  CB  . LYS B 8   ? 0.7447 0.2282 0.4043 -0.0185 0.0882  0.0072  8   LYS B CB  
1125 C  CG  . LYS B 8   ? 0.854  0.3305 0.5132 -0.0252 0.0822  0.003   8   LYS B CG  
1126 C  CD  . LYS B 8   ? 0.959  0.4054 0.601  -0.0482 0.0861  0.0037  8   LYS B CD  
1127 C  CE  . LYS B 8   ? 1.0337 0.4618 0.6625 -0.0527 0.079   -0.0008 8   LYS B CE  
1128 N  NZ  . LYS B 8   ? 1.0567 0.5251 0.7179 -0.0471 0.0709  -0.0048 8   LYS B NZ  
1129 N  N   . SER B 9   ? 0.7434 0.192  0.3496 0.0298  0.0819  0.0146  9   SER B N   
1130 C  CA  . SER B 9   ? 0.7727 0.1928 0.347  0.0504  0.0789  0.019   9   SER B CA  
1131 C  C   . SER B 9   ? 0.7495 0.2028 0.3415 0.0716  0.0702  0.0196  9   SER B C   
1132 O  O   . SER B 9   ? 0.7622 0.2056 0.344  0.0875  0.0672  0.0199  9   SER B O   
1133 C  CB  . SER B 9   ? 0.8103 0.2078 0.3592 0.0511  0.0832  0.0255  9   SER B CB  
1134 O  OG  . SER B 9   ? 0.877  0.2325 0.3874 0.0663  0.0826  0.0305  9   SER B OG  
1135 N  N   . ALA B 10  ? 0.722  0.214  0.3398 0.0707  0.067   0.0196  10  ALA B N   
1136 C  CA  . ALA B 10  ? 0.7149 0.2418 0.3512 0.0866  0.0584  0.0207  10  ALA B CA  
1137 C  C   . ALA B 10  ? 0.701  0.2487 0.3596 0.0885  0.0556  0.0153  10  ALA B C   
1138 O  O   . ALA B 10  ? 0.7084 0.2677 0.3696 0.106   0.0508  0.0171  10  ALA B O   
1139 C  CB  . ALA B 10  ? 0.7043 0.2619 0.3595 0.0798  0.0566  0.0207  10  ALA B CB  
1140 N  N   . VAL B 11  ? 0.6751 0.2284 0.3498 0.0707  0.059   0.0094  11  VAL B N   
1141 C  CA  . VAL B 11  ? 0.6544 0.2239 0.3468 0.0701  0.056   0.0044  11  VAL B CA  
1142 C  C   . VAL B 11  ? 0.683  0.2192 0.3486 0.0802  0.0569  0.0039  11  VAL B C   
1143 O  O   . VAL B 11  ? 0.6833 0.2314 0.3539 0.0939  0.0539  0.003   11  VAL B O   
1144 C  CB  . VAL B 11  ? 0.6422 0.2249 0.3569 0.0481  0.0583  -0.0002 11  VAL B CB  
1145 C  CG1 . VAL B 11  ? 0.6432 0.2293 0.3653 0.0448  0.0549  -0.0049 11  VAL B CG1 
1146 C  CG2 . VAL B 11  ? 0.6061 0.2262 0.3504 0.0437  0.0576  -0.0004 11  VAL B CG2 
1147 N  N   . THR B 12  ? 0.7068 0.1993 0.3421 0.0731  0.062   0.0046  12  THR B N   
1148 C  CA  . THR B 12  ? 0.7425 0.1926 0.3446 0.0807  0.0644  0.0035  12  THR B CA  
1149 C  C   . THR B 12  ? 0.7578 0.1994 0.343  0.1097  0.0639  0.0089  12  THR B C   
1150 O  O   . THR B 12  ? 0.7662 0.1918 0.337  0.1233  0.0653  0.0074  12  THR B O   
1151 C  CB  . THR B 12  ? 0.8029 0.2059 0.3734 0.0651  0.0702  0.0043  12  THR B CB  
1152 O  OG1 . THR B 12  ? 0.8099 0.2268 0.4005 0.0382  0.0708  0.0009  12  THR B OG1 
1153 C  CG2 . THR B 12  ? 0.8433 0.1932 0.3723 0.0709  0.0733  0.0026  12  THR B CG2 
1154 N  N   . ALA B 13  ? 0.7518 0.2006 0.3355 0.1194  0.0623  0.0159  13  ALA B N   
1155 C  CA  . ALA B 13  ? 0.762  0.2083 0.3332 0.1475  0.0604  0.0233  13  ALA B CA  
1156 C  C   . ALA B 13  ? 0.7389 0.2314 0.3406 0.1618  0.0556  0.0232  13  ALA B C   
1157 O  O   . ALA B 13  ? 0.7551 0.2396 0.3465 0.1834  0.0576  0.0257  13  ALA B O   
1158 C  CB  . ALA B 13  ? 0.7648 0.2125 0.3289 0.1516  0.0576  0.0313  13  ALA B CB  
1159 N  N   . LEU B 14  ? 0.6988 0.237  0.3361 0.1501  0.0506  0.0205  14  LEU B N   
1160 C  CA  . LEU B 14  ? 0.6834 0.2652 0.3492 0.1606  0.0463  0.0206  14  LEU B CA  
1161 C  C   . LEU B 14  ? 0.6802 0.2535 0.345  0.1606  0.0505  0.0139  14  LEU B C   
1162 O  O   . LEU B 14  ? 0.6667 0.2509 0.3341 0.1795  0.0517  0.0159  14  LEU B O   
1163 C  CB  . LEU B 14  ? 0.6804 0.3059 0.3795 0.1458  0.0406  0.0187  14  LEU B CB  
1164 C  CG  . LEU B 14  ? 0.702  0.3744 0.4292 0.1556  0.0349  0.0209  14  LEU B CG  
1165 C  CD1 . LEU B 14  ? 0.7159 0.4104 0.4475 0.1646  0.0277  0.0294  14  LEU B CD1 
1166 C  CD2 . LEU B 14  ? 0.7036 0.4054 0.4589 0.1379  0.0329  0.0147  14  LEU B CD2 
1167 N  N   . TRP B 15  ? 0.6909 0.2454 0.3512 0.1396  0.0529  0.0066  15  TRP B N   
1168 C  CA  . TRP B 15  ? 0.7107 0.254  0.3659 0.1364  0.0553  0       15  TRP B CA  
1169 C  C   . TRP B 15  ? 0.7592 0.2627 0.3795 0.1559  0.0617  0.0008  15  TRP B C   
1170 O  O   . TRP B 15  ? 0.7626 0.2648 0.3797 0.1622  0.0644  -0.003  15  TRP B O   
1171 C  CB  . TRP B 15  ? 0.7111 0.2378 0.3637 0.1093  0.0552  -0.0063 15  TRP B CB  
1172 C  CG  . TRP B 15  ? 0.7114 0.2432 0.3698 0.1016  0.0538  -0.0127 15  TRP B CG  
1173 C  CD1 . TRP B 15  ? 0.7498 0.2426 0.3789 0.0962  0.0563  -0.0175 15  TRP B CD1 
1174 C  CD2 . TRP B 15  ? 0.6822 0.2582 0.3742 0.0982  0.0493  -0.0147 15  TRP B CD2 
1175 N  NE1 . TRP B 15  ? 0.7408 0.252  0.3837 0.0889  0.0529  -0.0224 15  TRP B NE1 
1176 C  CE2 . TRP B 15  ? 0.7002 0.2626 0.3822 0.0905  0.0487  -0.0204 15  TRP B CE2 
1177 C  CE3 . TRP B 15  ? 0.6555 0.2778 0.3819 0.0991  0.0453  -0.0122 15  TRP B CE3 
1178 C  CZ2 . TRP B 15  ? 0.6886 0.2836 0.3951 0.0849  0.0444  -0.0231 15  TRP B CZ2 
1179 C  CZ3 . TRP B 15  ? 0.6502 0.303  0.4005 0.0934  0.0417  -0.0151 15  TRP B CZ3 
1180 C  CH2 . TRP B 15  ? 0.6563 0.2962 0.3973 0.0869  0.0412  -0.0201 15  TRP B CH2 
1181 N  N   . GLY B 16  ? 0.7912 0.2587 0.3823 0.1655  0.0651  0.0058  16  GLY B N   
1182 C  CA  . GLY B 16  ? 0.8273 0.2502 0.3805 0.1868  0.0726  0.0077  16  GLY B CA  
1183 C  C   . GLY B 16  ? 0.8278 0.278  0.3929 0.2172  0.0743  0.0137  16  GLY B C   
1184 O  O   . GLY B 16  ? 0.869  0.2908 0.4094 0.2363  0.0824  0.0136  16  GLY B O   
1185 N  N   . LYS B 17  ? 0.7832 0.2889 0.3858 0.2217  0.0674  0.0193  17  LYS B N   
1186 C  CA  . LYS B 17  ? 0.7686 0.3097 0.389  0.2484  0.068   0.0266  17  LYS B CA  
1187 C  C   . LYS B 17  ? 0.7427 0.3267 0.3943 0.2444  0.0674  0.0221  17  LYS B C   
1188 O  O   . LYS B 17  ? 0.7235 0.3425 0.394  0.2642  0.0685  0.0282  17  LYS B O   
1189 C  CB  . LYS B 17  ? 0.775  0.3522 0.4158 0.255   0.0592  0.0367  17  LYS B CB  
1190 C  CG  . LYS B 17  ? 0.8449 0.3824 0.4544 0.2623  0.0595  0.043   17  LYS B CG  
1191 C  CD  . LYS B 17  ? 0.8984 0.4735 0.5271 0.2669  0.0491  0.053   17  LYS B CD  
1192 C  CE  . LYS B 17  ? 0.9691 0.5064 0.5648 0.2815  0.0494  0.062   17  LYS B CE  
1193 N  NZ  . LYS B 17  ? 1.029  0.5684 0.624  0.2623  0.0417  0.0634  17  LYS B NZ  
1194 N  N   . VAL B 18  ? 0.7332 0.3177 0.3921 0.219   0.0653  0.0128  18  VAL B N   
1195 C  CA  . VAL B 18  ? 0.7226 0.3431 0.4076 0.2129  0.0643  0.0085  18  VAL B CA  
1196 C  C   . VAL B 18  ? 0.7661 0.369  0.433  0.2305  0.0743  0.0065  18  VAL B C   
1197 O  O   . VAL B 18  ? 0.8047 0.3548 0.4337 0.2315  0.0809  0.0019  18  VAL B O   
1198 C  CB  . VAL B 18  ? 0.7112 0.3314 0.4048 0.1826  0.0593  0.0001  18  VAL B CB  
1199 C  CG1 . VAL B 18  ? 0.6999 0.3415 0.4085 0.1767  0.0596  -0.0051 18  VAL B CG1 
1200 C  CG2 . VAL B 18  ? 0.6931 0.3419 0.4117 0.1681  0.0513  0.0025  18  VAL B CG2 
1201 N  N   . ASN B 19  ? 0.7585 0.404  0.4506 0.2433  0.076   0.0101  19  ASN B N   
1202 C  CA  . ASN B 19  ? 0.7768 0.4098 0.4538 0.2595  0.0873  0.0079  19  ASN B CA  
1203 C  C   . ASN B 19  ? 0.7849 0.4084 0.4581 0.2354  0.0856  -0.0027 19  ASN B C   
1204 O  O   . ASN B 19  ? 0.747  0.412  0.4512 0.2226  0.0799  -0.0038 19  ASN B O   
1205 C  CB  . ASN B 19  ? 0.7683 0.4556 0.4774 0.2791  0.09    0.0163  19  ASN B CB  
1206 C  CG  . ASN B 19  ? 0.8276 0.5055 0.5228 0.2979  0.1041  0.015   19  ASN B CG  
1207 O  OD1 . ASN B 19  ? 0.8502 0.4997 0.5243 0.2872  0.1085  0.0056  19  ASN B OD1 
1208 N  ND2 . ASN B 19  ? 0.84   0.5422 0.5461 0.327   0.1118  0.025   19  ASN B ND2 
1209 N  N   . VAL B 20  ? 0.8238 0.3911 0.4571 0.2283  0.0897  -0.0101 20  VAL B N   
1210 C  CA  . VAL B 20  ? 0.8466 0.399  0.4706 0.2046  0.0865  -0.0195 20  VAL B CA  
1211 C  C   . VAL B 20  ? 0.8402 0.4078 0.4668 0.2112  0.0926  -0.0221 20  VAL B C   
1212 O  O   . VAL B 20  ? 0.8298 0.3992 0.4579 0.1912  0.0874  -0.0282 20  VAL B O   
1213 C  CB  . VAL B 20  ? 0.9064 0.3929 0.4837 0.1936  0.0882  -0.026  20  VAL B CB  
1214 C  CG1 . VAL B 20  ? 0.9292 0.4011 0.5038 0.1856  0.0833  -0.023  20  VAL B CG1 
1215 C  CG2 . VAL B 20  ? 0.9431 0.3823 0.4766 0.217   0.1023  -0.0273 20  VAL B CG2 
1216 N  N   . ASP B 21  ? 0.84   0.4209 0.4684 0.2392  0.1035  -0.0166 21  ASP B N   
1217 C  CA  . ASP B 21  ? 0.8371 0.4354 0.4691 0.2466  0.1114  -0.018  21  ASP B CA  
1218 C  C   . ASP B 21  ? 0.7789 0.4448 0.4609 0.24    0.1047  -0.0133 21  ASP B C   
1219 O  O   . ASP B 21  ? 0.787  0.4688 0.4742 0.2379  0.1086  -0.0153 21  ASP B O   
1220 C  CB  . ASP B 21  ? 0.8892 0.4746 0.5029 0.2807  0.1283  -0.0133 21  ASP B CB  
1221 C  CG  . ASP B 21  ? 1.0218 0.5327 0.5782 0.2891  0.138   -0.019  21  ASP B CG  
1222 O  OD1 . ASP B 21  ? 1.0624 0.5315 0.5895 0.2654  0.1325  -0.0284 21  ASP B OD1 
1223 O  OD2 . ASP B 21  ? 1.0682 0.5622 0.608  0.3193  0.151   -0.0135 21  ASP B OD2 
1224 N  N   . GLU B 22  ? 0.7162 0.4191 0.4312 0.2372  0.0956  -0.0068 22  GLU B N   
1225 C  CA  . GLU B 22  ? 0.6591 0.4225 0.4174 0.2313  0.0899  -0.0019 22  GLU B CA  
1226 C  C   . GLU B 22  ? 0.604  0.3862 0.3849 0.2051  0.0757  -0.0038 22  GLU B C   
1227 O  O   . GLU B 22  ? 0.594  0.4067 0.3968 0.1925  0.0717  -0.0046 22  GLU B O   
1228 C  CB  . GLU B 22  ? 0.6766 0.4794 0.4588 0.2538  0.0926  0.0096  22  GLU B CB  
1229 C  CG  . GLU B 22  ? 0.7908 0.5789 0.5543 0.285   0.1082  0.0139  22  GLU B CG  
1230 C  CD  . GLU B 22  ? 0.9099 0.7234 0.6824 0.2967  0.1202  0.0157  22  GLU B CD  
1231 O  OE1 . GLU B 22  ? 0.9498 0.7687 0.7197 0.3256  0.1332  0.0227  22  GLU B OE1 
1232 O  OE2 . GLU B 22  ? 0.9298 0.7576 0.7116 0.278   0.1176  0.0107  22  GLU B OE2 
1233 N  N   . VAL B 23  ? 0.5736 0.3394 0.35   0.1984  0.0692  -0.0037 23  VAL B N   
1234 C  CA  . VAL B 23  ? 0.5397 0.3237 0.3377 0.1768  0.0579  -0.0045 23  VAL B CA  
1235 C  C   . VAL B 23  ? 0.5177 0.2998 0.3193 0.1549  0.0534  -0.0114 23  VAL B C   
1236 O  O   . VAL B 23  ? 0.4907 0.3044 0.3184 0.1427  0.0471  -0.0104 23  VAL B O   
1237 C  CB  . VAL B 23  ? 0.5534 0.3131 0.3398 0.1736  0.0542  -0.0036 23  VAL B CB  
1238 C  CG1 . VAL B 23  ? 0.5434 0.3135 0.3466 0.1505  0.0454  -0.006  23  VAL B CG1 
1239 C  CG2 . VAL B 23  ? 0.561  0.3364 0.353  0.193   0.0549  0.0054  23  VAL B CG2 
1240 N  N   . GLY B 24  ? 0.5322 0.2769 0.3065 0.1503  0.0563  -0.0176 24  GLY B N   
1241 C  CA  . GLY B 24  ? 0.5308 0.2731 0.3068 0.1302  0.0506  -0.023  24  GLY B CA  
1242 C  C   . GLY B 24  ? 0.522  0.2949 0.3138 0.1308  0.0517  -0.0221 24  GLY B C   
1243 O  O   . GLY B 24  ? 0.5054 0.3009 0.3183 0.1162  0.0447  -0.0222 24  GLY B O   
1244 N  N   . GLY B 25  ? 0.5197 0.294  0.3017 0.149   0.0617  -0.0205 25  GLY B N   
1245 C  CA  . GLY B 25  ? 0.5019 0.3059 0.2977 0.151   0.0651  -0.0187 25  GLY B CA  
1246 C  C   . GLY B 25  ? 0.4667 0.3188 0.3001 0.147   0.0599  -0.0127 25  GLY B C   
1247 O  O   . GLY B 25  ? 0.4619 0.3353 0.3099 0.1358  0.0567  -0.0126 25  GLY B O   
1248 N  N   . GLU B 26  ? 0.4478 0.3138 0.294  0.1546  0.058   -0.0076 26  GLU B N   
1249 C  CA  . GLU B 26  ? 0.4135 0.3216 0.2912 0.1488  0.0517  -0.002  26  GLU B CA  
1250 C  C   . GLU B 26  ? 0.3879 0.2954 0.2752 0.1273  0.0421  -0.0053 26  GLU B C   
1251 O  O   . GLU B 26  ? 0.3726 0.3071 0.279  0.1175  0.0383  -0.0036 26  GLU B O   
1252 C  CB  . GLU B 26  ? 0.4446 0.3657 0.3297 0.1624  0.0511  0.0048  26  GLU B CB  
1253 C  CG  . GLU B 26  ? 0.5318 0.4764 0.4231 0.1838  0.0599  0.0118  26  GLU B CG  
1254 C  CD  . GLU B 26  ? 0.6144 0.5654 0.5077 0.2013  0.0595  0.0193  26  GLU B CD  
1255 O  OE1 . GLU B 26  ? 0.6132 0.5728 0.5159 0.1927  0.0497  0.0217  26  GLU B OE1 
1256 O  OE2 . GLU B 26  ? 0.6416 0.5873 0.5251 0.2243  0.0695  0.0232  26  GLU B OE2 
1257 N  N   . ALA B 27  ? 0.3906 0.2669 0.2641 0.1198  0.0389  -0.0098 27  ALA B N   
1258 C  CA  . ALA B 27  ? 0.3894 0.2666 0.2739 0.1014  0.0314  -0.0121 27  ALA B CA  
1259 C  C   . ALA B 27  ? 0.384  0.2645 0.2715 0.0906  0.0294  -0.0148 27  ALA B C   
1260 O  O   . ALA B 27  ? 0.371  0.2703 0.2759 0.0803  0.025   -0.0136 27  ALA B O   
1261 C  CB  . ALA B 27  ? 0.4049 0.252  0.2766 0.0958  0.0295  -0.015  27  ALA B CB  
1262 N  N   . LEU B 28  ? 0.3954 0.2552 0.2633 0.0928  0.0324  -0.0181 28  LEU B N   
1263 C  CA  . LEU B 28  ? 0.4032 0.2641 0.27   0.0829  0.0298  -0.02   28  LEU B CA  
1264 C  C   . LEU B 28  ? 0.3653 0.2571 0.2466 0.0855  0.0327  -0.0162 28  LEU B C   
1265 O  O   . LEU B 28  ? 0.3506 0.2551 0.2438 0.0745  0.0281  -0.0152 28  LEU B O   
1266 C  CB  . LEU B 28  ? 0.4327 0.2617 0.2692 0.0848  0.0328  -0.0244 28  LEU B CB  
1267 C  CG  . LEU B 28  ? 0.4651 0.2922 0.2962 0.0737  0.0285  -0.026  28  LEU B CG  
1268 C  CD1 . LEU B 28  ? 0.462  0.2923 0.3079 0.0571  0.0173  -0.0256 28  LEU B CD1 
1269 C  CD2 . LEU B 28  ? 0.5083 0.3008 0.3031 0.0759  0.0321  -0.0307 28  LEU B CD2 
1270 N  N   . GLY B 29  ? 0.361  0.2654 0.242  0.1001  0.0407  -0.0132 29  GLY B N   
1271 C  CA  . GLY B 29  ? 0.344  0.2814 0.2405 0.102   0.0444  -0.0086 29  GLY B CA  
1272 C  C   . GLY B 29  ? 0.325  0.2887 0.246  0.0908  0.0373  -0.0052 29  GLY B C   
1273 O  O   . GLY B 29  ? 0.3125 0.2902 0.2421 0.0805  0.0355  -0.0038 29  GLY B O   
1274 N  N   . ARG B 30  ? 0.3158 0.2805 0.2437 0.0915  0.0333  -0.0042 30  ARG B N   
1275 C  CA  . ARG B 30  ? 0.2914 0.2742 0.2365 0.0803  0.0268  -0.0018 30  ARG B CA  
1276 C  C   . ARG B 30  ? 0.2826 0.2519 0.228  0.0659  0.0218  -0.0051 30  ARG B C   
1277 O  O   . ARG B 30  ? 0.2748 0.2575 0.2303 0.0559  0.0189  -0.0034 30  ARG B O   
1278 C  CB  . ARG B 30  ? 0.2982 0.2821 0.246  0.0848  0.0241  0.0002  30  ARG B CB  
1279 C  CG  . ARG B 30  ? 0.2967 0.3075 0.2527 0.0976  0.0266  0.0067  30  ARG B CG  
1280 C  CD  . ARG B 30  ? 0.3199 0.3283 0.2749 0.1022  0.0224  0.0092  30  ARG B CD  
1281 N  NE  . ARG B 30  ? 0.3158 0.3515 0.2796 0.1166  0.024   0.0169  30  ARG B NE  
1282 C  CZ  . ARG B 30  ? 0.3161 0.3865 0.2971 0.112   0.0185  0.0234  30  ARG B CZ  
1283 N  NH1 . ARG B 30  ? 0.2887 0.3649 0.2753 0.0929  0.0114  0.0222  30  ARG B NH1 
1284 N  NH2 . ARG B 30  ? 0.3176 0.4168 0.3096 0.1264  0.0198  0.0318  30  ARG B NH2 
1285 N  N   . LEU B 31  ? 0.287  0.2303 0.2209 0.0643  0.0206  -0.0093 31  LEU B N   
1286 C  CA  . LEU B 31  ? 0.2956 0.2305 0.2332 0.0522  0.0156  -0.0108 31  LEU B CA  
1287 C  C   . LEU B 31  ? 0.2972 0.2421 0.236  0.0472  0.0156  -0.0092 31  LEU B C   
1288 O  O   . LEU B 31  ? 0.2878 0.2384 0.2352 0.0385  0.0125  -0.0076 31  LEU B O   
1289 C  CB  . LEU B 31  ? 0.3045 0.2144 0.2301 0.0507  0.0135  -0.0143 31  LEU B CB  
1290 C  CG  . LEU B 31  ? 0.3274 0.2326 0.2597 0.0395  0.0074  -0.0142 31  LEU B CG  
1291 C  CD1 . LEU B 31  ? 0.3202 0.2288 0.2676 0.0349  0.0061  -0.0131 31  LEU B CD1 
1292 C  CD2 . LEU B 31  ? 0.3498 0.2349 0.2682 0.0361  0.0038  -0.0166 31  LEU B CD2 
1293 N  N   . LEU B 32  ? 0.3055 0.2498 0.2329 0.0534  0.0202  -0.0095 32  LEU B N   
1294 C  CA  . LEU B 32  ? 0.3134 0.2644 0.2379 0.049   0.0215  -0.0078 32  LEU B CA  
1295 C  C   . LEU B 32  ? 0.3061 0.2838 0.2449 0.0451  0.0233  -0.0033 32  LEU B C   
1296 O  O   . LEU B 32  ? 0.305  0.2863 0.2441 0.0366  0.0223  -0.0014 32  LEU B O   
1297 C  CB  . LEU B 32  ? 0.3486 0.2906 0.2542 0.0578  0.0283  -0.0093 32  LEU B CB  
1298 C  CG  . LEU B 32  ? 0.4147 0.3253 0.2992 0.0585  0.0258  -0.0142 32  LEU B CG  
1299 C  CD1 . LEU B 32  ? 0.4454 0.3424 0.3054 0.0664  0.0338  -0.0162 32  LEU B CD1 
1300 C  CD2 . LEU B 32  ? 0.4415 0.3416 0.3254 0.0459  0.0164  -0.0145 32  LEU B CD2 
1301 N  N   . VAL B 33  ? 0.2828 0.2789 0.2321 0.0503  0.0254  -0.001  33  VAL B N   
1302 C  CA  . VAL B 33  ? 0.2703 0.2942 0.2332 0.0441  0.0258  0.0038  33  VAL B CA  
1303 C  C   . VAL B 33  ? 0.2646 0.2855 0.234  0.0317  0.0189  0.0038  33  VAL B C   
1304 O  O   . VAL B 33  ? 0.2616 0.2902 0.2342 0.0203  0.0176  0.0062  33  VAL B O   
1305 C  CB  . VAL B 33  ? 0.271  0.32   0.2431 0.0551  0.03    0.0079  33  VAL B CB  
1306 C  CG1 . VAL B 33  ? 0.2667 0.3471 0.2551 0.0454  0.0274  0.0136  33  VAL B CG1 
1307 C  CG2 . VAL B 33  ? 0.27   0.3228 0.2349 0.0687  0.0399  0.0088  33  VAL B CG2 
1308 N  N   . VAL B 34  ? 0.2572 0.2647 0.2261 0.0339  0.0157  0.0011  34  VAL B N   
1309 C  CA  . VAL B 34  ? 0.2491 0.2508 0.221  0.0243  0.0113  0.0007  34  VAL B CA  
1310 C  C   . VAL B 34  ? 0.2498 0.2321 0.2182 0.0171  0.0096  -0.001  34  VAL B C   
1311 O  O   . VAL B 34  ? 0.2529 0.2321 0.2215 0.0077  0.008   -0.0002 34  VAL B O   
1312 C  CB  . VAL B 34  ? 0.2577 0.2524 0.2288 0.0296  0.01    -0.0008 34  VAL B CB  
1313 C  CG1 . VAL B 34  ? 0.2611 0.2465 0.2314 0.02    0.0072  -0.0017 34  VAL B CG1 
1314 C  CG2 . VAL B 34  ? 0.26   0.2754 0.235  0.0381  0.0107  0.0026  34  VAL B CG2 
1315 N  N   . TYR B 35  ? 0.2527 0.2208 0.2169 0.0216  0.0094  -0.003  35  TYR B N   
1316 C  CA  . TYR B 35  ? 0.2692 0.222  0.2329 0.017   0.0067  -0.0031 35  TYR B CA  
1317 C  C   . TYR B 35  ? 0.2813 0.2336 0.2379 0.0172  0.0063  -0.0021 35  TYR B C   
1318 O  O   . TYR B 35  ? 0.2889 0.2319 0.2392 0.0211  0.0049  -0.0038 35  TYR B O   
1319 C  CB  . TYR B 35  ? 0.2641 0.2038 0.2303 0.0204  0.0053  -0.0054 35  TYR B CB  
1320 C  CG  . TYR B 35  ? 0.2735 0.2127 0.2429 0.0209  0.0072  -0.0065 35  TYR B CG  
1321 C  CD1 . TYR B 35  ? 0.2905 0.2269 0.2616 0.0152  0.0079  -0.0057 35  TYR B CD1 
1322 C  CD2 . TYR B 35  ? 0.2879 0.2269 0.2547 0.0271  0.0085  -0.0082 35  TYR B CD2 
1323 C  CE1 . TYR B 35  ? 0.3031 0.2363 0.2726 0.0147  0.0096  -0.007  35  TYR B CE1 
1324 C  CE2 . TYR B 35  ? 0.2977 0.2347 0.2645 0.0272  0.0097  -0.0087 35  TYR B CE2 
1325 C  CZ  . TYR B 35  ? 0.3174 0.252  0.2852 0.0206  0.0102  -0.0082 35  TYR B CZ  
1326 O  OH  . TYR B 35  ? 0.3572 0.2869 0.3206 0.02    0.0114  -0.0089 35  TYR B OH  
1327 N  N   . PRO B 36  ? 0.284  0.2454 0.2385 0.0117  0.0079  0.0008  36  PRO B N   
1328 C  CA  . PRO B 36  ? 0.2832 0.2464 0.228  0.0128  0.01    0.0018  36  PRO B CA  
1329 C  C   . PRO B 36  ? 0.2915 0.2378 0.2272 0.0112  0.0053  0.0023  36  PRO B C   
1330 O  O   . PRO B 36  ? 0.3128 0.2557 0.2359 0.0133  0.0067  0.0019  36  PRO B O   
1331 C  CB  . PRO B 36  ? 0.295  0.2739 0.2412 0.0056  0.0135  0.0056  36  PRO B CB  
1332 C  CG  . PRO B 36  ? 0.3029 0.2817 0.2561 -0.0018 0.0111  0.0063  36  PRO B CG  
1333 C  CD  . PRO B 36  ? 0.2836 0.2548 0.2422 0.0037  0.0089  0.003   36  PRO B CD  
1334 N  N   . TRP B 37  ? 0.2778 0.2138 0.2191 0.0082  -0.0001 0.0035  37  TRP B N   
1335 C  CA  . TRP B 37  ? 0.2778 0.2015 0.2133 0.0072  -0.0066 0.0054  37  TRP B CA  
1336 C  C   . TRP B 37  ? 0.2872 0.2046 0.2173 0.011   -0.0094 0.002   37  TRP B C   
1337 O  O   . TRP B 37  ? 0.2871 0.1954 0.2076 0.0088  -0.0156 0.0032  37  TRP B O   
1338 C  CB  . TRP B 37  ? 0.2681 0.1855 0.2147 0.0059  -0.0109 0.0086  37  TRP B CB  
1339 C  CG  . TRP B 37  ? 0.2537 0.1725 0.2135 0.0093  -0.0096 0.0061  37  TRP B CG  
1340 C  CD1 . TRP B 37  ? 0.2611 0.1779 0.2281 0.0115  -0.0133 0.0053  37  TRP B CD1 
1341 C  CD2 . TRP B 37  ? 0.2542 0.1756 0.2201 0.0091  -0.0042 0.0045  37  TRP B CD2 
1342 N  NE1 . TRP B 37  ? 0.2525 0.1705 0.2296 0.0137  -0.0091 0.0033  37  TRP B NE1 
1343 C  CE2 . TRP B 37  ? 0.2604 0.18   0.2357 0.0126  -0.0038 0.0026  37  TRP B CE2 
1344 C  CE3 . TRP B 37  ? 0.2578 0.182  0.22   0.0046  -0.0002 0.0047  37  TRP B CE3 
1345 C  CZ2 . TRP B 37  ? 0.2598 0.1787 0.239  0.0131  0.001   0.0006  37  TRP B CZ2 
1346 C  CZ3 . TRP B 37  ? 0.2646 0.1882 0.2305 0.004   0.0031  0.0027  37  TRP B CZ3 
1347 C  CH2 . TRP B 37  ? 0.2635 0.1834 0.2368 0.0088  0.0039  0.0006  37  TRP B CH2 
1348 N  N   . THR B 38  ? 0.2949 0.2149 0.2288 0.0157  -0.0058 -0.0019 38  THR B N   
1349 C  CA  . THR B 38  ? 0.3171 0.226  0.2413 0.0181  -0.0078 -0.0054 38  THR B CA  
1350 C  C   . THR B 38  ? 0.3478 0.249  0.2498 0.0201  -0.0051 -0.0072 38  THR B C   
1351 O  O   . THR B 38  ? 0.3696 0.255  0.2566 0.019   -0.0087 -0.0096 38  THR B O   
1352 C  CB  . THR B 38  ? 0.3165 0.2258 0.2466 0.023   -0.004  -0.0085 38  THR B CB  
1353 O  OG1 . THR B 38  ? 0.3284 0.248  0.2567 0.0291  0.0035  -0.0092 38  THR B OG1 
1354 C  CG2 . THR B 38  ? 0.3007 0.2143 0.2495 0.0206  -0.0055 -0.0069 38  THR B CG2 
1355 N  N   . GLN B 39  ? 0.3537 0.2649 0.252  0.0219  0.0015  -0.0057 39  GLN B N   
1356 C  CA  . GLN B 39  ? 0.3622 0.2664 0.2384 0.0247  0.0066  -0.0068 39  GLN B CA  
1357 C  C   . GLN B 39  ? 0.3819 0.2693 0.2413 0.0175  -0.0015 -0.0058 39  GLN B C   
1358 O  O   . GLN B 39  ? 0.4029 0.2753 0.2374 0.0189  0.001   -0.0082 39  GLN B O   
1359 C  CB  . GLN B 39  ? 0.3538 0.2763 0.2334 0.0256  0.0152  -0.0036 39  GLN B CB  
1360 C  CG  . GLN B 39  ? 0.3474 0.2903 0.242  0.0328  0.0227  -0.0035 39  GLN B CG  
1361 C  CD  . GLN B 39  ? 0.3767 0.343  0.2803 0.0295  0.0287  0.0011  39  GLN B CD  
1362 O  OE1 . GLN B 39  ? 0.4132 0.3787 0.3065 0.0249  0.0314  0.0034  39  GLN B OE1 
1363 N  NE2 . GLN B 39  ? 0.3515 0.3393 0.2734 0.0305  0.0304  0.0029  39  GLN B NE2 
1364 N  N   . ARG B 40  ? 0.3702 0.2585 0.241  0.0106  -0.0113 -0.0018 40  ARG B N   
1365 C  CA  . ARG B 40  ? 0.4008 0.276  0.2574 0.0039  -0.0212 0.0009  40  ARG B CA  
1366 C  C   . ARG B 40  ? 0.4337 0.2915 0.2738 0.0017  -0.0273 -0.003  40  ARG B C   
1367 O  O   . ARG B 40  ? 0.4428 0.2847 0.2574 -0.0027 -0.0316 -0.0033 40  ARG B O   
1368 C  CB  . ARG B 40  ? 0.3858 0.2675 0.2618 -0.0001 -0.0303 0.007   40  ARG B CB  
1369 C  CG  . ARG B 40  ? 0.4304 0.3019 0.2932 -0.0061 -0.0421 0.0119  40  ARG B CG  
1370 C  CD  . ARG B 40  ? 0.443  0.3216 0.325  -0.0068 -0.0492 0.0197  40  ARG B CD  
1371 N  NE  . ARG B 40  ? 0.452  0.3243 0.326  -0.0116 -0.0635 0.0254  40  ARG B NE  
1372 C  CZ  . ARG B 40  ? 0.4907 0.3549 0.348  -0.0142 -0.068  0.0308  40  ARG B CZ  
1373 N  NH1 . ARG B 40  ? 0.4781 0.3392 0.3264 -0.0132 -0.0585 0.0315  40  ARG B NH1 
1374 N  NH2 . ARG B 40  ? 0.4953 0.3551 0.3456 -0.0187 -0.0828 0.0367  40  ARG B NH2 
1375 N  N   . PHE B 41  ? 0.4545 0.3129 0.3061 0.0033  -0.0277 -0.006  41  PHE B N   
1376 C  CA  . PHE B 41  ? 0.4996 0.3393 0.3345 -0.0011 -0.0334 -0.0098 41  PHE B CA  
1377 C  C   . PHE B 41  ? 0.5311 0.3499 0.3339 0.0041  -0.0243 -0.0161 41  PHE B C   
1378 O  O   . PHE B 41  ? 0.554  0.3495 0.3331 -0.0012 -0.0289 -0.0197 41  PHE B O   
1379 C  CB  . PHE B 41  ? 0.4949 0.3405 0.3508 -0.0011 -0.0344 -0.0107 41  PHE B CB  
1380 C  CG  . PHE B 41  ? 0.4974 0.3612 0.3831 -0.0048 -0.0418 -0.0045 41  PHE B CG  
1381 C  CD1 . PHE B 41  ? 0.5103 0.3747 0.4002 -0.0139 -0.055  -0.0001 41  PHE B CD1 
1382 C  CD2 . PHE B 41  ? 0.4951 0.3751 0.4034 0.001   -0.0354 -0.0025 41  PHE B CD2 
1383 C  CE1 . PHE B 41  ? 0.4984 0.3811 0.4173 -0.0144 -0.0601 0.0068  41  PHE B CE1 
1384 C  CE2 . PHE B 41  ? 0.491  0.3836 0.4233 -0.0005 -0.0401 0.0032  41  PHE B CE2 
1385 C  CZ  . PHE B 41  ? 0.4791 0.3739 0.4181 -0.0068 -0.0515 0.008   41  PHE B CZ  
1386 N  N   . PHE B 42  ? 0.5319 0.3586 0.3339 0.0144  -0.0109 -0.0171 42  PHE B N   
1387 C  CA  . PHE B 42  ? 0.5592 0.3687 0.3338 0.0233  0.0007  -0.0221 42  PHE B CA  
1388 C  C   . PHE B 42  ? 0.604  0.4149 0.3626 0.0268  0.0095  -0.0208 42  PHE B C   
1389 O  O   . PHE B 42  ? 0.61   0.4198 0.3578 0.0384  0.0236  -0.0228 42  PHE B O   
1390 C  CB  . PHE B 42  ? 0.5406 0.3609 0.3303 0.0354  0.0107  -0.0235 42  PHE B CB  
1391 C  CG  . PHE B 42  ? 0.5395 0.3558 0.3415 0.0322  0.0041  -0.0248 42  PHE B CG  
1392 C  CD1 . PHE B 42  ? 0.5663 0.3539 0.345  0.0314  0.0034  -0.0296 42  PHE B CD1 
1393 C  CD2 . PHE B 42  ? 0.5255 0.3644 0.3597 0.0296  0.0001  -0.0213 42  PHE B CD2 
1394 C  CE1 . PHE B 42  ? 0.5627 0.3468 0.3524 0.0271  -0.0017 -0.0302 42  PHE B CE1 
1395 C  CE2 . PHE B 42  ? 0.5305 0.3658 0.3752 0.0268  -0.004  -0.0222 42  PHE B CE2 
1396 C  CZ  . PHE B 42  ? 0.5394 0.3487 0.3629 0.0254  -0.0048 -0.0263 42  PHE B CZ  
1397 N  N   . GLU B 43  ? 0.6313 0.4449 0.3881 0.0175  0.0018  -0.0166 43  GLU B N   
1398 C  CA  . GLU B 43  ? 0.6736 0.4873 0.4138 0.0181  0.0092  -0.0145 43  GLU B CA  
1399 C  C   . GLU B 43  ? 0.7058 0.494  0.4074 0.0241  0.0199  -0.0195 43  GLU B C   
1400 O  O   . GLU B 43  ? 0.7247 0.5199 0.419  0.031   0.034   -0.0184 43  GLU B O   
1401 C  CB  . GLU B 43  ? 0.7335 0.5434 0.4689 0.006   -0.0039 -0.0094 43  GLU B CB  
1402 C  CG  . GLU B 43  ? 0.8231 0.6577 0.5928 0.003   -0.009  -0.0031 43  GLU B CG  
1403 C  CD  . GLU B 43  ? 0.9478 0.7779 0.7126 -0.0061 -0.021  0.0032  43  GLU B CD  
1404 O  OE1 . GLU B 43  ? 0.9923 0.8037 0.7357 -0.0124 -0.032  0.0033  43  GLU B OE1 
1405 O  OE2 . GLU B 43  ? 0.9609 0.8048 0.7416 -0.0073 -0.0199 0.0086  43  GLU B OE2 
1406 N  N   . SER B 44  ? 0.7106 0.4681 0.3858 0.021   0.0142  -0.0249 44  SER B N   
1407 C  CA  . SER B 44  ? 0.7282 0.4526 0.3591 0.0265  0.0247  -0.0307 44  SER B CA  
1408 C  C   . SER B 44  ? 0.7165 0.4409 0.3467 0.0449  0.0432  -0.0342 44  SER B C   
1409 O  O   . SER B 44  ? 0.7438 0.441  0.3371 0.0532  0.0559  -0.0386 44  SER B O   
1410 C  CB  . SER B 44  ? 0.7673 0.4549 0.3657 0.0143  0.0111  -0.0353 44  SER B CB  
1411 O  OG  . SER B 44  ? 0.8039 0.4852 0.4113 0.0155  0.008   -0.0388 44  SER B OG  
1412 N  N   . PHE B 45  ? 0.6798 0.4324 0.3478 0.0521  0.0451  -0.0319 45  PHE B N   
1413 C  CA  . PHE B 45  ? 0.675  0.4319 0.3466 0.0706  0.0607  -0.0333 45  PHE B CA  
1414 C  C   . PHE B 45  ? 0.6744 0.4551 0.3523 0.0836  0.0786  -0.0295 45  PHE B C   
1415 O  O   . PHE B 45  ? 0.6827 0.468  0.3619 0.1012  0.0928  -0.0295 45  PHE B O   
1416 C  CB  . PHE B 45  ? 0.6507 0.429  0.3583 0.0728  0.0551  -0.0315 45  PHE B CB  
1417 C  CG  . PHE B 45  ? 0.6597 0.4108 0.3565 0.0666  0.045   -0.036  45  PHE B CG  
1418 C  CD1 . PHE B 45  ? 0.6891 0.4059 0.3541 0.0536  0.0355  -0.0402 45  PHE B CD1 
1419 C  CD2 . PHE B 45  ? 0.6573 0.4169 0.3744 0.0724  0.0447  -0.0355 45  PHE B CD2 
1420 C  CE1 . PHE B 45  ? 0.7073 0.4007 0.3629 0.0456  0.0263  -0.0437 45  PHE B CE1 
1421 C  CE2 . PHE B 45  ? 0.6747 0.4091 0.3813 0.0653  0.0365  -0.0392 45  PHE B CE2 
1422 C  CZ  . PHE B 45  ? 0.6904 0.3931 0.3676 0.0513  0.0274  -0.0431 45  PHE B CZ  
1423 N  N   . GLY B 46  ? 0.6633 0.4592 0.3451 0.0753  0.0781  -0.0254 46  GLY B N   
1424 C  CA  . GLY B 46  ? 0.6523 0.4719 0.3397 0.0847  0.0953  -0.021  46  GLY B CA  
1425 C  C   . GLY B 46  ? 0.6053 0.4734 0.3382 0.0831  0.0953  -0.0136 46  GLY B C   
1426 O  O   . GLY B 46  ? 0.5926 0.4726 0.3449 0.069   0.0816  -0.0109 46  GLY B O   
1427 N  N   . ASP B 47  ? 0.5744 0.4703 0.3231 0.0975  0.1111  -0.0097 47  ASP B N   
1428 C  CA  . ASP B 47  ? 0.5385 0.4822 0.3279 0.0947  0.112   -0.002  47  ASP B CA  
1429 C  C   . ASP B 47  ? 0.5048 0.4637 0.3241 0.0923  0.0993  -0.0014 47  ASP B C   
1430 O  O   . ASP B 47  ? 0.5101 0.4696 0.3346 0.1059  0.1023  -0.0024 47  ASP B O   
1431 C  CB  . ASP B 47  ? 0.5556 0.5282 0.3546 0.1113  0.1324  0.0031  47  ASP B CB  
1432 C  CG  . ASP B 47  ? 0.5819 0.6062 0.4192 0.1052  0.1347  0.0122  47  ASP B CG  
1433 O  OD1 . ASP B 47  ? 0.5576 0.5916 0.411  0.0871  0.1207  0.0139  47  ASP B OD1 
1434 O  OD2 . ASP B 47  ? 0.6042 0.6594 0.4552 0.1183  0.1507  0.018   47  ASP B OD2 
1435 N  N   . LEU B 48  ? 0.476  0.4439 0.3116 0.0755  0.0859  0.0005  48  LEU B N   
1436 C  CA  . LEU B 48  ? 0.454  0.4359 0.3164 0.0705  0.0745  0.0015  48  LEU B CA  
1437 C  C   . LEU B 48  ? 0.4396 0.4548 0.3272 0.0584  0.0725  0.008   48  LEU B C   
1438 O  O   . LEU B 48  ? 0.4262 0.4449 0.3285 0.0488  0.0617  0.0085  48  LEU B O   
1439 C  CB  . LEU B 48  ? 0.4654 0.4182 0.3186 0.0606  0.0597  -0.0031 48  LEU B CB  
1440 C  CG  . LEU B 48  ? 0.4998 0.4151 0.3236 0.0655  0.0582  -0.0095 48  LEU B CG  
1441 C  CD1 . LEU B 48  ? 0.5141 0.4097 0.3344 0.0526  0.0426  -0.0117 48  LEU B CD1 
1442 C  CD2 . LEU B 48  ? 0.5006 0.4114 0.3246 0.08    0.0632  -0.0121 48  LEU B CD2 
1443 N  N   . SER B 49  ? 0.4415 0.4798 0.3326 0.0585  0.084   0.0132  49  SER B N   
1444 C  CA  . SER B 49  ? 0.435  0.5003 0.3443 0.0437  0.0826  0.0195  49  SER B CA  
1445 C  C   . SER B 49  ? 0.4112 0.5119 0.3514 0.0421  0.0797  0.024   49  SER B C   
1446 O  O   . SER B 49  ? 0.4143 0.5271 0.3664 0.0259  0.073   0.0273  49  SER B O   
1447 C  CB  . SER B 49  ? 0.4554 0.533  0.3567 0.0424  0.0962  0.0239  49  SER B CB  
1448 O  OG  . SER B 49  ? 0.4916 0.5884 0.3974 0.0601  0.1111  0.0259  49  SER B OG  
1449 N  N   . THR B 50  ? 0.3775 0.4919 0.3279 0.0585  0.084   0.0244  50  THR B N   
1450 C  CA  . THR B 50  ? 0.3462 0.4946 0.3246 0.0577  0.0795  0.0294  50  THR B CA  
1451 C  C   . THR B 50  ? 0.3441 0.4781 0.3217 0.0709  0.0743  0.0254  50  THR B C   
1452 O  O   . THR B 50  ? 0.3672 0.4744 0.3257 0.0849  0.0792  0.0206  50  THR B O   
1453 C  CB  . THR B 50  ? 0.3525 0.5463 0.3507 0.0662  0.0922  0.0381  50  THR B CB  
1454 O  OG1 . THR B 50  ? 0.3786 0.5669 0.3684 0.0904  0.104   0.0371  50  THR B OG1 
1455 C  CG2 . THR B 50  ? 0.3516 0.5618 0.3501 0.0536  0.1004  0.0429  50  THR B CG2 
1456 N  N   . PRO B 51  ? 0.3189 0.4724 0.3157 0.068   0.0661  0.0284  51  PRO B N   
1457 C  CA  . PRO B 51  ? 0.3234 0.4639 0.3183 0.0812  0.0622  0.0257  51  PRO B CA  
1458 C  C   . PRO B 51  ? 0.3412 0.4844 0.3315 0.1053  0.0744  0.0273  51  PRO B C   
1459 O  O   . PRO B 51  ? 0.3611 0.4709 0.3321 0.1163  0.0755  0.0217  51  PRO B O   
1460 C  CB  . PRO B 51  ? 0.3161 0.4845 0.3326 0.0728  0.0527  0.0308  51  PRO B CB  
1461 C  CG  . PRO B 51  ? 0.314  0.4902 0.335  0.05    0.0478  0.0321  51  PRO B CG  
1462 C  CD  . PRO B 51  ? 0.2967 0.4781 0.3126 0.05    0.0586  0.0336  51  PRO B CD  
1463 N  N   . ASP B 52  ? 0.3417 0.5231 0.3482 0.1134  0.0847  0.0352  52  ASP B N   
1464 C  CA  . ASP B 52  ? 0.3571 0.5409 0.3587 0.1393  0.0989  0.0376  52  ASP B CA  
1465 C  C   . ASP B 52  ? 0.39   0.5294 0.3567 0.1464  0.1087  0.0296  52  ASP B C   
1466 O  O   . ASP B 52  ? 0.4092 0.5228 0.3575 0.1653  0.1153  0.0265  52  ASP B O   
1467 C  CB  . ASP B 52  ? 0.3563 0.5942 0.3851 0.1466  0.1096  0.0488  52  ASP B CB  
1468 C  CG  . ASP B 52  ? 0.3896 0.674  0.4519 0.1455  0.1006  0.0585  52  ASP B CG  
1469 O  OD1 . ASP B 52  ? 0.3895 0.6605 0.4506 0.1423  0.0874  0.056   52  ASP B OD1 
1470 O  OD2 . ASP B 52  ? 0.3963 0.7311 0.4855 0.1464  0.1065  0.0688  52  ASP B OD2 
1471 N  N   . ALA B 53  ? 0.3925 0.5208 0.3473 0.1312  0.1096  0.0266  53  ALA B N   
1472 C  CA  . ALA B 53  ? 0.4195 0.5046 0.3381 0.1355  0.1168  0.0192  53  ALA B CA  
1473 C  C   . ALA B 53  ? 0.4348 0.4744 0.3318 0.1328  0.1056  0.0104  53  ALA B C   
1474 O  O   . ALA B 53  ? 0.4624 0.4663 0.3306 0.1443  0.1117  0.005   53  ALA B O   
1475 C  CB  . ALA B 53  ? 0.4234 0.5066 0.3338 0.1182  0.1175  0.0188  53  ALA B CB  
1476 N  N   . VAL B 54  ? 0.409  0.4493 0.3189 0.1172  0.09    0.0094  54  VAL B N   
1477 C  CA  . VAL B 54  ? 0.4243 0.4288 0.3199 0.1134  0.0796  0.0026  54  VAL B CA  
1478 C  C   . VAL B 54  ? 0.4449 0.4377 0.3346 0.1319  0.0834  0.0018  54  VAL B C   
1479 O  O   . VAL B 54  ? 0.4651 0.4192 0.3264 0.138   0.0859  -0.004  54  VAL B O   
1480 C  CB  . VAL B 54  ? 0.41   0.4223 0.3238 0.0956  0.065   0.0029  54  VAL B CB  
1481 C  CG1 . VAL B 54  ? 0.4204 0.4025 0.3246 0.0938  0.0562  -0.0025 54  VAL B CG1 
1482 C  CG2 . VAL B 54  ? 0.4098 0.4229 0.3229 0.0787  0.0609  0.0033  54  VAL B CG2 
1483 N  N   . MET B 55  ? 0.4314 0.4558 0.3454 0.14    0.0832  0.0082  55  MET B N   
1484 C  CA  . MET B 55  ? 0.4499 0.4646 0.3597 0.1576  0.0854  0.0091  55  MET B CA  
1485 C  C   . MET B 55  ? 0.4958 0.492  0.3833 0.1799  0.1009  0.0085  55  MET B C   
1486 O  O   . MET B 55  ? 0.5169 0.4818 0.3847 0.1922  0.1029  0.0057  55  MET B O   
1487 C  CB  . MET B 55  ? 0.4088 0.4659 0.3497 0.1616  0.0813  0.0178  55  MET B CB  
1488 C  CG  . MET B 55  ? 0.3806 0.4536 0.3401 0.1396  0.067   0.0183  55  MET B CG  
1489 S  SD  . MET B 55  ? 0.3973 0.4282 0.3409 0.1251  0.0554  0.0096  55  MET B SD  
1490 C  CE  . MET B 55  ? 0.3731 0.3877 0.3085 0.1417  0.0553  0.0104  55  MET B CE  
1491 N  N   . GLY B 56  ? 0.4998 0.5148 0.3894 0.1858  0.113   0.0117  56  GLY B N   
1492 C  CA  . GLY B 56  ? 0.5233 0.5214 0.3905 0.2088  0.1309  0.0116  56  GLY B CA  
1493 C  C   . GLY B 56  ? 0.5572 0.5051 0.3822 0.2045  0.1358  0.0021  56  GLY B C   
1494 O  O   . GLY B 56  ? 0.5793 0.5029 0.3775 0.2229  0.1513  0.0004  56  GLY B O   
1495 N  N   . ASN B 57  ? 0.5608 0.4911 0.3777 0.181   0.1228  -0.0037 57  ASN B N   
1496 C  CA  . ASN B 57  ? 0.5907 0.4761 0.3682 0.1732  0.1239  -0.0119 57  ASN B CA  
1497 C  C   . ASN B 57  ? 0.6252 0.4584 0.3668 0.1808  0.1244  -0.0189 57  ASN B C   
1498 O  O   . ASN B 57  ? 0.6191 0.4419 0.3657 0.1741  0.1125  -0.0206 57  ASN B O   
1499 C  CB  . ASN B 57  ? 0.5907 0.4767 0.3749 0.1468  0.1074  -0.0142 57  ASN B CB  
1500 C  CG  . ASN B 57  ? 0.6438 0.4938 0.3924 0.1362  0.1064  -0.0202 57  ASN B CG  
1501 O  OD1 . ASN B 57  ? 0.686  0.4918 0.3989 0.1381  0.1068  -0.0268 57  ASN B OD1 
1502 N  ND2 . ASN B 57  ? 0.6257 0.4919 0.3808 0.1235  0.104   -0.0178 57  ASN B ND2 
1503 N  N   . PRO B 58  ? 0.6578 0.4544 0.3598 0.1937  0.1388  -0.0231 58  PRO B N   
1504 C  CA  . PRO B 58  ? 0.6885 0.4296 0.3508 0.1997  0.14    -0.03   58  PRO B CA  
1505 C  C   . PRO B 58  ? 0.7014 0.4103 0.3474 0.1749  0.1216  -0.037  58  PRO B C   
1506 O  O   . PRO B 58  ? 0.7293 0.4104 0.3629 0.1745  0.1166  -0.0399 58  PRO B O   
1507 C  CB  . PRO B 58  ? 0.7269 0.4338 0.3462 0.2146  0.1592  -0.0337 58  PRO B CB  
1508 C  CG  . PRO B 58  ? 0.7142 0.47   0.3612 0.2253  0.1722  -0.026  58  PRO B CG  
1509 C  CD  . PRO B 58  ? 0.6598 0.4628 0.3498 0.2044  0.1565  -0.0214 58  PRO B CD  
1510 N  N   . LYS B 59  ? 0.681  0.3955 0.3286 0.1542  0.1115  -0.0385 59  LYS B N   
1511 C  CA  . LYS B 59  ? 0.6873 0.3796 0.326  0.1307  0.093   -0.0431 59  LYS B CA  
1512 C  C   . LYS B 59  ? 0.6555 0.3747 0.3329 0.1221  0.0797  -0.0397 59  LYS B C   
1513 O  O   . LYS B 59  ? 0.6632 0.3593 0.3323 0.1107  0.0692  -0.043  59  LYS B O   
1514 C  CB  . LYS B 59  ? 0.7103 0.4021 0.3396 0.1133  0.0858  -0.0442 59  LYS B CB  
1515 C  CG  . LYS B 59  ? 0.7705 0.42   0.3483 0.1175  0.0967  -0.0498 59  LYS B CG  
1516 C  CD  . LYS B 59  ? 0.8129 0.4617 0.3796 0.1003  0.0887  -0.0499 59  LYS B CD  
1517 C  CE  . LYS B 59  ? 0.8909 0.4917 0.4001 0.1019  0.098   -0.0562 59  LYS B CE  
1518 N  NZ  . LYS B 59  ? 0.9182 0.5206 0.4161 0.0866  0.091   -0.055  59  LYS B NZ  
1519 N  N   . VAL B 60  ? 0.6168 0.3831 0.3346 0.1276  0.0811  -0.0329 60  VAL B N   
1520 C  CA  . VAL B 60  ? 0.5886 0.379  0.3403 0.121   0.0704  -0.0297 60  VAL B CA  
1521 C  C   . VAL B 60  ? 0.6093 0.38   0.352  0.1331  0.0737  -0.0305 60  VAL B C   
1522 O  O   . VAL B 60  ? 0.6143 0.3722 0.3586 0.1229  0.0641  -0.0322 60  VAL B O   
1523 C  CB  . VAL B 60  ? 0.5601 0.4013 0.3508 0.1229  0.0712  -0.0225 60  VAL B CB  
1524 C  CG1 . VAL B 60  ? 0.5504 0.4112 0.3692 0.1202  0.0631  -0.0194 60  VAL B CG1 
1525 C  CG2 . VAL B 60  ? 0.558  0.4136 0.3566 0.1074  0.0656  -0.0215 60  VAL B CG2 
1526 N  N   . LYS B 61  ? 0.628  0.3939 0.359  0.1553  0.088   -0.0288 61  LYS B N   
1527 C  CA  . LYS B 61  ? 0.6567 0.3994 0.3747 0.1694  0.0922  -0.0287 61  LYS B CA  
1528 C  C   . LYS B 61  ? 0.7    0.3856 0.3772 0.1597  0.0885  -0.0366 61  LYS B C   
1529 O  O   . LYS B 61  ? 0.7101 0.3815 0.3869 0.155   0.0822  -0.0371 61  LYS B O   
1530 C  CB  . LYS B 61  ? 0.6909 0.4377 0.4019 0.1978  0.1098  -0.0246 61  LYS B CB  
1531 C  CG  . LYS B 61  ? 0.7268 0.5339 0.4802 0.2063  0.1129  -0.0154 61  LYS B CG  
1532 C  CD  . LYS B 61  ? 0.8156 0.6318 0.562  0.2287  0.1316  -0.0119 61  LYS B CD  
1533 C  CE  . LYS B 61  ? 0.8652 0.7109 0.633  0.2537  0.1396  -0.0023 61  LYS B CE  
1534 N  NZ  . LYS B 61  ? 0.8702 0.7708 0.6846 0.2449  0.1277  0.0054  61  LYS B NZ  
1535 N  N   . ALA B 62  ? 0.7214 0.3739 0.3629 0.1552  0.0922  -0.0426 62  ALA B N   
1536 C  CA  . ALA B 62  ? 0.7547 0.3516 0.3539 0.1428  0.0876  -0.0501 62  ALA B CA  
1537 C  C   . ALA B 62  ? 0.736  0.3391 0.3521 0.1159  0.0687  -0.051  62  ALA B C   
1538 O  O   . ALA B 62  ? 0.7613 0.3357 0.3629 0.1079  0.0637  -0.0534 62  ALA B O   
1539 C  CB  . ALA B 62  ? 0.7853 0.3491 0.3432 0.1409  0.0938  -0.0559 62  ALA B CB  
1540 N  N   . HIS B 63  ? 0.6892 0.3293 0.3358 0.1028  0.0592  -0.0484 63  HIS B N   
1541 C  CA  . HIS B 63  ? 0.6761 0.3265 0.3426 0.0805  0.043   -0.0478 63  HIS B CA  
1542 C  C   . HIS B 63  ? 0.6652 0.3348 0.361  0.0825  0.0406  -0.044  63  HIS B C   
1543 O  O   . HIS B 63  ? 0.6658 0.3253 0.364  0.0682  0.032   -0.0448 63  HIS B O   
1544 C  CB  . HIS B 63  ? 0.652  0.336  0.3434 0.0692  0.0348  -0.0449 63  HIS B CB  
1545 C  CG  . HIS B 63  ? 0.6534 0.3428 0.3601 0.0481  0.0192  -0.0441 63  HIS B CG  
1546 N  ND1 . HIS B 63  ? 0.6851 0.3432 0.3651 0.032   0.0103  -0.0478 63  HIS B ND1 
1547 C  CD2 . HIS B 63  ? 0.65   0.3723 0.3954 0.0416  0.012   -0.0396 63  HIS B CD2 
1548 C  CE1 . HIS B 63  ? 0.686  0.3637 0.3933 0.0169  -0.0021 -0.0445 63  HIS B CE1 
1549 N  NE2 . HIS B 63  ? 0.6619 0.3765 0.408  0.0231  -0.0005 -0.0397 63  HIS B NE2 
1550 N  N   . GLY B 64  ? 0.6468 0.3446 0.3643 0.0995  0.0483  -0.0394 64  GLY B N   
1551 C  CA  . GLY B 64  ? 0.6337 0.3479 0.3746 0.1026  0.0464  -0.0356 64  GLY B CA  
1552 C  C   . GLY B 64  ? 0.6594 0.3342 0.3742 0.1056  0.0489  -0.0378 64  GLY B C   
1553 O  O   . GLY B 64  ? 0.6527 0.3278 0.3784 0.0971  0.0433  -0.0366 64  GLY B O   
1554 N  N   . LYS B 65  ? 0.6909 0.327  0.3671 0.1165  0.0578  -0.0414 65  LYS B N   
1555 C  CA  . LYS B 65  ? 0.7301 0.3197 0.3736 0.1186  0.0609  -0.044  65  LYS B CA  
1556 C  C   . LYS B 65  ? 0.7382 0.3068 0.373  0.0919  0.0493  -0.0478 65  LYS B C   
1557 O  O   . LYS B 65  ? 0.7484 0.302  0.3803 0.0865  0.0472  -0.047  65  LYS B O   
1558 C  CB  . LYS B 65  ? 0.7947 0.3408 0.3929 0.1344  0.0735  -0.0479 65  LYS B CB  
1559 C  CG  . LYS B 65  ? 0.8637 0.423  0.4661 0.165   0.0875  -0.0428 65  LYS B CG  
1560 C  CD  . LYS B 65  ? 0.9577 0.4605 0.5081 0.182   0.1016  -0.0467 65  LYS B CD  
1561 C  CE  . LYS B 65  ? 1.0132 0.533  0.5679 0.2137  0.1176  -0.0414 65  LYS B CE  
1562 N  NZ  . LYS B 65  ? 1.0966 0.5567 0.5981 0.2328  0.1332  -0.0451 65  LYS B NZ  
1563 N  N   . LYS B 66  ? 0.7266 0.2947 0.3567 0.0751  0.0417  -0.0511 66  LYS B N   
1564 C  CA  . LYS B 66  ? 0.7299 0.2868 0.3573 0.0484  0.0288  -0.0531 66  LYS B CA  
1565 C  C   . LYS B 66  ? 0.7012 0.296  0.3724 0.0387  0.0212  -0.048  66  LYS B C   
1566 O  O   . LYS B 66  ? 0.7079 0.2891 0.3769 0.025   0.0167  -0.0479 66  LYS B O   
1567 C  CB  . LYS B 66  ? 0.7593 0.3165 0.3779 0.0348  0.021   -0.0557 66  LYS B CB  
1568 C  CG  . LYS B 66  ? 0.8619 0.3707 0.4275 0.0391  0.0277  -0.062  66  LYS B CG  
1569 C  CD  . LYS B 66  ? 0.944  0.4604 0.5043 0.0286  0.0206  -0.0634 66  LYS B CD  
1570 C  CE  . LYS B 66  ? 1.0551 0.5173 0.5579 0.0213  0.0214  -0.0704 66  LYS B CE  
1571 N  NZ  . LYS B 66  ? 1.0997 0.5689 0.6001 -0.0001 0.0065  -0.0706 66  LYS B NZ  
1572 N  N   . VAL B 67  ? 0.6618 0.3018 0.3705 0.0455  0.0209  -0.0438 67  VAL B N   
1573 C  CA  . VAL B 67  ? 0.6322 0.3052 0.3791 0.0388  0.0161  -0.0392 67  VAL B CA  
1574 C  C   . VAL B 67  ? 0.6333 0.2944 0.3775 0.0451  0.0213  -0.0377 67  VAL B C   
1575 O  O   . VAL B 67  ? 0.6307 0.2905 0.3838 0.0319  0.0174  -0.0365 67  VAL B O   
1576 C  CB  . VAL B 67  ? 0.6085 0.324  0.3875 0.0468  0.0166  -0.0356 67  VAL B CB  
1577 C  CG1 . VAL B 67  ? 0.5994 0.3424 0.4117 0.0417  0.0136  -0.0316 67  VAL B CG1 
1578 C  CG2 . VAL B 67  ? 0.5998 0.3253 0.3804 0.0394  0.0111  -0.0362 67  VAL B CG2 
1579 N  N   . LEU B 68  ? 0.6371 0.2892 0.3684 0.0653  0.0305  -0.037  68  LEU B N   
1580 C  CA  . LEU B 68  ? 0.6565 0.2946 0.3811 0.0735  0.0352  -0.0346 68  LEU B CA  
1581 C  C   . LEU B 68  ? 0.6914 0.2841 0.3848 0.0609  0.0345  -0.0377 68  LEU B C   
1582 O  O   . LEU B 68  ? 0.6912 0.2782 0.3882 0.0546  0.0342  -0.0355 68  LEU B O   
1583 C  CB  . LEU B 68  ? 0.6661 0.2997 0.378  0.0995  0.0448  -0.0326 68  LEU B CB  
1584 C  CG  . LEU B 68  ? 0.6959 0.3261 0.4077 0.1116  0.0484  -0.0278 68  LEU B CG  
1585 C  CD1 . LEU B 68  ? 0.6714 0.3482 0.4209 0.1129  0.0446  -0.0227 68  LEU B CD1 
1586 C  CD2 . LEU B 68  ? 0.7228 0.3331 0.4106 0.1367  0.0581  -0.0259 68  LEU B CD2 
1587 N  N   . GLY B 69  ? 0.7142 0.2742 0.376  0.0553  0.0343  -0.0427 69  GLY B N   
1588 C  CA  . GLY B 69  ? 0.7602 0.2739 0.388  0.0396  0.0324  -0.0462 69  GLY B CA  
1589 C  C   . GLY B 69  ? 0.7662 0.297  0.4177 0.0138  0.0224  -0.0445 69  GLY B C   
1590 O  O   . GLY B 69  ? 0.786  0.2947 0.4266 0.0028  0.0226  -0.0438 69  GLY B O   
1591 N  N   . ALA B 70  ? 0.7324 0.305  0.4187 0.0053  0.0146  -0.0428 70  ALA B N   
1592 C  CA  . ALA B 70  ? 0.7218 0.3178 0.4368 -0.0159 0.0063  -0.0397 70  ALA B CA  
1593 C  C   . ALA B 70  ? 0.7104 0.3264 0.451  -0.0121 0.0109  -0.0351 70  ALA B C   
1594 O  O   . ALA B 70  ? 0.7274 0.3391 0.4726 -0.0278 0.0094  -0.0332 70  ALA B O   
1595 C  CB  . ALA B 70  ? 0.703  0.3356 0.4461 -0.0224 -0.0024 -0.0381 70  ALA B CB  
1596 N  N   . PHE B 71  ? 0.6805 0.3168 0.4356 0.0074  0.0168  -0.0332 71  PHE B N   
1597 C  CA  . PHE B 71  ? 0.6655 0.3153 0.4382 0.0109  0.0212  -0.0292 71  PHE B CA  
1598 C  C   . PHE B 71  ? 0.6916 0.302  0.4346 0.0103  0.0266  -0.0292 71  PHE B C   
1599 O  O   . PHE B 71  ? 0.6841 0.296  0.4356 0.0016  0.0286  -0.0264 71  PHE B O   
1600 C  CB  . PHE B 71  ? 0.6434 0.3179 0.4307 0.0305  0.0249  -0.0271 71  PHE B CB  
1601 C  CG  . PHE B 71  ? 0.609  0.3248 0.4315 0.028   0.0212  -0.0253 71  PHE B CG  
1602 C  CD1 . PHE B 71  ? 0.5951 0.3304 0.4413 0.0218  0.0219  -0.0223 71  PHE B CD1 
1603 C  CD2 . PHE B 71  ? 0.6046 0.3365 0.4334 0.0327  0.0184  -0.0264 71  PHE B CD2 
1604 C  CE1 . PHE B 71  ? 0.5753 0.3427 0.4495 0.0209  0.0196  -0.0207 71  PHE B CE1 
1605 C  CE2 . PHE B 71  ? 0.5833 0.3486 0.4409 0.0308  0.0154  -0.0244 71  PHE B CE2 
1606 C  CZ  . PHE B 71  ? 0.561  0.3426 0.4404 0.0252  0.016   -0.0217 71  PHE B CZ  
1607 N  N   . SER B 72  ? 0.7219 0.2947 0.4278 0.02    0.0301  -0.0321 72  SER B N   
1608 C  CA  . SER B 72  ? 0.7632 0.2905 0.4339 0.0206  0.0355  -0.0322 72  SER B CA  
1609 C  C   . SER B 72  ? 0.7836 0.2922 0.4461 -0.0071 0.0311  -0.0333 72  SER B C   
1610 O  O   . SER B 72  ? 0.7921 0.2821 0.4451 -0.0145 0.0347  -0.031  72  SER B O   
1611 C  CB  . SER B 72  ? 0.8039 0.2927 0.4349 0.0375  0.0408  -0.0354 72  SER B CB  
1612 O  OG  . SER B 72  ? 0.8872 0.3235 0.478  0.035   0.0455  -0.0361 72  SER B OG  
1613 N  N   . ASP B 73  ? 0.7865 0.2999 0.4516 -0.0231 0.0231  -0.0362 73  ASP B N   
1614 C  CA  . ASP B 73  ? 0.8019 0.3053 0.4641 -0.0519 0.0165  -0.0361 73  ASP B CA  
1615 C  C   . ASP B 73  ? 0.7815 0.3234 0.4853 -0.0635 0.0163  -0.0302 73  ASP B C   
1616 O  O   . ASP B 73  ? 0.7946 0.3229 0.4932 -0.0819 0.0168  -0.0281 73  ASP B O   
1617 C  CB  . ASP B 73  ? 0.8166 0.3219 0.4744 -0.0658 0.0059  -0.0395 73  ASP B CB  
1618 C  CG  . ASP B 73  ? 0.9301 0.3878 0.5383 -0.0576 0.0079  -0.046  73  ASP B CG  
1619 O  OD1 . ASP B 73  ? 0.9643 0.3848 0.5406 -0.0413 0.018   -0.0476 73  ASP B OD1 
1620 O  OD2 . ASP B 73  ? 0.9756 0.432  0.5753 -0.0666 0       -0.0491 73  ASP B OD2 
1621 N  N   . GLY B 74  ? 0.7454 0.3307 0.4863 -0.0513 0.0174  -0.0275 74  GLY B N   
1622 C  CA  . GLY B 74  ? 0.7205 0.3393 0.4974 -0.057  0.0201  -0.0222 74  GLY B CA  
1623 C  C   . GLY B 74  ? 0.7292 0.3273 0.4921 -0.053  0.0298  -0.0201 74  GLY B C   
1624 O  O   . GLY B 74  ? 0.7206 0.327  0.4976 -0.0666 0.0332  -0.0162 74  GLY B O   
1625 N  N   . LEU B 75  ? 0.7423 0.313  0.4766 -0.034  0.0347  -0.0218 75  LEU B N   
1626 C  CA  . LEU B 75  ? 0.7608 0.3057 0.475  -0.0289 0.0428  -0.0191 75  LEU B CA  
1627 C  C   . LEU B 75  ? 0.7796 0.2846 0.4656 -0.0485 0.0445  -0.019  75  LEU B C   
1628 O  O   . LEU B 75  ? 0.7929 0.283  0.4697 -0.0519 0.0513  -0.0155 75  LEU B O   
1629 C  CB  . LEU B 75  ? 0.7872 0.3115 0.4761 -0.0031 0.0462  -0.0197 75  LEU B CB  
1630 C  CG  . LEU B 75  ? 0.8008 0.3626 0.5144 0.0159  0.0449  -0.0188 75  LEU B CG  
1631 C  CD1 . LEU B 75  ? 0.8259 0.3696 0.5159 0.0403  0.0479  -0.0178 75  LEU B CD1 
1632 C  CD2 . LEU B 75  ? 0.7983 0.391  0.54   0.0136  0.0469  -0.0151 75  LEU B CD2 
1633 N  N   . ALA B 76  ? 0.7897 0.2742 0.458  -0.0623 0.0385  -0.0226 76  ALA B N   
1634 C  CA  . ALA B 76  ? 0.8197 0.2646 0.4589 -0.0848 0.0388  -0.0227 76  ALA B CA  
1635 C  C   . ALA B 76  ? 0.8089 0.2854 0.4817 -0.1122 0.0359  -0.0184 76  ALA B C   
1636 O  O   . ALA B 76  ? 0.8097 0.2628 0.4672 -0.1312 0.039   -0.016  76  ALA B O   
1637 C  CB  . ALA B 76  ? 0.8389 0.2454 0.441  -0.0904 0.0331  -0.0286 76  ALA B CB  
1638 N  N   . HIS B 77  ? 0.7945 0.3241 0.5129 -0.1138 0.0306  -0.0165 77  HIS B N   
1639 C  CA  . HIS B 77  ? 0.7904 0.3556 0.5452 -0.137  0.028   -0.0112 77  HIS B CA  
1640 C  C   . HIS B 77  ? 0.7567 0.3724 0.5581 -0.1265 0.0333  -0.0067 77  HIS B C   
1641 O  O   . HIS B 77  ? 0.7212 0.3788 0.5601 -0.1321 0.0275  -0.0039 77  HIS B O   
1642 C  CB  . HIS B 77  ? 0.8144 0.3908 0.5757 -0.1546 0.0139  -0.0123 77  HIS B CB  
1643 C  CG  . HIS B 77  ? 0.9046 0.4272 0.6158 -0.1682 0.0087  -0.0172 77  HIS B CG  
1644 N  ND1 . HIS B 77  ? 0.9615 0.4468 0.6447 -0.1871 0.0128  -0.016  77  HIS B ND1 
1645 C  CD2 . HIS B 77  ? 0.9452 0.4418 0.6264 -0.165  0.0012  -0.0235 77  HIS B CD2 
1646 C  CE1 . HIS B 77  ? 0.9981 0.4342 0.6341 -0.1952 0.0072  -0.0218 77  HIS B CE1 
1647 N  NE2 . HIS B 77  ? 0.9984 0.4394 0.6312 -0.182  0.0005  -0.0266 77  HIS B NE2 
1648 N  N   . LEU B 78  ? 0.7686 0.378  0.5653 -0.1117 0.0443  -0.0056 78  LEU B N   
1649 C  CA  . LEU B 78  ? 0.7573 0.4066 0.5903 -0.1012 0.0507  -0.0023 78  LEU B CA  
1650 C  C   . LEU B 78  ? 0.749  0.4342 0.6205 -0.1186 0.0543  0.0042  78  LEU B C   
1651 O  O   . LEU B 78  ? 0.7286 0.4526 0.6356 -0.1114 0.0561  0.0066  78  LEU B O   
1652 C  CB  . LEU B 78  ? 0.7725 0.4032 0.5867 -0.0846 0.0607  -0.0022 78  LEU B CB  
1653 C  CG  . LEU B 78  ? 0.8026 0.4182 0.5954 -0.0616 0.0574  -0.0065 78  LEU B CG  
1654 C  CD1 . LEU B 78  ? 0.8226 0.4166 0.5929 -0.0483 0.0653  -0.0049 78  LEU B CD1 
1655 C  CD2 . LEU B 78  ? 0.7856 0.4389 0.6075 -0.0501 0.0522  -0.0079 78  LEU B CD2 
1656 N  N   . ASP B 79  ? 0.7652 0.4381 0.63   -0.1414 0.0553  0.0073  79  ASP B N   
1657 C  CA  . ASP B 79  ? 0.7596 0.4697 0.663  -0.1589 0.0594  0.0149  79  ASP B CA  
1658 C  C   . ASP B 79  ? 0.7419 0.4847 0.6741 -0.1746 0.0456  0.0178  79  ASP B C   
1659 O  O   . ASP B 79  ? 0.7289 0.5063 0.6958 -0.1907 0.0472  0.0254  79  ASP B O   
1660 C  CB  . ASP B 79  ? 0.8117 0.4974 0.6973 -0.1775 0.069   0.0185  79  ASP B CB  
1661 C  CG  . ASP B 79  ? 0.9176 0.572  0.7747 -0.1629 0.0822  0.0172  79  ASP B CG  
1662 O  OD1 . ASP B 79  ? 0.9291 0.5952 0.7938 -0.1406 0.0866  0.0155  79  ASP B OD1 
1663 O  OD2 . ASP B 79  ? 0.9738 0.5905 0.799  -0.1748 0.0876  0.0182  79  ASP B OD2 
1664 N  N   . ASN B 80  ? 0.737  0.4705 0.6554 -0.1698 0.0322  0.0125  80  ASN B N   
1665 C  CA  . ASN B 80  ? 0.7182 0.4806 0.6598 -0.1836 0.0173  0.0153  80  ASN B CA  
1666 C  C   . ASN B 80  ? 0.713  0.4715 0.6443 -0.1677 0.0074  0.0094  80  ASN B C   
1667 O  O   . ASN B 80  ? 0.7142 0.4555 0.6244 -0.1781 -0.0054 0.0061  80  ASN B O   
1668 C  CB  . ASN B 80  ? 0.7489 0.4943 0.6743 -0.2146 0.0082  0.017   80  ASN B CB  
1669 C  CG  . ASN B 80  ? 0.7661 0.556  0.7286 -0.2321 -0.0062 0.0238  80  ASN B CG  
1670 O  OD1 . ASN B 80  ? 0.7585 0.5876 0.7548 -0.2192 -0.0106 0.0266  80  ASN B OD1 
1671 N  ND2 . ASN B 80  ? 0.7841 0.5687 0.7405 -0.2625 -0.0144 0.0273  80  ASN B ND2 
1672 N  N   . LEU B 81  ? 0.7021 0.4746 0.6458 -0.1433 0.0138  0.0079  81  LEU B N   
1673 C  CA  . LEU B 81  ? 0.7143 0.4875 0.652  -0.1273 0.0065  0.0031  81  LEU B CA  
1674 C  C   . LEU B 81  ? 0.7015 0.5081 0.6664 -0.1361 -0.007  0.0072  81  LEU B C   
1675 O  O   . LEU B 81  ? 0.7132 0.5071 0.6593 -0.1355 -0.0175 0.003   81  LEU B O   
1676 C  CB  . LEU B 81  ? 0.7081 0.4922 0.6559 -0.103  0.0163  0.0019  81  LEU B CB  
1677 C  CG  . LEU B 81  ? 0.7492 0.4991 0.6658 -0.0924 0.0267  -0.0019 81  LEU B CG  
1678 C  CD1 . LEU B 81  ? 0.751  0.5155 0.6802 -0.0732 0.0354  -0.0018 81  LEU B CD1 
1679 C  CD2 . LEU B 81  ? 0.7767 0.488  0.6522 -0.0865 0.0219  -0.0084 81  LEU B CD2 
1680 N  N   . LYS B 82  ? 0.6784 0.5268 0.6862 -0.1443 -0.0066 0.0159  82  LYS B N   
1681 C  CA  . LYS B 82  ? 0.6705 0.5548 0.7077 -0.1518 -0.0203 0.0219  82  LYS B CA  
1682 C  C   . LYS B 82  ? 0.69   0.5567 0.704  -0.1748 -0.0367 0.0207  82  LYS B C   
1683 O  O   . LYS B 82  ? 0.6934 0.561  0.7004 -0.174  -0.0495 0.0191  82  LYS B O   
1684 C  CB  . LYS B 82  ? 0.6655 0.5988 0.7543 -0.1559 -0.0155 0.033   82  LYS B CB  
1685 N  N   . GLY B 83  ? 0.7033 0.5496 0.7007 -0.1954 -0.0358 0.0209  83  GLY B N   
1686 C  CA  . GLY B 83  ? 0.7278 0.5502 0.6964 -0.2203 -0.0508 0.0191  83  GLY B CA  
1687 C  C   . GLY B 83  ? 0.7661 0.5347 0.6794 -0.2125 -0.0534 0.0078  83  GLY B C   
1688 O  O   . GLY B 83  ? 0.786  0.5417 0.6784 -0.2237 -0.0679 0.0054  83  GLY B O   
1689 N  N   . THR B 84  ? 0.7767 0.5144 0.6656 -0.1927 -0.0392 0.0013  84  THR B N   
1690 C  CA  . THR B 84  ? 0.8147 0.503  0.6531 -0.1814 -0.0387 -0.0084 84  THR B CA  
1691 C  C   . THR B 84  ? 0.8001 0.5019 0.6423 -0.1659 -0.0453 -0.0109 84  THR B C   
1692 O  O   . THR B 84  ? 0.8262 0.4998 0.6342 -0.1702 -0.0534 -0.0161 84  THR B O   
1693 C  CB  . THR B 84  ? 0.8646 0.5247 0.683  -0.1626 -0.0224 -0.0122 84  THR B CB  
1694 O  OG1 . THR B 84  ? 0.895  0.5417 0.7087 -0.1789 -0.0165 -0.0092 84  THR B OG1 
1695 C  CG2 . THR B 84  ? 0.9114 0.521  0.6788 -0.1492 -0.0201 -0.0209 84  THR B CG2 
1696 N  N   . PHE B 85  ? 0.7571 0.5002 0.6388 -0.1494 -0.0416 -0.0069 85  PHE B N   
1697 C  CA  . PHE B 85  ? 0.7406 0.4977 0.6276 -0.135  -0.0468 -0.0083 85  PHE B CA  
1698 C  C   . PHE B 85  ? 0.715  0.5048 0.6266 -0.1483 -0.0627 -0.002  85  PHE B C   
1699 O  O   . PHE B 85  ? 0.702  0.5071 0.6221 -0.1363 -0.0665 -0.0017 85  PHE B O   
1700 C  CB  . PHE B 85  ? 0.7153 0.494  0.6258 -0.1106 -0.0352 -0.0076 85  PHE B CB  
1701 C  CG  . PHE B 85  ? 0.7397 0.4867 0.6215 -0.0942 -0.0231 -0.0138 85  PHE B CG  
1702 C  CD1 . PHE B 85  ? 0.7728 0.4933 0.6221 -0.0825 -0.0229 -0.0202 85  PHE B CD1 
1703 C  CD2 . PHE B 85  ? 0.742  0.487  0.6296 -0.0898 -0.0116 -0.0125 85  PHE B CD2 
1704 C  CE1 . PHE B 85  ? 0.7981 0.4942 0.6248 -0.0656 -0.0121 -0.0242 85  PHE B CE1 
1705 C  CE2 . PHE B 85  ? 0.7682 0.4853 0.6294 -0.0745 -0.0022 -0.0168 85  PHE B CE2 
1706 C  CZ  . PHE B 85  ? 0.7861 0.4808 0.6188 -0.062  -0.0029 -0.0222 85  PHE B CZ  
1707 N  N   . ALA B 86  ? 0.7012 0.5019 0.6234 -0.1733 -0.0725 0.0036  86  ALA B N   
1708 C  CA  . ALA B 86  ? 0.6897 0.5256 0.638  -0.1869 -0.0895 0.0115  86  ALA B CA  
1709 C  C   . ALA B 86  ? 0.7083 0.5289 0.6294 -0.1854 -0.1019 0.0076  86  ALA B C   
1710 O  O   . ALA B 86  ? 0.6915 0.544  0.6384 -0.1772 -0.1083 0.013   86  ALA B O   
1711 C  CB  . ALA B 86  ? 0.6891 0.532  0.6436 -0.2177 -0.0997 0.0173  86  ALA B CB  
1712 N  N   . THR B 87  ? 0.7399 0.5095 0.607  -0.1921 -0.104  -0.0016 87  THR B N   
1713 C  CA  . THR B 87  ? 0.7565 0.5056 0.5909 -0.1914 -0.1138 -0.0062 87  THR B CA  
1714 C  C   . THR B 87  ? 0.7306 0.4881 0.5712 -0.163  -0.1045 -0.0086 87  THR B C   
1715 O  O   . THR B 87  ? 0.7216 0.496  0.5692 -0.1608 -0.1141 -0.0054 87  THR B O   
1716 C  CB  . THR B 87  ? 0.8281 0.5157 0.5999 -0.2035 -0.1147 -0.0159 87  THR B CB  
1717 O  OG1 . THR B 87  ? 0.8574 0.5417 0.6231 -0.2356 -0.1296 -0.0123 87  THR B OG1 
1718 C  CG2 . THR B 87  ? 0.8611 0.5193 0.5921 -0.1955 -0.1177 -0.0227 87  THR B CG2 
1719 N  N   . LEU B 88  ? 0.7156 0.462  0.5536 -0.1426 -0.0868 -0.0132 88  LEU B N   
1720 C  CA  . LEU B 88  ? 0.7032 0.4591 0.5481 -0.1175 -0.0776 -0.0151 88  LEU B CA  
1721 C  C   . LEU B 88  ? 0.6551 0.4596 0.5488 -0.1112 -0.0801 -0.0066 88  LEU B C   
1722 O  O   . LEU B 88  ? 0.6499 0.4647 0.5475 -0.0992 -0.0806 -0.0061 88  LEU B O   
1723 C  CB  . LEU B 88  ? 0.7182 0.4579 0.5548 -0.0993 -0.06   -0.0201 88  LEU B CB  
1724 C  CG  . LEU B 88  ? 0.7775 0.4686 0.5643 -0.0927 -0.0529 -0.0288 88  LEU B CG  
1725 C  CD1 . LEU B 88  ? 0.7887 0.4749 0.5767 -0.072  -0.0371 -0.0309 88  LEU B CD1 
1726 C  CD2 . LEU B 88  ? 0.7877 0.4653 0.5484 -0.0869 -0.0563 -0.0327 88  LEU B CD2 
1727 N  N   . SER B 89  ? 0.6238 0.4568 0.5537 -0.1185 -0.0802 0.0005  89  SER B N   
1728 C  CA  . SER B 89  ? 0.5958 0.473  0.572  -0.1112 -0.0808 0.0093  89  SER B CA  
1729 C  C   . SER B 89  ? 0.5735 0.4684 0.5569 -0.1185 -0.0978 0.0153  89  SER B C   
1730 O  O   . SER B 89  ? 0.5517 0.4636 0.5494 -0.1051 -0.098  0.0185  89  SER B O   
1731 C  CB  . SER B 89  ? 0.606  0.508  0.6163 -0.1194 -0.077  0.0161  89  SER B CB  
1732 O  OG  . SER B 89  ? 0.6369 0.5794 0.6902 -0.1098 -0.0759 0.0249  89  SER B OG  
1733 N  N   . GLU B 90  ? 0.5776 0.4637 0.5451 -0.1405 -0.1126 0.0165  90  GLU B N   
1734 C  CA  . GLU B 90  ? 0.5803 0.479  0.5479 -0.1505 -0.1314 0.0222  90  GLU B CA  
1735 C  C   . GLU B 90  ? 0.5972 0.4706 0.5304 -0.1391 -0.1313 0.0158  90  GLU B C   
1736 O  O   . GLU B 90  ? 0.587  0.4799 0.5332 -0.1325 -0.1383 0.0215  90  GLU B O   
1737 C  CB  . GLU B 90  ? 0.6114 0.4995 0.5616 -0.1794 -0.1474 0.0235  90  GLU B CB  
1738 N  N   . LEU B 91  ? 0.6207 0.4516 0.5111 -0.135  -0.1219 0.0046  91  LEU B N   
1739 C  CA  . LEU B 91  ? 0.6431 0.4506 0.5009 -0.1231 -0.1184 -0.0016 91  LEU B CA  
1740 C  C   . LEU B 91  ? 0.611  0.4424 0.495  -0.101  -0.1086 0.001   91  LEU B C   
1741 O  O   . LEU B 91  ? 0.6044 0.443  0.4867 -0.0973 -0.1147 0.0041  91  LEU B O   
1742 C  CB  . LEU B 91  ? 0.6889 0.4494 0.5009 -0.1192 -0.1066 -0.013  91  LEU B CB  
1743 C  CG  . LEU B 91  ? 0.7379 0.4767 0.5192 -0.1034 -0.0984 -0.0193 91  LEU B CG  
1744 C  CD1 . LEU B 91  ? 0.7678 0.4924 0.5197 -0.115  -0.1123 -0.0191 91  LEU B CD1 
1745 C  CD2 . LEU B 91  ? 0.7694 0.4693 0.5154 -0.0941 -0.0835 -0.0287 91  LEU B CD2 
1746 N  N   . HIS B 92  ? 0.589  0.4298 0.4937 -0.0879 -0.0939 -0.0001 92  HIS B N   
1747 C  CA  . HIS B 92  ? 0.5714 0.4304 0.4965 -0.0694 -0.0845 0.0016  92  HIS B CA  
1748 C  C   . HIS B 92  ? 0.5704 0.4649 0.5334 -0.0678 -0.0914 0.012   92  HIS B C   
1749 O  O   . HIS B 92  ? 0.5632 0.4656 0.5325 -0.0559 -0.0878 0.0137  92  HIS B O   
1750 C  CB  . HIS B 92  ? 0.5529 0.41   0.4861 -0.0576 -0.0683 -0.0022 92  HIS B CB  
1751 C  CG  . HIS B 92  ? 0.5711 0.3958 0.469  -0.0519 -0.0593 -0.0111 92  HIS B CG  
1752 N  ND1 . HIS B 92  ? 0.6004 0.3978 0.4733 -0.0619 -0.06   -0.0154 92  HIS B ND1 
1753 C  CD2 . HIS B 92  ? 0.583  0.4002 0.4687 -0.0368 -0.0489 -0.0154 92  HIS B CD2 
1754 C  CE1 . HIS B 92  ? 0.6197 0.3922 0.4651 -0.0502 -0.0497 -0.0221 92  HIS B CE1 
1755 N  NE2 . HIS B 92  ? 0.6145 0.4006 0.4684 -0.035  -0.043  -0.0219 92  HIS B NE2 
1756 N  N   . CYS B 93  ? 0.5799 0.4962 0.5684 -0.0795 -0.1008 0.0196  93  CYS B N   
1757 C  CA  . CYS B 93  ? 0.5857 0.5371 0.612  -0.0754 -0.1068 0.0309  93  CYS B CA  
1758 C  C   . CYS B 93  ? 0.5984 0.5558 0.6182 -0.0849 -0.1258 0.0373  93  CYS B C   
1759 O  O   . CYS B 93  ? 0.5949 0.5551 0.6131 -0.0755 -0.128  0.0404  93  CYS B O   
1760 C  CB  . CYS B 93  ? 0.5951 0.5743 0.6603 -0.0786 -0.1037 0.0377  93  CYS B CB  
1761 S  SG  . CYS B 93  ? 0.6733 0.6981 0.7867 -0.0738 -0.1123 0.0539  93  CYS B SG  
1762 N  N   . ASP B 94  ? 0.6111 0.5696 0.6257 -0.1048 -0.1403 0.0398  94  ASP B N   
1763 C  CA  . ASP B 94  ? 0.6315 0.598  0.6404 -0.1163 -0.161  0.0472  94  ASP B CA  
1764 C  C   . ASP B 94  ? 0.661  0.5945 0.6241 -0.1152 -0.1643 0.0405  94  ASP B C   
1765 O  O   . ASP B 94  ? 0.6629 0.6049 0.625  -0.1148 -0.1764 0.0475  94  ASP B O   
1766 C  CB  . ASP B 94  ? 0.6694 0.6427 0.6794 -0.1413 -0.1768 0.0509  94  ASP B CB  
1767 C  CG  . ASP B 94  ? 0.74   0.7462 0.7944 -0.145  -0.1723 0.0576  94  ASP B CG  
1768 O  OD1 . ASP B 94  ? 0.7394 0.7656 0.8262 -0.1268 -0.1577 0.0606  94  ASP B OD1 
1769 O  OD2 . ASP B 94  ? 0.788  0.7986 0.8428 -0.1672 -0.183  0.06    94  ASP B OD2 
1770 N  N   . LYS B 95  ? 0.679  0.5748 0.6034 -0.114  -0.153  0.0277  95  LYS B N   
1771 C  CA  . LYS B 95  ? 0.7037 0.5679 0.5832 -0.1126 -0.154  0.0215  95  LYS B CA  
1772 C  C   . LYS B 95  ? 0.69   0.5502 0.5675 -0.0919 -0.1378 0.0179  95  LYS B C   
1773 O  O   . LYS B 95  ? 0.699  0.5558 0.5631 -0.088  -0.1416 0.0202  95  LYS B O   
1774 C  CB  . LYS B 95  ? 0.7656 0.5875 0.5972 -0.1247 -0.1532 0.0108  95  LYS B CB  
1775 C  CG  . LYS B 95  ? 0.8561 0.6451 0.6392 -0.1245 -0.1546 0.0053  95  LYS B CG  
1776 C  CD  . LYS B 95  ? 0.9497 0.692  0.6841 -0.1267 -0.1447 -0.0072 95  LYS B CD  
1777 C  CE  . LYS B 95  ? 1.024  0.7346 0.7113 -0.1236 -0.1425 -0.0124 95  LYS B CE  
1778 N  NZ  . LYS B 95  ? 1.0495 0.7582 0.7197 -0.1412 -0.1642 -0.0067 95  LYS B NZ  
1779 N  N   . LEU B 96  ? 0.665  0.5252 0.554  -0.0799 -0.1205 0.0127  96  LEU B N   
1780 C  CA  . LEU B 96  ? 0.65   0.5068 0.5356 -0.0628 -0.1057 0.0091  96  LEU B CA  
1781 C  C   . LEU B 96  ? 0.6056 0.4907 0.5279 -0.0513 -0.1018 0.0163  96  LEU B C   
1782 O  O   . LEU B 96  ? 0.6143 0.4969 0.5311 -0.0408 -0.0935 0.0151  96  LEU B O   
1783 C  CB  . LEU B 96  ? 0.6622 0.5014 0.5351 -0.0556 -0.0899 -0.0002 96  LEU B CB  
1784 C  CG  . LEU B 96  ? 0.7161 0.5198 0.5468 -0.0634 -0.0902 -0.0082 96  LEU B CG  
1785 C  CD1 . LEU B 96  ? 0.7352 0.5246 0.5598 -0.056  -0.0761 -0.015  96  LEU B CD1 
1786 C  CD2 . LEU B 96  ? 0.7436 0.5261 0.5377 -0.0611 -0.0897 -0.0115 96  LEU B CD2 
1787 N  N   . HIS B 97  ? 0.5564 0.4671 0.5145 -0.0531 -0.1066 0.0239  97  HIS B N   
1788 C  CA  . HIS B 97  ? 0.5225 0.4558 0.5131 -0.0412 -0.1015 0.0309  97  HIS B CA  
1789 C  C   . HIS B 97  ? 0.4899 0.4181 0.4826 -0.0286 -0.0836 0.0248  97  HIS B C   
1790 O  O   . HIS B 97  ? 0.4814 0.4131 0.4797 -0.0191 -0.0783 0.0272  97  HIS B O   
1791 C  CB  . HIS B 97  ? 0.5424 0.481  0.5316 -0.0383 -0.1108 0.0387  97  HIS B CB  
1792 C  CG  . HIS B 97  ? 0.578  0.5249 0.5669 -0.0509 -0.1304 0.0462  97  HIS B CG  
1793 N  ND1 . HIS B 97  ? 0.5932 0.5644 0.6122 -0.0578 -0.1386 0.0533  97  HIS B ND1 
1794 C  CD2 . HIS B 97  ? 0.6112 0.5452 0.572  -0.0588 -0.1433 0.0476  97  HIS B CD2 
1795 C  CE1 . HIS B 97  ? 0.6036 0.5778 0.6132 -0.0706 -0.1577 0.0591  97  HIS B CE1 
1796 N  NE2 . HIS B 97  ? 0.6174 0.5679 0.5905 -0.0715 -0.1615 0.0558  97  HIS B NE2 
1797 N  N   . VAL B 98  ? 0.4633 0.3818 0.4497 -0.0296 -0.0752 0.0176  98  VAL B N   
1798 C  CA  . VAL B 98  ? 0.4368 0.3522 0.4253 -0.019  -0.0603 0.0127  98  VAL B CA  
1799 C  C   . VAL B 98  ? 0.4133 0.3467 0.4336 -0.0143 -0.0549 0.0175  98  VAL B C   
1800 O  O   . VAL B 98  ? 0.404  0.3451 0.4391 -0.0196 -0.0557 0.0193  98  VAL B O   
1801 C  CB  . VAL B 98  ? 0.4405 0.3374 0.4083 -0.0198 -0.0533 0.0042  98  VAL B CB  
1802 C  CG1 . VAL B 98  ? 0.4306 0.3279 0.4018 -0.0089 -0.0399 0.0007  98  VAL B CG1 
1803 C  CG2 . VAL B 98  ? 0.4595 0.3354 0.3929 -0.0232 -0.0569 -0.0006 98  VAL B CG2 
1804 N  N   . ASP B 99  ? 0.3986 0.3369 0.4282 -0.0047 -0.0482 0.0196  99  ASP B N   
1805 C  CA  . ASP B 99  ? 0.3805 0.3303 0.4351 0.0014  -0.0403 0.0233  99  ASP B CA  
1806 C  C   . ASP B 99  ? 0.3773 0.3213 0.4303 0.001   -0.0306 0.0173  99  ASP B C   
1807 O  O   . ASP B 99  ? 0.3799 0.3105 0.4131 0.0021  -0.0261 0.0104  99  ASP B O   
1808 C  CB  . ASP B 99  ? 0.3871 0.3342 0.4425 0.0106  -0.0335 0.0247  99  ASP B CB  
1809 C  CG  . ASP B 99  ? 0.4235 0.3791 0.502  0.0175  -0.0252 0.029   99  ASP B CG  
1810 O  OD1 . ASP B 99  ? 0.4285 0.3983 0.5275 0.0201  -0.0297 0.0375  99  ASP B OD1 
1811 O  OD2 . ASP B 99  ? 0.4511 0.3995 0.5268 0.0204  -0.0142 0.0242  99  ASP B OD2 
1812 N  N   . PRO B 100 ? 0.3727 0.3276 0.4463 -0.0008 -0.0278 0.0206  100 PRO B N   
1813 C  CA  . PRO B 100 ? 0.3728 0.3196 0.4417 -0.0026 -0.0192 0.0155  100 PRO B CA  
1814 C  C   . PRO B 100 ? 0.3602 0.2958 0.419  0.0055  -0.0074 0.0104  100 PRO B C   
1815 O  O   . PRO B 100 ? 0.3604 0.2851 0.4069 0.0044  -0.0025 0.0055  100 PRO B O   
1816 C  CB  . PRO B 100 ? 0.3798 0.344  0.4762 -0.006  -0.0172 0.0219  100 PRO B CB  
1817 C  CG  . PRO B 100 ? 0.3699 0.3532 0.4887 -0.0017 -0.0222 0.0307  100 PRO B CG  
1818 C  CD  . PRO B 100 ? 0.3553 0.3319 0.4576 -0.0018 -0.0326 0.0302  100 PRO B CD  
1819 N  N   . GLU B 101 ? 0.3431 0.2792 0.4036 0.0127  -0.0038 0.0116  101 GLU B N   
1820 C  CA  . GLU B 101 ? 0.3516 0.2769 0.3996 0.0175  0.0049  0.007   101 GLU B CA  
1821 C  C   . GLU B 101 ? 0.3457 0.2622 0.3718 0.016   0.0024  0.0012  101 GLU B C   
1822 O  O   . GLU B 101 ? 0.3501 0.2599 0.3666 0.0178  0.0079  -0.0025 101 GLU B O   
1823 C  CB  . GLU B 101 ? 0.3856 0.3096 0.4356 0.0229  0.0078  0.0096  101 GLU B CB  
1824 C  CG  . GLU B 101 ? 0.4543 0.3666 0.4885 0.0245  0.0146  0.005   101 GLU B CG  
1825 C  CD  . GLU B 101 ? 0.544  0.4492 0.5767 0.0259  0.0242  0.0026  101 GLU B CD  
1826 O  OE1 . GLU B 101 ? 0.558  0.4677 0.6051 0.0271  0.0284  0.0052  101 GLU B OE1 
1827 O  OE2 . GLU B 101 ? 0.5748 0.471  0.592  0.0251  0.0274  -0.0013 101 GLU B OE2 
1828 N  N   . ASN B 102 ? 0.3285 0.2452 0.3463 0.0132  -0.0057 0.001   102 ASN B N   
1829 C  CA  . ASN B 102 ? 0.3269 0.2358 0.3245 0.014   -0.0062 -0.0038 102 ASN B CA  
1830 C  C   . ASN B 102 ? 0.3405 0.2394 0.3289 0.0133  -0.0039 -0.0073 102 ASN B C   
1831 O  O   . ASN B 102 ? 0.3482 0.2409 0.3223 0.0179  -0.0006 -0.0106 102 ASN B O   
1832 C  CB  . ASN B 102 ? 0.3162 0.224  0.304  0.0115  -0.0137 -0.0031 102 ASN B CB  
1833 C  CG  . ASN B 102 ? 0.3422 0.2566 0.3352 0.0127  -0.015  0.0006  102 ASN B CG  
1834 O  OD1 . ASN B 102 ? 0.3202 0.2358 0.31   0.0155  -0.0099 -0.0003 102 ASN B OD1 
1835 N  ND2 . ASN B 102 ? 0.338  0.2565 0.3389 0.0099  -0.0222 0.0056  102 ASN B ND2 
1836 N  N   . PHE B 103 ? 0.3355 0.2335 0.3324 0.0077  -0.0053 -0.0057 103 PHE B N   
1837 C  CA  . PHE B 103 ? 0.3493 0.234  0.3353 0.0055  -0.0026 -0.0085 103 PHE B CA  
1838 C  C   . PHE B 103 ? 0.3504 0.2323 0.3357 0.0113  0.0064  -0.0098 103 PHE B C   
1839 O  O   . PHE B 103 ? 0.3623 0.2315 0.3311 0.0147  0.0093  -0.0127 103 PHE B O   
1840 C  CB  . PHE B 103 ? 0.3563 0.2443 0.3551 -0.0044 -0.0057 -0.0053 103 PHE B CB  
1841 C  CG  . PHE B 103 ? 0.3805 0.2729 0.3808 -0.0125 -0.0167 -0.0029 103 PHE B CG  
1842 C  CD1 . PHE B 103 ? 0.4176 0.297  0.3949 -0.0129 -0.0221 -0.0063 103 PHE B CD1 
1843 C  CD2 . PHE B 103 ? 0.3796 0.2886 0.403  -0.0202 -0.0218 0.0033  103 PHE B CD2 
1844 C  CE1 . PHE B 103 ? 0.4331 0.3135 0.4071 -0.0218 -0.0333 -0.0041 103 PHE B CE1 
1845 C  CE2 . PHE B 103 ? 0.3946 0.3086 0.4182 -0.029  -0.0342 0.0064  103 PHE B CE2 
1846 C  CZ  . PHE B 103 ? 0.4114 0.3093 0.4085 -0.0304 -0.0404 0.0024  103 PHE B CZ  
1847 N  N   . ARG B 104 ? 0.3325 0.2241 0.3332 0.0128  0.0109  -0.0073 104 ARG B N   
1848 C  CA  . ARG B 104 ? 0.3464 0.2333 0.3428 0.0169  0.0187  -0.0086 104 ARG B CA  
1849 C  C   . ARG B 104 ? 0.3442 0.2303 0.3266 0.0223  0.0177  -0.0111 104 ARG B C   
1850 O  O   . ARG B 104 ? 0.3473 0.2269 0.3182 0.0256  0.0206  -0.0125 104 ARG B O   
1851 C  CB  . ARG B 104 ? 0.3669 0.2604 0.3783 0.0178  0.0243  -0.0059 104 ARG B CB  
1852 C  CG  . ARG B 104 ? 0.4592 0.3433 0.4629 0.0198  0.0333  -0.0073 104 ARG B CG  
1853 C  CD  . ARG B 104 ? 0.5129 0.397  0.5242 0.0221  0.0408  -0.0057 104 ARG B CD  
1854 N  NE  . ARG B 104 ? 0.5826 0.4679 0.5898 0.0238  0.0376  -0.0061 104 ARG B NE  
1855 C  CZ  . ARG B 104 ? 0.6231 0.5014 0.614  0.0234  0.0378  -0.0089 104 ARG B CZ  
1856 N  NH1 . ARG B 104 ? 0.6458 0.5157 0.623  0.0229  0.0405  -0.0111 104 ARG B NH1 
1857 N  NH2 . ARG B 104 ? 0.599  0.4786 0.5865 0.0225  0.0346  -0.0088 104 ARG B NH2 
1858 N  N   . LEU B 105 ? 0.3313 0.2257 0.3154 0.0229  0.0135  -0.0105 105 LEU B N   
1859 C  CA  . LEU B 105 ? 0.3333 0.2324 0.3081 0.0266  0.0128  -0.0116 105 LEU B CA  
1860 C  C   . LEU B 105 ? 0.3359 0.2301 0.2973 0.0316  0.0121  -0.0133 105 LEU B C   
1861 O  O   . LEU B 105 ? 0.3451 0.2414 0.2998 0.0365  0.0138  -0.0134 105 LEU B O   
1862 C  CB  . LEU B 105 ? 0.3267 0.2346 0.3054 0.0249  0.0094  -0.0101 105 LEU B CB  
1863 C  CG  . LEU B 105 ? 0.3259 0.2346 0.3144 0.022   0.011   -0.0078 105 LEU B CG  
1864 C  CD1 . LEU B 105 ? 0.3333 0.2469 0.322  0.0202  0.0074  -0.0057 105 LEU B CD1 
1865 C  CD2 . LEU B 105 ? 0.3422 0.2474 0.326  0.0216  0.0158  -0.0088 105 LEU B CD2 
1866 N  N   . LEU B 106 ? 0.3283 0.2144 0.2843 0.0305  0.0095  -0.0144 106 LEU B N   
1867 C  CA  . LEU B 106 ? 0.3365 0.2113 0.2753 0.0364  0.0105  -0.0163 106 LEU B CA  
1868 C  C   . LEU B 106 ? 0.3469 0.2096 0.278  0.0396  0.0143  -0.0167 106 LEU B C   
1869 O  O   . LEU B 106 ? 0.3533 0.2129 0.2731 0.0487  0.0165  -0.0166 106 LEU B O   
1870 C  CB  . LEU B 106 ? 0.3507 0.2128 0.2799 0.0319  0.0067  -0.0179 106 LEU B CB  
1871 C  CG  . LEU B 106 ? 0.395  0.2369 0.3006 0.0377  0.0089  -0.0207 106 LEU B CG  
1872 C  CD1 . LEU B 106 ? 0.402  0.2513 0.3007 0.0503  0.0134  -0.0204 106 LEU B CD1 
1873 C  CD2 . LEU B 106 ? 0.4202 0.2487 0.313  0.0308  0.0041  -0.0226 106 LEU B CD2 
1874 N  N   . GLY B 107 ? 0.3424 0.1999 0.2802 0.0331  0.0156  -0.0162 107 GLY B N   
1875 C  CA  . GLY B 107 ? 0.3553 0.1996 0.2839 0.035   0.0198  -0.016  107 GLY B CA  
1876 C  C   . GLY B 107 ? 0.3639 0.2162 0.2911 0.0414  0.0216  -0.0147 107 GLY B C   
1877 O  O   . GLY B 107 ? 0.3939 0.2372 0.3076 0.0483  0.023   -0.0139 107 GLY B O   
1878 N  N   . ASN B 108 ? 0.3364 0.2045 0.2755 0.039   0.0208  -0.0139 108 ASN B N   
1879 C  CA  . ASN B 108 ? 0.3529 0.2285 0.2891 0.0416  0.0208  -0.0126 108 ASN B CA  
1880 C  C   . ASN B 108 ? 0.3392 0.2277 0.2718 0.0494  0.0175  -0.011  108 ASN B C   
1881 O  O   . ASN B 108 ? 0.3419 0.2341 0.268  0.0545  0.0164  -0.0087 108 ASN B O   
1882 C  CB  . ASN B 108 ? 0.3828 0.2651 0.3283 0.0348  0.0217  -0.0126 108 ASN B CB  
1883 C  CG  . ASN B 108 ? 0.4628 0.3325 0.4088 0.0307  0.0277  -0.013  108 ASN B CG  
1884 O  OD1 . ASN B 108 ? 0.4654 0.3226 0.4041 0.0315  0.0309  -0.013  108 ASN B OD1 
1885 N  ND2 . ASN B 108 ? 0.4977 0.369  0.4513 0.0267  0.0305  -0.0131 108 ASN B ND2 
1886 N  N   . VAL B 109 ? 0.322  0.2176 0.2582 0.051   0.0162  -0.0116 109 VAL B N   
1887 C  CA  . VAL B 109 ? 0.318  0.2267 0.2518 0.06    0.0156  -0.0096 109 VAL B CA  
1888 C  C   . VAL B 109 ? 0.3254 0.2193 0.2446 0.0711  0.0181  -0.009  109 VAL B C   
1889 O  O   . VAL B 109 ? 0.3291 0.2335 0.2463 0.081   0.018   -0.0053 109 VAL B O   
1890 C  CB  . VAL B 109 ? 0.3429 0.2584 0.28   0.0592  0.0155  -0.0105 109 VAL B CB  
1891 C  CG1 . VAL B 109 ? 0.3556 0.2829 0.2891 0.0706  0.0178  -0.0082 109 VAL B CG1 
1892 C  CG2 . VAL B 109 ? 0.3459 0.2751 0.2951 0.0495  0.0132  -0.0098 109 VAL B CG2 
1893 N  N   . LEU B 110 ? 0.3281 0.1974 0.2368 0.0693  0.02    -0.0119 110 LEU B N   
1894 C  CA  . LEU B 110 ? 0.3593 0.2072 0.2492 0.0791  0.0229  -0.0115 110 LEU B CA  
1895 C  C   . LEU B 110 ? 0.3695 0.217  0.2559 0.0829  0.0226  -0.0079 110 LEU B C   
1896 O  O   . LEU B 110 ? 0.3739 0.2201 0.251  0.0959  0.0234  -0.0045 110 LEU B O   
1897 C  CB  . LEU B 110 ? 0.3856 0.2057 0.2636 0.0718  0.0241  -0.015  110 LEU B CB  
1898 C  CG  . LEU B 110 ? 0.4341 0.2244 0.2878 0.0794  0.0277  -0.0148 110 LEU B CG  
1899 C  CD1 . LEU B 110 ? 0.4297 0.2146 0.2691 0.0958  0.0309  -0.014  110 LEU B CD1 
1900 C  CD2 . LEU B 110 ? 0.4736 0.2371 0.3163 0.0671  0.028   -0.018  110 LEU B CD2 
1901 N  N   . VAL B 111 ? 0.3599 0.2098 0.2534 0.0725  0.0216  -0.0082 111 VAL B N   
1902 C  CA  . VAL B 111 ? 0.3723 0.2203 0.2591 0.0744  0.0208  -0.005  111 VAL B CA  
1903 C  C   . VAL B 111 ? 0.3639 0.2376 0.2563 0.0818  0.016   -0.0004 111 VAL B C   
1904 O  O   . VAL B 111 ? 0.3829 0.2553 0.2659 0.0913  0.0144  0.004   111 VAL B O   
1905 C  CB  . VAL B 111 ? 0.382  0.2258 0.2727 0.062   0.0224  -0.0067 111 VAL B CB  
1906 C  CG1 . VAL B 111 ? 0.3975 0.2406 0.2783 0.0629  0.0207  -0.0035 111 VAL B CG1 
1907 C  CG2 . VAL B 111 ? 0.4027 0.2242 0.2889 0.0559  0.0276  -0.0091 111 VAL B CG2 
1908 N  N   . CYS B 112 ? 0.3472 0.2447 0.2551 0.0773  0.0136  -0.0007 112 CYS B N   
1909 C  CA  . CYS B 112 ? 0.3323 0.2589 0.2487 0.0817  0.0088  0.0044  112 CYS B CA  
1910 C  C   . CYS B 112 ? 0.3323 0.2657 0.2463 0.0993  0.0104  0.0087  112 CYS B C   
1911 O  O   . CYS B 112 ? 0.329  0.282  0.2464 0.107   0.0064  0.0152  112 CYS B O   
1912 C  CB  . CYS B 112 ? 0.3214 0.2687 0.2528 0.0721  0.0072  0.0033  112 CYS B CB  
1913 S  SG  . CYS B 112 ? 0.3511 0.2922 0.2835 0.0542  0.0055  0       112 CYS B SG  
1914 N  N   . VAL B 113 ? 0.3401 0.2593 0.2487 0.1054  0.0161  0.0056  113 VAL B N   
1915 C  CA  . VAL B 113 ? 0.3554 0.2749 0.2577 0.1239  0.0205  0.0088  113 VAL B CA  
1916 C  C   . VAL B 113 ? 0.377  0.2755 0.262  0.1353  0.0209  0.0122  113 VAL B C   
1917 O  O   . VAL B 113 ? 0.383  0.2938 0.2682 0.1518  0.0212  0.019   113 VAL B O   
1918 C  CB  . VAL B 113 ? 0.3762 0.2775 0.2697 0.1256  0.0268  0.0035  113 VAL B CB  
1919 C  CG1 . VAL B 113 ? 0.4107 0.2986 0.2885 0.1462  0.0338  0.0057  113 VAL B CG1 
1920 C  CG2 . VAL B 113 ? 0.3497 0.2748 0.2591 0.1176  0.0264  0.0022  113 VAL B CG2 
1921 N  N   . LEU B 114 ? 0.3917 0.26   0.2626 0.127   0.0213  0.0085  114 LEU B N   
1922 C  CA  . LEU B 114 ? 0.4235 0.2679 0.2747 0.136   0.022   0.012   114 LEU B CA  
1923 C  C   . LEU B 114 ? 0.4274 0.2949 0.2849 0.1394  0.0149  0.0194  114 LEU B C   
1924 O  O   . LEU B 114 ? 0.4508 0.3173 0.2998 0.1558  0.014   0.0263  114 LEU B O   
1925 C  CB  . LEU B 114 ? 0.4416 0.2529 0.2789 0.1227  0.0242  0.007   114 LEU B CB  
1926 C  CG  . LEU B 114 ? 0.4728 0.2569 0.299  0.1186  0.0296  0.001   114 LEU B CG  
1927 C  CD1 . LEU B 114 ? 0.4838 0.2446 0.3027 0.1031  0.0311  -0.0024 114 LEU B CD1 
1928 C  CD2 . LEU B 114 ? 0.5075 0.2674 0.3113 0.1361  0.0345  0.0027  114 LEU B CD2 
1929 N  N   . ALA B 115 ? 0.4076 0.2963 0.2793 0.1244  0.0093  0.0186  115 ALA B N   
1930 C  CA  . ALA B 115 ? 0.4116 0.3225 0.2875 0.123   0.0007  0.025   115 ALA B CA  
1931 C  C   . ALA B 115 ? 0.4012 0.3495 0.2931 0.1368  -0.0032 0.0332  115 ALA B C   
1932 O  O   . ALA B 115 ? 0.403  0.3647 0.2935 0.1464  -0.0094 0.0418  115 ALA B O   
1933 C  CB  . ALA B 115 ? 0.4069 0.3278 0.2913 0.1028  -0.0029 0.0209  115 ALA B CB  
1934 N  N   . HIS B 116 ? 0.3811 0.3478 0.2887 0.1377  0.0006  0.0313  116 HIS B N   
1935 C  CA  . HIS B 116 ? 0.3731 0.3781 0.2989 0.15    -0.0004 0.039   116 HIS B CA  
1936 C  C   . HIS B 116 ? 0.4006 0.3973 0.3172 0.1757  0.0046  0.0452  116 HIS B C   
1937 O  O   . HIS B 116 ? 0.3947 0.4221 0.3231 0.1887  0.0004  0.0555  116 HIS B O   
1938 C  CB  . HIS B 116 ? 0.3726 0.3905 0.3121 0.1444  0.0053  0.0343  116 HIS B CB  
1939 C  CG  . HIS B 116 ? 0.3629 0.4266 0.3254 0.1508  0.0044  0.042   116 HIS B CG  
1940 N  ND1 . HIS B 116 ? 0.3852 0.4573 0.3544 0.159   0.0137  0.0411  116 HIS B ND1 
1941 C  CD2 . HIS B 116 ? 0.3619 0.4655 0.3418 0.1474  -0.0047 0.0508  116 HIS B CD2 
1942 C  CE1 . HIS B 116 ? 0.3683 0.4867 0.3607 0.1621  0.0114  0.0498  116 HIS B CE1 
1943 N  NE2 . HIS B 116 ? 0.3538 0.494  0.3545 0.1546  -0.0004 0.0561  116 HIS B NE2 
1944 N  N   . HIS B 117 ? 0.4417 0.3958 0.336  0.1826  0.0129  0.0397  117 HIS B N   
1945 C  CA  . HIS B 117 ? 0.4747 0.4108 0.3536 0.2076  0.0195  0.0446  117 HIS B CA  
1946 C  C   . HIS B 117 ? 0.5037 0.4256 0.3675 0.2156  0.0139  0.0514  117 HIS B C   
1947 O  O   . HIS B 117 ? 0.5026 0.434  0.3658 0.2379  0.0142  0.0612  117 HIS B O   
1948 C  CB  . HIS B 117 ? 0.5188 0.4081 0.3737 0.2085  0.0299  0.0354  117 HIS B CB  
1949 C  CG  . HIS B 117 ? 0.5741 0.4708 0.4348 0.2131  0.0382  0.0319  117 HIS B CG  
1950 N  ND1 . HIS B 117 ? 0.621  0.5014 0.4669 0.236   0.0488  0.0338  117 HIS B ND1 
1951 C  CD2 . HIS B 117 ? 0.575  0.4919 0.4522 0.1986  0.0378  0.0271  117 HIS B CD2 
1952 C  CE1 . HIS B 117 ? 0.6241 0.5151 0.4771 0.2336  0.0547  0.0296  117 HIS B CE1 
1953 N  NE2 . HIS B 117 ? 0.5987 0.5121 0.4709 0.2111  0.0479  0.0257  117 HIS B NE2 
1954 N  N   . PHE B 118 ? 0.5174 0.4164 0.3682 0.1984  0.0094  0.047   118 PHE B N   
1955 C  CA  . PHE B 118 ? 0.5347 0.4118 0.3649 0.2042  0.0054  0.0526  118 PHE B CA  
1956 C  C   . PHE B 118 ? 0.5232 0.431  0.3631 0.1981  -0.0079 0.0604  118 PHE B C   
1957 O  O   . PHE B 118 ? 0.5322 0.4275 0.3556 0.2066  -0.0126 0.0675  118 PHE B O   
1958 C  CB  . PHE B 118 ? 0.5537 0.3825 0.3591 0.1905  0.0104  0.044   118 PHE B CB  
1959 C  CG  . PHE B 118 ? 0.5814 0.372  0.3675 0.1997  0.0213  0.0394  118 PHE B CG  
1960 C  CD1 . PHE B 118 ? 0.6236 0.3852 0.3854 0.2202  0.0254  0.0451  118 PHE B CD1 
1961 C  CD2 . PHE B 118 ? 0.5904 0.3723 0.3801 0.1878  0.0269  0.0298  118 PHE B CD2 
1962 C  CE1 . PHE B 118 ? 0.6587 0.3796 0.3974 0.2273  0.0356  0.0403  118 PHE B CE1 
1963 C  CE2 . PHE B 118 ? 0.6243 0.3691 0.3925 0.1941  0.0357  0.0254  118 PHE B CE2 
1964 C  CZ  . PHE B 118 ? 0.6522 0.3652 0.3937 0.2135  0.0404  0.0302  118 PHE B CZ  
1965 N  N   . GLY B 119 ? 0.5077 0.4525 0.3708 0.183   -0.0142 0.0593  119 GLY B N   
1966 C  CA  . GLY B 119 ? 0.5044 0.4771 0.3739 0.174   -0.0278 0.0662  119 GLY B CA  
1967 C  C   . GLY B 119 ? 0.5322 0.4734 0.3755 0.1633  -0.0321 0.0649  119 GLY B C   
1968 O  O   . GLY B 119 ? 0.5437 0.4532 0.3739 0.1492  -0.0255 0.0552  119 GLY B O   
1969 N  N   . LYS B 120 ? 0.5427 0.4921 0.3773 0.1712  -0.0424 0.0756  120 LYS B N   
1970 C  CA  . LYS B 120 ? 0.5792 0.4993 0.3853 0.1624  -0.0472 0.0762  120 LYS B CA  
1971 C  C   . LYS B 120 ? 0.6022 0.4686 0.3805 0.1657  -0.0353 0.0705  120 LYS B C   
1972 O  O   . LYS B 120 ? 0.6234 0.4613 0.3785 0.1534  -0.035  0.0677  120 LYS B O   
1973 C  CB  . LYS B 120 ? 0.6249 0.5647 0.4263 0.1744  -0.0613 0.0908  120 LYS B CB  
1974 C  CG  . LYS B 120 ? 0.6849 0.6833 0.5158 0.1713  -0.0749 0.099   120 LYS B CG  
1975 C  CD  . LYS B 120 ? 0.7593 0.7706 0.5955 0.1422  -0.0806 0.0918  120 LYS B CD  
1976 C  CE  . LYS B 120 ? 0.8013 0.8661 0.658  0.1364  -0.0979 0.1026  120 LYS B CE  
1977 N  NZ  . LYS B 120 ? 0.8136 0.9245 0.7082 0.1462  -0.0953 0.1067  120 LYS B NZ  
1978 N  N   . GLU B 121 ? 0.5869 0.438  0.3651 0.1816  -0.0252 0.0693  121 GLU B N   
1979 C  CA  . GLU B 121 ? 0.6068 0.4065 0.3584 0.1824  -0.014  0.0639  121 GLU B CA  
1980 C  C   . GLU B 121 ? 0.585  0.3696 0.3397 0.1604  -0.0058 0.051   121 GLU B C   
1981 O  O   . GLU B 121 ? 0.6098 0.3566 0.3439 0.1527  0.0015  0.0466  121 GLU B O   
1982 C  CB  . GLU B 121 ? 0.6596 0.4447 0.406  0.2058  -0.0064 0.0667  121 GLU B CB  
1983 C  CG  . GLU B 121 ? 0.7944 0.5231 0.5091 0.2065  0.0041  0.0624  121 GLU B CG  
1984 C  CD  . GLU B 121 ? 0.9258 0.6318 0.6267 0.2305  0.0116  0.0658  121 GLU B CD  
1985 O  OE1 . GLU B 121 ? 0.9008 0.6352 0.6152 0.2519  0.0085  0.0744  121 GLU B OE1 
1986 O  OE2 . GLU B 121 ? 1.0068 0.666  0.6827 0.2277  0.0211  0.0601  121 GLU B OE2 
1987 N  N   . PHE B 122 ? 0.5456 0.3607 0.3264 0.1499  -0.0069 0.0458  122 PHE B N   
1988 C  CA  . PHE B 122 ? 0.5242 0.3292 0.3105 0.1309  -0.0002 0.0352  122 PHE B CA  
1989 C  C   . PHE B 122 ? 0.5176 0.3217 0.2969 0.1145  -0.0041 0.0341  122 PHE B C   
1990 O  O   . PHE B 122 ? 0.5047 0.3317 0.2988 0.103   -0.0079 0.0315  122 PHE B O   
1991 C  CB  . PHE B 122 ? 0.4861 0.3204 0.2998 0.128   0.0004  0.031   122 PHE B CB  
1992 C  CG  . PHE B 122 ? 0.4727 0.2919 0.2907 0.1141  0.0084  0.0214  122 PHE B CG  
1993 C  CD1 . PHE B 122 ? 0.4875 0.278  0.2949 0.1168  0.0162  0.0178  122 PHE B CD1 
1994 C  CD2 . PHE B 122 ? 0.4549 0.2883 0.2867 0.0982  0.0075  0.0167  122 PHE B CD2 
1995 C  CE1 . PHE B 122 ? 0.4921 0.2738 0.3064 0.1033  0.0217  0.0104  122 PHE B CE1 
1996 C  CE2 . PHE B 122 ? 0.4501 0.2728 0.2884 0.0874  0.0143  0.0095  122 PHE B CE2 
1997 C  CZ  . PHE B 122 ? 0.4685 0.2678 0.2995 0.0897  0.0206  0.0068  122 PHE B CZ  
1998 N  N   . THR B 123 ? 0.5341 0.3092 0.2875 0.1138  -0.0028 0.0365  123 THR B N   
1999 C  CA  . THR B 123 ? 0.5423 0.3094 0.2806 0.1001  -0.0053 0.0362  123 THR B CA  
2000 C  C   . THR B 123 ? 0.5489 0.3064 0.2927 0.0828  0.0044  0.0267  123 THR B C   
2001 O  O   . THR B 123 ? 0.5502 0.2998 0.3043 0.0814  0.0132  0.0214  123 THR B O   
2002 C  CB  . THR B 123 ? 0.5755 0.3081 0.2813 0.1052  -0.0039 0.0414  123 THR B CB  
2003 O  OG1 . THR B 123 ? 0.5929 0.2938 0.2905 0.1025  0.0091  0.0364  123 THR B OG1 
2004 C  CG2 . THR B 123 ? 0.5837 0.3225 0.2828 0.1255  -0.0127 0.0522  123 THR B CG2 
2005 N  N   . PRO B 124 ? 0.5515 0.3076 0.2864 0.0697  0.0031  0.0247  124 PRO B N   
2006 C  CA  . PRO B 124 ? 0.5536 0.2984 0.2925 0.0561  0.0144  0.0166  124 PRO B CA  
2007 C  C   . PRO B 124 ? 0.559  0.276  0.2915 0.055   0.0279  0.014   124 PRO B C   
2008 O  O   . PRO B 124 ? 0.5416 0.2636 0.2939 0.0506  0.035   0.0089  124 PRO B O   
2009 C  CB  . PRO B 124 ? 0.5693 0.3069 0.2878 0.0453  0.0115  0.0164  124 PRO B CB  
2010 C  CG  . PRO B 124 ? 0.5691 0.3323 0.2884 0.0494  -0.0054 0.023   124 PRO B CG  
2011 C  CD  . PRO B 124 ? 0.5533 0.3172 0.2728 0.0665  -0.0087 0.03    124 PRO B CD  
2012 N  N   . PRO B 125 ? 0.5759 0.2657 0.2835 0.0591  0.0306  0.0182  125 PRO B N   
2013 C  CA  . PRO B 125 ? 0.5863 0.252  0.2904 0.0553  0.0434  0.0159  125 PRO B CA  
2014 C  C   . PRO B 125 ? 0.5731 0.2453 0.2959 0.0605  0.0439  0.0142  125 PRO B C   
2015 O  O   . PRO B 125 ? 0.5791 0.2465 0.3132 0.0523  0.0526  0.0101  125 PRO B O   
2016 C  CB  . PRO B 125 ? 0.6218 0.2569 0.2921 0.0597  0.0439  0.0221  125 PRO B CB  
2017 C  CG  . PRO B 125 ? 0.6451 0.2857 0.299  0.0601  0.0343  0.0258  125 PRO B CG  
2018 C  CD  . PRO B 125 ? 0.5928 0.2707 0.2723 0.0649  0.0227  0.0256  125 PRO B CD  
2019 N  N   . VAL B 126 ? 0.5555 0.2378 0.2801 0.0742  0.035   0.0178  126 VAL B N   
2020 C  CA  . VAL B 126 ? 0.56   0.244  0.2963 0.0803  0.0358  0.0159  126 VAL B CA  
2021 C  C   . VAL B 126 ? 0.5296 0.2396 0.2957 0.0724  0.0364  0.0098  126 VAL B C   
2022 O  O   . VAL B 126 ? 0.5385 0.2426 0.3132 0.0667  0.0416  0.0059  126 VAL B O   
2023 C  CB  . VAL B 126 ? 0.5762 0.2659 0.3074 0.0992  0.0282  0.0216  126 VAL B CB  
2024 C  CG1 . VAL B 126 ? 0.5822 0.2752 0.325  0.1051  0.03    0.0184  126 VAL B CG1 
2025 C  CG2 . VAL B 126 ? 0.6199 0.2777 0.3192 0.1087  0.0285  0.0283  126 VAL B CG2 
2026 N  N   . GLN B 127 ? 0.4873 0.2237 0.267  0.0702  0.0309  0.0093  127 GLN B N   
2027 C  CA  . GLN B 127 ? 0.4589 0.2166 0.2641 0.0628  0.0318  0.0042  127 GLN B CA  
2028 C  C   . GLN B 127 ? 0.4586 0.2048 0.2686 0.0503  0.0419  0.0002  127 GLN B C   
2029 O  O   . GLN B 127 ? 0.4424 0.1952 0.2697 0.0463  0.0444  -0.0029 127 GLN B O   
2030 C  CB  . GLN B 127 ? 0.4405 0.222  0.2538 0.0599  0.0252  0.0046  127 GLN B CB  
2031 C  CG  . GLN B 127 ? 0.4209 0.2197 0.2572 0.0524  0.0269  -0.0003 127 GLN B CG  
2032 C  CD  . GLN B 127 ? 0.4145 0.2284 0.2539 0.0459  0.0223  -0.0007 127 GLN B CD  
2033 O  OE1 . GLN B 127 ? 0.4384 0.254  0.2642 0.0459  0.016   0.0026  127 GLN B OE1 
2034 N  NE2 . GLN B 127 ? 0.3888 0.2122 0.2443 0.0394  0.0248  -0.0045 127 GLN B NE2 
2035 N  N   . ALA B 128 ? 0.4685 0.1985 0.2631 0.0445  0.0478  0.0009  128 ALA B N   
2036 C  CA  . ALA B 128 ? 0.477  0.2001 0.2791 0.0341  0.0592  -0.0018 128 ALA B CA  
2037 C  C   . ALA B 128 ? 0.4858 0.2001 0.2945 0.0306  0.0641  -0.0021 128 ALA B C   
2038 O  O   . ALA B 128 ? 0.4788 0.2034 0.3085 0.0234  0.0691  -0.0041 128 ALA B O   
2039 C  CB  . ALA B 128 ? 0.4885 0.1919 0.2684 0.0296  0.0666  -0.0005 128 ALA B CB  
2040 N  N   . ALA B 129 ? 0.49   0.1853 0.2802 0.0357  0.0618  0.0004  129 ALA B N   
2041 C  CA  . ALA B 129 ? 0.5058 0.1871 0.2957 0.0303  0.0654  0       129 ALA B CA  
2042 C  C   . ALA B 129 ? 0.4958 0.1946 0.3059 0.0311  0.0595  -0.003  129 ALA B C   
2043 O  O   . ALA B 129 ? 0.4928 0.1958 0.3177 0.021   0.0623  -0.0046 129 ALA B O   
2044 C  CB  . ALA B 129 ? 0.5259 0.1767 0.2853 0.0367  0.0647  0.0034  129 ALA B CB  
2045 N  N   . TYR B 130 ? 0.4743 0.1854 0.2856 0.0425  0.0514  -0.0032 130 TYR B N   
2046 C  CA  . TYR B 130 ? 0.4668 0.1936 0.2944 0.0436  0.0467  -0.006  130 TYR B CA  
2047 C  C   . TYR B 130 ? 0.455  0.2058 0.3098 0.0348  0.0474  -0.0082 130 TYR B C   
2048 O  O   . TYR B 130 ? 0.4607 0.219  0.3285 0.0303  0.0452  -0.0101 130 TYR B O   
2049 C  CB  . TYR B 130 ? 0.4593 0.1976 0.2843 0.058   0.0398  -0.0048 130 TYR B CB  
2050 C  CG  . TYR B 130 ? 0.4886 0.2039 0.2923 0.0681  0.0396  -0.0036 130 TYR B CG  
2051 C  CD1 . TYR B 130 ? 0.5029 0.2111 0.3056 0.0675  0.0393  -0.0067 130 TYR B CD1 
2052 C  CD2 . TYR B 130 ? 0.5124 0.2087 0.2933 0.078   0.0401  0.0009  130 TYR B CD2 
2053 C  CE1 . TYR B 130 ? 0.5375 0.2176 0.3154 0.0769  0.0408  -0.0062 130 TYR B CE1 
2054 C  CE2 . TYR B 130 ? 0.5469 0.2171 0.3053 0.089   0.0413  0.0024  130 TYR B CE2 
2055 C  CZ  . TYR B 130 ? 0.5663 0.2269 0.3223 0.0885  0.0424  -0.0016 130 TYR B CZ  
2056 O  OH  . TYR B 130 ? 0.6202 0.249  0.3492 0.0996  0.0451  -0.0008 130 TYR B OH  
2057 N  N   . GLN B 131 ? 0.4411 0.2008 0.3017 0.0325  0.0505  -0.0078 131 GLN B N   
2058 C  CA  . GLN B 131 ? 0.4349 0.2133 0.3188 0.0264  0.0528  -0.0092 131 GLN B CA  
2059 C  C   . GLN B 131 ? 0.4394 0.216  0.336  0.0165  0.0589  -0.0087 131 GLN B C   
2060 O  O   . GLN B 131 ? 0.4356 0.2288 0.3535 0.0128  0.0569  -0.0091 131 GLN B O   
2061 C  CB  . GLN B 131 ? 0.4287 0.2111 0.311  0.0263  0.0561  -0.0093 131 GLN B CB  
2062 C  CG  . GLN B 131 ? 0.4271 0.2178 0.3012 0.0328  0.0478  -0.0091 131 GLN B CG  
2063 C  CD  . GLN B 131 ? 0.4278 0.2401 0.3182 0.0345  0.041   -0.0103 131 GLN B CD  
2064 O  OE1 . GLN B 131 ? 0.4354 0.258  0.3218 0.0389  0.0342  -0.0092 131 GLN B OE1 
2065 N  NE2 . GLN B 131 ? 0.3496 0.1707 0.2587 0.0307  0.0424  -0.0116 131 GLN B NE2 
2066 N  N   . LYS B 132 ? 0.4443 0.2022 0.3281 0.0117  0.0655  -0.007  132 LYS B N   
2067 C  CA  . LYS B 132 ? 0.4543 0.2135 0.3517 0.0002  0.071   -0.0054 132 LYS B CA  
2068 C  C   . LYS B 132 ? 0.4562 0.216  0.3575 -0.0043 0.0628  -0.0063 132 LYS B C   
2069 O  O   . LYS B 132 ? 0.4411 0.2175 0.3646 -0.0124 0.0614  -0.0053 132 LYS B O   
2070 C  CB  . LYS B 132 ? 0.4874 0.224  0.3668 -0.0055 0.0802  -0.0031 132 LYS B CB  
2071 C  CG  . LYS B 132 ? 0.5277 0.2618 0.402  -0.0036 0.0904  -0.0021 132 LYS B CG  
2072 C  CD  . LYS B 132 ? 0.5943 0.3023 0.4451 -0.0088 0.0991  0.0005  132 LYS B CD  
2073 C  CE  . LYS B 132 ? 0.6707 0.3756 0.5178 -0.01   0.1123  0.0018  132 LYS B CE  
2074 N  NZ  . LYS B 132 ? 0.7101 0.3869 0.5304 -0.0153 0.1205  0.0047  132 LYS B NZ  
2075 N  N   . VAL B 133 ? 0.4695 0.2111 0.3479 0.0019  0.0571  -0.008  133 VAL B N   
2076 C  CA  . VAL B 133 ? 0.4867 0.2215 0.3606 -0.0016 0.0502  -0.0097 133 VAL B CA  
2077 C  C   . VAL B 133 ? 0.4759 0.2355 0.3703 0       0.0431  -0.0113 133 VAL B C   
2078 O  O   . VAL B 133 ? 0.4732 0.2401 0.3796 -0.0102 0.0392  -0.0111 133 VAL B O   
2079 C  CB  . VAL B 133 ? 0.5162 0.2236 0.3586 0.0086  0.048   -0.0109 133 VAL B CB  
2080 C  CG1 . VAL B 133 ? 0.5336 0.2281 0.3655 0.0055  0.0424  -0.0136 133 VAL B CG1 
2081 C  CG2 . VAL B 133 ? 0.547  0.2261 0.3658 0.0072  0.0546  -0.0086 133 VAL B CG2 
2082 N  N   . VAL B 134 ? 0.462  0.2353 0.3605 0.0113  0.0411  -0.0121 134 VAL B N   
2083 C  CA  . VAL B 134 ? 0.4583 0.2517 0.3724 0.0127  0.0349  -0.0133 134 VAL B CA  
2084 C  C   . VAL B 134 ? 0.452  0.2665 0.3935 0.005   0.0359  -0.0112 134 VAL B C   
2085 O  O   . VAL B 134 ? 0.4449 0.2711 0.3983 0.0013  0.0297  -0.011  134 VAL B O   
2086 C  CB  . VAL B 134 ? 0.4629 0.2662 0.3742 0.0246  0.0321  -0.0142 134 VAL B CB  
2087 C  CG1 . VAL B 134 ? 0.4808 0.2673 0.3685 0.0346  0.0309  -0.0149 134 VAL B CG1 
2088 C  CG2 . VAL B 134 ? 0.4586 0.2717 0.3761 0.0272  0.0358  -0.013  134 VAL B CG2 
2089 N  N   . ALA B 135 ? 0.4469 0.265  0.3974 0.0029  0.044   -0.0091 135 ALA B N   
2090 C  CA  . ALA B 135 ? 0.4465 0.2845 0.4241 -0.0019 0.047   -0.006  135 ALA B CA  
2091 C  C   . ALA B 135 ? 0.4522 0.2946 0.4413 -0.0141 0.0443  -0.0032 135 ALA B C   
2092 O  O   . ALA B 135 ? 0.4476 0.3101 0.4588 -0.0176 0.0396  -0.0004 135 ALA B O   
2093 C  CB  . ALA B 135 ? 0.4525 0.2897 0.4332 -0.0003 0.0588  -0.0045 135 ALA B CB  
2094 N  N   . GLY B 136 ? 0.4603 0.2835 0.4332 -0.0212 0.0465  -0.0035 136 GLY B N   
2095 C  CA  . GLY B 136 ? 0.4675 0.2909 0.4462 -0.0362 0.0432  -0.0009 136 GLY B CA  
2096 C  C   . GLY B 136 ? 0.4781 0.3015 0.4527 -0.0403 0.0303  -0.0027 136 GLY B C   
2097 O  O   . GLY B 136 ? 0.4682 0.3088 0.4619 -0.0513 0.0241  0.0008  136 GLY B O   
2098 N  N   . VAL B 137 ? 0.4879 0.2936 0.438  -0.0312 0.0262  -0.0076 137 VAL B N   
2099 C  CA  . VAL B 137 ? 0.4953 0.2966 0.4359 -0.0336 0.0158  -0.01   137 VAL B CA  
2100 C  C   . VAL B 137 ? 0.4815 0.3122 0.4478 -0.0316 0.0101  -0.0076 137 VAL B C   
2101 O  O   . VAL B 137 ? 0.4728 0.3116 0.4464 -0.0416 0.0011  -0.0058 137 VAL B O   
2102 C  CB  . VAL B 137 ? 0.5188 0.2965 0.4288 -0.0211 0.016   -0.015  137 VAL B CB  
2103 C  CG1 . VAL B 137 ? 0.5244 0.2997 0.425  -0.0209 0.0075  -0.0176 137 VAL B CG1 
2104 C  CG2 . VAL B 137 ? 0.5393 0.2828 0.4197 -0.0226 0.0204  -0.0166 137 VAL B CG2 
2105 N  N   . ALA B 138 ? 0.4664 0.3113 0.4448 -0.02   0.0147  -0.0072 138 ALA B N   
2106 C  CA  . ALA B 138 ? 0.4577 0.326  0.4573 -0.0171 0.0104  -0.0045 138 ALA B CA  
2107 C  C   . ALA B 138 ? 0.4592 0.3502 0.4889 -0.0254 0.0093  0.002   138 ALA B C   
2108 O  O   . ALA B 138 ? 0.4457 0.3521 0.4887 -0.0279 0.0007  0.0053  138 ALA B O   
2109 C  CB  . ALA B 138 ? 0.4512 0.3249 0.4533 -0.0049 0.0164  -0.0055 138 ALA B CB  
2110 N  N   . ASN B 139 ? 0.4701 0.3642 0.5106 -0.0292 0.018   0.0048  139 ASN B N   
2111 C  CA  . ASN B 139 ? 0.476  0.3957 0.5484 -0.0363 0.0187  0.0123  139 ASN B CA  
2112 C  C   . ASN B 139 ? 0.4872 0.4102 0.5609 -0.053  0.0067  0.0147  139 ASN B C   
2113 O  O   . ASN B 139 ? 0.474  0.4225 0.5726 -0.0581 -0.0011 0.0212  139 ASN B O   
2114 C  CB  . ASN B 139 ? 0.5107 0.4316 0.5917 -0.0366 0.0331  0.0145  139 ASN B CB  
2115 C  CG  . ASN B 139 ? 0.5933 0.5171 0.6801 -0.0225 0.045   0.0144  139 ASN B CG  
2116 O  OD1 . ASN B 139 ? 0.6352 0.5483 0.7145 -0.0205 0.0572  0.0134  139 ASN B OD1 
2117 N  ND2 . ASN B 139 ? 0.6021 0.5368 0.6988 -0.0134 0.0419  0.0154  139 ASN B ND2 
2118 N  N   . ALA B 140 ? 0.5099 0.4054 0.5546 -0.0615 0.0046  0.0099  140 ALA B N   
2119 C  CA  . ALA B 140 ? 0.5239 0.4138 0.5607 -0.0797 -0.0069 0.0109  140 ALA B CA  
2120 C  C   . ALA B 140 ? 0.5463 0.4402 0.5787 -0.0801 -0.0208 0.0103  140 ALA B C   
2121 O  O   . ALA B 140 ? 0.5448 0.4524 0.5879 -0.0946 -0.0325 0.015   140 ALA B O   
2122 C  CB  . ALA B 140 ? 0.542  0.3922 0.5402 -0.0852 -0.0046 0.0046  140 ALA B CB  
2123 N  N   . LEU B 141 ? 0.5624 0.4447 0.578  -0.0654 -0.02   0.005   141 LEU B N   
2124 C  CA  . LEU B 141 ? 0.5818 0.4655 0.5899 -0.0648 -0.0314 0.0043  141 LEU B CA  
2125 C  C   . LEU B 141 ? 0.5687 0.4875 0.6118 -0.0623 -0.0365 0.0123  141 LEU B C   
2126 O  O   . LEU B 141 ? 0.5656 0.4923 0.61   -0.0692 -0.0494 0.0154  141 LEU B O   
2127 C  CB  . LEU B 141 ? 0.6074 0.4733 0.592  -0.0494 -0.0266 -0.0023 141 LEU B CB  
2128 C  CG  . LEU B 141 ? 0.6597 0.4917 0.6046 -0.0508 -0.0286 -0.0092 141 LEU B CG  
2129 C  CD1 . LEU B 141 ? 0.6854 0.4933 0.6126 -0.0559 -0.0228 -0.0119 141 LEU B CD1 
2130 C  CD2 . LEU B 141 ? 0.6755 0.5005 0.6066 -0.0341 -0.0228 -0.0134 141 LEU B CD2 
2131 N  N   . ALA B 142 ? 0.5626 0.4995 0.631  -0.0518 -0.026  0.0159  142 ALA B N   
2132 C  CA  . ALA B 142 ? 0.5624 0.5293 0.663  -0.0459 -0.028  0.024   142 ALA B CA  
2133 C  C   . ALA B 142 ? 0.5596 0.5549 0.6903 -0.0582 -0.0357 0.0336  142 ALA B C   
2134 O  O   . ALA B 142 ? 0.571  0.5636 0.6994 -0.0731 -0.0376 0.0339  142 ALA B O   
2135 C  CB  . ALA B 142 ? 0.559  0.5308 0.6726 -0.0313 -0.0128 0.0244  142 ALA B CB  
2136 N  N   . LYS C 5   ? 0.415  0.9421 0.4612 -0.0688 0.0817  0.2716  36  LYS C N   
2137 C  CA  . LYS C 5   ? 0.4493 0.9269 0.4734 -0.0693 0.0784  0.2644  36  LYS C CA  
2138 C  C   . LYS C 5   ? 0.4559 0.891  0.4718 -0.0614 0.0701  0.2432  36  LYS C C   
2139 O  O   . LYS C 5   ? 0.4837 0.8881 0.4829 -0.0505 0.0692  0.2347  36  LYS C O   
2140 C  CB  . LYS C 5   ? 0.4985 0.9589 0.5173 -0.0976 0.0756  0.2789  36  LYS C CB  
2141 N  N   . ASN C 6   ? 0.4215 0.8581 0.4496 -0.0668 0.0641  0.2359  37  ASN C N   
2142 C  CA  . ASN C 6   ? 0.4145 0.8147 0.4361 -0.0596 0.0571  0.2171  37  ASN C CA  
2143 C  C   . ASN C 6   ? 0.367  0.781  0.4041 -0.0617 0.0528  0.2113  37  ASN C C   
2144 O  O   . ASN C 6   ? 0.3452 0.7991 0.3989 -0.069  0.0546  0.2228  37  ASN C O   
2145 C  CB  . ASN C 6   ? 0.4656 0.8167 0.4715 -0.0724 0.0511  0.2143  37  ASN C CB  
2146 C  CG  . ASN C 6   ? 0.5349 0.8734 0.5417 -0.1008 0.046   0.2225  37  ASN C CG  
2147 O  OD1 . ASN C 6   ? 0.5611 0.8896 0.5723 -0.1099 0.0394  0.215   37  ASN C OD1 
2148 N  ND2 . ASN C 6   ? 0.5583 0.8939 0.5581 -0.1167 0.0489  0.2378  37  ASN C ND2 
2149 N  N   . ALA C 7   ? 0.339  0.7243 0.3712 -0.0536 0.0475  0.1946  38  ALA C N   
2150 C  CA  . ALA C 7   ? 0.3145 0.7069 0.3583 -0.0542 0.043   0.1881  38  ALA C CA  
2151 C  C   . ALA C 7   ? 0.324  0.673  0.3587 -0.0615 0.0348  0.1758  38  ALA C C   
2152 O  O   . ALA C 7   ? 0.3326 0.6505 0.3537 -0.0529 0.0343  0.1669  38  ALA C O   
2153 C  CB  . ALA C 7   ? 0.3089 0.7141 0.355  -0.0289 0.0481  0.1789  38  ALA C CB  
2154 N  N   . ASP C 8   ? 0.3144 0.6638 0.3562 -0.0762 0.0285  0.1754  39  ASP C N   
2155 C  CA  . ASP C 8   ? 0.3204 0.6303 0.353  -0.0812 0.0216  0.163   39  ASP C CA  
2156 C  C   . ASP C 8   ? 0.2966 0.6181 0.3391 -0.069  0.02    0.1539  39  ASP C C   
2157 O  O   . ASP C 8   ? 0.2732 0.6317 0.3306 -0.0694 0.0209  0.1612  39  ASP C O   
2158 C  CB  . ASP C 8   ? 0.3539 0.6503 0.382  -0.1091 0.0152  0.1685  39  ASP C CB  
2159 C  CG  . ASP C 8   ? 0.4338 0.7097 0.448  -0.1242 0.0168  0.1779  39  ASP C CG  
2160 O  OD1 . ASP C 8   ? 0.4562 0.7045 0.4575 -0.1127 0.0202  0.1743  39  ASP C OD1 
2161 O  OD2 . ASP C 8   ? 0.4487 0.7369 0.4647 -0.1482 0.0144  0.1896  39  ASP C OD2 
2162 N  N   . LEU C 9   ? 0.2918 0.5834 0.3264 -0.058  0.018   0.1394  40  LEU C N   
2163 C  CA  . LEU C 9   ? 0.2822 0.5782 0.3235 -0.0478 0.0165  0.1306  40  LEU C CA  
2164 C  C   . LEU C 9   ? 0.2878 0.5595 0.3247 -0.0611 0.0093  0.1248  40  LEU C C   
2165 O  O   . LEU C 9   ? 0.3037 0.5407 0.3273 -0.0653 0.0074  0.1194  40  LEU C O   
2166 C  CB  . LEU C 9   ? 0.2864 0.5679 0.3213 -0.0273 0.0195  0.1185  40  LEU C CB  
2167 C  CG  . LEU C 9   ? 0.3015 0.5754 0.3388 -0.0184 0.0175  0.1076  40  LEU C CG  
2168 C  CD1 . LEU C 9   ? 0.2853 0.5898 0.3337 -0.0096 0.0215  0.1126  40  LEU C CD1 
2169 C  CD2 . LEU C 9   ? 0.3303 0.5837 0.3579 -0.0052 0.0186  0.0959  40  LEU C CD2 
2170 N  N   . TYR C 10  ? 0.2633 0.553  0.31   -0.0652 0.006   0.1261  41  TYR C N   
2171 C  CA  . TYR C 10  ? 0.2637 0.5327 0.3047 -0.0767 -0.0008 0.1199  41  TYR C CA  
2172 C  C   . TYR C 10  ? 0.2434 0.5137 0.2896 -0.0605 -0.0004 0.1112  41  TYR C C   
2173 O  O   . TYR C 10  ? 0.2185 0.5192 0.277  -0.0499 0.0026  0.1159  41  TYR C O   
2174 C  CB  . TYR C 10  ? 0.2604 0.5534 0.3076 -0.0983 -0.0063 0.1305  41  TYR C CB  
2175 C  CG  . TYR C 10  ? 0.2791 0.5668 0.3185 -0.1196 -0.0076 0.1396  41  TYR C CG  
2176 C  CD1 . TYR C 10  ? 0.284  0.6028 0.3331 -0.1201 -0.003  0.1523  41  TYR C CD1 
2177 C  CD2 . TYR C 10  ? 0.3117 0.5619 0.332  -0.1397 -0.0126 0.1359  41  TYR C CD2 
2178 C  CE1 . TYR C 10  ? 0.3068 0.6196 0.348  -0.1411 -0.0038 0.1617  41  TYR C CE1 
2179 C  CE2 . TYR C 10  ? 0.3414 0.5808 0.351  -0.1608 -0.0134 0.1444  41  TYR C CE2 
2180 C  CZ  . TYR C 10  ? 0.3448 0.6162 0.3657 -0.1623 -0.0093 0.1577  41  TYR C CZ  
2181 O  OH  . TYR C 10  ? 0.3852 0.6448 0.3948 -0.1851 -0.0099 0.1671  41  TYR C OH  
2182 N  N   . TRP C 11  ? 0.2449 0.4822 0.2811 -0.0574 -0.0023 0.0995  42  TRP C N   
2183 C  CA  . TRP C 11  ? 0.2363 0.4722 0.2763 -0.044  -0.0019 0.0917  42  TRP C CA  
2184 C  C   . TRP C 11  ? 0.2422 0.4487 0.2723 -0.0497 -0.006  0.0831  42  TRP C C   
2185 O  O   . TRP C 11  ? 0.2551 0.4339 0.274  -0.0511 -0.0056 0.0781  42  TRP C O   
2186 C  CB  . TRP C 11  ? 0.2295 0.4594 0.2678 -0.026  0.0035  0.0855  42  TRP C CB  
2187 C  CG  . TRP C 11  ? 0.2286 0.4576 0.2693 -0.0123 0.0054  0.0788  42  TRP C CG  
2188 C  CD1 . TRP C 11  ? 0.2228 0.4666 0.2707 -0.009  0.0053  0.0817  42  TRP C CD1 
2189 C  CD2 . TRP C 11  ? 0.2342 0.4475 0.2686 -0.0005 0.0081  0.0695  42  TRP C CD2 
2190 N  NE1 . TRP C 11  ? 0.2224 0.4558 0.2674 0.005   0.0087  0.0745  42  TRP C NE1 
2191 C  CE2 . TRP C 11  ? 0.2387 0.4529 0.275  0.0087  0.01    0.0663  42  TRP C CE2 
2192 C  CE3 . TRP C 11  ? 0.2495 0.4497 0.2762 0.0027  0.0089  0.0645  42  TRP C CE3 
2193 C  CZ2 . TRP C 11  ? 0.2533 0.4513 0.2821 0.0182  0.0124  0.0573  42  TRP C CZ2 
2194 C  CZ3 . TRP C 11  ? 0.2609 0.4505 0.2819 0.0116  0.0102  0.0558  42  TRP C CZ3 
2195 C  CH2 . TRP C 11  ? 0.2568 0.4435 0.2781 0.0181  0.0119  0.0518  42  TRP C CH2 
2196 N  N   . GLY C 12  ? 0.2286 0.4419 0.2624 -0.0504 -0.0088 0.082   43  GLY C N   
2197 C  CA  . GLY C 12  ? 0.2334 0.421  0.2573 -0.0539 -0.0117 0.0739  43  GLY C CA  
2198 C  C   . GLY C 12  ? 0.2353 0.4104 0.2597 -0.0383 -0.0084 0.0652  43  GLY C C   
2199 O  O   . GLY C 12  ? 0.2556 0.4128 0.2735 -0.0388 -0.0097 0.0592  43  GLY C O   
2200 N  N   . PHE C 13  ? 0.2094 0.3938 0.24   -0.0252 -0.0041 0.0648  44  PHE C N   
2201 C  CA  . PHE C 13  ? 0.2115 0.3859 0.2414 -0.0129 -0.0013 0.0572  44  PHE C CA  
2202 C  C   . PHE C 13  ? 0.2059 0.3843 0.2394 -0.0078 -0.0012 0.0563  44  PHE C C   
2203 O  O   . PHE C 13  ? 0.2054 0.3946 0.2425 0.0023  0.0025  0.0582  44  PHE C O   
2204 C  CB  . PHE C 13  ? 0.2202 0.3719 0.2426 -0.0134 -0.0017 0.0507  44  PHE C CB  
2205 C  CG  . PHE C 13  ? 0.2306 0.3779 0.2529 -0.0038 0.0003  0.0446  44  PHE C CG  
2206 C  CD1 . PHE C 13  ? 0.2347 0.3876 0.2557 0.0012  0.0022  0.0446  44  PHE C CD1 
2207 C  CD2 . PHE C 13  ? 0.2452 0.3836 0.2673 -0.0016 0.0001  0.0392  44  PHE C CD2 
2208 C  CE1 . PHE C 13  ? 0.2499 0.3985 0.2679 0.0068  0.0029  0.0384  44  PHE C CE1 
2209 C  CE2 . PHE C 13  ? 0.2569 0.3916 0.2777 0.0034  0.0011  0.034   44  PHE C CE2 
2210 C  CZ  . PHE C 13  ? 0.2493 0.3886 0.2672 0.0068  0.002   0.0332  44  PHE C CZ  
2211 N  N   . SER C 14  ? 0.2031 0.3726 0.2337 -0.014  -0.0043 0.0546  45  SER C N   
2212 C  CA  . SER C 14  ? 0.202  0.3755 0.235  -0.0099 -0.0045 0.0553  45  SER C CA  
2213 C  C   . SER C 14  ? 0.2127 0.3831 0.2409 -0.0215 -0.0094 0.0564  45  SER C C   
2214 O  O   . SER C 14  ? 0.2197 0.3744 0.2391 -0.0304 -0.0112 0.053   45  SER C O   
2215 C  CB  . SER C 14  ? 0.219  0.3749 0.2488 -0.0019 -0.0016 0.0479  45  SER C CB  
2216 O  OG  . SER C 14  ? 0.2425 0.3812 0.2669 -0.0068 -0.0028 0.0422  45  SER C OG  
2217 N  N   . GLY C 15  ? 0.2064 0.3903 0.2378 -0.0209 -0.0112 0.0612  46  GLY C N   
2218 C  CA  . GLY C 15  ? 0.2049 0.3855 0.2286 -0.0323 -0.0164 0.0614  46  GLY C CA  
2219 C  C   . GLY C 15  ? 0.2166 0.3687 0.2295 -0.0322 -0.0149 0.0523  46  GLY C C   
2220 O  O   . GLY C 15  ? 0.2382 0.3755 0.2385 -0.0423 -0.0173 0.0491  46  GLY C O   
2221 N  N   . SER C 16  ? 0.1988 0.3418 0.2149 -0.021  -0.0102 0.0482  47  SER C N   
2222 C  CA  . SER C 16  ? 0.2142 0.3367 0.2234 -0.0198 -0.0079 0.0414  47  SER C CA  
2223 C  C   . SER C 16  ? 0.2388 0.3469 0.242  -0.0223 -0.0067 0.0373  47  SER C C   
2224 O  O   . SER C 16  ? 0.252  0.3453 0.2481 -0.0213 -0.0044 0.0333  47  SER C O   
2225 C  CB  . SER C 16  ? 0.2118 0.331  0.2262 -0.0104 -0.004  0.0393  47  SER C CB  
2226 O  OG  . SER C 16  ? 0.2351 0.3556 0.2543 -0.0056 -0.002  0.0377  47  SER C OG  
2227 N  N   . SER C 17  ? 0.2313 0.3444 0.2366 -0.0246 -0.0074 0.0394  48  SER C N   
2228 C  CA  . SER C 17  ? 0.2468 0.3441 0.2438 -0.0267 -0.006  0.0373  48  SER C CA  
2229 C  C   . SER C 17  ? 0.2792 0.3607 0.2601 -0.038  -0.0081 0.0371  48  SER C C   
2230 O  O   . SER C 17  ? 0.2946 0.3573 0.2644 -0.0398 -0.0061 0.036   48  SER C O   
2231 C  CB  . SER C 17  ? 0.2379 0.3439 0.2404 -0.0258 -0.0057 0.0405  48  SER C CB  
2232 O  OG  . SER C 17  ? 0.2345 0.3531 0.2473 -0.0169 -0.0041 0.04    48  SER C OG  
2233 N  N   . HIS C 18  ? 0.285  0.3721 0.2622 -0.0458 -0.012  0.0383  49  HIS C N   
2234 C  CA  . HIS C 18  ? 0.2981 0.3701 0.2566 -0.06   -0.0154 0.0374  49  HIS C CA  
2235 C  C   . HIS C 18  ? 0.3063 0.3665 0.2524 -0.0605 -0.0153 0.0332  49  HIS C C   
2236 O  O   . HIS C 18  ? 0.3194 0.3771 0.2521 -0.0734 -0.0203 0.0333  49  HIS C O   
2237 C  CB  . HIS C 18  ? 0.292  0.3866 0.2553 -0.0736 -0.0221 0.0446  49  HIS C CB  
2238 C  CG  . HIS C 18  ? 0.2944 0.3995 0.268  -0.0726 -0.0209 0.0491  49  HIS C CG  
2239 N  ND1 . HIS C 18  ? 0.3188 0.4042 0.2795 -0.0818 -0.0204 0.0491  49  HIS C ND1 
2240 C  CD2 . HIS C 18  ? 0.2926 0.4209 0.2848 -0.062  -0.0188 0.0532  49  HIS C CD2 
2241 C  CE1 . HIS C 18  ? 0.3153 0.4169 0.2894 -0.077  -0.0186 0.0541  49  HIS C CE1 
2242 N  NE2 . HIS C 18  ? 0.302  0.4293 0.2945 -0.0648 -0.0175 0.0561  49  HIS C NE2 
2243 N  N   . HIS C 19  ? 0.2884 0.3416 0.2372 -0.0475 -0.0096 0.0297  50  HIS C N   
2244 C  CA  . HIS C 19  ? 0.2995 0.3408 0.2359 -0.046  -0.0075 0.0261  50  HIS C CA  
2245 C  C   . HIS C 19  ? 0.3192 0.3274 0.2289 -0.0505 -0.0045 0.0209  50  HIS C C   
2246 O  O   . HIS C 19  ? 0.3243 0.3176 0.2296 -0.048  -0.0012 0.0203  50  HIS C O   
2247 C  CB  . HIS C 19  ? 0.2933 0.338  0.2414 -0.0316 -0.0014 0.0252  50  HIS C CB  
2248 C  CG  . HIS C 19  ? 0.3057 0.3693 0.2673 -0.0281 -0.0026 0.0281  50  HIS C CG  
2249 N  ND1 . HIS C 19  ? 0.3252 0.3871 0.2786 -0.0292 -0.0025 0.0282  50  HIS C ND1 
2250 C  CD2 . HIS C 19  ? 0.3135 0.393  0.2929 -0.0225 -0.0026 0.0309  50  HIS C CD2 
2251 C  CE1 . HIS C 19  ? 0.3272 0.4042 0.2949 -0.0242 -0.0025 0.032   50  HIS C CE1 
2252 N  NE2 . HIS C 19  ? 0.3234 0.4091 0.3056 -0.0201 -0.0023 0.0332  50  HIS C NE2 
2253 N  N   . LYS C 20  ? 0.3426 0.3364 0.2318 -0.0559 -0.0049 0.0174  51  LYS C N   
2254 C  CA  . LYS C 20  ? 0.3796 0.3348 0.2367 -0.0585 -0.0003 0.0111  51  LYS C CA  
2255 C  C   . LYS C 20  ? 0.3933 0.3342 0.2508 -0.0395 0.0109  0.0098  51  LYS C C   
2256 O  O   . LYS C 20  ? 0.4245 0.3373 0.2649 -0.0369 0.016   0.0079  51  LYS C O   
2257 C  CB  . LYS C 20  ? 0.4021 0.3485 0.2381 -0.0647 -0.0017 0.0073  51  LYS C CB  
2258 C  CG  . LYS C 20  ? 0.4842 0.3854 0.2814 -0.0657 0.0046  -0.0005 51  LYS C CG  
2259 C  CD  . LYS C 20  ? 0.5461 0.4392 0.3195 -0.0732 0.0025  -0.0047 51  LYS C CD  
2260 C  CE  . LYS C 20  ? 0.6383 0.4839 0.371  -0.0689 0.012   -0.0132 51  LYS C CE  
2261 N  NZ  . LYS C 20  ? 0.7094 0.5441 0.413  -0.08   0.0085  -0.0183 51  LYS C NZ  
2262 N  N   . TYR C 21  ? 0.3692 0.3317 0.2472 -0.0267 0.0145  0.0123  52  TYR C N   
2263 C  CA  . TYR C 21  ? 0.368  0.3283 0.2521 -0.0097 0.0238  0.0136  52  TYR C CA  
2264 C  C   . TYR C 21  ? 0.3522 0.3364 0.2632 -0.0065 0.0211  0.0181  52  TYR C C   
2265 O  O   . TYR C 21  ? 0.3325 0.3424 0.2643 -0.0087 0.0164  0.0204  52  TYR C O   
2266 C  CB  . TYR C 21  ? 0.3639 0.3338 0.252  -0.0002 0.0295  0.0142  52  TYR C CB  
2267 C  CG  . TYR C 21  ? 0.3926 0.3377 0.2508 -0.0018 0.0333  0.0095  52  TYR C CG  
2268 C  CD1 . TYR C 21  ? 0.428  0.345  0.2627 0.0096  0.044   0.007   52  TYR C CD1 
2269 C  CD2 . TYR C 21  ? 0.4    0.3489 0.2509 -0.0139 0.0266  0.0078  52  TYR C CD2 
2270 C  CE1 . TYR C 21  ? 0.4555 0.3459 0.258  0.0088  0.0485  0.0016  52  TYR C CE1 
2271 C  CE2 . TYR C 21  ? 0.4385 0.365  0.2593 -0.0161 0.0298  0.003   52  TYR C CE2 
2272 C  CZ  . TYR C 21  ? 0.4732 0.368  0.2679 -0.0055 0.0407  -0.001  52  TYR C CZ  
2273 O  OH  . TYR C 21  ? 0.511  0.3801 0.2717 -0.0072 0.0447  -0.0068 52  TYR C OH  
2274 N  N   . ASP C 22  ? 0.3518 0.325  0.2595 -0.0014 0.0242  0.0194  53  ASP C N   
2275 C  CA  . ASP C 22  ? 0.3526 0.3464 0.2814 -0.0002 0.0208  0.0234  53  ASP C CA  
2276 C  C   . ASP C 22  ? 0.3304 0.3517 0.2826 0.0091  0.0222  0.0264  53  ASP C C   
2277 O  O   . ASP C 22  ? 0.3343 0.3735 0.3023 0.0072  0.0178  0.0282  53  ASP C O   
2278 C  CB  . ASP C 22  ? 0.4138 0.3894 0.3322 0.002   0.0233  0.0254  53  ASP C CB  
2279 C  CG  . ASP C 22  ? 0.4916 0.4482 0.3968 0.0171  0.0332  0.0268  53  ASP C CG  
2280 O  OD1 . ASP C 22  ? 0.4958 0.4676 0.4112 0.0285  0.0378  0.0286  53  ASP C OD1 
2281 O  OD2 . ASP C 22  ? 0.5628 0.49   0.4477 0.018   0.0369  0.0271  53  ASP C OD2 
2282 N  N   . HIS C 23  ? 0.3229 0.3486 0.2765 0.0172  0.0276  0.027   54  HIS C N   
2283 C  CA  . HIS C 23  ? 0.3087 0.3623 0.2841 0.0211  0.0275  0.0302  54  HIS C CA  
2284 C  C   . HIS C 23  ? 0.2739 0.3401 0.2601 0.0116  0.0213  0.0286  54  HIS C C   
2285 O  O   . HIS C 23  ? 0.2586 0.3428 0.2599 0.0111  0.0201  0.0303  54  HIS C O   
2286 C  CB  . HIS C 23  ? 0.3411 0.3988 0.3153 0.0311  0.0356  0.033   54  HIS C CB  
2287 C  CG  . HIS C 23  ? 0.4091 0.4636 0.3786 0.0454  0.0432  0.0375  54  HIS C CG  
2288 N  ND1 . HIS C 23  ? 0.464  0.4867 0.4085 0.0524  0.0498  0.0358  54  HIS C ND1 
2289 C  CD2 . HIS C 23  ? 0.4218 0.5006 0.4071 0.0541  0.0451  0.0444  54  HIS C CD2 
2290 C  CE1 . HIS C 23  ? 0.4686 0.4958 0.4145 0.0678  0.0569  0.0423  54  HIS C CE1 
2291 N  NE2 . HIS C 23  ? 0.4505 0.5145 0.4223 0.0692  0.0538  0.0483  54  HIS C NE2 
2292 N  N   . ASN C 24  ? 0.2608 0.317  0.2377 0.004   0.018   0.0261  55  ASN C N   
2293 C  CA  . ASN C 24  ? 0.2422 0.3085 0.2267 -0.0018 0.0138  0.0264  55  ASN C CA  
2294 C  C   . ASN C 24  ? 0.2402 0.3162 0.2345 -0.0056 0.0084  0.027   55  ASN C C   
2295 O  O   . ASN C 24  ? 0.2461 0.3288 0.2456 -0.0075 0.0062  0.0281  55  ASN C O   
2296 C  CB  . ASN C 24  ? 0.2396 0.296  0.2099 -0.0065 0.0129  0.0253  55  ASN C CB  
2297 C  CG  . ASN C 24  ? 0.2822 0.3325 0.244  -0.0015 0.0192  0.0251  55  ASN C CG  
2298 O  OD1 . ASN C 24  ? 0.2779 0.3387 0.2503 0.0039  0.0233  0.0274  55  ASN C OD1 
2299 N  ND2 . ASN C 24  ? 0.3034 0.3379 0.2449 -0.0045 0.0199  0.0226  55  ASN C ND2 
2300 N  N   . GLY C 25  ? 0.2387 0.3144 0.234  -0.0051 0.0074  0.0271  56  GLY C N   
2301 C  CA  . GLY C 25  ? 0.2313 0.3168 0.2345 -0.0069 0.0038  0.028   56  GLY C CA  
2302 C  C   . GLY C 25  ? 0.2277 0.3144 0.2328 -0.004  0.0044  0.0286  56  GLY C C   
2303 O  O   . GLY C 25  ? 0.2209 0.2998 0.2205 0       0.0075  0.0291  56  GLY C O   
2304 N  N   . PRO C 26  ? 0.2186 0.3147 0.2296 -0.0045 0.0021  0.0294  57  PRO C N   
2305 C  CA  . PRO C 26  ? 0.2178 0.3163 0.2295 -0.0016 0.0025  0.0308  57  PRO C CA  
2306 C  C   . PRO C 26  ? 0.2461 0.3305 0.2471 -0.0028 0.0039  0.0331  57  PRO C C   
2307 O  O   . PRO C 26  ? 0.2447 0.3207 0.238  -0.0098 0.0026  0.0335  57  PRO C O   
2308 C  CB  . PRO C 26  ? 0.2162 0.3251 0.2322 -0.0027 0.0004  0.0315  57  PRO C CB  
2309 C  CG  . PRO C 26  ? 0.2152 0.3272 0.2348 -0.0024 0.0002  0.0294  57  PRO C CG  
2310 C  CD  . PRO C 26  ? 0.1967 0.3015 0.2127 -0.0054 0.0003  0.0298  57  PRO C CD  
2311 N  N   . LYS C 27  ? 0.2438 0.3243 0.2424 0.0038  0.0069  0.035   58  LYS C N   
2312 C  CA  . LYS C 27  ? 0.2675 0.3279 0.2521 0.0049  0.01    0.0376  58  LYS C CA  
2313 C  C   . LYS C 27  ? 0.2825 0.3485 0.2691 0.0089  0.0101  0.0422  58  LYS C C   
2314 O  O   . LYS C 27  ? 0.2845 0.3679 0.2811 0.0151  0.0096  0.0434  58  LYS C O   
2315 C  CB  . LYS C 27  ? 0.3141 0.3625 0.2913 0.0137  0.0158  0.0376  58  LYS C CB  
2316 C  CG  . LYS C 27  ? 0.4032 0.4242 0.3614 0.0182  0.0212  0.0402  58  LYS C CG  
2317 C  CD  . LYS C 27  ? 0.5128 0.5315 0.4686 0.0334  0.0286  0.0428  58  LYS C CD  
2318 C  CE  . LYS C 27  ? 0.6201 0.6085 0.5548 0.0427  0.0363  0.0465  58  LYS C CE  
2319 N  NZ  . LYS C 27  ? 0.6764 0.6587 0.6045 0.0585  0.0454  0.0486  58  LYS C NZ  
2320 N  N   . PHE C 28  ? 0.2912 0.343  0.2675 0.0041  0.0105  0.0452  59  PHE C N   
2321 C  CA  . PHE C 28  ? 0.2925 0.3496 0.2696 0.0075  0.0108  0.0508  59  PHE C CA  
2322 C  C   . PHE C 28  ? 0.3154 0.3467 0.2763 0.0134  0.0163  0.0556  59  PHE C C   
2323 O  O   . PHE C 28  ? 0.3331 0.3365 0.2774 0.0088  0.019   0.0539  59  PHE C O   
2324 C  CB  . PHE C 28  ? 0.2854 0.351  0.2651 -0.003  0.0073  0.0524  59  PHE C CB  
2325 C  CG  . PHE C 28  ? 0.267  0.356  0.2606 -0.0044 0.0038  0.0486  59  PHE C CG  
2326 C  CD1 . PHE C 28  ? 0.2746 0.3647 0.2703 -0.0104 0.0019  0.0453  59  PHE C CD1 
2327 C  CD2 . PHE C 28  ? 0.263  0.3703 0.2646 0.001   0.0029  0.0485  59  PHE C CD2 
2328 C  CE1 . PHE C 28  ? 0.2769 0.384  0.2828 -0.0089 0.0002  0.0427  59  PHE C CE1 
2329 C  CE2 . PHE C 28  ? 0.2664 0.3876 0.2756 0.0007  0.0011  0.0445  59  PHE C CE2 
2330 C  CZ  . PHE C 28  ? 0.2651 0.385  0.2766 -0.0031 0.0003  0.0419  59  PHE C CZ  
2331 N  N   . GLU C 29  ? 0.3192 0.3582 0.2825 0.0236  0.0183  0.0617  60  GLU C N   
2332 C  CA  . GLU C 29  ? 0.3434 0.3584 0.291  0.0331  0.0248  0.0685  60  GLU C CA  
2333 C  C   . GLU C 29  ? 0.3372 0.3681 0.2898 0.04    0.0243  0.0768  60  GLU C C   
2334 O  O   . GLU C 29  ? 0.3265 0.3875 0.2939 0.0381  0.019   0.0758  60  GLU C O   
2335 C  CB  . GLU C 29  ? 0.383  0.3932 0.3282 0.0476  0.0306  0.069   60  GLU C CB  
2336 C  CG  . GLU C 29  ? 0.4294 0.4778 0.3956 0.0556  0.0279  0.0702  60  GLU C CG  
2337 C  CD  . GLU C 29  ? 0.5488 0.5962 0.5134 0.071   0.0349  0.0736  60  GLU C CD  
2338 O  OE1 . GLU C 29  ? 0.5705 0.5946 0.5233 0.0708  0.0394  0.069   60  GLU C OE1 
2339 O  OE2 . GLU C 29  ? 0.5873 0.6591 0.5618 0.0835  0.0361  0.0817  60  GLU C OE2 
2340 N  N   . LYS C 30  ? 0.3536 0.3618 0.291  0.0485  0.0303  0.0849  61  LYS C N   
2341 C  CA  . LYS C 30  ? 0.3615 0.3838 0.3013 0.057   0.0306  0.0947  61  LYS C CA  
2342 C  C   . LYS C 30  ? 0.3584 0.3967 0.3041 0.0447  0.0251  0.0949  61  LYS C C   
2343 O  O   . LYS C 30  ? 0.3562 0.4225 0.3113 0.0493  0.0219  0.0987  61  LYS C O   
2344 C  CB  . LYS C 30  ? 0.3766 0.4327 0.3317 0.0714  0.0294  0.098   61  LYS C CB  
2345 C  CG  . LYS C 30  ? 0.4688 0.5124 0.4182 0.0872  0.037   0.1013  61  LYS C CG  
2346 C  CD  . LYS C 30  ? 0.5261 0.6112 0.494  0.0992  0.0351  0.1062  61  LYS C CD  
2347 C  CE  . LYS C 30  ? 0.5817 0.6597 0.5448 0.1187  0.0445  0.113   61  LYS C CE  
2348 N  NZ  . LYS C 30  ? 0.6302 0.6828 0.585  0.1147  0.0487  0.1037  61  LYS C NZ  
2349 N  N   . ALA C 31  ? 0.3593 0.3808 0.298  0.029   0.0242  0.0919  62  ALA C N   
2350 C  CA  . ALA C 31  ? 0.3559 0.3931 0.2996 0.0181  0.0207  0.0941  62  ALA C CA  
2351 C  C   . ALA C 31  ? 0.3683 0.3977 0.3019 0.0233  0.0244  0.1058  62  ALA C C   
2352 O  O   . ALA C 31  ? 0.3954 0.392  0.3116 0.028   0.0302  0.1116  62  ALA C O   
2353 C  CB  . ALA C 31  ? 0.3621 0.3857 0.3008 -0.0001 0.0193  0.0911  62  ALA C CB  
2354 N  N   . GLY C 32  ? 0.3447 0.4026 0.287  0.0244  0.0217  0.1092  63  GLY C N   
2355 C  CA  . GLY C 32  ? 0.3369 0.3938 0.2709 0.0297  0.0246  0.1211  63  GLY C CA  
2356 C  C   . GLY C 32  ? 0.3195 0.4041 0.2605 0.0233  0.0219  0.1227  63  GLY C C   
2357 O  O   . GLY C 32  ? 0.2958 0.4    0.248  0.0166  0.0184  0.1146  63  GLY C O   
2358 N  N   . LYS C 33  ? 0.317  0.4017 0.2497 0.0265  0.0247  0.1342  64  LYS C N   
2359 C  CA  . LYS C 33  ? 0.3256 0.4359 0.2616 0.0228  0.0239  0.1379  64  LYS C CA  
2360 C  C   . LYS C 33  ? 0.33   0.4452 0.271  0.0069  0.024   0.1357  64  LYS C C   
2361 O  O   . LYS C 33  ? 0.3156 0.4586 0.2652 0.006   0.0225  0.1321  64  LYS C O   
2362 C  CB  . LYS C 33  ? 0.3336 0.4767 0.2779 0.032   0.0193  0.1319  64  LYS C CB  
2363 C  CG  . LYS C 33  ? 0.4027 0.55   0.3445 0.0466  0.0179  0.1359  64  LYS C CG  
2364 C  CD  . LYS C 33  ? 0.4612 0.6421 0.4062 0.0513  0.0126  0.1323  64  LYS C CD  
2365 C  CE  . LYS C 33  ? 0.5336 0.727  0.4803 0.0631  0.0092  0.1357  64  LYS C CE  
2366 N  NZ  . LYS C 33  ? 0.5699 0.7943 0.5136 0.0661  0.0037  0.1365  64  LYS C NZ  
2367 N  N   . GLY C 34  ? 0.3474 0.436  0.2819 -0.0056 0.0257  0.1379  65  GLY C N   
2368 C  CA  . GLY C 34  ? 0.3408 0.4389 0.2813 -0.0227 0.0249  0.1382  65  GLY C CA  
2369 C  C   . GLY C 34  ? 0.3343 0.4324 0.2832 -0.0291 0.0211  0.1272  65  GLY C C   
2370 O  O   . GLY C 34  ? 0.3299 0.4309 0.2815 -0.0449 0.0198  0.1287  65  GLY C O   
2371 N  N   . ALA C 35  ? 0.3196 0.4166 0.2727 -0.0177 0.0189  0.1172  66  ALA C N   
2372 C  CA  . ALA C 35  ? 0.3143 0.408  0.2733 -0.0231 0.0158  0.1075  66  ALA C CA  
2373 C  C   . ALA C 35  ? 0.3499 0.4044 0.293  -0.0302 0.0171  0.1077  66  ALA C C   
2374 O  O   . ALA C 35  ? 0.3714 0.4005 0.3007 -0.0228 0.021   0.1122  66  ALA C O   
2375 C  CB  . ALA C 35  ? 0.2918 0.3968 0.2593 -0.0101 0.0136  0.0979  66  ALA C CB  
2376 N  N   . GLU C 36  ? 0.3586 0.4073 0.3015 -0.044  0.0143  0.1035  67  GLU C N   
2377 C  CA  . GLU C 36  ? 0.3961 0.4047 0.3195 -0.0534 0.0153  0.1018  67  GLU C CA  
2378 C  C   . GLU C 36  ? 0.4044 0.4161 0.3323 -0.06   0.011   0.0926  67  GLU C C   
2379 O  O   . GLU C 36  ? 0.3934 0.4353 0.3362 -0.0679 0.0068  0.0924  67  GLU C O   
2380 C  CB  . GLU C 36  ? 0.466  0.4609 0.3772 -0.0739 0.0155  0.1106  67  GLU C CB  
2381 C  CG  . GLU C 36  ? 0.6259 0.5694 0.5086 -0.0758 0.0208  0.1145  67  GLU C CG  
2382 C  CD  . GLU C 36  ? 0.7972 0.7179 0.6628 -0.103  0.0193  0.1195  67  GLU C CD  
2383 O  OE1 . GLU C 36  ? 0.8155 0.7543 0.6866 -0.1141 0.019   0.1298  67  GLU C OE1 
2384 O  OE2 . GLU C 36  ? 0.8838 0.7694 0.7293 -0.1147 0.0184  0.1132  67  GLU C OE2 
2385 N  N   . LEU C 37  ? 0.4188 0.3997 0.3327 -0.0564 0.0127  0.0862  68  LEU C N   
2386 C  CA  . LEU C 37  ? 0.4377 0.4172 0.3512 -0.0644 0.0088  0.078   68  LEU C CA  
2387 C  C   . LEU C 37  ? 0.4693 0.4221 0.3622 -0.0878 0.0068  0.0798  68  LEU C C   
2388 O  O   . LEU C 37  ? 0.4964 0.406  0.3636 -0.0906 0.0113  0.0812  68  LEU C O   
2389 C  CB  . LEU C 37  ? 0.4559 0.416  0.3624 -0.0491 0.0126  0.0708  68  LEU C CB  
2390 C  CG  . LEU C 37  ? 0.4632 0.4552 0.3918 -0.0326 0.0121  0.0681  68  LEU C CG  
2391 C  CD1 . LEU C 37  ? 0.496  0.4722 0.4184 -0.016  0.0172  0.0654  68  LEU C CD1 
2392 C  CD2 . LEU C 37  ? 0.4554 0.4732 0.3991 -0.0384 0.0067  0.063   68  LEU C CD2 
2393 N  N   . THR C 38  ? 0.4626 0.4418 0.3658 -0.1051 0.0001  0.0815  69  THR C N   
2394 C  CA  . THR C 38  ? 0.4851 0.4482 0.3713 -0.1321 -0.0038 0.085   69  THR C CA  
2395 C  C   . THR C 38  ? 0.4999 0.4654 0.3817 -0.1461 -0.0104 0.0788  69  THR C C   
2396 O  O   . THR C 38  ? 0.4676 0.4722 0.3719 -0.1411 -0.0143 0.0779  69  THR C O   
2397 C  CB  . THR C 38  ? 0.4826 0.4839 0.3862 -0.1434 -0.0064 0.0967  69  THR C CB  
2398 O  OG1 . THR C 38  ? 0.4978 0.5014 0.4064 -0.1283 -0.0003 0.1024  69  THR C OG1 
2399 C  CG2 . THR C 38  ? 0.497  0.4855 0.3845 -0.1742 -0.0107 0.1029  69  THR C CG2 
2400 N  N   . ASN C 39  ? 0.5469 0.4709 0.3981 -0.165  -0.012  0.0752  70  ASN C N   
2401 C  CA  . ASN C 39  ? 0.5785 0.5051 0.4221 -0.1814 -0.0195 0.0697  70  ASN C CA  
2402 C  C   . ASN C 39  ? 0.5732 0.555  0.441  -0.1988 -0.0285 0.0788  70  ASN C C   
2403 O  O   . ASN C 39  ? 0.5801 0.5771 0.4542 -0.211  -0.0294 0.089   70  ASN C O   
2404 C  CB  . ASN C 39  ? 0.649  0.5165 0.4498 -0.201  -0.0194 0.064   70  ASN C CB  
2405 C  CG  . ASN C 39  ? 0.7178 0.5867 0.5069 -0.2189 -0.0278 0.0576  70  ASN C CG  
2406 O  OD1 . ASN C 39  ? 0.7437 0.6266 0.5287 -0.2479 -0.0369 0.0621  70  ASN C OD1 
2407 N  ND2 . ASN C 39  ? 0.7381 0.5978 0.5231 -0.2028 -0.0253 0.0481  70  ASN C ND2 
2408 N  N   . ILE C 40  ? 0.5649 0.5796 0.4477 -0.1976 -0.0341 0.0768  71  ILE C N   
2409 C  CA  . ILE C 40  ? 0.5538 0.6261 0.4615 -0.2096 -0.0418 0.0872  71  ILE C CA  
2410 C  C   . ILE C 40  ? 0.5784 0.6532 0.4739 -0.2444 -0.0492 0.0954  71  ILE C C   
2411 O  O   . ILE C 40  ? 0.5684 0.6876 0.4858 -0.2514 -0.0511 0.1083  71  ILE C O   
2412 C  CB  . ILE C 40  ? 0.5458 0.6455 0.4653 -0.2031 -0.0465 0.084   71  ILE C CB  
2413 C  CG1 . ILE C 40  ? 0.5242 0.689  0.4732 -0.2083 -0.0523 0.0973  71  ILE C CG1 
2414 C  CG2 . ILE C 40  ? 0.5695 0.6347 0.4585 -0.2204 -0.0519 0.0752  71  ILE C CG2 
2415 C  CD1 . ILE C 40  ? 0.5088 0.7088 0.4856 -0.1902 -0.0458 0.1063  71  ILE C CD1 
2416 N  N   . ASP C 41  ? 0.6153 0.6402 0.4738 -0.2663 -0.0522 0.0884  72  ASP C N   
2417 C  CA  . ASP C 41  ? 0.6384 0.6593 0.4804 -0.3039 -0.0598 0.0956  72  ASP C CA  
2418 C  C   . ASP C 41  ? 0.6375 0.6555 0.4828 -0.309  -0.0548 0.106   72  ASP C C   
2419 O  O   . ASP C 41  ? 0.6482 0.6773 0.4888 -0.34   -0.061  0.1158  72  ASP C O   
2420 C  CB  . ASP C 41  ? 0.7154 0.6694 0.5092 -0.3246 -0.062  0.0838  72  ASP C CB  
2421 C  CG  . ASP C 41  ? 0.8153 0.7655 0.5989 -0.3223 -0.0666 0.0732  72  ASP C CG  
2422 O  OD1 . ASP C 41  ? 0.8125 0.821  0.6254 -0.3188 -0.0732 0.0785  72  ASP C OD1 
2423 O  OD2 . ASP C 41  ? 0.8865 0.7745 0.6314 -0.3227 -0.0629 0.0602  72  ASP C OD2 
2424 N  N   . ALA C 42  ? 0.6325 0.6344 0.4837 -0.2807 -0.044  0.1044  73  ALA C N   
2425 C  CA  . ALA C 42  ? 0.6277 0.6278 0.4821 -0.2818 -0.0384 0.1147  73  ALA C CA  
2426 C  C   . ALA C 42  ? 0.5926 0.6529 0.4874 -0.2598 -0.0348 0.1241  73  ALA C C   
2427 O  O   . ALA C 42  ? 0.5974 0.659  0.4967 -0.2543 -0.0288 0.132   73  ALA C O   
2428 C  CB  . ALA C 42  ? 0.6612 0.5945 0.4864 -0.2683 -0.0285 0.1078  73  ALA C CB  
2429 N  N   . ALA C 43  ? 0.5577 0.6648 0.4788 -0.2466 -0.0379 0.1233  74  ALA C N   
2430 C  CA  . ALA C 43  ? 0.5236 0.6837 0.4787 -0.2245 -0.0339 0.1305  74  ALA C CA  
2431 C  C   . ALA C 43  ? 0.4967 0.716  0.4743 -0.2351 -0.0414 0.1396  74  ALA C C   
2432 O  O   . ALA C 43  ? 0.4691 0.7204 0.4671 -0.2147 -0.0404 0.1385  74  ALA C O   
2433 C  CB  . ALA C 43  ? 0.5192 0.6685 0.48   -0.192  -0.0282 0.1191  74  ALA C CB  
2434 N  N   . SER C 44  ? 0.504  0.7384 0.4774 -0.2677 -0.0486 0.1499  75  SER C N   
2435 C  CA  . SER C 44  ? 0.4831 0.7772 0.4761 -0.2838 -0.0572 0.1618  75  SER C CA  
2436 C  C   . SER C 44  ? 0.4358 0.796  0.4657 -0.2611 -0.0524 0.1739  75  SER C C   
2437 O  O   . SER C 44  ? 0.4289 0.8361 0.4769 -0.2599 -0.0573 0.1805  75  SER C O   
2438 C  CB  . SER C 44  ? 0.5092 0.8083 0.4908 -0.325  -0.0651 0.1727  75  SER C CB  
2439 O  OG  . SER C 44  ? 0.5673 0.8712 0.5539 -0.3273 -0.0586 0.1831  75  SER C OG  
2440 N  N   . ALA C 45  ? 0.406  0.7693 0.4449 -0.2417 -0.0423 0.177   76  ALA C N   
2441 C  CA  . ALA C 45  ? 0.3623 0.7808 0.4307 -0.217  -0.0356 0.1869  76  ALA C CA  
2442 C  C   . ALA C 45  ? 0.341  0.7623 0.4175 -0.1885 -0.0334 0.1773  76  ALA C C   
2443 O  O   . ALA C 45  ? 0.3286 0.7986 0.4273 -0.1724 -0.0304 0.1864  76  ALA C O   
2444 C  CB  . ALA C 45  ? 0.3627 0.7751 0.4327 -0.2018 -0.0251 0.1895  76  ALA C CB  
2445 N  N   . TYR C 46  ? 0.335  0.7048 0.3926 -0.1824 -0.0345 0.1601  77  TYR C N   
2446 C  CA  . TYR C 46  ? 0.3175 0.6854 0.3802 -0.1587 -0.0328 0.151   77  TYR C CA  
2447 C  C   . TYR C 46  ? 0.3389 0.7139 0.3988 -0.1716 -0.0422 0.1498  77  TYR C C   
2448 O  O   . TYR C 46  ? 0.3435 0.7206 0.4082 -0.1534 -0.0411 0.1446  77  TYR C O   
2449 C  CB  . TYR C 46  ? 0.3133 0.6269 0.3594 -0.1431 -0.0278 0.1344  77  TYR C CB  
2450 C  CG  . TYR C 46  ? 0.2897 0.603  0.3432 -0.1158 -0.0233 0.1265  77  TYR C CG  
2451 C  CD1 . TYR C 46  ? 0.2722 0.6164 0.3422 -0.0945 -0.0163 0.1319  77  TYR C CD1 
2452 C  CD2 . TYR C 46  ? 0.3101 0.5876 0.3509 -0.1109 -0.0247 0.1132  77  TYR C CD2 
2453 C  CE1 . TYR C 46  ? 0.2754 0.6114 0.3474 -0.0711 -0.0116 0.1237  77  TYR C CE1 
2454 C  CE2 . TYR C 46  ? 0.3094 0.5837 0.3555 -0.0881 -0.0204 0.1062  77  TYR C CE2 
2455 C  CZ  . TYR C 46  ? 0.2934 0.5947 0.3541 -0.0692 -0.0141 0.1111  77  TYR C CZ  
2456 O  OH  . TYR C 46  ? 0.2909 0.5835 0.3529 -0.049  -0.0098 0.1038  77  TYR C OH  
2457 N  N   . ALA C 47  ? 0.3527 0.7287 0.4021 -0.2036 -0.0516 0.1544  78  ALA C N   
2458 C  CA  . ALA C 47  ? 0.3753 0.7551 0.4168 -0.2196 -0.0619 0.1526  78  ALA C CA  
2459 C  C   . ALA C 47  ? 0.3667 0.7978 0.4312 -0.2038 -0.0633 0.1609  78  ALA C C   
2460 O  O   . ALA C 47  ? 0.3853 0.8004 0.4425 -0.1958 -0.0653 0.1522  78  ALA C O   
2461 C  CB  . ALA C 47  ? 0.3829 0.7686 0.4123 -0.2594 -0.0724 0.16    78  ALA C CB  
2462 N  N   . GLU C 48  ? 0.3379 0.8296 0.4292 -0.1976 -0.0612 0.1785  79  GLU C N   
2463 C  CA  . GLU C 48  ? 0.315  0.8563 0.4272 -0.1804 -0.0614 0.1888  79  GLU C CA  
2464 C  C   . GLU C 48  ? 0.3096 0.8329 0.4256 -0.1426 -0.0505 0.1802  79  GLU C C   
2465 O  O   . GLU C 48  ? 0.2983 0.8263 0.4157 -0.1315 -0.0522 0.179   79  GLU C O   
2466 C  CB  . GLU C 48  ? 0.3307 0.9446 0.4695 -0.1844 -0.0615 0.2121  79  GLU C CB  
2467 C  CG  . GLU C 48  ? 0.4491 1.0894 0.585  -0.2257 -0.0756 0.2222  79  GLU C CG  
2468 C  CD  . GLU C 48  ? 0.6146 1.2538 0.7389 -0.2419 -0.0883 0.2187  79  GLU C CD  
2469 O  OE1 . GLU C 48  ? 0.6325 1.3217 0.7753 -0.2293 -0.0903 0.2307  79  GLU C OE1 
2470 O  OE2 . GLU C 48  ? 0.6874 1.2749 0.7823 -0.266  -0.0955 0.2044  79  GLU C OE2 
2471 N  N   . THR C 49  ? 0.3201 0.818  0.4344 -0.1249 -0.0399 0.1733  80  THR C N   
2472 C  CA  . THR C 49  ? 0.3471 0.8224 0.4607 -0.0933 -0.0305 0.1635  80  THR C CA  
2473 C  C   . THR C 49  ? 0.3755 0.8025 0.4704 -0.0954 -0.0344 0.1471  80  THR C C   
2474 O  O   . THR C 49  ? 0.3856 0.8116 0.4824 -0.0793 -0.0327 0.1447  80  THR C O   
2475 C  CB  . THR C 49  ? 0.3759 0.8318 0.4874 -0.0782 -0.0203 0.1583  80  THR C CB  
2476 O  OG1 . THR C 49  ? 0.3717 0.8745 0.5005 -0.0704 -0.0144 0.174   80  THR C OG1 
2477 C  CG2 . THR C 49  ? 0.3992 0.8216 0.5037 -0.0522 -0.0127 0.1451  80  THR C CG2 
2478 N  N   . PHE C 50  ? 0.3921 0.7792 0.4681 -0.1147 -0.0387 0.1369  81  PHE C N   
2479 C  CA  . PHE C 50  ? 0.4259 0.7675 0.4826 -0.1165 -0.0412 0.122   81  PHE C CA  
2480 C  C   . PHE C 50  ? 0.4415 0.7981 0.4971 -0.1228 -0.0487 0.1244  81  PHE C C   
2481 O  O   . PHE C 50  ? 0.4675 0.8071 0.5193 -0.1084 -0.0463 0.1171  81  PHE C O   
2482 C  CB  . PHE C 50  ? 0.4382 0.7374 0.4728 -0.1363 -0.0438 0.1136  81  PHE C CB  
2483 C  CG  . PHE C 50  ? 0.4583 0.7073 0.4738 -0.1299 -0.0416 0.098   81  PHE C CG  
2484 C  CD1 . PHE C 50  ? 0.4632 0.6956 0.4823 -0.1066 -0.0337 0.0905  81  PHE C CD1 
2485 C  CD2 . PHE C 50  ? 0.486  0.7056 0.4787 -0.1477 -0.0473 0.0912  81  PHE C CD2 
2486 C  CE1 . PHE C 50  ? 0.4869 0.6803 0.4912 -0.1007 -0.0315 0.0784  81  PHE C CE1 
2487 C  CE2 . PHE C 50  ? 0.5108 0.6878 0.4864 -0.1391 -0.0438 0.0782  81  PHE C CE2 
2488 C  CZ  . PHE C 50  ? 0.5033 0.6698 0.4866 -0.1157 -0.0358 0.0728  81  PHE C CZ  
2489 N  N   . LYS C 51  ? 0.4214 0.8138 0.4811 -0.144  -0.0577 0.136   82  LYS C N   
2490 C  CA  . LYS C 51  ? 0.4157 0.8269 0.4733 -0.1519 -0.0662 0.1398  82  LYS C CA  
2491 C  C   . LYS C 51  ? 0.3929 0.8345 0.4683 -0.1251 -0.0618 0.1473  82  LYS C C   
2492 O  O   . LYS C 51  ? 0.3978 0.8453 0.4686 -0.1264 -0.0672 0.1481  82  LYS C O   
2493 C  CB  . LYS C 51  ? 0.4325 0.8833 0.4925 -0.1821 -0.0777 0.1528  82  LYS C CB  
2494 C  CG  . LYS C 51  ? 0.5285 0.9396 0.5615 -0.2137 -0.0842 0.1438  82  LYS C CG  
2495 N  N   . LYS C 52  ? 0.3603 0.8203 0.4534 -0.1013 -0.0519 0.1536  83  LYS C N   
2496 C  CA  . LYS C 52  ? 0.3297 0.8124 0.4362 -0.0738 -0.0456 0.1613  83  LYS C CA  
2497 C  C   . LYS C 52  ? 0.3186 0.7556 0.4156 -0.0515 -0.0368 0.1472  83  LYS C C   
2498 O  O   . LYS C 52  ? 0.314  0.7599 0.4176 -0.0287 -0.0306 0.1522  83  LYS C O   
2499 C  CB  . LYS C 52  ? 0.3441 0.8734 0.4722 -0.0588 -0.0386 0.1774  83  LYS C CB  
2500 C  CG  . LYS C 52  ? 0.3669 0.9571 0.51   -0.0779 -0.0474 0.1966  83  LYS C CG  
2501 C  CD  . LYS C 52  ? 0.4085 1.0516 0.575  -0.0586 -0.0388 0.2152  83  LYS C CD  
2502 C  CE  . LYS C 52  ? 0.4711 1.1019 0.6383 -0.0554 -0.0304 0.2116  83  LYS C CE  
2503 N  NZ  . LYS C 52  ? 0.4764 1.1665 0.666  -0.0409 -0.0227 0.2322  83  LYS C NZ  
2504 N  N   . GLY C 53  ? 0.3089 0.6984 0.3905 -0.0577 -0.0358 0.1311  84  GLY C N   
2505 C  CA  . GLY C 53  ? 0.2979 0.6477 0.3713 -0.0403 -0.0285 0.1185  84  GLY C CA  
2506 C  C   . GLY C 53  ? 0.2706 0.6067 0.3359 -0.038  -0.031  0.1148  84  GLY C C   
2507 O  O   . GLY C 53  ? 0.2547 0.6051 0.3162 -0.0523 -0.0394 0.1192  84  GLY C O   
2508 N  N   . VAL C 54  ? 0.2555 0.5639 0.3168 -0.0207 -0.0237 0.1071  85  VAL C N   
2509 C  CA  . VAL C 54  ? 0.2505 0.5422 0.3033 -0.0175 -0.0244 0.1034  85  VAL C CA  
2510 C  C   . VAL C 54  ? 0.2595 0.5118 0.298  -0.0273 -0.025  0.0885  85  VAL C C   
2511 O  O   . VAL C 54  ? 0.2507 0.4822 0.2882 -0.0214 -0.0197 0.0808  85  VAL C O   
2512 C  CB  . VAL C 54  ? 0.2505 0.5357 0.3064 0.0058  -0.0157 0.1057  85  VAL C CB  
2513 C  CG1 . VAL C 54  ? 0.2588 0.5224 0.3045 0.0066  -0.0163 0.1013  85  VAL C CG1 
2514 C  CG2 . VAL C 54  ? 0.2428 0.5677 0.3117 0.0194  -0.0135 0.1224  85  VAL C CG2 
2515 N  N   . PHE C 55  ? 0.2663 0.5105 0.2924 -0.0422 -0.0314 0.0854  86  PHE C N   
2516 C  CA  . PHE C 55  ? 0.2864 0.4945 0.297  -0.0498 -0.0308 0.0728  86  PHE C CA  
2517 C  C   . PHE C 55  ? 0.2862 0.477  0.2871 -0.0458 -0.0294 0.0683  86  PHE C C   
2518 O  O   . PHE C 55  ? 0.2812 0.4888 0.2834 -0.0438 -0.032  0.0753  86  PHE C O   
2519 C  CB  . PHE C 55  ? 0.2945 0.4997 0.2922 -0.0716 -0.038  0.0716  86  PHE C CB  
2520 C  CG  . PHE C 55  ? 0.2964 0.5144 0.3019 -0.078  -0.0389 0.0758  86  PHE C CG  
2521 C  CD1 . PHE C 55  ? 0.3101 0.5045 0.3124 -0.0758 -0.034  0.069   86  PHE C CD1 
2522 C  CD2 . PHE C 55  ? 0.2875 0.5444 0.3039 -0.0863 -0.0444 0.088   86  PHE C CD2 
2523 C  CE1 . PHE C 55  ? 0.3133 0.5195 0.3221 -0.0813 -0.0342 0.0739  86  PHE C CE1 
2524 C  CE2 . PHE C 55  ? 0.2864 0.5574 0.3107 -0.0923 -0.0443 0.0931  86  PHE C CE2 
2525 C  CZ  . PHE C 55  ? 0.2976 0.5411 0.317  -0.0901 -0.0391 0.0856  86  PHE C CZ  
2526 N  N   . PRO C 56  ? 0.2941 0.4541 0.2852 -0.0443 -0.0251 0.058   87  PRO C N   
2527 C  CA  . PRO C 56  ? 0.3056 0.4518 0.287  -0.0416 -0.0233 0.0548  87  PRO C CA  
2528 C  C   . PRO C 56  ? 0.2983 0.4458 0.2631 -0.0552 -0.0298 0.0554  87  PRO C C   
2529 O  O   . PRO C 56  ? 0.2868 0.4352 0.2427 -0.0699 -0.0355 0.0548  87  PRO C O   
2530 C  CB  . PRO C 56  ? 0.3233 0.4419 0.2985 -0.0383 -0.0173 0.0454  87  PRO C CB  
2531 C  CG  . PRO C 56  ? 0.3301 0.4434 0.3038 -0.0446 -0.0184 0.0429  87  PRO C CG  
2532 C  CD  . PRO C 56  ? 0.296  0.4357 0.2842 -0.0449 -0.0216 0.0507  87  PRO C CD  
2533 N  N   . ASN C 57  ? 0.3134 0.459  0.2713 -0.0518 -0.0292 0.0564  88  ASN C N   
2534 C  CA  . ASN C 57  ? 0.3362 0.4811 0.2745 -0.0648 -0.0354 0.0561  88  ASN C CA  
2535 C  C   . ASN C 57  ? 0.3476 0.4607 0.262  -0.076  -0.0349 0.045   88  ASN C C   
2536 O  O   . ASN C 57  ? 0.3629 0.4739 0.2593 -0.0929 -0.042  0.0438  88  ASN C O   
2537 C  CB  . ASN C 57  ? 0.3771 0.5225 0.311  -0.057  -0.0331 0.0589  88  ASN C CB  
2538 C  CG  . ASN C 57  ? 0.4263 0.6009 0.3776 -0.0472 -0.0343 0.0715  88  ASN C CG  
2539 O  OD1 . ASN C 57  ? 0.4114 0.6151 0.3685 -0.0527 -0.0416 0.0805  88  ASN C OD1 
2540 N  ND2 . ASN C 57  ? 0.4368 0.6042 0.3959 -0.0325 -0.0268 0.0734  88  ASN C ND2 
2541 N  N   . ASN C 58  ? 0.3392 0.4276 0.252  -0.0668 -0.0263 0.0378  89  ASN C N   
2542 C  CA  . ASN C 58  ? 0.3712 0.4259 0.2605 -0.0717 -0.0228 0.0283  89  ASN C CA  
2543 C  C   . ASN C 58  ? 0.377  0.4273 0.2733 -0.0744 -0.0228 0.0275  89  ASN C C   
2544 O  O   . ASN C 58  ? 0.3714 0.4145 0.2777 -0.063  -0.0162 0.0256  89  ASN C O   
2545 C  CB  . ASN C 58  ? 0.387  0.4251 0.2748 -0.0568 -0.0124 0.0241  89  ASN C CB  
2546 C  CG  . ASN C 58  ? 0.4305 0.4342 0.2911 -0.0563 -0.006  0.0158  89  ASN C CG  
2547 O  OD1 . ASN C 58  ? 0.4457 0.4378 0.3097 -0.0444 0.0025  0.0135  89  ASN C OD1 
2548 N  ND2 . ASN C 58  ? 0.4243 0.4116 0.2559 -0.068  -0.0094 0.0116  89  ASN C ND2 
2549 N  N   . LYS C 59  ? 0.3854 0.445  0.2781 -0.0902 -0.0309 0.0305  90  LYS C N   
2550 C  CA  . LYS C 59  ? 0.397  0.4582 0.2974 -0.0951 -0.0319 0.0322  90  LYS C CA  
2551 C  C   . LYS C 59  ? 0.4123 0.4347 0.2844 -0.106  -0.0304 0.0249  90  LYS C C   
2552 O  O   . LYS C 59  ? 0.4236 0.4244 0.2677 -0.1179 -0.0328 0.0198  90  LYS C O   
2553 C  CB  . LYS C 59  ? 0.4338 0.5324 0.3481 -0.1067 -0.0411 0.0421  90  LYS C CB  
2554 C  CG  . LYS C 59  ? 0.5058 0.612  0.4277 -0.1152 -0.0432 0.046   90  LYS C CG  
2555 C  CD  . LYS C 59  ? 0.5666 0.7182 0.506  -0.1239 -0.0512 0.0582  90  LYS C CD  
2556 C  CE  . LYS C 59  ? 0.6202 0.7848 0.546  -0.1426 -0.0612 0.0613  90  LYS C CE  
2557 N  NZ  . LYS C 59  ? 0.6335 0.8488 0.5786 -0.1515 -0.0691 0.0757  90  LYS C NZ  
2558 N  N   . ARG C 60  ? 0.4092 0.4207 0.2863 -0.1015 -0.026  0.0246  91  ARG C N   
2559 C  CA  . ARG C 60  ? 0.4556 0.4279 0.3075 -0.1085 -0.0228 0.0195  91  ARG C CA  
2560 C  C   . ARG C 60  ? 0.4863 0.4561 0.3214 -0.1353 -0.0322 0.0212  91  ARG C C   
2561 O  O   . ARG C 60  ? 0.4639 0.4718 0.3188 -0.1446 -0.0399 0.0295  91  ARG C O   
2562 C  CB  . ARG C 60  ? 0.4646 0.441  0.3346 -0.0975 -0.0179 0.023   91  ARG C CB  
2563 C  CG  . ARG C 60  ? 0.5267 0.4629 0.375  -0.0966 -0.0116 0.0197  91  ARG C CG  
2564 C  CD  . ARG C 60  ? 0.5126 0.4609 0.3826 -0.082  -0.0069 0.0243  91  ARG C CD  
2565 N  NE  . ARG C 60  ? 0.531  0.4943 0.4189 -0.0621 -0.0019 0.0235  91  ARG C NE  
2566 C  CZ  . ARG C 60  ? 0.5047 0.4917 0.417  -0.0506 -0.0005 0.0272  91  ARG C CZ  
2567 N  NH1 . ARG C 60  ? 0.51   0.5082 0.4318 -0.0541 -0.0026 0.032   91  ARG C NH1 
2568 N  NH2 . ARG C 60  ? 0.431  0.4302 0.3565 -0.0366 0.003   0.0261  91  ARG C NH2 
2569 N  N   . GLU C 61  ? 0.5393 0.4645 0.3369 -0.1477 -0.0312 0.0139  92  GLU C N   
2570 C  CA  . GLU C 61  ? 0.5858 0.5035 0.3625 -0.1773 -0.0408 0.0146  92  GLU C CA  
2571 C  C   . GLU C 61  ? 0.6028 0.5258 0.3897 -0.1866 -0.0422 0.0214  92  GLU C C   
2572 O  O   . GLU C 61  ? 0.6078 0.5644 0.4069 -0.2056 -0.0519 0.0295  92  GLU C O   
2573 C  CB  . GLU C 61  ? 0.6736 0.5325 0.4003 -0.1887 -0.0382 0.0033  92  GLU C CB  
2574 C  CG  . GLU C 61  ? 0.7945 0.6464 0.496  -0.2241 -0.0502 0.0032  92  GLU C CG  
2575 C  CD  . GLU C 61  ? 0.988  0.7726 0.6396 -0.2406 -0.0469 -0.0058 92  GLU C CD  
2576 O  OE1 . GLU C 61  ? 1.0499 0.8056 0.6627 -0.2589 -0.0514 -0.0141 92  GLU C OE1 
2577 O  OE2 . GLU C 61  ? 1.0481 0.8071 0.697  -0.2361 -0.04   -0.0044 92  GLU C OE2 
2578 N  N   . LYS C 62  ? 0.6071 0.5003 0.3895 -0.173  -0.0324 0.0195  93  LYS C N   
2579 C  CA  . LYS C 62  ? 0.606  0.4996 0.3947 -0.1809 -0.0325 0.0262  93  LYS C CA  
2580 C  C   . LYS C 62  ? 0.577  0.495  0.3983 -0.1559 -0.026  0.0311  93  LYS C C   
2581 O  O   . LYS C 62  ? 0.6034 0.5011 0.422  -0.1344 -0.0167 0.0269  93  LYS C O   
2582 C  CB  . LYS C 62  ? 0.6726 0.5029 0.4198 -0.1906 -0.0272 0.0206  93  LYS C CB  
2583 N  N   . SER C 63  ? 0.5236 0.4872 0.375  -0.1583 -0.0306 0.0405  94  SER C N   
2584 C  CA  . SER C 63  ? 0.4948 0.4826 0.3749 -0.1363 -0.0253 0.0445  94  SER C CA  
2585 C  C   . SER C 63  ? 0.4746 0.4596 0.3583 -0.1375 -0.0224 0.0508  94  SER C C   
2586 O  O   . SER C 63  ? 0.4621 0.4477 0.3387 -0.1584 -0.0269 0.0564  94  SER C O   
2587 C  CB  . SER C 63  ? 0.4891 0.529  0.3999 -0.1317 -0.0299 0.0503  94  SER C CB  
2588 O  OG  . SER C 63  ? 0.5014 0.5443 0.4157 -0.119  -0.0287 0.0451  94  SER C OG  
2589 N  N   . ASP C 64  ? 0.4585 0.4438 0.354  -0.1156 -0.0153 0.0507  95  ASP C N   
2590 C  CA  . ASP C 64  ? 0.4653 0.4558 0.3691 -0.1106 -0.0118 0.0573  95  ASP C CA  
2591 C  C   . ASP C 64  ? 0.4349 0.474  0.3702 -0.1012 -0.0134 0.0622  95  ASP C C   
2592 O  O   . ASP C 64  ? 0.4392 0.496  0.388  -0.0895 -0.0137 0.0586  95  ASP C O   
2593 C  CB  . ASP C 64  ? 0.5067 0.4702 0.4028 -0.0907 -0.0033 0.0545  95  ASP C CB  
2594 C  CG  . ASP C 64  ? 0.6282 0.5397 0.4914 -0.0956 0.0017  0.053   95  ASP C CG  
2595 O  OD1 . ASP C 64  ? 0.6469 0.5385 0.4903 -0.1177 -0.002  0.0533  95  ASP C OD1 
2596 O  OD2 . ASP C 64  ? 0.6969 0.5873 0.5528 -0.0773 0.0094  0.0522  95  ASP C OD2 
2597 N  N   . ILE C 65  ? 0.4047 0.4611 0.349  -0.1049 -0.0133 0.0703  96  ILE C N   
2598 C  CA  . ILE C 65  ? 0.3736 0.4715 0.3424 -0.0962 -0.0131 0.0758  96  ILE C CA  
2599 C  C   . ILE C 65  ? 0.3475 0.4413 0.3182 -0.0834 -0.0075 0.0779  96  ILE C C   
2600 O  O   . ILE C 65  ? 0.3769 0.4432 0.332  -0.0879 -0.005  0.08    96  ILE C O   
2601 C  CB  . ILE C 65  ? 0.3862 0.5101 0.3601 -0.1166 -0.0182 0.0858  96  ILE C CB  
2602 C  CG1 . ILE C 65  ? 0.4043 0.5419 0.3793 -0.1278 -0.0251 0.0848  96  ILE C CG1 
2603 C  CG2 . ILE C 65  ? 0.3784 0.5423 0.3729 -0.1103 -0.0161 0.0951  96  ILE C CG2 
2604 C  CD1 . ILE C 65  ? 0.3952 0.5545 0.3863 -0.1102 -0.0241 0.082   96  ILE C CD1 
2605 N  N   . LEU C 66  ? 0.2952 0.4134 0.2822 -0.0676 -0.0053 0.0775  97  LEU C N   
2606 C  CA  . LEU C 66  ? 0.285  0.4038 0.2729 -0.057  -0.001  0.08    97  LEU C CA  
2607 C  C   . LEU C 66  ? 0.2821 0.421  0.2743 -0.0664 -0.0007 0.0906  97  LEU C C   
2608 O  O   . LEU C 66  ? 0.2765 0.4463 0.2818 -0.069  -0.002  0.0947  97  LEU C O   
2609 C  CB  . LEU C 66  ? 0.2692 0.406  0.269  -0.0401 0.0006  0.0754  97  LEU C CB  
2610 C  CG  . LEU C 66  ? 0.3037 0.4251 0.3012 -0.0309 0.0006  0.0664  97  LEU C CG  
2611 C  CD1 . LEU C 66  ? 0.2922 0.4308 0.2999 -0.0196 0.0011  0.0617  97  LEU C CD1 
2612 C  CD2 . LEU C 66  ? 0.332  0.4327 0.3195 -0.0249 0.0032  0.0666  97  LEU C CD2 
2613 N  N   . VAL C 67  ? 0.2903 0.4142 0.2723 -0.07   0.0019  0.0963  98  VAL C N   
2614 C  CA  . VAL C 67  ? 0.2886 0.4337 0.2753 -0.0781 0.0032  0.1076  98  VAL C CA  
2615 C  C   . VAL C 67  ? 0.2963 0.4413 0.281  -0.0646 0.0081  0.1104  98  VAL C C   
2616 O  O   . VAL C 67  ? 0.3171 0.4331 0.2884 -0.0604 0.0099  0.1095  98  VAL C O   
2617 C  CB  . VAL C 67  ? 0.3111 0.4428 0.2864 -0.1023 0.0009  0.1153  98  VAL C CB  
2618 C  CG1 . VAL C 67  ? 0.3014 0.4642 0.2859 -0.1106 0.0027  0.1287  98  VAL C CG1 
2619 C  CG2 . VAL C 67  ? 0.3195 0.452  0.2943 -0.1172 -0.0053 0.1119  98  VAL C CG2 
2620 N  N   . PHE C 68  ? 0.27   0.4471 0.2663 -0.0558 0.0105  0.1136  99  PHE C N   
2621 C  CA  . PHE C 68  ? 0.2763 0.4562 0.2689 -0.0435 0.0145  0.116   99  PHE C CA  
2622 C  C   . PHE C 68  ? 0.2811 0.4766 0.2736 -0.0525 0.0177  0.1295  99  PHE C C   
2623 O  O   . PHE C 68  ? 0.2621 0.4894 0.2662 -0.056  0.019   0.1353  99  PHE C O   
2624 C  CB  . PHE C 68  ? 0.2658 0.4649 0.2656 -0.0268 0.0157  0.1085  99  PHE C CB  
2625 C  CG  . PHE C 68  ? 0.278  0.4616 0.2764 -0.0179 0.013   0.0965  99  PHE C CG  
2626 C  CD1 . PHE C 68  ? 0.3056 0.4819 0.3082 -0.022  0.0099  0.0904  99  PHE C CD1 
2627 C  CD2 . PHE C 68  ? 0.2944 0.4744 0.2876 -0.0064 0.0132  0.0923  99  PHE C CD2 
2628 C  CE1 . PHE C 68  ? 0.3159 0.481  0.3181 -0.0143 0.0081  0.0806  99  PHE C CE1 
2629 C  CE2 . PHE C 68  ? 0.3096 0.4798 0.3031 -0.0004 0.0104  0.0828  99  PHE C CE2 
2630 C  CZ  . PHE C 68  ? 0.3142 0.4769 0.3125 -0.0042 0.0084  0.0772  99  PHE C CZ  
2631 N  N   . HIS C 69  ? 0.3029 0.4768 0.2824 -0.0559 0.0196  0.1359  100 HIS C N   
2632 C  CA  . HIS C 69  ? 0.3026 0.4866 0.2796 -0.066  0.023   0.1499  100 HIS C CA  
2633 C  C   . HIS C 69  ? 0.3028 0.5067 0.2801 -0.051  0.0278  0.1539  100 HIS C C   
2634 O  O   . HIS C 69  ? 0.3009 0.5031 0.2761 -0.0343 0.0275  0.1456  100 HIS C O   
2635 C  CB  . HIS C 69  ? 0.3391 0.4822 0.2972 -0.0787 0.0235  0.156   100 HIS C CB  
2636 C  CG  . HIS C 69  ? 0.4059 0.5272 0.3583 -0.0977 0.0191  0.1529  100 HIS C CG  
2637 N  ND1 . HIS C 69  ? 0.456  0.5463 0.3996 -0.0929 0.0169  0.1416  100 HIS C ND1 
2638 C  CD2 . HIS C 69  ? 0.4239 0.5533 0.3776 -0.1215 0.0164  0.16    100 HIS C CD2 
2639 C  CE1 . HIS C 69  ? 0.4736 0.5507 0.411  -0.1135 0.013   0.1409  100 HIS C CE1 
2640 N  NE2 . HIS C 69  ? 0.4677 0.5687 0.4114 -0.1323 0.0118  0.1517  100 HIS C NE2 
2641 N  N   . ASN C 70  ? 0.2911 0.5138 0.2694 -0.0588 0.0318  0.1674  101 ASN C N   
2642 C  CA  . ASN C 70  ? 0.294  0.5331 0.2683 -0.0468 0.0371  0.1736  101 ASN C CA  
2643 C  C   . ASN C 70  ? 0.2977 0.5624 0.2779 -0.0283 0.0388  0.1647  101 ASN C C   
2644 O  O   . ASN C 70  ? 0.3028 0.5675 0.2739 -0.0149 0.0404  0.1622  101 ASN C O   
2645 C  CB  . ASN C 70  ? 0.329  0.5368 0.2866 -0.0409 0.0374  0.1756  101 ASN C CB  
2646 C  CG  . ASN C 70  ? 0.3975 0.577  0.344  -0.0582 0.0384  0.1869  101 ASN C CG  
2647 O  OD1 . ASN C 70  ? 0.419  0.6117 0.369  -0.0749 0.0403  0.1978  101 ASN C OD1 
2648 N  ND2 . ASN C 70  ? 0.4138 0.553  0.3455 -0.0555 0.0377  0.1853  101 ASN C ND2 
2649 N  N   . GLY C 71  ? 0.2973 0.5827 0.2905 -0.0281 0.0387  0.1606  102 GLY C N   
2650 C  CA  . GLY C 71  ? 0.306  0.6119 0.3013 -0.0108 0.0423  0.1532  102 GLY C CA  
2651 C  C   . GLY C 71  ? 0.3136 0.6487 0.3072 -0.0052 0.0506  0.1641  102 GLY C C   
2652 O  O   . GLY C 71  ? 0.2973 0.6485 0.2964 -0.0173 0.0535  0.1791  102 GLY C O   
2653 N  N   . GLU C 72  ? 0.3345 0.6758 0.3185 0.0123  0.0547  0.1569  103 GLU C N   
2654 C  CA  . GLU C 72  ? 0.3659 0.7335 0.3443 0.0213  0.0639  0.1653  103 GLU C CA  
2655 C  C   . GLU C 72  ? 0.3843 0.7748 0.3691 0.0335  0.0706  0.1627  103 GLU C C   
2656 O  O   . GLU C 72  ? 0.3838 0.7605 0.3631 0.0442  0.0693  0.1483  103 GLU C O   
2657 C  CB  . GLU C 72  ? 0.4209 0.7768 0.3785 0.0334  0.0642  0.1578  103 GLU C CB  
2658 C  CG  . GLU C 72  ? 0.5448 0.8747 0.4946 0.0276  0.0566  0.1565  103 GLU C CG  
2659 C  CD  . GLU C 72  ? 0.6465 0.9729 0.5765 0.0392  0.0561  0.1506  103 GLU C CD  
2660 O  OE1 . GLU C 72  ? 0.679  1.0232 0.5984 0.0483  0.0633  0.1525  103 GLU C OE1 
2661 O  OE2 . GLU C 72  ? 0.6684 0.9761 0.5927 0.0392  0.0486  0.1443  103 GLU C OE2 
2662 N  N   . VAL C 73  ? 0.3959 0.8213 0.3911 0.0329  0.0784  0.1775  104 VAL C N   
2663 C  CA  . VAL C 73  ? 0.4141 0.8665 0.4174 0.0468  0.0865  0.179   104 VAL C CA  
2664 C  C   . VAL C 73  ? 0.4444 0.9174 0.4349 0.065   0.0994  0.1835  104 VAL C C   
2665 O  O   . VAL C 73  ? 0.4456 0.9362 0.4346 0.06    0.1037  0.1969  104 VAL C O   
2666 C  CB  . VAL C 73  ? 0.408  0.8941 0.4366 0.033   0.0862  0.195   104 VAL C CB  
2667 C  CG1 . VAL C 73  ? 0.4029 0.9159 0.4418 0.0496  0.0935  0.1964  104 VAL C CG1 
2668 C  CG2 . VAL C 73  ? 0.4224 0.8871 0.4597 0.0104  0.0736  0.1929  104 VAL C CG2 
2669 N  N   . LYS C 74  ? 0.4652 0.9346 0.4445 0.0864  0.1065  0.1732  105 LYS C N   
2670 C  CA  . LYS C 74  ? 0.4893 0.9755 0.4526 0.1073  0.1209  0.1761  105 LYS C CA  
2671 C  C   . LYS C 74  ? 0.5026 1.0157 0.4793 0.1222  0.1305  0.1824  105 LYS C C   
2672 O  O   . LYS C 74  ? 0.4979 0.9915 0.4743 0.1285  0.1278  0.1711  105 LYS C O   
2673 C  CB  . LYS C 74  ? 0.5334 0.9817 0.4636 0.1201  0.1211  0.1559  105 LYS C CB  
2674 C  CG  . LYS C 74  ? 0.5913 1.0482 0.4978 0.1435  0.1368  0.1553  105 LYS C CG  
2675 N  N   . THR C 75  ? 0.5057 1.0667 0.4969 0.1265  0.1411  0.2026  106 THR C N   
2676 C  CA  . THR C 75  ? 0.5225 1.1183 0.5298 0.1421  0.1508  0.2129  106 THR C CA  
2677 C  C   . THR C 75  ? 0.5402 1.1479 0.5274 0.1734  0.1702  0.2145  106 THR C C   
2678 O  O   . THR C 75  ? 0.546  1.1688 0.5229 0.1764  0.1779  0.222   106 THR C O   
2679 C  CB  . THR C 75  ? 0.5204 1.1691 0.562  0.1234  0.1486  0.2372  106 THR C CB  
2680 O  OG1 . THR C 75  ? 0.5388 1.211  0.5791 0.1163  0.1539  0.251   106 THR C OG1 
2681 C  CG2 . THR C 75  ? 0.5275 1.1623 0.5859 0.094   0.1309  0.2352  106 THR C CG2 
2682 N  N   . SER C 81  ? 0.4905 1.0769 0.4965 0.2383  0.1822  0.2028  112 SER C N   
2683 C  CA  . SER C 81  ? 0.5212 1.0467 0.5018 0.2247  0.1712  0.1784  112 SER C CA  
2684 C  C   . SER C 81  ? 0.4991 1.0283 0.494  0.1907  0.1547  0.1791  112 SER C C   
2685 O  O   . SER C 81  ? 0.494  1.0611 0.5024 0.1815  0.1563  0.1946  112 SER C O   
2686 C  CB  . SER C 81  ? 0.5863 1.0766 0.5255 0.2454  0.184   0.1647  112 SER C CB  
2687 O  OG  . SER C 81  ? 0.6585 1.1114 0.5766 0.2287  0.174   0.1481  112 SER C OG  
2688 N  N   . TYR C 82  ? 0.4862 0.9748 0.4768 0.1731  0.1399  0.1631  113 TYR C N   
2689 C  CA  . TYR C 82  ? 0.4629 0.9441 0.4614 0.1443  0.1251  0.1614  113 TYR C CA  
2690 C  C   . TYR C 82  ? 0.4572 0.8844 0.431  0.1403  0.1172  0.1389  113 TYR C C   
2691 O  O   . TYR C 82  ? 0.4633 0.8599 0.4253 0.1491  0.1169  0.1256  113 TYR C O   
2692 C  CB  . TYR C 82  ? 0.4524 0.9496 0.4801 0.1225  0.1126  0.1693  113 TYR C CB  
2693 C  CG  . TYR C 82  ? 0.4425 0.9978 0.4981 0.1195  0.1167  0.1927  113 TYR C CG  
2694 C  CD1 . TYR C 82  ? 0.4417 1.0238 0.5095 0.1362  0.1235  0.2013  113 TYR C CD1 
2695 C  CD2 . TYR C 82  ? 0.4428 1.0267 0.5127 0.0982  0.1127  0.2072  113 TYR C CD2 
2696 C  CE1 . TYR C 82  ? 0.4267 1.0691 0.5223 0.1322  0.1261  0.2246  113 TYR C CE1 
2697 C  CE2 . TYR C 82  ? 0.4302 1.0711 0.5263 0.0918  0.1153  0.2297  113 TYR C CE2 
2698 C  CZ  . TYR C 82  ? 0.4313 1.1042 0.5415 0.1085  0.1215  0.2386  113 TYR C CZ  
2699 O  OH  . TYR C 82  ? 0.4392 1.176  0.5773 0.1021  0.1236  0.2628  113 TYR C OH  
2700 N  N   . GLN C 83  ? 0.4345 0.8517 0.401  0.1264  0.1106  0.1361  114 GLN C N   
2701 C  CA  . GLN C 83  ? 0.4371 0.8124 0.3845 0.1193  0.1014  0.1183  114 GLN C CA  
2702 C  C   . GLN C 83  ? 0.3978 0.7771 0.3603 0.0963  0.0898  0.1247  114 GLN C C   
2703 O  O   . GLN C 83  ? 0.3884 0.7873 0.3531 0.0911  0.0922  0.1363  114 GLN C O   
2704 C  CB  . GLN C 83  ? 0.4948 0.8558 0.4102 0.1316  0.1084  0.1099  114 GLN C CB  
2705 C  CG  . GLN C 83  ? 0.602  0.9261 0.4976 0.1227  0.0978  0.0929  114 GLN C CG  
2706 C  CD  . GLN C 83  ? 0.7093 1.0022 0.6013 0.1217  0.092   0.0782  114 GLN C CD  
2707 O  OE1 . GLN C 83  ? 0.7516 1.0328 0.6549 0.1067  0.08    0.0742  114 GLN C OE1 
2708 N  NE2 . GLN C 83  ? 0.7304 1.008  0.6055 0.1385  0.1015  0.0709  114 GLN C NE2 
2709 N  N   . ILE C 84  ? 0.3726 0.7339 0.3453 0.0831  0.0787  0.1187  115 ILE C N   
2710 C  CA  . ILE C 84  ? 0.3473 0.7066 0.3316 0.0629  0.0691  0.1245  115 ILE C CA  
2711 C  C   . ILE C 84  ? 0.3522 0.6774 0.3263 0.0575  0.0595  0.1106  115 ILE C C   
2712 O  O   . ILE C 84  ? 0.3573 0.664  0.3287 0.0609  0.0566  0.0987  115 ILE C O   
2713 C  CB  . ILE C 84  ? 0.3311 0.7066 0.3392 0.0502  0.0652  0.1342  115 ILE C CB  
2714 C  CG1 . ILE C 84  ? 0.3115 0.7284 0.3331 0.0579  0.0746  0.1486  115 ILE C CG1 
2715 C  CG2 . ILE C 84  ? 0.3366 0.708  0.351  0.0293  0.0579  0.142   115 ILE C CG2 
2716 C  CD1 . ILE C 84  ? 0.2986 0.7355 0.3427 0.0453  0.0697  0.1578  115 ILE C CD1 
2717 N  N   . ASN C 85  ? 0.3442 0.6627 0.3134 0.0491  0.0551  0.1136  116 ASN C N   
2718 C  CA  . ASN C 85  ? 0.3517 0.6445 0.3126 0.0452  0.0465  0.1036  116 ASN C CA  
2719 C  C   . ASN C 85  ? 0.3259 0.6117 0.2964 0.0313  0.0407  0.1117  116 ASN C C   
2720 O  O   . ASN C 85  ? 0.332  0.6288 0.3049 0.0252  0.0434  0.1248  116 ASN C O   
2721 C  CB  . ASN C 85  ? 0.4159 0.7072 0.3566 0.052   0.0476  0.1006  116 ASN C CB  
2722 C  CG  . ASN C 85  ? 0.5159 0.8033 0.4389 0.0647  0.0526  0.0891  116 ASN C CG  
2723 O  OD1 . ASN C 85  ? 0.5629 0.8312 0.4791 0.0657  0.0484  0.0757  116 ASN C OD1 
2724 N  ND2 . ASN C 85  ? 0.5239 0.8271 0.4368 0.0745  0.0622  0.0943  116 ASN C ND2 
2725 N  N   . TRP C 86  ? 0.3048 0.5702 0.2779 0.0266  0.0336  0.1044  117 TRP C N   
2726 C  CA  . TRP C 86  ? 0.2936 0.5452 0.2708 0.016   0.0294  0.1106  117 TRP C CA  
2727 C  C   . TRP C 86  ? 0.299  0.5357 0.267  0.0198  0.0248  0.1066  117 TRP C C   
2728 O  O   . TRP C 86  ? 0.3014 0.5342 0.2657 0.0255  0.0215  0.0956  117 TRP C O   
2729 C  CB  . TRP C 86  ? 0.2849 0.5265 0.2733 0.0076  0.0259  0.1075  117 TRP C CB  
2730 C  CG  . TRP C 86  ? 0.2712 0.5313 0.2704 0.0001  0.0289  0.1158  117 TRP C CG  
2731 C  CD1 . TRP C 86  ? 0.2757 0.5381 0.2788 -0.0144 0.0287  0.1273  117 TRP C CD1 
2732 C  CD2 . TRP C 86  ? 0.2661 0.5466 0.2733 0.0065  0.0323  0.1143  117 TRP C CD2 
2733 N  NE1 . TRP C 86  ? 0.2651 0.555  0.2803 -0.0187 0.0312  0.1342  117 TRP C NE1 
2734 C  CE2 . TRP C 86  ? 0.265  0.5667 0.2836 -0.0043 0.0338  0.1268  117 TRP C CE2 
2735 C  CE3 . TRP C 86  ? 0.2761 0.5574 0.2805 0.02    0.0346  0.1043  117 TRP C CE3 
2736 C  CZ2 . TRP C 86  ? 0.2683 0.5972 0.2985 0.0002  0.0373  0.1307  117 TRP C CZ2 
2737 C  CZ3 . TRP C 86  ? 0.2812 0.5828 0.294  0.0259  0.0394  0.1075  117 TRP C CZ3 
2738 C  CH2 . TRP C 86  ? 0.2741 0.6019 0.3011 0.0171  0.0407  0.1212  117 TRP C CH2 
2739 N  N   . PRO C 87  ? 0.2992 0.5265 0.2634 0.016   0.0245  0.1163  118 PRO C N   
2740 C  CA  . PRO C 87  ? 0.3018 0.5192 0.2588 0.022   0.0207  0.1154  118 PRO C CA  
2741 C  C   . PRO C 87  ? 0.3083 0.5063 0.2699 0.0208  0.0167  0.1105  118 PRO C C   
2742 O  O   . PRO C 87  ? 0.3115 0.5073 0.2699 0.0275  0.0136  0.1094  118 PRO C O   
2743 C  CB  . PRO C 87  ? 0.3186 0.5336 0.2679 0.021   0.024   0.13    118 PRO C CB  
2744 C  CG  . PRO C 87  ? 0.3229 0.5325 0.2777 0.0083  0.0275  0.1372  118 PRO C CG  
2745 C  CD  . PRO C 87  ? 0.287  0.5137 0.2519 0.0064  0.0282  0.1301  118 PRO C CD  
2746 N  N   . GLY C 88  ? 0.3057 0.4926 0.2744 0.0126  0.017   0.1085  119 GLY C N   
2747 C  CA  . GLY C 88  ? 0.308  0.4741 0.2786 0.0109  0.0148  0.1045  119 GLY C CA  
2748 C  C   . GLY C 88  ? 0.3001 0.4687 0.2745 0.0178  0.0108  0.0944  119 GLY C C   
2749 O  O   . GLY C 88  ? 0.294  0.4774 0.2707 0.0204  0.0091  0.0868  119 GLY C O   
2750 N  N   . GLU C 89  ? 0.2938 0.4466 0.2671 0.0209  0.0102  0.0948  120 GLU C N   
2751 C  CA  . GLU C 89  ? 0.2885 0.4455 0.2673 0.0258  0.0068  0.087   120 GLU C CA  
2752 C  C   . GLU C 89  ? 0.2966 0.4325 0.2765 0.0238  0.0081  0.0848  120 GLU C C   
2753 O  O   . GLU C 89  ? 0.3133 0.4273 0.2851 0.0217  0.0116  0.0907  120 GLU C O   
2754 C  CB  . GLU C 89  ? 0.3179 0.4871 0.2943 0.0354  0.0048  0.0915  120 GLU C CB  
2755 C  CG  . GLU C 89  ? 0.394  0.5477 0.3642 0.043   0.0086  0.1024  120 GLU C CG  
2756 C  CD  . GLU C 89  ? 0.4961 0.6673 0.4646 0.0542  0.007   0.1106  120 GLU C CD  
2757 O  OE1 . GLU C 89  ? 0.4622 0.659  0.4331 0.0536  0.0016  0.1071  120 GLU C OE1 
2758 O  OE2 . GLU C 89  ? 0.544  0.702  0.5066 0.0638  0.0113  0.1209  120 GLU C OE2 
2759 N  N   . VAL C 90  ? 0.2792 0.4191 0.2664 0.0234  0.0056  0.0761  121 VAL C N   
2760 C  CA  . VAL C 90  ? 0.2831 0.4048 0.2701 0.0226  0.0071  0.0735  121 VAL C CA  
2761 C  C   . VAL C 90  ? 0.2767 0.4094 0.2716 0.0273  0.0048  0.0681  121 VAL C C   
2762 O  O   . VAL C 90  ? 0.2758 0.4269 0.2761 0.0263  0.0011  0.0636  121 VAL C O   
2763 C  CB  . VAL C 90  ? 0.294  0.4063 0.2812 0.0115  0.0071  0.0697  121 VAL C CB  
2764 C  CG1 . VAL C 90  ? 0.2834 0.413  0.28   0.0089  0.0043  0.0624  121 VAL C CG1 
2765 C  CG2 . VAL C 90  ? 0.3216 0.4102 0.3027 0.0093  0.009   0.0678  121 VAL C CG2 
2766 N  N   . THR C 91  ? 0.264  0.3844 0.2576 0.0321  0.0076  0.0689  122 THR C N   
2767 C  CA  . THR C 91  ? 0.2458 0.3789 0.2481 0.0354  0.0061  0.0653  122 THR C CA  
2768 C  C   . THR C 91  ? 0.2507 0.3739 0.255  0.0283  0.006   0.0575  122 THR C C   
2769 O  O   . THR C 91  ? 0.2572 0.3587 0.2535 0.0257  0.0091  0.0572  122 THR C O   
2770 C  CB  . THR C 91  ? 0.2566 0.3888 0.2572 0.0482  0.0103  0.0731  122 THR C CB  
2771 O  OG1 . THR C 91  ? 0.2719 0.4204 0.2727 0.0544  0.0088  0.0809  122 THR C OG1 
2772 C  CG2 . THR C 91  ? 0.2615 0.4092 0.2725 0.0513  0.01    0.0712  122 THR C CG2 
2773 N  N   . MET C 92  ? 0.228  0.3654 0.2407 0.024   0.0024  0.0513  123 MET C N   
2774 C  CA  . MET C 92  ? 0.2285 0.3582 0.2432 0.0185  0.0025  0.0452  123 MET C CA  
2775 C  C   . MET C 92  ? 0.2346 0.3722 0.2555 0.0217  0.0032  0.045   123 MET C C   
2776 O  O   . MET C 92  ? 0.223  0.3799 0.2504 0.0219  0.0002  0.0456  123 MET C O   
2777 C  CB  . MET C 92  ? 0.2262 0.3626 0.2437 0.0122  -0.0007 0.0395  123 MET C CB  
2778 C  CG  . MET C 92  ? 0.2571 0.3871 0.2768 0.008   -0.0005 0.0346  123 MET C CG  
2779 S  SD  . MET C 92  ? 0.2592 0.3921 0.2786 0.0048  -0.0019 0.0297  123 MET C SD  
2780 C  CE  . MET C 92  ? 0.271  0.4118 0.2906 0.0028  -0.0047 0.0251  123 MET C CE  
2781 N  N   . LYS C 93  ? 0.237  0.3612 0.2547 0.0234  0.007   0.0445  124 LYS C N   
2782 C  CA  . LYS C 93  ? 0.2385 0.3713 0.2622 0.0268  0.0091  0.0452  124 LYS C CA  
2783 C  C   . LYS C 93  ? 0.2317 0.3584 0.2563 0.0189  0.008   0.039   124 LYS C C   
2784 O  O   . LYS C 93  ? 0.2341 0.3439 0.251  0.0154  0.0086  0.0365  124 LYS C O   
2785 C  CB  . LYS C 93  ? 0.2921 0.4113 0.3075 0.0377  0.0163  0.05    124 LYS C CB  
2786 C  CG  . LYS C 93  ? 0.3864 0.5086 0.399  0.0487  0.0189  0.0582  124 LYS C CG  
2787 C  CD  . LYS C 93  ? 0.4781 0.6193 0.4977 0.0619  0.0235  0.0662  124 LYS C CD  
2788 C  CE  . LYS C 93  ? 0.5607 0.7085 0.5784 0.0745  0.0259  0.0762  124 LYS C CE  
2789 N  NZ  . LYS C 93  ? 0.6155 0.7408 0.6191 0.0916  0.0368  0.0826  124 LYS C NZ  
2790 N  N   . LEU C 94  ? 0.2192 0.3603 0.2525 0.0153  0.0063  0.0378  125 LEU C N   
2791 C  CA  . LEU C 94  ? 0.2178 0.3531 0.2517 0.0089  0.006   0.0335  125 LEU C CA  
2792 C  C   . LEU C 94  ? 0.2206 0.3616 0.258  0.0118  0.0101  0.0365  125 LEU C C   
2793 O  O   . LEU C 94  ? 0.2223 0.3834 0.2692 0.0108  0.0094  0.0397  125 LEU C O   
2794 C  CB  . LEU C 94  ? 0.2145 0.3573 0.2522 0.0008  0.0014  0.0298  125 LEU C CB  
2795 C  CG  . LEU C 94  ? 0.2283 0.3672 0.2612 -0.0003 -0.0013 0.0271  125 LEU C CG  
2796 C  CD1 . LEU C 94  ? 0.2401 0.3815 0.2714 -0.0071 -0.0046 0.0226  125 LEU C CD1 
2797 C  CD2 . LEU C 94  ? 0.2344 0.3593 0.2621 0.0005  0       0.0259  125 LEU C CD2 
2798 N  N   . GLY C 95  ? 0.2264 0.352  0.2556 0.0152  0.0143  0.0361  126 GLY C N   
2799 C  CA  . GLY C 95  ? 0.2165 0.3457 0.2463 0.0196  0.0198  0.0389  126 GLY C CA  
2800 C  C   . GLY C 95  ? 0.2153 0.357  0.2483 0.031   0.0248  0.0457  126 GLY C C   
2801 O  O   . GLY C 95  ? 0.2254 0.3544 0.2488 0.0397  0.028   0.0474  126 GLY C O   
2802 N  N   . TYR C 96  ? 0.2028 0.3702 0.2488 0.031   0.0257  0.0507  127 TYR C N   
2803 C  CA  . TYR C 96  ? 0.2022 0.3914 0.2553 0.0433  0.0307  0.06    127 TYR C CA  
2804 C  C   . TYR C 96  ? 0.2176 0.4343 0.2835 0.0402  0.0242  0.0643  127 TYR C C   
2805 O  O   . TYR C 96  ? 0.206  0.4495 0.2813 0.0494  0.0269  0.074   127 TYR C O   
2806 C  CB  . TYR C 96  ? 0.1858 0.3934 0.2468 0.0452  0.0363  0.0654  127 TYR C CB  
2807 C  CG  . TYR C 96  ? 0.2042 0.385  0.2489 0.0517  0.0441  0.0621  127 TYR C CG  
2808 C  CD1 . TYR C 96  ? 0.2111 0.3714 0.2477 0.0408  0.041   0.0543  127 TYR C CD1 
2809 C  CD2 . TYR C 96  ? 0.2123 0.3858 0.2466 0.0696  0.0548  0.0669  127 TYR C CD2 
2810 C  CE1 . TYR C 96  ? 0.2315 0.3679 0.2507 0.0452  0.0469  0.0511  127 TYR C CE1 
2811 C  CE2 . TYR C 96  ? 0.2349 0.3801 0.2492 0.0744  0.0618  0.0626  127 TYR C CE2 
2812 C  CZ  . TYR C 96  ? 0.2444 0.371  0.2507 0.061   0.0569  0.0542  127 TYR C CZ  
2813 O  OH  . TYR C 96  ? 0.2611 0.3613 0.2457 0.0645  0.0628  0.05    127 TYR C OH  
2814 N  N   . GLY C 97  ? 0.251  0.4616 0.3156 0.0286  0.0162  0.0579  128 GLY C N   
2815 C  CA  . GLY C 97  ? 0.2609 0.4946 0.3333 0.0237  0.0092  0.0603  128 GLY C CA  
2816 C  C   . GLY C 97  ? 0.2836 0.5203 0.3531 0.0361  0.0104  0.0661  128 GLY C C   
2817 O  O   . GLY C 97  ? 0.3058 0.5194 0.3644 0.0475  0.0167  0.0669  128 GLY C O   
2818 N  N   . ASP C 98  ? 0.2716 0.5354 0.3487 0.033   0.0043  0.0704  129 ASP C N   
2819 C  CA  . ASP C 98  ? 0.3018 0.57   0.3757 0.0441  0.0047  0.0768  129 ASP C CA  
2820 C  C   . ASP C 98  ? 0.3286 0.5692 0.3899 0.0374  0.0012  0.0676  129 ASP C C   
2821 O  O   . ASP C 98  ? 0.3341 0.5659 0.3931 0.0239  -0.0033 0.0583  129 ASP C O   
2822 C  CB  . ASP C 98  ? 0.3275 0.6386 0.4136 0.041   -0.0022 0.0849  129 ASP C CB  
2823 C  CG  . ASP C 98  ? 0.4218 0.7695 0.5239 0.046   0.0005  0.0961  129 ASP C CG  
2824 O  OD1 . ASP C 98  ? 0.4263 0.7645 0.5294 0.0515  0.0082  0.0964  129 ASP C OD1 
2825 O  OD2 . ASP C 98  ? 0.4703 0.8588 0.5837 0.044   -0.0052 0.1051  129 ASP C OD2 
2826 N  N   . GLY C 99  ? 0.3455 0.5715 0.3979 0.0473  0.0044  0.0711  130 GLY C N   
2827 C  CA  . GLY C 99  ? 0.3513 0.5556 0.3933 0.0413  0.0022  0.0646  130 GLY C CA  
2828 C  C   . GLY C 99  ? 0.3372 0.5578 0.3804 0.0316  -0.0058 0.0613  130 GLY C C   
2829 O  O   . GLY C 99  ? 0.3341 0.5832 0.3843 0.0299  -0.0105 0.0654  130 GLY C O   
2830 N  N   . LEU C 100 ? 0.3217 0.5254 0.357  0.025   -0.0073 0.054   131 LEU C N   
2831 C  CA  . LEU C 100 ? 0.3203 0.5314 0.3508 0.0178  -0.0128 0.0496  131 LEU C CA  
2832 C  C   . LEU C 100 ? 0.2943 0.4927 0.3164 0.0223  -0.0103 0.0518  131 LEU C C   
2833 O  O   . LEU C 100 ? 0.2971 0.4757 0.3163 0.0221  -0.0065 0.0499  131 LEU C O   
2834 C  CB  . LEU C 100 ? 0.3507 0.5503 0.3778 0.0073  -0.0145 0.039   131 LEU C CB  
2835 C  CG  . LEU C 100 ? 0.4039 0.6162 0.4339 -0.0028 -0.0194 0.0353  131 LEU C CG  
2836 C  CD1 . LEU C 100 ? 0.4321 0.6246 0.4566 -0.0103 -0.0186 0.0263  131 LEU C CD1 
2837 C  CD2 . LEU C 100 ? 0.4191 0.6493 0.4433 -0.0085 -0.026  0.0349  131 LEU C CD2 
2838 N  N   . VAL C 101 ? 0.2805 0.4916 0.2983 0.0248  -0.0127 0.0562  132 VAL C N   
2839 C  CA  . VAL C 101 ? 0.2845 0.4846 0.2943 0.0278  -0.0099 0.0592  132 VAL C CA  
2840 C  C   . VAL C 101 ? 0.2885 0.4829 0.2921 0.0209  -0.0107 0.0509  132 VAL C C   
2841 O  O   . VAL C 101 ? 0.2955 0.4988 0.2948 0.016   -0.0147 0.0448  132 VAL C O   
2842 C  CB  . VAL C 101 ? 0.2924 0.5075 0.2985 0.0347  -0.0111 0.0687  132 VAL C CB  
2843 C  CG1 . VAL C 101 ? 0.2987 0.5019 0.296  0.0362  -0.0075 0.0726  132 VAL C CG1 
2844 C  CG2 . VAL C 101 ? 0.3048 0.5259 0.3164 0.0454  -0.0086 0.079   132 VAL C CG2 
2845 N  N   . ILE C 102 ? 0.2776 0.4577 0.2792 0.0206  -0.0065 0.0512  133 ILE C N   
2846 C  CA  . ILE C 102 ? 0.2686 0.4468 0.2651 0.0178  -0.0053 0.0465  133 ILE C CA  
2847 C  C   . ILE C 102 ? 0.2723 0.4541 0.2634 0.0207  -0.0028 0.0543  133 ILE C C   
2848 O  O   . ILE C 102 ? 0.2824 0.4566 0.2747 0.0215  -0.0004 0.0618  133 ILE C O   
2849 C  CB  . ILE C 102 ? 0.2787 0.4452 0.2795 0.0149  -0.0026 0.0435  133 ILE C CB  
2850 C  CG1 . ILE C 102 ? 0.3022 0.4639 0.3079 0.0123  -0.0044 0.0373  133 ILE C CG1 
2851 C  CG2 . ILE C 102 ? 0.2821 0.4508 0.2788 0.0154  0.0002  0.0413  133 ILE C CG2 
2852 C  CD1 . ILE C 102 ? 0.3349 0.4866 0.3438 0.01    -0.0021 0.0348  133 ILE C CD1 
2853 N  N   . LYS C 103 ? 0.2666 0.4576 0.2496 0.0218  -0.003  0.0527  134 LYS C N   
2854 C  CA  . LYS C 103 ? 0.2826 0.4795 0.2598 0.0245  -0.0002 0.0609  134 LYS C CA  
2855 C  C   . LYS C 103 ? 0.2865 0.49   0.2542 0.026   0.0023  0.0567  134 LYS C C   
2856 O  O   . LYS C 103 ? 0.2833 0.4824 0.2475 0.0255  0.0023  0.0473  134 LYS C O   
2857 C  CB  . LYS C 103 ? 0.3075 0.5132 0.2815 0.0285  -0.0031 0.0679  134 LYS C CB  
2858 C  CG  . LYS C 103 ? 0.358  0.5776 0.3254 0.028   -0.0088 0.0622  134 LYS C CG  
2859 C  CD  . LYS C 103 ? 0.4363 0.6701 0.4037 0.0329  -0.0122 0.0719  134 LYS C CD  
2860 C  CE  . LYS C 103 ? 0.4957 0.7481 0.4557 0.0295  -0.0194 0.0671  134 LYS C CE  
2861 N  NZ  . LYS C 103 ? 0.5451 0.8175 0.5045 0.0355  -0.0228 0.0789  134 LYS C NZ  
2862 N  N   . ASP C 104 ? 0.2944 0.5063 0.2559 0.0288  0.0055  0.0642  135 ASP C N   
2863 C  CA  . ASP C 104 ? 0.3156 0.5348 0.2658 0.0326  0.0096  0.0617  135 ASP C CA  
2864 C  C   . ASP C 104 ? 0.3082 0.5237 0.2618 0.0341  0.0148  0.0574  135 ASP C C   
2865 O  O   . ASP C 104 ? 0.3159 0.5284 0.2576 0.0387  0.0174  0.0493  135 ASP C O   
2866 C  CB  . ASP C 104 ? 0.366  0.5873 0.2999 0.0336  0.0055  0.053   135 ASP C CB  
2867 C  CG  . ASP C 104 ? 0.4696 0.7009 0.4007 0.0328  -0.0006 0.0581  135 ASP C CG  
2868 O  OD1 . ASP C 104 ? 0.4835 0.7207 0.418  0.0354  0.0011  0.0701  135 ASP C OD1 
2869 O  OD2 . ASP C 104 ? 0.5162 0.7502 0.4407 0.0291  -0.0072 0.0509  135 ASP C OD2 
2870 N  N   . LEU C 105 ? 0.3041 0.5189 0.2719 0.0306  0.0163  0.0629  136 LEU C N   
2871 C  CA  . LEU C 105 ? 0.3067 0.5246 0.2799 0.0331  0.0211  0.062   136 LEU C CA  
2872 C  C   . LEU C 105 ? 0.3275 0.5602 0.2931 0.0409  0.0287  0.0663  136 LEU C C   
2873 O  O   . LEU C 105 ? 0.3317 0.5759 0.2963 0.0398  0.0306  0.0754  136 LEU C O   
2874 C  CB  . LEU C 105 ? 0.2946 0.5145 0.2829 0.0254  0.0203  0.0696  136 LEU C CB  
2875 C  CG  . LEU C 105 ? 0.3237 0.5299 0.3186 0.0214  0.016   0.0633  136 LEU C CG  
2876 C  CD1 . LEU C 105 ? 0.3426 0.536  0.3345 0.0192  0.0108  0.0592  136 LEU C CD1 
2877 C  CD2 . LEU C 105 ? 0.317  0.5259 0.3229 0.013   0.0153  0.0702  136 LEU C CD2 
2878 N  N   . ASN C 106 ? 0.3414 0.571  0.2984 0.0501  0.0338  0.0595  137 ASN C N   
2879 C  CA  . ASN C 106 ? 0.36   0.6009 0.3059 0.0614  0.0431  0.0621  137 ASN C CA  
2880 C  C   . ASN C 106 ? 0.3614 0.6065 0.3133 0.0702  0.0498  0.0634  137 ASN C C   
2881 O  O   . ASN C 106 ? 0.3653 0.5909 0.3104 0.074   0.0497  0.0536  137 ASN C O   
2882 C  CB  . ASN C 106 ? 0.4154 0.6402 0.3355 0.0667  0.0435  0.05    137 ASN C CB  
2883 C  CG  . ASN C 106 ? 0.5334 0.7639 0.4353 0.0801  0.0541  0.0504  137 ASN C CG  
2884 O  OD1 . ASN C 106 ? 0.5644 0.8012 0.4677 0.0917  0.0636  0.0538  137 ASN C OD1 
2885 N  ND2 . ASN C 106 ? 0.5694 0.7991 0.4525 0.0802  0.0532  0.0476  137 ASN C ND2 
2886 N  N   . LEU C 107 ? 0.3467 0.6185 0.3113 0.0731  0.0557  0.0767  138 LEU C N   
2887 C  CA  . LEU C 107 ? 0.3557 0.6398 0.3287 0.0831  0.0624  0.0816  138 LEU C CA  
2888 C  C   . LEU C 107 ? 0.3749 0.6743 0.3369 0.1009  0.0754  0.0865  138 LEU C C   
2889 O  O   . LEU C 107 ? 0.3641 0.6857 0.3279 0.1003  0.079   0.0962  138 LEU C O   
2890 C  CB  . LEU C 107 ? 0.34   0.6488 0.3384 0.0714  0.0585  0.0949  138 LEU C CB  
2891 C  CG  . LEU C 107 ? 0.3421 0.675  0.3537 0.0805  0.0644  0.1042  138 LEU C CG  
2892 C  CD1 . LEU C 107 ? 0.3546 0.6651 0.3635 0.086   0.0626  0.0948  138 LEU C CD1 
2893 C  CD2 . LEU C 107 ? 0.333  0.6968 0.3674 0.0649  0.0597  0.1192  138 LEU C CD2 
2894 N  N   . MET C 108 ? 0.4008 0.6853 0.3487 0.1177  0.0834  0.0798  139 MET C N   
2895 C  CA  . MET C 108 ? 0.4289 0.7239 0.3631 0.1391  0.0982  0.0841  139 MET C CA  
2896 C  C   . MET C 108 ? 0.4283 0.7438 0.3789 0.1512  0.1049  0.0949  139 MET C C   
2897 O  O   . MET C 108 ? 0.4281 0.7263 0.3824 0.1498  0.1006  0.0897  139 MET C O   
2898 C  CB  . MET C 108 ? 0.4819 0.7357 0.3791 0.1509  0.1037  0.0668  139 MET C CB  
2899 C  CG  . MET C 108 ? 0.5824 0.8413 0.4588 0.1751  0.1209  0.0699  139 MET C CG  
2900 S  SD  . MET C 108 ? 0.7849 1.0413 0.6585 0.2026  0.1362  0.0751  139 MET C SD  
2901 C  CE  . MET C 108 ? 0.8215 1.0091 0.6594 0.2016  0.1332  0.0509  139 MET C CE  
2902 N  N   . LEU C 109 ? 0.4209 0.7766 0.3826 0.1629  0.1151  0.1114  140 LEU C N   
2903 C  CA  . LEU C 109 ? 0.4256 0.8116 0.4052 0.1767  0.1224  0.1255  140 LEU C CA  
2904 C  C   . LEU C 109 ? 0.4574 0.8582 0.423  0.205   0.1412  0.1327  140 LEU C C   
2905 O  O   . LEU C 109 ? 0.4461 0.8641 0.4068 0.2058  0.1462  0.1376  140 LEU C O   
2906 C  CB  . LEU C 109 ? 0.3948 0.8291 0.4094 0.1584  0.1146  0.1437  140 LEU C CB  
2907 C  CG  . LEU C 109 ? 0.3972 0.8182 0.4243 0.1311  0.0975  0.1383  140 LEU C CG  
2908 C  CD1 . LEU C 109 ? 0.3741 0.8378 0.4281 0.1116  0.0911  0.1554  140 LEU C CD1 
2909 C  CD2 . LEU C 109 ? 0.4165 0.8157 0.4442 0.1341  0.0935  0.131   140 LEU C CD2 
2910 N  N   . LYS C 110 ? 0.4899 0.8837 0.4474 0.2299  0.1527  0.1344  141 LYS C N   
2911 C  CA  . LYS C 110 ? 0.5197 0.9236 0.4599 0.261   0.173   0.1411  141 LYS C CA  
2912 C  C   . LYS C 110 ? 0.5292 0.9549 0.4799 0.2864  0.1846  0.1553  141 LYS C C   
2913 O  O   . LYS C 110 ? 0.5314 0.9357 0.4841 0.2862  0.1796  0.1508  141 LYS C O   
2914 C  CB  . LYS C 110 ? 0.5797 0.9227 0.4726 0.2718  0.1799  0.1191  141 LYS C CB  
2915 C  CG  . LYS C 110 ? 0.651  0.9998 0.5193 0.2984  0.1996  0.1228  141 LYS C CG  
2916 N  N   . ASN C 111 ? 0.5336 1.0068 0.4932 0.3086  0.2001  0.1746  142 ASN C N   
2917 C  CA  . ASN C 111 ? 0.5462 1.0485 0.5157 0.3386  0.2143  0.1919  142 ASN C CA  
2918 C  C   . ASN C 111 ? 0.5206 1.0575 0.5266 0.327   0.2026  0.2054  142 ASN C C   
2919 O  O   . ASN C 111 ? 0.5214 1.0643 0.5288 0.3517  0.2119  0.2146  142 ASN C O   
2920 C  CB  . ASN C 111 ? 0.6244 1.065  0.5509 0.3695  0.2298  0.1777  142 ASN C CB  
2921 C  CG  . ASN C 111 ? 0.7241 1.1403 0.6124 0.39    0.2467  0.1696  142 ASN C CG  
2922 O  OD1 . ASN C 111 ? 0.7366 1.1944 0.6341 0.3894  0.2514  0.1803  142 ASN C OD1 
2923 N  ND2 . ASN C 111 ? 0.7816 1.1282 0.6235 0.4081  0.2568  0.1509  142 ASN C ND2 
2924 N  N   . GLY C 112 ? 0.4991 1.0551 0.5309 0.2909  0.1828  0.2062  143 GLY C N   
2925 C  CA  . GLY C 112 ? 0.4724 1.0593 0.5353 0.2764  0.1702  0.2175  143 GLY C CA  
2926 C  C   . GLY C 112 ? 0.4931 1.03   0.544  0.2755  0.1633  0.2029  143 GLY C C   
2927 O  O   . GLY C 112 ? 0.4771 1.032  0.5504 0.2578  0.15    0.2084  143 GLY C O   
2928 N  N   . ASN C 113 ? 0.5241 0.9973 0.538  0.293   0.1721  0.1843  144 ASN C N   
2929 C  CA  . ASN C 113 ? 0.5493 0.9748 0.5505 0.293   0.1672  0.172   144 ASN C CA  
2930 C  C   . ASN C 113 ? 0.5799 0.9318 0.5455 0.2848  0.1642  0.145   144 ASN C C   
2931 O  O   . ASN C 113 ? 0.6094 0.9178 0.5593 0.289   0.1637  0.1353  144 ASN C O   
2932 C  CB  . ASN C 113 ? 0.5773 1.0056 0.5728 0.3285  0.183   0.184   144 ASN C CB  
2933 C  CG  . ASN C 113 ? 0.6599 1.0535 0.6183 0.3626  0.2048  0.1788  144 ASN C CG  
2934 O  OD1 . ASN C 113 ? 0.6863 1.0744 0.6292 0.3636  0.2107  0.1724  144 ASN C OD1 
2935 N  ND2 . ASN C 113 ? 0.6997 1.067  0.6404 0.3922  0.2181  0.1818  144 ASN C ND2 
2936 N  N   . MET C 114 ? 0.5699 0.9092 0.5229 0.2723  0.1616  0.1339  145 MET C N   
2937 C  CA  . MET C 114 ? 0.5945 0.8705 0.5163 0.2606  0.1561  0.1095  145 MET C CA  
2938 C  C   . MET C 114 ? 0.5548 0.8359 0.4846 0.2306  0.1413  0.102   145 MET C C   
2939 O  O   . MET C 114 ? 0.5392 0.867  0.4944 0.2202  0.1371  0.115   145 MET C O   
2940 C  CB  . MET C 114 ? 0.6553 0.885  0.5331 0.2856  0.1729  0.0981  145 MET C CB  
2941 C  CG  . MET C 114 ? 0.7208 0.9621 0.5849 0.2921  0.1812  0.098   145 MET C CG  
2942 S  SD  . MET C 114 ? 0.9164 1.1118 0.7293 0.331   0.2063  0.0909  145 MET C SD  
2943 C  CE  . MET C 114 ? 0.9152 1.1574 0.7528 0.3636  0.2215  0.1175  145 MET C CE  
2944 N  N   . GLY C 115 ? 0.5344 0.7682 0.4429 0.2164  0.1333  0.0824  146 GLY C N   
2945 C  CA  . GLY C 115 ? 0.4999 0.7352 0.4136 0.191   0.12    0.0755  146 GLY C CA  
2946 C  C   . GLY C 115 ? 0.4677 0.6766 0.3851 0.1697  0.1053  0.0642  146 GLY C C   
2947 O  O   . GLY C 115 ? 0.4736 0.6588 0.3864 0.1738  0.1056  0.0601  146 GLY C O   
2948 N  N   . GLU C 116 ? 0.4338 0.6469 0.3592 0.1481  0.0932  0.0604  147 GLU C N   
2949 C  CA  . GLU C 116 ? 0.4231 0.6148 0.3526 0.129   0.0801  0.0508  147 GLU C CA  
2950 C  C   . GLU C 116 ? 0.3815 0.5888 0.3258 0.1089  0.0687  0.0525  147 GLU C C   
2951 O  O   . GLU C 116 ? 0.3747 0.5988 0.3179 0.1083  0.0704  0.057   147 GLU C O   
2952 C  CB  . GLU C 116 ? 0.4814 0.6258 0.3796 0.1291  0.0803  0.033   147 GLU C CB  
2953 C  CG  . GLU C 116 ? 0.56   0.694  0.4376 0.123   0.0782  0.0237  147 GLU C CG  
2954 C  CD  . GLU C 116 ? 0.6697 0.7987 0.5218 0.1417  0.0917  0.0229  147 GLU C CD  
2955 O  OE1 . GLU C 116 ? 0.6919 0.8015 0.5276 0.1599  0.1033  0.0215  147 GLU C OE1 
2956 O  OE2 . GLU C 116 ? 0.7121 0.8549 0.5587 0.1394  0.0914  0.0239  147 GLU C OE2 
2957 N  N   . LEU C 117 ? 0.3426 0.5424 0.299  0.0937  0.0581  0.0494  148 LEU C N   
2958 C  CA  . LEU C 117 ? 0.3196 0.526  0.2858 0.0768  0.0483  0.05    148 LEU C CA  
2959 C  C   . LEU C 117 ? 0.3382 0.5161 0.2885 0.07    0.0424  0.036   148 LEU C C   
2960 O  O   . LEU C 117 ? 0.3507 0.5078 0.2969 0.0684  0.0405  0.0286  148 LEU C O   
2961 C  CB  . LEU C 117 ? 0.2958 0.5138 0.2841 0.0652  0.0413  0.0568  148 LEU C CB  
2962 C  CG  . LEU C 117 ? 0.2906 0.5079 0.2854 0.0496  0.0325  0.057   148 LEU C CG  
2963 C  CD1 . LEU C 117 ? 0.2818 0.5172 0.2769 0.048   0.0345  0.0654  148 LEU C CD1 
2964 C  CD2 . LEU C 117 ? 0.2784 0.5001 0.289  0.0388  0.0268  0.0618  148 LEU C CD2 
2965 N  N   . LYS C 118 ? 0.3305 0.5094 0.2713 0.0659  0.0399  0.0335  149 LYS C N   
2966 C  CA  . LYS C 118 ? 0.3393 0.4998 0.2668 0.0575  0.033   0.0225  149 LYS C CA  
2967 C  C   . LYS C 118 ? 0.3188 0.4919 0.2597 0.0464  0.0246  0.0275  149 LYS C C   
2968 O  O   . LYS C 118 ? 0.3116 0.5025 0.2645 0.0457  0.0255  0.0381  149 LYS C O   
2969 C  CB  . LYS C 118 ? 0.3877 0.5387 0.2879 0.063   0.0369  0.0153  149 LYS C CB  
2970 C  CG  . LYS C 118 ? 0.4672 0.5953 0.3452 0.0752  0.0462  0.0077  149 LYS C CG  
2971 C  CD  . LYS C 118 ? 0.5269 0.6418 0.3733 0.0781  0.049   -0.001  149 LYS C CD  
2972 C  CE  . LYS C 118 ? 0.6081 0.6873 0.4235 0.0875  0.0575  -0.0123 149 LYS C CE  
2973 N  NZ  . LYS C 118 ? 0.6613 0.7257 0.4411 0.0898  0.0606  -0.0216 149 LYS C NZ  
2974 N  N   . ALA C 119 ? 0.3114 0.4756 0.2485 0.0379  0.0171  0.0209  150 ALA C N   
2975 C  CA  . ALA C 119 ? 0.3061 0.4808 0.2536 0.0307  0.0103  0.0262  150 ALA C CA  
2976 C  C   . ALA C 119 ? 0.3227 0.4935 0.2597 0.0241  0.0032  0.0187  150 ALA C C   
2977 O  O   . ALA C 119 ? 0.3449 0.501  0.2676 0.0216  0.0026  0.0086  150 ALA C O   
2978 C  CB  . ALA C 119 ? 0.2844 0.4578 0.2507 0.0264  0.008   0.0301  150 ALA C CB  
2979 N  N   . THR C 120 ? 0.3128 0.4967 0.2558 0.0209  -0.0022 0.0246  151 THR C N   
2980 C  CA  . THR C 120 ? 0.3101 0.4994 0.2506 0.0138  -0.0101 0.0215  151 THR C CA  
2981 C  C   . THR C 120 ? 0.3032 0.491  0.262  0.0108  -0.0121 0.0238  151 THR C C   
2982 O  O   . THR C 120 ? 0.2975 0.4863 0.2689 0.0145  -0.0094 0.0315  151 THR C O   
2983 C  CB  . THR C 120 ? 0.333  0.5407 0.2714 0.0155  -0.0134 0.0295  151 THR C CB  
2984 O  OG1 . THR C 120 ? 0.3599 0.5682 0.2787 0.0179  -0.0112 0.0263  151 THR C OG1 
2985 C  CG2 . THR C 120 ? 0.3354 0.5574 0.277  0.0092  -0.022  0.0302  151 THR C CG2 
2986 N  N   . VAL C 121 ? 0.3009 0.4835 0.2589 0.0033  -0.016  0.0168  152 VAL C N   
2987 C  CA  . VAL C 121 ? 0.3122 0.4943 0.2857 0.0009  -0.017  0.0188  152 VAL C CA  
2988 C  C   . VAL C 121 ? 0.3353 0.5341 0.3113 -0.0061 -0.0242 0.0197  152 VAL C C   
2989 O  O   . VAL C 121 ? 0.3523 0.5495 0.3161 -0.0156 -0.0287 0.0122  152 VAL C O   
2990 C  CB  . VAL C 121 ? 0.3244 0.487  0.2961 -0.0017 -0.0141 0.0115  152 VAL C CB  
2991 C  CG1 . VAL C 121 ? 0.3166 0.4803 0.3026 -0.005  -0.0153 0.0137  152 VAL C CG1 
2992 C  CG2 . VAL C 121 ? 0.3289 0.4818 0.3    0.0064  -0.007  0.0129  152 VAL C CG2 
2993 N  N   . GLY C 122 ? 0.3309 0.5463 0.3198 -0.0014 -0.0253 0.0296  153 GLY C N   
2994 C  CA  . GLY C 122 ? 0.3404 0.5807 0.3342 -0.0057 -0.032  0.034   153 GLY C CA  
2995 C  C   . GLY C 122 ? 0.3691 0.6231 0.3492 -0.0095 -0.0376 0.0332  153 GLY C C   
2996 O  O   . GLY C 122 ? 0.3685 0.6208 0.341  -0.0024 -0.0351 0.0362  153 GLY C O   
2997 N  N   . GLU C 123 ? 0.3904 0.6571 0.365  -0.0227 -0.0455 0.0288  154 GLU C N   
2998 C  CA  . GLU C 123 ? 0.4148 0.6947 0.3727 -0.0292 -0.0524 0.0267  154 GLU C CA  
2999 C  C   . GLU C 123 ? 0.4429 0.6937 0.3747 -0.0352 -0.0506 0.0125  154 GLU C C   
3000 O  O   . GLU C 123 ? 0.4508 0.7069 0.3632 -0.0422 -0.056  0.0082  154 GLU C O   
3001 C  CB  . GLU C 123 ? 0.4551 0.7651 0.4172 -0.0433 -0.063  0.0292  154 GLU C CB  
3002 N  N   . ASN C 124 ? 0.4475 0.6681 0.3772 -0.0315 -0.0427 0.0056  155 ASN C N   
3003 C  CA  . ASN C 124 ? 0.4683 0.6597 0.3724 -0.0339 -0.039  -0.0068 155 ASN C CA  
3004 C  C   . ASN C 124 ? 0.4549 0.6352 0.3548 -0.0188 -0.0296 -0.0052 155 ASN C C   
3005 O  O   . ASN C 124 ? 0.4473 0.6239 0.3632 -0.01   -0.0235 0       155 ASN C O   
3006 C  CB  . ASN C 124 ? 0.5117 0.6775 0.4122 -0.0416 -0.0372 -0.0155 155 ASN C CB  
3007 C  CG  . ASN C 124 ? 0.5885 0.7606 0.4819 -0.0614 -0.047  -0.0201 155 ASN C CG  
3008 O  OD1 . ASN C 124 ? 0.6153 0.8034 0.5281 -0.0679 -0.0508 -0.0147 155 ASN C OD1 
3009 N  ND2 . ASN C 124 ? 0.6211 0.7827 0.4857 -0.0721 -0.0514 -0.0295 155 ASN C ND2 
3010 N  N   . SER C 125 ? 0.4466 0.6235 0.3241 -0.0169 -0.0286 -0.0092 156 SER C N   
3011 C  CA  . SER C 125 ? 0.4497 0.6209 0.3227 -0.0028 -0.019  -0.0064 156 SER C CA  
3012 C  C   . SER C 125 ? 0.4618 0.6016 0.3169 0.0015  -0.0105 -0.0166 156 SER C C   
3013 O  O   . SER C 125 ? 0.4709 0.5893 0.312  -0.0076 -0.0127 -0.027  156 SER C O   
3014 C  CB  . SER C 125 ? 0.4732 0.6589 0.3304 -0.001  -0.021  -0.0039 156 SER C CB  
3015 O  OG  . SER C 125 ? 0.5293 0.6996 0.355  -0.0095 -0.0239 -0.0168 156 SER C OG  
3016 N  N   . ASN C 126 ? 0.459  0.5964 0.3137 0.0157  -0.0004 -0.0126 157 ASN C N   
3017 C  CA  . ASN C 126 ? 0.4745 0.5865 0.3121 0.025   0.0099  -0.0195 157 ASN C CA  
3018 C  C   . ASN C 126 ? 0.4592 0.5519 0.3046 0.0233  0.0114  -0.023  157 ASN C C   
3019 O  O   . ASN C 126 ? 0.4837 0.5459 0.306  0.0242  0.0158  -0.0329 157 ASN C O   
3020 C  CB  . ASN C 126 ? 0.5361 0.6266 0.3346 0.0229  0.0109  -0.032  157 ASN C CB  
3021 C  CG  . ASN C 126 ? 0.6518 0.7188 0.4289 0.0387  0.0247  -0.0364 157 ASN C CG  
3022 O  OD1 . ASN C 126 ? 0.6829 0.7652 0.4695 0.0535  0.0335  -0.0271 157 ASN C OD1 
3023 N  ND2 . ASN C 126 ? 0.703  0.7316 0.4492 0.0361  0.0275  -0.0499 157 ASN C ND2 
3024 N  N   . ILE C 127 ? 0.415  0.5222 0.2896 0.0207  0.008   -0.015  158 ILE C N   
3025 C  CA  . ILE C 127 ? 0.4068 0.4985 0.2897 0.0194  0.0093  -0.0168 158 ILE C CA  
3026 C  C   . ILE C 127 ? 0.3967 0.4911 0.2897 0.0338  0.0187  -0.0097 158 ILE C C   
3027 O  O   . ILE C 127 ? 0.3808 0.4982 0.2944 0.0364  0.0185  0.0006  158 ILE C O   
3028 C  CB  . ILE C 127 ? 0.3954 0.5022 0.3031 0.0097  0.0014  -0.0116 158 ILE C CB  
3029 C  CG1 . ILE C 127 ? 0.4162 0.5295 0.3188 -0.0046 -0.0084 -0.0157 158 ILE C CG1 
3030 C  CG2 . ILE C 127 ? 0.3901 0.4841 0.3076 0.0098  0.0037  -0.0117 158 ILE C CG2 
3031 C  CD1 . ILE C 127 ? 0.4583 0.5468 0.3362 -0.015  -0.0103 -0.0277 158 ILE C CD1 
3032 N  N   . THR C 128 ? 0.3949 0.4663 0.273  0.0429  0.0269  -0.014  159 THR C N   
3033 C  CA  . THR C 128 ? 0.3759 0.4558 0.2663 0.0571  0.0354  -0.0051 159 THR C CA  
3034 C  C   . THR C 128 ? 0.3443 0.4304 0.2583 0.0511  0.0308  -0.0001 159 THR C C   
3035 O  O   . THR C 128 ? 0.3463 0.4138 0.2564 0.0432  0.0273  -0.0061 159 THR C O   
3036 C  CB  . THR C 128 ? 0.4157 0.4697 0.2824 0.0722  0.047   -0.0095 159 THR C CB  
3037 O  OG1 . THR C 128 ? 0.4469 0.494  0.2887 0.0779  0.0517  -0.0147 159 THR C OG1 
3038 C  CG2 . THR C 128 ? 0.4121 0.4829 0.2943 0.0882  0.0555  0.0025  159 THR C CG2 
3039 N  N   . LEU C 129 ? 0.3051 0.4169 0.2417 0.053   0.0304  0.0109  160 LEU C N   
3040 C  CA  . LEU C 129 ? 0.2938 0.4116 0.2499 0.0478  0.0266  0.0158  160 LEU C CA  
3041 C  C   . LEU C 129 ? 0.3062 0.4206 0.2631 0.0595  0.0337  0.0201  160 LEU C C   
3042 O  O   . LEU C 129 ? 0.3118 0.4139 0.2708 0.0575  0.0326  0.0188  160 LEU C O   
3043 C  CB  . LEU C 129 ? 0.2728 0.4156 0.2477 0.0424  0.0226  0.025   160 LEU C CB  
3044 C  CG  . LEU C 129 ? 0.2828 0.4306 0.2575 0.0343  0.0169  0.0238  160 LEU C CG  
3045 C  CD1 . LEU C 129 ? 0.2828 0.4467 0.2725 0.0295  0.0144  0.0331  160 LEU C CD1 
3046 C  CD2 . LEU C 129 ? 0.3075 0.4423 0.2787 0.0257  0.0108  0.016   160 LEU C CD2 
3047 N  N   . PHE C 130 ? 0.306  0.4343 0.2619 0.0724  0.0414  0.0269  161 PHE C N   
3048 C  CA  . PHE C 130 ? 0.3371 0.4664 0.2933 0.0872  0.0495  0.0331  161 PHE C CA  
3049 C  C   . PHE C 130 ? 0.3539 0.4912 0.2996 0.1049  0.0606  0.0375  161 PHE C C   
3050 O  O   . PHE C 130 ? 0.3457 0.5012 0.2931 0.1038  0.0609  0.0403  161 PHE C O   
3051 C  CB  . PHE C 130 ? 0.326  0.4816 0.3066 0.0838  0.0458  0.0447  161 PHE C CB  
3052 C  CG  . PHE C 130 ? 0.3176 0.5084 0.3156 0.0781  0.043   0.0551  161 PHE C CG  
3053 C  CD1 . PHE C 130 ? 0.3164 0.5342 0.3196 0.0899  0.0503  0.0661  161 PHE C CD1 
3054 C  CD2 . PHE C 130 ? 0.3089 0.5054 0.3176 0.0611  0.0338  0.055   161 PHE C CD2 
3055 C  CE1 . PHE C 130 ? 0.3029 0.5533 0.3219 0.0815  0.0474  0.0766  161 PHE C CE1 
3056 C  CE2 . PHE C 130 ? 0.2995 0.5225 0.3206 0.0539  0.0315  0.0645  161 PHE C CE2 
3057 C  CZ  . PHE C 130 ? 0.2938 0.5441 0.3205 0.0625  0.0377  0.0753  161 PHE C CZ  
3058 N  N   . ASP C 131 ? 0.3815 0.5049 0.3152 0.1225  0.0707  0.039   162 ASP C N   
3059 C  CA  . ASP C 131 ? 0.412  0.5451 0.3364 0.144   0.0837  0.0455  162 ASP C CA  
3060 C  C   . ASP C 131 ? 0.3995 0.5802 0.3529 0.1495  0.0847  0.064   162 ASP C C   
3061 O  O   . ASP C 131 ? 0.3875 0.5803 0.3594 0.1408  0.0775  0.0694  162 ASP C O   
3062 C  CB  . ASP C 131 ? 0.4732 0.567  0.3697 0.1628  0.0955  0.0401  162 ASP C CB  
3063 C  CG  . ASP C 131 ? 0.5664 0.6122 0.4286 0.1565  0.0955  0.0218  162 ASP C CG  
3064 O  OD1 . ASP C 131 ? 0.5588 0.6081 0.4125 0.1501  0.0933  0.0161  162 ASP C OD1 
3065 O  OD2 . ASP C 131 ? 0.6344 0.6396 0.4774 0.1569  0.0974  0.0139  162 ASP C OD2 
3066 N  N   . VAL C 132 ? 0.4016 0.6107 0.3577 0.1635  0.0938  0.0743  163 VAL C N   
3067 C  CA  . VAL C 132 ? 0.3916 0.6522 0.3754 0.167   0.0947  0.0935  163 VAL C CA  
3068 C  C   . VAL C 132 ? 0.4121 0.6799 0.3938 0.1934  0.1071  0.1041  163 VAL C C   
3069 O  O   . VAL C 132 ? 0.4326 0.6767 0.3898 0.2153  0.1207  0.1003  163 VAL C O   
3070 C  CB  . VAL C 132 ? 0.3916 0.6858 0.3831 0.1642  0.0966  0.1011  163 VAL C CB  
3071 C  CG1 . VAL C 132 ? 0.3727 0.7235 0.3901 0.1707  0.1004  0.1228  163 VAL C CG1 
3072 C  CG2 . VAL C 132 ? 0.3968 0.688  0.3945 0.1378  0.0834  0.0945  163 VAL C CG2 
3073 N  N   . GLN C 133 ? 0.4075 0.7039 0.4119 0.1916  0.1027  0.1167  164 GLN C N   
3074 C  CA  . GLN C 133 ? 0.4312 0.7424 0.4376 0.2177  0.1139  0.1304  164 GLN C CA  
3075 C  C   . GLN C 133 ? 0.425  0.794  0.4491 0.2299  0.1217  0.1498  164 GLN C C   
3076 O  O   . GLN C 133 ? 0.4423 0.815  0.4554 0.2594  0.138   0.1573  164 GLN C O   
3077 C  CB  . GLN C 133 ? 0.4482 0.7726 0.4725 0.2094  0.1046  0.1377  164 GLN C CB  
3078 C  CG  . GLN C 133 ? 0.5207 0.8759 0.554  0.2357  0.1146  0.1573  164 GLN C CG  
3079 C  CD  . GLN C 133 ? 0.6459 0.9521 0.6499 0.263   0.1288  0.152   164 GLN C CD  
3080 O  OE1 . GLN C 133 ? 0.7056 0.9569 0.6887 0.2555  0.126   0.1353  164 GLN C OE1 
3081 N  NE2 . GLN C 133 ? 0.6591 0.9839 0.6602 0.2955  0.145   0.167   164 GLN C NE2 
3082 N  N   . GLU C 134 ? 0.4032 0.8155 0.4529 0.2071  0.1107  0.1581  165 GLU C N   
3083 C  CA  . GLU C 134 ? 0.3872 0.8596 0.4571 0.2119  0.1158  0.1776  165 GLU C CA  
3084 C  C   . GLU C 134 ? 0.3658 0.8627 0.4535 0.1791  0.1018  0.1792  165 GLU C C   
3085 O  O   . GLU C 134 ? 0.3592 0.8319 0.4466 0.155   0.0883  0.1679  165 GLU C O   
3086 C  CB  . GLU C 134 ? 0.3999 0.9216 0.4914 0.2265  0.1191  0.1998  165 GLU C CB  
3087 C  CG  . GLU C 134 ? 0.4785 1.0191 0.5906 0.2016  0.1022  0.2041  165 GLU C CG  
3088 C  CD  . GLU C 134 ? 0.5907 1.189  0.7257 0.214   0.1041  0.2282  165 GLU C CD  
3089 O  OE1 . GLU C 134 ? 0.6091 1.2634 0.7608 0.224   0.1113  0.2475  165 GLU C OE1 
3090 O  OE2 . GLU C 134 ? 0.6248 1.2153 0.7613 0.2142  0.0985  0.2289  165 GLU C OE2 
3091 N  N   . TYR C 135 ? 0.3531 0.8981 0.4554 0.1791  0.1062  0.1947  166 TYR C N   
3092 C  CA  . TYR C 135 ? 0.3592 0.9301 0.4775 0.1488  0.0949  0.1997  166 TYR C CA  
3093 C  C   . TYR C 135 ? 0.3468 0.9885 0.4895 0.1519  0.1002  0.225   166 TYR C C   
3094 O  O   . TYR C 135 ? 0.3412 1.0052 0.4828 0.181   0.1158  0.2354  166 TYR C O   
3095 C  CB  . TYR C 135 ? 0.3767 0.9114 0.4766 0.139   0.0941  0.1846  166 TYR C CB  
3096 C  CG  . TYR C 135 ? 0.3867 0.9265 0.4734 0.1615  0.1099  0.187   166 TYR C CG  
3097 C  CD1 . TYR C 135 ? 0.418  0.915  0.4764 0.1857  0.1208  0.1732  166 TYR C CD1 
3098 C  CD2 . TYR C 135 ? 0.3753 0.9619 0.4756 0.1577  0.1142  0.2032  166 TYR C CD2 
3099 C  CE1 . TYR C 135 ? 0.4355 0.9346 0.4773 0.2071  0.1361  0.1746  166 TYR C CE1 
3100 C  CE2 . TYR C 135 ? 0.3905 0.9838 0.4775 0.18    0.1299  0.2062  166 TYR C CE2 
3101 C  CZ  . TYR C 135 ? 0.4305 0.9788 0.4871 0.2052  0.1409  0.1913  166 TYR C CZ  
3102 O  OH  . TYR C 135 ? 0.4684 1.0198 0.5073 0.2274  0.157   0.1931  166 TYR C OH  
3103 N  N   . SER C 136 ? 0.3416 1.0183 0.5049 0.1219  0.0877  0.2355  167 SER C N   
3104 C  CA  . SER C 136 ? 0.3271 1.075  0.5152 0.1181  0.0906  0.2606  167 SER C CA  
3105 C  C   . SER C 136 ? 0.338  1.0917 0.5307 0.0842  0.0811  0.2619  167 SER C C   
3106 O  O   . SER C 136 ? 0.3505 1.0603 0.5319 0.061   0.0693  0.2463  167 SER C O   
3107 C  CB  . SER C 136 ? 0.3231 1.1221 0.5352 0.1153  0.0847  0.2785  167 SER C CB  
3108 O  OG  . SER C 136 ? 0.3595 1.1459 0.575  0.082   0.0661  0.2724  167 SER C OG  
3109 N  N   . VAL C 137 ? 0.331  1.1373 0.5385 0.0829  0.0877  0.2811  168 VAL C N   
3110 C  CA  . VAL C 137 ? 0.3504 1.1651 0.5615 0.0521  0.0809  0.2857  168 VAL C CA  
3111 C  C   . VAL C 137 ? 0.3403 1.2272 0.5808 0.0305  0.0745  0.3112  168 VAL C C   
3112 O  O   . VAL C 137 ? 0.3108 1.2585 0.5702 0.0493  0.0845  0.3317  168 VAL C O   
3113 C  CB  . VAL C 137 ? 0.3632 1.176  0.5633 0.0682  0.0953  0.2865  168 VAL C CB  
3114 C  CG1 . VAL C 137 ? 0.3606 1.1915 0.5671 0.0376  0.0902  0.2967  168 VAL C CG1 
3115 C  CG2 . VAL C 137 ? 0.4028 1.1459 0.572  0.0855  0.0998  0.2613  168 VAL C CG2 
3116 N  N   . SER C 138 ? 0.3545 1.235  0.5976 -0.009  0.0582  0.3105  169 SER C N   
3117 C  CA  . SER C 138 ? 0.3372 1.2829 0.605  -0.0371 0.0497  0.3338  169 SER C CA  
3118 C  C   . SER C 138 ? 0.3509 1.2756 0.61   -0.0741 0.0416  0.3321  169 SER C C   
3119 O  O   . SER C 138 ? 0.3756 1.2376 0.6139 -0.0914 0.032   0.3128  169 SER C O   
3120 C  CB  . SER C 138 ? 0.3574 1.3119 0.6325 -0.0511 0.0356  0.3338  169 SER C CB  
3121 O  OG  . SER C 138 ? 0.3638 1.3848 0.6617 -0.081  0.0261  0.3569  169 SER C OG  
3122 N  N   . ASP C 139 ? 0.3355 1.3094 0.6086 -0.0835 0.047   0.3524  170 ASP C N   
3123 C  CA  . ASP C 139 ? 0.3555 1.3141 0.6207 -0.1176 0.0417  0.3549  170 ASP C CA  
3124 C  C   . ASP C 139 ? 0.38   1.268  0.6173 -0.1019 0.0489  0.3339  170 ASP C C   
3125 O  O   . ASP C 139 ? 0.3976 1.2908 0.6325 -0.0681 0.0639  0.3332  170 ASP C O   
3126 C  CB  . ASP C 139 ? 0.4077 1.3528 0.6693 -0.1631 0.0221  0.3535  170 ASP C CB  
3127 C  CG  . ASP C 139 ? 0.5085 1.4615 0.7686 -0.2037 0.0165  0.3659  170 ASP C CG  
3128 O  OD1 . ASP C 139 ? 0.5234 1.4968 0.7878 -0.1975 0.0276  0.3773  170 ASP C OD1 
3129 O  OD2 . ASP C 139 ? 0.5623 1.4986 0.8143 -0.2423 0.0013  0.3641  170 ASP C OD2 
3130 N  N   . ASN C 140 ? 0.3728 1.1969 0.5881 -0.1241 0.0392  0.3175  171 ASN C N   
3131 C  CA  . ASN C 140 ? 0.3747 1.1379 0.5655 -0.109  0.045   0.2995  171 ASN C CA  
3132 C  C   . ASN C 140 ? 0.3532 1.0594 0.5279 -0.0953 0.0402  0.2748  171 ASN C C   
3133 O  O   . ASN C 140 ? 0.3767 1.0269 0.5301 -0.093  0.0398  0.2588  171 ASN C O   
3134 C  CB  . ASN C 140 ? 0.4197 1.153  0.5964 -0.139  0.0405  0.3013  171 ASN C CB  
3135 C  CG  . ASN C 140 ? 0.5075 1.1969 0.6705 -0.1726 0.0256  0.2926  171 ASN C CG  
3136 O  OD1 . ASN C 140 ? 0.5326 1.2238 0.6997 -0.1814 0.0161  0.2882  171 ASN C OD1 
3137 N  ND2 . ASN C 140 ? 0.5409 1.187  0.6843 -0.1912 0.024   0.2902  171 ASN C ND2 
3138 N  N   . THR C 141 ? 0.3113 1.0342 0.4964 -0.086  0.0369  0.2733  172 THR C N   
3139 C  CA  . THR C 141 ? 0.3099 0.9821 0.4809 -0.0767 0.0318  0.252   172 THR C CA  
3140 C  C   . THR C 141 ? 0.2805 0.958  0.454  -0.0399 0.0409  0.2465  172 THR C C   
3141 O  O   . THR C 141 ? 0.2563 0.9848 0.4481 -0.0276 0.0454  0.2609  172 THR C O   
3142 C  CB  . THR C 141 ? 0.3292 0.9989 0.5024 -0.1055 0.0169  0.2519  172 THR C CB  
3143 O  OG1 . THR C 141 ? 0.3547 1.0067 0.5184 -0.1395 0.0095  0.2546  172 THR C OG1 
3144 C  CG2 . THR C 141 ? 0.3498 0.9701 0.5089 -0.0978 0.0116  0.2315  172 THR C CG2 
3145 N  N   . ILE C 142 ? 0.2765 0.9008 0.4305 -0.0227 0.0437  0.2263  173 ILE C N   
3146 C  CA  . ILE C 142 ? 0.2712 0.8873 0.4211 0.0092  0.0519  0.2183  173 ILE C CA  
3147 C  C   . ILE C 142 ? 0.2679 0.852  0.4128 0.0049  0.0425  0.2053  173 ILE C C   
3148 O  O   . ILE C 142 ? 0.2829 0.8235 0.4148 -0.0103 0.0344  0.1918  173 ILE C O   
3149 C  CB  . ILE C 142 ? 0.3043 0.8829 0.4333 0.0297  0.0613  0.2045  173 ILE C CB  
3150 C  CG1 . ILE C 142 ? 0.3164 0.9175 0.4452 0.0297  0.0693  0.2153  173 ILE C CG1 
3151 C  CG2 . ILE C 142 ? 0.3139 0.8828 0.4351 0.0617  0.0711  0.1974  173 ILE C CG2 
3152 C  CD1 . ILE C 142 ? 0.3608 0.9232 0.4659 0.0454  0.0761  0.2009  173 ILE C CD1 
3153 N  N   . THR C 143 ? 0.247  0.8515 0.4009 0.0206  0.0447  0.2098  174 THR C N   
3154 C  CA  . THR C 143 ? 0.2525 0.8284 0.401  0.0199  0.0375  0.1984  174 THR C CA  
3155 C  C   . THR C 143 ? 0.253  0.7986 0.3877 0.0507  0.0479  0.1867  174 THR C C   
3156 O  O   . THR C 143 ? 0.2493 0.82   0.3881 0.0752  0.0595  0.1959  174 THR C O   
3157 C  CB  . THR C 143 ? 0.2585 0.8796 0.4257 0.0144  0.032   0.2135  174 THR C CB  
3158 O  OG1 . THR C 143 ? 0.2687 0.9168 0.4458 -0.0181 0.0215  0.224   174 THR C OG1 
3159 C  CG2 . THR C 143 ? 0.2717 0.8642 0.4321 0.0167  0.0259  0.2026  174 THR C CG2 
3160 N  N   . VAL C 144 ? 0.2531 0.7453 0.3701 0.0496  0.0445  0.1674  175 VAL C N   
3161 C  CA  . VAL C 144 ? 0.2678 0.7254 0.3678 0.0737  0.0532  0.1547  175 VAL C CA  
3162 C  C   . VAL C 144 ? 0.2771 0.7099 0.3731 0.0765  0.0489  0.1465  175 VAL C C   
3163 O  O   . VAL C 144 ? 0.2811 0.6892 0.3738 0.0587  0.0388  0.1372  175 VAL C O   
3164 C  CB  . VAL C 144 ? 0.2942 0.7122 0.3758 0.0703  0.0534  0.1396  175 VAL C CB  
3165 C  CG1 . VAL C 144 ? 0.3259 0.7064 0.3871 0.0906  0.0607  0.1256  175 VAL C CG1 
3166 C  CG2 . VAL C 144 ? 0.2803 0.7217 0.3641 0.0682  0.0582  0.1484  175 VAL C CG2 
3167 N  N   . THR C 145 ? 0.2759 0.7127 0.3699 0.1004  0.0578  0.1503  176 THR C N   
3168 C  CA  . THR C 145 ? 0.2921 0.7062 0.3813 0.1058  0.0556  0.1447  176 THR C CA  
3169 C  C   . THR C 145 ? 0.2998 0.6614 0.3648 0.1195  0.0619  0.1278  176 THR C C   
3170 O  O   . THR C 145 ? 0.3047 0.6586 0.3571 0.1411  0.0743  0.1275  176 THR C O   
3171 C  CB  . THR C 145 ? 0.3156 0.7691 0.4181 0.123   0.061   0.1625  176 THR C CB  
3172 O  OG1 . THR C 145 ? 0.3212 0.827  0.4464 0.1059  0.0532  0.1786  176 THR C OG1 
3173 C  CG2 . THR C 145 ? 0.3169 0.7476 0.4137 0.1301  0.0595  0.1587  176 THR C CG2 
3174 N  N   . PRO C 146 ? 0.3031 0.6283 0.36   0.1066  0.0539  0.1141  177 PRO C N   
3175 C  CA  . PRO C 146 ? 0.3249 0.602  0.3593 0.1154  0.0584  0.0986  177 PRO C CA  
3176 C  C   . PRO C 146 ? 0.341  0.6056 0.3664 0.1373  0.0676  0.1018  177 PRO C C   
3177 O  O   . PRO C 146 ? 0.3192 0.6078 0.3579 0.1417  0.0667  0.1138  177 PRO C O   
3178 C  CB  . PRO C 146 ? 0.3367 0.5896 0.3704 0.0947  0.0469  0.0876  177 PRO C CB  
3179 C  CG  . PRO C 146 ? 0.331  0.6122 0.3817 0.0757  0.0377  0.0945  177 PRO C CG  
3180 C  CD  . PRO C 146 ? 0.2914 0.6174 0.3575 0.0829  0.0409  0.1121  177 PRO C CD  
3181 N  N   . LYS C 147 ? 0.3727 0.598  0.3735 0.1506  0.0764  0.0911  178 LYS C N   
3182 C  CA  . LYS C 147 ? 0.3981 0.5987 0.3833 0.1718  0.0866  0.0922  178 LYS C CA  
3183 C  C   . LYS C 147 ? 0.4107 0.578  0.3904 0.159   0.0791  0.0827  178 LYS C C   
3184 O  O   . LYS C 147 ? 0.4362 0.5712 0.4029 0.1452  0.0744  0.0677  178 LYS C O   
3185 C  CB  . LYS C 147 ? 0.4544 0.6199 0.4096 0.1886  0.0993  0.083   178 LYS C CB  
3186 C  CG  . LYS C 147 ? 0.5545 0.6856 0.4873 0.2123  0.112   0.0837  178 LYS C CG  
3187 C  CD  . LYS C 147 ? 0.6611 0.7525 0.5585 0.2279  0.1252  0.0732  178 LYS C CD  
3188 C  CE  . LYS C 147 ? 0.7212 0.848  0.6228 0.2454  0.1352  0.0834  178 LYS C CE  
3189 N  NZ  . LYS C 147 ? 0.7908 0.8757 0.6531 0.2628  0.1494  0.0728  178 LYS C NZ  
3190 N  N   . ILE C 148 ? 0.3805 0.5611 0.372  0.1617  0.0769  0.0927  179 ILE C N   
3191 C  CA  . ILE C 148 ? 0.387  0.5409 0.3751 0.1492  0.07    0.0857  179 ILE C CA  
3192 C  C   . ILE C 148 ? 0.4068 0.5399 0.3827 0.1687  0.0791  0.0917  179 ILE C C   
3193 O  O   . ILE C 148 ? 0.3919 0.555  0.3783 0.1854  0.084   0.1079  179 ILE C O   
3194 C  CB  . ILE C 148 ? 0.3712 0.5571 0.3826 0.129   0.0568  0.0905  179 ILE C CB  
3195 C  CG1 . ILE C 148 ? 0.3802 0.5823 0.4005 0.1116  0.0495  0.0858  179 ILE C CG1 
3196 C  CG2 . ILE C 148 ? 0.3787 0.5387 0.3859 0.1167  0.0504  0.0835  179 ILE C CG2 
3197 C  CD1 . ILE C 148 ? 0.3779 0.6124 0.4177 0.0934  0.0383  0.0923  179 ILE C CD1 
3198 N  N   . PRO C 149 ? 0.4347 0.5167 0.3875 0.1672  0.082   0.08    180 PRO C N   
3199 C  CA  . PRO C 149 ? 0.453  0.5077 0.3901 0.1861  0.0919  0.0859  180 PRO C CA  
3200 C  C   . PRO C 149 ? 0.4503 0.5286 0.4057 0.1825  0.0853  0.0976  180 PRO C C   
3201 O  O   . PRO C 149 ? 0.4349 0.5302 0.4061 0.1604  0.0728  0.0944  180 PRO C O   
3202 C  CB  . PRO C 149 ? 0.4925 0.4872 0.4015 0.1759  0.0931  0.0688  180 PRO C CB  
3203 C  CG  . PRO C 149 ? 0.4947 0.4986 0.4155 0.1477  0.0795  0.0576  180 PRO C CG  
3204 C  CD  . PRO C 149 ? 0.4459 0.4942 0.3857 0.1474  0.0763  0.0621  180 PRO C CD  
3205 N  N   . PRO C 150 ? 0.4569 0.5349 0.408  0.2049  0.0941  0.1113  181 PRO C N   
3206 C  CA  . PRO C 150 ? 0.4511 0.5499 0.4167 0.2008  0.0874  0.1223  181 PRO C CA  
3207 C  C   . PRO C 150 ? 0.4688 0.5268 0.4228 0.1823  0.0821  0.1103  181 PRO C C   
3208 O  O   . PRO C 150 ? 0.4799 0.4874 0.4097 0.1816  0.0881  0.0985  181 PRO C O   
3209 C  CB  . PRO C 150 ? 0.4653 0.5663 0.4242 0.2327  0.1004  0.1398  181 PRO C CB  
3210 C  CG  . PRO C 150 ? 0.502  0.5572 0.4321 0.2515  0.1155  0.1325  181 PRO C CG  
3211 C  CD  . PRO C 150 ? 0.4785 0.5334 0.4084 0.2357  0.1113  0.1173  181 PRO C CD  
3212 N  N   . CYS C 151 ? 0.4663 0.5466 0.4362 0.1656  0.0708  0.1129  182 CYS C N   
3213 C  CA  . CYS C 151 ? 0.4986 0.5464 0.4596 0.1495  0.0668  0.1041  182 CYS C CA  
3214 C  C   . CYS C 151 ? 0.5416 0.572  0.4914 0.1667  0.0746  0.1161  182 CYS C C   
3215 O  O   . CYS C 151 ? 0.5362 0.6024 0.4994 0.175   0.0724  0.1314  182 CYS C O   
3216 C  CB  . CYS C 151 ? 0.4715 0.5481 0.4507 0.127   0.0534  0.102   182 CYS C CB  
3217 S  SG  . CYS C 151 ? 0.4849 0.5269 0.4554 0.1058  0.049   0.0897  182 CYS C SG  
3218 N  N   . THR C 152 ? 0.5852 0.5611 0.509  0.1725  0.0841  0.1104  183 THR C N   
3219 C  CA  . THR C 152 ? 0.6203 0.57   0.5283 0.191   0.0939  0.1221  183 THR C CA  
3220 C  C   . THR C 152 ? 0.6422 0.5551 0.5384 0.1739  0.0916  0.1166  183 THR C C   
3221 O  O   . THR C 152 ? 0.6409 0.5718 0.5464 0.1723  0.0875  0.1268  183 THR C O   
3222 C  CB  . THR C 152 ? 0.6775 0.5901 0.5602 0.2163  0.1097  0.1229  183 THR C CB  
3223 O  OG1 . THR C 152 ? 0.7232 0.5907 0.5854 0.2007  0.1104  0.1034  183 THR C OG1 
3224 C  CG2 . THR C 152 ? 0.6702 0.6258 0.5663 0.237   0.1138  0.1326  183 THR C CG2 
3225 N  N   . THR C 153 ? 0.6578 0.5222 0.5333 0.1601  0.0939  0.1012  184 THR C N   
3226 C  CA  . THR C 153 ? 0.6665 0.4955 0.5301 0.1402  0.0919  0.0948  184 THR C CA  
3227 C  C   . THR C 153 ? 0.6605 0.4613 0.512  0.1196  0.0894  0.076   184 THR C C   
3228 O  O   . THR C 153 ? 0.6732 0.472  0.5191 0.1252  0.0916  0.0687  184 THR C O   
3229 C  CB  . THR C 153 ? 0.7171 0.502  0.5562 0.1551  0.1036  0.1051  184 THR C CB  
3230 O  OG1 . THR C 153 ? 0.7386 0.5035 0.5733 0.1344  0.1001  0.1032  184 THR C OG1 
3231 C  CG2 . THR C 153 ? 0.7564 0.4853 0.5616 0.1697  0.117   0.1     184 THR C CG2 
3232 N  N   . GLY C 154 ? 0.6376 0.4217 0.4861 0.0958  0.0844  0.0693  185 GLY C N   
3233 C  CA  . GLY C 154 ? 0.6282 0.3922 0.467  0.074   0.0803  0.0534  185 GLY C CA  
3234 C  C   . GLY C 154 ? 0.5731 0.382  0.4365 0.0634  0.0698  0.0462  185 GLY C C   
3235 O  O   . GLY C 154 ? 0.5437 0.3964 0.4324 0.0642  0.0636  0.0524  185 GLY C O   
3236 N  N   . THR C 155 ? 0.5573 0.354  0.4109 0.0531  0.0677  0.0334  186 THR C N   
3237 C  CA  . THR C 155 ? 0.5275 0.3642 0.4024 0.044   0.0584  0.0275  186 THR C CA  
3238 C  C   . THR C 155 ? 0.4976 0.3599 0.3813 0.0636  0.0607  0.0314  186 THR C C   
3239 O  O   . THR C 155 ? 0.5259 0.3657 0.3906 0.079   0.0692  0.0303  186 THR C O   
3240 C  CB  . THR C 155 ? 0.5649 0.3853 0.428  0.0236  0.0538  0.014   186 THR C CB  
3241 O  OG1 . THR C 155 ? 0.5882 0.3896 0.4452 0.0042  0.0517  0.0129  186 THR C OG1 
3242 C  CG2 . THR C 155 ? 0.5596 0.4226 0.4458 0.0147  0.0443  0.0101  186 THR C CG2 
3243 N  N   . TRP C 156 ? 0.4369 0.345  0.3474 0.0629  0.0538  0.0363  187 TRP C N   
3244 C  CA  . TRP C 156 ? 0.4049 0.3431 0.3266 0.0775  0.0547  0.0415  187 TRP C CA  
3245 C  C   . TRP C 156 ? 0.3739 0.3301 0.304  0.0658  0.0479  0.0326  187 TRP C C   
3246 O  O   . TRP C 156 ? 0.3522 0.3227 0.2948 0.0496  0.0399  0.0291  187 TRP C O   
3247 C  CB  . TRP C 156 ? 0.3908 0.3654 0.3333 0.0824  0.0511  0.0538  187 TRP C CB  
3248 C  CG  . TRP C 156 ? 0.3858 0.3952 0.3409 0.0949  0.0514  0.0611  187 TRP C CG  
3249 C  CD1 . TRP C 156 ? 0.3989 0.4078 0.3468 0.1158  0.0604  0.0674  187 TRP C CD1 
3250 C  CD2 . TRP C 156 ? 0.3644 0.4146 0.3407 0.0868  0.0429  0.0639  187 TRP C CD2 
3251 N  NE1 . TRP C 156 ? 0.3817 0.4343 0.3482 0.12    0.0574  0.075   187 TRP C NE1 
3252 C  CE2 . TRP C 156 ? 0.3692 0.4453 0.3522 0.1009  0.0462  0.0725  187 TRP C CE2 
3253 C  CE3 . TRP C 156 ? 0.3575 0.4224 0.3456 0.0691  0.0337  0.0601  187 TRP C CE3 
3254 C  CZ2 . TRP C 156 ? 0.355  0.4713 0.3564 0.0946  0.0394  0.0776  187 TRP C CZ2 
3255 C  CZ3 . TRP C 156 ? 0.3516 0.45   0.3544 0.0645  0.0278  0.0636  187 TRP C CZ3 
3256 C  CH2 . TRP C 156 ? 0.3433 0.4672 0.3528 0.0756  0.03    0.0726  187 TRP C CH2 
3257 N  N   . LYS C 157 ? 0.3603 0.3126 0.2809 0.0749  0.0522  0.0292  188 LYS C N   
3258 C  CA  . LYS C 157 ? 0.3679 0.3345 0.2933 0.0652  0.0467  0.0214  188 LYS C CA  
3259 C  C   . LYS C 157 ? 0.3514 0.3489 0.2876 0.0777  0.0485  0.0276  188 LYS C C   
3260 O  O   . LYS C 157 ? 0.3665 0.3536 0.2883 0.0907  0.0561  0.0263  188 LYS C O   
3261 C  CB  . LYS C 157 ? 0.4338 0.3635 0.3327 0.0593  0.0492  0.0093  188 LYS C CB  
3262 C  CG  . LYS C 157 ? 0.5124 0.4166 0.4027 0.0415  0.0458  0.0038  188 LYS C CG  
3263 C  CD  . LYS C 157 ? 0.6264 0.4815 0.4823 0.0393  0.0516  -0.0055 188 LYS C CD  
3264 C  CE  . LYS C 157 ? 0.7083 0.5561 0.557  0.0148  0.0433  -0.0162 188 LYS C CE  
3265 N  NZ  . LYS C 157 ? 0.7691 0.5691 0.5899 0.0029  0.0461  -0.0219 188 LYS C NZ  
3266 N  N   . PRO C 158 ? 0.3201 0.3544 0.2798 0.0727  0.0418  0.0342  189 PRO C N   
3267 C  CA  . PRO C 158 ? 0.3    0.367  0.2717 0.0812  0.0428  0.0419  189 PRO C CA  
3268 C  C   . PRO C 158 ? 0.2941 0.3702 0.266  0.0758  0.0405  0.0363  189 PRO C C   
3269 O  O   . PRO C 158 ? 0.2832 0.385  0.2634 0.0826  0.0423  0.0433  189 PRO C O   
3270 C  CB  . PRO C 158 ? 0.2923 0.3884 0.2842 0.0735  0.0355  0.0498  189 PRO C CB  
3271 C  CG  . PRO C 158 ? 0.3038 0.3852 0.2956 0.0569  0.029   0.0417  189 PRO C CG  
3272 C  CD  . PRO C 158 ? 0.3061 0.3518 0.2799 0.0598  0.0342  0.036   189 PRO C CD  
3273 N  N   . TRP C 159 ? 0.2977 0.3562 0.2611 0.0633  0.0364  0.0253  190 TRP C N   
3274 C  CA  . TRP C 159 ? 0.3046 0.37   0.2655 0.0588  0.0342  0.0202  190 TRP C CA  
3275 C  C   . TRP C 159 ? 0.3402 0.3746 0.2746 0.0623  0.0394  0.0104  190 TRP C C   
3276 O  O   . TRP C 159 ? 0.3595 0.3632 0.2779 0.0639  0.0432  0.0062  190 TRP C O   
3277 C  CB  . TRP C 159 ? 0.285  0.3582 0.2559 0.042   0.0249  0.0165  190 TRP C CB  
3278 C  CG  . TRP C 159 ? 0.2517 0.3487 0.2421 0.0375  0.0203  0.024   190 TRP C CG  
3279 C  CD1 . TRP C 159 ? 0.2455 0.3439 0.2437 0.0345  0.0183  0.0277  190 TRP C CD1 
3280 C  CD2 . TRP C 159 ? 0.2284 0.3469 0.2289 0.0338  0.0171  0.0282  190 TRP C CD2 
3281 N  NE1 . TRP C 159 ? 0.2319 0.3499 0.2426 0.0287  0.0139  0.0328  190 TRP C NE1 
3282 C  CE2 . TRP C 159 ? 0.2273 0.3563 0.2394 0.0277  0.0131  0.0332  190 TRP C CE2 
3283 C  CE3 . TRP C 159 ? 0.24   0.368  0.2387 0.0345  0.0174  0.0282  190 TRP C CE3 
3284 C  CZ2 . TRP C 159 ? 0.2308 0.3749 0.2507 0.0214  0.0097  0.0376  190 TRP C CZ2 
3285 C  CZ3 . TRP C 159 ? 0.2388 0.3845 0.2478 0.0289  0.0142  0.034   190 TRP C CZ3 
3286 C  CH2 . TRP C 159 ? 0.2264 0.3779 0.245  0.022   0.0104  0.0383  190 TRP C CH2 
3287 N  N   . HIS C 160 ? 0.3392 0.379  0.2662 0.0632  0.04    0.0068  191 HIS C N   
3288 C  CA  . HIS C 160 ? 0.3689 0.3775 0.2664 0.0649  0.0443  -0.0037 191 HIS C CA  
3289 C  C   . HIS C 160 ? 0.392  0.3797 0.28   0.0458  0.0367  -0.0138 191 HIS C C   
3290 O  O   . HIS C 160 ? 0.383  0.3897 0.2887 0.0323  0.0277  -0.0127 191 HIS C O   
3291 C  CB  . HIS C 160 ? 0.3671 0.3894 0.2586 0.0687  0.0457  -0.0049 191 HIS C CB  
3292 C  CG  . HIS C 160 ? 0.4174 0.4081 0.2746 0.0761  0.0533  -0.0143 191 HIS C CG  
3293 N  ND1 . HIS C 160 ? 0.4556 0.4219 0.2906 0.0614  0.0481  -0.027  191 HIS C ND1 
3294 C  CD2 . HIS C 160 ? 0.4378 0.4198 0.2785 0.0964  0.0657  -0.0124 191 HIS C CD2 
3295 C  CE1 . HIS C 160 ? 0.4792 0.4169 0.2816 0.072   0.0572  -0.0339 191 HIS C CE1 
3296 N  NE2 . HIS C 160 ? 0.479  0.4242 0.2835 0.0948  0.069   -0.0254 191 HIS C NE2 
3297 N  N   . ASN C 161 ? 0.4207 0.3695 0.2799 0.0447  0.0409  -0.0228 192 ASN C N   
3298 C  CA  . ASN C 161 ? 0.4583 0.3852 0.3042 0.0247  0.0342  -0.0322 192 ASN C CA  
3299 C  C   . ASN C 161 ? 0.4635 0.4114 0.3131 0.0095  0.0242  -0.0365 192 ASN C C   
3300 O  O   . ASN C 161 ? 0.4723 0.4239 0.3269 -0.0086 0.0157  -0.0389 192 ASN C O   
3301 C  CB  . ASN C 161 ? 0.5364 0.4125 0.343  0.0269  0.0419  -0.0419 192 ASN C CB  
3302 C  CG  . ASN C 161 ? 0.6519 0.5029 0.4436 0.0031  0.0349  -0.0505 192 ASN C CG  
3303 O  OD1 . ASN C 161 ? 0.683  0.527  0.4831 -0.0041 0.0336  -0.0471 192 ASN C OD1 
3304 N  ND2 . ASN C 161 ? 0.6858 0.5271 0.456  -0.0114 0.0295  -0.0609 192 ASN C ND2 
3305 N  N   . ASP C 162 ? 0.4494 0.4134 0.2966 0.017   0.0253  -0.0362 193 ASP C N   
3306 C  CA  . ASP C 162 ? 0.4343 0.4208 0.285  0.0051  0.0161  -0.0382 193 ASP C CA  
3307 C  C   . ASP C 162 ? 0.4148 0.4342 0.298  -0.0032 0.0079  -0.0301 193 ASP C C   
3308 O  O   . ASP C 162 ? 0.4247 0.4561 0.3113 -0.0178 -0.0009 -0.0318 193 ASP C O   
3309 C  CB  . ASP C 162 ? 0.428  0.4317 0.2771 0.0177  0.0201  -0.0351 193 ASP C CB  
3310 C  CG  . ASP C 162 ? 0.4759 0.4527 0.2898 0.0252  0.0274  -0.0438 193 ASP C CG  
3311 O  OD1 . ASP C 162 ? 0.483  0.4204 0.2691 0.021   0.0303  -0.0535 193 ASP C OD1 
3312 O  OD2 . ASP C 162 ? 0.4911 0.4834 0.3027 0.0353  0.0311  -0.0408 193 ASP C OD2 
3313 N  N   . LEU C 163 ? 0.3842 0.4188 0.2895 0.0068  0.011   -0.0209 194 LEU C N   
3314 C  CA  . LEU C 163 ? 0.3583 0.4183 0.2901 0.0015  0.0052  -0.0136 194 LEU C CA  
3315 C  C   . LEU C 163 ? 0.3579 0.4113 0.2942 -0.0106 0.0011  -0.0152 194 LEU C C   
3316 O  O   . LEU C 163 ? 0.3439 0.415  0.2902 -0.0204 -0.0056 -0.0138 194 LEU C O   
3317 C  CB  . LEU C 163 ? 0.3382 0.4114 0.2873 0.0128  0.0094  -0.0044 194 LEU C CB  
3318 C  CG  . LEU C 163 ? 0.3313 0.4235 0.3021 0.0081  0.0048  0.0021  194 LEU C CG  
3319 C  CD1 . LEU C 163 ? 0.3172 0.4271 0.293  0.0029  -0.0007 0.0036  194 LEU C CD1 
3320 C  CD2 . LEU C 163 ? 0.3287 0.4315 0.3114 0.0157  0.0079  0.01    194 LEU C CD2 
3321 N  N   . THR C 164 ? 0.3719 0.402  0.3012 -0.009  0.0057  -0.0168 195 THR C N   
3322 C  CA  . THR C 164 ? 0.3769 0.4005 0.3104 -0.0206 0.0029  -0.017  195 THR C CA  
3323 C  C   . THR C 164 ? 0.4043 0.418  0.3228 -0.0383 -0.0027 -0.0244 195 THR C C   
3324 O  O   . THR C 164 ? 0.3965 0.4229 0.3259 -0.0511 -0.0081 -0.0222 195 THR C O   
3325 C  CB  . THR C 164 ? 0.3922 0.3937 0.3213 -0.013  0.0097  -0.015  195 THR C CB  
3326 O  OG1 . THR C 164 ? 0.415  0.386  0.3188 -0.0052 0.0166  -0.0205 195 THR C OG1 
3327 C  CG2 . THR C 164 ? 0.3713 0.3921 0.3202 -0.001  0.0121  -0.0059 195 THR C CG2 
3328 N  N   . SER C 165 ? 0.4285 0.4216 0.3213 -0.0397 -0.0017 -0.0328 196 SER C N   
3329 C  CA  . SER C 165 ? 0.4572 0.4415 0.3328 -0.0599 -0.0086 -0.0404 196 SER C CA  
3330 C  C   . SER C 165 ? 0.4446 0.4705 0.3376 -0.0677 -0.018  -0.0362 196 SER C C   
3331 O  O   . SER C 165 ? 0.4535 0.4917 0.3495 -0.0856 -0.0256 -0.0362 196 SER C O   
3332 C  CB  . SER C 165 ? 0.5264 0.4731 0.3647 -0.0599 -0.0046 -0.0515 196 SER C CB  
3333 O  OG  . SER C 165 ? 0.591  0.549  0.4264 -0.0459 -0.002  -0.0515 196 SER C OG  
3334 N  N   . LYS C 166 ? 0.4283 0.4779 0.3346 -0.0543 -0.0173 -0.0308 197 LYS C N   
3335 C  CA  . LYS C 166 ? 0.4212 0.5084 0.3436 -0.0579 -0.0247 -0.0248 197 LYS C CA  
3336 C  C   . LYS C 166 ? 0.3975 0.5077 0.347  -0.0596 -0.0265 -0.0158 197 LYS C C   
3337 O  O   . LYS C 166 ? 0.3882 0.5243 0.3476 -0.0698 -0.0333 -0.0117 197 LYS C O   
3338 C  CB  . LYS C 166 ? 0.4465 0.5465 0.3734 -0.0421 -0.0216 -0.0206 197 LYS C CB  
3339 C  CG  . LYS C 166 ? 0.4905 0.626  0.4396 -0.0386 -0.0256 -0.0103 197 LYS C CG  
3340 C  CD  . LYS C 166 ? 0.5687 0.7262 0.514  -0.0496 -0.0344 -0.0099 197 LYS C CD  
3341 C  CE  . LYS C 166 ? 0.6125 0.804  0.5791 -0.0434 -0.0371 0.0021  197 LYS C CE  
3342 N  NZ  . LYS C 166 ? 0.6385 0.8397 0.6257 -0.0425 -0.0359 0.0086  197 LYS C NZ  
3343 N  N   . LEU C 167 ? 0.3756 0.4784 0.3362 -0.0488 -0.0201 -0.012  198 LEU C N   
3344 C  CA  . LEU C 167 ? 0.3622 0.4823 0.3444 -0.048  -0.0201 -0.0041 198 LEU C CA  
3345 C  C   . LEU C 167 ? 0.3707 0.4908 0.3549 -0.0626 -0.0227 -0.0042 198 LEU C C   
3346 O  O   . LEU C 167 ? 0.3747 0.5195 0.3763 -0.0644 -0.0244 0.003   198 LEU C O   
3347 C  CB  . LEU C 167 ? 0.3498 0.4598 0.3388 -0.0352 -0.0134 -0.001  198 LEU C CB  
3348 C  CG  . LEU C 167 ? 0.3469 0.4622 0.3385 -0.0227 -0.0109 0.0019  198 LEU C CG  
3349 C  CD1 . LEU C 167 ? 0.3405 0.4477 0.3378 -0.0142 -0.0057 0.0051  198 LEU C CD1 
3350 C  CD2 . LEU C 167 ? 0.3421 0.4817 0.3455 -0.0203 -0.0138 0.0083  198 LEU C CD2 
3351 N  N   . GLY C 168 ? 0.3751 0.4662 0.3408 -0.0718 -0.0218 -0.0115 199 GLY C N   
3352 C  CA  . GLY C 168 ? 0.3801 0.467  0.3458 -0.0876 -0.0236 -0.0111 199 GLY C CA  
3353 C  C   . GLY C 168 ? 0.3901 0.4622 0.3617 -0.0809 -0.0168 -0.0076 199 GLY C C   
3354 O  O   . GLY C 168 ? 0.3721 0.4444 0.3515 -0.0646 -0.0119 -0.0044 199 GLY C O   
3355 N  N   . SER C 169 ? 0.404  0.4631 0.3703 -0.0947 -0.0167 -0.0077 200 SER C N   
3356 C  CA  . SER C 169 ? 0.4242 0.4666 0.3924 -0.0905 -0.0104 -0.0041 200 SER C CA  
3357 C  C   . SER C 169 ? 0.3984 0.4634 0.3886 -0.0772 -0.0072 0.0044  200 SER C C   
3358 O  O   . SER C 169 ? 0.4018 0.4522 0.3905 -0.0651 -0.0018 0.0059  200 SER C O   
3359 C  CB  . SER C 169 ? 0.4706 0.5049 0.4334 -0.1115 -0.0123 -0.0033 200 SER C CB  
3360 O  OG  . SER C 169 ? 0.5587 0.5497 0.5011 -0.1115 -0.0064 -0.0064 200 SER C OG  
3361 N  N   . LEU C 170 ? 0.3666 0.4664 0.3752 -0.0796 -0.0102 0.0104  201 LEU C N   
3362 C  CA  . LEU C 170 ? 0.3533 0.4695 0.3777 -0.0689 -0.0062 0.0177  201 LEU C CA  
3363 C  C   . LEU C 170 ? 0.3373 0.4594 0.366  -0.0524 -0.0049 0.018   201 LEU C C   
3364 O  O   . LEU C 170 ? 0.3374 0.4522 0.3673 -0.0425 -0.0007 0.0199  201 LEU C O   
3365 C  CB  . LEU C 170 ? 0.3495 0.4976 0.3893 -0.0773 -0.0077 0.0253  201 LEU C CB  
3366 C  CG  . LEU C 170 ? 0.3743 0.5182 0.4095 -0.0983 -0.01   0.0258  201 LEU C CG  
3367 C  CD1 . LEU C 170 ? 0.3626 0.5467 0.4163 -0.1067 -0.0113 0.0357  201 LEU C CD1 
3368 C  CD2 . LEU C 170 ? 0.3987 0.51   0.4229 -0.0991 -0.0044 0.025   201 LEU C CD2 
3369 N  N   . LYS C 171 ? 0.3136 0.445  0.3413 -0.0507 -0.0087 0.0158  202 LYS C N   
3370 C  CA  . LYS C 171 ? 0.3037 0.4354 0.3326 -0.0368 -0.007  0.0162  202 LYS C CA  
3371 C  C   . LYS C 171 ? 0.2842 0.3912 0.3018 -0.0315 -0.0043 0.0119  202 LYS C C   
3372 O  O   . LYS C 171 ? 0.2842 0.3905 0.304  -0.022  -0.002  0.0139  202 LYS C O   
3373 C  CB  . LYS C 171 ? 0.3419 0.4907 0.3726 -0.0353 -0.011  0.0167  202 LYS C CB  
3374 C  CG  . LYS C 171 ? 0.4066 0.5843 0.451  -0.0353 -0.0122 0.0242  202 LYS C CG  
3375 C  CD  . LYS C 171 ? 0.5026 0.6975 0.5487 -0.0308 -0.0155 0.0268  202 LYS C CD  
3376 C  CE  . LYS C 171 ? 0.5675 0.7855 0.6262 -0.0211 -0.0129 0.0365  202 LYS C CE  
3377 N  NZ  . LYS C 171 ? 0.6224 0.8475 0.6797 -0.0115 -0.0137 0.0399  202 LYS C NZ  
3378 N  N   . SER C 172 ? 0.2788 0.3652 0.2832 -0.0374 -0.0038 0.0069  203 SER C N   
3379 C  CA  . SER C 172 ? 0.2889 0.3535 0.2827 -0.0287 0.0005  0.0049  203 SER C CA  
3380 C  C   . SER C 172 ? 0.2846 0.3434 0.2824 -0.0236 0.0044  0.0097  203 SER C C   
3381 O  O   . SER C 172 ? 0.2987 0.3481 0.2919 -0.0141 0.0078  0.011   203 SER C O   
3382 C  CB  . SER C 172 ? 0.3167 0.3558 0.2906 -0.0335 0.0016  -0.0018 203 SER C CB  
3383 O  OG  . SER C 172 ? 0.3305 0.3762 0.2985 -0.037  -0.0023 -0.0064 203 SER C OG  
3384 N  N   . VAL C 173 ? 0.2584 0.3273 0.2657 -0.0283 0.0041  0.0136  204 VAL C N   
3385 C  CA  . VAL C 173 ? 0.2461 0.3121 0.256  -0.0231 0.0073  0.0184  204 VAL C CA  
3386 C  C   . VAL C 173 ? 0.2375 0.312  0.2512 -0.0132 0.0073  0.0206  204 VAL C C   
3387 O  O   . VAL C 173 ? 0.2383 0.3083 0.2499 -0.0078 0.0091  0.0237  204 VAL C O   
3388 C  CB  . VAL C 173 ? 0.2544 0.332  0.2725 -0.0288 0.0078  0.0223  204 VAL C CB  
3389 C  CG1 . VAL C 173 ? 0.2575 0.3344 0.2765 -0.0229 0.0108  0.0269  204 VAL C CG1 
3390 C  CG2 . VAL C 173 ? 0.2711 0.3407 0.2852 -0.0412 0.0078  0.0219  204 VAL C CG2 
3391 N  N   . PHE C 174 ? 0.2216 0.3083 0.2396 -0.0117 0.0049  0.0195  205 PHE C N   
3392 C  CA  . PHE C 174 ? 0.2174 0.3098 0.237  -0.0058 0.0045  0.0216  205 PHE C CA  
3393 C  C   . PHE C 174 ? 0.2248 0.3139 0.2401 -0.0002 0.0054  0.0219  205 PHE C C   
3394 O  O   . PHE C 174 ? 0.2255 0.3224 0.243  0.0029  0.0049  0.0253  205 PHE C O   
3395 C  CB  . PHE C 174 ? 0.2132 0.3163 0.2368 -0.0058 0.0027  0.0216  205 PHE C CB  
3396 C  CG  . PHE C 174 ? 0.2148 0.3227 0.2419 -0.0063 0.0038  0.0236  205 PHE C CG  
3397 C  CD1 . PHE C 174 ? 0.2238 0.3398 0.2557 -0.0096 0.0038  0.024   205 PHE C CD1 
3398 C  CD2 . PHE C 174 ? 0.2216 0.3262 0.2458 -0.0038 0.0051  0.0256  205 PHE C CD2 
3399 C  CE1 . PHE C 174 ? 0.2334 0.3566 0.2689 -0.0073 0.0066  0.0275  205 PHE C CE1 
3400 C  CE2 . PHE C 174 ? 0.2286 0.3339 0.2522 -0.0017 0.008   0.0273  205 PHE C CE2 
3401 C  CZ  . PHE C 174 ? 0.2267 0.3427 0.2571 -0.002  0.0094  0.0288  205 PHE C CZ  
3402 N  N   . PHE C 175 ? 0.2346 0.3121 0.2422 0.0007  0.0072  0.0185  206 PHE C N   
3403 C  CA  . PHE C 175 ? 0.2434 0.317  0.2446 0.0087  0.0099  0.0185  206 PHE C CA  
3404 C  C   . PHE C 175 ? 0.2773 0.3316 0.2679 0.0148  0.015   0.0191  206 PHE C C   
3405 O  O   . PHE C 175 ? 0.2863 0.3356 0.2695 0.0245  0.0193  0.0198  206 PHE C O   
3406 C  CB  . PHE C 175 ? 0.2419 0.3147 0.2371 0.0066  0.0088  0.013   206 PHE C CB  
3407 C  CG  . PHE C 175 ? 0.2409 0.3321 0.2451 0.0046  0.0052  0.0148  206 PHE C CG  
3408 C  CD1 . PHE C 175 ? 0.2417 0.3397 0.2516 -0.0021 0.0018  0.0142  206 PHE C CD1 
3409 C  CD2 . PHE C 175 ? 0.24   0.342  0.2466 0.01    0.006   0.0184  206 PHE C CD2 
3410 C  CE1 . PHE C 175 ? 0.2317 0.3425 0.2474 -0.0015 -0.0001 0.017   206 PHE C CE1 
3411 C  CE2 . PHE C 175 ? 0.2314 0.3454 0.2438 0.0075  0.0034  0.0209  206 PHE C CE2 
3412 C  CZ  . PHE C 175 ? 0.2209 0.3368 0.2365 0.0027  0.0007  0.0199  206 PHE C CZ  
3413 N  N   . GLU C 176 ? 0.2801 0.3232 0.269  0.0103  0.0156  0.0197  207 GLU C N   
3414 C  CA  . GLU C 176 ? 0.3049 0.3256 0.2817 0.0164  0.0211  0.0215  207 GLU C CA  
3415 C  C   . GLU C 176 ? 0.3146 0.3328 0.2948 0.013   0.0212  0.0261  207 GLU C C   
3416 O  O   . GLU C 176 ? 0.307  0.3381 0.2967 0.0045  0.0174  0.0262  207 GLU C O   
3417 C  CB  . GLU C 176 ? 0.3636 0.3569 0.3225 0.0121  0.0234  0.0137  207 GLU C CB  
3418 C  CG  . GLU C 176 ? 0.4414 0.4288 0.3992 -0.0049 0.0194  0.0091  207 GLU C CG  
3419 C  CD  . GLU C 176 ? 0.5181 0.4828 0.457  -0.0133 0.0193  0.0003  207 GLU C CD  
3420 O  OE1 . GLU C 176 ? 0.5474 0.5042 0.4748 -0.0054 0.0218  -0.0036 207 GLU C OE1 
3421 O  OE2 . GLU C 176 ? 0.5257 0.4814 0.4601 -0.0289 0.0165  -0.0025 207 GLU C OE2 
3422 N  N   . SER C 177 ? 0.3291 0.3294 0.2997 0.0208  0.0266  0.0307  208 SER C N   
3423 C  CA  . SER C 177 ? 0.3467 0.3436 0.3185 0.0183  0.0273  0.0363  208 SER C CA  
3424 C  C   . SER C 177 ? 0.3762 0.3409 0.3309 0.0239  0.0342  0.0391  208 SER C C   
3425 O  O   . SER C 177 ? 0.4037 0.3505 0.3456 0.0346  0.0395  0.0383  208 SER C O   
3426 C  CB  . SER C 177 ? 0.3618 0.3836 0.3444 0.0254  0.0253  0.0444  208 SER C CB  
3427 O  OG  . SER C 177 ? 0.413  0.4357 0.392  0.0405  0.0293  0.0507  208 SER C OG  
3428 N  N   A TYR C 178 ? 0.3768 0.3317 0.3292 0.0179  0.0353  0.0429  209 TYR C N   
3429 N  N   B TYR C 178 ? 0.3769 0.3324 0.3297 0.0176  0.0352  0.0429  209 TYR C N   
3430 C  CA  A TYR C 178 ? 0.4017 0.3236 0.3366 0.0239  0.0426  0.0478  209 TYR C CA  
3431 C  CA  B TYR C 178 ? 0.4019 0.3248 0.3378 0.0219  0.0421  0.0477  209 TYR C CA  
3432 C  C   A TYR C 178 ? 0.4154 0.35   0.354  0.0414  0.0454  0.0601  209 TYR C C   
3433 C  C   B TYR C 178 ? 0.4135 0.3482 0.3534 0.0355  0.0443  0.0602  209 TYR C C   
3434 O  O   A TYR C 178 ? 0.4301 0.3417 0.3544 0.0552  0.0529  0.0662  209 TYR C O   
3435 O  O   B TYR C 178 ? 0.4234 0.3346 0.3512 0.0396  0.05    0.0668  209 TYR C O   
3436 C  CB  A TYR C 178 ? 0.4052 0.3124 0.3361 0.008   0.0427  0.0481  209 TYR C CB  
3437 C  CB  B TYR C 178 ? 0.4069 0.3131 0.3376 0.0032  0.0415  0.0448  209 TYR C CB  
3438 C  CG  A TYR C 178 ? 0.4109 0.308  0.3377 -0.0111 0.0396  0.0384  209 TYR C CG  
3439 C  CG  B TYR C 178 ? 0.4333 0.2934 0.3397 0.0012  0.0485  0.0453  209 TYR C CG  
3440 C  CD1 A TYR C 178 ? 0.4349 0.3049 0.3441 -0.0127 0.0414  0.0303  209 TYR C CD1 
3441 C  CD1 B TYR C 178 ? 0.4656 0.2932 0.3512 0.0056  0.0528  0.0387  209 TYR C CD1 
3442 C  CD2 A TYR C 178 ? 0.4065 0.3198 0.3444 -0.0277 0.0356  0.0385  209 TYR C CD2 
3443 C  CD2 B TYR C 178 ? 0.4467 0.2928 0.3482 -0.0076 0.0509  0.0513  209 TYR C CD2 
3444 C  CE1 A TYR C 178 ? 0.452  0.3145 0.3557 -0.0327 0.0373  0.0219  209 TYR C CE1 
3445 C  CE1 B TYR C 178 ? 0.4997 0.2773 0.3576 0.0023  0.0598  0.0379  209 TYR C CE1 
3446 C  CE2 A TYR C 178 ? 0.4167 0.3264 0.3522 -0.0462 0.0321  0.0318  209 TYR C CE2 
3447 C  CE2 B TYR C 178 ? 0.4772 0.2761 0.3537 -0.0127 0.0573  0.0515  209 TYR C CE2 
3448 C  CZ  A TYR C 178 ? 0.4502 0.3353 0.3687 -0.0499 0.032   0.0233  209 TYR C CZ  
3449 C  CZ  B TYR C 178 ? 0.5108 0.2732 0.3642 -0.0076 0.0618  0.0445  209 TYR C CZ  
3450 O  OH  A TYR C 178 ? 0.4676 0.3525 0.3829 -0.0704 0.027   0.0169  209 TYR C OH  
3451 O  OH  B TYR C 178 ? 0.5609 0.2694 0.3844 -0.0131 0.0689  0.044   209 TYR C OH  
3452 N  N   . THR C 179 ? 0.405  0.3757 0.3606 0.0409  0.0395  0.0641  210 THR C N   
3453 C  CA  . THR C 179 ? 0.4274 0.4171 0.3874 0.0529  0.0396  0.0762  210 THR C CA  
3454 C  C   . THR C 179 ? 0.4147 0.436  0.3861 0.0609  0.036   0.0787  210 THR C C   
3455 O  O   . THR C 179 ? 0.4128 0.4424 0.39   0.0557  0.033   0.0708  210 THR C O   
3456 C  CB  . THR C 179 ? 0.4719 0.4744 0.4369 0.0441  0.0359  0.0801  210 THR C CB  
3457 O  OG1 . THR C 179 ? 0.5022 0.519  0.4764 0.0302  0.0302  0.0715  210 THR C OG1 
3458 C  CG2 . THR C 179 ? 0.5119 0.4873 0.4652 0.0412  0.0412  0.084   210 THR C CG2 
3459 N  N   . CYS C 180 ? 0.4007 0.4416 0.3754 0.0732  0.0363  0.0913  211 CYS C N   
3460 C  CA  . CYS C 180 ? 0.3923 0.4679 0.3785 0.08    0.0329  0.0971  211 CYS C CA  
3461 C  C   . CYS C 180 ? 0.3652 0.4741 0.3618 0.0697  0.0235  0.1005  211 CYS C C   
3462 O  O   . CYS C 180 ? 0.366  0.5066 0.3707 0.0752  0.0203  0.1101  211 CYS C O   
3463 C  CB  . CYS C 180 ? 0.4222 0.4997 0.4043 0.1024  0.0404  0.1102  211 CYS C CB  
3464 S  SG  . CYS C 180 ? 0.5138 0.5453 0.4768 0.1157  0.0528  0.1043  211 CYS C SG  
3465 N  N   . ASN C 181 ? 0.3336 0.4362 0.3288 0.0546  0.0193  0.0932  212 ASN C N   
3466 C  CA  . ASN C 181 ? 0.3229 0.4491 0.3215 0.0441  0.0113  0.0945  212 ASN C CA  
3467 C  C   . ASN C 181 ? 0.3046 0.4509 0.3111 0.0364  0.0053  0.0905  212 ASN C C   
3468 O  O   . ASN C 181 ? 0.3001 0.4392 0.3099 0.0369  0.0074  0.0839  212 ASN C O   
3469 C  CB  . ASN C 181 ? 0.3615 0.4721 0.3536 0.0327  0.0108  0.0876  212 ASN C CB  
3470 C  CG  . ASN C 181 ? 0.454  0.545  0.4381 0.0379  0.0167  0.0927  212 ASN C CG  
3471 O  OD1 . ASN C 181 ? 0.4828 0.5802 0.4635 0.0471  0.0179  0.1042  212 ASN C OD1 
3472 N  ND2 . ASN C 181 ? 0.4793 0.5476 0.4602 0.0317  0.0206  0.0854  212 ASN C ND2 
3473 N  N   . ASN C 182 ? 0.2821 0.4526 0.2895 0.0277  -0.0024 0.0944  213 ASN C N   
3474 C  CA  . ASN C 182 ? 0.2754 0.4642 0.2883 0.0178  -0.0085 0.0919  213 ASN C CA  
3475 C  C   . ASN C 182 ? 0.2659 0.4358 0.2781 0.0104  -0.0074 0.0791  213 ASN C C   
3476 O  O   . ASN C 182 ? 0.2499 0.4271 0.2686 0.0106  -0.0075 0.078   213 ASN C O   
3477 C  CB  . ASN C 182 ? 0.2863 0.494  0.2937 0.0042  -0.0176 0.095   213 ASN C CB  
3478 C  CG  . ASN C 182 ? 0.3017 0.5232 0.3115 -0.0093 -0.0239 0.0924  213 ASN C CG  
3479 O  OD1 . ASN C 182 ? 0.3005 0.5515 0.3206 -0.0085 -0.0269 0.1016  213 ASN C OD1 
3480 N  ND2 . ASN C 182 ? 0.2899 0.4898 0.2903 -0.0209 -0.0249 0.0807  213 ASN C ND2 
3481 N  N   . ASP C 183 ? 0.2685 0.4171 0.2728 0.0046  -0.0062 0.0709  214 ASP C N   
3482 C  CA  . ASP C 183 ? 0.2675 0.4013 0.2714 -0.0007 -0.0049 0.0606  214 ASP C CA  
3483 C  C   . ASP C 183 ? 0.2456 0.3699 0.2555 0.0068  0.0001  0.0575  214 ASP C C   
3484 O  O   . ASP C 183 ? 0.2403 0.3601 0.2521 0.0035  0.0001  0.0514  214 ASP C O   
3485 C  CB  . ASP C 183 ? 0.3187 0.4367 0.3135 -0.0061 -0.0035 0.0547  214 ASP C CB  
3486 C  CG  . ASP C 183 ? 0.4167 0.5374 0.4    -0.0159 -0.0084 0.0536  214 ASP C CG  
3487 O  OD1 . ASP C 183 ? 0.4306 0.568  0.4135 -0.021  -0.0144 0.0585  214 ASP C OD1 
3488 O  OD2 . ASP C 183 ? 0.4699 0.5766 0.4432 -0.0187 -0.0061 0.0485  214 ASP C OD2 
3489 N  N   . ASP C 184 ? 0.2352 0.3535 0.2451 0.0167  0.0047  0.0618  215 ASP C N   
3490 C  CA  . ASP C 184 ? 0.2388 0.3436 0.2489 0.0231  0.0097  0.0583  215 ASP C CA  
3491 C  C   . ASP C 184 ? 0.2411 0.361  0.2561 0.0307  0.0101  0.0625  215 ASP C C   
3492 O  O   . ASP C 184 ? 0.2438 0.3597 0.2595 0.031   0.0115  0.0572  215 ASP C O   
3493 C  CB  . ASP C 184 ? 0.2801 0.3654 0.283  0.0301  0.0153  0.0609  215 ASP C CB  
3494 C  CG  . ASP C 184 ? 0.3756 0.4481 0.3752 0.0209  0.0155  0.0567  215 ASP C CG  
3495 O  OD1 . ASP C 184 ? 0.3939 0.4634 0.3957 0.0131  0.0143  0.0493  215 ASP C OD1 
3496 O  OD2 . ASP C 184 ? 0.4374 0.5055 0.4326 0.0223  0.0171  0.0622  215 ASP C OD2 
3497 N  N   . ILE C 185 ? 0.2316 0.3726 0.2503 0.0368  0.009   0.0731  216 ILE C N   
3498 C  CA  . ILE C 185 ? 0.2401 0.4035 0.2661 0.0443  0.0098  0.0796  216 ILE C CA  
3499 C  C   . ILE C 185 ? 0.2265 0.4012 0.2577 0.0321  0.0047  0.0749  216 ILE C C   
3500 O  O   . ILE C 185 ? 0.2232 0.4029 0.2574 0.0363  0.0073  0.0743  216 ILE C O   
3501 C  CB  . ILE C 185 ? 0.2477 0.4406 0.2795 0.0509  0.0081  0.0942  216 ILE C CB  
3502 C  CG1 . ILE C 185 ? 0.2849 0.4646 0.3099 0.0652  0.0141  0.1007  216 ILE C CG1 
3503 C  CG2 . ILE C 185 ? 0.2483 0.4717 0.2902 0.0585  0.0093  0.1031  216 ILE C CG2 
3504 C  CD1 . ILE C 185 ? 0.3178 0.47   0.3343 0.0803  0.0244  0.098   216 ILE C CD1 
3505 N  N   . ALA C 186 ? 0.2196 0.3933 0.2486 0.0177  -0.0014 0.0709  217 ALA C N   
3506 C  CA  . ALA C 186 ? 0.2094 0.3867 0.2393 0.0059  -0.0056 0.0666  217 ALA C CA  
3507 C  C   . ALA C 186 ? 0.2138 0.3748 0.2428 0.0076  -0.0021 0.0583  217 ALA C C   
3508 O  O   . ALA C 186 ? 0.2133 0.3789 0.2437 0.0013  -0.0041 0.057   217 ALA C O   
3509 C  CB  . ALA C 186 ? 0.2077 0.3766 0.2294 -0.0071 -0.0105 0.0626  217 ALA C CB  
3510 N  N   . LYS C 187 ? 0.2084 0.3502 0.2338 0.0144  0.0026  0.0531  218 LYS C N   
3511 C  CA  . LYS C 187 ? 0.212  0.3415 0.2356 0.0145  0.0047  0.0456  218 LYS C CA  
3512 C  C   . LYS C 187 ? 0.2385 0.3768 0.2638 0.0219  0.0076  0.0476  218 LYS C C   
3513 O  O   . LYS C 187 ? 0.253  0.3863 0.2765 0.0205  0.008   0.0424  218 LYS C O   
3514 C  CB  . LYS C 187 ? 0.1901 0.2986 0.2079 0.0163  0.0078  0.0399  218 LYS C CB  
3515 C  CG  . LYS C 187 ? 0.2284 0.3299 0.2449 0.01    0.0064  0.0387  218 LYS C CG  
3516 C  CD  . LYS C 187 ? 0.2699 0.3536 0.2816 0.0099  0.0096  0.0351  218 LYS C CD  
3517 C  CE  . LYS C 187 ? 0.2629 0.3436 0.2746 0.0038  0.0092  0.0349  218 LYS C CE  
3518 N  NZ  . LYS C 187 ? 0.2573 0.3231 0.2648 0.0016  0.0122  0.0338  218 LYS C NZ  
3519 N  N   . LYS C 188 ? 0.2354 0.3884 0.2637 0.031   0.0102  0.0559  219 LYS C N   
3520 C  CA  . LYS C 188 ? 0.2334 0.3952 0.262  0.0411  0.0151  0.0587  219 LYS C CA  
3521 C  C   . LYS C 188 ? 0.231  0.4106 0.2657 0.034   0.0122  0.0604  219 LYS C C   
3522 O  O   . LYS C 188 ? 0.2252 0.4151 0.2649 0.022   0.0063  0.0627  219 LYS C O   
3523 C  CB  . LYS C 188 ? 0.2475 0.4248 0.2789 0.0555  0.0199  0.0697  219 LYS C CB  
3524 C  CG  . LYS C 188 ? 0.2601 0.4723 0.3041 0.0509  0.0149  0.0815  219 LYS C CG  
3525 C  CD  . LYS C 188 ? 0.3009 0.5264 0.3471 0.0666  0.0195  0.0931  219 LYS C CD  
3526 C  CE  . LYS C 188 ? 0.3457 0.6112 0.4047 0.0613  0.0134  0.1065  219 LYS C CE  
3527 N  NZ  . LYS C 188 ? 0.3746 0.6738 0.4446 0.0613  0.0138  0.1149  219 LYS C NZ  
3528 N  N   . PRO C 189 ? 0.2338 0.4138 0.2653 0.0408  0.0167  0.0589  220 PRO C N   
3529 C  CA  . PRO C 189 ? 0.2282 0.4248 0.2649 0.034   0.0146  0.0618  220 PRO C CA  
3530 C  C   . PRO C 189 ? 0.2322 0.4612 0.2806 0.031   0.0127  0.0743  220 PRO C C   
3531 O  O   . PRO C 189 ? 0.2202 0.4665 0.2733 0.0419  0.0164  0.0828  220 PRO C O   
3532 C  CB  . PRO C 189 ? 0.2411 0.4332 0.27   0.0451  0.0213  0.0589  220 PRO C CB  
3533 C  CG  . PRO C 189 ? 0.2532 0.4328 0.2739 0.0603  0.0283  0.0583  220 PRO C CG  
3534 C  CD  . PRO C 189 ? 0.2351 0.3977 0.255  0.0542  0.0242  0.0544  220 PRO C CD  
3535 N  N   . LEU C 190 ? 0.2255 0.4626 0.2775 0.0157  0.0069  0.0764  221 LEU C N   
3536 C  CA  . LEU C 190 ? 0.2207 0.4905 0.2829 0.0078  0.0038  0.0886  221 LEU C CA  
3537 C  C   . LEU C 190 ? 0.2336 0.5265 0.3014 0.015   0.0095  0.0963  221 LEU C C   
3538 O  O   . LEU C 190 ? 0.242  0.5204 0.3028 0.0213  0.0139  0.0902  221 LEU C O   
3539 C  CB  . LEU C 190 ? 0.2228 0.4846 0.2813 -0.0132 -0.0039 0.0868  221 LEU C CB  
3540 C  CG  . LEU C 190 ? 0.2466 0.4959 0.2997 -0.0222 -0.0097 0.0833  221 LEU C CG  
3541 C  CD1 . LEU C 190 ? 0.267  0.4938 0.3089 -0.039  -0.0143 0.0777  221 LEU C CD1 
3542 C  CD2 . LEU C 190 ? 0.2399 0.5211 0.3013 -0.0262 -0.0137 0.0945  221 LEU C CD2 
3543 N  N   . PRO C 191 ? 0.2315 0.5633 0.3117 0.0135  0.0093  0.1105  222 PRO C N   
3544 C  CA  . PRO C 191 ? 0.2339 0.591  0.32   0.0203  0.0156  0.1191  222 PRO C CA  
3545 C  C   . PRO C 191 ? 0.2412 0.592  0.324  0.0047  0.0128  0.1176  222 PRO C C   
3546 O  O   . PRO C 191 ? 0.2523 0.5843 0.3296 -0.0131 0.0054  0.1127  222 PRO C O   
3547 C  CB  . PRO C 191 ? 0.2216 0.6275 0.3244 0.0192  0.0145  0.1368  222 PRO C CB  
3548 C  CG  . PRO C 191 ? 0.23   0.6333 0.3335 0.0172  0.009   0.1365  222 PRO C CG  
3549 C  CD  . PRO C 191 ? 0.2265 0.5848 0.3159 0.0051  0.0032  0.1204  222 PRO C CD  
3550 N  N   . LEU C 192 ? 0.2415 0.6069 0.3257 0.0124  0.0195  0.1227  223 LEU C N   
3551 C  CA  . LEU C 192 ? 0.2532 0.6141 0.3338 -0.0012 0.0178  0.1235  223 LEU C CA  
3552 C  C   . LEU C 192 ? 0.2437 0.6473 0.3381 -0.0136 0.0167  0.1407  223 LEU C C   
3553 O  O   . LEU C 192 ? 0.2371 0.679  0.3442 -0.0033 0.0213  0.1525  223 LEU C O   
3554 C  CB  . LEU C 192 ? 0.2619 0.6113 0.333  0.0135  0.0257  0.1182  223 LEU C CB  
3555 C  CG  . LEU C 192 ? 0.2917 0.6091 0.3496 0.0285  0.0288  0.1038  223 LEU C CG  
3556 C  CD1 . LEU C 192 ? 0.2997 0.614  0.3467 0.0415  0.0367  0.1012  223 LEU C CD1 
3557 C  CD2 . LEU C 192 ? 0.31   0.593  0.3599 0.0176  0.0215  0.0921  223 LEU C CD2 
3558 N  N   . THR C 193 ? 0.2461 0.6434 0.3372 -0.0347 0.0116  0.1431  224 THR C N   
3559 C  CA  . THR C 193 ? 0.2369 0.672  0.3389 -0.0492 0.0111  0.1596  224 THR C CA  
3560 C  C   . THR C 193 ? 0.2398 0.661  0.3329 -0.0496 0.0158  0.1592  224 THR C C   
3561 O  O   . THR C 193 ? 0.2471 0.628  0.3256 -0.0556 0.013   0.149   224 THR C O   
3562 C  CB  . THR C 193 ? 0.2673 0.7037 0.3693 -0.0781 0.0002  0.1638  224 THR C CB  
3563 O  OG1 . THR C 193 ? 0.2668 0.7233 0.3778 -0.076  -0.0039 0.1661  224 THR C OG1 
3564 C  CG2 . THR C 193 ? 0.2687 0.7393 0.3791 -0.099  -0.0014 0.1805  224 THR C CG2 
3565 N  N   . VAL C 194 ? 0.238  0.6924 0.3389 -0.0402 0.024   0.1704  225 VAL C N   
3566 C  CA  . VAL C 194 ? 0.2546 0.6988 0.3465 -0.0401 0.0288  0.1715  225 VAL C CA  
3567 C  C   . VAL C 194 ? 0.2538 0.7345 0.3565 -0.0592 0.0285  0.1901  225 VAL C C   
3568 O  O   . VAL C 194 ? 0.2338 0.763  0.3533 -0.055  0.0324  0.2039  225 VAL C O   
3569 C  CB  . VAL C 194 ? 0.2636 0.7107 0.3503 -0.0124 0.0397  0.1674  225 VAL C CB  
3570 C  CG1 . VAL C 194 ? 0.2753 0.7175 0.3524 -0.013  0.0443  0.1705  225 VAL C CG1 
3571 C  CG2 . VAL C 194 ? 0.2779 0.6879 0.3525 0.0025  0.039   0.1492  225 VAL C CG2 
3572 N  N   . VAL C 195 ? 0.2687 0.7269 0.3615 -0.0806 0.0241  0.1917  226 VAL C N   
3573 C  CA  . VAL C 195 ? 0.2764 0.7646 0.3768 -0.103  0.0233  0.2095  226 VAL C CA  
3574 C  C   . VAL C 195 ? 0.3007 0.7907 0.3953 -0.0956 0.0321  0.2155  226 VAL C C   
3575 O  O   . VAL C 195 ? 0.3201 0.7682 0.3971 -0.094  0.0322  0.2068  226 VAL C O   
3576 C  CB  . VAL C 195 ? 0.2886 0.7487 0.3787 -0.1357 0.0127  0.2093  226 VAL C CB  
3577 C  CG1 . VAL C 195 ? 0.2877 0.7749 0.3827 -0.1617 0.0121  0.2281  226 VAL C CG1 
3578 C  CG2 . VAL C 195 ? 0.286  0.7474 0.3802 -0.144  0.0038  0.2039  226 VAL C CG2 
3579 N  N   . LEU C 196 ? 0.3034 0.8434 0.4122 -0.089  0.04    0.231   227 LEU C N   
3580 C  CA  . LEU C 196 ? 0.3322 0.8802 0.4356 -0.0815 0.0494  0.2386  227 LEU C CA  
3581 C  C   . LEU C 196 ? 0.3658 0.9202 0.4692 -0.1118 0.0465  0.2541  227 LEU C C   
3582 O  O   . LEU C 196 ? 0.3432 0.9373 0.4627 -0.1313 0.0434  0.2692  227 LEU C O   
3583 C  CB  . LEU C 196 ? 0.3172 0.9173 0.4344 -0.0582 0.0612  0.249   227 LEU C CB  
3584 C  CG  . LEU C 196 ? 0.3484 0.9465 0.4657 -0.0291 0.0655  0.2369  227 LEU C CG  
3585 C  CD1 . LEU C 196 ? 0.3401 0.9928 0.471  -0.0074 0.0783  0.2509  227 LEU C CD1 
3586 C  CD2 . LEU C 196 ? 0.3813 0.9284 0.4757 -0.0124 0.0668  0.2166  227 LEU C CD2 
3587 N  N   . ASN C 197 ? 0.4121 0.931  0.4973 -0.1156 0.0481  0.2523  228 ASN C N   
3588 C  CA  . ASN C 197 ? 0.4376 0.9533 0.5181 -0.1446 0.0463  0.267   228 ASN C CA  
3589 C  C   . ASN C 197 ? 0.4464 0.9822 0.5249 -0.1356 0.057   0.2793  228 ASN C C   
3590 O  O   . ASN C 197 ? 0.464  0.9758 0.5283 -0.1142 0.062   0.2702  228 ASN C O   
3591 C  CB  . ASN C 197 ? 0.4968 0.9455 0.5536 -0.1589 0.039   0.2558  228 ASN C CB  
3592 C  CG  . ASN C 197 ? 0.5567 0.9799 0.6113 -0.1648 0.0293  0.2414  228 ASN C CG  
3593 O  OD1 . ASN C 197 ? 0.5725 1.0174 0.6375 -0.1849 0.0228  0.2468  228 ASN C OD1 
3594 N  ND2 . ASN C 197 ? 0.5643 0.9441 0.6053 -0.1479 0.0281  0.2236  228 ASN C ND2 
3595 C  CHA . HEM D .   ? 0.2542 0.2761 0.2058 0.0181  0.0045  0.0114  201 HEM A CHA 
3596 C  CHB . HEM D .   ? 0.2487 0.2365 0.2025 0.0152  0.001   0.0181  201 HEM A CHB 
3597 C  CHC . HEM D .   ? 0.2338 0.2355 0.211  0.0194  0.003   0.0011  201 HEM A CHC 
3598 C  CHD . HEM D .   ? 0.215  0.2402 0.1906 0.0186  0.0059  -0.0092 201 HEM A CHD 
3599 C  C1A . HEM D .   ? 0.2569 0.2684 0.2071 0.0168  0.0036  0.0158  201 HEM A C1A 
3600 C  C2A . HEM D .   ? 0.2752 0.2788 0.2167 0.0151  0.0042  0.0228  201 HEM A C2A 
3601 C  C3A . HEM D .   ? 0.2596 0.2521 0.2017 0.014   0.0032  0.0245  201 HEM A C3A 
3602 C  C4A . HEM D .   ? 0.2516 0.247  0.2027 0.0155  0.002   0.0188  201 HEM A C4A 
3603 C  CMA . HEM D .   ? 0.2661 0.2444 0.2002 0.0112  0.0039  0.0306  201 HEM A CMA 
3604 C  CAA . HEM D .   ? 0.302  0.3079 0.2345 0.0143  0.0062  0.0275  201 HEM A CAA 
3605 C  CBA . HEM D .   ? 0.3249 0.3347 0.2597 0.0075  0.0106  0.0295  201 HEM A CBA 
3606 C  CGA . HEM D .   ? 0.3464 0.3558 0.2711 0.0052  0.0138  0.0357  201 HEM A CGA 
3607 O  O1A . HEM D .   ? 0.3474 0.3571 0.2632 0.0097  0.0129  0.0377  201 HEM A O1A 
3608 O  O2A . HEM D .   ? 0.3569 0.3661 0.2828 -0.0021 0.0176  0.0387  201 HEM A O2A 
3609 C  C1B . HEM D .   ? 0.2508 0.2408 0.2117 0.0168  0.0006  0.0135  201 HEM A C1B 
3610 C  C2B . HEM D .   ? 0.2518 0.2338 0.2139 0.0171  -0.0003 0.013   201 HEM A C2B 
3611 C  C3B . HEM D .   ? 0.2529 0.2402 0.2216 0.0187  0.0003  0.0085  201 HEM A C3B 
3612 C  C4B . HEM D .   ? 0.2465 0.2431 0.218  0.0188  0.0015  0.0059  201 HEM A C4B 
3613 C  CMB . HEM D .   ? 0.2538 0.2232 0.2099 0.0153  -0.001  0.0165  201 HEM A CMB 
3614 C  CAB . HEM D .   ? 0.2772 0.2611 0.249  0.0199  0.0004  0.0063  201 HEM A CAB 
3615 C  CBB . HEM D .   ? 0.3063 0.2824 0.2752 0.0219  -0.0012 0.0069  201 HEM A CBB 
3616 C  C1C . HEM D .   ? 0.2296 0.2383 0.2089 0.0189  0.0044  -0.0026 201 HEM A C1C 
3617 C  C2C . HEM D .   ? 0.2207 0.2318 0.2053 0.0183  0.0065  -0.008  201 HEM A C2C 
3618 C  C3C . HEM D .   ? 0.2277 0.2445 0.2119 0.0175  0.0072  -0.0113 201 HEM A C3C 
3619 C  C4C . HEM D .   ? 0.2261 0.245  0.2047 0.0184  0.0057  -0.0075 201 HEM A C4C 
3620 C  CMC . HEM D .   ? 0.2001 0.2077 0.1887 0.018   0.0081  -0.0096 201 HEM A CMC 
3621 C  CAC . HEM D .   ? 0.2322 0.2516 0.2203 0.0155  0.0097  -0.018  201 HEM A CAC 
3622 C  CBC . HEM D .   ? 0.2373 0.2593 0.2305 0.0138  0.0103  -0.0228 201 HEM A CBC 
3623 C  C1D . HEM D .   ? 0.2261 0.2538 0.1953 0.0193  0.0051  -0.005  201 HEM A C1D 
3624 C  C2D . HEM D .   ? 0.2314 0.2666 0.1964 0.0201  0.0054  -0.0072 201 HEM A C2D 
3625 C  C3D . HEM D .   ? 0.2467 0.2821 0.2048 0.0205  0.005   -0.001  201 HEM A C3D 
3626 C  C4D . HEM D .   ? 0.2436 0.2703 0.2018 0.0193  0.0044  0.0045  201 HEM A C4D 
3627 C  CMD . HEM D .   ? 0.2308 0.2713 0.1981 0.0199  0.0065  -0.0153 201 HEM A CMD 
3628 C  CAD . HEM D .   ? 0.2726 0.3151 0.223  0.0218  0.0053  -0.0001 201 HEM A CAD 
3629 C  CBD . HEM D .   ? 0.3066 0.3519 0.2503 0.0257  0.0012  0.0008  201 HEM A CBD 
3630 C  CGD . HEM D .   ? 0.3405 0.3932 0.2747 0.0278  0.0014  0.0018  201 HEM A CGD 
3631 O  O1D . HEM D .   ? 0.3262 0.3859 0.2604 0.0273  0.0033  -0.0028 201 HEM A O1D 
3632 O  O2D . HEM D .   ? 0.3737 0.4239 0.2985 0.031   -0.0006 0.0081  201 HEM A O2D 
3633 N  NA  . HEM D .   ? 0.2582 0.2644 0.2139 0.0169  0.0026  0.014   201 HEM A NA  
3634 N  NB  . HEM D .   ? 0.247  0.2457 0.2137 0.018   0.0014  0.0088  201 HEM A NB  
3635 N  NC  . HEM D .   ? 0.2329 0.2463 0.2087 0.0188  0.0042  -0.0019 201 HEM A NC  
3636 N  ND  . HEM D .   ? 0.2331 0.2559 0.1982 0.019   0.0042  0.0016  201 HEM A ND  
3637 FE FE  . HEM D .   ? 0.2496 0.2606 0.2161 0.0184  0.0028  0.0057  201 HEM A FE  
3644 C  CHA . HEM F .   ? 0.6276 0.3257 0.3681 -0.0282 -0.0361 -0.0377 201 HEM B CHA 
3645 C  CHB . HEM F .   ? 0.5782 0.2925 0.3739 -0.0173 -0.0172 -0.0339 201 HEM B CHB 
3646 C  CHC . HEM F .   ? 0.4943 0.3206 0.3954 0.0006  -0.0159 -0.0201 201 HEM B CHC 
3647 C  CHD . HEM F .   ? 0.5206 0.3347 0.3732 -0.0054 -0.0316 -0.0207 201 HEM B CHD 
3648 C  C1A . HEM F .   ? 0.6294 0.3212 0.3758 -0.0269 -0.031  -0.0385 201 HEM B C1A 
3649 C  C2A . HEM F .   ? 0.6712 0.3213 0.3817 -0.0315 -0.0283 -0.0436 201 HEM B C2A 
3650 C  C3A . HEM F .   ? 0.6483 0.3033 0.3752 -0.0278 -0.0228 -0.0422 201 HEM B C3A 
3651 C  C4A . HEM F .   ? 0.6034 0.3024 0.3748 -0.0216 -0.0223 -0.0366 201 HEM B C4A 
3652 C  CMA . HEM F .   ? 0.6743 0.2926 0.3747 -0.0294 -0.0174 -0.0455 201 HEM B CMA 
3653 C  CAA . HEM F .   ? 0.7283 0.3347 0.3894 -0.0403 -0.0314 -0.0494 201 HEM B CAA 
3654 C  CBA . HEM F .   ? 0.7682 0.3682 0.4253 -0.0673 -0.0479 -0.048  201 HEM B CBA 
3655 C  CGA . HEM F .   ? 0.8408 0.3945 0.4447 -0.0802 -0.0534 -0.0539 201 HEM B CGA 
3656 O  O1A . HEM F .   ? 0.8586 0.4155 0.4568 -0.0968 -0.0677 -0.0522 201 HEM B O1A 
3657 O  O2A . HEM F .   ? 0.8872 0.395  0.4498 -0.0726 -0.042  -0.0605 201 HEM B O2A 
3658 C  C1B . HEM F .   ? 0.547  0.2973 0.3794 -0.0115 -0.0157 -0.0294 201 HEM B C1B 
3659 C  C2B . HEM F .   ? 0.5364 0.2975 0.3879 -0.0074 -0.0097 -0.0271 201 HEM B C2B 
3660 C  C3B . HEM F .   ? 0.5139 0.306  0.394  -0.0024 -0.0093 -0.0237 201 HEM B C3B 
3661 C  C4B . HEM F .   ? 0.5114 0.3124 0.3915 -0.0033 -0.015  -0.0233 201 HEM B C4B 
3662 C  CMB . HEM F .   ? 0.5487 0.2862 0.3856 -0.009  -0.0047 -0.0284 201 HEM B CMB 
3663 C  CAB . HEM F .   ? 0.5113 0.3193 0.4131 0.0019  -0.0037 -0.021  201 HEM B CAB 
3664 C  CBB . HEM F .   ? 0.5026 0.3347 0.4307 0.0019  -0.0036 -0.0175 201 HEM B CBB 
3665 C  C1C . HEM F .   ? 0.4892 0.322  0.3874 0.0007  -0.0202 -0.0192 201 HEM B C1C 
3666 C  C2C . HEM F .   ? 0.4688 0.3238 0.3858 0.0053  -0.0195 -0.0158 201 HEM B C2C 
3667 C  C3C . HEM F .   ? 0.4803 0.3322 0.3843 0.0036  -0.0239 -0.0156 201 HEM B C3C 
3668 C  C4C . HEM F .   ? 0.5024 0.3299 0.379  -0.0018 -0.0273 -0.0194 201 HEM B C4C 
3669 C  CMC . HEM F .   ? 0.4503 0.3223 0.3901 0.01    -0.0142 -0.0134 201 HEM B CMC 
3670 C  CAC . HEM F .   ? 0.481  0.3469 0.392  0.0058  -0.0247 -0.0124 201 HEM B CAC 
3671 C  CBC . HEM F .   ? 0.4767 0.3587 0.404  0.0109  -0.02   -0.0101 201 HEM B CBC 
3672 C  C1D . HEM F .   ? 0.5585 0.3426 0.378  -0.0119 -0.0347 -0.0252 201 HEM B C1D 
3673 C  C2D . HEM F .   ? 0.5869 0.3539 0.3772 -0.0165 -0.0392 -0.0268 201 HEM B C2D 
3674 C  C3D . HEM F .   ? 0.6255 0.3591 0.3829 -0.0228 -0.0404 -0.0321 201 HEM B C3D 
3675 C  C4D . HEM F .   ? 0.6098 0.3413 0.3784 -0.0224 -0.0368 -0.033  201 HEM B C4D 
3676 C  CMD . HEM F .   ? 0.5886 0.3687 0.3812 -0.0156 -0.042  -0.0232 201 HEM B CMD 
3677 C  CAD . HEM F .   ? 0.6735 0.3739 0.3863 -0.0284 -0.0429 -0.0365 201 HEM B CAD 
3678 C  CBD . HEM F .   ? 0.7209 0.4032 0.4078 -0.011  -0.0262 -0.0415 201 HEM B CBD 
3679 C  CGD . HEM F .   ? 0.7783 0.4313 0.4219 -0.0136 -0.0258 -0.0453 201 HEM B CGD 
3680 O  O1D . HEM F .   ? 0.785  0.4482 0.4282 -0.0177 -0.031  -0.0423 201 HEM B O1D 
3681 O  O2D . HEM F .   ? 0.8207 0.433  0.4242 -0.0109 -0.0185 -0.052  201 HEM B O2D 
3682 N  NA  . HEM F .   ? 0.5914 0.3106 0.3732 -0.0211 -0.0272 -0.0346 201 HEM B NA  
3683 N  NB  . HEM F .   ? 0.5287 0.3042 0.3792 -0.009  -0.019  -0.0267 201 HEM B NB  
3684 N  NC  . HEM F .   ? 0.5049 0.3204 0.3784 -0.0038 -0.025  -0.0215 201 HEM B NC  
3685 N  ND  . HEM F .   ? 0.5654 0.3288 0.372  -0.0155 -0.0334 -0.0286 201 HEM B ND  
3686 FE FE  . HEM F .   ? 0.5465 0.3178 0.3776 -0.0122 -0.0266 -0.0278 201 HEM B FE  
# 
