data_9B2E
# 
_entry.id   9B2E 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   9B2E         pdb_00009b2e 10.2210/pdb9b2e/pdb 
WWPDB D_1000282523 ?            ?                   
# 
_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       2025-02-19 
# 
_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                        9B2E 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-15 
_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_contact_author.id                 2 
_pdbx_contact_author.email              cristiano.bizarro@pucrs.br 
_pdbx_contact_author.name_first         Cristiano 
_pdbx_contact_author.name_last          Bizarro 
_pdbx_contact_author.name_mi            V 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2609-8996 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Czeczot, A.M.'     1 ? 
'Silva, E.E.D.'     2 ? 
'Timmers, L.F.S.M.' 3 ? 
'Machado, P.'       4 ? 
'Basso, L.A.'       5 ? 
'Bizarro, C.V.'     6 ? 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'J Enzyme Inhib Med Chem' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1475-6374 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            39 
_citation.language                  ? 
_citation.page_first                2388207 
_citation.page_last                 2388207 
_citation.title                     
;Crystal structure of dihydroneopterin aldolase from Mycobacterium tuberculosis associated with 8-mercaptoguanine, and development of novel S8-functionalized analogues as inhibitors: Synthesis, enzyme inhibition, in vitro toxicity and antitubercular activity.
;
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1080/14756366.2024.2388207 
_citation.pdbx_database_id_PubMed   39140692 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Czeczot, A.M.'         1  ? 
primary 'Muniz, M.N.'           2  ? 
primary 'Perello, M.A.'         3  ? 
primary 'Silva, E.E.D.'         4  ? 
primary 'Timmers, L.F.S.M.'     5  ? 
primary 'Berger, A.'            6  ? 
primary 'Gonzalez, L.C.'        7  ? 
primary 'Arrache Goncalves, G.' 8  ? 
primary 'Moura, S.'             9  ? 
primary 'Machado, P.'           10 ? 
primary 'Bizarro, C.V.'         11 ? 
primary 'Basso, L.A.'           12 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man '7,8-dihydroneopterin aldolase'               13466.166 2   4.1.2.25 ? ? ? 
2 non-polymer syn 2-amino-8-sulfanyl-1,9-dihydro-6H-purin-6-one 183.191   2   ?        ? ? ? 
3 water       nat water                                         18.015    282 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MADRIELRGLTVHGRHGVYDHERVAGQRFVIDVTVWIDLAEAANSDDLADTYDYVRLASRAAEIVAGPPRKLIETVGAEI
ADHVMDDQRVHAVEVAVHKPQAPIPQTFDDVAVVIRRSRRG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MADRIELRGLTVHGRHGVYDHERVAGQRFVIDVTVWIDLAEAANSDDLADTYDYVRLASRAAEIVAGPPRKLIETVGAEI
ADHVMDDQRVHAVEVAVHKPQAPIPQTFDDVAVVIRRSRRG
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 2-amino-8-sulfanyl-1,9-dihydro-6H-purin-6-one B55 
3 water                                         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   ASP n 
1 4   ARG n 
1 5   ILE n 
1 6   GLU n 
1 7   LEU n 
1 8   ARG n 
1 9   GLY n 
1 10  LEU n 
1 11  THR n 
1 12  VAL n 
1 13  HIS n 
1 14  GLY n 
1 15  ARG n 
1 16  HIS n 
1 17  GLY n 
1 18  VAL n 
1 19  TYR n 
1 20  ASP n 
1 21  HIS n 
1 22  GLU n 
1 23  ARG n 
1 24  VAL n 
1 25  ALA n 
1 26  GLY n 
1 27  GLN n 
1 28  ARG n 
1 29  PHE n 
1 30  VAL n 
1 31  ILE n 
1 32  ASP n 
1 33  VAL n 
1 34  THR n 
1 35  VAL n 
1 36  TRP n 
1 37  ILE n 
1 38  ASP n 
1 39  LEU n 
1 40  ALA n 
1 41  GLU n 
1 42  ALA n 
1 43  ALA n 
1 44  ASN n 
1 45  SER n 
1 46  ASP n 
1 47  ASP n 
1 48  LEU n 
1 49  ALA n 
1 50  ASP n 
1 51  THR n 
1 52  TYR n 
1 53  ASP n 
1 54  TYR n 
1 55  VAL n 
1 56  ARG n 
1 57  LEU n 
1 58  ALA n 
1 59  SER n 
1 60  ARG n 
1 61  ALA n 
1 62  ALA n 
1 63  GLU n 
1 64  ILE n 
1 65  VAL n 
1 66  ALA n 
1 67  GLY n 
1 68  PRO n 
1 69  PRO n 
1 70  ARG n 
1 71  LYS n 
1 72  LEU n 
1 73  ILE n 
1 74  GLU n 
1 75  THR n 
1 76  VAL n 
1 77  GLY n 
1 78  ALA n 
1 79  GLU n 
1 80  ILE n 
1 81  ALA n 
1 82  ASP n 
1 83  HIS n 
1 84  VAL n 
1 85  MET n 
1 86  ASP n 
1 87  ASP n 
1 88  GLN n 
1 89  ARG n 
1 90  VAL n 
1 91  HIS n 
1 92  ALA n 
1 93  VAL n 
1 94  GLU n 
1 95  VAL n 
1 96  ALA n 
1 97  VAL n 
1 98  HIS n 
1 99  LYS n 
1 100 PRO n 
1 101 GLN n 
1 102 ALA n 
1 103 PRO n 
1 104 ILE n 
1 105 PRO n 
1 106 GLN n 
1 107 THR n 
1 108 PHE n 
1 109 ASP n 
1 110 ASP n 
1 111 VAL n 
1 112 ALA n 
1 113 VAL n 
1 114 VAL n 
1 115 ILE n 
1 116 ARG n 
1 117 ARG n 
1 118 SER n 
1 119 ARG n 
1 120 ARG n 
1 121 GLY n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   121 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 
;folB, A4S10_03776, DSI28_17580, DSI46_08595, ERS007661_01319, ERS007679_04035, ERS007681_03220, ERS027646_01565, ERS027659_03938, ERS027661_02230, ERS053720_02853, GJE03_18950, SAMEA2683035_00705
;
_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      'Mycobacterium tuberculosis' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     1773 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                       ?                                       'C3 H7 N O2'     
89.093  
ARG 'L-peptide linking' y ARGININE                                      ?                                       'C6 H15 N4 O2 1' 
175.209 
ASN 'L-peptide linking' y ASPARAGINE                                    ?                                       'C4 H8 N2 O3'    
132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                               ?                                       'C4 H7 N O4'     
133.103 
B55 non-polymer         . 2-amino-8-sulfanyl-1,9-dihydro-6H-purin-6-one '2-amino-8-mercapto-1H-purin-6(9H)-one' 'C5 H5 N5 O S'   
183.191 
GLN 'L-peptide linking' y GLUTAMINE                                     ?                                       'C5 H10 N2 O3'   
146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                               ?                                       'C5 H9 N O4'     
147.129 
GLY 'peptide linking'   y GLYCINE                                       ?                                       'C2 H5 N O2'     
75.067  
HIS 'L-peptide linking' y HISTIDINE                                     ?                                       'C6 H10 N3 O2 1' 
156.162 
HOH non-polymer         . WATER                                         ?                                       'H2 O'           
18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                    ?                                       'C6 H13 N O2'    
131.173 
LEU 'L-peptide linking' y LEUCINE                                       ?                                       'C6 H13 N O2'    
131.173 
LYS 'L-peptide linking' y LYSINE                                        ?                                       'C6 H15 N2 O2 1' 
147.195 
MET 'L-peptide linking' y METHIONINE                                    ?                                       'C5 H11 N O2 S'  
149.211 
PHE 'L-peptide linking' y PHENYLALANINE                                 ?                                       'C9 H11 N O2'    
165.189 
PRO 'L-peptide linking' y PROLINE                                       ?                                       'C5 H9 N O2'     
115.130 
SER 'L-peptide linking' y SERINE                                        ?                                       'C3 H7 N O3'     
105.093 
THR 'L-peptide linking' y THREONINE                                     ?                                       'C4 H9 N O3'     
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                    ?                                       'C11 H12 N2 O2'  
204.225 
TYR 'L-peptide linking' y TYROSINE                                      ?                                       'C9 H11 N O3'    
181.189 
VAL 'L-peptide linking' y VALINE                                        ?                                       'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   ASP 3   3   3   ASP ASP A . n 
A 1 4   ARG 4   4   4   ARG ARG A . n 
A 1 5   ILE 5   5   5   ILE ILE A . n 
A 1 6   GLU 6   6   6   GLU GLU A . n 
A 1 7   LEU 7   7   7   LEU LEU A . n 
A 1 8   ARG 8   8   8   ARG ARG A . n 
A 1 9   GLY 9   9   9   GLY GLY A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  THR 11  11  11  THR THR A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  HIS 13  13  13  HIS HIS A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  ARG 15  15  15  ARG ARG A . n 
A 1 16  HIS 16  16  16  HIS HIS A . n 
A 1 17  GLY 17  17  17  GLY GLY A . n 
A 1 18  VAL 18  18  18  VAL VAL A . n 
A 1 19  TYR 19  19  19  TYR TYR A . n 
A 1 20  ASP 20  20  20  ASP ASP A . n 
A 1 21  HIS 21  21  21  HIS HIS A . n 
A 1 22  GLU 22  22  22  GLU GLU A . n 
A 1 23  ARG 23  23  23  ARG ARG A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  ALA 25  25  25  ALA ALA A . n 
A 1 26  GLY 26  26  26  GLY GLY A . n 
A 1 27  GLN 27  27  27  GLN GLN A . n 
A 1 28  ARG 28  28  28  ARG ARG A . n 
A 1 29  PHE 29  29  29  PHE PHE A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  ILE 31  31  31  ILE ILE A . n 
A 1 32  ASP 32  32  32  ASP ASP A . n 
A 1 33  VAL 33  33  33  VAL VAL A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  TRP 36  36  36  TRP TRP A . n 
A 1 37  ILE 37  37  37  ILE ILE A . n 
A 1 38  ASP 38  38  38  ASP ASP A . n 
A 1 39  LEU 39  39  39  LEU LEU A . n 
A 1 40  ALA 40  40  40  ALA ALA A . n 
A 1 41  GLU 41  41  41  GLU GLU A . n 
A 1 42  ALA 42  42  42  ALA ALA A . n 
A 1 43  ALA 43  43  43  ALA ALA A . n 
A 1 44  ASN 44  44  44  ASN ASN A . n 
A 1 45  SER 45  45  45  SER SER A . n 
A 1 46  ASP 46  46  46  ASP ASP 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  ALA 49  49  49  ALA ALA A . n 
A 1 50  ASP 50  50  50  ASP ASP A . n 
A 1 51  THR 51  51  51  THR THR A . n 
A 1 52  TYR 52  52  52  TYR TYR A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  TYR 54  54  54  TYR TYR A . n 
A 1 55  VAL 55  55  55  VAL VAL A . n 
A 1 56  ARG 56  56  56  ARG ARG A . n 
A 1 57  LEU 57  57  57  LEU LEU A . n 
A 1 58  ALA 58  58  58  ALA ALA A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ARG 60  60  60  ARG ARG A . n 
A 1 61  ALA 61  61  61  ALA ALA A . n 
A 1 62  ALA 62  62  62  ALA ALA A . n 
A 1 63  GLU 63  63  63  GLU GLU A . n 
A 1 64  ILE 64  64  64  ILE ILE A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  ALA 66  66  66  ALA ALA A . n 
A 1 67  GLY 67  67  67  GLY GLY A . n 
A 1 68  PRO 68  68  68  PRO PRO A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  ARG 70  70  70  ARG ARG A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  LEU 72  72  72  LEU LEU A . n 
A 1 73  ILE 73  73  73  ILE ILE A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  THR 75  75  75  THR THR A . n 
A 1 76  VAL 76  76  76  VAL VAL A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ALA 78  78  78  ALA ALA A . n 
A 1 79  GLU 79  79  79  GLU GLU A . n 
A 1 80  ILE 80  80  80  ILE ILE A . n 
A 1 81  ALA 81  81  81  ALA ALA A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  HIS 83  83  83  HIS HIS A . n 
A 1 84  VAL 84  84  84  VAL VAL A . n 
A 1 85  MET 85  85  85  MET MET A . n 
A 1 86  ASP 86  86  86  ASP ASP A . n 
A 1 87  ASP 87  87  87  ASP ASP A . n 
A 1 88  GLN 88  88  88  GLN GLN A . n 
A 1 89  ARG 89  89  89  ARG ARG A . n 
A 1 90  VAL 90  90  90  VAL VAL A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  ALA 96  96  96  ALA ALA A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  HIS 98  98  98  HIS HIS A . n 
A 1 99  LYS 99  99  99  LYS LYS A . n 
A 1 100 PRO 100 100 100 PRO PRO A . n 
A 1 101 GLN 101 101 101 GLN GLN A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 PRO 103 103 103 PRO PRO A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 PRO 105 105 105 PRO PRO A . n 
A 1 106 GLN 106 106 106 GLN GLN A . n 
A 1 107 THR 107 107 107 THR THR A . n 
A 1 108 PHE 108 108 108 PHE PHE A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 ASP 110 110 110 ASP ASP A . n 
A 1 111 VAL 111 111 111 VAL VAL A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 VAL 113 113 113 VAL VAL A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ILE 115 115 115 ILE ILE A . n 
A 1 116 ARG 116 116 116 ARG ARG A . n 
A 1 117 ARG 117 117 117 ARG ARG A . n 
A 1 118 SER 118 118 118 SER SER A . n 
A 1 119 ARG 119 119 119 ARG ARG A . n 
A 1 120 ARG 120 120 ?   ?   ?   A . n 
A 1 121 GLY 121 121 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   ARG 4   4   4   ARG ARG B . n 
B 1 5   ILE 5   5   5   ILE ILE B . n 
B 1 6   GLU 6   6   6   GLU GLU B . n 
B 1 7   LEU 7   7   7   LEU LEU B . n 
B 1 8   ARG 8   8   8   ARG ARG B . n 
B 1 9   GLY 9   9   9   GLY GLY B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  THR 11  11  11  THR THR B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  HIS 13  13  13  HIS HIS B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  ARG 15  15  15  ARG ARG B . n 
B 1 16  HIS 16  16  16  HIS HIS B . n 
B 1 17  GLY 17  17  17  GLY GLY B . n 
B 1 18  VAL 18  18  18  VAL VAL B . n 
B 1 19  TYR 19  19  19  TYR TYR B . n 
B 1 20  ASP 20  20  20  ASP ASP B . n 
B 1 21  HIS 21  21  21  HIS HIS B . n 
B 1 22  GLU 22  22  22  GLU GLU B . n 
B 1 23  ARG 23  23  23  ARG ARG B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  ALA 25  25  25  ALA ALA B . n 
B 1 26  GLY 26  26  26  GLY GLY B . n 
B 1 27  GLN 27  27  27  GLN GLN B . n 
B 1 28  ARG 28  28  28  ARG ARG B . n 
B 1 29  PHE 29  29  29  PHE PHE B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  ILE 31  31  31  ILE ILE B . n 
B 1 32  ASP 32  32  32  ASP ASP B . n 
B 1 33  VAL 33  33  33  VAL VAL B . n 
B 1 34  THR 34  34  34  THR THR B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  TRP 36  36  36  TRP TRP B . n 
B 1 37  ILE 37  37  37  ILE ILE B . n 
B 1 38  ASP 38  38  38  ASP ASP B . n 
B 1 39  LEU 39  39  39  LEU LEU B . n 
B 1 40  ALA 40  40  40  ALA ALA B . n 
B 1 41  GLU 41  41  41  GLU GLU B . n 
B 1 42  ALA 42  42  42  ALA ALA B . n 
B 1 43  ALA 43  43  43  ALA ALA B . n 
B 1 44  ASN 44  44  44  ASN ASN B . n 
B 1 45  SER 45  45  45  SER SER B . n 
B 1 46  ASP 46  46  46  ASP ASP B . n 
B 1 47  ASP 47  47  47  ASP ASP B . n 
B 1 48  LEU 48  48  48  LEU LEU B . n 
B 1 49  ALA 49  49  49  ALA ALA B . n 
B 1 50  ASP 50  50  50  ASP ASP B . n 
B 1 51  THR 51  51  51  THR THR B . n 
B 1 52  TYR 52  52  52  TYR TYR B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  TYR 54  54  54  TYR TYR B . n 
B 1 55  VAL 55  55  55  VAL VAL B . n 
B 1 56  ARG 56  56  56  ARG ARG B . n 
B 1 57  LEU 57  57  57  LEU LEU B . n 
B 1 58  ALA 58  58  58  ALA ALA B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ARG 60  60  60  ARG ARG B . n 
B 1 61  ALA 61  61  61  ALA ALA B . n 
B 1 62  ALA 62  62  62  ALA ALA B . n 
B 1 63  GLU 63  63  63  GLU GLU B . n 
B 1 64  ILE 64  64  64  ILE ILE B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  ALA 66  66  66  ALA ALA B . n 
B 1 67  GLY 67  67  67  GLY GLY B . n 
B 1 68  PRO 68  68  68  PRO PRO B . n 
B 1 69  PRO 69  69  69  PRO PRO B . n 
B 1 70  ARG 70  70  70  ARG ARG B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  LEU 72  72  72  LEU LEU B . n 
B 1 73  ILE 73  73  73  ILE ILE B . n 
B 1 74  GLU 74  74  74  GLU GLU B . n 
B 1 75  THR 75  75  75  THR THR B . n 
B 1 76  VAL 76  76  76  VAL VAL B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  ALA 78  78  78  ALA ALA B . n 
B 1 79  GLU 79  79  79  GLU GLU B . n 
B 1 80  ILE 80  80  80  ILE ILE B . n 
B 1 81  ALA 81  81  81  ALA ALA B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  HIS 83  83  83  HIS HIS B . n 
B 1 84  VAL 84  84  84  VAL VAL B . n 
B 1 85  MET 85  85  85  MET MET B . n 
B 1 86  ASP 86  86  86  ASP ASP B . n 
B 1 87  ASP 87  87  87  ASP ASP B . n 
B 1 88  GLN 88  88  88  GLN GLN B . n 
B 1 89  ARG 89  89  89  ARG ARG B . n 
B 1 90  VAL 90  90  90  VAL VAL B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  GLU 94  94  94  GLU GLU B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  ALA 96  96  96  ALA ALA B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  HIS 98  98  98  HIS HIS B . n 
B 1 99  LYS 99  99  99  LYS LYS B . n 
B 1 100 PRO 100 100 100 PRO PRO B . n 
B 1 101 GLN 101 101 101 GLN GLN B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 PRO 103 103 103 PRO PRO B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 PRO 105 105 105 PRO PRO B . n 
B 1 106 GLN 106 106 106 GLN GLN B . n 
B 1 107 THR 107 107 107 THR THR B . n 
B 1 108 PHE 108 108 108 PHE PHE B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 ASP 110 110 110 ASP ASP B . n 
B 1 111 VAL 111 111 111 VAL VAL B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 VAL 113 113 113 VAL VAL B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 ILE 115 115 115 ILE ILE B . n 
B 1 116 ARG 116 116 116 ARG ARG B . n 
B 1 117 ARG 117 117 117 ARG ARG B . n 
B 1 118 SER 118 118 118 SER SER B . n 
B 1 119 ARG 119 119 119 ARG ARG B . n 
B 1 120 ARG 120 120 ?   ?   ?   B . n 
B 1 121 GLY 121 121 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        B55 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   B55 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 B55 1   201 201 B55 8MG A . 
D 2 B55 1   201 201 B55 8MG B . 
E 3 HOH 1   301 185 HOH HOH A . 
E 3 HOH 2   302 68  HOH HOH A . 
E 3 HOH 3   303 20  HOH HOH A . 
E 3 HOH 4   304 141 HOH HOH A . 
E 3 HOH 5   305 44  HOH HOH A . 
E 3 HOH 6   306 234 HOH HOH A . 
E 3 HOH 7   307 86  HOH HOH A . 
E 3 HOH 8   308 147 HOH HOH A . 
E 3 HOH 9   309 39  HOH HOH A . 
E 3 HOH 10  310 110 HOH HOH A . 
E 3 HOH 11  311 243 HOH HOH A . 
E 3 HOH 12  312 92  HOH HOH A . 
E 3 HOH 13  313 7   HOH HOH A . 
E 3 HOH 14  314 146 HOH HOH A . 
E 3 HOH 15  315 201 HOH HOH A . 
E 3 HOH 16  316 42  HOH HOH A . 
E 3 HOH 17  317 55  HOH HOH A . 
E 3 HOH 18  318 19  HOH HOH A . 
E 3 HOH 19  319 29  HOH HOH A . 
E 3 HOH 20  320 89  HOH HOH A . 
E 3 HOH 21  321 239 HOH HOH A . 
E 3 HOH 22  322 143 HOH HOH A . 
E 3 HOH 23  323 214 HOH HOH A . 
E 3 HOH 24  324 117 HOH HOH A . 
E 3 HOH 25  325 11  HOH HOH A . 
E 3 HOH 26  326 165 HOH HOH A . 
E 3 HOH 27  327 77  HOH HOH A . 
E 3 HOH 28  328 238 HOH HOH A . 
E 3 HOH 29  329 112 HOH HOH A . 
E 3 HOH 30  330 241 HOH HOH A . 
E 3 HOH 31  331 18  HOH HOH A . 
E 3 HOH 32  332 102 HOH HOH A . 
E 3 HOH 33  333 34  HOH HOH A . 
E 3 HOH 34  334 135 HOH HOH A . 
E 3 HOH 35  335 10  HOH HOH A . 
E 3 HOH 36  336 82  HOH HOH A . 
E 3 HOH 37  337 136 HOH HOH A . 
E 3 HOH 38  338 9   HOH HOH A . 
E 3 HOH 39  339 64  HOH HOH A . 
E 3 HOH 40  340 176 HOH HOH A . 
E 3 HOH 41  341 13  HOH HOH A . 
E 3 HOH 42  342 125 HOH HOH A . 
E 3 HOH 43  343 132 HOH HOH A . 
E 3 HOH 44  344 137 HOH HOH A . 
E 3 HOH 45  345 271 HOH HOH A . 
E 3 HOH 46  346 208 HOH HOH A . 
E 3 HOH 47  347 49  HOH HOH A . 
E 3 HOH 48  348 61  HOH HOH A . 
E 3 HOH 49  349 73  HOH HOH A . 
E 3 HOH 50  350 70  HOH HOH A . 
E 3 HOH 51  351 14  HOH HOH A . 
E 3 HOH 52  352 53  HOH HOH A . 
E 3 HOH 53  353 57  HOH HOH A . 
E 3 HOH 54  354 159 HOH HOH A . 
E 3 HOH 55  355 67  HOH HOH A . 
E 3 HOH 56  356 221 HOH HOH A . 
E 3 HOH 57  357 254 HOH HOH A . 
E 3 HOH 58  358 226 HOH HOH A . 
E 3 HOH 59  359 27  HOH HOH A . 
E 3 HOH 60  360 123 HOH HOH A . 
E 3 HOH 61  361 229 HOH HOH A . 
E 3 HOH 62  362 40  HOH HOH A . 
E 3 HOH 63  363 45  HOH HOH A . 
E 3 HOH 64  364 31  HOH HOH A . 
E 3 HOH 65  365 63  HOH HOH A . 
E 3 HOH 66  366 114 HOH HOH A . 
E 3 HOH 67  367 2   HOH HOH A . 
E 3 HOH 68  368 104 HOH HOH A . 
E 3 HOH 69  369 116 HOH HOH A . 
E 3 HOH 70  370 81  HOH HOH A . 
E 3 HOH 71  371 93  HOH HOH A . 
E 3 HOH 72  372 121 HOH HOH A . 
E 3 HOH 73  373 119 HOH HOH A . 
E 3 HOH 74  374 218 HOH HOH A . 
E 3 HOH 75  375 222 HOH HOH A . 
E 3 HOH 76  376 169 HOH HOH A . 
E 3 HOH 77  377 202 HOH HOH A . 
E 3 HOH 78  378 97  HOH HOH A . 
E 3 HOH 79  379 246 HOH HOH A . 
E 3 HOH 80  380 181 HOH HOH A . 
E 3 HOH 81  381 192 HOH HOH A . 
E 3 HOH 82  382 252 HOH HOH A . 
E 3 HOH 83  383 225 HOH HOH A . 
E 3 HOH 84  384 253 HOH HOH A . 
E 3 HOH 85  385 90  HOH HOH A . 
E 3 HOH 86  386 41  HOH HOH A . 
E 3 HOH 87  387 228 HOH HOH A . 
E 3 HOH 88  388 152 HOH HOH A . 
E 3 HOH 89  389 256 HOH HOH A . 
E 3 HOH 90  390 187 HOH HOH A . 
E 3 HOH 91  391 273 HOH HOH A . 
E 3 HOH 92  392 183 HOH HOH A . 
E 3 HOH 93  393 155 HOH HOH A . 
E 3 HOH 94  394 3   HOH HOH A . 
E 3 HOH 95  395 134 HOH HOH A . 
E 3 HOH 96  396 6   HOH HOH A . 
E 3 HOH 97  397 160 HOH HOH A . 
E 3 HOH 98  398 217 HOH HOH A . 
E 3 HOH 99  399 182 HOH HOH A . 
E 3 HOH 100 400 244 HOH HOH A . 
E 3 HOH 101 401 191 HOH HOH A . 
E 3 HOH 102 402 269 HOH HOH A . 
E 3 HOH 103 403 251 HOH HOH A . 
E 3 HOH 104 404 174 HOH HOH A . 
E 3 HOH 105 405 280 HOH HOH A . 
E 3 HOH 106 406 205 HOH HOH A . 
E 3 HOH 107 407 28  HOH HOH A . 
E 3 HOH 108 408 140 HOH HOH A . 
E 3 HOH 109 409 203 HOH HOH A . 
E 3 HOH 110 410 98  HOH HOH A . 
E 3 HOH 111 411 145 HOH HOH A . 
E 3 HOH 112 412 242 HOH HOH A . 
E 3 HOH 113 413 83  HOH HOH A . 
E 3 HOH 114 414 78  HOH HOH A . 
E 3 HOH 115 415 247 HOH HOH A . 
E 3 HOH 116 416 236 HOH HOH A . 
E 3 HOH 117 417 120 HOH HOH A . 
E 3 HOH 118 418 139 HOH HOH A . 
E 3 HOH 119 419 215 HOH HOH A . 
E 3 HOH 120 420 186 HOH HOH A . 
E 3 HOH 121 421 209 HOH HOH A . 
E 3 HOH 122 422 130 HOH HOH A . 
E 3 HOH 123 423 164 HOH HOH A . 
E 3 HOH 124 424 157 HOH HOH A . 
E 3 HOH 125 425 240 HOH HOH A . 
E 3 HOH 126 426 166 HOH HOH A . 
E 3 HOH 127 427 118 HOH HOH A . 
E 3 HOH 128 428 100 HOH HOH A . 
E 3 HOH 129 429 178 HOH HOH A . 
E 3 HOH 130 430 219 HOH HOH A . 
E 3 HOH 131 431 268 HOH HOH A . 
E 3 HOH 132 432 171 HOH HOH A . 
E 3 HOH 133 433 266 HOH HOH A . 
E 3 HOH 134 434 281 HOH HOH A . 
E 3 HOH 135 435 276 HOH HOH A . 
F 3 HOH 1   301 257 HOH HOH B . 
F 3 HOH 2   302 259 HOH HOH B . 
F 3 HOH 3   303 270 HOH HOH B . 
F 3 HOH 4   304 122 HOH HOH B . 
F 3 HOH 5   305 282 HOH HOH B . 
F 3 HOH 6   306 262 HOH HOH B . 
F 3 HOH 7   307 261 HOH HOH B . 
F 3 HOH 8   308 33  HOH HOH B . 
F 3 HOH 9   309 263 HOH HOH B . 
F 3 HOH 10  310 25  HOH HOH B . 
F 3 HOH 11  311 107 HOH HOH B . 
F 3 HOH 12  312 154 HOH HOH B . 
F 3 HOH 13  313 235 HOH HOH B . 
F 3 HOH 14  314 56  HOH HOH B . 
F 3 HOH 15  315 60  HOH HOH B . 
F 3 HOH 16  316 66  HOH HOH B . 
F 3 HOH 17  317 74  HOH HOH B . 
F 3 HOH 18  318 38  HOH HOH B . 
F 3 HOH 19  319 101 HOH HOH B . 
F 3 HOH 20  320 198 HOH HOH B . 
F 3 HOH 21  321 22  HOH HOH B . 
F 3 HOH 22  322 80  HOH HOH B . 
F 3 HOH 23  323 50  HOH HOH B . 
F 3 HOH 24  324 15  HOH HOH B . 
F 3 HOH 25  325 88  HOH HOH B . 
F 3 HOH 26  326 23  HOH HOH B . 
F 3 HOH 27  327 21  HOH HOH B . 
F 3 HOH 28  328 204 HOH HOH B . 
F 3 HOH 29  329 26  HOH HOH B . 
F 3 HOH 30  330 24  HOH HOH B . 
F 3 HOH 31  331 211 HOH HOH B . 
F 3 HOH 32  332 94  HOH HOH B . 
F 3 HOH 33  333 184 HOH HOH B . 
F 3 HOH 34  334 30  HOH HOH B . 
F 3 HOH 35  335 5   HOH HOH B . 
F 3 HOH 36  336 4   HOH HOH B . 
F 3 HOH 37  337 72  HOH HOH B . 
F 3 HOH 38  338 113 HOH HOH B . 
F 3 HOH 39  339 148 HOH HOH B . 
F 3 HOH 40  340 277 HOH HOH B . 
F 3 HOH 41  341 79  HOH HOH B . 
F 3 HOH 42  342 54  HOH HOH B . 
F 3 HOH 43  343 213 HOH HOH B . 
F 3 HOH 44  344 96  HOH HOH B . 
F 3 HOH 45  345 46  HOH HOH B . 
F 3 HOH 46  346 126 HOH HOH B . 
F 3 HOH 47  347 105 HOH HOH B . 
F 3 HOH 48  348 95  HOH HOH B . 
F 3 HOH 49  349 87  HOH HOH B . 
F 3 HOH 50  350 129 HOH HOH B . 
F 3 HOH 51  351 58  HOH HOH B . 
F 3 HOH 52  352 103 HOH HOH B . 
F 3 HOH 53  353 1   HOH HOH B . 
F 3 HOH 54  354 127 HOH HOH B . 
F 3 HOH 55  355 180 HOH HOH B . 
F 3 HOH 56  356 35  HOH HOH B . 
F 3 HOH 57  357 158 HOH HOH B . 
F 3 HOH 58  358 128 HOH HOH B . 
F 3 HOH 59  359 245 HOH HOH B . 
F 3 HOH 60  360 144 HOH HOH B . 
F 3 HOH 61  361 51  HOH HOH B . 
F 3 HOH 62  362 220 HOH HOH B . 
F 3 HOH 63  363 195 HOH HOH B . 
F 3 HOH 64  364 43  HOH HOH B . 
F 3 HOH 65  365 48  HOH HOH B . 
F 3 HOH 66  366 230 HOH HOH B . 
F 3 HOH 67  367 71  HOH HOH B . 
F 3 HOH 68  368 212 HOH HOH B . 
F 3 HOH 69  369 16  HOH HOH B . 
F 3 HOH 70  370 161 HOH HOH B . 
F 3 HOH 71  371 250 HOH HOH B . 
F 3 HOH 72  372 47  HOH HOH B . 
F 3 HOH 73  373 167 HOH HOH B . 
F 3 HOH 74  374 177 HOH HOH B . 
F 3 HOH 75  375 76  HOH HOH B . 
F 3 HOH 76  376 36  HOH HOH B . 
F 3 HOH 77  377 275 HOH HOH B . 
F 3 HOH 78  378 115 HOH HOH B . 
F 3 HOH 79  379 99  HOH HOH B . 
F 3 HOH 80  380 199 HOH HOH B . 
F 3 HOH 81  381 37  HOH HOH B . 
F 3 HOH 82  382 175 HOH HOH B . 
F 3 HOH 83  383 206 HOH HOH B . 
F 3 HOH 84  384 163 HOH HOH B . 
F 3 HOH 85  385 52  HOH HOH B . 
F 3 HOH 86  386 138 HOH HOH B . 
F 3 HOH 87  387 142 HOH HOH B . 
F 3 HOH 88  388 153 HOH HOH B . 
F 3 HOH 89  389 216 HOH HOH B . 
F 3 HOH 90  390 149 HOH HOH B . 
F 3 HOH 91  391 227 HOH HOH B . 
F 3 HOH 92  392 12  HOH HOH B . 
F 3 HOH 93  393 179 HOH HOH B . 
F 3 HOH 94  394 264 HOH HOH B . 
F 3 HOH 95  395 274 HOH HOH B . 
F 3 HOH 96  396 91  HOH HOH B . 
F 3 HOH 97  397 32  HOH HOH B . 
F 3 HOH 98  398 189 HOH HOH B . 
F 3 HOH 99  399 108 HOH HOH B . 
F 3 HOH 100 400 223 HOH HOH B . 
F 3 HOH 101 401 150 HOH HOH B . 
F 3 HOH 102 402 133 HOH HOH B . 
F 3 HOH 103 403 170 HOH HOH B . 
F 3 HOH 104 404 196 HOH HOH B . 
F 3 HOH 105 405 248 HOH HOH B . 
F 3 HOH 106 406 75  HOH HOH B . 
F 3 HOH 107 407 8   HOH HOH B . 
F 3 HOH 108 408 65  HOH HOH B . 
F 3 HOH 109 409 231 HOH HOH B . 
F 3 HOH 110 410 255 HOH HOH B . 
F 3 HOH 111 411 279 HOH HOH B . 
F 3 HOH 112 412 197 HOH HOH B . 
F 3 HOH 113 413 111 HOH HOH B . 
F 3 HOH 114 414 188 HOH HOH B . 
F 3 HOH 115 415 172 HOH HOH B . 
F 3 HOH 116 416 210 HOH HOH B . 
F 3 HOH 117 417 265 HOH HOH B . 
F 3 HOH 118 418 62  HOH HOH B . 
F 3 HOH 119 419 233 HOH HOH B . 
F 3 HOH 120 420 106 HOH HOH B . 
F 3 HOH 121 421 17  HOH HOH B . 
F 3 HOH 122 422 267 HOH HOH B . 
F 3 HOH 123 423 278 HOH HOH B . 
F 3 HOH 124 424 151 HOH HOH B . 
F 3 HOH 125 425 124 HOH HOH B . 
F 3 HOH 126 426 194 HOH HOH B . 
F 3 HOH 127 427 193 HOH HOH B . 
F 3 HOH 128 428 207 HOH HOH B . 
F 3 HOH 129 429 84  HOH HOH B . 
F 3 HOH 130 430 59  HOH HOH B . 
F 3 HOH 131 431 237 HOH HOH B . 
F 3 HOH 132 432 232 HOH HOH B . 
F 3 HOH 133 433 272 HOH HOH B . 
F 3 HOH 134 434 131 HOH HOH B . 
F 3 HOH 135 435 258 HOH HOH B . 
F 3 HOH 136 436 190 HOH HOH B . 
F 3 HOH 137 437 109 HOH HOH B . 
F 3 HOH 138 438 173 HOH HOH B . 
F 3 HOH 139 439 156 HOH HOH B . 
F 3 HOH 140 440 168 HOH HOH B . 
F 3 HOH 141 441 69  HOH HOH B . 
F 3 HOH 142 442 162 HOH HOH B . 
F 3 HOH 143 443 85  HOH HOH B . 
F 3 HOH 144 444 260 HOH HOH B . 
F 3 HOH 145 445 200 HOH HOH B . 
F 3 HOH 146 446 249 HOH HOH B . 
F 3 HOH 147 447 224 HOH HOH B . 
# 
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 A ARG 60 ? CZ  ? A ARG 60 CZ  
2 1 Y 1 A ARG 60 ? NH1 ? A ARG 60 NH1 
3 1 Y 1 A ARG 60 ? NH2 ? A ARG 60 NH2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? '(1.19.2_4158: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? SCALA  ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? MOSFLM ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9B2E 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     81.386 
_cell.length_a_esd                 ? 
_cell.length_b                     81.386 
_cell.length_b_esd                 ? 
_cell.length_c                     74.862 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         9B2E 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                90 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 4 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                   9B2E 
_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             2.30 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          46.55 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_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    '8% PEG4000, 100 mM lithium sulfate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            298.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     125 
_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                         'Bruker PHOTON III' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2020-11-20 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.56 
_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                      'ROTATING ANODE' 
_diffrn_source.target                      ? 
_diffrn_source.type                        'BRUKER X8 PROTEUM' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.56 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_synchrotron_site       ? 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9B2E 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               19.33 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     34614 
_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                           97.95 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                1.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.45 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.95 
_reflns_shell.d_res_low                                     2.02 
_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                             1847 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.939 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9B2E 
_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                            1.95 
_refine.ls_d_res_low                             19.33 
_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                     33742 
_refine.ls_number_reflns_R_free                  3393 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    96.29 
_refine.ls_percent_reflns_R_free                 10.06 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2056 
_refine.ls_R_factor_R_free                       0.2131 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2048 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.33 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 23.73 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.19 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1845 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         24 
_refine_hist.number_atoms_solvent             282 
_refine_hist.number_atoms_total               2151 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        19.33 
# 
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  ? 1937 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.089  ? 2648 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.847 ? 704  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.071  ? 301  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 350  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.95 1.98  . . 123 1169 88.00  . . . . 0.2048 . . . . . . . . . . . 0.2131 
'X-RAY DIFFRACTION' 1.98 2.01  . . 127 1214 93.00  . . . . 0.2561 . . . . . . . . . . . 0.2996 
'X-RAY DIFFRACTION' 2.01 2.04  . . 150 1251 96.00  . . . . 0.2252 . . . . . . . . . . . 0.2895 
'X-RAY DIFFRACTION' 2.04 2.07  . . 152 1289 98.00  . . . . 0.2261 . . . . . . . . . . . 0.2466 
'X-RAY DIFFRACTION' 2.07 2.11  . . 132 1275 99.00  . . . . 0.2271 . . . . . . . . . . . 0.1905 
'X-RAY DIFFRACTION' 2.11 2.15  . . 149 1327 99.00  . . . . 0.2156 . . . . . . . . . . . 0.2433 
'X-RAY DIFFRACTION' 2.15 2.19  . . 146 1300 100.00 . . . . 0.2106 . . . . . . . . . . . 0.1822 
'X-RAY DIFFRACTION' 2.19 2.23  . . 136 1294 100.00 . . . . 0.2198 . . . . . . . . . . . 0.2661 
'X-RAY DIFFRACTION' 2.23 2.28  . . 156 1304 98.00  . . . . 0.2175 . . . . . . . . . . . 0.2442 
'X-RAY DIFFRACTION' 2.28 2.33  . . 145 1317 99.00  . . . . 0.2445 . . . . . . . . . . . 0.2085 
'X-RAY DIFFRACTION' 2.33 2.39  . . 146 1265 98.00  . . . . 0.2275 . . . . . . . . . . . 0.2471 
'X-RAY DIFFRACTION' 2.39 2.46  . . 152 1259 96.00  . . . . 0.2602 . . . . . . . . . . . 0.2658 
'X-RAY DIFFRACTION' 2.46 2.53  . . 131 1187 91.00  . . . . 0.2980 . . . . . . . . . . . 0.2945 
'X-RAY DIFFRACTION' 2.53 2.61  . . 122 1162 89.00  . . . . 0.2719 . . . . . . . . . . . 0.3191 
'X-RAY DIFFRACTION' 2.61 2.70  . . 144 1261 94.00  . . . . 0.2496 . . . . . . . . . . . 0.2550 
'X-RAY DIFFRACTION' 2.70 2.81  . . 135 1218 93.00  . . . . 0.2341 . . . . . . . . . . . 0.3130 
'X-RAY DIFFRACTION' 2.81 2.94  . . 138 1255 97.00  . . . . 0.2170 . . . . . . . . . . . 0.1991 
'X-RAY DIFFRACTION' 2.94 3.09  . . 149 1285 99.00  . . . . 0.1912 . . . . . . . . . . . 0.2187 
'X-RAY DIFFRACTION' 3.09 3.28  . . 144 1321 99.00  . . . . 0.1810 . . . . . . . . . . . 0.1897 
'X-RAY DIFFRACTION' 3.29 3.54  . . 149 1293 99.00  . . . . 0.1753 . . . . . . . . . . . 0.1686 
'X-RAY DIFFRACTION' 3.54 3.89  . . 142 1307 100.00 . . . . 0.1504 . . . . . . . . . . . 0.1584 
'X-RAY DIFFRACTION' 3.89 4.44  . . 148 1286 97.00  . . . . 0.1659 . . . . . . . . . . . 0.1522 
'X-RAY DIFFRACTION' 4.45 5.58  . . 139 1209 93.00  . . . . 0.1771 . . . . . . . . . . . 0.1819 
'X-RAY DIFFRACTION' 5.58 19.33 . . 138 1301 97.00  . . . . 0.2079 . . . . . . . . . . . 0.2284 
# 
_struct.entry_id                     9B2E 
_struct.title                        'DHNA associated with an inhibitor' 
_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        9B2E 
_struct_keywords.text            'protein complex, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    A0A045KE67_MYCTX 
_struct_ref.pdbx_db_accession          A0A045KE67 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MADRIELRGLTVHGRHGVYDHERVAGQRFVIDVTVWIDLAEAANSDDLADTYDYVRLASRAAEIVAGPPRKLIETVGAEI
ADHVMDDQRVHAVEVAVHKPQAPIPQTFDDVAVVIRRSRRG
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9B2E A 1 ? 121 ? A0A045KE67 1 ? 121 ? 1 121 
2 1 9B2E B 1 ? 121 ? A0A045KE67 1 ? 121 ? 1 121 
# 
_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   octameric 
_pdbx_struct_assembly.oligomeric_count     8 
# 
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)' 21370 ? 
1 MORE         -89   ? 
1 'SSA (A^2)'  34180 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
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' 2_565 -x,-y+1,z      -1.0000000000 0.0000000000  0.0000000000 0.0000000000   0.0000000000  
-1.0000000000 0.0000000000 81.3860000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
3 'crystal symmetry operation' 3_555 -y+1/2,x+1/2,z 0.0000000000  -1.0000000000 0.0000000000 40.6930000000  1.0000000000  
0.0000000000  0.0000000000 40.6930000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 
4 'crystal symmetry operation' 4_455 y-1/2,-x+1/2,z 0.0000000000  1.0000000000  0.0000000000 -40.6930000000 -1.0000000000 
0.0000000000  0.0000000000 40.6930000000 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 TYR A 19 ? VAL A 24 ? TYR A 19 VAL A 24 5 ? 6  
HELX_P HELX_P2  AA2 LEU A 39 ? ASP A 46 ? LEU A 39 ASP A 46 1 ? 8  
HELX_P HELX_P3  AA3 ASP A 47 ? THR A 51 ? ASP A 47 THR A 51 5 ? 5  
HELX_P HELX_P4  AA4 ASP A 53 ? GLY A 67 ? ASP A 53 GLY A 67 1 ? 15 
HELX_P HELX_P5  AA5 LEU A 72 ? ASP A 86 ? LEU A 72 ASP A 86 1 ? 15 
HELX_P HELX_P6  AA6 TYR B 19 ? VAL B 24 ? TYR B 19 VAL B 24 1 ? 6  
HELX_P HELX_P7  AA7 LEU B 39 ? ASP B 46 ? LEU B 39 ASP B 46 1 ? 8  
HELX_P HELX_P8  AA8 ASP B 47 ? THR B 51 ? ASP B 47 THR B 51 5 ? 5  
HELX_P HELX_P9  AA9 ASP B 53 ? GLY B 67 ? ASP B 53 GLY B 67 1 ? 15 
HELX_P HELX_P10 AB1 LEU B 72 ? MET B 85 ? LEU B 72 MET B 85 1 ? 14 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? 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 ARG A 4   ? GLY A 14  ? ARG A 4   GLY A 14  
AA1 2 GLN A 27  ? ILE A 37  ? GLN A 27  ILE A 37  
AA1 3 VAL A 90  ? HIS A 98  ? VAL A 90  HIS A 98  
AA1 4 ALA A 112 ? SER A 118 ? ALA A 112 SER A 118 
AA2 1 ARG B 4   ? GLY B 14  ? ARG B 4   GLY B 14  
AA2 2 GLN B 27  ? ILE B 37  ? GLN B 27  ILE B 37  
AA2 3 VAL B 90  ? HIS B 98  ? VAL B 90  HIS B 98  
AA2 4 ALA B 112 ? SER B 118 ? ALA B 112 SER B 118 
# 
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 LEU A 7  ? N LEU A 7  O VAL A 33  ? O VAL A 33  
AA1 2 3 N VAL A 30 ? N VAL A 30 O HIS A 98  ? O HIS A 98  
AA1 3 4 N VAL A 95 ? N VAL A 95 O ILE A 115 ? O ILE A 115 
AA2 1 2 N LEU B 10 ? N LEU B 10 O ILE B 31  ? O ILE B 31  
AA2 2 3 N VAL B 30 ? N VAL B 30 O HIS B 98  ? O HIS B 98  
AA2 3 4 N VAL B 95 ? N VAL B 95 O ILE B 115 ? O ILE B 115 
# 
_pdbx_entry_details.entry_id                   9B2E 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 NH1 B ARG 117 ? ? O   B HOH 301 ? ? 1.65 
2  1 OE1 B GLU 94  ? ? O   B HOH 302 ? ? 1.84 
3  1 O   A HOH 340 ? ? O   A HOH 377 ? ? 1.85 
4  1 OD2 B ASP 82  ? ? O   B HOH 303 ? ? 1.94 
5  1 O   A HOH 354 ? ? O   A HOH 400 ? ? 1.95 
6  1 O   B HOH 303 ? ? O   B HOH 393 ? ? 2.04 
7  1 O   B HOH 320 ? ? O   B HOH 343 ? ? 2.05 
8  1 O   B HOH 359 ? ? O   B HOH 389 ? ? 2.05 
9  1 NH2 B ARG 60  ? ? OE2 B GLU 63  ? ? 2.13 
10 1 O   B HOH 333 ? ? O   B HOH 350 ? ? 2.14 
11 1 O   A HOH 433 ? ? O   A HOH 435 ? ? 2.18 
12 1 OD1 B ASP 82  ? ? O   B HOH 304 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 336 ? ? 1_555 O B HOH 325 ? ? 4_455 2.04 
2 1 O A HOH 310 ? ? 1_555 O B HOH 364 ? ? 4_455 2.15 
3 1 O A HOH 330 ? ? 1_555 O A HOH 390 ? ? 5_556 2.18 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_1              60 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_2              60 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CD 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ARG 
_pdbx_validate_rmsd_angle.auth_seq_id_3              60 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                128.04 
_pdbx_validate_rmsd_angle.angle_target_value         111.60 
_pdbx_validate_rmsd_angle.angle_deviation            16.44 
_pdbx_validate_rmsd_angle.angle_standard_deviation   2.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_struct_special_symmetry.id 
_pdbx_struct_special_symmetry.PDB_model_num 
_pdbx_struct_special_symmetry.auth_asym_id 
_pdbx_struct_special_symmetry.auth_comp_id 
_pdbx_struct_special_symmetry.auth_seq_id 
_pdbx_struct_special_symmetry.PDB_ins_code 
_pdbx_struct_special_symmetry.label_asym_id 
_pdbx_struct_special_symmetry.label_comp_id 
_pdbx_struct_special_symmetry.label_seq_id 
1 1 A HOH 425 ? E HOH . 
2 1 B HOH 345 ? F HOH . 
3 1 B HOH 447 ? F HOH . 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 435 ? 6.64 . 
2 1 O ? B HOH 447 ? 5.83 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A MET 1   ? A MET 1   
2 1 Y 1 A ARG 120 ? A ARG 120 
3 1 Y 1 A GLY 121 ? A GLY 121 
4 1 Y 1 B MET 1   ? B MET 1   
5 1 Y 1 B ARG 120 ? B ARG 120 
6 1 Y 1 B GLY 121 ? B GLY 121 
# 
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  
B55 O1   O N N 74  
B55 C5   C N N 75  
B55 C2   C Y N 76  
B55 N1   N Y N 77  
B55 N4   N N N 78  
B55 C4   C N N 79  
B55 N3   N N N 80  
B55 N2   N N N 81  
B55 C3   C Y N 82  
B55 N5   N Y N 83  
B55 C1   C Y N 84  
B55 S1   S N N 85  
B55 HN4  H N N 86  
B55 HN3  H N N 87  
B55 HN3A H N N 88  
B55 HN5  H N N 89  
B55 HS1  H N N 90  
GLN N    N N N 91  
GLN CA   C N S 92  
GLN C    C N N 93  
GLN O    O N N 94  
GLN CB   C N N 95  
GLN CG   C N N 96  
GLN CD   C N N 97  
GLN OE1  O N N 98  
GLN NE2  N N N 99  
GLN OXT  O N N 100 
GLN H    H N N 101 
GLN H2   H N N 102 
GLN HA   H N N 103 
GLN HB2  H N N 104 
GLN HB3  H N N 105 
GLN HG2  H N N 106 
GLN HG3  H N N 107 
GLN HE21 H N N 108 
GLN HE22 H N N 109 
GLN HXT  H N N 110 
GLU N    N N N 111 
GLU CA   C N S 112 
GLU C    C N N 113 
GLU O    O N N 114 
GLU CB   C N N 115 
GLU CG   C N N 116 
GLU CD   C N N 117 
GLU OE1  O N N 118 
GLU OE2  O N N 119 
GLU OXT  O N N 120 
GLU H    H N N 121 
GLU H2   H N N 122 
GLU HA   H N N 123 
GLU HB2  H N N 124 
GLU HB3  H N N 125 
GLU HG2  H N N 126 
GLU HG3  H N N 127 
GLU HE2  H N N 128 
GLU HXT  H N N 129 
GLY N    N N N 130 
GLY CA   C N N 131 
GLY C    C N N 132 
GLY O    O N N 133 
GLY OXT  O N N 134 
GLY H    H N N 135 
GLY H2   H N N 136 
GLY HA2  H N N 137 
GLY HA3  H N N 138 
GLY HXT  H N N 139 
HIS N    N N N 140 
HIS CA   C N S 141 
HIS C    C N N 142 
HIS O    O N N 143 
HIS CB   C N N 144 
HIS CG   C Y N 145 
HIS ND1  N Y N 146 
HIS CD2  C Y N 147 
HIS CE1  C Y N 148 
HIS NE2  N Y N 149 
HIS OXT  O N N 150 
HIS H    H N N 151 
HIS H2   H N N 152 
HIS HA   H N N 153 
HIS HB2  H N N 154 
HIS HB3  H N N 155 
HIS HD1  H N N 156 
HIS HD2  H N N 157 
HIS HE1  H N N 158 
HIS HE2  H N N 159 
HIS HXT  H N N 160 
HOH O    O N N 161 
HOH H1   H N N 162 
HOH H2   H N N 163 
ILE N    N N N 164 
ILE CA   C N S 165 
ILE C    C N N 166 
ILE O    O N N 167 
ILE CB   C N S 168 
ILE CG1  C N N 169 
ILE CG2  C N N 170 
ILE CD1  C N N 171 
ILE OXT  O N N 172 
ILE H    H N N 173 
ILE H2   H N N 174 
ILE HA   H N N 175 
ILE HB   H N N 176 
ILE HG12 H N N 177 
ILE HG13 H N N 178 
ILE HG21 H N N 179 
ILE HG22 H N N 180 
ILE HG23 H N N 181 
ILE HD11 H N N 182 
ILE HD12 H N N 183 
ILE HD13 H N N 184 
ILE HXT  H N N 185 
LEU N    N N N 186 
LEU CA   C N S 187 
LEU C    C N N 188 
LEU O    O N N 189 
LEU CB   C N N 190 
LEU CG   C N N 191 
LEU CD1  C N N 192 
LEU CD2  C N N 193 
LEU OXT  O N N 194 
LEU H    H N N 195 
LEU H2   H N N 196 
LEU HA   H N N 197 
LEU HB2  H N N 198 
LEU HB3  H N N 199 
LEU HG   H N N 200 
LEU HD11 H N N 201 
LEU HD12 H N N 202 
LEU HD13 H N N 203 
LEU HD21 H N N 204 
LEU HD22 H N N 205 
LEU HD23 H N N 206 
LEU HXT  H N N 207 
LYS N    N N N 208 
LYS CA   C N S 209 
LYS C    C N N 210 
LYS O    O N N 211 
LYS CB   C N N 212 
LYS CG   C N N 213 
LYS CD   C N N 214 
LYS CE   C N N 215 
LYS NZ   N N N 216 
LYS OXT  O N N 217 
LYS H    H N N 218 
LYS H2   H N N 219 
LYS HA   H N N 220 
LYS HB2  H N N 221 
LYS HB3  H N N 222 
LYS HG2  H N N 223 
LYS HG3  H N N 224 
LYS HD2  H N N 225 
LYS HD3  H N N 226 
LYS HE2  H N N 227 
LYS HE3  H N N 228 
LYS HZ1  H N N 229 
LYS HZ2  H N N 230 
LYS HZ3  H N N 231 
LYS HXT  H N N 232 
MET N    N N N 233 
MET CA   C N S 234 
MET C    C N N 235 
MET O    O N N 236 
MET CB   C N N 237 
MET CG   C N N 238 
MET SD   S N N 239 
MET CE   C N N 240 
MET OXT  O N N 241 
MET H    H N N 242 
MET H2   H N N 243 
MET HA   H N N 244 
MET HB2  H N N 245 
MET HB3  H N N 246 
MET HG2  H N N 247 
MET HG3  H N N 248 
MET HE1  H N N 249 
MET HE2  H N N 250 
MET HE3  H N N 251 
MET HXT  H N N 252 
PHE N    N N N 253 
PHE CA   C N S 254 
PHE C    C N N 255 
PHE O    O N N 256 
PHE CB   C N N 257 
PHE CG   C Y N 258 
PHE CD1  C Y N 259 
PHE CD2  C Y N 260 
PHE CE1  C Y N 261 
PHE CE2  C Y N 262 
PHE CZ   C Y N 263 
PHE OXT  O N N 264 
PHE H    H N N 265 
PHE H2   H N N 266 
PHE HA   H N N 267 
PHE HB2  H N N 268 
PHE HB3  H N N 269 
PHE HD1  H N N 270 
PHE HD2  H N N 271 
PHE HE1  H N N 272 
PHE HE2  H N N 273 
PHE HZ   H N N 274 
PHE HXT  H N N 275 
PRO N    N N N 276 
PRO CA   C N S 277 
PRO C    C N N 278 
PRO O    O N N 279 
PRO CB   C N N 280 
PRO CG   C N N 281 
PRO CD   C N N 282 
PRO OXT  O N N 283 
PRO H    H N N 284 
PRO HA   H N N 285 
PRO HB2  H N N 286 
PRO HB3  H N N 287 
PRO HG2  H N N 288 
PRO HG3  H N N 289 
PRO HD2  H N N 290 
PRO HD3  H N N 291 
PRO HXT  H N N 292 
SER N    N N N 293 
SER CA   C N S 294 
SER C    C N N 295 
SER O    O N N 296 
SER CB   C N N 297 
SER OG   O N N 298 
SER OXT  O N N 299 
SER H    H N N 300 
SER H2   H N N 301 
SER HA   H N N 302 
SER HB2  H N N 303 
SER HB3  H N N 304 
SER HG   H N N 305 
SER HXT  H N N 306 
THR N    N N N 307 
THR CA   C N S 308 
THR C    C N N 309 
THR O    O N N 310 
THR CB   C N R 311 
THR OG1  O N N 312 
THR CG2  C N N 313 
THR OXT  O N N 314 
THR H    H N N 315 
THR H2   H N N 316 
THR HA   H N N 317 
THR HB   H N N 318 
THR HG1  H N N 319 
THR HG21 H N N 320 
THR HG22 H N N 321 
THR HG23 H N N 322 
THR HXT  H N N 323 
TRP N    N N N 324 
TRP CA   C N S 325 
TRP C    C N N 326 
TRP O    O N N 327 
TRP CB   C N N 328 
TRP CG   C Y N 329 
TRP CD1  C Y N 330 
TRP CD2  C Y N 331 
TRP NE1  N Y N 332 
TRP CE2  C Y N 333 
TRP CE3  C Y N 334 
TRP CZ2  C Y N 335 
TRP CZ3  C Y N 336 
TRP CH2  C Y N 337 
TRP OXT  O N N 338 
TRP H    H N N 339 
TRP H2   H N N 340 
TRP HA   H N N 341 
TRP HB2  H N N 342 
TRP HB3  H N N 343 
TRP HD1  H N N 344 
TRP HE1  H N N 345 
TRP HE3  H N N 346 
TRP HZ2  H N N 347 
TRP HZ3  H N N 348 
TRP HH2  H N N 349 
TRP HXT  H N N 350 
TYR N    N N N 351 
TYR CA   C N S 352 
TYR C    C N N 353 
TYR O    O N N 354 
TYR CB   C N N 355 
TYR CG   C Y N 356 
TYR CD1  C Y N 357 
TYR CD2  C Y N 358 
TYR CE1  C Y N 359 
TYR CE2  C Y N 360 
TYR CZ   C Y N 361 
TYR OH   O N N 362 
TYR OXT  O N N 363 
TYR H    H N N 364 
TYR H2   H N N 365 
TYR HA   H N N 366 
TYR HB2  H N N 367 
TYR HB3  H N N 368 
TYR HD1  H N N 369 
TYR HD2  H N N 370 
TYR HE1  H N N 371 
TYR HE2  H N N 372 
TYR HH   H N N 373 
TYR HXT  H N N 374 
VAL N    N N N 375 
VAL CA   C N S 376 
VAL C    C N N 377 
VAL O    O N N 378 
VAL CB   C N N 379 
VAL CG1  C N N 380 
VAL CG2  C N N 381 
VAL OXT  O N N 382 
VAL H    H N N 383 
VAL H2   H N N 384 
VAL HA   H N N 385 
VAL HB   H N N 386 
VAL HG11 H N N 387 
VAL HG12 H N N 388 
VAL HG13 H N N 389 
VAL HG21 H N N 390 
VAL HG22 H N N 391 
VAL HG23 H N N 392 
VAL HXT  H N N 393 
# 
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  
B55 O1  C5   doub N N 70  
B55 C5  C2   sing N N 71  
B55 C5  N4   sing N N 72  
B55 C2  N1   sing Y N 73  
B55 C2  C3   doub Y N 74  
B55 N1  C1   doub Y N 75  
B55 N4  C4   sing N N 76  
B55 C4  N3   sing N N 77  
B55 C4  N2   doub N N 78  
B55 N2  C3   sing N N 79  
B55 C3  N5   sing Y N 80  
B55 N5  C1   sing Y N 81  
B55 C1  S1   sing N N 82  
B55 N4  HN4  sing N N 83  
B55 N3  HN3  sing N N 84  
B55 N3  HN3A sing N N 85  
B55 N5  HN5  sing N N 86  
B55 S1  HS1  sing N N 87  
GLN N   CA   sing N N 88  
GLN N   H    sing N N 89  
GLN N   H2   sing N N 90  
GLN CA  C    sing N N 91  
GLN CA  CB   sing N N 92  
GLN CA  HA   sing N N 93  
GLN C   O    doub N N 94  
GLN C   OXT  sing N N 95  
GLN CB  CG   sing N N 96  
GLN CB  HB2  sing N N 97  
GLN CB  HB3  sing N N 98  
GLN CG  CD   sing N N 99  
GLN CG  HG2  sing N N 100 
GLN CG  HG3  sing N N 101 
GLN CD  OE1  doub N N 102 
GLN CD  NE2  sing N N 103 
GLN NE2 HE21 sing N N 104 
GLN NE2 HE22 sing N N 105 
GLN OXT HXT  sing N N 106 
GLU N   CA   sing N N 107 
GLU N   H    sing N N 108 
GLU N   H2   sing N N 109 
GLU CA  C    sing N N 110 
GLU CA  CB   sing N N 111 
GLU CA  HA   sing N N 112 
GLU C   O    doub N N 113 
GLU C   OXT  sing N N 114 
GLU CB  CG   sing N N 115 
GLU CB  HB2  sing N N 116 
GLU CB  HB3  sing N N 117 
GLU CG  CD   sing N N 118 
GLU CG  HG2  sing N N 119 
GLU CG  HG3  sing N N 120 
GLU CD  OE1  doub N N 121 
GLU CD  OE2  sing N N 122 
GLU OE2 HE2  sing N N 123 
GLU OXT HXT  sing N N 124 
GLY N   CA   sing N N 125 
GLY N   H    sing N N 126 
GLY N   H2   sing N N 127 
GLY CA  C    sing N N 128 
GLY CA  HA2  sing N N 129 
GLY CA  HA3  sing N N 130 
GLY C   O    doub N N 131 
GLY C   OXT  sing N N 132 
GLY OXT HXT  sing N N 133 
HIS N   CA   sing N N 134 
HIS N   H    sing N N 135 
HIS N   H2   sing N N 136 
HIS CA  C    sing N N 137 
HIS CA  CB   sing N N 138 
HIS CA  HA   sing N N 139 
HIS C   O    doub N N 140 
HIS C   OXT  sing N N 141 
HIS CB  CG   sing N N 142 
HIS CB  HB2  sing N N 143 
HIS CB  HB3  sing N N 144 
HIS CG  ND1  sing Y N 145 
HIS CG  CD2  doub Y N 146 
HIS ND1 CE1  doub Y N 147 
HIS ND1 HD1  sing N N 148 
HIS CD2 NE2  sing Y N 149 
HIS CD2 HD2  sing N N 150 
HIS CE1 NE2  sing Y N 151 
HIS CE1 HE1  sing N N 152 
HIS NE2 HE2  sing N N 153 
HIS OXT HXT  sing N N 154 
HOH O   H1   sing N N 155 
HOH O   H2   sing N N 156 
ILE N   CA   sing N N 157 
ILE N   H    sing N N 158 
ILE N   H2   sing N N 159 
ILE CA  C    sing N N 160 
ILE CA  CB   sing N N 161 
ILE CA  HA   sing N N 162 
ILE C   O    doub N N 163 
ILE C   OXT  sing N N 164 
ILE CB  CG1  sing N N 165 
ILE CB  CG2  sing N N 166 
ILE CB  HB   sing N N 167 
ILE CG1 CD1  sing N N 168 
ILE CG1 HG12 sing N N 169 
ILE CG1 HG13 sing N N 170 
ILE CG2 HG21 sing N N 171 
ILE CG2 HG22 sing N N 172 
ILE CG2 HG23 sing N N 173 
ILE CD1 HD11 sing N N 174 
ILE CD1 HD12 sing N N 175 
ILE CD1 HD13 sing N N 176 
ILE OXT HXT  sing N N 177 
LEU N   CA   sing N N 178 
LEU N   H    sing N N 179 
LEU N   H2   sing N N 180 
LEU CA  C    sing N N 181 
LEU CA  CB   sing N N 182 
LEU CA  HA   sing N N 183 
LEU C   O    doub N N 184 
LEU C   OXT  sing N N 185 
LEU CB  CG   sing N N 186 
LEU CB  HB2  sing N N 187 
LEU CB  HB3  sing N N 188 
LEU CG  CD1  sing N N 189 
LEU CG  CD2  sing N N 190 
LEU CG  HG   sing N N 191 
LEU CD1 HD11 sing N N 192 
LEU CD1 HD12 sing N N 193 
LEU CD1 HD13 sing N N 194 
LEU CD2 HD21 sing N N 195 
LEU CD2 HD22 sing N N 196 
LEU CD2 HD23 sing N N 197 
LEU OXT HXT  sing N N 198 
LYS N   CA   sing N N 199 
LYS N   H    sing N N 200 
LYS N   H2   sing N N 201 
LYS CA  C    sing N N 202 
LYS CA  CB   sing N N 203 
LYS CA  HA   sing N N 204 
LYS C   O    doub N N 205 
LYS C   OXT  sing N N 206 
LYS CB  CG   sing N N 207 
LYS CB  HB2  sing N N 208 
LYS CB  HB3  sing N N 209 
LYS CG  CD   sing N N 210 
LYS CG  HG2  sing N N 211 
LYS CG  HG3  sing N N 212 
LYS CD  CE   sing N N 213 
LYS CD  HD2  sing N N 214 
LYS CD  HD3  sing N N 215 
LYS CE  NZ   sing N N 216 
LYS CE  HE2  sing N N 217 
LYS CE  HE3  sing N N 218 
LYS NZ  HZ1  sing N N 219 
LYS NZ  HZ2  sing N N 220 
LYS NZ  HZ3  sing N N 221 
LYS OXT HXT  sing N N 222 
MET N   CA   sing N N 223 
MET N   H    sing N N 224 
MET N   H2   sing N N 225 
MET CA  C    sing N N 226 
MET CA  CB   sing N N 227 
MET CA  HA   sing N N 228 
MET C   O    doub N N 229 
MET C   OXT  sing N N 230 
MET CB  CG   sing N N 231 
MET CB  HB2  sing N N 232 
MET CB  HB3  sing N N 233 
MET CG  SD   sing N N 234 
MET CG  HG2  sing N N 235 
MET CG  HG3  sing N N 236 
MET SD  CE   sing N N 237 
MET CE  HE1  sing N N 238 
MET CE  HE2  sing N N 239 
MET CE  HE3  sing N N 240 
MET OXT HXT  sing N N 241 
PHE N   CA   sing N N 242 
PHE N   H    sing N N 243 
PHE N   H2   sing N N 244 
PHE CA  C    sing N N 245 
PHE CA  CB   sing N N 246 
PHE CA  HA   sing N N 247 
PHE C   O    doub N N 248 
PHE C   OXT  sing N N 249 
PHE CB  CG   sing N N 250 
PHE CB  HB2  sing N N 251 
PHE CB  HB3  sing N N 252 
PHE CG  CD1  doub Y N 253 
PHE CG  CD2  sing Y N 254 
PHE CD1 CE1  sing Y N 255 
PHE CD1 HD1  sing N N 256 
PHE CD2 CE2  doub Y N 257 
PHE CD2 HD2  sing N N 258 
PHE CE1 CZ   doub Y N 259 
PHE CE1 HE1  sing N N 260 
PHE CE2 CZ   sing Y N 261 
PHE CE2 HE2  sing N N 262 
PHE CZ  HZ   sing N N 263 
PHE OXT HXT  sing N N 264 
PRO N   CA   sing N N 265 
PRO N   CD   sing N N 266 
PRO N   H    sing N N 267 
PRO CA  C    sing N N 268 
PRO CA  CB   sing N N 269 
PRO CA  HA   sing N N 270 
PRO C   O    doub N N 271 
PRO C   OXT  sing N N 272 
PRO CB  CG   sing N N 273 
PRO CB  HB2  sing N N 274 
PRO CB  HB3  sing N N 275 
PRO CG  CD   sing N N 276 
PRO CG  HG2  sing N N 277 
PRO CG  HG3  sing N N 278 
PRO CD  HD2  sing N N 279 
PRO CD  HD3  sing N N 280 
PRO OXT HXT  sing N N 281 
SER N   CA   sing N N 282 
SER N   H    sing N N 283 
SER N   H2   sing N N 284 
SER CA  C    sing N N 285 
SER CA  CB   sing N N 286 
SER CA  HA   sing N N 287 
SER C   O    doub N N 288 
SER C   OXT  sing N N 289 
SER CB  OG   sing N N 290 
SER CB  HB2  sing N N 291 
SER CB  HB3  sing N N 292 
SER OG  HG   sing N N 293 
SER OXT HXT  sing N N 294 
THR N   CA   sing N N 295 
THR N   H    sing N N 296 
THR N   H2   sing N N 297 
THR CA  C    sing N N 298 
THR CA  CB   sing N N 299 
THR CA  HA   sing N N 300 
THR C   O    doub N N 301 
THR C   OXT  sing N N 302 
THR CB  OG1  sing N N 303 
THR CB  CG2  sing N N 304 
THR CB  HB   sing N N 305 
THR OG1 HG1  sing N N 306 
THR CG2 HG21 sing N N 307 
THR CG2 HG22 sing N N 308 
THR CG2 HG23 sing N N 309 
THR OXT HXT  sing N N 310 
TRP N   CA   sing N N 311 
TRP N   H    sing N N 312 
TRP N   H2   sing N N 313 
TRP CA  C    sing N N 314 
TRP CA  CB   sing N N 315 
TRP CA  HA   sing N N 316 
TRP C   O    doub N N 317 
TRP C   OXT  sing N N 318 
TRP CB  CG   sing N N 319 
TRP CB  HB2  sing N N 320 
TRP CB  HB3  sing N N 321 
TRP CG  CD1  doub Y N 322 
TRP CG  CD2  sing Y N 323 
TRP CD1 NE1  sing Y N 324 
TRP CD1 HD1  sing N N 325 
TRP CD2 CE2  doub Y N 326 
TRP CD2 CE3  sing Y N 327 
TRP NE1 CE2  sing Y N 328 
TRP NE1 HE1  sing N N 329 
TRP CE2 CZ2  sing Y N 330 
TRP CE3 CZ3  doub Y N 331 
TRP CE3 HE3  sing N N 332 
TRP CZ2 CH2  doub Y N 333 
TRP CZ2 HZ2  sing N N 334 
TRP CZ3 CH2  sing Y N 335 
TRP CZ3 HZ3  sing N N 336 
TRP CH2 HH2  sing N N 337 
TRP OXT HXT  sing N N 338 
TYR N   CA   sing N N 339 
TYR N   H    sing N N 340 
TYR N   H2   sing N N 341 
TYR CA  C    sing N N 342 
TYR CA  CB   sing N N 343 
TYR CA  HA   sing N N 344 
TYR C   O    doub N N 345 
TYR C   OXT  sing N N 346 
TYR CB  CG   sing N N 347 
TYR CB  HB2  sing N N 348 
TYR CB  HB3  sing N N 349 
TYR CG  CD1  doub Y N 350 
TYR CG  CD2  sing Y N 351 
TYR CD1 CE1  sing Y N 352 
TYR CD1 HD1  sing N N 353 
TYR CD2 CE2  doub Y N 354 
TYR CD2 HD2  sing N N 355 
TYR CE1 CZ   doub Y N 356 
TYR CE1 HE1  sing N N 357 
TYR CE2 CZ   sing Y N 358 
TYR CE2 HE2  sing N N 359 
TYR CZ  OH   sing N N 360 
TYR OH  HH   sing N N 361 
TYR OXT HXT  sing N N 362 
VAL N   CA   sing N N 363 
VAL N   H    sing N N 364 
VAL N   H2   sing N N 365 
VAL CA  C    sing N N 366 
VAL CA  CB   sing N N 367 
VAL CA  HA   sing N N 368 
VAL C   O    doub N N 369 
VAL C   OXT  sing N N 370 
VAL CB  CG1  sing N N 371 
VAL CB  CG2  sing N N 372 
VAL CB  HB   sing N N 373 
VAL CG1 HG11 sing N N 374 
VAL CG1 HG12 sing N N 375 
VAL CG1 HG13 sing N N 376 
VAL CG2 HG21 sing N N 377 
VAL CG2 HG22 sing N N 378 
VAL CG2 HG23 sing N N 379 
VAL OXT HXT  sing N N 380 
# 
_pdbx_audit_support.funding_organization   'Brazilian National Council for Scientific and Technological Development (CNPq)' 
_pdbx_audit_support.country                Brazil 
_pdbx_audit_support.grant_number           42170320172 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1NBU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9B2E 
_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]   0.012287 
_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]   0.012287 
_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]   0.013358 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
H 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N    . ALA A 1 2   ? 11.626  42.865 49.790  1.00 58.53 ? 2   ALA A N    1 
ATOM   2    C CA   . ALA A 1 2   ? 13.040  42.676 49.389  1.00 46.39 ? 2   ALA A CA   1 
ATOM   3    C C    . ALA A 1 2   ? 13.166  42.808 47.867  1.00 36.07 ? 2   ALA A C    1 
ATOM   4    O O    . ALA A 1 2   ? 12.178  43.213 47.224  1.00 33.44 ? 2   ALA A O    1 
ATOM   5    C CB   . ALA A 1 2   ? 13.537  41.335 49.871  1.00 39.56 ? 2   ALA A CB   1 
ATOM   6    N N    . ASP A 1 3   ? 14.338  42.484 47.317  1.00 29.11 ? 3   ASP A N    1 
ATOM   7    C CA   . ASP A 1 3   ? 14.548  42.593 45.856  1.00 24.55 ? 3   ASP A CA   1 
ATOM   8    C C    . ASP A 1 3   ? 14.252  41.257 45.164  1.00 24.89 ? 3   ASP A C    1 
ATOM   9    O O    . ASP A 1 3   ? 14.124  40.270 45.834  1.00 21.11 ? 3   ASP A O    1 
ATOM   10   C CB   . ASP A 1 3   ? 15.939  43.090 45.524  1.00 30.48 ? 3   ASP A CB   1 
ATOM   11   C CG   . ASP A 1 3   ? 16.287  44.329 46.315  1.00 25.33 ? 3   ASP A CG   1 
ATOM   12   O OD1  . ASP A 1 3   ? 15.456  45.208 46.385  1.00 24.55 ? 3   ASP A OD1  1 
ATOM   13   O OD2  . ASP A 1 3   ? 17.336  44.332 46.864  1.00 23.96 ? 3   ASP A OD2  1 
ATOM   14   N N    . ARG A 1 4   ? 14.170  41.275 43.841  1.00 24.51 ? 4   ARG A N    1 
ATOM   15   C CA   . ARG A 1 4   ? 13.930  40.006 43.125  1.00 22.22 ? 4   ARG A CA   1 
ATOM   16   C C    . ARG A 1 4   ? 14.527  40.003 41.721  1.00 18.20 ? 4   ARG A C    1 
ATOM   17   O O    . ARG A 1 4   ? 14.740  41.060 41.158  1.00 20.29 ? 4   ARG A O    1 
ATOM   18   C CB   . ARG A 1 4   ? 12.456  39.615 43.102  1.00 23.45 ? 4   ARG A CB   1 
ATOM   19   C CG   . ARG A 1 4   ? 11.465  40.728 42.871  1.00 25.54 ? 4   ARG A CG   1 
ATOM   20   C CD   . ARG A 1 4   ? 10.050  40.239 42.997  1.00 21.20 ? 4   ARG A CD   1 
ATOM   21   N NE   . ARG A 1 4   ? 9.292   41.035 42.081  1.00 22.81 ? 4   ARG A NE   1 
ATOM   22   C CZ   . ARG A 1 4   ? 8.732   42.184 42.366  1.00 24.93 ? 4   ARG A CZ   1 
ATOM   23   N NH1  . ARG A 1 4   ? 8.815   42.694 43.576  1.00 26.12 ? 4   ARG A NH1  1 
ATOM   24   N NH2  . ARG A 1 4   ? 8.073   42.826 41.439  1.00 23.74 ? 4   ARG A NH2  1 
ATOM   25   N N    . ILE A 1 5   ? 14.822  38.799 41.269  1.00 14.96 ? 5   ILE A N    1 
ATOM   26   C CA   . ILE A 1 5   ? 15.311  38.499 39.906  1.00 14.72 ? 5   ILE A CA   1 
ATOM   27   C C    . ILE A 1 5   ? 14.168  37.723 39.249  1.00 20.09 ? 5   ILE A C    1 
ATOM   28   O O    . ILE A 1 5   ? 13.670  36.797 39.856  1.00 15.14 ? 5   ILE A O    1 
ATOM   29   C CB   . ILE A 1 5   ? 16.603  37.680 39.946  1.00 17.58 ? 5   ILE A CB   1 
ATOM   30   C CG1  . ILE A 1 5   ? 17.736  38.470 40.594  1.00 21.52 ? 5   ILE A CG1  1 
ATOM   31   C CG2  . ILE A 1 5   ? 16.962  37.245 38.546  1.00 18.28 ? 5   ILE A CG2  1 
ATOM   32   C CD1  . ILE A 1 5   ? 18.682  37.644 41.366  1.00 21.10 ? 5   ILE A CD1  1 
ATOM   33   N N    . GLU A 1 6   ? 13.799  38.107 38.048  1.00 15.92 ? 6   GLU A N    1 
ATOM   34   C CA   . GLU A 1 6   ? 12.643  37.523 37.382  1.00 19.77 ? 6   GLU A CA   1 
ATOM   35   C C    . GLU A 1 6   ? 13.071  37.042 36.007  1.00 15.46 ? 6   GLU A C    1 
ATOM   36   O O    . GLU A 1 6   ? 13.503  37.840 35.170  1.00 18.65 ? 6   GLU A O    1 
ATOM   37   C CB   . GLU A 1 6   ? 11.505  38.545 37.284  1.00 22.56 ? 6   GLU A CB   1 
ATOM   38   C CG   . GLU A 1 6   ? 10.938  38.936 38.638  1.00 15.71 ? 6   GLU A CG   1 
ATOM   39   C CD   . GLU A 1 6   ? 9.723   39.827 38.514  1.00 25.25 ? 6   GLU A CD   1 
ATOM   40   O OE1  . GLU A 1 6   ? 9.566   40.451 37.445  1.00 22.89 ? 6   GLU A OE1  1 
ATOM   41   O OE2  . GLU A 1 6   ? 8.931   39.897 39.478  1.00 23.38 ? 6   GLU A OE2  1 
ATOM   42   N N    . LEU A 1 7   ? 12.979  35.742 35.791  1.00 15.85 ? 7   LEU A N    1 
ATOM   43   C CA   . LEU A 1 7   ? 13.201  35.145 34.481  1.00 13.85 ? 7   LEU A CA   1 
ATOM   44   C C    . LEU A 1 7   ? 11.834  34.749 33.940  1.00 16.24 ? 7   LEU A C    1 
ATOM   45   O O    . LEU A 1 7   ? 11.055  34.119 34.656  1.00 16.14 ? 7   LEU A O    1 
ATOM   46   C CB   . LEU A 1 7   ? 14.113  33.918 34.604  1.00 19.24 ? 7   LEU A CB   1 
ATOM   47   C CG   . LEU A 1 7   ? 14.359  33.068 33.342  1.00 20.35 ? 7   LEU A CG   1 
ATOM   48   C CD1  . LEU A 1 7   ? 14.886  33.941 32.192  1.00 20.13 ? 7   LEU A CD1  1 
ATOM   49   C CD2  . LEU A 1 7   ? 15.270  31.898 33.619  1.00 14.60 ? 7   LEU A CD2  1 
ATOM   50   N N    . ARG A 1 8   ? 11.532  35.112 32.695  1.00 13.35 ? 8   ARG A N    1 
ATOM   51   C CA   . ARG A 1 8   ? 10.196  34.882 32.158  1.00 16.12 ? 8   ARG A CA   1 
ATOM   52   C C    . ARG A 1 8   ? 10.269  34.245 30.776  1.00 13.93 ? 8   ARG A C    1 
ATOM   53   O O    . ARG A 1 8   ? 11.083  34.648 29.942  1.00 15.58 ? 8   ARG A O    1 
ATOM   54   C CB   . ARG A 1 8   ? 9.403   36.206 32.074  1.00 15.69 ? 8   ARG A CB   1 
ATOM   55   C CG   . ARG A 1 8   ? 9.137   36.830 33.457  1.00 18.16 ? 8   ARG A CG   1 
ATOM   56   C CD   . ARG A 1 8   ? 8.127   35.997 34.246  1.00 18.25 ? 8   ARG A CD   1 
ATOM   57   N NE   . ARG A 1 8   ? 7.716   36.587 35.523  1.00 19.65 ? 8   ARG A NE   1 
ATOM   58   C CZ   . ARG A 1 8   ? 8.325   36.353 36.680  1.00 22.20 ? 8   ARG A CZ   1 
ATOM   59   N NH1  . ARG A 1 8   ? 9.427   35.626 36.744  1.00 16.78 ? 8   ARG A NH1  1 
ATOM   60   N NH2  . ARG A 1 8   ? 7.827   36.878 37.797  1.00 22.21 ? 8   ARG A NH2  1 
ATOM   61   N N    . GLY A 1 9   ? 9.402   33.265 30.530  1.00 14.10 ? 9   GLY A N    1 
ATOM   62   C CA   . GLY A 1 9   ? 9.263   32.726 29.186  1.00 14.00 ? 9   GLY A CA   1 
ATOM   63   C C    . GLY A 1 9   ? 10.384  31.826 28.717  1.00 16.38 ? 9   GLY A C    1 
ATOM   64   O O    . GLY A 1 9   ? 10.602  31.708 27.518  1.00 14.32 ? 9   GLY A O    1 
ATOM   65   N N    . LEU A 1 10  ? 11.110  31.196 29.634  1.00 13.85 ? 10  LEU A N    1 
ATOM   66   C CA   . LEU A 1 10  ? 12.155  30.257 29.243  1.00 14.36 ? 10  LEU A CA   1 
ATOM   67   C C    . LEU A 1 10  ? 11.496  29.074 28.538  1.00 18.09 ? 10  LEU A C    1 
ATOM   68   O O    . LEU A 1 10  ? 10.690  28.357 29.141  1.00 14.06 ? 10  LEU A O    1 
ATOM   69   C CB   . LEU A 1 10  ? 12.934  29.813 30.475  1.00 13.56 ? 10  LEU A CB   1 
ATOM   70   C CG   . LEU A 1 10  ? 13.994  28.719 30.299  1.00 18.02 ? 10  LEU A CG   1 
ATOM   71   C CD1  . LEU A 1 10  ? 15.090  29.222 29.375  1.00 15.19 ? 10  LEU A CD1  1 
ATOM   72   C CD2  . LEU A 1 10  ? 14.568  28.304 31.642  1.00 15.29 ? 10  LEU A CD2  1 
ATOM   73   N N    . THR A 1 11  ? 11.787  28.906 27.247  1.00 15.35 ? 11  THR A N    1 
ATOM   74   C CA   . THR A 1 11  ? 11.064  27.966 26.387  1.00 15.60 ? 11  THR A CA   1 
ATOM   75   C C    . THR A 1 11  ? 11.958  26.792 26.009  1.00 16.86 ? 11  THR A C    1 
ATOM   76   O O    . THR A 1 11  ? 12.988  26.975 25.345  1.00 16.07 ? 11  THR A O    1 
ATOM   77   C CB   . THR A 1 11  ? 10.542  28.690 25.149  1.00 14.86 ? 11  THR A CB   1 
ATOM   78   O OG1  . THR A 1 11  ? 9.760   29.806 25.582  1.00 16.10 ? 11  THR A OG1  1 
ATOM   79   C CG2  . THR A 1 11  ? 9.709   27.794 24.271  1.00 16.63 ? 11  THR A CG2  1 
ATOM   80   N N    . VAL A 1 12  ? 11.543  25.588 26.408  1.00 17.10 ? 12  VAL A N    1 
ATOM   81   C CA   . VAL A 1 12  ? 12.375  24.392 26.329  1.00 17.92 ? 12  VAL A CA   1 
ATOM   82   C C    . VAL A 1 12  ? 11.503  23.209 25.931  1.00 15.84 ? 12  VAL A C    1 
ATOM   83   O O    . VAL A 1 12  ? 10.447  22.988 26.528  1.00 12.52 ? 12  VAL A O    1 
ATOM   84   C CB   . VAL A 1 12  ? 13.083  24.117 27.674  1.00 20.19 ? 12  VAL A CB   1 
ATOM   85   C CG1  . VAL A 1 12  ? 13.987  22.896 27.566  1.00 15.11 ? 12  VAL A CG1  1 
ATOM   86   C CG2  . VAL A 1 12  ? 13.892  25.340 28.114  1.00 18.90 ? 12  VAL A CG2  1 
ATOM   87   N N    . HIS A 1 13  ? 11.933  22.463 24.911  1.00 15.59 ? 13  HIS A N    1 
ATOM   88   C CA   . HIS A 1 13  ? 11.256  21.227 24.547  1.00 16.75 ? 13  HIS A CA   1 
ATOM   89   C C    . HIS A 1 13  ? 11.478  20.167 25.625  1.00 17.87 ? 13  HIS A C    1 
ATOM   90   O O    . HIS A 1 13  ? 12.589  20.000 26.130  1.00 15.18 ? 13  HIS A O    1 
ATOM   91   C CB   . HIS A 1 13  ? 11.764  20.735 23.188  1.00 17.18 ? 13  HIS A CB   1 
ATOM   92   C CG   . HIS A 1 13  ? 10.946  19.621 22.600  1.00 18.69 ? 13  HIS A CG   1 
ATOM   93   N ND1  . HIS A 1 13  ? 11.239  18.291 22.810  1.00 19.87 ? 13  HIS A ND1  1 
ATOM   94   C CD2  . HIS A 1 13  ? 9.834   19.643 21.831  1.00 19.36 ? 13  HIS A CD2  1 
ATOM   95   C CE1  . HIS A 1 13  ? 10.346  17.540 22.189  1.00 19.86 ? 13  HIS A CE1  1 
ATOM   96   N NE2  . HIS A 1 13  ? 9.483   18.337 21.585  1.00 24.58 ? 13  HIS A NE2  1 
ATOM   97   N N    . GLY A 1 14  ? 10.407  19.450 25.988  1.00 15.33 ? 14  GLY A N    1 
ATOM   98   C CA   . GLY A 1 14  ? 10.534  18.366 26.943  1.00 17.49 ? 14  GLY A CA   1 
ATOM   99   C C    . GLY A 1 14  ? 9.559   17.244 26.655  1.00 19.50 ? 14  GLY A C    1 
ATOM   100  O O    . GLY A 1 14  ? 8.806   17.283 25.680  1.00 16.80 ? 14  GLY A O    1 
ATOM   101  N N    . ARG A 1 15  ? 9.570   16.229 27.528  1.00 17.66 ? 15  ARG A N    1 
ATOM   102  C CA   . ARG A 1 15  ? 8.703   15.070 27.341  1.00 17.44 ? 15  ARG A CA   1 
ATOM   103  C C    . ARG A 1 15  ? 7.877   14.727 28.584  1.00 16.93 ? 15  ARG A C    1 
ATOM   104  O O    . ARG A 1 15  ? 7.233   13.676 28.613  1.00 15.29 ? 15  ARG A O    1 
ATOM   105  C CB   . ARG A 1 15  ? 9.546   13.867 26.892  1.00 21.68 ? 15  ARG A CB   1 
ATOM   106  C CG   . ARG A 1 15  ? 9.956   13.954 25.430  1.00 25.30 ? 15  ARG A CG   1 
ATOM   107  C CD   . ARG A 1 15  ? 11.015  12.906 25.069  1.00 31.96 ? 15  ARG A CD   1 
ATOM   108  N NE   . ARG A 1 15  ? 10.766  12.245 23.794  1.00 38.24 ? 15  ARG A NE   1 
ATOM   109  C CZ   . ARG A 1 15  ? 11.385  12.559 22.661  1.00 41.36 ? 15  ARG A CZ   1 
ATOM   110  N NH1  . ARG A 1 15  ? 12.239  13.572 22.595  1.00 46.43 ? 15  ARG A NH1  1 
ATOM   111  N NH2  . ARG A 1 15  ? 11.139  11.844 21.565  1.00 43.17 ? 15  ARG A NH2  1 
ATOM   112  N N    . HIS A 1 16  ? 7.837   15.602 29.582  1.00 15.72 ? 16  HIS A N    1 
ATOM   113  C CA   . HIS A 1 16  ? 7.057   15.334 30.783  1.00 16.35 ? 16  HIS A CA   1 
ATOM   114  C C    . HIS A 1 16  ? 5.599   15.070 30.453  1.00 18.34 ? 16  HIS A C    1 
ATOM   115  O O    . HIS A 1 16  ? 5.029   15.676 29.540  1.00 15.81 ? 16  HIS A O    1 
ATOM   116  C CB   . HIS A 1 16  ? 7.176   16.518 31.740  1.00 17.35 ? 16  HIS A CB   1 
ATOM   117  C CG   . HIS A 1 16  ? 8.563   17.055 31.826  1.00 20.66 ? 16  HIS A CG   1 
ATOM   118  N ND1  . HIS A 1 16  ? 9.586   16.371 32.452  1.00 18.18 ? 16  HIS A ND1  1 
ATOM   119  C CD2  . HIS A 1 16  ? 9.120   18.169 31.298  1.00 15.94 ? 16  HIS A CD2  1 
ATOM   120  C CE1  . HIS A 1 16  ? 10.700  17.074 32.351  1.00 16.32 ? 16  HIS A CE1  1 
ATOM   121  N NE2  . HIS A 1 16  ? 10.446  18.163 31.648  1.00 15.60 ? 16  HIS A NE2  1 
ATOM   122  N N    . GLY A 1 17  ? 4.989   14.171 31.217  1.00 23.21 ? 17  GLY A N    1 
ATOM   123  C CA   . GLY A 1 17  ? 3.586   13.850 31.034  1.00 17.84 ? 17  GLY A CA   1 
ATOM   124  C C    . GLY A 1 17  ? 3.166   12.571 31.729  1.00 20.28 ? 17  GLY A C    1 
ATOM   125  O O    . GLY A 1 17  ? 3.948   11.619 31.850  1.00 17.61 ? 17  GLY A O    1 
ATOM   126  N N    . VAL A 1 18  ? 1.918   12.545 32.198  1.00 17.78 ? 18  VAL A N    1 
ATOM   127  C CA   . VAL A 1 18  ? 1.409   11.334 32.836  1.00 19.93 ? 18  VAL A CA   1 
ATOM   128  C C    . VAL A 1 18  ? 1.229   10.225 31.820  1.00 23.02 ? 18  VAL A C    1 
ATOM   129  O O    . VAL A 1 18  ? 1.418   9.047  32.155  1.00 18.62 ? 18  VAL A O    1 
ATOM   130  C CB   . VAL A 1 18  ? 0.097   11.621 33.593  1.00 23.06 ? 18  VAL A CB   1 
ATOM   131  C CG1  . VAL A 1 18  ? -0.513  10.325 34.143  1.00 25.47 ? 18  VAL A CG1  1 
ATOM   132  C CG2  . VAL A 1 18  ? 0.357   12.563 34.740  1.00 22.20 ? 18  VAL A CG2  1 
ATOM   133  N N    . TYR A 1 19  ? 0.894   10.564 30.567  1.00 19.99 ? 19  TYR A N    1 
ATOM   134  C CA   . TYR A 1 19  ? 0.418   9.581  29.596  1.00 25.13 ? 19  TYR A CA   1 
ATOM   135  C C    . TYR A 1 19  ? 1.479   9.241  28.553  1.00 23.60 ? 19  TYR A C    1 
ATOM   136  O O    . TYR A 1 19  ? 2.204   10.116 28.061  1.00 22.83 ? 19  TYR A O    1 
ATOM   137  C CB   . TYR A 1 19  ? -0.871  10.063 28.908  1.00 25.22 ? 19  TYR A CB   1 
ATOM   138  C CG   . TYR A 1 19  ? -2.006  10.186 29.895  1.00 28.38 ? 19  TYR A CG   1 
ATOM   139  C CD1  . TYR A 1 19  ? -2.685  9.061  30.337  1.00 32.56 ? 19  TYR A CD1  1 
ATOM   140  C CD2  . TYR A 1 19  ? -2.375  11.418 30.411  1.00 33.61 ? 19  TYR A CD2  1 
ATOM   141  C CE1  . TYR A 1 19  ? -3.716  9.159  31.250  1.00 42.66 ? 19  TYR A CE1  1 
ATOM   142  C CE2  . TYR A 1 19  ? -3.405  11.527 31.332  1.00 32.13 ? 19  TYR A CE2  1 
ATOM   143  C CZ   . TYR A 1 19  ? -4.069  10.396 31.748  1.00 34.78 ? 19  TYR A CZ   1 
ATOM   144  O OH   . TYR A 1 19  ? -5.091  10.503 32.662  1.00 45.62 ? 19  TYR A OH   1 
ATOM   145  N N    . ASP A 1 20  ? 1.541   7.949  28.220  1.00 23.65 ? 20  ASP A N    1 
ATOM   146  C CA   . ASP A 1 20  ? 2.559   7.433  27.312  1.00 29.19 ? 20  ASP A CA   1 
ATOM   147  C C    . ASP A 1 20  ? 2.670   8.289  26.061  1.00 23.40 ? 20  ASP A C    1 
ATOM   148  O O    . ASP A 1 20  ? 3.772   8.647  25.633  1.00 29.55 ? 20  ASP A O    1 
ATOM   149  C CB   . ASP A 1 20  ? 2.229   5.987  26.934  1.00 24.92 ? 20  ASP A CB   1 
ATOM   150  C CG   . ASP A 1 20  ? 2.578   4.989  28.035  1.00 36.40 ? 20  ASP A CG   1 
ATOM   151  O OD1  . ASP A 1 20  ? 3.152   5.398  29.068  1.00 31.50 ? 20  ASP A OD1  1 
ATOM   152  O OD2  . ASP A 1 20  ? 2.272   3.789  27.856  1.00 33.58 ? 20  ASP A OD2  1 
ATOM   153  N N    . HIS A 1 21  ? 1.530   8.624  25.458  1.00 22.31 ? 21  HIS A N    1 
ATOM   154  C CA   . HIS A 1 21  ? 1.546   9.296  24.171  1.00 25.56 ? 21  HIS A CA   1 
ATOM   155  C C    . HIS A 1 21  ? 2.253   10.647 24.226  1.00 30.99 ? 21  HIS A C    1 
ATOM   156  O O    . HIS A 1 21  ? 2.745   11.115 23.188  1.00 26.18 ? 21  HIS A O    1 
ATOM   157  C CB   . HIS A 1 21  ? 0.115   9.433  23.652  1.00 22.99 ? 21  HIS A CB   1 
ATOM   158  C CG   . HIS A 1 21  ? -0.634  10.595 24.229  1.00 22.10 ? 21  HIS A CG   1 
ATOM   159  N ND1  . HIS A 1 21  ? -0.590  11.863 23.687  1.00 26.29 ? 21  HIS A ND1  1 
ATOM   160  C CD2  . HIS A 1 21  ? -1.461  10.675 25.298  1.00 21.21 ? 21  HIS A CD2  1 
ATOM   161  C CE1  . HIS A 1 21  ? -1.346  12.673 24.402  1.00 22.24 ? 21  HIS A CE1  1 
ATOM   162  N NE2  . HIS A 1 21  ? -1.889  11.977 25.385  1.00 26.30 ? 21  HIS A NE2  1 
ATOM   163  N N    . GLU A 1 22  ? 2.330   11.257 25.416  1.00 25.26 ? 22  GLU A N    1 
ATOM   164  C CA   . GLU A 1 22  ? 3.015   12.527 25.622  1.00 22.60 ? 22  GLU A CA   1 
ATOM   165  C C    . GLU A 1 22  ? 4.523   12.393 25.572  1.00 25.52 ? 22  GLU A C    1 
ATOM   166  O O    . GLU A 1 22  ? 5.218   13.403 25.431  1.00 25.15 ? 22  GLU A O    1 
ATOM   167  C CB   . GLU A 1 22  ? 2.639   13.101 26.984  1.00 21.72 ? 22  GLU A CB   1 
ATOM   168  C CG   . GLU A 1 22  ? 1.221   13.614 27.056  1.00 20.70 ? 22  GLU A CG   1 
ATOM   169  C CD   . GLU A 1 22  ? 0.943   14.345 28.350  1.00 26.34 ? 22  GLU A CD   1 
ATOM   170  O OE1  . GLU A 1 22  ? 1.230   15.559 28.407  1.00 24.61 ? 22  GLU A OE1  1 
ATOM   171  O OE2  . GLU A 1 22  ? 0.434   13.707 29.301  1.00 28.80 ? 22  GLU A OE2  1 
ATOM   172  N N    . ARG A 1 23  ? 5.048   11.188 25.730  1.00 24.37 ? 23  ARG A N    1 
ATOM   173  C CA   . ARG A 1 23  ? 6.486   11.004 25.838  1.00 26.20 ? 23  ARG A CA   1 
ATOM   174  C C    . ARG A 1 23  ? 7.103   10.473 24.555  1.00 24.63 ? 23  ARG A C    1 
ATOM   175  O O    . ARG A 1 23  ? 8.316   10.259 24.514  1.00 30.52 ? 23  ARG A O    1 
ATOM   176  C CB   . ARG A 1 23  ? 6.798   10.076 27.025  1.00 30.45 ? 23  ARG A CB   1 
ATOM   177  C CG   . ARG A 1 23  ? 6.334   10.702 28.341  1.00 40.17 ? 23  ARG A CG   1 
ATOM   178  C CD   . ARG A 1 23  ? 6.047   9.705  29.456  1.00 36.57 ? 23  ARG A CD   1 
ATOM   179  N NE   . ARG A 1 23  ? 7.269   9.175  30.051  1.00 34.52 ? 23  ARG A NE   1 
ATOM   180  C CZ   . ARG A 1 23  ? 7.644   9.399  31.305  1.00 30.32 ? 23  ARG A CZ   1 
ATOM   181  N NH1  . ARG A 1 23  ? 6.964   10.214 32.099  1.00 20.00 ? 23  ARG A NH1  1 
ATOM   182  N NH2  . ARG A 1 23  ? 8.726   8.789  31.776  1.00 27.89 ? 23  ARG A NH2  1 
ATOM   183  N N    . VAL A 1 24  ? 6.300   10.267 23.505  1.00 26.44 ? 24  VAL A N    1 
ATOM   184  C CA   . VAL A 1 24  ? 6.847   9.809  22.231  1.00 28.06 ? 24  VAL A CA   1 
ATOM   185  C C    . VAL A 1 24  ? 7.626   10.934 21.560  1.00 26.55 ? 24  VAL A C    1 
ATOM   186  O O    . VAL A 1 24  ? 8.798   10.777 21.207  1.00 25.80 ? 24  VAL A O    1 
ATOM   187  C CB   . VAL A 1 24  ? 5.728   9.271  21.318  1.00 29.53 ? 24  VAL A CB   1 
ATOM   188  C CG1  . VAL A 1 24  ? 6.284   8.874  19.939  1.00 20.74 ? 24  VAL A CG1  1 
ATOM   189  C CG2  . VAL A 1 24  ? 5.035   8.070  21.968  1.00 26.26 ? 24  VAL A CG2  1 
ATOM   190  N N    . ALA A 1 25  ? 6.982   12.093 21.390  1.00 19.72 ? 25  ALA A N    1 
ATOM   191  C CA   . ALA A 1 25  ? 7.595   13.260 20.770  1.00 23.01 ? 25  ALA A CA   1 
ATOM   192  C C    . ALA A 1 25  ? 7.761   14.449 21.709  1.00 24.47 ? 25  ALA A C    1 
ATOM   193  O O    . ALA A 1 25  ? 8.620   15.297 21.448  1.00 22.07 ? 25  ALA A O    1 
ATOM   194  C CB   . ALA A 1 25  ? 6.773   13.708 19.550  1.00 21.42 ? 25  ALA A CB   1 
ATOM   195  N N    . GLY A 1 26  ? 6.968   14.541 22.785  1.00 22.35 ? 26  GLY A N    1 
ATOM   196  C CA   . GLY A 1 26  ? 7.127   15.638 23.728  1.00 17.84 ? 26  GLY A CA   1 
ATOM   197  C C    . GLY A 1 26  ? 6.472   16.912 23.220  1.00 19.94 ? 26  GLY A C    1 
ATOM   198  O O    . GLY A 1 26  ? 5.755   16.913 22.228  1.00 14.19 ? 26  GLY A O    1 
ATOM   199  N N    . GLN A 1 27  ? 6.732   18.016 23.915  1.00 15.62 ? 27  GLN A N    1 
ATOM   200  C CA   . GLN A 1 27  ? 6.000   19.245 23.635  1.00 15.66 ? 27  GLN A CA   1 
ATOM   201  C C    . GLN A 1 27  ? 6.763   20.419 24.244  1.00 17.31 ? 27  GLN A C    1 
ATOM   202  O O    . GLN A 1 27  ? 7.807   20.248 24.883  1.00 15.23 ? 27  GLN A O    1 
ATOM   203  C CB   . GLN A 1 27  ? 4.574   19.161 24.171  1.00 14.76 ? 27  GLN A CB   1 
ATOM   204  C CG   . GLN A 1 27  ? 4.534   19.097 25.704  1.00 15.24 ? 27  GLN A CG   1 
ATOM   205  C CD   . GLN A 1 27  ? 3.185   18.679 26.231  1.00 20.40 ? 27  GLN A CD   1 
ATOM   206  O OE1  . GLN A 1 27  ? 2.239   19.481 26.308  1.00 17.53 ? 27  GLN A OE1  1 
ATOM   207  N NE2  . GLN A 1 27  ? 3.075   17.399 26.584  1.00 18.65 ? 27  GLN A NE2  1 
ATOM   208  N N    . ARG A 1 28  ? 6.232   21.616 24.022  1.00 16.23 ? 28  ARG A N    1 
ATOM   209  C CA   . ARG A 1 28  ? 6.835   22.851 24.509  1.00 17.47 ? 28  ARG A CA   1 
ATOM   210  C C    . ARG A 1 28  ? 6.493   23.096 25.971  1.00 20.10 ? 28  ARG A C    1 
ATOM   211  O O    . ARG A 1 28  ? 5.316   23.072 26.359  1.00 15.33 ? 28  ARG A O    1 
ATOM   212  C CB   . ARG A 1 28  ? 6.326   24.035 23.690  1.00 19.73 ? 28  ARG A CB   1 
ATOM   213  C CG   . ARG A 1 28  ? 6.826   25.392 24.159  1.00 27.45 ? 28  ARG A CG   1 
ATOM   214  C CD   . ARG A 1 28  ? 6.663   26.366 23.004  1.00 28.58 ? 28  ARG A CD   1 
ATOM   215  N NE   . ARG A 1 28  ? 7.255   25.759 21.820  1.00 36.19 ? 28  ARG A NE   1 
ATOM   216  C CZ   . ARG A 1 28  ? 6.772   25.851 20.588  1.00 31.35 ? 28  ARG A CZ   1 
ATOM   217  N NH1  . ARG A 1 28  ? 5.653   26.517 20.324  1.00 34.85 ? 28  ARG A NH1  1 
ATOM   218  N NH2  . ARG A 1 28  ? 7.412   25.235 19.601  1.00 24.90 ? 28  ARG A NH2  1 
ATOM   219  N N    . PHE A 1 29  ? 7.509   23.425 26.755  1.00 14.53 ? 29  PHE A N    1 
ATOM   220  C CA   . PHE A 1 29  ? 7.346   23.864 28.125  1.00 14.79 ? 29  PHE A CA   1 
ATOM   221  C C    . PHE A 1 29  ? 7.881   25.282 28.256  1.00 15.92 ? 29  PHE A C    1 
ATOM   222  O O    . PHE A 1 29  ? 8.797   25.677 27.534  1.00 16.54 ? 29  PHE A O    1 
ATOM   223  C CB   . PHE A 1 29  ? 8.071   22.900 29.060  1.00 14.83 ? 29  PHE A CB   1 
ATOM   224  C CG   . PHE A 1 29  ? 7.425   21.545 29.095  1.00 13.96 ? 29  PHE A CG   1 
ATOM   225  C CD1  . PHE A 1 29  ? 7.769   20.583 28.162  1.00 13.38 ? 29  PHE A CD1  1 
ATOM   226  C CD2  . PHE A 1 29  ? 6.455   21.247 30.026  1.00 13.11 ? 29  PHE A CD2  1 
ATOM   227  C CE1  . PHE A 1 29  ? 7.147   19.340 28.174  1.00 14.25 ? 29  PHE A CE1  1 
ATOM   228  C CE2  . PHE A 1 29  ? 5.849   20.010 30.044  1.00 15.32 ? 29  PHE A CE2  1 
ATOM   229  C CZ   . PHE A 1 29  ? 6.197   19.060 29.111  1.00 16.13 ? 29  PHE A CZ   1 
ATOM   230  N N    . VAL A 1 30  ? 7.277   26.060 29.147  1.00 11.34 ? 30  VAL A N    1 
ATOM   231  C CA   . VAL A 1 30  ? 7.683   27.449 29.378  1.00 14.76 ? 30  VAL A CA   1 
ATOM   232  C C    . VAL A 1 30  ? 7.847   27.645 30.878  1.00 14.56 ? 30  VAL A C    1 
ATOM   233  O O    . VAL A 1 30  ? 6.948   27.290 31.646  1.00 15.97 ? 30  VAL A O    1 
ATOM   234  C CB   . VAL A 1 30  ? 6.651   28.447 28.811  1.00 16.18 ? 30  VAL A CB   1 
ATOM   235  C CG1  . VAL A 1 30  ? 7.048   29.889 29.141  1.00 15.06 ? 30  VAL A CG1  1 
ATOM   236  C CG2  . VAL A 1 30  ? 6.492   28.230 27.316  1.00 15.81 ? 30  VAL A CG2  1 
ATOM   237  N N    . ILE A 1 31  ? 9.013   28.162 31.298  1.00 16.27 ? 31  ILE A N    1 
ATOM   238  C CA   . ILE A 1 31  ? 9.372   28.295 32.718  1.00 14.00 ? 31  ILE A CA   1 
ATOM   239  C C    . ILE A 1 31  ? 9.510   29.766 33.075  1.00 13.06 ? 31  ILE A C    1 
ATOM   240  O O    . ILE A 1 31  ? 10.163  30.531 32.354  1.00 11.63 ? 31  ILE A O    1 
ATOM   241  C CB   . ILE A 1 31  ? 10.694  27.571 33.084  1.00 14.15 ? 31  ILE A CB   1 
ATOM   242  C CG1  . ILE A 1 31  ? 10.717  26.076 32.732  1.00 22.05 ? 31  ILE A CG1  1 
ATOM   243  C CG2  . ILE A 1 31  ? 11.088  27.830 34.571  1.00 16.23 ? 31  ILE A CG2  1 
ATOM   244  C CD1  . ILE A 1 31  ? 9.388   25.339 32.779  1.00 20.65 ? 31  ILE A CD1  1 
ATOM   245  N N    . ASP A 1 32  ? 8.942   30.148 34.210  1.00 13.64 ? 32  ASP A N    1 
ATOM   246  C CA   . ASP A 1 32  ? 9.233   31.413 34.873  1.00 14.17 ? 32  ASP A CA   1 
ATOM   247  C C    . ASP A 1 32  ? 9.921   31.108 36.190  1.00 14.43 ? 32  ASP A C    1 
ATOM   248  O O    . ASP A 1 32  ? 9.553   30.138 36.863  1.00 17.79 ? 32  ASP A O    1 
ATOM   249  C CB   . ASP A 1 32  ? 7.964   32.223 35.184  1.00 13.95 ? 32  ASP A CB   1 
ATOM   250  C CG   . ASP A 1 32  ? 7.117   32.508 33.973  1.00 17.74 ? 32  ASP A CG   1 
ATOM   251  O OD1  . ASP A 1 32  ? 7.663   32.668 32.847  1.00 16.40 ? 32  ASP A OD1  1 
ATOM   252  O OD2  . ASP A 1 32  ? 5.886   32.571 34.167  1.00 19.24 ? 32  ASP A OD2  1 
ATOM   253  N N    . VAL A 1 33  ? 10.897  31.921 36.575  1.00 16.55 ? 33  VAL A N    1 
ATOM   254  C CA   . VAL A 1 33  ? 11.519  31.807 37.891  1.00 15.42 ? 33  VAL A CA   1 
ATOM   255  C C    . VAL A 1 33  ? 11.566  33.190 38.509  1.00 19.22 ? 33  VAL A C    1 
ATOM   256  O O    . VAL A 1 33  ? 11.975  34.146 37.846  1.00 16.46 ? 33  VAL A O    1 
ATOM   257  C CB   . VAL A 1 33  ? 12.936  31.207 37.834  1.00 18.71 ? 33  VAL A CB   1 
ATOM   258  C CG1  . VAL A 1 33  ? 13.484  31.041 39.263  1.00 17.09 ? 33  VAL A CG1  1 
ATOM   259  C CG2  . VAL A 1 33  ? 12.923  29.871 37.078  1.00 17.50 ? 33  VAL A CG2  1 
ATOM   260  N N    . THR A 1 34  ? 11.132  33.294 39.765  1.00 17.61 ? 34  THR A N    1 
ATOM   261  C CA   . THR A 1 34  ? 11.245  34.513 40.555  1.00 16.02 ? 34  THR A CA   1 
ATOM   262  C C    . THR A 1 34  ? 12.025  34.188 41.819  1.00 16.71 ? 34  THR A C    1 
ATOM   263  O O    . THR A 1 34  ? 11.679  33.243 42.541  1.00 16.44 ? 34  THR A O    1 
ATOM   264  C CB   . THR A 1 34  ? 9.871   35.093 40.906  1.00 17.20 ? 34  THR A CB   1 
ATOM   265  O OG1  . THR A 1 34  ? 9.146   35.384 39.695  1.00 15.83 ? 34  THR A OG1  1 
ATOM   266  C CG2  . THR A 1 34  ? 10.023  36.390 41.703  1.00 17.23 ? 34  THR A CG2  1 
ATOM   267  N N    . VAL A 1 35  ? 13.070  34.966 42.074  1.00 13.93 ? 35  VAL A N    1 
ATOM   268  C CA   . VAL A 1 35  ? 14.004  34.731 43.166  1.00 14.30 ? 35  VAL A CA   1 
ATOM   269  C C    . VAL A 1 35  ? 13.988  35.961 44.057  1.00 22.06 ? 35  VAL A C    1 
ATOM   270  O O    . VAL A 1 35  ? 14.262  37.071 43.588  1.00 18.91 ? 35  VAL A O    1 
ATOM   271  C CB   . VAL A 1 35  ? 15.427  34.453 42.657  1.00 20.23 ? 35  VAL A CB   1 
ATOM   272  C CG1  . VAL A 1 35  ? 16.352  34.077 43.818  1.00 19.91 ? 35  VAL A CG1  1 
ATOM   273  C CG2  . VAL A 1 35  ? 15.423  33.340 41.606  1.00 15.95 ? 35  VAL A CG2  1 
ATOM   274  N N    . TRP A 1 36  ? 13.682  35.770 45.338  1.00 19.99 ? 36  TRP A N    1 
ATOM   275  C CA   . TRP A 1 36  ? 13.732  36.859 46.307  1.00 19.66 ? 36  TRP A CA   1 
ATOM   276  C C    . TRP A 1 36  ? 15.069  36.819 47.038  1.00 22.32 ? 36  TRP A C    1 
ATOM   277  O O    . TRP A 1 36  ? 15.439  35.799 47.642  1.00 19.63 ? 36  TRP A O    1 
ATOM   278  C CB   . TRP A 1 36  ? 12.567  36.794 47.289  1.00 21.04 ? 36  TRP A CB   1 
ATOM   279  C CG   . TRP A 1 36  ? 11.259  37.250 46.699  1.00 24.90 ? 36  TRP A CG   1 
ATOM   280  C CD1  . TRP A 1 36  ? 10.707  38.500 46.792  1.00 24.78 ? 36  TRP A CD1  1 
ATOM   281  C CD2  . TRP A 1 36  ? 10.330  36.455 45.949  1.00 23.45 ? 36  TRP A CD2  1 
ATOM   282  N NE1  . TRP A 1 36  ? 9.497   38.528 46.142  1.00 23.99 ? 36  TRP A NE1  1 
ATOM   283  C CE2  . TRP A 1 36  ? 9.242   37.287 45.619  1.00 20.14 ? 36  TRP A CE2  1 
ATOM   284  C CE3  . TRP A 1 36  ? 10.309  35.116 45.529  1.00 19.44 ? 36  TRP A CE3  1 
ATOM   285  C CZ2  . TRP A 1 36  ? 8.135   36.828 44.884  1.00 22.43 ? 36  TRP A CZ2  1 
ATOM   286  C CZ3  . TRP A 1 36  ? 9.217   34.664 44.794  1.00 19.54 ? 36  TRP A CZ3  1 
ATOM   287  C CH2  . TRP A 1 36  ? 8.138   35.518 44.488  1.00 21.42 ? 36  TRP A CH2  1 
ATOM   288  N N    . ILE A 1 37  ? 15.798  37.929 46.965  1.00 18.41 ? 37  ILE A N    1 
ATOM   289  C CA   . ILE A 1 37  ? 17.178  37.969 47.430  1.00 25.07 ? 37  ILE A CA   1 
ATOM   290  C C    . ILE A 1 37  ? 17.546  39.431 47.619  1.00 21.93 ? 37  ILE A C    1 
ATOM   291  O O    . ILE A 1 37  ? 17.088  40.296 46.880  1.00 23.44 ? 37  ILE A O    1 
ATOM   292  C CB   . ILE A 1 37  ? 18.121  37.257 46.427  1.00 21.24 ? 37  ILE A CB   1 
ATOM   293  C CG1  . ILE A 1 37  ? 19.580  37.377 46.881  1.00 21.87 ? 37  ILE A CG1  1 
ATOM   294  C CG2  . ILE A 1 37  ? 17.943  37.838 45.016  1.00 24.47 ? 37  ILE A CG2  1 
ATOM   295  C CD1  . ILE A 1 37  ? 20.568  36.696 45.984  1.00 18.98 ? 37  ILE A CD1  1 
ATOM   296  N N    . ASP A 1 38  ? 18.356  39.707 48.631  1.00 22.84 ? 38  ASP A N    1 
ATOM   297  C CA   . ASP A 1 38  ? 18.808  41.074 48.871  1.00 24.06 ? 38  ASP A CA   1 
ATOM   298  C C    . ASP A 1 38  ? 19.825  41.469 47.806  1.00 22.78 ? 38  ASP A C    1 
ATOM   299  O O    . ASP A 1 38  ? 20.870  40.823 47.675  1.00 25.56 ? 38  ASP A O    1 
ATOM   300  C CB   . ASP A 1 38  ? 19.428  41.170 50.260  1.00 29.46 ? 38  ASP A CB   1 
ATOM   301  C CG   . ASP A 1 38  ? 19.505  42.596 50.774  1.00 41.13 ? 38  ASP A CG   1 
ATOM   302  O OD1  . ASP A 1 38  ? 19.733  43.539 49.971  1.00 43.51 ? 38  ASP A OD1  1 
ATOM   303  O OD2  . ASP A 1 38  ? 19.369  42.762 52.005  1.00 44.46 ? 38  ASP A OD2  1 
ATOM   304  N N    . LEU A 1 39  ? 19.547  42.543 47.063  1.00 23.47 ? 39  LEU A N    1 
ATOM   305  C CA   . LEU A 1 39  ? 20.426  42.982 45.983  1.00 26.00 ? 39  LEU A CA   1 
ATOM   306  C C    . LEU A 1 39  ? 21.240  44.233 46.320  1.00 25.72 ? 39  LEU A C    1 
ATOM   307  O O    . LEU A 1 39  ? 21.929  44.770 45.440  1.00 22.04 ? 39  LEU A O    1 
ATOM   308  C CB   . LEU A 1 39  ? 19.605  43.233 44.723  1.00 19.54 ? 39  LEU A CB   1 
ATOM   309  C CG   . LEU A 1 39  ? 18.928  41.944 44.221  1.00 24.42 ? 39  LEU A CG   1 
ATOM   310  C CD1  . LEU A 1 39  ? 18.083  42.230 42.991  1.00 23.98 ? 39  LEU A CD1  1 
ATOM   311  C CD2  . LEU A 1 39  ? 19.986  40.899 43.951  1.00 23.47 ? 39  LEU A CD2  1 
ATOM   312  N N    . ALA A 1 40  ? 21.174  44.720 47.555  1.00 19.63 ? 40  ALA A N    1 
ATOM   313  C CA   . ALA A 1 40  ? 21.879  45.954 47.882  1.00 27.60 ? 40  ALA A CA   1 
ATOM   314  C C    . ALA A 1 40  ? 23.384  45.777 47.744  1.00 30.59 ? 40  ALA A C    1 
ATOM   315  O O    . ALA A 1 40  ? 24.079  46.654 47.216  1.00 25.22 ? 40  ALA A O    1 
ATOM   316  C CB   . ALA A 1 40  ? 21.513  46.408 49.292  1.00 24.52 ? 40  ALA A CB   1 
ATOM   317  N N    . GLU A 1 41  ? 23.908  44.641 48.202  1.00 25.66 ? 41  GLU A N    1 
ATOM   318  C CA   . GLU A 1 41  ? 25.352  44.456 48.185  1.00 24.50 ? 41  GLU A CA   1 
ATOM   319  C C    . GLU A 1 41  ? 25.887  44.498 46.759  1.00 25.58 ? 41  GLU A C    1 
ATOM   320  O O    . GLU A 1 41  ? 26.945  45.086 46.502  1.00 27.78 ? 41  GLU A O    1 
ATOM   321  C CB   . GLU A 1 41  ? 25.718  43.141 48.867  1.00 30.06 ? 41  GLU A CB   1 
ATOM   322  C CG   . GLU A 1 41  ? 27.219  42.945 49.055  1.00 27.42 ? 41  GLU A CG   1 
ATOM   323  C CD   . GLU A 1 41  ? 27.556  41.959 50.167  1.00 42.73 ? 41  GLU A CD   1 
ATOM   324  O OE1  . GLU A 1 41  ? 26.696  41.108 50.500  1.00 48.53 ? 41  GLU A OE1  1 
ATOM   325  O OE2  . GLU A 1 41  ? 28.687  42.033 50.702  1.00 46.23 ? 41  GLU A OE2  1 
ATOM   326  N N    . ALA A 1 42  ? 25.152  43.893 45.816  1.00 24.94 ? 42  ALA A N    1 
ATOM   327  C CA   . ALA A 1 42  ? 25.590  43.845 44.422  1.00 20.06 ? 42  ALA A CA   1 
ATOM   328  C C    . ALA A 1 42  ? 25.566  45.220 43.766  1.00 23.05 ? 42  ALA A C    1 
ATOM   329  O O    . ALA A 1 42  ? 26.383  45.500 42.882  1.00 22.48 ? 42  ALA A O    1 
ATOM   330  C CB   . ALA A 1 42  ? 24.708  42.873 43.647  1.00 20.70 ? 42  ALA A CB   1 
ATOM   331  N N    . ALA A 1 43  ? 24.639  46.092 44.168  1.00 25.66 ? 43  ALA A N    1 
ATOM   332  C CA   . ALA A 1 43  ? 24.666  47.450 43.638  1.00 21.13 ? 43  ALA A CA   1 
ATOM   333  C C    . ALA A 1 43  ? 25.852  48.225 44.193  1.00 26.33 ? 43  ALA A C    1 
ATOM   334  O O    . ALA A 1 43  ? 26.401  49.090 43.509  1.00 29.02 ? 43  ALA A O    1 
ATOM   335  C CB   . ALA A 1 43  ? 23.355  48.164 43.943  1.00 26.49 ? 43  ALA A CB   1 
ATOM   336  N N    . ASN A 1 44  ? 26.287  47.904 45.409  1.00 28.42 ? 44  ASN A N    1 
ATOM   337  C CA   . ASN A 1 44  ? 27.481  48.534 45.961  1.00 29.09 ? 44  ASN A CA   1 
ATOM   338  C C    . ASN A 1 44  ? 28.745  48.077 45.244  1.00 30.54 ? 44  ASN A C    1 
ATOM   339  O O    . ASN A 1 44  ? 29.628  48.889 44.933  1.00 29.88 ? 44  ASN A O    1 
ATOM   340  C CB   . ASN A 1 44  ? 27.600  48.232 47.448  1.00 34.04 ? 44  ASN A CB   1 
ATOM   341  C CG   . ASN A 1 44  ? 28.604  49.134 48.132  1.00 44.01 ? 44  ASN A CG   1 
ATOM   342  O OD1  . ASN A 1 44  ? 28.655  50.338 47.863  1.00 37.91 ? 44  ASN A OD1  1 
ATOM   343  N ND2  . ASN A 1 44  ? 29.447  48.549 48.986  1.00 44.20 ? 44  ASN A ND2  1 
ATOM   344  N N    . SER A 1 45  ? 28.879  46.775 45.024  1.00 28.58 ? 45  SER A N    1 
ATOM   345  C CA   . SER A 1 45  ? 30.101  46.238 44.454  1.00 23.92 ? 45  SER A CA   1 
ATOM   346  C C    . SER A 1 45  ? 30.088  46.246 42.941  1.00 22.36 ? 45  SER A C    1 
ATOM   347  O O    . SER A 1 45  ? 31.158  46.243 42.322  1.00 26.07 ? 45  SER A O    1 
ATOM   348  C CB   . SER A 1 45  ? 30.310  44.801 44.920  1.00 30.66 ? 45  SER A CB   1 
ATOM   349  O OG   . SER A 1 45  ? 29.240  43.997 44.457  1.00 23.18 ? 45  SER A OG   1 
ATOM   350  N N    . ASP A 1 46  ? 28.900  46.245 42.345  1.00 22.64 ? 46  ASP A N    1 
ATOM   351  C CA   . ASP A 1 46  ? 28.720  46.037 40.912  1.00 21.64 ? 46  ASP A CA   1 
ATOM   352  C C    . ASP A 1 46  ? 29.443  44.770 40.463  1.00 25.36 ? 46  ASP A C    1 
ATOM   353  O O    . ASP A 1 46  ? 29.914  44.669 39.330  1.00 25.76 ? 46  ASP A O    1 
ATOM   354  C CB   . ASP A 1 46  ? 29.158  47.272 40.121  1.00 19.78 ? 46  ASP A CB   1 
ATOM   355  C CG   . ASP A 1 46  ? 28.525  47.334 38.740  1.00 22.13 ? 46  ASP A CG   1 
ATOM   356  O OD1  . ASP A 1 46  ? 27.373  46.879 38.605  1.00 18.11 ? 46  ASP A OD1  1 
ATOM   357  O OD2  . ASP A 1 46  ? 29.141  47.910 37.808  1.00 26.51 ? 46  ASP A OD2  1 
ATOM   358  N N    . ASP A 1 47  ? 29.497  43.786 41.368  1.00 22.91 ? 47  ASP A N    1 
ATOM   359  C CA   . ASP A 1 47  ? 30.200  42.523 41.181  1.00 28.56 ? 47  ASP A CA   1 
ATOM   360  C C    . ASP A 1 47  ? 29.177  41.399 41.042  1.00 21.80 ? 47  ASP A C    1 
ATOM   361  O O    . ASP A 1 47  ? 28.407  41.135 41.973  1.00 23.28 ? 47  ASP A O    1 
ATOM   362  C CB   . ASP A 1 47  ? 31.131  42.262 42.369  1.00 25.15 ? 47  ASP A CB   1 
ATOM   363  C CG   . ASP A 1 47  ? 32.238  41.281 42.052  1.00 37.21 ? 47  ASP A CG   1 
ATOM   364  O OD1  . ASP A 1 47  ? 31.970  40.220 41.429  1.00 39.59 ? 47  ASP A OD1  1 
ATOM   365  O OD2  . ASP A 1 47  ? 33.392  41.582 42.430  1.00 45.36 ? 47  ASP A OD2  1 
ATOM   366  N N    . LEU A 1 48  ? 29.181  40.740 39.882  1.00 21.03 ? 48  LEU A N    1 
ATOM   367  C CA   . LEU A 1 48  ? 28.283  39.617 39.632  1.00 23.46 ? 48  LEU A CA   1 
ATOM   368  C C    . LEU A 1 48  ? 28.319  38.575 40.750  1.00 24.90 ? 48  LEU A C    1 
ATOM   369  O O    . LEU A 1 48  ? 27.291  37.958 41.067  1.00 22.06 ? 48  LEU A O    1 
ATOM   370  C CB   . LEU A 1 48  ? 28.655  38.981 38.294  1.00 28.48 ? 48  LEU A CB   1 
ATOM   371  C CG   . LEU A 1 48  ? 27.926  37.707 37.911  1.00 21.76 ? 48  LEU A CG   1 
ATOM   372  C CD1  . LEU A 1 48  ? 26.441  38.000 37.687  1.00 17.45 ? 48  LEU A CD1  1 
ATOM   373  C CD2  . LEU A 1 48  ? 28.539  37.125 36.662  1.00 25.77 ? 48  LEU A CD2  1 
ATOM   374  N N    . ALA A 1 49  ? 29.489  38.358 41.360  1.00 21.50 ? 49  ALA A N    1 
ATOM   375  C CA   . ALA A 1 49  ? 29.587  37.398 42.457  1.00 25.02 ? 49  ALA A CA   1 
ATOM   376  C C    . ALA A 1 49  ? 28.662  37.742 43.624  1.00 30.13 ? 49  ALA A C    1 
ATOM   377  O O    . ALA A 1 49  ? 28.303  36.847 44.397  1.00 26.02 ? 49  ALA A O    1 
ATOM   378  C CB   . ALA A 1 49  ? 31.031  37.301 42.946  1.00 26.25 ? 49  ALA A CB   1 
ATOM   379  N N    . ASP A 1 50  ? 28.244  38.999 43.756  1.00 26.05 ? 50  ASP A N    1 
ATOM   380  C CA   . ASP A 1 50  ? 27.379  39.416 44.852  1.00 20.71 ? 50  ASP A CA   1 
ATOM   381  C C    . ASP A 1 50  ? 25.891  39.301 44.537  1.00 20.90 ? 50  ASP A C    1 
ATOM   382  O O    . ASP A 1 50  ? 25.056  39.650 45.376  1.00 21.99 ? 50  ASP A O    1 
ATOM   383  C CB   . ASP A 1 50  ? 27.731  40.841 45.285  1.00 23.02 ? 50  ASP A CB   1 
ATOM   384  C CG   . ASP A 1 50  ? 29.078  40.905 46.014  1.00 25.26 ? 50  ASP A CG   1 
ATOM   385  O OD1  . ASP A 1 50  ? 29.409  39.917 46.704  1.00 24.53 ? 50  ASP A OD1  1 
ATOM   386  O OD2  . ASP A 1 50  ? 29.805  41.917 45.894  1.00 26.46 ? 50  ASP A OD2  1 
ATOM   387  N N    . THR A 1 51  ? 25.528  38.805 43.363  1.00 20.18 ? 51  THR A N    1 
ATOM   388  C CA   . THR A 1 51  ? 24.132  38.552 43.075  1.00 20.47 ? 51  THR A CA   1 
ATOM   389  C C    . THR A 1 51  ? 23.975  37.119 42.590  1.00 22.27 ? 51  THR A C    1 
ATOM   390  O O    . THR A 1 51  ? 24.934  36.341 42.552  1.00 19.04 ? 51  THR A O    1 
ATOM   391  C CB   . THR A 1 51  ? 23.578  39.564 42.061  1.00 20.44 ? 51  THR A CB   1 
ATOM   392  O OG1  . THR A 1 51  ? 22.153  39.427 41.985  1.00 18.46 ? 51  THR A OG1  1 
ATOM   393  C CG2  . THR A 1 51  ? 24.193  39.379 40.682  1.00 19.72 ? 51  THR A CG2  1 
ATOM   394  N N    . TYR A 1 52  ? 22.733  36.768 42.266  1.00 21.52 ? 52  TYR A N    1 
ATOM   395  C CA   . TYR A 1 52  ? 22.384  35.462 41.719  1.00 22.98 ? 52  TYR A CA   1 
ATOM   396  C C    . TYR A 1 52  ? 22.377  35.578 40.201  1.00 20.77 ? 52  TYR A C    1 
ATOM   397  O O    . TYR A 1 52  ? 21.533  36.278 39.629  1.00 18.13 ? 52  TYR A O    1 
ATOM   398  C CB   . TYR A 1 52  ? 21.021  35.021 42.243  1.00 20.34 ? 52  TYR A CB   1 
ATOM   399  C CG   . TYR A 1 52  ? 20.738  33.556 42.078  1.00 20.29 ? 52  TYR A CG   1 
ATOM   400  C CD1  . TYR A 1 52  ? 21.335  32.614 42.909  1.00 26.00 ? 52  TYR A CD1  1 
ATOM   401  C CD2  . TYR A 1 52  ? 19.857  33.111 41.110  1.00 23.87 ? 52  TYR A CD2  1 
ATOM   402  C CE1  . TYR A 1 52  ? 21.067  31.262 42.765  1.00 24.57 ? 52  TYR A CE1  1 
ATOM   403  C CE2  . TYR A 1 52  ? 19.584  31.771 40.960  1.00 24.55 ? 52  TYR A CE2  1 
ATOM   404  C CZ   . TYR A 1 52  ? 20.198  30.848 41.782  1.00 23.51 ? 52  TYR A CZ   1 
ATOM   405  O OH   . TYR A 1 52  ? 19.922  29.511 41.613  1.00 23.26 ? 52  TYR A OH   1 
ATOM   406  N N    . ASP A 1 53  ? 23.314  34.890 39.558  1.00 16.53 ? 53  ASP A N    1 
ATOM   407  C CA   . ASP A 1 53  ? 23.559  34.992 38.122  1.00 16.72 ? 53  ASP A CA   1 
ATOM   408  C C    . ASP A 1 53  ? 22.393  34.412 37.326  1.00 17.54 ? 53  ASP A C    1 
ATOM   409  O O    . ASP A 1 53  ? 22.161  33.200 37.349  1.00 19.47 ? 53  ASP A O    1 
ATOM   410  C CB   . ASP A 1 53  ? 24.865  34.265 37.811  1.00 17.65 ? 53  ASP A CB   1 
ATOM   411  C CG   . ASP A 1 53  ? 25.328  34.445 36.385  1.00 24.36 ? 53  ASP A CG   1 
ATOM   412  O OD1  . ASP A 1 53  ? 24.636  35.109 35.580  1.00 18.79 ? 53  ASP A OD1  1 
ATOM   413  O OD2  . ASP A 1 53  ? 26.423  33.925 36.075  1.00 27.48 ? 53  ASP A OD2  1 
ATOM   414  N N    . TYR A 1 54  ? 21.673  35.261 36.590  1.00 18.69 ? 54  TYR A N    1 
ATOM   415  C CA   A TYR A 1 54  ? 20.557  34.804 35.761  0.47 17.56 ? 54  TYR A CA   1 
ATOM   416  C CA   B TYR A 1 54  ? 20.558  34.733 35.807  0.53 17.97 ? 54  TYR A CA   1 
ATOM   417  C C    . TYR A 1 54  ? 20.999  33.928 34.591  1.00 20.88 ? 54  TYR A C    1 
ATOM   418  O O    . TYR A 1 54  ? 20.167  33.217 34.011  1.00 19.47 ? 54  TYR A O    1 
ATOM   419  C CB   A TYR A 1 54  ? 19.745  36.015 35.267  0.47 20.68 ? 54  TYR A CB   1 
ATOM   420  C CB   B TYR A 1 54  ? 19.597  35.858 35.402  0.53 20.58 ? 54  TYR A CB   1 
ATOM   421  C CG   A TYR A 1 54  ? 20.423  36.930 34.248  0.47 19.74 ? 54  TYR A CG   1 
ATOM   422  C CG   B TYR A 1 54  ? 20.191  37.040 34.665  0.53 20.14 ? 54  TYR A CG   1 
ATOM   423  C CD1  A TYR A 1 54  ? 20.833  36.464 33.004  0.47 21.16 ? 54  TYR A CD1  1 
ATOM   424  C CD1  B TYR A 1 54  ? 20.832  36.908 33.442  0.53 21.18 ? 54  TYR A CD1  1 
ATOM   425  C CD2  A TYR A 1 54  ? 20.608  38.284 34.525  0.47 19.27 ? 54  TYR A CD2  1 
ATOM   426  C CD2  B TYR A 1 54  ? 20.027  38.323 35.179  0.53 20.16 ? 54  TYR A CD2  1 
ATOM   427  C CE1  A TYR A 1 54  ? 21.438  37.309 32.082  0.47 21.56 ? 54  TYR A CE1  1 
ATOM   428  C CE1  B TYR A 1 54  ? 21.350  38.035 32.786  0.53 20.49 ? 54  TYR A CE1  1 
ATOM   429  C CE2  A TYR A 1 54  ? 21.203  39.137 33.604  0.47 19.47 ? 54  TYR A CE2  1 
ATOM   430  C CE2  B TYR A 1 54  ? 20.520  39.427 34.537  0.53 18.51 ? 54  TYR A CE2  1 
ATOM   431  C CZ   A TYR A 1 54  ? 21.619  38.644 32.385  0.47 21.44 ? 54  TYR A CZ   1 
ATOM   432  C CZ   B TYR A 1 54  ? 21.173  39.289 33.343  0.53 19.42 ? 54  TYR A CZ   1 
ATOM   433  O OH   A TYR A 1 54  ? 22.220  39.474 31.455  0.47 20.19 ? 54  TYR A OH   1 
ATOM   434  O OH   B TYR A 1 54  ? 21.643  40.434 32.744  0.53 15.98 ? 54  TYR A OH   1 
ATOM   435  N N    . VAL A 1 55  ? 22.273  33.985 34.207  1.00 18.69 ? 55  VAL A N    1 
ATOM   436  C CA   . VAL A 1 55  ? 22.752  33.137 33.120  1.00 21.58 ? 55  VAL A CA   1 
ATOM   437  C C    . VAL A 1 55  ? 22.797  31.682 33.580  1.00 26.17 ? 55  VAL A C    1 
ATOM   438  O O    . VAL A 1 55  ? 22.325  30.771 32.889  1.00 18.42 ? 55  VAL A O    1 
ATOM   439  C CB   . VAL A 1 55  ? 24.128  33.631 32.633  1.00 22.40 ? 55  VAL A CB   1 
ATOM   440  C CG1  . VAL A 1 55  ? 24.736  32.662 31.646  1.00 26.06 ? 55  VAL A CG1  1 
ATOM   441  C CG2  . VAL A 1 55  ? 23.984  34.983 31.991  1.00 24.22 ? 55  VAL A CG2  1 
ATOM   442  N N    . ARG A 1 56  ? 23.323  31.444 34.775  1.00 21.51 ? 56  ARG A N    1 
ATOM   443  C CA   . ARG A 1 56  ? 23.398  30.077 35.334  1.00 24.63 ? 56  ARG A CA   1 
ATOM   444  C C    . ARG A 1 56  ? 21.985  29.580 35.630  1.00 25.14 ? 56  ARG A C    1 
ATOM   445  O O    . ARG A 1 56  ? 21.718  28.449 35.363  1.00 21.78 ? 56  ARG A O    1 
ATOM   446  C CB   . ARG A 1 56  ? 24.290  30.058 36.575  1.00 27.06 ? 56  ARG A CB   1 
ATOM   447  C CG   . ARG A 1 56  ? 25.770  30.180 36.233  1.00 35.80 ? 56  ARG A CG   1 
ATOM   448  C CD   . ARG A 1 56  ? 26.744  29.273 36.958  1.00 41.56 ? 56  ARG A CD   1 
ATOM   449  N NE   . ARG A 1 56  ? 26.494  29.134 38.386  1.00 48.78 ? 56  ARG A NE   1 
ATOM   450  C CZ   . ARG A 1 56  ? 27.401  28.799 39.302  1.00 53.21 ? 56  ARG A CZ   1 
ATOM   451  N NH1  . ARG A 1 56  ? 28.660  28.580 38.968  1.00 55.59 ? 56  ARG A NH1  1 
ATOM   452  N NH2  . ARG A 1 56  ? 27.044  28.708 40.562  1.00 55.98 ? 56  ARG A NH2  1 
ATOM   453  N N    . LEU A 1 57  ? 21.134  30.452 36.141  1.00 22.67 ? 57  LEU A N    1 
ATOM   454  C CA   . LEU A 1 57  ? 19.761  30.062 36.435  1.00 18.95 ? 57  LEU A CA   1 
ATOM   455  C C    . LEU A 1 57  ? 19.068  29.558 35.179  1.00 21.21 ? 57  LEU A C    1 
ATOM   456  O O    . LEU A 1 57  ? 18.417  28.506 35.193  1.00 17.60 ? 57  LEU A O    1 
ATOM   457  C CB   . LEU A 1 57  ? 18.999  31.256 37.016  1.00 20.26 ? 57  LEU A CB   1 
ATOM   458  C CG   . LEU A 1 57  ? 17.485  31.098 37.251  1.00 19.84 ? 57  LEU A CG   1 
ATOM   459  C CD1  . LEU A 1 57  ? 17.173  29.989 38.284  1.00 20.26 ? 57  LEU A CD1  1 
ATOM   460  C CD2  . LEU A 1 57  ? 16.833  32.412 37.660  1.00 20.36 ? 57  LEU A CD2  1 
ATOM   461  N N    . ALA A 1 58  ? 19.182  30.305 34.077  1.00 16.99 ? 58  ALA A N    1 
ATOM   462  C CA   . ALA A 1 58  ? 18.492  29.884 32.855  1.00 20.66 ? 58  ALA A CA   1 
ATOM   463  C C    . ALA A 1 58  ? 19.030  28.549 32.347  1.00 19.80 ? 58  ALA A C    1 
ATOM   464  O O    . ALA A 1 58  ? 18.255  27.668 31.967  1.00 20.75 ? 58  ALA A O    1 
ATOM   465  C CB   . ALA A 1 58  ? 18.601  30.954 31.769  1.00 18.09 ? 58  ALA A CB   1 
ATOM   466  N N    . SER A 1 59  ? 20.352  28.369 32.343  1.00 18.38 ? 59  SER A N    1 
ATOM   467  C CA   . SER A 1 59  ? 20.885  27.106 31.839  1.00 21.87 ? 59  SER A CA   1 
ATOM   468  C C    . SER A 1 59  ? 20.474  25.931 32.727  1.00 21.01 ? 59  SER A C    1 
ATOM   469  O O    . SER A 1 59  ? 20.129  24.858 32.220  1.00 22.17 ? 59  SER A O    1 
ATOM   470  C CB   . SER A 1 59  ? 22.403  27.187 31.717  1.00 26.16 ? 59  SER A CB   1 
ATOM   471  O OG   . SER A 1 59  ? 23.010  27.007 32.984  1.00 36.31 ? 59  SER A OG   1 
ATOM   472  N N    . ARG A 1 60  ? 20.494  26.118 34.032  1.00 17.79 ? 60  ARG A N    1 
ATOM   473  C CA   . ARG A 1 60  ? 20.138  25.041 34.979  1.00 19.46 ? 60  ARG A CA   1 
ATOM   474  C C    . ARG A 1 60  ? 18.649  24.714 34.820  1.00 20.04 ? 60  ARG A C    1 
ATOM   475  O O    . ARG A 1 60  ? 18.326  23.579 34.686  1.00 21.04 ? 60  ARG A O    1 
ATOM   476  C CB   . ARG A 1 60  ? 20.518  25.478 36.389  1.00 21.49 ? 60  ARG A CB   1 
ATOM   477  C CG   . ARG A 1 60  ? 21.999  25.351 36.723  1.00 29.14 ? 60  ARG A CG   1 
ATOM   478  C CD   . ARG A 1 60  ? 23.197  25.406 35.758  1.00 44.26 ? 60  ARG A CD   1 
ATOM   479  N NE   . ARG A 1 60  ? 23.450  24.372 34.746  1.00 32.48 ? 60  ARG A NE   1 
ATOM   480  N N    . ALA A 1 61  ? 17.797  25.731 34.822  1.00 20.53 ? 61  ALA A N    1 
ATOM   481  C CA   . ALA A 1 61  ? 16.370  25.500 34.629  1.00 17.14 ? 61  ALA A CA   1 
ATOM   482  C C    . ALA A 1 61  ? 16.120  24.748 33.335  1.00 17.95 ? 61  ALA A C    1 
ATOM   483  O O    . ALA A 1 61  ? 15.358  23.775 33.303  1.00 14.83 ? 61  ALA A O    1 
ATOM   484  C CB   . ALA A 1 61  ? 15.617  26.830 34.633  1.00 13.88 ? 61  ALA A CB   1 
ATOM   485  N N    . ALA A 1 62  ? 16.765  25.180 32.251  1.00 14.94 ? 62  ALA A N    1 
ATOM   486  C CA   . ALA A 1 62  ? 16.518  24.551 30.959  1.00 17.34 ? 62  ALA A CA   1 
ATOM   487  C C    . ALA A 1 62  ? 16.979  23.092 30.950  1.00 17.50 ? 62  ALA A C    1 
ATOM   488  O O    . ALA A 1 62  ? 16.310  22.221 30.378  1.00 17.95 ? 62  ALA A O    1 
ATOM   489  C CB   . ALA A 1 62  ? 17.209  25.350 29.860  1.00 19.97 ? 62  ALA A CB   1 
ATOM   490  N N    . GLU A 1 63  ? 18.132  22.809 31.550  1.00 16.69 ? 63  GLU A N    1 
ATOM   491  C CA   . GLU A 1 63  ? 18.627  21.437 31.564  1.00 21.66 ? 63  GLU A CA   1 
ATOM   492  C C    . GLU A 1 63  ? 17.662  20.530 32.308  1.00 16.31 ? 63  GLU A C    1 
ATOM   493  O O    . GLU A 1 63  ? 17.395  19.403 31.880  1.00 17.96 ? 63  GLU A O    1 
ATOM   494  C CB   . GLU A 1 63  ? 20.021  21.399 32.202  1.00 18.35 ? 63  GLU A CB   1 
ATOM   495  C CG   . GLU A 1 63  ? 21.078  22.000 31.301  1.00 21.07 ? 63  GLU A CG   1 
ATOM   496  C CD   . GLU A 1 63  ? 22.417  22.158 31.991  1.00 34.81 ? 63  GLU A CD   1 
ATOM   497  O OE1  . GLU A 1 63  ? 22.536  21.718 33.159  1.00 30.81 ? 63  GLU A OE1  1 
ATOM   498  O OE2  . GLU A 1 63  ? 23.328  22.756 31.374  1.00 29.49 ? 63  GLU A OE2  1 
ATOM   499  N N    . ILE A 1 64  ? 17.102  21.011 33.416  1.00 17.44 ? 64  ILE A N    1 
ATOM   500  C CA   . ILE A 1 64  ? 16.116  20.207 34.139  1.00 17.29 ? 64  ILE A CA   1 
ATOM   501  C C    . ILE A 1 64  ? 14.925  19.907 33.242  1.00 21.26 ? 64  ILE A C    1 
ATOM   502  O O    . ILE A 1 64  ? 14.463  18.757 33.149  1.00 18.14 ? 64  ILE A O    1 
ATOM   503  C CB   . ILE A 1 64  ? 15.686  20.913 35.438  1.00 21.35 ? 64  ILE A CB   1 
ATOM   504  C CG1  . ILE A 1 64  ? 16.830  20.907 36.454  1.00 19.19 ? 64  ILE A CG1  1 
ATOM   505  C CG2  . ILE A 1 64  ? 14.432  20.260 36.033  1.00 17.48 ? 64  ILE A CG2  1 
ATOM   506  C CD1  . ILE A 1 64  ? 16.721  21.990 37.476  1.00 16.55 ? 64  ILE A CD1  1 
ATOM   507  N N    . VAL A 1 65  ? 14.407  20.935 32.566  1.00 14.92 ? 65  VAL A N    1 
ATOM   508  C CA   . VAL A 1 65  ? 13.204  20.754 31.751  1.00 13.46 ? 65  VAL A CA   1 
ATOM   509  C C    . VAL A 1 65  ? 13.481  19.794 30.602  1.00 17.04 ? 65  VAL A C    1 
ATOM   510  O O    . VAL A 1 65  ? 12.641  18.957 30.254  1.00 17.22 ? 65  VAL A O    1 
ATOM   511  C CB   . VAL A 1 65  ? 12.694  22.109 31.223  1.00 16.80 ? 65  VAL A CB   1 
ATOM   512  C CG1  . VAL A 1 65  ? 11.555  21.870 30.251  1.00 14.24 ? 65  VAL A CG1  1 
ATOM   513  C CG2  . VAL A 1 65  ? 12.222  22.985 32.365  1.00 14.28 ? 65  VAL A CG2  1 
ATOM   514  N N    . ALA A 1 66  ? 14.659  19.908 29.990  1.00 15.20 ? 66  ALA A N    1 
ATOM   515  C CA   . ALA A 1 66  ? 15.076  19.051 28.881  1.00 18.70 ? 66  ALA A CA   1 
ATOM   516  C C    . ALA A 1 66  ? 15.469  17.644 29.312  1.00 20.91 ? 66  ALA A C    1 
ATOM   517  O O    . ALA A 1 66  ? 15.698  16.795 28.444  1.00 20.58 ? 66  ALA A O    1 
ATOM   518  C CB   . ALA A 1 66  ? 16.261  19.689 28.143  1.00 17.64 ? 66  ALA A CB   1 
ATOM   519  N N    . GLY A 1 67  ? 15.550  17.371 30.612  1.00 20.94 ? 67  GLY A N    1 
ATOM   520  C CA   . GLY A 1 67  ? 16.115  16.131 31.098  1.00 18.23 ? 67  GLY A CA   1 
ATOM   521  C C    . GLY A 1 67  ? 15.138  14.979 30.962  1.00 21.31 ? 67  GLY A C    1 
ATOM   522  O O    . GLY A 1 67  ? 14.095  15.095 30.311  1.00 19.99 ? 67  GLY A O    1 
ATOM   523  N N    . PRO A 1 68  ? 15.449  13.842 31.575  1.00 18.07 ? 68  PRO A N    1 
ATOM   524  C CA   . PRO A 1 68  ? 14.519  12.707 31.531  1.00 18.59 ? 68  PRO A CA   1 
ATOM   525  C C    . PRO A 1 68  ? 13.162  13.098 32.086  1.00 16.57 ? 68  PRO A C    1 
ATOM   526  O O    . PRO A 1 68  ? 13.073  13.795 33.108  1.00 18.35 ? 68  PRO A O    1 
ATOM   527  C CB   . PRO A 1 68  ? 15.202  11.639 32.401  1.00 17.39 ? 68  PRO A CB   1 
ATOM   528  C CG   . PRO A 1 68  ? 16.669  11.995 32.380  1.00 15.09 ? 68  PRO A CG   1 
ATOM   529  C CD   . PRO A 1 68  ? 16.731  13.514 32.231  1.00 17.74 ? 68  PRO A CD   1 
ATOM   530  N N    . PRO A 1 69  ? 12.078  12.653 31.449  1.00 17.78 ? 69  PRO A N    1 
ATOM   531  C CA   . PRO A 1 69  ? 10.757  13.206 31.767  1.00 15.21 ? 69  PRO A CA   1 
ATOM   532  C C    . PRO A 1 69  ? 10.248  12.806 33.141  1.00 20.20 ? 69  PRO A C    1 
ATOM   533  O O    . PRO A 1 69  ? 10.534  11.717 33.657  1.00 21.12 ? 69  PRO A O    1 
ATOM   534  C CB   . PRO A 1 69  ? 9.858   12.635 30.659  1.00 17.84 ? 69  PRO A CB   1 
ATOM   535  C CG   . PRO A 1 69  ? 10.579  11.413 30.174  1.00 17.83 ? 69  PRO A CG   1 
ATOM   536  C CD   . PRO A 1 69  ? 12.035  11.774 30.267  1.00 18.88 ? 69  PRO A CD   1 
ATOM   537  N N    . ARG A 1 70  ? 9.474   13.720 33.725  1.00 16.73 ? 70  ARG A N    1 
ATOM   538  C CA   . ARG A 1 70  ? 8.654   13.485 34.897  1.00 17.90 ? 70  ARG A CA   1 
ATOM   539  C C    . ARG A 1 70  ? 7.236   13.157 34.448  1.00 18.95 ? 70  ARG A C    1 
ATOM   540  O O    . ARG A 1 70  ? 6.819   13.516 33.343  1.00 16.57 ? 70  ARG A O    1 
ATOM   541  C CB   . ARG A 1 70  ? 8.631   14.725 35.803  1.00 14.94 ? 70  ARG A CB   1 
ATOM   542  C CG   . ARG A 1 70  ? 10.008  15.175 36.224  1.00 18.61 ? 70  ARG A CG   1 
ATOM   543  C CD   . ARG A 1 70  ? 10.617  14.243 37.256  1.00 21.38 ? 70  ARG A CD   1 
ATOM   544  N NE   . ARG A 1 70  ? 11.905  14.736 37.735  1.00 19.31 ? 70  ARG A NE   1 
ATOM   545  C CZ   . ARG A 1 70  ? 12.601  14.192 38.726  1.00 24.38 ? 70  ARG A CZ   1 
ATOM   546  N NH1  . ARG A 1 70  ? 12.171  13.115 39.360  1.00 19.12 ? 70  ARG A NH1  1 
ATOM   547  N NH2  . ARG A 1 70  ? 13.752  14.747 39.094  1.00 19.70 ? 70  ARG A NH2  1 
ATOM   548  N N    . LYS A 1 71  ? 6.472   12.504 35.330  1.00 14.98 ? 71  LYS A N    1 
ATOM   549  C CA   . LYS A 1 71  ? 5.044   12.396 35.055  1.00 20.55 ? 71  LYS A CA   1 
ATOM   550  C C    . LYS A 1 71  ? 4.369   13.752 35.215  1.00 17.25 ? 71  LYS A C    1 
ATOM   551  O O    . LYS A 1 71  ? 3.557   14.152 34.375  1.00 18.74 ? 71  LYS A O    1 
ATOM   552  C CB   . LYS A 1 71  ? 4.391   11.362 35.979  1.00 20.06 ? 71  LYS A CB   1 
ATOM   553  C CG   . LYS A 1 71  ? 5.027   9.992  35.869  1.00 24.08 ? 71  LYS A CG   1 
ATOM   554  C CD   . LYS A 1 71  ? 4.503   9.218  34.689  1.00 27.03 ? 71  LYS A CD   1 
ATOM   555  C CE   . LYS A 1 71  ? 5.163   7.835  34.637  1.00 33.03 ? 71  LYS A CE   1 
ATOM   556  N NZ   . LYS A 1 71  ? 4.499   6.861  35.536  1.00 43.01 ? 71  LYS A NZ   1 
ATOM   557  N N    . LEU A 1 72  ? 4.731   14.484 36.263  1.00 16.09 ? 72  LEU A N    1 
ATOM   558  C CA   . LEU A 1 72  ? 4.060   15.713 36.679  1.00 17.81 ? 72  LEU A CA   1 
ATOM   559  C C    . LEU A 1 72  ? 4.943   16.936 36.441  1.00 17.25 ? 72  LEU A C    1 
ATOM   560  O O    . LEU A 1 72  ? 6.160   16.882 36.651  1.00 14.31 ? 72  LEU A O    1 
ATOM   561  C CB   . LEU A 1 72  ? 3.732   15.633 38.168  1.00 17.40 ? 72  LEU A CB   1 
ATOM   562  C CG   . LEU A 1 72  ? 2.806   14.504 38.635  1.00 17.08 ? 72  LEU A CG   1 
ATOM   563  C CD1  . LEU A 1 72  ? 2.327   14.804 40.037  1.00 17.44 ? 72  LEU A CD1  1 
ATOM   564  C CD2  . LEU A 1 72  ? 1.611   14.377 37.694  1.00 18.51 ? 72  LEU A CD2  1 
ATOM   565  N N    . ILE A 1 73  ? 4.324   18.065 36.065  1.00 16.83 ? 73  ILE A N    1 
ATOM   566  C CA   . ILE A 1 73  ? 5.099   19.307 36.022  1.00 16.12 ? 73  ILE A CA   1 
ATOM   567  C C    . ILE A 1 73  ? 5.352   19.841 37.426  1.00 15.03 ? 73  ILE A C    1 
ATOM   568  O O    . ILE A 1 73  ? 6.305   20.601 37.639  1.00 16.33 ? 73  ILE A O    1 
ATOM   569  C CB   . ILE A 1 73  ? 4.421   20.376 35.150  1.00 16.52 ? 73  ILE A CB   1 
ATOM   570  C CG1  . ILE A 1 73  ? 2.942   20.539 35.545  1.00 18.12 ? 73  ILE A CG1  1 
ATOM   571  C CG2  . ILE A 1 73  ? 4.605   20.027 33.658  1.00 14.66 ? 73  ILE A CG2  1 
ATOM   572  C CD1  . ILE A 1 73  ? 2.263   21.835 34.997  1.00 19.22 ? 73  ILE A CD1  1 
ATOM   573  N N    . GLU A 1 74  ? 4.523   19.460 38.396  1.00 15.25 ? 74  GLU A N    1 
ATOM   574  C CA   . GLU A 1 74  ? 4.868   19.682 39.798  1.00 15.60 ? 74  GLU A CA   1 
ATOM   575  C C    . GLU A 1 74  ? 6.283   19.216 40.119  1.00 20.34 ? 74  GLU A C    1 
ATOM   576  O O    . GLU A 1 74  ? 7.015   19.881 40.865  1.00 18.44 ? 74  GLU A O    1 
ATOM   577  C CB   . GLU A 1 74  ? 3.871   18.951 40.701  1.00 21.39 ? 74  GLU A CB   1 
ATOM   578  C CG   . GLU A 1 74  ? 2.545   19.670 40.839  1.00 20.60 ? 74  GLU A CG   1 
ATOM   579  C CD   . GLU A 1 74  ? 1.512   19.263 39.800  1.00 18.21 ? 74  GLU A CD   1 
ATOM   580  O OE1  . GLU A 1 74  ? 1.865   18.774 38.702  1.00 17.05 ? 74  GLU A OE1  1 
ATOM   581  O OE2  . GLU A 1 74  ? 0.320   19.432 40.100  1.00 21.97 ? 74  GLU A OE2  1 
ATOM   582  N N    . THR A 1 75  ? 6.676   18.057 39.599  1.00 17.43 ? 75  THR A N    1 
ATOM   583  C CA   . THR A 1 75  ? 7.978   17.509 39.978  1.00 18.28 ? 75  THR A CA   1 
ATOM   584  C C    . THR A 1 75  ? 9.107   18.259 39.288  1.00 15.83 ? 75  THR A C    1 
ATOM   585  O O    . THR A 1 75  ? 10.175  18.470 39.876  1.00 15.65 ? 75  THR A O    1 
ATOM   586  C CB   . THR A 1 75  ? 8.023   16.017 39.649  1.00 19.14 ? 75  THR A CB   1 
ATOM   587  O OG1  . THR A 1 75  ? 6.770   15.415 40.038  1.00 19.22 ? 75  THR A OG1  1 
ATOM   588  C CG2  . THR A 1 75  ? 9.200   15.330 40.382  1.00 17.97 ? 75  THR A CG2  1 
ATOM   589  N N    . VAL A 1 76  ? 8.880   18.680 38.050  1.00 15.39 ? 76  VAL A N    1 
ATOM   590  C CA   . VAL A 1 76  ? 9.843   19.543 37.367  1.00 17.28 ? 76  VAL A CA   1 
ATOM   591  C C    . VAL A 1 76  ? 10.034  20.851 38.129  1.00 19.25 ? 76  VAL A C    1 
ATOM   592  O O    . VAL A 1 76  ? 11.163  21.316 38.333  1.00 16.40 ? 76  VAL A O    1 
ATOM   593  C CB   . VAL A 1 76  ? 9.390   19.792 35.918  1.00 13.56 ? 76  VAL A CB   1 
ATOM   594  C CG1  . VAL A 1 76  ? 10.358  20.747 35.210  1.00 15.57 ? 76  VAL A CG1  1 
ATOM   595  C CG2  . VAL A 1 76  ? 9.272   18.461 35.178  1.00 13.85 ? 76  VAL A CG2  1 
ATOM   596  N N    . GLY A 1 77  ? 8.935   21.474 38.556  1.00 17.75 ? 77  GLY A N    1 
ATOM   597  C CA   . GLY A 1 77  ? 9.056   22.740 39.259  1.00 13.73 ? 77  GLY A CA   1 
ATOM   598  C C    . GLY A 1 77  ? 9.761   22.594 40.592  1.00 15.51 ? 77  GLY A C    1 
ATOM   599  O O    . GLY A 1 77  ? 10.566  23.450 40.978  1.00 14.24 ? 77  GLY A O    1 
ATOM   600  N N    . ALA A 1 78  ? 9.465   21.512 41.318  1.00 15.90 ? 78  ALA A N    1 
ATOM   601  C CA   . ALA A 1 78  ? 10.160  21.250 42.576  1.00 17.99 ? 78  ALA A CA   1 
ATOM   602  C C    . ALA A 1 78  ? 11.662  21.062 42.365  1.00 18.72 ? 78  ALA A C    1 
ATOM   603  O O    . ALA A 1 78  ? 12.465  21.504 43.192  1.00 17.05 ? 78  ALA A O    1 
ATOM   604  C CB   . ALA A 1 78  ? 9.559   20.023 43.257  1.00 19.54 ? 78  ALA A CB   1 
ATOM   605  N N    . GLU A 1 79  ? 12.072  20.414 41.264  1.00 16.35 ? 79  GLU A N    1 
ATOM   606  C CA   . GLU A 1 79  ? 13.508  20.264 41.036  1.00 14.70 ? 79  GLU A CA   1 
ATOM   607  C C    . GLU A 1 79  ? 14.170  21.613 40.763  1.00 18.57 ? 79  GLU A C    1 
ATOM   608  O O    . GLU A 1 79  ? 15.297  21.866 41.215  1.00 15.17 ? 79  GLU A O    1 
ATOM   609  C CB   . GLU A 1 79  ? 13.783  19.313 39.880  1.00 14.85 ? 79  GLU A CB   1 
ATOM   610  C CG   . GLU A 1 79  ? 15.246  18.875 39.841  1.00 17.14 ? 79  GLU A CG   1 
ATOM   611  C CD   . GLU A 1 79  ? 15.540  17.890 38.731  1.00 21.68 ? 79  GLU A CD   1 
ATOM   612  O OE1  . GLU A 1 79  ? 14.582  17.311 38.185  1.00 21.31 ? 79  GLU A OE1  1 
ATOM   613  O OE2  . GLU A 1 79  ? 16.735  17.658 38.440  1.00 22.08 ? 79  GLU A OE2  1 
ATOM   614  N N    . ILE A 1 80  ? 13.500  22.498 40.019  1.00 15.13 ? 80  ILE A N    1 
ATOM   615  C CA   . ILE A 1 80  ? 14.096  23.807 39.788  1.00 14.41 ? 80  ILE A CA   1 
ATOM   616  C C    . ILE A 1 80  ? 14.163  24.593 41.089  1.00 15.16 ? 80  ILE A C    1 
ATOM   617  O O    . ILE A 1 80  ? 15.198  25.175 41.429  1.00 20.75 ? 80  ILE A O    1 
ATOM   618  C CB   . ILE A 1 80  ? 13.337  24.580 38.691  1.00 16.38 ? 80  ILE A CB   1 
ATOM   619  C CG1  . ILE A 1 80  ? 13.377  23.814 37.373  1.00 17.75 ? 80  ILE A CG1  1 
ATOM   620  C CG2  . ILE A 1 80  ? 13.948  25.948 38.511  1.00 13.28 ? 80  ILE A CG2  1 
ATOM   621  C CD1  . ILE A 1 80  ? 12.425  24.375 36.322  1.00 18.92 ? 80  ILE A CD1  1 
ATOM   622  N N    . ALA A 1 81  ? 13.070  24.594 41.854  1.00 16.16 ? 81  ALA A N    1 
ATOM   623  C CA   . ALA A 1 81  ? 13.032  25.336 43.112  1.00 17.53 ? 81  ALA A CA   1 
ATOM   624  C C    . ALA A 1 81  ? 14.085  24.834 44.092  1.00 19.58 ? 81  ALA A C    1 
ATOM   625  O O    . ALA A 1 81  ? 14.730  25.632 44.782  1.00 18.84 ? 81  ALA A O    1 
ATOM   626  C CB   . ALA A 1 81  ? 11.648  25.227 43.731  1.00 18.44 ? 81  ALA A CB   1 
ATOM   627  N N    . ASP A 1 82  ? 14.239  23.511 44.193  1.00 17.71 ? 82  ASP A N    1 
ATOM   628  C CA   . ASP A 1 82  ? 15.315  22.932 44.991  1.00 23.39 ? 82  ASP A CA   1 
ATOM   629  C C    . ASP A 1 82  ? 16.660  23.529 44.620  1.00 19.79 ? 82  ASP A C    1 
ATOM   630  O O    . ASP A 1 82  ? 17.478  23.836 45.494  1.00 18.88 ? 82  ASP A O    1 
ATOM   631  C CB   . ASP A 1 82  ? 15.360  21.416 44.785  1.00 25.98 ? 82  ASP A CB   1 
ATOM   632  C CG   . ASP A 1 82  ? 14.275  20.670 45.557  1.00 25.62 ? 82  ASP A CG   1 
ATOM   633  O OD1  . ASP A 1 82  ? 13.638  21.261 46.451  1.00 30.34 ? 82  ASP A OD1  1 
ATOM   634  O OD2  . ASP A 1 82  ? 14.081  19.471 45.267  1.00 29.83 ? 82  ASP A OD2  1 
ATOM   635  N N    . HIS A 1 83  ? 16.921  23.676 43.322  1.00 20.31 ? 83  HIS A N    1 
ATOM   636  C CA   . HIS A 1 83  ? 18.216  24.203 42.909  1.00 20.91 ? 83  HIS A CA   1 
ATOM   637  C C    . HIS A 1 83  ? 18.414  25.620 43.426  1.00 23.04 ? 83  HIS A C    1 
ATOM   638  O O    . HIS A 1 83  ? 19.482  25.955 43.951  1.00 22.59 ? 83  HIS A O    1 
ATOM   639  C CB   . HIS A 1 83  ? 18.361  24.181 41.388  1.00 20.09 ? 83  HIS A CB   1 
ATOM   640  C CG   . HIS A 1 83  ? 19.412  25.127 40.883  1.00 23.87 ? 83  HIS A CG   1 
ATOM   641  N ND1  . HIS A 1 83  ? 20.752  24.802 40.851  1.00 20.41 ? 83  HIS A ND1  1 
ATOM   642  C CD2  . HIS A 1 83  ? 19.322  26.401 40.422  1.00 21.89 ? 83  HIS A CD2  1 
ATOM   643  C CE1  . HIS A 1 83  ? 21.437  25.824 40.366  1.00 27.38 ? 83  HIS A CE1  1 
ATOM   644  N NE2  . HIS A 1 83  ? 20.593  26.805 40.099  1.00 22.96 ? 83  HIS A NE2  1 
ATOM   645  N N    . VAL A 1 84  ? 17.387  26.471 43.281  1.00 20.77 ? 84  VAL A N    1 
ATOM   646  C CA   . VAL A 1 84  ? 17.523  27.874 43.668  1.00 19.25 ? 84  VAL A CA   1 
ATOM   647  C C    . VAL A 1 84  ? 17.777  28.000 45.171  1.00 21.78 ? 84  VAL A C    1 
ATOM   648  O O    . VAL A 1 84  ? 18.635  28.778 45.603  1.00 23.17 ? 84  VAL A O    1 
ATOM   649  C CB   . VAL A 1 84  ? 16.283  28.682 43.239  1.00 23.28 ? 84  VAL A CB   1 
ATOM   650  C CG1  . VAL A 1 84  ? 16.344  30.093 43.838  1.00 16.33 ? 84  VAL A CG1  1 
ATOM   651  C CG2  . VAL A 1 84  ? 16.150  28.737 41.711  1.00 19.27 ? 84  VAL A CG2  1 
ATOM   652  N N    . MET A 1 85  ? 17.045  27.235 45.991  1.00 19.88 ? 85  MET A N    1 
ATOM   653  C CA   A MET A 1 85  ? 17.195  27.364 47.438  0.92 23.71 ? 85  MET A CA   1 
ATOM   654  C CA   B MET A 1 85  ? 17.176  27.329 47.442  0.08 23.64 ? 85  MET A CA   1 
ATOM   655  C C    . MET A 1 85  ? 18.521  26.828 47.951  1.00 29.04 ? 85  MET A C    1 
ATOM   656  O O    . MET A 1 85  ? 18.870  27.099 49.108  1.00 27.42 ? 85  MET A O    1 
ATOM   657  C CB   A MET A 1 85  ? 16.046  26.674 48.177  0.92 25.03 ? 85  MET A CB   1 
ATOM   658  C CB   B MET A 1 85  ? 16.050  26.548 48.121  0.08 25.07 ? 85  MET A CB   1 
ATOM   659  C CG   A MET A 1 85  ? 14.647  27.177 47.819  0.92 25.28 ? 85  MET A CG   1 
ATOM   660  C CG   B MET A 1 85  ? 14.662  27.091 47.847  0.08 25.30 ? 85  MET A CG   1 
ATOM   661  S SD   A MET A 1 85  ? 14.457  28.911 48.327  0.92 26.96 ? 85  MET A SD   1 
ATOM   662  S SD   B MET A 1 85  ? 14.557  28.854 48.202  0.08 26.78 ? 85  MET A SD   1 
ATOM   663  C CE   A MET A 1 85  ? 14.443  28.754 50.116  0.92 25.41 ? 85  MET A CE   1 
ATOM   664  C CE   B MET A 1 85  ? 14.516  28.829 49.993  0.08 25.88 ? 85  MET A CE   1 
ATOM   665  N N    . ASP A 1 86  ? 19.271  26.093 47.130  1.00 22.23 ? 86  ASP A N    1 
ATOM   666  C CA   . ASP A 1 86  ? 20.591  25.665 47.561  1.00 26.60 ? 86  ASP A CA   1 
ATOM   667  C C    . ASP A 1 86  ? 21.544  26.839 47.701  1.00 25.73 ? 86  ASP A C    1 
ATOM   668  O O    . ASP A 1 86  ? 22.624  26.683 48.276  1.00 28.74 ? 86  ASP A O    1 
ATOM   669  C CB   . ASP A 1 86  ? 21.129  24.616 46.591  1.00 22.73 ? 86  ASP A CB   1 
ATOM   670  C CG   . ASP A 1 86  ? 20.486  23.252 46.800  1.00 35.08 ? 86  ASP A CG   1 
ATOM   671  O OD1  . ASP A 1 86  ? 19.935  23.007 47.896  1.00 37.58 ? 86  ASP A OD1  1 
ATOM   672  O OD2  . ASP A 1 86  ? 20.510  22.429 45.864  1.00 33.69 ? 86  ASP A OD2  1 
ATOM   673  N N    . ASP A 1 87  ? 21.169  28.015 47.207  1.00 24.81 ? 87  ASP A N    1 
ATOM   674  C CA   . ASP A 1 87  ? 21.951  29.218 47.433  1.00 22.72 ? 87  ASP A CA   1 
ATOM   675  C C    . ASP A 1 87  ? 21.421  29.891 48.694  1.00 24.25 ? 87  ASP A C    1 
ATOM   676  O O    . ASP A 1 87  ? 20.276  30.353 48.730  1.00 26.57 ? 87  ASP A O    1 
ATOM   677  C CB   . ASP A 1 87  ? 21.897  30.135 46.212  1.00 24.15 ? 87  ASP A CB   1 
ATOM   678  C CG   . ASP A 1 87  ? 22.748  31.372 46.370  1.00 21.75 ? 87  ASP A CG   1 
ATOM   679  O OD1  . ASP A 1 87  ? 22.782  31.925 47.477  1.00 23.47 ? 87  ASP A OD1  1 
ATOM   680  O OD2  . ASP A 1 87  ? 23.407  31.779 45.382  1.00 27.12 ? 87  ASP A OD2  1 
ATOM   681  N N    . GLN A 1 88  ? 22.263  29.951 49.722  1.00 27.59 ? 88  GLN A N    1 
ATOM   682  C CA   . GLN A 1 88  ? 21.854  30.372 51.057  1.00 27.89 ? 88  GLN A CA   1 
ATOM   683  C C    . GLN A 1 88  ? 21.386  31.820 51.105  1.00 23.04 ? 88  GLN A C    1 
ATOM   684  O O    . GLN A 1 88  ? 20.749  32.222 52.083  1.00 29.02 ? 88  GLN A O    1 
ATOM   685  C CB   . GLN A 1 88  ? 23.030  30.163 52.002  1.00 34.83 ? 88  GLN A CB   1 
ATOM   686  C CG   . GLN A 1 88  ? 23.686  28.829 51.735  1.00 43.00 ? 88  GLN A CG   1 
ATOM   687  C CD   . GLN A 1 88  ? 25.040  28.972 51.041  1.00 47.90 ? 88  GLN A CD   1 
ATOM   688  O OE1  . GLN A 1 88  ? 25.111  29.358 49.861  1.00 39.50 ? 88  GLN A OE1  1 
ATOM   689  N NE2  . GLN A 1 88  ? 26.114  28.624 51.752  1.00 39.45 ? 88  GLN A NE2  1 
ATOM   690  N N    . ARG A 1 89  ? 21.691  32.609 50.077  1.00 27.32 ? 89  ARG A N    1 
ATOM   691  C CA   . ARG A 1 89  ? 21.298  34.012 50.043  1.00 29.96 ? 89  ARG A CA   1 
ATOM   692  C C    . ARG A 1 89  ? 19.849  34.201 49.640  1.00 23.30 ? 89  ARG A C    1 
ATOM   693  O O    . ARG A 1 89  ? 19.292  35.285 49.851  1.00 24.61 ? 89  ARG A O    1 
ATOM   694  C CB   . ARG A 1 89  ? 22.184  34.778 49.061  1.00 27.46 ? 89  ARG A CB   1 
ATOM   695  C CG   . ARG A 1 89  ? 23.657  34.732 49.425  1.00 30.80 ? 89  ARG A CG   1 
ATOM   696  C CD   . ARG A 1 89  ? 24.515  35.246 48.293  1.00 25.94 ? 89  ARG A CD   1 
ATOM   697  N NE   . ARG A 1 89  ? 24.313  34.497 47.059  1.00 27.64 ? 89  ARG A NE   1 
ATOM   698  C CZ   . ARG A 1 89  ? 24.757  34.886 45.873  1.00 27.90 ? 89  ARG A CZ   1 
ATOM   699  N NH1  . ARG A 1 89  ? 25.443  36.011 45.725  1.00 22.84 ? 89  ARG A NH1  1 
ATOM   700  N NH2  . ARG A 1 89  ? 24.504  34.133 44.810  1.00 23.72 ? 89  ARG A NH2  1 
ATOM   701  N N    . VAL A 1 90  ? 19.246  33.184 49.040  1.00 22.77 ? 90  VAL A N    1 
ATOM   702  C CA   . VAL A 1 90  ? 17.898  33.299 48.516  1.00 21.11 ? 90  VAL A CA   1 
ATOM   703  C C    . VAL A 1 90  ? 16.910  33.197 49.671  1.00 26.38 ? 90  VAL A C    1 
ATOM   704  O O    . VAL A 1 90  ? 16.987  32.277 50.502  1.00 28.85 ? 90  VAL A O    1 
ATOM   705  C CB   . VAL A 1 90  ? 17.640  32.222 47.452  1.00 24.97 ? 90  VAL A CB   1 
ATOM   706  C CG1  . VAL A 1 90  ? 16.174  32.257 47.013  1.00 16.85 ? 90  VAL A CG1  1 
ATOM   707  C CG2  . VAL A 1 90  ? 18.586  32.408 46.262  1.00 18.78 ? 90  VAL A CG2  1 
ATOM   708  N N    . HIS A 1 91  ? 15.998  34.164 49.746  1.00 21.08 ? 91  HIS A N    1 
ATOM   709  C CA   . HIS A 1 91  ? 14.946  34.137 50.756  1.00 22.44 ? 91  HIS A CA   1 
ATOM   710  C C    . HIS A 1 91  ? 13.800  33.223 50.343  1.00 26.13 ? 91  HIS A C    1 
ATOM   711  O O    . HIS A 1 91  ? 13.261  32.478 51.171  1.00 23.98 ? 91  HIS A O    1 
ATOM   712  C CB   . HIS A 1 91  ? 14.413  35.546 50.994  1.00 24.70 ? 91  HIS A CB   1 
ATOM   713  C CG   . HIS A 1 91  ? 15.417  36.472 51.602  1.00 31.52 ? 91  HIS A CG   1 
ATOM   714  N ND1  . HIS A 1 91  ? 15.776  37.667 51.020  1.00 30.61 ? 91  HIS A ND1  1 
ATOM   715  C CD2  . HIS A 1 91  ? 16.166  36.361 52.725  1.00 36.19 ? 91  HIS A CD2  1 
ATOM   716  C CE1  . HIS A 1 91  ? 16.689  38.261 51.764  1.00 26.92 ? 91  HIS A CE1  1 
ATOM   717  N NE2  . HIS A 1 91  ? 16.942  37.491 52.806  1.00 35.81 ? 91  HIS A NE2  1 
ATOM   718  N N    . ALA A 1 92  ? 13.417  33.270 49.069  1.00 25.53 ? 92  ALA A N    1 
ATOM   719  C CA   . ALA A 1 92  ? 12.274  32.518 48.573  1.00 19.99 ? 92  ALA A CA   1 
ATOM   720  C C    . ALA A 1 92  ? 12.393  32.413 47.059  1.00 20.18 ? 92  ALA A C    1 
ATOM   721  O O    . ALA A 1 92  ? 13.197  33.100 46.438  1.00 18.83 ? 92  ALA A O    1 
ATOM   722  C CB   . ALA A 1 92  ? 10.956  33.186 48.965  1.00 21.02 ? 92  ALA A CB   1 
ATOM   723  N N    . VAL A 1 93  ? 11.596  31.526 46.478  1.00 19.92 ? 93  VAL A N    1 
ATOM   724  C CA   . VAL A 1 93  ? 11.562  31.357 45.031  1.00 16.28 ? 93  VAL A CA   1 
ATOM   725  C C    . VAL A 1 93  ? 10.171  30.880 44.640  1.00 19.42 ? 93  VAL A C    1 
ATOM   726  O O    . VAL A 1 93  ? 9.521   30.138 45.382  1.00 22.19 ? 93  VAL A O    1 
ATOM   727  C CB   . VAL A 1 93  ? 12.657  30.368 44.553  1.00 18.35 ? 93  VAL A CB   1 
ATOM   728  C CG1  . VAL A 1 93  ? 12.366  28.955 45.071  1.00 23.00 ? 93  VAL A CG1  1 
ATOM   729  C CG2  . VAL A 1 93  ? 12.764  30.365 43.024  1.00 15.68 ? 93  VAL A CG2  1 
ATOM   730  N N    . GLU A 1 94  ? 9.708   31.330 43.475  1.00 19.43 ? 94  GLU A N    1 
ATOM   731  C CA   . GLU A 1 94  ? 8.520   30.795 42.825  1.00 18.75 ? 94  GLU A CA   1 
ATOM   732  C C    . GLU A 1 94  ? 8.954   30.306 41.450  1.00 21.42 ? 94  GLU A C    1 
ATOM   733  O O    . GLU A 1 94  ? 9.567   31.075 40.699  1.00 17.74 ? 94  GLU A O    1 
ATOM   734  C CB   . GLU A 1 94  ? 7.431   31.864 42.638  1.00 24.55 ? 94  GLU A CB   1 
ATOM   735  C CG   . GLU A 1 94  ? 6.535   32.010 43.804  1.00 27.42 ? 94  GLU A CG   1 
ATOM   736  C CD   . GLU A 1 94  ? 5.242   32.781 43.562  1.00 25.45 ? 94  GLU A CD   1 
ATOM   737  O OE1  . GLU A 1 94  ? 5.017   33.226 42.431  1.00 30.46 ? 94  GLU A OE1  1 
ATOM   738  O OE2  . GLU A 1 94  ? 4.441   32.919 44.509  1.00 37.09 ? 94  GLU A OE2  1 
ATOM   739  N N    . VAL A 1 95  ? 8.674   29.040 41.130  1.00 17.42 ? 95  VAL A N    1 
ATOM   740  C CA   . VAL A 1 95  ? 8.939   28.478 39.797  1.00 17.93 ? 95  VAL A CA   1 
ATOM   741  C C    . VAL A 1 95  ? 7.602   28.117 39.162  1.00 17.77 ? 95  VAL A C    1 
ATOM   742  O O    . VAL A 1 95  ? 6.862   27.279 39.696  1.00 15.15 ? 95  VAL A O    1 
ATOM   743  C CB   . VAL A 1 95  ? 9.860   27.238 39.844  1.00 19.72 ? 95  VAL A CB   1 
ATOM   744  C CG1  . VAL A 1 95  ? 9.998   26.605 38.437  1.00 13.03 ? 95  VAL A CG1  1 
ATOM   745  C CG2  . VAL A 1 95  ? 11.235  27.588 40.421  1.00 13.70 ? 95  VAL A CG2  1 
ATOM   746  N N    . ALA A 1 96  ? 7.296   28.737 38.022  1.00 15.76 ? 96  ALA A N    1 
ATOM   747  C CA   . ALA A 1 96  ? 6.091   28.441 37.254  1.00 15.27 ? 96  ALA A CA   1 
ATOM   748  C C    . ALA A 1 96  ? 6.472   27.544 36.085  1.00 17.19 ? 96  ALA A C    1 
ATOM   749  O O    . ALA A 1 96  ? 7.303   27.915 35.255  1.00 14.98 ? 96  ALA A O    1 
ATOM   750  C CB   . ALA A 1 96  ? 5.422   29.722 36.748  1.00 16.52 ? 96  ALA A CB   1 
ATOM   751  N N    . VAL A 1 97  ? 5.910   26.350 36.043  1.00 14.36 ? 97  VAL A N    1 
ATOM   752  C CA   . VAL A 1 97  ? 6.100   25.458 34.911  1.00 16.36 ? 97  VAL A CA   1 
ATOM   753  C C    . VAL A 1 97  ? 4.804   25.490 34.132  1.00 13.05 ? 97  VAL A C    1 
ATOM   754  O O    . VAL A 1 97  ? 3.771   25.033 34.637  1.00 12.85 ? 97  VAL A O    1 
ATOM   755  C CB   . VAL A 1 97  ? 6.463   24.027 35.343  1.00 15.02 ? 97  VAL A CB   1 
ATOM   756  C CG1  . VAL A 1 97  ? 6.673   23.150 34.122  1.00 12.02 ? 97  VAL A CG1  1 
ATOM   757  C CG2  . VAL A 1 97  ? 7.729   24.034 36.201  1.00 15.64 ? 97  VAL A CG2  1 
ATOM   758  N N    . HIS A 1 98  ? 4.859   26.055 32.923  1.00 14.18 ? 98  HIS A N    1 
ATOM   759  C CA   . HIS A 1 98  ? 3.715   26.166 32.022  1.00 12.65 ? 98  HIS A CA   1 
ATOM   760  C C    . HIS A 1 98  ? 3.735   25.044 30.998  1.00 17.17 ? 98  HIS A C    1 
ATOM   761  O O    . HIS A 1 98  ? 4.783   24.720 30.436  1.00 11.79 ? 98  HIS A O    1 
ATOM   762  C CB   . HIS A 1 98  ? 3.692   27.494 31.263  1.00 17.73 ? 98  HIS A CB   1 
ATOM   763  C CG   . HIS A 1 98  ? 3.835   28.701 32.135  1.00 17.48 ? 98  HIS A CG   1 
ATOM   764  N ND1  . HIS A 1 98  ? 2.757   29.476 32.504  1.00 18.46 ? 98  HIS A ND1  1 
ATOM   765  C CD2  . HIS A 1 98  ? 4.931   29.289 32.679  1.00 16.21 ? 98  HIS A CD2  1 
ATOM   766  C CE1  . HIS A 1 98  ? 3.183   30.488 33.245  1.00 19.32 ? 98  HIS A CE1  1 
ATOM   767  N NE2  . HIS A 1 98  ? 4.496   30.391 33.376  1.00 17.02 ? 98  HIS A NE2  1 
ATOM   768  N N    . LYS A 1 99  ? 2.566   24.468 30.746  1.00 13.95 ? 99  LYS A N    1 
ATOM   769  C CA   . LYS A 1 99  ? 2.423   23.369 29.801  1.00 15.51 ? 99  LYS A CA   1 
ATOM   770  C C    . LYS A 1 99  ? 1.343   23.797 28.822  1.00 20.83 ? 99  LYS A C    1 
ATOM   771  O O    . LYS A 1 99  ? 0.222   23.273 28.825  1.00 23.22 ? 99  LYS A O    1 
ATOM   772  C CB   . LYS A 1 99  ? 2.094   22.065 30.524  1.00 16.76 ? 99  LYS A CB   1 
ATOM   773  C CG   . LYS A 1 99  ? 2.262   20.830 29.674  1.00 19.65 ? 99  LYS A CG   1 
ATOM   774  C CD   . LYS A 1 99  ? 1.825   19.606 30.433  1.00 21.19 ? 99  LYS A CD   1 
ATOM   775  C CE   . LYS A 1 99  ? 1.858   18.375 29.566  1.00 26.96 ? 99  LYS A CE   1 
ATOM   776  N NZ   . LYS A 1 99  ? 1.434   17.167 30.323  1.00 29.77 ? 99  LYS A NZ   1 
ATOM   777  N N    . PRO A 1 100 ? 1.645   24.796 27.991  1.00 19.03 ? 100 PRO A N    1 
ATOM   778  C CA   . PRO A 1 100 ? 0.600   25.443 27.192  1.00 21.46 ? 100 PRO A CA   1 
ATOM   779  C C    . PRO A 1 100 ? 0.025   24.563 26.095  1.00 24.15 ? 100 PRO A C    1 
ATOM   780  O O    . PRO A 1 100 ? -1.056  24.872 25.576  1.00 31.03 ? 100 PRO A O    1 
ATOM   781  C CB   . PRO A 1 100 ? 1.323   26.663 26.616  1.00 20.32 ? 100 PRO A CB   1 
ATOM   782  C CG   . PRO A 1 100 ? 2.754   26.191 26.482  1.00 21.63 ? 100 PRO A CG   1 
ATOM   783  C CD   . PRO A 1 100 ? 2.992   25.307 27.675  1.00 17.73 ? 100 PRO A CD   1 
ATOM   784  N N    . GLN A 1 101 ? 0.674   23.459 25.762  1.00 20.85 ? 101 GLN A N    1 
ATOM   785  C CA   . GLN A 1 101 ? 0.191   22.541 24.744  1.00 19.15 ? 101 GLN A CA   1 
ATOM   786  C C    . GLN A 1 101 ? -0.407  21.294 25.367  1.00 23.66 ? 101 GLN A C    1 
ATOM   787  O O    . GLN A 1 101 ? -0.587  20.286 24.677  1.00 23.76 ? 101 GLN A O    1 
ATOM   788  C CB   . GLN A 1 101 ? 1.345   22.164 23.829  1.00 26.36 ? 101 GLN A CB   1 
ATOM   789  C CG   . GLN A 1 101 ? 1.934   23.377 23.158  1.00 28.52 ? 101 GLN A CG   1 
ATOM   790  C CD   . GLN A 1 101 ? 3.067   23.056 22.206  1.00 28.97 ? 101 GLN A CD   1 
ATOM   791  O OE1  . GLN A 1 101 ? 3.764   22.018 22.324  1.00 14.21 ? 101 GLN A OE1  1 
ATOM   792  N NE2  . GLN A 1 101 ? 3.281   23.966 21.263  1.00 23.10 ? 101 GLN A NE2  1 
ATOM   793  N N    . ALA A 1 102 ? -0.679  21.333 26.664  1.00 21.39 ? 102 ALA A N    1 
ATOM   794  C CA   . ALA A 1 102 ? -1.145  20.148 27.359  1.00 21.51 ? 102 ALA A CA   1 
ATOM   795  C C    . ALA A 1 102 ? -2.306  19.522 26.587  1.00 24.98 ? 102 ALA A C    1 
ATOM   796  O O    . ALA A 1 102 ? -3.105  20.244 25.973  1.00 23.97 ? 102 ALA A O    1 
ATOM   797  C CB   . ALA A 1 102 ? -1.575  20.502 28.785  1.00 22.00 ? 102 ALA A CB   1 
ATOM   798  N N    . PRO A 1 103 ? -2.412  18.199 26.566  1.00 25.60 ? 103 PRO A N    1 
ATOM   799  C CA   . PRO A 1 103 ? -3.570  17.563 25.926  1.00 23.49 ? 103 PRO A CA   1 
ATOM   800  C C    . PRO A 1 103 ? -4.817  17.708 26.773  1.00 25.92 ? 103 PRO A C    1 
ATOM   801  O O    . PRO A 1 103 ? -5.017  16.955 27.731  1.00 28.99 ? 103 PRO A O    1 
ATOM   802  C CB   . PRO A 1 103 ? -3.143  16.095 25.790  1.00 31.01 ? 103 PRO A CB   1 
ATOM   803  C CG   . PRO A 1 103 ? -2.119  15.885 26.860  1.00 29.02 ? 103 PRO A CG   1 
ATOM   804  C CD   . PRO A 1 103 ? -1.428  17.221 27.064  1.00 26.97 ? 103 PRO A CD   1 
ATOM   805  N N    . ILE A 1 104 ? -5.639  18.701 26.451  1.00 34.56 ? 104 ILE A N    1 
ATOM   806  C CA   . ILE A 1 104 ? -6.899  18.958 27.147  1.00 22.66 ? 104 ILE A CA   1 
ATOM   807  C C    . ILE A 1 104 ? -7.914  19.142 26.029  1.00 27.32 ? 104 ILE A C    1 
ATOM   808  O O    . ILE A 1 104 ? -7.675  19.941 25.118  1.00 27.18 ? 104 ILE A O    1 
ATOM   809  C CB   . ILE A 1 104 ? -6.811  20.195 28.059  1.00 26.54 ? 104 ILE A CB   1 
ATOM   810  C CG1  . ILE A 1 104 ? -5.891  19.930 29.251  1.00 30.87 ? 104 ILE A CG1  1 
ATOM   811  C CG2  . ILE A 1 104 ? -8.182  20.563 28.635  1.00 33.45 ? 104 ILE A CG2  1 
ATOM   812  C CD1  . ILE A 1 104 ? -5.739  21.119 30.192  1.00 26.11 ? 104 ILE A CD1  1 
ATOM   813  N N    . PRO A 1 105 ? -9.041  18.430 26.033  1.00 24.44 ? 105 PRO A N    1 
ATOM   814  C CA   . PRO A 1 105 ? -10.001 18.586 24.929  1.00 24.92 ? 105 PRO A CA   1 
ATOM   815  C C    . PRO A 1 105 ? -10.567 20.007 24.801  1.00 23.69 ? 105 PRO A C    1 
ATOM   816  O O    . PRO A 1 105 ? -11.137 20.329 23.753  1.00 34.13 ? 105 PRO A O    1 
ATOM   817  C CB   . PRO A 1 105 ? -11.100 17.566 25.271  1.00 23.49 ? 105 PRO A CB   1 
ATOM   818  C CG   . PRO A 1 105 ? -10.509 16.664 26.273  1.00 26.00 ? 105 PRO A CG   1 
ATOM   819  C CD   . PRO A 1 105 ? -9.519  17.478 27.045  1.00 25.32 ? 105 PRO A CD   1 
ATOM   820  N N    . GLN A 1 106 ? -10.390 20.867 25.803  1.00 27.75 ? 106 GLN A N    1 
ATOM   821  C CA   . GLN A 1 106 ? -10.973 22.198 25.842  1.00 20.26 ? 106 GLN A CA   1 
ATOM   822  C C    . GLN A 1 106 ? -10.029 23.232 25.235  1.00 22.17 ? 106 GLN A C    1 
ATOM   823  O O    . GLN A 1 106 ? -8.827  23.006 25.088  1.00 22.93 ? 106 GLN A O    1 
ATOM   824  C CB   . GLN A 1 106 ? -11.311 22.574 27.288  1.00 20.35 ? 106 GLN A CB   1 
ATOM   825  C CG   . GLN A 1 106 ? -12.573 21.930 27.814  1.00 19.22 ? 106 GLN A CG   1 
ATOM   826  C CD   . GLN A 1 106 ? -12.280 20.582 28.445  1.00 27.35 ? 106 GLN A CD   1 
ATOM   827  O OE1  . GLN A 1 106 ? -11.120 20.265 28.747  1.00 27.84 ? 106 GLN A OE1  1 
ATOM   828  N NE2  . GLN A 1 106 ? -13.315 19.768 28.615  1.00 28.74 ? 106 GLN A NE2  1 
ATOM   829  N N    . THR A 1 107 ? -10.591 24.389 24.886  1.00 17.79 ? 107 THR A N    1 
ATOM   830  C CA   . THR A 1 107 ? -9.805  25.506 24.385  1.00 15.34 ? 107 THR A CA   1 
ATOM   831  C C    . THR A 1 107 ? -9.334  26.361 25.564  1.00 17.37 ? 107 THR A C    1 
ATOM   832  O O    . THR A 1 107 ? -10.156 26.875 26.331  1.00 18.35 ? 107 THR A O    1 
ATOM   833  C CB   . THR A 1 107 ? -10.611 26.345 23.391  1.00 19.53 ? 107 THR A CB   1 
ATOM   834  O OG1  . THR A 1 107 ? -11.064 25.523 22.302  1.00 22.34 ? 107 THR A OG1  1 
ATOM   835  C CG2  . THR A 1 107 ? -9.748  27.472 22.837  1.00 20.15 ? 107 THR A CG2  1 
ATOM   836  N N    . PHE A 1 108 ? -8.019  26.543 25.695  1.00 16.68 ? 108 PHE A N    1 
ATOM   837  C CA   . PHE A 1 108 ? -7.484  27.298 26.822  1.00 17.04 ? 108 PHE A CA   1 
ATOM   838  C C    . PHE A 1 108 ? -6.145  27.908 26.430  1.00 18.59 ? 108 PHE A C    1 
ATOM   839  O O    . PHE A 1 108 ? -5.491  27.457 25.487  1.00 19.98 ? 108 PHE A O    1 
ATOM   840  C CB   . PHE A 1 108 ? -7.326  26.417 28.067  1.00 16.24 ? 108 PHE A CB   1 
ATOM   841  C CG   . PHE A 1 108 ? -6.235  25.397 27.939  1.00 21.15 ? 108 PHE A CG   1 
ATOM   842  C CD1  . PHE A 1 108 ? -6.368  24.321 27.078  1.00 23.40 ? 108 PHE A CD1  1 
ATOM   843  C CD2  . PHE A 1 108 ? -5.043  25.550 28.631  1.00 23.00 ? 108 PHE A CD2  1 
ATOM   844  C CE1  . PHE A 1 108 ? -5.353  23.383 26.940  1.00 25.93 ? 108 PHE A CE1  1 
ATOM   845  C CE2  . PHE A 1 108 ? -4.021  24.620 28.491  1.00 22.93 ? 108 PHE A CE2  1 
ATOM   846  C CZ   . PHE A 1 108 ? -4.183  23.530 27.653  1.00 22.89 ? 108 PHE A CZ   1 
ATOM   847  N N    . ASP A 1 109 ? -5.752  28.966 27.150  1.00 13.30 ? 109 ASP A N    1 
ATOM   848  C CA   . ASP A 1 109 ? -4.492  29.627 26.824  1.00 19.19 ? 109 ASP A CA   1 
ATOM   849  C C    . ASP A 1 109 ? -3.312  28.927 27.474  1.00 17.87 ? 109 ASP A C    1 
ATOM   850  O O    . ASP A 1 109 ? -2.263  28.750 26.846  1.00 19.86 ? 109 ASP A O    1 
ATOM   851  C CB   . ASP A 1 109 ? -4.514  31.080 27.268  1.00 11.33 ? 109 ASP A CB   1 
ATOM   852  C CG   . ASP A 1 109 ? -5.376  31.953 26.393  1.00 22.91 ? 109 ASP A CG   1 
ATOM   853  O OD1  . ASP A 1 109 ? -5.616  31.591 25.223  1.00 25.85 ? 109 ASP A OD1  1 
ATOM   854  O OD2  . ASP A 1 109 ? -5.820  33.002 26.896  1.00 24.07 ? 109 ASP A OD2  1 
ATOM   855  N N    . ASP A 1 110 ? -3.451  28.540 28.731  1.00 19.33 ? 110 ASP A N    1 
ATOM   856  C CA   . ASP A 1 110 ? -2.283  28.027 29.428  1.00 17.53 ? 110 ASP A CA   1 
ATOM   857  C C    . ASP A 1 110 ? -2.744  27.239 30.634  1.00 17.75 ? 110 ASP A C    1 
ATOM   858  O O    . ASP A 1 110 ? -3.808  27.509 31.194  1.00 15.74 ? 110 ASP A O    1 
ATOM   859  C CB   . ASP A 1 110 ? -1.371  29.168 29.875  1.00 16.85 ? 110 ASP A CB   1 
ATOM   860  C CG   . ASP A 1 110 ? -0.023  28.678 30.352  1.00 21.65 ? 110 ASP A CG   1 
ATOM   861  O OD1  . ASP A 1 110 ? 0.685   28.047 29.548  1.00 23.81 ? 110 ASP A OD1  1 
ATOM   862  O OD2  . ASP A 1 110 ? 0.297   28.875 31.540  1.00 20.14 ? 110 ASP A OD2  1 
ATOM   863  N N    . VAL A 1 111 ? -1.926  26.264 31.033  1.00 16.53 ? 111 VAL A N    1 
ATOM   864  C CA   . VAL A 1 111 ? -2.048  25.620 32.332  1.00 15.00 ? 111 VAL A CA   1 
ATOM   865  C C    . VAL A 1 111 ? -0.652  25.525 32.938  1.00 19.48 ? 111 VAL A C    1 
ATOM   866  O O    . VAL A 1 111 ? 0.329   25.309 32.221  1.00 15.99 ? 111 VAL A O    1 
ATOM   867  C CB   . VAL A 1 111 ? -2.731  24.235 32.251  1.00 19.04 ? 111 VAL A CB   1 
ATOM   868  C CG1  . VAL A 1 111 ? -1.785  23.156 31.673  1.00 15.77 ? 111 VAL A CG1  1 
ATOM   869  C CG2  . VAL A 1 111 ? -3.231  23.815 33.650  1.00 14.99 ? 111 VAL A CG2  1 
ATOM   870  N N    . ALA A 1 112 ? -0.559  25.742 34.250  1.00 15.53 ? 112 ALA A N    1 
ATOM   871  C CA   . ALA A 1 112 ? 0.736   25.798 34.914  1.00 15.08 ? 112 ALA A CA   1 
ATOM   872  C C    . ALA A 1 112 ? 0.587   25.417 36.380  1.00 16.93 ? 112 ALA A C    1 
ATOM   873  O O    . ALA A 1 112 ? -0.509  25.436 36.950  1.00 15.04 ? 112 ALA A O    1 
ATOM   874  C CB   . ALA A 1 112 ? 1.381   27.191 34.795  1.00 14.52 ? 112 ALA A CB   1 
ATOM   875  N N    . VAL A 1 113 ? 1.716   25.044 36.968  1.00 14.93 ? 113 VAL A N    1 
ATOM   876  C CA   . VAL A 1 113 ? 1.856   24.879 38.405  1.00 16.48 ? 113 VAL A CA   1 
ATOM   877  C C    . VAL A 1 113 ? 2.939   25.844 38.841  1.00 17.93 ? 113 VAL A C    1 
ATOM   878  O O    . VAL A 1 113 ? 3.870   26.125 38.084  1.00 17.22 ? 113 VAL A O    1 
ATOM   879  C CB   . VAL A 1 113 ? 2.208   23.431 38.797  1.00 16.93 ? 113 VAL A CB   1 
ATOM   880  C CG1  . VAL A 1 113 ? 1.155   22.455 38.209  1.00 15.45 ? 113 VAL A CG1  1 
ATOM   881  C CG2  . VAL A 1 113 ? 3.603   23.079 38.291  1.00 16.63 ? 113 VAL A CG2  1 
ATOM   882  N N    . VAL A 1 114 ? 2.805   26.376 40.051  1.00 15.86 ? 114 VAL A N    1 
ATOM   883  C CA   . VAL A 1 114 ? 3.798   27.279 40.599  1.00 16.65 ? 114 VAL A CA   1 
ATOM   884  C C    . VAL A 1 114 ? 4.244   26.677 41.917  1.00 21.30 ? 114 VAL A C    1 
ATOM   885  O O    . VAL A 1 114 ? 3.414   26.440 42.806  1.00 20.31 ? 114 VAL A O    1 
ATOM   886  C CB   . VAL A 1 114 ? 3.242   28.697 40.807  1.00 17.38 ? 114 VAL A CB   1 
ATOM   887  C CG1  . VAL A 1 114 ? 4.336   29.594 41.377  1.00 16.75 ? 114 VAL A CG1  1 
ATOM   888  C CG2  . VAL A 1 114 ? 2.653   29.263 39.499  1.00 17.05 ? 114 VAL A CG2  1 
ATOM   889  N N    . ILE A 1 115 ? 5.530   26.400 42.024  1.00 15.10 ? 115 ILE A N    1 
ATOM   890  C CA   . ILE A 1 115 ? 6.073   25.774 43.253  1.00 17.14 ? 115 ILE A CA   1 
ATOM   891  C C    . ILE A 1 115 ? 6.773   26.889 44.028  1.00 21.29 ? 115 ILE A C    1 
ATOM   892  O O    . ILE A 1 115 ? 7.639   27.504 43.472  1.00 22.73 ? 115 ILE A O    1 
ATOM   893  C CB   . ILE A 1 115 ? 7.007   24.611 42.879  1.00 19.91 ? 115 ILE A CB   1 
ATOM   894  C CG1  . ILE A 1 115 ? 6.284   23.534 42.073  1.00 25.54 ? 115 ILE A CG1  1 
ATOM   895  C CG2  . ILE A 1 115 ? 7.657   24.039 44.106  1.00 24.02 ? 115 ILE A CG2  1 
ATOM   896  C CD1  . ILE A 1 115 ? 5.205   22.857 42.835  1.00 22.32 ? 115 ILE A CD1  1 
ATOM   897  N N    . ARG A 1 116 ? 6.329   27.153 45.238  1.00 23.26 ? 116 ARG A N    1 
ATOM   898  C CA   . ARG A 1 116 ? 6.907   28.203 46.099  1.00 23.45 ? 116 ARG A CA   1 
ATOM   899  C C    . ARG A 1 116 ? 7.719   27.574 47.230  1.00 31.61 ? 116 ARG A C    1 
ATOM   900  O O    . ARG A 1 116 ? 7.307   26.558 47.769  1.00 27.45 ? 116 ARG A O    1 
ATOM   901  C CB   . ARG A 1 116 ? 5.818   29.114 46.672  1.00 29.42 ? 116 ARG A CB   1 
ATOM   902  C CG   . ARG A 1 116 ? 6.370   30.249 47.520  1.00 37.05 ? 116 ARG A CG   1 
ATOM   903  C CD   . ARG A 1 116 ? 5.531   30.819 48.645  1.00 45.48 ? 116 ARG A CD   1 
ATOM   904  N NE   . ARG A 1 116 ? 6.194   31.870 49.385  1.00 45.01 ? 116 ARG A NE   1 
ATOM   905  C CZ   . ARG A 1 116 ? 6.625   33.023 48.887  1.00 45.09 ? 116 ARG A CZ   1 
ATOM   906  N NH1  . ARG A 1 116 ? 6.505   33.299 47.605  1.00 44.52 ? 116 ARG A NH1  1 
ATOM   907  N NH2  . ARG A 1 116 ? 7.207   33.892 49.683  1.00 40.56 ? 116 ARG A NH2  1 
ATOM   908  N N    . ARG A 1 117 ? 8.859   28.179 47.526  1.00 25.87 ? 117 ARG A N    1 
ATOM   909  C CA   . ARG A 1 117 ? 9.756   27.790 48.630  1.00 29.39 ? 117 ARG A CA   1 
ATOM   910  C C    . ARG A 1 117 ? 10.246  29.072 49.295  1.00 36.69 ? 117 ARG A C    1 
ATOM   911  O O    . ARG A 1 117 ? 10.330  30.080 48.618  1.00 23.52 ? 117 ARG A O    1 
ATOM   912  C CB   . ARG A 1 117 ? 10.995  27.086 48.098  1.00 31.79 ? 117 ARG A CB   1 
ATOM   913  C CG   . ARG A 1 117 ? 10.711  25.762 47.433  1.00 35.27 ? 117 ARG A CG   1 
ATOM   914  C CD   . ARG A 1 117 ? 11.183  24.624 48.290  1.00 42.18 ? 117 ARG A CD   1 
ATOM   915  N NE   . ARG A 1 117 ? 11.384  23.486 47.422  1.00 38.60 ? 117 ARG A NE   1 
ATOM   916  C CZ   . ARG A 1 117 ? 10.396  22.752 47.008  1.00 39.09 ? 117 ARG A CZ   1 
ATOM   917  N NH1  . ARG A 1 117 ? 9.173   23.023 47.415  1.00 37.95 ? 117 ARG A NH1  1 
ATOM   918  N NH2  . ARG A 1 117 ? 10.629  21.763 46.189  1.00 36.46 ? 117 ARG A NH2  1 
ATOM   919  N N    . SER A 1 118 ? 10.523  29.005 50.597  1.00 37.21 ? 118 SER A N    1 
ATOM   920  C CA   . SER A 1 118 ? 11.055  30.150 51.321  1.00 37.86 ? 118 SER A CA   1 
ATOM   921  C C    . SER A 1 118 ? 11.692  29.647 52.603  1.00 38.44 ? 118 SER A C    1 
ATOM   922  O O    . SER A 1 118 ? 11.480  28.503 53.016  1.00 35.33 ? 118 SER A O    1 
ATOM   923  C CB   . SER A 1 118 ? 9.972   31.186 51.616  1.00 41.63 ? 118 SER A CB   1 
ATOM   924  O OG   . SER A 1 118 ? 8.749   30.565 51.962  1.00 45.25 ? 118 SER A OG   1 
ATOM   925  N N    . ARG A 1 119 ? 12.495  30.510 53.212  1.00 45.41 ? 119 ARG A N    1 
ATOM   926  C CA   . ARG A 1 119 ? 13.184  30.155 54.451  1.00 40.71 ? 119 ARG A CA   1 
ATOM   927  C C    . ARG A 1 119 ? 12.264  30.342 55.650  1.00 58.57 ? 119 ARG A C    1 
ATOM   928  O O    . ARG A 1 119 ? 11.141  29.831 55.664  1.00 65.41 ? 119 ARG A O    1 
ATOM   929  C CB   . ARG A 1 119 ? 14.441  30.989 54.629  1.00 40.69 ? 119 ARG A CB   1 
ATOM   930  C CG   . ARG A 1 119 ? 15.342  30.953 53.420  1.00 38.77 ? 119 ARG A CG   1 
ATOM   931  C CD   . ARG A 1 119 ? 16.498  29.995 53.547  1.00 37.54 ? 119 ARG A CD   1 
ATOM   932  N NE   . ARG A 1 119 ? 17.340  30.170 52.377  1.00 45.80 ? 119 ARG A NE   1 
ATOM   933  C CZ   . ARG A 1 119 ? 17.787  29.198 51.594  1.00 30.37 ? 119 ARG A CZ   1 
ATOM   934  N NH1  . ARG A 1 119 ? 17.599  27.920 51.890  1.00 34.96 ? 119 ARG A NH1  1 
ATOM   935  N NH2  . ARG A 1 119 ? 18.424  29.519 50.478  1.00 27.68 ? 119 ARG A NH2  1 
ATOM   936  N N    . ALA B 1 2   ? -1.792  30.390 -4.758  1.00 48.90 ? 2   ALA B N    1 
ATOM   937  C CA   . ALA B 1 2   ? -1.655  28.929 -4.962  1.00 50.55 ? 2   ALA B CA   1 
ATOM   938  C C    . ALA B 1 2   ? -1.462  28.236 -3.609  1.00 40.50 ? 2   ALA B C    1 
ATOM   939  O O    . ALA B 1 2   ? -1.443  28.940 -2.580  1.00 40.46 ? 2   ALA B O    1 
ATOM   940  C CB   . ALA B 1 2   ? -0.505  28.646 -5.898  1.00 46.07 ? 2   ALA B CB   1 
ATOM   941  N N    . ASP B 1 3   ? -1.324  26.906 -3.621  1.00 34.07 ? 3   ASP B N    1 
ATOM   942  C CA   . ASP B 1 3   ? -1.134  26.136 -2.399  1.00 23.52 ? 3   ASP B CA   1 
ATOM   943  C C    . ASP B 1 3   ? 0.218   26.488 -1.789  1.00 25.22 ? 3   ASP B C    1 
ATOM   944  O O    . ASP B 1 3   ? 1.201   26.700 -2.508  1.00 20.40 ? 3   ASP B O    1 
ATOM   945  C CB   . ASP B 1 3   ? -1.188  24.645 -2.731  1.00 23.67 ? 3   ASP B CB   1 
ATOM   946  C CG   . ASP B 1 3   ? -2.555  24.194 -3.233  1.00 28.28 ? 3   ASP B CG   1 
ATOM   947  O OD1  . ASP B 1 3   ? -3.538  24.972 -3.168  1.00 28.32 ? 3   ASP B OD1  1 
ATOM   948  O OD2  . ASP B 1 3   ? -2.622  23.062 -3.750  1.00 26.26 ? 3   ASP B OD2  1 
ATOM   949  N N    . ARG B 1 4   ? 0.284   26.548 -0.458  1.00 19.74 ? 4   ARG B N    1 
ATOM   950  C CA   . ARG B 1 4   ? 1.590   26.751 0.157   1.00 18.87 ? 4   ARG B CA   1 
ATOM   951  C C    . ARG B 1 4   ? 1.642   26.142 1.551   1.00 19.04 ? 4   ARG B C    1 
ATOM   952  O O    . ARG B 1 4   ? 0.616   25.860 2.179   1.00 20.90 ? 4   ARG B O    1 
ATOM   953  C CB   . ARG B 1 4   ? 1.962   28.237 0.211   1.00 21.56 ? 4   ARG B CB   1 
ATOM   954  C CG   . ARG B 1 4   ? 0.853   29.117 0.682   1.00 23.67 ? 4   ARG B CG   1 
ATOM   955  C CD   . ARG B 1 4   ? 1.127   30.592 0.432   1.00 24.14 ? 4   ARG B CD   1 
ATOM   956  N NE   . ARG B 1 4   ? 0.294   31.383 1.329   1.00 31.86 ? 4   ARG B NE   1 
ATOM   957  C CZ   . ARG B 1 4   ? -0.944  31.767 1.043   1.00 28.83 ? 4   ARG B CZ   1 
ATOM   958  N NH1  . ARG B 1 4   ? -1.511  31.466 -0.113  1.00 28.21 ? 4   ARG B NH1  1 
ATOM   959  N NH2  . ARG B 1 4   ? -1.627  32.474 1.937   1.00 30.37 ? 4   ARG B NH2  1 
ATOM   960  N N    . ILE B 1 5   ? 2.872   25.922 2.009   1.00 17.65 ? 5   ILE B N    1 
ATOM   961  C CA   . ILE B 1 5   ? 3.167   25.492 3.373   1.00 22.39 ? 5   ILE B CA   1 
ATOM   962  C C    . ILE B 1 5   ? 3.875   26.644 4.069   1.00 17.01 ? 5   ILE B C    1 
ATOM   963  O O    . ILE B 1 5   ? 4.834   27.202 3.525   1.00 18.21 ? 5   ILE B O    1 
ATOM   964  C CB   . ILE B 1 5   ? 4.044   24.229 3.386   1.00 20.31 ? 5   ILE B CB   1 
ATOM   965  C CG1  . ILE B 1 5   ? 3.346   23.088 2.637   1.00 16.23 ? 5   ILE B CG1  1 
ATOM   966  C CG2  . ILE B 1 5   ? 4.381   23.838 4.818   1.00 16.82 ? 5   ILE B CG2  1 
ATOM   967  C CD1  . ILE B 1 5   ? 4.294   21.972 2.173   1.00 17.39 ? 5   ILE B CD1  1 
ATOM   968  N N    . GLU B 1 6   ? 3.438   26.975 5.282   1.00 14.86 ? 6   GLU B N    1 
ATOM   969  C CA   . GLU B 1 6   ? 3.933   28.166 5.967   1.00 17.03 ? 6   GLU B CA   1 
ATOM   970  C C    . GLU B 1 6   ? 4.441   27.774 7.345   1.00 18.75 ? 6   GLU B C    1 
ATOM   971  O O    . GLU B 1 6   ? 3.661   27.347 8.199   1.00 19.22 ? 6   GLU B O    1 
ATOM   972  C CB   . GLU B 1 6   ? 2.842   29.234 6.067   1.00 22.37 ? 6   GLU B CB   1 
ATOM   973  C CG   . GLU B 1 6   ? 2.581   29.943 4.758   1.00 17.63 ? 6   GLU B CG   1 
ATOM   974  C CD   . GLU B 1 6   ? 1.514   31.002 4.868   1.00 23.26 ? 6   GLU B CD   1 
ATOM   975  O OE1  . GLU B 1 6   ? 0.911   31.126 5.952   1.00 20.13 ? 6   GLU B OE1  1 
ATOM   976  O OE2  . GLU B 1 6   ? 1.282   31.701 3.864   1.00 25.09 ? 6   GLU B OE2  1 
ATOM   977  N N    . LEU B 1 7   ? 5.749   27.886 7.537   1.00 19.06 ? 7   LEU B N    1 
ATOM   978  C CA   . LEU B 1 7   ? 6.379   27.752 8.841   1.00 19.64 ? 7   LEU B CA   1 
ATOM   979  C C    . LEU B 1 7   ? 6.706   29.155 9.363   1.00 19.34 ? 7   LEU B C    1 
ATOM   980  O O    . LEU B 1 7   ? 7.324   29.962 8.656   1.00 14.30 ? 7   LEU B O    1 
ATOM   981  C CB   . LEU B 1 7   ? 7.647   26.900 8.729   1.00 17.56 ? 7   LEU B CB   1 
ATOM   982  C CG   . LEU B 1 7   ? 8.584   26.868 9.938   1.00 16.39 ? 7   LEU B CG   1 
ATOM   983  C CD1  . LEU B 1 7   ? 7.859   26.236 11.131  1.00 14.01 ? 7   LEU B CD1  1 
ATOM   984  C CD2  . LEU B 1 7   ? 9.830   26.086 9.591   1.00 13.53 ? 7   LEU B CD2  1 
ATOM   985  N N    . ARG B 1 8   ? 6.288   29.455 10.590  1.00 15.60 ? 8   ARG B N    1 
ATOM   986  C CA   . ARG B 1 8   ? 6.445   30.808 11.099  1.00 18.74 ? 8   ARG B CA   1 
ATOM   987  C C    . ARG B 1 8   ? 7.131   30.782 12.451  1.00 16.60 ? 8   ARG B C    1 
ATOM   988  O O    . ARG B 1 8   ? 6.743   30.005 13.334  1.00 17.35 ? 8   ARG B O    1 
ATOM   989  C CB   . ARG B 1 8   ? 5.091   31.526 11.202  1.00 20.22 ? 8   ARG B CB   1 
ATOM   990  C CG   . ARG B 1 8   ? 4.431   31.788 9.831   1.00 20.50 ? 8   ARG B CG   1 
ATOM   991  C CD   . ARG B 1 8   ? 5.189   32.854 9.050   1.00 23.64 ? 8   ARG B CD   1 
ATOM   992  N NE   . ARG B 1 8   ? 4.550   33.188 7.777   1.00 22.23 ? 8   ARG B NE   1 
ATOM   993  C CZ   . ARG B 1 8   ? 4.830   32.585 6.628   1.00 21.68 ? 8   ARG B CZ   1 
ATOM   994  N NH1  . ARG B 1 8   ? 5.703   31.592 6.565   1.00 20.85 ? 8   ARG B NH1  1 
ATOM   995  N NH2  . ARG B 1 8   ? 4.223   32.988 5.515   1.00 25.76 ? 8   ARG B NH2  1 
ATOM   996  N N    . GLY B 1 9   ? 8.132   31.640 12.613  1.00 14.03 ? 9   GLY B N    1 
ATOM   997  C CA   . GLY B 1 9   ? 8.679   31.875 13.932  1.00 12.69 ? 9   GLY B CA   1 
ATOM   998  C C    . GLY B 1 9   ? 9.566   30.778 14.453  1.00 15.08 ? 9   GLY B C    1 
ATOM   999  O O    . GLY B 1 9   ? 9.639   30.596 15.664  1.00 15.78 ? 9   GLY B O    1 
ATOM   1000 N N    . LEU B 1 10  ? 10.229  30.022 13.572  1.00 15.29 ? 10  LEU B N    1 
ATOM   1001 C CA   . LEU B 1 10  ? 11.264  29.072 14.005  1.00 18.21 ? 10  LEU B CA   1 
ATOM   1002 C C    . LEU B 1 10  ? 12.373  29.829 14.727  1.00 18.02 ? 10  LEU B C    1 
ATOM   1003 O O    . LEU B 1 10  ? 13.029  30.671 14.124  1.00 16.63 ? 10  LEU B O    1 
ATOM   1004 C CB   . LEU B 1 10  ? 11.832  28.316 12.798  1.00 14.56 ? 10  LEU B CB   1 
ATOM   1005 C CG   . LEU B 1 10  ? 12.942  27.272 13.046  1.00 16.42 ? 10  LEU B CG   1 
ATOM   1006 C CD1  . LEU B 1 10  ? 12.434  26.081 13.841  1.00 20.24 ? 10  LEU B CD1  1 
ATOM   1007 C CD2  . LEU B 1 10  ? 13.555  26.806 11.722  1.00 16.96 ? 10  LEU B CD2  1 
ATOM   1008 N N    . THR B 1 11  ? 12.600  29.519 16.004  1.00 17.32 ? 11  THR B N    1 
ATOM   1009 C CA   . THR B 1 11  ? 13.480  30.319 16.862  1.00 13.82 ? 11  THR B CA   1 
ATOM   1010 C C    . THR B 1 11  ? 14.720  29.518 17.235  1.00 17.58 ? 11  THR B C    1 
ATOM   1011 O O    . THR B 1 11  ? 14.615  28.463 17.883  1.00 16.99 ? 11  THR B O    1 
ATOM   1012 C CB   . THR B 1 11  ? 12.727  30.761 18.118  1.00 15.71 ? 11  THR B CB   1 
ATOM   1013 O OG1  . THR B 1 11  ? 11.537  31.461 17.727  1.00 15.87 ? 11  THR B OG1  1 
ATOM   1014 C CG2  . THR B 1 11  ? 13.593  31.655 18.986  1.00 14.95 ? 11  THR B CG2  1 
ATOM   1015 N N    . VAL B 1 12  ? 15.892  30.040 16.864  1.00 18.27 ? 12  VAL B N    1 
ATOM   1016 C CA   . VAL B 1 12  ? 17.143  29.290 16.951  1.00 18.72 ? 12  VAL B CA   1 
ATOM   1017 C C    . VAL B 1 12  ? 18.260  30.247 17.332  1.00 22.77 ? 12  VAL B C    1 
ATOM   1018 O O    . VAL B 1 12  ? 18.411  31.302 16.716  1.00 14.38 ? 12  VAL B O    1 
ATOM   1019 C CB   . VAL B 1 12  ? 17.487  28.594 15.620  1.00 17.53 ? 12  VAL B CB   1 
ATOM   1020 C CG1  . VAL B 1 12  ? 18.751  27.737 15.779  1.00 17.94 ? 12  VAL B CG1  1 
ATOM   1021 C CG2  . VAL B 1 12  ? 16.277  27.778 15.110  1.00 23.03 ? 12  VAL B CG2  1 
ATOM   1022 N N    . HIS B 1 13  ? 19.027  29.885 18.356  1.00 19.54 ? 13  HIS B N    1 
ATOM   1023 C CA   . HIS B 1 13  ? 20.229  30.634 18.703  1.00 16.01 ? 13  HIS B CA   1 
ATOM   1024 C C    . HIS B 1 13  ? 21.321  30.431 17.661  1.00 19.84 ? 13  HIS B C    1 
ATOM   1025 O O    . HIS B 1 13  ? 21.590  29.303 17.240  1.00 20.51 ? 13  HIS B O    1 
ATOM   1026 C CB   . HIS B 1 13  ? 20.737  30.188 20.070  1.00 18.92 ? 13  HIS B CB   1 
ATOM   1027 C CG   . HIS B 1 13  ? 21.890  30.998 20.573  1.00 20.27 ? 13  HIS B CG   1 
ATOM   1028 N ND1  . HIS B 1 13  ? 21.730  32.176 21.266  1.00 19.32 ? 13  HIS B ND1  1 
ATOM   1029 C CD2  . HIS B 1 13  ? 23.225  30.812 20.448  1.00 23.99 ? 13  HIS B CD2  1 
ATOM   1030 C CE1  . HIS B 1 13  ? 22.917  32.677 21.561  1.00 23.65 ? 13  HIS B CE1  1 
ATOM   1031 N NE2  . HIS B 1 13  ? 23.842  31.868 21.074  1.00 25.52 ? 13  HIS B NE2  1 
ATOM   1032 N N    . GLY B 1 14  ? 21.989  31.524 17.283  1.00 16.12 ? 14  GLY B N    1 
ATOM   1033 C CA   . GLY B 1 14  ? 23.056  31.476 16.304  1.00 19.41 ? 14  GLY B CA   1 
ATOM   1034 C C    . GLY B 1 14  ? 24.108  32.537 16.571  1.00 19.99 ? 14  GLY B C    1 
ATOM   1035 O O    . GLY B 1 14  ? 23.998  33.327 17.511  1.00 20.46 ? 14  GLY B O    1 
ATOM   1036 N N    . ARG B 1 15  ? 25.157  32.538 15.737  1.00 19.89 ? 15  ARG B N    1 
ATOM   1037 C CA   . ARG B 1 15  ? 26.280  33.459 15.915  1.00 18.53 ? 15  ARG B CA   1 
ATOM   1038 C C    . ARG B 1 15  ? 26.579  34.261 14.654  1.00 17.39 ? 15  ARG B C    1 
ATOM   1039 O O    . ARG B 1 15  ? 27.679  34.802 14.519  1.00 20.58 ? 15  ARG B O    1 
ATOM   1040 C CB   . ARG B 1 15  ? 27.538  32.709 16.387  1.00 23.71 ? 15  ARG B CB   1 
ATOM   1041 C CG   . ARG B 1 15  ? 27.569  32.386 17.899  1.00 30.51 ? 15  ARG B CG   1 
ATOM   1042 C CD   . ARG B 1 15  ? 28.741  31.441 18.253  1.00 35.38 ? 15  ARG B CD   1 
ATOM   1043 N NE   . ARG B 1 15  ? 29.144  31.456 19.661  1.00 42.11 ? 15  ARG B NE   1 
ATOM   1044 C CZ   . ARG B 1 15  ? 28.345  31.203 20.693  1.00 45.95 ? 15  ARG B CZ   1 
ATOM   1045 N NH1  . ARG B 1 15  ? 27.057  30.921 20.523  1.00 34.84 ? 15  ARG B NH1  1 
ATOM   1046 N NH2  . ARG B 1 15  ? 28.851  31.237 21.930  1.00 35.45 ? 15  ARG B NH2  1 
ATOM   1047 N N    . HIS B 1 16  ? 25.615  34.379 13.741  1.00 19.91 ? 16  HIS B N    1 
ATOM   1048 C CA   . HIS B 1 16  ? 25.808  35.192 12.543  1.00 18.40 ? 16  HIS B CA   1 
ATOM   1049 C C    . HIS B 1 16  ? 25.921  36.675 12.892  1.00 22.83 ? 16  HIS B C    1 
ATOM   1050 O O    . HIS B 1 16  ? 25.351  37.155 13.874  1.00 21.07 ? 16  HIS B O    1 
ATOM   1051 C CB   . HIS B 1 16  ? 24.655  34.959 11.568  1.00 16.08 ? 16  HIS B CB   1 
ATOM   1052 C CG   . HIS B 1 16  ? 24.261  33.521 11.461  1.00 18.98 ? 16  HIS B CG   1 
ATOM   1053 N ND1  . HIS B 1 16  ? 25.035  32.591 10.800  1.00 19.53 ? 16  HIS B ND1  1 
ATOM   1054 C CD2  . HIS B 1 16  ? 23.219  32.837 11.987  1.00 20.25 ? 16  HIS B CD2  1 
ATOM   1055 C CE1  . HIS B 1 16  ? 24.469  31.402 10.895  1.00 24.09 ? 16  HIS B CE1  1 
ATOM   1056 N NE2  . HIS B 1 16  ? 23.367  31.523 11.613  1.00 16.60 ? 16  HIS B NE2  1 
ATOM   1057 N N    . GLY B 1 17  ? 26.668  37.398 12.080  1.00 22.38 ? 17  GLY B N    1 
ATOM   1058 C CA   . GLY B 1 17  ? 26.863  38.814 12.306  1.00 21.79 ? 17  GLY B CA   1 
ATOM   1059 C C    . GLY B 1 17  ? 28.175  39.289 11.716  1.00 25.33 ? 17  GLY B C    1 
ATOM   1060 O O    . GLY B 1 17  ? 29.144  38.549 11.583  1.00 21.66 ? 17  GLY B O    1 
ATOM   1061 N N    . VAL B 1 18  ? 28.203  40.576 11.381  1.00 19.34 ? 18  VAL B N    1 
ATOM   1062 C CA   . VAL B 1 18  ? 29.376  41.198 10.776  1.00 26.54 ? 18  VAL B CA   1 
ATOM   1063 C C    . VAL B 1 18  ? 30.477  41.441 11.802  1.00 23.35 ? 18  VAL B C    1 
ATOM   1064 O O    . VAL B 1 18  ? 31.664  41.379 11.468  1.00 22.84 ? 18  VAL B O    1 
ATOM   1065 C CB   . VAL B 1 18  ? 28.970  42.508 10.071  1.00 21.64 ? 18  VAL B CB   1 
ATOM   1066 C CG1  . VAL B 1 18  ? 30.192  43.263 9.597   1.00 25.85 ? 18  VAL B CG1  1 
ATOM   1067 C CG2  . VAL B 1 18  ? 28.083  42.217 8.878   1.00 22.90 ? 18  VAL B CG2  1 
ATOM   1068 N N    . TYR B 1 19  ? 30.121  41.728 13.045  1.00 22.13 ? 19  TYR B N    1 
ATOM   1069 C CA   . TYR B 1 19  ? 31.073  42.260 14.015  1.00 23.12 ? 19  TYR B CA   1 
ATOM   1070 C C    . TYR B 1 19  ? 31.535  41.209 15.022  1.00 27.37 ? 19  TYR B C    1 
ATOM   1071 O O    . TYR B 1 19  ? 30.771  40.327 15.428  1.00 21.69 ? 19  TYR B O    1 
ATOM   1072 C CB   . TYR B 1 19  ? 30.463  43.457 14.740  1.00 20.63 ? 19  TYR B CB   1 
ATOM   1073 C CG   . TYR B 1 19  ? 30.187  44.586 13.776  1.00 31.40 ? 19  TYR B CG   1 
ATOM   1074 C CD1  . TYR B 1 19  ? 31.229  45.368 13.284  1.00 31.28 ? 19  TYR B CD1  1 
ATOM   1075 C CD2  . TYR B 1 19  ? 28.903  44.838 13.316  1.00 29.55 ? 19  TYR B CD2  1 
ATOM   1076 C CE1  . TYR B 1 19  ? 30.994  46.396 12.381  1.00 33.91 ? 19  TYR B CE1  1 
ATOM   1077 C CE2  . TYR B 1 19  ? 28.654  45.862 12.414  1.00 27.51 ? 19  TYR B CE2  1 
ATOM   1078 C CZ   . TYR B 1 19  ? 29.706  46.635 11.953  1.00 36.80 ? 19  TYR B CZ   1 
ATOM   1079 O OH   . TYR B 1 19  ? 29.471  47.650 11.057  1.00 40.41 ? 19  TYR B OH   1 
ATOM   1080 N N    . ASP B 1 20  ? 32.810  41.320 15.418  1.00 22.75 ? 20  ASP B N    1 
ATOM   1081 C CA   . ASP B 1 20  ? 33.402  40.383 16.369  1.00 24.42 ? 20  ASP B CA   1 
ATOM   1082 C C    . ASP B 1 20  ? 32.561  40.241 17.631  1.00 27.54 ? 20  ASP B C    1 
ATOM   1083 O O    . ASP B 1 20  ? 32.389  39.132 18.150  1.00 28.54 ? 20  ASP B O    1 
ATOM   1084 C CB   . ASP B 1 20  ? 34.814  40.832 16.765  1.00 34.61 ? 20  ASP B CB   1 
ATOM   1085 C CG   . ASP B 1 20  ? 35.850  40.625 15.670  1.00 39.66 ? 20  ASP B CG   1 
ATOM   1086 O OD1  . ASP B 1 20  ? 35.547  40.015 14.618  1.00 32.66 ? 20  ASP B OD1  1 
ATOM   1087 O OD2  . ASP B 1 20  ? 36.993  41.074 15.889  1.00 34.93 ? 20  ASP B OD2  1 
ATOM   1088 N N    . HIS B 1 21  ? 32.036  41.353 18.154  1.00 25.90 ? 21  HIS B N    1 
ATOM   1089 C CA   . HIS B 1 21  ? 31.316  41.270 19.418  1.00 21.22 ? 21  HIS B CA   1 
ATOM   1090 C C    . HIS B 1 21  ? 30.090  40.369 19.316  1.00 26.27 ? 21  HIS B C    1 
ATOM   1091 O O    . HIS B 1 21  ? 29.633  39.851 20.345  1.00 29.81 ? 21  HIS B O    1 
ATOM   1092 C CB   . HIS B 1 21  ? 30.948  42.675 19.911  1.00 25.39 ? 21  HIS B CB   1 
ATOM   1093 C CG   . HIS B 1 21  ? 29.777  43.292 19.207  1.00 26.89 ? 21  HIS B CG   1 
ATOM   1094 N ND1  . HIS B 1 21  ? 28.470  43.085 19.601  1.00 25.48 ? 21  HIS B ND1  1 
ATOM   1095 C CD2  . HIS B 1 21  ? 29.720  44.134 18.148  1.00 21.79 ? 21  HIS B CD2  1 
ATOM   1096 C CE1  . HIS B 1 21  ? 27.662  43.760 18.800  1.00 23.99 ? 21  HIS B CE1  1 
ATOM   1097 N NE2  . HIS B 1 21  ? 28.397  44.398 17.906  1.00 19.59 ? 21  HIS B NE2  1 
ATOM   1098 N N    . GLU B 1 22  ? 29.576  40.139 18.101  1.00 23.54 ? 22  GLU B N    1 
ATOM   1099 C CA   . GLU B 1 22  ? 28.390  39.310 17.901  1.00 20.18 ? 22  GLU B CA   1 
ATOM   1100 C C    . GLU B 1 22  ? 28.703  37.826 17.887  1.00 23.06 ? 22  GLU B C    1 
ATOM   1101 O O    . GLU B 1 22  ? 27.786  37.007 18.047  1.00 26.99 ? 22  GLU B O    1 
ATOM   1102 C CB   . GLU B 1 22  ? 27.718  39.662 16.582  1.00 20.51 ? 22  GLU B CB   1 
ATOM   1103 C CG   . GLU B 1 22  ? 27.114  41.044 16.525  1.00 22.59 ? 22  GLU B CG   1 
ATOM   1104 C CD   . GLU B 1 22  ? 26.439  41.302 15.189  1.00 24.68 ? 22  GLU B CD   1 
ATOM   1105 O OE1  . GLU B 1 22  ? 25.235  40.972 15.071  1.00 20.10 ? 22  GLU B OE1  1 
ATOM   1106 O OE2  . GLU B 1 22  ? 27.125  41.813 14.267  1.00 24.51 ? 22  GLU B OE2  1 
ATOM   1107 N N    . ARG B 1 23  ? 29.963  37.457 17.657  1.00 25.33 ? 23  ARG B N    1 
ATOM   1108 C CA   . ARG B 1 23  ? 30.354  36.058 17.658  1.00 22.75 ? 23  ARG B CA   1 
ATOM   1109 C C    . ARG B 1 23  ? 30.700  35.524 19.039  1.00 27.99 ? 23  ARG B C    1 
ATOM   1110 O O    . ARG B 1 23  ? 30.860  34.307 19.185  1.00 30.27 ? 23  ARG B O    1 
ATOM   1111 C CB   . ARG B 1 23  ? 31.532  35.835 16.700  1.00 30.47 ? 23  ARG B CB   1 
ATOM   1112 C CG   . ARG B 1 23  ? 31.107  35.820 15.236  1.00 39.95 ? 23  ARG B CG   1 
ATOM   1113 C CD   . ARG B 1 23  ? 32.272  35.861 14.252  1.00 46.61 ? 23  ARG B CD   1 
ATOM   1114 N NE   . ARG B 1 23  ? 32.399  37.159 13.595  1.00 41.19 ? 23  ARG B NE   1 
ATOM   1115 C CZ   . ARG B 1 23  ? 33.528  37.847 13.497  1.00 48.46 ? 23  ARG B CZ   1 
ATOM   1116 N NH1  . ARG B 1 23  ? 34.660  37.397 14.022  1.00 50.26 ? 23  ARG B NH1  1 
ATOM   1117 N NH2  . ARG B 1 23  ? 33.523  39.013 12.851  1.00 39.06 ? 23  ARG B NH2  1 
ATOM   1118 N N    . VAL B 1 24  ? 30.805  36.384 20.053  1.00 20.72 ? 24  VAL B N    1 
ATOM   1119 C CA   . VAL B 1 24  ? 31.189  35.913 21.385  1.00 27.22 ? 24  VAL B CA   1 
ATOM   1120 C C    . VAL B 1 24  ? 30.081  35.054 21.993  1.00 24.06 ? 24  VAL B C    1 
ATOM   1121 O O    . VAL B 1 24  ? 30.303  33.889 22.346  1.00 27.04 ? 24  VAL B O    1 
ATOM   1122 C CB   . VAL B 1 24  ? 31.556  37.095 22.303  1.00 25.42 ? 24  VAL B CB   1 
ATOM   1123 C CG1  . VAL B 1 24  ? 31.900  36.594 23.705  1.00 24.26 ? 24  VAL B CG1  1 
ATOM   1124 C CG2  . VAL B 1 24  ? 32.745  37.863 21.742  1.00 20.71 ? 24  VAL B CG2  1 
ATOM   1125 N N    . ALA B 1 25  ? 28.877  35.623 22.139  1.00 20.12 ? 25  ALA B N    1 
ATOM   1126 C CA   . ALA B 1 25  ? 27.740  34.925 22.730  1.00 26.26 ? 25  ALA B CA   1 
ATOM   1127 C C    . ALA B 1 25  ? 26.625  34.599 21.743  1.00 24.14 ? 25  ALA B C    1 
ATOM   1128 O O    . ALA B 1 25  ? 25.795  33.739 22.039  1.00 20.69 ? 25  ALA B O    1 
ATOM   1129 C CB   . ALA B 1 25  ? 27.148  35.752 23.880  1.00 21.35 ? 25  ALA B CB   1 
ATOM   1130 N N    . GLY B 1 26  ? 26.588  35.243 20.589  1.00 22.54 ? 26  GLY B N    1 
ATOM   1131 C CA   . GLY B 1 26  ? 25.525  34.982 19.658  1.00 20.26 ? 26  GLY B CA   1 
ATOM   1132 C C    . GLY B 1 26  ? 24.235  35.650 20.097  1.00 24.29 ? 26  GLY B C    1 
ATOM   1133 O O    . GLY B 1 26  ? 24.190  36.436 21.048  1.00 19.06 ? 26  GLY B O    1 
ATOM   1134 N N    . GLN B 1 27  ? 23.164  35.330 19.375  1.00 19.97 ? 27  GLN B N    1 
ATOM   1135 C CA   . GLN B 1 27  ? 21.885  35.992 19.605  1.00 17.66 ? 27  GLN B CA   1 
ATOM   1136 C C    . GLN B 1 27  ? 20.782  35.144 18.982  1.00 20.16 ? 27  GLN B C    1 
ATOM   1137 O O    . GLN B 1 27  ? 21.049  34.130 18.334  1.00 16.96 ? 27  GLN B O    1 
ATOM   1138 C CB   . GLN B 1 27  ? 21.876  37.409 19.026  1.00 18.04 ? 27  GLN B CB   1 
ATOM   1139 C CG   . GLN B 1 27  ? 22.067  37.422 17.511  1.00 17.21 ? 27  GLN B CG   1 
ATOM   1140 C CD   . GLN B 1 27  ? 22.396  38.795 16.975  1.00 20.58 ? 27  GLN B CD   1 
ATOM   1141 O OE1  . GLN B 1 27  ? 21.510  39.624 16.803  1.00 14.55 ? 27  GLN B OE1  1 
ATOM   1142 N NE2  . GLN B 1 27  ? 23.676  39.038 16.699  1.00 18.44 ? 27  GLN B NE2  1 
ATOM   1143 N N    . ARG B 1 28  ? 19.538  35.579 19.200  1.00 17.60 ? 28  ARG B N    1 
ATOM   1144 C CA   . ARG B 1 28  ? 18.336  34.922 18.694  1.00 18.76 ? 28  ARG B CA   1 
ATOM   1145 C C    . ARG B 1 28  ? 18.124  35.198 17.216  1.00 19.72 ? 28  ARG B C    1 
ATOM   1146 O O    . ARG B 1 28  ? 18.142  36.360 16.789  1.00 17.02 ? 28  ARG B O    1 
ATOM   1147 C CB   . ARG B 1 28  ? 17.105  35.445 19.449  1.00 18.05 ? 28  ARG B CB   1 
ATOM   1148 C CG   . ARG B 1 28  ? 15.766  34.823 19.023  1.00 24.01 ? 28  ARG B CG   1 
ATOM   1149 C CD   . ARG B 1 28  ? 14.744  34.829 20.174  1.00 20.13 ? 28  ARG B CD   1 
ATOM   1150 N NE   . ARG B 1 28  ? 15.358  34.442 21.440  1.00 33.39 ? 28  ARG B NE   1 
ATOM   1151 C CZ   . ARG B 1 28  ? 15.197  35.067 22.600  1.00 37.55 ? 28  ARG B CZ   1 
ATOM   1152 N NH1  . ARG B 1 28  ? 14.475  36.182 22.698  1.00 32.50 ? 28  ARG B NH1  1 
ATOM   1153 N NH2  . ARG B 1 28  ? 15.781  34.566 23.687  1.00 22.99 ? 28  ARG B NH2  1 
ATOM   1154 N N    . PHE B 1 29  ? 17.826  34.150 16.450  1.00 15.63 ? 29  PHE B N    1 
ATOM   1155 C CA   . PHE B 1 29  ? 17.344  34.319 15.085  1.00 16.13 ? 29  PHE B CA   1 
ATOM   1156 C C    . PHE B 1 29  ? 15.964  33.688 14.943  1.00 17.62 ? 29  PHE B C    1 
ATOM   1157 O O    . PHE B 1 29  ? 15.664  32.675 15.570  1.00 16.23 ? 29  PHE B O    1 
ATOM   1158 C CB   . PHE B 1 29  ? 18.312  33.706 14.073  1.00 14.85 ? 29  PHE B CB   1 
ATOM   1159 C CG   . PHE B 1 29  ? 19.640  34.392 14.049  1.00 16.32 ? 29  PHE B CG   1 
ATOM   1160 C CD1  . PHE B 1 29  ? 20.632  34.035 14.945  1.00 17.06 ? 29  PHE B CD1  1 
ATOM   1161 C CD2  . PHE B 1 29  ? 19.877  35.439 13.167  1.00 16.58 ? 29  PHE B CD2  1 
ATOM   1162 C CE1  . PHE B 1 29  ? 21.849  34.700 14.959  1.00 17.59 ? 29  PHE B CE1  1 
ATOM   1163 C CE2  . PHE B 1 29  ? 21.114  36.104 13.161  1.00 17.40 ? 29  PHE B CE2  1 
ATOM   1164 C CZ   . PHE B 1 29  ? 22.091  35.734 14.067  1.00 17.88 ? 29  PHE B CZ   1 
ATOM   1165 N N    . VAL B 1 30  ? 15.122  34.294 14.112  1.00 17.02 ? 30  VAL B N    1 
ATOM   1166 C CA   . VAL B 1 30  ? 13.754  33.816 13.926  1.00 15.17 ? 30  VAL B CA   1 
ATOM   1167 C C    . VAL B 1 30  ? 13.525  33.637 12.436  1.00 16.19 ? 30  VAL B C    1 
ATOM   1168 O O    . VAL B 1 30  ? 13.727  34.578 11.661  1.00 17.35 ? 30  VAL B O    1 
ATOM   1169 C CB   . VAL B 1 30  ? 12.727  34.778 14.552  1.00 18.74 ? 30  VAL B CB   1 
ATOM   1170 C CG1  . VAL B 1 30  ? 11.313  34.263 14.368  1.00 17.28 ? 30  VAL B CG1  1 
ATOM   1171 C CG2  . VAL B 1 30  ? 13.024  34.941 16.045  1.00 12.81 ? 30  VAL B CG2  1 
ATOM   1172 N N    . ILE B 1 31  ? 13.115  32.425 12.042  1.00 17.27 ? 31  ILE B N    1 
ATOM   1173 C CA   . ILE B 1 31  ? 13.015  32.032 10.634  1.00 15.75 ? 31  ILE B CA   1 
ATOM   1174 C C    . ILE B 1 31  ? 11.547  31.821 10.284  1.00 15.26 ? 31  ILE B C    1 
ATOM   1175 O O    . ILE B 1 31  ? 10.814  31.151 11.022  1.00 14.65 ? 31  ILE B O    1 
ATOM   1176 C CB   . ILE B 1 31  ? 13.809  30.738 10.350  1.00 14.44 ? 31  ILE B CB   1 
ATOM   1177 C CG1  . ILE B 1 31  ? 15.308  30.903 10.597  1.00 21.31 ? 31  ILE B CG1  1 
ATOM   1178 C CG2  . ILE B 1 31  ? 13.529  30.235 8.918   1.00 16.69 ? 31  ILE B CG2  1 
ATOM   1179 C CD1  . ILE B 1 31  ? 15.871  32.296 10.438  1.00 22.06 ? 31  ILE B CD1  1 
ATOM   1180 N N    . ASP B 1 32  ? 11.129  32.367 9.148   1.00 16.29 ? 32  ASP B N    1 
ATOM   1181 C CA   . ASP B 1 32  ? 9.912   31.953 8.460   1.00 15.21 ? 32  ASP B CA   1 
ATOM   1182 C C    . ASP B 1 32  ? 10.292  31.322 7.124   1.00 16.48 ? 32  ASP B C    1 
ATOM   1183 O O    . ASP B 1 32  ? 11.178  31.829 6.427   1.00 15.24 ? 32  ASP B O    1 
ATOM   1184 C CB   . ASP B 1 32  ? 8.968   33.126 8.153   1.00 14.32 ? 32  ASP B CB   1 
ATOM   1185 C CG   . ASP B 1 32  ? 8.679   34.007 9.347   1.00 20.62 ? 32  ASP B CG   1 
ATOM   1186 O OD1  . ASP B 1 32  ? 8.514   33.480 10.480  1.00 17.04 ? 32  ASP B OD1  1 
ATOM   1187 O OD2  . ASP B 1 32  ? 8.585   35.239 9.133   1.00 18.64 ? 32  ASP B OD2  1 
ATOM   1188 N N    . VAL B 1 33  ? 9.599   30.244 6.747   1.00 18.21 ? 33  VAL B N    1 
ATOM   1189 C CA   . VAL B 1 33  ? 9.722   29.672 5.404   1.00 17.85 ? 33  VAL B CA   1 
ATOM   1190 C C    . VAL B 1 33  ? 8.333   29.567 4.796   1.00 19.57 ? 33  VAL B C    1 
ATOM   1191 O O    . VAL B 1 33  ? 7.376   29.176 5.474   1.00 18.34 ? 33  VAL B O    1 
ATOM   1192 C CB   . VAL B 1 33  ? 10.388  28.284 5.395   1.00 18.26 ? 33  VAL B CB   1 
ATOM   1193 C CG1  . VAL B 1 33  ? 10.611  27.786 3.905   1.00 16.98 ? 33  VAL B CG1  1 
ATOM   1194 C CG2  . VAL B 1 33  ? 11.675  28.285 6.221   1.00 20.13 ? 33  VAL B CG2  1 
ATOM   1195 N N    . THR B 1 34  ? 8.224   29.919 3.517   1.00 16.23 ? 34  THR B N    1 
ATOM   1196 C CA   . THR B 1 34  ? 6.998   29.705 2.764   1.00 21.15 ? 34  THR B CA   1 
ATOM   1197 C C    . THR B 1 34  ? 7.359   28.930 1.508   1.00 19.72 ? 34  THR B C    1 
ATOM   1198 O O    . THR B 1 34  ? 8.268   29.329 0.773   1.00 20.17 ? 34  THR B O    1 
ATOM   1199 C CB   . THR B 1 34  ? 6.290   31.026 2.409   1.00 23.58 ? 34  THR B CB   1 
ATOM   1200 O OG1  . THR B 1 34  ? 5.990   31.764 3.604   1.00 18.86 ? 34  THR B OG1  1 
ATOM   1201 C CG2  . THR B 1 34  ? 4.997   30.734 1.670   1.00 21.02 ? 34  THR B CG2  1 
ATOM   1202 N N    . VAL B 1 35  ? 6.678   27.810 1.291   1.00 16.14 ? 35  VAL B N    1 
ATOM   1203 C CA   . VAL B 1 35  ? 6.950   26.898 0.185   1.00 16.59 ? 35  VAL B CA   1 
ATOM   1204 C C    . VAL B 1 35  ? 5.716   26.839 -0.700  1.00 24.10 ? 35  VAL B C    1 
ATOM   1205 O O    . VAL B 1 35  ? 4.640   26.430 -0.241  1.00 18.93 ? 35  VAL B O    1 
ATOM   1206 C CB   . VAL B 1 35  ? 7.310   25.489 0.681   1.00 19.65 ? 35  VAL B CB   1 
ATOM   1207 C CG1  . VAL B 1 35  ? 7.641   24.602 -0.511  1.00 19.43 ? 35  VAL B CG1  1 
ATOM   1208 C CG2  . VAL B 1 35  ? 8.484   25.542 1.645   1.00 18.12 ? 35  VAL B CG2  1 
ATOM   1209 N N    . TRP B 1 36  ? 5.872   27.226 -1.967  1.00 20.67 ? 36  TRP B N    1 
ATOM   1210 C CA   . TRP B 1 36  ? 4.802   27.122 -2.954  1.00 20.20 ? 36  TRP B CA   1 
ATOM   1211 C C    . TRP B 1 36  ? 4.915   25.776 -3.670  1.00 23.11 ? 36  TRP B C    1 
ATOM   1212 O O    . TRP B 1 36  ? 5.949   25.473 -4.281  1.00 20.68 ? 36  TRP B O    1 
ATOM   1213 C CB   . TRP B 1 36  ? 4.849   28.289 -3.947  1.00 20.69 ? 36  TRP B CB   1 
ATOM   1214 C CG   . TRP B 1 36  ? 4.316   29.580 -3.343  1.00 24.32 ? 36  TRP B CG   1 
ATOM   1215 C CD1  . TRP B 1 36  ? 3.011   30.028 -3.354  1.00 23.27 ? 36  TRP B CD1  1 
ATOM   1216 C CD2  . TRP B 1 36  ? 5.071   30.571 -2.624  1.00 19.68 ? 36  TRP B CD2  1 
ATOM   1217 N NE1  . TRP B 1 36  ? 2.922   31.228 -2.686  1.00 21.70 ? 36  TRP B NE1  1 
ATOM   1218 C CE2  . TRP B 1 36  ? 4.164   31.580 -2.222  1.00 18.51 ? 36  TRP B CE2  1 
ATOM   1219 C CE3  . TRP B 1 36  ? 6.419   30.693 -2.267  1.00 18.59 ? 36  TRP B CE3  1 
ATOM   1220 C CZ2  . TRP B 1 36  ? 4.571   32.712 -1.507  1.00 22.45 ? 36  TRP B CZ2  1 
ATOM   1221 C CZ3  . TRP B 1 36  ? 6.818   31.817 -1.536  1.00 23.78 ? 36  TRP B CZ3  1 
ATOM   1222 C CH2  . TRP B 1 36  ? 5.900   32.811 -1.176  1.00 22.34 ? 36  TRP B CH2  1 
ATOM   1223 N N    . ILE B 1 37  ? 3.853   24.975 -3.587  1.00 21.12 ? 37  ILE B N    1 
ATOM   1224 C CA   . ILE B 1 37  ? 3.882   23.569 -3.989  1.00 22.67 ? 37  ILE B CA   1 
ATOM   1225 C C    . ILE B 1 37  ? 2.440   23.111 -4.184  1.00 32.21 ? 37  ILE B C    1 
ATOM   1226 O O    . ILE B 1 37  ? 1.546   23.500 -3.424  1.00 27.34 ? 37  ILE B O    1 
ATOM   1227 C CB   . ILE B 1 37  ? 4.622   22.703 -2.937  1.00 19.27 ? 37  ILE B CB   1 
ATOM   1228 C CG1  . ILE B 1 37  ? 4.516   21.216 -3.268  1.00 23.76 ? 37  ILE B CG1  1 
ATOM   1229 C CG2  . ILE B 1 37  ? 4.072   22.956 -1.516  1.00 22.06 ? 37  ILE B CG2  1 
ATOM   1230 C CD1  . ILE B 1 37  ? 5.606   20.338 -2.601  1.00 27.56 ? 37  ILE B CD1  1 
ATOM   1231 N N    . ASP B 1 38  ? 2.216   22.271 -5.202  1.00 26.45 ? 38  ASP B N    1 
ATOM   1232 C CA   . ASP B 1 38  ? 0.876   21.737 -5.439  1.00 28.70 ? 38  ASP B CA   1 
ATOM   1233 C C    . ASP B 1 38  ? 0.544   20.686 -4.388  1.00 28.06 ? 38  ASP B C    1 
ATOM   1234 O O    . ASP B 1 38  ? 1.251   19.683 -4.263  1.00 24.93 ? 38  ASP B O    1 
ATOM   1235 C CB   . ASP B 1 38  ? 0.756   21.138 -6.838  1.00 32.47 ? 38  ASP B CB   1 
ATOM   1236 C CG   . ASP B 1 38  ? -0.697  21.059 -7.321  1.00 43.07 ? 38  ASP B CG   1 
ATOM   1237 O OD1  . ASP B 1 38  ? -1.624  21.255 -6.502  1.00 40.78 ? 38  ASP B OD1  1 
ATOM   1238 O OD2  . ASP B 1 38  ? -0.915  20.803 -8.526  1.00 49.03 ? 38  ASP B OD2  1 
ATOM   1239 N N    . LEU B 1 39  ? -0.552  20.903 -3.654  1.00 23.26 ? 39  LEU B N    1 
ATOM   1240 C CA   . LEU B 1 39  ? -0.940  20.045 -2.540  1.00 20.29 ? 39  LEU B CA   1 
ATOM   1241 C C    . LEU B 1 39  ? -2.155  19.171 -2.841  1.00 23.53 ? 39  LEU B C    1 
ATOM   1242 O O    . LEU B 1 39  ? -2.585  18.399 -1.971  1.00 22.76 ? 39  LEU B O    1 
ATOM   1243 C CB   . LEU B 1 39  ? -1.218  20.910 -1.315  1.00 21.58 ? 39  LEU B CB   1 
ATOM   1244 C CG   . LEU B 1 39  ? -0.011  21.684 -0.777  1.00 19.23 ? 39  LEU B CG   1 
ATOM   1245 C CD1  . LEU B 1 39  ? -0.432  22.520 0.424   1.00 17.54 ? 39  LEU B CD1  1 
ATOM   1246 C CD2  . LEU B 1 39  ? 1.063   20.699 -0.396  1.00 19.81 ? 39  LEU B CD2  1 
ATOM   1247 N N    . ALA B 1 40  ? -2.708  19.251 -4.050  1.00 20.96 ? 40  ALA B N    1 
ATOM   1248 C CA   . ALA B 1 40  ? -3.885  18.453 -4.376  1.00 25.03 ? 40  ALA B CA   1 
ATOM   1249 C C    . ALA B 1 40  ? -3.594  16.962 -4.265  1.00 27.93 ? 40  ALA B C    1 
ATOM   1250 O O    . ALA B 1 40  ? -4.428  16.197 -3.766  1.00 27.03 ? 40  ALA B O    1 
ATOM   1251 C CB   . ALA B 1 40  ? -4.384  18.795 -5.783  1.00 28.82 ? 40  ALA B CB   1 
ATOM   1252 N N    . GLU B 1 41  ? -2.423  16.524 -4.743  1.00 27.30 ? 41  GLU B N    1 
ATOM   1253 C CA   . GLU B 1 41  ? -2.106  15.099 -4.712  1.00 26.46 ? 41  GLU B CA   1 
ATOM   1254 C C    . GLU B 1 41  ? -2.066  14.591 -3.275  1.00 26.08 ? 41  GLU B C    1 
ATOM   1255 O O    . GLU B 1 41  ? -2.657  13.553 -2.947  1.00 27.03 ? 41  GLU B O    1 
ATOM   1256 C CB   . GLU B 1 41  ? -0.774  14.839 -5.428  1.00 27.41 ? 41  GLU B CB   1 
ATOM   1257 C CG   . GLU B 1 41  ? -0.255  13.405 -5.291  1.00 35.07 ? 41  GLU B CG   1 
ATOM   1258 C CD   . GLU B 1 41  ? 0.934   13.096 -6.213  1.00 47.27 ? 41  GLU B CD   1 
ATOM   1259 O OE1  . GLU B 1 41  ? 1.338   13.980 -7.003  1.00 47.51 ? 41  GLU B OE1  1 
ATOM   1260 O OE2  . GLU B 1 41  ? 1.451   11.955 -6.161  1.00 56.31 ? 41  GLU B OE2  1 
ATOM   1261 N N    . ALA B 1 42  ? -1.378  15.327 -2.402  1.00 22.14 ? 42  ALA B N    1 
ATOM   1262 C CA   . ALA B 1 42  ? -1.297  14.950 -0.996  1.00 20.77 ? 42  ALA B CA   1 
ATOM   1263 C C    . ALA B 1 42  ? -2.672  14.897 -0.345  1.00 23.14 ? 42  ALA B C    1 
ATOM   1264 O O    . ALA B 1 42  ? -2.940  14.021 0.482   1.00 25.69 ? 42  ALA B O    1 
ATOM   1265 C CB   . ALA B 1 42  ? -0.389  15.931 -0.260  1.00 21.22 ? 42  ALA B CB   1 
ATOM   1266 N N    . ALA B 1 43  ? -3.550  15.843 -0.673  1.00 25.65 ? 43  ALA B N    1 
ATOM   1267 C CA   . ALA B 1 43  ? -4.902  15.782 -0.129  1.00 27.22 ? 43  ALA B CA   1 
ATOM   1268 C C    . ALA B 1 43  ? -5.676  14.605 -0.703  1.00 31.30 ? 43  ALA B C    1 
ATOM   1269 O O    . ALA B 1 43  ? -6.515  14.022 -0.012  1.00 26.98 ? 43  ALA B O    1 
ATOM   1270 C CB   . ALA B 1 43  ? -5.642  17.090 -0.399  1.00 23.10 ? 43  ALA B CB   1 
ATOM   1271 N N    . ASN B 1 44  ? -5.398  14.231 -1.954  1.00 26.07 ? 44  ASN B N    1 
ATOM   1272 C CA   . ASN B 1 44  ? -6.047  13.065 -2.541  1.00 30.35 ? 44  ASN B CA   1 
ATOM   1273 C C    . ASN B 1 44  ? -5.575  11.785 -1.852  1.00 31.29 ? 44  ASN B C    1 
ATOM   1274 O O    . ASN B 1 44  ? -6.389  10.954 -1.434  1.00 31.30 ? 44  ASN B O    1 
ATOM   1275 C CB   . ASN B 1 44  ? -5.750  13.014 -4.044  1.00 31.12 ? 44  ASN B CB   1 
ATOM   1276 C CG   . ASN B 1 44  ? -6.402  11.812 -4.741  1.00 43.29 ? 44  ASN B CG   1 
ATOM   1277 O OD1  . ASN B 1 44  ? -7.454  11.325 -4.315  1.00 45.13 ? 44  ASN B OD1  1 
ATOM   1278 N ND2  . ASN B 1 44  ? -5.757  11.314 -5.796  1.00 44.58 ? 44  ASN B ND2  1 
ATOM   1279 N N    . SER B 1 45  ? -4.255  11.622 -1.704  1.00 30.35 ? 45  SER B N    1 
ATOM   1280 C CA   . SER B 1 45  ? -3.682  10.404 -1.135  1.00 24.03 ? 45  SER B CA   1 
ATOM   1281 C C    . SER B 1 45  ? -3.718  10.388 0.390   1.00 26.99 ? 45  SER B C    1 
ATOM   1282 O O    . SER B 1 45  ? -3.744  9.307  0.994   1.00 25.28 ? 45  SER B O    1 
ATOM   1283 C CB   . SER B 1 45  ? -2.232  10.240 -1.583  1.00 28.98 ? 45  SER B CB   1 
ATOM   1284 O OG   . SER B 1 45  ? -1.411  11.263 -1.026  1.00 22.88 ? 45  SER B OG   1 
ATOM   1285 N N    . ASP B 1 46  ? -3.687  11.561 1.021   1.00 22.43 ? 46  ASP B N    1 
ATOM   1286 C CA   . ASP B 1 46  ? -3.471  11.689 2.462   1.00 26.14 ? 46  ASP B CA   1 
ATOM   1287 C C    . ASP B 1 46  ? -2.158  11.020 2.872   1.00 27.21 ? 46  ASP B C    1 
ATOM   1288 O O    . ASP B 1 46  ? -2.032  10.514 3.986   1.00 25.77 ? 46  ASP B O    1 
ATOM   1289 C CB   . ASP B 1 46  ? -4.655  11.123 3.261   1.00 24.12 ? 46  ASP B CB   1 
ATOM   1290 C CG   . ASP B 1 46  ? -4.744  11.695 4.689   1.00 22.76 ? 46  ASP B CG   1 
ATOM   1291 O OD1  . ASP B 1 46  ? -4.338  12.849 4.902   1.00 21.31 ? 46  ASP B OD1  1 
ATOM   1292 O OD2  . ASP B 1 46  ? -5.242  10.996 5.602   1.00 24.99 ? 46  ASP B OD2  1 
ATOM   1293 N N    A ASP B 1 47  ? -1.178  11.019 1.963   0.50 24.86 ? 47  ASP B N    1 
ATOM   1294 N N    B ASP B 1 47  ? -1.198  11.039 1.959   0.50 24.82 ? 47  ASP B N    1 
ATOM   1295 C CA   A ASP B 1 47  ? 0.119   10.373 2.156   0.50 25.85 ? 47  ASP B CA   1 
ATOM   1296 C CA   B ASP B 1 47  ? 0.103   10.362 2.160   0.50 25.84 ? 47  ASP B CA   1 
ATOM   1297 C C    A ASP B 1 47  ? 1.192   11.438 2.332   0.50 24.57 ? 47  ASP B C    1 
ATOM   1298 C C    B ASP B 1 47  ? 1.191   11.424 2.340   0.50 24.56 ? 47  ASP B C    1 
ATOM   1299 O O    A ASP B 1 47  ? 1.389   12.272 1.444   0.50 24.35 ? 47  ASP B O    1 
ATOM   1300 O O    B ASP B 1 47  ? 1.334   12.250 1.466   0.50 24.29 ? 47  ASP B O    1 
ATOM   1301 C CB   A ASP B 1 47  ? 0.479   9.482  0.964   0.50 25.06 ? 47  ASP B CB   1 
ATOM   1302 C CB   B ASP B 1 47  ? 0.341   9.428  0.977   0.50 25.09 ? 47  ASP B CB   1 
ATOM   1303 C CG   A ASP B 1 47  ? -0.270  8.158  0.966   0.50 26.47 ? 47  ASP B CG   1 
ATOM   1304 C CG   B ASP B 1 47  ? 1.649   8.681  1.036   0.50 26.78 ? 47  ASP B CG   1 
ATOM   1305 O OD1  A ASP B 1 47  ? -0.539  7.628  2.066   0.50 29.73 ? 47  ASP B OD1  1 
ATOM   1306 O OD1  B ASP B 1 47  ? 2.591   9.231  1.598   0.50 26.48 ? 47  ASP B OD1  1 
ATOM   1307 O OD2  A ASP B 1 47  ? -0.596  7.647  -0.132  0.50 25.87 ? 47  ASP B OD2  1 
ATOM   1308 O OD2  B ASP B 1 47  ? 1.709   7.578  0.483   0.50 26.20 ? 47  ASP B OD2  1 
ATOM   1309 N N    . LEU B 1 48  ? 1.904   11.380 3.461   1.00 23.94 ? 48  LEU B N    1 
ATOM   1310 C CA   . LEU B 1 48  ? 2.935   12.368 3.752   1.00 25.23 ? 48  LEU B CA   1 
ATOM   1311 C C    . LEU B 1 48  ? 3.959   12.456 2.631   1.00 21.26 ? 48  LEU B C    1 
ATOM   1312 O O    . LEU B 1 48  ? 4.471   13.541 2.333   1.00 22.62 ? 48  LEU B O    1 
ATOM   1313 C CB   . LEU B 1 48  ? 3.611   12.016 5.080   1.00 24.34 ? 48  LEU B CB   1 
ATOM   1314 C CG   . LEU B 1 48  ? 4.749   12.891 5.618   1.00 28.26 ? 48  LEU B CG   1 
ATOM   1315 C CD1  . LEU B 1 48  ? 4.410   14.392 5.738   1.00 19.92 ? 48  LEU B CD1  1 
ATOM   1316 C CD2  . LEU B 1 48  ? 5.300   12.322 6.920   1.00 21.63 ? 48  LEU B CD2  1 
ATOM   1317 N N    . ALA B 1 49  ? 4.258   11.328 1.989   1.00 25.98 ? 49  ALA B N    1 
ATOM   1318 C CA   . ALA B 1 49  ? 5.206   11.315 0.886   1.00 28.54 ? 49  ALA B CA   1 
ATOM   1319 C C    . ALA B 1 49  ? 4.803   12.250 -0.249  1.00 26.45 ? 49  ALA B C    1 
ATOM   1320 O O    . ALA B 1 49  ? 5.671   12.703 -0.999  1.00 24.72 ? 49  ALA B O    1 
ATOM   1321 C CB   . ALA B 1 49  ? 5.369   9.886  0.356   1.00 26.86 ? 49  ALA B CB   1 
ATOM   1322 N N    . ASP B 1 50  ? 3.522   12.569 -0.392  1.00 26.99 ? 50  ASP B N    1 
ATOM   1323 C CA   . ASP B 1 50  ? 3.092   13.406 -1.500  1.00 25.32 ? 50  ASP B CA   1 
ATOM   1324 C C    . ASP B 1 50  ? 3.159   14.905 -1.199  1.00 19.49 ? 50  ASP B C    1 
ATOM   1325 O O    . ASP B 1 50  ? 2.769   15.710 -2.053  1.00 25.92 ? 50  ASP B O    1 
ATOM   1326 C CB   . ASP B 1 50  ? 1.677   13.009 -1.919  1.00 22.49 ? 50  ASP B CB   1 
ATOM   1327 C CG   . ASP B 1 50  ? 1.641   11.669 -2.639  1.00 25.63 ? 50  ASP B CG   1 
ATOM   1328 O OD1  . ASP B 1 50  ? 2.663   11.295 -3.231  1.00 27.56 ? 50  ASP B OD1  1 
ATOM   1329 O OD2  . ASP B 1 50  ? 0.608   10.970 -2.580  1.00 28.86 ? 50  ASP B OD2  1 
ATOM   1330 N N    . THR B 1 51  ? 3.642   15.311 -0.028  1.00 24.42 ? 51  THR B N    1 
ATOM   1331 C CA   . THR B 1 51  ? 3.799   16.728 0.292   1.00 21.22 ? 51  THR B CA   1 
ATOM   1332 C C    . THR B 1 51  ? 5.214   16.956 0.813   1.00 20.91 ? 51  THR B C    1 
ATOM   1333 O O    . THR B 1 51  ? 6.020   16.021 0.902   1.00 20.36 ? 51  THR B O    1 
ATOM   1334 C CB   . THR B 1 51  ? 2.738   17.201 1.302   1.00 22.40 ? 51  THR B CB   1 
ATOM   1335 O OG1  . THR B 1 51  ? 2.809   18.623 1.444   1.00 19.96 ? 51  THR B OG1  1 
ATOM   1336 C CG2  . THR B 1 51  ? 2.944   16.546 2.671   1.00 20.62 ? 51  THR B CG2  1 
ATOM   1337 N N    . TYR B 1 52  ? 5.536   18.213 1.128   1.00 18.97 ? 52  TYR B N    1 
ATOM   1338 C CA   . TYR B 1 52  ? 6.810   18.545 1.766   1.00 21.60 ? 52  TYR B CA   1 
ATOM   1339 C C    . TYR B 1 52  ? 6.637   18.484 3.280   1.00 23.24 ? 52  TYR B C    1 
ATOM   1340 O O    . TYR B 1 52  ? 5.851   19.251 3.847   1.00 21.45 ? 52  TYR B O    1 
ATOM   1341 C CB   . TYR B 1 52  ? 7.291   19.930 1.339   1.00 20.44 ? 52  TYR B CB   1 
ATOM   1342 C CG   . TYR B 1 52  ? 8.784   20.185 1.508   1.00 21.56 ? 52  TYR B CG   1 
ATOM   1343 C CD1  . TYR B 1 52  ? 9.385   20.142 2.763   1.00 23.06 ? 52  TYR B CD1  1 
ATOM   1344 C CD2  . TYR B 1 52  ? 9.574   20.515 0.424   1.00 21.51 ? 52  TYR B CD2  1 
ATOM   1345 C CE1  . TYR B 1 52  ? 10.739  20.388 2.924   1.00 20.78 ? 52  TYR B CE1  1 
ATOM   1346 C CE2  . TYR B 1 52  ? 10.940  20.771 0.575   1.00 25.79 ? 52  TYR B CE2  1 
ATOM   1347 C CZ   . TYR B 1 52  ? 11.518  20.712 1.824   1.00 23.38 ? 52  TYR B CZ   1 
ATOM   1348 O OH   . TYR B 1 52  ? 12.888  20.969 1.983   1.00 22.04 ? 52  TYR B OH   1 
ATOM   1349 N N    . ASP B 1 53  ? 7.367   17.579 3.931   1.00 19.16 ? 53  ASP B N    1 
ATOM   1350 C CA   . ASP B 1 53  ? 7.193   17.352 5.365   1.00 20.39 ? 53  ASP B CA   1 
ATOM   1351 C C    . ASP B 1 53  ? 7.667   18.561 6.156   1.00 16.69 ? 53  ASP B C    1 
ATOM   1352 O O    . ASP B 1 53  ? 8.833   18.944 6.051   1.00 21.18 ? 53  ASP B O    1 
ATOM   1353 C CB   . ASP B 1 53  ? 7.957   16.095 5.780   1.00 22.09 ? 53  ASP B CB   1 
ATOM   1354 C CG   . ASP B 1 53  ? 7.785   15.756 7.246   1.00 23.07 ? 53  ASP B CG   1 
ATOM   1355 O OD1  . ASP B 1 53  ? 7.101   16.505 7.984   1.00 19.50 ? 53  ASP B OD1  1 
ATOM   1356 O OD2  . ASP B 1 53  ? 8.316   14.704 7.663   1.00 25.70 ? 53  ASP B OD2  1 
ATOM   1357 N N    . TYR B 1 54  ? 6.769   19.176 6.946   1.00 17.78 ? 54  TYR B N    1 
ATOM   1358 C CA   . TYR B 1 54  ? 7.158   20.396 7.655   1.00 20.43 ? 54  TYR B CA   1 
ATOM   1359 C C    . TYR B 1 54  ? 8.151   20.118 8.786   1.00 19.18 ? 54  TYR B C    1 
ATOM   1360 O O    . TYR B 1 54  ? 8.807   21.052 9.274   1.00 18.35 ? 54  TYR B O    1 
ATOM   1361 C CB   . TYR B 1 54  ? 5.923   21.165 8.198   1.00 18.88 ? 54  TYR B CB   1 
ATOM   1362 C CG   . TYR B 1 54  ? 5.037   20.428 9.193   1.00 18.80 ? 54  TYR B CG   1 
ATOM   1363 C CD1  . TYR B 1 54  ? 5.547   19.920 10.371  1.00 23.54 ? 54  TYR B CD1  1 
ATOM   1364 C CD2  . TYR B 1 54  ? 3.677   20.269 8.961   1.00 23.15 ? 54  TYR B CD2  1 
ATOM   1365 C CE1  . TYR B 1 54  ? 4.734   19.241 11.290  1.00 26.74 ? 54  TYR B CE1  1 
ATOM   1366 C CE2  . TYR B 1 54  ? 2.848   19.588 9.882   1.00 22.02 ? 54  TYR B CE2  1 
ATOM   1367 C CZ   . TYR B 1 54  ? 3.383   19.077 11.039  1.00 27.57 ? 54  TYR B CZ   1 
ATOM   1368 O OH   . TYR B 1 54  ? 2.571   18.388 11.955  1.00 25.92 ? 54  TYR B OH   1 
ATOM   1369 N N    . VAL B 1 55  ? 8.270   18.863 9.218   1.00 16.75 ? 55  VAL B N    1 
ATOM   1370 C CA   . VAL B 1 55  ? 9.311   18.496 10.179  1.00 19.70 ? 55  VAL B CA   1 
ATOM   1371 C C    . VAL B 1 55  ? 10.693  18.615 9.539   1.00 20.76 ? 55  VAL B C    1 
ATOM   1372 O O    . VAL B 1 55  ? 11.620  19.200 10.117  1.00 17.85 ? 55  VAL B O    1 
ATOM   1373 C CB   . VAL B 1 55  ? 9.053   17.076 10.716  1.00 17.24 ? 55  VAL B CB   1 
ATOM   1374 C CG1  . VAL B 1 55  ? 10.188  16.629 11.639  1.00 19.41 ? 55  VAL B CG1  1 
ATOM   1375 C CG2  . VAL B 1 55  ? 7.726   17.029 11.450  1.00 20.20 ? 55  VAL B CG2  1 
ATOM   1376 N N    . ARG B 1 56  ? 10.819  18.098 8.327   1.00 18.30 ? 56  ARG B N    1 
ATOM   1377 C CA   . ARG B 1 56  ? 12.088  18.200 7.575   1.00 21.45 ? 56  ARG B CA   1 
ATOM   1378 C C    . ARG B 1 56  ? 12.396  19.689 7.358   1.00 24.28 ? 56  ARG B C    1 
ATOM   1379 O O    . ARG B 1 56  ? 13.499  20.077 7.543   1.00 23.27 ? 56  ARG B O    1 
ATOM   1380 C CB   . ARG B 1 56  ? 11.944  17.476 6.236   1.00 22.07 ? 56  ARG B CB   1 
ATOM   1381 C CG   . ARG B 1 56  ? 12.943  17.894 5.175   1.00 32.57 ? 56  ARG B CG   1 
ATOM   1382 C CD   . ARG B 1 56  ? 13.144  16.952 3.998   1.00 36.40 ? 56  ARG B CD   1 
ATOM   1383 N NE   . ARG B 1 56  ? 12.159  16.954 2.922   1.00 43.81 ? 56  ARG B NE   1 
ATOM   1384 C CZ   . ARG B 1 56  ? 12.411  17.265 1.646   1.00 46.96 ? 56  ARG B CZ   1 
ATOM   1385 N NH1  . ARG B 1 56  ? 13.618  17.680 1.303   1.00 49.84 ? 56  ARG B NH1  1 
ATOM   1386 N NH2  . ARG B 1 56  ? 11.467  17.192 0.719   1.00 27.60 ? 56  ARG B NH2  1 
ATOM   1387 N N    . LEU B 1 57  ? 11.380  20.462 7.002   1.00 20.26 ? 57  LEU B N    1 
ATOM   1388 C CA   A LEU B 1 57  ? 11.570  21.892 6.786   0.34 21.31 ? 57  LEU B CA   1 
ATOM   1389 C CA   B LEU B 1 57  ? 11.561  21.891 6.786   0.66 21.24 ? 57  LEU B CA   1 
ATOM   1390 C C    . LEU B 1 57  ? 12.127  22.574 8.031   1.00 22.80 ? 57  LEU B C    1 
ATOM   1391 O O    . LEU B 1 57  ? 13.113  23.315 7.959   1.00 17.39 ? 57  LEU B O    1 
ATOM   1392 C CB   A LEU B 1 57  ? 10.242  22.524 6.365   0.34 22.42 ? 57  LEU B CB   1 
ATOM   1393 C CB   B LEU B 1 57  ? 10.214  22.502 6.390   0.66 21.69 ? 57  LEU B CB   1 
ATOM   1394 C CG   A LEU B 1 57  ? 10.176  24.037 6.157   0.34 21.52 ? 57  LEU B CG   1 
ATOM   1395 C CG   B LEU B 1 57  ? 10.160  23.813 5.613   0.66 23.54 ? 57  LEU B CG   1 
ATOM   1396 C CD1  A LEU B 1 57  ? 11.197  24.486 5.121   0.34 19.86 ? 57  LEU B CD1  1 
ATOM   1397 C CD1  B LEU B 1 57  ? 10.666  23.592 4.190   0.66 17.87 ? 57  LEU B CD1  1 
ATOM   1398 C CD2  A LEU B 1 57  ? 8.762   24.432 5.734   0.34 20.13 ? 57  LEU B CD2  1 
ATOM   1399 C CD2  B LEU B 1 57  ? 8.728   24.373 5.612   0.66 20.05 ? 57  LEU B CD2  1 
ATOM   1400 N N    . ALA B 1 58  ? 11.515  22.326 9.191   1.00 17.45 ? 58  ALA B N    1 
ATOM   1401 C CA   . ALA B 1 58  ? 11.958  22.983 10.417  1.00 16.34 ? 58  ALA B CA   1 
ATOM   1402 C C    . ALA B 1 58  ? 13.333  22.489 10.862  1.00 19.45 ? 58  ALA B C    1 
ATOM   1403 O O    . ALA B 1 58  ? 14.213  23.290 11.203  1.00 20.60 ? 58  ALA B O    1 
ATOM   1404 C CB   . ALA B 1 58  ? 10.917  22.763 11.518  1.00 12.61 ? 58  ALA B CB   1 
ATOM   1405 N N    . SER B 1 59  ? 13.536  21.170 10.895  1.00 16.58 ? 59  SER B N    1 
ATOM   1406 C CA   . SER B 1 59  ? 14.781  20.646 11.446  1.00 24.15 ? 59  SER B CA   1 
ATOM   1407 C C    . SER B 1 59  ? 15.978  21.084 10.616  1.00 21.41 ? 59  SER B C    1 
ATOM   1408 O O    . SER B 1 59  ? 17.008  21.483 11.167  1.00 21.74 ? 59  SER B O    1 
ATOM   1409 C CB   . SER B 1 59  ? 14.721  19.122 11.547  1.00 30.06 ? 59  SER B CB   1 
ATOM   1410 O OG   . SER B 1 59  ? 14.434  18.540 10.291  1.00 35.98 ? 59  SER B OG   1 
ATOM   1411 N N    . ARG B 1 60  ? 15.862  21.028 9.287   1.00 24.17 ? 60  ARG B N    1 
ATOM   1412 C CA   . ARG B 1 60  ? 16.993  21.410 8.444   1.00 23.28 ? 60  ARG B CA   1 
ATOM   1413 C C    . ARG B 1 60  ? 17.276  22.909 8.535   1.00 20.23 ? 60  ARG B C    1 
ATOM   1414 O O    . ARG B 1 60  ? 18.437  23.317 8.667   1.00 21.01 ? 60  ARG B O    1 
ATOM   1415 C CB   . ARG B 1 60  ? 16.741  20.982 6.997   1.00 25.03 ? 60  ARG B CB   1 
ATOM   1416 C CG   . ARG B 1 60  ? 16.448  19.480 6.808   1.00 24.57 ? 60  ARG B CG   1 
ATOM   1417 C CD   . ARG B 1 60  ? 17.701  18.609 6.983   1.00 29.30 ? 60  ARG B CD   1 
ATOM   1418 N NE   . ARG B 1 60  ? 18.002  18.377 8.390   1.00 32.55 ? 60  ARG B NE   1 
ATOM   1419 C CZ   . ARG B 1 60  ? 17.439  17.419 9.117   1.00 32.99 ? 60  ARG B CZ   1 
ATOM   1420 N NH1  . ARG B 1 60  ? 16.546  16.590 8.596   1.00 33.59 ? 60  ARG B NH1  1 
ATOM   1421 N NH2  . ARG B 1 60  ? 17.762  17.304 10.402  1.00 39.85 ? 60  ARG B NH2  1 
ATOM   1422 N N    . ALA B 1 61  ? 16.237  23.751 8.482   1.00 18.19 ? 61  ALA B N    1 
ATOM   1423 C CA   . ALA B 1 61  ? 16.470  25.188 8.624   1.00 17.35 ? 61  ALA B CA   1 
ATOM   1424 C C    . ALA B 1 61  ? 17.171  25.500 9.940   1.00 19.57 ? 61  ALA B C    1 
ATOM   1425 O O    . ALA B 1 61  ? 18.128  26.284 9.974   1.00 18.93 ? 61  ALA B O    1 
ATOM   1426 C CB   . ALA B 1 61  ? 15.155  25.971 8.538   1.00 18.58 ? 61  ALA B CB   1 
ATOM   1427 N N    . ALA B 1 62  ? 16.713  24.887 11.034  1.00 18.81 ? 62  ALA B N    1 
ATOM   1428 C CA   . ALA B 1 62  ? 17.335  25.093 12.341  1.00 18.59 ? 62  ALA B CA   1 
ATOM   1429 C C    . ALA B 1 62  ? 18.807  24.679 12.341  1.00 21.81 ? 62  ALA B C    1 
ATOM   1430 O O    . ALA B 1 62  ? 19.665  25.395 12.872  1.00 18.88 ? 62  ALA B O    1 
ATOM   1431 C CB   . ALA B 1 62  ? 16.551  24.322 13.405  1.00 20.02 ? 62  ALA B CB   1 
ATOM   1432 N N    . GLU B 1 63  ? 19.118  23.512 11.759  1.00 20.56 ? 63  GLU B N    1 
ATOM   1433 C CA   . GLU B 1 63  ? 20.510  23.073 11.679  1.00 24.59 ? 63  GLU B CA   1 
ATOM   1434 C C    . GLU B 1 63  ? 21.383  24.105 10.968  1.00 18.43 ? 63  GLU B C    1 
ATOM   1435 O O    . GLU B 1 63  ? 22.511  24.382 11.402  1.00 19.19 ? 63  GLU B O    1 
ATOM   1436 C CB   . GLU B 1 63  ? 20.609  21.720 10.965  1.00 21.46 ? 63  GLU B CB   1 
ATOM   1437 C CG   . GLU B 1 63  ? 20.334  20.533 11.845  1.00 33.60 ? 63  GLU B CG   1 
ATOM   1438 C CD   . GLU B 1 63  ? 19.929  19.300 11.041  1.00 37.92 ? 63  GLU B CD   1 
ATOM   1439 O OE1  . GLU B 1 63  ? 20.423  19.172 9.898   1.00 38.88 ? 63  GLU B OE1  1 
ATOM   1440 O OE2  . GLU B 1 63  ? 19.131  18.473 11.547  1.00 39.26 ? 63  GLU B OE2  1 
ATOM   1441 N N    . ILE B 1 64  ? 20.885  24.683 9.878   1.00 15.89 ? 64  ILE B N    1 
ATOM   1442 C CA   . ILE B 1 64  ? 21.648  25.724 9.186   1.00 24.17 ? 64  ILE B CA   1 
ATOM   1443 C C    . ILE B 1 64  ? 21.846  26.931 10.107  1.00 20.80 ? 64  ILE B C    1 
ATOM   1444 O O    . ILE B 1 64  ? 22.967  27.404 10.309  1.00 19.32 ? 64  ILE B O    1 
ATOM   1445 C CB   . ILE B 1 64  ? 20.954  26.113 7.861   1.00 20.62 ? 64  ILE B CB   1 
ATOM   1446 C CG1  . ILE B 1 64  ? 21.036  24.976 6.834   1.00 18.43 ? 64  ILE B CG1  1 
ATOM   1447 C CG2  . ILE B 1 64  ? 21.500  27.444 7.281   1.00 16.86 ? 64  ILE B CG2  1 
ATOM   1448 C CD1  . ILE B 1 64  ? 20.023  25.120 5.695   1.00 15.97 ? 64  ILE B CD1  1 
ATOM   1449 N N    . VAL B 1 65  ? 20.764  27.406 10.732  1.00 20.98 ? 65  VAL B N    1 
ATOM   1450 C CA   . VAL B 1 65  ? 20.854  28.615 11.556  1.00 17.18 ? 65  VAL B CA   1 
ATOM   1451 C C    . VAL B 1 65  ? 21.845  28.428 12.702  1.00 21.66 ? 65  VAL B C    1 
ATOM   1452 O O    . VAL B 1 65  ? 22.621  29.335 13.032  1.00 19.48 ? 65  VAL B O    1 
ATOM   1453 C CB   . VAL B 1 65  ? 19.461  28.996 12.083  1.00 19.12 ? 65  VAL B CB   1 
ATOM   1454 C CG1  . VAL B 1 65  ? 19.584  30.183 13.034  1.00 17.87 ? 65  VAL B CG1  1 
ATOM   1455 C CG2  . VAL B 1 65  ? 18.522  29.301 10.921  1.00 13.49 ? 65  VAL B CG2  1 
ATOM   1456 N N    . ALA B 1 66  ? 21.809  27.267 13.351  1.00 19.08 ? 66  ALA B N    1 
ATOM   1457 C CA   . ALA B 1 66  ? 22.700  26.957 14.463  1.00 22.68 ? 66  ALA B CA   1 
ATOM   1458 C C    . ALA B 1 66  ? 24.111  26.587 14.028  1.00 25.06 ? 66  ALA B C    1 
ATOM   1459 O O    . ALA B 1 66  ? 24.979  26.425 14.892  1.00 23.58 ? 66  ALA B O    1 
ATOM   1460 C CB   . ALA B 1 66  ? 22.126  25.806 15.285  1.00 25.36 ? 66  ALA B CB   1 
ATOM   1461 N N    . GLY B 1 67  ? 24.359  26.447 12.730  1.00 20.39 ? 67  GLY B N    1 
ATOM   1462 C CA   . GLY B 1 67  ? 25.618  25.939 12.228  1.00 21.66 ? 67  GLY B CA   1 
ATOM   1463 C C    . GLY B 1 67  ? 26.671  27.018 12.053  1.00 22.67 ? 67  GLY B C    1 
ATOM   1464 O O    . GLY B 1 67  ? 26.697  28.009 12.791  1.00 20.35 ? 67  GLY B O    1 
ATOM   1465 N N    . PRO B 1 68  ? 27.585  26.831 11.098  1.00 25.54 ? 68  PRO B N    1 
ATOM   1466 C CA   . PRO B 1 68  ? 28.716  27.764 10.957  1.00 27.01 ? 68  PRO B CA   1 
ATOM   1467 C C    . PRO B 1 68  ? 28.227  29.192 10.821  1.00 24.26 ? 68  PRO B C    1 
ATOM   1468 O O    . PRO B 1 68  ? 27.314  29.474 10.026  1.00 21.93 ? 68  PRO B O    1 
ATOM   1469 C CB   . PRO B 1 68  ? 29.433  27.297 9.678   1.00 27.87 ? 68  PRO B CB   1 
ATOM   1470 C CG   . PRO B 1 68  ? 28.912  25.948 9.377   1.00 28.66 ? 68  PRO B CG   1 
ATOM   1471 C CD   . PRO B 1 68  ? 27.706  25.657 10.217  1.00 28.96 ? 68  PRO B CD   1 
ATOM   1472 N N    . PRO B 1 69  ? 28.816  30.120 11.572  1.00 25.69 ? 69  PRO B N    1 
ATOM   1473 C CA   . PRO B 1 69  ? 28.309  31.497 11.564  1.00 26.52 ? 69  PRO B CA   1 
ATOM   1474 C C    . PRO B 1 69  ? 28.566  32.156 10.220  1.00 24.90 ? 69  PRO B C    1 
ATOM   1475 O O    . PRO B 1 69  ? 29.641  32.011 9.633   1.00 27.03 ? 69  PRO B O    1 
ATOM   1476 C CB   . PRO B 1 69  ? 29.115  32.184 12.672  1.00 24.92 ? 69  PRO B CB   1 
ATOM   1477 C CG   . PRO B 1 69  ? 29.543  31.090 13.581  1.00 30.67 ? 69  PRO B CG   1 
ATOM   1478 C CD   . PRO B 1 69  ? 29.680  29.845 12.736  1.00 25.02 ? 69  PRO B CD   1 
ATOM   1479 N N    . ARG B 1 70  ? 27.583  32.902 9.740   1.00 18.91 ? 70  ARG B N    1 
ATOM   1480 C CA   . ARG B 1 70  ? 27.783  33.730 8.562   1.00 26.25 ? 70  ARG B CA   1 
ATOM   1481 C C    . ARG B 1 70  ? 27.893  35.190 8.995   1.00 22.42 ? 70  ARG B C    1 
ATOM   1482 O O    . ARG B 1 70  ? 27.455  35.583 10.078  1.00 21.41 ? 70  ARG B O    1 
ATOM   1483 C CB   . ARG B 1 70  ? 26.632  33.570 7.563   1.00 20.25 ? 70  ARG B CB   1 
ATOM   1484 C CG   . ARG B 1 70  ? 26.354  32.122 7.171   1.00 22.39 ? 70  ARG B CG   1 
ATOM   1485 C CD   . ARG B 1 70  ? 27.579  31.323 6.748   1.00 25.11 ? 70  ARG B CD   1 
ATOM   1486 N NE   . ARG B 1 70  ? 27.169  30.000 6.281   1.00 23.89 ? 70  ARG B NE   1 
ATOM   1487 C CZ   . ARG B 1 70  ? 27.992  28.974 6.108   1.00 28.81 ? 70  ARG B CZ   1 
ATOM   1488 N NH1  . ARG B 1 70  ? 29.294  29.096 6.302   1.00 23.22 ? 70  ARG B NH1  1 
ATOM   1489 N NH2  . ARG B 1 70  ? 27.493  27.792 5.740   1.00 22.82 ? 70  ARG B NH2  1 
ATOM   1490 N N    . LYS B 1 71  ? 28.496  36.005 8.137   1.00 21.74 ? 71  LYS B N    1 
ATOM   1491 C CA   . LYS B 1 71  ? 28.536  37.430 8.434   1.00 19.05 ? 71  LYS B CA   1 
ATOM   1492 C C    . LYS B 1 71  ? 27.158  38.062 8.212   1.00 19.54 ? 71  LYS B C    1 
ATOM   1493 O O    . LYS B 1 71  ? 26.706  38.880 9.019   1.00 15.56 ? 71  LYS B O    1 
ATOM   1494 C CB   . LYS B 1 71  ? 29.614  38.074 7.567   1.00 22.05 ? 71  LYS B CB   1 
ATOM   1495 C CG   . LYS B 1 71  ? 31.016  37.986 8.191   1.00 23.45 ? 71  LYS B CG   1 
ATOM   1496 C CD   . LYS B 1 71  ? 31.820  39.209 7.848   1.00 33.98 ? 71  LYS B CD   1 
ATOM   1497 C CE   . LYS B 1 71  ? 32.418  39.896 9.072   1.00 47.77 ? 71  LYS B CE   1 
ATOM   1498 N NZ   . LYS B 1 71  ? 33.343  41.003 8.664   1.00 43.46 ? 71  LYS B NZ   1 
ATOM   1499 N N    . LEU B 1 72  ? 26.458  37.658 7.152   1.00 19.34 ? 72  LEU B N    1 
ATOM   1500 C CA   . LEU B 1 72  ? 25.189  38.255 6.739   1.00 17.18 ? 72  LEU B CA   1 
ATOM   1501 C C    . LEU B 1 72  ? 24.034  37.280 6.942   1.00 16.32 ? 72  LEU B C    1 
ATOM   1502 O O    . LEU B 1 72  ? 24.175  36.077 6.689   1.00 18.14 ? 72  LEU B O    1 
ATOM   1503 C CB   . LEU B 1 72  ? 25.246  38.652 5.251   1.00 19.08 ? 72  LEU B CB   1 
ATOM   1504 C CG   . LEU B 1 72  ? 26.325  39.645 4.816   1.00 20.51 ? 72  LEU B CG   1 
ATOM   1505 C CD1  . LEU B 1 72  ? 26.077  40.097 3.411   1.00 16.77 ? 72  LEU B CD1  1 
ATOM   1506 C CD2  . LEU B 1 72  ? 26.385  40.854 5.751   1.00 18.02 ? 72  LEU B CD2  1 
ATOM   1507 N N    . ILE B 1 73  ? 22.866  37.803 7.332   1.00 17.02 ? 73  ILE B N    1 
ATOM   1508 C CA   . ILE B 1 73  ? 21.681  36.949 7.350   1.00 14.41 ? 73  ILE B CA   1 
ATOM   1509 C C    . ILE B 1 73  ? 21.220  36.616 5.925   1.00 17.17 ? 73  ILE B C    1 
ATOM   1510 O O    . ILE B 1 73  ? 20.557  35.597 5.727   1.00 19.60 ? 73  ILE B O    1 
ATOM   1511 C CB   . ILE B 1 73  ? 20.559  37.585 8.207   1.00 14.40 ? 73  ILE B CB   1 
ATOM   1512 C CG1  . ILE B 1 73  ? 20.296  39.038 7.816   1.00 18.27 ? 73  ILE B CG1  1 
ATOM   1513 C CG2  . ILE B 1 73  ? 20.938  37.575 9.711   1.00 16.90 ? 73  ILE B CG2  1 
ATOM   1514 C CD1  . ILE B 1 73  ? 19.091  39.655 8.547   1.00 17.52 ? 73  ILE B CD1  1 
ATOM   1515 N N    . GLU B 1 74  ? 21.583  37.432 4.919   1.00 15.67 ? 74  GLU B N    1 
ATOM   1516 C CA   . GLU B 1 74  ? 21.351  37.077 3.514   1.00 16.06 ? 74  GLU B CA   1 
ATOM   1517 C C    . GLU B 1 74  ? 21.923  35.700 3.170   1.00 20.38 ? 74  GLU B C    1 
ATOM   1518 O O    . GLU B 1 74  ? 21.297  34.902 2.452   1.00 18.96 ? 74  GLU B O    1 
ATOM   1519 C CB   . GLU B 1 74  ? 21.987  38.134 2.599   1.00 17.25 ? 74  GLU B CB   1 
ATOM   1520 C CG   . GLU B 1 74  ? 21.200  39.454 2.453   1.00 18.78 ? 74  GLU B CG   1 
ATOM   1521 C CD   . GLU B 1 74  ? 21.536  40.483 3.529   1.00 17.93 ? 74  GLU B CD   1 
ATOM   1522 O OE1  . GLU B 1 74  ? 22.071  40.090 4.589   1.00 17.07 ? 74  GLU B OE1  1 
ATOM   1523 O OE2  . GLU B 1 74  ? 21.276  41.689 3.308   1.00 18.92 ? 74  GLU B OE2  1 
ATOM   1524 N N    . THR B 1 75  ? 23.119  35.413 3.671   1.00 19.12 ? 75  THR B N    1 
ATOM   1525 C CA   . THR B 1 75  ? 23.788  34.156 3.376   1.00 17.19 ? 75  THR B CA   1 
ATOM   1526 C C    . THR B 1 75  ? 23.072  32.978 4.021   1.00 19.70 ? 75  THR B C    1 
ATOM   1527 O O    . THR B 1 75  ? 22.985  31.894 3.427   1.00 17.67 ? 75  THR B O    1 
ATOM   1528 C CB   . THR B 1 75  ? 25.230  34.246 3.865   1.00 19.38 ? 75  THR B CB   1 
ATOM   1529 O OG1  . THR B 1 75  ? 25.790  35.483 3.401   1.00 23.52 ? 75  THR B OG1  1 
ATOM   1530 C CG2  . THR B 1 75  ? 26.058  33.079 3.303   1.00 19.12 ? 75  THR B CG2  1 
ATOM   1531 N N    . VAL B 1 76  ? 22.586  33.171 5.246   1.00 15.64 ? 76  VAL B N    1 
ATOM   1532 C CA   . VAL B 1 76  ? 21.801  32.143 5.924   1.00 19.12 ? 76  VAL B CA   1 
ATOM   1533 C C    . VAL B 1 76  ? 20.528  31.855 5.147   1.00 20.36 ? 76  VAL B C    1 
ATOM   1534 O O    . VAL B 1 76  ? 20.191  30.698 4.881   1.00 19.69 ? 76  VAL B O    1 
ATOM   1535 C CB   . VAL B 1 76  ? 21.481  32.583 7.364   1.00 15.70 ? 76  VAL B CB   1 
ATOM   1536 C CG1  . VAL B 1 76  ? 20.638  31.528 8.080   1.00 16.65 ? 76  VAL B CG1  1 
ATOM   1537 C CG2  . VAL B 1 76  ? 22.766  32.895 8.135   1.00 18.44 ? 76  VAL B CG2  1 
ATOM   1538 N N    . GLY B 1 77  ? 19.791  32.906 4.789   1.00 15.70 ? 77  GLY B N    1 
ATOM   1539 C CA   . GLY B 1 77  ? 18.545  32.708 4.076   1.00 16.02 ? 77  GLY B CA   1 
ATOM   1540 C C    . GLY B 1 77  ? 18.736  32.011 2.745   1.00 17.64 ? 77  GLY B C    1 
ATOM   1541 O O    . GLY B 1 77  ? 17.916  31.178 2.342   1.00 19.04 ? 77  GLY B O    1 
ATOM   1542 N N    . ALA B 1 78  ? 19.799  32.371 2.026   1.00 18.85 ? 78  ALA B N    1 
ATOM   1543 C CA   . ALA B 1 78  ? 20.051  31.738 0.741   1.00 20.43 ? 78  ALA B CA   1 
ATOM   1544 C C    . ALA B 1 78  ? 20.404  30.258 0.915   1.00 17.37 ? 78  ALA B C    1 
ATOM   1545 O O    . ALA B 1 78  ? 20.008  29.421 0.098   1.00 21.83 ? 78  ALA B O    1 
ATOM   1546 C CB   . ALA B 1 78  ? 21.155  32.498 0.003   1.00 20.09 ? 78  ALA B CB   1 
ATOM   1547 N N    . GLU B 1 79  ? 21.144  29.906 1.972   1.00 19.11 ? 79  GLU B N    1 
ATOM   1548 C CA   . GLU B 1 79  ? 21.428  28.489 2.193   1.00 19.43 ? 79  GLU B CA   1 
ATOM   1549 C C    . GLU B 1 79  ? 20.135  27.717 2.427   1.00 18.69 ? 79  GLU B C    1 
ATOM   1550 O O    . GLU B 1 79  ? 19.908  26.659 1.819   1.00 18.61 ? 79  GLU B O    1 
ATOM   1551 C CB   . GLU B 1 79  ? 22.392  28.298 3.366   1.00 16.81 ? 79  GLU B CB   1 
ATOM   1552 C CG   . GLU B 1 79  ? 22.830  26.839 3.556   1.00 20.12 ? 79  GLU B CG   1 
ATOM   1553 C CD   . GLU B 1 79  ? 23.976  26.675 4.541   1.00 24.18 ? 79  GLU B CD   1 
ATOM   1554 O OE1  . GLU B 1 79  ? 24.629  27.679 4.879   1.00 23.84 ? 79  GLU B OE1  1 
ATOM   1555 O OE2  . GLU B 1 79  ? 24.233  25.532 4.979   1.00 26.94 ? 79  GLU B OE2  1 
ATOM   1556 N N    . ILE B 1 80  ? 19.267  28.229 3.303   1.00 15.93 ? 80  ILE B N    1 
ATOM   1557 C CA   . ILE B 1 80  ? 18.015  27.528 3.581   1.00 17.39 ? 80  ILE B CA   1 
ATOM   1558 C C    . ILE B 1 80  ? 17.209  27.381 2.295   1.00 19.93 ? 80  ILE B C    1 
ATOM   1559 O O    . ILE B 1 80  ? 16.722  26.295 1.965   1.00 18.93 ? 80  ILE B O    1 
ATOM   1560 C CB   . ILE B 1 80  ? 17.208  28.259 4.675   1.00 22.15 ? 80  ILE B CB   1 
ATOM   1561 C CG1  . ILE B 1 80  ? 18.009  28.314 5.981   1.00 15.54 ? 80  ILE B CG1  1 
ATOM   1562 C CG2  . ILE B 1 80  ? 15.841  27.570 4.898   1.00 17.46 ? 80  ILE B CG2  1 
ATOM   1563 C CD1  . ILE B 1 80  ? 17.454  29.312 7.015   1.00 16.35 ? 80  ILE B CD1  1 
ATOM   1564 N N    . ALA B 1 81  ? 17.112  28.452 1.531   1.00 19.41 ? 81  ALA B N    1 
ATOM   1565 C CA   . ALA B 1 81  ? 16.306  28.461 0.294   1.00 18.83 ? 81  ALA B CA   1 
ATOM   1566 C C    . ALA B 1 81  ? 16.858  27.482 -0.742  1.00 22.62 ? 81  ALA B C    1 
ATOM   1567 O O    . ALA B 1 81  ? 16.094  26.742 -1.263  1.00 21.66 ? 81  ALA B O    1 
ATOM   1568 C CB   . ALA B 1 81  ? 16.215  29.850 -0.240  1.00 21.57 ? 81  ALA B CB   1 
ATOM   1569 N N    . ASP B 1 82  ? 18.169  27.474 -0.948  1.00 21.03 ? 82  ASP B N    1 
ATOM   1570 C CA   . ASP B 1 82  ? 18.853  26.608 -1.941  1.00 21.94 ? 82  ASP B CA   1 
ATOM   1571 C C    . ASP B 1 82  ? 18.571  25.124 -1.658  1.00 22.29 ? 82  ASP B C    1 
ATOM   1572 O O    . ASP B 1 82  ? 18.273  24.392 -2.571  1.00 21.23 ? 82  ASP B O    1 
ATOM   1573 C CB   . ASP B 1 82  ? 20.351  26.854 -1.886  1.00 22.43 ? 82  ASP B CB   1 
ATOM   1574 C CG   . ASP B 1 82  ? 21.075  26.071 -2.953  1.00 34.39 ? 82  ASP B CG   1 
ATOM   1575 O OD1  . ASP B 1 82  ? 20.925  26.427 -4.095  1.00 33.13 ? 82  ASP B OD1  1 
ATOM   1576 O OD2  . ASP B 1 82  ? 21.736  25.089 -2.603  1.00 37.33 ? 82  ASP B OD2  1 
ATOM   1577 N N    . HIS B 1 83  ? 18.661  24.747 -0.389  1.00 24.38 ? 83  HIS B N    1 
ATOM   1578 C CA   . HIS B 1 83  ? 18.409  23.359 0.043   1.00 21.79 ? 83  HIS B CA   1 
ATOM   1579 C C    . HIS B 1 83  ? 16.928  23.013 -0.155  1.00 22.84 ? 83  HIS B C    1 
ATOM   1580 O O    . HIS B 1 83  ? 16.657  21.896 -0.556  1.00 24.56 ? 83  HIS B O    1 
ATOM   1581 C CB   . HIS B 1 83  ? 18.907  23.180 1.469   1.00 20.59 ? 83  HIS B CB   1 
ATOM   1582 C CG   . HIS B 1 83  ? 20.357  22.888 1.590   1.00 23.17 ? 83  HIS B CG   1 
ATOM   1583 N ND1  . HIS B 1 83  ? 21.324  23.863 1.506   1.00 28.09 ? 83  HIS B ND1  1 
ATOM   1584 C CD2  . HIS B 1 83  ? 21.007  21.726 1.771   1.00 22.97 ? 83  HIS B CD2  1 
ATOM   1585 C CE1  . HIS B 1 83  ? 22.499  23.317 1.660   1.00 25.02 ? 83  HIS B CE1  1 
ATOM   1586 N NE2  . HIS B 1 83  ? 22.326  22.009 1.817   1.00 32.05 ? 83  HIS B NE2  1 
ATOM   1587 N N    . VAL B 1 84  ? 16.024  23.953 0.101   1.00 17.73 ? 84  VAL B N    1 
ATOM   1588 C CA   . VAL B 1 84  ? 14.573  23.658 -0.070  1.00 18.86 ? 84  VAL B CA   1 
ATOM   1589 C C    . VAL B 1 84  ? 14.292  23.339 -1.548  1.00 20.37 ? 84  VAL B C    1 
ATOM   1590 O O    . VAL B 1 84  ? 13.606  22.386 -1.801  1.00 21.59 ? 84  VAL B O    1 
ATOM   1591 C CB   . VAL B 1 84  ? 13.660  24.776 0.452   1.00 21.74 ? 84  VAL B CB   1 
ATOM   1592 C CG1  . VAL B 1 84  ? 12.250  24.602 -0.047  1.00 22.09 ? 84  VAL B CG1  1 
ATOM   1593 C CG2  . VAL B 1 84  ? 13.693  24.904 1.964   1.00 21.37 ? 84  VAL B CG2  1 
ATOM   1594 N N    . MET B 1 85  ? 14.842  24.114 -2.476  1.00 23.69 ? 85  MET B N    1 
ATOM   1595 C CA   . MET B 1 85  ? 14.643  23.848 -3.911  1.00 22.84 ? 85  MET B CA   1 
ATOM   1596 C C    . MET B 1 85  ? 15.292  22.578 -4.445  1.00 20.91 ? 85  MET B C    1 
ATOM   1597 O O    . MET B 1 85  ? 15.066  22.291 -5.629  1.00 20.76 ? 85  MET B O    1 
ATOM   1598 C CB   . MET B 1 85  ? 15.071  25.043 -4.777  1.00 22.79 ? 85  MET B CB   1 
ATOM   1599 C CG   . MET B 1 85  ? 14.656  26.396 -4.228  1.00 18.94 ? 85  MET B CG   1 
ATOM   1600 S SD   . MET B 1 85  ? 12.923  26.578 -4.816  1.00 26.21 ? 85  MET B SD   1 
ATOM   1601 C CE   . MET B 1 85  ? 13.147  26.519 -6.594  1.00 28.30 ? 85  MET B CE   1 
ATOM   1602 N N    . ASP B 1 86  ? 16.023  21.787 -3.659  1.00 19.94 ? 86  ASP B N    1 
ATOM   1603 C CA   . ASP B 1 86  ? 16.369  20.457 -4.149  1.00 19.80 ? 86  ASP B CA   1 
ATOM   1604 C C    . ASP B 1 86  ? 15.112  19.635 -4.410  1.00 25.69 ? 86  ASP B C    1 
ATOM   1605 O O    . ASP B 1 86  ? 15.086  18.804 -5.321  1.00 21.27 ? 86  ASP B O    1 
ATOM   1606 C CB   . ASP B 1 86  ? 17.276  19.731 -3.157  1.00 23.36 ? 86  ASP B CB   1 
ATOM   1607 C CG   . ASP B 1 86  ? 18.677  20.322 -3.076  1.00 22.33 ? 86  ASP B CG   1 
ATOM   1608 O OD1  . ASP B 1 86  ? 19.101  21.090 -3.972  1.00 20.39 ? 86  ASP B OD1  1 
ATOM   1609 O OD2  . ASP B 1 86  ? 19.350  20.030 -2.071  1.00 23.77 ? 86  ASP B OD2  1 
ATOM   1610 N N    . ASP B 1 87  ? 14.052  19.866 -3.643  1.00 24.15 ? 87  ASP B N    1 
ATOM   1611 C CA   . ASP B 1 87  ? 12.793  19.178 -3.898  1.00 24.11 ? 87  ASP B CA   1 
ATOM   1612 C C    . ASP B 1 87  ? 12.175  19.726 -5.186  1.00 21.44 ? 87  ASP B C    1 
ATOM   1613 O O    . ASP B 1 87  ? 11.708  20.865 -5.222  1.00 27.60 ? 87  ASP B O    1 
ATOM   1614 C CB   . ASP B 1 87  ? 11.856  19.333 -2.700  1.00 20.67 ? 87  ASP B CB   1 
ATOM   1615 C CG   . ASP B 1 87  ? 10.640  18.425 -2.800  1.00 24.83 ? 87  ASP B CG   1 
ATOM   1616 O OD1  . ASP B 1 87  ? 10.134  18.259 -3.927  1.00 21.81 ? 87  ASP B OD1  1 
ATOM   1617 O OD2  . ASP B 1 87  ? 10.218  17.843 -1.772  1.00 27.89 ? 87  ASP B OD2  1 
ATOM   1618 N N    . GLN B 1 88  ? 12.170  18.913 -6.248  1.00 22.64 ? 88  GLN B N    1 
ATOM   1619 C CA   . GLN B 1 88  ? 11.743  19.393 -7.560  1.00 29.23 ? 88  GLN B CA   1 
ATOM   1620 C C    . GLN B 1 88  ? 10.255  19.738 -7.601  1.00 26.67 ? 88  GLN B C    1 
ATOM   1621 O O    . GLN B 1 88  ? 9.822   20.455 -8.510  1.00 25.85 ? 88  GLN B O    1 
ATOM   1622 C CB   . GLN B 1 88  ? 12.062  18.350 -8.635  1.00 24.38 ? 88  GLN B CB   1 
ATOM   1623 C CG   . GLN B 1 88  ? 13.569  18.055 -8.862  1.00 33.04 ? 88  GLN B CG   1 
ATOM   1624 C CD   . GLN B 1 88  ? 14.408  19.310 -9.031  1.00 32.68 ? 88  GLN B CD   1 
ATOM   1625 O OE1  . GLN B 1 88  ? 14.431  19.891 -10.111 1.00 32.65 ? 88  GLN B OE1  1 
ATOM   1626 N NE2  . GLN B 1 88  ? 15.127  19.713 -7.978  1.00 31.27 ? 88  GLN B NE2  1 
ATOM   1627 N N    . ARG B 1 89  ? 9.464   19.261 -6.640  1.00 26.42 ? 89  ARG B N    1 
ATOM   1628 C CA   . ARG B 1 89  ? 8.052   19.624 -6.632  1.00 25.41 ? 89  ARG B CA   1 
ATOM   1629 C C    . ARG B 1 89  ? 7.825   21.076 -6.229  1.00 25.79 ? 89  ARG B C    1 
ATOM   1630 O O    . ARG B 1 89  ? 6.733   21.607 -6.462  1.00 23.42 ? 89  ARG B O    1 
ATOM   1631 C CB   . ARG B 1 89  ? 7.281   18.707 -5.691  1.00 25.69 ? 89  ARG B CB   1 
ATOM   1632 C CG   . ARG B 1 89  ? 7.412   17.237 -6.003  1.00 25.26 ? 89  ARG B CG   1 
ATOM   1633 C CD   . ARG B 1 89  ? 6.844   16.427 -4.857  1.00 27.28 ? 89  ARG B CD   1 
ATOM   1634 N NE   . ARG B 1 89  ? 7.598   16.639 -3.626  1.00 32.09 ? 89  ARG B NE   1 
ATOM   1635 C CZ   . ARG B 1 89  ? 7.286   16.089 -2.462  1.00 32.32 ? 89  ARG B CZ   1 
ATOM   1636 N NH1  . ARG B 1 89  ? 6.259   15.257 -2.342  1.00 33.60 ? 89  ARG B NH1  1 
ATOM   1637 N NH2  . ARG B 1 89  ? 8.035   16.353 -1.400  1.00 25.92 ? 89  ARG B NH2  1 
ATOM   1638 N N    . VAL B 1 90  ? 8.825   21.721 -5.634  1.00 23.24 ? 90  VAL B N    1 
ATOM   1639 C CA   . VAL B 1 90  ? 8.685   23.080 -5.118  1.00 22.48 ? 90  VAL B CA   1 
ATOM   1640 C C    . VAL B 1 90  ? 8.739   24.082 -6.266  1.00 24.92 ? 90  VAL B C    1 
ATOM   1641 O O    . VAL B 1 90  ? 9.706   24.116 -7.034  1.00 25.86 ? 90  VAL B O    1 
ATOM   1642 C CB   . VAL B 1 90  ? 9.762   23.383 -4.067  1.00 21.12 ? 90  VAL B CB   1 
ATOM   1643 C CG1  . VAL B 1 90  ? 9.683   24.845 -3.606  1.00 17.31 ? 90  VAL B CG1  1 
ATOM   1644 C CG2  . VAL B 1 90  ? 9.586   22.462 -2.867  1.00 20.71 ? 90  VAL B CG2  1 
ATOM   1645 N N    . HIS B 1 91  ? 7.687   24.898 -6.377  1.00 21.19 ? 91  HIS B N    1 
ATOM   1646 C CA   . HIS B 1 91  ? 7.635   25.981 -7.355  1.00 25.52 ? 91  HIS B CA   1 
ATOM   1647 C C    . HIS B 1 91  ? 8.542   27.134 -6.963  1.00 25.10 ? 91  HIS B C    1 
ATOM   1648 O O    . HIS B 1 91  ? 9.268   27.682 -7.800  1.00 25.40 ? 91  HIS B O    1 
ATOM   1649 C CB   . HIS B 1 91  ? 6.199   26.501 -7.484  1.00 26.01 ? 91  HIS B CB   1 
ATOM   1650 C CG   . HIS B 1 91  ? 5.228   25.483 -7.976  1.00 33.81 ? 91  HIS B CG   1 
ATOM   1651 N ND1  . HIS B 1 91  ? 3.875   25.573 -7.737  1.00 36.71 ? 91  HIS B ND1  1 
ATOM   1652 C CD2  . HIS B 1 91  ? 5.406   24.372 -8.725  1.00 32.28 ? 91  HIS B CD2  1 
ATOM   1653 C CE1  . HIS B 1 91  ? 3.263   24.550 -8.300  1.00 39.77 ? 91  HIS B CE1  1 
ATOM   1654 N NE2  . HIS B 1 91  ? 4.168   23.807 -8.909  1.00 39.31 ? 91  HIS B NE2  1 
ATOM   1655 N N    . ALA B 1 92  ? 8.436   27.576 -5.715  1.00 21.52 ? 92  ALA B N    1 
ATOM   1656 C CA   . ALA B 1 92  ? 9.204   28.707 -5.222  1.00 17.62 ? 92  ALA B CA   1 
ATOM   1657 C C    . ALA B 1 92  ? 9.304   28.576 -3.712  1.00 17.51 ? 92  ALA B C    1 
ATOM   1658 O O    . ALA B 1 92  ? 8.493   27.892 -3.080  1.00 18.69 ? 92  ALA B O    1 
ATOM   1659 C CB   . ALA B 1 92  ? 8.545   30.040 -5.603  1.00 26.07 ? 92  ALA B CB   1 
ATOM   1660 N N    . VAL B 1 93  ? 10.299  29.245 -3.137  1.00 16.67 ? 93  VAL B N    1 
ATOM   1661 C CA   . VAL B 1 93  ? 10.418  29.321 -1.688  1.00 16.03 ? 93  VAL B CA   1 
ATOM   1662 C C    . VAL B 1 93  ? 10.820  30.737 -1.307  1.00 22.50 ? 93  VAL B C    1 
ATOM   1663 O O    . VAL B 1 93  ? 11.549  31.421 -2.029  1.00 21.05 ? 93  VAL B O    1 
ATOM   1664 C CB   . VAL B 1 93  ? 11.422  28.297 -1.106  1.00 21.51 ? 93  VAL B CB   1 
ATOM   1665 C CG1  . VAL B 1 93  ? 12.805  28.515 -1.667  1.00 19.56 ? 93  VAL B CG1  1 
ATOM   1666 C CG2  . VAL B 1 93  ? 11.462  28.405 0.421   1.00 16.53 ? 93  VAL B CG2  1 
ATOM   1667 N N    . GLU B 1 94  ? 10.328  31.175 -0.157  1.00 19.15 ? 94  GLU B N    1 
ATOM   1668 C CA   . GLU B 1 94  ? 10.661  32.475 0.393   1.00 18.22 ? 94  GLU B CA   1 
ATOM   1669 C C    . GLU B 1 94  ? 11.070  32.246 1.835   1.00 20.79 ? 94  GLU B C    1 
ATOM   1670 O O    . GLU B 1 94  ? 10.260  31.737 2.622   1.00 18.36 ? 94  GLU B O    1 
ATOM   1671 C CB   . GLU B 1 94  ? 9.452   33.412 0.306   1.00 23.71 ? 94  GLU B CB   1 
ATOM   1672 C CG   . GLU B 1 94  ? 9.604   34.699 1.076   1.00 32.13 ? 94  GLU B CG   1 
ATOM   1673 C CD   . GLU B 1 94  ? 8.540   35.723 0.712   1.00 29.16 ? 94  GLU B CD   1 
ATOM   1674 O OE1  . GLU B 1 94  ? 8.513   36.203 -0.438  1.00 25.48 ? 94  GLU B OE1  1 
ATOM   1675 O OE2  . GLU B 1 94  ? 7.745   36.041 1.626   1.00 30.65 ? 94  GLU B OE2  1 
ATOM   1676 N N    . VAL B 1 95  ? 12.319  32.591 2.166   1.00 15.47 ? 95  VAL B N    1 
ATOM   1677 C CA   . VAL B 1 95  ? 12.873  32.413 3.508   1.00 17.69 ? 95  VAL B CA   1 
ATOM   1678 C C    . VAL B 1 95  ? 13.100  33.799 4.101   1.00 19.55 ? 95  VAL B C    1 
ATOM   1679 O O    . VAL B 1 95  ? 13.820  34.620 3.519   1.00 16.38 ? 95  VAL B O    1 
ATOM   1680 C CB   . VAL B 1 95  ? 14.182  31.599 3.488   1.00 21.08 ? 95  VAL B CB   1 
ATOM   1681 C CG1  . VAL B 1 95  ? 14.753  31.446 4.911   1.00 16.07 ? 95  VAL B CG1  1 
ATOM   1682 C CG2  . VAL B 1 95  ? 13.996  30.217 2.804   1.00 16.03 ? 95  VAL B CG2  1 
ATOM   1683 N N    . ALA B 1 96  ? 12.467  34.079 5.238   1.00 16.23 ? 96  ALA B N    1 
ATOM   1684 C CA   . ALA B 1 96  ? 12.739  35.296 5.988   1.00 15.81 ? 96  ALA B CA   1 
ATOM   1685 C C    . ALA B 1 96  ? 13.638  34.945 7.166   1.00 15.91 ? 96  ALA B C    1 
ATOM   1686 O O    . ALA B 1 96  ? 13.295  34.077 7.975   1.00 14.92 ? 96  ALA B O    1 
ATOM   1687 C CB   . ALA B 1 96  ? 11.443  35.959 6.469   1.00 17.60 ? 96  ALA B CB   1 
ATOM   1688 N N    . VAL B 1 97  ? 14.791  35.601 7.250   1.00 13.35 ? 97  VAL B N    1 
ATOM   1689 C CA   . VAL B 1 97  ? 15.675  35.501 8.405   1.00 13.86 ? 97  VAL B CA   1 
ATOM   1690 C C    . VAL B 1 97  ? 15.551  36.809 9.181   1.00 15.44 ? 97  VAL B C    1 
ATOM   1691 O O    . VAL B 1 97  ? 15.943  37.876 8.689   1.00 13.59 ? 97  VAL B O    1 
ATOM   1692 C CB   . VAL B 1 97  ? 17.127  35.206 8.002   1.00 18.94 ? 97  VAL B CB   1 
ATOM   1693 C CG1  . VAL B 1 97  ? 18.017  35.092 9.236   1.00 14.28 ? 97  VAL B CG1  1 
ATOM   1694 C CG2  . VAL B 1 97  ? 17.203  33.884 7.176   1.00 16.01 ? 97  VAL B CG2  1 
ATOM   1695 N N    . HIS B 1 98  ? 14.969  36.726 10.380  1.00 15.18 ? 98  HIS B N    1 
ATOM   1696 C CA   . HIS B 1 98  ? 14.800  37.864 11.268  1.00 16.55 ? 98  HIS B CA   1 
ATOM   1697 C C    . HIS B 1 98  ? 15.940  37.889 12.265  1.00 19.17 ? 98  HIS B C    1 
ATOM   1698 O O    . HIS B 1 98  ? 16.363  36.844 12.771  1.00 15.00 ? 98  HIS B O    1 
ATOM   1699 C CB   . HIS B 1 98  ? 13.487  37.804 12.053  1.00 15.49 ? 98  HIS B CB   1 
ATOM   1700 C CG   . HIS B 1 98  ? 12.266  37.633 11.211  1.00 18.58 ? 98  HIS B CG   1 
ATOM   1701 N ND1  . HIS B 1 98  ? 11.393  38.667 10.950  1.00 18.39 ? 98  HIS B ND1  1 
ATOM   1702 C CD2  . HIS B 1 98  ? 11.738  36.535 10.620  1.00 18.53 ? 98  HIS B CD2  1 
ATOM   1703 C CE1  . HIS B 1 98  ? 10.397  38.219 10.204  1.00 20.68 ? 98  HIS B CE1  1 
ATOM   1704 N NE2  . HIS B 1 98  ? 10.587  36.929 9.985   1.00 17.78 ? 98  HIS B NE2  1 
ATOM   1705 N N    . LYS B 1 99  ? 16.403  39.089 12.578  1.00 17.57 ? 99  LYS B N    1 
ATOM   1706 C CA   . LYS B 1 99  ? 17.466  39.311 13.547  1.00 14.06 ? 99  LYS B CA   1 
ATOM   1707 C C    . LYS B 1 99  ? 16.938  40.328 14.540  1.00 18.08 ? 99  LYS B C    1 
ATOM   1708 O O    . LYS B 1 99  ? 17.393  41.473 14.575  1.00 18.82 ? 99  LYS B O    1 
ATOM   1709 C CB   . LYS B 1 99  ? 18.747  39.791 12.864  1.00 13.12 ? 99  LYS B CB   1 
ATOM   1710 C CG   . LYS B 1 99  ? 20.035  39.540 13.645  1.00 19.46 ? 99  LYS B CG   1 
ATOM   1711 C CD   . LYS B 1 99  ? 21.247  40.013 12.807  1.00 18.53 ? 99  LYS B CD   1 
ATOM   1712 C CE   . LYS B 1 99  ? 22.573  39.824 13.527  1.00 20.04 ? 99  LYS B CE   1 
ATOM   1713 N NZ   . LYS B 1 99  ? 23.602  40.692 12.879  1.00 25.25 ? 99  LYS B NZ   1 
ATOM   1714 N N    . PRO B 1 100 ? 15.944  39.943 15.344  1.00 16.58 ? 100 PRO B N    1 
ATOM   1715 C CA   . PRO B 1 100 ? 15.235  40.930 16.169  1.00 18.82 ? 100 PRO B CA   1 
ATOM   1716 C C    . PRO B 1 100 ? 16.122  41.606 17.176  1.00 22.73 ? 100 PRO B C    1 
ATOM   1717 O O    . PRO B 1 100 ? 15.777  42.695 17.651  1.00 25.85 ? 100 PRO B O    1 
ATOM   1718 C CB   . PRO B 1 100 ? 14.157  40.090 16.858  1.00 18.95 ? 100 PRO B CB   1 
ATOM   1719 C CG   . PRO B 1 100 ? 14.826  38.709 16.974  1.00 16.79 ? 100 PRO B CG   1 
ATOM   1720 C CD   . PRO B 1 100 ? 15.513  38.565 15.649  1.00 18.54 ? 100 PRO B CD   1 
ATOM   1721 N N    . GLN B 1 101 ? 17.262  41.009 17.501  1.00 16.07 ? 101 GLN B N    1 
ATOM   1722 C CA   . GLN B 1 101 ? 18.152  41.539 18.524  1.00 18.95 ? 101 GLN B CA   1 
ATOM   1723 C C    . GLN B 1 101 ? 19.347  42.255 17.919  1.00 24.74 ? 101 GLN B C    1 
ATOM   1724 O O    . GLN B 1 101 ? 20.302  42.559 18.632  1.00 19.36 ? 101 GLN B O    1 
ATOM   1725 C CB   . GLN B 1 101 ? 18.619  40.404 19.435  1.00 25.47 ? 101 GLN B CB   1 
ATOM   1726 C CG   . GLN B 1 101 ? 17.489  39.832 20.259  1.00 26.71 ? 101 GLN B CG   1 
ATOM   1727 C CD   . GLN B 1 101 ? 17.894  38.669 21.146  1.00 28.85 ? 101 GLN B CD   1 
ATOM   1728 O OE1  . GLN B 1 101 ? 18.953  38.037 20.970  1.00 16.31 ? 101 GLN B OE1  1 
ATOM   1729 N NE2  . GLN B 1 101 ? 17.051  38.397 22.139  1.00 26.36 ? 101 GLN B NE2  1 
ATOM   1730 N N    . ALA B 1 102 ? 19.315  42.507 16.619  1.00 20.97 ? 102 ALA B N    1 
ATOM   1731 C CA   . ALA B 1 102 ? 20.459  43.081 15.933  1.00 21.00 ? 102 ALA B CA   1 
ATOM   1732 C C    . ALA B 1 102 ? 20.948  44.315 16.688  1.00 25.25 ? 102 ALA B C    1 
ATOM   1733 O O    . ALA B 1 102 ? 20.129  45.072 17.229  1.00 23.43 ? 102 ALA B O    1 
ATOM   1734 C CB   . ALA B 1 102 ? 20.079  43.445 14.498  1.00 15.71 ? 102 ALA B CB   1 
ATOM   1735 N N    . PRO B 1 103 ? 22.283  44.516 16.802  1.00 21.36 ? 103 PRO B N    1 
ATOM   1736 C CA   . PRO B 1 103 ? 22.789  45.738 17.434  1.00 21.68 ? 103 PRO B CA   1 
ATOM   1737 C C    . PRO B 1 103 ? 22.615  46.913 16.491  1.00 25.53 ? 103 PRO B C    1 
ATOM   1738 O O    . PRO B 1 103 ? 23.304  47.030 15.470  1.00 28.23 ? 103 PRO B O    1 
ATOM   1739 C CB   . PRO B 1 103 ? 24.273  45.425 17.708  1.00 24.72 ? 103 PRO B CB   1 
ATOM   1740 C CG   . PRO B 1 103 ? 24.474  43.977 17.328  1.00 30.13 ? 103 PRO B CG   1 
ATOM   1741 C CD   . PRO B 1 103 ? 23.375  43.626 16.370  1.00 25.79 ? 103 PRO B CD   1 
ATOM   1742 N N    . ILE B 1 104 ? 21.617  47.734 16.788  1.00 22.77 ? 104 ILE B N    1 
ATOM   1743 C CA   . ILE B 1 104 ? 21.331  48.962 16.057  1.00 23.80 ? 104 ILE B CA   1 
ATOM   1744 C C    . ILE B 1 104 ? 21.103  49.978 17.163  1.00 23.93 ? 104 ILE B C    1 
ATOM   1745 O O    . ILE B 1 104 ? 20.449  49.644 18.162  1.00 25.44 ? 104 ILE B O    1 
ATOM   1746 C CB   . ILE B 1 104 ? 20.090  48.829 15.163  1.00 22.29 ? 104 ILE B CB   1 
ATOM   1747 C CG1  . ILE B 1 104 ? 20.366  47.899 13.981  1.00 24.12 ? 104 ILE B CG1  1 
ATOM   1748 C CG2  . ILE B 1 104 ? 19.731  50.195 14.576  1.00 25.03 ? 104 ILE B CG2  1 
ATOM   1749 C CD1  . ILE B 1 104 ? 19.130  47.663 13.115  1.00 25.14 ? 104 ILE B CD1  1 
ATOM   1750 N N    . PRO B 1 105 ? 21.619  51.200 17.060  1.00 20.42 ? 105 PRO B N    1 
ATOM   1751 C CA   . PRO B 1 105 ? 21.464  52.138 18.181  1.00 19.35 ? 105 PRO B CA   1 
ATOM   1752 C C    . PRO B 1 105 ? 20.045  52.664 18.325  1.00 23.88 ? 105 PRO B C    1 
ATOM   1753 O O    . PRO B 1 105 ? 19.671  53.085 19.424  1.00 25.55 ? 105 PRO B O    1 
ATOM   1754 C CB   . PRO B 1 105 ? 22.460  53.252 17.845  1.00 27.84 ? 105 PRO B CB   1 
ATOM   1755 C CG   . PRO B 1 105 ? 22.631  53.185 16.384  1.00 27.27 ? 105 PRO B CG   1 
ATOM   1756 C CD   . PRO B 1 105 ? 22.459  51.747 15.983  1.00 21.83 ? 105 PRO B CD   1 
ATOM   1757 N N    . GLN B 1 106 ? 19.236  52.606 17.272  1.00 21.80 ? 106 GLN B N    1 
ATOM   1758 C CA   . GLN B 1 106 ? 17.847  53.035 17.305  1.00 26.34 ? 106 GLN B CA   1 
ATOM   1759 C C    . GLN B 1 106 ? 16.945  51.959 17.923  1.00 23.30 ? 106 GLN B C    1 
ATOM   1760 O O    . GLN B 1 106 ? 17.299  50.780 18.011  1.00 26.90 ? 106 GLN B O    1 
ATOM   1761 C CB   . GLN B 1 106 ? 17.360  53.368 15.890  1.00 18.37 ? 106 GLN B CB   1 
ATOM   1762 C CG   . GLN B 1 106 ? 17.837  54.729 15.381  1.00 20.99 ? 106 GLN B CG   1 
ATOM   1763 C CD   . GLN B 1 106 ? 19.295  54.683 15.023  1.00 29.18 ? 106 GLN B CD   1 
ATOM   1764 O OE1  . GLN B 1 106 ? 19.814  53.621 14.693  1.00 25.96 ? 106 GLN B OE1  1 
ATOM   1765 N NE2  . GLN B 1 106 ? 19.980  55.822 15.115  1.00 30.11 ? 106 GLN B NE2  1 
ATOM   1766 N N    . THR B 1 107 ? 15.762  52.387 18.351  1.00 19.07 ? 107 THR B N    1 
ATOM   1767 C CA   . THR B 1 107 ? 14.741  51.492 18.884  1.00 19.01 ? 107 THR B CA   1 
ATOM   1768 C C    . THR B 1 107 ? 13.880  50.982 17.729  1.00 18.45 ? 107 THR B C    1 
ATOM   1769 O O    . THR B 1 107 ? 13.342  51.778 16.955  1.00 17.04 ? 107 THR B O    1 
ATOM   1770 C CB   . THR B 1 107 ? 13.902  52.226 19.937  1.00 19.58 ? 107 THR B CB   1 
ATOM   1771 O OG1  . THR B 1 107 ? 14.765  52.595 21.020  1.00 21.62 ? 107 THR B OG1  1 
ATOM   1772 C CG2  . THR B 1 107 ? 12.770  51.348 20.478  1.00 22.76 ? 107 THR B CG2  1 
ATOM   1773 N N    . PHE B 1 108 ? 13.778  49.660 17.588  1.00 17.12 ? 108 PHE B N    1 
ATOM   1774 C CA   . PHE B 1 108 ? 13.023  49.086 16.479  1.00 18.99 ? 108 PHE B CA   1 
ATOM   1775 C C    . PHE B 1 108 ? 12.491  47.734 16.917  1.00 19.39 ? 108 PHE B C    1 
ATOM   1776 O O    . PHE B 1 108 ? 12.955  47.157 17.907  1.00 21.86 ? 108 PHE B O    1 
ATOM   1777 C CB   . PHE B 1 108 ? 13.905  48.951 15.226  1.00 16.64 ? 108 PHE B CB   1 
ATOM   1778 C CG   . PHE B 1 108 ? 14.999  47.938 15.392  1.00 15.01 ? 108 PHE B CG   1 
ATOM   1779 C CD1  . PHE B 1 108 ? 16.121  48.225 16.161  1.00 19.89 ? 108 PHE B CD1  1 
ATOM   1780 C CD2  . PHE B 1 108 ? 14.880  46.676 14.817  1.00 21.94 ? 108 PHE B CD2  1 
ATOM   1781 C CE1  . PHE B 1 108 ? 17.119  47.274 16.353  1.00 22.50 ? 108 PHE B CE1  1 
ATOM   1782 C CE2  . PHE B 1 108 ? 15.873  45.716 14.996  1.00 17.48 ? 108 PHE B CE2  1 
ATOM   1783 C CZ   . PHE B 1 108 ? 16.993  46.014 15.758  1.00 23.73 ? 108 PHE B CZ   1 
ATOM   1784 N N    . ASP B 1 109 ? 11.501  47.234 16.172  1.00 16.72 ? 109 ASP B N    1 
ATOM   1785 C CA   . ASP B 1 109 ? 10.893  45.945 16.486  1.00 16.10 ? 109 ASP B CA   1 
ATOM   1786 C C    . ASP B 1 109 ? 11.623  44.788 15.828  1.00 16.43 ? 109 ASP B C    1 
ATOM   1787 O O    . ASP B 1 109 ? 11.844  43.751 16.453  1.00 17.62 ? 109 ASP B O    1 
ATOM   1788 C CB   . ASP B 1 109 ? 9.424   45.912 16.054  1.00 13.21 ? 109 ASP B CB   1 
ATOM   1789 C CG   . ASP B 1 109 ? 8.527   46.790 16.909  1.00 25.61 ? 109 ASP B CG   1 
ATOM   1790 O OD1  . ASP B 1 109 ? 8.878   47.048 18.072  1.00 33.65 ? 109 ASP B OD1  1 
ATOM   1791 O OD2  . ASP B 1 109 ? 7.469   47.238 16.402  1.00 25.35 ? 109 ASP B OD2  1 
ATOM   1792 N N    . ASP B 1 110 ? 11.990  44.929 14.568  1.00 14.19 ? 110 ASP B N    1 
ATOM   1793 C CA   . ASP B 1 110 ? 12.507  43.776 13.856  1.00 15.08 ? 110 ASP B CA   1 
ATOM   1794 C C    . ASP B 1 110 ? 13.307  44.241 12.656  1.00 15.14 ? 110 ASP B C    1 
ATOM   1795 O O    . ASP B 1 110 ? 13.058  45.315 12.104  1.00 12.89 ? 110 ASP B O    1 
ATOM   1796 C CB   . ASP B 1 110 ? 11.376  42.846 13.402  1.00 17.74 ? 110 ASP B CB   1 
ATOM   1797 C CG   . ASP B 1 110 ? 11.909  41.521 12.903  1.00 18.67 ? 110 ASP B CG   1 
ATOM   1798 O OD1  . ASP B 1 110 ? 12.534  40.812 13.718  1.00 18.70 ? 110 ASP B OD1  1 
ATOM   1799 O OD2  . ASP B 1 110 ? 11.747  41.227 11.702  1.00 17.28 ? 110 ASP B OD2  1 
ATOM   1800 N N    . VAL B 1 111 ? 14.287  43.428 12.275  1.00 13.02 ? 111 VAL B N    1 
ATOM   1801 C CA   . VAL B 1 111 ? 14.980  43.618 11.014  1.00 14.85 ? 111 VAL B CA   1 
ATOM   1802 C C    . VAL B 1 111 ? 15.138  42.240 10.415  1.00 15.06 ? 111 VAL B C    1 
ATOM   1803 O O    . VAL B 1 111 ? 15.367  41.270 11.140  1.00 16.07 ? 111 VAL B O    1 
ATOM   1804 C CB   . VAL B 1 111 ? 16.340  44.348 11.159  1.00 20.22 ? 111 VAL B CB   1 
ATOM   1805 C CG1  . VAL B 1 111 ? 17.450  43.433 11.707  1.00 15.00 ? 111 VAL B CG1  1 
ATOM   1806 C CG2  . VAL B 1 111 ? 16.750  44.947 9.817   1.00 18.62 ? 111 VAL B CG2  1 
ATOM   1807 N N    . ALA B 1 112 ? 14.977  42.144 9.101   1.00 14.99 ? 112 ALA B N    1 
ATOM   1808 C CA   . ALA B 1 112 ? 14.967  40.832 8.469   1.00 18.00 ? 112 ALA B CA   1 
ATOM   1809 C C    . ALA B 1 112 ? 15.307  40.989 6.994   1.00 19.73 ? 112 ALA B C    1 
ATOM   1810 O O    . ALA B 1 112 ? 15.144  42.065 6.412   1.00 15.85 ? 112 ALA B O    1 
ATOM   1811 C CB   . ALA B 1 112 ? 13.611  40.147 8.639   1.00 18.00 ? 112 ALA B CB   1 
ATOM   1812 N N    . VAL B 1 113 ? 15.793  39.901 6.401   1.00 15.72 ? 113 VAL B N    1 
ATOM   1813 C CA   . VAL B 1 113 ? 15.909  39.820 4.953   1.00 15.73 ? 113 VAL B CA   1 
ATOM   1814 C C    . VAL B 1 113 ? 15.075  38.641 4.502   1.00 14.53 ? 113 VAL B C    1 
ATOM   1815 O O    . VAL B 1 113 ? 14.896  37.665 5.239   1.00 18.73 ? 113 VAL B O    1 
ATOM   1816 C CB   . VAL B 1 113 ? 17.368  39.683 4.455   1.00 19.39 ? 113 VAL B CB   1 
ATOM   1817 C CG1  . VAL B 1 113 ? 18.235  40.813 5.017   1.00 15.23 ? 113 VAL B CG1  1 
ATOM   1818 C CG2  . VAL B 1 113 ? 17.941  38.282 4.780   1.00 16.51 ? 113 VAL B CG2  1 
ATOM   1819 N N    . VAL B 1 114 ? 14.530  38.757 3.297   1.00 15.94 ? 114 VAL B N    1 
ATOM   1820 C CA   . VAL B 1 114 ? 13.715  37.715 2.685   1.00 18.21 ? 114 VAL B CA   1 
ATOM   1821 C C    . VAL B 1 114 ? 14.382  37.323 1.378   1.00 19.74 ? 114 VAL B C    1 
ATOM   1822 O O    . VAL B 1 114 ? 14.605  38.179 0.509   1.00 18.32 ? 114 VAL B O    1 
ATOM   1823 C CB   . VAL B 1 114 ? 12.269  38.177 2.447   1.00 19.23 ? 114 VAL B CB   1 
ATOM   1824 C CG1  . VAL B 1 114 ? 11.417  37.024 1.972   1.00 16.71 ? 114 VAL B CG1  1 
ATOM   1825 C CG2  . VAL B 1 114 ? 11.674  38.756 3.731   1.00 21.58 ? 114 VAL B CG2  1 
ATOM   1826 N N    . ILE B 1 115 ? 14.707  36.041 1.250   1.00 17.36 ? 115 ILE B N    1 
ATOM   1827 C CA   . ILE B 1 115 ? 15.331  35.482 0.058   1.00 18.30 ? 115 ILE B CA   1 
ATOM   1828 C C    . ILE B 1 115 ? 14.274  34.675 -0.676  1.00 22.37 ? 115 ILE B C    1 
ATOM   1829 O O    . ILE B 1 115 ? 13.571  33.857 -0.066  1.00 17.49 ? 115 ILE B O    1 
ATOM   1830 C CB   . ILE B 1 115 ? 16.550  34.607 0.415   1.00 23.79 ? 115 ILE B CB   1 
ATOM   1831 C CG1  . ILE B 1 115 ? 17.554  35.400 1.251   1.00 23.93 ? 115 ILE B CG1  1 
ATOM   1832 C CG2  . ILE B 1 115 ? 17.199  34.048 -0.833  1.00 27.20 ? 115 ILE B CG2  1 
ATOM   1833 C CD1  . ILE B 1 115 ? 18.223  36.519 0.451   1.00 20.45 ? 115 ILE B CD1  1 
ATOM   1834 N N    . ARG B 1 116 ? 14.138  34.915 -1.972  1.00 25.23 ? 116 ARG B N    1 
ATOM   1835 C CA   . ARG B 1 116 ? 13.189  34.164 -2.766  1.00 26.52 ? 116 ARG B CA   1 
ATOM   1836 C C    . ARG B 1 116 ? 13.933  33.396 -3.856  1.00 31.84 ? 116 ARG B C    1 
ATOM   1837 O O    . ARG B 1 116 ? 14.983  33.829 -4.353  1.00 32.56 ? 116 ARG B O    1 
ATOM   1838 C CB   . ARG B 1 116 ? 12.097  35.099 -3.339  1.00 29.97 ? 116 ARG B CB   1 
ATOM   1839 C CG   . ARG B 1 116 ? 11.174  34.435 -4.329  1.00 40.89 ? 116 ARG B CG   1 
ATOM   1840 C CD   . ARG B 1 116 ? 10.764  35.348 -5.464  1.00 45.50 ? 116 ARG B CD   1 
ATOM   1841 N NE   . ARG B 1 116 ? 9.842   34.686 -6.383  1.00 43.80 ? 116 ARG B NE   1 
ATOM   1842 C CZ   . ARG B 1 116 ? 8.645   34.203 -6.060  1.00 42.61 ? 116 ARG B CZ   1 
ATOM   1843 N NH1  . ARG B 1 116 ? 8.167   34.282 -4.824  1.00 36.66 ? 116 ARG B NH1  1 
ATOM   1844 N NH2  . ARG B 1 116 ? 7.908   33.621 -7.004  1.00 44.55 ? 116 ARG B NH2  1 
ATOM   1845 N N    . ARG B 1 117 ? 13.426  32.205 -4.158  1.00 21.88 ? 117 ARG B N    1 
ATOM   1846 C CA   . ARG B 1 117 ? 13.926  31.378 -5.248  1.00 28.46 ? 117 ARG B CA   1 
ATOM   1847 C C    . ARG B 1 117 ? 12.723  30.707 -5.890  1.00 25.18 ? 117 ARG B C    1 
ATOM   1848 O O    . ARG B 1 117 ? 11.722  30.443 -5.220  1.00 22.72 ? 117 ARG B O    1 
ATOM   1849 C CB   . ARG B 1 117 ? 14.931  30.318 -4.761  1.00 23.11 ? 117 ARG B CB   1 
ATOM   1850 C CG   . ARG B 1 117 ? 16.186  30.894 -4.094  1.00 34.48 ? 117 ARG B CG   1 
ATOM   1851 C CD   . ARG B 1 117 ? 17.423  30.841 -4.992  1.00 37.22 ? 117 ARG B CD   1 
ATOM   1852 N NE   . ARG B 1 117 ? 18.617  31.364 -4.328  1.00 41.66 ? 117 ARG B NE   1 
ATOM   1853 C CZ   . ARG B 1 117 ? 18.799  32.645 -4.029  1.00 45.83 ? 117 ARG B CZ   1 
ATOM   1854 N NH1  . ARG B 1 117 ? 17.863  33.548 -4.274  1.00 35.04 ? 117 ARG B NH1  1 
ATOM   1855 N NH2  . ARG B 1 117 ? 19.950  33.031 -3.470  1.00 38.18 ? 117 ARG B NH2  1 
ATOM   1856 N N    . SER B 1 118 ? 12.815  30.440 -7.190  1.00 26.64 ? 118 SER B N    1 
ATOM   1857 C CA   . SER B 1 118 ? 11.695  29.865 -7.924  1.00 31.63 ? 118 SER B CA   1 
ATOM   1858 C C    . SER B 1 118 ? 12.236  29.167 -9.157  1.00 38.18 ? 118 SER B C    1 
ATOM   1859 O O    . SER B 1 118 ? 13.352  29.438 -9.603  1.00 29.19 ? 118 SER B O    1 
ATOM   1860 C CB   . SER B 1 118 ? 10.672  30.925 -8.339  1.00 34.24 ? 118 SER B CB   1 
ATOM   1861 O OG   . SER B 1 118 ? 11.303  31.979 -9.031  1.00 36.68 ? 118 SER B OG   1 
ATOM   1862 N N    . ARG B 1 119 ? 11.428  28.270 -9.710  1.00 32.30 ? 119 ARG B N    1 
ATOM   1863 C CA   . ARG B 1 119 ? 11.821  27.594 -10.947 1.00 37.72 ? 119 ARG B CA   1 
ATOM   1864 C C    . ARG B 1 119 ? 11.855  28.578 -12.108 1.00 52.04 ? 119 ARG B C    1 
ATOM   1865 O O    . ARG B 1 119 ? 10.859  29.249 -12.389 1.00 57.05 ? 119 ARG B O    1 
ATOM   1866 C CB   . ARG B 1 119 ? 10.863  26.461 -11.268 1.00 46.28 ? 119 ARG B CB   1 
ATOM   1867 C CG   . ARG B 1 119 ? 10.840  25.372 -10.225 1.00 36.78 ? 119 ARG B CG   1 
ATOM   1868 C CD   . ARG B 1 119 ? 12.197  24.792 -9.904  1.00 40.22 ? 119 ARG B CD   1 
ATOM   1869 N NE   . ARG B 1 119 ? 12.014  23.825 -8.831  1.00 45.74 ? 119 ARG B NE   1 
ATOM   1870 C CZ   . ARG B 1 119 ? 12.972  23.250 -8.120  1.00 36.63 ? 119 ARG B CZ   1 
ATOM   1871 N NH1  . ARG B 1 119 ? 14.255  23.375 -8.439  1.00 29.15 ? 119 ARG B NH1  1 
ATOM   1872 N NH2  . ARG B 1 119 ? 12.634  22.534 -7.056  1.00 33.34 ? 119 ARG B NH2  1 
HETATM 1873 O O1   . B55 C 2 .   ? 23.321  42.108 35.501  1.00 21.44 ? 201 B55 A O1   1 
HETATM 1874 C C5   . B55 C 2 .   ? 23.205  40.793 35.936  1.00 20.81 ? 201 B55 A C5   1 
HETATM 1875 C C2   . B55 C 2 .   ? 23.909  39.747 35.243  1.00 22.67 ? 201 B55 A C2   1 
HETATM 1876 N N1   . B55 C 2 .   ? 24.714  39.767 34.201  1.00 21.39 ? 201 B55 A N1   1 
HETATM 1877 N N4   . B55 C 2 .   ? 22.429  40.486 37.010  1.00 19.78 ? 201 B55 A N4   1 
HETATM 1878 C C4   . B55 C 2 .   ? 22.300  39.134 37.432  1.00 16.35 ? 201 B55 A C4   1 
HETATM 1879 N N3   . B55 C 2 .   ? 21.479  38.807 38.562  1.00 18.28 ? 201 B55 A N3   1 
HETATM 1880 N N2   . B55 C 2 .   ? 22.980  38.130 36.771  1.00 19.57 ? 201 B55 A N2   1 
HETATM 1881 C C3   . B55 C 2 .   ? 23.769  38.450 35.675  1.00 20.81 ? 201 B55 A C3   1 
HETATM 1882 N N5   . B55 C 2 .   ? 24.484  37.697 34.919  1.00 18.95 ? 201 B55 A N5   1 
HETATM 1883 C C1   . B55 C 2 .   ? 25.067  38.492 34.028  1.00 21.92 ? 201 B55 A C1   1 
HETATM 1884 S S1   . B55 C 2 .   ? 26.188  37.904 32.752  1.00 23.54 ? 201 B55 A S1   1 
HETATM 1885 H HN4  . B55 C 2 .   ? 21.932  41.213 37.495  1.00 23.74 ? 201 B55 A HN4  1 
HETATM 1886 H HN3  . B55 C 2 .   ? 21.789  39.034 39.491  1.00 21.93 ? 201 B55 A HN3  1 
HETATM 1887 H HN3A . B55 C 2 .   ? 20.611  38.319 38.428  1.00 21.93 ? 201 B55 A HN3A 1 
HETATM 1888 H HS1  . B55 C 2 .   ? 27.359  37.596 33.299  1.00 28.25 ? 201 B55 A HS1  1 
HETATM 1889 O O1   . B55 D 2 .   ? -0.025  17.434 7.988   1.00 19.66 ? 201 B55 B O1   1 
HETATM 1890 C C5   . B55 D 2 .   ? 1.283   17.615 7.518   1.00 19.47 ? 201 B55 B C5   1 
HETATM 1891 C C2   . B55 D 2 .   ? 2.393   16.982 8.192   1.00 21.47 ? 201 B55 B C2   1 
HETATM 1892 N N1   . B55 D 2 .   ? 2.444   16.220 9.281   1.00 19.87 ? 201 B55 B N1   1 
HETATM 1893 N N4   . B55 D 2 .   ? 1.512   18.388 6.420   1.00 20.49 ? 201 B55 B N4   1 
HETATM 1894 C C4   . B55 D 2 .   ? 2.858   18.565 5.944   1.00 18.10 ? 201 B55 B C4   1 
HETATM 1895 N N3   . B55 D 2 .   ? 3.089   19.371 4.771   1.00 20.40 ? 201 B55 B N3   1 
HETATM 1896 N N2   . B55 D 2 .   ? 3.938   17.968 6.615   1.00 17.64 ? 201 B55 B N2   1 
HETATM 1897 C C3   . B55 D 2 .   ? 3.678   17.180 7.736   1.00 19.20 ? 201 B55 B C3   1 
HETATM 1898 N N5   . B55 D 2 .   ? 4.476   16.522 8.514   1.00 22.49 ? 201 B55 B N5   1 
HETATM 1899 C C1   . B55 D 2 .   ? 3.735   15.927 9.447   1.00 22.03 ? 201 B55 B C1   1 
HETATM 1900 S S1   . B55 D 2 .   ? 4.380   14.878 10.771  1.00 22.71 ? 201 B55 B S1   1 
HETATM 1901 H HN4  . B55 D 2 .   ? 0.743   18.818 5.935   1.00 24.59 ? 201 B55 B HN4  1 
HETATM 1902 H HN3  . B55 D 2 .   ? 3.101   18.943 3.862   1.00 24.48 ? 201 B55 B HN3  1 
HETATM 1903 H HN3A . B55 D 2 .   ? 3.266   20.356 4.865   1.00 24.48 ? 201 B55 B HN3A 1 
HETATM 1904 H HS1  . B55 D 2 .   ? 4.418   13.616 10.357  1.00 27.25 ? 201 B55 B HS1  1 
HETATM 1905 O O    . HOH E 3 .   ? 10.460  42.083 46.037  1.00 34.70 ? 301 HOH A O    1 
HETATM 1906 O O    . HOH E 3 .   ? -5.391  33.951 29.105  1.00 23.37 ? 302 HOH A O    1 
HETATM 1907 O O    . HOH E 3 .   ? 0.218   14.732 31.531  1.00 23.83 ? 303 HOH A O    1 
HETATM 1908 O O    . HOH E 3 .   ? 7.953   21.339 46.050  1.00 38.57 ? 304 HOH A O    1 
HETATM 1909 O O    . HOH E 3 .   ? 21.281  27.886 43.014  1.00 24.18 ? 305 HOH A O    1 
HETATM 1910 O O    . HOH E 3 .   ? -3.534  12.599 27.219  1.00 28.55 ? 306 HOH A O    1 
HETATM 1911 O O    . HOH E 3 .   ? 33.617  45.997 42.959  1.00 27.73 ? 307 HOH A O    1 
HETATM 1912 O O    . HOH E 3 .   ? 24.318  42.934 33.301  1.00 21.58 ? 308 HOH A O    1 
HETATM 1913 O O    . HOH E 3 .   ? -3.216  26.072 24.934  1.00 24.03 ? 309 HOH A O    1 
HETATM 1914 O O    . HOH E 3 .   ? -13.504 24.725 22.413  1.00 25.65 ? 310 HOH A O    1 
HETATM 1915 O O    . HOH E 3 .   ? 19.325  20.231 46.622  1.00 40.61 ? 311 HOH A O    1 
HETATM 1916 O O    . HOH E 3 .   ? -3.363  22.473 24.613  1.00 32.15 ? 312 HOH A O    1 
HETATM 1917 O O    . HOH E 3 .   ? 2.888   22.109 26.642  1.00 21.49 ? 313 HOH A O    1 
HETATM 1918 O O    . HOH E 3 .   ? 33.120  38.378 39.950  1.00 36.41 ? 314 HOH A O    1 
HETATM 1919 O O    . HOH E 3 .   ? 3.393   7.470  31.421  1.00 40.07 ? 315 HOH A O    1 
HETATM 1920 O O    . HOH E 3 .   ? 12.731  16.995 36.340  1.00 21.48 ? 316 HOH A O    1 
HETATM 1921 O O    . HOH E 3 .   ? 1.374   25.759 20.918  1.00 31.81 ? 317 HOH A O    1 
HETATM 1922 O O    . HOH E 3 .   ? 22.010  28.710 38.928  1.00 22.14 ? 318 HOH A O    1 
HETATM 1923 O O    . HOH E 3 .   ? -10.240 18.269 30.256  1.00 23.02 ? 319 HOH A O    1 
HETATM 1924 O O    . HOH E 3 .   ? 34.604  39.313 43.089  1.00 43.27 ? 320 HOH A O    1 
HETATM 1925 O O    . HOH E 3 .   ? 21.430  20.640 35.321  1.00 33.01 ? 321 HOH A O    1 
HETATM 1926 O O    . HOH E 3 .   ? 28.544  34.199 44.446  1.00 34.91 ? 322 HOH A O    1 
HETATM 1927 O O    . HOH E 3 .   ? -5.561  14.396 28.233  1.00 37.24 ? 323 HOH A O    1 
HETATM 1928 O O    . HOH E 3 .   ? 19.759  37.847 50.440  1.00 26.64 ? 324 HOH A O    1 
HETATM 1929 O O    . HOH E 3 .   ? 4.415   12.982 22.229  1.00 19.52 ? 325 HOH A O    1 
HETATM 1930 O O    . HOH E 3 .   ? 11.911  18.338 46.367  1.00 35.83 ? 326 HOH A O    1 
HETATM 1931 O O    . HOH E 3 .   ? 14.087  16.148 33.925  1.00 25.36 ? 327 HOH A O    1 
HETATM 1932 O O    . HOH E 3 .   ? 15.060  45.634 49.024  1.00 38.44 ? 328 HOH A O    1 
HETATM 1933 O O    . HOH E 3 .   ? 6.463   23.023 47.431  1.00 37.06 ? 329 HOH A O    1 
HETATM 1934 O O    . HOH E 3 .   ? 26.961  52.450 47.599  1.00 38.27 ? 330 HOH A O    1 
HETATM 1935 O O    . HOH E 3 .   ? 31.711  48.442 38.535  1.00 22.76 ? 331 HOH A O    1 
HETATM 1936 O O    . HOH E 3 .   ? 22.750  31.730 39.567  1.00 27.20 ? 332 HOH A O    1 
HETATM 1937 O O    . HOH E 3 .   ? 17.777  20.807 41.617  1.00 23.31 ? 333 HOH A O    1 
HETATM 1938 O O    . HOH E 3 .   ? -7.827  34.680 26.123  1.00 32.85 ? 334 HOH A O    1 
HETATM 1939 O O    . HOH E 3 .   ? 11.998  16.376 29.099  1.00 16.58 ? 335 HOH A O    1 
HETATM 1940 O O    . HOH E 3 .   ? 14.093  26.120 22.983  1.00 23.86 ? 336 HOH A O    1 
HETATM 1941 O O    . HOH E 3 .   ? 10.281  11.352 38.427  1.00 26.04 ? 337 HOH A O    1 
HETATM 1942 O O    . HOH E 3 .   ? 5.397   15.897 26.823  1.00 17.44 ? 338 HOH A O    1 
HETATM 1943 O O    . HOH E 3 .   ? 15.697  27.450 25.393  1.00 24.58 ? 339 HOH A O    1 
HETATM 1944 O O    . HOH E 3 .   ? 29.056  45.459 48.226  1.00 36.93 ? 340 HOH A O    1 
HETATM 1945 O O    . HOH E 3 .   ? -1.644  29.245 33.458  1.00 20.23 ? 341 HOH A O    1 
HETATM 1946 O O    . HOH E 3 .   ? 26.910  35.155 41.029  1.00 30.31 ? 342 HOH A O    1 
HETATM 1947 O O    . HOH E 3 .   ? 15.096  19.947 24.962  1.00 30.81 ? 343 HOH A O    1 
HETATM 1948 O O    . HOH E 3 .   ? 28.691  33.024 37.390  1.00 31.53 ? 344 HOH A O    1 
HETATM 1949 O O    . HOH E 3 .   ? 5.841   38.597 36.890  1.00 39.78 ? 345 HOH A O    1 
HETATM 1950 O O    . HOH E 3 .   ? 30.867  42.636 48.361  1.00 40.40 ? 346 HOH A O    1 
HETATM 1951 O O    . HOH E 3 .   ? 22.726  42.854 49.975  1.00 28.81 ? 347 HOH A O    1 
HETATM 1952 O O    . HOH E 3 .   ? 19.244  17.824 30.530  1.00 21.73 ? 348 HOH A O    1 
HETATM 1953 O O    . HOH E 3 .   ? 9.551   40.613 34.667  1.00 28.94 ? 349 HOH A O    1 
HETATM 1954 O O    . HOH E 3 .   ? 11.912  9.361  33.075  1.00 20.49 ? 350 HOH A O    1 
HETATM 1955 O O    . HOH E 3 .   ? 23.400  41.622 46.783  1.00 25.03 ? 351 HOH A O    1 
HETATM 1956 O O    . HOH E 3 .   ? 5.923   33.174 30.701  1.00 22.48 ? 352 HOH A O    1 
HETATM 1957 O O    . HOH E 3 .   ? 3.070   29.434 28.932  1.00 23.08 ? 353 HOH A O    1 
HETATM 1958 O O    . HOH E 3 .   ? 30.415  42.407 37.690  1.00 28.03 ? 354 HOH A O    1 
HETATM 1959 O O    . HOH E 3 .   ? 7.347   30.817 24.477  1.00 28.31 ? 355 HOH A O    1 
HETATM 1960 O O    . HOH E 3 .   ? -2.220  19.320 22.552  1.00 39.80 ? 356 HOH A O    1 
HETATM 1961 O O    . HOH E 3 .   ? 24.666  27.126 39.269  1.00 32.55 ? 357 HOH A O    1 
HETATM 1962 O O    . HOH E 3 .   ? 0.805   13.578 21.879  1.00 33.29 ? 358 HOH A O    1 
HETATM 1963 O O    . HOH E 3 .   ? 8.729   9.719  34.620  1.00 24.11 ? 359 HOH A O    1 
HETATM 1964 O O    . HOH E 3 .   ? -5.595  13.241 33.443  1.00 25.85 ? 360 HOH A O    1 
HETATM 1965 O O    . HOH E 3 .   ? -8.009  30.856 23.768  1.00 39.93 ? 361 HOH A O    1 
HETATM 1966 O O    . HOH E 3 .   ? -0.390  6.042  29.236  1.00 28.57 ? 362 HOH A O    1 
HETATM 1967 O O    . HOH E 3 .   ? 14.444  23.090 23.605  1.00 19.77 ? 363 HOH A O    1 
HETATM 1968 O O    . HOH E 3 .   ? 3.394   15.363 21.543  1.00 21.88 ? 364 HOH A O    1 
HETATM 1969 O O    . HOH E 3 .   ? -1.607  28.370 24.028  1.00 33.45 ? 365 HOH A O    1 
HETATM 1970 O O    . HOH E 3 .   ? -4.450  30.101 22.999  1.00 35.91 ? 366 HOH A O    1 
HETATM 1971 O O    . HOH E 3 .   ? -9.028  23.949 20.920  1.00 13.26 ? 367 HOH A O    1 
HETATM 1972 O O    . HOH E 3 .   ? 7.297   18.012 19.673  1.00 29.03 ? 368 HOH A O    1 
HETATM 1973 O O    . HOH E 3 .   ? 18.843  19.500 39.305  1.00 30.53 ? 369 HOH A O    1 
HETATM 1974 O O    . HOH E 3 .   ? 23.955  37.614 29.995  1.00 30.45 ? 370 HOH A O    1 
HETATM 1975 O O    . HOH E 3 .   ? 9.272   11.141 18.311  1.00 37.11 ? 371 HOH A O    1 
HETATM 1976 O O    . HOH E 3 .   ? 7.978   32.888 38.610  1.00 26.95 ? 372 HOH A O    1 
HETATM 1977 O O    . HOH E 3 .   ? -12.091 22.717 22.250  1.00 25.97 ? 373 HOH A O    1 
HETATM 1978 O O    . HOH E 3 .   ? 23.792  40.807 51.154  1.00 43.37 ? 374 HOH A O    1 
HETATM 1979 O O    . HOH E 3 .   ? 22.259  38.577 49.085  1.00 34.48 ? 375 HOH A O    1 
HETATM 1980 O O    . HOH E 3 .   ? 1.164   18.050 23.710  1.00 30.23 ? 376 HOH A O    1 
HETATM 1981 O O    . HOH E 3 .   ? 30.820  46.004 48.155  1.00 42.92 ? 377 HOH A O    1 
HETATM 1982 O O    . HOH E 3 .   ? -13.793 16.780 28.363  1.00 31.95 ? 378 HOH A O    1 
HETATM 1983 O O    . HOH E 3 .   ? 18.837  45.752 52.011  1.00 44.93 ? 379 HOH A O    1 
HETATM 1984 O O    . HOH E 3 .   ? -5.361  20.543 23.227  1.00 28.69 ? 380 HOH A O    1 
HETATM 1985 O O    . HOH E 3 .   ? 0.335   30.315 26.405  1.00 34.48 ? 381 HOH A O    1 
HETATM 1986 O O    . HOH E 3 .   ? 4.460   35.005 32.941  1.00 32.86 ? 382 HOH A O    1 
HETATM 1987 O O    . HOH E 3 .   ? 0.131   3.254  25.713  1.00 37.57 ? 383 HOH A O    1 
HETATM 1988 O O    . HOH E 3 .   ? 16.328  13.821 27.900  1.00 36.22 ? 384 HOH A O    1 
HETATM 1989 O O    . HOH E 3 .   ? 7.377   40.797 45.970  1.00 27.62 ? 385 HOH A O    1 
HETATM 1990 O O    . HOH E 3 .   ? 25.737  28.460 32.439  1.00 28.58 ? 386 HOH A O    1 
HETATM 1991 O O    . HOH E 3 .   ? 6.006   6.492  25.097  1.00 33.37 ? 387 HOH A O    1 
HETATM 1992 O O    . HOH E 3 .   ? 24.521  49.628 48.166  1.00 40.84 ? 388 HOH A O    1 
HETATM 1993 O O    . HOH E 3 .   ? -13.066 18.548 21.979  1.00 37.10 ? 389 HOH A O    1 
HETATM 1994 O O    . HOH E 3 .   ? 13.877  13.929 27.362  1.00 43.75 ? 390 HOH A O    1 
HETATM 1995 O O    . HOH E 3 .   ? 18.209  24.597 50.958  1.00 33.04 ? 391 HOH A O    1 
HETATM 1996 O O    . HOH E 3 .   ? 9.647   26.024 51.896  1.00 31.94 ? 392 HOH A O    1 
HETATM 1997 O O    . HOH E 3 .   ? -0.400  32.071 31.259  1.00 30.91 ? 393 HOH A O    1 
HETATM 1998 O O    . HOH E 3 .   ? -1.355  7.217  26.189  1.00 14.25 ? 394 HOH A O    1 
HETATM 1999 O O    . HOH E 3 .   ? 33.016  46.079 39.580  1.00 30.20 ? 395 HOH A O    1 
HETATM 2000 O O    . HOH E 3 .   ? 25.146  32.749 41.342  1.00 16.07 ? 396 HOH A O    1 
HETATM 2001 O O    . HOH E 3 .   ? 13.433  10.001 23.195  1.00 41.05 ? 397 HOH A O    1 
HETATM 2002 O O    . HOH E 3 .   ? 8.869   26.849 54.434  1.00 39.56 ? 398 HOH A O    1 
HETATM 2003 O O    . HOH E 3 .   ? 12.766  16.121 24.999  1.00 23.20 ? 399 HOH A O    1 
HETATM 2004 O O    . HOH E 3 .   ? 31.800  41.032 37.645  1.00 36.32 ? 400 HOH A O    1 
HETATM 2005 O O    . HOH E 3 .   ? 14.869  11.774 24.010  1.00 39.92 ? 401 HOH A O    1 
HETATM 2006 O O    . HOH E 3 .   ? 2.375   27.120 22.527  1.00 32.54 ? 402 HOH A O    1 
HETATM 2007 O O    . HOH E 3 .   ? 7.579   6.221  28.075  1.00 36.66 ? 403 HOH A O    1 
HETATM 2008 O O    . HOH E 3 .   ? 24.817  51.230 46.013  1.00 32.98 ? 404 HOH A O    1 
HETATM 2009 O O    . HOH E 3 .   ? 25.221  48.450 50.220  1.00 39.70 ? 405 HOH A O    1 
HETATM 2010 O O    . HOH E 3 .   ? 1.870   15.367 23.717  1.00 34.06 ? 406 HOH A O    1 
HETATM 2011 O O    . HOH E 3 .   ? 3.906   31.766 29.767  1.00 21.86 ? 407 HOH A O    1 
HETATM 2012 O O    . HOH E 3 .   ? 31.561  35.998 39.253  1.00 35.66 ? 408 HOH A O    1 
HETATM 2013 O O    . HOH E 3 .   ? -0.619  32.172 27.309  1.00 39.30 ? 409 HOH A O    1 
HETATM 2014 O O    . HOH E 3 .   ? 5.731   40.155 43.395  1.00 38.37 ? 410 HOH A O    1 
HETATM 2015 O O    . HOH E 3 .   ? 23.980  27.372 42.641  1.00 32.41 ? 411 HOH A O    1 
HETATM 2016 O O    . HOH E 3 .   ? 6.402   22.736 50.227  1.00 42.26 ? 412 HOH A O    1 
HETATM 2017 O O    . HOH E 3 .   ? -0.692  5.347  24.393  1.00 34.03 ? 413 HOH A O    1 
HETATM 2018 O O    . HOH E 3 .   ? 24.912  29.538 29.702  1.00 30.71 ? 414 HOH A O    1 
HETATM 2019 O O    . HOH E 3 .   ? 4.199   42.344 43.314  1.00 52.42 ? 415 HOH A O    1 
HETATM 2020 O O    . HOH E 3 .   ? -5.079  9.879  27.486  1.00 36.15 ? 416 HOH A O    1 
HETATM 2021 O O    . HOH E 3 .   ? 29.383  34.223 39.968  1.00 30.45 ? 417 HOH A O    1 
HETATM 2022 O O    . HOH E 3 .   ? -8.087  36.794 27.114  1.00 34.87 ? 418 HOH A O    1 
HETATM 2023 O O    . HOH E 3 .   ? -7.966  13.895 26.480  1.00 37.90 ? 419 HOH A O    1 
HETATM 2024 O O    . HOH E 3 .   ? 2.008   33.647 31.103  1.00 38.25 ? 420 HOH A O    1 
HETATM 2025 O O    . HOH E 3 .   ? 4.221   4.576  23.790  1.00 36.52 ? 421 HOH A O    1 
HETATM 2026 O O    . HOH E 3 .   ? 2.922   30.203 26.270  1.00 31.46 ? 422 HOH A O    1 
HETATM 2027 O O    . HOH E 3 .   ? -2.372  33.102 29.834  1.00 31.82 ? 423 HOH A O    1 
HETATM 2028 O O    . HOH E 3 .   ? 7.289   40.917 33.426  1.00 36.00 ? 424 HOH A O    1 
HETATM 2029 O O    . HOH E 3 .   ? 20.521  20.521 37.431  0.50 31.38 ? 425 HOH A O    1 
HETATM 2030 O O    . HOH E 3 .   ? 0.955   29.514 23.370  1.00 37.04 ? 426 HOH A O    1 
HETATM 2031 O O    . HOH E 3 .   ? 17.233  24.728 25.827  1.00 20.84 ? 427 HOH A O    1 
HETATM 2032 O O    . HOH E 3 .   ? -15.171 23.057 22.929  1.00 32.26 ? 428 HOH A O    1 
HETATM 2033 O O    . HOH E 3 .   ? 16.987  21.969 25.106  1.00 35.39 ? 429 HOH A O    1 
HETATM 2034 O O    . HOH E 3 .   ? -3.509  31.274 20.641  1.00 39.99 ? 430 HOH A O    1 
HETATM 2035 O O    . HOH E 3 .   ? -9.385  13.958 28.482  1.00 32.19 ? 431 HOH A O    1 
HETATM 2036 O O    . HOH E 3 .   ? 4.479   29.698 24.197  1.00 31.81 ? 432 HOH A O    1 
HETATM 2037 O O    . HOH E 3 .   ? 3.144   39.180 35.612  1.00 50.14 ? 433 HOH A O    1 
HETATM 2038 O O    . HOH E 3 .   ? 30.732  33.135 41.418  1.00 43.35 ? 434 HOH A O    1 
HETATM 2039 O O    . HOH E 3 .   ? 2.853   40.961 34.392  1.00 49.93 ? 435 HOH A O    1 
HETATM 2040 O O    . HOH F 3 .   ? 18.090  35.175 -4.100  1.00 46.71 ? 301 HOH B O    1 
HETATM 2041 O O    . HOH F 3 .   ? 8.690   35.930 -2.250  1.00 34.19 ? 302 HOH B O    1 
HETATM 2042 O O    . HOH F 3 .   ? 23.546  24.850 -1.959  1.00 39.72 ? 303 HOH B O    1 
HETATM 2043 O O    . HOH F 3 .   ? 21.286  25.188 -5.850  1.00 30.99 ? 304 HOH B O    1 
HETATM 2044 O O    . HOH F 3 .   ? 35.945  36.895 15.902  1.00 44.13 ? 305 HOH B O    1 
HETATM 2045 O O    . HOH F 3 .   ? 30.697  47.499 9.041   1.00 43.80 ? 306 HOH B O    1 
HETATM 2046 O O    . HOH F 3 .   ? -2.948  32.038 -6.039  1.00 45.60 ? 307 HOH B O    1 
HETATM 2047 O O    . HOH F 3 .   ? 6.476   46.729 14.272  1.00 26.90 ? 308 HOH B O    1 
HETATM 2048 O O    . HOH F 3 .   ? -2.484  7.714  3.485   1.00 38.70 ? 309 HOH B O    1 
HETATM 2049 O O    . HOH F 3 .   ? 24.376  29.582 6.415   1.00 18.13 ? 310 HOH B O    1 
HETATM 2050 O O    . HOH F 3 .   ? 5.948   48.802 17.586  1.00 35.79 ? 311 HOH B O    1 
HETATM 2051 O O    . HOH F 3 .   ? 29.637  36.264 12.468  1.00 31.90 ? 312 HOH B O    1 
HETATM 2052 O O    . HOH F 3 .   ? 19.390  33.045 21.433  1.00 33.22 ? 313 HOH B O    1 
HETATM 2053 O O    . HOH F 3 .   ? 14.248  44.657 18.277  1.00 26.07 ? 314 HOH B O    1 
HETATM 2054 O O    . HOH F 3 .   ? 23.822  45.284 13.659  1.00 29.58 ? 315 HOH B O    1 
HETATM 2055 O O    . HOH F 3 .   ? 14.178  20.881 4.214   1.00 25.01 ? 316 HOH B O    1 
HETATM 2056 O O    . HOH F 3 .   ? 4.229   21.013 -6.840  1.00 29.32 ? 317 HOH B O    1 
HETATM 2057 O O    . HOH F 3 .   ? 7.374   13.789 9.921   1.00 22.69 ? 318 HOH B O    1 
HETATM 2058 O O    . HOH F 3 .   ? 9.153   12.789 6.089   1.00 25.35 ? 319 HOH B O    1 
HETATM 2059 O O    . HOH F 3 .   ? -0.025  9.875  -4.874  1.00 36.93 ? 320 HOH B O    1 
HETATM 2060 O O    . HOH F 3 .   ? 27.860  38.044 21.077  1.00 19.84 ? 321 HOH B O    1 
HETATM 2061 O O    . HOH F 3 .   ? 2.531   34.404 8.961   1.00 38.18 ? 322 HOH B O    1 
HETATM 2062 O O    . HOH F 3 .   ? 7.956   34.983 12.576  1.00 18.22 ? 323 HOH B O    1 
HETATM 2063 O O    . HOH F 3 .   ? 0.611   17.305 -3.310  1.00 22.15 ? 324 HOH B O    1 
HETATM 2064 O O    . HOH F 3 .   ? 15.353  55.179 21.138  1.00 28.84 ? 325 HOH B O    1 
HETATM 2065 O O    . HOH F 3 .   ? 11.295  42.951 9.732   1.00 19.42 ? 326 HOH B O    1 
HETATM 2066 O O    . HOH F 3 .   ? 25.185  28.051 8.986   1.00 21.51 ? 327 HOH B O    1 
HETATM 2067 O O    . HOH F 3 .   ? 37.316  42.815 17.880  1.00 40.66 ? 328 HOH B O    1 
HETATM 2068 O O    . HOH F 3 .   ? 23.601  22.938 4.903   1.00 21.69 ? 329 HOH B O    1 
HETATM 2069 O O    . HOH F 3 .   ? 25.969  42.138 11.878  1.00 17.39 ? 330 HOH B O    1 
HETATM 2070 O O    . HOH F 3 .   ? 14.846  39.890 22.456  1.00 35.23 ? 331 HOH B O    1 
HETATM 2071 O O    . HOH F 3 .   ? -0.698  16.354 10.353  1.00 22.57 ? 332 HOH B O    1 
HETATM 2072 O O    . HOH F 3 .   ? 19.616  45.306 19.856  1.00 26.52 ? 333 HOH B O    1 
HETATM 2073 O O    . HOH F 3 .   ? 14.985  54.877 17.668  1.00 26.86 ? 334 HOH B O    1 
HETATM 2074 O O    . HOH F 3 .   ? 25.475  36.732 16.670  1.00 17.18 ? 335 HOH B O    1 
HETATM 2075 O O    . HOH F 3 .   ? 18.860  38.961 16.548  1.00 21.50 ? 336 HOH B O    1 
HETATM 2076 O O    . HOH F 3 .   ? 21.596  21.109 -5.060  1.00 29.65 ? 337 HOH B O    1 
HETATM 2077 O O    . HOH F 3 .   ? 4.177   8.162  3.539   1.00 28.08 ? 338 HOH B O    1 
HETATM 2078 O O    . HOH F 3 .   ? 27.782  46.397 16.158  1.00 29.10 ? 339 HOH B O    1 
HETATM 2079 O O    . HOH F 3 .   ? 17.798  20.339 13.512  1.00 36.85 ? 340 HOH B O    1 
HETATM 2080 O O    . HOH F 3 .   ? 20.373  47.578 19.943  1.00 24.08 ? 341 HOH B O    1 
HETATM 2081 O O    . HOH F 3 .   ? -1.218  18.045 -6.675  1.00 29.72 ? 342 HOH B O    1 
HETATM 2082 O O    . HOH F 3 .   ? 0.943   9.286  -6.579  1.00 44.04 ? 343 HOH B O    1 
HETATM 2083 O O    . HOH F 3 .   ? 21.865  26.871 18.516  1.00 26.05 ? 344 HOH B O    1 
HETATM 2084 O O    . HOH F 3 .   ? 18.445  18.445 0.000   0.50 26.87 ? 345 HOH B O    1 
HETATM 2085 O O    . HOH F 3 .   ? 8.383   32.717 4.616   1.00 27.30 ? 346 HOH B O    1 
HETATM 2086 O O    . HOH F 3 .   ? 24.020  23.063 13.321  1.00 33.28 ? 347 HOH B O    1 
HETATM 2087 O O    . HOH F 3 .   ? 14.391  23.679 5.513   1.00 22.25 ? 348 HOH B O    1 
HETATM 2088 O O    . HOH F 3 .   ? 25.307  38.831 21.944  1.00 31.78 ? 349 HOH B O    1 
HETATM 2089 O O    . HOH F 3 .   ? 17.788  45.262 18.749  1.00 29.53 ? 350 HOH B O    1 
HETATM 2090 O O    . HOH F 3 .   ? 3.514   18.604 -5.514  1.00 24.90 ? 351 HOH B O    1 
HETATM 2091 O O    . HOH F 3 .   ? 12.153  43.177 19.183  1.00 37.67 ? 352 HOH B O    1 
HETATM 2092 O O    . HOH F 3 .   ? 16.326  50.635 22.288  1.00 11.83 ? 353 HOH B O    1 
HETATM 2093 O O    . HOH F 3 .   ? 16.838  24.479 4.115   1.00 22.08 ? 354 HOH B O    1 
HETATM 2094 O O    . HOH F 3 .   ? 12.351  34.505 -7.651  1.00 37.18 ? 355 HOH B O    1 
HETATM 2095 O O    . HOH F 3 .   ? 24.486  30.896 1.248   1.00 19.96 ? 356 HOH B O    1 
HETATM 2096 O O    . HOH F 3 .   ? 10.463  33.893 18.699  1.00 32.61 ? 357 HOH B O    1 
HETATM 2097 O O    . HOH F 3 .   ? 34.679  37.528 18.609  1.00 34.43 ? 358 HOH B O    1 
HETATM 2098 O O    . HOH F 3 .   ? 32.558  32.663 21.143  1.00 40.18 ? 359 HOH B O    1 
HETATM 2099 O O    . HOH F 3 .   ? 21.698  17.462 8.031   1.00 35.24 ? 360 HOH B O    1 
HETATM 2100 O O    . HOH F 3 .   ? 17.369  54.071 20.757  1.00 23.26 ? 361 HOH B O    1 
HETATM 2101 O O    . HOH F 3 .   ? 7.824   32.759 -9.709  1.00 41.96 ? 362 HOH B O    1 
HETATM 2102 O O    . HOH F 3 .   ? 22.270  41.138 20.114  1.00 30.17 ? 363 HOH B O    1 
HETATM 2103 O O    . HOH F 3 .   ? 15.451  27.282 20.332  1.00 24.09 ? 364 HOH B O    1 
HETATM 2104 O O    . HOH F 3 .   ? 25.333  25.715 7.596   1.00 22.85 ? 365 HOH B O    1 
HETATM 2105 O O    . HOH F 3 .   ? 25.256  26.247 17.718  1.00 42.69 ? 366 HOH B O    1 
HETATM 2106 O O    . HOH F 3 .   ? -9.216  10.679 -1.610  1.00 31.55 ? 367 HOH B O    1 
HETATM 2107 O O    . HOH F 3 .   ? 10.333  49.350 18.906  1.00 29.82 ? 368 HOH B O    1 
HETATM 2108 O O    . HOH F 3 .   ? 11.548  38.298 14.665  1.00 17.35 ? 369 HOH B O    1 
HETATM 2109 O O    . HOH F 3 .   ? 31.073  31.435 7.213   1.00 41.26 ? 370 HOH B O    1 
HETATM 2110 O O    . HOH F 3 .   ? 9.561   15.766 2.357   1.00 20.30 ? 371 HOH B O    1 
HETATM 2111 O O    . HOH F 3 .   ? 26.121  29.141 2.872   1.00 24.05 ? 372 HOH B O    1 
HETATM 2112 O O    . HOH F 3 .   ? -9.386  14.276 -0.320  1.00 41.99 ? 373 HOH B O    1 
HETATM 2113 O O    . HOH F 3 .   ? 31.981  30.309 9.449   1.00 40.69 ? 374 HOH B O    1 
HETATM 2114 O O    . HOH F 3 .   ? -7.229  16.955 -3.819  1.00 31.38 ? 375 HOH B O    1 
HETATM 2115 O O    . HOH F 3 .   ? 25.169  30.046 14.234  1.00 22.25 ? 376 HOH B O    1 
HETATM 2116 O O    . HOH F 3 .   ? 2.837   35.541 5.697   1.00 38.19 ? 377 HOH B O    1 
HETATM 2117 O O    . HOH F 3 .   ? 0.939   31.454 8.846   1.00 33.31 ? 378 HOH B O    1 
HETATM 2118 O O    . HOH F 3 .   ? 29.880  32.665 24.962  1.00 43.84 ? 379 HOH B O    1 
HETATM 2119 O O    . HOH F 3 .   ? -0.905  33.488 4.615   1.00 39.92 ? 380 HOH B O    1 
HETATM 2120 O O    . HOH F 3 .   ? 20.235  21.122 7.729   1.00 26.39 ? 381 HOH B O    1 
HETATM 2121 O O    . HOH F 3 .   ? 4.685   14.015 -4.515  1.00 37.27 ? 382 HOH B O    1 
HETATM 2122 O O    . HOH F 3 .   ? -5.415  7.295  2.377   1.00 42.09 ? 383 HOH B O    1 
HETATM 2123 O O    . HOH F 3 .   ? 18.406  49.465 20.427  1.00 29.57 ? 384 HOH B O    1 
HETATM 2124 O O    . HOH F 3 .   ? 34.419  43.346 13.951  1.00 32.76 ? 385 HOH B O    1 
HETATM 2125 O O    . HOH F 3 .   ? 29.080  25.459 13.298  1.00 34.72 ? 386 HOH B O    1 
HETATM 2126 O O    . HOH F 3 .   ? 19.090  24.231 -5.447  1.00 32.88 ? 387 HOH B O    1 
HETATM 2127 O O    . HOH F 3 .   ? 26.220  47.583 15.072  1.00 36.06 ? 388 HOH B O    1 
HETATM 2128 O O    . HOH F 3 .   ? 33.091  32.996 23.094  1.00 42.02 ? 389 HOH B O    1 
HETATM 2129 O O    . HOH F 3 .   ? 7.473   13.853 2.559   1.00 25.80 ? 390 HOH B O    1 
HETATM 2130 O O    . HOH F 3 .   ? 24.964  33.064 24.879  1.00 33.78 ? 391 HOH B O    1 
HETATM 2131 O O    . HOH F 3 .   ? 18.479  27.233 19.759  1.00 19.40 ? 392 HOH B O    1 
HETATM 2132 O O    . HOH F 3 .   ? 23.589  26.165 -0.397  1.00 38.14 ? 393 HOH B O    1 
HETATM 2133 O O    . HOH F 3 .   ? 27.465  49.206 12.795  1.00 51.63 ? 394 HOH B O    1 
HETATM 2134 O O    . HOH F 3 .   ? 27.007  24.508 4.078   1.00 37.30 ? 395 HOH B O    1 
HETATM 2135 O O    . HOH F 3 .   ? 16.049  15.869 -5.480  1.00 33.25 ? 396 HOH B O    1 
HETATM 2136 O O    . HOH F 3 .   ? 12.833  15.886 -6.133  1.00 20.68 ? 397 HOH B O    1 
HETATM 2137 O O    . HOH F 3 .   ? 27.683  25.172 15.830  1.00 37.25 ? 398 HOH B O    1 
HETATM 2138 O O    . HOH F 3 .   ? 22.970  56.757 14.925  1.00 36.41 ? 399 HOH B O    1 
HETATM 2139 O O    . HOH F 3 .   ? 4.092   20.809 -9.885  1.00 46.24 ? 400 HOH B O    1 
HETATM 2140 O O    . HOH F 3 .   ? 0.274   32.944 -2.718  1.00 26.75 ? 401 HOH B O    1 
HETATM 2141 O O    . HOH F 3 .   ? 24.234  49.826 18.257  1.00 34.16 ? 402 HOH B O    1 
HETATM 2142 O O    . HOH F 3 .   ? 2.925   34.253 2.814   1.00 43.93 ? 403 HOH B O    1 
HETATM 2143 O O    . HOH F 3 .   ? 19.932  22.470 14.753  1.00 44.68 ? 404 HOH B O    1 
HETATM 2144 O O    . HOH F 3 .   ? 10.133  40.993 16.945  1.00 37.99 ? 405 HOH B O    1 
HETATM 2145 O O    . HOH F 3 .   ? 16.122  17.237 3.380   1.00 31.37 ? 406 HOH B O    1 
HETATM 2146 O O    . HOH F 3 .   ? 33.273  44.322 17.418  1.00 18.38 ? 407 HOH B O    1 
HETATM 2147 O O    . HOH F 3 .   ? 24.869  23.590 9.195   1.00 26.38 ? 408 HOH B O    1 
HETATM 2148 O O    . HOH F 3 .   ? 19.130  58.903 16.089  1.00 45.10 ? 409 HOH B O    1 
HETATM 2149 O O    . HOH F 3 .   ? 25.043  23.454 16.495  1.00 42.21 ? 410 HOH B O    1 
HETATM 2150 O O    . HOH F 3 .   ? 22.977  26.867 -6.769  1.00 43.95 ? 411 HOH B O    1 
HETATM 2151 O O    . HOH F 3 .   ? -7.417  12.851 -8.344  1.00 41.73 ? 412 HOH B O    1 
HETATM 2152 O O    . HOH F 3 .   ? 23.390  28.969 -0.476  1.00 31.23 ? 413 HOH B O    1 
HETATM 2153 O O    . HOH F 3 .   ? 4.395   35.217 1.297   1.00 38.33 ? 414 HOH B O    1 
HETATM 2154 O O    . HOH F 3 .   ? 13.361  38.497 20.330  1.00 30.26 ? 415 HOH B O    1 
HETATM 2155 O O    . HOH F 3 .   ? -7.397  8.953  1.268   1.00 37.57 ? 416 HOH B O    1 
HETATM 2156 O O    . HOH F 3 .   ? 8.157   41.362 11.934  1.00 40.84 ? 417 HOH B O    1 
HETATM 2157 O O    . HOH F 3 .   ? 21.842  18.494 -4.243  1.00 27.48 ? 418 HOH B O    1 
HETATM 2158 O O    . HOH F 3 .   ? 25.310  40.081 19.847  1.00 42.36 ? 419 HOH B O    1 
HETATM 2159 O O    . HOH F 3 .   ? 19.954  16.531 -3.103  1.00 28.34 ? 420 HOH B O    1 
HETATM 2160 O O    . HOH F 3 .   ? 9.028   37.311 13.576  1.00 27.06 ? 421 HOH B O    1 
HETATM 2161 O O    . HOH F 3 .   ? 4.983   44.820 17.935  1.00 45.36 ? 422 HOH B O    1 
HETATM 2162 O O    . HOH F 3 .   ? 3.880   46.250 15.665  1.00 38.10 ? 423 HOH B O    1 
HETATM 2163 O O    . HOH F 3 .   ? 34.279  41.691 21.236  1.00 31.43 ? 424 HOH B O    1 
HETATM 2164 O O    . HOH F 3 .   ? 6.542   9.239  4.378   1.00 29.82 ? 425 HOH B O    1 
HETATM 2165 O O    . HOH F 3 .   ? 14.799  13.021 8.261   1.00 35.84 ? 426 HOH B O    1 
HETATM 2166 O O    . HOH F 3 .   ? -8.944  15.995 -2.653  1.00 38.40 ? 427 HOH B O    1 
HETATM 2167 O O    . HOH F 3 .   ? 34.759  34.901 20.259  1.00 37.30 ? 428 HOH B O    1 
HETATM 2168 O O    . HOH F 3 .   ? 35.172  43.700 19.472  1.00 30.75 ? 429 HOH B O    1 
HETATM 2169 O O    . HOH F 3 .   ? 7.973   11.579 3.830   1.00 29.32 ? 430 HOH B O    1 
HETATM 2170 O O    . HOH F 3 .   ? 36.387  39.285 19.905  1.00 36.06 ? 431 HOH B O    1 
HETATM 2171 O O    . HOH F 3 .   ? 27.031  26.744 1.331   1.00 53.85 ? 432 HOH B O    1 
HETATM 2172 O O    . HOH F 3 .   ? 7.192   43.820 13.651  1.00 36.76 ? 433 HOH B O    1 
HETATM 2173 O O    . HOH F 3 .   ? 30.196  48.024 16.153  1.00 39.16 ? 434 HOH B O    1 
HETATM 2174 O O    . HOH F 3 .   ? 7.772   39.379 13.445  1.00 34.82 ? 435 HOH B O    1 
HETATM 2175 O O    . HOH F 3 .   ? 3.400   49.102 16.419  1.00 43.52 ? 436 HOH B O    1 
HETATM 2176 O O    . HOH F 3 .   ? 5.015   47.871 20.211  1.00 48.78 ? 437 HOH B O    1 
HETATM 2177 O O    . HOH F 3 .   ? 16.423  57.560 17.349  1.00 27.05 ? 438 HOH B O    1 
HETATM 2178 O O    . HOH F 3 .   ? 23.576  21.660 7.699   1.00 36.85 ? 439 HOH B O    1 
HETATM 2179 O O    . HOH F 3 .   ? 22.356  21.479 15.022  1.00 43.20 ? 440 HOH B O    1 
HETATM 2180 O O    . HOH F 3 .   ? 16.489  56.964 20.521  1.00 31.00 ? 441 HOH B O    1 
HETATM 2181 O O    . HOH F 3 .   ? 11.316  40.583 19.955  1.00 37.98 ? 442 HOH B O    1 
HETATM 2182 O O    . HOH F 3 .   ? 10.896  38.291 17.520  1.00 32.75 ? 443 HOH B O    1 
HETATM 2183 O O    . HOH F 3 .   ? 25.762  20.662 12.472  1.00 45.90 ? 444 HOH B O    1 
HETATM 2184 O O    . HOH F 3 .   ? 33.140  47.187 16.744  1.00 37.70 ? 445 HOH B O    1 
HETATM 2185 O O    . HOH F 3 .   ? 19.133  58.531 21.011  1.00 38.78 ? 446 HOH B O    1 
HETATM 2186 O O    . HOH F 3 .   ? 28.345  28.345 0.000   0.50 40.53 ? 447 HOH B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . ALA A 2   ? 0.8087 0.7470 0.6682 -0.0144 -0.0411 -0.0200 2   ALA A N   
2    C CA  . ALA A 2   ? 0.6514 0.5930 0.5182 -0.0160 -0.0477 -0.0170 2   ALA A CA  
3    C C   . ALA A 2   ? 0.5146 0.4598 0.3961 -0.0142 -0.0465 -0.0161 2   ALA A C   
4    O O   . ALA A 2   ? 0.4806 0.4249 0.3652 -0.0121 -0.0412 -0.0182 2   ALA A O   
5    C CB  . ALA A 2   ? 0.5643 0.5092 0.4297 -0.0164 -0.0508 -0.0117 2   ALA A CB  
6    N N   . ASP A 3   ? 0.4222 0.3714 0.3125 -0.0150 -0.0511 -0.0130 3   ASP A N   
7    C CA  . ASP A 3   ? 0.3587 0.3116 0.2625 -0.0136 -0.0501 -0.0119 3   ASP A CA  
8    C C   . ASP A 3   ? 0.3590 0.3168 0.2698 -0.0113 -0.0476 -0.0078 3   ASP A C   
9    O O   . ASP A 3   ? 0.3123 0.2709 0.2187 -0.0112 -0.0480 -0.0052 3   ASP A O   
10   C CB  . ASP A 3   ? 0.4311 0.3856 0.3413 -0.0158 -0.0556 -0.0113 3   ASP A CB  
11   C CG  . ASP A 3   ? 0.3701 0.3194 0.2729 -0.0185 -0.0586 -0.0155 3   ASP A CG  
12   O OD1 . ASP A 3   ? 0.3633 0.3079 0.2615 -0.0180 -0.0551 -0.0195 3   ASP A OD1 
13   O OD2 . ASP A 3   ? 0.3527 0.3028 0.2547 -0.0210 -0.0644 -0.0146 3   ASP A OD2 
14   N N   . ARG A 4   ? 0.3499 0.3105 0.2709 -0.0100 -0.0460 -0.0071 4   ARG A N   
15   C CA  . ARG A 4   ? 0.3173 0.2822 0.2447 -0.0078 -0.0434 -0.0037 4   ARG A CA  
16   C C   . ARG A 4   ? 0.2611 0.2299 0.2007 -0.0068 -0.0430 -0.0026 4   ARG A C   
17   O O   . ARG A 4   ? 0.2868 0.2545 0.2295 -0.0073 -0.0430 -0.0047 4   ARG A O   
18   C CB  . ARG A 4   ? 0.3345 0.2981 0.2584 -0.0058 -0.0376 -0.0047 4   ARG A CB  
19   C CG  . ARG A 4   ? 0.3608 0.3227 0.2868 -0.0043 -0.0334 -0.0080 4   ARG A CG  
20   C CD  . ARG A 4   ? 0.3072 0.2685 0.2299 -0.0026 -0.0282 -0.0087 4   ARG A CD  
21   N NE  . ARG A 4   ? 0.3269 0.2871 0.2528 -0.0010 -0.0246 -0.0115 4   ARG A NE  
22   C CZ  . ARG A 4   ? 0.3567 0.3126 0.2778 -0.0011 -0.0233 -0.0153 4   ARG A CZ  
23   N NH1 . ARG A 4   ? 0.3761 0.3282 0.2881 -0.0029 -0.0253 -0.0172 4   ARG A NH1 
24   N NH2 . ARG A 4   ? 0.3406 0.2958 0.2658 0.0007  -0.0202 -0.0172 4   ARG A NH2 
25   N N   . ILE A 5   ? 0.2162 0.1894 0.1629 -0.0058 -0.0433 0.0010  5   ILE A N   
26   C CA  . ILE A 5   ? 0.2080 0.1853 0.1659 -0.0047 -0.0426 0.0024  5   ILE A CA  
27   C C   . ILE A 5   ? 0.2750 0.2534 0.2349 -0.0023 -0.0377 0.0028  5   ILE A C   
28   O O   . ILE A 5   ? 0.2136 0.1917 0.1698 -0.0018 -0.0368 0.0042  5   ILE A O   
29   C CB  . ILE A 5   ? 0.2408 0.2221 0.2050 -0.0053 -0.0466 0.0058  5   ILE A CB  
30   C CG1 . ILE A 5   ? 0.2912 0.2720 0.2544 -0.0079 -0.0518 0.0055  5   ILE A CG1 
31   C CG2 . ILE A 5   ? 0.2446 0.2301 0.2197 -0.0038 -0.0447 0.0071  5   ILE A CG2 
32   C CD1 . ILE A 5   ? 0.2851 0.2681 0.2486 -0.0087 -0.0566 0.0086  5   ILE A CD1 
33   N N   . GLU A 6   ? 0.2201 0.1994 0.1854 -0.0012 -0.0349 0.0017  6   GLU A N   
34   C CA  . GLU A 6   ? 0.2680 0.2482 0.2350 0.0009  -0.0306 0.0016  6   GLU A CA  
35   C C   . GLU A 6   ? 0.2090 0.1930 0.1853 0.0019  -0.0298 0.0029  6   GLU A C   
36   O O   . GLU A 6   ? 0.2480 0.2325 0.2281 0.0016  -0.0299 0.0020  6   GLU A O   
37   C CB  . GLU A 6   ? 0.3056 0.2827 0.2688 0.0015  -0.0276 -0.0015 6   GLU A CB  
38   C CG  . GLU A 6   ? 0.2234 0.1966 0.1770 0.0008  -0.0274 -0.0032 6   GLU A CG  
39   C CD  . GLU A 6   ? 0.3460 0.3165 0.2969 0.0020  -0.0238 -0.0063 6   GLU A CD  
40   O OE1 . GLU A 6   ? 0.3143 0.2852 0.2703 0.0028  -0.0228 -0.0072 6   GLU A OE1 
41   O OE2 . GLU A 6   ? 0.3255 0.2935 0.2694 0.0020  -0.0220 -0.0077 6   GLU A OE2 
42   N N   . LEU A 7   ? 0.2122 0.1985 0.1917 0.0030  -0.0289 0.0049  7   LEU A N   
43   C CA  . LEU A 7   ? 0.1830 0.1727 0.1706 0.0041  -0.0274 0.0056  7   LEU A CA  
44   C C   . LEU A 7   ? 0.2135 0.2030 0.2007 0.0056  -0.0235 0.0046  7   LEU A C   
45   O O   . LEU A 7   ? 0.2137 0.2021 0.1973 0.0059  -0.0224 0.0050  7   LEU A O   
46   C CB  . LEU A 7   ? 0.2488 0.2411 0.2412 0.0043  -0.0292 0.0084  7   LEU A CB  
47   C CG  . LEU A 7   ? 0.2591 0.2546 0.2596 0.0057  -0.0273 0.0091  7   LEU A CG  
48   C CD1 . LEU A 7   ? 0.2544 0.2514 0.2591 0.0054  -0.0267 0.0079  7   LEU A CD1 
49   C CD2 . LEU A 7   ? 0.1840 0.1815 0.1894 0.0060  -0.0292 0.0118  7   LEU A CD2 
50   N N   . ARG A 8   ? 0.1753 0.1659 0.1662 0.0064  -0.0216 0.0034  8   ARG A N   
51   C CA  . ARG A 8   ? 0.2104 0.2010 0.2010 0.0077  -0.0185 0.0023  8   ARG A CA  
52   C C   . ARG A 8   ? 0.1798 0.1731 0.1764 0.0086  -0.0171 0.0025  8   ARG A C   
53   O O   . ARG A 8   ? 0.1991 0.1938 0.1991 0.0084  -0.0177 0.0026  8   ARG A O   
54   C CB  . ARG A 8   ? 0.2069 0.1952 0.1941 0.0079  -0.0174 0.0001  8   ARG A CB  
55   C CG  . ARG A 8   ? 0.2415 0.2265 0.2219 0.0071  -0.0181 -0.0008 8   ARG A CG  
56   C CD  . ARG A 8   ? 0.2439 0.2285 0.2211 0.0076  -0.0161 -0.0006 8   ARG A CD  
57   N NE  . ARG A 8   ? 0.2650 0.2465 0.2350 0.0070  -0.0159 -0.0018 8   ARG A NE  
58   C CZ  . ARG A 8   ? 0.2994 0.2795 0.2645 0.0057  -0.0180 -0.0008 8   ARG A CZ  
59   N NH1 . ARG A 8   ? 0.2295 0.2111 0.1969 0.0050  -0.0207 0.0016  8   ARG A NH1 
60   N NH2 . ARG A 8   ? 0.3031 0.2801 0.2607 0.0052  -0.0173 -0.0023 8   ARG A NH2 
61   N N   . GLY A 9   ? 0.1812 0.1754 0.1791 0.0095  -0.0152 0.0024  9   GLY A N   
62   C CA  . GLY A 9   ? 0.1777 0.1740 0.1802 0.0103  -0.0137 0.0020  9   GLY A CA  
63   C C   . GLY A 9   ? 0.2055 0.2038 0.2130 0.0104  -0.0143 0.0031  9   GLY A C   
64   O O   . GLY A 9   ? 0.1778 0.1777 0.1886 0.0108  -0.0132 0.0025  9   GLY A O   
65   N N   . LEU A 10  ? 0.1734 0.1715 0.1815 0.0101  -0.0159 0.0049  10  LEU A N   
66   C CA  . LEU A 10  ? 0.1772 0.1772 0.1912 0.0105  -0.0163 0.0061  10  LEU A CA  
67   C C   . LEU A 10  ? 0.2233 0.2237 0.2402 0.0114  -0.0141 0.0055  10  LEU A C   
68   O O   . LEU A 10  ? 0.1732 0.1723 0.1886 0.0115  -0.0135 0.0060  10  LEU A O   
69   C CB  . LEU A 10  ? 0.1673 0.1668 0.1812 0.0100  -0.0189 0.0085  10  LEU A CB  
70   C CG  . LEU A 10  ? 0.2209 0.2222 0.2415 0.0107  -0.0197 0.0102  10  LEU A CG  
71   C CD1 . LEU A 10  ? 0.1825 0.1865 0.2082 0.0107  -0.0198 0.0097  10  LEU A CD1 
72   C CD2 . LEU A 10  ? 0.1869 0.1874 0.2065 0.0103  -0.0228 0.0130  10  LEU A CD2 
73   N N   . THR A 11  ? 0.1868 0.1890 0.2075 0.0120  -0.0126 0.0042  11  THR A N   
74   C CA  . THR A 11  ? 0.1892 0.1916 0.2119 0.0127  -0.0105 0.0028  11  THR A CA  
75   C C   . THR A 11  ? 0.2029 0.2062 0.2315 0.0135  -0.0100 0.0032  11  THR A C   
76   O O   . THR A 11  ? 0.1911 0.1963 0.2231 0.0137  -0.0097 0.0031  11  THR A O   
77   C CB  . THR A 11  ? 0.1801 0.1833 0.2013 0.0127  -0.0091 0.0007  11  THR A CB  
78   O OG1 . THR A 11  ? 0.1978 0.1999 0.2142 0.0123  -0.0097 0.0005  11  THR A OG1 
79   C CG2 . THR A 11  ? 0.2021 0.2054 0.2245 0.0132  -0.0073 -0.0011 11  THR A CG2 
80   N N   . VAL A 12  ? 0.2059 0.2078 0.2362 0.0139  -0.0096 0.0038  12  VAL A N   
81   C CA  . VAL A 12  ? 0.2142 0.2163 0.2505 0.0148  -0.0094 0.0046  12  VAL A CA  
82   C C   . VAL A 12  ? 0.1878 0.1882 0.2257 0.0151  -0.0076 0.0033  12  VAL A C   
83   O O   . VAL A 12  ? 0.1473 0.1461 0.1824 0.0145  -0.0076 0.0038  12  VAL A O   
84   C CB  . VAL A 12  ? 0.2428 0.2442 0.2800 0.0148  -0.0120 0.0080  12  VAL A CB  
85   C CG1 . VAL A 12  ? 0.1761 0.1776 0.2205 0.0161  -0.0120 0.0091  12  VAL A CG1 
86   C CG2 . VAL A 12  ? 0.2267 0.2295 0.2620 0.0141  -0.0141 0.0090  12  VAL A CG2 
87   N N   . HIS A 13  ? 0.1829 0.1838 0.2255 0.0160  -0.0060 0.0016  13  HIS A N   
88   C CA  . HIS A 13  ? 0.1975 0.1964 0.2424 0.0162  -0.0045 0.0002  13  HIS A CA  
89   C C   . HIS A 13  ? 0.2114 0.2080 0.2595 0.0166  -0.0055 0.0031  13  HIS A C   
90   O O   . HIS A 13  ? 0.1760 0.1732 0.2276 0.0175  -0.0068 0.0053  13  HIS A O   
91   C CB  . HIS A 13  ? 0.2015 0.2011 0.2501 0.0171  -0.0023 -0.0027 13  HIS A CB  
92   C CG  . HIS A 13  ? 0.2209 0.2183 0.2709 0.0170  -0.0008 -0.0051 13  HIS A CG  
93   N ND1 . HIS A 13  ? 0.2348 0.2298 0.2903 0.0178  -0.0002 -0.0048 13  HIS A ND1 
94   C CD2 . HIS A 13  ? 0.2305 0.2276 0.2776 0.0161  0.0001  -0.0079 13  HIS A CD2 
95   C CE1 . HIS A 13  ? 0.2353 0.2284 0.2910 0.0173  0.0010  -0.0075 13  HIS A CE1 
96   N NE2 . HIS A 13  ? 0.2963 0.2909 0.3469 0.0162  0.0011  -0.0094 13  HIS A NE2 
97   N N   . GLY A 14  ? 0.1803 0.1746 0.2276 0.0160  -0.0050 0.0032  14  GLY A N   
98   C CA  . GLY A 14  ? 0.2076 0.1992 0.2578 0.0162  -0.0057 0.0062  14  GLY A CA  
99   C C   . GLY A 14  ? 0.2332 0.2221 0.2855 0.0157  -0.0041 0.0049  14  GLY A C   
100  O O   . GLY A 14  ? 0.1992 0.1885 0.2508 0.0151  -0.0026 0.0014  14  GLY A O   
101  N N   . ARG A 15  ? 0.2101 0.1960 0.2649 0.0157  -0.0046 0.0078  15  ARG A N   
102  C CA  . ARG A 15  ? 0.2074 0.1903 0.2651 0.0150  -0.0031 0.0070  15  ARG A CA  
103  C C   . ARG A 15  ? 0.2025 0.1831 0.2576 0.0137  -0.0035 0.0105  15  ARG A C   
104  O O   . ARG A 15  ? 0.1817 0.1594 0.2398 0.0129  -0.0024 0.0106  15  ARG A O   
105  C CB  . ARG A 15  ? 0.2594 0.2399 0.3245 0.0166  -0.0026 0.0066  15  ARG A CB  
106  C CG  . ARG A 15  ? 0.3040 0.2860 0.3714 0.0175  -0.0010 0.0019  15  ARG A CG  
107  C CD  . ARG A 15  ? 0.3864 0.3664 0.4614 0.0195  -0.0003 0.0016  15  ARG A CD  
108  N NE  . ARG A 15  ? 0.4655 0.4441 0.5432 0.0197  0.0021  -0.0033 15  ARG A NE  
109  C CZ  . ARG A 15  ? 0.5042 0.4849 0.5825 0.0207  0.0036  -0.0069 15  ARG A CZ  
110  N NH1 . ARG A 15  ? 0.5675 0.5521 0.6445 0.0214  0.0032  -0.0061 15  ARG A NH1 
111  N NH2 . ARG A 15  ? 0.5271 0.5058 0.6073 0.0207  0.0058  -0.0114 15  ARG A NH2 
112  N N   . HIS A 16  ? 0.1886 0.1705 0.2381 0.0131  -0.0048 0.0130  16  HIS A N   
113  C CA  . HIS A 16  ? 0.1984 0.1783 0.2445 0.0117  -0.0046 0.0164  16  HIS A CA  
114  C C   . HIS A 16  ? 0.2237 0.2033 0.2698 0.0101  -0.0023 0.0143  16  HIS A C   
115  O O   . HIS A 16  ? 0.1910 0.1730 0.2366 0.0098  -0.0015 0.0106  16  HIS A O   
116  C CB  . HIS A 16  ? 0.2128 0.1945 0.2518 0.0113  -0.0060 0.0183  16  HIS A CB  
117  C CG  . HIS A 16  ? 0.2543 0.2374 0.2934 0.0126  -0.0085 0.0192  16  HIS A CG  
118  N ND1 . HIS A 16  ? 0.2225 0.2039 0.2645 0.0136  -0.0106 0.0227  16  HIS A ND1 
119  C CD2 . HIS A 16  ? 0.1939 0.1800 0.2317 0.0132  -0.0093 0.0171  16  HIS A CD2 
120  C CE1 . HIS A 16  ? 0.1980 0.1818 0.2404 0.0146  -0.0127 0.0227  16  HIS A CE1 
121  N NE2 . HIS A 16  ? 0.1887 0.1753 0.2286 0.0143  -0.0117 0.0193  16  HIS A NE2 
122  N N   . GLY A 17  ? 0.2861 0.2628 0.3330 0.0089  -0.0015 0.0171  17  GLY A N   
123  C CA  . GLY A 17  ? 0.2178 0.1943 0.2656 0.0070  0.0007  0.0156  17  GLY A CA  
124  C C   . GLY A 17  ? 0.2491 0.2216 0.2998 0.0058  0.0017  0.0189  17  GLY A C   
125  O O   . GLY A 17  ? 0.2152 0.1843 0.2697 0.0067  0.0008  0.0209  17  GLY A O   
126  N N   . VAL A 18  ? 0.2179 0.1907 0.2671 0.0038  0.0036  0.0195  18  VAL A N   
127  C CA  . VAL A 18  ? 0.2454 0.2143 0.2974 0.0022  0.0049  0.0227  18  VAL A CA  
128  C C   . VAL A 18  ? 0.2827 0.2493 0.3427 0.0018  0.0054  0.0201  18  VAL A C   
129  O O   . VAL A 18  ? 0.2272 0.1892 0.2911 0.0015  0.0056  0.0227  18  VAL A O   
130  C CB  . VAL A 18  ? 0.2856 0.2560 0.3344 0.0000  0.0073  0.0240  18  VAL A CB  
131  C CG1 . VAL A 18  ? 0.3163 0.2827 0.3689 -0.0021 0.0091  0.0273  18  VAL A CG1 
132  C CG2 . VAL A 18  ? 0.2772 0.2487 0.3176 0.0003  0.0070  0.0269  18  VAL A CG2 
133  N N   . TYR A 19  ? 0.2426 0.2119 0.3049 0.0020  0.0056  0.0148  19  TYR A N   
134  C CA  . TYR A 19  ? 0.3062 0.2735 0.3751 0.0010  0.0063  0.0115  19  TYR A CA  
135  C C   . TYR A 19  ? 0.2863 0.2521 0.3584 0.0030  0.0052  0.0085  19  TYR A C   
136  O O   . TYR A 19  ? 0.2766 0.2452 0.3458 0.0047  0.0041  0.0066  19  TYR A O   
137  C CB  . TYR A 19  ? 0.3060 0.2771 0.3753 -0.0008 0.0072  0.0077  19  TYR A CB  
138  C CG  . TYR A 19  ? 0.3459 0.3183 0.4140 -0.0029 0.0090  0.0106  19  TYR A CG  
139  C CD1 . TYR A 19  ? 0.3985 0.3676 0.4711 -0.0051 0.0106  0.0127  19  TYR A CD1 
140  C CD2 . TYR A 19  ? 0.4128 0.3892 0.4752 -0.0027 0.0094  0.0112  19  TYR A CD2 
141  C CE1 . TYR A 19  ? 0.5263 0.4968 0.5979 -0.0072 0.0127  0.0154  19  TYR A CE1 
142  C CE2 . TYR A 19  ? 0.3939 0.3716 0.4553 -0.0045 0.0116  0.0137  19  TYR A CE2 
143  C CZ  . TYR A 19  ? 0.4268 0.4017 0.4928 -0.0068 0.0134  0.0158  19  TYR A CZ  
144  O OH  . TYR A 19  ? 0.5640 0.5404 0.6290 -0.0087 0.0160  0.0183  19  TYR A OH  
145  N N   . ASP A 20  ? 0.2863 0.2476 0.3646 0.0026  0.0057  0.0078  20  ASP A N   
146  C CA  . ASP A 20  ? 0.3560 0.3151 0.4381 0.0046  0.0052  0.0050  20  ASP A CA  
147  C C   . ASP A 20  ? 0.2820 0.2451 0.3619 0.0054  0.0049  -0.0004 20  ASP A C   
148  O O   . ASP A 20  ? 0.3598 0.3238 0.4390 0.0076  0.0043  -0.0014 20  ASP A O   
149  C CB  . ASP A 20  ? 0.3014 0.2550 0.3905 0.0035  0.0061  0.0036  20  ASP A CB  
150  C CG  . ASP A 20  ? 0.4475 0.3958 0.5398 0.0036  0.0062  0.0092  20  ASP A CG  
151  O OD1 . ASP A 20  ? 0.3863 0.3354 0.4752 0.0047  0.0052  0.0141  20  ASP A OD1 
152  O OD2 . ASP A 20  ? 0.4114 0.3547 0.5097 0.0025  0.0070  0.0087  20  ASP A OD2 
153  N N   . HIS A 21  ? 0.2677 0.2334 0.3465 0.0034  0.0053  -0.0036 21  HIS A N   
154  C CA  . HIS A 21  ? 0.3085 0.2774 0.3852 0.0039  0.0048  -0.0087 21  HIS A CA  
155  C C   . HIS A 21  ? 0.3778 0.3508 0.4488 0.0057  0.0040  -0.0079 21  HIS A C   
156  O O   . HIS A 21  ? 0.3168 0.2916 0.3862 0.0068  0.0038  -0.0113 21  HIS A O   
157  C CB  . HIS A 21  ? 0.2753 0.2464 0.3520 0.0014  0.0048  -0.0115 21  HIS A CB  
158  C CG  . HIS A 21  ? 0.2637 0.2396 0.3363 0.0008  0.0046  -0.0096 21  HIS A CG  
159  N ND1 . HIS A 21  ? 0.3169 0.2972 0.3847 0.0017  0.0037  -0.0113 21  HIS A ND1 
160  C CD2 . HIS A 21  ? 0.2523 0.2289 0.3248 -0.0007 0.0053  -0.0062 21  HIS A CD2 
161  C CE1 . HIS A 21  ? 0.2654 0.2488 0.3308 0.0011  0.0038  -0.0092 21  HIS A CE1 
162  N NE2 . HIS A 21  ? 0.3165 0.2980 0.3846 -0.0004 0.0050  -0.0062 21  HIS A NE2 
163  N N   . GLU A 22  ? 0.3058 0.2801 0.3737 0.0059  0.0036  -0.0034 22  GLU A N   
164  C CA  . GLU A 22  ? 0.2727 0.2504 0.3356 0.0074  0.0027  -0.0024 22  GLU A CA  
165  C C   . GLU A 22  ? 0.3096 0.2861 0.3738 0.0097  0.0021  -0.0015 22  GLU A C   
166  O O   . GLU A 22  ? 0.3050 0.2844 0.3660 0.0109  0.0013  -0.0016 22  GLU A O   
167  C CB  . GLU A 22  ? 0.2626 0.2412 0.3216 0.0068  0.0025  0.0019  22  GLU A CB  
168  C CG  . GLU A 22  ? 0.2494 0.2306 0.3066 0.0050  0.0033  0.0010  22  GLU A CG  
169  C CD  . GLU A 22  ? 0.3220 0.3044 0.3745 0.0047  0.0035  0.0047  22  GLU A CD  
170  O OE1 . GLU A 22  ? 0.3007 0.2859 0.3486 0.0056  0.0028  0.0044  22  GLU A OE1 
171  O OE2 . GLU A 22  ? 0.3536 0.3340 0.4068 0.0034  0.0046  0.0077  22  GLU A OE2 
172  N N   . ARG A 23  ? 0.2947 0.2672 0.3642 0.0103  0.0024  -0.0004 23  ARG A N   
173  C CA  . ARG A 23  ? 0.3173 0.2889 0.3892 0.0127  0.0018  0.0010  23  ARG A CA  
174  C C   . ARG A 23  ? 0.2964 0.2670 0.3726 0.0140  0.0029  -0.0034 23  ARG A C   
175  O O   . ARG A 23  ? 0.3699 0.3402 0.4495 0.0161  0.0028  -0.0026 23  ARG A O   
176  C CB  . ARG A 23  ? 0.3714 0.3391 0.4465 0.0129  0.0011  0.0061  23  ARG A CB  
177  C CG  . ARG A 23  ? 0.4960 0.4648 0.5656 0.0117  0.0001  0.0105  23  ARG A CG  
178  C CD  . ARG A 23  ? 0.4513 0.4158 0.5225 0.0109  0.0000  0.0152  23  ARG A CD  
179  N NE  . ARG A 23  ? 0.4250 0.3872 0.4993 0.0128  -0.0016 0.0190  23  ARG A NE  
180  C CZ  . ARG A 23  ? 0.3731 0.3351 0.4439 0.0129  -0.0034 0.0242  23  ARG A CZ  
181  N NH1 . ARG A 23  ? 0.2442 0.2081 0.3076 0.0113  -0.0035 0.0259  23  ARG A NH1 
182  N NH2 . ARG A 23  ? 0.3418 0.3016 0.4164 0.0147  -0.0053 0.0277  23  ARG A NH2 
183  N N   . VAL A 24  ? 0.3194 0.2898 0.3954 0.0127  0.0040  -0.0080 24  VAL A N   
184  C CA  . VAL A 24  ? 0.3393 0.3088 0.4181 0.0138  0.0054  -0.0128 24  VAL A CA  
185  C C   . VAL A 24  ? 0.3199 0.2937 0.3950 0.0151  0.0054  -0.0144 24  VAL A C   
186  O O   . VAL A 24  ? 0.3095 0.2833 0.3876 0.0171  0.0063  -0.0150 24  VAL A O   
187  C CB  . VAL A 24  ? 0.3585 0.3263 0.4373 0.0117  0.0061  -0.0174 24  VAL A CB  
188  C CG1 . VAL A 24  ? 0.2471 0.2139 0.3272 0.0127  0.0076  -0.0229 24  VAL A CG1 
189  C CG2 . VAL A 24  ? 0.3170 0.2802 0.4006 0.0103  0.0062  -0.0157 24  VAL A CG2 
190  N N   . ALA A 25  ? 0.2342 0.2117 0.3032 0.0139  0.0047  -0.0148 25  ALA A N   
191  C CA  . ALA A 25  ? 0.2758 0.2574 0.3409 0.0148  0.0047  -0.0160 25  ALA A CA  
192  C C   . ALA A 25  ? 0.2946 0.2792 0.3559 0.0149  0.0031  -0.0121 25  ALA A C   
193  O O   . ALA A 25  ? 0.2638 0.2511 0.3235 0.0159  0.0030  -0.0119 25  ALA A O   
194  C CB  . ALA A 25  ? 0.2567 0.2399 0.3174 0.0135  0.0050  -0.0204 25  ALA A CB  
195  N N   . GLY A 26  ? 0.2684 0.2525 0.3283 0.0137  0.0020  -0.0091 26  GLY A N   
196  C CA  . GLY A 26  ? 0.2119 0.1983 0.2678 0.0138  0.0007  -0.0057 26  GLY A CA  
197  C C   . GLY A 26  ? 0.2391 0.2288 0.2896 0.0130  0.0004  -0.0074 26  GLY A C   
198  O O   . GLY A 26  ? 0.1664 0.1568 0.2161 0.0123  0.0009  -0.0107 26  GLY A O   
199  N N   . GLN A 27  ? 0.1850 0.1767 0.2318 0.0132  -0.0008 -0.0051 27  GLN A N   
200  C CA  . GLN A 27  ? 0.1863 0.1805 0.2282 0.0125  -0.0011 -0.0061 27  GLN A CA  
201  C C   . GLN A 27  ? 0.2077 0.2035 0.2464 0.0131  -0.0023 -0.0039 27  GLN A C   
202  O O   . GLN A 27  ? 0.1811 0.1762 0.2214 0.0138  -0.0030 -0.0016 27  GLN A O   
203  C CB  . GLN A 27  ? 0.1753 0.1693 0.2162 0.0112  -0.0010 -0.0057 27  GLN A CB  
204  C CG  . GLN A 27  ? 0.1822 0.1749 0.2220 0.0109  -0.0013 -0.0019 27  GLN A CG  
205  C CD  . GLN A 27  ? 0.2476 0.2397 0.2878 0.0094  -0.0004 -0.0014 27  GLN A CD  
206  O OE1 . GLN A 27  ? 0.2114 0.2056 0.2491 0.0088  -0.0002 -0.0020 27  GLN A OE1 
207  N NE2 . GLN A 27  ? 0.2251 0.2144 0.2691 0.0089  0.0002  -0.0002 27  GLN A NE2 
208  N N   . ARG A 28  ? 0.1948 0.1925 0.2294 0.0127  -0.0027 -0.0047 28  ARG A N   
209  C CA  . ARG A 28  ? 0.2113 0.2101 0.2425 0.0130  -0.0038 -0.0031 28  ARG A CA  
210  C C   . ARG A 28  ? 0.2457 0.2435 0.2744 0.0125  -0.0045 -0.0005 28  ARG A C   
211  O O   . ARG A 28  ? 0.1859 0.1834 0.2132 0.0118  -0.0039 -0.0005 28  ARG A O   
212  C CB  . ARG A 28  ? 0.2403 0.2410 0.2682 0.0129  -0.0039 -0.0049 28  ARG A CB  
213  C CG  . ARG A 28  ? 0.3390 0.3404 0.3634 0.0130  -0.0050 -0.0036 28  ARG A CG  
214  C CD  . ARG A 28  ? 0.3536 0.3565 0.3758 0.0131  -0.0049 -0.0053 28  ARG A CD  
215  N NE  . ARG A 28  ? 0.4490 0.4525 0.4735 0.0134  -0.0039 -0.0070 28  ARG A NE  
216  C CZ  . ARG A 28  ? 0.3878 0.3922 0.4111 0.0132  -0.0034 -0.0092 28  ARG A CZ  
217  N NH1 . ARG A 28  ? 0.4329 0.4379 0.4535 0.0129  -0.0041 -0.0098 28  ARG A NH1 
218  N NH2 . ARG A 28  ? 0.3056 0.3102 0.3303 0.0135  -0.0022 -0.0108 28  ARG A NH2 
219  N N   . PHE A 29  ? 0.1755 0.1731 0.2034 0.0128  -0.0059 0.0018  29  PHE A N   
220  C CA  . PHE A 29  ? 0.1804 0.1770 0.2044 0.0123  -0.0068 0.0041  29  PHE A CA  
221  C C   . PHE A 29  ? 0.1956 0.1932 0.2160 0.0123  -0.0081 0.0040  29  PHE A C   
222  O O   . PHE A 29  ? 0.2025 0.2014 0.2247 0.0127  -0.0086 0.0034  29  PHE A O   
223  C CB  . PHE A 29  ? 0.1809 0.1757 0.2067 0.0124  -0.0078 0.0070  29  PHE A CB  
224  C CG  . PHE A 29  ? 0.1695 0.1626 0.1985 0.0122  -0.0065 0.0074  29  PHE A CG  
225  C CD1 . PHE A 29  ? 0.1603 0.1531 0.1949 0.0129  -0.0058 0.0061  29  PHE A CD1 
226  C CD2 . PHE A 29  ? 0.1600 0.1516 0.1865 0.0112  -0.0058 0.0089  29  PHE A CD2 
227  C CE1 . PHE A 29  ? 0.1709 0.1616 0.2088 0.0125  -0.0046 0.0063  29  PHE A CE1 
228  C CE2 . PHE A 29  ? 0.1875 0.1773 0.2173 0.0108  -0.0045 0.0094  29  PHE A CE2 
229  C CZ  . PHE A 29  ? 0.1959 0.1852 0.2316 0.0114  -0.0040 0.0081  29  PHE A CZ  
230  N N   . VAL A 30  ? 0.1395 0.1364 0.1550 0.0117  -0.0083 0.0046  30  VAL A N   
231  C CA  . VAL A 30  ? 0.1839 0.1810 0.1958 0.0115  -0.0096 0.0043  30  VAL A CA  
232  C C   . VAL A 30  ? 0.1835 0.1788 0.1908 0.0109  -0.0108 0.0063  30  VAL A C   
233  O O   . VAL A 30  ? 0.2026 0.1967 0.2074 0.0105  -0.0097 0.0069  30  VAL A O   
234  C CB  . VAL A 30  ? 0.2025 0.2002 0.2122 0.0116  -0.0084 0.0021  30  VAL A CB  
235  C CG1 . VAL A 30  ? 0.1897 0.1868 0.1956 0.0114  -0.0097 0.0019  30  VAL A CG1 
236  C CG2 . VAL A 30  ? 0.1960 0.1954 0.2092 0.0121  -0.0076 0.0003  30  VAL A CG2 
237  N N   . ILE A 31  ? 0.2055 0.2008 0.2120 0.0106  -0.0132 0.0074  31  ILE A N   
238  C CA  . ILE A 31  ? 0.1789 0.1725 0.1807 0.0098  -0.0151 0.0094  31  ILE A CA  
239  C C   . ILE A 31  ? 0.1688 0.1617 0.1658 0.0091  -0.0162 0.0082  31  ILE A C   
240  O O   . ILE A 31  ? 0.1496 0.1436 0.1487 0.0092  -0.0170 0.0072  31  ILE A O   
241  C CB  . ILE A 31  ? 0.1796 0.1736 0.1846 0.0098  -0.0177 0.0120  31  ILE A CB  
242  C CG1 . ILE A 31  ? 0.2776 0.2718 0.2883 0.0107  -0.0167 0.0133  31  ILE A CG1 
243  C CG2 . ILE A 31  ? 0.2084 0.2007 0.2076 0.0088  -0.0203 0.0141  31  ILE A CG2 
244  C CD1 . ILE A 31  ? 0.2606 0.2535 0.2704 0.0106  -0.0141 0.0130  31  ILE A CD1 
245  N N   . ASP A 32  ? 0.1790 0.1698 0.1695 0.0085  -0.0161 0.0083  32  ASP A N   
246  C CA  . ASP A 32  ? 0.1880 0.1773 0.1731 0.0076  -0.0176 0.0073  32  ASP A CA  
247  C C   . ASP A 32  ? 0.1932 0.1810 0.1739 0.0066  -0.0203 0.0096  32  ASP A C   
248  O O   . ASP A 32  ? 0.2366 0.2236 0.2156 0.0065  -0.0197 0.0115  32  ASP A O   
249  C CB  . ASP A 32  ? 0.1874 0.1750 0.1675 0.0077  -0.0152 0.0051  32  ASP A CB  
250  C CG  . ASP A 32  ? 0.2337 0.2227 0.2178 0.0088  -0.0128 0.0032  32  ASP A CG  
251  O OD1 . ASP A 32  ? 0.2146 0.2053 0.2034 0.0092  -0.0134 0.0028  32  ASP A OD1 
252  O OD2 . ASP A 32  ? 0.2534 0.2420 0.2358 0.0092  -0.0102 0.0021  32  ASP A OD2 
253  N N   . VAL A 33  ? 0.2209 0.2082 0.1997 0.0056  -0.0234 0.0095  33  VAL A N   
254  C CA  . VAL A 33  ? 0.2089 0.1946 0.1823 0.0043  -0.0266 0.0114  33  VAL A CA  
255  C C   . VAL A 33  ? 0.2600 0.2434 0.2268 0.0031  -0.0278 0.0092  33  VAL A C   
256  O O   . VAL A 33  ? 0.2240 0.2079 0.1935 0.0029  -0.0284 0.0074  33  VAL A O   
257  C CB  . VAL A 33  ? 0.2480 0.2359 0.2270 0.0042  -0.0303 0.0141  33  VAL A CB  
258  C CG1 . VAL A 33  ? 0.2302 0.2164 0.2029 0.0029  -0.0340 0.0164  33  VAL A CG1 
259  C CG2 . VAL A 33  ? 0.2295 0.2194 0.2160 0.0056  -0.0288 0.0158  33  VAL A CG2 
260  N N   . THR A 34  ? 0.2435 0.2241 0.2015 0.0022  -0.0279 0.0092  34  THR A N   
261  C CA  . THR A 34  ? 0.2269 0.2045 0.1772 0.0008  -0.0294 0.0069  34  THR A CA  
262  C C   . THR A 34  ? 0.2381 0.2145 0.1824 -0.0008 -0.0335 0.0091  34  THR A C   
263  O O   . THR A 34  ? 0.2362 0.2120 0.1766 -0.0008 -0.0329 0.0115  34  THR A O   
264  C CB  . THR A 34  ? 0.2448 0.2198 0.1890 0.0013  -0.0252 0.0041  34  THR A CB  
265  O OG1 . THR A 34  ? 0.2248 0.2013 0.1752 0.0028  -0.0220 0.0024  34  THR A OG1 
266  C CG2 . THR A 34  ? 0.2490 0.2204 0.1854 -0.0001 -0.0266 0.0013  34  THR A CG2 
267  N N   . VAL A 35  ? 0.2033 0.1793 0.1468 -0.0022 -0.0376 0.0085  35  VAL A N   
268  C CA  . VAL A 35  ? 0.2097 0.1851 0.1485 -0.0039 -0.0426 0.0107  35  VAL A CA  
269  C C   . VAL A 35  ? 0.3125 0.2840 0.2416 -0.0058 -0.0441 0.0075  35  VAL A C   
270  O O   . VAL A 35  ? 0.2721 0.2431 0.2034 -0.0063 -0.0446 0.0047  35  VAL A O   
271  C CB  . VAL A 35  ? 0.2805 0.2596 0.2285 -0.0042 -0.0470 0.0130  35  VAL A CB  
272  C CG1 . VAL A 35  ? 0.2780 0.2569 0.2217 -0.0057 -0.0527 0.0158  35  VAL A CG1 
273  C CG2 . VAL A 35  ? 0.2217 0.2043 0.1799 -0.0021 -0.0449 0.0153  35  VAL A CG2 
274  N N   . TRP A 36  ? 0.2909 0.2596 0.2092 -0.0069 -0.0448 0.0080  36  TRP A N   
275  C CA  . TRP A 36  ? 0.2916 0.2561 0.1994 -0.0089 -0.0466 0.0049  36  TRP A CA  
276  C C   . TRP A 36  ? 0.3258 0.2908 0.2315 -0.0110 -0.0536 0.0068  36  TRP A C   
277  O O   . TRP A 36  ? 0.2919 0.2580 0.1958 -0.0113 -0.0563 0.0109  36  TRP A O   
278  C CB  . TRP A 36  ? 0.3142 0.2751 0.2103 -0.0089 -0.0428 0.0036  36  TRP A CB  
279  C CG  . TRP A 36  ? 0.3630 0.3229 0.2603 -0.0071 -0.0363 0.0004  36  TRP A CG  
280  C CD1 . TRP A 36  ? 0.3640 0.3205 0.2571 -0.0072 -0.0340 -0.0044 36  TRP A CD1 
281  C CD2 . TRP A 36  ? 0.3416 0.3040 0.2453 -0.0050 -0.0315 0.0018  36  TRP A CD2 
282  N NE1 . TRP A 36  ? 0.3525 0.3096 0.2493 -0.0051 -0.0282 -0.0058 36  TRP A NE1 
283  C CE2 . TRP A 36  ? 0.3004 0.2612 0.2037 -0.0039 -0.0267 -0.0021 36  TRP A CE2 
284  C CE3 . TRP A 36  ? 0.2877 0.2534 0.1977 -0.0040 -0.0309 0.0058  36  TRP A CE3 
285  C CZ2 . TRP A 36  ? 0.3268 0.2896 0.2357 -0.0018 -0.0216 -0.0020 36  TRP A CZ2 
286  C CZ3 . TRP A 36  ? 0.2867 0.2539 0.2019 -0.0021 -0.0258 0.0057  36  TRP A CZ3 
287  C CH2 . TRP A 36  ? 0.3111 0.2771 0.2257 -0.0012 -0.0213 0.0018  36  TRP A CH2 
288  N N   . ILE A 37  ? 0.2762 0.2404 0.1828 -0.0126 -0.0568 0.0042  37  ILE A N   
289  C CA  . ILE A 37  ? 0.3597 0.3254 0.2674 -0.0148 -0.0640 0.0059  37  ILE A CA  
290  C C   . ILE A 37  ? 0.3221 0.2847 0.2264 -0.0170 -0.0662 0.0015  37  ILE A C   
291  O O   . ILE A 37  ? 0.3406 0.3019 0.2481 -0.0163 -0.0626 -0.0018 37  ILE A O   
292  C CB  . ILE A 37  ? 0.3044 0.2760 0.2266 -0.0137 -0.0659 0.0095  37  ILE A CB  
293  C CG1 . ILE A 37  ? 0.3108 0.2845 0.2356 -0.0159 -0.0734 0.0113  37  ILE A CG1 
294  C CG2 . ILE A 37  ? 0.3416 0.3147 0.2736 -0.0124 -0.0621 0.0074  37  ILE A CG2 
295  C CD1 . ILE A 37  ? 0.2674 0.2471 0.2068 -0.0148 -0.0753 0.0147  37  ILE A CD1 
296  N N   . ASP A 38  ? 0.3362 0.2975 0.2340 -0.0197 -0.0722 0.0015  38  ASP A N   
297  C CA  . ASP A 38  ? 0.3537 0.3119 0.2485 -0.0222 -0.0750 -0.0028 38  ASP A CA  
298  C C   . ASP A 38  ? 0.3314 0.2936 0.2404 -0.0226 -0.0773 -0.0022 38  ASP A C   
299  O O   . ASP A 38  ? 0.3625 0.3296 0.2792 -0.0230 -0.0817 0.0016  38  ASP A O   
300  C CB  . ASP A 38  ? 0.4265 0.3824 0.3103 -0.0252 -0.0813 -0.0028 38  ASP A CB  
301  C CG  . ASP A 38  ? 0.5787 0.5292 0.4549 -0.0278 -0.0829 -0.0084 38  ASP A CG  
302  O OD1 . ASP A 38  ? 0.6064 0.5566 0.4902 -0.0282 -0.0822 -0.0111 38  ASP A OD1 
303  O OD2 . ASP A 38  ? 0.6270 0.5733 0.4891 -0.0297 -0.0851 -0.0101 38  ASP A OD2 
304  N N   . LEU A 39  ? 0.3397 0.2999 0.2521 -0.0226 -0.0743 -0.0059 39  LEU A N   
305  C CA  . LEU A 39  ? 0.3661 0.3299 0.2917 -0.0231 -0.0756 -0.0053 39  LEU A CA  
306  C C   . LEU A 39  ? 0.3638 0.3250 0.2885 -0.0265 -0.0802 -0.0084 39  LEU A C   
307  O O   . LEU A 39  ? 0.3129 0.2764 0.2481 -0.0273 -0.0809 -0.0083 39  LEU A O   
308  C CB  . LEU A 39  ? 0.2823 0.2461 0.2141 -0.0205 -0.0691 -0.0064 39  LEU A CB  
309  C CG  . LEU A 39  ? 0.3419 0.3090 0.2768 -0.0174 -0.0650 -0.0032 39  LEU A CG  
310  C CD1 . LEU A 39  ? 0.3345 0.3016 0.2749 -0.0150 -0.0590 -0.0044 39  LEU A CD1 
311  C CD2 . LEU A 39  ? 0.3249 0.2980 0.2689 -0.0172 -0.0684 0.0014  39  LEU A CD2 
312  N N   . ALA A 40  ? 0.2924 0.2488 0.2048 -0.0287 -0.0832 -0.0112 40  ALA A N   
313  C CA  . ALA A 40  ? 0.3947 0.3479 0.3059 -0.0322 -0.0875 -0.0146 40  ALA A CA  
314  C C   . ALA A 40  ? 0.4274 0.3862 0.3486 -0.0345 -0.0942 -0.0116 40  ALA A C   
315  O O   . ALA A 40  ? 0.3567 0.3159 0.2857 -0.0365 -0.0959 -0.0130 40  ALA A O   
316  C CB  . ALA A 40  ? 0.3633 0.3101 0.2582 -0.0342 -0.0896 -0.0184 40  ALA A CB  
317  N N   . GLU A 41  ? 0.3632 0.3266 0.2853 -0.0342 -0.0979 -0.0073 41  GLU A N   
318  C CA  . GLU A 41  ? 0.3433 0.3123 0.2751 -0.0363 -0.1047 -0.0044 41  GLU A CA  
319  C C   . GLU A 41  ? 0.3496 0.3240 0.2982 -0.0353 -0.1023 -0.0026 41  GLU A C   
320  O O   . GLU A 41  ? 0.3737 0.3507 0.3310 -0.0379 -0.1062 -0.0027 41  GLU A O   
321  C CB  . GLU A 41  ? 0.4130 0.3859 0.3433 -0.0355 -0.1086 0.0004  41  GLU A CB  
322  C CG  . GLU A 41  ? 0.3745 0.3533 0.3142 -0.0378 -0.1165 0.0034  41  GLU A CG  
323  C CD  . GLU A 41  ? 0.5700 0.5503 0.5033 -0.0380 -0.1223 0.0071  41  GLU A CD  
324  O OE1 . GLU A 41  ? 0.6467 0.6252 0.5721 -0.0356 -0.1190 0.0088  41  GLU A OE1 
325  O OE2 . GLU A 41  ? 0.6122 0.5956 0.5486 -0.0407 -0.1301 0.0085  41  GLU A OE2 
326  N N   . ALA A 42  ? 0.3395 0.3155 0.2926 -0.0317 -0.0958 -0.0011 42  ALA A N   
327  C CA  . ALA A 42  ? 0.2711 0.2521 0.2389 -0.0305 -0.0929 0.0006  42  ALA A CA  
328  C C   . ALA A 42  ? 0.3092 0.2870 0.2796 -0.0321 -0.0909 -0.0028 42  ALA A C   
329  O O   . ALA A 42  ? 0.2966 0.2785 0.2791 -0.0330 -0.0911 -0.0016 42  ALA A O   
330  C CB  . ALA A 42  ? 0.2780 0.2606 0.2479 -0.0264 -0.0866 0.0026  42  ALA A CB  
331  N N   . ALA A 43  ? 0.3483 0.3188 0.3080 -0.0325 -0.0887 -0.0071 43  ALA A N   
332  C CA  . ALA A 43  ? 0.2914 0.2581 0.2535 -0.0343 -0.0874 -0.0103 43  ALA A CA  
333  C C   . ALA A 43  ? 0.3565 0.3232 0.3209 -0.0387 -0.0942 -0.0115 43  ALA A C   
334  O O   . ALA A 43  ? 0.3878 0.3546 0.3602 -0.0406 -0.0942 -0.0122 43  ALA A O   
335  C CB  . ALA A 43  ? 0.3656 0.3245 0.3164 -0.0333 -0.0832 -0.0146 43  ALA A CB  
336  N N   . ASN A 44  ? 0.3852 0.3519 0.3429 -0.0405 -0.1000 -0.0115 44  ASN A N   
337  C CA  . ASN A 44  ? 0.3925 0.3599 0.3529 -0.0449 -0.1073 -0.0123 44  ASN A CA  
338  C C   . ASN A 44  ? 0.4024 0.3786 0.3792 -0.0456 -0.1100 -0.0080 44  ASN A C   
339  O O   . ASN A 44  ? 0.3909 0.3683 0.3760 -0.0487 -0.1127 -0.0086 44  ASN A O   
340  C CB  . ASN A 44  ? 0.4600 0.4253 0.4082 -0.0466 -0.1132 -0.0131 44  ASN A CB  
341  C CG  . ASN A 44  ? 0.5867 0.5507 0.5347 -0.0516 -0.1207 -0.0154 44  ASN A CG  
342  O OD1 . ASN A 44  ? 0.5105 0.4702 0.4597 -0.0538 -0.1201 -0.0191 44  ASN A OD1 
343  N ND2 . ASN A 44  ? 0.5881 0.5560 0.5353 -0.0534 -0.1280 -0.0131 44  ASN A ND2 
344  N N   . SER A 45  ? 0.3739 0.3563 0.3557 -0.0428 -0.1094 -0.0036 45  SER A N   
345  C CA  . SER A 45  ? 0.3069 0.2979 0.3041 -0.0431 -0.1120 0.0005  45  SER A CA  
346  C C   . SER A 45  ? 0.2820 0.2763 0.2911 -0.0411 -0.1057 0.0019  45  SER A C   
347  O O   . SER A 45  ? 0.3223 0.3229 0.3452 -0.0423 -0.1071 0.0041  45  SER A O   
348  C CB  . SER A 45  ? 0.3904 0.3863 0.3882 -0.0409 -0.1145 0.0048  45  SER A CB  
349  O OG  . SER A 45  ? 0.2972 0.2921 0.2916 -0.0367 -0.1080 0.0058  45  SER A OG  
350  N N   . ASP A 46  ? 0.2885 0.2791 0.2926 -0.0383 -0.0988 0.0006  46  ASP A N   
351  C CA  . ASP A 46  ? 0.2718 0.2654 0.2852 -0.0358 -0.0925 0.0023  46  ASP A CA  
352  C C   . ASP A 46  ? 0.3124 0.3144 0.3368 -0.0338 -0.0927 0.0067  46  ASP A C   
353  O O   . ASP A 46  ? 0.3120 0.3187 0.3479 -0.0331 -0.0896 0.0084  46  ASP A O   
354  C CB  . ASP A 46  ? 0.2462 0.2389 0.2664 -0.0383 -0.0913 0.0008  46  ASP A CB  
355  C CG  . ASP A 46  ? 0.2747 0.2673 0.2988 -0.0358 -0.0838 0.0013  46  ASP A CG  
356  O OD1 . ASP A 46  ? 0.2271 0.2170 0.2441 -0.0326 -0.0796 0.0008  46  ASP A OD1 
357  O OD2 . ASP A 46  ? 0.3262 0.3211 0.3599 -0.0372 -0.0823 0.0021  46  ASP A OD2 
358  N N   . ASP A 47  ? 0.2822 0.2856 0.3026 -0.0328 -0.0963 0.0086  47  ASP A N   
359  C CA  . ASP A 47  ? 0.3481 0.3589 0.3783 -0.0309 -0.0976 0.0128  47  ASP A CA  
360  C C   . ASP A 47  ? 0.2645 0.2742 0.2896 -0.0268 -0.0930 0.0141  47  ASP A C   
361  O O   . ASP A 47  ? 0.2888 0.2940 0.3017 -0.0263 -0.0940 0.0134  47  ASP A O   
362  C CB  . ASP A 47  ? 0.3040 0.3173 0.3344 -0.0330 -0.1060 0.0145  47  ASP A CB  
363  C CG  . ASP A 47  ? 0.4490 0.4709 0.4939 -0.0318 -0.1083 0.0189  47  ASP A CG  
364  O OD1 . ASP A 47  ? 0.4767 0.5013 0.5262 -0.0282 -0.1040 0.0212  47  ASP A OD1 
365  O OD2 . ASP A 47  ? 0.5483 0.5744 0.6007 -0.0346 -0.1144 0.0199  47  ASP A OD2 
366  N N   . LEU A 48  ? 0.2503 0.2641 0.2847 -0.0241 -0.0881 0.0159  48  LEU A N   
367  C CA  . LEU A 48  ? 0.2823 0.2955 0.3136 -0.0204 -0.0837 0.0171  48  LEU A CA  
368  C C   . LEU A 48  ? 0.3019 0.3154 0.3287 -0.0195 -0.0880 0.0196  48  LEU A C   
369  O O   . LEU A 48  ? 0.2700 0.2800 0.2880 -0.0175 -0.0855 0.0197  48  LEU A O   
370  C CB  . LEU A 48  ? 0.3399 0.3585 0.3838 -0.0181 -0.0793 0.0189  48  LEU A CB  
371  C CG  . LEU A 48  ? 0.2548 0.2737 0.2982 -0.0143 -0.0751 0.0203  48  LEU A CG  
372  C CD1 . LEU A 48  ? 0.2058 0.2188 0.2384 -0.0132 -0.0701 0.0176  48  LEU A CD1 
373  C CD2 . LEU A 48  ? 0.2992 0.3240 0.3559 -0.0125 -0.0715 0.0218  48  LEU A CD2 
374  N N   . ALA A 49  ? 0.2555 0.2731 0.2882 -0.0210 -0.0944 0.0220  49  ALA A N   
375  C CA  . ALA A 49  ? 0.3015 0.3193 0.3297 -0.0203 -0.0991 0.0250  49  ALA A CA  
376  C C   . ALA A 49  ? 0.3744 0.3851 0.3852 -0.0216 -0.1006 0.0230  49  ALA A C   
377  O O   . ALA A 49  ? 0.3251 0.3344 0.3293 -0.0203 -0.1021 0.0253  49  ALA A O   
378  C CB  . ALA A 49  ? 0.3121 0.3356 0.3496 -0.0221 -0.1065 0.0277  49  ALA A CB  
379  N N   . ASP A 50  ? 0.3269 0.3328 0.3300 -0.0239 -0.0998 0.0188  50  ASP A N   
380  C CA  . ASP A 50  ? 0.2671 0.2662 0.2537 -0.0251 -0.1007 0.0163  50  ASP A CA  
381  C C   . ASP A 50  ? 0.2738 0.2682 0.2522 -0.0228 -0.0935 0.0144  50  ASP A C   
382  O O   . ASP A 50  ? 0.2940 0.2827 0.2589 -0.0235 -0.0930 0.0121  50  ASP A O   
383  C CB  . ASP A 50  ? 0.2987 0.2947 0.2811 -0.0290 -0.1042 0.0125  50  ASP A CB  
384  C CG  . ASP A 50  ? 0.3244 0.3241 0.3111 -0.0319 -0.1129 0.0143  50  ASP A CG  
385  O OD1 . ASP A 50  ? 0.3147 0.3168 0.3004 -0.0312 -0.1169 0.0180  50  ASP A OD1 
386  O OD2 . ASP A 50  ? 0.3379 0.3383 0.3293 -0.0350 -0.1157 0.0123  50  ASP A OD2 
387  N N   . THR A 51  ? 0.2613 0.2580 0.2476 -0.0200 -0.0878 0.0152  51  THR A N   
388  C CA  . THR A 51  ? 0.2684 0.2614 0.2480 -0.0176 -0.0814 0.0139  51  THR A CA  
389  C C   . THR A 51  ? 0.2880 0.2845 0.2737 -0.0145 -0.0789 0.0174  51  THR A C   
390  O O   . THR A 51  ? 0.2426 0.2438 0.2370 -0.0140 -0.0821 0.0208  51  THR A O   
391  C CB  . THR A 51  ? 0.2681 0.2592 0.2494 -0.0175 -0.0764 0.0104  51  THR A CB  
392  O OG1 . THR A 51  ? 0.2469 0.2340 0.2204 -0.0155 -0.0710 0.0088  51  THR A OG1 
393  C CG2 . THR A 51  ? 0.2526 0.2489 0.2479 -0.0164 -0.0741 0.0118  51  THR A CG2 
394  N N   . TYR A 52  ? 0.2809 0.2747 0.2620 -0.0124 -0.0732 0.0165  52  TYR A N   
395  C CA  . TYR A 52  ? 0.2970 0.2931 0.2831 -0.0095 -0.0700 0.0191  52  TYR A CA  
396  C C   . TYR A 52  ? 0.2648 0.2636 0.2608 -0.0080 -0.0654 0.0181  52  TYR A C   
397  O O   . TYR A 52  ? 0.2332 0.2295 0.2262 -0.0078 -0.0612 0.0152  52  TYR A O   
398  C CB  . TYR A 52  ? 0.2685 0.2602 0.2440 -0.0084 -0.0665 0.0187  52  TYR A CB  
399  C CG  . TYR A 52  ? 0.2663 0.2595 0.2453 -0.0060 -0.0647 0.0220  52  TYR A CG  
400  C CD1 . TYR A 52  ? 0.3382 0.3325 0.3172 -0.0060 -0.0690 0.0259  52  TYR A CD1 
401  C CD2 . TYR A 52  ? 0.3105 0.3039 0.2927 -0.0039 -0.0589 0.0211  52  TYR A CD2 
402  C CE1 . TYR A 52  ? 0.3186 0.3138 0.3010 -0.0038 -0.0673 0.0291  52  TYR A CE1 
403  C CE2 . TYR A 52  ? 0.3177 0.3120 0.3032 -0.0019 -0.0572 0.0239  52  TYR A CE2 
404  C CZ  . TYR A 52  ? 0.3042 0.2992 0.2900 -0.0018 -0.0613 0.0279  52  TYR A CZ  
405  O OH  . TYR A 52  ? 0.2996 0.2950 0.2891 0.0002  -0.0595 0.0306  52  TYR A OH  
406  N N   . ASP A 53  ? 0.2054 0.2094 0.2132 -0.0070 -0.0661 0.0206  53  ASP A N   
407  C CA  . ASP A 53  ? 0.2035 0.2107 0.2212 -0.0059 -0.0623 0.0198  53  ASP A CA  
408  C C   . ASP A 53  ? 0.2148 0.2205 0.2311 -0.0035 -0.0563 0.0189  53  ASP A C   
409  O O   . ASP A 53  ? 0.2384 0.2448 0.2564 -0.0016 -0.0553 0.0209  53  ASP A O   
410  C CB  . ASP A 53  ? 0.2091 0.2222 0.2393 -0.0053 -0.0647 0.0228  53  ASP A CB  
411  C CG  . ASP A 53  ? 0.2893 0.3062 0.3299 -0.0046 -0.0610 0.0221  53  ASP A CG  
412  O OD1 . ASP A 53  ? 0.2204 0.2353 0.2584 -0.0046 -0.0567 0.0195  53  ASP A OD1 
413  O OD2 . ASP A 53  ? 0.3234 0.3455 0.3751 -0.0040 -0.0624 0.0242  53  ASP A OD2 
414  N N   . TYR A 54  ? 0.2309 0.2346 0.2447 -0.0036 -0.0525 0.0160  54  TYR A N   
415  C CA  A TYR A 54  ? 0.2173 0.2199 0.2301 -0.0015 -0.0471 0.0150  54  TYR A CA  
416  C CA  B TYR A 54  ? 0.2224 0.2251 0.2352 -0.0014 -0.0473 0.0152  54  TYR A CA  
417  C C   . TYR A 54  ? 0.2545 0.2613 0.2775 0.0004  -0.0446 0.0162  54  TYR A C   
418  O O   . TYR A 54  ? 0.2370 0.2432 0.2597 0.0022  -0.0409 0.0158  54  TYR A O   
419  C CB  A TYR A 54  ? 0.2594 0.2590 0.2675 -0.0021 -0.0444 0.0119  54  TYR A CB  
420  C CB  B TYR A 54  ? 0.2586 0.2578 0.2657 -0.0019 -0.0443 0.0120  54  TYR A CB  
421  C CG  A TYR A 54  ? 0.2447 0.2462 0.2590 -0.0030 -0.0436 0.0110  54  TYR A CG  
422  C CG  B TYR A 54  ? 0.2514 0.2515 0.2624 -0.0033 -0.0442 0.0107  54  TYR A CG  
423  C CD1 A TYR A 54  ? 0.2587 0.2640 0.2814 -0.0018 -0.0409 0.0118  54  TYR A CD1 
424  C CD1 B TYR A 54  ? 0.2603 0.2642 0.2802 -0.0027 -0.0423 0.0113  54  TYR A CD1 
425  C CD2 A TYR A 54  ? 0.2407 0.2397 0.2518 -0.0052 -0.0453 0.0093  54  TYR A CD2 
426  C CD2 B TYR A 54  ? 0.2548 0.2512 0.2598 -0.0052 -0.0457 0.0086  54  TYR A CD2 
427  C CE1 A TYR A 54  ? 0.2614 0.2684 0.2892 -0.0028 -0.0399 0.0112  54  TYR A CE1 
428  C CE1 B TYR A 54  ? 0.2504 0.2547 0.2734 -0.0043 -0.0421 0.0104  54  TYR A CE1 
429  C CE2 A TYR A 54  ? 0.2408 0.2413 0.2576 -0.0063 -0.0445 0.0089  54  TYR A CE2 
430  C CE2 B TYR A 54  ? 0.2328 0.2292 0.2412 -0.0066 -0.0456 0.0076  54  TYR A CE2 
431  C CZ  A TYR A 54  ? 0.2617 0.2662 0.2866 -0.0051 -0.0417 0.0100  54  TYR A CZ  
432  C CZ  B TYR A 54  ? 0.2400 0.2405 0.2574 -0.0062 -0.0438 0.0087  54  TYR A CZ  
433  O OH  A TYR A 54  ? 0.2437 0.2497 0.2739 -0.0063 -0.0406 0.0098  54  TYR A OH  
434  O OH  B TYR A 54  ? 0.1956 0.1958 0.2158 -0.0080 -0.0436 0.0079  54  TYR A OH  
435  N N   . VAL A 55  ? 0.2224 0.2333 0.2543 -0.0002 -0.0463 0.0174  55  VAL A N   
436  C CA  . VAL A 55  ? 0.2544 0.2694 0.2961 0.0017  -0.0435 0.0182  55  VAL A CA  
437  C C   . VAL A 55  ? 0.3116 0.3272 0.3557 0.0036  -0.0444 0.0206  55  VAL A C   
438  O O   . VAL A 55  ? 0.2126 0.2283 0.2590 0.0056  -0.0409 0.0204  55  VAL A O   
439  C CB  . VAL A 55  ? 0.2601 0.2796 0.3113 0.0006  -0.0449 0.0189  55  VAL A CB  
440  C CG1 . VAL A 55  ? 0.3016 0.3255 0.3632 0.0026  -0.0421 0.0198  55  VAL A CG1 
441  C CG2 . VAL A 55  ? 0.2842 0.3026 0.3333 -0.0011 -0.0431 0.0167  55  VAL A CG2 
442  N N   . ARG A 56  ? 0.2528 0.2685 0.2959 0.0028  -0.0493 0.0229  56  ARG A N   
443  C CA  . ARG A 56  ? 0.2917 0.3075 0.3368 0.0045  -0.0507 0.0257  56  ARG A CA  
444  C C   . ARG A 56  ? 0.3026 0.3139 0.3388 0.0053  -0.0481 0.0251  56  ARG A C   
445  O O   . ARG A 56  ? 0.2591 0.2702 0.2983 0.0072  -0.0462 0.0262  56  ARG A O   
446  C CB  . ARG A 56  ? 0.3220 0.3388 0.3672 0.0033  -0.0571 0.0286  56  ARG A CB  
447  C CG  . ARG A 56  ? 0.4268 0.4493 0.4840 0.0030  -0.0597 0.0298  56  ARG A CG  
448  C CD  . ARG A 56  ? 0.4966 0.5220 0.5606 0.0039  -0.0645 0.0338  56  ARG A CD  
449  N NE  . ARG A 56  ? 0.5923 0.6144 0.6469 0.0028  -0.0694 0.0359  56  ARG A NE  
450  C CZ  . ARG A 56  ? 0.6466 0.6708 0.7042 0.0024  -0.0756 0.0393  56  ARG A CZ  
451  N NH1 . ARG A 56  ? 0.6704 0.7004 0.7413 0.0030  -0.0779 0.0411  56  ARG A NH1 
452  N NH2 . ARG A 56  ? 0.6864 0.7070 0.7335 0.0013  -0.0795 0.0410  56  ARG A NH2 
453  N N   . LEU A 57  ? 0.2760 0.2836 0.3019 0.0039  -0.0479 0.0233  57  LEU A N   
454  C CA  . LEU A 57  ? 0.2328 0.2365 0.2507 0.0045  -0.0452 0.0226  57  LEU A CA  
455  C C   . LEU A 57  ? 0.2600 0.2642 0.2818 0.0062  -0.0400 0.0210  57  LEU A C   
456  O O   . LEU A 57  ? 0.2148 0.2177 0.2364 0.0075  -0.0381 0.0219  57  LEU A O   
457  C CB  . LEU A 57  ? 0.2540 0.2543 0.2615 0.0027  -0.0452 0.0203  57  LEU A CB  
458  C CG  . LEU A 57  ? 0.2527 0.2492 0.2521 0.0032  -0.0416 0.0190  57  LEU A CG  
459  C CD1 . LEU A 57  ? 0.2599 0.2547 0.2553 0.0035  -0.0427 0.0219  57  LEU A CD1 
460  C CD2 . LEU A 57  ? 0.2631 0.2566 0.2539 0.0018  -0.0412 0.0161  57  LEU A CD2 
461  N N   . ALA A 58  ? 0.2049 0.2107 0.2300 0.0061  -0.0377 0.0187  58  ALA A N   
462  C CA  . ALA A 58  ? 0.2504 0.2565 0.2781 0.0076  -0.0331 0.0170  58  ALA A CA  
463  C C   . ALA A 58  ? 0.2359 0.2442 0.2721 0.0095  -0.0322 0.0185  58  ALA A C   
464  O O   . ALA A 58  ? 0.2484 0.2554 0.2846 0.0107  -0.0294 0.0180  58  ALA A O   
465  C CB  . ALA A 58  ? 0.2170 0.2243 0.2462 0.0071  -0.0311 0.0147  58  ALA A CB  
466  N N   . SER A 59  ? 0.2143 0.2260 0.2582 0.0096  -0.0344 0.0202  59  SER A N   
467  C CA  . SER A 59  ? 0.2548 0.2685 0.3075 0.0117  -0.0333 0.0213  59  SER A CA  
468  C C   . SER A 59  ? 0.2454 0.2564 0.2964 0.0126  -0.0346 0.0238  59  SER A C   
469  O O   . SER A 59  ? 0.2592 0.2695 0.3137 0.0142  -0.0320 0.0236  59  SER A O   
470  C CB  . SER A 59  ? 0.3046 0.3227 0.3668 0.0118  -0.0355 0.0228  59  SER A CB  
471  O OG  . SER A 59  ? 0.4330 0.4513 0.4952 0.0112  -0.0406 0.0259  59  SER A OG  
472  N N   . ARG A 60  ? 0.2070 0.2165 0.2525 0.0114  -0.0385 0.0260  60  ARG A N   
473  C CA  . ARG A 60  ? 0.2299 0.2366 0.2728 0.0121  -0.0400 0.0289  60  ARG A CA  
474  C C   . ARG A 60  ? 0.2406 0.2437 0.2772 0.0122  -0.0361 0.0273  60  ARG A C   
475  O O   . ARG A 60  ? 0.2527 0.2545 0.2922 0.0135  -0.0346 0.0284  60  ARG A O   
476  C CB  . ARG A 60  ? 0.2579 0.2638 0.2949 0.0104  -0.0452 0.0314  60  ARG A CB  
477  C CG  . ARG A 60  ? 0.3510 0.3604 0.3958 0.0106  -0.0498 0.0342  60  ARG A CG  
478  C CD  . ARG A 60  ? 0.5366 0.5512 0.5938 0.0116  -0.0496 0.0337  60  ARG A CD  
479  N NE  . ARG A 60  ? 0.3835 0.3998 0.4509 0.0141  -0.0463 0.0335  60  ARG A NE  
480  N N   . ALA A 61  ? 0.2498 0.2515 0.2787 0.0108  -0.0347 0.0248  61  ALA A N   
481  C CA  . ALA A 61  ? 0.2095 0.2085 0.2334 0.0109  -0.0310 0.0232  61  ALA A CA  
482  C C   . ALA A 61  ? 0.2172 0.2172 0.2478 0.0124  -0.0274 0.0215  61  ALA A C   
483  O O   . ALA A 61  ? 0.1782 0.1762 0.2089 0.0131  -0.0255 0.0219  61  ALA A O   
484  C CB  . ALA A 61  ? 0.1709 0.1689 0.1874 0.0096  -0.0299 0.0204  61  ALA A CB  
485  N N   . ALA A 62  ? 0.1763 0.1791 0.2123 0.0129  -0.0264 0.0196  62  ALA A N   
486  C CA  . ALA A 62  ? 0.2047 0.2083 0.2459 0.0142  -0.0228 0.0175  62  ALA A CA  
487  C C   . ALA A 62  ? 0.2045 0.2078 0.2527 0.0158  -0.0227 0.0193  62  ALA A C   
488  O O   . ALA A 62  ? 0.2101 0.2118 0.2600 0.0166  -0.0200 0.0181  62  ALA A O   
489  C CB  . ALA A 62  ? 0.2357 0.2424 0.2806 0.0142  -0.0216 0.0154  62  ALA A CB  
490  N N   . GLU A 63  ? 0.1922 0.1969 0.2452 0.0163  -0.0258 0.0221  63  GLU A N   
491  C CA  . GLU A 63  ? 0.2527 0.2569 0.3132 0.0181  -0.0260 0.0241  63  GLU A CA  
492  C C   . GLU A 63  ? 0.1877 0.1877 0.2442 0.0180  -0.0259 0.0259  63  GLU A C   
493  O O   . GLU A 63  ? 0.2078 0.2060 0.2687 0.0193  -0.0238 0.0257  63  GLU A O   
494  C CB  . GLU A 63  ? 0.2079 0.2148 0.2744 0.0187  -0.0300 0.0273  63  GLU A CB  
495  C CG  . GLU A 63  ? 0.2385 0.2499 0.3120 0.0191  -0.0294 0.0256  63  GLU A CG  
496  C CD  . GLU A 63  ? 0.4095 0.4242 0.4888 0.0191  -0.0338 0.0287  63  GLU A CD  
497  O OE1 . GLU A 63  ? 0.3600 0.3731 0.4377 0.0191  -0.0377 0.0323  63  GLU A OE1 
498  O OE2 . GLU A 63  ? 0.3388 0.3576 0.4239 0.0191  -0.0335 0.0277  63  GLU A OE2 
499  N N   . ILE A 64  ? 0.2055 0.2037 0.2535 0.0165  -0.0278 0.0275  64  ILE A N   
500  C CA  . ILE A 64  ? 0.2064 0.2007 0.2499 0.0161  -0.0273 0.0294  64  ILE A CA  
501  C C   . ILE A 64  ? 0.2573 0.2502 0.3003 0.0161  -0.0229 0.0261  64  ILE A C   
502  O O   . ILE A 64  ? 0.2177 0.2081 0.2635 0.0166  -0.0213 0.0268  64  ILE A O   
503  C CB  . ILE A 64  ? 0.2617 0.2545 0.2951 0.0142  -0.0295 0.0312  64  ILE A CB  
504  C CG1 . ILE A 64  ? 0.2339 0.2274 0.2677 0.0142  -0.0345 0.0351  64  ILE A CG1 
505  C CG2 . ILE A 64  ? 0.2158 0.2048 0.2436 0.0135  -0.0276 0.0323  64  ILE A CG2 
506  C CD1 . ILE A 64  ? 0.2040 0.1970 0.2280 0.0122  -0.0370 0.0355  64  ILE A CD1 
507  N N   . VAL A 65  ? 0.1776 0.1720 0.2172 0.0153  -0.0210 0.0226  65  VAL A N   
508  C CA  . VAL A 65  ? 0.1599 0.1533 0.1984 0.0151  -0.0174 0.0196  65  VAL A CA  
509  C C   . VAL A 65  ? 0.2024 0.1961 0.2489 0.0165  -0.0153 0.0178  65  VAL A C   
510  O O   . VAL A 65  ? 0.2051 0.1967 0.2526 0.0165  -0.0132 0.0168  65  VAL A O   
511  C CB  . VAL A 65  ? 0.2031 0.1982 0.2369 0.0142  -0.0163 0.0165  65  VAL A CB  
512  C CG1 . VAL A 65  ? 0.1708 0.1655 0.2047 0.0142  -0.0131 0.0134  65  VAL A CG1 
513  C CG2 . VAL A 65  ? 0.1743 0.1684 0.1999 0.0128  -0.0177 0.0176  65  VAL A CG2 
514  N N   . ALA A 66  ? 0.1764 0.1726 0.2285 0.0177  -0.0158 0.0173  66  ALA A N   
515  C CA  . ALA A 66  ? 0.2181 0.2147 0.2779 0.0192  -0.0136 0.0153  66  ALA A CA  
516  C C   . ALA A 66  ? 0.2447 0.2389 0.3107 0.0206  -0.0142 0.0178  66  ALA A C   
517  O O   . ALA A 66  ? 0.2387 0.2323 0.3110 0.0219  -0.0121 0.0159  66  ALA A O   
518  C CB  . ALA A 66  ? 0.2020 0.2023 0.2660 0.0200  -0.0135 0.0141  66  ALA A CB  
519  N N   . GLY A 67  ? 0.2464 0.2389 0.3105 0.0202  -0.0171 0.0220  67  GLY A N   
520  C CA  . GLY A 67  ? 0.2107 0.2010 0.2811 0.0217  -0.0184 0.0253  67  GLY A CA  
521  C C   . GLY A 67  ? 0.2508 0.2369 0.3220 0.0216  -0.0161 0.0249  67  GLY A C   
522  O O   . GLY A 67  ? 0.2354 0.2208 0.3035 0.0206  -0.0133 0.0215  67  GLY A O   
523  N N   . PRO A 68  ? 0.2093 0.1923 0.2851 0.0226  -0.0174 0.0284  68  PRO A N   
524  C CA  . PRO A 68  ? 0.2170 0.1954 0.2938 0.0223  -0.0153 0.0284  68  PRO A CA  
525  C C   . PRO A 68  ? 0.1949 0.1720 0.2628 0.0198  -0.0145 0.0287  68  PRO A C   
526  O O   . PRO A 68  ? 0.2195 0.1973 0.2805 0.0186  -0.0166 0.0314  68  PRO A O   
527  C CB  . PRO A 68  ? 0.2011 0.1766 0.2832 0.0236  -0.0178 0.0336  68  PRO A CB  
528  C CG  . PRO A 68  ? 0.1688 0.1481 0.2564 0.0256  -0.0203 0.0347  68  PRO A CG  
529  C CD  . PRO A 68  ? 0.2029 0.1867 0.2843 0.0243  -0.0208 0.0325  68  PRO A CD  
530  N N   . PRO A 69  ? 0.2109 0.1860 0.2787 0.0188  -0.0115 0.0257  69  PRO A N   
531  C CA  . PRO A 69  ? 0.1808 0.1560 0.2411 0.0165  -0.0103 0.0250  69  PRO A CA  
532  C C   . PRO A 69  ? 0.2465 0.2187 0.3024 0.0152  -0.0112 0.0299  69  PRO A C   
533  O O   . PRO A 69  ? 0.2580 0.2267 0.3177 0.0158  -0.0121 0.0334  69  PRO A O   
534  C CB  . PRO A 69  ? 0.2135 0.1874 0.2769 0.0160  -0.0072 0.0208  69  PRO A CB  
535  C CG  . PRO A 69  ? 0.2114 0.1826 0.2834 0.0178  -0.0068 0.0207  69  PRO A CG  
536  C CD  . PRO A 69  ? 0.2229 0.1965 0.2978 0.0198  -0.0090 0.0221  69  PRO A CD  
537  N N   . ARG A 70  ? 0.2047 0.1782 0.2526 0.0135  -0.0109 0.0300  70  ARG A N   
538  C CA  . ARG A 70  ? 0.2222 0.1934 0.2645 0.0118  -0.0106 0.0336  70  ARG A CA  
539  C C   . ARG A 70  ? 0.2357 0.2060 0.2784 0.0102  -0.0071 0.0311  70  ARG A C   
540  O O   . ARG A 70  ? 0.2041 0.1766 0.2489 0.0102  -0.0056 0.0265  70  ARG A O   
541  C CB  . ARG A 70  ? 0.1871 0.1602 0.2202 0.0109  -0.0119 0.0347  70  ARG A CB  
542  C CG  . ARG A 70  ? 0.2334 0.2078 0.2660 0.0121  -0.0158 0.0367  70  ARG A CG  
543  C CD  . ARG A 70  ? 0.2693 0.2406 0.3024 0.0124  -0.0183 0.0424  70  ARG A CD  
544  N NE  . ARG A 70  ? 0.2427 0.2157 0.2752 0.0133  -0.0225 0.0445  70  ARG A NE  
545  C CZ  . ARG A 70  ? 0.3078 0.2789 0.3398 0.0137  -0.0259 0.0497  70  ARG A CZ  
546  N NH1 . ARG A 70  ? 0.2426 0.2096 0.2743 0.0132  -0.0255 0.0537  70  ARG A NH1 
547  N NH2 . ARG A 70  ? 0.2477 0.2212 0.2795 0.0144  -0.0300 0.0511  70  ARG A NH2 
548  N N   . LYS A 71  ? 0.1870 0.1544 0.2276 0.0086  -0.0060 0.0345  71  LYS A N   
549  C CA  . LYS A 71  ? 0.2576 0.2251 0.2981 0.0067  -0.0028 0.0323  71  LYS A CA  
550  C C   . LYS A 71  ? 0.2168 0.1881 0.2505 0.0059  -0.0018 0.0302  71  LYS A C   
551  O O   . LYS A 71  ? 0.2344 0.2081 0.2696 0.0054  0.0000  0.0261  71  LYS A O   
552  C CB  . LYS A 71  ? 0.2528 0.2163 0.2930 0.0050  -0.0014 0.0367  71  LYS A CB  
553  C CG  . LYS A 71  ? 0.3029 0.2620 0.3502 0.0059  -0.0024 0.0391  71  LYS A CG  
554  C CD  . LYS A 71  ? 0.3379 0.2959 0.3932 0.0056  -0.0005 0.0352  71  LYS A CD  
555  C CE  . LYS A 71  ? 0.4131 0.3661 0.4757 0.0067  -0.0013 0.0376  71  LYS A CE  
556  N NZ  . LYS A 71  ? 0.5410 0.4894 0.6037 0.0047  -0.0001 0.0423  71  LYS A NZ  
557  N N   . LEU A 72  ? 0.2045 0.1761 0.2308 0.0058  -0.0032 0.0328  72  LEU A N   
558  C CA  . LEU A 72  ? 0.2278 0.2020 0.2469 0.0050  -0.0021 0.0313  72  LEU A CA  
559  C C   . LEU A 72  ? 0.2208 0.1976 0.2370 0.0063  -0.0044 0.0293  72  LEU A C   
560  O O   . LEU A 72  ? 0.1836 0.1599 0.2002 0.0073  -0.0075 0.0312  72  LEU A O   
561  C CB  . LEU A 72  ? 0.2258 0.1979 0.2374 0.0035  -0.0015 0.0356  72  LEU A CB  
562  C CG  . LEU A 72  ? 0.2221 0.1915 0.2354 0.0018  0.0012  0.0385  72  LEU A CG  
563  C CD1 . LEU A 72  ? 0.2301 0.1984 0.2341 0.0003  0.0025  0.0418  72  LEU A CD1 
564  C CD2 . LEU A 72  ? 0.2377 0.2089 0.2566 0.0010  0.0044  0.0346  72  LEU A CD2 
565  N N   . ILE A 73  ? 0.2155 0.1951 0.2290 0.0061  -0.0032 0.0258  73  ILE A N   
566  C CA  . ILE A 73  ? 0.2071 0.1886 0.2169 0.0070  -0.0053 0.0243  73  ILE A CA  
567  C C   . ILE A 73  ? 0.1965 0.1768 0.1977 0.0062  -0.0066 0.0271  73  ILE A C   
568  O O   . ILE A 73  ? 0.2138 0.1947 0.2121 0.0067  -0.0093 0.0271  73  ILE A O   
569  C CB  . ILE A 73  ? 0.2111 0.1956 0.2209 0.0072  -0.0038 0.0199  73  ILE A CB  
570  C CG1 . ILE A 73  ? 0.2321 0.2170 0.2394 0.0060  -0.0006 0.0193  73  ILE A CG1 
571  C CG2 . ILE A 73  ? 0.1846 0.1706 0.2018 0.0081  -0.0038 0.0171  73  ILE A CG2 
572  C CD1 . ILE A 73  ? 0.2456 0.2333 0.2514 0.0063  0.0006  0.0155  73  ILE A CD1 
573  N N   . GLU A 74  ? 0.2014 0.1799 0.1982 0.0048  -0.0045 0.0294  74  GLU A N   
574  C CA  . GLU A 74  ? 0.2094 0.1859 0.1975 0.0040  -0.0060 0.0327  74  GLU A CA  
575  C C   . GLU A 74  ? 0.2696 0.2447 0.2585 0.0047  -0.0103 0.0360  74  GLU A C   
576  O O   . GLU A 74  ? 0.2476 0.2225 0.2304 0.0046  -0.0132 0.0371  74  GLU A O   
577  C CB  . GLU A 74  ? 0.2846 0.2589 0.2692 0.0024  -0.0029 0.0357  74  GLU A CB  
578  C CG  . GLU A 74  ? 0.2752 0.2511 0.2564 0.0015  0.0012  0.0330  74  GLU A CG  
579  C CD  . GLU A 74  ? 0.2415 0.2193 0.2310 0.0015  0.0042  0.0304  74  GLU A CD  
580  O OE1 . GLU A 74  ? 0.2241 0.2025 0.2214 0.0024  0.0030  0.0291  74  GLU A OE1 
581  O OE2 . GLU A 74  ? 0.2893 0.2681 0.2773 0.0004  0.0080  0.0296  74  GLU A OE2 
582  N N   . THR A 75  ? 0.2304 0.2045 0.2272 0.0055  -0.0110 0.0377  75  THR A N   
583  C CA  . THR A 75  ? 0.2410 0.2139 0.2397 0.0064  -0.0150 0.0413  75  THR A CA  
584  C C   . THR A 75  ? 0.2079 0.1836 0.2100 0.0078  -0.0179 0.0390  75  THR A C   
585  O O   . THR A 75  ? 0.2062 0.1820 0.2065 0.0081  -0.0218 0.0413  75  THR A O   
586  C CB  . THR A 75  ? 0.2500 0.2205 0.2566 0.0070  -0.0146 0.0437  75  THR A CB  
587  O OG1 . THR A 75  ? 0.2524 0.2207 0.2570 0.0054  -0.0110 0.0449  75  THR A OG1 
588  C CG2 . THR A 75  ? 0.2356 0.2040 0.2430 0.0078  -0.0187 0.0488  75  THR A CG2 
589  N N   . VAL A 76  ? 0.1998 0.1780 0.2068 0.0085  -0.0161 0.0345  76  VAL A N   
590  C CA  . VAL A 76  ? 0.2220 0.2031 0.2316 0.0096  -0.0181 0.0321  76  VAL A CA  
591  C C   . VAL A 76  ? 0.2494 0.2313 0.2506 0.0086  -0.0199 0.0316  76  VAL A C   
592  O O   . VAL A 76  ? 0.2129 0.1959 0.2142 0.0090  -0.0234 0.0324  76  VAL A O   
593  C CB  . VAL A 76  ? 0.1724 0.1556 0.1871 0.0102  -0.0154 0.0275  76  VAL A CB  
594  C CG1 . VAL A 76  ? 0.1962 0.1823 0.2130 0.0111  -0.0171 0.0252  76  VAL A CG1 
595  C CG2 . VAL A 76  ? 0.1739 0.1559 0.1965 0.0110  -0.0139 0.0275  76  VAL A CG2 
596  N N   . GLY A 77  ? 0.2330 0.2142 0.2272 0.0075  -0.0174 0.0302  77  GLY A N   
597  C CA  . GLY A 77  ? 0.1847 0.1661 0.1709 0.0066  -0.0188 0.0292  77  GLY A CA  
598  C C   . GLY A 77  ? 0.2100 0.1895 0.1899 0.0058  -0.0223 0.0331  77  GLY A C   
599  O O   . GLY A 77  ? 0.1949 0.1750 0.1713 0.0054  -0.0255 0.0328  77  GLY A O   
600  N N   . ALA A 78  ? 0.2163 0.1933 0.1946 0.0053  -0.0219 0.0370  78  ALA A N   
601  C CA  . ALA A 78  ? 0.2454 0.2204 0.2176 0.0045  -0.0256 0.0414  78  ALA A CA  
602  C C   . ALA A 78  ? 0.2522 0.2287 0.2305 0.0057  -0.0306 0.0431  78  ALA A C   
603  O O   . ALA A 78  ? 0.2327 0.2091 0.2060 0.0050  -0.0348 0.0449  78  ALA A O   
604  C CB  . ALA A 78  ? 0.2667 0.2386 0.2371 0.0039  -0.0241 0.0456  78  ALA A CB  
605  N N   . GLU A 79  ? 0.2179 0.1960 0.2073 0.0073  -0.0302 0.0426  79  GLU A N   
606  C CA  . GLU A 79  ? 0.1941 0.1741 0.1904 0.0085  -0.0344 0.0441  79  GLU A CA  
607  C C   . GLU A 79  ? 0.2423 0.2254 0.2378 0.0082  -0.0364 0.0410  79  GLU A C   
608  O O   . GLU A 79  ? 0.1987 0.1830 0.1947 0.0081  -0.0410 0.0428  79  GLU A O   
609  C CB  . GLU A 79  ? 0.1916 0.1726 0.1999 0.0105  -0.0329 0.0436  79  GLU A CB  
610  C CG  . GLU A 79  ? 0.2174 0.2001 0.2336 0.0120  -0.0372 0.0462  79  GLU A CG  
611  C CD  . GLU A 79  ? 0.2709 0.2542 0.2988 0.0141  -0.0353 0.0455  79  GLU A CD  
612  O OE1 . GLU A 79  ? 0.2663 0.2477 0.2955 0.0141  -0.0313 0.0439  79  GLU A OE1 
613  O OE2 . GLU A 79  ? 0.2724 0.2579 0.3085 0.0156  -0.0379 0.0466  79  GLU A OE2 
614  N N   . ILE A 80  ? 0.1988 0.1829 0.1933 0.0080  -0.0332 0.0364  80  ILE A N   
615  C CA  . ILE A 80  ? 0.1892 0.1756 0.1827 0.0075  -0.0349 0.0337  80  ILE A CA  
616  C C   . ILE A 80  ? 0.2029 0.1876 0.1857 0.0057  -0.0377 0.0345  80  ILE A C   
617  O O   . ILE A 80  ? 0.2734 0.2593 0.2558 0.0051  -0.0419 0.0350  80  ILE A O   
618  C CB  . ILE A 80  ? 0.2134 0.2009 0.2081 0.0077  -0.0309 0.0290  80  ILE A CB  
619  C CG1 . ILE A 80  ? 0.2268 0.2161 0.2315 0.0093  -0.0286 0.0280  80  ILE A CG1 
620  C CG2 . ILE A 80  ? 0.1740 0.1632 0.1674 0.0070  -0.0328 0.0266  80  ILE A CG2 
621  C CD1 . ILE A 80  ? 0.2413 0.2313 0.2464 0.0095  -0.0247 0.0238  80  ILE A CD1 
622  N N   . ALA A 81  ? 0.2195 0.2013 0.1933 0.0047  -0.0353 0.0347  81  ALA A N   
623  C CA  . ALA A 81  ? 0.2413 0.2210 0.2037 0.0029  -0.0374 0.0350  81  ALA A CA  
624  C C   . ALA A 81  ? 0.2682 0.2474 0.2285 0.0023  -0.0429 0.0395  81  ALA A C   
625  O O   . ALA A 81  ? 0.2607 0.2397 0.2153 0.0010  -0.0468 0.0393  81  ALA A O   
626  C CB  . ALA A 81  ? 0.2566 0.2335 0.2106 0.0021  -0.0332 0.0347  81  ALA A CB  
627  N N   . ASP A 82  ? 0.2433 0.2218 0.2079 0.0032  -0.0435 0.0437  82  ASP A N   
628  C CA  . ASP A 82  ? 0.3152 0.2936 0.2800 0.0032  -0.0491 0.0485  82  ASP A CA  
629  C C   . ASP A 82  ? 0.2663 0.2482 0.2376 0.0035  -0.0537 0.0478  82  ASP A C   
630  O O   . ASP A 82  ? 0.2561 0.2382 0.2232 0.0023  -0.0591 0.0498  82  ASP A O   
631  C CB  . ASP A 82  ? 0.3458 0.3234 0.3181 0.0047  -0.0486 0.0526  82  ASP A CB  
632  C CG  . ASP A 82  ? 0.3450 0.3186 0.3097 0.0038  -0.0458 0.0554  82  ASP A CG  
633  O OD1 . ASP A 82  ? 0.4096 0.3811 0.3622 0.0020  -0.0449 0.0549  82  ASP A OD1 
634  O OD2 . ASP A 82  ? 0.3967 0.3690 0.3677 0.0050  -0.0442 0.0580  82  ASP A OD2 
635  N N   . HIS A 83  ? 0.2682 0.2532 0.2501 0.0049  -0.0518 0.0449  83  HIS A N   
636  C CA  . HIS A 83  ? 0.2722 0.2610 0.2614 0.0051  -0.0556 0.0444  83  HIS A CA  
637  C C   . HIS A 83  ? 0.3017 0.2905 0.2832 0.0030  -0.0580 0.0418  83  HIS A C   
638  O O   . HIS A 83  ? 0.2953 0.2857 0.2772 0.0021  -0.0634 0.0433  83  HIS A O   
639  C CB  . HIS A 83  ? 0.2569 0.2487 0.2576 0.0068  -0.0522 0.0414  83  HIS A CB  
640  C CG  . HIS A 83  ? 0.3017 0.2974 0.3079 0.0065  -0.0546 0.0395  83  HIS A CG  
641  N ND1 . HIS A 83  ? 0.2537 0.2527 0.2689 0.0072  -0.0588 0.0420  83  HIS A ND1 
642  C CD2 . HIS A 83  ? 0.2769 0.2735 0.2812 0.0054  -0.0534 0.0355  83  HIS A CD2 
643  C CE1 . HIS A 83  ? 0.3397 0.3419 0.3586 0.0064  -0.0598 0.0396  83  HIS A CE1 
644  N NE2 . HIS A 83  ? 0.2866 0.2870 0.2987 0.0052  -0.0567 0.0357  83  HIS A NE2 
645  N N   . VAL A 84  ? 0.2758 0.2628 0.2504 0.0021  -0.0540 0.0378  84  VAL A N   
646  C CA  . VAL A 84  ? 0.2591 0.2455 0.2268 0.0002  -0.0557 0.0347  84  VAL A CA  
647  C C   . VAL A 84  ? 0.2957 0.2796 0.2524 -0.0017 -0.0602 0.0369  84  VAL A C   
648  O O   . VAL A 84  ? 0.3136 0.2983 0.2684 -0.0033 -0.0649 0.0364  84  VAL A O   
649  C CB  . VAL A 84  ? 0.3124 0.2970 0.2753 0.0001  -0.0502 0.0302  84  VAL A CB  
650  C CG1 . VAL A 84  ? 0.2277 0.2105 0.1821 -0.0020 -0.0520 0.0271  84  VAL A CG1 
651  C CG2 . VAL A 84  ? 0.2573 0.2445 0.2304 0.0017  -0.0466 0.0278  84  VAL A CG2 
652  N N   . MET A 85  ? 0.2752 0.2560 0.2242 -0.0018 -0.0590 0.0396  85  MET A N   
653  C CA  A MET A 85  ? 0.3286 0.3067 0.2654 -0.0038 -0.0630 0.0416  85  MET A CA  
654  C CA  B MET A 85  ? 0.3278 0.3059 0.2647 -0.0038 -0.0629 0.0417  85  MET A CA  
655  C C   . MET A 85  ? 0.3944 0.3743 0.3348 -0.0040 -0.0701 0.0462  85  MET A C   
656  O O   . MET A 85  ? 0.3777 0.3559 0.3083 -0.0059 -0.0747 0.0477  85  MET A O   
657  C CB  A MET A 85  ? 0.3497 0.3240 0.2772 -0.0040 -0.0594 0.0436  85  MET A CB  
658  C CB  B MET A 85  ? 0.3499 0.3244 0.2783 -0.0038 -0.0593 0.0439  85  MET A CB  
659  C CG  A MET A 85  ? 0.3548 0.3274 0.2783 -0.0039 -0.0524 0.0393  85  MET A CG  
660  C CG  B MET A 85  ? 0.3550 0.3276 0.2785 -0.0039 -0.0525 0.0397  85  MET A CG  
661  S SD  A MET A 85  ? 0.3803 0.3510 0.2930 -0.0059 -0.0525 0.0338  85  MET A SD  
662  S SD  B MET A 85  ? 0.3774 0.3485 0.2918 -0.0057 -0.0528 0.0340  85  MET A SD  
663  C CE  A MET A 85  ? 0.3676 0.3342 0.2636 -0.0082 -0.0557 0.0367  85  MET A CE  
664  C CE  B MET A 85  ? 0.3731 0.3400 0.2703 -0.0081 -0.0558 0.0363  85  MET A CE  
665  N N   . ASP A 86  ? 0.3022 0.2858 0.2565 -0.0020 -0.0712 0.0483  86  ASP A N   
666  C CA  . ASP A 86  ? 0.3551 0.3411 0.3146 -0.0020 -0.0782 0.0525  86  ASP A CA  
667  C C   . ASP A 86  ? 0.3432 0.3316 0.3029 -0.0038 -0.0830 0.0502  86  ASP A C   
668  O O   . ASP A 86  ? 0.3799 0.3702 0.3417 -0.0044 -0.0897 0.0534  86  ASP A O   
669  C CB  . ASP A 86  ? 0.2998 0.2890 0.2748 0.0008  -0.0775 0.0549  86  ASP A CB  
670  C CG  . ASP A 86  ? 0.4573 0.4437 0.4320 0.0023  -0.0751 0.0588  86  ASP A CG  
671  O OD1 . ASP A 86  ? 0.4942 0.4767 0.4569 0.0010  -0.0758 0.0613  86  ASP A OD1 
672  O OD2 . ASP A 86  ? 0.4355 0.4232 0.4214 0.0046  -0.0723 0.0593  86  ASP A OD2 
673  N N   . ASP A 87  ? 0.3323 0.3205 0.2900 -0.0048 -0.0801 0.0449  87  ASP A N   
674  C CA  . ASP A 87  ? 0.3059 0.2953 0.2622 -0.0070 -0.0844 0.0423  87  ASP A CA  
675  C C   . ASP A 87  ? 0.3325 0.3172 0.2718 -0.0095 -0.0859 0.0409  87  ASP A C   
676  O O   . ASP A 87  ? 0.3658 0.3469 0.2967 -0.0098 -0.0807 0.0376  87  ASP A O   
677  C CB  . ASP A 87  ? 0.3209 0.3122 0.2845 -0.0067 -0.0806 0.0376  87  ASP A CB  
678  C CG  . ASP A 87  ? 0.2901 0.2827 0.2537 -0.0091 -0.0849 0.0351  87  ASP A CG  
679  O OD1 . ASP A 87  ? 0.3165 0.3063 0.2690 -0.0115 -0.0887 0.0345  87  ASP A OD1 
680  O OD2 . ASP A 87  ? 0.3530 0.3494 0.3280 -0.0088 -0.0846 0.0337  87  ASP A OD2 
681  N N   . GLN A 88  ? 0.3764 0.3611 0.3109 -0.0114 -0.0931 0.0433  88  GLN A N   
682  C CA  . GLN A 88  ? 0.3875 0.3675 0.3047 -0.0138 -0.0952 0.0428  88  GLN A CA  
683  C C   . GLN A 88  ? 0.3297 0.3069 0.2390 -0.0158 -0.0930 0.0364  88  GLN A C   
684  O O   . GLN A 88  ? 0.4119 0.3845 0.3061 -0.0175 -0.0925 0.0348  88  GLN A O   
685  C CB  . GLN A 88  ? 0.4754 0.4569 0.3909 -0.0154 -0.1043 0.0467  88  GLN A CB  
686  C CG  . GLN A 88  ? 0.5738 0.5590 0.5011 -0.0131 -0.1067 0.0528  88  GLN A CG  
687  C CD  . GLN A 88  ? 0.6283 0.6197 0.5718 -0.0126 -0.1113 0.0534  88  GLN A CD  
688  O OE1 . GLN A 88  ? 0.5174 0.5115 0.4718 -0.0115 -0.1074 0.0503  88  GLN A OE1 
689  N NE2 . GLN A 88  ? 0.5199 0.5137 0.4654 -0.0134 -0.1194 0.0577  88  GLN A NE2 
690  N N   . ARG A 89  ? 0.3797 0.3594 0.2988 -0.0156 -0.0916 0.0329  89  ARG A N   
691  C CA  . ARG A 89  ? 0.4162 0.3929 0.3292 -0.0173 -0.0897 0.0270  89  ARG A CA  
692  C C   . ARG A 89  ? 0.3344 0.3079 0.2429 -0.0159 -0.0814 0.0238  89  ARG A C   
693  O O   . ARG A 89  ? 0.3549 0.3247 0.2555 -0.0171 -0.0793 0.0191  89  ARG A O   
694  C CB  . ARG A 89  ? 0.3790 0.3595 0.3047 -0.0177 -0.0912 0.0249  89  ARG A CB  
695  C CG  . ARG A 89  ? 0.4181 0.4025 0.3496 -0.0193 -0.0994 0.0276  89  ARG A CG  
696  C CD  . ARG A 89  ? 0.3500 0.3391 0.2966 -0.0192 -0.0998 0.0264  89  ARG A CD  
697  N NE  . ARG A 89  ? 0.3664 0.3588 0.3249 -0.0161 -0.0946 0.0279  89  ARG A NE  
698  C CZ  . ARG A 89  ? 0.3644 0.3604 0.3352 -0.0155 -0.0925 0.0265  89  ARG A CZ  
699  N NH1 . ARG A 89  ? 0.2990 0.2959 0.2728 -0.0178 -0.0951 0.0240  89  ARG A NH1 
700  N NH2 . ARG A 89  ? 0.3076 0.3061 0.2877 -0.0126 -0.0876 0.0277  89  ARG A NH2 
701  N N   . VAL A 90  ? 0.3254 0.3002 0.2394 -0.0133 -0.0769 0.0262  90  VAL A N   
702  C CA  . VAL A 90  ? 0.3057 0.2785 0.2179 -0.0119 -0.0693 0.0234  90  VAL A CA  
703  C C   . VAL A 90  ? 0.3791 0.3472 0.2762 -0.0127 -0.0671 0.0232  90  VAL A C   
704  O O   . VAL A 90  ? 0.4124 0.3797 0.3041 -0.0130 -0.0692 0.0274  90  VAL A O   
705  C CB  . VAL A 90  ? 0.3497 0.3256 0.2735 -0.0091 -0.0655 0.0259  90  VAL A CB  
706  C CG1 . VAL A 90  ? 0.2483 0.2222 0.1696 -0.0078 -0.0581 0.0234  90  VAL A CG1 
707  C CG2 . VAL A 90  ? 0.2650 0.2455 0.2032 -0.0083 -0.0669 0.0256  90  VAL A CG2 
708  N N   . HIS A 91  ? 0.3154 0.2802 0.2055 -0.0131 -0.0628 0.0184  91  HIS A N   
709  C CA  . HIS A 91  ? 0.3387 0.2992 0.2149 -0.0137 -0.0594 0.0175  91  HIS A CA  
710  C C   . HIS A 91  ? 0.3844 0.3454 0.2632 -0.0116 -0.0529 0.0191  91  HIS A C   
711  O O   . HIS A 91  ? 0.3604 0.3196 0.2312 -0.0119 -0.0514 0.0218  91  HIS A O   
712  C CB  . HIS A 91  ? 0.3711 0.3278 0.2395 -0.0148 -0.0570 0.0114  91  HIS A CB  
713  C CG  . HIS A 91  ? 0.4597 0.4148 0.3230 -0.0174 -0.0633 0.0093  91  HIS A CG  
714  N ND1 . HIS A 91  ? 0.4468 0.4015 0.3147 -0.0179 -0.0641 0.0051  91  HIS A ND1 
715  C CD2 . HIS A 91  ? 0.5223 0.4761 0.3766 -0.0197 -0.0694 0.0111  91  HIS A CD2 
716  C CE1 . HIS A 91  ? 0.4024 0.3556 0.2647 -0.0206 -0.0703 0.0041  91  HIS A CE1 
717  N NE2 . HIS A 91  ? 0.5181 0.4708 0.3719 -0.0217 -0.0737 0.0076  91  HIS A NE2 
718  N N   . ALA A 92  ? 0.3721 0.3356 0.2622 -0.0097 -0.0491 0.0176  92  ALA A N   
719  C CA  . ALA A 92  ? 0.3007 0.2648 0.1942 -0.0078 -0.0429 0.0184  92  ALA A CA  
720  C C   . ALA A 92  ? 0.2970 0.2649 0.2049 -0.0059 -0.0415 0.0178  92  ALA A C   
721  O O   . ALA A 92  ? 0.2774 0.2469 0.1912 -0.0060 -0.0441 0.0162  92  ALA A O   
722  C CB  . ALA A 92  ? 0.3175 0.2786 0.2025 -0.0079 -0.0372 0.0145  92  ALA A CB  
723  N N   . VAL A 93  ? 0.2915 0.2607 0.2047 -0.0043 -0.0372 0.0193  93  VAL A N   
724  C CA  . VAL A 93  ? 0.2402 0.2126 0.1659 -0.0025 -0.0353 0.0185  93  VAL A CA  
725  C C   . VAL A 93  ? 0.2795 0.2519 0.2065 -0.0012 -0.0292 0.0179  93  VAL A C   
726  O O   . VAL A 93  ? 0.3169 0.2878 0.2386 -0.0016 -0.0272 0.0200  93  VAL A O   
727  C CB  . VAL A 93  ? 0.2623 0.2377 0.1973 -0.0018 -0.0389 0.0224  93  VAL A CB  
728  C CG1 . VAL A 93  ? 0.3217 0.2964 0.2557 -0.0015 -0.0383 0.0268  93  VAL A CG1 
729  C CG2 . VAL A 93  ? 0.2233 0.2020 0.1704 -0.0002 -0.0371 0.0209  93  VAL A CG2 
730  N N   . GLU A 94  ? 0.2767 0.2509 0.2107 0.0000  -0.0263 0.0150  94  GLU A N   
731  C CA  . GLU A 94  ? 0.2663 0.2415 0.2046 0.0013  -0.0213 0.0146  94  GLU A CA  
732  C C   . GLU A 94  ? 0.2951 0.2736 0.2451 0.0027  -0.0218 0.0150  94  GLU A C   
733  O O   . GLU A 94  ? 0.2468 0.2265 0.2009 0.0029  -0.0234 0.0132  94  GLU A O   
734  C CB  . GLU A 94  ? 0.3408 0.3151 0.2767 0.0018  -0.0174 0.0104  94  GLU A CB  
735  C CG  . GLU A 94  ? 0.3814 0.3531 0.3075 0.0010  -0.0145 0.0097  94  GLU A CG  
736  C CD  . GLU A 94  ? 0.3566 0.3280 0.2823 0.0019  -0.0096 0.0060  94  GLU A CD  
737  O OE1 . GLU A 94  ? 0.4169 0.3902 0.3501 0.0032  -0.0087 0.0041  94  GLU A OE1 
738  O OE2 . GLU A 94  ? 0.5072 0.4767 0.4253 0.0014  -0.0064 0.0052  94  GLU A OE2 
739  N N   . VAL A 95  ? 0.2425 0.2219 0.1974 0.0033  -0.0204 0.0175  95  VAL A N   
740  C CA  . VAL A 95  ? 0.2445 0.2267 0.2100 0.0046  -0.0201 0.0175  95  VAL A CA  
741  C C   . VAL A 95  ? 0.2413 0.2242 0.2097 0.0054  -0.0155 0.0161  95  VAL A C   
742  O O   . VAL A 95  ? 0.2091 0.1909 0.1757 0.0050  -0.0134 0.0178  95  VAL A O   
743  C CB  . VAL A 95  ? 0.2654 0.2483 0.2357 0.0049  -0.0228 0.0213  95  VAL A CB  
744  C CG1 . VAL A 95  ? 0.1763 0.1616 0.1571 0.0063  -0.0216 0.0207  95  VAL A CG1 
745  C CG2 . VAL A 95  ? 0.1897 0.1726 0.1584 0.0042  -0.0278 0.0229  95  VAL A CG2 
746  N N   . ALA A 96  ? 0.2137 0.1984 0.1868 0.0063  -0.0141 0.0131  96  ALA A N   
747  C CA  . ALA A 96  ? 0.2058 0.1916 0.1827 0.0070  -0.0105 0.0116  96  ALA A CA  
748  C C   . ALA A 96  ? 0.2266 0.2144 0.2121 0.0078  -0.0108 0.0121  96  ALA A C   
749  O O   . ALA A 96  ? 0.1969 0.1861 0.1862 0.0084  -0.0125 0.0112  96  ALA A O   
750  C CB  . ALA A 96  ? 0.2217 0.2081 0.1979 0.0075  -0.0089 0.0081  96  ALA A CB  
751  N N   . VAL A 97  ? 0.1898 0.1776 0.1783 0.0078  -0.0091 0.0135  97  VAL A N   
752  C CA  . VAL A 97  ? 0.2121 0.2012 0.2084 0.0086  -0.0089 0.0133  97  VAL A CA  
753  C C   . VAL A 97  ? 0.1688 0.1593 0.1677 0.0087  -0.0059 0.0109  97  VAL A C   
754  O O   . VAL A 97  ? 0.1668 0.1567 0.1647 0.0081  -0.0036 0.0114  97  VAL A O   
755  C CB  . VAL A 97  ? 0.1947 0.1824 0.1935 0.0084  -0.0095 0.0166  97  VAL A CB  
756  C CG1 . VAL A 97  ? 0.1537 0.1424 0.1607 0.0092  -0.0090 0.0157  97  VAL A CG1 
757  C CG2 . VAL A 97  ? 0.2038 0.1904 0.2001 0.0082  -0.0130 0.0194  97  VAL A CG2 
758  N N   . HIS A 98  ? 0.1814 0.1737 0.1835 0.0095  -0.0060 0.0083  98  HIS A N   
759  C CA  . HIS A 98  ? 0.1606 0.1546 0.1656 0.0098  -0.0039 0.0059  98  HIS A CA  
760  C C   . HIS A 98  ? 0.2154 0.2102 0.2267 0.0100  -0.0036 0.0055  98  HIS A C   
761  O O   . HIS A 98  ? 0.1464 0.1412 0.1603 0.0105  -0.0050 0.0056  98  HIS A O   
762  C CB  . HIS A 98  ? 0.2247 0.2200 0.2289 0.0105  -0.0044 0.0035  98  HIS A CB  
763  C CG  . HIS A 98  ? 0.2239 0.2180 0.2224 0.0103  -0.0050 0.0034  98  HIS A CG  
764  N ND1 . HIS A 98  ? 0.2372 0.2312 0.2330 0.0105  -0.0032 0.0021  98  HIS A ND1 
765  C CD2 . HIS A 98  ? 0.2093 0.2021 0.2045 0.0101  -0.0071 0.0043  98  HIS A CD2 
766  C CE1 . HIS A 98  ? 0.2504 0.2427 0.2411 0.0103  -0.0041 0.0019  98  HIS A CE1 
767  N NE2 . HIS A 98  ? 0.2217 0.2133 0.2117 0.0099  -0.0067 0.0032  98  HIS A NE2 
768  N N   . LYS A 99  ? 0.1736 0.1689 0.1874 0.0095  -0.0017 0.0046  99  LYS A N   
769  C CA  . LYS A 99  ? 0.1914 0.1871 0.2109 0.0094  -0.0013 0.0038  99  LYS A CA  
770  C C   . LYS A 99  ? 0.2573 0.2554 0.2787 0.0095  -0.0005 0.0009  99  LYS A C   
771  O O   . LYS A 99  ? 0.2865 0.2853 0.3104 0.0087  0.0010  0.0005  99  LYS A O   
772  C CB  . LYS A 99  ? 0.2072 0.2010 0.2286 0.0085  -0.0002 0.0059  99  LYS A CB  
773  C CG  . LYS A 99  ? 0.2422 0.2352 0.2694 0.0085  -0.0002 0.0052  99  LYS A CG  
774  C CD  . LYS A 99  ? 0.2617 0.2524 0.2909 0.0074  0.0010  0.0076  99  LYS A CD  
775  C CE  . LYS A 99  ? 0.3331 0.3226 0.3685 0.0072  0.0012  0.0064  99  LYS A CE  
776  N NZ  . LYS A 99  ? 0.3689 0.3555 0.4066 0.0060  0.0024  0.0090  99  LYS A NZ  
777  N N   . PRO A 100 ? 0.2345 0.2339 0.2547 0.0103  -0.0015 -0.0008 100 PRO A N   
778  C CA  . PRO A 100 ? 0.2642 0.2659 0.2854 0.0105  -0.0012 -0.0030 100 PRO A CA  
779  C C   . PRO A 100 ? 0.2964 0.2992 0.3221 0.0100  -0.0011 -0.0048 100 PRO A C   
780  O O   . PRO A 100 ? 0.3823 0.3873 0.4095 0.0099  -0.0010 -0.0063 100 PRO A O   
781  C CB  . PRO A 100 ? 0.2505 0.2527 0.2690 0.0114  -0.0026 -0.0037 100 PRO A CB  
782  C CG  . PRO A 100 ? 0.2674 0.2683 0.2862 0.0115  -0.0035 -0.0028 100 PRO A CG  
783  C CD  . PRO A 100 ? 0.2186 0.2177 0.2375 0.0110  -0.0031 -0.0006 100 PRO A CD  
784  N N   . GLN A 101 ? 0.2542 0.2557 0.2823 0.0097  -0.0012 -0.0048 101 GLN A N   
785  C CA  . GLN A 101 ? 0.2312 0.2331 0.2632 0.0091  -0.0011 -0.0069 101 GLN A CA  
786  C C   . GLN A 101 ? 0.2875 0.2881 0.3232 0.0079  0.0001  -0.0060 101 GLN A C   
787  O O   . GLN A 101 ? 0.2879 0.2877 0.3273 0.0072  0.0002  -0.0076 101 GLN A O   
788  C CB  . GLN A 101 ? 0.3227 0.3237 0.3552 0.0097  -0.0018 -0.0081 101 GLN A CB  
789  C CG  . GLN A 101 ? 0.3507 0.3531 0.3798 0.0106  -0.0027 -0.0088 101 GLN A CG  
790  C CD  . GLN A 101 ? 0.3564 0.3583 0.3860 0.0112  -0.0028 -0.0100 101 GLN A CD  
791  O OE1 . GLN A 101 ? 0.1692 0.1693 0.2016 0.0113  -0.0022 -0.0098 101 GLN A OE1 
792  N NE2 . GLN A 101 ? 0.2825 0.2859 0.3094 0.0116  -0.0033 -0.0112 101 GLN A NE2 
793  N N   . ALA A 102 ? 0.2596 0.2593 0.2939 0.0075  0.0011  -0.0035 102 ALA A N   
794  C CA  . ALA A 102 ? 0.2607 0.2587 0.2980 0.0062  0.0025  -0.0019 102 ALA A CA  
795  C C   . ALA A 102 ? 0.3025 0.3019 0.3448 0.0049  0.0030  -0.0041 102 ALA A C   
796  O O   . ALA A 102 ? 0.2884 0.2910 0.3312 0.0050  0.0025  -0.0061 102 ALA A O   
797  C CB  . ALA A 102 ? 0.2679 0.2657 0.3022 0.0058  0.0039  0.0008  102 ALA A CB  
798  N N   . PRO A 103 ? 0.3096 0.3068 0.3561 0.0038  0.0036  -0.0039 103 PRO A N   
799  C CA  . PRO A 103 ? 0.2808 0.2793 0.3325 0.0021  0.0038  -0.0061 103 PRO A CA  
800  C C   . PRO A 103 ? 0.3103 0.3109 0.3636 0.0009  0.0056  -0.0046 103 PRO A C   
801  O O   . PRO A 103 ? 0.3494 0.3479 0.4041 -0.0003 0.0074  -0.0020 103 PRO A O   
802  C CB  . PRO A 103 ? 0.3761 0.3707 0.4316 0.0013  0.0041  -0.0060 103 PRO A CB  
803  C CG  . PRO A 103 ? 0.3527 0.3442 0.4057 0.0022  0.0046  -0.0024 103 PRO A CG  
804  C CD  . PRO A 103 ? 0.3281 0.3213 0.3753 0.0039  0.0037  -0.0018 103 PRO A CD  
805  N N   . ILE A 104 ? 0.4185 0.4231 0.4717 0.0012  0.0054  -0.0061 104 ILE A N   
806  C CA  . ILE A 104 ? 0.2660 0.2734 0.3217 0.0002  0.0073  -0.0051 104 ILE A CA  
807  C C   . ILE A 104 ? 0.3220 0.3334 0.3825 -0.0003 0.0059  -0.0082 104 ILE A C   
808  O O   . ILE A 104 ? 0.3205 0.3334 0.3789 0.0010  0.0037  -0.0102 104 ILE A O   
809  C CB  . ILE A 104 ? 0.3165 0.3249 0.3669 0.0017  0.0084  -0.0036 104 ILE A CB  
810  C CG1 . ILE A 104 ? 0.3743 0.3788 0.4198 0.0018  0.0096  -0.0004 104 ILE A CG1 
811  C CG2 . ILE A 104 ? 0.4019 0.4138 0.4554 0.0010  0.0108  -0.0033 104 ILE A CG2 
812  C CD1 . ILE A 104 ? 0.3159 0.3208 0.3553 0.0030  0.0105  0.0008  104 ILE A CD1 
813  N N   . PRO A 105 ? 0.2828 0.2960 0.3498 -0.0023 0.0068  -0.0086 105 PRO A N   
814  C CA  . PRO A 105 ? 0.2859 0.3032 0.3578 -0.0030 0.0048  -0.0115 105 PRO A CA  
815  C C   . PRO A 105 ? 0.2691 0.2907 0.3402 -0.0013 0.0042  -0.0120 105 PRO A C   
816  O O   . PRO A 105 ? 0.3994 0.4242 0.4731 -0.0012 0.0016  -0.0143 105 PRO A O   
817  C CB  . PRO A 105 ? 0.2648 0.2832 0.3444 -0.0057 0.0064  -0.0111 105 PRO A CB  
818  C CG  . PRO A 105 ? 0.2986 0.3124 0.3768 -0.0065 0.0088  -0.0083 105 PRO A CG  
819  C CD  . PRO A 105 ? 0.2933 0.3051 0.3637 -0.0043 0.0096  -0.0061 105 PRO A CD  
820  N N   . GLN A 106 ? 0.3219 0.3435 0.3891 0.0002  0.0062  -0.0099 106 GLN A N   
821  C CA  . GLN A 106 ? 0.2258 0.2510 0.2928 0.0019  0.0062  -0.0103 106 GLN A CA  
822  C C   . GLN A 106 ? 0.2527 0.2765 0.3133 0.0041  0.0038  -0.0110 106 GLN A C   
823  O O   . GLN A 106 ? 0.2651 0.2853 0.3208 0.0044  0.0030  -0.0107 106 GLN A O   
824  C CB  . GLN A 106 ? 0.2274 0.2527 0.2932 0.0022  0.0101  -0.0080 106 GLN A CB  
825  C CG  . GLN A 106 ? 0.2095 0.2379 0.2827 0.0003  0.0128  -0.0074 106 GLN A CG  
826  C CD  . GLN A 106 ? 0.3136 0.3385 0.3870 -0.0019 0.0146  -0.0055 106 GLN A CD  
827  O OE1 . GLN A 106 ? 0.3234 0.3435 0.3908 -0.0016 0.0143  -0.0043 106 GLN A OE1 
828  N NE2 . GLN A 106 ? 0.3280 0.3551 0.4089 -0.0042 0.0164  -0.0052 106 GLN A NE2 
829  N N   . THR A 107 ? 0.1958 0.2229 0.2572 0.0057  0.0028  -0.0117 107 THR A N   
830  C CA  . THR A 107 ? 0.1670 0.1929 0.2228 0.0077  0.0009  -0.0120 107 THR A CA  
831  C C   . THR A 107 ? 0.1951 0.2189 0.2459 0.0091  0.0032  -0.0105 107 THR A C   
832  O O   . THR A 107 ? 0.2062 0.2319 0.2591 0.0096  0.0054  -0.0100 107 THR A O   
833  C CB  . THR A 107 ? 0.2178 0.2475 0.2766 0.0088  -0.0017 -0.0134 107 THR A CB  
834  O OG1 . THR A 107 ? 0.2515 0.2831 0.3143 0.0072  -0.0042 -0.0150 107 THR A OG1 
835  C CG2 . THR A 107 ? 0.2283 0.2563 0.2811 0.0107  -0.0037 -0.0133 107 THR A CG2 
836  N N   . PHE A 108 ? 0.1897 0.2098 0.2341 0.0096  0.0026  -0.0098 108 PHE A N   
837  C CA  . PHE A 108 ? 0.1968 0.2146 0.2360 0.0106  0.0043  -0.0085 108 PHE A CA  
838  C C   . PHE A 108 ? 0.2194 0.2343 0.2528 0.0115  0.0023  -0.0084 108 PHE A C   
839  O O   . PHE A 108 ? 0.2372 0.2516 0.2705 0.0112  0.0004  -0.0089 108 PHE A O   
840  C CB  . PHE A 108 ? 0.1879 0.2035 0.2258 0.0093  0.0070  -0.0067 108 PHE A CB  
841  C CG  . PHE A 108 ? 0.2516 0.2643 0.2878 0.0083  0.0060  -0.0058 108 PHE A CG  
842  C CD1 . PHE A 108 ? 0.2784 0.2916 0.3190 0.0071  0.0049  -0.0067 108 PHE A CD1 
843  C CD2 . PHE A 108 ? 0.2781 0.2874 0.3084 0.0086  0.0059  -0.0043 108 PHE A CD2 
844  C CE1 . PHE A 108 ? 0.3119 0.3220 0.3513 0.0065  0.0042  -0.0061 108 PHE A CE1 
845  C CE2 . PHE A 108 ? 0.2782 0.2850 0.3079 0.0080  0.0048  -0.0034 108 PHE A CE2 
846  C CZ  . PHE A 108 ? 0.2761 0.2832 0.3105 0.0071  0.0042  -0.0044 108 PHE A CZ  
847  N N   . ASP A 109 ? 0.1543 0.1676 0.1833 0.0126  0.0030  -0.0078 109 ASP A N   
848  C CA  . ASP A 109 ? 0.2313 0.2422 0.2555 0.0133  0.0011  -0.0076 109 ASP A CA  
849  C C   . ASP A 109 ? 0.2167 0.2246 0.2375 0.0124  0.0013  -0.0062 109 ASP A C   
850  O O   . ASP A 109 ? 0.2427 0.2496 0.2624 0.0124  -0.0004 -0.0061 109 ASP A O   
851  C CB  . ASP A 109 ? 0.1332 0.1431 0.1543 0.0147  0.0013  -0.0078 109 ASP A CB  
852  C CG  . ASP A 109 ? 0.2779 0.2902 0.3022 0.0160  0.0003  -0.0089 109 ASP A CG  
853  O OD1 . ASP A 109 ? 0.3136 0.3279 0.3408 0.0158  -0.0015 -0.0094 109 ASP A OD1 
854  O OD2 . ASP A 109 ? 0.2930 0.3050 0.3166 0.0173  0.0012  -0.0092 109 ASP A OD2 
855  N N   . ASP A 110 ? 0.2361 0.2429 0.2554 0.0118  0.0032  -0.0050 110 ASP A N   
856  C CA  . ASP A 110 ? 0.2155 0.2194 0.2312 0.0112  0.0029  -0.0032 110 ASP A CA  
857  C C   . ASP A 110 ? 0.2187 0.2218 0.2338 0.0101  0.0052  -0.0016 110 ASP A C   
858  O O   . ASP A 110 ? 0.1927 0.1970 0.2083 0.0100  0.0075  -0.0019 110 ASP A O   
859  C CB  . ASP A 110 ? 0.2093 0.2113 0.2196 0.0119  0.0018  -0.0030 110 ASP A CB  
860  C CG  . ASP A 110 ? 0.2718 0.2714 0.2793 0.0113  0.0005  -0.0013 110 ASP A CG  
861  O OD1 . ASP A 110 ? 0.2982 0.2980 0.3083 0.0112  -0.0009 -0.0012 110 ASP A OD1 
862  O OD2 . ASP A 110 ? 0.2549 0.2525 0.2578 0.0109  0.0008  -0.0001 110 ASP A OD2 
863  N N   . VAL A 111 ? 0.2043 0.2053 0.2185 0.0093  0.0047  0.0003  111 VAL A N   
864  C CA  . VAL A 111 ? 0.1863 0.1856 0.1980 0.0082  0.0064  0.0026  111 VAL A CA  
865  C C   . VAL A 111 ? 0.2455 0.2419 0.2526 0.0082  0.0045  0.0046  111 VAL A C   
866  O O   . VAL A 111 ? 0.2009 0.1969 0.2097 0.0086  0.0022  0.0045  111 VAL A O   
867  C CB  . VAL A 111 ? 0.2356 0.2353 0.2524 0.0069  0.0079  0.0035  111 VAL A CB  
868  C CG1 . VAL A 111 ? 0.1938 0.1918 0.2134 0.0067  0.0060  0.0043  111 VAL A CG1 
869  C CG2 . VAL A 111 ? 0.1858 0.1842 0.1997 0.0057  0.0106  0.0060  111 VAL A CG2 
870  N N   . ALA A 112 ? 0.1981 0.1926 0.1992 0.0077  0.0053  0.0063  112 ALA A N   
871  C CA  . ALA A 112 ? 0.1948 0.1869 0.1912 0.0076  0.0029  0.0082  112 ALA A CA  
872  C C   . ALA A 112 ? 0.2209 0.2108 0.2116 0.0065  0.0042  0.0108  112 ALA A C   
873  O O   . ALA A 112 ? 0.1973 0.1876 0.1866 0.0059  0.0074  0.0107  112 ALA A O   
874  C CB  . ALA A 112 ? 0.1890 0.1810 0.1818 0.0084  0.0011  0.0065  112 ALA A CB  
875  N N   . VAL A 113 ? 0.1973 0.1850 0.1849 0.0061  0.0017  0.0133  113 VAL A N   
876  C CA  . VAL A 113 ? 0.2203 0.2055 0.2005 0.0051  0.0019  0.0161  113 VAL A CA  
877  C C   . VAL A 113 ? 0.2409 0.2250 0.2154 0.0053  -0.0013 0.0158  113 VAL A C   
878  O O   . VAL A 113 ? 0.2305 0.2154 0.2083 0.0061  -0.0040 0.0150  113 VAL A O   
879  C CB  . VAL A 113 ? 0.2260 0.2095 0.2079 0.0043  0.0012  0.0200  113 VAL A CB  
880  C CG1 . VAL A 113 ? 0.2046 0.1891 0.1934 0.0039  0.0042  0.0199  113 VAL A CG1 
881  C CG2 . VAL A 113 ? 0.2211 0.2042 0.2065 0.0051  -0.0027 0.0211  113 VAL A CG2 
882  N N   . VAL A 114 ? 0.2182 0.2005 0.1840 0.0045  -0.0007 0.0163  114 VAL A N   
883  C CA  . VAL A 114 ? 0.2307 0.2115 0.1904 0.0043  -0.0039 0.0159  114 VAL A CA  
884  C C   . VAL A 114 ? 0.2929 0.2711 0.2454 0.0030  -0.0053 0.0196  114 VAL A C   
885  O O   . VAL A 114 ? 0.2827 0.2595 0.2296 0.0021  -0.0023 0.0206  114 VAL A O   
886  C CB  . VAL A 114 ? 0.2417 0.2222 0.1966 0.0045  -0.0022 0.0123  114 VAL A CB  
887  C CG1 . VAL A 114 ? 0.2365 0.2150 0.1851 0.0040  -0.0059 0.0118  114 VAL A CG1 
888  C CG2 . VAL A 114 ? 0.2342 0.2172 0.1963 0.0059  -0.0008 0.0091  114 VAL A CG2 
889  N N   . ILE A 115 ? 0.2145 0.1921 0.1673 0.0029  -0.0098 0.0218  115 ILE A N   
890  C CA  . ILE A 115 ? 0.2433 0.2184 0.1895 0.0017  -0.0120 0.0259  115 ILE A CA  
891  C C   . ILE A 115 ? 0.2991 0.2729 0.2368 0.0010  -0.0151 0.0247  115 ILE A C   
892  O O   . ILE A 115 ? 0.3158 0.2908 0.2569 0.0014  -0.0181 0.0232  115 ILE A O   
893  C CB  . ILE A 115 ? 0.2759 0.2515 0.2292 0.0023  -0.0151 0.0294  115 ILE A CB  
894  C CG1 . ILE A 115 ? 0.3441 0.3205 0.3057 0.0029  -0.0120 0.0300  115 ILE A CG1 
895  C CG2 . ILE A 115 ? 0.3309 0.3040 0.2777 0.0013  -0.0182 0.0340  115 ILE A CG2 
896  C CD1 . ILE A 115 ? 0.3053 0.2799 0.2629 0.0018  -0.0084 0.0321  115 ILE A CD1 
897  N N   . ARG A 116 ? 0.3285 0.2998 0.2556 -0.0003 -0.0139 0.0251  116 ARG A N   
898  C CA  . ARG A 116 ? 0.3348 0.3041 0.2522 -0.0014 -0.0167 0.0237  116 ARG A CA  
899  C C   . ARG A 116 ? 0.4412 0.4084 0.3515 -0.0028 -0.0208 0.0281  116 ARG A C   
900  O O   . ARG A 116 ? 0.3896 0.3557 0.2976 -0.0033 -0.0192 0.0318  116 ARG A O   
901  C CB  . ARG A 116 ? 0.4136 0.3812 0.3229 -0.0019 -0.0123 0.0201  116 ARG A CB  
902  C CG  . ARG A 116 ? 0.5144 0.4795 0.4137 -0.0030 -0.0149 0.0179  116 ARG A CG  
903  C CD  . ARG A 116 ? 0.6263 0.5884 0.5134 -0.0041 -0.0114 0.0159  116 ARG A CD  
904  N NE  . ARG A 116 ? 0.6243 0.5837 0.5021 -0.0053 -0.0146 0.0135  116 ARG A NE  
905  C CZ  . ARG A 116 ? 0.6246 0.5839 0.5047 -0.0050 -0.0165 0.0096  116 ARG A CZ  
906  N NH1 . ARG A 116 ? 0.6127 0.5746 0.5041 -0.0033 -0.0155 0.0078  116 ARG A NH1 
907  N NH2 . ARG A 116 ? 0.5714 0.5276 0.4422 -0.0064 -0.0195 0.0075  116 ARG A NH2 
908  N N   . ARG A 117 ? 0.3695 0.3364 0.2771 -0.0034 -0.0261 0.0279  117 ARG A N   
909  C CA  . ARG A 117 ? 0.4171 0.3822 0.3174 -0.0048 -0.0311 0.0318  117 ARG A CA  
910  C C   . ARG A 117 ? 0.5131 0.4766 0.4044 -0.0062 -0.0341 0.0287  117 ARG A C   
911  O O   . ARG A 117 ? 0.3447 0.3091 0.2397 -0.0058 -0.0338 0.0245  117 ARG A O   
912  C CB  . ARG A 117 ? 0.4434 0.4109 0.3535 -0.0040 -0.0362 0.0352  117 ARG A CB  
913  C CG  . ARG A 117 ? 0.4839 0.4526 0.4035 -0.0025 -0.0341 0.0382  117 ARG A CG  
914  C CD  . ARG A 117 ? 0.5729 0.5399 0.4897 -0.0031 -0.0372 0.0443  117 ARG A CD  
915  N NE  . ARG A 117 ? 0.5230 0.4915 0.4520 -0.0014 -0.0369 0.0467  117 ARG A NE  
916  C CZ  . ARG A 117 ? 0.5281 0.4962 0.4608 -0.0008 -0.0320 0.0470  117 ARG A CZ  
917  N NH1 . ARG A 117 ? 0.5167 0.4832 0.4422 -0.0018 -0.0272 0.0454  117 ARG A NH1 
918  N NH2 . ARG A 117 ? 0.4909 0.4600 0.4346 0.0006  -0.0319 0.0487  117 ARG A NH2 
919  N N   . SER A 118 ? 0.5246 0.4853 0.4039 -0.0080 -0.0369 0.0309  118 SER A N   
920  C CA  . SER A 118 ? 0.5367 0.4953 0.4065 -0.0097 -0.0403 0.0280  118 SER A CA  
921  C C   . SER A 118 ? 0.5483 0.5048 0.4076 -0.0116 -0.0453 0.0323  118 SER A C   
922  O O   . SER A 118 ? 0.5095 0.4654 0.3673 -0.0115 -0.0447 0.0372  118 SER A O   
923  C CB  . SER A 118 ? 0.5880 0.5440 0.4496 -0.0101 -0.0350 0.0227  118 SER A CB  
924  O OG  . SER A 118 ? 0.6356 0.5906 0.4932 -0.0098 -0.0289 0.0238  118 SER A OG  
925  N N   . ARG A 119 ? 0.6393 0.5944 0.4916 -0.0133 -0.0504 0.0305  119 ARG A N   
926  C CA  . ARG A 119 ? 0.5841 0.5372 0.4256 -0.0153 -0.0561 0.0343  119 ARG A CA  
927  C C   . ARG A 119 ? 0.8175 0.7661 0.6418 -0.0169 -0.0524 0.0333  119 ARG A C   
928  O O   . ARG A 119 ? 0.9049 0.8526 0.7277 -0.0162 -0.0459 0.0340  119 ARG A O   
929  C CB  . ARG A 119 ? 0.5838 0.5375 0.4249 -0.0167 -0.0635 0.0327  119 ARG A CB  
930  C CG  . ARG A 119 ? 0.5522 0.5105 0.4102 -0.0152 -0.0664 0.0330  119 ARG A CG  
931  C CD  . ARG A 119 ? 0.5336 0.4947 0.3979 -0.0151 -0.0731 0.0390  119 ARG A CD  
932  N NE  . ARG A 119 ? 0.6315 0.5970 0.5116 -0.0138 -0.0751 0.0382  119 ARG A NE  
933  C CZ  . ARG A 119 ? 0.4304 0.3995 0.3239 -0.0117 -0.0756 0.0418  119 ARG A CZ  
934  N NH1 . ARG A 119 ? 0.4886 0.4572 0.3824 -0.0107 -0.0753 0.0471  119 ARG A NH1 
935  N NH2 . ARG A 119 ? 0.3906 0.3636 0.2975 -0.0106 -0.0762 0.0401  119 ARG A NH2 
936  N N   . ALA B 2   ? 0.6506 0.6639 0.5435 -0.0023 -0.0367 -0.0287 2   ALA B N   
937  C CA  . ALA B 2   ? 0.6720 0.6842 0.5644 -0.0037 -0.0347 -0.0354 2   ALA B CA  
938  C C   . ALA B 2   ? 0.5403 0.5528 0.4459 -0.0026 -0.0316 -0.0371 2   ALA B C   
939  O O   . ALA B 2   ? 0.5367 0.5502 0.4504 -0.0009 -0.0313 -0.0331 2   ALA B O   
940  C CB  . ALA B 2   ? 0.6197 0.6295 0.5012 -0.0047 -0.0297 -0.0377 2   ALA B CB  
941  N N   . ASP B 3   ? 0.4587 0.4699 0.3658 -0.0036 -0.0296 -0.0427 3   ASP B N   
942  C CA  . ASP B 3   ? 0.3213 0.3322 0.2402 -0.0027 -0.0268 -0.0443 3   ASP B CA  
943  C C   . ASP B 3   ? 0.3423 0.3521 0.2637 -0.0011 -0.0209 -0.0422 3   ASP B C   
944  O O   . ASP B 3   ? 0.2843 0.2927 0.1980 -0.0013 -0.0173 -0.0423 3   ASP B O   
945  C CB  . ASP B 3   ? 0.3239 0.3328 0.2425 -0.0042 -0.0258 -0.0509 3   ASP B CB  
946  C CG  . ASP B 3   ? 0.3822 0.3924 0.2999 -0.0061 -0.0319 -0.0534 3   ASP B CG  
947  O OD1 . ASP B 3   ? 0.3812 0.3943 0.3005 -0.0059 -0.0371 -0.0500 3   ASP B OD1 
948  O OD2 . ASP B 3   ? 0.3581 0.3663 0.2733 -0.0077 -0.0316 -0.0591 3   ASP B OD2 
949  N N   . ARG B 4   ? 0.2692 0.2796 0.2014 0.0003  -0.0198 -0.0402 4   ARG B N   
950  C CA  . ARG B 4   ? 0.2574 0.2668 0.1926 0.0017  -0.0145 -0.0385 4   ARG B CA  
951  C C   . ARG B 4   ? 0.2557 0.2652 0.2025 0.0027  -0.0131 -0.0388 4   ARG B C   
952  O O   . ARG B 4   ? 0.2769 0.2874 0.2298 0.0026  -0.0162 -0.0390 4   ARG B O   
953  C CB  . ARG B 4   ? 0.2920 0.3022 0.2248 0.0025  -0.0145 -0.0330 4   ARG B CB  
954  C CG  . ARG B 4   ? 0.3170 0.3290 0.2532 0.0031  -0.0194 -0.0294 4   ARG B CG  
955  C CD  . ARG B 4   ? 0.3244 0.3364 0.2563 0.0037  -0.0200 -0.0243 4   ARG B CD  
956  N NE  . ARG B 4   ? 0.4194 0.4328 0.3582 0.0050  -0.0232 -0.0209 4   ARG B NE  
957  C CZ  . ARG B 4   ? 0.3807 0.3956 0.3190 0.0050  -0.0284 -0.0197 4   ARG B CZ  
958  N NH1 . ARG B 4   ? 0.3752 0.3905 0.3063 0.0037  -0.0315 -0.0214 4   ARG B NH1 
959  N NH2 . ARG B 4   ? 0.3974 0.4135 0.3429 0.0064  -0.0306 -0.0169 4   ARG B NH2 
960  N N   . ILE B 5   ? 0.2375 0.2459 0.1873 0.0036  -0.0083 -0.0388 5   ILE B N   
961  C CA  . ILE B 5   ? 0.2942 0.3024 0.2542 0.0047  -0.0066 -0.0381 5   ILE B CA  
962  C C   . ILE B 5   ? 0.2250 0.2341 0.1872 0.0060  -0.0053 -0.0333 5   ILE B C   
963  O O   . ILE B 5   ? 0.2418 0.2507 0.1994 0.0060  -0.0027 -0.0321 5   ILE B O   
964  C CB  . ILE B 5   ? 0.2676 0.2738 0.2303 0.0049  -0.0025 -0.0419 5   ILE B CB  
965  C CG1 . ILE B 5   ? 0.2172 0.2219 0.1774 0.0035  -0.0037 -0.0471 5   ILE B CG1 
966  C CG2 . ILE B 5   ? 0.2201 0.2261 0.1930 0.0061  -0.0011 -0.0405 5   ILE B CG2 
967  C CD1 . ILE B 5   ? 0.2330 0.2352 0.1926 0.0035  0.0008  -0.0516 5   ILE B CD1 
968  N N   . GLU B 6   ? 0.1952 0.2050 0.1643 0.0068  -0.0069 -0.0308 6   GLU B N   
969  C CA  . GLU B 6   ? 0.2220 0.2324 0.1928 0.0077  -0.0065 -0.0264 6   GLU B CA  
970  C C   . GLU B 6   ? 0.2412 0.2512 0.2202 0.0087  -0.0047 -0.0257 6   GLU B C   
971  O O   . GLU B 6   ? 0.2452 0.2554 0.2295 0.0089  -0.0063 -0.0259 6   GLU B O   
972  C CB  . GLU B 6   ? 0.2895 0.3010 0.2593 0.0079  -0.0105 -0.0235 6   GLU B CB  
973  C CG  . GLU B 6   ? 0.2324 0.2441 0.1935 0.0072  -0.0123 -0.0228 6   GLU B CG  
974  C CD  . GLU B 6   ? 0.3033 0.3160 0.2645 0.0077  -0.0165 -0.0197 6   GLU B CD  
975  O OE1 . GLU B 6   ? 0.2611 0.2745 0.2292 0.0086  -0.0177 -0.0187 6   GLU B OE1 
976  O OE2 . GLU B 6   ? 0.3287 0.3415 0.2830 0.0073  -0.0184 -0.0182 6   GLU B OE2 
977  N N   . LEU B 7   ? 0.2448 0.2544 0.2250 0.0092  -0.0015 -0.0248 7   LEU B N   
978  C CA  . LEU B 7   ? 0.2498 0.2594 0.2372 0.0100  -0.0002 -0.0233 7   LEU B CA  
979  C C   . LEU B 7   ? 0.2459 0.2559 0.2331 0.0104  -0.0009 -0.0193 7   LEU B C   
980  O O   . LEU B 7   ? 0.1833 0.1936 0.1663 0.0100  0.0002  -0.0179 7   LEU B O   
981  C CB  . LEU B 7   ? 0.2227 0.2319 0.2126 0.0104  0.0036  -0.0250 7   LEU B CB  
982  C CG  . LEU B 7   ? 0.2055 0.2149 0.2023 0.0113  0.0049  -0.0230 7   LEU B CG  
983  C CD1 . LEU B 7   ? 0.1739 0.1824 0.1760 0.0117  0.0031  -0.0228 7   LEU B CD1 
984  C CD2 . LEU B 7   ? 0.1684 0.1778 0.1678 0.0118  0.0087  -0.0247 7   LEU B CD2 
985  N N   . ARG B 8   ? 0.1970 0.2070 0.1886 0.0109  -0.0025 -0.0175 8   ARG B N   
986  C CA  . ARG B 8   ? 0.2370 0.2469 0.2283 0.0112  -0.0034 -0.0141 8   ARG B CA  
987  C C   . ARG B 8   ? 0.2082 0.2177 0.2049 0.0117  -0.0027 -0.0128 8   ARG B C   
988  O O   . ARG B 8   ? 0.2164 0.2257 0.2171 0.0120  -0.0031 -0.0135 8   ARG B O   
989  C CB  . ARG B 8   ? 0.2561 0.2661 0.2460 0.0114  -0.0066 -0.0131 8   ARG B CB  
990  C CG  . ARG B 8   ? 0.2615 0.2719 0.2454 0.0109  -0.0081 -0.0137 8   ARG B CG  
991  C CD  . ARG B 8   ? 0.3031 0.3130 0.2820 0.0105  -0.0073 -0.0114 8   ARG B CD  
992  N NE  . ARG B 8   ? 0.2874 0.2975 0.2598 0.0100  -0.0091 -0.0114 8   ARG B NE  
993  C CZ  . ARG B 8   ? 0.2821 0.2924 0.2493 0.0092  -0.0079 -0.0135 8   ARG B CZ  
994  N NH1 . ARG B 8   ? 0.2711 0.2814 0.2396 0.0089  -0.0047 -0.0160 8   ARG B NH1 
995  N NH2 . ARG B 8   ? 0.3360 0.3464 0.2965 0.0086  -0.0101 -0.0130 8   ARG B NH2 
996  N N   . GLY B 9   ? 0.1756 0.1851 0.1723 0.0115  -0.0018 -0.0106 9   GLY B N   
997  C CA  . GLY B 9   ? 0.1573 0.1665 0.1584 0.0118  -0.0020 -0.0090 9   GLY B CA  
998  C C   . GLY B 9   ? 0.1858 0.1955 0.1918 0.0121  -0.0003 -0.0098 9   GLY B C   
999  O O   . GLY B 9   ? 0.1936 0.2028 0.2030 0.0124  -0.0012 -0.0090 9   GLY B O   
1000 N N   . LEU B 10  ? 0.1881 0.1986 0.1944 0.0121  0.0020  -0.0116 10  LEU B N   
1001 C CA  . LEU B 10  ? 0.2230 0.2341 0.2349 0.0126  0.0038  -0.0121 10  LEU B CA  
1002 C C   . LEU B 10  ? 0.2193 0.2312 0.2343 0.0124  0.0038  -0.0094 10  LEU B C   
1003 O O   . LEU B 10  ? 0.2018 0.2146 0.2153 0.0118  0.0049  -0.0084 10  LEU B O   
1004 C CB  . LEU B 10  ? 0.1767 0.1885 0.1881 0.0127  0.0069  -0.0146 10  LEU B CB  
1005 C CG  . LEU B 10  ? 0.1979 0.2103 0.2157 0.0136  0.0092  -0.0154 10  LEU B CG  
1006 C CD1 . LEU B 10  ? 0.2455 0.2564 0.2672 0.0143  0.0082  -0.0165 10  LEU B CD1 
1007 C CD2 . LEU B 10  ? 0.2050 0.2182 0.2213 0.0136  0.0128  -0.0180 10  LEU B CD2 
1008 N N   . THR B 11  ? 0.2090 0.2207 0.2285 0.0128  0.0025  -0.0083 11  THR B N   
1009 C CA  . THR B 11  ? 0.1636 0.1759 0.1856 0.0124  0.0015  -0.0058 11  THR B CA  
1010 C C   . THR B 11  ? 0.2084 0.2223 0.2371 0.0130  0.0026  -0.0054 11  THR B C   
1011 O O   . THR B 11  ? 0.2001 0.2133 0.2321 0.0138  0.0021  -0.0058 11  THR B O   
1012 C CB  . THR B 11  ? 0.1886 0.1991 0.2093 0.0123  -0.0013 -0.0045 11  THR B CB  
1013 O OG1 . THR B 11  ? 0.1926 0.2020 0.2082 0.0121  -0.0022 -0.0049 11  THR B OG1 
1014 C CG2 . THR B 11  ? 0.1782 0.1890 0.2007 0.0116  -0.0027 -0.0023 11  THR B CG2 
1015 N N   . VAL B 12  ? 0.2157 0.2316 0.2470 0.0125  0.0039  -0.0045 12  VAL B N   
1016 C CA  . VAL B 12  ? 0.2181 0.2364 0.2567 0.0132  0.0055  -0.0043 12  VAL B CA  
1017 C C   . VAL B 12  ? 0.2676 0.2880 0.3097 0.0122  0.0048  -0.0020 12  VAL B C   
1018 O O   . VAL B 12  ? 0.1621 0.1829 0.2013 0.0110  0.0056  -0.0013 12  VAL B O   
1019 C CB  . VAL B 12  ? 0.2024 0.2219 0.2416 0.0139  0.0094  -0.0068 12  VAL B CB  
1020 C CG1 . VAL B 12  ? 0.2039 0.2257 0.2519 0.0150  0.0112  -0.0068 12  VAL B CG1 
1021 C CG2 . VAL B 12  ? 0.2744 0.2914 0.3091 0.0144  0.0098  -0.0095 12  VAL B CG2 
1022 N N   . HIS B 13  ? 0.2242 0.2457 0.2725 0.0126  0.0031  -0.0005 13  HIS B N   
1023 C CA  . HIS B 13  ? 0.1769 0.2011 0.2302 0.0116  0.0023  0.0016  13  HIS B CA  
1024 C C   . HIS B 13  ? 0.2225 0.2502 0.2811 0.0118  0.0062  0.0011  13  HIS B C   
1025 O O   . HIS B 13  ? 0.2293 0.2581 0.2918 0.0134  0.0086  -0.0005 13  HIS B O   
1026 C CB  . HIS B 13  ? 0.2119 0.2366 0.2704 0.0120  -0.0009 0.0033  13  HIS B CB  
1027 C CG  . HIS B 13  ? 0.2264 0.2538 0.2899 0.0107  -0.0027 0.0055  13  HIS B CG  
1028 N ND1 . HIS B 13  ? 0.2161 0.2420 0.2760 0.0089  -0.0057 0.0067  13  HIS B ND1 
1029 C CD2 . HIS B 13  ? 0.2692 0.3007 0.3416 0.0108  -0.0018 0.0064  13  HIS B CD2 
1030 C CE1 . HIS B 13  ? 0.2679 0.2968 0.3339 0.0078  -0.0068 0.0084  13  HIS B CE1 
1031 N NE2 . HIS B 13  ? 0.2877 0.3204 0.3617 0.0089  -0.0045 0.0084  13  HIS B NE2 
1032 N N   . GLY B 14  ? 0.1745 0.2041 0.2338 0.0102  0.0070  0.0024  14  GLY B N   
1033 C CA  . GLY B 14  ? 0.2133 0.2465 0.2776 0.0101  0.0111  0.0021  14  GLY B CA  
1034 C C   . GLY B 14  ? 0.2182 0.2542 0.2873 0.0082  0.0103  0.0046  14  GLY B C   
1035 O O   . GLY B 14  ? 0.2249 0.2595 0.2930 0.0069  0.0064  0.0063  14  GLY B O   
1036 N N   . ARG B 15  ? 0.2137 0.2537 0.2885 0.0079  0.0143  0.0047  15  ARG B N   
1037 C CA  . ARG B 15  ? 0.1932 0.2365 0.2743 0.0059  0.0140  0.0071  15  ARG B CA  
1038 C C   . ARG B 15  ? 0.1793 0.2237 0.2578 0.0043  0.0184  0.0074  15  ARG B C   
1039 O O   . ARG B 15  ? 0.2160 0.2643 0.3015 0.0027  0.0199  0.0091  15  ARG B O   
1040 C CB  . ARG B 15  ? 0.2529 0.3012 0.3466 0.0069  0.0142  0.0077  15  ARG B CB  
1041 C CG  . ARG B 15  ? 0.3380 0.3858 0.4353 0.0075  0.0084  0.0089  15  ARG B CG  
1042 C CD  . ARG B 15  ? 0.3938 0.4466 0.5039 0.0091  0.0086  0.0096  15  ARG B CD  
1043 N NE  . ARG B 15  ? 0.4771 0.5307 0.5921 0.0087  0.0027  0.0117  15  ARG B NE  
1044 C CZ  . ARG B 15  ? 0.5288 0.5785 0.6385 0.0092  -0.0017 0.0120  15  ARG B CZ  
1045 N NH1 . ARG B 15  ? 0.3931 0.4378 0.4930 0.0100  -0.0011 0.0103  15  ARG B NH1 
1046 N NH2 . ARG B 15  ? 0.3940 0.4449 0.5082 0.0087  -0.0069 0.0141  15  ARG B NH2 
1047 N N   . HIS B 16  ? 0.2156 0.2568 0.2842 0.0044  0.0204  0.0061  16  HIS B N   
1048 C CA  . HIS B 16  ? 0.1976 0.2392 0.2622 0.0027  0.0243  0.0068  16  HIS B CA  
1049 C C   . HIS B 16  ? 0.2546 0.2949 0.3180 0.0000  0.0218  0.0097  16  HIS B C   
1050 O O   . HIS B 16  ? 0.2340 0.2712 0.2952 -0.0004 0.0170  0.0104  16  HIS B O   
1051 C CB  . HIS B 16  ? 0.1731 0.2112 0.2267 0.0034  0.0260  0.0049  16  HIS B CB  
1052 C CG  . HIS B 16  ? 0.2098 0.2478 0.2635 0.0059  0.0270  0.0017  16  HIS B CG  
1053 N ND1 . HIS B 16  ? 0.2141 0.2552 0.2727 0.0072  0.0317  -0.0002 16  HIS B ND1 
1054 C CD2 . HIS B 16  ? 0.2282 0.2630 0.2783 0.0074  0.0241  0.0001  16  HIS B CD2 
1055 C CE1 . HIS B 16  ? 0.2726 0.3122 0.3305 0.0093  0.0314  -0.0029 16  HIS B CE1 
1056 N NE2 . HIS B 16  ? 0.1807 0.2166 0.2336 0.0094  0.0268  -0.0027 16  HIS B NE2 
1057 N N   . GLY B 17  ? 0.2477 0.2901 0.3125 -0.0019 0.0253  0.0114  17  GLY B N   
1058 C CA  . GLY B 17  ? 0.2408 0.2818 0.3052 -0.0047 0.0234  0.0142  17  GLY B CA  
1059 C C   . GLY B 17  ? 0.2818 0.3273 0.3534 -0.0068 0.0274  0.0161  17  GLY B C   
1060 O O   . GLY B 17  ? 0.2305 0.2813 0.3110 -0.0061 0.0304  0.0155  17  GLY B O   
1061 N N   . VAL B 18  ? 0.2076 0.2511 0.2761 -0.0095 0.0275  0.0186  18  VAL B N   
1062 C CA  . VAL B 18  ? 0.2955 0.3428 0.3702 -0.0121 0.0315  0.0209  18  VAL B CA  
1063 C C   . VAL B 18  ? 0.2496 0.3007 0.3369 -0.0136 0.0289  0.0221  18  VAL B C   
1064 O O   . VAL B 18  ? 0.2381 0.2950 0.3349 -0.0147 0.0325  0.0231  18  VAL B O   
1065 C CB  . VAL B 18  ? 0.2375 0.2806 0.3042 -0.0145 0.0323  0.0236  18  VAL B CB  
1066 C CG1 . VAL B 18  ? 0.2872 0.3339 0.3610 -0.0177 0.0359  0.0264  18  VAL B CG1 
1067 C CG2 . VAL B 18  ? 0.2582 0.2986 0.3132 -0.0133 0.0354  0.0227  18  VAL B CG2 
1068 N N   . TYR B 19  ? 0.2349 0.2834 0.3226 -0.0137 0.0227  0.0221  19  TYR B N   
1069 C CA  . TYR B 19  ? 0.2432 0.2942 0.3410 -0.0159 0.0193  0.0235  19  TYR B CA  
1070 C C   . TYR B 19  ? 0.2930 0.3479 0.3991 -0.0139 0.0164  0.0221  19  TYR B C   
1071 O O   . TYR B 19  ? 0.2231 0.2760 0.3249 -0.0112 0.0145  0.0201  19  TYR B O   
1072 C CB  . TYR B 19  ? 0.2155 0.2605 0.3079 -0.0178 0.0143  0.0245  19  TYR B CB  
1073 C CG  . TYR B 19  ? 0.3552 0.3966 0.4413 -0.0200 0.0170  0.0265  19  TYR B CG  
1074 C CD1 . TYR B 19  ? 0.3506 0.3948 0.4432 -0.0232 0.0197  0.0291  19  TYR B CD1 
1075 C CD2 . TYR B 19  ? 0.3377 0.3732 0.4117 -0.0188 0.0169  0.0261  19  TYR B CD2 
1076 C CE1 . TYR B 19  ? 0.3871 0.4276 0.4737 -0.0253 0.0223  0.0315  19  TYR B CE1 
1077 C CE2 . TYR B 19  ? 0.3151 0.3470 0.3832 -0.0207 0.0191  0.0285  19  TYR B CE2 
1078 C CZ  . TYR B 19  ? 0.4299 0.4642 0.5041 -0.0239 0.0218  0.0312  19  TYR B CZ  
1079 O OH  . TYR B 19  ? 0.4789 0.5094 0.5471 -0.0259 0.0240  0.0340  19  TYR B OH  
1080 N N   . ASP B 20  ? 0.2284 0.2889 0.3470 -0.0156 0.0158  0.0235  20  ASP B N   
1081 C CA  . ASP B 20  ? 0.2450 0.3098 0.3730 -0.0139 0.0127  0.0228  20  ASP B CA  
1082 C C   . ASP B 20  ? 0.2880 0.3481 0.4102 -0.0129 0.0061  0.0218  20  ASP B C   
1083 O O   . ASP B 20  ? 0.3000 0.3609 0.4236 -0.0101 0.0046  0.0206  20  ASP B O   
1084 C CB  . ASP B 20  ? 0.3674 0.4383 0.5092 -0.0166 0.0116  0.0248  20  ASP B CB  
1085 C CG  . ASP B 20  ? 0.4261 0.5037 0.5771 -0.0170 0.0184  0.0257  20  ASP B CG  
1086 O OD1 . ASP B 20  ? 0.3388 0.4165 0.4855 -0.0149 0.0242  0.0244  20  ASP B OD1 
1087 O OD2 . ASP B 20  ? 0.3605 0.4434 0.5233 -0.0194 0.0179  0.0275  20  ASP B OD2 
1088 N N   . HIS B 21  ? 0.2711 0.3260 0.3870 -0.0151 0.0024  0.0223  21  HIS B N   
1089 C CA  . HIS B 21  ? 0.2150 0.2657 0.3257 -0.0144 -0.0036 0.0213  21  HIS B CA  
1090 C C   . HIS B 21  ? 0.2832 0.3303 0.3847 -0.0110 -0.0029 0.0193  21  HIS B C   
1091 O O   . HIS B 21  ? 0.3293 0.3746 0.4286 -0.0096 -0.0069 0.0184  21  HIS B O   
1092 C CB  . HIS B 21  ? 0.2715 0.3167 0.3766 -0.0173 -0.0071 0.0218  21  HIS B CB  
1093 C CG  . HIS B 21  ? 0.2963 0.3353 0.3900 -0.0170 -0.0049 0.0214  21  HIS B CG  
1094 N ND1 . HIS B 21  ? 0.2836 0.3173 0.3673 -0.0150 -0.0068 0.0197  21  HIS B ND1 
1095 C CD2 . HIS B 21  ? 0.2332 0.2706 0.3241 -0.0186 -0.0013 0.0226  21  HIS B CD2 
1096 C CE1 . HIS B 21  ? 0.2688 0.2982 0.3447 -0.0151 -0.0046 0.0199  21  HIS B CE1 
1097 N NE2 . HIS B 21  ? 0.2111 0.2424 0.2908 -0.0173 -0.0013 0.0218  21  HIS B NE2 
1098 N N   . GLU B 22  ? 0.2506 0.2968 0.3470 -0.0098 0.0022  0.0186  22  GLU B N   
1099 C CA  . GLU B 22  ? 0.2119 0.2549 0.3000 -0.0069 0.0030  0.0167  22  GLU B CA  
1100 C C   . GLU B 22  ? 0.2453 0.2921 0.3388 -0.0041 0.0046  0.0155  22  GLU B C   
1101 O O   . GLU B 22  ? 0.2977 0.3419 0.3858 -0.0018 0.0040  0.0138  22  GLU B O   
1102 C CB  . GLU B 22  ? 0.2195 0.2600 0.2996 -0.0069 0.0074  0.0164  22  GLU B CB  
1103 C CG  . GLU B 22  ? 0.2499 0.2854 0.3229 -0.0090 0.0059  0.0175  22  GLU B CG  
1104 C CD  . GLU B 22  ? 0.2798 0.3131 0.3448 -0.0087 0.0099  0.0176  22  GLU B CD  
1105 O OE1 . GLU B 22  ? 0.2258 0.2555 0.2825 -0.0069 0.0093  0.0161  22  GLU B OE1 
1106 O OE2 . GLU B 22  ? 0.2763 0.3116 0.3434 -0.0105 0.0136  0.0192  22  GLU B OE2 
1107 N N   . ARG B 23  ? 0.2684 0.3212 0.3730 -0.0042 0.0067  0.0163  23  ARG B N   
1108 C CA  . ARG B 23  ? 0.2322 0.2887 0.3435 -0.0014 0.0082  0.0152  23  ARG B CA  
1109 C C   . ARG B 23  ? 0.2962 0.3539 0.4135 -0.0006 0.0027  0.0159  23  ARG B C   
1110 O O   . ARG B 23  ? 0.3229 0.3825 0.4449 0.0020  0.0032  0.0152  23  ARG B O   
1111 C CB  . ARG B 23  ? 0.3247 0.3874 0.4456 -0.0015 0.0137  0.0156  23  ARG B CB  
1112 C CG  . ARG B 23  ? 0.4475 0.5090 0.5616 -0.0011 0.0200  0.0142  23  ARG B CG  
1113 C CD  . ARG B 23  ? 0.5271 0.5945 0.6495 -0.0019 0.0260  0.0147  23  ARG B CD  
1114 N NE  . ARG B 23  ? 0.4599 0.5266 0.5787 -0.0051 0.0280  0.0165  23  ARG B NE  
1115 C CZ  . ARG B 23  ? 0.5473 0.6186 0.6752 -0.0076 0.0294  0.0187  23  ARG B CZ  
1116 N NH1 . ARG B 23  ? 0.5634 0.6410 0.7053 -0.0072 0.0288  0.0193  23  ARG B NH1 
1117 N NH2 . ARG B 23  ? 0.4303 0.5001 0.5537 -0.0106 0.0314  0.0205  23  ARG B NH2 
1118 N N   . VAL B 24  ? 0.2046 0.2610 0.3215 -0.0028 -0.0025 0.0173  24  VAL B N   
1119 C CA  . VAL B 24  ? 0.2849 0.3426 0.4069 -0.0024 -0.0081 0.0182  24  VAL B CA  
1120 C C   . VAL B 24  ? 0.2489 0.3021 0.3632 0.0001  -0.0102 0.0170  24  VAL B C   
1121 O O   . VAL B 24  ? 0.2843 0.3394 0.4036 0.0024  -0.0108 0.0172  24  VAL B O   
1122 C CB  . VAL B 24  ? 0.2621 0.3191 0.3846 -0.0056 -0.0133 0.0196  24  VAL B CB  
1123 C CG1 . VAL B 24  ? 0.2459 0.3039 0.3721 -0.0052 -0.0195 0.0206  24  VAL B CG1 
1124 C CG2 . VAL B 24  ? 0.1976 0.2596 0.3296 -0.0082 -0.0113 0.0210  24  VAL B CG2 
1125 N N   . ALA B 25  ? 0.2049 0.2521 0.3074 -0.0005 -0.0112 0.0161  25  ALA B N   
1126 C CA  . ALA B 25  ? 0.2866 0.3295 0.3815 0.0014  -0.0129 0.0150  25  ALA B CA  
1127 C C   . ALA B 25  ? 0.2634 0.3032 0.3506 0.0029  -0.0087 0.0130  25  ALA B C   
1128 O O   . ALA B 25  ? 0.2219 0.2592 0.3050 0.0048  -0.0092 0.0121  25  ALA B O   
1129 C CB  . ALA B 25  ? 0.2284 0.2669 0.3160 -0.0003 -0.0179 0.0152  25  ALA B CB  
1130 N N   . GLY B 26  ? 0.2439 0.2838 0.3289 0.0020  -0.0049 0.0125  26  GLY B N   
1131 C CA  . GLY B 26  ? 0.2185 0.2555 0.2958 0.0032  -0.0016 0.0108  26  GLY B CA  
1132 C C   . GLY B 26  ? 0.2748 0.3063 0.3419 0.0027  -0.0040 0.0103  26  GLY B C   
1133 O O   . GLY B 26  ? 0.2097 0.2393 0.2752 0.0012  -0.0078 0.0111  26  GLY B O   
1134 N N   . GLN B 27  ? 0.2232 0.2521 0.2835 0.0039  -0.0018 0.0087  27  GLN B N   
1135 C CA  . GLN B 27  ? 0.1986 0.2227 0.2498 0.0036  -0.0035 0.0082  27  GLN B CA  
1136 C C   . GLN B 27  ? 0.2324 0.2549 0.2786 0.0055  -0.0016 0.0062  27  GLN B C   
1137 O O   . GLN B 27  ? 0.1902 0.2149 0.2394 0.0068  0.0011  0.0052  27  GLN B O   
1138 C CB  . GLN B 27  ? 0.2049 0.2276 0.2529 0.0017  -0.0029 0.0091  27  GLN B CB  
1139 C CG  . GLN B 27  ? 0.1941 0.2184 0.2414 0.0016  0.0016  0.0090  27  GLN B CG  
1140 C CD  . GLN B 27  ? 0.2376 0.2610 0.2835 -0.0006 0.0023  0.0107  27  GLN B CD  
1141 O OE1 . GLN B 27  ? 0.1647 0.1842 0.2038 -0.0011 0.0014  0.0110  27  GLN B OE1 
1142 N NE2 . GLN B 27  ? 0.2068 0.2340 0.2597 -0.0021 0.0040  0.0121  27  GLN B NE2 
1143 N N   . ARG B 28  ? 0.2037 0.2224 0.2426 0.0056  -0.0031 0.0057  28  ARG B N   
1144 C CA  . ARG B 28  ? 0.2206 0.2376 0.2545 0.0071  -0.0020 0.0039  28  ARG B CA  
1145 C C   . ARG B 28  ? 0.2339 0.2512 0.2643 0.0069  0.0011  0.0033  28  ARG B C   
1146 O O   . ARG B 28  ? 0.2009 0.2172 0.2286 0.0056  0.0012  0.0045  28  ARG B O   
1147 C CB  . ARG B 28  ? 0.2148 0.2282 0.2430 0.0071  -0.0046 0.0037  28  ARG B CB  
1148 C CG  . ARG B 28  ? 0.2923 0.3041 0.3159 0.0085  -0.0039 0.0020  28  ARG B CG  
1149 C CD  . ARG B 28  ? 0.2449 0.2542 0.2658 0.0089  -0.0064 0.0017  28  ARG B CD  
1150 N NE  . ARG B 28  ? 0.4116 0.4213 0.4359 0.0088  -0.0083 0.0026  28  ARG B NE  
1151 C CZ  . ARG B 28  ? 0.4656 0.4733 0.4880 0.0082  -0.0107 0.0032  28  ARG B CZ  
1152 N NH1 . ARG B 28  ? 0.4039 0.4090 0.4218 0.0077  -0.0115 0.0030  28  ARG B NH1 
1153 N NH2 . ARG B 28  ? 0.2801 0.2883 0.3051 0.0080  -0.0125 0.0040  28  ARG B NH2 
1154 N N   . PHE B 29  ? 0.1820 0.2000 0.2117 0.0081  0.0034  0.0015  29  PHE B N   
1155 C CA  . PHE B 29  ? 0.1903 0.2079 0.2147 0.0080  0.0057  0.0006  29  PHE B CA  
1156 C C   . PHE B 29  ? 0.2114 0.2270 0.2310 0.0091  0.0049  -0.0013 29  PHE B C   
1157 O O   . PHE B 29  ? 0.1931 0.2085 0.2150 0.0102  0.0041  -0.0025 29  PHE B O   
1158 C CB  . PHE B 29  ? 0.1721 0.1927 0.1995 0.0081  0.0098  -0.0003 29  PHE B CB  
1159 C CG  . PHE B 29  ? 0.1881 0.2113 0.2206 0.0068  0.0111  0.0017  29  PHE B CG  
1160 C CD1 . PHE B 29  ? 0.1939 0.2195 0.2347 0.0070  0.0103  0.0025  29  PHE B CD1 
1161 C CD2 . PHE B 29  ? 0.1926 0.2158 0.2217 0.0053  0.0128  0.0032  29  PHE B CD2 
1162 C CE1 . PHE B 29  ? 0.1979 0.2262 0.2442 0.0056  0.0112  0.0044  29  PHE B CE1 
1163 C CE2 . PHE B 29  ? 0.2004 0.2260 0.2349 0.0038  0.0141  0.0052  29  PHE B CE2 
1164 C CZ  . PHE B 29  ? 0.2024 0.2309 0.2459 0.0039  0.0132  0.0057  29  PHE B CZ  
1165 N N   . VAL B 30  ? 0.2064 0.2205 0.2196 0.0088  0.0048  -0.0014 30  VAL B N   
1166 C CA  . VAL B 30  ? 0.1849 0.1975 0.1939 0.0096  0.0037  -0.0031 30  VAL B CA  
1167 C C   . VAL B 30  ? 0.1994 0.2123 0.2034 0.0094  0.0057  -0.0044 30  VAL B C   
1168 O O   . VAL B 30  ? 0.2153 0.2281 0.2157 0.0085  0.0065  -0.0029 30  VAL B O   
1169 C CB  . VAL B 30  ? 0.2320 0.2422 0.2380 0.0096  0.0006  -0.0019 30  VAL B CB  
1170 C CG1 . VAL B 30  ? 0.2148 0.2241 0.2177 0.0104  -0.0006 -0.0036 30  VAL B CG1 
1171 C CG2 . VAL B 30  ? 0.1557 0.1653 0.1657 0.0096  -0.0012 -0.0009 30  VAL B CG2 
1172 N N   . ILE B 31  ? 0.2131 0.2263 0.2168 0.0102  0.0066  -0.0071 31  ILE B N   
1173 C CA  . ILE B 31  ? 0.1953 0.2088 0.1942 0.0100  0.0089  -0.0090 31  ILE B CA  
1174 C C   . ILE B 31  ? 0.1912 0.2034 0.1852 0.0102  0.0065  -0.0105 31  ILE B C   
1175 O O   . ILE B 31  ? 0.1829 0.1944 0.1794 0.0108  0.0048  -0.0116 31  ILE B O   
1176 C CB  . ILE B 31  ? 0.1770 0.1918 0.1797 0.0106  0.0121  -0.0116 31  ILE B CB  
1177 C CG1 . ILE B 31  ? 0.2613 0.2783 0.2700 0.0105  0.0145  -0.0102 31  ILE B CG1 
1178 C CG2 . ILE B 31  ? 0.2076 0.2222 0.2042 0.0103  0.0142  -0.0144 31  ILE B CG2 
1179 C CD1 . ILE B 31  ? 0.2711 0.2888 0.2784 0.0092  0.0147  -0.0071 31  ILE B CD1 
1180 N N   . ASP B 32  ? 0.2066 0.2184 0.1938 0.0095  0.0065  -0.0103 32  ASP B N   
1181 C CA  . ASP B 32  ? 0.1949 0.2060 0.1771 0.0095  0.0047  -0.0123 32  ASP B CA  
1182 C C   . ASP B 32  ? 0.2125 0.2240 0.1898 0.0089  0.0075  -0.0148 32  ASP B C   
1183 O O   . ASP B 32  ? 0.1974 0.2095 0.1720 0.0083  0.0101  -0.0136 32  ASP B O   
1184 C CB  . ASP B 32  ? 0.1856 0.1958 0.1628 0.0092  0.0016  -0.0100 32  ASP B CB  
1185 C CG  . ASP B 32  ? 0.2643 0.2737 0.2453 0.0097  -0.0006 -0.0074 32  ASP B CG  
1186 O OD1 . ASP B 32  ? 0.2172 0.2266 0.2036 0.0104  -0.0012 -0.0081 32  ASP B OD1 
1187 O OD2 . ASP B 32  ? 0.2405 0.2490 0.2187 0.0094  -0.0018 -0.0046 32  ASP B OD2 
1188 N N   . VAL B 33  ? 0.2349 0.2460 0.2109 0.0091  0.0070  -0.0182 33  VAL B N   
1189 C CA  . VAL B 33  ? 0.2325 0.2435 0.2022 0.0084  0.0091  -0.0212 33  VAL B CA  
1190 C C   . VAL B 33  ? 0.2564 0.2667 0.2204 0.0079  0.0056  -0.0225 33  VAL B C   
1191 O O   . VAL B 33  ? 0.2397 0.2498 0.2074 0.0082  0.0027  -0.0232 33  VAL B O   
1192 C CB  . VAL B 33  ? 0.2364 0.2473 0.2102 0.0090  0.0125  -0.0249 33  VAL B CB  
1193 C CG1 . VAL B 33  ? 0.2229 0.2333 0.1890 0.0082  0.0153  -0.0283 33  VAL B CG1 
1194 C CG2 . VAL B 33  ? 0.2571 0.2691 0.2387 0.0098  0.0152  -0.0234 33  VAL B CG2 
1195 N N   . THR B 34  ? 0.2171 0.2272 0.1723 0.0069  0.0057  -0.0228 34  THR B N   
1196 C CA  . THR B 34  ? 0.2816 0.2913 0.2308 0.0062  0.0023  -0.0245 34  THR B CA  
1197 C C   . THR B 34  ? 0.2661 0.2751 0.2081 0.0052  0.0049  -0.0284 34  THR B C   
1198 O O   . THR B 34  ? 0.2734 0.2825 0.2104 0.0048  0.0083  -0.0276 34  THR B O   
1199 C CB  . THR B 34  ? 0.3140 0.3238 0.2581 0.0058  -0.0013 -0.0206 34  THR B CB  
1200 O OG1 . THR B 34  ? 0.2520 0.2620 0.2027 0.0068  -0.0034 -0.0174 34  THR B OG1 
1201 C CG2 . THR B 34  ? 0.2834 0.2932 0.2221 0.0052  -0.0055 -0.0224 34  THR B CG2 
1202 N N   . VAL B 35  ? 0.2211 0.2293 0.1629 0.0049  0.0037  -0.0327 35  VAL B N   
1203 C CA  . VAL B 35  ? 0.2293 0.2364 0.1648 0.0040  0.0062  -0.0374 35  VAL B CA  
1204 C C   . VAL B 35  ? 0.3271 0.3339 0.2547 0.0027  0.0017  -0.0390 35  VAL B C   
1205 O O   . VAL B 35  ? 0.2602 0.2671 0.1918 0.0026  -0.0022 -0.0400 35  VAL B O   
1206 C CB  . VAL B 35  ? 0.2660 0.2720 0.2087 0.0047  0.0088  -0.0417 35  VAL B CB  
1207 C CG1 . VAL B 35  ? 0.2661 0.2705 0.2018 0.0039  0.0118  -0.0469 35  VAL B CG1 
1208 C CG2 . VAL B 35  ? 0.2435 0.2502 0.1949 0.0062  0.0125  -0.0397 35  VAL B CG2 
1209 N N   . TRP B 36  ? 0.2875 0.2938 0.2039 0.0015  0.0023  -0.0393 36  TRP B N   
1210 C CA  . TRP B 36  ? 0.2847 0.2906 0.1923 0.0000  -0.0020 -0.0411 36  TRP B CA  
1211 C C   . TRP B 36  ? 0.3234 0.3275 0.2271 -0.0009 0.0001  -0.0477 36  TRP B C   
1212 O O   . TRP B 36  ? 0.2945 0.2975 0.1937 -0.0010 0.0054  -0.0500 36  TRP B O   
1213 C CB  . TRP B 36  ? 0.2945 0.3007 0.1911 -0.0008 -0.0030 -0.0374 36  TRP B CB  
1214 C CG  . TRP B 36  ? 0.3388 0.3463 0.2388 0.0000  -0.0069 -0.0313 36  TRP B CG  
1215 C CD1 . TRP B 36  ? 0.3254 0.3338 0.2250 -0.0002 -0.0132 -0.0295 36  TRP B CD1 
1216 C CD2 . TRP B 36  ? 0.2783 0.2862 0.1832 0.0011  -0.0047 -0.0266 36  TRP B CD2 
1217 N NE1 . TRP B 36  ? 0.3038 0.3130 0.2078 0.0010  -0.0147 -0.0240 36  TRP B NE1 
1218 C CE2 . TRP B 36  ? 0.2626 0.2712 0.1696 0.0016  -0.0097 -0.0222 36  TRP B CE2 
1219 C CE3 . TRP B 36  ? 0.2634 0.2712 0.1718 0.0016  0.0009  -0.0257 36  TRP B CE3 
1220 C CZ2 . TRP B 36  ? 0.3109 0.3196 0.2225 0.0026  -0.0091 -0.0173 36  TRP B CZ2 
1221 C CZ3 . TRP B 36  ? 0.3273 0.3356 0.2405 0.0023  0.0011  -0.0206 36  TRP B CZ3 
1222 C CH2 . TRP B 36  ? 0.3086 0.3171 0.2230 0.0028  -0.0038 -0.0166 36  TRP B CH2 
1223 N N   . ILE B 37  ? 0.2976 0.3013 0.2035 -0.0017 -0.0038 -0.0510 37  ILE B N   
1224 C CA  . ILE B 37  ? 0.3183 0.3197 0.2234 -0.0025 -0.0021 -0.0577 37  ILE B CA  
1225 C C   . ILE B 37  ? 0.4394 0.4408 0.3438 -0.0040 -0.0083 -0.0600 37  ILE B C   
1226 O O   . ILE B 37  ? 0.3747 0.3781 0.2859 -0.0037 -0.0127 -0.0569 37  ILE B O   
1227 C CB  . ILE B 37  ? 0.2717 0.2721 0.1885 -0.0009 0.0021  -0.0593 37  ILE B CB  
1228 C CG1 . ILE B 37  ? 0.3294 0.3268 0.2466 -0.0017 0.0034  -0.0662 37  ILE B CG1 
1229 C CG2 . ILE B 37  ? 0.3026 0.3046 0.2310 0.0002  -0.0007 -0.0555 37  ILE B CG2 
1230 C CD1 . ILE B 37  ? 0.3751 0.3709 0.3012 0.0000  0.0091  -0.0682 37  ILE B CD1 
1231 N N   . ASP B 38  ? 0.3697 0.3690 0.2663 -0.0058 -0.0087 -0.0657 38  ASP B N   
1232 C CA  . ASP B 38  ? 0.3983 0.3977 0.2946 -0.0076 -0.0147 -0.0685 38  ASP B CA  
1233 C C   . ASP B 38  ? 0.3861 0.3847 0.2952 -0.0072 -0.0147 -0.0708 38  ASP B C   
1234 O O   . ASP B 38  ? 0.3464 0.3422 0.2586 -0.0069 -0.0101 -0.0749 38  ASP B O   
1235 C CB  . ASP B 38  ? 0.4510 0.4481 0.3346 -0.0098 -0.0153 -0.0741 38  ASP B CB  
1236 C CG  . ASP B 38  ? 0.5858 0.5842 0.4663 -0.0120 -0.0231 -0.0753 38  ASP B CG  
1237 O OD1 . ASP B 38  ? 0.5528 0.5537 0.4428 -0.0117 -0.0275 -0.0726 38  ASP B OD1 
1238 O OD2 . ASP B 38  ? 0.6658 0.6628 0.5342 -0.0140 -0.0248 -0.0791 38  ASP B OD2 
1239 N N   . LEU B 39  ? 0.3219 0.3230 0.2388 -0.0074 -0.0196 -0.0682 39  LEU B N   
1240 C CA  . LEU B 39  ? 0.2802 0.2809 0.2097 -0.0071 -0.0196 -0.0693 39  LEU B CA  
1241 C C   . LEU B 39  ? 0.3209 0.3212 0.2518 -0.0095 -0.0244 -0.0735 39  LEU B C   
1242 O O   . LEU B 39  ? 0.3078 0.3077 0.2491 -0.0097 -0.0247 -0.0745 39  LEU B O   
1243 C CB  . LEU B 39  ? 0.2926 0.2963 0.2311 -0.0055 -0.0208 -0.0632 39  LEU B CB  
1244 C CG  . LEU B 39  ? 0.2624 0.2662 0.2019 -0.0032 -0.0162 -0.0591 39  LEU B CG  
1245 C CD1 . LEU B 39  ? 0.2373 0.2439 0.1852 -0.0018 -0.0180 -0.0536 39  LEU B CD1 
1246 C CD2 . LEU B 39  ? 0.2692 0.2702 0.2131 -0.0024 -0.0106 -0.0620 39  LEU B CD2 
1247 N N   . ALA B 40  ? 0.2918 0.2923 0.2124 -0.0115 -0.0282 -0.0760 40  ALA B N   
1248 C CA  . ALA B 40  ? 0.3428 0.3433 0.2649 -0.0141 -0.0333 -0.0801 40  ALA B CA  
1249 C C   . ALA B 40  ? 0.3797 0.3758 0.3058 -0.0151 -0.0302 -0.0863 40  ALA B C   
1250 O O   . ALA B 40  ? 0.3654 0.3615 0.3002 -0.0164 -0.0327 -0.0881 40  ALA B O   
1251 C CB  . ALA B 40  ? 0.3950 0.3962 0.3038 -0.0162 -0.0379 -0.0818 40  ALA B CB  
1252 N N   . GLU B 41  ? 0.3749 0.3672 0.2951 -0.0144 -0.0245 -0.0896 41  GLU B N   
1253 C CA  . GLU B 41  ? 0.3647 0.3521 0.2884 -0.0151 -0.0214 -0.0959 41  GLU B CA  
1254 C C   . GLU B 41  ? 0.3551 0.3421 0.2939 -0.0137 -0.0194 -0.0937 41  GLU B C   
1255 O O   . GLU B 41  ? 0.3655 0.3504 0.3113 -0.0152 -0.0208 -0.0970 41  GLU B O   
1256 C CB  . GLU B 41  ? 0.3807 0.3646 0.2963 -0.0141 -0.0150 -0.0993 41  GLU B CB  
1257 C CG  . GLU B 41  ? 0.4778 0.4563 0.3984 -0.0140 -0.0107 -0.1054 41  GLU B CG  
1258 C CD  . GLU B 41  ? 0.6366 0.6116 0.5480 -0.0133 -0.0046 -0.1099 41  GLU B CD  
1259 O OE1 . GLU B 41  ? 0.6427 0.6195 0.5429 -0.0131 -0.0038 -0.1084 41  GLU B OE1 
1260 O OE2 . GLU B 41  ? 0.7512 0.7216 0.6666 -0.0129 -0.0006 -0.1150 41  GLU B OE2 
1261 N N   . ALA B 42  ? 0.3029 0.2919 0.2465 -0.0111 -0.0165 -0.0881 42  ALA B N   
1262 C CA  . ALA B 42  ? 0.2811 0.2700 0.2379 -0.0097 -0.0147 -0.0854 42  ALA B CA  
1263 C C   . ALA B 42  ? 0.3078 0.2992 0.2724 -0.0112 -0.0199 -0.0836 42  ALA B C   
1264 O O   . ALA B 42  ? 0.3374 0.3271 0.3117 -0.0116 -0.0193 -0.0843 42  ALA B O   
1265 C CB  . ALA B 42  ? 0.2855 0.2765 0.2444 -0.0069 -0.0115 -0.0795 42  ALA B CB  
1266 N N   . ALA B 43  ? 0.3394 0.3350 0.3003 -0.0120 -0.0248 -0.0810 43  ALA B N   
1267 C CA  . ALA B 43  ? 0.3556 0.3542 0.3245 -0.0135 -0.0296 -0.0796 43  ALA B CA  
1268 C C   . ALA B 43  ? 0.4078 0.4042 0.3773 -0.0166 -0.0324 -0.0856 43  ALA B C   
1269 O O   . ALA B 43  ? 0.3496 0.3466 0.3289 -0.0179 -0.0342 -0.0857 43  ALA B O   
1270 C CB  . ALA B 43  ? 0.3028 0.3066 0.2682 -0.0133 -0.0343 -0.0754 43  ALA B CB  
1271 N N   . ASN B 44  ? 0.3460 0.3396 0.3050 -0.0180 -0.0326 -0.0909 44  ASN B N   
1272 C CA  . ASN B 44  ? 0.4011 0.3918 0.3601 -0.0211 -0.0352 -0.0973 44  ASN B CA  
1273 C C   . ASN B 44  ? 0.4119 0.3975 0.3795 -0.0210 -0.0308 -0.1003 44  ASN B C   
1274 O O   . ASN B 44  ? 0.4095 0.3942 0.3857 -0.0230 -0.0329 -0.1020 44  ASN B O   
1275 C CB  . ASN B 44  ? 0.4166 0.4050 0.3609 -0.0225 -0.0359 -0.1024 44  ASN B CB  
1276 C CG  . ASN B 44  ? 0.5723 0.5572 0.5153 -0.0260 -0.0388 -0.1098 44  ASN B CG  
1277 O OD1 . ASN B 44  ? 0.5922 0.5784 0.5441 -0.0281 -0.0427 -0.1102 44  ASN B OD1 
1278 N ND2 . ASN B 44  ? 0.5938 0.5741 0.5258 -0.0267 -0.0366 -0.1157 44  ASN B ND2 
1279 N N   . SER B 45  ? 0.4017 0.3838 0.3678 -0.0185 -0.0246 -0.1005 45  SER B N   
1280 C CA  . SER B 45  ? 0.3209 0.2977 0.2946 -0.0180 -0.0203 -0.1033 45  SER B CA  
1281 C C   . SER B 45  ? 0.3536 0.3317 0.3401 -0.0165 -0.0189 -0.0978 45  SER B C   
1282 O O   . SER B 45  ? 0.3305 0.3046 0.3255 -0.0170 -0.0173 -0.0995 45  SER B O   
1283 C CB  . SER B 45  ? 0.3867 0.3598 0.3545 -0.0158 -0.0142 -0.1057 45  SER B CB  
1284 O OG  . SER B 45  ? 0.3083 0.2846 0.2764 -0.0127 -0.0114 -0.0997 45  SER B OG  
1285 N N   . ASP B 46  ? 0.2939 0.2768 0.2815 -0.0146 -0.0193 -0.0914 46  ASP B N   
1286 C CA  . ASP B 46  ? 0.3372 0.3211 0.3348 -0.0127 -0.0171 -0.0860 46  ASP B CA  
1287 C C   . ASP B 46  ? 0.3513 0.3306 0.3518 -0.0105 -0.0114 -0.0867 46  ASP B C   
1288 O O   . ASP B 46  ? 0.3305 0.3084 0.3403 -0.0097 -0.0096 -0.0843 46  ASP B O   
1289 C CB  . ASP B 46  ? 0.3080 0.2927 0.3157 -0.0147 -0.0199 -0.0851 46  ASP B CB  
1290 C CG  . ASP B 46  ? 0.2871 0.2748 0.3028 -0.0130 -0.0190 -0.0784 46  ASP B CG  
1291 O OD1 . ASP B 46  ? 0.2687 0.2597 0.2812 -0.0110 -0.0185 -0.0742 46  ASP B OD1 
1292 O OD2 . ASP B 46  ? 0.3126 0.2992 0.3376 -0.0140 -0.0188 -0.0773 46  ASP B OD2 
1293 N N   A ASP B 47  ? 0.3249 0.3021 0.3174 -0.0095 -0.0084 -0.0899 47  ASP B N   
1294 N N   B ASP B 47  ? 0.3244 0.3017 0.3169 -0.0095 -0.0085 -0.0898 47  ASP B N   
1295 C CA  A ASP B 47  ? 0.3380 0.3111 0.3331 -0.0073 -0.0028 -0.0913 47  ASP B CA  
1296 C CA  B ASP B 47  ? 0.3379 0.3109 0.3330 -0.0073 -0.0029 -0.0913 47  ASP B CA  
1297 C C   A ASP B 47  ? 0.3218 0.2978 0.3139 -0.0045 0.0001  -0.0870 47  ASP B C   
1298 C C   B ASP B 47  ? 0.3217 0.2977 0.3139 -0.0045 0.0001  -0.0870 47  ASP B C   
1299 O O   A ASP B 47  ? 0.3214 0.2997 0.3039 -0.0045 -0.0002 -0.0872 47  ASP B O   
1300 O O   B ASP B 47  ? 0.3206 0.2989 0.3034 -0.0046 -0.0003 -0.0872 47  ASP B O   
1301 C CB  A ASP B 47  ? 0.3317 0.2999 0.3206 -0.0082 -0.0009 -0.0989 47  ASP B CB  
1302 C CB  B ASP B 47  ? 0.3319 0.3001 0.3212 -0.0085 -0.0014 -0.0990 47  ASP B CB  
1303 C CG  A ASP B 47  ? 0.3493 0.3129 0.3436 -0.0106 -0.0025 -0.1036 47  ASP B CG  
1304 C CG  B ASP B 47  ? 0.3539 0.3177 0.3461 -0.0061 0.0045  -0.1013 47  ASP B CG  
1305 O OD1 A ASP B 47  ? 0.3874 0.3498 0.3923 -0.0105 -0.0026 -0.1010 47  ASP B OD1 
1306 O OD1 B ASP B 47  ? 0.3487 0.3143 0.3432 -0.0034 0.0076  -0.0971 47  ASP B OD1 
1307 O OD2 A ASP B 47  ? 0.3449 0.3058 0.3324 -0.0127 -0.0037 -0.1099 47  ASP B OD2 
1308 O OD2 B ASP B 47  ? 0.3483 0.3067 0.3403 -0.0070 0.0059  -0.1075 47  ASP B OD2 
1309 N N   . LEU B 48  ? 0.3112 0.2870 0.3114 -0.0022 0.0028  -0.0830 48  LEU B N   
1310 C CA  . LEU B 48  ? 0.3270 0.3057 0.3258 0.0003  0.0054  -0.0787 48  LEU B CA  
1311 C C   . LEU B 48  ? 0.2796 0.2573 0.2707 0.0012  0.0091  -0.0821 48  LEU B C   
1312 O O   . LEU B 48  ? 0.2977 0.2787 0.2832 0.0020  0.0099  -0.0794 48  LEU B O   
1313 C CB  . LEU B 48  ? 0.3127 0.2904 0.3217 0.0024  0.0077  -0.0749 48  LEU B CB  
1314 C CG  . LEU B 48  ? 0.3611 0.3415 0.3711 0.0049  0.0102  -0.0702 48  LEU B CG  
1315 C CD1 . LEU B 48  ? 0.2554 0.2408 0.2607 0.0048  0.0077  -0.0656 48  LEU B CD1 
1316 C CD2 . LEU B 48  ? 0.2742 0.2531 0.2945 0.0067  0.0118  -0.0671 48  LEU B CD2 
1317 N N   . ALA B 49  ? 0.3412 0.3143 0.3317 0.0009  0.0116  -0.0881 49  ALA B N   
1318 C CA  . ALA B 49  ? 0.3764 0.3483 0.3595 0.0017  0.0157  -0.0921 49  ALA B CA  
1319 C C   . ALA B 49  ? 0.3534 0.3280 0.3236 0.0000  0.0136  -0.0929 49  ALA B C   
1320 O O   . ALA B 49  ? 0.3335 0.3089 0.2968 0.0009  0.0172  -0.0937 49  ALA B O   
1321 C CB  . ALA B 49  ? 0.3568 0.3227 0.3411 0.0013  0.0182  -0.0992 49  ALA B CB  
1322 N N   . ASP B 50  ? 0.3607 0.3370 0.3277 -0.0023 0.0081  -0.0923 50  ASP B N   
1323 C CA  . ASP B 50  ? 0.3429 0.3215 0.2977 -0.0039 0.0055  -0.0929 50  ASP B CA  
1324 C C   . ASP B 50  ? 0.2682 0.2518 0.2207 -0.0030 0.0041  -0.0861 50  ASP B C   
1325 O O   . ASP B 50  ? 0.3521 0.3379 0.2948 -0.0042 0.0016  -0.0856 50  ASP B O   
1326 C CB  . ASP B 50  ? 0.3080 0.2861 0.2604 -0.0070 -0.0002 -0.0959 50  ASP B CB  
1327 C CG  . ASP B 50  ? 0.3503 0.3229 0.3006 -0.0085 0.0010  -0.1038 50  ASP B CG  
1328 O OD1 . ASP B 50  ? 0.3771 0.3469 0.3233 -0.0074 0.0062  -0.1075 50  ASP B OD1 
1329 O OD2 . ASP B 50  ? 0.3907 0.3617 0.3443 -0.0107 -0.0029 -0.1065 50  ASP B OD2 
1330 N N   . THR B 51  ? 0.3271 0.3126 0.2883 -0.0010 0.0055  -0.0809 51  THR B N   
1331 C CA  . THR B 51  ? 0.2857 0.2753 0.2451 0.0000  0.0046  -0.0747 51  THR B CA  
1332 C C   . THR B 51  ? 0.2802 0.2703 0.2439 0.0024  0.0098  -0.0722 51  THR B C   
1333 O O   . THR B 51  ? 0.2727 0.2601 0.2408 0.0035  0.0138  -0.0752 51  THR B O   
1334 C CB  . THR B 51  ? 0.2977 0.2899 0.2634 -0.0004 -0.0001 -0.0703 51  THR B CB  
1335 O OG1 . THR B 51  ? 0.2665 0.2624 0.2293 0.0004  -0.0013 -0.0650 51  THR B OG1 
1336 C CG2 . THR B 51  ? 0.2715 0.2626 0.2492 0.0009  0.0013  -0.0687 51  THR B CG2 
1337 N N   . TYR B 52  ? 0.2549 0.2482 0.2175 0.0033  0.0095  -0.0669 52  TYR B N   
1338 C CA  . TYR B 52  ? 0.2861 0.2805 0.2540 0.0054  0.0136  -0.0638 52  TYR B CA  
1339 C C   . TYR B 52  ? 0.3031 0.2981 0.2817 0.0064  0.0121  -0.0600 52  TYR B C   
1340 O O   . TYR B 52  ? 0.2795 0.2766 0.2589 0.0060  0.0083  -0.0563 52  TYR B O   
1341 C CB  . TYR B 52  ? 0.2727 0.2700 0.2341 0.0055  0.0142  -0.0600 52  TYR B CB  
1342 C CG  . TYR B 52  ? 0.2855 0.2838 0.2500 0.0072  0.0194  -0.0584 52  TYR B CG  
1343 C CD1 . TYR B 52  ? 0.3007 0.2998 0.2756 0.0089  0.0203  -0.0553 52  TYR B CD1 
1344 C CD2 . TYR B 52  ? 0.2872 0.2860 0.2442 0.0070  0.0232  -0.0597 52  TYR B CD2 
1345 C CE1 . TYR B 52  ? 0.2702 0.2707 0.2487 0.0103  0.0246  -0.0537 52  TYR B CE1 
1346 C CE2 . TYR B 52  ? 0.3397 0.3399 0.3004 0.0085  0.0280  -0.0580 52  TYR B CE2 
1347 C CZ  . TYR B 52  ? 0.3051 0.3063 0.2770 0.0101  0.0285  -0.0551 52  TYR B CZ  
1348 O OH  . TYR B 52  ? 0.2859 0.2891 0.2625 0.0114  0.0330  -0.0534 52  TYR B OH  
1349 N N   . ASP B 53  ? 0.2494 0.2425 0.2362 0.0078  0.0150  -0.0609 53  ASP B N   
1350 C CA  . ASP B 53  ? 0.2617 0.2548 0.2581 0.0087  0.0136  -0.0575 53  ASP B CA  
1351 C C   . ASP B 53  ? 0.2132 0.2096 0.2114 0.0097  0.0132  -0.0518 53  ASP B C   
1352 O O   . ASP B 53  ? 0.2695 0.2671 0.2680 0.0109  0.0163  -0.0506 53  ASP B O   
1353 C CB  . ASP B 53  ? 0.2816 0.2717 0.2859 0.0101  0.0168  -0.0597 53  ASP B CB  
1354 C CG  . ASP B 53  ? 0.2911 0.2807 0.3047 0.0108  0.0153  -0.0562 53  ASP B CG  
1355 O OD1 . ASP B 53  ? 0.2451 0.2369 0.2591 0.0102  0.0121  -0.0523 53  ASP B OD1 
1356 O OD2 . ASP B 53  ? 0.3230 0.3098 0.3435 0.0119  0.0173  -0.0574 53  ASP B OD2 
1357 N N   . TYR B 54  ? 0.2261 0.2240 0.2256 0.0091  0.0095  -0.0484 54  TYR B N   
1358 C CA  . TYR B 54  ? 0.2585 0.2590 0.2588 0.0099  0.0089  -0.0433 54  TYR B CA  
1359 C C   . TYR B 54  ? 0.2401 0.2404 0.2484 0.0115  0.0108  -0.0409 54  TYR B C   
1360 O O   . TYR B 54  ? 0.2286 0.2310 0.2378 0.0122  0.0111  -0.0373 54  TYR B O   
1361 C CB  . TYR B 54  ? 0.2386 0.2406 0.2381 0.0091  0.0047  -0.0405 54  TYR B CB  
1362 C CG  . TYR B 54  ? 0.2359 0.2369 0.2417 0.0088  0.0028  -0.0403 54  TYR B CG  
1363 C CD1 . TYR B 54  ? 0.2938 0.2938 0.3068 0.0098  0.0040  -0.0384 54  TYR B CD1 
1364 C CD2 . TYR B 54  ? 0.2912 0.2925 0.2959 0.0073  -0.0002 -0.0416 54  TYR B CD2 
1365 C CE1 . TYR B 54  ? 0.3330 0.3318 0.3512 0.0093  0.0025  -0.0379 54  TYR B CE1 
1366 C CE2 . TYR B 54  ? 0.2751 0.2756 0.2859 0.0068  -0.0016 -0.0413 54  TYR B CE2 
1367 C CZ  . TYR B 54  ? 0.3437 0.3429 0.3609 0.0078  0.0000  -0.0393 54  TYR B CZ  
1368 O OH  . TYR B 54  ? 0.3212 0.3194 0.3441 0.0071  -0.0011 -0.0387 54  TYR B OH  
1369 N N   . VAL B 55  ? 0.2080 0.2059 0.2225 0.0121  0.0119  -0.0427 55  VAL B N   
1370 C CA  . VAL B 55  ? 0.2429 0.2405 0.2651 0.0137  0.0136  -0.0405 55  VAL B CA  
1371 C C   . VAL B 55  ? 0.2559 0.2545 0.2782 0.0149  0.0174  -0.0414 55  VAL B C   
1372 O O   . VAL B 55  ? 0.2173 0.2180 0.2429 0.0160  0.0182  -0.0381 55  VAL B O   
1373 C CB  . VAL B 55  ? 0.2107 0.2049 0.2393 0.0140  0.0137  -0.0421 55  VAL B CB  
1374 C CG1 . VAL B 55  ? 0.2357 0.2294 0.2724 0.0159  0.0153  -0.0397 55  VAL B CG1 
1375 C CG2 . VAL B 55  ? 0.2482 0.2418 0.2774 0.0127  0.0103  -0.0407 55  VAL B CG2 
1376 N N   . ARG B 56  ? 0.2265 0.2238 0.2449 0.0147  0.0199  -0.0459 56  ARG B N   
1377 C CA  . ARG B 56  ? 0.2662 0.2647 0.2841 0.0157  0.0242  -0.0472 56  ARG B CA  
1378 C C   . ARG B 56  ? 0.3026 0.3046 0.3155 0.0152  0.0239  -0.0438 56  ARG B C   
1379 O O   . ARG B 56  ? 0.2878 0.2920 0.3043 0.0162  0.0262  -0.0418 56  ARG B O   
1380 C CB  . ARG B 56  ? 0.2766 0.2729 0.2890 0.0152  0.0266  -0.0530 56  ARG B CB  
1381 C CG  . ARG B 56  ? 0.4105 0.4085 0.4184 0.0155  0.0310  -0.0545 56  ARG B CG  
1382 C CD  . ARG B 56  ? 0.4611 0.4565 0.4654 0.0155  0.0347  -0.0608 56  ARG B CD  
1383 N NE  . ARG B 56  ? 0.5591 0.5528 0.5526 0.0135  0.0332  -0.0644 56  ARG B NE  
1384 C CZ  . ARG B 56  ? 0.6020 0.5962 0.5862 0.0126  0.0359  -0.0671 56  ARG B CZ  
1385 N NH1 . ARG B 56  ? 0.6376 0.6340 0.6220 0.0137  0.0406  -0.0662 56  ARG B NH1 
1386 N NH2 . ARG B 56  ? 0.3607 0.3531 0.3350 0.0107  0.0339  -0.0703 56  ARG B NH2 
1387 N N   . LEU B 57  ? 0.2539 0.2564 0.2594 0.0136  0.0209  -0.0431 57  LEU B N   
1388 C CA  A LEU B 57  ? 0.2680 0.2732 0.2686 0.0130  0.0204  -0.0398 57  LEU B CA  
1389 C CA  B LEU B 57  ? 0.2671 0.2723 0.2677 0.0130  0.0203  -0.0398 57  LEU B CA  
1390 C C   . LEU B 57  ? 0.2841 0.2911 0.2910 0.0138  0.0194  -0.0350 57  LEU B C   
1391 O O   . LEU B 57  ? 0.2146 0.2238 0.2222 0.0140  0.0213  -0.0329 57  LEU B O   
1392 C CB  A LEU B 57  ? 0.2846 0.2897 0.2776 0.0114  0.0166  -0.0395 57  LEU B CB  
1393 C CB  B LEU B 57  ? 0.2753 0.2803 0.2684 0.0114  0.0165  -0.0395 57  LEU B CB  
1394 C CG  A LEU B 57  ? 0.2742 0.2814 0.2619 0.0108  0.0152  -0.0358 57  LEU B CG  
1395 C CG  B LEU B 57  ? 0.3009 0.3076 0.2859 0.0105  0.0159  -0.0375 57  LEU B CG  
1396 C CD1 A LEU B 57  ? 0.2545 0.2627 0.2374 0.0106  0.0190  -0.0361 57  LEU B CD1 
1397 C CD1 B LEU B 57  ? 0.2315 0.2379 0.2094 0.0100  0.0194  -0.0408 57  LEU B CD1 
1398 C CD2 A LEU B 57  ? 0.2589 0.2657 0.2402 0.0095  0.0111  -0.0360 57  LEU B CD2 
1399 C CD2 B LEU B 57  ? 0.2581 0.2649 0.2389 0.0094  0.0112  -0.0364 57  LEU B CD2 
1400 N N   . ALA B 58  ? 0.2151 0.2213 0.2267 0.0140  0.0164  -0.0333 58  ALA B N   
1401 C CA  . ALA B 58  ? 0.1990 0.2066 0.2154 0.0145  0.0150  -0.0290 58  ALA B CA  
1402 C C   . ALA B 58  ? 0.2355 0.2439 0.2596 0.0160  0.0176  -0.0284 58  ALA B C   
1403 O O   . ALA B 58  ? 0.2486 0.2593 0.2748 0.0162  0.0181  -0.0255 58  ALA B O   
1404 C CB  . ALA B 58  ? 0.1514 0.1577 0.1700 0.0143  0.0116  -0.0277 58  ALA B CB  
1405 N N   . SER B 59  ? 0.1981 0.2047 0.2271 0.0170  0.0192  -0.0309 59  SER B N   
1406 C CA  . SER B 59  ? 0.2908 0.2982 0.3284 0.0186  0.0211  -0.0299 59  SER B CA  
1407 C C   . SER B 59  ? 0.2551 0.2653 0.2930 0.0190  0.0249  -0.0304 59  SER B C   
1408 O O   . SER B 59  ? 0.2566 0.2693 0.3002 0.0197  0.0254  -0.0276 59  SER B O   
1409 C CB  . SER B 59  ? 0.3650 0.3694 0.4078 0.0198  0.0222  -0.0327 59  SER B CB  
1410 O OG  . SER B 59  ? 0.4420 0.4447 0.4804 0.0194  0.0247  -0.0376 59  SER B OG  
1411 N N   . ARG B 60  ? 0.2924 0.3021 0.3240 0.0185  0.0277  -0.0339 60  ARG B N   
1412 C CA  . ARG B 60  ? 0.2802 0.2926 0.3117 0.0187  0.0320  -0.0345 60  ARG B CA  
1413 C C   . ARG B 60  ? 0.2415 0.2569 0.2702 0.0175  0.0309  -0.0305 60  ARG B C   
1414 O O   . ARG B 60  ? 0.2486 0.2670 0.2825 0.0180  0.0330  -0.0286 60  ARG B O   
1415 C CB  . ARG B 60  ? 0.3053 0.3162 0.3294 0.0182  0.0352  -0.0393 60  ARG B CB  
1416 C CG  . ARG B 60  ? 0.2999 0.3073 0.3265 0.0192  0.0363  -0.0439 60  ARG B CG  
1417 C CD  . ARG B 60  ? 0.3562 0.3642 0.3930 0.0215  0.0403  -0.0451 60  ARG B CD  
1418 N NE  . ARG B 60  ? 0.3939 0.4023 0.4405 0.0228  0.0377  -0.0414 60  ARG B NE  
1419 C CZ  . ARG B 60  ? 0.3991 0.4043 0.4499 0.0234  0.0354  -0.0418 60  ARG B CZ  
1420 N NH1 . ARG B 60  ? 0.4095 0.4106 0.4563 0.0229  0.0353  -0.0459 60  ARG B NH1 
1421 N NH2 . ARG B 60  ? 0.4832 0.4889 0.5419 0.0244  0.0329  -0.0379 60  ARG B NH2 
1422 N N   . ALA B 61  ? 0.2185 0.2331 0.2396 0.0160  0.0277  -0.0292 61  ALA B N   
1423 C CA  . ALA B 61  ? 0.2080 0.2245 0.2267 0.0149  0.0265  -0.0253 61  ALA B CA  
1424 C C   . ALA B 61  ? 0.2328 0.2510 0.2599 0.0155  0.0248  -0.0217 61  ALA B C   
1425 O O   . ALA B 61  ? 0.2229 0.2437 0.2525 0.0151  0.0261  -0.0194 61  ALA B O   
1426 C CB  . ALA B 61  ? 0.2268 0.2418 0.2374 0.0136  0.0228  -0.0243 61  ALA B CB  
1427 N N   . ALA B 62  ? 0.2222 0.2389 0.2535 0.0162  0.0219  -0.0212 62  ALA B N   
1428 C CA  . ALA B 62  ? 0.2166 0.2346 0.2551 0.0167  0.0199  -0.0179 62  ALA B CA  
1429 C C   . ALA B 62  ? 0.2536 0.2743 0.3007 0.0179  0.0229  -0.0177 62  ALA B C   
1430 O O   . ALA B 62  ? 0.2142 0.2376 0.2657 0.0176  0.0223  -0.0148 62  ALA B O   
1431 C CB  . ALA B 62  ? 0.2348 0.2503 0.2755 0.0173  0.0168  -0.0177 62  ALA B CB  
1432 N N   . GLU B 63  ? 0.2369 0.2571 0.2872 0.0193  0.0261  -0.0209 63  GLU B N   
1433 C CA  . GLU B 63  ? 0.2840 0.3070 0.3432 0.0207  0.0294  -0.0210 63  GLU B CA  
1434 C C   . GLU B 63  ? 0.2051 0.2317 0.2635 0.0197  0.0322  -0.0199 63  GLU B C   
1435 O O   . GLU B 63  ? 0.2107 0.2410 0.2773 0.0200  0.0328  -0.0176 63  GLU B O   
1436 C CB  . GLU B 63  ? 0.2442 0.2655 0.3057 0.0223  0.0330  -0.0253 63  GLU B CB  
1437 C CG  . GLU B 63  ? 0.3969 0.4154 0.4643 0.0239  0.0310  -0.0256 63  GLU B CG  
1438 C CD  . GLU B 63  ? 0.4531 0.4683 0.5194 0.0248  0.0338  -0.0305 63  GLU B CD  
1439 O OE1 . GLU B 63  ? 0.4654 0.4815 0.5302 0.0251  0.0384  -0.0337 63  GLU B OE1 
1440 O OE2 . GLU B 63  ? 0.4712 0.4827 0.5378 0.0251  0.0315  -0.0312 63  GLU B OE2 
1441 N N   . ILE B 64  ? 0.1763 0.2023 0.2253 0.0183  0.0340  -0.0213 64  ILE B N   
1442 C CA  . ILE B 64  ? 0.2806 0.3097 0.3280 0.0170  0.0368  -0.0199 64  ILE B CA  
1443 C C   . ILE B 64  ? 0.2368 0.2674 0.2861 0.0157  0.0331  -0.0153 64  ILE B C   
1444 O O   . ILE B 64  ? 0.2146 0.2488 0.2706 0.0154  0.0344  -0.0132 64  ILE B O   
1445 C CB  . ILE B 64  ? 0.2402 0.2676 0.2758 0.0156  0.0387  -0.0219 64  ILE B CB  
1446 C CG1 . ILE B 64  ? 0.2132 0.2397 0.2473 0.0167  0.0432  -0.0267 64  ILE B CG1 
1447 C CG2 . ILE B 64  ? 0.1928 0.2227 0.2250 0.0138  0.0405  -0.0192 64  ILE B CG2 
1448 C CD1 . ILE B 64  ? 0.1872 0.2110 0.2084 0.0154  0.0435  -0.0292 64  ILE B CD1 
1449 N N   . VAL B 65  ? 0.2417 0.2696 0.2857 0.0149  0.0285  -0.0140 65  VAL B N   
1450 C CA  . VAL B 65  ? 0.1933 0.2218 0.2378 0.0135  0.0251  -0.0102 65  VAL B CA  
1451 C C   . VAL B 65  ? 0.2457 0.2767 0.3007 0.0142  0.0236  -0.0081 65  VAL B C   
1452 O O   . VAL B 65  ? 0.2161 0.2495 0.2747 0.0130  0.0230  -0.0055 65  VAL B O   
1453 C CB  . VAL B 65  ? 0.2213 0.2463 0.2589 0.0130  0.0208  -0.0097 65  VAL B CB  
1454 C CG1 . VAL B 65  ? 0.2051 0.2303 0.2437 0.0118  0.0174  -0.0062 65  VAL B CG1 
1455 C CG2 . VAL B 65  ? 0.1540 0.1770 0.1817 0.0122  0.0217  -0.0113 65  VAL B CG2 
1456 N N   . ALA B 66  ? 0.2116 0.2418 0.2717 0.0160  0.0226  -0.0091 66  ALA B N   
1457 C CA  . ALA B 66  ? 0.2531 0.2854 0.3231 0.0168  0.0206  -0.0070 66  ALA B CA  
1458 C C   . ALA B 66  ? 0.2787 0.3154 0.3582 0.0178  0.0245  -0.0073 66  ALA B C   
1459 O O   . ALA B 66  ? 0.2560 0.2952 0.3446 0.0184  0.0227  -0.0052 66  ALA B O   
1460 C CB  . ALA B 66  ? 0.2873 0.3169 0.3592 0.0184  0.0183  -0.0076 66  ALA B CB  
1461 N N   . GLY B 67  ? 0.2198 0.2575 0.2974 0.0179  0.0296  -0.0097 67  GLY B N   
1462 C CA  . GLY B 67  ? 0.2315 0.2732 0.3183 0.0191  0.0341  -0.0106 67  GLY B CA  
1463 C C   . GLY B 67  ? 0.2413 0.2877 0.3323 0.0175  0.0356  -0.0081 67  GLY B C   
1464 O O   . GLY B 67  ? 0.2119 0.2587 0.3026 0.0158  0.0318  -0.0049 67  GLY B O   
1465 N N   . PRO B 68  ? 0.2750 0.3249 0.3704 0.0180  0.0414  -0.0095 68  PRO B N   
1466 C CA  . PRO B 68  ? 0.2900 0.3449 0.3915 0.0164  0.0433  -0.0069 68  PRO B CA  
1467 C C   . PRO B 68  ? 0.2586 0.3120 0.3511 0.0133  0.0414  -0.0046 68  PRO B C   
1468 O O   . PRO B 68  ? 0.2341 0.2841 0.3150 0.0125  0.0425  -0.0060 68  PRO B O   
1469 C CB  . PRO B 68  ? 0.2991 0.3568 0.4029 0.0172  0.0509  -0.0096 68  PRO B CB  
1470 C CG  . PRO B 68  ? 0.3107 0.3653 0.4129 0.0198  0.0525  -0.0137 68  PRO B CG  
1471 C CD  . PRO B 68  ? 0.3181 0.3676 0.4146 0.0201  0.0465  -0.0136 68  PRO B CD  
1472 N N   . PRO B 69  ? 0.2742 0.3300 0.3719 0.0116  0.0384  -0.0012 69  PRO B N   
1473 C CA  . PRO B 69  ? 0.2882 0.3418 0.3778 0.0088  0.0361  0.0011  69  PRO B CA  
1474 C C   . PRO B 69  ? 0.2688 0.3235 0.3536 0.0072  0.0415  0.0011  69  PRO B C   
1475 O O   . PRO B 69  ? 0.2920 0.3513 0.3839 0.0072  0.0465  0.0009  69  PRO B O   
1476 C CB  . PRO B 69  ? 0.2639 0.3204 0.3624 0.0075  0.0321  0.0043  69  PRO B CB  
1477 C CG  . PRO B 69  ? 0.3330 0.3913 0.4410 0.0098  0.0299  0.0039  69  PRO B CG  
1478 C CD  . PRO B 69  ? 0.2605 0.3197 0.3706 0.0124  0.0351  0.0008  69  PRO B CD  
1479 N N   . ARG B 70  ? 0.1983 0.2489 0.2712 0.0057  0.0406  0.0014  70  ARG B N   
1480 C CA  . ARG B 70  ? 0.2931 0.3441 0.3603 0.0037  0.0449  0.0024  70  ARG B CA  
1481 C C   . ARG B 70  ? 0.2449 0.2953 0.3117 0.0009  0.0419  0.0062  70  ARG B C   
1482 O O   . ARG B 70  ? 0.2328 0.2809 0.2999 0.0007  0.0363  0.0074  70  ARG B O   
1483 C CB  . ARG B 70  ? 0.2230 0.2698 0.2767 0.0040  0.0462  0.0002  70  ARG B CB  
1484 C CG  . ARG B 70  ? 0.2505 0.2968 0.3034 0.0066  0.0486  -0.0040 70  ARG B CG  
1485 C CD  . ARG B 70  ? 0.2802 0.3313 0.3425 0.0078  0.0544  -0.0058 70  ARG B CD  
1486 N NE  . ARG B 70  ? 0.2661 0.3155 0.3260 0.0102  0.0566  -0.0102 70  ARG B NE  
1487 C CZ  . ARG B 70  ? 0.3247 0.3770 0.3931 0.0122  0.0608  -0.0127 70  ARG B CZ  
1488 N NH1 . ARG B 70  ? 0.2480 0.3058 0.3283 0.0123  0.0635  -0.0111 70  ARG B NH1 
1489 N NH2 . ARG B 70  ? 0.2505 0.3003 0.3161 0.0143  0.0622  -0.0170 70  ARG B NH2 
1490 N N   . LYS B 71  ? 0.2360 0.2881 0.3019 -0.0013 0.0459  0.0081  71  LYS B N   
1491 C CA  . LYS B 71  ? 0.2029 0.2535 0.2676 -0.0041 0.0433  0.0117  71  LYS B CA  
1492 C C   . LYS B 71  ? 0.2154 0.2598 0.2671 -0.0045 0.0402  0.0122  71  LYS B C   
1493 O O   . LYS B 71  ? 0.1665 0.2077 0.2169 -0.0055 0.0353  0.0139  71  LYS B O   
1494 C CB  . LYS B 71  ? 0.2384 0.2928 0.3067 -0.0064 0.0488  0.0139  71  LYS B CB  
1495 C CG  . LYS B 71  ? 0.2489 0.3095 0.3326 -0.0070 0.0495  0.0149  71  LYS B CG  
1496 C CD  . LYS B 71  ? 0.3805 0.4431 0.4675 -0.0105 0.0517  0.0185  71  LYS B CD  
1497 C CE  . LYS B 71  ? 0.5514 0.6154 0.6483 -0.0124 0.0466  0.0208  71  LYS B CE  
1498 N NZ  . LYS B 71  ? 0.4943 0.5609 0.5962 -0.0160 0.0494  0.0241  71  LYS B NZ  
1499 N N   . LEU B 72  ? 0.2168 0.2592 0.2587 -0.0037 0.0429  0.0104  72  LEU B N   
1500 C CA  . LEU B 72  ? 0.1954 0.2325 0.2250 -0.0040 0.0405  0.0110  72  LEU B CA  
1501 C C   . LEU B 72  ? 0.1870 0.2215 0.2115 -0.0016 0.0378  0.0077  72  LEU B C   
1502 O O   . LEU B 72  ? 0.2088 0.2451 0.2352 0.0002  0.0403  0.0046  72  LEU B O   
1503 C CB  . LEU B 72  ? 0.2223 0.2591 0.2435 -0.0054 0.0454  0.0120  72  LEU B CB  
1504 C CG  . LEU B 72  ? 0.2385 0.2776 0.2632 -0.0082 0.0489  0.0156  72  LEU B CG  
1505 C CD1 . LEU B 72  ? 0.1954 0.2328 0.2090 -0.0096 0.0527  0.0169  72  LEU B CD1 
1506 C CD2 . LEU B 72  ? 0.2063 0.2435 0.2350 -0.0101 0.0444  0.0189  72  LEU B CD2 
1507 N N   . ILE B 73  ? 0.1994 0.2295 0.2176 -0.0015 0.0330  0.0085  73  ILE B N   
1508 C CA  . ILE B 73  ? 0.1690 0.1967 0.1817 0.0005  0.0309  0.0055  73  ILE B CA  
1509 C C   . ILE B 73  ? 0.2075 0.2344 0.2106 0.0006  0.0340  0.0040  73  ILE B C   
1510 O O   . ILE B 73  ? 0.2395 0.2656 0.2396 0.0022  0.0338  0.0007  73  ILE B O   
1511 C CB  . ILE B 73  ? 0.1712 0.1950 0.1809 0.0007  0.0251  0.0066  73  ILE B CB  
1512 C CG1 . ILE B 73  ? 0.2229 0.2440 0.2271 -0.0011 0.0241  0.0101  73  ILE B CG1 
1513 C CG2 . ILE B 73  ? 0.1997 0.2242 0.2182 0.0010  0.0219  0.0071  73  ILE B CG2 
1514 C CD1 . ILE B 73  ? 0.2159 0.2329 0.2168 -0.0006 0.0188  0.0108  73  ILE B CD1 
1515 N N   . GLU B 74  ? 0.1902 0.2171 0.1882 -0.0013 0.0371  0.0063  74  GLU B N   
1516 C CA  . GLU B 74  ? 0.1983 0.2250 0.1870 -0.0014 0.0407  0.0048  74  GLU B CA  
1517 C C   . GLU B 74  ? 0.2509 0.2804 0.2429 0.0000  0.0451  0.0006  74  GLU B C   
1518 O O   . GLU B 74  ? 0.2357 0.2639 0.2207 0.0009  0.0460  -0.0027 74  GLU B O   
1519 C CB  . GLU B 74  ? 0.2146 0.2416 0.1993 -0.0039 0.0442  0.0083  74  GLU B CB  
1520 C CG  . GLU B 74  ? 0.2377 0.2607 0.2152 -0.0052 0.0405  0.0123  74  GLU B CG  
1521 C CD  . GLU B 74  ? 0.2246 0.2469 0.2097 -0.0062 0.0375  0.0156  74  GLU B CD  
1522 O OE1 . GLU B 74  ? 0.2097 0.2342 0.2048 -0.0055 0.0366  0.0144  74  GLU B OE1 
1523 O OE2 . GLU B 74  ? 0.2396 0.2589 0.2204 -0.0078 0.0359  0.0193  74  GLU B OE2 
1524 N N   . THR B 75  ? 0.2300 0.2634 0.2331 0.0002  0.0477  0.0006  75  THR B N   
1525 C CA  . THR B 75  ? 0.2030 0.2392 0.2109 0.0018  0.0523  -0.0032 75  THR B CA  
1526 C C   . THR B 75  ? 0.2347 0.2694 0.2445 0.0042  0.0492  -0.0068 75  THR B C   
1527 O O   . THR B 75  ? 0.2097 0.2443 0.2175 0.0055  0.0521  -0.0107 75  THR B O   
1528 C CB  . THR B 75  ? 0.2248 0.2659 0.2456 0.0015  0.0551  -0.0017 75  THR B CB  
1529 O OG1 . THR B 75  ? 0.2774 0.3195 0.2967 -0.0011 0.0572  0.0022  75  THR B OG1 
1530 C CG2 . THR B 75  ? 0.2187 0.2632 0.2444 0.0030  0.0612  -0.0054 75  THR B CG2 
1531 N N   . VAL B 76  ? 0.1823 0.2157 0.1961 0.0046  0.0437  -0.0054 76  VAL B N   
1532 C CA  . VAL B 76  ? 0.2267 0.2581 0.2418 0.0066  0.0404  -0.0082 76  VAL B CA  
1533 C C   . VAL B 76  ? 0.2472 0.2752 0.2510 0.0067  0.0393  -0.0104 76  VAL B C   
1534 O O   . VAL B 76  ? 0.2393 0.2665 0.2422 0.0080  0.0403  -0.0143 76  VAL B O   
1535 C CB  . VAL B 76  ? 0.1820 0.2125 0.2020 0.0067  0.0348  -0.0058 76  VAL B CB  
1536 C CG1 . VAL B 76  ? 0.1944 0.2229 0.2155 0.0085  0.0317  -0.0083 76  VAL B CG1 
1537 C CG2 . VAL B 76  ? 0.2119 0.2459 0.2429 0.0063  0.0354  -0.0035 76  VAL B CG2 
1538 N N   . GLY B 77  ? 0.1917 0.2176 0.1873 0.0053  0.0369  -0.0081 77  GLY B N   
1539 C CA  . GLY B 77  ? 0.2002 0.2231 0.1855 0.0053  0.0351  -0.0099 77  GLY B CA  
1540 C C   . GLY B 77  ? 0.2227 0.2459 0.2016 0.0052  0.0397  -0.0131 77  GLY B C   
1541 O O   . GLY B 77  ? 0.2428 0.2641 0.2166 0.0059  0.0388  -0.0166 77  GLY B O   
1542 N N   . ALA B 78  ? 0.2374 0.2629 0.2161 0.0042  0.0448  -0.0121 78  ALA B N   
1543 C CA  . ALA B 78  ? 0.2595 0.2852 0.2315 0.0040  0.0499  -0.0154 78  ALA B CA  
1544 C C   . ALA B 78  ? 0.2184 0.2449 0.1967 0.0060  0.0525  -0.0203 78  ALA B C   
1545 O O   . ALA B 78  ? 0.2775 0.3025 0.2494 0.0064  0.0542  -0.0245 78  ALA B O   
1546 C CB  . ALA B 78  ? 0.2547 0.2829 0.2257 0.0024  0.0553  -0.0129 78  ALA B CB  
1547 N N   . GLU B 79  ? 0.2354 0.2642 0.2265 0.0073  0.0526  -0.0199 79  GLU B N   
1548 C CA  . GLU B 79  ? 0.2371 0.2662 0.2349 0.0095  0.0546  -0.0242 79  GLU B CA  
1549 C C   . GLU B 79  ? 0.2304 0.2557 0.2242 0.0103  0.0502  -0.0270 79  GLU B C   
1550 O O   . GLU B 79  ? 0.2308 0.2545 0.2217 0.0111  0.0524  -0.0317 79  GLU B O   
1551 C CB  . GLU B 79  ? 0.1981 0.2302 0.2103 0.0107  0.0544  -0.0225 79  GLU B CB  
1552 C CG  . GLU B 79  ? 0.2372 0.2697 0.2574 0.0132  0.0569  -0.0266 79  GLU B CG  
1553 C CD  . GLU B 79  ? 0.2825 0.3188 0.3174 0.0144  0.0574  -0.0246 79  GLU B CD  
1554 O OE1 . GLU B 79  ? 0.2759 0.3151 0.3147 0.0132  0.0571  -0.0207 79  GLU B OE1 
1555 O OE2 . GLU B 79  ? 0.3149 0.3510 0.3576 0.0166  0.0580  -0.0270 79  GLU B OE2 
1556 N N   . ILE B 80  ? 0.1959 0.2198 0.1897 0.0099  0.0443  -0.0244 80  ILE B N   
1557 C CA  . ILE B 80  ? 0.2164 0.2371 0.2074 0.0105  0.0402  -0.0268 80  ILE B CA  
1558 C C   . ILE B 80  ? 0.2533 0.2719 0.2321 0.0095  0.0407  -0.0296 80  ILE B C   
1559 O O   . ILE B 80  ? 0.2419 0.2585 0.2188 0.0101  0.0410  -0.0340 80  ILE B O   
1560 C CB  . ILE B 80  ? 0.2765 0.2963 0.2688 0.0102  0.0343  -0.0233 80  ILE B CB  
1561 C CG1 . ILE B 80  ? 0.1883 0.2100 0.1921 0.0111  0.0336  -0.0208 80  ILE B CG1 
1562 C CG2 . ILE B 80  ? 0.2190 0.2359 0.2084 0.0106  0.0304  -0.0256 80  ILE B CG2 
1563 C CD1 . ILE B 80  ? 0.1986 0.2196 0.2030 0.0105  0.0286  -0.0170 80  ILE B CD1 
1564 N N   . ALA B 81  ? 0.2495 0.2682 0.2199 0.0079  0.0407  -0.0270 81  ALA B N   
1565 C CA  . ALA B 81  ? 0.2470 0.2638 0.2045 0.0067  0.0403  -0.0288 81  ALA B CA  
1566 C C   . ALA B 81  ? 0.2964 0.3130 0.2502 0.0069  0.0458  -0.0337 81  ALA B C   
1567 O O   . ALA B 81  ? 0.2868 0.3011 0.2352 0.0068  0.0448  -0.0378 81  ALA B O   
1568 C CB  . ALA B 81  ? 0.2841 0.3011 0.2344 0.0050  0.0396  -0.0244 81  ALA B CB  
1569 N N   . ASP B 82  ? 0.2739 0.2930 0.2323 0.0072  0.0517  -0.0337 82  ASP B N   
1570 C CA  . ASP B 82  ? 0.2860 0.3053 0.2422 0.0077  0.0581  -0.0386 82  ASP B CA  
1571 C C   . ASP B 82  ? 0.2898 0.3071 0.2501 0.0094  0.0591  -0.0446 82  ASP B C   
1572 O O   . ASP B 82  ? 0.2795 0.2942 0.2328 0.0094  0.0607  -0.0500 82  ASP B O   
1573 C CB  . ASP B 82  ? 0.2884 0.3116 0.2521 0.0080  0.0642  -0.0370 82  ASP B CB  
1574 C CG  . ASP B 82  ? 0.4407 0.4643 0.4018 0.0085  0.0715  -0.0418 82  ASP B CG  
1575 O OD1 . ASP B 82  ? 0.4291 0.4518 0.3779 0.0069  0.0739  -0.0427 82  ASP B OD1 
1576 O OD2 . ASP B 82  ? 0.4742 0.4988 0.4455 0.0106  0.0745  -0.0447 82  ASP B OD2 
1577 N N   . HIS B 83  ? 0.3124 0.3299 0.2839 0.0108  0.0558  -0.0434 83  HIS B N   
1578 C CA  . HIS B 83  ? 0.2781 0.2936 0.2564 0.0126  0.0555  -0.0476 83  HIS B CA  
1579 C C   . HIS B 83  ? 0.2952 0.3070 0.2658 0.0117  0.0504  -0.0498 83  HIS B C   
1580 O O   . HIS B 83  ? 0.3183 0.3274 0.2876 0.0122  0.0515  -0.0549 83  HIS B O   
1581 C CB  . HIS B 83  ? 0.2576 0.2748 0.2499 0.0143  0.0538  -0.0447 83  HIS B CB  
1582 C CG  . HIS B 83  ? 0.2859 0.3061 0.2883 0.0158  0.0591  -0.0447 83  HIS B CG  
1583 N ND1 . HIS B 83  ? 0.3461 0.3703 0.3509 0.0152  0.0618  -0.0411 83  HIS B ND1 
1584 C CD2 . HIS B 83  ? 0.2805 0.3006 0.2918 0.0180  0.0623  -0.0480 83  HIS B CD2 
1585 C CE1 . HIS B 83  ? 0.3029 0.3297 0.3182 0.0170  0.0662  -0.0421 83  HIS B CE1 
1586 N NE2 . HIS B 83  ? 0.3914 0.4157 0.4108 0.0188  0.0666  -0.0462 83  HIS B NE2 
1587 N N   . VAL B 84  ? 0.2320 0.2437 0.1979 0.0104  0.0451  -0.0460 84  VAL B N   
1588 C CA  . VAL B 84  ? 0.2494 0.2583 0.2089 0.0094  0.0401  -0.0479 84  VAL B CA  
1589 C C   . VAL B 84  ? 0.2732 0.2803 0.2204 0.0081  0.0421  -0.0523 84  VAL B C   
1590 O O   . VAL B 84  ? 0.2902 0.2947 0.2353 0.0080  0.0408  -0.0568 84  VAL B O   
1591 C CB  . VAL B 84  ? 0.2864 0.2958 0.2437 0.0085  0.0343  -0.0431 84  VAL B CB  
1592 C CG1 . VAL B 84  ? 0.2942 0.3016 0.2436 0.0073  0.0298  -0.0451 84  VAL B CG1 
1593 C CG2 . VAL B 84  ? 0.2778 0.2881 0.2462 0.0096  0.0316  -0.0398 84  VAL B CG2 
1594 N N   . MET B 85  ? 0.3174 0.3259 0.2567 0.0071  0.0453  -0.0510 85  MET B N   
1595 C CA  . MET B 85  ? 0.3116 0.3183 0.2378 0.0058  0.0475  -0.0551 85  MET B CA  
1596 C C   . MET B 85  ? 0.2874 0.2926 0.2146 0.0067  0.0532  -0.0615 85  MET B C   
1597 O O   . MET B 85  ? 0.2900 0.2933 0.2055 0.0055  0.0549  -0.0655 85  MET B O   
1598 C CB  . MET B 85  ? 0.3137 0.3220 0.2304 0.0043  0.0497  -0.0515 85  MET B CB  
1599 C CG  . MET B 85  ? 0.2642 0.2740 0.1813 0.0036  0.0450  -0.0448 85  MET B CG  
1600 S SD  . MET B 85  ? 0.3612 0.3684 0.2663 0.0020  0.0376  -0.0453 85  MET B SD  
1601 C CE  . MET B 85  ? 0.3936 0.3996 0.2821 0.0001  0.0416  -0.0484 85  MET B CE  
1602 N N   . ASP B 86  ? 0.2707 0.2763 0.2106 0.0088  0.0560  -0.0629 86  ASP B N   
1603 C CA  . ASP B 86  ? 0.2694 0.2726 0.2102 0.0098  0.0604  -0.0697 86  ASP B CA  
1604 C C   . ASP B 86  ? 0.3473 0.3463 0.2826 0.0089  0.0560  -0.0742 86  ASP B C   
1605 O O   . ASP B 86  ? 0.2944 0.2906 0.2233 0.0085  0.0589  -0.0804 86  ASP B O   
1606 C CB  . ASP B 86  ? 0.3090 0.3130 0.2655 0.0125  0.0631  -0.0699 86  ASP B CB  
1607 C CG  . ASP B 86  ? 0.2924 0.3008 0.2552 0.0135  0.0685  -0.0668 86  ASP B CG  
1608 O OD1 . ASP B 86  ? 0.2701 0.2803 0.2245 0.0122  0.0719  -0.0658 86  ASP B OD1 
1609 O OD2 . ASP B 86  ? 0.3055 0.3156 0.2819 0.0155  0.0691  -0.0650 86  ASP B OD2 
1610 N N   . ASP B 87  ? 0.3271 0.3258 0.2647 0.0083  0.0492  -0.0715 87  ASP B N   
1611 C CA  . ASP B 87  ? 0.3294 0.3247 0.2621 0.0070  0.0447  -0.0753 87  ASP B CA  
1612 C C   . ASP B 87  ? 0.3011 0.2959 0.2178 0.0046  0.0431  -0.0764 87  ASP B C   
1613 O O   . ASP B 87  ? 0.3801 0.3769 0.2918 0.0035  0.0395  -0.0715 87  ASP B O   
1614 C CB  . ASP B 87  ? 0.2832 0.2789 0.2234 0.0070  0.0382  -0.0716 87  ASP B CB  
1615 C CG  . ASP B 87  ? 0.3375 0.3299 0.2760 0.0058  0.0340  -0.0759 87  ASP B CG  
1616 O OD1 . ASP B 87  ? 0.3036 0.2943 0.2309 0.0041  0.0333  -0.0798 87  ASP B OD1 
1617 O OD2 . ASP B 87  ? 0.3733 0.3648 0.3216 0.0065  0.0315  -0.0754 87  ASP B OD2 
1618 N N   . GLN B 88  ? 0.3200 0.3118 0.2284 0.0038  0.0458  -0.0830 88  GLN B N   
1619 C CA  . GLN B 88  ? 0.4091 0.4003 0.3011 0.0015  0.0450  -0.0843 88  GLN B CA  
1620 C C   . GLN B 88  ? 0.3786 0.3695 0.2651 -0.0005 0.0367  -0.0828 88  GLN B C   
1621 O O   . GLN B 88  ? 0.3724 0.3637 0.2461 -0.0023 0.0345  -0.0816 88  GLN B O   
1622 C CB  . GLN B 88  ? 0.3515 0.3392 0.2358 0.0011  0.0498  -0.0922 88  GLN B CB  
1623 C CG  . GLN B 88  ? 0.4597 0.4480 0.3477 0.0029  0.0590  -0.0942 88  GLN B CG  
1624 C CD  . GLN B 88  ? 0.4546 0.4471 0.3401 0.0030  0.0623  -0.0883 88  GLN B CD  
1625 O OE1 . GLN B 88  ? 0.4587 0.4514 0.3304 0.0012  0.0637  -0.0883 88  GLN B OE1 
1626 N NE2 . GLN B 88  ? 0.4312 0.4269 0.3301 0.0048  0.0635  -0.0834 88  GLN B NE2 
1627 N N   . ARG B 89  ? 0.3725 0.3628 0.2686 -0.0001 0.0320  -0.0827 89  ARG B N   
1628 C CA  . ARG B 89  ? 0.3608 0.3514 0.2531 -0.0018 0.0243  -0.0810 89  ARG B CA  
1629 C C   . ARG B 89  ? 0.3645 0.3587 0.2568 -0.0017 0.0210  -0.0733 89  ARG B C   
1630 O O   . ARG B 89  ? 0.3360 0.3309 0.2231 -0.0031 0.0149  -0.0714 89  ARG B O   
1631 C CB  . ARG B 89  ? 0.3612 0.3504 0.2644 -0.0016 0.0207  -0.0828 89  ARG B CB  
1632 C CG  . ARG B 89  ? 0.3567 0.3418 0.2612 -0.0017 0.0234  -0.0904 89  ARG B CG  
1633 C CD  . ARG B 89  ? 0.3785 0.3623 0.2959 -0.0012 0.0207  -0.0907 89  ARG B CD  
1634 N NE  . ARG B 89  ? 0.4347 0.4203 0.3644 0.0013  0.0231  -0.0861 89  ARG B NE  
1635 C CZ  . ARG B 89  ? 0.4339 0.4189 0.3754 0.0021  0.0214  -0.0849 89  ARG B CZ  
1636 N NH1 . ARG B 89  ? 0.4501 0.4327 0.3939 0.0007  0.0177  -0.0880 89  ARG B NH1 
1637 N NH2 . ARG B 89  ? 0.3489 0.3356 0.3002 0.0042  0.0234  -0.0805 89  ARG B NH2 
1638 N N   . VAL B 90  ? 0.3295 0.3258 0.2279 -0.0001 0.0247  -0.0690 90  VAL B N   
1639 C CA  . VAL B 90  ? 0.3184 0.3175 0.2182 0.0001  0.0219  -0.0618 90  VAL B CA  
1640 C C   . VAL B 90  ? 0.3536 0.3533 0.2398 -0.0014 0.0219  -0.0595 90  VAL B C   
1641 O O   . VAL B 90  ? 0.3676 0.3671 0.2477 -0.0016 0.0276  -0.0607 90  VAL B O   
1642 C CB  . VAL B 90  ? 0.2967 0.2977 0.2080 0.0021  0.0256  -0.0582 90  VAL B CB  
1643 C CG1 . VAL B 90  ? 0.2474 0.2509 0.1594 0.0021  0.0230  -0.0512 90  VAL B CG1 
1644 C CG2 . VAL B 90  ? 0.2875 0.2877 0.2116 0.0034  0.0246  -0.0596 90  VAL B CG2 
1645 N N   . HIS B 91  ? 0.3076 0.3081 0.1893 -0.0024 0.0157  -0.0560 91  HIS B N   
1646 C CA  . HIS B 91  ? 0.3664 0.3675 0.2357 -0.0037 0.0147  -0.0525 91  HIS B CA  
1647 C C   . HIS B 91  ? 0.3594 0.3622 0.2319 -0.0028 0.0177  -0.0464 91  HIS B C   
1648 O O   . HIS B 91  ? 0.3661 0.3689 0.2300 -0.0036 0.0215  -0.0449 91  HIS B O   
1649 C CB  . HIS B 91  ? 0.3737 0.3752 0.2392 -0.0046 0.0066  -0.0502 91  HIS B CB  
1650 C CG  . HIS B 91  ? 0.4743 0.4744 0.3359 -0.0059 0.0029  -0.0558 91  HIS B CG  
1651 N ND1 . HIS B 91  ? 0.5100 0.5110 0.3737 -0.0065 -0.0045 -0.0549 91  HIS B ND1 
1652 C CD2 . HIS B 91  ? 0.4576 0.4554 0.3135 -0.0070 0.0054  -0.0626 91  HIS B CD2 
1653 C CE1 . HIS B 91  ? 0.5506 0.5501 0.4103 -0.0079 -0.0065 -0.0608 91  HIS B CE1 
1654 N NE2 . HIS B 91  ? 0.5473 0.5445 0.4018 -0.0083 -0.0007 -0.0656 91  HIS B NE2 
1655 N N   . ALA B 92  ? 0.3098 0.3141 0.1939 -0.0015 0.0157  -0.0426 92  ALA B N   
1656 C CA  . ALA B 92  ? 0.2586 0.2643 0.1466 -0.0008 0.0177  -0.0369 92  ALA B CA  
1657 C C   . ALA B 92  ? 0.2520 0.2587 0.1546 0.0009  0.0170  -0.0356 92  ALA B C   
1658 O O   . ALA B 92  ? 0.2651 0.2715 0.1734 0.0014  0.0136  -0.0378 92  ALA B O   
1659 C CB  . ALA B 92  ? 0.3679 0.3737 0.2489 -0.0017 0.0132  -0.0314 92  ALA B CB  
1660 N N   . VAL B 93  ? 0.2389 0.2469 0.1474 0.0016  0.0201  -0.0320 93  VAL B N   
1661 C CA  . VAL B 93  ? 0.2263 0.2353 0.1475 0.0030  0.0190  -0.0300 93  VAL B CA  
1662 C C   . VAL B 93  ? 0.3074 0.3173 0.2301 0.0029  0.0187  -0.0240 93  VAL B C   
1663 O O   . VAL B 93  ? 0.2908 0.3010 0.2080 0.0020  0.0218  -0.0218 93  VAL B O   
1664 C CB  . VAL B 93  ? 0.2925 0.3020 0.2227 0.0042  0.0237  -0.0331 93  VAL B CB  
1665 C CG1 . VAL B 93  ? 0.2678 0.2785 0.1968 0.0040  0.0300  -0.0326 93  VAL B CG1 
1666 C CG2 . VAL B 93  ? 0.2252 0.2355 0.1674 0.0055  0.0218  -0.0307 93  VAL B CG2 
1667 N N   . GLU B 94  ? 0.2625 0.2726 0.1926 0.0038  0.0150  -0.0214 94  GLU B N   
1668 C CA  . GLU B 94  ? 0.2497 0.2601 0.1826 0.0038  0.0143  -0.0162 94  GLU B CA  
1669 C C   . GLU B 94  ? 0.2779 0.2892 0.2227 0.0050  0.0145  -0.0159 94  GLU B C   
1670 O O   . GLU B 94  ? 0.2458 0.2567 0.1952 0.0058  0.0114  -0.0172 94  GLU B O   
1671 C CB  . GLU B 94  ? 0.3209 0.3303 0.2496 0.0036  0.0088  -0.0131 94  GLU B CB  
1672 C CG  . GLU B 94  ? 0.4262 0.4353 0.3592 0.0039  0.0074  -0.0081 94  GLU B CG  
1673 C CD  . GLU B 94  ? 0.3909 0.3987 0.3185 0.0037  0.0027  -0.0048 94  GLU B CD  
1674 O OE1 . GLU B 94  ? 0.3476 0.3546 0.2659 0.0026  0.0027  -0.0032 94  GLU B OE1 
1675 O OE2 . GLU B 94  ? 0.4080 0.4155 0.3411 0.0048  -0.0010 -0.0037 94  GLU B OE2 
1676 N N   . VAL B 95  ? 0.2086 0.2210 0.1581 0.0050  0.0182  -0.0141 95  VAL B N   
1677 C CA  . VAL B 95  ? 0.2328 0.2462 0.1932 0.0060  0.0184  -0.0135 95  VAL B CA  
1678 C C   . VAL B 95  ? 0.2557 0.2689 0.2182 0.0055  0.0168  -0.0088 95  VAL B C   
1679 O O   . VAL B 95  ? 0.2164 0.2299 0.1761 0.0044  0.0191  -0.0062 95  VAL B O   
1680 C CB  . VAL B 95  ? 0.2733 0.2885 0.2391 0.0064  0.0235  -0.0157 95  VAL B CB  
1681 C CG1 . VAL B 95  ? 0.2058 0.2221 0.1828 0.0074  0.0230  -0.0146 95  VAL B CG1 
1682 C CG2 . VAL B 95  ? 0.2104 0.2251 0.1737 0.0068  0.0255  -0.0208 95  VAL B CG2 
1683 N N   . ALA B 96  ? 0.2123 0.2248 0.1796 0.0063  0.0131  -0.0076 96  ALA B N   
1684 C CA  . ALA B 96  ? 0.2062 0.2180 0.1766 0.0059  0.0117  -0.0037 96  ALA B CA  
1685 C C   . ALA B 96  ? 0.2038 0.2170 0.1836 0.0064  0.0127  -0.0039 96  ALA B C   
1686 O O   . ALA B 96  ? 0.1898 0.2031 0.1740 0.0075  0.0115  -0.0059 96  ALA B O   
1687 C CB  . ALA B 96  ? 0.2300 0.2399 0.1990 0.0065  0.0069  -0.0023 96  ALA B CB  
1688 N N   . VAL B 97  ? 0.1700 0.1843 0.1530 0.0055  0.0149  -0.0016 97  VAL B N   
1689 C CA  . VAL B 97  ? 0.1731 0.1887 0.1650 0.0057  0.0152  -0.0011 97  VAL B CA  
1690 C C   . VAL B 97  ? 0.1932 0.2071 0.1862 0.0050  0.0122  0.0021  97  VAL B C   
1691 O O   . VAL B 97  ? 0.1707 0.1841 0.1614 0.0037  0.0130  0.0048  97  VAL B O   
1692 C CB  . VAL B 97  ? 0.2350 0.2535 0.2312 0.0052  0.0197  -0.0012 97  VAL B CB  
1693 C CG1 . VAL B 97  ? 0.1720 0.1924 0.1781 0.0054  0.0192  -0.0005 97  VAL B CG1 
1694 C CG2 . VAL B 97  ? 0.1979 0.2177 0.1926 0.0061  0.0230  -0.0050 97  VAL B CG2 
1695 N N   . HIS B 98  ? 0.1893 0.2021 0.1854 0.0059  0.0090  0.0018  98  HIS B N   
1696 C CA  . HIS B 98  ? 0.2069 0.2176 0.2042 0.0054  0.0062  0.0041  98  HIS B CA  
1697 C C   . HIS B 98  ? 0.2372 0.2494 0.2419 0.0049  0.0064  0.0048  98  HIS B C   
1698 O O   . HIS B 98  ? 0.1821 0.1963 0.1916 0.0057  0.0070  0.0032  98  HIS B O   
1699 C CB  . HIS B 98  ? 0.1946 0.2033 0.1907 0.0067  0.0027  0.0033  98  HIS B CB  
1700 C CG  . HIS B 98  ? 0.2360 0.2438 0.2262 0.0073  0.0018  0.0023  98  HIS B CG  
1701 N ND1 . HIS B 98  ? 0.2357 0.2412 0.2218 0.0074  -0.0004 0.0041  98  HIS B ND1 
1702 C CD2 . HIS B 98  ? 0.2357 0.2446 0.2239 0.0080  0.0024  -0.0002 98  HIS B CD2 
1703 C CE1 . HIS B 98  ? 0.2661 0.2718 0.2480 0.0080  -0.0012 0.0028  98  HIS B CE1 
1704 N NE2 . HIS B 98  ? 0.2283 0.2360 0.2111 0.0083  0.0004  0.0001  98  HIS B NE2 
1705 N N   . LYS B 99  ? 0.2168 0.2279 0.2227 0.0035  0.0056  0.0073  99  LYS B N   
1706 C CA  . LYS B 99  ? 0.1698 0.1821 0.1825 0.0026  0.0050  0.0081  99  LYS B CA  
1707 C C   . LYS B 99  ? 0.2220 0.2309 0.2339 0.0023  0.0015  0.0091  99  LYS B C   
1708 O O   . LYS B 99  ? 0.2318 0.2392 0.2442 0.0007  0.0010  0.0112  99  LYS B O   
1709 C CB  . LYS B 99  ? 0.1561 0.1706 0.1718 0.0009  0.0080  0.0099  99  LYS B CB  
1710 C CG  . LYS B 99  ? 0.2325 0.2501 0.2569 0.0001  0.0082  0.0102  99  LYS B CG  
1711 C CD  . LYS B 99  ? 0.2186 0.2390 0.2463 -0.0017 0.0118  0.0120  99  LYS B CD  
1712 C CE  . LYS B 99  ? 0.2332 0.2574 0.2708 -0.0026 0.0118  0.0126  99  LYS B CE  
1713 N NZ  . LYS B 99  ? 0.2975 0.3235 0.3382 -0.0050 0.0145  0.0149  99  LYS B NZ  
1714 N N   . PRO B 100 ? 0.2041 0.2113 0.2145 0.0037  -0.0009 0.0076  100 PRO B N   
1715 C CA  . PRO B 100 ? 0.2344 0.2379 0.2429 0.0037  -0.0038 0.0082  100 PRO B CA  
1716 C C   . PRO B 100 ? 0.2827 0.2856 0.2952 0.0022  -0.0053 0.0091  100 PRO B C   
1717 O O   . PRO B 100 ? 0.3240 0.3233 0.3347 0.0016  -0.0071 0.0097  100 PRO B O   
1718 C CB  . PRO B 100 ? 0.2365 0.2396 0.2438 0.0054  -0.0052 0.0061  100 PRO B CB  
1719 C CG  . PRO B 100 ? 0.2067 0.2133 0.2181 0.0059  -0.0038 0.0049  100 PRO B CG  
1720 C CD  . PRO B 100 ? 0.2281 0.2368 0.2395 0.0053  -0.0008 0.0054  100 PRO B CD  
1721 N N   . GLN B 101 ? 0.1955 0.2016 0.2134 0.0015  -0.0046 0.0091  101 GLN B N   
1722 C CA  . GLN B 101 ? 0.2306 0.2365 0.2528 0.0000  -0.0066 0.0098  101 GLN B CA  
1723 C C   . GLN B 101 ? 0.3021 0.3096 0.3282 -0.0022 -0.0051 0.0117  101 GLN B C   
1724 O O   . GLN B 101 ? 0.2320 0.2406 0.2631 -0.0038 -0.0065 0.0124  101 GLN B O   
1725 C CB  . GLN B 101 ? 0.3108 0.3195 0.3374 0.0007  -0.0076 0.0088  101 GLN B CB  
1726 C CG  . GLN B 101 ? 0.3284 0.3351 0.3514 0.0023  -0.0093 0.0072  101 GLN B CG  
1727 C CD  . GLN B 101 ? 0.3535 0.3624 0.3803 0.0031  -0.0103 0.0067  101 GLN B CD  
1728 O OE1 . GLN B 101 ? 0.1915 0.2040 0.2241 0.0029  -0.0094 0.0073  101 GLN B OE1 
1729 N NE2 . GLN B 101 ? 0.3237 0.3305 0.3474 0.0039  -0.0122 0.0058  101 GLN B NE2 
1730 N N   . ALA B 102 ? 0.2551 0.2629 0.2788 -0.0025 -0.0023 0.0128  102 ALA B N   
1731 C CA  . ALA B 102 ? 0.2536 0.2634 0.2810 -0.0046 0.0000  0.0148  102 ALA B CA  
1732 C C   . ALA B 102 ? 0.3074 0.3148 0.3373 -0.0068 -0.0025 0.0161  102 ALA B C   
1733 O O   . ALA B 102 ? 0.2873 0.2899 0.3132 -0.0067 -0.0051 0.0159  102 ALA B O   
1734 C CB  . ALA B 102 ? 0.1887 0.1975 0.2107 -0.0047 0.0028  0.0160  102 ALA B CB  
1735 N N   . PRO B 103 ? 0.2547 0.2652 0.2918 -0.0090 -0.0019 0.0173  103 PRO B N   
1736 C CA  . PRO B 103 ? 0.2587 0.2666 0.2983 -0.0115 -0.0043 0.0185  103 PRO B CA  
1737 C C   . PRO B 103 ? 0.3098 0.3143 0.3460 -0.0130 -0.0027 0.0208  103 PRO B C   
1738 O O   . PRO B 103 ? 0.3425 0.3496 0.3807 -0.0143 0.0008  0.0227  103 PRO B O   
1739 C CB  . PRO B 103 ? 0.2922 0.3055 0.3414 -0.0133 -0.0039 0.0192  103 PRO B CB  
1740 C CG  . PRO B 103 ? 0.3583 0.3767 0.4099 -0.0111 -0.0014 0.0182  103 PRO B CG  
1741 C CD  . PRO B 103 ? 0.3066 0.3231 0.3503 -0.0091 0.0010  0.0175  103 PRO B CD  
1742 N N   . ILE B 104 ? 0.2786 0.2773 0.3092 -0.0126 -0.0049 0.0206  104 ILE B N   
1743 C CA  . ILE B 104 ? 0.2943 0.2885 0.3215 -0.0138 -0.0043 0.0229  104 ILE B CA  
1744 C C   . ILE B 104 ? 0.2978 0.2866 0.3250 -0.0148 -0.0080 0.0222  104 ILE B C   
1745 O O   . ILE B 104 ? 0.3179 0.3053 0.3433 -0.0131 -0.0106 0.0197  104 ILE B O   
1746 C CB  . ILE B 104 ? 0.2785 0.2706 0.2980 -0.0115 -0.0032 0.0232  104 ILE B CB  
1747 C CG1 . ILE B 104 ? 0.3003 0.2972 0.3189 -0.0109 0.0007  0.0237  104 ILE B CG1 
1748 C CG2 . ILE B 104 ? 0.3161 0.3028 0.3322 -0.0126 -0.0033 0.0259  104 ILE B CG2 
1749 C CD1 . ILE B 104 ? 0.3164 0.3116 0.3271 -0.0087 0.0013  0.0237  104 ILE B CD1 
1750 N N   . PRO B 105 ? 0.2537 0.2393 0.2829 -0.0175 -0.0083 0.0242  105 PRO B N   
1751 C CA  . PRO B 105 ? 0.2418 0.2221 0.2714 -0.0185 -0.0120 0.0229  105 PRO B CA  
1752 C C   . PRO B 105 ? 0.3035 0.2776 0.3264 -0.0162 -0.0133 0.0219  105 PRO B C   
1753 O O   . PRO B 105 ? 0.3263 0.2964 0.3482 -0.0160 -0.0162 0.0197  105 PRO B O   
1754 C CB  . PRO B 105 ? 0.3483 0.3270 0.3825 -0.0222 -0.0114 0.0255  105 PRO B CB  
1755 C CG  . PRO B 105 ? 0.3407 0.3215 0.3739 -0.0225 -0.0074 0.0287  105 PRO B CG  
1756 C CD  . PRO B 105 ? 0.2702 0.2570 0.3021 -0.0200 -0.0053 0.0275  105 PRO B CD  
1757 N N   . GLN B 106 ? 0.2789 0.2523 0.2972 -0.0143 -0.0114 0.0235  106 GLN B N   
1758 C CA  . GLN B 106 ? 0.3398 0.3082 0.3527 -0.0118 -0.0127 0.0229  106 GLN B CA  
1759 C C   . GLN B 106 ? 0.3015 0.2720 0.3118 -0.0088 -0.0135 0.0197  106 GLN B C   
1760 O O   . GLN B 106 ? 0.3448 0.3208 0.3566 -0.0084 -0.0127 0.0186  106 GLN B O   
1761 C CB  . GLN B 106 ? 0.2406 0.2078 0.2496 -0.0111 -0.0107 0.0261  106 GLN B CB  
1762 C CG  . GLN B 106 ? 0.2750 0.2376 0.2851 -0.0137 -0.0104 0.0295  106 GLN B CG  
1763 C CD  . GLN B 106 ? 0.3757 0.3421 0.3908 -0.0170 -0.0083 0.0313  106 GLN B CD  
1764 O OE1 . GLN B 106 ? 0.3324 0.3051 0.3488 -0.0169 -0.0062 0.0309  106 GLN B OE1 
1765 N NE2 . GLN B 106 ? 0.3877 0.3503 0.4061 -0.0200 -0.0087 0.0332  106 GLN B NE2 
1766 N N   . THR B 107 ? 0.2504 0.2166 0.2574 -0.0067 -0.0151 0.0184  107 THR B N   
1767 C CA  . THR B 107 ? 0.2500 0.2177 0.2545 -0.0038 -0.0156 0.0158  107 THR B CA  
1768 C C   . THR B 107 ? 0.2434 0.2131 0.2447 -0.0017 -0.0142 0.0170  107 THR B C   
1769 O O   . THR B 107 ? 0.2272 0.1937 0.2264 -0.0012 -0.0142 0.0192  107 THR B O   
1770 C CB  . THR B 107 ? 0.2596 0.2218 0.2626 -0.0027 -0.0176 0.0135  107 THR B CB  
1771 O OG1 . THR B 107 ? 0.2852 0.2459 0.2905 -0.0049 -0.0191 0.0120  107 THR B OG1 
1772 C CG2 . THR B 107 ? 0.3001 0.2639 0.3006 0.0002  -0.0178 0.0110  107 THR B CG2 
1773 N N   . PHE B 108 ? 0.2249 0.1996 0.2258 -0.0006 -0.0132 0.0158  108 PHE B N   
1774 C CA  . PHE B 108 ? 0.2490 0.2259 0.2468 0.0011  -0.0121 0.0167  108 PHE B CA  
1775 C C   . PHE B 108 ? 0.2529 0.2335 0.2505 0.0028  -0.0120 0.0140  108 PHE B C   
1776 O O   . PHE B 108 ? 0.2827 0.2649 0.2828 0.0024  -0.0123 0.0122  108 PHE B O   
1777 C CB  . PHE B 108 ? 0.2184 0.1980 0.2160 -0.0006 -0.0097 0.0192  108 PHE B CB  
1778 C CG  . PHE B 108 ? 0.1949 0.1795 0.1960 -0.0017 -0.0081 0.0181  108 PHE B CG  
1779 C CD1 . PHE B 108 ? 0.2550 0.2398 0.2609 -0.0038 -0.0084 0.0181  108 PHE B CD1 
1780 C CD2 . PHE B 108 ? 0.2816 0.2705 0.2816 -0.0006 -0.0064 0.0171  108 PHE B CD2 
1781 C CE1 . PHE B 108 ? 0.2850 0.2748 0.2951 -0.0046 -0.0072 0.0173  108 PHE B CE1 
1782 C CE2 . PHE B 108 ? 0.2223 0.2157 0.2263 -0.0013 -0.0048 0.0161  108 PHE B CE2 
1783 C CZ  . PHE B 108 ? 0.2994 0.2934 0.3087 -0.0032 -0.0053 0.0163  108 PHE B CZ  
1784 N N   . ASP B 109 ? 0.2195 0.2014 0.2142 0.0046  -0.0117 0.0139  109 ASP B N   
1785 C CA  . ASP B 109 ? 0.2106 0.1958 0.2053 0.0062  -0.0116 0.0115  109 ASP B CA  
1786 C C   . ASP B 109 ? 0.2131 0.2029 0.2084 0.0056  -0.0096 0.0112  109 ASP B C   
1787 O O   . ASP B 109 ? 0.2266 0.2188 0.2241 0.0058  -0.0092 0.0094  109 ASP B O   
1788 C CB  . ASP B 109 ? 0.1750 0.1597 0.1671 0.0084  -0.0126 0.0112  109 ASP B CB  
1789 C CG  . ASP B 109 ? 0.3333 0.3141 0.3258 0.0097  -0.0143 0.0106  109 ASP B CG  
1790 O OD1 . ASP B 109 ? 0.4351 0.4142 0.4293 0.0092  -0.0146 0.0093  109 ASP B OD1 
1791 O OD2 . ASP B 109 ? 0.3308 0.3103 0.3219 0.0113  -0.0153 0.0114  109 ASP B OD2 
1792 N N   . ASP B 110 ? 0.1851 0.1757 0.1784 0.0048  -0.0081 0.0131  110 ASP B N   
1793 C CA  . ASP B 110 ? 0.1950 0.1897 0.1882 0.0045  -0.0058 0.0123  110 ASP B CA  
1794 C C   . ASP B 110 ? 0.1962 0.1914 0.1877 0.0029  -0.0036 0.0147  110 ASP B C   
1795 O O   . ASP B 110 ? 0.1697 0.1619 0.1582 0.0025  -0.0042 0.0172  110 ASP B O   
1796 C CB  . ASP B 110 ? 0.2292 0.2254 0.2196 0.0063  -0.0062 0.0106  110 ASP B CB  
1797 C CG  . ASP B 110 ? 0.2394 0.2394 0.2304 0.0062  -0.0039 0.0089  110 ASP B CG  
1798 O OD1 . ASP B 110 ? 0.2378 0.2394 0.2332 0.0061  -0.0033 0.0076  110 ASP B OD1 
1799 O OD2 . ASP B 110 ? 0.2229 0.2239 0.2099 0.0061  -0.0026 0.0090  110 ASP B OD2 
1800 N N   . VAL B 111 ? 0.1675 0.1662 0.1609 0.0021  -0.0009 0.0141  111 VAL B N   
1801 C CA  . VAL B 111 ? 0.1911 0.1910 0.1821 0.0007  0.0019  0.0160  111 VAL B CA  
1802 C C   . VAL B 111 ? 0.1928 0.1964 0.1831 0.0014  0.0044  0.0137  111 VAL B C   
1803 O O   . VAL B 111 ? 0.2034 0.2092 0.1981 0.0022  0.0045  0.0113  111 VAL B O   
1804 C CB  . VAL B 111 ? 0.2575 0.2577 0.2530 -0.0016 0.0035  0.0181  111 VAL B CB  
1805 C CG1 . VAL B 111 ? 0.1877 0.1921 0.1900 -0.0019 0.0052  0.0164  111 VAL B CG1 
1806 C CG2 . VAL B 111 ? 0.2386 0.2386 0.2301 -0.0031 0.0062  0.0209  111 VAL B CG2 
1807 N N   . ALA B 112 ? 0.1936 0.1977 0.1782 0.0012  0.0062  0.0142  112 ALA B N   
1808 C CA  . ALA B 112 ? 0.2314 0.2383 0.2143 0.0020  0.0084  0.0115  112 ALA B CA  
1809 C C   . ALA B 112 ? 0.2552 0.2627 0.2319 0.0008  0.0115  0.0127  112 ALA B C   
1810 O O   . ALA B 112 ? 0.2083 0.2135 0.1805 -0.0002 0.0110  0.0159  112 ALA B O   
1811 C CB  . ALA B 112 ? 0.2325 0.2388 0.2128 0.0038  0.0057  0.0091  112 ALA B CB  
1812 N N   . VAL B 113 ? 0.2035 0.2138 0.1798 0.0010  0.0148  0.0103  113 VAL B N   
1813 C CA  . VAL B 113 ? 0.2061 0.2168 0.1749 0.0001  0.0178  0.0105  113 VAL B CA  
1814 C C   . VAL B 113 ? 0.1921 0.2033 0.1566 0.0015  0.0173  0.0068  113 VAL B C   
1815 O O   . VAL B 113 ? 0.2433 0.2556 0.2127 0.0028  0.0166  0.0038  113 VAL B O   
1816 C CB  . VAL B 113 ? 0.2505 0.2642 0.2221 -0.0012 0.0232  0.0109  113 VAL B CB  
1817 C CG1 . VAL B 113 ? 0.1959 0.2094 0.1732 -0.0028 0.0234  0.0145  113 VAL B CG1 
1818 C CG2 . VAL B 113 ? 0.2109 0.2279 0.1886 0.0000  0.0257  0.0069  113 VAL B CG2 
1819 N N   . VAL B 114 ? 0.2135 0.2237 0.1686 0.0010  0.0175  0.0071  114 VAL B N   
1820 C CA  . VAL B 114 ? 0.2439 0.2543 0.1937 0.0018  0.0168  0.0035  114 VAL B CA  
1821 C C   . VAL B 114 ? 0.2650 0.2766 0.2083 0.0007  0.0215  0.0024  114 VAL B C   
1822 O O   . VAL B 114 ? 0.2496 0.2602 0.1862 -0.0007 0.0228  0.0055  114 VAL B O   
1823 C CB  . VAL B 114 ? 0.2596 0.2677 0.2035 0.0023  0.0118  0.0046  114 VAL B CB  
1824 C CG1 . VAL B 114 ? 0.2288 0.2374 0.1688 0.0030  0.0106  0.0005  114 VAL B CG1 
1825 C CG2 . VAL B 114 ? 0.2876 0.2944 0.2379 0.0033  0.0078  0.0061  114 VAL B CG2 
1826 N N   . ILE B 115 ? 0.2338 0.2470 0.1788 0.0014  0.0243  -0.0020 115 ILE B N   
1827 C CA  . ILE B 115 ? 0.2473 0.2617 0.1864 0.0006  0.0293  -0.0041 115 ILE B CA  
1828 C C   . ILE B 115 ? 0.3020 0.3150 0.2329 0.0010  0.0273  -0.0077 115 ILE B C   
1829 O O   . ILE B 115 ? 0.2391 0.2518 0.1738 0.0022  0.0245  -0.0106 115 ILE B O   
1830 C CB  . ILE B 115 ? 0.3130 0.3302 0.2608 0.0013  0.0342  -0.0067 115 ILE B CB  
1831 C CG1 . ILE B 115 ? 0.3112 0.3300 0.2681 0.0008  0.0353  -0.0032 115 ILE B CG1 
1832 C CG2 . ILE B 115 ? 0.3579 0.3761 0.2995 0.0006  0.0400  -0.0093 115 ILE B CG2 
1833 C CD1 . ILE B 115 ? 0.2686 0.2875 0.2209 -0.0012 0.0383  0.0008  115 ILE B CD1 
1834 N N   . ARG B 116 ? 0.3423 0.3544 0.2618 -0.0003 0.0286  -0.0073 116 ARG B N   
1835 C CA  . ARG B 116 ? 0.3619 0.3728 0.2728 -0.0003 0.0266  -0.0109 116 ARG B CA  
1836 C C   . ARG B 116 ? 0.4312 0.4428 0.3359 -0.0010 0.0325  -0.0146 116 ARG B C   
1837 O O   . ARG B 116 ? 0.4405 0.4532 0.3435 -0.0020 0.0376  -0.0128 116 ARG B O   
1838 C CB  . ARG B 116 ? 0.4093 0.4183 0.3111 -0.0011 0.0215  -0.0075 116 ARG B CB  
1839 C CG  . ARG B 116 ? 0.5514 0.5594 0.4430 -0.0016 0.0192  -0.0108 116 ARG B CG  
1840 C CD  . ARG B 116 ? 0.6145 0.6210 0.4934 -0.0030 0.0174  -0.0072 116 ARG B CD  
1841 N NE  . ARG B 116 ? 0.5965 0.6021 0.4655 -0.0036 0.0145  -0.0106 116 ARG B NE  
1842 C CZ  . ARG B 116 ? 0.5808 0.5864 0.4518 -0.0029 0.0090  -0.0127 116 ARG B CZ  
1843 N NH1 . ARG B 116 ? 0.5015 0.5077 0.3838 -0.0014 0.0058  -0.0120 116 ARG B NH1 
1844 N NH2 . ARG B 116 ? 0.6088 0.6137 0.4702 -0.0038 0.0065  -0.0159 116 ARG B NH2 
1845 N N   . ARG B 117 ? 0.3060 0.3170 0.2082 -0.0005 0.0321  -0.0200 117 ARG B N   
1846 C CA  . ARG B 117 ? 0.3919 0.4027 0.2868 -0.0012 0.0372  -0.0244 117 ARG B CA  
1847 C C   . ARG B 117 ? 0.3540 0.3628 0.2401 -0.0016 0.0331  -0.0282 117 ARG B C   
1848 O O   . ARG B 117 ? 0.3216 0.3298 0.2120 -0.0008 0.0277  -0.0289 117 ARG B O   
1849 C CB  . ARG B 117 ? 0.3203 0.3327 0.2252 0.0002  0.0424  -0.0284 117 ARG B CB  
1850 C CG  . ARG B 117 ? 0.4601 0.4751 0.3750 0.0006  0.0463  -0.0249 117 ARG B CG  
1851 C CD  . ARG B 117 ? 0.4951 0.5119 0.4071 -0.0001 0.0541  -0.0258 117 ARG B CD  
1852 N NE  . ARG B 117 ? 0.5468 0.5666 0.4696 0.0001  0.0574  -0.0225 117 ARG B NE  
1853 C CZ  . ARG B 117 ? 0.5990 0.6194 0.5231 -0.0011 0.0559  -0.0167 117 ARG B CZ  
1854 N NH1 . ARG B 117 ? 0.4659 0.4838 0.3817 -0.0022 0.0511  -0.0133 117 ARG B NH1 
1855 N NH2 . ARG B 117 ? 0.4977 0.5210 0.4320 -0.0011 0.0592  -0.0142 117 ARG B NH2 
1856 N N   . SER B 118 ? 0.3769 0.3847 0.2506 -0.0029 0.0358  -0.0308 118 SER B N   
1857 C CA  . SER B 118 ? 0.4440 0.4498 0.3080 -0.0037 0.0317  -0.0344 118 SER B CA  
1858 C C   . SER B 118 ? 0.5308 0.5357 0.3842 -0.0048 0.0372  -0.0392 118 SER B C   
1859 O O   . SER B 118 ? 0.4173 0.4232 0.2685 -0.0051 0.0437  -0.0383 118 SER B O   
1860 C CB  . SER B 118 ? 0.4802 0.4852 0.3356 -0.0048 0.0254  -0.0297 118 SER B CB  
1861 O OG  . SER B 118 ? 0.5136 0.5188 0.3614 -0.0060 0.0282  -0.0250 118 SER B OG  
1862 N N   . ARG B 119 ? 0.4592 0.4621 0.3058 -0.0053 0.0346  -0.0445 119 ARG B N   
1863 C CA  . ARG B 119 ? 0.5323 0.5337 0.3671 -0.0065 0.0394  -0.0497 119 ARG B CA  
1864 C C   . ARG B 119 ? 0.7190 0.7200 0.5382 -0.0086 0.0398  -0.0460 119 ARG B C   
1865 O O   . ARG B 119 ? 0.7850 0.7853 0.5972 -0.0096 0.0331  -0.0426 119 ARG B O   
1866 C CB  . ARG B 119 ? 0.6429 0.6420 0.4737 -0.0070 0.0357  -0.0562 119 ARG B CB  
1867 C CG  . ARG B 119 ? 0.5178 0.5166 0.3629 -0.0052 0.0358  -0.0603 119 ARG B CG  
1868 C CD  . ARG B 119 ? 0.5583 0.5578 0.4120 -0.0036 0.0439  -0.0626 119 ARG B CD  
1869 N NE  . ARG B 119 ? 0.6238 0.6229 0.4912 -0.0019 0.0425  -0.0655 119 ARG B NE  
1870 C CZ  . ARG B 119 ? 0.5041 0.5039 0.3836 0.0001  0.0474  -0.0668 119 ARG B CZ  
1871 N NH1 . ARG B 119 ? 0.4087 0.4100 0.2889 0.0007  0.0548  -0.0667 119 ARG B NH1 
1872 N NH2 . ARG B 119 ? 0.4586 0.4579 0.3501 0.0015  0.0448  -0.0680 119 ARG B NH2 
# 
