data_9OB9
# 
_entry.id   9OB9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   9OB9         pdb_00009ob9 10.2210/pdb9ob9/pdb 
WWPDB D_1000295223 ?            ?                   
# 
_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       2025-04-30 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        9OB9 
_pdbx_database_status.recvd_initial_deposition_date   2025-04-22 
_pdbx_database_status.SG_entry                        Y 
_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 
# 
loop_
_pdbx_contact_author.id 
_pdbx_contact_author.email 
_pdbx_contact_author.name_first 
_pdbx_contact_author.name_last 
_pdbx_contact_author.name_mi 
_pdbx_contact_author.role 
_pdbx_contact_author.identifier_ORCID 
2 swlovell@ku.edu                    Scott    Lovell ? 'principal investigator/group leader' 0000-0002-3215-4472 
3 isabelle.phan@seattlechildrens.org Isabelle Phan   ? 'principal investigator/group leader' 0000-0001-6873-3401 
4 julie.early@seattlechildrens.org   Julie    Early  ? 'principal investigator/group leader' 0000-0003-1224-2747 
5 peter.myler@seattlechildrens.org   Peter    Myler  ? 'principal investigator/group leader' 0000-0002-0056-0513 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Seattle Structural Genomics Center for Infectious Disease'          1 ? 
'Seattle Structural Genomics Center for Infectious Disease (SSGCID)' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To be published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Crystal structure of nucleoside-diphosphate kinase Cryptosporidium parvum in complex with ADP and CTP' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, L.'        1 0000-0003-0514-281X 
primary 'Lovell, S.'     2 0000-0002-3215-4472 
primary 'Battaile, K.P.' 3 0000-0003-0833-3259 
# 
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 'nucleoside-diphosphate kinase' 17612.361 3   2.7.4.6 ? ? ? 
2 non-polymer syn "CYTIDINE-5'-TRIPHOSPHATE"      483.156   3   ?       ? ? ? 
3 non-polymer syn "ADENOSINE-5'-DIPHOSPHATE"      427.201   3   ?       ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                 24.305    3   ?       ? ? ? 
5 water       nat water                           18.015    372 ?       ? ? ? 
# 
_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       
;MAHHHHHHVEQTYLMIKPDGIQRQVVGEIISRFEKRGYRIAAMKLTIATPAILEEHYAEHKGKPFLPGLIEKMTGPVLCM
VFEGVDVIAQARKMMGSTRPGEAAPGTIRADFCQQAGRNLIHGSDSAESAKREISLWFKPEEIQSYKLALSDYIFE
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MAHHHHHHVEQTYLMIKPDGIQRQVVGEIISRFEKRGYRIAAMKLTIATPAILEEHYAEHKGKPFLPGLIEKMTGPVLCM
VFEGVDVIAQARKMMGSTRPGEAAPGTIRADFCQQAGRNLIHGSDSAESAKREISLWFKPEEIQSYKLALSDYIFE
;
_entity_poly.pdbx_strand_id                 A,B,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 "CYTIDINE-5'-TRIPHOSPHATE" CTP 
3 "ADENOSINE-5'-DIPHOSPHATE" ADP 
4 'MAGNESIUM ION'            MG  
5 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   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   VAL n 
1 10  GLU n 
1 11  GLN n 
1 12  THR n 
1 13  TYR n 
1 14  LEU n 
1 15  MET n 
1 16  ILE n 
1 17  LYS n 
1 18  PRO n 
1 19  ASP n 
1 20  GLY n 
1 21  ILE n 
1 22  GLN n 
1 23  ARG n 
1 24  GLN n 
1 25  VAL n 
1 26  VAL n 
1 27  GLY n 
1 28  GLU n 
1 29  ILE n 
1 30  ILE n 
1 31  SER n 
1 32  ARG n 
1 33  PHE n 
1 34  GLU n 
1 35  LYS n 
1 36  ARG n 
1 37  GLY n 
1 38  TYR n 
1 39  ARG n 
1 40  ILE n 
1 41  ALA n 
1 42  ALA n 
1 43  MET n 
1 44  LYS n 
1 45  LEU n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  THR n 
1 50  PRO n 
1 51  ALA n 
1 52  ILE n 
1 53  LEU n 
1 54  GLU n 
1 55  GLU n 
1 56  HIS n 
1 57  TYR n 
1 58  ALA n 
1 59  GLU n 
1 60  HIS n 
1 61  LYS n 
1 62  GLY n 
1 63  LYS n 
1 64  PRO n 
1 65  PHE n 
1 66  LEU n 
1 67  PRO n 
1 68  GLY n 
1 69  LEU n 
1 70  ILE n 
1 71  GLU n 
1 72  LYS n 
1 73  MET n 
1 74  THR n 
1 75  GLY n 
1 76  PRO n 
1 77  VAL n 
1 78  LEU n 
1 79  CYS n 
1 80  MET n 
1 81  VAL n 
1 82  PHE n 
1 83  GLU n 
1 84  GLY n 
1 85  VAL n 
1 86  ASP n 
1 87  VAL n 
1 88  ILE n 
1 89  ALA n 
1 90  GLN n 
1 91  ALA n 
1 92  ARG n 
1 93  LYS n 
1 94  MET n 
1 95  MET n 
1 96  GLY n 
1 97  SER n 
1 98  THR n 
1 99  ARG n 
1 100 PRO n 
1 101 GLY n 
1 102 GLU n 
1 103 ALA n 
1 104 ALA n 
1 105 PRO n 
1 106 GLY n 
1 107 THR n 
1 108 ILE n 
1 109 ARG n 
1 110 ALA n 
1 111 ASP n 
1 112 PHE n 
1 113 CYS n 
1 114 GLN n 
1 115 GLN n 
1 116 ALA n 
1 117 GLY n 
1 118 ARG n 
1 119 ASN n 
1 120 LEU n 
1 121 ILE n 
1 122 HIS n 
1 123 GLY n 
1 124 SER n 
1 125 ASP n 
1 126 SER n 
1 127 ALA n 
1 128 GLU n 
1 129 SER n 
1 130 ALA n 
1 131 LYS n 
1 132 ARG n 
1 133 GLU n 
1 134 ILE n 
1 135 SER n 
1 136 LEU n 
1 137 TRP n 
1 138 PHE n 
1 139 LYS n 
1 140 PRO n 
1 141 GLU n 
1 142 GLU n 
1 143 ILE n 
1 144 GLN n 
1 145 SER n 
1 146 TYR n 
1 147 LYS n 
1 148 LEU n 
1 149 ALA n 
1 150 LEU n 
1 151 SER n 
1 152 ASP n 
1 153 TYR n 
1 154 ILE n 
1 155 PHE n 
1 156 GLU 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                   156 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 cgd4_1940 
_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      'Cryptosporidium parvum Iowa II' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     353152 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       CrpaA.01302.a.B2 
_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 
ADP non-polymer         n "ADENOSINE-5'-DIPHOSPHATE" ? 'C10 H15 N5 O10 P2' 427.201 
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 
CTP non-polymer         . "CYTIDINE-5'-TRIPHOSPHATE" ? 'C9 H16 N3 O14 P3'  483.156 
CYS 'L-peptide linking' y CYSTEINE                   ? 'C3 H7 N O2 S'      121.158 
GLN 'L-peptide linking' y GLUTAMINE                  ? 'C5 H10 N2 O3'      146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'            ? 'C5 H9 N O4'        147.129 
GLY 'peptide linking'   y GLYCINE                    ? 'C2 H5 N O2'        75.067  
HIS 'L-peptide linking' y HISTIDINE                  ? 'C6 H10 N3 O2 1'    156.162 
HOH non-polymer         . WATER                      ? 'H2 O'              18.015  
ILE 'L-peptide linking' y ISOLEUCINE                 ? 'C6 H13 N O2'       131.173 
LEU 'L-peptide linking' y LEUCINE                    ? 'C6 H13 N O2'       131.173 
LYS 'L-peptide linking' y LYSINE                     ? 'C6 H15 N2 O2 1'    147.195 
MET 'L-peptide linking' y METHIONINE                 ? 'C5 H11 N O2 S'     149.211 
MG  non-polymer         . 'MAGNESIUM ION'            ? 'Mg 2'              24.305  
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   18  ?   ?   ?   A . n 
A 1 2   ALA 2   19  ?   ?   ?   A . n 
A 1 3   HIS 3   20  ?   ?   ?   A . n 
A 1 4   HIS 4   21  ?   ?   ?   A . n 
A 1 5   HIS 5   22  ?   ?   ?   A . n 
A 1 6   HIS 6   23  ?   ?   ?   A . n 
A 1 7   HIS 7   24  ?   ?   ?   A . n 
A 1 8   HIS 8   25  25  HIS HIS A . n 
A 1 9   VAL 9   26  26  VAL VAL A . n 
A 1 10  GLU 10  27  27  GLU GLU A . n 
A 1 11  GLN 11  28  28  GLN GLN A . n 
A 1 12  THR 12  29  29  THR THR A . n 
A 1 13  TYR 13  30  30  TYR TYR A . n 
A 1 14  LEU 14  31  31  LEU LEU A . n 
A 1 15  MET 15  32  32  MET MET A . n 
A 1 16  ILE 16  33  33  ILE ILE A . n 
A 1 17  LYS 17  34  34  LYS LYS A . n 
A 1 18  PRO 18  35  35  PRO PRO A . n 
A 1 19  ASP 19  36  36  ASP ASP A . n 
A 1 20  GLY 20  37  37  GLY GLY A . n 
A 1 21  ILE 21  38  38  ILE ILE A . n 
A 1 22  GLN 22  39  39  GLN GLN A . n 
A 1 23  ARG 23  40  40  ARG ARG A . n 
A 1 24  GLN 24  41  41  GLN GLN A . n 
A 1 25  VAL 25  42  42  VAL VAL A . n 
A 1 26  VAL 26  43  43  VAL VAL A . n 
A 1 27  GLY 27  44  44  GLY GLY A . n 
A 1 28  GLU 28  45  45  GLU GLU A . n 
A 1 29  ILE 29  46  46  ILE ILE A . n 
A 1 30  ILE 30  47  47  ILE ILE A . n 
A 1 31  SER 31  48  48  SER SER A . n 
A 1 32  ARG 32  49  49  ARG ARG A . n 
A 1 33  PHE 33  50  50  PHE PHE A . n 
A 1 34  GLU 34  51  51  GLU GLU A . n 
A 1 35  LYS 35  52  52  LYS LYS A . n 
A 1 36  ARG 36  53  53  ARG ARG A . n 
A 1 37  GLY 37  54  54  GLY GLY A . n 
A 1 38  TYR 38  55  55  TYR TYR A . n 
A 1 39  ARG 39  56  56  ARG ARG A . n 
A 1 40  ILE 40  57  57  ILE ILE A . n 
A 1 41  ALA 41  58  58  ALA ALA A . n 
A 1 42  ALA 42  59  59  ALA ALA A . n 
A 1 43  MET 43  60  60  MET MET A . n 
A 1 44  LYS 44  61  61  LYS LYS A . n 
A 1 45  LEU 45  62  62  LEU LEU A . n 
A 1 46  THR 46  63  63  THR THR A . n 
A 1 47  ILE 47  64  64  ILE ILE A . n 
A 1 48  ALA 48  65  65  ALA ALA A . n 
A 1 49  THR 49  66  66  THR THR A . n 
A 1 50  PRO 50  67  67  PRO PRO A . n 
A 1 51  ALA 51  68  68  ALA ALA A . n 
A 1 52  ILE 52  69  69  ILE ILE A . n 
A 1 53  LEU 53  70  70  LEU LEU A . n 
A 1 54  GLU 54  71  71  GLU GLU A . n 
A 1 55  GLU 55  72  72  GLU GLU A . n 
A 1 56  HIS 56  73  73  HIS HIS A . n 
A 1 57  TYR 57  74  74  TYR TYR A . n 
A 1 58  ALA 58  75  75  ALA ALA A . n 
A 1 59  GLU 59  76  76  GLU GLU A . n 
A 1 60  HIS 60  77  77  HIS HIS A . n 
A 1 61  LYS 61  78  78  LYS LYS A . n 
A 1 62  GLY 62  79  79  GLY GLY A . n 
A 1 63  LYS 63  80  80  LYS LYS A . n 
A 1 64  PRO 64  81  81  PRO PRO A . n 
A 1 65  PHE 65  82  82  PHE PHE A . n 
A 1 66  LEU 66  83  83  LEU LEU A . n 
A 1 67  PRO 67  84  84  PRO PRO A . n 
A 1 68  GLY 68  85  85  GLY GLY A . n 
A 1 69  LEU 69  86  86  LEU LEU A . n 
A 1 70  ILE 70  87  87  ILE ILE A . n 
A 1 71  GLU 71  88  88  GLU GLU A . n 
A 1 72  LYS 72  89  89  LYS LYS A . n 
A 1 73  MET 73  90  90  MET MET A . n 
A 1 74  THR 74  91  91  THR THR A . n 
A 1 75  GLY 75  92  92  GLY GLY A . n 
A 1 76  PRO 76  93  93  PRO PRO A . n 
A 1 77  VAL 77  94  94  VAL VAL A . n 
A 1 78  LEU 78  95  95  LEU LEU A . n 
A 1 79  CYS 79  96  96  CYS CYS A . n 
A 1 80  MET 80  97  97  MET MET A . n 
A 1 81  VAL 81  98  98  VAL VAL A . n 
A 1 82  PHE 82  99  99  PHE PHE A . n 
A 1 83  GLU 83  100 100 GLU GLU A . n 
A 1 84  GLY 84  101 101 GLY GLY A . n 
A 1 85  VAL 85  102 102 VAL VAL A . n 
A 1 86  ASP 86  103 103 ASP ASP A . n 
A 1 87  VAL 87  104 104 VAL VAL A . n 
A 1 88  ILE 88  105 105 ILE ILE A . n 
A 1 89  ALA 89  106 106 ALA ALA A . n 
A 1 90  GLN 90  107 107 GLN GLN A . n 
A 1 91  ALA 91  108 108 ALA ALA A . n 
A 1 92  ARG 92  109 109 ARG ARG A . n 
A 1 93  LYS 93  110 110 LYS LYS A . n 
A 1 94  MET 94  111 111 MET MET A . n 
A 1 95  MET 95  112 112 MET MET A . n 
A 1 96  GLY 96  113 113 GLY GLY A . n 
A 1 97  SER 97  114 114 SER SER A . n 
A 1 98  THR 98  115 115 THR THR A . n 
A 1 99  ARG 99  116 116 ARG ARG A . n 
A 1 100 PRO 100 117 117 PRO PRO A . n 
A 1 101 GLY 101 118 118 GLY GLY A . n 
A 1 102 GLU 102 119 119 GLU GLU A . n 
A 1 103 ALA 103 120 120 ALA ALA A . n 
A 1 104 ALA 104 121 121 ALA ALA A . n 
A 1 105 PRO 105 122 122 PRO PRO A . n 
A 1 106 GLY 106 123 123 GLY GLY A . n 
A 1 107 THR 107 124 124 THR THR A . n 
A 1 108 ILE 108 125 125 ILE ILE A . n 
A 1 109 ARG 109 126 126 ARG ARG A . n 
A 1 110 ALA 110 127 127 ALA ALA A . n 
A 1 111 ASP 111 128 128 ASP ASP A . n 
A 1 112 PHE 112 129 129 PHE PHE A . n 
A 1 113 CYS 113 130 130 CYS CYS A . n 
A 1 114 GLN 114 131 131 GLN GLN A . n 
A 1 115 GLN 115 132 132 GLN GLN A . n 
A 1 116 ALA 116 133 133 ALA ALA A . n 
A 1 117 GLY 117 134 134 GLY GLY A . n 
A 1 118 ARG 118 135 135 ARG ARG A . n 
A 1 119 ASN 119 136 136 ASN ASN A . n 
A 1 120 LEU 120 137 137 LEU LEU A . n 
A 1 121 ILE 121 138 138 ILE ILE A . n 
A 1 122 HIS 122 139 139 HIS HIS A . n 
A 1 123 GLY 123 140 140 GLY GLY A . n 
A 1 124 SER 124 141 141 SER SER A . n 
A 1 125 ASP 125 142 142 ASP ASP A . n 
A 1 126 SER 126 143 143 SER SER A . n 
A 1 127 ALA 127 144 144 ALA ALA A . n 
A 1 128 GLU 128 145 145 GLU GLU A . n 
A 1 129 SER 129 146 146 SER SER A . n 
A 1 130 ALA 130 147 147 ALA ALA A . n 
A 1 131 LYS 131 148 148 LYS LYS A . n 
A 1 132 ARG 132 149 149 ARG ARG A . n 
A 1 133 GLU 133 150 150 GLU GLU A . n 
A 1 134 ILE 134 151 151 ILE ILE A . n 
A 1 135 SER 135 152 152 SER SER A . n 
A 1 136 LEU 136 153 153 LEU LEU A . n 
A 1 137 TRP 137 154 154 TRP TRP A . n 
A 1 138 PHE 138 155 155 PHE PHE A . n 
A 1 139 LYS 139 156 156 LYS LYS A . n 
A 1 140 PRO 140 157 157 PRO PRO A . n 
A 1 141 GLU 141 158 158 GLU GLU A . n 
A 1 142 GLU 142 159 159 GLU GLU A . n 
A 1 143 ILE 143 160 160 ILE ILE A . n 
A 1 144 GLN 144 161 161 GLN GLN A . n 
A 1 145 SER 145 162 162 SER SER A . n 
A 1 146 TYR 146 163 163 TYR TYR A . n 
A 1 147 LYS 147 164 164 LYS LYS A . n 
A 1 148 LEU 148 165 165 LEU LEU A . n 
A 1 149 ALA 149 166 166 ALA ALA A . n 
A 1 150 LEU 150 167 167 LEU LEU A . n 
A 1 151 SER 151 168 168 SER SER A . n 
A 1 152 ASP 152 169 169 ASP ASP A . n 
A 1 153 TYR 153 170 170 TYR TYR A . n 
A 1 154 ILE 154 171 171 ILE ILE A . n 
A 1 155 PHE 155 172 172 PHE PHE A . n 
A 1 156 GLU 156 173 173 GLU GLU A . n 
B 1 1   MET 1   18  ?   ?   ?   B . n 
B 1 2   ALA 2   19  ?   ?   ?   B . n 
B 1 3   HIS 3   20  ?   ?   ?   B . n 
B 1 4   HIS 4   21  ?   ?   ?   B . n 
B 1 5   HIS 5   22  ?   ?   ?   B . n 
B 1 6   HIS 6   23  ?   ?   ?   B . n 
B 1 7   HIS 7   24  ?   ?   ?   B . n 
B 1 8   HIS 8   25  25  HIS HIS B . n 
B 1 9   VAL 9   26  26  VAL VAL B . n 
B 1 10  GLU 10  27  27  GLU GLU B . n 
B 1 11  GLN 11  28  28  GLN GLN B . n 
B 1 12  THR 12  29  29  THR THR B . n 
B 1 13  TYR 13  30  30  TYR TYR B . n 
B 1 14  LEU 14  31  31  LEU LEU B . n 
B 1 15  MET 15  32  32  MET MET B . n 
B 1 16  ILE 16  33  33  ILE ILE B . n 
B 1 17  LYS 17  34  34  LYS LYS B . n 
B 1 18  PRO 18  35  35  PRO PRO B . n 
B 1 19  ASP 19  36  36  ASP ASP B . n 
B 1 20  GLY 20  37  37  GLY GLY B . n 
B 1 21  ILE 21  38  38  ILE ILE B . n 
B 1 22  GLN 22  39  39  GLN GLN B . n 
B 1 23  ARG 23  40  40  ARG ARG B . n 
B 1 24  GLN 24  41  41  GLN GLN B . n 
B 1 25  VAL 25  42  42  VAL VAL B . n 
B 1 26  VAL 26  43  43  VAL VAL B . n 
B 1 27  GLY 27  44  44  GLY GLY B . n 
B 1 28  GLU 28  45  45  GLU GLU B . n 
B 1 29  ILE 29  46  46  ILE ILE B . n 
B 1 30  ILE 30  47  47  ILE ILE B . n 
B 1 31  SER 31  48  48  SER SER B . n 
B 1 32  ARG 32  49  49  ARG ARG B . n 
B 1 33  PHE 33  50  50  PHE PHE B . n 
B 1 34  GLU 34  51  51  GLU GLU B . n 
B 1 35  LYS 35  52  52  LYS LYS B . n 
B 1 36  ARG 36  53  53  ARG ARG B . n 
B 1 37  GLY 37  54  54  GLY GLY B . n 
B 1 38  TYR 38  55  55  TYR TYR B . n 
B 1 39  ARG 39  56  56  ARG ARG B . n 
B 1 40  ILE 40  57  57  ILE ILE B . n 
B 1 41  ALA 41  58  58  ALA ALA B . n 
B 1 42  ALA 42  59  59  ALA ALA B . n 
B 1 43  MET 43  60  60  MET MET B . n 
B 1 44  LYS 44  61  61  LYS LYS B . n 
B 1 45  LEU 45  62  62  LEU LEU B . n 
B 1 46  THR 46  63  63  THR THR B . n 
B 1 47  ILE 47  64  64  ILE ILE B . n 
B 1 48  ALA 48  65  65  ALA ALA B . n 
B 1 49  THR 49  66  66  THR THR B . n 
B 1 50  PRO 50  67  67  PRO PRO B . n 
B 1 51  ALA 51  68  68  ALA ALA B . n 
B 1 52  ILE 52  69  69  ILE ILE B . n 
B 1 53  LEU 53  70  70  LEU LEU B . n 
B 1 54  GLU 54  71  71  GLU GLU B . n 
B 1 55  GLU 55  72  72  GLU GLU B . n 
B 1 56  HIS 56  73  73  HIS HIS B . n 
B 1 57  TYR 57  74  74  TYR TYR B . n 
B 1 58  ALA 58  75  75  ALA ALA B . n 
B 1 59  GLU 59  76  76  GLU GLU B . n 
B 1 60  HIS 60  77  77  HIS HIS B . n 
B 1 61  LYS 61  78  78  LYS LYS B . n 
B 1 62  GLY 62  79  79  GLY GLY B . n 
B 1 63  LYS 63  80  80  LYS LYS B . n 
B 1 64  PRO 64  81  81  PRO PRO B . n 
B 1 65  PHE 65  82  82  PHE PHE B . n 
B 1 66  LEU 66  83  83  LEU LEU B . n 
B 1 67  PRO 67  84  84  PRO PRO B . n 
B 1 68  GLY 68  85  85  GLY GLY B . n 
B 1 69  LEU 69  86  86  LEU LEU B . n 
B 1 70  ILE 70  87  87  ILE ILE B . n 
B 1 71  GLU 71  88  88  GLU GLU B . n 
B 1 72  LYS 72  89  89  LYS LYS B . n 
B 1 73  MET 73  90  90  MET MET B . n 
B 1 74  THR 74  91  91  THR THR B . n 
B 1 75  GLY 75  92  92  GLY GLY B . n 
B 1 76  PRO 76  93  93  PRO PRO B . n 
B 1 77  VAL 77  94  94  VAL VAL B . n 
B 1 78  LEU 78  95  95  LEU LEU B . n 
B 1 79  CYS 79  96  96  CYS CYS B . n 
B 1 80  MET 80  97  97  MET MET B . n 
B 1 81  VAL 81  98  98  VAL VAL B . n 
B 1 82  PHE 82  99  99  PHE PHE B . n 
B 1 83  GLU 83  100 100 GLU GLU B . n 
B 1 84  GLY 84  101 101 GLY GLY B . n 
B 1 85  VAL 85  102 102 VAL VAL B . n 
B 1 86  ASP 86  103 103 ASP ASP B . n 
B 1 87  VAL 87  104 104 VAL VAL B . n 
B 1 88  ILE 88  105 105 ILE ILE B . n 
B 1 89  ALA 89  106 106 ALA ALA B . n 
B 1 90  GLN 90  107 107 GLN GLN B . n 
B 1 91  ALA 91  108 108 ALA ALA B . n 
B 1 92  ARG 92  109 109 ARG ARG B . n 
B 1 93  LYS 93  110 110 LYS LYS B . n 
B 1 94  MET 94  111 111 MET MET B . n 
B 1 95  MET 95  112 112 MET MET B . n 
B 1 96  GLY 96  113 113 GLY GLY B . n 
B 1 97  SER 97  114 114 SER SER B . n 
B 1 98  THR 98  115 115 THR THR B . n 
B 1 99  ARG 99  116 116 ARG ARG B . n 
B 1 100 PRO 100 117 117 PRO PRO B . n 
B 1 101 GLY 101 118 118 GLY GLY B . n 
B 1 102 GLU 102 119 119 GLU GLU B . n 
B 1 103 ALA 103 120 120 ALA ALA B . n 
B 1 104 ALA 104 121 121 ALA ALA B . n 
B 1 105 PRO 105 122 122 PRO PRO B . n 
B 1 106 GLY 106 123 123 GLY GLY B . n 
B 1 107 THR 107 124 124 THR THR B . n 
B 1 108 ILE 108 125 125 ILE ILE B . n 
B 1 109 ARG 109 126 126 ARG ARG B . n 
B 1 110 ALA 110 127 127 ALA ALA B . n 
B 1 111 ASP 111 128 128 ASP ASP B . n 
B 1 112 PHE 112 129 129 PHE PHE B . n 
B 1 113 CYS 113 130 130 CYS CYS B . n 
B 1 114 GLN 114 131 131 GLN GLN B . n 
B 1 115 GLN 115 132 132 GLN GLN B . n 
B 1 116 ALA 116 133 133 ALA ALA B . n 
B 1 117 GLY 117 134 134 GLY GLY B . n 
B 1 118 ARG 118 135 135 ARG ARG B . n 
B 1 119 ASN 119 136 136 ASN ASN B . n 
B 1 120 LEU 120 137 137 LEU LEU B . n 
B 1 121 ILE 121 138 138 ILE ILE B . n 
B 1 122 HIS 122 139 139 HIS HIS B . n 
B 1 123 GLY 123 140 140 GLY GLY B . n 
B 1 124 SER 124 141 141 SER SER B . n 
B 1 125 ASP 125 142 142 ASP ASP B . n 
B 1 126 SER 126 143 143 SER SER B . n 
B 1 127 ALA 127 144 144 ALA ALA B . n 
B 1 128 GLU 128 145 145 GLU GLU B . n 
B 1 129 SER 129 146 146 SER SER B . n 
B 1 130 ALA 130 147 147 ALA ALA B . n 
B 1 131 LYS 131 148 148 LYS LYS B . n 
B 1 132 ARG 132 149 149 ARG ARG B . n 
B 1 133 GLU 133 150 150 GLU GLU B . n 
B 1 134 ILE 134 151 151 ILE ILE B . n 
B 1 135 SER 135 152 152 SER SER B . n 
B 1 136 LEU 136 153 153 LEU LEU B . n 
B 1 137 TRP 137 154 154 TRP TRP B . n 
B 1 138 PHE 138 155 155 PHE PHE B . n 
B 1 139 LYS 139 156 156 LYS LYS B . n 
B 1 140 PRO 140 157 157 PRO PRO B . n 
B 1 141 GLU 141 158 158 GLU GLU B . n 
B 1 142 GLU 142 159 159 GLU GLU B . n 
B 1 143 ILE 143 160 160 ILE ILE B . n 
B 1 144 GLN 144 161 161 GLN GLN B . n 
B 1 145 SER 145 162 162 SER SER B . n 
B 1 146 TYR 146 163 163 TYR TYR B . n 
B 1 147 LYS 147 164 164 LYS LYS B . n 
B 1 148 LEU 148 165 165 LEU LEU B . n 
B 1 149 ALA 149 166 166 ALA ALA B . n 
B 1 150 LEU 150 167 167 LEU LEU B . n 
B 1 151 SER 151 168 168 SER SER B . n 
B 1 152 ASP 152 169 169 ASP ASP B . n 
B 1 153 TYR 153 170 170 TYR TYR B . n 
B 1 154 ILE 154 171 171 ILE ILE B . n 
B 1 155 PHE 155 172 172 PHE PHE B . n 
B 1 156 GLU 156 173 173 GLU GLU B . n 
C 1 1   MET 1   18  ?   ?   ?   C . n 
C 1 2   ALA 2   19  ?   ?   ?   C . n 
C 1 3   HIS 3   20  ?   ?   ?   C . n 
C 1 4   HIS 4   21  ?   ?   ?   C . n 
C 1 5   HIS 5   22  ?   ?   ?   C . n 
C 1 6   HIS 6   23  ?   ?   ?   C . n 
C 1 7   HIS 7   24  ?   ?   ?   C . n 
C 1 8   HIS 8   25  25  HIS HIS C . n 
C 1 9   VAL 9   26  26  VAL VAL C . n 
C 1 10  GLU 10  27  27  GLU GLU C . n 
C 1 11  GLN 11  28  28  GLN GLN C . n 
C 1 12  THR 12  29  29  THR THR C . n 
C 1 13  TYR 13  30  30  TYR TYR C . n 
C 1 14  LEU 14  31  31  LEU LEU C . n 
C 1 15  MET 15  32  32  MET MET C . n 
C 1 16  ILE 16  33  33  ILE ILE C . n 
C 1 17  LYS 17  34  34  LYS LYS C . n 
C 1 18  PRO 18  35  35  PRO PRO C . n 
C 1 19  ASP 19  36  36  ASP ASP C . n 
C 1 20  GLY 20  37  37  GLY GLY C . n 
C 1 21  ILE 21  38  38  ILE ILE C . n 
C 1 22  GLN 22  39  39  GLN GLN C . n 
C 1 23  ARG 23  40  40  ARG ARG C . n 
C 1 24  GLN 24  41  41  GLN GLN C . n 
C 1 25  VAL 25  42  42  VAL VAL C . n 
C 1 26  VAL 26  43  43  VAL VAL C . n 
C 1 27  GLY 27  44  44  GLY GLY C . n 
C 1 28  GLU 28  45  45  GLU GLU C . n 
C 1 29  ILE 29  46  46  ILE ILE C . n 
C 1 30  ILE 30  47  47  ILE ILE C . n 
C 1 31  SER 31  48  48  SER SER C . n 
C 1 32  ARG 32  49  49  ARG ARG C . n 
C 1 33  PHE 33  50  50  PHE PHE C . n 
C 1 34  GLU 34  51  51  GLU GLU C . n 
C 1 35  LYS 35  52  52  LYS LYS C . n 
C 1 36  ARG 36  53  53  ARG ARG C . n 
C 1 37  GLY 37  54  54  GLY GLY C . n 
C 1 38  TYR 38  55  55  TYR TYR C . n 
C 1 39  ARG 39  56  56  ARG ARG C . n 
C 1 40  ILE 40  57  57  ILE ILE C . n 
C 1 41  ALA 41  58  58  ALA ALA C . n 
C 1 42  ALA 42  59  59  ALA ALA C . n 
C 1 43  MET 43  60  60  MET MET C . n 
C 1 44  LYS 44  61  61  LYS LYS C . n 
C 1 45  LEU 45  62  62  LEU LEU C . n 
C 1 46  THR 46  63  63  THR THR C . n 
C 1 47  ILE 47  64  64  ILE ILE C . n 
C 1 48  ALA 48  65  65  ALA ALA C . n 
C 1 49  THR 49  66  66  THR THR C . n 
C 1 50  PRO 50  67  67  PRO PRO C . n 
C 1 51  ALA 51  68  68  ALA ALA C . n 
C 1 52  ILE 52  69  69  ILE ILE C . n 
C 1 53  LEU 53  70  70  LEU LEU C . n 
C 1 54  GLU 54  71  71  GLU GLU C . n 
C 1 55  GLU 55  72  72  GLU GLU C . n 
C 1 56  HIS 56  73  73  HIS HIS C . n 
C 1 57  TYR 57  74  74  TYR TYR C . n 
C 1 58  ALA 58  75  75  ALA ALA C . n 
C 1 59  GLU 59  76  76  GLU GLU C . n 
C 1 60  HIS 60  77  77  HIS HIS C . n 
C 1 61  LYS 61  78  78  LYS LYS C . n 
C 1 62  GLY 62  79  79  GLY GLY C . n 
C 1 63  LYS 63  80  80  LYS LYS C . n 
C 1 64  PRO 64  81  81  PRO PRO C . n 
C 1 65  PHE 65  82  82  PHE PHE C . n 
C 1 66  LEU 66  83  83  LEU LEU C . n 
C 1 67  PRO 67  84  84  PRO PRO C . n 
C 1 68  GLY 68  85  85  GLY GLY C . n 
C 1 69  LEU 69  86  86  LEU LEU C . n 
C 1 70  ILE 70  87  87  ILE ILE C . n 
C 1 71  GLU 71  88  88  GLU GLU C . n 
C 1 72  LYS 72  89  89  LYS LYS C . n 
C 1 73  MET 73  90  90  MET MET C . n 
C 1 74  THR 74  91  91  THR THR C . n 
C 1 75  GLY 75  92  92  GLY GLY C . n 
C 1 76  PRO 76  93  93  PRO PRO C . n 
C 1 77  VAL 77  94  94  VAL VAL C . n 
C 1 78  LEU 78  95  95  LEU LEU C . n 
C 1 79  CYS 79  96  96  CYS CYS C . n 
C 1 80  MET 80  97  97  MET MET C . n 
C 1 81  VAL 81  98  98  VAL VAL C . n 
C 1 82  PHE 82  99  99  PHE PHE C . n 
C 1 83  GLU 83  100 100 GLU GLU C . n 
C 1 84  GLY 84  101 101 GLY GLY C . n 
C 1 85  VAL 85  102 102 VAL VAL C . n 
C 1 86  ASP 86  103 103 ASP ASP C . n 
C 1 87  VAL 87  104 104 VAL VAL C . n 
C 1 88  ILE 88  105 105 ILE ILE C . n 
C 1 89  ALA 89  106 106 ALA ALA C . n 
C 1 90  GLN 90  107 107 GLN GLN C . n 
C 1 91  ALA 91  108 108 ALA ALA C . n 
C 1 92  ARG 92  109 109 ARG ARG C . n 
C 1 93  LYS 93  110 110 LYS LYS C . n 
C 1 94  MET 94  111 111 MET MET C . n 
C 1 95  MET 95  112 112 MET MET C . n 
C 1 96  GLY 96  113 113 GLY GLY C . n 
C 1 97  SER 97  114 114 SER SER C . n 
C 1 98  THR 98  115 115 THR THR C . n 
C 1 99  ARG 99  116 116 ARG ARG C . n 
C 1 100 PRO 100 117 117 PRO PRO C . n 
C 1 101 GLY 101 118 118 GLY GLY C . n 
C 1 102 GLU 102 119 119 GLU GLU C . n 
C 1 103 ALA 103 120 120 ALA ALA C . n 
C 1 104 ALA 104 121 121 ALA ALA C . n 
C 1 105 PRO 105 122 122 PRO PRO C . n 
C 1 106 GLY 106 123 123 GLY GLY C . n 
C 1 107 THR 107 124 124 THR THR C . n 
C 1 108 ILE 108 125 125 ILE ILE C . n 
C 1 109 ARG 109 126 126 ARG ARG C . n 
C 1 110 ALA 110 127 127 ALA ALA C . n 
C 1 111 ASP 111 128 128 ASP ASP C . n 
C 1 112 PHE 112 129 129 PHE PHE C . n 
C 1 113 CYS 113 130 130 CYS CYS C . n 
C 1 114 GLN 114 131 131 GLN GLN C . n 
C 1 115 GLN 115 132 132 GLN GLN C . n 
C 1 116 ALA 116 133 133 ALA ALA C . n 
C 1 117 GLY 117 134 134 GLY GLY C . n 
C 1 118 ARG 118 135 135 ARG ARG C . n 
C 1 119 ASN 119 136 136 ASN ASN C . n 
C 1 120 LEU 120 137 137 LEU LEU C . n 
C 1 121 ILE 121 138 138 ILE ILE C . n 
C 1 122 HIS 122 139 139 HIS HIS C . n 
C 1 123 GLY 123 140 140 GLY GLY C . n 
C 1 124 SER 124 141 141 SER SER C . n 
C 1 125 ASP 125 142 142 ASP ASP C . n 
C 1 126 SER 126 143 143 SER SER C . n 
C 1 127 ALA 127 144 144 ALA ALA C . n 
C 1 128 GLU 128 145 145 GLU GLU C . n 
C 1 129 SER 129 146 146 SER SER C . n 
C 1 130 ALA 130 147 147 ALA ALA C . n 
C 1 131 LYS 131 148 148 LYS LYS C . n 
C 1 132 ARG 132 149 149 ARG ARG C . n 
C 1 133 GLU 133 150 150 GLU GLU C . n 
C 1 134 ILE 134 151 151 ILE ILE C . n 
C 1 135 SER 135 152 152 SER SER C . n 
C 1 136 LEU 136 153 153 LEU LEU C . n 
C 1 137 TRP 137 154 154 TRP TRP C . n 
C 1 138 PHE 138 155 155 PHE PHE C . n 
C 1 139 LYS 139 156 156 LYS LYS C . n 
C 1 140 PRO 140 157 157 PRO PRO C . n 
C 1 141 GLU 141 158 158 GLU GLU C . n 
C 1 142 GLU 142 159 159 GLU GLU C . n 
C 1 143 ILE 143 160 160 ILE ILE C . n 
C 1 144 GLN 144 161 161 GLN GLN C . n 
C 1 145 SER 145 162 162 SER SER C . n 
C 1 146 TYR 146 163 163 TYR TYR C . n 
C 1 147 LYS 147 164 164 LYS LYS C . n 
C 1 148 LEU 148 165 165 LEU LEU C . n 
C 1 149 ALA 149 166 166 ALA ALA C . n 
C 1 150 LEU 150 167 167 LEU LEU C . n 
C 1 151 SER 151 168 168 SER SER C . n 
C 1 152 ASP 152 169 169 ASP ASP C . n 
C 1 153 TYR 153 170 170 TYR TYR C . n 
C 1 154 ILE 154 171 171 ILE ILE C . n 
C 1 155 PHE 155 172 172 PHE PHE C . n 
C 1 156 GLU 156 173 173 GLU GLU C . n 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 ADP ? ? ADP ? ? 'SUBJECT OF INVESTIGATION' ? 
2 CTP ? ? CTP ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
D 2 CTP 1   201 101 CTP CTP A . 
E 3 ADP 1   202 201 ADP ADP A . 
F 4 MG  1   203 302 MG  MG  A . 
G 2 CTP 1   201 102 CTP CTP B . 
H 3 ADP 1   202 202 ADP ADP B . 
I 4 MG  1   203 303 MG  MG  B . 
J 2 CTP 1   201 103 CTP CTP C . 
K 3 ADP 1   202 203 ADP ADP C . 
L 4 MG  1   203 301 MG  MG  C . 
M 5 HOH 1   301 347 HOH HOH A . 
M 5 HOH 2   302 141 HOH HOH A . 
M 5 HOH 3   303 175 HOH HOH A . 
M 5 HOH 4   304 61  HOH HOH A . 
M 5 HOH 5   305 351 HOH HOH A . 
M 5 HOH 6   306 137 HOH HOH A . 
M 5 HOH 7   307 310 HOH HOH A . 
M 5 HOH 8   308 326 HOH HOH A . 
M 5 HOH 9   309 370 HOH HOH A . 
M 5 HOH 10  310 352 HOH HOH A . 
M 5 HOH 11  311 107 HOH HOH A . 
M 5 HOH 12  312 233 HOH HOH A . 
M 5 HOH 13  313 115 HOH HOH A . 
M 5 HOH 14  314 15  HOH HOH A . 
M 5 HOH 15  315 34  HOH HOH A . 
M 5 HOH 16  316 289 HOH HOH A . 
M 5 HOH 17  317 18  HOH HOH A . 
M 5 HOH 18  318 354 HOH HOH A . 
M 5 HOH 19  319 104 HOH HOH A . 
M 5 HOH 20  320 280 HOH HOH A . 
M 5 HOH 21  321 109 HOH HOH A . 
M 5 HOH 22  322 3   HOH HOH A . 
M 5 HOH 23  323 273 HOH HOH A . 
M 5 HOH 24  324 294 HOH HOH A . 
M 5 HOH 25  325 305 HOH HOH A . 
M 5 HOH 26  326 325 HOH HOH A . 
M 5 HOH 27  327 88  HOH HOH A . 
M 5 HOH 28  328 174 HOH HOH A . 
M 5 HOH 29  329 218 HOH HOH A . 
M 5 HOH 30  330 228 HOH HOH A . 
M 5 HOH 31  331 369 HOH HOH A . 
M 5 HOH 32  332 260 HOH HOH A . 
M 5 HOH 33  333 265 HOH HOH A . 
M 5 HOH 34  334 134 HOH HOH A . 
M 5 HOH 35  335 304 HOH HOH A . 
M 5 HOH 36  336 23  HOH HOH A . 
M 5 HOH 37  337 11  HOH HOH A . 
M 5 HOH 38  338 164 HOH HOH A . 
M 5 HOH 39  339 17  HOH HOH A . 
M 5 HOH 40  340 135 HOH HOH A . 
M 5 HOH 41  341 208 HOH HOH A . 
M 5 HOH 42  342 28  HOH HOH A . 
M 5 HOH 43  343 16  HOH HOH A . 
M 5 HOH 44  344 2   HOH HOH A . 
M 5 HOH 45  345 226 HOH HOH A . 
M 5 HOH 46  346 4   HOH HOH A . 
M 5 HOH 47  347 38  HOH HOH A . 
M 5 HOH 48  348 72  HOH HOH A . 
M 5 HOH 49  349 37  HOH HOH A . 
M 5 HOH 50  350 350 HOH HOH A . 
M 5 HOH 51  351 111 HOH HOH A . 
M 5 HOH 52  352 207 HOH HOH A . 
M 5 HOH 53  353 123 HOH HOH A . 
M 5 HOH 54  354 5   HOH HOH A . 
M 5 HOH 55  355 92  HOH HOH A . 
M 5 HOH 56  356 297 HOH HOH A . 
M 5 HOH 57  357 62  HOH HOH A . 
M 5 HOH 58  358 41  HOH HOH A . 
M 5 HOH 59  359 145 HOH HOH A . 
M 5 HOH 60  360 189 HOH HOH A . 
M 5 HOH 61  361 150 HOH HOH A . 
M 5 HOH 62  362 56  HOH HOH A . 
M 5 HOH 63  363 36  HOH HOH A . 
M 5 HOH 64  364 281 HOH HOH A . 
M 5 HOH 65  365 158 HOH HOH A . 
M 5 HOH 66  366 19  HOH HOH A . 
M 5 HOH 67  367 67  HOH HOH A . 
M 5 HOH 68  368 221 HOH HOH A . 
M 5 HOH 69  369 9   HOH HOH A . 
M 5 HOH 70  370 83  HOH HOH A . 
M 5 HOH 71  371 97  HOH HOH A . 
M 5 HOH 72  372 276 HOH HOH A . 
M 5 HOH 73  373 266 HOH HOH A . 
M 5 HOH 74  374 91  HOH HOH A . 
M 5 HOH 75  375 95  HOH HOH A . 
M 5 HOH 76  376 99  HOH HOH A . 
M 5 HOH 77  377 76  HOH HOH A . 
M 5 HOH 78  378 247 HOH HOH A . 
M 5 HOH 79  379 20  HOH HOH A . 
M 5 HOH 80  380 149 HOH HOH A . 
M 5 HOH 81  381 46  HOH HOH A . 
M 5 HOH 82  382 98  HOH HOH A . 
M 5 HOH 83  383 271 HOH HOH A . 
M 5 HOH 84  384 85  HOH HOH A . 
M 5 HOH 85  385 140 HOH HOH A . 
M 5 HOH 86  386 193 HOH HOH A . 
M 5 HOH 87  387 295 HOH HOH A . 
M 5 HOH 88  388 144 HOH HOH A . 
M 5 HOH 89  389 106 HOH HOH A . 
M 5 HOH 90  390 89  HOH HOH A . 
M 5 HOH 91  391 177 HOH HOH A . 
M 5 HOH 92  392 84  HOH HOH A . 
M 5 HOH 93  393 25  HOH HOH A . 
M 5 HOH 94  394 51  HOH HOH A . 
M 5 HOH 95  395 127 HOH HOH A . 
M 5 HOH 96  396 311 HOH HOH A . 
M 5 HOH 97  397 330 HOH HOH A . 
M 5 HOH 98  398 268 HOH HOH A . 
M 5 HOH 99  399 361 HOH HOH A . 
M 5 HOH 100 400 308 HOH HOH A . 
M 5 HOH 101 401 119 HOH HOH A . 
M 5 HOH 102 402 172 HOH HOH A . 
M 5 HOH 103 403 210 HOH HOH A . 
M 5 HOH 104 404 120 HOH HOH A . 
M 5 HOH 105 405 10  HOH HOH A . 
M 5 HOH 106 406 244 HOH HOH A . 
M 5 HOH 107 407 252 HOH HOH A . 
M 5 HOH 108 408 199 HOH HOH A . 
M 5 HOH 109 409 192 HOH HOH A . 
M 5 HOH 110 410 372 HOH HOH A . 
M 5 HOH 111 411 256 HOH HOH A . 
M 5 HOH 112 412 188 HOH HOH A . 
M 5 HOH 113 413 269 HOH HOH A . 
M 5 HOH 114 414 238 HOH HOH A . 
M 5 HOH 115 415 249 HOH HOH A . 
M 5 HOH 116 416 101 HOH HOH A . 
M 5 HOH 117 417 358 HOH HOH A . 
M 5 HOH 118 418 197 HOH HOH A . 
M 5 HOH 119 419 346 HOH HOH A . 
M 5 HOH 120 420 359 HOH HOH A . 
M 5 HOH 121 421 300 HOH HOH A . 
M 5 HOH 122 422 185 HOH HOH A . 
M 5 HOH 123 423 121 HOH HOH A . 
M 5 HOH 124 424 219 HOH HOH A . 
M 5 HOH 125 425 222 HOH HOH A . 
M 5 HOH 126 426 215 HOH HOH A . 
M 5 HOH 127 427 45  HOH HOH A . 
M 5 HOH 128 428 293 HOH HOH A . 
M 5 HOH 129 429 360 HOH HOH A . 
M 5 HOH 130 430 291 HOH HOH A . 
M 5 HOH 131 431 243 HOH HOH A . 
M 5 HOH 132 432 148 HOH HOH A . 
M 5 HOH 133 433 263 HOH HOH A . 
M 5 HOH 134 434 318 HOH HOH A . 
M 5 HOH 135 435 335 HOH HOH A . 
M 5 HOH 136 436 213 HOH HOH A . 
M 5 HOH 137 437 368 HOH HOH A . 
M 5 HOH 138 438 371 HOH HOH A . 
M 5 HOH 139 439 201 HOH HOH A . 
M 5 HOH 140 440 232 HOH HOH A . 
M 5 HOH 141 441 251 HOH HOH A . 
N 5 HOH 1   301 353 HOH HOH B . 
N 5 HOH 2   302 272 HOH HOH B . 
N 5 HOH 3   303 303 HOH HOH B . 
N 5 HOH 4   304 153 HOH HOH B . 
N 5 HOH 5   305 279 HOH HOH B . 
N 5 HOH 6   306 170 HOH HOH B . 
N 5 HOH 7   307 302 HOH HOH B . 
N 5 HOH 8   308 173 HOH HOH B . 
N 5 HOH 9   309 146 HOH HOH B . 
N 5 HOH 10  310 50  HOH HOH B . 
N 5 HOH 11  311 274 HOH HOH B . 
N 5 HOH 12  312 317 HOH HOH B . 
N 5 HOH 13  313 316 HOH HOH B . 
N 5 HOH 14  314 54  HOH HOH B . 
N 5 HOH 15  315 125 HOH HOH B . 
N 5 HOH 16  316 286 HOH HOH B . 
N 5 HOH 17  317 63  HOH HOH B . 
N 5 HOH 18  318 264 HOH HOH B . 
N 5 HOH 19  319 349 HOH HOH B . 
N 5 HOH 20  320 57  HOH HOH B . 
N 5 HOH 21  321 78  HOH HOH B . 
N 5 HOH 22  322 74  HOH HOH B . 
N 5 HOH 23  323 198 HOH HOH B . 
N 5 HOH 24  324 166 HOH HOH B . 
N 5 HOH 25  325 112 HOH HOH B . 
N 5 HOH 26  326 283 HOH HOH B . 
N 5 HOH 27  327 209 HOH HOH B . 
N 5 HOH 28  328 195 HOH HOH B . 
N 5 HOH 29  329 167 HOH HOH B . 
N 5 HOH 30  330 52  HOH HOH B . 
N 5 HOH 31  331 58  HOH HOH B . 
N 5 HOH 32  332 13  HOH HOH B . 
N 5 HOH 33  333 181 HOH HOH B . 
N 5 HOH 34  334 159 HOH HOH B . 
N 5 HOH 35  335 248 HOH HOH B . 
N 5 HOH 36  336 328 HOH HOH B . 
N 5 HOH 37  337 332 HOH HOH B . 
N 5 HOH 38  338 24  HOH HOH B . 
N 5 HOH 39  339 27  HOH HOH B . 
N 5 HOH 40  340 102 HOH HOH B . 
N 5 HOH 41  341 105 HOH HOH B . 
N 5 HOH 42  342 31  HOH HOH B . 
N 5 HOH 43  343 309 HOH HOH B . 
N 5 HOH 44  344 47  HOH HOH B . 
N 5 HOH 45  345 301 HOH HOH B . 
N 5 HOH 46  346 254 HOH HOH B . 
N 5 HOH 47  347 114 HOH HOH B . 
N 5 HOH 48  348 49  HOH HOH B . 
N 5 HOH 49  349 220 HOH HOH B . 
N 5 HOH 50  350 39  HOH HOH B . 
N 5 HOH 51  351 29  HOH HOH B . 
N 5 HOH 52  352 245 HOH HOH B . 
N 5 HOH 53  353 235 HOH HOH B . 
N 5 HOH 54  354 138 HOH HOH B . 
N 5 HOH 55  355 108 HOH HOH B . 
N 5 HOH 56  356 229 HOH HOH B . 
N 5 HOH 57  357 184 HOH HOH B . 
N 5 HOH 58  358 225 HOH HOH B . 
N 5 HOH 59  359 340 HOH HOH B . 
N 5 HOH 60  360 117 HOH HOH B . 
N 5 HOH 61  361 70  HOH HOH B . 
N 5 HOH 62  362 139 HOH HOH B . 
N 5 HOH 63  363 314 HOH HOH B . 
N 5 HOH 64  364 128 HOH HOH B . 
N 5 HOH 65  365 154 HOH HOH B . 
N 5 HOH 66  366 323 HOH HOH B . 
N 5 HOH 67  367 126 HOH HOH B . 
N 5 HOH 68  368 200 HOH HOH B . 
N 5 HOH 69  369 306 HOH HOH B . 
N 5 HOH 70  370 239 HOH HOH B . 
N 5 HOH 71  371 124 HOH HOH B . 
N 5 HOH 72  372 55  HOH HOH B . 
N 5 HOH 73  373 131 HOH HOH B . 
N 5 HOH 74  374 253 HOH HOH B . 
N 5 HOH 75  375 44  HOH HOH B . 
N 5 HOH 76  376 142 HOH HOH B . 
N 5 HOH 77  377 180 HOH HOH B . 
N 5 HOH 78  378 355 HOH HOH B . 
N 5 HOH 79  379 224 HOH HOH B . 
N 5 HOH 80  380 204 HOH HOH B . 
N 5 HOH 81  381 59  HOH HOH B . 
N 5 HOH 82  382 143 HOH HOH B . 
N 5 HOH 83  383 241 HOH HOH B . 
N 5 HOH 84  384 242 HOH HOH B . 
N 5 HOH 85  385 290 HOH HOH B . 
N 5 HOH 86  386 288 HOH HOH B . 
N 5 HOH 87  387 214 HOH HOH B . 
N 5 HOH 88  388 206 HOH HOH B . 
N 5 HOH 89  389 345 HOH HOH B . 
N 5 HOH 90  390 30  HOH HOH B . 
N 5 HOH 91  391 230 HOH HOH B . 
N 5 HOH 92  392 319 HOH HOH B . 
N 5 HOH 93  393 255 HOH HOH B . 
N 5 HOH 94  394 48  HOH HOH B . 
N 5 HOH 95  395 327 HOH HOH B . 
N 5 HOH 96  396 257 HOH HOH B . 
N 5 HOH 97  397 287 HOH HOH B . 
N 5 HOH 98  398 227 HOH HOH B . 
N 5 HOH 99  399 223 HOH HOH B . 
N 5 HOH 100 400 336 HOH HOH B . 
N 5 HOH 101 401 152 HOH HOH B . 
N 5 HOH 102 402 298 HOH HOH B . 
N 5 HOH 103 403 285 HOH HOH B . 
O 5 HOH 1   301 169 HOH HOH C . 
O 5 HOH 2   302 341 HOH HOH C . 
O 5 HOH 3   303 362 HOH HOH C . 
O 5 HOH 4   304 331 HOH HOH C . 
O 5 HOH 5   305 171 HOH HOH C . 
O 5 HOH 6   306 163 HOH HOH C . 
O 5 HOH 7   307 357 HOH HOH C . 
O 5 HOH 8   308 356 HOH HOH C . 
O 5 HOH 9   309 80  HOH HOH C . 
O 5 HOH 10  310 363 HOH HOH C . 
O 5 HOH 11  311 79  HOH HOH C . 
O 5 HOH 12  312 179 HOH HOH C . 
O 5 HOH 13  313 299 HOH HOH C . 
O 5 HOH 14  314 113 HOH HOH C . 
O 5 HOH 15  315 329 HOH HOH C . 
O 5 HOH 16  316 71  HOH HOH C . 
O 5 HOH 17  317 338 HOH HOH C . 
O 5 HOH 18  318 212 HOH HOH C . 
O 5 HOH 19  319 22  HOH HOH C . 
O 5 HOH 20  320 160 HOH HOH C . 
O 5 HOH 21  321 133 HOH HOH C . 
O 5 HOH 22  322 315 HOH HOH C . 
O 5 HOH 23  323 116 HOH HOH C . 
O 5 HOH 24  324 267 HOH HOH C . 
O 5 HOH 25  325 21  HOH HOH C . 
O 5 HOH 26  326 100 HOH HOH C . 
O 5 HOH 27  327 231 HOH HOH C . 
O 5 HOH 28  328 348 HOH HOH C . 
O 5 HOH 29  329 110 HOH HOH C . 
O 5 HOH 30  330 313 HOH HOH C . 
O 5 HOH 31  331 147 HOH HOH C . 
O 5 HOH 32  332 32  HOH HOH C . 
O 5 HOH 33  333 136 HOH HOH C . 
O 5 HOH 34  334 33  HOH HOH C . 
O 5 HOH 35  335 53  HOH HOH C . 
O 5 HOH 36  336 130 HOH HOH C . 
O 5 HOH 37  337 35  HOH HOH C . 
O 5 HOH 38  338 156 HOH HOH C . 
O 5 HOH 39  339 211 HOH HOH C . 
O 5 HOH 40  340 165 HOH HOH C . 
O 5 HOH 41  341 194 HOH HOH C . 
O 5 HOH 42  342 12  HOH HOH C . 
O 5 HOH 43  343 26  HOH HOH C . 
O 5 HOH 44  344 282 HOH HOH C . 
O 5 HOH 45  345 65  HOH HOH C . 
O 5 HOH 46  346 277 HOH HOH C . 
O 5 HOH 47  347 77  HOH HOH C . 
O 5 HOH 48  348 14  HOH HOH C . 
O 5 HOH 49  349 151 HOH HOH C . 
O 5 HOH 50  350 90  HOH HOH C . 
O 5 HOH 51  351 68  HOH HOH C . 
O 5 HOH 52  352 155 HOH HOH C . 
O 5 HOH 53  353 7   HOH HOH C . 
O 5 HOH 54  354 186 HOH HOH C . 
O 5 HOH 55  355 296 HOH HOH C . 
O 5 HOH 56  356 157 HOH HOH C . 
O 5 HOH 57  357 60  HOH HOH C . 
O 5 HOH 58  358 216 HOH HOH C . 
O 5 HOH 59  359 364 HOH HOH C . 
O 5 HOH 60  360 103 HOH HOH C . 
O 5 HOH 61  361 270 HOH HOH C . 
O 5 HOH 62  362 6   HOH HOH C . 
O 5 HOH 63  363 162 HOH HOH C . 
O 5 HOH 64  364 1   HOH HOH C . 
O 5 HOH 65  365 132 HOH HOH C . 
O 5 HOH 66  366 240 HOH HOH C . 
O 5 HOH 67  367 322 HOH HOH C . 
O 5 HOH 68  368 321 HOH HOH C . 
O 5 HOH 69  369 82  HOH HOH C . 
O 5 HOH 70  370 96  HOH HOH C . 
O 5 HOH 71  371 87  HOH HOH C . 
O 5 HOH 72  372 122 HOH HOH C . 
O 5 HOH 73  373 183 HOH HOH C . 
O 5 HOH 74  374 236 HOH HOH C . 
O 5 HOH 75  375 261 HOH HOH C . 
O 5 HOH 76  376 93  HOH HOH C . 
O 5 HOH 77  377 129 HOH HOH C . 
O 5 HOH 78  378 365 HOH HOH C . 
O 5 HOH 79  379 196 HOH HOH C . 
O 5 HOH 80  380 64  HOH HOH C . 
O 5 HOH 81  381 307 HOH HOH C . 
O 5 HOH 82  382 161 HOH HOH C . 
O 5 HOH 83  383 258 HOH HOH C . 
O 5 HOH 84  384 191 HOH HOH C . 
O 5 HOH 85  385 66  HOH HOH C . 
O 5 HOH 86  386 275 HOH HOH C . 
O 5 HOH 87  387 344 HOH HOH C . 
O 5 HOH 88  388 176 HOH HOH C . 
O 5 HOH 89  389 43  HOH HOH C . 
O 5 HOH 90  390 8   HOH HOH C . 
O 5 HOH 91  391 337 HOH HOH C . 
O 5 HOH 92  392 86  HOH HOH C . 
O 5 HOH 93  393 118 HOH HOH C . 
O 5 HOH 94  394 69  HOH HOH C . 
O 5 HOH 95  395 339 HOH HOH C . 
O 5 HOH 96  396 40  HOH HOH C . 
O 5 HOH 97  397 259 HOH HOH C . 
O 5 HOH 98  398 312 HOH HOH C . 
O 5 HOH 99  399 284 HOH HOH C . 
O 5 HOH 100 400 262 HOH HOH C . 
O 5 HOH 101 401 73  HOH HOH C . 
O 5 HOH 102 402 343 HOH HOH C . 
O 5 HOH 103 403 42  HOH HOH C . 
O 5 HOH 104 404 333 HOH HOH C . 
O 5 HOH 105 405 292 HOH HOH C . 
O 5 HOH 106 406 320 HOH HOH C . 
O 5 HOH 107 407 342 HOH HOH C . 
O 5 HOH 108 408 202 HOH HOH C . 
O 5 HOH 109 409 190 HOH HOH C . 
O 5 HOH 110 410 168 HOH HOH C . 
O 5 HOH 111 411 237 HOH HOH C . 
O 5 HOH 112 412 250 HOH HOH C . 
O 5 HOH 113 413 217 HOH HOH C . 
O 5 HOH 114 414 94  HOH HOH C . 
O 5 HOH 115 415 246 HOH HOH C . 
O 5 HOH 116 416 324 HOH HOH C . 
O 5 HOH 117 417 182 HOH HOH C . 
O 5 HOH 118 418 81  HOH HOH C . 
O 5 HOH 119 419 366 HOH HOH C . 
O 5 HOH 120 420 334 HOH HOH C . 
O 5 HOH 121 421 367 HOH HOH C . 
O 5 HOH 122 422 278 HOH HOH C . 
O 5 HOH 123 423 75  HOH HOH C . 
O 5 HOH 124 424 203 HOH HOH C . 
O 5 HOH 125 425 187 HOH HOH C . 
O 5 HOH 126 426 178 HOH HOH C . 
O 5 HOH 127 427 205 HOH HOH C . 
O 5 HOH 128 428 234 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A HIS 25 ? CG  ? A HIS 8 CG  
2  1 Y 1 A HIS 25 ? ND1 ? A HIS 8 ND1 
3  1 Y 1 A HIS 25 ? CD2 ? A HIS 8 CD2 
4  1 Y 1 A HIS 25 ? CE1 ? A HIS 8 CE1 
5  1 Y 1 A HIS 25 ? NE2 ? A HIS 8 NE2 
6  1 Y 1 B HIS 25 ? CG  ? B HIS 8 CG  
7  1 Y 1 B HIS 25 ? ND1 ? B HIS 8 ND1 
8  1 Y 1 B HIS 25 ? CD2 ? B HIS 8 CD2 
9  1 Y 1 B HIS 25 ? CE1 ? B HIS 8 CE1 
10 1 Y 1 B HIS 25 ? NE2 ? B HIS 8 NE2 
11 1 Y 1 C HIS 25 ? CG  ? C HIS 8 CG  
12 1 Y 1 C HIS 25 ? ND1 ? C HIS 8 ND1 
13 1 Y 1 C HIS 25 ? CD2 ? C HIS 8 CD2 
14 1 Y 1 C HIS 25 ? CE1 ? C HIS 8 CE1 
15 1 Y 1 C HIS 25 ? NE2 ? C HIS 8 NE2 
# 
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_reference_DOI 
_software.pdbx_ordinal 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? '(dev_5438: ???)' ? 1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? .                 ? 2 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .                 ? 3 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHASER      ? ? ? .                 ? 4 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? .                 ? 5 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  120.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9OB9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     69.784 
_cell.length_a_esd                 ? 
_cell.length_b                     69.784 
_cell.length_b_esd                 ? 
_cell.length_c                     315.704 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        36 
_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                         9OB9 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                179 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 65 2 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                   9OB9 
_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             2.10 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          41.43 
_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              5.5 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Berkeley F12: 25% MPD, 0.1M sodium Formate, 0.1M Citrate pH 5.5. CrpaA.01302.a.B2.PW39348 at 8.9 mg/mL. Crystals soaked for 4 hours in 10mM ADP and CTP, 5mM MgCl2 in 40% MPD, 0.1M sodium Formate, 0.1M Citrate pH 5.5. Partial ADP and CTP occupancy at same sites. plate Liu-S-177 D2, Puck: PSL-0514, Cryo: direct from soaking solution
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2025-04-05 
_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                    'Double Crystal Si 111' 
_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   0.9786 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'NSLS-II BEAMLINE 19-ID' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9786 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   19-ID 
_diffrn_source.pdbx_synchrotron_site       NSLS-II 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9OB9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.60 
_reflns.d_resolution_low                               47.98 
_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                                     61450 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                16.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          18.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.93 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.105 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       1030537 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.102 
_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                                    1.60 
_reflns_shell.d_res_low                                     1.64 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           31376 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             4320 
_reflns_shell.percent_possible_obs                          97.7 
_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                               7.3 
_reflns_shell.pdbx_chi_squared                              0.66 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.7 
_reflns_shell.pdbx_Rrim_I_all                               0.991 
_reflns_shell.pdbx_Rpim_I_all                               0.361 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.816 
_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                                  0.920 
_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                                 9OB9 
_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                            1.60 
_refine.ls_d_res_low                             47.98 
_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                     61289 
_refine.ls_number_reflns_R_free                  3066 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.65 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1515 
_refine.ls_R_factor_R_free                       0.1785 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1500 
_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.correlation_coeff_I_to_Fcsqd_work        ? 
_refine.correlation_coeff_I_to_Fcsqd_free        ? 
_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                          1.35 
_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             1.10 
_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                 16.76 
_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                            0.15 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.60 
_refine_hist.d_res_low                        47.98 
_refine_hist.number_atoms_solvent             372 
_refine_hist.number_atoms_total               4044 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3501 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         171 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_Zscore 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? 3833 ? f_bond_d           ? ? ? 
'X-RAY DIFFRACTION' ? 1.161  ? 5225 ? f_angle_d          ? ? ? 
'X-RAY DIFFRACTION' ? 18.289 ? 1509 ? f_dihedral_angle_d ? ? ? 
'X-RAY DIFFRACTION' ? 0.057  ? 566  ? f_chiral_restr     ? ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 653  ? 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.correlation_coeff_Fo_to_Fc 
_refine_ls_shell.correlation_coeff_Fo_to_Fc_free 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_work 
_refine_ls_shell.correlation_coeff_I_to_Fcsqd_free 
_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' 1.60 1.62  . . 131 2537 97.00  . . . . 0.2536 . . . . . . . . . . . . . . . 0.2844 
'X-RAY DIFFRACTION' 1.63 1.65  . . 130 2512 98.00  . . . . 0.2390 . . . . . . . . . . . . . . . 0.2499 
'X-RAY DIFFRACTION' 1.65 1.68  . . 115 2582 99.00  . . . . 0.2034 . . . . . . . . . . . . . . . 0.2235 
'X-RAY DIFFRACTION' 1.68 1.71  . . 141 2573 99.00  . . . . 0.1870 . . . . . . . . . . . . . . . 0.2177 
'X-RAY DIFFRACTION' 1.71 1.74  . . 148 2610 100.00 . . . . 0.1706 . . . . . . . . . . . . . . . 0.2314 
'X-RAY DIFFRACTION' 1.74 1.78  . . 122 2602 100.00 . . . . 0.1646 . . . . . . . . . . . . . . . 0.1927 
'X-RAY DIFFRACTION' 1.78 1.82  . . 138 2586 100.00 . . . . 0.1558 . . . . . . . . . . . . . . . 0.1989 
'X-RAY DIFFRACTION' 1.82 1.86  . . 151 2597 100.00 . . . . 0.1556 . . . . . . . . . . . . . . . 0.1802 
'X-RAY DIFFRACTION' 1.86 1.91  . . 117 2624 100.00 . . . . 0.1586 . . . . . . . . . . . . . . . 0.1845 
'X-RAY DIFFRACTION' 1.91 1.96  . . 145 2611 100.00 . . . . 0.1701 . . . . . . . . . . . . . . . 0.2004 
'X-RAY DIFFRACTION' 1.96 2.02  . . 141 2629 100.00 . . . . 0.1451 . . . . . . . . . . . . . . . 0.1943 
'X-RAY DIFFRACTION' 2.02 2.08  . . 153 2615 100.00 . . . . 0.1432 . . . . . . . . . . . . . . . 0.1773 
'X-RAY DIFFRACTION' 2.08 2.16  . . 130 2633 100.00 . . . . 0.1381 . . . . . . . . . . . . . . . 0.1598 
'X-RAY DIFFRACTION' 2.16 2.24  . . 152 2646 100.00 . . . . 0.1360 . . . . . . . . . . . . . . . 0.1955 
'X-RAY DIFFRACTION' 2.24 2.34  . . 123 2650 100.00 . . . . 0.1390 . . . . . . . . . . . . . . . 0.1803 
'X-RAY DIFFRACTION' 2.34 2.47  . . 159 2634 100.00 . . . . 0.1388 . . . . . . . . . . . . . . . 0.1870 
'X-RAY DIFFRACTION' 2.47 2.62  . . 147 2656 100.00 . . . . 0.1455 . . . . . . . . . . . . . . . 0.1668 
'X-RAY DIFFRACTION' 2.62 2.82  . . 134 2686 100.00 . . . . 0.1472 . . . . . . . . . . . . . . . 0.1699 
'X-RAY DIFFRACTION' 2.82 3.11  . . 157 2697 100.00 . . . . 0.1495 . . . . . . . . . . . . . . . 0.1727 
'X-RAY DIFFRACTION' 3.11 3.56  . . 148 2734 100.00 . . . . 0.1401 . . . . . . . . . . . . . . . 0.1634 
'X-RAY DIFFRACTION' 3.56 4.48  . . 146 2787 100.00 . . . . 0.1257 . . . . . . . . . . . . . . . 0.1478 
'X-RAY DIFFRACTION' 4.48 47.98 . . 138 3022 100.00 . . . . 0.1649 . . . . . . . . . . . . . . . 0.1826 
# 
_struct.entry_id                     9OB9 
_struct.title                        
'Crystal structure of nucleoside-diphosphate kinase from Cryptosporidium parvum in complex with with ADP and CTP' 
_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        9OB9 
_struct_keywords.text            
'SSGCID, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 2 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q5CR64_CRYPI 
_struct_ref.pdbx_db_accession          Q5CR64 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VEQTYLMIKPDGIQRQVVGEIISRFEKRGYRIAAMKLTIATPAILEEHYAEHKGKPFLPGLIEKMTGPVLCMVFEGVDVI
AQARKMMGSTRPGEAAPGTIRADFCQQAGRNLIHGSDSAESAKREISLWFKPEEIQSYKLALSDYIFE
;
_struct_ref.pdbx_align_begin           26 
# 
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 9OB9 A 9 ? 156 ? Q5CR64 26 ? 173 ? 26 173 
2 1 9OB9 B 9 ? 156 ? Q5CR64 26 ? 173 ? 26 173 
3 1 9OB9 C 9 ? 156 ? Q5CR64 26 ? 173 ? 26 173 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9OB9 MET A 1 ? UNP Q5CR64 ? ? 'expression tag' 18 1  
1 9OB9 ALA A 2 ? UNP Q5CR64 ? ? 'expression tag' 19 2  
1 9OB9 HIS A 3 ? UNP Q5CR64 ? ? 'expression tag' 20 3  
1 9OB9 HIS A 4 ? UNP Q5CR64 ? ? 'expression tag' 21 4  
1 9OB9 HIS A 5 ? UNP Q5CR64 ? ? 'expression tag' 22 5  
1 9OB9 HIS A 6 ? UNP Q5CR64 ? ? 'expression tag' 23 6  
1 9OB9 HIS A 7 ? UNP Q5CR64 ? ? 'expression tag' 24 7  
1 9OB9 HIS A 8 ? UNP Q5CR64 ? ? 'expression tag' 25 8  
2 9OB9 MET B 1 ? UNP Q5CR64 ? ? 'expression tag' 18 9  
2 9OB9 ALA B 2 ? UNP Q5CR64 ? ? 'expression tag' 19 10 
2 9OB9 HIS B 3 ? UNP Q5CR64 ? ? 'expression tag' 20 11 
2 9OB9 HIS B 4 ? UNP Q5CR64 ? ? 'expression tag' 21 12 
2 9OB9 HIS B 5 ? UNP Q5CR64 ? ? 'expression tag' 22 13 
2 9OB9 HIS B 6 ? UNP Q5CR64 ? ? 'expression tag' 23 14 
2 9OB9 HIS B 7 ? UNP Q5CR64 ? ? 'expression tag' 24 15 
2 9OB9 HIS B 8 ? UNP Q5CR64 ? ? 'expression tag' 25 16 
3 9OB9 MET C 1 ? UNP Q5CR64 ? ? 'expression tag' 18 17 
3 9OB9 ALA C 2 ? UNP Q5CR64 ? ? 'expression tag' 19 18 
3 9OB9 HIS C 3 ? UNP Q5CR64 ? ? 'expression tag' 20 19 
3 9OB9 HIS C 4 ? UNP Q5CR64 ? ? 'expression tag' 21 20 
3 9OB9 HIS C 5 ? UNP Q5CR64 ? ? 'expression tag' 22 21 
3 9OB9 HIS C 6 ? UNP Q5CR64 ? ? 'expression tag' 23 22 
3 9OB9 HIS C 7 ? UNP Q5CR64 ? ? 'expression tag' 24 23 
3 9OB9 HIS C 8 ? UNP Q5CR64 ? ? 'expression tag' 25 24 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LYS A 17  ? ARG A 23  ? LYS A 34  ARG A 40  1 ? 7  
HELX_P HELX_P2  AA2 VAL A 25  ? LYS A 35  ? VAL A 42  LYS A 52  1 ? 11 
HELX_P HELX_P3  AA3 THR A 49  ? TYR A 57  ? THR A 66  TYR A 74  1 ? 9  
HELX_P HELX_P4  AA4 ALA A 58  ? LYS A 61  ? ALA A 75  LYS A 78  5 ? 4  
HELX_P HELX_P5  AA5 PHE A 65  ? THR A 74  ? PHE A 82  THR A 91  1 ? 10 
HELX_P HELX_P6  AA6 ASP A 86  ? GLY A 96  ? ASP A 103 GLY A 113 1 ? 11 
HELX_P HELX_P7  AA7 THR A 107 ? CYS A 113 ? THR A 124 CYS A 130 1 ? 7  
HELX_P HELX_P8  AA8 GLN A 115 ? ASN A 119 ? GLN A 132 ASN A 136 5 ? 5  
HELX_P HELX_P9  AA9 SER A 126 ? PHE A 138 ? SER A 143 PHE A 155 1 ? 13 
HELX_P HELX_P10 AB1 LYS A 139 ? ILE A 143 ? LYS A 156 ILE A 160 5 ? 5  
HELX_P HELX_P11 AB2 LEU A 150 ? PHE A 155 ? LEU A 167 PHE A 172 1 ? 6  
HELX_P HELX_P12 AB3 LYS B 17  ? ARG B 23  ? LYS B 34  ARG B 40  1 ? 7  
HELX_P HELX_P13 AB4 VAL B 25  ? LYS B 35  ? VAL B 42  LYS B 52  1 ? 11 
HELX_P HELX_P14 AB5 THR B 49  ? TYR B 57  ? THR B 66  TYR B 74  1 ? 9  
HELX_P HELX_P15 AB6 ALA B 58  ? LYS B 61  ? ALA B 75  LYS B 78  5 ? 4  
HELX_P HELX_P16 AB7 PHE B 65  ? THR B 74  ? PHE B 82  THR B 91  1 ? 10 
HELX_P HELX_P17 AB8 ASP B 86  ? GLY B 96  ? ASP B 103 GLY B 113 1 ? 11 
HELX_P HELX_P18 AB9 ARG B 99  ? ALA B 103 ? ARG B 116 ALA B 120 5 ? 5  
HELX_P HELX_P19 AC1 THR B 107 ? CYS B 113 ? THR B 124 CYS B 130 1 ? 7  
HELX_P HELX_P20 AC2 GLN B 115 ? ASN B 119 ? GLN B 132 ASN B 136 5 ? 5  
HELX_P HELX_P21 AC3 SER B 126 ? PHE B 138 ? SER B 143 PHE B 155 1 ? 13 
HELX_P HELX_P22 AC4 LYS B 139 ? ILE B 143 ? LYS B 156 ILE B 160 5 ? 5  
HELX_P HELX_P23 AC5 LEU B 150 ? PHE B 155 ? LEU B 167 PHE B 172 1 ? 6  
HELX_P HELX_P24 AC6 LYS C 17  ? ARG C 23  ? LYS C 34  ARG C 40  1 ? 7  
HELX_P HELX_P25 AC7 VAL C 25  ? LYS C 35  ? VAL C 42  LYS C 52  1 ? 11 
HELX_P HELX_P26 AC8 THR C 49  ? TYR C 57  ? THR C 66  TYR C 74  1 ? 9  
HELX_P HELX_P27 AC9 ALA C 58  ? LYS C 61  ? ALA C 75  LYS C 78  5 ? 4  
HELX_P HELX_P28 AD1 PHE C 65  ? THR C 74  ? PHE C 82  THR C 91  1 ? 10 
HELX_P HELX_P29 AD2 ASP C 86  ? GLY C 96  ? ASP C 103 GLY C 113 1 ? 11 
HELX_P HELX_P30 AD3 ARG C 99  ? ALA C 103 ? ARG C 116 ALA C 120 5 ? 5  
HELX_P HELX_P31 AD4 THR C 107 ? CYS C 113 ? THR C 124 CYS C 130 1 ? 7  
HELX_P HELX_P32 AD5 GLN C 115 ? ASN C 119 ? GLN C 132 ASN C 136 5 ? 5  
HELX_P HELX_P33 AD6 SER C 126 ? PHE C 138 ? SER C 143 PHE C 155 1 ? 13 
HELX_P HELX_P34 AD7 LYS C 139 ? ILE C 143 ? LYS C 156 ILE C 160 5 ? 5  
HELX_P HELX_P35 AD8 LEU C 150 ? PHE C 155 ? LEU C 167 PHE C 172 1 ? 6  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? D CTP . O1A A ? ? 1_555 F MG  . MG ? ? A CTP 201 A MG  203 1_555 ? ? ? ? ? ? ? 2.242 ? ? 
metalc2  metalc ? ? D CTP . O1B A ? ? 1_555 F MG  . MG ? ? A CTP 201 A MG  203 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc3  metalc ? ? D CTP . O1G A ? ? 1_555 F MG  . MG ? ? A CTP 201 A MG  203 1_555 ? ? ? ? ? ? ? 2.324 ? ? 
metalc4  metalc ? ? E ADP . O2B B ? ? 1_555 F MG  . MG ? ? A ADP 202 A MG  203 1_555 ? ? ? ? ? ? ? 2.365 ? ? 
metalc5  metalc ? ? E ADP . O1A B ? ? 1_555 F MG  . MG ? ? A ADP 202 A MG  203 1_555 ? ? ? ? ? ? ? 2.090 ? ? 
metalc6  metalc ? ? F MG  . MG  ? ? ? 1_555 M HOH . O  ? ? A MG  203 A HOH 373 1_555 ? ? ? ? ? ? ? 2.558 ? ? 
metalc7  metalc ? ? F MG  . MG  ? ? ? 1_555 M HOH . O  ? ? A MG  203 A HOH 374 1_555 ? ? ? ? ? ? ? 2.438 ? ? 
metalc8  metalc ? ? F MG  . MG  ? ? ? 1_555 M HOH . O  ? ? A MG  203 A HOH 389 1_555 ? ? ? ? ? ? ? 2.413 ? ? 
metalc9  metalc ? ? G CTP . O1A A ? ? 1_555 I MG  . MG ? ? B CTP 201 B MG  203 1_555 ? ? ? ? ? ? ? 2.908 ? ? 
metalc10 metalc ? ? G CTP . O1B A ? ? 1_555 I MG  . MG ? ? B CTP 201 B MG  203 1_555 ? ? ? ? ? ? ? 2.402 ? ? 
metalc11 metalc ? ? G CTP . O1G A ? ? 1_555 I MG  . MG ? ? B CTP 201 B MG  203 1_555 ? ? ? ? ? ? ? 2.687 ? ? 
metalc12 metalc ? ? H ADP . O2B B ? ? 1_555 I MG  . MG ? ? B ADP 202 B MG  203 1_555 ? ? ? ? ? ? ? 2.622 ? ? 
metalc13 metalc ? ? H ADP . O1A B ? ? 1_555 I MG  . MG ? ? B ADP 202 B MG  203 1_555 ? ? ? ? ? ? ? 2.541 ? ? 
metalc14 metalc ? ? J CTP . O1A A ? ? 1_555 L MG  . MG ? ? C CTP 201 C MG  203 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc15 metalc ? ? J CTP . O1B A ? ? 1_555 L MG  . MG ? ? C CTP 201 C MG  203 1_555 ? ? ? ? ? ? ? 2.156 ? ? 
metalc16 metalc ? ? J CTP . O1G A ? ? 1_555 L MG  . MG ? ? C CTP 201 C MG  203 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc17 metalc ? ? K ADP . O2B B ? ? 1_555 L MG  . MG ? ? C ADP 202 C MG  203 1_555 ? ? ? ? ? ? ? 2.390 ? ? 
metalc18 metalc ? ? K ADP . O1A B ? ? 1_555 L MG  . MG ? ? C ADP 202 C MG  203 1_555 ? ? ? ? ? ? ? 1.985 ? ? 
metalc19 metalc ? ? L MG  . MG  ? ? ? 1_555 O HOH . O  ? ? C MG  203 C HOH 302 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc20 metalc ? ? L MG  . MG  ? ? ? 1_555 O HOH . O  ? ? C MG  203 C HOH 391 1_555 ? ? ? ? ? ? ? 2.449 ? ? 
metalc21 metalc ? ? L MG  . MG  ? ? ? 1_555 O HOH . O  ? ? C MG  203 C HOH 397 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O1A A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O1B A D CTP . ? A CTP 201 ? 1_555 79.2  ? 
2  O1A A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O1G A D CTP . ? A CTP 201 ? 1_555 94.9  ? 
3  O1B A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O1G A D CTP . ? A CTP 201 ? 1_555 75.3  ? 
4  O1A A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2B B E ADP . ? A ADP 202 ? 1_555 78.5  ? 
5  O1B A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2B B E ADP . ? A ADP 202 ? 1_555 9.4   ? 
6  O1G A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O2B B E ADP . ? A ADP 202 ? 1_555 84.6  ? 
7  O1A A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O1A B E ADP . ? A ADP 202 ? 1_555 7.9   ? 
8  O1B A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O1A B E ADP . ? A ADP 202 ? 1_555 81.4  ? 
9  O1G A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O1A B E ADP . ? A ADP 202 ? 1_555 88.1  ? 
10 O2B B E ADP . ? A ADP 202 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O1A B E ADP . ? A ADP 202 ? 1_555 81.9  ? 
11 O1A A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 373 ? 1_555 90.5  ? 
12 O1B A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 373 ? 1_555 107.2 ? 
13 O1G A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 373 ? 1_555 174.4 ? 
14 O2B B E ADP . ? A ADP 202 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 373 ? 1_555 97.9  ? 
15 O1A B E ADP . ? A ADP 202 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 373 ? 1_555 97.1  ? 
16 O1A A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 374 ? 1_555 95.6  ? 
17 O1B A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 374 ? 1_555 158.6 ? 
18 O1G A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 374 ? 1_555 84.6  ? 
19 O2B B E ADP . ? A ADP 202 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 374 ? 1_555 167.3 ? 
20 O1A B E ADP . ? A ADP 202 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 374 ? 1_555 90.9  ? 
21 O   ? M HOH . ? A HOH 373 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 374 ? 1_555 93.5  ? 
22 O1A A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 389 ? 1_555 173.3 ? 
23 O1B A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 389 ? 1_555 94.3  ? 
24 O1G A D CTP . ? A CTP 201 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 389 ? 1_555 84.9  ? 
25 O2B B E ADP . ? A ADP 202 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 389 ? 1_555 94.8  ? 
26 O1A B E ADP . ? A ADP 202 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 389 ? 1_555 172.6 ? 
27 O   ? M HOH . ? A HOH 373 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 389 ? 1_555 89.9  ? 
28 O   ? M HOH . ? A HOH 374 ? 1_555 MG ? F MG . ? A MG 203 ? 1_555 O   ? M HOH . ? A HOH 389 ? 1_555 91.0  ? 
29 O1A A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O1B A G CTP . ? B CTP 201 ? 1_555 60.1  ? 
30 O1A A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O1G A G CTP . ? B CTP 201 ? 1_555 79.9  ? 
31 O1B A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O1G A G CTP . ? B CTP 201 ? 1_555 65.6  ? 
32 O1A A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O2B B H ADP . ? B ADP 202 ? 1_555 63.2  ? 
33 O1B A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O2B B H ADP . ? B ADP 202 ? 1_555 14.1  ? 
34 O1G A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O2B B H ADP . ? B ADP 202 ? 1_555 79.5  ? 
35 O1A A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O1A B H ADP . ? B ADP 202 ? 1_555 7.7   ? 
36 O1B A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O1A B H ADP . ? B ADP 202 ? 1_555 57.0  ? 
37 O1G A G CTP . ? B CTP 201 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O1A B H ADP . ? B ADP 202 ? 1_555 72.3  ? 
38 O2B B H ADP . ? B ADP 202 ? 1_555 MG ? I MG . ? B MG 203 ? 1_555 O1A B H ADP . ? B ADP 202 ? 1_555 62.0  ? 
39 O1A A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O1B A J CTP . ? C CTP 201 ? 1_555 80.2  ? 
40 O1A A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O1G A J CTP . ? C CTP 201 ? 1_555 95.3  ? 
41 O1B A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O1G A J CTP . ? C CTP 201 ? 1_555 78.4  ? 
42 O1A A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O2B B K ADP . ? C ADP 202 ? 1_555 80.7  ? 
43 O1B A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O2B B K ADP . ? C ADP 202 ? 1_555 6.2   ? 
44 O1G A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O2B B K ADP . ? C ADP 202 ? 1_555 84.4  ? 
45 O1A A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O1A B K ADP . ? C ADP 202 ? 1_555 6.0   ? 
46 O1B A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O1A B K ADP . ? C ADP 202 ? 1_555 77.8  ? 
47 O1G A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O1A B K ADP . ? C ADP 202 ? 1_555 89.5  ? 
48 O2B B K ADP . ? C ADP 202 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O1A B K ADP . ? C ADP 202 ? 1_555 78.9  ? 
49 O1A A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 302 ? 1_555 89.2  ? 
50 O1B A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 302 ? 1_555 108.3 ? 
51 O1G A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 302 ? 1_555 172.6 ? 
52 O2B B K ADP . ? C ADP 202 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 302 ? 1_555 102.1 ? 
53 O1A B K ADP . ? C ADP 202 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 302 ? 1_555 95.1  ? 
54 O1A A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 391 ? 1_555 94.6  ? 
55 O1B A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 391 ? 1_555 162.4 ? 
56 O1G A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 391 ? 1_555 85.5  ? 
57 O2B B K ADP . ? C ADP 202 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 391 ? 1_555 168.4 ? 
58 O1A B K ADP . ? C ADP 202 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 391 ? 1_555 95.3  ? 
59 O   ? O HOH . ? C HOH 302 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 391 ? 1_555 88.3  ? 
60 O1A A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 397 ? 1_555 175.4 ? 
61 O1B A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 397 ? 1_555 95.3  ? 
62 O1G A J CTP . ? C CTP 201 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 397 ? 1_555 82.8  ? 
63 O2B B K ADP . ? C ADP 202 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 397 ? 1_555 94.9  ? 
64 O1A B K ADP . ? C ADP 202 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 397 ? 1_555 170.6 ? 
65 O   ? O HOH . ? C HOH 302 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 397 ? 1_555 93.1  ? 
66 O   ? O HOH . ? C HOH 391 ? 1_555 MG ? L MG . ? C MG 203 ? 1_555 O   ? O HOH . ? C HOH 397 ? 1_555 89.4  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 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 39  ? ILE A 47  ? ARG A 56  ILE A 64  
AA1 2 PRO A 76  ? GLY A 84  ? PRO A 93  GLY A 101 
AA1 3 GLU A 10  ? ILE A 16  ? GLU A 27  ILE A 33  
AA1 4 ILE A 121 ? GLY A 123 ? ILE A 138 GLY A 140 
AA2 1 ARG B 39  ? ILE B 47  ? ARG B 56  ILE B 64  
AA2 2 PRO B 76  ? GLY B 84  ? PRO B 93  GLY B 101 
AA2 3 GLU B 10  ? ILE B 16  ? GLU B 27  ILE B 33  
AA2 4 ILE B 121 ? GLY B 123 ? ILE B 138 GLY B 140 
AA3 1 ARG C 39  ? ILE C 47  ? ARG C 56  ILE C 64  
AA3 2 PRO C 76  ? GLY C 84  ? PRO C 93  GLY C 101 
AA3 3 GLU C 10  ? ILE C 16  ? GLU C 27  ILE C 33  
AA3 4 ILE C 121 ? GLY C 123 ? ILE C 138 GLY C 140 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LYS A 44 ? N LYS A 61  O CYS A 79  ? O CYS A 96  
AA1 2 3 O GLY A 84 ? O GLY A 101 N GLU A 10  ? N GLU A 27  
AA1 3 4 N MET A 15 ? N MET A 32  O HIS A 122 ? O HIS A 139 
AA2 1 2 N LYS B 44 ? N LYS B 61  O CYS B 79  ? O CYS B 96  
AA2 2 3 O GLY B 84 ? O GLY B 101 N GLU B 10  ? N GLU B 27  
AA2 3 4 N MET B 15 ? N MET B 32  O HIS B 122 ? O HIS B 139 
AA3 1 2 N LYS C 44 ? N LYS C 61  O CYS C 79  ? O CYS C 96  
AA3 2 3 O MET C 80 ? O MET C 97  N LEU C 14  ? N LEU C 31  
AA3 3 4 N MET C 15 ? N MET C 32  O HIS C 122 ? O HIS C 139 
# 
_pdbx_entry_details.entry_id                   9OB9 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 TYR A 74  ? ? -99.77 35.34  
2 1 LEU A 137 ? ? 74.06  -29.11 
3 1 TYR B 74  ? ? -98.97 35.26  
4 1 LEU B 137 ? ? 74.35  -29.25 
5 1 LEU C 137 ? ? 73.25  -29.45 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'NIAID, National Institute of Allergy and Infectious Diseases' 
_pdbx_SG_project.full_name_of_center   'Seattle Structural Genomics Center for Infectious Disease' 
_pdbx_SG_project.initial_of_center     SSGCID 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     381 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   M 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 3.2372   37.2027 19.5947 0.0891  ? 0.0398  ? -0.0078 ? 0.1413 ? -0.0103 ? 0.1542 ? 0.0682 ? 
0.0367  ? 0.0808  ? 0.0222 ? 0.0407  ? 0.1609 ? -0.0199 ? -0.0240 ? 0.0556  ? -0.0386 ? -0.0641 ? 0.0076  ? -0.0696 ? -0.1362 ? 
-0.0806 ? 
2  'X-RAY DIFFRACTION' ? refined -14.4037 34.7662 13.5815 0.1030  ? 0.0217  ? -0.0112 ? 0.3489 ? -0.0503 ? 0.2266 ? 0.0416 ? 
-0.0100 ? -0.0341 ? 0.0111 ? -0.0252 ? 0.1517 ? -0.0527 ? -0.0034 ? 0.0404  ? 0.0128  ? -0.0784 ? 0.0530  ? 0.0224  ? -0.1136 ? 
-0.0300 ? 
3  'X-RAY DIFFRACTION' ? refined -11.5308 29.6076 4.3880  0.3694  ? -0.1365 ? 0.0755  ? 0.3914 ? -0.0266 ? 0.1639 ? 0.9609 ? 
-0.0638 ? 0.4906  ? 0.0714 ? -0.0107 ? 0.2579 ? -0.1835 ? 0.0539  ? -0.0015 ? -0.0396 ? -0.0553 ? -0.0216 ? 0.1477  ? -0.0330 ? 
-0.0521 ? 
4  'X-RAY DIFFRACTION' ? refined -11.6418 25.9844 13.6180 0.2040  ? -0.0605 ? 0.0237  ? 0.3566 ? -0.0539 ? 0.2525 ? 0.0022 ? 
-0.0032 ? -0.0007 ? 0.0054 ? -0.0012 ? 0.0016 ? -0.1111 ? 0.0384  ? -0.0001 ? -0.0982 ? -0.0116 ? -0.1239 ? 0.1079  ? -0.0573 ? 
0.0000  ? 
5  'X-RAY DIFFRACTION' ? refined 4.3007   31.9569 11.8511 0.1078  ? 0.0332  ? -0.0103 ? 0.1518 ? -0.0035 ? 0.1677 ? 0.0581 ? 
0.0338  ? 0.0859  ? 0.0663 ? 0.0748  ? 0.1294 ? 0.0033  ? 0.0431  ? 0.0046  ? -0.0509 ? -0.0382 ? 0.0329  ? -0.0138 ? -0.1039 ? 
-0.0408 ? 
6  'X-RAY DIFFRACTION' ? refined -6.6176  43.4075 9.8575  0.1695  ? 0.1008  ? -0.0696 ? 0.2126 ? -0.0246 ? 0.2344 ? 0.0379 ? 
0.0094  ? -0.0527 ? 0.0667 ? -0.0363 ? 0.0896 ? -0.0548 ? -0.0040 ? 0.0844  ? -0.1579 ? -0.1337 ? 0.0737  ? -0.0707 ? -0.0730 ? 
-0.0829 ? 
7  'X-RAY DIFFRACTION' ? refined 6.5135   51.4934 19.1847 0.1950  ? 0.0874  ? -0.0456 ? 0.1279 ? -0.0132 ? 0.2433 ? 0.1214 ? 
-0.0147 ? 0.1965  ? 0.0141 ? -0.0079 ? 0.3081 ? -0.1090 ? 0.0650  ? 0.1193  ? -0.1358 ? -0.0172 ? 0.0501  ? -0.2995 ? -0.0268 ? 
-0.0551 ? 
8  'X-RAY DIFFRACTION' ? refined 18.6668  12.1687 20.9126 0.1989  ? 0.0879  ? 0.0062  ? 0.1428 ? 0.0076  ? 0.1450 ? 0.1730 ? 
0.0779  ? 0.0270  ? 0.0842 ? -0.0693 ? 0.2582 ? -0.0561 ? -0.0268 ? 0.0178  ? 0.0291  ? 0.0409  ? 0.0594  ? 0.3836  ? 0.1226  ? 
0.0052  ? 
9  'X-RAY DIFFRACTION' ? refined 30.0794  -0.6530 9.5144  0.4917  ? 0.2211  ? -0.0465 ? 0.2930 ? -0.0313 ? 0.1655 ? 0.4228 ? 
0.0670  ? 0.2849  ? 0.0090 ? 0.0447  ? 0.1906 ? -0.0274 ? 0.1745  ? -0.0917 ? -0.2329 ? 0.0008  ? 0.0570  ? -0.0699 ? 0.0935  ? 
-0.0105 ? 
10 'X-RAY DIFFRACTION' ? refined 35.3769  4.6976  13.6367 0.3765  ? 0.1953  ? 0.0524  ? 0.3199 ? -0.0089 ? 0.2018 ? 0.0992 ? 
0.0871  ? -0.0106 ? 0.0787 ? -0.0034 ? 0.0138 ? 0.0016  ? 0.0658  ? -0.0062 ? -0.0899 ? -0.0126 ? -0.0084 ? -0.0473 ? 0.0217  ? 
-0.0200 ? 
11 'X-RAY DIFFRACTION' ? refined 21.5219  14.9610 12.4825 0.1751  ? 0.0645  ? -0.0007 ? 0.1504 ? 0.0042  ? 0.1512 ? 0.1141 ? 
0.0291  ? -0.0884 ? 0.0821 ? 0.0482  ? 0.1503 ? -0.0221 ? 0.0709  ? 0.0089  ? -0.0605 ? 0.0380  ? 0.0080  ? 0.2485  ? 0.1435  ? 
0.0248  ? 
12 'X-RAY DIFFRACTION' ? refined 17.4583  -0.3659 12.2286 0.5717  ? 0.0999  ? 0.0164  ? 0.0160 ? -0.0809 ? 0.2251 ? 0.0617 ? 
-0.0040 ? 0.0305  ? 0.0180 ? -0.0157 ? 0.0291 ? -0.0472 ? 0.0138  ? -0.0699 ? 0.0766  ? 0.0278  ? -0.0549 ? 0.1242  ? 0.0285  ? 
-0.0463 ? 
13 'X-RAY DIFFRACTION' ? refined 4.5481   8.3210  22.6563 0.3029  ? -0.0650 ? 0.0219  ? 0.1621 ? 0.0301  ? 0.1486 ? 0.1089 ? 
0.2064  ? 0.0786  ? 0.3986 ? 0.1688  ? 0.0827 ? 0.0371  ? 0.0034  ? 0.0033  ? 0.1258  ? -0.1855 ? 0.1416  ? 0.3371  ? -0.2155 ? 
-0.0471 ? 
14 'X-RAY DIFFRACTION' ? refined 33.8734  40.5478 16.6663 0.1143  ? -0.0094 ? 0.0126  ? 0.2433 ? 0.0169  ? 0.1545 ? 0.0755 ? 
-0.0756 ? -0.0987 ? 0.0720 ? 0.0363  ? 0.3236 ? 0.0319  ? 0.0270  ? 0.0022  ? -0.0209 ? -0.0204 ? -0.0002 ? -0.1340 ? 0.2844  ? 
0.0045  ? 
15 'X-RAY DIFFRACTION' ? refined 33.6558  52.4998 0.5162  0.4191  ? 0.1764  ? 0.0307  ? 0.5942 ? 0.1343  ? 0.1237 ? 0.0004 ? 
-0.0025 ? 0.0001  ? 0.0097 ? 0.0018  ? 0.0005 ? -0.0140 ? 0.0163  ? -0.0009 ? -0.0529 ? -0.0322 ? 0.0072  ? -0.0222 ? -0.0678 ? 
-0.0146 ? 
16 'X-RAY DIFFRACTION' ? refined 30.6239  55.3735 9.9666  0.3250  ? 0.0380  ? 0.0404  ? 0.3002 ? 0.0958  ? 0.2191 ? 0.0018 ? 
0.0004  ? 0.0021  ? 0.0025 ? -0.0050 ? 0.0062 ? 0.1322  ? 0.0963  ? 0.0073  ? -0.0211 ? -0.0366 ? 0.0008  ? -0.0723 ? -0.1050 ? 
0.0000  ? 
17 'X-RAY DIFFRACTION' ? refined 27.5033  38.2402 10.2275 0.1094  ? 0.0073  ? 0.0051  ? 0.2136 ? 0.0213  ? 0.1568 ? 0.0861 ? 
-0.0980 ? -0.0611 ? 0.0828 ? 0.0272  ? 0.1564 ? 0.0099  ? 0.0683  ? -0.0303 ? -0.0631 ? -0.0237 ? 0.0294  ? -0.0746 ? 0.2155  ? 
-0.0075 ? 
18 'X-RAY DIFFRACTION' ? refined 43.1043  32.5774 15.1065 -0.0343 ? 0.0371  ? 0.0276  ? 0.4083 ? 0.0096  ? 0.1569 ? 0.0976 ? 
0.0435  ? 0.0298  ? 0.1206 ? -0.0015 ? 0.1945 ? -0.0460 ? 0.0425  ? -0.0359 ? -0.0548 ? 0.0848  ? -0.1030 ? 0.0373  ? 0.4460  ? 
0.1052  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 25 through 65 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 66 through 73 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 74 through 82 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 83 through 91 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 92 through 143 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 144 through 154 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 155 through 173 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 25 through 65 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 66 through 82 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 83 through 91 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 92 through 143 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 144 through 154 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 155 through 173 )
;
14 'X-RAY DIFFRACTION' 14 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 25 through 73 )
;
15 'X-RAY DIFFRACTION' 15 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 74 through 82 )
;
16 'X-RAY DIFFRACTION' 16 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 83 through 92 )
;
17 'X-RAY DIFFRACTION' 17 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 93 through 143 )
;
18 'X-RAY DIFFRACTION' 18 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'C' and (resid 144 through 173 )
;
# 
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 18 ? A MET 1 
2  1 Y 1 A ALA 19 ? A ALA 2 
3  1 Y 1 A HIS 20 ? A HIS 3 
4  1 Y 1 A HIS 21 ? A HIS 4 
5  1 Y 1 A HIS 22 ? A HIS 5 
6  1 Y 1 A HIS 23 ? A HIS 6 
7  1 Y 1 A HIS 24 ? A HIS 7 
8  1 Y 1 B MET 18 ? B MET 1 
9  1 Y 1 B ALA 19 ? B ALA 2 
10 1 Y 1 B HIS 20 ? B HIS 3 
11 1 Y 1 B HIS 21 ? B HIS 4 
12 1 Y 1 B HIS 22 ? B HIS 5 
13 1 Y 1 B HIS 23 ? B HIS 6 
14 1 Y 1 B HIS 24 ? B HIS 7 
15 1 Y 1 C MET 18 ? C MET 1 
16 1 Y 1 C ALA 19 ? C ALA 2 
17 1 Y 1 C HIS 20 ? C HIS 3 
18 1 Y 1 C HIS 21 ? C HIS 4 
19 1 Y 1 C HIS 22 ? C HIS 5 
20 1 Y 1 C HIS 23 ? C HIS 6 
21 1 Y 1 C HIS 24 ? C HIS 7 
# 
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 
ADP PB     P  N N 1   
ADP O1B    O  N N 2   
ADP O2B    O  N N 3   
ADP O3B    O  N N 4   
ADP PA     P  N S 5   
ADP O1A    O  N N 6   
ADP O2A    O  N N 7   
ADP O3A    O  N N 8   
ADP "O5'"  O  N N 9   
ADP "C5'"  C  N N 10  
ADP "C4'"  C  N R 11  
ADP "O4'"  O  N N 12  
ADP "C3'"  C  N S 13  
ADP "O3'"  O  N N 14  
ADP "C2'"  C  N R 15  
ADP "O2'"  O  N N 16  
ADP "C1'"  C  N R 17  
ADP N9     N  Y N 18  
ADP C8     C  Y N 19  
ADP N7     N  Y N 20  
ADP C5     C  Y N 21  
ADP C6     C  Y N 22  
ADP N6     N  N N 23  
ADP N1     N  Y N 24  
ADP C2     C  Y N 25  
ADP N3     N  Y N 26  
ADP C4     C  Y N 27  
ADP HOB2   H  N N 28  
ADP HOB3   H  N N 29  
ADP HOA2   H  N N 30  
ADP "H5'1" H  N N 31  
ADP "H5'2" H  N N 32  
ADP "H4'"  H  N N 33  
ADP "H3'"  H  N N 34  
ADP "HO3'" H  N N 35  
ADP "H2'"  H  N N 36  
ADP "HO2'" H  N N 37  
ADP "H1'"  H  N N 38  
ADP H8     H  N N 39  
ADP HN61   H  N N 40  
ADP HN62   H  N N 41  
ADP H2     H  N N 42  
ALA N      N  N N 43  
ALA CA     C  N S 44  
ALA C      C  N N 45  
ALA O      O  N N 46  
ALA CB     C  N N 47  
ALA OXT    O  N N 48  
ALA H      H  N N 49  
ALA H2     H  N N 50  
ALA HA     H  N N 51  
ALA HB1    H  N N 52  
ALA HB2    H  N N 53  
ALA HB3    H  N N 54  
ALA HXT    H  N N 55  
ARG N      N  N N 56  
ARG CA     C  N S 57  
ARG C      C  N N 58  
ARG O      O  N N 59  
ARG CB     C  N N 60  
ARG CG     C  N N 61  
ARG CD     C  N N 62  
ARG NE     N  N N 63  
ARG CZ     C  N N 64  
ARG NH1    N  N N 65  
ARG NH2    N  N N 66  
ARG OXT    O  N N 67  
ARG H      H  N N 68  
ARG H2     H  N N 69  
ARG HA     H  N N 70  
ARG HB2    H  N N 71  
ARG HB3    H  N N 72  
ARG HG2    H  N N 73  
ARG HG3    H  N N 74  
ARG HD2    H  N N 75  
ARG HD3    H  N N 76  
ARG HE     H  N N 77  
ARG HH11   H  N N 78  
ARG HH12   H  N N 79  
ARG HH21   H  N N 80  
ARG HH22   H  N N 81  
ARG HXT    H  N N 82  
ASN N      N  N N 83  
ASN CA     C  N S 84  
ASN C      C  N N 85  
ASN O      O  N N 86  
ASN CB     C  N N 87  
ASN CG     C  N N 88  
ASN OD1    O  N N 89  
ASN ND2    N  N N 90  
ASN OXT    O  N N 91  
ASN H      H  N N 92  
ASN H2     H  N N 93  
ASN HA     H  N N 94  
ASN HB2    H  N N 95  
ASN HB3    H  N N 96  
ASN HD21   H  N N 97  
ASN HD22   H  N N 98  
ASN HXT    H  N N 99  
ASP N      N  N N 100 
ASP CA     C  N S 101 
ASP C      C  N N 102 
ASP O      O  N N 103 
ASP CB     C  N N 104 
ASP CG     C  N N 105 
ASP OD1    O  N N 106 
ASP OD2    O  N N 107 
ASP OXT    O  N N 108 
ASP H      H  N N 109 
ASP H2     H  N N 110 
ASP HA     H  N N 111 
ASP HB2    H  N N 112 
ASP HB3    H  N N 113 
ASP HD2    H  N N 114 
ASP HXT    H  N N 115 
CTP N1     N  N N 116 
CTP C2     C  N N 117 
CTP N3     N  N N 118 
CTP C4     C  N N 119 
CTP C5     C  N N 120 
CTP C6     C  N N 121 
CTP O2     O  N N 122 
CTP N4     N  N N 123 
CTP "C1'"  C  N R 124 
CTP "C2'"  C  N R 125 
CTP "O2'"  O  N N 126 
CTP "C3'"  C  N S 127 
CTP "C4'"  C  N R 128 
CTP "O4'"  O  N N 129 
CTP "O3'"  O  N N 130 
CTP "C5'"  C  N N 131 
CTP "O5'"  O  N N 132 
CTP PA     P  N S 133 
CTP O1A    O  N N 134 
CTP O2A    O  N N 135 
CTP O3A    O  N N 136 
CTP PB     P  N R 137 
CTP O1B    O  N N 138 
CTP O2B    O  N N 139 
CTP O3B    O  N N 140 
CTP PG     P  N N 141 
CTP O1G    O  N N 142 
CTP O2G    O  N N 143 
CTP O3G    O  N N 144 
CTP H5     H  N N 145 
CTP H6     H  N N 146 
CTP HN41   H  N N 147 
CTP HN42   H  N N 148 
CTP "H1'"  H  N N 149 
CTP "H2'"  H  N N 150 
CTP "HO2'" H  N N 151 
CTP "H3'"  H  N N 152 
CTP "H4'"  H  N N 153 
CTP "HO3'" H  N N 154 
CTP "H5'1" H  N N 155 
CTP "H5'2" H  N N 156 
CTP HOA2   H  N N 157 
CTP HOB2   H  N N 158 
CTP HOG2   H  N N 159 
CTP HOG3   H  N N 160 
CYS N      N  N N 161 
CYS CA     C  N R 162 
CYS C      C  N N 163 
CYS O      O  N N 164 
CYS CB     C  N N 165 
CYS SG     S  N N 166 
CYS OXT    O  N N 167 
CYS H      H  N N 168 
CYS H2     H  N N 169 
CYS HA     H  N N 170 
CYS HB2    H  N N 171 
CYS HB3    H  N N 172 
CYS HG     H  N N 173 
CYS HXT    H  N N 174 
GLN N      N  N N 175 
GLN CA     C  N S 176 
GLN C      C  N N 177 
GLN O      O  N N 178 
GLN CB     C  N N 179 
GLN CG     C  N N 180 
GLN CD     C  N N 181 
GLN OE1    O  N N 182 
GLN NE2    N  N N 183 
GLN OXT    O  N N 184 
GLN H      H  N N 185 
GLN H2     H  N N 186 
GLN HA     H  N N 187 
GLN HB2    H  N N 188 
GLN HB3    H  N N 189 
GLN HG2    H  N N 190 
GLN HG3    H  N N 191 
GLN HE21   H  N N 192 
GLN HE22   H  N N 193 
GLN HXT    H  N N 194 
GLU N      N  N N 195 
GLU CA     C  N S 196 
GLU C      C  N N 197 
GLU O      O  N N 198 
GLU CB     C  N N 199 
GLU CG     C  N N 200 
GLU CD     C  N N 201 
GLU OE1    O  N N 202 
GLU OE2    O  N N 203 
GLU OXT    O  N N 204 
GLU H      H  N N 205 
GLU H2     H  N N 206 
GLU HA     H  N N 207 
GLU HB2    H  N N 208 
GLU HB3    H  N N 209 
GLU HG2    H  N N 210 
GLU HG3    H  N N 211 
GLU HE2    H  N N 212 
GLU HXT    H  N N 213 
GLY N      N  N N 214 
GLY CA     C  N N 215 
GLY C      C  N N 216 
GLY O      O  N N 217 
GLY OXT    O  N N 218 
GLY H      H  N N 219 
GLY H2     H  N N 220 
GLY HA2    H  N N 221 
GLY HA3    H  N N 222 
GLY HXT    H  N N 223 
HIS N      N  N N 224 
HIS CA     C  N S 225 
HIS C      C  N N 226 
HIS O      O  N N 227 
HIS CB     C  N N 228 
HIS CG     C  Y N 229 
HIS ND1    N  Y N 230 
HIS CD2    C  Y N 231 
HIS CE1    C  Y N 232 
HIS NE2    N  Y N 233 
HIS OXT    O  N N 234 
HIS H      H  N N 235 
HIS H2     H  N N 236 
HIS HA     H  N N 237 
HIS HB2    H  N N 238 
HIS HB3    H  N N 239 
HIS HD1    H  N N 240 
HIS HD2    H  N N 241 
HIS HE1    H  N N 242 
HIS HE2    H  N N 243 
HIS HXT    H  N N 244 
HOH O      O  N N 245 
HOH H1     H  N N 246 
HOH H2     H  N N 247 
ILE N      N  N N 248 
ILE CA     C  N S 249 
ILE C      C  N N 250 
ILE O      O  N N 251 
ILE CB     C  N S 252 
ILE CG1    C  N N 253 
ILE CG2    C  N N 254 
ILE CD1    C  N N 255 
ILE OXT    O  N N 256 
ILE H      H  N N 257 
ILE H2     H  N N 258 
ILE HA     H  N N 259 
ILE HB     H  N N 260 
ILE HG12   H  N N 261 
ILE HG13   H  N N 262 
ILE HG21   H  N N 263 
ILE HG22   H  N N 264 
ILE HG23   H  N N 265 
ILE HD11   H  N N 266 
ILE HD12   H  N N 267 
ILE HD13   H  N N 268 
ILE HXT    H  N N 269 
LEU N      N  N N 270 
LEU CA     C  N S 271 
LEU C      C  N N 272 
LEU O      O  N N 273 
LEU CB     C  N N 274 
LEU CG     C  N N 275 
LEU CD1    C  N N 276 
LEU CD2    C  N N 277 
LEU OXT    O  N N 278 
LEU H      H  N N 279 
LEU H2     H  N N 280 
LEU HA     H  N N 281 
LEU HB2    H  N N 282 
LEU HB3    H  N N 283 
LEU HG     H  N N 284 
LEU HD11   H  N N 285 
LEU HD12   H  N N 286 
LEU HD13   H  N N 287 
LEU HD21   H  N N 288 
LEU HD22   H  N N 289 
LEU HD23   H  N N 290 
LEU HXT    H  N N 291 
LYS N      N  N N 292 
LYS CA     C  N S 293 
LYS C      C  N N 294 
LYS O      O  N N 295 
LYS CB     C  N N 296 
LYS CG     C  N N 297 
LYS CD     C  N N 298 
LYS CE     C  N N 299 
LYS NZ     N  N N 300 
LYS OXT    O  N N 301 
LYS H      H  N N 302 
LYS H2     H  N N 303 
LYS HA     H  N N 304 
LYS HB2    H  N N 305 
LYS HB3    H  N N 306 
LYS HG2    H  N N 307 
LYS HG3    H  N N 308 
LYS HD2    H  N N 309 
LYS HD3    H  N N 310 
LYS HE2    H  N N 311 
LYS HE3    H  N N 312 
LYS HZ1    H  N N 313 
LYS HZ2    H  N N 314 
LYS HZ3    H  N N 315 
LYS HXT    H  N N 316 
MET N      N  N N 317 
MET CA     C  N S 318 
MET C      C  N N 319 
MET O      O  N N 320 
MET CB     C  N N 321 
MET CG     C  N N 322 
MET SD     S  N N 323 
MET CE     C  N N 324 
MET OXT    O  N N 325 
MET H      H  N N 326 
MET H2     H  N N 327 
MET HA     H  N N 328 
MET HB2    H  N N 329 
MET HB3    H  N N 330 
MET HG2    H  N N 331 
MET HG3    H  N N 332 
MET HE1    H  N N 333 
MET HE2    H  N N 334 
MET HE3    H  N N 335 
MET HXT    H  N N 336 
MG  MG     MG N N 337 
PHE N      N  N N 338 
PHE CA     C  N S 339 
PHE C      C  N N 340 
PHE O      O  N N 341 
PHE CB     C  N N 342 
PHE CG     C  Y N 343 
PHE CD1    C  Y N 344 
PHE CD2    C  Y N 345 
PHE CE1    C  Y N 346 
PHE CE2    C  Y N 347 
PHE CZ     C  Y N 348 
PHE OXT    O  N N 349 
PHE H      H  N N 350 
PHE H2     H  N N 351 
PHE HA     H  N N 352 
PHE HB2    H  N N 353 
PHE HB3    H  N N 354 
PHE HD1    H  N N 355 
PHE HD2    H  N N 356 
PHE HE1    H  N N 357 
PHE HE2    H  N N 358 
PHE HZ     H  N N 359 
PHE HXT    H  N N 360 
PRO N      N  N N 361 
PRO CA     C  N S 362 
PRO C      C  N N 363 
PRO O      O  N N 364 
PRO CB     C  N N 365 
PRO CG     C  N N 366 
PRO CD     C  N N 367 
PRO OXT    O  N N 368 
PRO H      H  N N 369 
PRO HA     H  N N 370 
PRO HB2    H  N N 371 
PRO HB3    H  N N 372 
PRO HG2    H  N N 373 
PRO HG3    H  N N 374 
PRO HD2    H  N N 375 
PRO HD3    H  N N 376 
PRO HXT    H  N N 377 
SER N      N  N N 378 
SER CA     C  N S 379 
SER C      C  N N 380 
SER O      O  N N 381 
SER CB     C  N N 382 
SER OG     O  N N 383 
SER OXT    O  N N 384 
SER H      H  N N 385 
SER H2     H  N N 386 
SER HA     H  N N 387 
SER HB2    H  N N 388 
SER HB3    H  N N 389 
SER HG     H  N N 390 
SER HXT    H  N N 391 
THR N      N  N N 392 
THR CA     C  N S 393 
THR C      C  N N 394 
THR O      O  N N 395 
THR CB     C  N R 396 
THR OG1    O  N N 397 
THR CG2    C  N N 398 
THR OXT    O  N N 399 
THR H      H  N N 400 
THR H2     H  N N 401 
THR HA     H  N N 402 
THR HB     H  N N 403 
THR HG1    H  N N 404 
THR HG21   H  N N 405 
THR HG22   H  N N 406 
THR HG23   H  N N 407 
THR HXT    H  N N 408 
TRP N      N  N N 409 
TRP CA     C  N S 410 
TRP C      C  N N 411 
TRP O      O  N N 412 
TRP CB     C  N N 413 
TRP CG     C  Y N 414 
TRP CD1    C  Y N 415 
TRP CD2    C  Y N 416 
TRP NE1    N  Y N 417 
TRP CE2    C  Y N 418 
TRP CE3    C  Y N 419 
TRP CZ2    C  Y N 420 
TRP CZ3    C  Y N 421 
TRP CH2    C  Y N 422 
TRP OXT    O  N N 423 
TRP H      H  N N 424 
TRP H2     H  N N 425 
TRP HA     H  N N 426 
TRP HB2    H  N N 427 
TRP HB3    H  N N 428 
TRP HD1    H  N N 429 
TRP HE1    H  N N 430 
TRP HE3    H  N N 431 
TRP HZ2    H  N N 432 
TRP HZ3    H  N N 433 
TRP HH2    H  N N 434 
TRP HXT    H  N N 435 
TYR N      N  N N 436 
TYR CA     C  N S 437 
TYR C      C  N N 438 
TYR O      O  N N 439 
TYR CB     C  N N 440 
TYR CG     C  Y N 441 
TYR CD1    C  Y N 442 
TYR CD2    C  Y N 443 
TYR CE1    C  Y N 444 
TYR CE2    C  Y N 445 
TYR CZ     C  Y N 446 
TYR OH     O  N N 447 
TYR OXT    O  N N 448 
TYR H      H  N N 449 
TYR H2     H  N N 450 
TYR HA     H  N N 451 
TYR HB2    H  N N 452 
TYR HB3    H  N N 453 
TYR HD1    H  N N 454 
TYR HD2    H  N N 455 
TYR HE1    H  N N 456 
TYR HE2    H  N N 457 
TYR HH     H  N N 458 
TYR HXT    H  N N 459 
VAL N      N  N N 460 
VAL CA     C  N S 461 
VAL C      C  N N 462 
VAL O      O  N N 463 
VAL CB     C  N N 464 
VAL CG1    C  N N 465 
VAL CG2    C  N N 466 
VAL OXT    O  N N 467 
VAL H      H  N N 468 
VAL H2     H  N N 469 
VAL HA     H  N N 470 
VAL HB     H  N N 471 
VAL HG11   H  N N 472 
VAL HG12   H  N N 473 
VAL HG13   H  N N 474 
VAL HG21   H  N N 475 
VAL HG22   H  N N 476 
VAL HG23   H  N N 477 
VAL HXT    H  N N 478 
# 
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 
ADP PB    O1B    doub N N 1   
ADP PB    O2B    sing N N 2   
ADP PB    O3B    sing N N 3   
ADP PB    O3A    sing N N 4   
ADP O2B   HOB2   sing N N 5   
ADP O3B   HOB3   sing N N 6   
ADP PA    O1A    doub N N 7   
ADP PA    O2A    sing N N 8   
ADP PA    O3A    sing N N 9   
ADP PA    "O5'"  sing N N 10  
ADP O2A   HOA2   sing N N 11  
ADP "O5'" "C5'"  sing N N 12  
ADP "C5'" "C4'"  sing N N 13  
ADP "C5'" "H5'1" sing N N 14  
ADP "C5'" "H5'2" sing N N 15  
ADP "C4'" "O4'"  sing N N 16  
ADP "C4'" "C3'"  sing N N 17  
ADP "C4'" "H4'"  sing N N 18  
ADP "O4'" "C1'"  sing N N 19  
ADP "C3'" "O3'"  sing N N 20  
ADP "C3'" "C2'"  sing N N 21  
ADP "C3'" "H3'"  sing N N 22  
ADP "O3'" "HO3'" sing N N 23  
ADP "C2'" "O2'"  sing N N 24  
ADP "C2'" "C1'"  sing N N 25  
ADP "C2'" "H2'"  sing N N 26  
ADP "O2'" "HO2'" sing N N 27  
ADP "C1'" N9     sing N N 28  
ADP "C1'" "H1'"  sing N N 29  
ADP N9    C8     sing Y N 30  
ADP N9    C4     sing Y N 31  
ADP C8    N7     doub Y N 32  
ADP C8    H8     sing N N 33  
ADP N7    C5     sing Y N 34  
ADP C5    C6     sing Y N 35  
ADP C5    C4     doub Y N 36  
ADP C6    N6     sing N N 37  
ADP C6    N1     doub Y N 38  
ADP N6    HN61   sing N N 39  
ADP N6    HN62   sing N N 40  
ADP N1    C2     sing Y N 41  
ADP C2    N3     doub Y N 42  
ADP C2    H2     sing N N 43  
ADP N3    C4     sing Y N 44  
ALA N     CA     sing N N 45  
ALA N     H      sing N N 46  
ALA N     H2     sing N N 47  
ALA CA    C      sing N N 48  
ALA CA    CB     sing N N 49  
ALA CA    HA     sing N N 50  
ALA C     O      doub N N 51  
ALA C     OXT    sing N N 52  
ALA CB    HB1    sing N N 53  
ALA CB    HB2    sing N N 54  
ALA CB    HB3    sing N N 55  
ALA OXT   HXT    sing N N 56  
ARG N     CA     sing N N 57  
ARG N     H      sing N N 58  
ARG N     H2     sing N N 59  
ARG CA    C      sing N N 60  
ARG CA    CB     sing N N 61  
ARG CA    HA     sing N N 62  
ARG C     O      doub N N 63  
ARG C     OXT    sing N N 64  
ARG CB    CG     sing N N 65  
ARG CB    HB2    sing N N 66  
ARG CB    HB3    sing N N 67  
ARG CG    CD     sing N N 68  
ARG CG    HG2    sing N N 69  
ARG CG    HG3    sing N N 70  
ARG CD    NE     sing N N 71  
ARG CD    HD2    sing N N 72  
ARG CD    HD3    sing N N 73  
ARG NE    CZ     sing N N 74  
ARG NE    HE     sing N N 75  
ARG CZ    NH1    sing N N 76  
ARG CZ    NH2    doub N N 77  
ARG NH1   HH11   sing N N 78  
ARG NH1   HH12   sing N N 79  
ARG NH2   HH21   sing N N 80  
ARG NH2   HH22   sing N N 81  
ARG OXT   HXT    sing N N 82  
ASN N     CA     sing N N 83  
ASN N     H      sing N N 84  
ASN N     H2     sing N N 85  
ASN CA    C      sing N N 86  
ASN CA    CB     sing N N 87  
ASN CA    HA     sing N N 88  
ASN C     O      doub N N 89  
ASN C     OXT    sing N N 90  
ASN CB    CG     sing N N 91  
ASN CB    HB2    sing N N 92  
ASN CB    HB3    sing N N 93  
ASN CG    OD1    doub N N 94  
ASN CG    ND2    sing N N 95  
ASN ND2   HD21   sing N N 96  
ASN ND2   HD22   sing N N 97  
ASN OXT   HXT    sing N N 98  
ASP N     CA     sing N N 99  
ASP N     H      sing N N 100 
ASP N     H2     sing N N 101 
ASP CA    C      sing N N 102 
ASP CA    CB     sing N N 103 
ASP CA    HA     sing N N 104 
ASP C     O      doub N N 105 
ASP C     OXT    sing N N 106 
ASP CB    CG     sing N N 107 
ASP CB    HB2    sing N N 108 
ASP CB    HB3    sing N N 109 
ASP CG    OD1    doub N N 110 
ASP CG    OD2    sing N N 111 
ASP OD2   HD2    sing N N 112 
ASP OXT   HXT    sing N N 113 
CTP N1    C2     sing N N 114 
CTP N1    C6     sing N N 115 
CTP N1    "C1'"  sing N N 116 
CTP C2    N3     sing N N 117 
CTP C2    O2     doub N N 118 
CTP N3    C4     doub N N 119 
CTP C4    C5     sing N N 120 
CTP C4    N4     sing N N 121 
CTP C5    C6     doub N N 122 
CTP C5    H5     sing N N 123 
CTP C6    H6     sing N N 124 
CTP N4    HN41   sing N N 125 
CTP N4    HN42   sing N N 126 
CTP "C1'" "C2'"  sing N N 127 
CTP "C1'" "O4'"  sing N N 128 
CTP "C1'" "H1'"  sing N N 129 
CTP "C2'" "O2'"  sing N N 130 
CTP "C2'" "C3'"  sing N N 131 
CTP "C2'" "H2'"  sing N N 132 
CTP "O2'" "HO2'" sing N N 133 
CTP "C3'" "C4'"  sing N N 134 
CTP "C3'" "O3'"  sing N N 135 
CTP "C3'" "H3'"  sing N N 136 
CTP "C4'" "O4'"  sing N N 137 
CTP "C4'" "C5'"  sing N N 138 
CTP "C4'" "H4'"  sing N N 139 
CTP "O3'" "HO3'" sing N N 140 
CTP "C5'" "O5'"  sing N N 141 
CTP "C5'" "H5'1" sing N N 142 
CTP "C5'" "H5'2" sing N N 143 
CTP "O5'" PA     sing N N 144 
CTP PA    O1A    doub N N 145 
CTP PA    O2A    sing N N 146 
CTP PA    O3A    sing N N 147 
CTP O2A   HOA2   sing N N 148 
CTP O3A   PB     sing N N 149 
CTP PB    O1B    doub N N 150 
CTP PB    O2B    sing N N 151 
CTP PB    O3B    sing N N 152 
CTP O2B   HOB2   sing N N 153 
CTP O3B   PG     sing N N 154 
CTP PG    O1G    doub N N 155 
CTP PG    O2G    sing N N 156 
CTP PG    O3G    sing N N 157 
CTP O2G   HOG2   sing N N 158 
CTP O3G   HOG3   sing N N 159 
CYS N     CA     sing N N 160 
CYS N     H      sing N N 161 
CYS N     H2     sing N N 162 
CYS CA    C      sing N N 163 
CYS CA    CB     sing N N 164 
CYS CA    HA     sing N N 165 
CYS C     O      doub N N 166 
CYS C     OXT    sing N N 167 
CYS CB    SG     sing N N 168 
CYS CB    HB2    sing N N 169 
CYS CB    HB3    sing N N 170 
CYS SG    HG     sing N N 171 
CYS OXT   HXT    sing N N 172 
GLN N     CA     sing N N 173 
GLN N     H      sing N N 174 
GLN N     H2     sing N N 175 
GLN CA    C      sing N N 176 
GLN CA    CB     sing N N 177 
GLN CA    HA     sing N N 178 
GLN C     O      doub N N 179 
GLN C     OXT    sing N N 180 
GLN CB    CG     sing N N 181 
GLN CB    HB2    sing N N 182 
GLN CB    HB3    sing N N 183 
GLN CG    CD     sing N N 184 
GLN CG    HG2    sing N N 185 
GLN CG    HG3    sing N N 186 
GLN CD    OE1    doub N N 187 
GLN CD    NE2    sing N N 188 
GLN NE2   HE21   sing N N 189 
GLN NE2   HE22   sing N N 190 
GLN OXT   HXT    sing N N 191 
GLU N     CA     sing N N 192 
GLU N     H      sing N N 193 
GLU N     H2     sing N N 194 
GLU CA    C      sing N N 195 
GLU CA    CB     sing N N 196 
GLU CA    HA     sing N N 197 
GLU C     O      doub N N 198 
GLU C     OXT    sing N N 199 
GLU CB    CG     sing N N 200 
GLU CB    HB2    sing N N 201 
GLU CB    HB3    sing N N 202 
GLU CG    CD     sing N N 203 
GLU CG    HG2    sing N N 204 
GLU CG    HG3    sing N N 205 
GLU CD    OE1    doub N N 206 
GLU CD    OE2    sing N N 207 
GLU OE2   HE2    sing N N 208 
GLU OXT   HXT    sing N N 209 
GLY N     CA     sing N N 210 
GLY N     H      sing N N 211 
GLY N     H2     sing N N 212 
GLY CA    C      sing N N 213 
GLY CA    HA2    sing N N 214 
GLY CA    HA3    sing N N 215 
GLY C     O      doub N N 216 
GLY C     OXT    sing N N 217 
GLY OXT   HXT    sing N N 218 
HIS N     CA     sing N N 219 
HIS N     H      sing N N 220 
HIS N     H2     sing N N 221 
HIS CA    C      sing N N 222 
HIS CA    CB     sing N N 223 
HIS CA    HA     sing N N 224 
HIS C     O      doub N N 225 
HIS C     OXT    sing N N 226 
HIS CB    CG     sing N N 227 
HIS CB    HB2    sing N N 228 
HIS CB    HB3    sing N N 229 
HIS CG    ND1    sing Y N 230 
HIS CG    CD2    doub Y N 231 
HIS ND1   CE1    doub Y N 232 
HIS ND1   HD1    sing N N 233 
HIS CD2   NE2    sing Y N 234 
HIS CD2   HD2    sing N N 235 
HIS CE1   NE2    sing Y N 236 
HIS CE1   HE1    sing N N 237 
HIS NE2   HE2    sing N N 238 
HIS OXT   HXT    sing N N 239 
HOH O     H1     sing N N 240 
HOH O     H2     sing N N 241 
ILE N     CA     sing N N 242 
ILE N     H      sing N N 243 
ILE N     H2     sing N N 244 
ILE CA    C      sing N N 245 
ILE CA    CB     sing N N 246 
ILE CA    HA     sing N N 247 
ILE C     O      doub N N 248 
ILE C     OXT    sing N N 249 
ILE CB    CG1    sing N N 250 
ILE CB    CG2    sing N N 251 
ILE CB    HB     sing N N 252 
ILE CG1   CD1    sing N N 253 
ILE CG1   HG12   sing N N 254 
ILE CG1   HG13   sing N N 255 
ILE CG2   HG21   sing N N 256 
ILE CG2   HG22   sing N N 257 
ILE CG2   HG23   sing N N 258 
ILE CD1   HD11   sing N N 259 
ILE CD1   HD12   sing N N 260 
ILE CD1   HD13   sing N N 261 
ILE OXT   HXT    sing N N 262 
LEU N     CA     sing N N 263 
LEU N     H      sing N N 264 
LEU N     H2     sing N N 265 
LEU CA    C      sing N N 266 
LEU CA    CB     sing N N 267 
LEU CA    HA     sing N N 268 
LEU C     O      doub N N 269 
LEU C     OXT    sing N N 270 
LEU CB    CG     sing N N 271 
LEU CB    HB2    sing N N 272 
LEU CB    HB3    sing N N 273 
LEU CG    CD1    sing N N 274 
LEU CG    CD2    sing N N 275 
LEU CG    HG     sing N N 276 
LEU CD1   HD11   sing N N 277 
LEU CD1   HD12   sing N N 278 
LEU CD1   HD13   sing N N 279 
LEU CD2   HD21   sing N N 280 
LEU CD2   HD22   sing N N 281 
LEU CD2   HD23   sing N N 282 
LEU OXT   HXT    sing N N 283 
LYS N     CA     sing N N 284 
LYS N     H      sing N N 285 
LYS N     H2     sing N N 286 
LYS CA    C      sing N N 287 
LYS CA    CB     sing N N 288 
LYS CA    HA     sing N N 289 
LYS C     O      doub N N 290 
LYS C     OXT    sing N N 291 
LYS CB    CG     sing N N 292 
LYS CB    HB2    sing N N 293 
LYS CB    HB3    sing N N 294 
LYS CG    CD     sing N N 295 
LYS CG    HG2    sing N N 296 
LYS CG    HG3    sing N N 297 
LYS CD    CE     sing N N 298 
LYS CD    HD2    sing N N 299 
LYS CD    HD3    sing N N 300 
LYS CE    NZ     sing N N 301 
LYS CE    HE2    sing N N 302 
LYS CE    HE3    sing N N 303 
LYS NZ    HZ1    sing N N 304 
LYS NZ    HZ2    sing N N 305 
LYS NZ    HZ3    sing N N 306 
LYS OXT   HXT    sing N N 307 
MET N     CA     sing N N 308 
MET N     H      sing N N 309 
MET N     H2     sing N N 310 
MET CA    C      sing N N 311 
MET CA    CB     sing N N 312 
MET CA    HA     sing N N 313 
MET C     O      doub N N 314 
MET C     OXT    sing N N 315 
MET CB    CG     sing N N 316 
MET CB    HB2    sing N N 317 
MET CB    HB3    sing N N 318 
MET CG    SD     sing N N 319 
MET CG    HG2    sing N N 320 
MET CG    HG3    sing N N 321 
MET SD    CE     sing N N 322 
MET CE    HE1    sing N N 323 
MET CE    HE2    sing N N 324 
MET CE    HE3    sing N N 325 
MET OXT   HXT    sing N N 326 
PHE N     CA     sing N N 327 
PHE N     H      sing N N 328 
PHE N     H2     sing N N 329 
PHE CA    C      sing N N 330 
PHE CA    CB     sing N N 331 
PHE CA    HA     sing N N 332 
PHE C     O      doub N N 333 
PHE C     OXT    sing N N 334 
PHE CB    CG     sing N N 335 
PHE CB    HB2    sing N N 336 
PHE CB    HB3    sing N N 337 
PHE CG    CD1    doub Y N 338 
PHE CG    CD2    sing Y N 339 
PHE CD1   CE1    sing Y N 340 
PHE CD1   HD1    sing N N 341 
PHE CD2   CE2    doub Y N 342 
PHE CD2   HD2    sing N N 343 
PHE CE1   CZ     doub Y N 344 
PHE CE1   HE1    sing N N 345 
PHE CE2   CZ     sing Y N 346 
PHE CE2   HE2    sing N N 347 
PHE CZ    HZ     sing N N 348 
PHE OXT   HXT    sing N N 349 
PRO N     CA     sing N N 350 
PRO N     CD     sing N N 351 
PRO N     H      sing N N 352 
PRO CA    C      sing N N 353 
PRO CA    CB     sing N N 354 
PRO CA    HA     sing N N 355 
PRO C     O      doub N N 356 
PRO C     OXT    sing N N 357 
PRO CB    CG     sing N N 358 
PRO CB    HB2    sing N N 359 
PRO CB    HB3    sing N N 360 
PRO CG    CD     sing N N 361 
PRO CG    HG2    sing N N 362 
PRO CG    HG3    sing N N 363 
PRO CD    HD2    sing N N 364 
PRO CD    HD3    sing N N 365 
PRO OXT   HXT    sing N N 366 
SER N     CA     sing N N 367 
SER N     H      sing N N 368 
SER N     H2     sing N N 369 
SER CA    C      sing N N 370 
SER CA    CB     sing N N 371 
SER CA    HA     sing N N 372 
SER C     O      doub N N 373 
SER C     OXT    sing N N 374 
SER CB    OG     sing N N 375 
SER CB    HB2    sing N N 376 
SER CB    HB3    sing N N 377 
SER OG    HG     sing N N 378 
SER OXT   HXT    sing N N 379 
THR N     CA     sing N N 380 
THR N     H      sing N N 381 
THR N     H2     sing N N 382 
THR CA    C      sing N N 383 
THR CA    CB     sing N N 384 
THR CA    HA     sing N N 385 
THR C     O      doub N N 386 
THR C     OXT    sing N N 387 
THR CB    OG1    sing N N 388 
THR CB    CG2    sing N N 389 
THR CB    HB     sing N N 390 
THR OG1   HG1    sing N N 391 
THR CG2   HG21   sing N N 392 
THR CG2   HG22   sing N N 393 
THR CG2   HG23   sing N N 394 
THR OXT   HXT    sing N N 395 
TRP N     CA     sing N N 396 
TRP N     H      sing N N 397 
TRP N     H2     sing N N 398 
TRP CA    C      sing N N 399 
TRP CA    CB     sing N N 400 
TRP CA    HA     sing N N 401 
TRP C     O      doub N N 402 
TRP C     OXT    sing N N 403 
TRP CB    CG     sing N N 404 
TRP CB    HB2    sing N N 405 
TRP CB    HB3    sing N N 406 
TRP CG    CD1    doub Y N 407 
TRP CG    CD2    sing Y N 408 
TRP CD1   NE1    sing Y N 409 
TRP CD1   HD1    sing N N 410 
TRP CD2   CE2    doub Y N 411 
TRP CD2   CE3    sing Y N 412 
TRP NE1   CE2    sing Y N 413 
TRP NE1   HE1    sing N N 414 
TRP CE2   CZ2    sing Y N 415 
TRP CE3   CZ3    doub Y N 416 
TRP CE3   HE3    sing N N 417 
TRP CZ2   CH2    doub Y N 418 
TRP CZ2   HZ2    sing N N 419 
TRP CZ3   CH2    sing Y N 420 
TRP CZ3   HZ3    sing N N 421 
TRP CH2   HH2    sing N N 422 
TRP OXT   HXT    sing N N 423 
TYR N     CA     sing N N 424 
TYR N     H      sing N N 425 
TYR N     H2     sing N N 426 
TYR CA    C      sing N N 427 
TYR CA    CB     sing N N 428 
TYR CA    HA     sing N N 429 
TYR C     O      doub N N 430 
TYR C     OXT    sing N N 431 
TYR CB    CG     sing N N 432 
TYR CB    HB2    sing N N 433 
TYR CB    HB3    sing N N 434 
TYR CG    CD1    doub Y N 435 
TYR CG    CD2    sing Y N 436 
TYR CD1   CE1    sing Y N 437 
TYR CD1   HD1    sing N N 438 
TYR CD2   CE2    doub Y N 439 
TYR CD2   HD2    sing N N 440 
TYR CE1   CZ     doub Y N 441 
TYR CE1   HE1    sing N N 442 
TYR CE2   CZ     sing Y N 443 
TYR CE2   HE2    sing N N 444 
TYR CZ    OH     sing N N 445 
TYR OH    HH     sing N N 446 
TYR OXT   HXT    sing N N 447 
VAL N     CA     sing N N 448 
VAL N     H      sing N N 449 
VAL N     H2     sing N N 450 
VAL CA    C      sing N N 451 
VAL CA    CB     sing N N 452 
VAL CA    HA     sing N N 453 
VAL C     O      doub N N 454 
VAL C     OXT    sing N N 455 
VAL CB    CG1    sing N N 456 
VAL CB    CG2    sing N N 457 
VAL CB    HB     sing N N 458 
VAL CG1   HG11   sing N N 459 
VAL CG1   HG12   sing N N 460 
VAL CG1   HG13   sing N N 461 
VAL CG2   HG21   sing N N 462 
VAL CG2   HG22   sing N N 463 
VAL CG2   HG23   sing N N 464 
VAL OXT   HXT    sing N N 465 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 'United States' 75N93022C00036 1 
'National Institutes of Health/Office of the Director'                                            'United States' S10OD030394    2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      AlphaFold 
_pdbx_initial_refinement_model.accession_code   AF-Q5CR64-F1 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9OB9 
_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]   0.014330 
_atom_sites.fract_transf_matrix[1][2]   0.008273 
_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]   0.016547 
_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]   0.003168 
_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  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N     . HIS A 1 8   ? 10.718  53.538 6.728  1.00 51.04  ? 25  HIS A N     1 
ATOM   2    C  CA    . HIS A 1 8   ? 9.394   53.574 7.346  1.00 43.39  ? 25  HIS A CA    1 
ATOM   3    C  C     . HIS A 1 8   ? 9.005   52.206 7.928  1.00 37.16  ? 25  HIS A C     1 
ATOM   4    O  O     . HIS A 1 8   ? 9.131   51.171 7.275  1.00 37.72  ? 25  HIS A O     1 
ATOM   5    C  CB    . HIS A 1 8   ? 8.340   54.021 6.329  1.00 44.67  ? 25  HIS A CB    1 
ATOM   6    N  N     . VAL A 1 9   ? 8.506   52.205 9.146  1.00 35.53  ? 26  VAL A N     1 
ATOM   7    C  CA    . VAL A 1 9   ? 8.064   50.969 9.760  1.00 24.07  ? 26  VAL A CA    1 
ATOM   8    C  C     . VAL A 1 9   ? 6.606   50.725 9.397  1.00 21.87  ? 26  VAL A C     1 
ATOM   9    O  O     . VAL A 1 9   ? 5.876   51.619 8.948  1.00 24.08  ? 26  VAL A O     1 
ATOM   10   C  CB    . VAL A 1 9   ? 8.265   50.980 11.298 1.00 25.23  ? 26  VAL A CB    1 
ATOM   11   C  CG1   . VAL A 1 9   ? 9.729   51.211 11.632 1.00 28.91  ? 26  VAL A CG1   1 
ATOM   12   C  CG2   . VAL A 1 9   ? 7.389   52.007 11.973 1.00 28.70  ? 26  VAL A CG2   1 
ATOM   13   N  N     . GLU A 1 10  ? 6.167   49.489 9.592  1.00 17.56  ? 27  GLU A N     1 
ATOM   14   C  CA    . GLU A 1 10  ? 4.771   49.136 9.473  1.00 19.34  ? 27  GLU A CA    1 
ATOM   15   C  C     . GLU A 1 10  ? 4.395   48.285 10.685 1.00 15.77  ? 27  GLU A C     1 
ATOM   16   O  O     . GLU A 1 10  ? 5.241   47.994 11.541 1.00 16.06  ? 27  GLU A O     1 
ATOM   17   C  CB    . GLU A 1 10  ? 4.509   48.428 8.146  1.00 26.94  ? 27  GLU A CB    1 
ATOM   18   C  CG    . GLU A 1 10  ? 5.155   47.113 8.064  1.00 20.41  ? 27  GLU A CG    1 
ATOM   19   C  CD    . GLU A 1 10  ? 5.261   46.591 6.639  1.00 28.53  ? 27  GLU A CD    1 
ATOM   20   O  OE1   . GLU A 1 10  ? 4.949   47.340 5.695  1.00 39.84  ? 27  GLU A OE1   1 
ATOM   21   O  OE2   . GLU A 1 10  ? 5.631   45.422 6.472  1.00 20.83  ? 27  GLU A OE2   1 
ATOM   22   N  N     . GLN A 1 11  ? 3.103   47.941 10.775 1.00 15.91  ? 28  GLN A N     1 
ATOM   23   C  CA    . GLN A 1 11  ? 2.562   47.115 11.851 1.00 15.73  ? 28  GLN A CA    1 
ATOM   24   C  C     . GLN A 1 11  ? 1.886   45.881 11.274 1.00 15.46  ? 28  GLN A C     1 
ATOM   25   O  O     . GLN A 1 11  ? 1.186   45.953 10.252 1.00 18.43  ? 28  GLN A O     1 
ATOM   26   C  CB    . GLN A 1 11  ? 1.555   47.889 12.724 1.00 15.55  ? 28  GLN A CB    1 
ATOM   27   C  CG    . GLN A 1 11  ? 2.238   48.990 13.466 1.00 19.46  ? 28  GLN A CG    1 
ATOM   28   C  CD    . GLN A 1 11  ? 1.372   49.661 14.487 1.00 25.93  ? 28  GLN A CD    1 
ATOM   29   O  OE1   . GLN A 1 11  ? 0.157   49.462 14.527 1.00 24.78  ? 28  GLN A OE1   1 
ATOM   30   N  NE2   . GLN A 1 11  ? 1.998   50.485 15.319 1.00 25.25  ? 28  GLN A NE2   1 
ATOM   31   N  N     . THR A 1 12  ? 2.100   44.742 11.919 1.00 14.19  ? 29  THR A N     1 
ATOM   32   C  CA    . THR A 1 12  ? 1.458   43.503 11.518 1.00 14.40  ? 29  THR A CA    1 
ATOM   33   C  C     . THR A 1 12  ? 0.672   42.922 12.684 1.00 14.48  ? 29  THR A C     1 
ATOM   34   O  O     . THR A 1 12  ? 0.979   43.182 13.845 1.00 15.23  ? 29  THR A O     1 
ATOM   35   C  CB    . THR A 1 12  ? 2.463   42.483 10.989 1.00 16.01  ? 29  THR A CB    1 
ATOM   36   O  OG1   . THR A 1 12  ? 1.727   41.464 10.283 1.00 16.40  ? 29  THR A OG1   1 
ATOM   37   C  CG2   . THR A 1 12  ? 3.350   41.874 12.095 1.00 13.35  ? 29  THR A CG2   1 
ATOM   38   N  N     . TYR A 1 13  ? -0.354  42.130 12.364 1.00 13.95  ? 30  TYR A N     1 
ATOM   39   C  CA    . TYR A 1 13  ? -1.127  41.411 13.363 1.00 12.05  ? 30  TYR A CA    1 
ATOM   40   C  C     . TYR A 1 13  ? -0.596  39.990 13.475 1.00 14.66  ? 30  TYR A C     1 
ATOM   41   O  O     . TYR A 1 13  ? -0.494  39.276 12.468 1.00 14.71  ? 30  TYR A O     1 
ATOM   42   C  CB    . TYR A 1 13  ? -2.620  41.386 13.012 1.00 13.74  ? 30  TYR A CB    1 
ATOM   43   C  CG    . TYR A 1 13  ? -3.425  40.600 14.021 1.00 14.94  ? 30  TYR A CG    1 
ATOM   44   C  CD1   . TYR A 1 13  ? -3.645  41.089 15.295 1.00 15.13  ? 30  TYR A CD1   1 
ATOM   45   C  CD2   . TYR A 1 13  ? -3.930  39.340 13.711 1.00 13.73  ? 30  TYR A CD2   1 
ATOM   46   C  CE1   . TYR A 1 13  ? -4.349  40.366 16.221 1.00 15.03  ? 30  TYR A CE1   1 
ATOM   47   C  CE2   . TYR A 1 13  ? -4.658  38.600 14.657 1.00 13.56  ? 30  TYR A CE2   1 
ATOM   48   C  CZ    . TYR A 1 13  ? -4.859  39.120 15.908 1.00 14.62  ? 30  TYR A CZ    1 
ATOM   49   O  OH    . TYR A 1 13  ? -5.538  38.403 16.885 1.00 16.38  ? 30  TYR A OH    1 
ATOM   50   N  N     . LEU A 1 14  ? -0.177  39.610 14.679 1.00 13.01  ? 31  LEU A N     1 
ATOM   51   C  CA    . LEU A 1 14  ? 0.296   38.267 14.967 1.00 12.96  ? 31  LEU A CA    1 
ATOM   52   C  C     . LEU A 1 14  ? -0.569  37.699 16.082 1.00 15.32  ? 31  LEU A C     1 
ATOM   53   O  O     . LEU A 1 14  ? -0.890  38.401 17.048 1.00 17.42  ? 31  LEU A O     1 
ATOM   54   C  CB    . LEU A 1 14  ? 1.786   38.262 15.368 1.00 13.65  ? 31  LEU A CB    1 
ATOM   55   C  CG    . LEU A 1 14  ? 2.785   38.563 14.241 1.00 15.34  ? 31  LEU A CG    1 
ATOM   56   C  CD1   . LEU A 1 14  ? 4.096   39.118 14.764 1.00 17.20  ? 31  LEU A CD1   1 
ATOM   57   C  CD2   . LEU A 1 14  ? 3.075   37.288 13.458 1.00 19.78  ? 31  LEU A CD2   1 
ATOM   58   N  N     . MET A 1 15  ? -0.983  36.443 15.947 1.00 13.12  ? 32  MET A N     1 
ATOM   59   C  CA    . MET A 1 15  ? -1.865  35.826 16.931 1.00 12.89  ? 32  MET A CA    1 
ATOM   60   C  C     . MET A 1 15  ? -1.299  34.474 17.333 1.00 13.11  ? 32  MET A C     1 
ATOM   61   O  O     . MET A 1 15  ? -1.082  33.613 16.478 1.00 14.02  ? 32  MET A O     1 
ATOM   62   C  CB    . MET A 1 15  ? -3.282  35.661 16.357 1.00 14.96  ? 32  MET A CB    1 
ATOM   63   C  CG    . MET A 1 15  ? -4.239  35.026 17.321 1.00 16.98  ? 32  MET A CG    1 
ATOM   64   S  SD    . MET A 1 15  ? -5.963  35.258 16.791 1.00 19.31  ? 32  MET A SD    1 
ATOM   65   C  CE    . MET A 1 15  ? -5.877  34.678 15.121 1.00 19.55  ? 32  MET A CE    1 
ATOM   66   N  N     . ILE A 1 16  ? -1.053  34.287 18.623 1.00 12.74  ? 33  ILE A N     1 
ATOM   67   C  CA    . ILE A 1 16  ? -0.650  32.979 19.123 1.00 13.68  ? 33  ILE A CA    1 
ATOM   68   C  C     . ILE A 1 16  ? -1.917  32.140 19.260 1.00 13.55  ? 33  ILE A C     1 
ATOM   69   O  O     . ILE A 1 16  ? -2.883  32.559 19.908 1.00 14.30  ? 33  ILE A O     1 
ATOM   70   C  CB    . ILE A 1 16  ? 0.103   33.076 20.457 1.00 11.63  ? 33  ILE A CB    1 
ATOM   71   C  CG1   . ILE A 1 16  ? 1.349   33.958 20.288 1.00 13.94  ? 33  ILE A CG1   1 
ATOM   72   C  CG2   . ILE A 1 16  ? 0.482   31.661 20.886 1.00 12.60  ? 33  ILE A CG2   1 
ATOM   73   C  CD1   . ILE A 1 16  ? 2.180   34.141 21.544 1.00 14.18  ? 33  ILE A CD1   1 
ATOM   74   N  N     . LYS A 1 17  ? -1.936  30.997 18.589 1.00 13.60  ? 34  LYS A N     1 
ATOM   75   C  CA    . LYS A 1 17  ? -3.102  30.129 18.524 1.00 14.53  ? 34  LYS A CA    1 
ATOM   76   C  C     . LYS A 1 17  ? -3.205  29.314 19.804 1.00 13.83  ? 34  LYS A C     1 
ATOM   77   O  O     . LYS A 1 17  ? -2.295  29.328 20.641 1.00 12.80  ? 34  LYS A O     1 
ATOM   78   C  CB    . LYS A 1 17  ? -2.994  29.226 17.291 1.00 15.32  ? 34  LYS A CB    1 
ATOM   79   C  CG    . LYS A 1 17  ? -2.922  29.967 15.962 1.00 15.42  ? 34  LYS A CG    1 
ATOM   80   C  CD    . LYS A 1 17  ? -2.754  29.025 14.762 1.00 15.51  ? 34  LYS A CD    1 
ATOM   81   C  CE    . LYS A 1 17  ? -2.865  29.764 13.452 1.00 17.33  ? 34  LYS A CE    1 
ATOM   82   N  NZ    . LYS A 1 17  ? -2.843  28.797 12.307 1.00 19.02  ? 34  LYS A NZ    1 
ATOM   83   N  N     . PRO A 1 18  ? -4.326  28.618 20.012 1.00 13.53  ? 35  PRO A N     1 
ATOM   84   C  CA    . PRO A 1 18  ? -4.497  27.907 21.292 1.00 14.14  ? 35  PRO A CA    1 
ATOM   85   C  C     . PRO A 1 18  ? -3.400  26.906 21.587 1.00 14.15  ? 35  PRO A C     1 
ATOM   86   O  O     . PRO A 1 18  ? -3.063  26.710 22.765 1.00 14.26  ? 35  PRO A O     1 
ATOM   87   C  CB    . PRO A 1 18  ? -5.880  27.252 21.136 1.00 15.89  ? 35  PRO A CB    1 
ATOM   88   C  CG    . PRO A 1 18  ? -6.617  28.206 20.212 1.00 15.86  ? 35  PRO A CG    1 
ATOM   89   C  CD    . PRO A 1 18  ? -5.562  28.616 19.211 1.00 15.30  ? 35  PRO A CD    1 
ATOM   90   N  N     . ASP A 1 19  ? -2.781  26.294 20.560 1.00 14.39  ? 36  ASP A N     1 
ATOM   91   C  CA    . ASP A 1 19  ? -1.693  25.374 20.820 1.00 15.57  ? 36  ASP A CA    1 
ATOM   92   C  C     . ASP A 1 19  ? -0.475  26.104 21.369 1.00 13.53  ? 36  ASP A C     1 
ATOM   93   O  O     . ASP A 1 19  ? 0.253   25.556 22.207 1.00 15.42  ? 36  ASP A O     1 
ATOM   94   C  CB    . ASP A 1 19  ? -1.361  24.555 19.562 1.00 16.33  ? 36  ASP A CB    1 
ATOM   95   C  CG    . ASP A 1 19  ? -1.147  25.381 18.305 1.00 17.45  ? 36  ASP A CG    1 
ATOM   96   O  OD1   . ASP A 1 19  ? -1.841  26.390 18.089 1.00 19.48  ? 36  ASP A OD1   1 
ATOM   97   O  OD2   . ASP A 1 19  ? -0.321  24.936 17.462 1.00 16.28  ? 36  ASP A OD2   1 
ATOM   98   N  N     . GLY A 1 20  ? -0.244  27.345 20.953 1.00 12.85  ? 37  GLY A N     1 
ATOM   99   C  CA    . GLY A 1 20  ? 0.852   28.095 21.559 1.00 13.74  ? 37  GLY A CA    1 
ATOM   100  C  C     . GLY A 1 20  ? 0.605   28.424 23.025 1.00 12.97  ? 37  GLY A C     1 
ATOM   101  O  O     . GLY A 1 20  ? 1.528   28.386 23.857 1.00 14.80  ? 37  GLY A O     1 
ATOM   102  N  N     . ILE A 1 21  ? -0.648  28.739 23.368 1.00 12.77  ? 38  ILE A N     1 
ATOM   103  C  CA    . ILE A 1 21  ? -1.001  28.976 24.765 1.00 12.29  ? 38  ILE A CA    1 
ATOM   104  C  C     . ILE A 1 21  ? -0.861  27.695 25.583 1.00 12.77  ? 38  ILE A C     1 
ATOM   105  O  O     . ILE A 1 21  ? -0.221  27.680 26.643 1.00 13.40  ? 38  ILE A O     1 
ATOM   106  C  CB    . ILE A 1 21  ? -2.432  29.528 24.864 1.00 15.28  ? 38  ILE A CB    1 
ATOM   107  C  CG1   . ILE A 1 21  ? -2.671  30.775 23.997 1.00 17.63  ? 38  ILE A CG1   1 
ATOM   108  C  CG2   . ILE A 1 21  ? -2.775  29.776 26.306 1.00 16.45  ? 38  ILE A CG2   1 
ATOM   109  C  CD1   . ILE A 1 21  ? -1.796  31.940 24.310 1.00 21.36  ? 38  ILE A CD1   1 
ATOM   110  N  N     . GLN A 1 22  ? -1.444  26.594 25.083 1.00 13.64  ? 39  GLN A N     1 
ATOM   111  C  CA    . GLN A 1 22  ? -1.531  25.358 25.857 1.00 14.58  ? 39  GLN A CA    1 
ATOM   112  C  C     . GLN A 1 22  ? -0.177  24.685 26.002 1.00 14.89  ? 39  GLN A C     1 
ATOM   113  O  O     . GLN A 1 22  ? 0.080   24.021 27.009 1.00 17.42  ? 39  GLN A O     1 
ATOM   114  C  CB    . GLN A 1 22  ? -2.555  24.410 25.214 1.00 14.89  ? 39  GLN A CB    1 
ATOM   115  C  CG    . GLN A 1 22  ? -3.972  24.840 25.419 1.00 17.41  ? 39  GLN A CG    1 
ATOM   116  C  CD    . GLN A 1 22  ? -4.450  24.504 26.806 1.00 19.29  ? 39  GLN A CD    1 
ATOM   117  O  OE1   . GLN A 1 22  ? -3.673  24.043 27.651 1.00 21.54  ? 39  GLN A OE1   1 
ATOM   118  N  NE2   . GLN A 1 22  ? -5.720  24.719 27.050 1.00 20.38  ? 39  GLN A NE2   1 
ATOM   119  N  N     . ARG A 1 23  ? 0.704   24.829 25.019 1.00 12.76  ? 40  ARG A N     1 
ATOM   120  C  CA    . ARG A 1 23  ? 2.049   24.274 25.129 1.00 13.53  ? 40  ARG A CA    1 
ATOM   121  C  C     . ARG A 1 23  ? 2.974   25.203 25.903 1.00 14.47  ? 40  ARG A C     1 
ATOM   122  O  O     . ARG A 1 23  ? 4.136   24.848 26.154 1.00 14.73  ? 40  ARG A O     1 
ATOM   123  C  CB    . ARG A 1 23  ? 2.586   23.958 23.736 1.00 15.05  ? 40  ARG A CB    1 
ATOM   124  C  CG    . ARG A 1 23  ? 1.758   22.864 23.064 1.00 15.99  ? 40  ARG A CG    1 
ATOM   125  C  CD    . ARG A 1 23  ? 2.181   22.623 21.627 1.00 15.77  ? 40  ARG A CD    1 
ATOM   126  N  NE    . ARG A 1 23  ? 3.524   22.066 21.595 1.00 16.58  ? 40  ARG A NE    1 
ATOM   127  C  CZ    . ARG A 1 23  ? 4.321   22.085 20.543 1.00 13.96  ? 40  ARG A CZ    1 
ATOM   128  N  NH1   . ARG A 1 23  ? 3.942   22.621 19.393 1.00 16.30  ? 40  ARG A NH1   1 
ATOM   129  N  NH2   . ARG A 1 23  ? 5.543   21.571 20.649 1.00 16.21  ? 40  ARG A NH2   1 
ATOM   130  N  N     . GLN A 1 24  ? 2.458   26.374 26.288 1.00 13.87  ? 41  GLN A N     1 
ATOM   131  C  CA    . GLN A 1 24  ? 3.139   27.320 27.178 1.00 16.45  ? 41  GLN A CA    1 
ATOM   132  C  C     . GLN A 1 24  ? 4.476   27.788 26.606 1.00 13.81  ? 41  GLN A C     1 
ATOM   133  O  O     . GLN A 1 24  ? 5.507   27.795 27.274 1.00 14.05  ? 41  GLN A O     1 
ATOM   134  C  CB    . GLN A 1 24  ? 3.302   26.730 28.580 1.00 16.91  ? 41  GLN A CB    1 
ATOM   135  C  CG    . GLN A 1 24  ? 1.935   26.370 29.163 1.00 17.80  ? 41  GLN A CG    1 
ATOM   136  C  CD    . GLN A 1 24  ? 1.832   26.649 30.642 1.00 18.98  ? 41  GLN A CD    1 
ATOM   137  O  OE1   . GLN A 1 24  ? 2.093   25.769 31.456 1.00 18.85  ? 41  GLN A OE1   1 
ATOM   138  N  NE2   . GLN A 1 24  ? 1.455   27.873 31.001 1.00 17.33  ? 41  GLN A NE2   1 
ATOM   139  N  N     . VAL A 1 25  ? 4.429   28.245 25.359 1.00 12.06  ? 42  VAL A N     1 
ATOM   140  C  CA    . VAL A 1 25  ? 5.567   28.815 24.648 1.00 11.01  ? 42  VAL A CA    1 
ATOM   141  C  C     . VAL A 1 25  ? 5.297   30.261 24.232 1.00 10.65  ? 42  VAL A C     1 
ATOM   142  O  O     . VAL A 1 25  ? 5.984   30.801 23.352 1.00 12.21  ? 42  VAL A O     1 
ATOM   143  C  CB    . VAL A 1 25  ? 5.969   27.950 23.432 1.00 12.28  ? 42  VAL A CB    1 
ATOM   144  C  CG1   . VAL A 1 25  ? 6.389   26.554 23.897 1.00 15.30  ? 42  VAL A CG1   1 
ATOM   145  C  CG2   . VAL A 1 25  ? 4.850   27.846 22.423 1.00 14.52  ? 42  VAL A CG2   1 
ATOM   146  N  N     . VAL A 1 26  ? 4.367   30.923 24.923 1.00 12.28  ? 43  VAL A N     1 
ATOM   147  C  CA    . VAL A 1 26  ? 4.064   32.325 24.631 1.00 11.68  ? 43  VAL A CA    1 
ATOM   148  C  C     . VAL A 1 26  ? 5.308   33.199 24.764 1.00 11.81  ? 43  VAL A C     1 
ATOM   149  O  O     . VAL A 1 26  ? 5.631   34.008 23.879 1.00 11.81  ? 43  VAL A O     1 
ATOM   150  C  CB    . VAL A 1 26  ? 2.941   32.821 25.555 1.00 12.59  ? 43  VAL A CB    1 
ATOM   151  C  CG1   . VAL A 1 26  ? 2.784   34.317 25.418 1.00 13.44  ? 43  VAL A CG1   1 
ATOM   152  C  CG2   . VAL A 1 26  ? 1.636   32.067 25.252 1.00 14.49  ? 43  VAL A CG2   1 
ATOM   153  N  N     . GLY A 1 27  ? 6.011   33.075 25.884 1.00 10.65  ? 44  GLY A N     1 
ATOM   154  C  CA    . GLY A 1 27  ? 7.184   33.899 26.092 1.00 11.21  ? 44  GLY A CA    1 
ATOM   155  C  C     . GLY A 1 27  ? 8.235   33.680 25.028 1.00 10.31  ? 44  GLY A C     1 
ATOM   156  O  O     . GLY A 1 27  ? 8.868   34.630 24.569 1.00 10.52  ? 44  GLY A O     1 
ATOM   157  N  N     . GLU A 1 28  ? 8.464   32.420 24.651 1.00 11.28  ? 45  GLU A N     1 
ATOM   158  C  CA    . GLU A 1 28  ? 9.484   32.126 23.654 1.00 11.48  ? 45  GLU A CA    1 
ATOM   159  C  C     . GLU A 1 28  ? 9.135   32.774 22.327 1.00 11.25  ? 45  GLU A C     1 
ATOM   160  O  O     . GLU A 1 28  ? 10.024  33.252 21.606 1.00 12.91  ? 45  GLU A O     1 
ATOM   161  C  CB    . GLU A 1 28  ? 9.634   30.623 23.443 1.00 15.45  ? 45  GLU A CB    1 
ATOM   162  C  CG    . GLU A 1 28  ? 10.363  29.881 24.521 1.00 15.20  ? 45  GLU A CG    1 
ATOM   163  C  CD    . GLU A 1 28  ? 10.591  28.460 24.051 1.00 23.83  ? 45  GLU A CD    1 
ATOM   164  O  OE1   . GLU A 1 28  ? 11.465  28.267 23.191 1.00 27.02  ? 45  GLU A OE1   1 
ATOM   165  O  OE2   . GLU A 1 28  ? 9.837   27.579 24.465 1.00 27.36  ? 45  GLU A OE2   1 
ATOM   166  N  N     . ILE A 1 29  ? 7.848   32.760 21.971 1.00 11.91  ? 46  ILE A N     1 
ATOM   167  C  CA    . ILE A 1 29  ? 7.414   33.364 20.719 1.00 11.68  ? 46  ILE A CA    1 
ATOM   168  C  C     . ILE A 1 29  ? 7.651   34.866 20.758 1.00 10.21  ? 46  ILE A C     1 
ATOM   169  O  O     . ILE A 1 29  ? 8.244   35.445 19.841 1.00 12.97  ? 46  ILE A O     1 
ATOM   170  C  CB    . ILE A 1 29  ? 5.938   33.031 20.438 1.00 11.26  ? 46  ILE A CB    1 
ATOM   171  C  CG1   . ILE A 1 29  ? 5.755   31.538 20.150 1.00 13.98  ? 46  ILE A CG1   1 
ATOM   172  C  CG2   . ILE A 1 29  ? 5.395   33.888 19.296 1.00 14.02  ? 46  ILE A CG2   1 
ATOM   173  C  CD1   . ILE A 1 29  ? 4.285   31.077 20.171 1.00 15.49  ? 46  ILE A CD1   1 
ATOM   174  N  N     . ILE A 1 30  ? 7.205   35.518 21.832 1.00 11.14  ? 47  ILE A N     1 
ATOM   175  C  CA    . ILE A 1 30  ? 7.387   36.959 21.953 1.00 11.09  ? 47  ILE A CA    1 
ATOM   176  C  C     . ILE A 1 30  ? 8.869   37.306 21.870 1.00 11.31  ? 47  ILE A C     1 
ATOM   177  O  O     . ILE A 1 30  ? 9.257   38.263 21.183 1.00 12.47  ? 47  ILE A O     1 
ATOM   178  C  CB    . ILE A 1 30  ? 6.747   37.450 23.258 1.00 10.98  ? 47  ILE A CB    1 
ATOM   179  C  CG1   . ILE A 1 30  ? 5.236   37.316 23.170 1.00 11.03  ? 47  ILE A CG1   1 
ATOM   180  C  CG2   . ILE A 1 30  ? 7.169   38.886 23.570 1.00 11.21  ? 47  ILE A CG2   1 
ATOM   181  C  CD1   . ILE A 1 30  ? 4.529   37.500 24.481 1.00 13.48  ? 47  ILE A CD1   1 
ATOM   182  N  N     . SER A 1 31  ? 9.715   36.544 22.567 1.00 10.61  ? 48  SER A N     1 
ATOM   183  C  CA    . SER A 1 31  ? 11.150  36.809 22.551 1.00 9.89   ? 48  SER A CA    1 
ATOM   184  C  C     . SER A 1 31  ? 11.738  36.794 21.144 1.00 11.91  ? 48  SER A C     1 
ATOM   185  O  O     . SER A 1 31  ? 12.669  37.542 20.858 1.00 13.18  ? 48  SER A O     1 
ATOM   186  C  CB    . SER A 1 31  ? 11.904  35.796 23.427 1.00 12.16  ? 48  SER A CB    1 
ATOM   187  O  OG    . SER A 1 31  ? 11.687  36.070 24.817 1.00 12.43  ? 48  SER A OG    1 
ATOM   188  N  N     . ARG A 1 32  ? 11.245  35.922 20.257 1.00 10.95  ? 49  ARG A N     1 
ATOM   189  C  CA    . ARG A 1 32  ? 11.825  35.884 18.922 1.00 11.23  ? 49  ARG A CA    1 
ATOM   190  C  C     . ARG A 1 32  ? 11.608  37.201 18.196 1.00 14.23  ? 49  ARG A C     1 
ATOM   191  O  O     . ARG A 1 32  ? 12.463  37.642 17.421 1.00 12.84  ? 49  ARG A O     1 
ATOM   192  C  CB    . ARG A 1 32  ? 11.227  34.750 18.122 1.00 13.36  ? 49  ARG A CB    1 
ATOM   193  C  CG    . ARG A 1 32  ? 11.672  33.413 18.610 1.00 13.37  ? 49  ARG A CG    1 
ATOM   194  C  CD    . ARG A 1 32  ? 11.377  32.405 17.575 1.00 24.21  ? 49  ARG A CD    1 
ATOM   195  N  NE    . ARG A 1 32  ? 11.819  31.078 17.964 1.00 21.38  ? 49  ARG A NE    1 
ATOM   196  C  CZ    . ARG A 1 32  ? 12.177  30.130 17.114 1.00 19.57  ? 49  ARG A CZ    1 
ATOM   197  N  NH1   . ARG A 1 32  ? 12.187  30.339 15.815 1.00 17.76  ? 49  ARG A NH1   1 
ATOM   198  N  NH2   . ARG A 1 32  ? 12.520  28.941 17.586 1.00 21.72  ? 49  ARG A NH2   1 
ATOM   199  N  N     . PHE A 1 33  ? 10.449  37.821 18.397 1.00 13.42  ? 50  PHE A N     1 
ATOM   200  C  CA    . PHE A 1 33  ? 10.168  39.088 17.734 1.00 11.85  ? 50  PHE A CA    1 
ATOM   201  C  C     . PHE A 1 33  ? 10.869  40.254 18.434 1.00 12.01  ? 50  PHE A C     1 
ATOM   202  O  O     . PHE A 1 33  ? 11.422  41.142 17.776 1.00 13.32  ? 50  PHE A O     1 
ATOM   203  C  CB    . PHE A 1 33  ? 8.662   39.289 17.647 1.00 12.38  ? 50  PHE A CB    1 
ATOM   204  C  CG    . PHE A 1 33  ? 7.987   38.280 16.773 1.00 13.40  ? 50  PHE A CG    1 
ATOM   205  C  CD1   . PHE A 1 33  ? 8.186   38.306 15.407 1.00 14.63  ? 50  PHE A CD1   1 
ATOM   206  C  CD2   . PHE A 1 33  ? 7.204   37.271 17.300 1.00 17.13  ? 50  PHE A CD2   1 
ATOM   207  C  CE1   . PHE A 1 33  ? 7.585   37.338 14.575 1.00 14.79  ? 50  PHE A CE1   1 
ATOM   208  C  CE2   . PHE A 1 33  ? 6.599   36.307 16.469 1.00 17.50  ? 50  PHE A CE2   1 
ATOM   209  C  CZ    . PHE A 1 33  ? 6.816   36.341 15.118 1.00 14.60  ? 50  PHE A CZ    1 
ATOM   210  N  N     . GLU A 1 34  ? 10.902  40.248 19.762 1.00 12.56  ? 51  GLU A N     1 
ATOM   211  C  CA    . GLU A 1 34  ? 11.666  41.265 20.479 1.00 12.96  ? 51  GLU A CA    1 
ATOM   212  C  C     . GLU A 1 34  ? 13.140  41.246 20.106 1.00 12.64  ? 51  GLU A C     1 
ATOM   213  O  O     . GLU A 1 34  ? 13.806  42.290 20.133 1.00 13.93  ? 51  GLU A O     1 
ATOM   214  C  CB    . GLU A 1 34  ? 11.570  41.048 21.981 1.00 13.05  ? 51  GLU A CB    1 
ATOM   215  C  CG    . GLU A 1 34  ? 10.271  41.489 22.625 1.00 14.25  ? 51  GLU A CG    1 
ATOM   216  C  CD    . GLU A 1 34  ? 10.293  41.257 24.136 1.00 13.49  ? 51  GLU A CD    1 
ATOM   217  O  OE1   . GLU A 1 34  ? 10.486  40.094 24.553 1.00 15.68  ? 51  GLU A OE1   1 
ATOM   218  O  OE2   . GLU A 1 34  ? 10.155  42.255 24.892 1.00 14.36  ? 51  GLU A OE2   1 
ATOM   219  N  N     . LYS A 1 35  ? 13.673  40.060 19.816 1.00 11.68  ? 52  LYS A N     1 
ATOM   220  C  CA    . LYS A 1 35  ? 15.088  39.912 19.512 1.00 11.67  ? 52  LYS A CA    1 
ATOM   221  C  C     . LYS A 1 35  ? 15.509  40.738 18.312 1.00 12.87  ? 52  LYS A C     1 
ATOM   222  O  O     . LYS A 1 35  ? 16.672  41.129 18.230 1.00 13.48  ? 52  LYS A O     1 
ATOM   223  C  CB    . LYS A 1 35  ? 15.408  38.441 19.271 1.00 12.43  ? 52  LYS A CB    1 
ATOM   224  C  CG    . LYS A 1 35  ? 16.876  38.125 19.321 1.00 15.83  ? 52  LYS A CG    1 
ATOM   225  C  CD    . LYS A 1 35  ? 17.042  36.619 19.175 1.00 22.27  ? 52  LYS A CD    1 
ATOM   226  C  CE    . LYS A 1 35  ? 18.367  36.108 19.672 1.00 33.01  ? 52  LYS A CE    1 
ATOM   227  N  NZ    . LYS A 1 35  ? 18.402  36.132 21.158 1.00 30.14  ? 52  LYS A NZ    1 
ATOM   228  N  N     . ARG A 1 36  ? 14.599  41.024 17.379 1.00 12.68  ? 53  ARG A N     1 
ATOM   229  C  CA    . ARG A 1 36  ? 14.941  41.839 16.220 1.00 12.07  ? 53  ARG A CA    1 
ATOM   230  C  C     . ARG A 1 36  ? 14.695  43.316 16.445 1.00 11.85  ? 53  ARG A C     1 
ATOM   231  O  O     . ARG A 1 36  ? 14.798  44.105 15.504 1.00 14.01  ? 53  ARG A O     1 
ATOM   232  C  CB    . ARG A 1 36  ? 14.156  41.373 14.977 1.00 11.44  ? 53  ARG A CB    1 
ATOM   233  C  CG    . ARG A 1 36  ? 14.521  39.981 14.567 1.00 12.94  ? 53  ARG A CG    1 
ATOM   234  C  CD    . ARG A 1 36  ? 13.902  39.564 13.243 1.00 14.08  ? 53  ARG A CD    1 
ATOM   235  N  NE    . ARG A 1 36  ? 14.461  40.264 12.097 1.00 12.68  ? 53  ARG A NE    1 
ATOM   236  C  CZ    . ARG A 1 36  ? 14.133  39.996 10.841 1.00 14.19  ? 53  ARG A CZ    1 
ATOM   237  N  NH1   . ARG A 1 36  ? 13.189  39.113 10.551 1.00 15.62  ? 53  ARG A NH1   1 
ATOM   238  N  NH2   . ARG A 1 36  ? 14.755  40.637 9.854  1.00 15.21  ? 53  ARG A NH2   1 
ATOM   239  N  N     . GLY A 1 37  ? 14.313  43.718 17.654 1.00 13.30  ? 54  GLY A N     1 
ATOM   240  C  CA    . GLY A 1 37  ? 13.967  45.091 17.874 1.00 13.09  ? 54  GLY A CA    1 
ATOM   241  C  C     . GLY A 1 37  ? 12.583  45.467 17.394 1.00 11.61  ? 54  GLY A C     1 
ATOM   242  O  O     . GLY A 1 37  ? 12.317  46.653 17.192 1.00 14.61  ? 54  GLY A O     1 
ATOM   243  N  N     . TYR A 1 38  ? 11.711  44.488 17.152 1.00 12.16  ? 55  TYR A N     1 
ATOM   244  C  CA    . TYR A 1 38  ? 10.331  44.803 16.852 1.00 13.71  ? 55  TYR A CA    1 
ATOM   245  C  C     . TYR A 1 38  ? 9.636   45.258 18.122 1.00 14.63  ? 55  TYR A C     1 
ATOM   246  O  O     . TYR A 1 38  ? 9.880   44.727 19.205 1.00 14.90  ? 55  TYR A O     1 
ATOM   247  C  CB    . TYR A 1 38  ? 9.614   43.582 16.252 1.00 13.23  ? 55  TYR A CB    1 
ATOM   248  C  CG    . TYR A 1 38  ? 10.145  43.122 14.914 1.00 11.04  ? 55  TYR A CG    1 
ATOM   249  C  CD1   . TYR A 1 38  ? 10.674  44.016 13.991 1.00 16.76  ? 55  TYR A CD1   1 
ATOM   250  C  CD2   . TYR A 1 38  ? 10.054  41.790 14.545 1.00 12.43  ? 55  TYR A CD2   1 
ATOM   251  C  CE1   . TYR A 1 38  ? 11.125  43.583 12.744 1.00 14.19  ? 55  TYR A CE1   1 
ATOM   252  C  CE2   . TYR A 1 38  ? 10.479  41.347 13.300 1.00 14.51  ? 55  TYR A CE2   1 
ATOM   253  C  CZ    . TYR A 1 38  ? 11.023  42.240 12.412 1.00 12.63  ? 55  TYR A CZ    1 
ATOM   254  O  OH    . TYR A 1 38  ? 11.455  41.777 11.186 1.00 15.01  ? 55  TYR A OH    1 
ATOM   255  N  N     . ARG A 1 39  ? 8.780   46.252 17.974 1.00 12.25  ? 56  ARG A N     1 
ATOM   256  C  CA    . ARG A 1 39  ? 8.118   46.901 19.091 1.00 14.09  ? 56  ARG A CA    1 
ATOM   257  C  C     . ARG A 1 39  ? 6.726   46.323 19.283 1.00 15.14  ? 56  ARG A C     1 
ATOM   258  O  O     . ARG A 1 39  ? 5.939   46.254 18.336 1.00 14.34  ? 56  ARG A O     1 
ATOM   259  C  CB    . ARG A 1 39  ? 8.057   48.403 18.827 1.00 14.71  ? 56  ARG A CB    1 
ATOM   260  C  CG    . ARG A 1 39  ? 7.515   49.213 19.990 1.00 15.90  ? 56  ARG A CG    1 
ATOM   261  C  CD    . ARG A 1 39  ? 7.498   50.708 19.653 1.00 15.69  ? 56  ARG A CD    1 
ATOM   262  N  NE    . ARG A 1 39  ? 6.481   51.065 18.655 1.00 14.17  ? 56  ARG A NE    1 
ATOM   263  C  CZ    . ARG A 1 39  ? 5.201   51.292 18.914 1.00 16.29  ? 56  ARG A CZ    1 
ATOM   264  N  NH1   . ARG A 1 39  ? 4.702   51.155 20.132 1.00 18.74  ? 56  ARG A NH1   1 
ATOM   265  N  NH2   . ARG A 1 39  ? 4.392   51.676 17.930 1.00 21.72  ? 56  ARG A NH2   1 
ATOM   266  N  N     . ILE A 1 40  ? 6.412   45.944 20.526 1.00 12.47  ? 57  ILE A N     1 
ATOM   267  C  CA    . ILE A 1 40  ? 5.055   45.556 20.887 1.00 10.94  ? 57  ILE A CA    1 
ATOM   268  C  C     . ILE A 1 40  ? 4.176   46.807 20.915 1.00 13.48  ? 57  ILE A C     1 
ATOM   269  O  O     . ILE A 1 40  ? 4.319   47.666 21.800 1.00 14.95  ? 57  ILE A O     1 
ATOM   270  C  CB    . ILE A 1 40  ? 5.015   44.841 22.235 1.00 11.34  ? 57  ILE A CB    1 
ATOM   271  C  CG1   . ILE A 1 40  ? 6.015   43.673 22.276 1.00 14.30  ? 57  ILE A CG1   1 
ATOM   272  C  CG2   . ILE A 1 40  ? 3.615   44.330 22.494 1.00 17.57  ? 57  ILE A CG2   1 
ATOM   273  C  CD1   . ILE A 1 40  ? 6.180   43.055 23.687 1.00 18.44  ? 57  ILE A CD1   1 
ATOM   274  N  N     . ALA A 1 41  ? 3.238   46.889 19.972 1.00 13.65  ? 58  ALA A N     1 
ATOM   275  C  CA    . ALA A 1 41  ? 2.303   48.004 19.929 1.00 14.02  ? 58  ALA A CA    1 
ATOM   276  C  C     . ALA A 1 41  ? 0.959   47.671 20.542 1.00 16.39  ? 58  ALA A C     1 
ATOM   277  O  O     . ALA A 1 41  ? 0.233   48.587 20.936 1.00 18.39  ? 58  ALA A O     1 
ATOM   278  C  CB    . ALA A 1 41  ? 2.097   48.472 18.487 1.00 16.31  ? 58  ALA A CB    1 
ATOM   279  N  N     . ALA A 1 42  ? 0.606   46.396 20.635 1.00 14.16  ? 59  ALA A N     1 
ATOM   280  C  CA    . ALA A 1 42  ? -0.640  45.996 21.254 1.00 13.81  ? 59  ALA A CA    1 
ATOM   281  C  C     . ALA A 1 42  ? -0.510  44.531 21.638 1.00 15.62  ? 59  ALA A C     1 
ATOM   282  O  O     . ALA A 1 42  ? 0.222   43.773 20.987 1.00 14.18  ? 59  ALA A O     1 
ATOM   283  C  CB    . ALA A 1 42  ? -1.825  46.230 20.323 1.00 17.36  ? 59  ALA A CB    1 
ATOM   284  N  N     . MET A 1 43  ? -1.220  44.149 22.699 1.00 14.26  ? 60  MET A N     1 
ATOM   285  C  CA    . MET A 1 43  ? -1.193  42.768 23.170 1.00 14.69  ? 60  MET A CA    1 
ATOM   286  C  C     . MET A 1 43  ? -2.426  42.523 24.031 1.00 18.02  ? 60  MET A C     1 
ATOM   287  O  O     . MET A 1 43  ? -2.748  43.344 24.890 1.00 18.66  ? 60  MET A O     1 
ATOM   288  C  CB    . MET A 1 43  ? 0.108   42.494 23.962 1.00 16.45  ? 60  MET A CB    1 
ATOM   289  C  CG    . MET A 1 43  ? 0.344   41.054 24.333 1.00 20.75  ? 60  MET A CG    1 
ATOM   290  S  SD    . MET A 1 43  ? 2.080   40.759 24.828 1.00 19.23  ? 60  MET A SD    1 
ATOM   291  C  CE    . MET A 1 43  ? 2.894   40.452 23.249 1.00 16.37  ? 60  MET A CE    1 
ATOM   292  N  N     . LYS A 1 44  ? -3.130  41.423 23.776 1.00 14.72  ? 61  LYS A N     1 
ATOM   293  C  CA    . LYS A 1 44  ? -4.361  41.117 24.502 1.00 16.26  ? 61  LYS A CA    1 
ATOM   294  C  C     . LYS A 1 44  ? -4.605  39.618 24.492 1.00 18.28  ? 61  LYS A C     1 
ATOM   295  O  O     . LYS A 1 44  ? -4.642  39.012 23.419 1.00 16.57  ? 61  LYS A O     1 
ATOM   296  C  CB    . LYS A 1 44  ? -5.548  41.829 23.835 1.00 19.78  ? 61  LYS A CB    1 
ATOM   297  C  CG    . LYS A 1 44  ? -6.905  41.267 24.166 1.00 27.04  ? 61  LYS A CG    1 
ATOM   298  C  CD    . LYS A 1 44  ? -7.982  42.268 23.773 1.00 27.06  ? 61  LYS A CD    1 
ATOM   299  C  CE    . LYS A 1 44  ? -8.018  42.568 22.292 1.00 23.83  ? 61  LYS A CE    1 
ATOM   300  N  NZ    . LYS A 1 44  ? -9.142  43.542 21.990 1.00 22.65  ? 61  LYS A NZ    1 
ATOM   301  N  N     . LEU A 1 45  ? -4.805  39.023 25.662 1.00 17.17  ? 62  LEU A N     1 
ATOM   302  C  CA    . LEU A 1 45  ? -5.284  37.648 25.739 1.00 14.90  ? 62  LEU A CA    1 
ATOM   303  C  C     . LEU A 1 45  ? -6.803  37.648 25.666 1.00 15.56  ? 62  LEU A C     1 
ATOM   304  O  O     . LEU A 1 45  ? -7.464  38.413 26.381 1.00 15.77  ? 62  LEU A O     1 
ATOM   305  C  CB    . LEU A 1 45  ? -4.847  36.961 27.031 1.00 13.61  ? 62  LEU A CB    1 
ATOM   306  C  CG    . LEU A 1 45  ? -5.171  35.470 27.107 1.00 18.04  ? 62  LEU A CG    1 
ATOM   307  C  CD1   . LEU A 1 45  ? -4.086  34.673 26.389 1.00 17.73  ? 62  LEU A CD1   1 
ATOM   308  C  CD2   . LEU A 1 45  ? -5.346  35.002 28.553 1.00 17.78  ? 62  LEU A CD2   1 
ATOM   309  N  N     . THR A 1 46  ? -7.349  36.799 24.799 1.00 16.27  ? 63  THR A N     1 
ATOM   310  C  CA    . THR A 1 46  ? -8.793  36.607 24.735 1.00 16.33  ? 63  THR A CA    1 
ATOM   311  C  C     . THR A 1 46  ? -9.063  35.142 24.450 1.00 17.71  ? 63  THR A C     1 
ATOM   312  O  O     . THR A 1 46  ? -8.142  34.343 24.301 1.00 18.39  ? 63  THR A O     1 
ATOM   313  C  CB    . THR A 1 46  ? -9.417  37.578 23.715 1.00 15.96  ? 63  THR A CB    1 
ATOM   314  O  OG1   . THR A 1 46  ? -10.856 37.571 23.875 1.00 19.75  ? 63  THR A OG1   1 
ATOM   315  C  CG2   . THR A 1 46  ? -9.039  37.280 22.279 1.00 17.06  ? 63  THR A CG2   1 
ATOM   316  N  N     . ILE A 1 47  ? -10.339 34.775 24.395 1.00 18.27  ? 64  ILE A N     1 
ATOM   317  C  CA    . ILE A 1 47  ? -10.749 33.467 23.915 1.00 18.59  ? 64  ILE A CA    1 
ATOM   318  C  C     . ILE A 1 47  ? -11.488 33.704 22.614 1.00 18.83  ? 64  ILE A C     1 
ATOM   319  O  O     . ILE A 1 47  ? -12.538 34.361 22.591 1.00 20.98  ? 64  ILE A O     1 
ATOM   320  C  CB    . ILE A 1 47  ? -11.598 32.707 24.947 1.00 22.18  ? 64  ILE A CB    1 
ATOM   321  C  CG1   . ILE A 1 47  ? -10.700 32.298 26.130 1.00 23.72  ? 64  ILE A CG1   1 
ATOM   322  C  CG2   . ILE A 1 47  ? -12.214 31.468 24.300 1.00 27.03  ? 64  ILE A CG2   1 
ATOM   323  C  CD1   . ILE A 1 47  ? -11.430 31.731 27.296 1.00 23.03  ? 64  ILE A CD1   1 
ATOM   324  N  N     . ALA A 1 48  ? -10.925 33.180 21.535 1.00 16.70  ? 65  ALA A N     1 
ATOM   325  C  CA    . ALA A 1 48  ? -11.498 33.323 20.207 1.00 15.69  ? 65  ALA A CA    1 
ATOM   326  C  C     . ALA A 1 48  ? -12.793 32.532 20.118 1.00 18.72  ? 65  ALA A C     1 
ATOM   327  O  O     . ALA A 1 48  ? -12.907 31.421 20.651 1.00 23.34  ? 65  ALA A O     1 
ATOM   328  C  CB    . ALA A 1 48  ? -10.509 32.850 19.145 1.00 18.98  ? 65  ALA A CB    1 
ATOM   329  N  N     . THR A 1 49  ? -13.778 33.126 19.463 1.00 20.06  ? 66  THR A N     1 
ATOM   330  C  CA    . THR A 1 49  ? -15.085 32.540 19.266 1.00 18.59  ? 66  THR A CA    1 
ATOM   331  C  C     . THR A 1 49  ? -15.368 32.373 17.783 1.00 18.44  ? 66  THR A C     1 
ATOM   332  O  O     . THR A 1 49  ? -14.767 33.052 16.941 1.00 19.58  ? 66  THR A O     1 
ATOM   333  C  CB    . THR A 1 49  ? -16.167 33.438 19.867 1.00 21.49  ? 66  THR A CB    1 
ATOM   334  O  OG1   . THR A 1 49  ? -16.227 34.636 19.092 1.00 25.26  ? 66  THR A OG1   1 
ATOM   335  C  CG2   . THR A 1 49  ? -15.839 33.773 21.316 1.00 27.90  ? 66  THR A CG2   1 
ATOM   336  N  N     . PRO A 1 50  ? -16.284 31.478 17.428 1.00 20.64  ? 67  PRO A N     1 
ATOM   337  C  CA    . PRO A 1 50  ? -16.542 31.254 16.006 1.00 22.00  ? 67  PRO A CA    1 
ATOM   338  C  C     . PRO A 1 50  ? -16.912 32.506 15.241 1.00 22.82  ? 67  PRO A C     1 
ATOM   339  O  O     . PRO A 1 50  ? -16.467 32.664 14.100 1.00 23.48  ? 67  PRO A O     1 
ATOM   340  C  CB    . PRO A 1 50  ? -17.677 30.223 16.031 1.00 24.20  ? 67  PRO A CB    1 
ATOM   341  C  CG    . PRO A 1 50  ? -17.393 29.431 17.297 1.00 23.50  ? 67  PRO A CG    1 
ATOM   342  C  CD    . PRO A 1 50  ? -16.985 30.489 18.277 1.00 22.41  ? 67  PRO A CD    1 
ATOM   343  N  N     . ALA A 1 51  ? -17.694 33.417 15.818 1.00 21.86  ? 68  ALA A N     1 
ATOM   344  C  CA    . ALA A 1 51  ? -18.136 34.569 15.036 1.00 24.17  ? 68  ALA A CA    1 
ATOM   345  C  C     . ALA A 1 51  ? -16.959 35.455 14.636 1.00 22.42  ? 68  ALA A C     1 
ATOM   346  O  O     . ALA A 1 51  ? -16.887 35.934 13.495 1.00 27.51  ? 68  ALA A O     1 
ATOM   347  C  CB    . ALA A 1 51  ? -19.169 35.373 15.821 1.00 28.91  ? 68  ALA A CB    1 
ATOM   348  N  N     . ILE A 1 52  ? -16.045 35.718 15.565 1.00 21.22  ? 69  ILE A N     1 
ATOM   349  C  CA    . ILE A 1 52  ? -14.914 36.561 15.209 1.00 18.76  ? 69  ILE A CA    1 
ATOM   350  C  C     . ILE A 1 52  ? -13.957 35.804 14.294 1.00 18.45  ? 69  ILE A C     1 
ATOM   351  O  O     . ILE A 1 52  ? -13.374 36.387 13.374 1.00 20.68  ? 69  ILE A O     1 
ATOM   352  C  CB    . ILE A 1 52  ? -14.220 37.110 16.465 1.00 20.41  ? 69  ILE A CB    1 
ATOM   353  C  CG1   . ILE A 1 52  ? -13.147 38.135 16.075 1.00 24.85  ? 69  ILE A CG1   1 
ATOM   354  C  CG2   . ILE A 1 52  ? -13.542 36.026 17.250 1.00 25.16  ? 69  ILE A CG2   1 
ATOM   355  C  CD1   . ILE A 1 52  ? -12.791 39.060 17.179 1.00 32.74  ? 69  ILE A CD1   1 
ATOM   356  N  N     . LEU A 1 53  ? -13.778 34.502 14.530 1.00 19.15  ? 70  LEU A N     1 
ATOM   357  C  CA    . LEU A 1 53  ? -12.899 33.702 13.674 1.00 19.92  ? 70  LEU A CA    1 
ATOM   358  C  C     . LEU A 1 53  ? -13.424 33.625 12.248 1.00 19.92  ? 70  LEU A C     1 
ATOM   359  O  O     . LEU A 1 53  ? -12.628 33.581 11.303 1.00 20.85  ? 70  LEU A O     1 
ATOM   360  C  CB    . LEU A 1 53  ? -12.737 32.300 14.235 1.00 18.57  ? 70  LEU A CB    1 
ATOM   361  C  CG    . LEU A 1 53  ? -11.907 32.190 15.519 1.00 19.27  ? 70  LEU A CG    1 
ATOM   362  C  CD1   . LEU A 1 53  ? -12.127 30.823 16.172 1.00 21.77  ? 70  LEU A CD1   1 
ATOM   363  C  CD2   . LEU A 1 53  ? -10.397 32.470 15.261 1.00 18.87  ? 70  LEU A CD2   1 
ATOM   364  N  N     . GLU A 1 54  ? -14.744 33.607 12.073 1.00 20.44  ? 71  GLU A N     1 
ATOM   365  C  CA    . GLU A 1 54  ? -15.303 33.605 10.719 1.00 18.69  ? 71  GLU A CA    1 
ATOM   366  C  C     . GLU A 1 54  ? -14.930 34.873 9.971  1.00 24.88  ? 71  GLU A C     1 
ATOM   367  O  O     . GLU A 1 54  ? -14.588 34.819 8.780  1.00 26.25  ? 71  GLU A O     1 
ATOM   368  C  CB    . GLU A 1 54  ? -16.811 33.421 10.779 1.00 29.22  ? 71  GLU A CB    1 
ATOM   369  C  CG    . GLU A 1 54  ? -17.199 31.971 10.992 1.00 48.88  ? 71  GLU A CG    1 
ATOM   370  C  CD    . GLU A 1 54  ? -18.694 31.789 11.154 1.00 74.89  ? 71  GLU A CD    1 
ATOM   371  O  OE1   . GLU A 1 54  ? -19.461 32.562 10.527 1.00 63.11  ? 71  GLU A OE1   1 
ATOM   372  O  OE2   . GLU A 1 54  ? -19.092 30.880 11.924 1.00 60.27  ? 71  GLU A OE2   1 
ATOM   373  N  N     . GLU A 1 55  ? -14.935 36.016 10.662 1.00 18.41  ? 72  GLU A N     1 
ATOM   374  C  CA    . GLU A 1 55  ? -14.480 37.252 10.037 1.00 23.21  ? 72  GLU A CA    1 
ATOM   375  C  C     . GLU A 1 55  ? -12.975 37.234 9.814  1.00 23.01  ? 72  GLU A C     1 
ATOM   376  O  O     . GLU A 1 55  ? -12.492 37.663 8.764  1.00 23.52  ? 72  GLU A O     1 
ATOM   377  C  CB    . GLU A 1 55  ? -14.854 38.449 10.886 1.00 23.51  ? 72  GLU A CB    1 
ATOM   378  C  CG    . GLU A 1 55  ? -16.321 38.530 11.163 1.00 42.12  ? 72  GLU A CG    1 
ATOM   379  C  CD    . GLU A 1 55  ? -16.930 39.749 10.543 1.00 61.38  ? 72  GLU A CD    1 
ATOM   380  O  OE1   . GLU A 1 55  ? -16.481 40.864 10.898 1.00 57.70  ? 72  GLU A OE1   1 
ATOM   381  O  OE2   . GLU A 1 55  ? -17.835 39.583 9.695  1.00 69.87  ? 72  GLU A OE2   1 
ATOM   382  N  N     . HIS A 1 56  ? -12.221 36.729 10.788 1.00 19.69  ? 73  HIS A N     1 
ATOM   383  C  CA    . HIS A 1 56  ? -10.768 36.677 10.649 1.00 18.12  ? 73  HIS A CA    1 
ATOM   384  C  C     . HIS A 1 56  ? -10.363 35.868 9.425  1.00 19.75  ? 73  HIS A C     1 
ATOM   385  O  O     . HIS A 1 56  ? -9.463  36.272 8.662  1.00 21.44  ? 73  HIS A O     1 
ATOM   386  C  CB    . HIS A 1 56  ? -10.170 36.079 11.924 1.00 17.64  ? 73  HIS A CB    1 
ATOM   387  C  CG    . HIS A 1 56  ? -8.689  35.952 11.873 1.00 19.19  ? 73  HIS A CG    1 
ATOM   388  N  ND1   . HIS A 1 56  ? -7.858  37.030 12.051 1.00 17.65  ? 73  HIS A ND1   1 
ATOM   389  C  CD2   . HIS A 1 56  ? -7.887  34.891 11.632 1.00 20.13  ? 73  HIS A CD2   1 
ATOM   390  C  CE1   . HIS A 1 56  ? -6.600  36.641 11.937 1.00 18.89  ? 73  HIS A CE1   1 
ATOM   391  N  NE2   . HIS A 1 56  ? -6.592  35.349 11.656 1.00 19.70  ? 73  HIS A NE2   1 
ATOM   392  N  N     . TYR A 1 57  ? -10.983 34.703 9.252  1.00 23.65  ? 74  TYR A N     1 
ATOM   393  C  CA    . TYR A 1 57  ? -10.678 33.782 8.166  1.00 23.70  ? 74  TYR A CA    1 
ATOM   394  C  C     . TYR A 1 57  ? -11.682 33.897 7.021  1.00 26.11  ? 74  TYR A C     1 
ATOM   395  O  O     . TYR A 1 57  ? -11.986 32.911 6.359  1.00 27.57  ? 74  TYR A O     1 
ATOM   396  C  CB    . TYR A 1 57  ? -10.626 32.356 8.723  1.00 24.72  ? 74  TYR A CB    1 
ATOM   397  C  CG    . TYR A 1 57  ? -9.351  32.039 9.510  1.00 25.11  ? 74  TYR A CG    1 
ATOM   398  C  CD1   . TYR A 1 57  ? -8.100  32.276 8.955  1.00 26.81  ? 74  TYR A CD1   1 
ATOM   399  C  CD2   . TYR A 1 57  ? -9.400  31.497 10.803 1.00 27.39  ? 74  TYR A CD2   1 
ATOM   400  C  CE1   . TYR A 1 57  ? -6.929  31.991 9.652  1.00 28.32  ? 74  TYR A CE1   1 
ATOM   401  C  CE2   . TYR A 1 57  ? -8.222  31.208 11.504 1.00 28.22  ? 74  TYR A CE2   1 
ATOM   402  C  CZ    . TYR A 1 57  ? -6.991  31.460 10.919 1.00 36.88  ? 74  TYR A CZ    1 
ATOM   403  O  OH    . TYR A 1 57  ? -5.808  31.188 11.604 1.00 33.30  ? 74  TYR A OH    1 
ATOM   404  N  N     . ALA A 1 58  ? -12.163 35.113 6.757  1.00 24.33  ? 75  ALA A N     1 
ATOM   405  C  CA    . ALA A 1 58  ? -13.177 35.319 5.724  1.00 29.75  ? 75  ALA A CA    1 
ATOM   406  C  C     . ALA A 1 58  ? -12.691 34.878 4.348  1.00 29.70  ? 75  ALA A C     1 
ATOM   407  O  O     . ALA A 1 58  ? -13.485 34.392 3.533  1.00 32.66  ? 75  ALA A O     1 
ATOM   408  C  CB    . ALA A 1 58  ? -13.576 36.795 5.701  1.00 28.37  ? 75  ALA A CB    1 
ATOM   409  N  N     . GLU A 1 59  ? -11.399 35.058 4.047  1.00 26.32  ? 76  GLU A N     1 
ATOM   410  C  CA    . GLU A 1 59  ? -10.912 34.632 2.738  1.00 27.57  ? 76  GLU A CA    1 
ATOM   411  C  C     . GLU A 1 59  ? -11.088 33.144 2.508  1.00 26.09  ? 76  GLU A C     1 
ATOM   412  O  O     . GLU A 1 59  ? -11.067 32.701 1.354  1.00 30.71  ? 76  GLU A O     1 
ATOM   413  C  CB    . GLU A 1 59  ? -9.431  34.962 2.565  1.00 26.17  ? 76  GLU A CB    1 
ATOM   414  C  CG    . GLU A 1 59  ? -8.511  34.134 3.475  1.00 26.60  ? 76  GLU A CG    1 
ATOM   415  C  CD    . GLU A 1 59  ? -7.042  34.523 3.352  1.00 41.02  ? 76  GLU A CD    1 
ATOM   416  O  OE1   . GLU A 1 59  ? -6.442  34.253 2.286  1.00 44.30  ? 76  GLU A OE1   1 
ATOM   417  O  OE2   . GLU A 1 59  ? -6.507  35.106 4.317  1.00 50.37  ? 76  GLU A OE2   1 
ATOM   418  N  N     . HIS A 1 60  ? -11.194 32.359 3.564  1.00 26.54  ? 77  HIS A N     1 
ATOM   419  C  CA    . HIS A 1 60  ? -11.314 30.912 3.457  1.00 34.36  ? 77  HIS A CA    1 
ATOM   420  C  C     . HIS A 1 60  ? -12.756 30.447 3.440  1.00 40.24  ? 77  HIS A C     1 
ATOM   421  O  O     . HIS A 1 60  ? -13.008 29.240 3.515  1.00 36.53  ? 77  HIS A O     1 
ATOM   422  C  CB    . HIS A 1 60  ? -10.575 30.244 4.613  1.00 30.54  ? 77  HIS A CB    1 
ATOM   423  C  CG    . HIS A 1 60  ? -9.107  30.513 4.603  1.00 28.21  ? 77  HIS A CG    1 
ATOM   424  N  ND1   . HIS A 1 60  ? -8.359  30.483 3.444  1.00 30.03  ? 77  HIS A ND1   1 
ATOM   425  C  CD2   . HIS A 1 60  ? -8.251  30.829 5.601  1.00 29.12  ? 77  HIS A CD2   1 
ATOM   426  C  CE1   . HIS A 1 60  ? -7.102  30.768 3.732  1.00 31.11  ? 77  HIS A CE1   1 
ATOM   427  N  NE2   . HIS A 1 60  ? -7.009  30.987 5.032  1.00 27.97  ? 77  HIS A NE2   1 
ATOM   428  N  N     . LYS A 1 61  ? -13.701 31.375 3.370  1.00 33.72  ? 78  LYS A N     1 
ATOM   429  C  CA    . LYS A 1 61  ? -15.103 31.015 3.354  1.00 38.99  ? 78  LYS A CA    1 
ATOM   430  C  C     . LYS A 1 61  ? -15.366 29.990 2.259  1.00 48.27  ? 78  LYS A C     1 
ATOM   431  O  O     . LYS A 1 61  ? -14.825 30.085 1.153  1.00 45.10  ? 78  LYS A O     1 
ATOM   432  C  CB    . LYS A 1 61  ? -15.938 32.275 3.138  1.00 45.96  ? 78  LYS A CB    1 
ATOM   433  C  CG    . LYS A 1 61  ? -17.428 32.031 3.061  1.00 58.09  ? 78  LYS A CG    1 
ATOM   434  C  CD    . LYS A 1 61  ? -18.182 33.353 3.071  1.00 67.86  ? 78  LYS A CD    1 
ATOM   435  C  CE    . LYS A 1 61  ? -19.610 33.178 3.559  1.00 75.04  ? 78  LYS A CE    1 
ATOM   436  N  NZ    . LYS A 1 61  ? -20.541 34.106 2.852  1.00 67.13  ? 78  LYS A NZ    1 
ATOM   437  N  N     . GLY A 1 62  ? -16.160 28.974 2.597  1.00 57.53  ? 79  GLY A N     1 
ATOM   438  C  CA    . GLY A 1 62  ? -16.511 27.911 1.687  1.00 45.18  ? 79  GLY A CA    1 
ATOM   439  C  C     . GLY A 1 62  ? -15.542 26.743 1.648  1.00 58.14  ? 79  GLY A C     1 
ATOM   440  O  O     . GLY A 1 62  ? -15.953 25.624 1.328  1.00 70.22  ? 79  GLY A O     1 
ATOM   441  N  N     . LYS A 1 63  ? -14.269 26.969 1.962  1.00 51.46  ? 80  LYS A N     1 
ATOM   442  C  CA    . LYS A 1 63  ? -13.271 25.922 1.799  1.00 56.97  ? 80  LYS A CA    1 
ATOM   443  C  C     . LYS A 1 63  ? -13.542 24.754 2.751  1.00 65.88  ? 80  LYS A C     1 
ATOM   444  O  O     . LYS A 1 63  ? -14.046 24.947 3.864  1.00 59.65  ? 80  LYS A O     1 
ATOM   445  C  CB    . LYS A 1 63  ? -11.870 26.482 2.031  1.00 48.85  ? 80  LYS A CB    1 
ATOM   446  C  CG    . LYS A 1 63  ? -11.501 27.556 1.012  1.00 45.68  ? 80  LYS A CG    1 
ATOM   447  C  CD    . LYS A 1 63  ? -10.079 28.052 1.158  1.00 47.27  ? 80  LYS A CD    1 
ATOM   448  C  CE    . LYS A 1 63  ? -9.851  29.259 0.246  1.00 35.50  ? 80  LYS A CE    1 
ATOM   449  N  NZ    . LYS A 1 63  ? -8.568  29.951 0.505  1.00 39.62  ? 80  LYS A NZ    1 
ATOM   450  N  N     . PRO A 1 64  ? -13.211 23.526 2.334  1.00 75.48  ? 81  PRO A N     1 
ATOM   451  C  CA    . PRO A 1 64  ? -13.548 22.357 3.162  1.00 77.95  ? 81  PRO A CA    1 
ATOM   452  C  C     . PRO A 1 64  ? -12.890 22.362 4.526  1.00 62.21  ? 81  PRO A C     1 
ATOM   453  O  O     . PRO A 1 64  ? -13.455 21.798 5.469  1.00 50.03  ? 81  PRO A O     1 
ATOM   454  C  CB    . PRO A 1 64  ? -13.061 21.174 2.311  1.00 75.02  ? 81  PRO A CB    1 
ATOM   455  C  CG    . PRO A 1 64  ? -11.974 21.743 1.468  1.00 77.46  ? 81  PRO A CG    1 
ATOM   456  C  CD    . PRO A 1 64  ? -12.415 23.147 1.152  1.00 75.46  ? 81  PRO A CD    1 
ATOM   457  N  N     . PHE A 1 65  ? -11.702 22.956 4.659  1.00 49.99  ? 82  PHE A N     1 
ATOM   458  C  CA    . PHE A 1 65  ? -10.970 22.882 5.914  1.00 50.40  ? 82  PHE A CA    1 
ATOM   459  C  C     . PHE A 1 65  ? -11.414 23.933 6.926  1.00 36.09  ? 82  PHE A C     1 
ATOM   460  O  O     . PHE A 1 65  ? -10.985 23.863 8.079  1.00 35.85  ? 82  PHE A O     1 
ATOM   461  C  CB    . PHE A 1 65  ? -9.456  22.996 5.659  1.00 48.97  ? 82  PHE A CB    1 
ATOM   462  C  CG    . PHE A 1 65  ? -8.992  24.353 5.169  1.00 50.21  ? 82  PHE A CG    1 
ATOM   463  C  CD1   . PHE A 1 65  ? -8.628  25.346 6.068  1.00 44.36  ? 82  PHE A CD1   1 
ATOM   464  C  CD2   . PHE A 1 65  ? -8.872  24.614 3.810  1.00 60.69  ? 82  PHE A CD2   1 
ATOM   465  C  CE1   . PHE A 1 65  ? -8.187  26.584 5.622  1.00 43.89  ? 82  PHE A CE1   1 
ATOM   466  C  CE2   . PHE A 1 65  ? -8.428  25.850 3.358  1.00 41.17  ? 82  PHE A CE2   1 
ATOM   467  C  CZ    . PHE A 1 65  ? -8.082  26.834 4.263  1.00 46.45  ? 82  PHE A CZ    1 
ATOM   468  N  N     . LEU A 1 66  ? -12.266 24.882 6.538  1.00 33.79  ? 83  LEU A N     1 
ATOM   469  C  CA    . LEU A 1 66  ? -12.585 25.995 7.431  1.00 38.87  ? 83  LEU A CA    1 
ATOM   470  C  C     . LEU A 1 66  ? -13.288 25.551 8.703  1.00 38.27  ? 83  LEU A C     1 
ATOM   471  O  O     . LEU A 1 66  ? -12.925 26.040 9.790  1.00 25.70  ? 83  LEU A O     1 
ATOM   472  C  CB    . LEU A 1 66  ? -13.432 27.037 6.695  1.00 32.12  ? 83  LEU A CB    1 
ATOM   473  C  CG    . LEU A 1 66  ? -13.858 28.244 7.534  1.00 34.83  ? 83  LEU A CG    1 
ATOM   474  C  CD1   . LEU A 1 66  ? -12.638 28.966 8.075  1.00 27.08  ? 83  LEU A CD1   1 
ATOM   475  C  CD2   . LEU A 1 66  ? -14.734 29.181 6.725  1.00 30.40  ? 83  LEU A CD2   1 
ATOM   476  N  N     . PRO A 1 67  ? -14.307 24.692 8.662  1.00 28.07  ? 84  PRO A N     1 
ATOM   477  C  CA    . PRO A 1 67  ? -14.952 24.332 9.939  1.00 28.94  ? 84  PRO A CA    1 
ATOM   478  C  C     . PRO A 1 67  ? -13.983 23.721 10.942 1.00 31.09  ? 84  PRO A C     1 
ATOM   479  O  O     . PRO A 1 67  ? -14.054 24.042 12.135 1.00 28.53  ? 84  PRO A O     1 
ATOM   480  C  CB    . PRO A 1 67  ? -16.065 23.362 9.513  1.00 29.86  ? 84  PRO A CB    1 
ATOM   481  C  CG    . PRO A 1 67  ? -16.317 23.683 8.036  1.00 34.81  ? 84  PRO A CG    1 
ATOM   482  C  CD    . PRO A 1 67  ? -14.948 24.026 7.509  1.00 39.66  ? 84  PRO A CD    1 
ATOM   483  N  N     . GLY A 1 68  ? -13.047 22.879 10.503 1.00 35.01  ? 85  GLY A N     1 
ATOM   484  C  CA    . GLY A 1 68  ? -12.074 22.346 11.439 1.00 30.99  ? 85  GLY A CA    1 
ATOM   485  C  C     . GLY A 1 68  ? -11.080 23.390 11.903 1.00 34.88  ? 85  GLY A C     1 
ATOM   486  O  O     . GLY A 1 68  ? -10.607 23.344 13.040 1.00 29.65  ? 85  GLY A O     1 
ATOM   487  N  N     . LEU A 1 69  ? -10.743 24.339 11.035 1.00 26.87  ? 86  LEU A N     1 
ATOM   488  C  CA    . LEU A 1 69  ? -9.885  25.437 11.451 1.00 25.34  ? 86  LEU A CA    1 
ATOM   489  C  C     . LEU A 1 69  ? -10.552 26.260 12.549 1.00 24.77  ? 86  LEU A C     1 
ATOM   490  O  O     . LEU A 1 69  ? -9.921  26.592 13.560 1.00 24.84  ? 86  LEU A O     1 
ATOM   491  C  CB    . LEU A 1 69  ? -9.565  26.305 10.240 1.00 26.98  ? 86  LEU A CB    1 
ATOM   492  C  CG    . LEU A 1 69  ? -8.847  27.615 10.533 1.00 25.33  ? 86  LEU A CG    1 
ATOM   493  C  CD1   . LEU A 1 69  ? -7.509  27.408 11.260 1.00 28.48  ? 86  LEU A CD1   1 
ATOM   494  C  CD2   . LEU A 1 69  ? -8.663  28.314 9.199  1.00 26.31  ? 86  LEU A CD2   1 
ATOM   495  N  N     . ILE A 1 70  ? -11.837 26.585 12.371 1.00 23.48  ? 87  ILE A N     1 
ATOM   496  C  CA    A ILE A 1 70  ? -12.533 27.383 13.379 0.62 23.36  ? 87  ILE A CA    1 
ATOM   497  C  CA    B ILE A 1 70  ? -12.558 27.373 13.373 0.38 23.44  ? 87  ILE A CA    1 
ATOM   498  C  C     . ILE A 1 70  ? -12.594 26.629 14.701 1.00 25.91  ? 87  ILE A C     1 
ATOM   499  O  O     . ILE A 1 70  ? -12.402 27.218 15.770 1.00 25.28  ? 87  ILE A O     1 
ATOM   500  C  CB    A ILE A 1 70  ? -13.933 27.790 12.879 0.62 24.64  ? 87  ILE A CB    1 
ATOM   501  C  CB    B ILE A 1 70  ? -13.982 27.704 12.880 0.38 24.68  ? 87  ILE A CB    1 
ATOM   502  C  CG1   A ILE A 1 70  ? -13.797 28.858 11.792 0.62 27.69  ? 87  ILE A CG1   1 
ATOM   503  C  CG1   B ILE A 1 70  ? -13.949 28.487 11.565 0.38 29.14  ? 87  ILE A CG1   1 
ATOM   504  C  CG2   A ILE A 1 70  ? -14.797 28.318 14.042 0.62 26.28  ? 87  ILE A CG2   1 
ATOM   505  C  CG2   B ILE A 1 70  ? -14.754 28.496 13.941 0.38 26.10  ? 87  ILE A CG2   1 
ATOM   506  C  CD1   A ILE A 1 70  ? -15.109 29.293 11.181 0.62 29.72  ? 87  ILE A CD1   1 
ATOM   507  C  CD1   B ILE A 1 70  ? -13.240 29.819 11.644 0.38 22.12  ? 87  ILE A CD1   1 
ATOM   508  N  N     . GLU A 1 71  ? -12.835 25.318 14.651 1.00 26.92  ? 88  GLU A N     1 
ATOM   509  C  CA    . GLU A 1 71  ? -12.872 24.517 15.871 1.00 29.59  ? 88  GLU A CA    1 
ATOM   510  C  C     . GLU A 1 71  ? -11.523 24.517 16.577 1.00 29.30  ? 88  GLU A C     1 
ATOM   511  O  O     . GLU A 1 71  ? -11.446 24.696 17.799 1.00 27.57  ? 88  GLU A O     1 
ATOM   512  C  CB    . GLU A 1 71  ? -13.292 23.084 15.538 1.00 37.68  ? 88  GLU A CB    1 
ATOM   513  C  CG    . GLU A 1 71  ? -14.769 22.948 15.168 1.00 57.99  ? 88  GLU A CG    1 
ATOM   514  C  CD    . GLU A 1 71  ? -15.128 21.549 14.683 1.00 82.63  ? 88  GLU A CD    1 
ATOM   515  O  OE1   . GLU A 1 71  ? -14.253 20.656 14.731 1.00 66.93  ? 88  GLU A OE1   1 
ATOM   516  O  OE2   . GLU A 1 71  ? -16.285 21.346 14.252 1.00 90.30  ? 88  GLU A OE2   1 
ATOM   517  N  N     . LYS A 1 72  ? -10.444 24.327 15.824 1.00 25.39  ? 89  LYS A N     1 
ATOM   518  C  CA    . LYS A 1 72  ? -9.130  24.285 16.444 1.00 27.67  ? 89  LYS A CA    1 
ATOM   519  C  C     . LYS A 1 72  ? -8.763  25.631 17.031 1.00 23.13  ? 89  LYS A C     1 
ATOM   520  O  O     . LYS A 1 72  ? -8.021  25.695 18.024 1.00 25.29  ? 89  LYS A O     1 
ATOM   521  C  CB    . LYS A 1 72  ? -8.093  23.841 15.420 1.00 31.29  ? 89  LYS A CB    1 
ATOM   522  C  CG    . LYS A 1 72  ? -8.410  22.488 14.838 1.00 45.04  ? 89  LYS A CG    1 
ATOM   523  C  CD    . LYS A 1 72  ? -7.808  21.382 15.662 1.00 50.16  ? 89  LYS A CD    1 
ATOM   524  C  CE    . LYS A 1 72  ? -6.950  20.496 14.802 1.00 46.52  ? 89  LYS A CE    1 
ATOM   525  N  NZ    . LYS A 1 72  ? -6.033  21.317 13.978 1.00 55.95  ? 89  LYS A NZ    1 
ATOM   526  N  N     . MET A 1 73  ? -9.284  26.711 16.444 1.00 24.95  ? 90  MET A N     1 
ATOM   527  C  CA    . MET A 1 73  ? -8.946  28.060 16.872 1.00 21.63  ? 90  MET A CA    1 
ATOM   528  C  C     . MET A 1 73  ? -9.860  28.587 17.966 1.00 20.71  ? 90  MET A C     1 
ATOM   529  O  O     . MET A 1 73  ? -9.597  29.677 18.480 1.00 20.55  ? 90  MET A O     1 
ATOM   530  C  CB    . MET A 1 73  ? -8.996  29.019 15.674 1.00 23.78  ? 90  MET A CB    1 
ATOM   531  C  CG    . MET A 1 73  ? -7.834  28.880 14.719 1.00 24.17  ? 90  MET A CG    1 
ATOM   532  S  SD    . MET A 1 73  ? -6.300  29.377 15.501 1.00 22.59  ? 90  MET A SD    1 
ATOM   533  C  CE    . MET A 1 73  ? -6.596  31.122 15.749 1.00 28.40  ? 90  MET A CE    1 
ATOM   534  N  N     . THR A 1 74  ? -10.923 27.848 18.320 1.00 22.18  ? 91  THR A N     1 
ATOM   535  C  CA    . THR A 1 74  ? -11.831 28.236 19.398 1.00 20.44  ? 91  THR A CA    1 
ATOM   536  C  C     . THR A 1 74  ? -11.160 27.892 20.719 1.00 21.85  ? 91  THR A C     1 
ATOM   537  O  O     . THR A 1 74  ? -11.177 26.745 21.177 1.00 27.17  ? 91  THR A O     1 
ATOM   538  C  CB    . THR A 1 74  ? -13.179 27.540 19.270 1.00 20.44  ? 91  THR A CB    1 
ATOM   539  O  OG1   . THR A 1 74  ? -13.814 27.970 18.059 1.00 24.74  ? 91  THR A OG1   1 
ATOM   540  C  CG2   . THR A 1 74  ? -14.076 27.910 20.405 1.00 22.24  ? 91  THR A CG2   1 
ATOM   541  N  N     . GLY A 1 75  ? -10.609 28.900 21.356 1.00 16.89  ? 92  GLY A N     1 
ATOM   542  C  CA    . GLY A 1 75  ? -9.790  28.705 22.522 1.00 17.63  ? 92  GLY A CA    1 
ATOM   543  C  C     . GLY A 1 75  ? -9.022  29.967 22.824 1.00 14.77  ? 92  GLY A C     1 
ATOM   544  O  O     . GLY A 1 75  ? -9.174  30.985 22.145 1.00 16.20  ? 92  GLY A O     1 
ATOM   545  N  N     . PRO A 1 76  ? -8.209  29.934 23.877 1.00 15.45  ? 93  PRO A N     1 
ATOM   546  C  CA    . PRO A 1 76  ? -7.396  31.107 24.216 1.00 16.44  ? 93  PRO A CA    1 
ATOM   547  C  C     . PRO A 1 76  ? -6.431  31.435 23.090 1.00 14.86  ? 93  PRO A C     1 
ATOM   548  O  O     . PRO A 1 76  ? -5.828  30.546 22.482 1.00 14.70  ? 93  PRO A O     1 
ATOM   549  C  CB    . PRO A 1 76  ? -6.663  30.671 25.486 1.00 15.46  ? 93  PRO A CB    1 
ATOM   550  C  CG    . PRO A 1 76  ? -6.615  29.175 25.403 1.00 16.51  ? 93  PRO A CG    1 
ATOM   551  C  CD    . PRO A 1 76  ? -7.913  28.787 24.744 1.00 17.58  ? 93  PRO A CD    1 
ATOM   552  N  N     . VAL A 1 77  ? -6.288  32.728 22.828 1.00 15.76  ? 94  VAL A N     1 
ATOM   553  C  CA    . VAL A 1 77  ? -5.339  33.245 21.848 1.00 16.06  ? 94  VAL A CA    1 
ATOM   554  C  C     . VAL A 1 77  ? -4.690  34.500 22.413 1.00 16.33  ? 94  VAL A C     1 
ATOM   555  O  O     . VAL A 1 77  ? -5.279  35.209 23.238 1.00 15.02  ? 94  VAL A O     1 
ATOM   556  C  CB    . VAL A 1 77  ? -5.978  33.578 20.492 1.00 13.84  ? 94  VAL A CB    1 
ATOM   557  C  CG1   . VAL A 1 77  ? -6.536  32.347 19.890 1.00 15.60  ? 94  VAL A CG1   1 
ATOM   558  C  CG2   . VAL A 1 77  ? -7.060  34.651 20.620 1.00 13.84  ? 94  VAL A CG2   1 
ATOM   559  N  N     . LEU A 1 78  ? -3.460  34.780 21.976 1.00 13.69  ? 95  LEU A N     1 
ATOM   560  C  CA    . LEU A 1 78  ? -2.806  36.044 22.312 1.00 12.68  ? 95  LEU A CA    1 
ATOM   561  C  C     . LEU A 1 78  ? -2.761  36.895 21.044 1.00 12.97  ? 95  LEU A C     1 
ATOM   562  O  O     . LEU A 1 78  ? -2.054  36.568 20.084 1.00 15.00  ? 95  LEU A O     1 
ATOM   563  C  CB    . LEU A 1 78  ? -1.413  35.849 22.923 1.00 13.00  ? 95  LEU A CB    1 
ATOM   564  C  CG    . LEU A 1 78  ? -0.852  37.140 23.504 1.00 13.09  ? 95  LEU A CG    1 
ATOM   565  C  CD1   . LEU A 1 78  ? -1.579  37.566 24.782 1.00 15.27  ? 95  LEU A CD1   1 
ATOM   566  C  CD2   . LEU A 1 78  ? 0.619   36.982 23.816 1.00 12.64  ? 95  LEU A CD2   1 
ATOM   567  N  N     . CYS A 1 79  ? -3.572  37.953 21.034 1.00 13.06  ? 96  CYS A N     1 
ATOM   568  C  CA    . CYS A 1 79  ? -3.566  38.950 19.975 1.00 12.37  ? 96  CYS A CA    1 
ATOM   569  C  C     . CYS A 1 79  ? -2.369  39.881 20.151 1.00 14.53  ? 96  CYS A C     1 
ATOM   570  O  O     . CYS A 1 79  ? -2.127  40.369 21.251 1.00 15.68  ? 96  CYS A O     1 
ATOM   571  C  CB    . CYS A 1 79  ? -4.847  39.775 20.011 1.00 14.35  ? 96  CYS A CB    1 
ATOM   572  S  SG    . CYS A 1 79  ? -6.368  38.806 20.133 1.00 17.42  ? 96  CYS A SG    1 
ATOM   573  N  N     . MET A 1 80  ? -1.639  40.158 19.071 1.00 13.85  ? 97  MET A N     1 
ATOM   574  C  CA    . MET A 1 80  ? -0.455  40.997 19.165 1.00 13.38  ? 97  MET A CA    1 
ATOM   575  C  C     . MET A 1 80  ? -0.368  41.904 17.951 1.00 14.93  ? 97  MET A C     1 
ATOM   576  O  O     . MET A 1 80  ? -0.765  41.529 16.842 1.00 15.36  ? 97  MET A O     1 
ATOM   577  C  CB    . MET A 1 80  ? 0.839   40.156 19.276 1.00 14.11  ? 97  MET A CB    1 
ATOM   578  C  CG    . MET A 1 80  ? 0.705   38.987 20.245 1.00 15.76  ? 97  MET A CG    1 
ATOM   579  S  SD    . MET A 1 80  ? 2.253   38.058 20.480 1.00 14.90  ? 97  MET A SD    1 
ATOM   580  C  CE    . MET A 1 80  ? 2.501   37.295 18.870 1.00 17.84  ? 97  MET A CE    1 
ATOM   581  N  N     . VAL A 1 81  ? 0.186   43.088 18.156 1.00 13.78  ? 98  VAL A N     1 
ATOM   582  C  CA    . VAL A 1 81  ? 0.636   43.930 17.054 1.00 14.12  ? 98  VAL A CA    1 
ATOM   583  C  C     . VAL A 1 81  ? 2.101   44.245 17.283 1.00 14.62  ? 98  VAL A C     1 
ATOM   584  O  O     . VAL A 1 81  ? 2.458   44.738 18.354 1.00 15.01  ? 98  VAL A O     1 
ATOM   585  C  CB    . VAL A 1 81  ? -0.171  45.224 16.935 1.00 15.00  ? 98  VAL A CB    1 
ATOM   586  C  CG1   . VAL A 1 81  ? 0.399   46.061 15.798 1.00 16.65  ? 98  VAL A CG1   1 
ATOM   587  C  CG2   . VAL A 1 81  ? -1.639  44.903 16.714 1.00 16.58  ? 98  VAL A CG2   1 
ATOM   588  N  N     . PHE A 1 82  ? 2.946   43.926 16.294 1.00 11.43  ? 99  PHE A N     1 
ATOM   589  C  CA    . PHE A 1 82  ? 4.366   44.247 16.291 1.00 13.54  ? 99  PHE A CA    1 
ATOM   590  C  C     . PHE A 1 82  ? 4.671   45.240 15.174 1.00 14.57  ? 99  PHE A C     1 
ATOM   591  O  O     . PHE A 1 82  ? 4.069   45.198 14.095 1.00 14.07  ? 99  PHE A O     1 
ATOM   592  C  CB    . PHE A 1 82  ? 5.223   42.982 16.119 1.00 14.99  ? 99  PHE A CB    1 
ATOM   593  C  CG    . PHE A 1 82  ? 5.466   42.240 17.395 1.00 13.19  ? 99  PHE A CG    1 
ATOM   594  C  CD1   . PHE A 1 82  ? 6.534   42.594 18.207 1.00 12.39  ? 99  PHE A CD1   1 
ATOM   595  C  CD2   . PHE A 1 82  ? 4.632   41.215 17.804 1.00 16.87  ? 99  PHE A CD2   1 
ATOM   596  C  CE1   . PHE A 1 82  ? 6.772   41.923 19.399 1.00 15.75  ? 99  PHE A CE1   1 
ATOM   597  C  CE2   . PHE A 1 82  ? 4.889   40.526 19.015 1.00 17.88  ? 99  PHE A CE2   1 
ATOM   598  C  CZ    . PHE A 1 82  ? 5.940   40.904 19.790 1.00 13.84  ? 99  PHE A CZ    1 
ATOM   599  N  N     . GLU A 1 83  ? 5.612   46.138 15.452 1.00 13.48  ? 100 GLU A N     1 
ATOM   600  C  CA    . GLU A 1 83  ? 6.032   47.214 14.562 1.00 14.88  ? 100 GLU A CA    1 
ATOM   601  C  C     . GLU A 1 83  ? 7.506   47.056 14.206 1.00 15.69  ? 100 GLU A C     1 
ATOM   602  O  O     . GLU A 1 83  ? 8.346   46.815 15.082 1.00 15.96  ? 100 GLU A O     1 
ATOM   603  C  CB    . GLU A 1 83  ? 5.814   48.574 15.239 1.00 14.92  ? 100 GLU A CB    1 
ATOM   604  C  CG    . GLU A 1 83  ? 6.249   49.756 14.400 1.00 16.96  ? 100 GLU A CG    1 
ATOM   605  C  CD    . GLU A 1 83  ? 6.033   51.061 15.147 1.00 19.17  ? 100 GLU A CD    1 
ATOM   606  O  OE1   . GLU A 1 83  ? 4.892   51.579 15.086 1.00 20.61  ? 100 GLU A OE1   1 
ATOM   607  O  OE2   . GLU A 1 83  ? 6.998   51.504 15.836 1.00 23.06  ? 100 GLU A OE2   1 
ATOM   608  N  N     . GLY A 1 84  ? 7.828   47.225 12.932 1.00 13.61  ? 101 GLY A N     1 
ATOM   609  C  CA    . GLY A 1 84  ? 9.207   47.161 12.492 1.00 15.50  ? 101 GLY A CA    1 
ATOM   610  C  C     . GLY A 1 84  ? 9.276   47.406 10.998 1.00 13.95  ? 101 GLY A C     1 
ATOM   611  O  O     . GLY A 1 84  ? 8.252   47.515 10.316 1.00 15.67  ? 101 GLY A O     1 
ATOM   612  N  N     . VAL A 1 85  ? 10.513  47.534 10.518 1.00 15.09  ? 102 VAL A N     1 
ATOM   613  C  CA    . VAL A 1 85  ? 10.759  47.668 9.084  1.00 15.35  ? 102 VAL A CA    1 
ATOM   614  C  C     . VAL A 1 85  ? 10.328  46.374 8.408  1.00 13.32  ? 102 VAL A C     1 
ATOM   615  O  O     . VAL A 1 85  ? 10.775  45.283 8.769  1.00 15.75  ? 102 VAL A O     1 
ATOM   616  C  CB    . VAL A 1 85  ? 12.233  47.982 8.811  1.00 17.43  ? 102 VAL A CB    1 
ATOM   617  C  CG1   . VAL A 1 85  ? 12.528  47.961 7.313  1.00 18.76  ? 102 VAL A CG1   1 
ATOM   618  C  CG2   . VAL A 1 85  ? 12.592  49.334 9.400  1.00 17.96  ? 102 VAL A CG2   1 
ATOM   619  N  N     . ASP A 1 86  ? 9.419   46.485 7.430  1.00 14.40  ? 103 ASP A N     1 
ATOM   620  C  CA    . ASP A 1 86  ? 9.034   45.329 6.621  1.00 15.40  ? 103 ASP A CA    1 
ATOM   621  C  C     . ASP A 1 86  ? 8.485   44.197 7.490  1.00 15.29  ? 103 ASP A C     1 
ATOM   622  O  O     . ASP A 1 86  ? 8.602   43.027 7.142  1.00 15.21  ? 103 ASP A O     1 
ATOM   623  C  CB    . ASP A 1 86  ? 10.237  44.858 5.791  1.00 17.44  ? 103 ASP A CB    1 
ATOM   624  C  CG    . ASP A 1 86  ? 9.883   43.873 4.686  1.00 23.81  ? 103 ASP A CG    1 
ATOM   625  O  OD1   . ASP A 1 86  ? 8.838   44.030 3.977  1.00 23.45  ? 103 ASP A OD1   1 
ATOM   626  O  OD2   . ASP A 1 86  ? 10.724  42.965 4.458  1.00 21.94  ? 103 ASP A OD2   1 
ATOM   627  N  N     . VAL A 1 87  ? 7.868   44.525 8.627  1.00 15.04  ? 104 VAL A N     1 
ATOM   628  C  CA    . VAL A 1 87  ? 7.591   43.484 9.616  1.00 14.22  ? 104 VAL A CA    1 
ATOM   629  C  C     . VAL A 1 87  ? 6.506   42.527 9.143  1.00 12.44  ? 104 VAL A C     1 
ATOM   630  O  O     . VAL A 1 87  ? 6.446   41.389 9.617  1.00 14.34  ? 104 VAL A O     1 
ATOM   631  C  CB    . VAL A 1 87  ? 7.245   44.093 10.987 1.00 14.40  ? 104 VAL A CB    1 
ATOM   632  C  CG1   . VAL A 1 87  ? 5.910   44.818 10.987 1.00 14.45  ? 104 VAL A CG1   1 
ATOM   633  C  CG2   . VAL A 1 87  ? 7.260   43.011 12.098 1.00 13.10  ? 104 VAL A CG2   1 
ATOM   634  N  N     . ILE A 1 88  ? 5.607   42.957 8.245  1.00 13.09  ? 105 ILE A N     1 
ATOM   635  C  CA    . ILE A 1 88  ? 4.582   42.021 7.766  1.00 14.78  ? 105 ILE A CA    1 
ATOM   636  C  C     . ILE A 1 88  ? 5.241   40.834 7.066  1.00 14.47  ? 105 ILE A C     1 
ATOM   637  O  O     . ILE A 1 88  ? 5.061   39.671 7.451  1.00 15.20  ? 105 ILE A O     1 
ATOM   638  C  CB    . ILE A 1 88  ? 3.573   42.724 6.841  1.00 15.70  ? 105 ILE A CB    1 
ATOM   639  C  CG1   . ILE A 1 88  ? 2.795   43.796 7.609  1.00 14.25  ? 105 ILE A CG1   1 
ATOM   640  C  CG2   . ILE A 1 88  ? 2.598   41.711 6.312  1.00 15.60  ? 105 ILE A CG2   1 
ATOM   641  C  CD1   . ILE A 1 88  ? 2.037   44.772 6.709  1.00 17.82  ? 105 ILE A CD1   1 
ATOM   642  N  N     . ALA A 1 89  ? 6.037   41.111 6.027  1.00 14.30  ? 106 ALA A N     1 
ATOM   643  C  CA    . ALA A 1 89  ? 6.725   40.038 5.323  1.00 15.37  ? 106 ALA A CA    1 
ATOM   644  C  C     . ALA A 1 89  ? 7.763   39.337 6.191  1.00 13.07  ? 106 ALA A C     1 
ATOM   645  O  O     . ALA A 1 89  ? 7.935   38.117 6.082  1.00 14.73  ? 106 ALA A O     1 
ATOM   646  C  CB    . ALA A 1 89  ? 7.413   40.580 4.075  1.00 16.11  ? 106 ALA A CB    1 
ATOM   647  N  N     . GLN A 1 90  ? 8.487   40.088 7.030  1.00 14.20  ? 107 GLN A N     1 
ATOM   648  C  CA    . GLN A 1 90  ? 9.519   39.468 7.859  1.00 12.90  ? 107 GLN A CA    1 
ATOM   649  C  C     . GLN A 1 90  ? 8.908   38.528 8.887  1.00 13.44  ? 107 GLN A C     1 
ATOM   650  O  O     . GLN A 1 90  ? 9.446   37.442 9.147  1.00 13.36  ? 107 GLN A O     1 
ATOM   651  C  CB    . GLN A 1 90  ? 10.360  40.534 8.539  1.00 14.23  ? 107 GLN A CB    1 
ATOM   652  C  CG    . GLN A 1 90  ? 11.278  41.275 7.571  1.00 15.27  ? 107 GLN A CG    1 
ATOM   653  C  CD    . GLN A 1 90  ? 12.302  40.350 6.923  1.00 15.62  ? 107 GLN A CD    1 
ATOM   654  O  OE1   . GLN A 1 90  ? 13.035  39.649 7.594  1.00 15.52  ? 107 GLN A OE1   1 
ATOM   655  N  NE2   . GLN A 1 90  ? 12.317  40.327 5.592  1.00 16.48  ? 107 GLN A NE2   1 
ATOM   656  N  N     . ALA A 1 91  ? 7.783   38.924 9.488  1.00 12.36  ? 108 ALA A N     1 
ATOM   657  C  CA    . ALA A 1 91  ? 7.175   38.032 10.467 1.00 13.11  ? 108 ALA A CA    1 
ATOM   658  C  C     . ALA A 1 91  ? 6.693   36.756 9.794  1.00 13.24  ? 108 ALA A C     1 
ATOM   659  O  O     . ALA A 1 91  ? 6.804   35.667 10.367 1.00 13.82  ? 108 ALA A O     1 
ATOM   660  C  CB    . ALA A 1 91  ? 6.020   38.713 11.202 1.00 14.23  ? 108 ALA A CB    1 
ATOM   661  N  N     . ARG A 1 92  ? 6.161   36.867 8.573  1.00 14.86  ? 109 ARG A N     1 
ATOM   662  C  CA    . ARG A 1 92  ? 5.762   35.665 7.846  1.00 15.13  ? 109 ARG A CA    1 
ATOM   663  C  C     . ARG A 1 92  ? 6.957   34.754 7.582  1.00 13.23  ? 109 ARG A C     1 
ATOM   664  O  O     . ARG A 1 92  ? 6.852   33.521 7.686  1.00 15.22  ? 109 ARG A O     1 
ATOM   665  C  CB    . ARG A 1 92  ? 5.070   36.047 6.542  1.00 15.30  ? 109 ARG A CB    1 
ATOM   666  C  CG    . ARG A 1 92  ? 3.750   36.753 6.741  1.00 17.28  ? 109 ARG A CG    1 
ATOM   667  C  CD    . ARG A 1 92  ? 2.669   35.775 7.046  1.00 21.93  ? 109 ARG A CD    1 
ATOM   668  N  NE    . ARG A 1 92  ? 2.305   35.071 5.823  1.00 29.11  ? 109 ARG A NE    1 
ATOM   669  C  CZ    . ARG A 1 92  ? 1.326   34.184 5.734  1.00 37.94  ? 109 ARG A CZ    1 
ATOM   670  N  NH1   . ARG A 1 92  ? 0.632   33.822 6.802  1.00 32.86  ? 109 ARG A NH1   1 
ATOM   671  N  NH2   . ARG A 1 92  ? 1.022   33.667 4.540  1.00 36.66  ? 109 ARG A NH2   1 
ATOM   672  N  N     . LYS A 1 93  ? 8.105   35.340 7.238  1.00 12.82  ? 110 LYS A N     1 
ATOM   673  C  CA    . LYS A 1 93  ? 9.328   34.562 7.038  1.00 13.18  ? 110 LYS A CA    1 
ATOM   674  C  C     . LYS A 1 93  ? 9.768   33.871 8.326  1.00 12.81  ? 110 LYS A C     1 
ATOM   675  O  O     . LYS A 1 93  ? 10.239  32.723 8.307  1.00 14.83  ? 110 LYS A O     1 
ATOM   676  C  CB    . LYS A 1 93  ? 10.421  35.497 6.524  1.00 15.77  ? 110 LYS A CB    1 
ATOM   677  C  CG    . LYS A 1 93  ? 11.735  34.830 6.252  1.00 15.03  ? 110 LYS A CG    1 
ATOM   678  C  CD    . LYS A 1 93  ? 12.653  35.828 5.559  1.00 19.01  ? 110 LYS A CD    1 
ATOM   679  C  CE    . LYS A 1 93  ? 14.032  35.242 5.394  1.00 25.51  ? 110 LYS A CE    1 
ATOM   680  N  NZ    . LYS A 1 93  ? 14.911  36.206 4.692  1.00 22.37  ? 110 LYS A NZ    1 
ATOM   681  N  N     . MET A 1 94  ? 9.632   34.565 9.459  1.00 13.60  ? 111 MET A N     1 
ATOM   682  C  CA    . MET A 1 94  ? 10.030  33.993 10.744 1.00 13.58  ? 111 MET A CA    1 
ATOM   683  C  C     . MET A 1 94  ? 9.105   32.865 11.174 1.00 13.08  ? 111 MET A C     1 
ATOM   684  O  O     . MET A 1 94  ? 9.546   31.936 11.860 1.00 12.59  ? 111 MET A O     1 
ATOM   685  C  CB    . MET A 1 94  ? 10.051  35.066 11.817 1.00 14.23  ? 111 MET A CB    1 
ATOM   686  C  CG    . MET A 1 94  ? 11.113  36.111 11.586 1.00 14.04  ? 111 MET A CG    1 
ATOM   687  S  SD    . MET A 1 94  ? 10.853  37.596 12.564 1.00 14.92  ? 111 MET A SD    1 
ATOM   688  C  CE    . MET A 1 94  ? 11.380  37.031 14.178 1.00 17.15  ? 111 MET A CE    1 
ATOM   689  N  N     . MET A 1 95  ? 7.819   32.964 10.828 1.00 11.92  ? 112 MET A N     1 
ATOM   690  C  CA    . MET A 1 95  ? 6.851   31.917 11.133 1.00 11.00  ? 112 MET A CA    1 
ATOM   691  C  C     . MET A 1 95  ? 7.151   30.649 10.352 1.00 14.32  ? 112 MET A C     1 
ATOM   692  O  O     . MET A 1 95  ? 7.070   29.538 10.889 1.00 12.73  ? 112 MET A O     1 
ATOM   693  C  CB    . MET A 1 95  ? 5.439   32.410 10.791 1.00 14.25  ? 112 MET A CB    1 
ATOM   694  C  CG    . MET A 1 95  ? 4.926   33.423 11.758 1.00 15.19  ? 112 MET A CG    1 
ATOM   695  S  SD    . MET A 1 95  ? 3.348   34.097 11.198 1.00 20.53  ? 112 MET A SD    1 
ATOM   696  C  CE    . MET A 1 95  ? 2.489   32.696 10.542 1.00 21.78  ? 112 MET A CE    1 
ATOM   697  N  N     . GLY A 1 96  ? 7.489   30.805 9.068  1.00 12.41  ? 113 GLY A N     1 
ATOM   698  C  CA    . GLY A 1 96  ? 7.727   29.692 8.162  1.00 13.69  ? 113 GLY A CA    1 
ATOM   699  C  C     . GLY A 1 96  ? 6.459   29.224 7.478  1.00 13.13  ? 113 GLY A C     1 
ATOM   700  O  O     . GLY A 1 96  ? 5.348   29.682 7.758  1.00 15.48  ? 113 GLY A O     1 
ATOM   701  N  N     . SER A 1 97  ? 6.645   28.257 6.580  1.00 13.74  ? 114 SER A N     1 
ATOM   702  C  CA    A SER A 1 97  ? 5.563   27.709 5.769  0.68 14.52  ? 114 SER A CA    1 
ATOM   703  C  CA    B SER A 1 97  ? 5.526   27.806 5.770  0.32 14.64  ? 114 SER A CA    1 
ATOM   704  C  C     . SER A 1 97  ? 4.418   27.199 6.633  1.00 12.79  ? 114 SER A C     1 
ATOM   705  O  O     . SER A 1 97  ? 4.641   26.703 7.735  1.00 14.95  ? 114 SER A O     1 
ATOM   706  C  CB    A SER A 1 97  ? 6.081   26.545 4.914  0.68 16.07  ? 114 SER A CB    1 
ATOM   707  C  CB    B SER A 1 97  ? 5.997   26.793 4.730  0.32 17.13  ? 114 SER A CB    1 
ATOM   708  O  OG    A SER A 1 97  ? 7.335   26.834 4.323  0.68 18.22  ? 114 SER A OG    1 
ATOM   709  O  OG    B SER A 1 97  ? 6.614   25.692 5.358  0.32 12.58  ? 114 SER A OG    1 
ATOM   710  N  N     . THR A 1 98  ? 3.202   27.224 6.059  1.00 14.95  ? 115 THR A N     1 
ATOM   711  C  CA    . THR A 1 98  ? 1.996   26.718 6.714  1.00 14.77  ? 115 THR A CA    1 
ATOM   712  C  C     . THR A 1 98  ? 2.204   25.316 7.265  1.00 15.02  ? 115 THR A C     1 
ATOM   713  O  O     . THR A 1 98  ? 1.826   25.017 8.409  1.00 15.73  ? 115 THR A O     1 
ATOM   714  C  CB    . THR A 1 98  ? 0.847   26.715 5.702  1.00 17.48  ? 115 THR A CB    1 
ATOM   715  O  OG1   . THR A 1 98  ? 0.728   28.016 5.104  1.00 18.54  ? 115 THR A OG1   1 
ATOM   716  C  CG2   . THR A 1 98  ? -0.452  26.318 6.350  1.00 21.32  ? 115 THR A CG2   1 
ATOM   717  N  N     . ARG A 1 99  ? 2.803   24.446 6.463  1.00 13.16  ? 116 ARG A N     1 
ATOM   718  C  CA    . ARG A 1 99  ? 3.159   23.106 6.899  1.00 14.35  ? 116 ARG A CA    1 
ATOM   719  C  C     . ARG A 1 99  ? 4.490   23.149 7.641  1.00 14.66  ? 116 ARG A C     1 
ATOM   720  O  O     . ARG A 1 99  ? 5.516   23.443 7.030  1.00 15.38  ? 116 ARG A O     1 
ATOM   721  C  CB    . ARG A 1 99  ? 3.287   22.161 5.717  1.00 16.02  ? 116 ARG A CB    1 
ATOM   722  C  CG    . ARG A 1 99  ? 1.992   21.848 5.048  1.00 18.16  ? 116 ARG A CG    1 
ATOM   723  C  CD    . ARG A 1 99  ? 2.274   21.160 3.747  1.00 20.14  ? 116 ARG A CD    1 
ATOM   724  N  NE    . ARG A 1 99  ? 1.074   20.546 3.215  1.00 26.41  ? 116 ARG A NE    1 
ATOM   725  C  CZ    . ARG A 1 99  ? 0.970   20.140 1.960  1.00 33.08  ? 116 ARG A CZ    1 
ATOM   726  N  NH1   . ARG A 1 99  ? 1.956   20.337 1.091  1.00 25.65  ? 116 ARG A NH1   1 
ATOM   727  N  NH2   . ARG A 1 99  ? -0.148  19.537 1.566  1.00 26.57  ? 116 ARG A NH2   1 
ATOM   728  N  N     . PRO A 1 100 ? 4.525   22.855 8.945  1.00 12.40  ? 117 PRO A N     1 
ATOM   729  C  CA    . PRO A 1 100 ? 5.813   22.834 9.652  1.00 12.65  ? 117 PRO A CA    1 
ATOM   730  C  C     . PRO A 1 100 ? 6.857   21.950 9.019  1.00 13.66  ? 117 PRO A C     1 
ATOM   731  O  O     . PRO A 1 100 ? 8.061   22.243 9.097  1.00 14.64  ? 117 PRO A O     1 
ATOM   732  C  CB    . PRO A 1 100 ? 5.419   22.303 11.037 1.00 13.11  ? 117 PRO A CB    1 
ATOM   733  C  CG    . PRO A 1 100 ? 3.957   22.744 11.184 1.00 12.96  ? 117 PRO A CG    1 
ATOM   734  C  CD    . PRO A 1 100 ? 3.380   22.585 9.832  1.00 12.14  ? 117 PRO A CD    1 
ATOM   735  N  N     . GLY A 1 101 ? 6.438   20.853 8.399  1.00 12.38  ? 118 GLY A N     1 
ATOM   736  C  CA    . GLY A 1 101 ? 7.406   19.963 7.778  1.00 14.06  ? 118 GLY A CA    1 
ATOM   737  C  C     . GLY A 1 101 ? 8.099   20.541 6.558  1.00 14.59  ? 118 GLY A C     1 
ATOM   738  O  O     . GLY A 1 101 ? 9.133   20.005 6.150  1.00 14.75  ? 118 GLY A O     1 
ATOM   739  N  N     . GLU A 1 102 ? 7.530   21.592 5.949  1.00 12.19  ? 119 GLU A N     1 
ATOM   740  C  CA    . GLU A 1 102 ? 8.129   22.290 4.827  1.00 13.94  ? 119 GLU A CA    1 
ATOM   741  C  C     . GLU A 1 102 ? 8.842   23.554 5.260  1.00 16.68  ? 119 GLU A C     1 
ATOM   742  O  O     . GLU A 1 102 ? 9.582   24.144 4.459  1.00 16.10  ? 119 GLU A O     1 
ATOM   743  C  CB    . GLU A 1 102 ? 7.051   22.652 3.782  1.00 15.50  ? 119 GLU A CB    1 
ATOM   744  C  CG    . GLU A 1 102 ? 6.315   21.454 3.192  1.00 12.99  ? 119 GLU A CG    1 
ATOM   745  C  CD    . GLU A 1 102 ? 5.259   21.863 2.153  1.00 15.45  ? 119 GLU A CD    1 
ATOM   746  O  OE1   . GLU A 1 102 ? 4.889   23.063 2.126  1.00 19.47  ? 119 GLU A OE1   1 
ATOM   747  O  OE2   . GLU A 1 102 ? 4.803   20.956 1.406  1.00 20.18  ? 119 GLU A OE2   1 
ATOM   748  N  N     . ALA A 1 103 ? 8.630   23.981 6.499  1.00 14.97  ? 120 ALA A N     1 
ATOM   749  C  CA    . ALA A 1 103 ? 9.180   25.243 6.959  1.00 12.84  ? 120 ALA A CA    1 
ATOM   750  C  C     . ALA A 1 103 ? 10.687  25.147 7.158  1.00 15.44  ? 120 ALA A C     1 
ATOM   751  O  O     . ALA A 1 103 ? 11.238  24.086 7.462  1.00 15.33  ? 120 ALA A O     1 
ATOM   752  C  CB    . ALA A 1 103 ? 8.524   25.669 8.270  1.00 14.72  ? 120 ALA A CB    1 
ATOM   753  N  N     . ALA A 1 104 ? 11.347  26.277 6.992  1.00 15.74  ? 121 ALA A N     1 
ATOM   754  C  CA    . ALA A 1 104 ? 12.797  26.289 7.050  1.00 18.11  ? 121 ALA A CA    1 
ATOM   755  C  C     . ALA A 1 104 ? 13.290  26.099 8.484  1.00 16.83  ? 121 ALA A C     1 
ATOM   756  O  O     . ALA A 1 104 ? 12.715  26.647 9.430  1.00 13.40  ? 121 ALA A O     1 
ATOM   757  C  CB    . ALA A 1 104 ? 13.314  27.604 6.475  1.00 17.30  ? 121 ALA A CB    1 
ATOM   758  N  N     . PRO A 1 105 ? 14.394  25.386 8.691  1.00 19.70  ? 122 PRO A N     1 
ATOM   759  C  CA    . PRO A 1 105 ? 14.945  25.310 10.050 1.00 19.29  ? 122 PRO A CA    1 
ATOM   760  C  C     . PRO A 1 105 ? 15.222  26.712 10.564 1.00 14.95  ? 122 PRO A C     1 
ATOM   761  O  O     . PRO A 1 105 ? 15.568  27.610 9.795  1.00 18.05  ? 122 PRO A O     1 
ATOM   762  C  CB    . PRO A 1 105 ? 16.229  24.487 9.878  1.00 25.62  ? 122 PRO A CB    1 
ATOM   763  C  CG    . PRO A 1 105 ? 15.993  23.695 8.631  1.00 30.06  ? 122 PRO A CG    1 
ATOM   764  C  CD    . PRO A 1 105 ? 15.169  24.583 7.727  1.00 27.46  ? 122 PRO A CD    1 
ATOM   765  N  N     . GLY A 1 106 ? 14.962  26.919 11.851 1.00 15.80  ? 123 GLY A N     1 
ATOM   766  C  CA    . GLY A 1 106 ? 15.064  28.237 12.452 1.00 16.49  ? 123 GLY A CA    1 
ATOM   767  C  C     . GLY A 1 106 ? 13.796  29.060 12.440 1.00 14.99  ? 123 GLY A C     1 
ATOM   768  O  O     . GLY A 1 106 ? 13.759  30.136 13.060 1.00 16.68  ? 123 GLY A O     1 
ATOM   769  N  N     . THR A 1 107 ? 12.763  28.620 11.738 1.00 13.91  ? 124 THR A N     1 
ATOM   770  C  CA    . THR A 1 107 ? 11.474  29.283 11.813 1.00 13.00  ? 124 THR A CA    1 
ATOM   771  C  C     . THR A 1 107 ? 10.663  28.722 12.977 1.00 12.35  ? 124 THR A C     1 
ATOM   772  O  O     . THR A 1 107 ? 10.916  27.620 13.468 1.00 13.56  ? 124 THR A O     1 
ATOM   773  C  CB    . THR A 1 107 ? 10.671  29.128 10.507 1.00 12.89  ? 124 THR A CB    1 
ATOM   774  O  OG1   . THR A 1 107 ? 10.365  27.749 10.241 1.00 13.56  ? 124 THR A OG1   1 
ATOM   775  C  CG2   . THR A 1 107 ? 11.415  29.738 9.337  1.00 13.90  ? 124 THR A CG2   1 
ATOM   776  N  N     . ILE A 1 108 ? 9.629   29.477 13.370 1.00 11.35  ? 125 ILE A N     1 
ATOM   777  C  CA    . ILE A 1 108 ? 8.782   29.073 14.489 1.00 10.78  ? 125 ILE A CA    1 
ATOM   778  C  C     . ILE A 1 108 ? 8.109   27.747 14.195 1.00 14.44  ? 125 ILE A C     1 
ATOM   779  O  O     . ILE A 1 108 ? 8.140   26.820 15.011 1.00 12.61  ? 125 ILE A O     1 
ATOM   780  C  CB    . ILE A 1 108 ? 7.769   30.175 14.811 1.00 13.79  ? 125 ILE A CB    1 
ATOM   781  C  CG1   . ILE A 1 108 ? 8.526   31.381 15.355 1.00 13.81  ? 125 ILE A CG1   1 
ATOM   782  C  CG2   . ILE A 1 108 ? 6.727   29.691 15.821 1.00 15.73  ? 125 ILE A CG2   1 
ATOM   783  C  CD1   . ILE A 1 108 ? 7.689   32.651 15.460 1.00 14.26  ? 125 ILE A CD1   1 
ATOM   784  N  N     . ARG A 1 109 ? 7.475   27.633 13.038 1.00 12.03  ? 126 ARG A N     1 
ATOM   785  C  CA    . ARG A 1 109 ? 6.732   26.406 12.760 1.00 12.02  ? 126 ARG A CA    1 
ATOM   786  C  C     . ARG A 1 109 ? 7.663   25.194 12.634 1.00 13.30  ? 126 ARG A C     1 
ATOM   787  O  O     . ARG A 1 109 ? 7.332   24.107 13.125 1.00 13.16  ? 126 ARG A O     1 
ATOM   788  C  CB    . ARG A 1 109 ? 5.853   26.618 11.540 1.00 12.70  ? 126 ARG A CB    1 
ATOM   789  C  CG    . ARG A 1 109 ? 4.709   27.589 11.890 1.00 12.14  ? 126 ARG A CG    1 
ATOM   790  C  CD    . ARG A 1 109 ? 3.975   28.048 10.666 1.00 13.07  ? 126 ARG A CD    1 
ATOM   791  N  NE    . ARG A 1 109 ? 2.800   28.858 10.965 1.00 15.47  ? 126 ARG A NE    1 
ATOM   792  C  CZ    . ARG A 1 109 ? 2.073   29.438 10.025 1.00 16.47  ? 126 ARG A CZ    1 
ATOM   793  N  NH1   . ARG A 1 109 ? 2.450   29.420 8.755  1.00 17.07  ? 126 ARG A NH1   1 
ATOM   794  N  NH2   . ARG A 1 109 ? 0.938   30.035 10.357 1.00 16.72  ? 126 ARG A NH2   1 
ATOM   795  N  N     . ALA A 1 110 ? 8.846   25.346 12.021 1.00 10.98  ? 127 ALA A N     1 
ATOM   796  C  CA    . ALA A 1 110 ? 9.772   24.216 11.944 1.00 14.61  ? 127 ALA A CA    1 
ATOM   797  C  C     . ALA A 1 110 ? 10.304  23.825 13.313 1.00 15.11  ? 127 ALA A C     1 
ATOM   798  O  O     . ALA A 1 110 ? 10.567  22.636 13.579 1.00 14.67  ? 127 ALA A O     1 
ATOM   799  C  CB    . ALA A 1 110 ? 10.945  24.566 11.032 1.00 13.52  ? 127 ALA A CB    1 
ATOM   800  N  N     . ASP A 1 111 ? 10.527  24.814 14.171 1.00 12.23  ? 128 ASP A N     1 
ATOM   801  C  CA    . ASP A 1 111 ? 11.192  24.530 15.440 1.00 11.48  ? 128 ASP A CA    1 
ATOM   802  C  C     . ASP A 1 111 ? 10.244  23.954 16.486 1.00 12.29  ? 128 ASP A C     1 
ATOM   803  O  O     . ASP A 1 111 ? 10.719  23.245 17.390 1.00 12.58  ? 128 ASP A O     1 
ATOM   804  C  CB    . ASP A 1 111 ? 11.836  25.797 16.006 1.00 13.20  ? 128 ASP A CB    1 
ATOM   805  C  CG    . ASP A 1 111 ? 13.088  26.250 15.247 1.00 18.17  ? 128 ASP A CG    1 
ATOM   806  O  OD1   . ASP A 1 111 ? 13.634  25.484 14.399 1.00 22.74  ? 128 ASP A OD1   1 
ATOM   807  O  OD2   . ASP A 1 111 ? 13.520  27.419 15.478 1.00 21.10  ? 128 ASP A OD2   1 
ATOM   808  N  N     . PHE A 1 112 ? 8.936   24.235 16.393 1.00 12.59  ? 129 PHE A N     1 
ATOM   809  C  CA    . PHE A 1 112 ? 7.960   23.854 17.409 1.00 12.68  ? 129 PHE A CA    1 
ATOM   810  C  C     . PHE A 1 112 ? 6.898   22.857 16.964 1.00 12.80  ? 129 PHE A C     1 
ATOM   811  O  O     . PHE A 1 112 ? 6.230   22.288 17.827 1.00 12.91  ? 129 PHE A O     1 
ATOM   812  C  CB    . PHE A 1 112 ? 7.179   25.077 17.912 1.00 12.15  ? 129 PHE A CB    1 
ATOM   813  C  CG    . PHE A 1 112 ? 7.965   26.058 18.763 1.00 12.09  ? 129 PHE A CG    1 
ATOM   814  C  CD1   . PHE A 1 112 ? 8.627   27.142 18.189 1.00 15.21  ? 129 PHE A CD1   1 
ATOM   815  C  CD2   . PHE A 1 112 ? 7.974   25.933 20.157 1.00 13.86  ? 129 PHE A CD2   1 
ATOM   816  C  CE1   . PHE A 1 112 ? 9.306   28.056 18.969 1.00 19.12  ? 129 PHE A CE1   1 
ATOM   817  C  CE2   . PHE A 1 112 ? 8.651   26.863 20.923 1.00 15.84  ? 129 PHE A CE2   1 
ATOM   818  C  CZ    . PHE A 1 112 ? 9.295   27.917 20.342 1.00 15.22  ? 129 PHE A CZ    1 
ATOM   819  N  N     . CYS A 1 113 ? 6.667   22.656 15.664 1.00 12.44  ? 130 CYS A N     1 
ATOM   820  C  CA    . CYS A 1 113 ? 5.406   22.047 15.235 1.00 11.46  ? 130 CYS A CA    1 
ATOM   821  C  C     . CYS A 1 113 ? 5.620   20.896 14.255 1.00 13.18  ? 130 CYS A C     1 
ATOM   822  O  O     . CYS A 1 113 ? 6.711   20.683 13.729 1.00 13.92  ? 130 CYS A O     1 
ATOM   823  C  CB    . CYS A 1 113 ? 4.481   23.095 14.609 1.00 11.01  ? 130 CYS A CB    1 
ATOM   824  S  SG    . CYS A 1 113 ? 4.062   24.398 15.779 1.00 14.46  ? 130 CYS A SG    1 
ATOM   825  N  N     . GLN A 1 114 ? 4.533   20.148 14.035 1.00 11.49  ? 131 GLN A N     1 
ATOM   826  C  CA    . GLN A 1 114 ? 4.532   18.979 13.152 1.00 12.65  ? 131 GLN A CA    1 
ATOM   827  C  C     . GLN A 1 114 ? 3.562   19.092 11.991 1.00 13.92  ? 131 GLN A C     1 
ATOM   828  O  O     . GLN A 1 114 ? 3.898   18.658 10.883 1.00 16.62  ? 131 GLN A O     1 
ATOM   829  C  CB    . GLN A 1 114 ? 4.193   17.716 13.954 1.00 14.44  ? 131 GLN A CB    1 
ATOM   830  C  CG    . GLN A 1 114 ? 5.287   17.337 14.966 1.00 13.86  ? 131 GLN A CG    1 
ATOM   831  C  CD    . GLN A 1 114 ? 5.010   16.006 15.638 1.00 17.24  ? 131 GLN A CD    1 
ATOM   832  O  OE1   . GLN A 1 114 ? 4.682   15.020 14.975 1.00 16.39  ? 131 GLN A OE1   1 
ATOM   833  N  NE2   . GLN A 1 114 ? 5.173   15.961 16.946 1.00 14.55  ? 131 GLN A NE2   1 
ATOM   834  N  N     . GLN A 1 115 ? 2.356   19.620 12.218 1.00 13.49  ? 132 GLN A N     1 
ATOM   835  C  CA    . GLN A 1 115 ? 1.287   19.594 11.228 1.00 15.70  ? 132 GLN A CA    1 
ATOM   836  C  C     . GLN A 1 115 ? 0.646   20.963 11.057 1.00 15.01  ? 132 GLN A C     1 
ATOM   837  O  O     . GLN A 1 115 ? 0.573   21.765 11.985 1.00 14.71  ? 132 GLN A O     1 
ATOM   838  C  CB    . GLN A 1 115 ? 0.221   18.586 11.605 1.00 16.44  ? 132 GLN A CB    1 
ATOM   839  C  CG    . GLN A 1 115 ? 0.757   17.172 11.701 1.00 17.86  ? 132 GLN A CG    1 
ATOM   840  C  CD    . GLN A 1 115 ? -0.351  16.160 11.824 1.00 24.04  ? 132 GLN A CD    1 
ATOM   841  O  OE1   . GLN A 1 115 ? -0.924  15.963 12.894 1.00 22.74  ? 132 GLN A OE1   1 
ATOM   842  N  NE2   . GLN A 1 115 ? -0.674  15.526 10.720 1.00 24.35  ? 132 GLN A NE2   1 
ATOM   843  N  N     . ALA A 1 116 ? 0.130   21.201 9.855  1.00 16.02  ? 133 ALA A N     1 
ATOM   844  C  CA    . ALA A 1 116 ? -0.415  22.516 9.535  1.00 16.33  ? 133 ALA A CA    1 
ATOM   845  C  C     . ALA A 1 116 ? -1.566  22.895 10.446 1.00 17.02  ? 133 ALA A C     1 
ATOM   846  O  O     . ALA A 1 116 ? -1.757  24.085 10.765 1.00 18.37  ? 133 ALA A O     1 
ATOM   847  C  CB    . ALA A 1 116 ? -0.898  22.534 8.082  1.00 18.54  ? 133 ALA A CB    1 
ATOM   848  N  N     . GLY A 1 117 ? -2.378  21.916 10.841 1.00 16.60  ? 134 GLY A N     1 
ATOM   849  C  CA    . GLY A 1 117 ? -3.513  22.232 11.675 1.00 19.39  ? 134 GLY A CA    1 
ATOM   850  C  C     . GLY A 1 117 ? -3.162  22.646 13.092 1.00 18.74  ? 134 GLY A C     1 
ATOM   851  O  O     . GLY A 1 117 ? -4.043  23.110 13.821 1.00 19.13  ? 134 GLY A O     1 
ATOM   852  N  N     . ARG A 1 118 ? -1.926  22.448 13.511 1.00 14.18  ? 135 ARG A N     1 
ATOM   853  C  CA    . ARG A 1 118 ? -1.441  22.915 14.811 1.00 15.61  ? 135 ARG A CA    1 
ATOM   854  C  C     . ARG A 1 118 ? -0.077  23.565 14.567 1.00 13.95  ? 135 ARG A C     1 
ATOM   855  O  O     . ARG A 1 118 ? 0.966   22.999 14.928 1.00 13.98  ? 135 ARG A O     1 
ATOM   856  C  CB    . ARG A 1 118 ? -1.342  21.758 15.788 1.00 13.86  ? 135 ARG A CB    1 
ATOM   857  C  CG    . ARG A 1 118 ? -2.693  21.201 16.250 1.00 14.86  ? 135 ARG A CG    1 
ATOM   858  C  CD    . ARG A 1 118 ? -3.468  22.278 17.017 1.00 17.14  ? 135 ARG A CD    1 
ATOM   859  N  NE    . ARG A 1 118 ? -4.571  21.761 17.822 1.00 22.12  ? 135 ARG A NE    1 
ATOM   860  C  CZ    . ARG A 1 118 ? -5.483  22.537 18.393 1.00 23.05  ? 135 ARG A CZ    1 
ATOM   861  N  NH1   . ARG A 1 118 ? -5.430  23.855 18.291 1.00 23.23  ? 135 ARG A NH1   1 
ATOM   862  N  NH2   . ARG A 1 118 ? -6.484  21.977 19.068 1.00 25.48  ? 135 ARG A NH2   1 
ATOM   863  N  N     . ASN A 1 119 ? -0.084  24.791 14.029 1.00 13.21  ? 136 ASN A N     1 
ATOM   864  C  CA    . ASN A 1 119 ? 1.137   25.461 13.613 1.00 11.48  ? 136 ASN A CA    1 
ATOM   865  C  C     . ASN A 1 119 ? 1.336   26.783 14.355 1.00 13.66  ? 136 ASN A C     1 
ATOM   866  O  O     . ASN A 1 119 ? 2.018   27.674 13.878 1.00 12.06  ? 136 ASN A O     1 
ATOM   867  C  CB    . ASN A 1 119 ? 1.165   25.606 12.083 1.00 12.68  ? 136 ASN A CB    1 
ATOM   868  C  CG    . ASN A 1 119 ? 0.117   26.544 11.569 1.00 15.24  ? 136 ASN A CG    1 
ATOM   869  O  OD1   . ASN A 1 119 ? -0.687  27.083 12.332 1.00 14.12  ? 136 ASN A OD1   1 
ATOM   870  N  ND2   . ASN A 1 119 ? 0.124   26.764 10.256 1.00 15.45  ? 136 ASN A ND2   1 
ATOM   871  N  N     . LEU A 1 120 ? 0.777   26.871 15.573 1.00 14.66  ? 137 LEU A N     1 
ATOM   872  C  CA    . LEU A 1 120 ? 1.179   27.733 16.683 1.00 11.33  ? 137 LEU A CA    1 
ATOM   873  C  C     . LEU A 1 120 ? 0.853   29.226 16.587 1.00 12.22  ? 137 LEU A C     1 
ATOM   874  O  O     . LEU A 1 120 ? 0.523   29.842 17.612 1.00 12.50  ? 137 LEU A O     1 
ATOM   875  C  CB    . LEU A 1 120 ? 2.712   27.649 16.858 1.00 13.52  ? 137 LEU A CB    1 
ATOM   876  C  CG    . LEU A 1 120 ? 3.228   27.663 18.294 1.00 13.43  ? 137 LEU A CG    1 
ATOM   877  C  CD1   . LEU A 1 120 ? 2.873   26.340 18.956 1.00 16.03  ? 137 LEU A CD1   1 
ATOM   878  C  CD2   . LEU A 1 120 ? 4.743   27.947 18.331 1.00 14.40  ? 137 LEU A CD2   1 
ATOM   879  N  N     . ILE A 1 121 ? 0.785   29.783 15.388 1.00 13.47  ? 138 ILE A N     1 
ATOM   880  C  CA    . ILE A 1 121 ? 0.834   31.235 15.227 1.00 12.47  ? 138 ILE A CA    1 
ATOM   881  C  C     . ILE A 1 121 ? 0.243   31.602 13.871 1.00 14.47  ? 138 ILE A C     1 
ATOM   882  O  O     . ILE A 1 121 ? 0.395   30.877 12.876 1.00 14.63  ? 138 ILE A O     1 
ATOM   883  C  CB    . ILE A 1 121 ? 2.281   31.772 15.395 1.00 13.63  ? 138 ILE A CB    1 
ATOM   884  C  CG1   . ILE A 1 121 ? 2.288   33.307 15.421 1.00 14.72  ? 138 ILE A CG1   1 
ATOM   885  C  CG2   . ILE A 1 121 ? 3.212   31.183 14.335 1.00 14.12  ? 138 ILE A CG2   1 
ATOM   886  C  CD1   . ILE A 1 121 ? 3.589   33.906 15.910 1.00 14.94  ? 138 ILE A CD1   1 
ATOM   887  N  N     . HIS A 1 122 ? -0.496  32.711 13.868 1.00 13.53  ? 139 HIS A N     1 
ATOM   888  C  CA    . HIS A 1 122 ? -0.996  33.388 12.683 1.00 14.14  ? 139 HIS A CA    1 
ATOM   889  C  C     . HIS A 1 122 ? -0.270  34.717 12.506 1.00 13.35  ? 139 HIS A C     1 
ATOM   890  O  O     . HIS A 1 122 ? -0.034  35.435 13.482 1.00 14.59  ? 139 HIS A O     1 
ATOM   891  C  CB    . HIS A 1 122 ? -2.493  33.688 12.805 1.00 14.80  ? 139 HIS A CB    1 
ATOM   892  C  CG    . HIS A 1 122 ? -2.964  34.726 11.843 1.00 14.73  ? 139 HIS A CG    1 
ATOM   893  N  ND1   . HIS A 1 122 ? -3.383  34.417 10.572 1.00 16.99  ? 139 HIS A ND1   1 
ATOM   894  C  CD2   . HIS A 1 122 ? -3.009  36.076 11.937 1.00 15.22  ? 139 HIS A CD2   1 
ATOM   895  C  CE1   . HIS A 1 122 ? -3.712  35.527 9.936  1.00 17.49  ? 139 HIS A CE1   1 
ATOM   896  N  NE2   . HIS A 1 122 ? -3.479  36.549 10.734 1.00 18.42  ? 139 HIS A NE2   1 
ATOM   897  N  N     . GLY A 1 123 ? 0.012   35.085 11.258 1.00 15.17  ? 140 GLY A N     1 
ATOM   898  C  CA    . GLY A 1 123 ? 0.466   36.436 10.953 1.00 12.86  ? 140 GLY A CA    1 
ATOM   899  C  C     . GLY A 1 123 ? -0.162  36.965 9.677  1.00 14.20  ? 140 GLY A C     1 
ATOM   900  O  O     . GLY A 1 123 ? -0.380  36.221 8.721  1.00 14.81  ? 140 GLY A O     1 
ATOM   901  N  N     . SER A 1 124 ? -0.380  38.287 9.651  1.00 13.99  ? 141 SER A N     1 
ATOM   902  C  CA    . SER A 1 124 ? -0.934  38.944 8.463  1.00 14.41  ? 141 SER A CA    1 
ATOM   903  C  C     . SER A 1 124 ? -0.069  38.670 7.240  1.00 15.11  ? 141 SER A C     1 
ATOM   904  O  O     . SER A 1 124 ? 1.153   38.695 7.311  1.00 15.93  ? 141 SER A O     1 
ATOM   905  C  CB    . SER A 1 124 ? -1.013  40.449 8.662  1.00 16.32  ? 141 SER A CB    1 
ATOM   906  O  OG    . SER A 1 124 ? -1.748  40.760 9.810  1.00 16.95  ? 141 SER A OG    1 
ATOM   907  N  N     . ASP A 1 125 ? -0.706  38.454 6.090  1.00 15.87  ? 142 ASP A N     1 
ATOM   908  C  CA    . ASP A 1 125 ? 0.039   38.119 4.882  1.00 18.07  ? 142 ASP A CA    1 
ATOM   909  C  C     . ASP A 1 125 ? 0.253   39.301 3.945  1.00 20.50  ? 142 ASP A C     1 
ATOM   910  O  O     . ASP A 1 125 ? 0.929   39.131 2.924  1.00 21.51  ? 142 ASP A O     1 
ATOM   911  C  CB    . ASP A 1 125 ? -0.646  36.962 4.137  1.00 19.16  ? 142 ASP A CB    1 
ATOM   912  C  CG    . ASP A 1 125 ? -1.947  37.348 3.472  1.00 24.82  ? 142 ASP A CG    1 
ATOM   913  O  OD1   . ASP A 1 125 ? -2.367  38.522 3.533  1.00 26.34  ? 142 ASP A OD1   1 
ATOM   914  O  OD2   . ASP A 1 125 ? -2.563  36.439 2.854  1.00 31.47  ? 142 ASP A OD2   1 
ATOM   915  N  N     . SER A 1 126 ? -0.279  40.479 4.261  1.00 17.63  ? 143 SER A N     1 
ATOM   916  C  CA    . SER A 1 126 ? -0.165  41.640 3.381  1.00 18.54  ? 143 SER A CA    1 
ATOM   917  C  C     . SER A 1 126 ? -0.494  42.901 4.160  1.00 16.39  ? 143 SER A C     1 
ATOM   918  O  O     . SER A 1 126 ? -1.060  42.853 5.258  1.00 17.61  ? 143 SER A O     1 
ATOM   919  C  CB    . SER A 1 126 ? -1.107  41.529 2.184  1.00 20.59  ? 143 SER A CB    1 
ATOM   920  O  OG    . SER A 1 126 ? -2.453  41.729 2.619  1.00 22.81  ? 143 SER A OG    1 
ATOM   921  N  N     . ALA A 1 127 ? -0.195  44.050 3.539  1.00 21.93  ? 144 ALA A N     1 
ATOM   922  C  CA    . ALA A 1 127 ? -0.540  45.318 4.169  1.00 22.14  ? 144 ALA A CA    1 
ATOM   923  C  C     . ALA A 1 127 ? -2.044  45.432 4.380  1.00 19.64  ? 144 ALA A C     1 
ATOM   924  O  O     . ALA A 1 127 ? -2.500  45.887 5.438  1.00 21.96  ? 144 ALA A O     1 
ATOM   925  C  CB    . ALA A 1 127 ? -0.026  46.484 3.331  1.00 26.13  ? 144 ALA A CB    1 
ATOM   926  N  N     . GLU A 1 128 ? -2.836  45.022 3.380  1.00 21.23  ? 145 GLU A N     1 
ATOM   927  C  CA    . GLU A 1 128 ? -4.287  45.120 3.498  1.00 21.39  ? 145 GLU A CA    1 
ATOM   928  C  C     . GLU A 1 128 ? -4.831  44.207 4.588  1.00 20.62  ? 145 GLU A C     1 
ATOM   929  O  O     . GLU A 1 128 ? -5.732  44.607 5.348  1.00 22.54  ? 145 GLU A O     1 
ATOM   930  C  CB    . GLU A 1 128 ? -4.933  44.798 2.148  1.00 31.15  ? 145 GLU A CB    1 
ATOM   931  C  CG    . GLU A 1 128 ? -4.573  45.821 1.062  1.00 49.62  ? 145 GLU A CG    1 
ATOM   932  C  CD    . GLU A 1 128 ? -3.175  45.626 0.439  1.00 53.70  ? 145 GLU A CD    1 
ATOM   933  O  OE1   . GLU A 1 128 ? -2.494  44.599 0.708  1.00 34.04  ? 145 GLU A OE1   1 
ATOM   934  O  OE2   . GLU A 1 128 ? -2.760  46.518 -0.338 1.00 58.43  ? 145 GLU A OE2   1 
ATOM   935  N  N     . SER A 1 129 ? -4.326  42.971 4.662  1.00 20.24  ? 146 SER A N     1 
ATOM   936  C  CA    A SER A 1 129 ? -4.831  42.068 5.680  0.68 18.61  ? 146 SER A CA    1 
ATOM   937  C  CA    B SER A 1 129 ? -4.792  42.039 5.681  0.32 18.57  ? 146 SER A CA    1 
ATOM   938  C  C     . SER A 1 129 ? -4.372  42.500 7.064  1.00 19.93  ? 146 SER A C     1 
ATOM   939  O  O     . SER A 1 129 ? -5.122  42.348 8.028  1.00 19.92  ? 146 SER A O     1 
ATOM   940  C  CB    A SER A 1 129 ? -4.420  40.628 5.392  0.68 20.21  ? 146 SER A CB    1 
ATOM   941  C  CB    B SER A 1 129 ? -4.259  40.638 5.405  0.32 20.19  ? 146 SER A CB    1 
ATOM   942  O  OG    A SER A 1 129 ? -3.021  40.478 5.394  0.68 20.41  ? 146 SER A OG    1 
ATOM   943  O  OG    B SER A 1 129 ? -4.853  40.110 4.241  0.32 20.17  ? 146 SER A OG    1 
ATOM   944  N  N     . ALA A 1 130 ? -3.182  43.076 7.171  1.00 17.34  ? 147 ALA A N     1 
ATOM   945  C  CA    . ALA A 1 130 ? -2.746  43.575 8.473  1.00 18.05  ? 147 ALA A CA    1 
ATOM   946  C  C     . ALA A 1 130 ? -3.663  44.688 8.969  1.00 20.69  ? 147 ALA A C     1 
ATOM   947  O  O     . ALA A 1 130 ? -4.080  44.693 10.134 1.00 20.23  ? 147 ALA A O     1 
ATOM   948  C  CB    . ALA A 1 130 ? -1.298  44.060 8.397  1.00 17.51  ? 147 ALA A CB    1 
ATOM   949  N  N     . LYS A 1 131 ? -4.018  45.627 8.093  1.00 19.21  ? 148 LYS A N     1 
ATOM   950  C  CA    . LYS A 1 131 ? -4.915  46.698 8.508  1.00 21.06  ? 148 LYS A CA    1 
ATOM   951  C  C     . LYS A 1 131 ? -6.245  46.121 8.965  1.00 19.45  ? 148 LYS A C     1 
ATOM   952  O  O     . LYS A 1 131 ? -6.773  46.485 10.028 1.00 23.54  ? 148 LYS A O     1 
ATOM   953  C  CB    . LYS A 1 131 ? -5.100  47.671 7.349  1.00 21.99  ? 148 LYS A CB    1 
ATOM   954  C  CG    . LYS A 1 131 ? -5.852  48.937 7.734  1.00 42.42  ? 148 LYS A CG    1 
ATOM   955  C  CD    . LYS A 1 131 ? -5.908  49.925 6.567  1.00 53.49  ? 148 LYS A CD    1 
ATOM   956  C  CE    . LYS A 1 131 ? -6.727  51.162 6.911  1.00 68.11  ? 148 LYS A CE    1 
ATOM   957  N  NZ    . LYS A 1 131 ? -8.140  50.819 7.227  1.00 75.12  ? 148 LYS A NZ    1 
ATOM   958  N  N     . ARG A 1 132 ? -6.792  45.187 8.182  1.00 19.16  ? 149 ARG A N     1 
ATOM   959  C  CA    . ARG A 1 132 ? -8.105  44.634 8.501  1.00 22.17  ? 149 ARG A CA    1 
ATOM   960  C  C     . ARG A 1 132 ? -8.075  43.831 9.795  1.00 22.50  ? 149 ARG A C     1 
ATOM   961  O  O     . ARG A 1 132 ? -8.995  43.921 10.621 1.00 20.14  ? 149 ARG A O     1 
ATOM   962  C  CB    . ARG A 1 132 ? -8.567  43.751 7.355  1.00 23.77  ? 149 ARG A CB    1 
ATOM   963  C  CG    . ARG A 1 132 ? -9.934  43.212 7.550  1.00 24.73  ? 149 ARG A CG    1 
ATOM   964  C  CD    . ARG A 1 132 ? -10.360 42.434 6.326  1.00 31.73  ? 149 ARG A CD    1 
ATOM   965  N  NE    . ARG A 1 132 ? -9.912  41.068 6.488  1.00 38.40  ? 149 ARG A NE    1 
ATOM   966  C  CZ    . ARG A 1 132 ? -10.591 40.150 7.155  1.00 38.58  ? 149 ARG A CZ    1 
ATOM   967  N  NH1   . ARG A 1 132 ? -11.830 40.372 7.568  1.00 38.56  ? 149 ARG A NH1   1 
ATOM   968  N  NH2   . ARG A 1 132 ? -10.015 38.984 7.412  1.00 31.27  ? 149 ARG A NH2   1 
ATOM   969  N  N     . GLU A 1 133 ? -7.037  43.014 9.975  1.00 18.01  ? 150 GLU A N     1 
ATOM   970  C  CA    . GLU A 1 133 ? -6.973  42.150 11.144 1.00 16.62  ? 150 GLU A CA    1 
ATOM   971  C  C     . GLU A 1 133 ? -6.731  42.963 12.404 1.00 19.40  ? 150 GLU A C     1 
ATOM   972  O  O     . GLU A 1 133 ? -7.319  42.679 13.454 1.00 17.78  ? 150 GLU A O     1 
ATOM   973  C  CB    . GLU A 1 133 ? -5.874  41.102 10.937 1.00 17.81  ? 150 GLU A CB    1 
ATOM   974  C  CG    . GLU A 1 133 ? -6.244  40.083 9.868  1.00 19.33  ? 150 GLU A CG    1 
ATOM   975  C  CD    . GLU A 1 133 ? -5.106  39.156 9.445  1.00 18.36  ? 150 GLU A CD    1 
ATOM   976  O  OE1   . GLU A 1 133 ? -4.013  39.202 10.064 1.00 19.61  ? 150 GLU A OE1   1 
ATOM   977  O  OE2   . GLU A 1 133 ? -5.345  38.354 8.494  1.00 20.97  ? 150 GLU A OE2   1 
ATOM   978  N  N     . ILE A 1 134 ? -5.856  43.967 12.331 1.00 20.22  ? 151 ILE A N     1 
ATOM   979  C  CA    . ILE A 1 134 ? -5.640  44.815 13.503 1.00 22.64  ? 151 ILE A CA    1 
ATOM   980  C  C     . ILE A 1 134 ? -6.950  45.478 13.926 1.00 23.11  ? 151 ILE A C     1 
ATOM   981  O  O     . ILE A 1 134 ? -7.279  45.543 15.119 1.00 23.29  ? 151 ILE A O     1 
ATOM   982  C  CB    . ILE A 1 134 ? -4.534  45.847 13.225 1.00 17.28  ? 151 ILE A CB    1 
ATOM   983  C  CG1   . ILE A 1 134 ? -3.170  45.143 13.071 1.00 18.49  ? 151 ILE A CG1   1 
ATOM   984  C  CG2   . ILE A 1 134 ? -4.445  46.867 14.374 1.00 20.26  ? 151 ILE A CG2   1 
ATOM   985  C  CD1   . ILE A 1 134 ? -2.031  46.047 12.639 1.00 21.41  ? 151 ILE A CD1   1 
ATOM   986  N  N     . SER A 1 135 ? -7.731  45.952 12.959 1.00 20.10  ? 152 SER A N     1 
ATOM   987  C  CA    . SER A 1 135 ? -9.004  46.594 13.282 1.00 22.35  ? 152 SER A CA    1 
ATOM   988  C  C     . SER A 1 135 ? -10.035 45.601 13.811 1.00 23.73  ? 152 SER A C     1 
ATOM   989  O  O     . SER A 1 135 ? -10.907 45.982 14.596 1.00 25.73  ? 152 SER A O     1 
ATOM   990  C  CB    . SER A 1 135 ? -9.540  47.326 12.049 1.00 26.63  ? 152 SER A CB    1 
ATOM   991  O  OG    . SER A 1 135 ? -8.673  48.407 11.724 1.00 33.60  ? 152 SER A OG    1 
ATOM   992  N  N     . LEU A 1 136 ? -9.969  44.336 13.383 1.00 20.18  ? 153 LEU A N     1 
ATOM   993  C  CA    . LEU A 1 136 ? -10.926 43.338 13.845 1.00 16.28  ? 153 LEU A CA    1 
ATOM   994  C  C     . LEU A 1 136 ? -10.738 43.014 15.319 1.00 19.72  ? 153 LEU A C     1 
ATOM   995  O  O     . LEU A 1 136 ? -11.718 42.901 16.069 1.00 20.69  ? 153 LEU A O     1 
ATOM   996  C  CB    . LEU A 1 136 ? -10.796 42.077 12.993 1.00 20.22  ? 153 LEU A CB    1 
ATOM   997  C  CG    . LEU A 1 136 ? -11.612 40.848 13.405 1.00 20.88  ? 153 LEU A CG    1 
ATOM   998  C  CD1   . LEU A 1 136 ? -13.120 41.163 13.354 1.00 25.22  ? 153 LEU A CD1   1 
ATOM   999  C  CD2   . LEU A 1 136 ? -11.308 39.658 12.504 1.00 21.72  ? 153 LEU A CD2   1 
ATOM   1000 N  N     . TRP A 1 137 ? -9.489  42.841 15.747 1.00 18.80  ? 154 TRP A N     1 
ATOM   1001 C  CA    . TRP A 1 137 ? -9.177  42.325 17.067 1.00 16.57  ? 154 TRP A CA    1 
ATOM   1002 C  C     . TRP A 1 137 ? -8.858  43.408 18.092 1.00 17.01  ? 154 TRP A C     1 
ATOM   1003 O  O     . TRP A 1 137 ? -8.885  43.117 19.294 1.00 21.46  ? 154 TRP A O     1 
ATOM   1004 C  CB    . TRP A 1 137 ? -7.983  41.374 16.979 1.00 17.86  ? 154 TRP A CB    1 
ATOM   1005 C  CG    . TRP A 1 137 ? -8.225  40.117 16.219 1.00 17.72  ? 154 TRP A CG    1 
ATOM   1006 C  CD1   . TRP A 1 137 ? -7.975  39.900 14.908 1.00 19.15  ? 154 TRP A CD1   1 
ATOM   1007 C  CD2   . TRP A 1 137 ? -8.766  38.893 16.734 1.00 16.42  ? 154 TRP A CD2   1 
ATOM   1008 N  NE1   . TRP A 1 137 ? -8.291  38.609 14.569 1.00 17.68  ? 154 TRP A NE1   1 
ATOM   1009 C  CE2   . TRP A 1 137 ? -8.806  37.977 15.665 1.00 16.80  ? 154 TRP A CE2   1 
ATOM   1010 C  CE3   . TRP A 1 137 ? -9.241  38.493 17.984 1.00 16.34  ? 154 TRP A CE3   1 
ATOM   1011 C  CZ2   . TRP A 1 137 ? -9.250  36.671 15.814 1.00 20.31  ? 154 TRP A CZ2   1 
ATOM   1012 C  CZ3   . TRP A 1 137 ? -9.679  37.192 18.140 1.00 18.77  ? 154 TRP A CZ3   1 
ATOM   1013 C  CH2   . TRP A 1 137 ? -9.698  36.298 17.051 1.00 19.94  ? 154 TRP A CH2   1 
ATOM   1014 N  N     . PHE A 1 138 ? -8.545  44.628 17.652 1.00 18.47  ? 155 PHE A N     1 
ATOM   1015 C  CA    . PHE A 1 138 ? -8.159  45.722 18.538 1.00 21.32  ? 155 PHE A CA    1 
ATOM   1016 C  C     . PHE A 1 138 ? -8.975  46.966 18.241 1.00 22.82  ? 155 PHE A C     1 
ATOM   1017 O  O     . PHE A 1 138 ? -9.184  47.318 17.079 1.00 24.51  ? 155 PHE A O     1 
ATOM   1018 C  CB    . PHE A 1 138 ? -6.665  46.069 18.390 1.00 18.49  ? 155 PHE A CB    1 
ATOM   1019 C  CG    . PHE A 1 138 ? -5.741  45.051 18.979 1.00 16.03  ? 155 PHE A CG    1 
ATOM   1020 C  CD1   . PHE A 1 138 ? -5.533  45.005 20.345 1.00 16.50  ? 155 PHE A CD1   1 
ATOM   1021 C  CD2   . PHE A 1 138 ? -5.049  44.155 18.181 1.00 17.72  ? 155 PHE A CD2   1 
ATOM   1022 C  CE1   . PHE A 1 138 ? -4.669  44.076 20.912 1.00 17.97  ? 155 PHE A CE1   1 
ATOM   1023 C  CE2   . PHE A 1 138 ? -4.186  43.227 18.746 1.00 16.55  ? 155 PHE A CE2   1 
ATOM   1024 C  CZ    . PHE A 1 138 ? -3.997  43.187 20.115 1.00 17.92  ? 155 PHE A CZ    1 
ATOM   1025 N  N     . LYS A 1 139 ? -9.394  47.643 19.288 1.00 20.71  ? 156 LYS A N     1 
ATOM   1026 C  CA    . LYS A 1 139 ? -9.870  49.000 19.133 1.00 27.18  ? 156 LYS A CA    1 
ATOM   1027 C  C     . LYS A 1 139 ? -8.673  49.940 19.013 1.00 21.39  ? 156 LYS A C     1 
ATOM   1028 O  O     . LYS A 1 139 ? -7.586  49.637 19.512 1.00 20.75  ? 156 LYS A O     1 
ATOM   1029 C  CB    . LYS A 1 139 ? -10.711 49.414 20.332 1.00 30.01  ? 156 LYS A CB    1 
ATOM   1030 C  CG    . LYS A 1 139 ? -11.829 48.448 20.713 1.00 37.80  ? 156 LYS A CG    1 
ATOM   1031 C  CD    . LYS A 1 139 ? -12.129 48.572 22.212 1.00 50.25  ? 156 LYS A CD    1 
ATOM   1032 C  CE    . LYS A 1 139 ? -13.558 48.192 22.561 1.00 54.89  ? 156 LYS A CE    1 
ATOM   1033 N  NZ    . LYS A 1 139 ? -13.878 46.775 22.219 1.00 68.55  ? 156 LYS A NZ    1 
ATOM   1034 N  N     . PRO A 1 140 ? -8.853  51.090 18.378 1.00 21.67  ? 157 PRO A N     1 
ATOM   1035 C  CA    . PRO A 1 140 ? -7.725  52.011 18.212 1.00 22.36  ? 157 PRO A CA    1 
ATOM   1036 C  C     . PRO A 1 140 ? -7.092  52.439 19.522 1.00 23.73  ? 157 PRO A C     1 
ATOM   1037 O  O     . PRO A 1 140 ? -5.867  52.611 19.573 1.00 23.01  ? 157 PRO A O     1 
ATOM   1038 C  CB    . PRO A 1 140 ? -8.362  53.197 17.473 1.00 33.44  ? 157 PRO A CB    1 
ATOM   1039 C  CG    . PRO A 1 140 ? -9.479  52.607 16.742 1.00 26.82  ? 157 PRO A CG    1 
ATOM   1040 C  CD    . PRO A 1 140 ? -10.029 51.517 17.590 1.00 26.32  ? 157 PRO A CD    1 
ATOM   1041 N  N     . GLU A 1 141 ? -7.887  52.591 20.587 1.00 22.88  ? 158 GLU A N     1 
ATOM   1042 C  CA    . GLU A 1 141 ? -7.356  52.972 21.894 1.00 25.64  ? 158 GLU A CA    1 
ATOM   1043 C  C     . GLU A 1 141 ? -6.469  51.904 22.515 1.00 24.71  ? 158 GLU A C     1 
ATOM   1044 O  O     . GLU A 1 141 ? -5.772  52.200 23.490 1.00 23.84  ? 158 GLU A O     1 
ATOM   1045 C  CB    . GLU A 1 141 ? -8.507  53.288 22.854 1.00 30.96  ? 158 GLU A CB    1 
ATOM   1046 C  CG    . GLU A 1 141 ? -9.593  52.225 22.901 1.00 42.05  ? 158 GLU A CG    1 
ATOM   1047 C  CD    . GLU A 1 141 ? -10.847 52.596 22.087 1.00 55.49  ? 158 GLU A CD    1 
ATOM   1048 O  OE1   . GLU A 1 141 ? -10.746 52.951 20.873 1.00 37.09  ? 158 GLU A OE1   1 
ATOM   1049 O  OE2   . GLU A 1 141 ? -11.944 52.523 22.683 1.00 58.87  ? 158 GLU A OE2   1 
ATOM   1050 N  N     . GLU A 1 142 ? -6.478  50.682 21.989 1.00 20.66  ? 159 GLU A N     1 
ATOM   1051 C  CA    A GLU A 1 142 ? -5.627  49.625 22.514 0.47 19.53  ? 159 GLU A CA    1 
ATOM   1052 C  CA    B GLU A 1 142 ? -5.639  49.596 22.480 0.53 19.50  ? 159 GLU A CA    1 
ATOM   1053 C  C     . GLU A 1 142 ? -4.251  49.588 21.854 1.00 17.68  ? 159 GLU A C     1 
ATOM   1054 O  O     . GLU A 1 142 ? -3.371  48.849 22.326 1.00 19.28  ? 159 GLU A O     1 
ATOM   1055 C  CB    A GLU A 1 142 ? -6.344  48.276 22.367 0.47 19.53  ? 159 GLU A CB    1 
ATOM   1056 C  CB    B GLU A 1 142 ? -6.312  48.247 22.209 0.53 19.29  ? 159 GLU A CB    1 
ATOM   1057 C  CG    A GLU A 1 142 ? -7.550  48.183 23.312 0.47 21.23  ? 159 GLU A CG    1 
ATOM   1058 C  CG    B GLU A 1 142 ? -7.653  48.074 22.899 0.53 22.11  ? 159 GLU A CG    1 
ATOM   1059 C  CD    A GLU A 1 142 ? -8.426  46.956 23.098 0.47 25.37  ? 159 GLU A CD    1 
ATOM   1060 C  CD    B GLU A 1 142 ? -8.276  46.724 22.604 0.53 22.43  ? 159 GLU A CD    1 
ATOM   1061 O  OE1   A GLU A 1 142 ? -8.406  46.372 21.998 0.47 26.69  ? 159 GLU A OE1   1 
ATOM   1062 O  OE1   B GLU A 1 142 ? -7.792  45.726 23.177 0.53 22.60  ? 159 GLU A OE1   1 
ATOM   1063 O  OE2   A GLU A 1 142 ? -9.160  46.589 24.041 0.47 31.13  ? 159 GLU A OE2   1 
ATOM   1064 O  OE2   B GLU A 1 142 ? -9.229  46.657 21.786 0.53 23.08  ? 159 GLU A OE2   1 
ATOM   1065 N  N     . ILE A 1 143 ? -4.032  50.379 20.814 1.00 15.65  ? 160 ILE A N     1 
ATOM   1066 C  CA    . ILE A 1 143 ? -2.766  50.412 20.097 1.00 18.26  ? 160 ILE A CA    1 
ATOM   1067 C  C     . ILE A 1 143 ? -1.921  51.514 20.729 1.00 17.34  ? 160 ILE A C     1 
ATOM   1068 O  O     . ILE A 1 143 ? -2.329  52.683 20.789 1.00 21.25  ? 160 ILE A O     1 
ATOM   1069 C  CB    . ILE A 1 143 ? -2.986  50.659 18.592 1.00 21.10  ? 160 ILE A CB    1 
ATOM   1070 C  CG1   . ILE A 1 143 ? -4.000  49.671 17.979 1.00 19.99  ? 160 ILE A CG1   1 
ATOM   1071 C  CG2   . ILE A 1 143 ? -1.645  50.649 17.851 1.00 21.86  ? 160 ILE A CG2   1 
ATOM   1072 C  CD1   . ILE A 1 143 ? -3.604  48.258 18.012 1.00 24.36  ? 160 ILE A CD1   1 
ATOM   1073 N  N     . GLN A 1 144 ? -0.746  51.142 21.207 1.00 17.09  ? 161 GLN A N     1 
ATOM   1074 C  CA    . GLN A 1 144 ? 0.082   52.013 22.015 1.00 19.34  ? 161 GLN A CA    1 
ATOM   1075 C  C     . GLN A 1 144 ? 1.263   52.522 21.210 1.00 17.03  ? 161 GLN A C     1 
ATOM   1076 O  O     . GLN A 1 144 ? 1.981   51.734 20.578 1.00 20.52  ? 161 GLN A O     1 
ATOM   1077 C  CB    . GLN A 1 144 ? 0.592   51.269 23.250 1.00 17.27  ? 161 GLN A CB    1 
ATOM   1078 C  CG    . GLN A 1 144 ? -0.481  50.497 23.984 1.00 18.79  ? 161 GLN A CG    1 
ATOM   1079 C  CD    . GLN A 1 144 ? -1.532  51.408 24.537 1.00 19.28  ? 161 GLN A CD    1 
ATOM   1080 O  OE1   . GLN A 1 144 ? -1.237  52.519 24.951 1.00 21.28  ? 161 GLN A OE1   1 
ATOM   1081 N  NE2   . GLN A 1 144 ? -2.759  50.954 24.531 1.00 19.38  ? 161 GLN A NE2   1 
ATOM   1082 N  N     . SER A 1 145 ? 1.480   53.835 21.265 1.00 18.58  ? 162 SER A N     1 
ATOM   1083 C  CA    A SER A 1 145 ? 2.583   54.475 20.568 0.59 17.98  ? 162 SER A CA    1 
ATOM   1084 C  CA    B SER A 1 145 ? 2.585   54.474 20.568 0.41 18.03  ? 162 SER A CA    1 
ATOM   1085 C  C     . SER A 1 145 ? 3.648   54.888 21.572 1.00 20.62  ? 162 SER A C     1 
ATOM   1086 O  O     . SER A 1 145 ? 3.374   55.678 22.485 1.00 20.97  ? 162 SER A O     1 
ATOM   1087 C  CB    A SER A 1 145 ? 2.100   55.698 19.792 0.59 21.42  ? 162 SER A CB    1 
ATOM   1088 C  CB    B SER A 1 145 ? 2.104   55.692 19.781 0.41 21.46  ? 162 SER A CB    1 
ATOM   1089 O  OG    A SER A 1 145 ? 3.200   56.435 19.306 0.59 25.08  ? 162 SER A OG    1 
ATOM   1090 O  OG    B SER A 1 145 ? 1.245   55.291 18.734 0.41 21.28  ? 162 SER A OG    1 
ATOM   1091 N  N     . TYR A 1 146 ? 4.848   54.377 21.386 1.00 20.31  ? 163 TYR A N     1 
ATOM   1092 C  CA    . TYR A 1 146 ? 6.017   54.803 22.134 1.00 17.60  ? 163 TYR A CA    1 
ATOM   1093 C  C     . TYR A 1 146 ? 7.225   54.473 21.275 1.00 19.34  ? 163 TYR A C     1 
ATOM   1094 O  O     . TYR A 1 146 ? 7.131   53.723 20.295 1.00 19.52  ? 163 TYR A O     1 
ATOM   1095 C  CB    . TYR A 1 146 ? 6.097   54.138 23.517 1.00 16.97  ? 163 TYR A CB    1 
ATOM   1096 C  CG    . TYR A 1 146 ? 6.161   52.629 23.477 1.00 14.60  ? 163 TYR A CG    1 
ATOM   1097 C  CD1   . TYR A 1 146 ? 5.006   51.874 23.367 1.00 16.43  ? 163 TYR A CD1   1 
ATOM   1098 C  CD2   . TYR A 1 146 ? 7.378   51.963 23.524 1.00 14.69  ? 163 TYR A CD2   1 
ATOM   1099 C  CE1   . TYR A 1 146 ? 5.060   50.478 23.309 1.00 16.23  ? 163 TYR A CE1   1 
ATOM   1100 C  CE2   . TYR A 1 146 ? 7.447   50.577 23.467 1.00 14.84  ? 163 TYR A CE2   1 
ATOM   1101 C  CZ    . TYR A 1 146 ? 6.272   49.842 23.368 1.00 13.54  ? 163 TYR A CZ    1 
ATOM   1102 O  OH    . TYR A 1 146 ? 6.338   48.476 23.297 1.00 16.43  ? 163 TYR A OH    1 
ATOM   1103 N  N     . LYS A 1 147 ? 8.356   55.056 21.638 1.00 18.67  ? 164 LYS A N     1 
ATOM   1104 C  CA    . LYS A 1 147 ? 9.605   54.869 20.910 1.00 19.26  ? 164 LYS A CA    1 
ATOM   1105 C  C     . LYS A 1 147 ? 10.561  53.987 21.703 1.00 19.45  ? 164 LYS A C     1 
ATOM   1106 O  O     . LYS A 1 147 ? 10.788  54.226 22.897 1.00 19.83  ? 164 LYS A O     1 
ATOM   1107 C  CB    . LYS A 1 147 ? 10.259  56.224 20.627 1.00 23.49  ? 164 LYS A CB    1 
ATOM   1108 C  CG    . LYS A 1 147 ? 11.535  56.128 19.806 1.00 29.21  ? 164 LYS A CG    1 
ATOM   1109 C  CD    . LYS A 1 147 ? 12.256  57.459 19.780 1.00 36.75  ? 164 LYS A CD    1 
ATOM   1110 C  CE    . LYS A 1 147 ? 13.431  57.429 18.826 1.00 39.70  ? 164 LYS A CE    1 
ATOM   1111 N  NZ    . LYS A 1 147 ? 14.241  58.680 18.916 1.00 58.37  ? 164 LYS A NZ    1 
ATOM   1112 N  N     . LEU A 1 148 ? 11.162  53.009 21.026 1.00 18.67  ? 165 LEU A N     1 
ATOM   1113 C  CA    . LEU A 1 148 ? 12.154  52.165 21.672 1.00 14.35  ? 165 LEU A CA    1 
ATOM   1114 C  C     . LEU A 1 148 ? 13.421  52.956 21.962 1.00 18.53  ? 165 LEU A C     1 
ATOM   1115 O  O     . LEU A 1 148 ? 13.937  53.676 21.100 1.00 18.22  ? 165 LEU A O     1 
ATOM   1116 C  CB    . LEU A 1 148 ? 12.475  50.944 20.803 1.00 17.99  ? 165 LEU A CB    1 
ATOM   1117 C  CG    . LEU A 1 148 ? 11.416  49.851 20.742 1.00 19.57  ? 165 LEU A CG    1 
ATOM   1118 C  CD1   . LEU A 1 148 ? 11.840  48.796 19.708 1.00 19.61  ? 165 LEU A CD1   1 
ATOM   1119 C  CD2   . LEU A 1 148 ? 11.195  49.234 22.109 1.00 21.40  ? 165 LEU A CD2   1 
ATOM   1120 N  N     . ALA A 1 149 ? 13.930  52.803 23.186 1.00 19.76  ? 166 ALA A N     1 
ATOM   1121 C  CA    . ALA A 1 149 ? 15.132  53.522 23.607 1.00 20.93  ? 166 ALA A CA    1 
ATOM   1122 C  C     . ALA A 1 149 ? 16.347  53.169 22.757 1.00 17.40  ? 166 ALA A C     1 
ATOM   1123 O  O     . ALA A 1 149 ? 17.245  54.006 22.582 1.00 20.32  ? 166 ALA A O     1 
ATOM   1124 C  CB    . ALA A 1 149 ? 15.431  53.210 25.069 1.00 26.46  ? 166 ALA A CB    1 
ATOM   1125 N  N     . LEU A 1 150 ? 16.386  51.966 22.189 1.00 16.33  ? 167 LEU A N     1 
ATOM   1126 C  CA    . LEU A 1 150 ? 17.520  51.555 21.370 1.00 16.16  ? 167 LEU A CA    1 
ATOM   1127 C  C     . LEU A 1 150 ? 17.313  51.831 19.876 1.00 16.26  ? 167 LEU A C     1 
ATOM   1128 O  O     . LEU A 1 150 ? 18.063  51.288 19.055 1.00 17.07  ? 167 LEU A O     1 
ATOM   1129 C  CB    . LEU A 1 150 ? 17.816  50.075 21.615 1.00 18.20  ? 167 LEU A CB    1 
ATOM   1130 C  CG    . LEU A 1 150 ? 18.687  49.748 22.841 1.00 20.05  ? 167 LEU A CG    1 
ATOM   1131 C  CD1   . LEU A 1 150 ? 18.638  48.276 23.164 1.00 26.79  ? 167 LEU A CD1   1 
ATOM   1132 C  CD2   . LEU A 1 150 ? 20.113  50.174 22.632 1.00 30.96  ? 167 LEU A CD2   1 
ATOM   1133 N  N     . SER A 1 151 ? 16.378  52.727 19.535 1.00 18.31  ? 168 SER A N     1 
ATOM   1134 C  CA    A SER A 1 151 ? 16.031  52.984 18.138 0.35 18.09  ? 168 SER A CA    1 
ATOM   1135 C  CA    B SER A 1 151 ? 16.032  52.967 18.132 0.65 18.01  ? 168 SER A CA    1 
ATOM   1136 C  C     . SER A 1 151 ? 17.255  53.334 17.294 1.00 18.87  ? 168 SER A C     1 
ATOM   1137 O  O     . SER A 1 151 ? 17.387  52.871 16.153 1.00 19.18  ? 168 SER A O     1 
ATOM   1138 C  CB    A SER A 1 151 ? 15.000  54.115 18.077 0.35 20.74  ? 168 SER A CB    1 
ATOM   1139 C  CB    B SER A 1 151 ? 14.974  54.071 18.031 0.65 20.71  ? 168 SER A CB    1 
ATOM   1140 O  OG    A SER A 1 151 ? 14.721  54.492 16.743 0.35 22.19  ? 168 SER A OG    1 
ATOM   1141 O  OG    B SER A 1 151 ? 13.678  53.564 18.295 0.65 26.37  ? 168 SER A OG    1 
ATOM   1142 N  N     . ASP A 1 152 ? 18.159  54.151 17.834 1.00 19.39  ? 169 ASP A N     1 
ATOM   1143 C  CA    . ASP A 1 152 ? 19.319  54.577 17.050 1.00 20.68  ? 169 ASP A CA    1 
ATOM   1144 C  C     . ASP A 1 152 ? 20.208  53.404 16.647 1.00 18.62  ? 169 ASP A C     1 
ATOM   1145 O  O     . ASP A 1 152 ? 20.975  53.522 15.679 1.00 21.62  ? 169 ASP A O     1 
ATOM   1146 C  CB    . ASP A 1 152 ? 20.168  55.590 17.830 1.00 24.67  ? 169 ASP A CB    1 
ATOM   1147 C  CG    . ASP A 1 152 ? 19.462  56.931 18.036 1.00 34.26  ? 169 ASP A CG    1 
ATOM   1148 O  OD1   . ASP A 1 152 ? 18.588  57.289 17.225 1.00 34.49  ? 169 ASP A OD1   1 
ATOM   1149 O  OD2   . ASP A 1 152 ? 19.804  57.633 19.008 1.00 45.09  ? 169 ASP A OD2   1 
ATOM   1150 N  N     . TYR A 1 153 ? 20.154  52.298 17.382 1.00 15.79  ? 170 TYR A N     1 
ATOM   1151 C  CA    . TYR A 1 153 ? 20.964  51.123 17.123 1.00 14.95  ? 170 TYR A CA    1 
ATOM   1152 C  C     . TYR A 1 153 ? 20.191  50.017 16.416 1.00 14.94  ? 170 TYR A C     1 
ATOM   1153 O  O     . TYR A 1 153 ? 20.777  48.994 16.090 1.00 18.03  ? 170 TYR A O     1 
ATOM   1154 C  CB    . TYR A 1 153 ? 21.575  50.624 18.447 1.00 15.64  ? 170 TYR A CB    1 
ATOM   1155 C  CG    . TYR A 1 153 ? 22.516  51.668 18.997 1.00 17.98  ? 170 TYR A CG    1 
ATOM   1156 C  CD1   . TYR A 1 153 ? 23.793  51.796 18.481 1.00 17.25  ? 170 TYR A CD1   1 
ATOM   1157 C  CD2   . TYR A 1 153 ? 22.097  52.586 19.956 1.00 17.28  ? 170 TYR A CD2   1 
ATOM   1158 C  CE1   . TYR A 1 153 ? 24.650  52.775 18.932 1.00 22.86  ? 170 TYR A CE1   1 
ATOM   1159 C  CE2   . TYR A 1 153 ? 22.944  53.555 20.421 1.00 19.71  ? 170 TYR A CE2   1 
ATOM   1160 C  CZ    . TYR A 1 153 ? 24.221  53.639 19.910 1.00 23.52  ? 170 TYR A CZ    1 
ATOM   1161 O  OH    . TYR A 1 153 ? 25.101  54.583 20.350 1.00 25.63  ? 170 TYR A OH    1 
ATOM   1162 N  N     . ILE A 1 154 ? 18.899  50.212 16.171 1.00 17.28  ? 171 ILE A N     1 
ATOM   1163 C  CA    . ILE A 1 154 ? 18.066  49.248 15.448 1.00 16.99  ? 171 ILE A CA    1 
ATOM   1164 C  C     . ILE A 1 154 ? 17.817  49.703 14.018 1.00 18.07  ? 171 ILE A C     1 
ATOM   1165 O  O     . ILE A 1 154 ? 17.870  48.902 13.086 1.00 21.99  ? 171 ILE A O     1 
ATOM   1166 C  CB    . ILE A 1 154 ? 16.732  49.053 16.200 1.00 20.45  ? 171 ILE A CB    1 
ATOM   1167 C  CG1   . ILE A 1 154 ? 16.958  48.391 17.557 1.00 17.79  ? 171 ILE A CG1   1 
ATOM   1168 C  CG2   . ILE A 1 154 ? 15.726  48.228 15.366 1.00 20.25  ? 171 ILE A CG2   1 
ATOM   1169 C  CD1   . ILE A 1 154 ? 15.788  48.550 18.488 1.00 23.10  ? 171 ILE A CD1   1 
ATOM   1170 N  N     . PHE A 1 155 ? 17.554  50.991 13.832 1.00 18.73  ? 172 PHE A N     1 
ATOM   1171 C  CA    . PHE A 1 155 ? 17.208  51.557 12.538 1.00 18.14  ? 172 PHE A CA    1 
ATOM   1172 C  C     . PHE A 1 155 ? 18.385  52.338 11.978 1.00 25.01  ? 172 PHE A C     1 
ATOM   1173 O  O     . PHE A 1 155 ? 19.129  52.985 12.719 1.00 26.58  ? 172 PHE A O     1 
ATOM   1174 C  CB    . PHE A 1 155 ? 15.986  52.459 12.668 1.00 19.23  ? 172 PHE A CB    1 
ATOM   1175 C  CG    . PHE A 1 155 ? 14.821  51.770 13.309 1.00 19.56  ? 172 PHE A CG    1 
ATOM   1176 C  CD1   . PHE A 1 155 ? 14.178  50.735 12.665 1.00 18.68  ? 172 PHE A CD1   1 
ATOM   1177 C  CD2   . PHE A 1 155 ? 14.412  52.105 14.584 1.00 22.48  ? 172 PHE A CD2   1 
ATOM   1178 C  CE1   . PHE A 1 155 ? 13.123  50.075 13.271 1.00 19.97  ? 172 PHE A CE1   1 
ATOM   1179 C  CE2   . PHE A 1 155 ? 13.354  51.451 15.180 1.00 23.96  ? 172 PHE A CE2   1 
ATOM   1180 C  CZ    . PHE A 1 155 ? 12.714  50.434 14.518 1.00 21.13  ? 172 PHE A CZ    1 
ATOM   1181 N  N     . GLU A 1 156 ? 18.570  52.260 10.672 1.00 28.83  ? 173 GLU A N     1 
ATOM   1182 C  CA    . GLU A 1 156 ? 19.680  52.979 10.063 1.00 34.51  ? 173 GLU A CA    1 
ATOM   1183 C  C     . GLU A 1 156 ? 19.284  54.445 9.932  1.00 44.42  ? 173 GLU A C     1 
ATOM   1184 O  O     . GLU A 1 156 ? 20.144  55.322 9.786  1.00 48.07  ? 173 GLU A O     1 
ATOM   1185 C  CB    . GLU A 1 156 ? 20.079  52.349 8.710  1.00 34.08  ? 173 GLU A CB    1 
ATOM   1186 C  CG    . GLU A 1 156 ? 18.970  52.213 7.705  1.00 35.69  ? 173 GLU A CG    1 
ATOM   1187 C  CD    . GLU A 1 156 ? 19.388  51.502 6.406  1.00 39.75  ? 173 GLU A CD    1 
ATOM   1188 O  OE1   . GLU A 1 156 ? 20.113  50.473 6.423  1.00 25.15  ? 173 GLU A OE1   1 
ATOM   1189 O  OE2   . GLU A 1 156 ? 18.956  51.981 5.344  1.00 37.36  ? 173 GLU A OE2   1 
ATOM   1190 O  OXT   . GLU A 1 156 ? 18.097  54.796 10.022 1.00 41.47  ? 173 GLU A OXT   1 
ATOM   1191 N  N     . HIS B 1 8   ? -1.071  9.555  11.580 1.00 43.99  ? 25  HIS B N     1 
ATOM   1192 C  CA    . HIS B 1 8   ? -0.134  8.442  11.454 1.00 41.59  ? 25  HIS B CA    1 
ATOM   1193 C  C     . HIS B 1 8   ? 1.275   8.916  11.827 1.00 30.12  ? 25  HIS B C     1 
ATOM   1194 O  O     . HIS B 1 8   ? 1.798   9.861  11.236 1.00 34.23  ? 25  HIS B O     1 
ATOM   1195 C  CB    . HIS B 1 8   ? -0.152  7.873  10.035 1.00 42.81  ? 25  HIS B CB    1 
ATOM   1196 N  N     . VAL B 1 9   ? 1.869   8.278  12.828 1.00 37.93  ? 26  VAL B N     1 
ATOM   1197 C  CA    . VAL B 1 9   ? 3.210   8.618  13.279 1.00 29.67  ? 26  VAL B CA    1 
ATOM   1198 C  C     . VAL B 1 9   ? 4.148   7.482  12.899 1.00 25.78  ? 26  VAL B C     1 
ATOM   1199 O  O     . VAL B 1 9   ? 3.732   6.352  12.614 1.00 27.16  ? 26  VAL B O     1 
ATOM   1200 C  CB    . VAL B 1 9   ? 3.273   8.895  14.803 1.00 21.14  ? 26  VAL B CB    1 
ATOM   1201 C  CG1   . VAL B 1 9   ? 2.476   10.129 15.131 1.00 26.23  ? 26  VAL B CG1   1 
ATOM   1202 C  CG2   . VAL B 1 9   ? 2.800   7.689  15.600 1.00 25.64  ? 26  VAL B CG2   1 
ATOM   1203 N  N     . GLU B 1 10  ? 5.434   7.795  12.854 1.00 20.85  ? 27  GLU B N     1 
ATOM   1204 C  CA    . GLU B 1 10  ? 6.444   6.772  12.665 1.00 23.43  ? 27  GLU B CA    1 
ATOM   1205 C  C     . GLU B 1 10  ? 7.518   6.944  13.726 1.00 19.55  ? 27  GLU B C     1 
ATOM   1206 O  O     . GLU B 1 10  ? 7.470   7.869  14.545 1.00 18.54  ? 27  GLU B O     1 
ATOM   1207 C  CB    . GLU B 1 10  ? 7.033   6.820  11.262 1.00 28.14  ? 27  GLU B CB    1 
ATOM   1208 C  CG    . GLU B 1 10  ? 7.548   8.154  10.897 1.00 25.50  ? 27  GLU B CG    1 
ATOM   1209 C  CD    . GLU B 1 10  ? 7.888   8.310  9.412  1.00 28.57  ? 27  GLU B CD    1 
ATOM   1210 O  OE1   . GLU B 1 10  ? 7.263   7.676  8.534  1.00 40.78  ? 27  GLU B OE1   1 
ATOM   1211 O  OE2   . GLU B 1 10  ? 8.800   9.095  9.137  1.00 22.14  ? 27  GLU B OE2   1 
ATOM   1212 N  N     . GLN B 1 11  ? 8.468   6.015  13.735 1.00 21.68  ? 28  GLN B N     1 
ATOM   1213 C  CA    . GLN B 1 11  ? 9.574   6.044  14.684 1.00 19.64  ? 28  GLN B CA    1 
ATOM   1214 C  C     . GLN B 1 11  ? 10.889  6.036  13.929 1.00 20.19  ? 28  GLN B C     1 
ATOM   1215 O  O     . GLN B 1 11  ? 11.022  5.361  12.906 1.00 21.00  ? 28  GLN B O     1 
ATOM   1216 C  CB    . GLN B 1 11  ? 9.517   4.870  15.656 1.00 22.10  ? 28  GLN B CB    1 
ATOM   1217 C  CG    . GLN B 1 11  ? 8.298   4.954  16.563 1.00 24.02  ? 28  GLN B CG    1 
ATOM   1218 C  CD    . GLN B 1 11  ? 8.249   3.895  17.643 1.00 24.62  ? 28  GLN B CD    1 
ATOM   1219 O  OE1   . GLN B 1 11  ? 9.009   2.934  17.637 1.00 31.19  ? 28  GLN B OE1   1 
ATOM   1220 N  NE2   . GLN B 1 11  ? 7.353   4.095  18.603 1.00 25.20  ? 28  GLN B NE2   1 
ATOM   1221 N  N     . THR B 1 12  ? 11.846  6.832  14.399 1.00 18.85  ? 29  THR B N     1 
ATOM   1222 C  CA    . THR B 1 12  ? 13.177  6.838  13.828 1.00 17.01  ? 29  THR B CA    1 
ATOM   1223 C  C     . THR B 1 12  ? 14.200  6.521  14.909 1.00 18.32  ? 29  THR B C     1 
ATOM   1224 O  O     . THR B 1 12  ? 13.958  6.731  16.092 1.00 18.57  ? 29  THR B O     1 
ATOM   1225 C  CB    . THR B 1 12  ? 13.501  8.177  13.147 1.00 16.93  ? 29  THR B CB    1 
ATOM   1226 O  OG1   . THR B 1 12  ? 14.652  7.972  12.319 1.00 18.71  ? 29  THR B OG1   1 
ATOM   1227 C  CG2   . THR B 1 12  ? 13.728  9.302  14.189 1.00 19.17  ? 29  THR B CG2   1 
ATOM   1228 N  N     . TYR B 1 13  ? 15.334  5.969  14.484 1.00 18.05  ? 30  TYR B N     1 
ATOM   1229 C  CA    . TYR B 1 13  ? 16.480  5.759  15.364 1.00 17.45  ? 30  TYR B CA    1 
ATOM   1230 C  C     . TYR B 1 13  ? 17.405  6.967  15.258 1.00 16.61  ? 30  TYR B C     1 
ATOM   1231 O  O     . TYR B 1 13  ? 17.838  7.328  14.167 1.00 18.69  ? 30  TYR B O     1 
ATOM   1232 C  CB    . TYR B 1 13  ? 17.239  4.483  14.990 1.00 18.71  ? 30  TYR B CB    1 
ATOM   1233 C  CG    . TYR B 1 13  ? 18.444  4.266  15.881 1.00 18.08  ? 30  TYR B CG    1 
ATOM   1234 C  CD1   . TYR B 1 13  ? 18.271  3.975  17.216 1.00 18.53  ? 30  TYR B CD1   1 
ATOM   1235 C  CD2   . TYR B 1 13  ? 19.753  4.393  15.395 1.00 19.72  ? 30  TYR B CD2   1 
ATOM   1236 C  CE1   . TYR B 1 13  ? 19.343  3.797  18.063 1.00 20.22  ? 30  TYR B CE1   1 
ATOM   1237 C  CE2   . TYR B 1 13  ? 20.842  4.207  16.243 1.00 21.33  ? 30  TYR B CE2   1 
ATOM   1238 C  CZ    . TYR B 1 13  ? 20.624  3.918  17.575 1.00 20.24  ? 30  TYR B CZ    1 
ATOM   1239 O  OH    . TYR B 1 13  ? 21.676  3.748  18.451 1.00 23.15  ? 30  TYR B OH    1 
ATOM   1240 N  N     . LEU B 1 14  ? 17.696  7.595  16.399 1.00 18.42  ? 31  LEU B N     1 
ATOM   1241 C  CA    . LEU B 1 14  ? 18.626  8.710  16.499 1.00 17.19  ? 31  LEU B CA    1 
ATOM   1242 C  C     . LEU B 1 14  ? 19.693  8.318  17.507 1.00 18.27  ? 31  LEU B C     1 
ATOM   1243 O  O     . LEU B 1 14  ? 19.380  7.720  18.541 1.00 19.95  ? 31  LEU B O     1 
ATOM   1244 C  CB    . LEU B 1 14  ? 17.911  10.010 16.955 1.00 19.15  ? 31  LEU B CB    1 
ATOM   1245 C  CG    . LEU B 1 14  ? 17.024  10.655 15.883 1.00 19.73  ? 31  LEU B CG    1 
ATOM   1246 C  CD1   . LEU B 1 14  ? 16.021  11.602 16.506 1.00 23.83  ? 31  LEU B CD1   1 
ATOM   1247 C  CD2   . LEU B 1 14  ? 17.879  11.416 14.870 1.00 21.78  ? 31  LEU B CD2   1 
ATOM   1248 N  N     . MET B 1 15  ? 20.950  8.626  17.206 1.00 16.01  ? 32  MET B N     1 
ATOM   1249 C  CA    . MET B 1 15  ? 22.047  8.244  18.087 1.00 17.22  ? 32  MET B CA    1 
ATOM   1250 C  C     . MET B 1 15  ? 22.980  9.434  18.264 1.00 16.20  ? 32  MET B C     1 
ATOM   1251 O  O     . MET B 1 15  ? 23.504  9.977  17.284 1.00 17.27  ? 32  MET B O     1 
ATOM   1252 C  CB    . MET B 1 15  ? 22.795  7.022  17.540 1.00 17.30  ? 32  MET B CB    1 
ATOM   1253 C  CG    . MET B 1 15  ? 23.941  6.616  18.405 1.00 19.88  ? 32  MET B CG    1 
ATOM   1254 S  SD    . MET B 1 15  ? 24.644  5.021  17.872 1.00 24.16  ? 32  MET B SD    1 
ATOM   1255 C  CE    . MET B 1 15  ? 24.925  5.351  16.162 1.00 28.39  ? 32  MET B CE    1 
ATOM   1256 N  N     . ILE B 1 16  ? 23.139  9.871  19.510 1.00 15.31  ? 33  ILE B N     1 
ATOM   1257 C  CA    . ILE B 1 16  ? 24.158  10.868 19.822 1.00 17.22  ? 33  ILE B CA    1 
ATOM   1258 C  C     . ILE B 1 16  ? 25.511  10.165 19.855 1.00 15.81  ? 33  ILE B C     1 
ATOM   1259 O  O     . ILE B 1 16  ? 25.700  9.197  20.600 1.00 16.89  ? 33  ILE B O     1 
ATOM   1260 C  CB    . ILE B 1 16  ? 23.865  11.585 21.145 1.00 17.02  ? 33  ILE B CB    1 
ATOM   1261 C  CG1   . ILE B 1 16  ? 22.476  12.227 21.089 1.00 18.48  ? 33  ILE B CG1   1 
ATOM   1262 C  CG2   . ILE B 1 16  ? 24.915  12.636 21.397 1.00 16.02  ? 33  ILE B CG2   1 
ATOM   1263 C  CD1   . ILE B 1 16  ? 22.059  12.986 22.379 1.00 18.10  ? 33  ILE B CD1   1 
ATOM   1264 N  N     . LYS B 1 17  ? 26.427  10.637 19.028 1.00 17.22  ? 34  LYS B N     1 
ATOM   1265 C  CA    . LYS B 1 17  ? 27.740  10.054 18.839 1.00 17.79  ? 34  LYS B CA    1 
ATOM   1266 C  C     . LYS B 1 17  ? 28.641  10.486 19.981 1.00 15.58  ? 34  LYS B C     1 
ATOM   1267 O  O     . LYS B 1 17  ? 28.285  11.373 20.754 1.00 15.97  ? 34  LYS B O     1 
ATOM   1268 C  CB    . LYS B 1 17  ? 28.292  10.499 17.495 1.00 15.38  ? 34  LYS B CB    1 
ATOM   1269 C  CG    . LYS B 1 17  ? 27.391  10.169 16.299 1.00 17.50  ? 34  LYS B CG    1 
ATOM   1270 C  CD    . LYS B 1 17  ? 28.030  10.588 14.963 1.00 18.02  ? 34  LYS B CD    1 
ATOM   1271 C  CE    . LYS B 1 17  ? 27.294  9.930  13.802 1.00 21.64  ? 34  LYS B CE    1 
ATOM   1272 N  NZ    . LYS B 1 17  ? 27.781  10.380 12.459 1.00 23.88  ? 34  LYS B NZ    1 
ATOM   1273 N  N     . PRO B 1 18  ? 29.825  9.885  20.111 1.00 16.07  ? 35  PRO B N     1 
ATOM   1274 C  CA    . PRO B 1 18  ? 30.679  10.202 21.269 1.00 18.69  ? 35  PRO B CA    1 
ATOM   1275 C  C     . PRO B 1 18  ? 31.035  11.675 21.360 1.00 18.59  ? 35  PRO B C     1 
ATOM   1276 O  O     . PRO B 1 18  ? 31.259  12.172 22.478 1.00 18.79  ? 35  PRO B O     1 
ATOM   1277 C  CB    . PRO B 1 18  ? 31.916  9.307  21.035 1.00 21.05  ? 35  PRO B CB    1 
ATOM   1278 C  CG    . PRO B 1 18  ? 31.393  8.167  20.223 1.00 19.55  ? 35  PRO B CG    1 
ATOM   1279 C  CD    . PRO B 1 18  ? 30.405  8.823  19.276 1.00 16.29  ? 35  PRO B CD    1 
ATOM   1280 N  N     . ASP B 1 19  ? 31.096  12.401 20.236 1.00 17.13  ? 36  ASP B N     1 
ATOM   1281 C  CA    . ASP B 1 19  ? 31.379  13.827 20.355 1.00 18.69  ? 36  ASP B CA    1 
ATOM   1282 C  C     . ASP B 1 19  ? 30.230  14.580 21.009 1.00 16.16  ? 36  ASP B C     1 
ATOM   1283 O  O     . ASP B 1 19  ? 30.469  15.551 21.736 1.00 17.23  ? 36  ASP B O     1 
ATOM   1284 C  CB    . ASP B 1 19  ? 31.741  14.457 18.997 1.00 19.66  ? 36  ASP B CB    1 
ATOM   1285 C  CG    . ASP B 1 19  ? 30.768  14.118 17.852 1.00 19.69  ? 36  ASP B CG    1 
ATOM   1286 O  OD1   . ASP B 1 19  ? 30.181  13.012 17.813 1.00 21.42  ? 36  ASP B OD1   1 
ATOM   1287 O  OD2   . ASP B 1 19  ? 30.635  14.984 16.948 1.00 19.51  ? 36  ASP B OD2   1 
ATOM   1288 N  N     . GLY B 1 20  ? 28.982  14.161 20.779 1.00 16.05  ? 37  GLY B N     1 
ATOM   1289 C  CA    . GLY B 1 20  ? 27.871  14.787 21.490 1.00 15.15  ? 37  GLY B CA    1 
ATOM   1290 C  C     . GLY B 1 20  ? 27.947  14.546 22.990 1.00 15.22  ? 37  GLY B C     1 
ATOM   1291 O  O     . GLY B 1 20  ? 27.629  15.432 23.793 1.00 15.48  ? 37  GLY B O     1 
ATOM   1292 N  N     . ILE B 1 21  ? 28.350  13.333 23.389 1.00 17.23  ? 38  ILE B N     1 
ATOM   1293 C  CA    . ILE B 1 21  ? 28.514  13.013 24.807 1.00 15.05  ? 38  ILE B CA    1 
ATOM   1294 C  C     . ILE B 1 21  ? 29.651  13.831 25.408 1.00 14.46  ? 38  ILE B C     1 
ATOM   1295 O  O     . ILE B 1 21  ? 29.503  14.465 26.452 1.00 16.87  ? 38  ILE B O     1 
ATOM   1296 C  CB    . ILE B 1 21  ? 28.780  11.504 24.990 1.00 16.78  ? 38  ILE B CB    1 
ATOM   1297 C  CG1   . ILE B 1 21  ? 27.720  10.612 24.344 1.00 20.86  ? 38  ILE B CG1   1 
ATOM   1298 C  CG2   . ILE B 1 21  ? 28.932  11.176 26.466 1.00 19.38  ? 38  ILE B CG2   1 
ATOM   1299 C  CD1   . ILE B 1 21  ? 26.305  10.844 24.749 1.00 22.79  ? 38  ILE B CD1   1 
ATOM   1300 N  N     . GLN B 1 22  ? 30.818  13.825 24.749 1.00 16.89  ? 39  GLN B N     1 
ATOM   1301 C  CA    . GLN B 1 22  ? 32.015  14.443 25.314 1.00 17.19  ? 39  GLN B CA    1 
ATOM   1302 C  C     . GLN B 1 22  ? 31.949  15.957 25.311 1.00 16.92  ? 39  GLN B C     1 
ATOM   1303 O  O     . GLN B 1 22  ? 32.517  16.601 26.202 1.00 17.45  ? 39  GLN B O     1 
ATOM   1304 C  CB    . GLN B 1 22  ? 33.250  13.980 24.532 1.00 18.04  ? 39  GLN B CB    1 
ATOM   1305 C  CG    . GLN B 1 22  ? 33.589  12.559 24.800 1.00 20.34  ? 39  GLN B CG    1 
ATOM   1306 C  CD    . GLN B 1 22  ? 34.275  12.360 26.131 1.00 20.31  ? 39  GLN B CD    1 
ATOM   1307 O  OE1   . GLN B 1 22  ? 34.411  13.287 26.930 1.00 22.12  ? 39  GLN B OE1   1 
ATOM   1308 N  NE2   . GLN B 1 22  ? 34.703  11.143 26.381 1.00 20.67  ? 39  GLN B NE2   1 
ATOM   1309 N  N     . ARG B 1 23  ? 31.254  16.550 24.347 1.00 16.65  ? 40  ARG B N     1 
ATOM   1310 C  CA    . ARG B 1 23  ? 31.070  17.994 24.370 1.00 15.72  ? 40  ARG B CA    1 
ATOM   1311 C  C     . ARG B 1 23  ? 29.911  18.402 25.272 1.00 17.93  ? 40  ARG B C     1 
ATOM   1312 O  O     . ARG B 1 23  ? 29.677  19.606 25.466 1.00 17.55  ? 40  ARG B O     1 
ATOM   1313 C  CB    . ARG B 1 23  ? 30.874  18.524 22.948 1.00 15.91  ? 40  ARG B CB    1 
ATOM   1314 C  CG    . ARG B 1 23  ? 32.100  18.240 22.061 1.00 15.45  ? 40  ARG B CG    1 
ATOM   1315 C  CD    . ARG B 1 23  ? 31.868  18.620 20.613 1.00 18.36  ? 40  ARG B CD    1 
ATOM   1316 N  NE    . ARG B 1 23  ? 31.685  20.052 20.483 1.00 17.17  ? 40  ARG B NE    1 
ATOM   1317 C  CZ    . ARG B 1 23  ? 31.117  20.631 19.431 1.00 18.37  ? 40  ARG B CZ    1 
ATOM   1318 N  NH1   . ARG B 1 23  ? 30.712  19.922 18.377 1.00 18.04  ? 40  ARG B NH1   1 
ATOM   1319 N  NH2   . ARG B 1 23  ? 30.891  21.941 19.463 1.00 16.76  ? 40  ARG B NH2   1 
ATOM   1320 N  N     . GLN B 1 24  ? 29.198  17.415 25.828 1.00 15.46  ? 41  GLN B N     1 
ATOM   1321 C  CA    . GLN B 1 24  ? 28.201  17.619 26.886 1.00 14.34  ? 41  GLN B CA    1 
ATOM   1322 C  C     . GLN B 1 24  ? 27.050  18.495 26.390 1.00 14.47  ? 41  GLN B C     1 
ATOM   1323 O  O     . GLN B 1 24  ? 26.598  19.436 27.050 1.00 15.79  ? 41  GLN B O     1 
ATOM   1324 C  CB    . GLN B 1 24  ? 28.839  18.186 28.162 1.00 17.20  ? 41  GLN B CB    1 
ATOM   1325 C  CG    . GLN B 1 24  ? 29.973  17.282 28.693 1.00 17.65  ? 41  GLN B CG    1 
ATOM   1326 C  CD    . GLN B 1 24  ? 29.927  17.114 30.177 1.00 20.50  ? 41  GLN B CD    1 
ATOM   1327 O  OE1   . GLN B 1 24  ? 30.635  17.803 30.879 1.00 20.35  ? 41  GLN B OE1   1 
ATOM   1328 N  NE2   . GLN B 1 24  ? 29.074  16.222 30.664 1.00 19.23  ? 41  GLN B NE2   1 
ATOM   1329 N  N     . VAL B 1 25  ? 26.528  18.114 25.230 1.00 14.66  ? 42  VAL B N     1 
ATOM   1330 C  CA    . VAL B 1 25  ? 25.378  18.761 24.615 1.00 13.36  ? 42  VAL B CA    1 
ATOM   1331 C  C     . VAL B 1 25  ? 24.206  17.785 24.450 1.00 16.07  ? 42  VAL B C     1 
ATOM   1332 O  O     . VAL B 1 25  ? 23.287  18.028 23.658 1.00 14.29  ? 42  VAL B O     1 
ATOM   1333 C  CB    . VAL B 1 25  ? 25.758  19.408 23.264 1.00 15.45  ? 42  VAL B CB    1 
ATOM   1334 C  CG1   . VAL B 1 25  ? 26.752  20.560 23.473 1.00 17.15  ? 42  VAL B CG1   1 
ATOM   1335 C  CG2   . VAL B 1 25  ? 26.302  18.370 22.287 1.00 16.87  ? 42  VAL B CG2   1 
ATOM   1336 N  N     . VAL B 1 26  ? 24.198  16.699 25.216 1.00 14.80  ? 43  VAL B N     1 
ATOM   1337 C  CA    . VAL B 1 26  ? 23.134  15.704 25.112 1.00 14.34  ? 43  VAL B CA    1 
ATOM   1338 C  C     . VAL B 1 26  ? 21.764  16.339 25.363 1.00 13.31  ? 43  VAL B C     1 
ATOM   1339 O  O     . VAL B 1 26  ? 20.811  16.158 24.591 1.00 13.92  ? 43  VAL B O     1 
ATOM   1340 C  CB    . VAL B 1 26  ? 23.411  14.558 26.105 1.00 14.66  ? 43  VAL B CB    1 
ATOM   1341 C  CG1   . VAL B 1 26  ? 22.213  13.660 26.278 1.00 17.88  ? 43  VAL B CG1   1 
ATOM   1342 C  CG2   . VAL B 1 26  ? 24.664  13.763 25.668 1.00 15.76  ? 43  VAL B CG2   1 
ATOM   1343 N  N     . GLY B 1 27  ? 21.640  17.084 26.457 1.00 12.62  ? 44  GLY B N     1 
ATOM   1344 C  CA    . GLY B 1 27  ? 20.361  17.715 26.778 1.00 12.25  ? 44  GLY B CA    1 
ATOM   1345 C  C     . GLY B 1 27  ? 19.888  18.689 25.714 1.00 11.31  ? 44  GLY B C     1 
ATOM   1346 O  O     . GLY B 1 27  ? 18.700  18.755 25.402 1.00 13.66  ? 44  GLY B O     1 
ATOM   1347 N  N     . GLU B 1 28  ? 20.805  19.492 25.178 1.00 13.62  ? 45  GLU B N     1 
ATOM   1348 C  CA    . GLU B 1 28  ? 20.437  20.421 24.119 1.00 12.71  ? 45  GLU B CA    1 
ATOM   1349 C  C     . GLU B 1 28  ? 19.897  19.681 22.903 1.00 13.42  ? 45  GLU B C     1 
ATOM   1350 O  O     . GLU B 1 28  ? 18.929  20.130 22.267 1.00 12.83  ? 45  GLU B O     1 
ATOM   1351 C  CB    . GLU B 1 28  ? 21.648  21.238 23.707 1.00 16.27  ? 45  GLU B CB    1 
ATOM   1352 C  CG    . GLU B 1 28  ? 22.010  22.357 24.607 1.00 21.11  ? 45  GLU B CG    1 
ATOM   1353 C  CD    . GLU B 1 28  ? 22.973  23.266 23.861 1.00 31.19  ? 45  GLU B CD    1 
ATOM   1354 O  OE1   . GLU B 1 28  ? 22.510  24.031 22.978 1.00 30.74  ? 45  GLU B OE1   1 
ATOM   1355 O  OE2   . GLU B 1 28  ? 24.183  23.148 24.101 1.00 30.71  ? 45  GLU B OE2   1 
ATOM   1356 N  N     . ILE B 1 29  ? 20.509  18.540 22.570 1.00 14.26  ? 46  ILE B N     1 
ATOM   1357 C  CA    . ILE B 1 29  ? 20.044  17.784 21.412 1.00 14.34  ? 46  ILE B CA    1 
ATOM   1358 C  C     . ILE B 1 29  ? 18.641  17.248 21.664 1.00 14.39  ? 46  ILE B C     1 
ATOM   1359 O  O     . ILE B 1 29  ? 17.726  17.419 20.853 1.00 13.59  ? 46  ILE B O     1 
ATOM   1360 C  CB    . ILE B 1 29  ? 21.019  16.647 21.077 1.00 14.18  ? 46  ILE B CB    1 
ATOM   1361 C  CG1   . ILE B 1 29  ? 22.355  17.218 20.574 1.00 16.32  ? 46  ILE B CG1   1 
ATOM   1362 C  CG2   . ILE B 1 29  ? 20.362  15.688 20.085 1.00 16.09  ? 46  ILE B CG2   1 
ATOM   1363 C  CD1   . ILE B 1 29  ? 23.487  16.151 20.513 1.00 17.02  ? 46  ILE B CD1   1 
ATOM   1364 N  N     . ILE B 1 30  ? 18.443  16.614 22.815 1.00 12.58  ? 47  ILE B N     1 
ATOM   1365 C  CA    . ILE B 1 30  ? 17.127  16.084 23.144 1.00 15.03  ? 47  ILE B CA    1 
ATOM   1366 C  C     . ILE B 1 30  ? 16.080  17.191 23.124 1.00 13.50  ? 47  ILE B C     1 
ATOM   1367 O  O     . ILE B 1 30  ? 14.951  16.996 22.648 1.00 12.44  ? 47  ILE B O     1 
ATOM   1368 C  CB    . ILE B 1 30  ? 17.187  15.381 24.505 1.00 15.66  ? 47  ILE B CB    1 
ATOM   1369 C  CG1   . ILE B 1 30  ? 18.054  14.124 24.386 1.00 12.89  ? 47  ILE B CG1   1 
ATOM   1370 C  CG2   . ILE B 1 30  ? 15.774  15.067 24.992 1.00 16.42  ? 47  ILE B CG2   1 
ATOM   1371 C  CD1   . ILE B 1 30  ? 18.449  13.561 25.727 1.00 15.82  ? 47  ILE B CD1   1 
ATOM   1372 N  N     . SER B 1 31  ? 16.415  18.353 23.682 1.00 12.86  ? 48  SER B N     1 
ATOM   1373 C  CA    . SER B 1 31  ? 15.459  19.449 23.733 1.00 12.44  ? 48  SER B CA    1 
ATOM   1374 C  C     . SER B 1 31  ? 14.983  19.851 22.338 1.00 12.06  ? 48  SER B C     1 
ATOM   1375 O  O     . SER B 1 31  ? 13.841  20.278 22.194 1.00 13.54  ? 48  SER B O     1 
ATOM   1376 C  CB    . SER B 1 31  ? 16.057  20.665 24.439 1.00 13.64  ? 48  SER B CB    1 
ATOM   1377 O  OG    . SER B 1 31  ? 16.172  20.444 25.848 1.00 14.55  ? 48  SER B OG    1 
ATOM   1378 N  N     . ARG B 1 32  ? 15.841  19.757 21.326 1.00 12.51  ? 49  ARG B N     1 
ATOM   1379 C  CA    . ARG B 1 32  ? 15.407  20.169 19.993 1.00 13.60  ? 49  ARG B CA    1 
ATOM   1380 C  C     . ARG B 1 32  ? 14.277  19.285 19.484 1.00 12.48  ? 49  ARG B C     1 
ATOM   1381 O  O     . ARG B 1 32  ? 13.369  19.754 18.784 1.00 14.22  ? 49  ARG B O     1 
ATOM   1382 C  CB    . ARG B 1 32  ? 16.578  20.134 19.027 1.00 14.53  ? 49  ARG B CB    1 
ATOM   1383 C  CG    . ARG B 1 32  ? 17.543  21.244 19.292 1.00 15.55  ? 49  ARG B CG    1 
ATOM   1384 C  CD    . ARG B 1 32  ? 18.389  21.422 18.064 1.00 29.68  ? 49  ARG B CD    1 
ATOM   1385 N  NE    . ARG B 1 32  ? 19.362  22.478 18.260 1.00 20.19  ? 49  ARG B NE    1 
ATOM   1386 C  CZ    . ARG B 1 32  ? 19.871  23.210 17.284 1.00 19.71  ? 49  ARG B CZ    1 
ATOM   1387 N  NH1   . ARG B 1 32  ? 19.533  23.003 16.026 1.00 20.38  ? 49  ARG B NH1   1 
ATOM   1388 N  NH2   . ARG B 1 32  ? 20.726  24.180 17.586 1.00 21.68  ? 49  ARG B NH2   1 
ATOM   1389 N  N     . PHE B 1 33  ? 14.353  17.985 19.770 1.00 13.03  ? 50  PHE B N     1 
ATOM   1390 C  CA    . PHE B 1 33  ? 13.307  17.058 19.336 1.00 13.75  ? 50  PHE B CA    1 
ATOM   1391 C  C     . PHE B 1 33  ? 12.059  17.141 20.213 1.00 13.53  ? 50  PHE B C     1 
ATOM   1392 O  O     . PHE B 1 33  ? 10.933  17.103 19.706 1.00 13.76  ? 50  PHE B O     1 
ATOM   1393 C  CB    . PHE B 1 33  ? 13.889  15.638 19.289 1.00 14.08  ? 50  PHE B CB    1 
ATOM   1394 C  CG    . PHE B 1 33  ? 14.980  15.496 18.261 1.00 13.36  ? 50  PHE B CG    1 
ATOM   1395 C  CD1   . PHE B 1 33  ? 14.672  15.524 16.909 1.00 14.58  ? 50  PHE B CD1   1 
ATOM   1396 C  CD2   . PHE B 1 33  ? 16.307  15.381 18.617 1.00 16.27  ? 50  PHE B CD2   1 
ATOM   1397 C  CE1   . PHE B 1 33  ? 15.663  15.423 15.948 1.00 15.29  ? 50  PHE B CE1   1 
ATOM   1398 C  CE2   . PHE B 1 33  ? 17.294  15.266 17.633 1.00 18.95  ? 50  PHE B CE2   1 
ATOM   1399 C  CZ    . PHE B 1 33  ? 16.941  15.321 16.298 1.00 15.10  ? 50  PHE B CZ    1 
ATOM   1400 N  N     . GLU B 1 34  ? 12.232  17.275 21.528 1.00 12.88  ? 51  GLU B N     1 
ATOM   1401 C  CA    . GLU B 1 34  ? 11.090  17.485 22.399 1.00 13.50  ? 51  GLU B CA    1 
ATOM   1402 C  C     . GLU B 1 34  ? 10.320  18.740 22.042 1.00 12.60  ? 51  GLU B C     1 
ATOM   1403 O  O     . GLU B 1 34  ? 9.094   18.795 22.215 1.00 14.37  ? 51  GLU B O     1 
ATOM   1404 C  CB    . GLU B 1 34  ? 11.549  17.593 23.852 1.00 14.95  ? 51  GLU B CB    1 
ATOM   1405 C  CG    . GLU B 1 34  ? 11.882  16.309 24.544 1.00 16.40  ? 51  GLU B CG    1 
ATOM   1406 C  CD    . GLU B 1 34  ? 12.285  16.578 25.992 1.00 15.14  ? 51  GLU B CD    1 
ATOM   1407 O  OE1   . GLU B 1 34  ? 13.278  17.344 26.204 1.00 15.53  ? 51  GLU B OE1   1 
ATOM   1408 O  OE2   . GLU B 1 34  ? 11.566  16.066 26.909 1.00 15.85  ? 51  GLU B OE2   1 
ATOM   1409 N  N     . LYS B 1 35  ? 11.014  19.766 21.534 1.00 12.60  ? 52  LYS B N     1 
ATOM   1410 C  CA    . LYS B 1 35  ? 10.380  21.043 21.251 1.00 13.56  ? 52  LYS B CA    1 
ATOM   1411 C  C     . LYS B 1 35  ? 9.303   20.914 20.191 1.00 13.33  ? 52  LYS B C     1 
ATOM   1412 O  O     . LYS B 1 35  ? 8.359   21.704 20.186 1.00 13.73  ? 52  LYS B O     1 
ATOM   1413 C  CB    . LYS B 1 35  ? 11.419  22.047 20.783 1.00 14.50  ? 52  LYS B CB    1 
ATOM   1414 C  CG    . LYS B 1 35  ? 10.964  23.499 20.747 1.00 14.89  ? 52  LYS B CG    1 
ATOM   1415 C  CD    . LYS B 1 35  ? 12.156  24.357 20.389 1.00 21.27  ? 52  LYS B CD    1 
ATOM   1416 C  CE    . LYS B 1 35  ? 12.035  25.758 20.950 1.00 34.36  ? 52  LYS B CE    1 
ATOM   1417 N  NZ    . LYS B 1 35  ? 12.091  25.738 22.451 1.00 36.36  ? 52  LYS B NZ    1 
ATOM   1418 N  N     . ARG B 1 36  ? 9.437   19.952 19.279 1.00 14.07  ? 53  ARG B N     1 
ATOM   1419 C  CA    . ARG B 1 36  ? 8.416   19.742 18.259 1.00 13.15  ? 53  ARG B CA    1 
ATOM   1420 C  C     . ARG B 1 36  ? 7.320   18.796 18.695 1.00 14.35  ? 53  ARG B C     1 
ATOM   1421 O  O     . ARG B 1 36  ? 6.451   18.453 17.881 1.00 13.40  ? 53  ARG B O     1 
ATOM   1422 C  CB    . ARG B 1 36  ? 9.061   19.224 16.962 1.00 12.12  ? 53  ARG B CB    1 
ATOM   1423 C  CG    . ARG B 1 36  ? 9.979   20.238 16.345 1.00 14.10  ? 53  ARG B CG    1 
ATOM   1424 C  CD    . ARG B 1 36  ? 10.499  19.792 14.998 1.00 16.18  ? 53  ARG B CD    1 
ATOM   1425 N  NE    . ARG B 1 36  ? 9.448   19.806 13.987 1.00 13.84  ? 53  ARG B NE    1 
ATOM   1426 C  CZ    . ARG B 1 36  ? 9.645   19.533 12.707 1.00 15.03  ? 53  ARG B CZ    1 
ATOM   1427 N  NH1   . ARG B 1 36  ? 10.824  19.120 12.261 1.00 16.23  ? 53  ARG B NH1   1 
ATOM   1428 N  NH2   . ARG B 1 36  ? 8.643   19.698 11.846 1.00 15.54  ? 53  ARG B NH2   1 
ATOM   1429 N  N     . GLY B 1 37  ? 7.344   18.335 19.943 1.00 13.48  ? 54  GLY B N     1 
ATOM   1430 C  CA    . GLY B 1 37  ? 6.360   17.389 20.382 1.00 12.85  ? 54  GLY B CA    1 
ATOM   1431 C  C     . GLY B 1 37  ? 6.647   15.966 19.979 1.00 13.19  ? 54  GLY B C     1 
ATOM   1432 O  O     . GLY B 1 37  ? 5.734   15.137 19.965 1.00 15.75  ? 54  GLY B O     1 
ATOM   1433 N  N     . TYR B 1 38  ? 7.884   15.664 19.605 1.00 14.75  ? 55  TYR B N     1 
ATOM   1434 C  CA    . TYR B 1 38  ? 8.254   14.285 19.338 1.00 14.31  ? 55  TYR B CA    1 
ATOM   1435 C  C     . TYR B 1 38  ? 8.360   13.533 20.659 1.00 16.24  ? 55  TYR B C     1 
ATOM   1436 O  O     . TYR B 1 38  ? 8.843   14.072 21.665 1.00 14.93  ? 55  TYR B O     1 
ATOM   1437 C  CB    . TYR B 1 38  ? 9.579   14.210 18.571 1.00 13.13  ? 55  TYR B CB    1 
ATOM   1438 C  CG    . TYR B 1 38  ? 9.536   14.793 17.176 1.00 13.88  ? 55  TYR B CG    1 
ATOM   1439 C  CD1   . TYR B 1 38  ? 8.395   14.698 16.393 1.00 14.33  ? 55  TYR B CD1   1 
ATOM   1440 C  CD2   . TYR B 1 38  ? 10.657  15.392 16.633 1.00 13.66  ? 55  TYR B CD2   1 
ATOM   1441 C  CE1   . TYR B 1 38  ? 8.371   15.228 15.102 1.00 13.84  ? 55  TYR B CE1   1 
ATOM   1442 C  CE2   . TYR B 1 38  ? 10.642  15.911 15.346 1.00 15.14  ? 55  TYR B CE2   1 
ATOM   1443 C  CZ    . TYR B 1 38  ? 9.506   15.829 14.613 1.00 12.25  ? 55  TYR B CZ    1 
ATOM   1444 O  OH    . TYR B 1 38  ? 9.519   16.329 13.354 1.00 14.13  ? 55  TYR B OH    1 
ATOM   1445 N  N     . ARG B 1 39  ? 7.888   12.295 20.653 1.00 15.06  ? 56  ARG B N     1 
ATOM   1446 C  CA    . ARG B 1 39  ? 7.825   11.471 21.858 1.00 15.90  ? 56  ARG B CA    1 
ATOM   1447 C  C     . ARG B 1 39  ? 9.077   10.614 21.973 1.00 16.46  ? 56  ARG B C     1 
ATOM   1448 O  O     . ARG B 1 39  ? 9.477   9.952  21.003 1.00 16.99  ? 56  ARG B O     1 
ATOM   1449 C  CB    . ARG B 1 39  ? 6.584   10.573 21.824 1.00 18.14  ? 56  ARG B CB    1 
ATOM   1450 C  CG    . ARG B 1 39  ? 6.351   9.772  23.099 1.00 17.05  ? 56  ARG B CG    1 
ATOM   1451 C  CD    . ARG B 1 39  ? 5.071   8.931  22.996 1.00 21.00  ? 56  ARG B CD    1 
ATOM   1452 N  NE    . ARG B 1 39  ? 5.174   7.815  22.053 1.00 19.00  ? 56  ARG B NE    1 
ATOM   1453 C  CZ    . ARG B 1 39  ? 5.668   6.620  22.350 1.00 21.68  ? 56  ARG B CZ    1 
ATOM   1454 N  NH1   . ARG B 1 39  ? 6.174   6.354  23.548 1.00 23.12  ? 56  ARG B NH1   1 
ATOM   1455 N  NH2   . ARG B 1 39  ? 5.631   5.654  21.434 1.00 24.96  ? 56  ARG B NH2   1 
ATOM   1456 N  N     . ILE B 1 40  ? 9.676   10.600 23.167 1.00 15.86  ? 57  ILE B N     1 
ATOM   1457 C  CA    . ILE B 1 40  ? 10.793  9.704  23.446 1.00 14.09  ? 57  ILE B CA    1 
ATOM   1458 C  C     . ILE B 1 40  ? 10.201  8.314  23.675 1.00 15.87  ? 57  ILE B C     1 
ATOM   1459 O  O     . ILE B 1 40  ? 9.553   8.062  24.699 1.00 19.29  ? 57  ILE B O     1 
ATOM   1460 C  CB    . ILE B 1 40  ? 11.612  10.150 24.669 1.00 16.90  ? 57  ILE B CB    1 
ATOM   1461 C  CG1   . ILE B 1 40  ? 12.112  11.592 24.536 1.00 19.84  ? 57  ILE B CG1   1 
ATOM   1462 C  CG2   . ILE B 1 40  ? 12.791  9.193  24.874 1.00 18.66  ? 57  ILE B CG2   1 
ATOM   1463 C  CD1   . ILE B 1 40  ? 12.647  12.199 25.865 1.00 17.90  ? 57  ILE B CD1   1 
ATOM   1464 N  N     . ALA B 1 41  ? 10.414  7.412  22.731 1.00 17.44  ? 58  ALA B N     1 
ATOM   1465 C  CA    . ALA B 1 41  ? 9.942   6.048  22.890 1.00 18.76  ? 58  ALA B CA    1 
ATOM   1466 C  C     . ALA B 1 41  ? 11.001  5.114  23.446 1.00 21.61  ? 58  ALA B C     1 
ATOM   1467 O  O     . ALA B 1 41  ? 10.649  4.055  23.978 1.00 23.67  ? 58  ALA B O     1 
ATOM   1468 C  CB    . ALA B 1 41  ? 9.451   5.509  21.542 1.00 23.28  ? 58  ALA B CB    1 
ATOM   1469 N  N     . ALA B 1 42  ? 12.277  5.475  23.336 1.00 20.79  ? 59  ALA B N     1 
ATOM   1470 C  CA    . ALA B 1 42  ? 13.375  4.667  23.853 1.00 20.99  ? 59  ALA B CA    1 
ATOM   1471 C  C     . ALA B 1 42  ? 14.593  5.555  24.033 1.00 20.23  ? 59  ALA B C     1 
ATOM   1472 O  O     . ALA B 1 42  ? 14.811  6.496  23.270 1.00 19.73  ? 59  ALA B O     1 
ATOM   1473 C  CB    . ALA B 1 42  ? 13.714  3.511  22.912 1.00 20.55  ? 59  ALA B CB    1 
ATOM   1474 N  N     . MET B 1 43  ? 15.388  5.239  25.043 1.00 20.83  ? 60  MET B N     1 
ATOM   1475 C  CA    . MET B 1 43  ? 16.592  6.004  25.322 1.00 20.86  ? 60  MET B CA    1 
ATOM   1476 C  C     . MET B 1 43  ? 17.493  5.127  26.168 1.00 24.59  ? 60  MET B C     1 
ATOM   1477 O  O     . MET B 1 43  ? 17.032  4.545  27.149 1.00 26.58  ? 60  MET B O     1 
ATOM   1478 C  CB    . MET B 1 43  ? 16.246  7.316  26.034 1.00 20.89  ? 60  MET B CB    1 
ATOM   1479 C  CG    . MET B 1 43  ? 17.409  8.287  26.240 1.00 23.37  ? 60  MET B CG    1 
ATOM   1480 S  SD    . MET B 1 43  ? 16.864  9.977  26.635 1.00 22.85  ? 60  MET B SD    1 
ATOM   1481 C  CE    . MET B 1 43  ? 16.541  10.611 24.980 1.00 18.95  ? 60  MET B CE    1 
ATOM   1482 N  N     . LYS B 1 44  ? 18.749  4.992  25.758 1.00 21.12  ? 61  LYS B N     1 
ATOM   1483 C  CA    . LYS B 1 44  ? 19.692  4.151  26.476 1.00 21.07  ? 61  LYS B CA    1 
ATOM   1484 C  C     . LYS B 1 44  ? 21.106  4.642  26.215 1.00 22.98  ? 61  LYS B C     1 
ATOM   1485 O  O     . LYS B 1 44  ? 21.482  4.847  25.059 1.00 24.09  ? 61  LYS B O     1 
ATOM   1486 C  CB    . LYS B 1 44  ? 19.532  2.692  26.010 1.00 30.74  ? 61  LYS B CB    1 
ATOM   1487 C  CG    . LYS B 1 44  ? 20.744  1.827  26.213 1.00 36.70  ? 61  LYS B CG    1 
ATOM   1488 C  CD    . LYS B 1 44  ? 20.401  0.386  25.929 1.00 36.49  ? 61  LYS B CD    1 
ATOM   1489 C  CE    . LYS B 1 44  ? 20.303  0.108  24.444 1.00 34.86  ? 61  LYS B CE    1 
ATOM   1490 N  NZ    . LYS B 1 44  ? 19.950  -1.327 24.227 1.00 43.42  ? 61  LYS B NZ    1 
ATOM   1491 N  N     . LEU B 1 45  ? 21.890  4.809  27.273 1.00 19.24  ? 62  LEU B N     1 
ATOM   1492 C  CA    . LEU B 1 45  ? 23.313  5.066  27.126 1.00 17.98  ? 62  LEU B CA    1 
ATOM   1493 C  C     . LEU B 1 45  ? 24.052  3.742  27.038 1.00 18.31  ? 62  LEU B C     1 
ATOM   1494 O  O     . LEU B 1 45  ? 23.838  2.847  27.868 1.00 20.62  ? 62  LEU B O     1 
ATOM   1495 C  CB    . LEU B 1 45  ? 23.853  5.869  28.301 1.00 20.16  ? 62  LEU B CB    1 
ATOM   1496 C  CG    . LEU B 1 45  ? 25.319  6.267  28.196 1.00 20.80  ? 62  LEU B CG    1 
ATOM   1497 C  CD1   . LEU B 1 45  ? 25.463  7.489  27.311 1.00 22.18  ? 62  LEU B CD1   1 
ATOM   1498 C  CD2   . LEU B 1 45  ? 25.912  6.520  29.587 1.00 22.98  ? 62  LEU B CD2   1 
ATOM   1499 N  N     . THR B 1 46  ? 24.920  3.612  26.047 1.00 18.72  ? 63  THR B N     1 
ATOM   1500 C  CA    . THR B 1 46  ? 25.797  2.449  25.996 1.00 22.98  ? 63  THR B CA    1 
ATOM   1501 C  C     . THR B 1 46  ? 27.162  2.902  25.504 1.00 22.96  ? 63  THR B C     1 
ATOM   1502 O  O     . THR B 1 46  ? 27.406  4.089  25.293 1.00 23.77  ? 63  THR B O     1 
ATOM   1503 C  CB    . THR B 1 46  ? 25.169  1.349  25.138 1.00 22.41  ? 63  THR B CB    1 
ATOM   1504 O  OG1   . THR B 1 46  ? 25.912  0.118  25.308 1.00 25.09  ? 63  THR B OG1   1 
ATOM   1505 C  CG2   . THR B 1 46  ? 25.129  1.721  23.661 1.00 23.55  ? 63  THR B CG2   1 
ATOM   1506 N  N     . ILE B 1 47  ? 28.088  1.963  25.362 1.00 21.07  ? 64  ILE B N     1 
ATOM   1507 C  CA    . ILE B 1 47  ? 29.360  2.242  24.706 1.00 21.63  ? 64  ILE B CA    1 
ATOM   1508 C  C     . ILE B 1 47  ? 29.397  1.411  23.438 1.00 24.13  ? 64  ILE B C     1 
ATOM   1509 O  O     . ILE B 1 47  ? 29.312  0.178  23.496 1.00 25.57  ? 64  ILE B O     1 
ATOM   1510 C  CB    . ILE B 1 47  ? 30.559  1.958  25.631 1.00 21.96  ? 64  ILE B CB    1 
ATOM   1511 C  CG1   . ILE B 1 47  ? 30.585  2.997  26.757 1.00 24.78  ? 64  ILE B CG1   1 
ATOM   1512 C  CG2   . ILE B 1 47  ? 31.866  2.014  24.844 1.00 27.53  ? 64  ILE B CG2   1 
ATOM   1513 C  CD1   . ILE B 1 47  ? 31.610  2.772  27.842 1.00 31.09  ? 64  ILE B CD1   1 
ATOM   1514 N  N     . ALA B 1 48  ? 29.466  2.092  22.294 1.00 21.15  ? 65  ALA B N     1 
ATOM   1515 C  CA    . ALA B 1 48  ? 29.472  1.408  21.017 1.00 22.10  ? 65  ALA B CA    1 
ATOM   1516 C  C     . ALA B 1 48  ? 30.790  0.661  20.862 1.00 23.38  ? 65  ALA B C     1 
ATOM   1517 O  O     . ALA B 1 48  ? 31.857  1.165  21.226 1.00 24.80  ? 65  ALA B O     1 
ATOM   1518 C  CB    . ALA B 1 48  ? 29.274  2.394  19.873 1.00 22.70  ? 65  ALA B CB    1 
ATOM   1519 N  N     . THR B 1 49  ? 30.699  -0.550 20.342 1.00 22.36  ? 66  THR B N     1 
ATOM   1520 C  CA    . THR B 1 49  ? 31.844  -1.401 20.078 1.00 23.23  ? 66  THR B CA    1 
ATOM   1521 C  C     . THR B 1 49  ? 32.010  -1.647 18.583 1.00 25.66  ? 66  THR B C     1 
ATOM   1522 O  O     . THR B 1 49  ? 31.055  -1.516 17.806 1.00 25.95  ? 66  THR B O     1 
ATOM   1523 C  CB    . THR B 1 49  ? 31.678  -2.758 20.770 1.00 23.39  ? 66  THR B CB    1 
ATOM   1524 O  OG1   . THR B 1 49  ? 30.578  -3.437 20.152 1.00 28.89  ? 66  THR B OG1   1 
ATOM   1525 C  CG2   . THR B 1 49  ? 31.433  -2.597 22.233 1.00 29.44  ? 66  THR B CG2   1 
ATOM   1526 N  N     . PRO B 1 50  ? 33.210  -2.033 18.145 1.00 26.01  ? 67  PRO B N     1 
ATOM   1527 C  CA    . PRO B 1 50  ? 33.415  -2.298 16.718 1.00 27.09  ? 67  PRO B CA    1 
ATOM   1528 C  C     . PRO B 1 50  ? 32.449  -3.310 16.117 1.00 25.40  ? 67  PRO B C     1 
ATOM   1529 O  O     . PRO B 1 50  ? 31.984  -3.103 14.994 1.00 27.76  ? 67  PRO B O     1 
ATOM   1530 C  CB    . PRO B 1 50  ? 34.865  -2.790 16.677 1.00 28.94  ? 67  PRO B CB    1 
ATOM   1531 C  CG    . PRO B 1 50  ? 35.509  -2.031 17.783 1.00 27.15  ? 67  PRO B CG    1 
ATOM   1532 C  CD    . PRO B 1 50  ? 34.487  -1.982 18.878 1.00 25.84  ? 67  PRO B CD    1 
ATOM   1533 N  N     . ALA B 1 51  ? 32.093  -4.371 16.841 1.00 26.32  ? 68  ALA B N     1 
ATOM   1534 C  CA    . ALA B 1 51  ? 31.209  -5.387 16.268 1.00 26.78  ? 68  ALA B CA    1 
ATOM   1535 C  C     . ALA B 1 51  ? 29.816  -4.835 15.973 1.00 23.54  ? 68  ALA B C     1 
ATOM   1536 O  O     . ALA B 1 51  ? 29.251  -5.100 14.904 1.00 27.94  ? 68  ALA B O     1 
ATOM   1537 C  CB    . ALA B 1 51  ? 31.123  -6.590 17.206 1.00 29.97  ? 68  ALA B CB    1 
ATOM   1538 N  N     . ILE B 1 52  ? 29.233  -4.080 16.913 1.00 26.34  ? 69  ILE B N     1 
ATOM   1539 C  CA    . ILE B 1 52  ? 27.909  -3.514 16.649 1.00 24.45  ? 69  ILE B CA    1 
ATOM   1540 C  C     . ILE B 1 52  ? 28.005  -2.414 15.596 1.00 22.97  ? 69  ILE B C     1 
ATOM   1541 O  O     . ILE B 1 52  ? 27.106  -2.263 14.761 1.00 24.36  ? 69  ILE B O     1 
ATOM   1542 C  CB    . ILE B 1 52  ? 27.247  -3.025 17.955 1.00 29.93  ? 69  ILE B CB    1 
ATOM   1543 C  CG1   . ILE B 1 52  ? 25.809  -2.550 17.682 1.00 35.08  ? 69  ILE B CG1   1 
ATOM   1544 C  CG2   . ILE B 1 52  ? 28.041  -1.905 18.575 1.00 32.98  ? 69  ILE B CG2   1 
ATOM   1545 C  CD1   . ILE B 1 52  ? 24.793  -2.966 18.758 1.00 39.84  ? 69  ILE B CD1   1 
ATOM   1546 N  N     . LEU B 1 53  ? 29.082  -1.623 15.625 1.00 24.60  ? 70  LEU B N     1 
ATOM   1547 C  CA    . LEU B 1 53  ? 29.234  -0.565 14.622 1.00 30.76  ? 70  LEU B CA    1 
ATOM   1548 C  C     . LEU B 1 53  ? 29.429  -1.132 13.227 1.00 30.05  ? 70  LEU B C     1 
ATOM   1549 O  O     . LEU B 1 53  ? 29.014  -0.508 12.241 1.00 29.88  ? 70  LEU B O     1 
ATOM   1550 C  CB    . LEU B 1 53  ? 30.409  0.337  14.975 1.00 25.21  ? 70  LEU B CB    1 
ATOM   1551 C  CG    . LEU B 1 53  ? 30.192  1.149  16.245 1.00 24.01  ? 70  LEU B CG    1 
ATOM   1552 C  CD1   . LEU B 1 53  ? 31.493  1.726  16.722 1.00 23.45  ? 70  LEU B CD1   1 
ATOM   1553 C  CD2   . LEU B 1 53  ? 29.146  2.260  15.961 1.00 27.97  ? 70  LEU B CD2   1 
ATOM   1554 N  N     . GLU B 1 54  ? 30.071  -2.298 13.105 1.00 26.98  ? 71  GLU B N     1 
ATOM   1555 C  CA    . GLU B 1 54  ? 30.155  -2.928 11.793 1.00 28.71  ? 71  GLU B CA    1 
ATOM   1556 C  C     . GLU B 1 54  ? 28.773  -3.264 11.248 1.00 27.85  ? 71  GLU B C     1 
ATOM   1557 O  O     . GLU B 1 54  ? 28.516  -3.085 10.052 1.00 32.71  ? 71  GLU B O     1 
ATOM   1558 C  CB    . GLU B 1 54  ? 31.018  -4.179 11.865 1.00 31.29  ? 71  GLU B CB    1 
ATOM   1559 C  CG    . GLU B 1 54  ? 32.486  -3.883 11.885 1.00 41.73  ? 71  GLU B CG    1 
ATOM   1560 C  CD    . GLU B 1 54  ? 33.301  -5.141 12.088 1.00 73.47  ? 71  GLU B CD    1 
ATOM   1561 O  OE1   . GLU B 1 54  ? 32.969  -6.167 11.447 1.00 69.70  ? 71  GLU B OE1   1 
ATOM   1562 O  OE2   . GLU B 1 54  ? 34.252  -5.106 12.902 1.00 68.10  ? 71  GLU B OE2   1 
ATOM   1563 N  N     . GLU B 1 55  ? 27.872  -3.767 12.098 1.00 28.95  ? 72  GLU B N     1 
ATOM   1564 C  CA    A GLU B 1 55  ? 26.502  -4.025 11.663 0.33 31.28  ? 72  GLU B CA    1 
ATOM   1565 C  CA    B GLU B 1 55  ? 26.516  -4.028 11.630 0.67 31.20  ? 72  GLU B CA    1 
ATOM   1566 C  C     . GLU B 1 55  ? 25.776  -2.726 11.337 1.00 32.29  ? 72  GLU B C     1 
ATOM   1567 O  O     . GLU B 1 55  ? 25.054  -2.637 10.340 1.00 34.65  ? 72  GLU B O     1 
ATOM   1568 C  CB    A GLU B 1 55  ? 25.732  -4.776 12.747 0.33 33.86  ? 72  GLU B CB    1 
ATOM   1569 C  CB    B GLU B 1 55  ? 25.740  -4.859 12.649 0.67 33.79  ? 72  GLU B CB    1 
ATOM   1570 C  CG    A GLU B 1 55  ? 26.274  -6.145 13.096 0.33 40.99  ? 72  GLU B CG    1 
ATOM   1571 C  CG    B GLU B 1 55  ? 26.310  -6.250 12.906 0.67 41.59  ? 72  GLU B CG    1 
ATOM   1572 C  CD    A GLU B 1 55  ? 25.290  -7.249 12.773 0.33 40.68  ? 72  GLU B CD    1 
ATOM   1573 C  CD    B GLU B 1 55  ? 26.288  -7.153 11.681 0.67 40.74  ? 72  GLU B CD    1 
ATOM   1574 O  OE1   A GLU B 1 55  ? 24.783  -7.275 11.631 0.33 44.27  ? 72  GLU B OE1   1 
ATOM   1575 O  OE1   B GLU B 1 55  ? 25.701  -6.762 10.648 0.67 39.61  ? 72  GLU B OE1   1 
ATOM   1576 O  OE2   A GLU B 1 55  ? 25.012  -8.079 13.664 0.33 44.39  ? 72  GLU B OE2   1 
ATOM   1577 O  OE2   B GLU B 1 55  ? 26.856  -8.263 11.760 0.67 49.25  ? 72  GLU B OE2   1 
ATOM   1578 N  N     . HIS B 1 56  ? 25.938  -1.714 12.194 1.00 28.23  ? 73  HIS B N     1 
ATOM   1579 C  CA    . HIS B 1 56  ? 25.284  -0.429 11.960 1.00 26.72  ? 73  HIS B CA    1 
ATOM   1580 C  C     . HIS B 1 56  ? 25.703  0.155  10.617 1.00 28.95  ? 73  HIS B C     1 
ATOM   1581 O  O     . HIS B 1 56  ? 24.857  0.622  9.837  1.00 31.84  ? 73  HIS B O     1 
ATOM   1582 C  CB    . HIS B 1 56  ? 25.627  0.516  13.108 1.00 26.51  ? 73  HIS B CB    1 
ATOM   1583 C  CG    . HIS B 1 56  ? 25.065  1.894  12.953 1.00 27.79  ? 73  HIS B CG    1 
ATOM   1584 N  ND1   . HIS B 1 56  ? 23.747  2.182  13.214 1.00 30.22  ? 73  HIS B ND1   1 
ATOM   1585 C  CD2   . HIS B 1 56  ? 25.646  3.061  12.583 1.00 36.05  ? 73  HIS B CD2   1 
ATOM   1586 C  CE1   . HIS B 1 56  ? 23.531  3.472  12.995 1.00 30.14  ? 73  HIS B CE1   1 
ATOM   1587 N  NE2   . HIS B 1 56  ? 24.669  4.028  12.619 1.00 33.65  ? 73  HIS B NE2   1 
ATOM   1588 N  N     . TYR B 1 57  ? 27.000  0.112  10.316 1.00 28.22  ? 74  TYR B N     1 
ATOM   1589 C  CA    . TYR B 1 57  ? 27.564  0.675  9.085  1.00 28.29  ? 74  TYR B CA    1 
ATOM   1590 C  C     . TYR B 1 57  ? 27.794  -0.390 8.024  1.00 36.94  ? 74  TYR B C     1 
ATOM   1591 O  O     . TYR B 1 57  ? 28.764  -0.334 7.255  1.00 39.80  ? 74  TYR B O     1 
ATOM   1592 C  CB    . TYR B 1 57  ? 28.865  1.407  9.399  1.00 37.31  ? 74  TYR B CB    1 
ATOM   1593 C  CG    . TYR B 1 57  ? 28.667  2.719  10.121 1.00 38.83  ? 74  TYR B CG    1 
ATOM   1594 C  CD1   . TYR B 1 57  ? 27.762  3.667  9.652  1.00 37.24  ? 74  TYR B CD1   1 
ATOM   1595 C  CD2   . TYR B 1 57  ? 29.377  3.009  11.284 1.00 37.77  ? 74  TYR B CD2   1 
ATOM   1596 C  CE1   . TYR B 1 57  ? 27.569  4.873  10.313 1.00 42.12  ? 74  TYR B CE1   1 
ATOM   1597 C  CE2   . TYR B 1 57  ? 29.187  4.218  11.958 1.00 39.20  ? 74  TYR B CE2   1 
ATOM   1598 C  CZ    . TYR B 1 57  ? 28.288  5.145  11.464 1.00 42.96  ? 74  TYR B CZ    1 
ATOM   1599 O  OH    . TYR B 1 57  ? 28.083  6.347  12.111 1.00 49.63  ? 74  TYR B OH    1 
ATOM   1600 N  N     . ALA B 1 58  ? 26.906  -1.381 7.971  1.00 32.04  ? 75  ALA B N     1 
ATOM   1601 C  CA    . ALA B 1 58  ? 27.107  -2.498 7.061  1.00 36.74  ? 75  ALA B CA    1 
ATOM   1602 C  C     . ALA B 1 58  ? 27.144  -2.028 5.615  1.00 40.88  ? 75  ALA B C     1 
ATOM   1603 O  O     . ALA B 1 58  ? 27.887  -2.586 4.798  1.00 42.98  ? 75  ALA B O     1 
ATOM   1604 C  CB    . ALA B 1 58  ? 26.009  -3.538 7.261  1.00 35.31  ? 75  ALA B CB    1 
ATOM   1605 N  N     . GLU B 1 59  ? 26.371  -0.993 5.279  1.00 41.18  ? 76  GLU B N     1 
ATOM   1606 C  CA    . GLU B 1 59  ? 26.384  -0.527 3.895  1.00 41.82  ? 76  GLU B CA    1 
ATOM   1607 C  C     . GLU B 1 59  ? 27.791  -0.118 3.466  1.00 51.72  ? 76  GLU B C     1 
ATOM   1608 O  O     . GLU B 1 59  ? 28.149  -0.268 2.294  1.00 53.60  ? 76  GLU B O     1 
ATOM   1609 C  CB    . GLU B 1 59  ? 25.374  0.616  3.706  1.00 44.22  ? 76  GLU B CB    1 
ATOM   1610 C  CG    . GLU B 1 59  ? 25.634  1.890  4.493  1.00 51.34  ? 76  GLU B CG    1 
ATOM   1611 C  CD    . GLU B 1 59  ? 24.488  2.899  4.377  1.00 69.76  ? 76  GLU B CD    1 
ATOM   1612 O  OE1   . GLU B 1 59  ? 24.196  3.347  3.240  1.00 49.11  ? 76  GLU B OE1   1 
ATOM   1613 O  OE2   . GLU B 1 59  ? 23.869  3.234  5.418  1.00 52.50  ? 76  GLU B OE2   1 
ATOM   1614 N  N     . HIS B 1 60  ? 28.626  0.325  4.407  1.00 50.00  ? 77  HIS B N     1 
ATOM   1615 C  CA    . HIS B 1 60  ? 29.965  0.806  4.094  1.00 45.90  ? 77  HIS B CA    1 
ATOM   1616 C  C     . HIS B 1 60  ? 31.040  -0.250 4.286  1.00 44.17  ? 77  HIS B C     1 
ATOM   1617 O  O     . HIS B 1 60  ? 32.229  0.089  4.325  1.00 45.64  ? 77  HIS B O     1 
ATOM   1618 C  CB    . HIS B 1 60  ? 30.291  2.034  4.946  1.00 49.42  ? 77  HIS B CB    1 
ATOM   1619 C  CG    . HIS B 1 60  ? 29.230  3.091  4.920  1.00 53.66  ? 77  HIS B CG    1 
ATOM   1620 N  ND1   . HIS B 1 60  ? 28.754  3.645  3.752  1.00 48.14  ? 77  HIS B ND1   1 
ATOM   1621 C  CD2   . HIS B 1 60  ? 28.561  3.702  5.926  1.00 47.71  ? 77  HIS B CD2   1 
ATOM   1622 C  CE1   . HIS B 1 60  ? 27.835  4.551  4.039  1.00 54.00  ? 77  HIS B CE1   1 
ATOM   1623 N  NE2   . HIS B 1 60  ? 27.697  4.602  5.352  1.00 61.37  ? 77  HIS B NE2   1 
ATOM   1624 N  N     . LYS B 1 61  ? 30.662  -1.519 4.412  1.00 39.34  ? 78  LYS B N     1 
ATOM   1625 C  CA    . LYS B 1 61  ? 31.652  -2.569 4.581  1.00 42.30  ? 78  LYS B CA    1 
ATOM   1626 C  C     . LYS B 1 61  ? 32.669  -2.524 3.446  1.00 56.89  ? 78  LYS B C     1 
ATOM   1627 O  O     . LYS B 1 61  ? 32.324  -2.272 2.291  1.00 55.20  ? 78  LYS B O     1 
ATOM   1628 C  CB    . LYS B 1 61  ? 30.970  -3.938 4.620  1.00 54.03  ? 78  LYS B CB    1 
ATOM   1629 C  CG    . LYS B 1 61  ? 31.933  -5.102 4.874  1.00 54.81  ? 78  LYS B CG    1 
ATOM   1630 C  CD    . LYS B 1 61  ? 31.234  -6.467 4.802  1.00 71.13  ? 78  LYS B CD    1 
ATOM   1631 C  CE    . LYS B 1 61  ? 31.684  -7.275 3.578  1.00 75.26  ? 78  LYS B CE    1 
ATOM   1632 N  NZ    . LYS B 1 61  ? 30.794  -8.442 3.276  1.00 72.74  ? 78  LYS B NZ    1 
ATOM   1633 N  N     . GLY B 1 62  ? 33.940  -2.722 3.794  1.00 60.16  ? 79  GLY B N     1 
ATOM   1634 C  CA    . GLY B 1 62  ? 35.003  -2.811 2.815  1.00 68.48  ? 79  GLY B CA    1 
ATOM   1635 C  C     . GLY B 1 62  ? 35.561  -1.488 2.337  1.00 65.23  ? 79  GLY B C     1 
ATOM   1636 O  O     . GLY B 1 62  ? 36.647  -1.469 1.746  1.00 62.85  ? 79  GLY B O     1 
ATOM   1637 N  N     . LYS B 1 63  ? 34.868  -0.381 2.579  1.00 50.84  ? 80  LYS B N     1 
ATOM   1638 C  CA    . LYS B 1 63  ? 35.344  0.911  2.123  1.00 46.86  ? 80  LYS B CA    1 
ATOM   1639 C  C     . LYS B 1 63  ? 36.530  1.377  2.965  1.00 62.19  ? 80  LYS B C     1 
ATOM   1640 O  O     . LYS B 1 63  ? 36.728  0.916  4.093  1.00 58.64  ? 80  LYS B O     1 
ATOM   1641 C  CB    . LYS B 1 63  ? 34.209  1.926  2.165  1.00 48.58  ? 80  LYS B CB    1 
ATOM   1642 C  CG    . LYS B 1 63  ? 33.015  1.473  1.343  1.00 51.34  ? 80  LYS B CG    1 
ATOM   1643 C  CD    . LYS B 1 63  ? 31.855  2.449  1.363  1.00 50.41  ? 80  LYS B CD    1 
ATOM   1644 C  CE    . LYS B 1 63  ? 30.686  1.860  0.591  1.00 56.43  ? 80  LYS B CE    1 
ATOM   1645 N  NZ    . LYS B 1 63  ? 29.436  2.664  0.712  1.00 64.03  ? 80  LYS B NZ    1 
ATOM   1646 N  N     . PRO B 1 64  ? 37.349  2.288  2.426  1.00 86.49  ? 81  PRO B N     1 
ATOM   1647 C  CA    . PRO B 1 64  ? 38.575  2.679  3.137  1.00 80.83  ? 81  PRO B CA    1 
ATOM   1648 C  C     . PRO B 1 64  ? 38.349  3.615  4.309  1.00 62.80  ? 81  PRO B C     1 
ATOM   1649 O  O     . PRO B 1 64  ? 39.226  3.699  5.179  1.00 59.97  ? 81  PRO B O     1 
ATOM   1650 C  CB    . PRO B 1 64  ? 39.405  3.369  2.046  1.00 86.11  ? 81  PRO B CB    1 
ATOM   1651 C  CG    . PRO B 1 64  ? 38.378  3.949  1.130  1.00 84.39  ? 81  PRO B CG    1 
ATOM   1652 C  CD    . PRO B 1 64  ? 37.230  2.966  1.121  1.00 80.36  ? 81  PRO B CD    1 
ATOM   1653 N  N     . PHE B 1 65  ? 37.230  4.332  4.355  1.00 52.32  ? 82  PHE B N     1 
ATOM   1654 C  CA    . PHE B 1 65  ? 36.977  5.254  5.449  1.00 58.74  ? 82  PHE B CA    1 
ATOM   1655 C  C     . PHE B 1 65  ? 36.306  4.590  6.644  1.00 61.90  ? 82  PHE B C     1 
ATOM   1656 O  O     . PHE B 1 65  ? 36.222  5.215  7.710  1.00 50.49  ? 82  PHE B O     1 
ATOM   1657 C  CB    . PHE B 1 65  ? 36.119  6.428  4.967  1.00 55.08  ? 82  PHE B CB    1 
ATOM   1658 C  CG    . PHE B 1 65  ? 34.703  6.061  4.635  1.00 65.98  ? 82  PHE B CG    1 
ATOM   1659 C  CD1   . PHE B 1 65  ? 34.384  5.513  3.402  1.00 70.12  ? 82  PHE B CD1   1 
ATOM   1660 C  CD2   . PHE B 1 65  ? 33.685  6.290  5.545  1.00 63.01  ? 82  PHE B CD2   1 
ATOM   1661 C  CE1   . PHE B 1 65  ? 33.078  5.182  3.090  1.00 63.74  ? 82  PHE B CE1   1 
ATOM   1662 C  CE2   . PHE B 1 65  ? 32.376  5.967  5.238  1.00 67.85  ? 82  PHE B CE2   1 
ATOM   1663 C  CZ    . PHE B 1 65  ? 32.073  5.412  4.008  1.00 72.21  ? 82  PHE B CZ    1 
ATOM   1664 N  N     . LEU B 1 66  ? 35.845  3.346  6.503  1.00 56.51  ? 83  LEU B N     1 
ATOM   1665 C  CA    . LEU B 1 66  ? 35.138  2.697  7.605  1.00 52.06  ? 83  LEU B CA    1 
ATOM   1666 C  C     . LEU B 1 66  ? 36.018  2.492  8.830  1.00 46.94  ? 83  LEU B C     1 
ATOM   1667 O  O     . LEU B 1 66  ? 35.542  2.742  9.951  1.00 36.20  ? 83  LEU B O     1 
ATOM   1668 C  CB    . LEU B 1 66  ? 34.545  1.363  7.137  1.00 44.84  ? 83  LEU B CB    1 
ATOM   1669 C  CG    . LEU B 1 66  ? 33.665  0.645  8.161  1.00 44.24  ? 83  LEU B CG    1 
ATOM   1670 C  CD1   . LEU B 1 66  ? 32.459  1.492  8.496  1.00 38.00  ? 83  LEU B CD1   1 
ATOM   1671 C  CD2   . LEU B 1 66  ? 33.234  -0.728 7.675  1.00 45.58  ? 83  LEU B CD2   1 
ATOM   1672 N  N     . PRO B 1 67  ? 37.260  2.029  8.717  1.00 40.33  ? 84  PRO B N     1 
ATOM   1673 C  CA    . PRO B 1 67  ? 38.046  1.801  9.941  1.00 34.84  ? 84  PRO B CA    1 
ATOM   1674 C  C     . PRO B 1 67  ? 38.150  3.037  10.824 1.00 41.15  ? 84  PRO B C     1 
ATOM   1675 O  O     . PRO B 1 67  ? 38.006  2.936  12.050 1.00 37.37  ? 84  PRO B O     1 
ATOM   1676 C  CB    . PRO B 1 67  ? 39.407  1.363  9.397  1.00 47.39  ? 84  PRO B CB    1 
ATOM   1677 C  CG    . PRO B 1 67  ? 39.096  0.797  8.046  1.00 39.34  ? 84  PRO B CG    1 
ATOM   1678 C  CD    . PRO B 1 67  ? 37.988  1.614  7.505  1.00 50.91  ? 84  PRO B CD    1 
ATOM   1679 N  N     . GLY B 1 68  ? 38.360  4.214  10.232 1.00 42.97  ? 85  GLY B N     1 
ATOM   1680 C  CA    . GLY B 1 68  ? 38.447  5.424  11.026 1.00 43.60  ? 85  GLY B CA    1 
ATOM   1681 C  C     . GLY B 1 68  ? 37.097  5.879  11.527 1.00 37.98  ? 85  GLY B C     1 
ATOM   1682 O  O     . GLY B 1 68  ? 36.991  6.440  12.622 1.00 35.47  ? 85  GLY B O     1 
ATOM   1683 N  N     . LEU B 1 69  ? 36.050  5.640  10.746 1.00 38.29  ? 86  LEU B N     1 
ATOM   1684 C  CA    . LEU B 1 69  ? 34.704  5.877  11.236 1.00 34.08  ? 86  LEU B CA    1 
ATOM   1685 C  C     . LEU B 1 69  ? 34.427  5.037  12.481 1.00 31.99  ? 86  LEU B C     1 
ATOM   1686 O  O     . LEU B 1 69  ? 33.913  5.538  13.489 1.00 29.99  ? 86  LEU B O     1 
ATOM   1687 C  CB    . LEU B 1 69  ? 33.706  5.560  10.126 1.00 42.12  ? 86  LEU B CB    1 
ATOM   1688 C  CG    . LEU B 1 69  ? 32.237  5.540  10.537 1.00 38.28  ? 86  LEU B CG    1 
ATOM   1689 C  CD1   . LEU B 1 69  ? 31.816  6.860  11.166 1.00 46.46  ? 86  LEU B CD1   1 
ATOM   1690 C  CD2   . LEU B 1 69  ? 31.398  5.233  9.310  1.00 53.37  ? 86  LEU B CD2   1 
ATOM   1691 N  N     . ILE B 1 70  ? 34.774  3.754  12.432 1.00 31.68  ? 87  ILE B N     1 
ATOM   1692 C  CA    A ILE B 1 70  ? 34.524  2.889  13.578 0.67 29.23  ? 87  ILE B CA    1 
ATOM   1693 C  CA    B ILE B 1 70  ? 34.536  2.878  13.575 0.33 29.31  ? 87  ILE B CA    1 
ATOM   1694 C  C     . ILE B 1 70  ? 35.325  3.368  14.781 1.00 30.75  ? 87  ILE B C     1 
ATOM   1695 O  O     . ILE B 1 70  ? 34.816  3.390  15.913 1.00 26.05  ? 87  ILE B O     1 
ATOM   1696 C  CB    A ILE B 1 70  ? 34.822  1.425  13.206 0.67 30.74  ? 87  ILE B CB    1 
ATOM   1697 C  CB    B ILE B 1 70  ? 34.890  1.424  13.210 0.33 30.75  ? 87  ILE B CB    1 
ATOM   1698 C  CG1   A ILE B 1 70  ? 33.754  0.947  12.208 0.67 33.18  ? 87  ILE B CG1   1 
ATOM   1699 C  CG1   B ILE B 1 70  ? 34.042  0.941  12.025 0.33 34.16  ? 87  ILE B CG1   1 
ATOM   1700 C  CG2   A ILE B 1 70  ? 34.863  0.554  14.453 0.67 30.57  ? 87  ILE B CG2   1 
ATOM   1701 C  CG2   B ILE B 1 70  ? 34.698  0.515  14.407 0.33 30.61  ? 87  ILE B CG2   1 
ATOM   1702 C  CD1   A ILE B 1 70  ? 33.891  -0.494 11.758 0.67 33.20  ? 87  ILE B CD1   1 
ATOM   1703 C  CD1   B ILE B 1 70  ? 32.554  0.889  12.288 0.33 27.80  ? 87  ILE B CD1   1 
ATOM   1704 N  N     . GLU B 1 71  ? 36.573  3.790  14.562 1.00 27.43  ? 88  GLU B N     1 
ATOM   1705 C  CA    . GLU B 1 71  ? 37.374  4.289  15.682 1.00 31.96  ? 88  GLU B CA    1 
ATOM   1706 C  C     . GLU B 1 71  ? 36.720  5.497  16.332 1.00 35.00  ? 88  GLU B C     1 
ATOM   1707 O  O     . GLU B 1 71  ? 36.609  5.570  17.565 1.00 33.10  ? 88  GLU B O     1 
ATOM   1708 C  CB    . GLU B 1 71  ? 38.777  4.662  15.222 1.00 35.88  ? 88  GLU B CB    1 
ATOM   1709 C  CG    . GLU B 1 71  ? 39.760  3.513  15.188 1.00 54.98  ? 88  GLU B CG    1 
ATOM   1710 C  CD    . GLU B 1 71  ? 41.092  3.932  14.593 1.00 79.22  ? 88  GLU B CD    1 
ATOM   1711 O  OE1   . GLU B 1 71  ? 41.655  4.948  15.061 1.00 65.55  ? 88  GLU B OE1   1 
ATOM   1712 O  OE2   . GLU B 1 71  ? 41.563  3.260  13.647 1.00 80.33  ? 88  GLU B OE2   1 
ATOM   1713 N  N     . LYS B 1 72  ? 36.287  6.468  15.522 1.00 31.35  ? 89  LYS B N     1 
ATOM   1714 C  CA    A LYS B 1 72  ? 35.703  7.664  16.112 0.58 29.86  ? 89  LYS B CA    1 
ATOM   1715 C  CA    B LYS B 1 72  ? 35.679  7.672  16.081 0.42 29.92  ? 89  LYS B CA    1 
ATOM   1716 C  C     . LYS B 1 72  ? 34.392  7.351  16.820 1.00 31.24  ? 89  LYS B C     1 
ATOM   1717 O  O     . LYS B 1 72  ? 34.066  8.009  17.810 1.00 27.53  ? 89  LYS B O     1 
ATOM   1718 C  CB    A LYS B 1 72  ? 35.520  8.745  15.047 0.58 31.46  ? 89  LYS B CB    1 
ATOM   1719 C  CB    B LYS B 1 72  ? 35.393  8.695  14.983 0.42 31.52  ? 89  LYS B CB    1 
ATOM   1720 C  CG    A LYS B 1 72  ? 36.862  9.178  14.469 0.58 41.39  ? 89  LYS B CG    1 
ATOM   1721 C  CG    B LYS B 1 72  ? 36.624  9.160  14.244 0.42 41.18  ? 89  LYS B CG    1 
ATOM   1722 C  CD    A LYS B 1 72  ? 36.775  10.374 13.539 0.58 40.78  ? 89  LYS B CD    1 
ATOM   1723 C  CD    B LYS B 1 72  ? 36.630  10.664 14.070 0.42 39.86  ? 89  LYS B CD    1 
ATOM   1724 C  CE    A LYS B 1 72  ? 38.129  10.606 12.866 0.58 44.49  ? 89  LYS B CE    1 
ATOM   1725 C  CE    B LYS B 1 72  ? 37.412  11.050 12.840 0.42 45.71  ? 89  LYS B CE    1 
ATOM   1726 N  NZ    A LYS B 1 72  ? 39.246  10.684 13.857 0.58 52.39  ? 89  LYS B NZ    1 
ATOM   1727 N  NZ    B LYS B 1 72  ? 36.650  10.767 11.591 0.42 52.61  ? 89  LYS B NZ    1 
ATOM   1728 N  N     . MET B 1 73  ? 33.656  6.335  16.360 1.00 26.07  ? 90  MET B N     1 
ATOM   1729 C  CA    . MET B 1 73  ? 32.376  5.976  16.961 1.00 23.16  ? 90  MET B CA    1 
ATOM   1730 C  C     . MET B 1 73  ? 32.506  5.034  18.161 1.00 22.96  ? 90  MET B C     1 
ATOM   1731 O  O     . MET B 1 73  ? 31.499  4.812  18.847 1.00 22.86  ? 90  MET B O     1 
ATOM   1732 C  CB    . MET B 1 73  ? 31.468  5.318  15.913 1.00 28.31  ? 90  MET B CB    1 
ATOM   1733 C  CG    . MET B 1 73  ? 30.840  6.303  14.909 1.00 30.70  ? 90  MET B CG    1 
ATOM   1734 S  SD    . MET B 1 73  ? 29.684  7.424  15.707 1.00 27.82  ? 90  MET B SD    1 
ATOM   1735 C  CE    . MET B 1 73  ? 28.493  6.301  16.430 1.00 33.58  ? 90  MET B CE    1 
ATOM   1736 N  N     . THR B 1 74  ? 33.700  4.489  18.430 1.00 23.93  ? 91  THR B N     1 
ATOM   1737 C  CA    . THR B 1 74  ? 33.928  3.603  19.583 1.00 23.96  ? 91  THR B CA    1 
ATOM   1738 C  C     . THR B 1 74  ? 34.046  4.471  20.833 1.00 24.76  ? 91  THR B C     1 
ATOM   1739 O  O     . THR B 1 74  ? 35.094  5.050  21.125 1.00 31.30  ? 91  THR B O     1 
ATOM   1740 C  CB    . THR B 1 74  ? 35.167  2.738  19.380 1.00 24.15  ? 91  THR B CB    1 
ATOM   1741 O  OG1   . THR B 1 74  ? 35.034  2.002  18.160 1.00 26.44  ? 91  THR B OG1   1 
ATOM   1742 C  CG2   . THR B 1 74  ? 35.314  1.725  20.504 1.00 24.28  ? 91  THR B CG2   1 
ATOM   1743 N  N     . GLY B 1 75  ? 32.979  4.522  21.589 1.00 21.21  ? 92  GLY B N     1 
ATOM   1744 C  CA    . GLY B 1 75  ? 32.842  5.499  22.636 1.00 21.33  ? 92  GLY B CA    1 
ATOM   1745 C  C     . GLY B 1 75  ? 31.418  5.480  23.122 1.00 17.93  ? 92  GLY B C     1 
ATOM   1746 O  O     . GLY B 1 75  ? 30.569  4.744  22.604 1.00 18.22  ? 92  GLY B O     1 
ATOM   1747 N  N     . PRO B 1 76  ? 31.143  6.258  24.171 1.00 17.47  ? 93  PRO B N     1 
ATOM   1748 C  CA    . PRO B 1 76  ? 29.768  6.365  24.671 1.00 17.91  ? 93  PRO B CA    1 
ATOM   1749 C  C     . PRO B 1 76  ? 28.870  6.956  23.602 1.00 15.80  ? 93  PRO B C     1 
ATOM   1750 O  O     . PRO B 1 76  ? 29.272  7.862  22.869 1.00 19.61  ? 93  PRO B O     1 
ATOM   1751 C  CB    . PRO B 1 76  ? 29.899  7.301  25.878 1.00 19.19  ? 93  PRO B CB    1 
ATOM   1752 C  CG    . PRO B 1 76  ? 31.103  8.138  25.550 1.00 18.42  ? 93  PRO B CG    1 
ATOM   1753 C  CD    . PRO B 1 76  ? 32.058  7.171  24.873 1.00 22.06  ? 93  PRO B CD    1 
ATOM   1754 N  N     . VAL B 1 77  ? 27.667  6.405  23.505 1.00 18.28  ? 94  VAL B N     1 
ATOM   1755 C  CA    . VAL B 1 77  ? 26.625  6.921  22.628 1.00 17.05  ? 94  VAL B CA    1 
ATOM   1756 C  C     . VAL B 1 77  ? 25.297  6.890  23.362 1.00 20.44  ? 94  VAL B C     1 
ATOM   1757 O  O     . VAL B 1 77  ? 25.094  6.094  24.283 1.00 19.60  ? 94  VAL B O     1 
ATOM   1758 C  CB    . VAL B 1 77  ? 26.504  6.131  21.310 1.00 17.03  ? 94  VAL B CB    1 
ATOM   1759 C  CG1   . VAL B 1 77  ? 27.775  6.277  20.491 1.00 18.31  ? 94  VAL B CG1   1 
ATOM   1760 C  CG2   . VAL B 1 77  ? 26.158  4.647  21.572 1.00 22.22  ? 94  VAL B CG2   1 
ATOM   1761 N  N     . LEU B 1 78  ? 24.383  7.788  22.968 1.00 18.03  ? 95  LEU B N     1 
ATOM   1762 C  CA    . LEU B 1 78  ? 23.008  7.743  23.455 1.00 17.48  ? 95  LEU B CA    1 
ATOM   1763 C  C     . LEU B 1 78  ? 22.115  7.247  22.323 1.00 18.62  ? 95  LEU B C     1 
ATOM   1764 O  O     . LEU B 1 78  ? 21.912  7.942  21.314 1.00 19.42  ? 95  LEU B O     1 
ATOM   1765 C  CB    . LEU B 1 78  ? 22.530  9.096  23.990 1.00 15.65  ? 95  LEU B CB    1 
ATOM   1766 C  CG    . LEU B 1 78  ? 21.240  8.984  24.794 1.00 16.13  ? 95  LEU B CG    1 
ATOM   1767 C  CD1   . LEU B 1 78  ? 21.467  8.279  26.099 1.00 19.51  ? 95  LEU B CD1   1 
ATOM   1768 C  CD2   . LEU B 1 78  ? 20.635  10.337 25.106 1.00 16.57  ? 95  LEU B CD2   1 
ATOM   1769 N  N     . CYS B 1 79  ? 21.601  6.036  22.495 1.00 19.12  ? 96  CYS B N     1 
ATOM   1770 C  CA    . CYS B 1 79  ? 20.638  5.443  21.588 1.00 18.97  ? 96  CYS B CA    1 
ATOM   1771 C  C     . CYS B 1 79  ? 19.257  6.007  21.896 1.00 19.05  ? 96  CYS B C     1 
ATOM   1772 O  O     . CYS B 1 79  ? 18.834  6.021  23.056 1.00 19.60  ? 96  CYS B O     1 
ATOM   1773 C  CB    . CYS B 1 79  ? 20.637  3.930  21.766 1.00 19.87  ? 96  CYS B CB    1 
ATOM   1774 S  SG    . CYS B 1 79  ? 22.289  3.191  21.703 1.00 22.71  ? 96  CYS B SG    1 
ATOM   1775 N  N     . MET B 1 80  ? 18.543  6.453  20.865 1.00 17.51  ? 97  MET B N     1 
ATOM   1776 C  CA    . MET B 1 80  ? 17.223  7.038  21.059 1.00 17.58  ? 97  MET B CA    1 
ATOM   1777 C  C     . MET B 1 80  ? 16.256  6.565  19.981 1.00 18.71  ? 97  MET B C     1 
ATOM   1778 O  O     . MET B 1 80  ? 16.640  6.308  18.838 1.00 17.22  ? 97  MET B O     1 
ATOM   1779 C  CB    . MET B 1 80  ? 17.300  8.574  21.050 1.00 15.13  ? 97  MET B CB    1 
ATOM   1780 C  CG    . MET B 1 80  ? 18.423  9.134  21.902 1.00 19.49  ? 97  MET B CG    1 
ATOM   1781 S  SD    . MET B 1 80  ? 18.501  10.934 21.932 1.00 18.60  ? 97  MET B SD    1 
ATOM   1782 C  CE    . MET B 1 80  ? 18.846  11.272 20.214 1.00 19.84  ? 97  MET B CE    1 
ATOM   1783 N  N     . VAL B 1 81  ? 14.983  6.469  20.344 1.00 17.82  ? 98  VAL B N     1 
ATOM   1784 C  CA    . VAL B 1 81  ? 13.905  6.338  19.367 1.00 18.22  ? 98  VAL B CA    1 
ATOM   1785 C  C     . VAL B 1 81  ? 12.935  7.485  19.604 1.00 16.50  ? 98  VAL B C     1 
ATOM   1786 O  O     . VAL B 1 81  ? 12.430  7.654  20.718 1.00 17.03  ? 98  VAL B O     1 
ATOM   1787 C  CB    . VAL B 1 81  ? 13.176  4.990  19.462 1.00 18.32  ? 98  VAL B CB    1 
ATOM   1788 C  CG1   . VAL B 1 81  ? 11.991  4.990  18.532 1.00 19.72  ? 98  VAL B CG1   1 
ATOM   1789 C  CG2   . VAL B 1 81  ? 14.118  3.829  19.133 1.00 20.66  ? 98  VAL B CG2   1 
ATOM   1790 N  N     . PHE B 1 82  ? 12.693  8.298  18.573 1.00 15.75  ? 99  PHE B N     1 
ATOM   1791 C  CA    . PHE B 1 82  ? 11.674  9.335  18.644 1.00 15.67  ? 99  PHE B CA    1 
ATOM   1792 C  C     . PHE B 1 82  ? 10.499  9.023  17.725 1.00 17.67  ? 99  PHE B C     1 
ATOM   1793 O  O     . PHE B 1 82  ? 10.662  8.462  16.640 1.00 17.34  ? 99  PHE B O     1 
ATOM   1794 C  CB    . PHE B 1 82  ? 12.255  10.709 18.278 1.00 18.61  ? 99  PHE B CB    1 
ATOM   1795 C  CG    . PHE B 1 82  ? 12.935  11.417 19.450 1.00 15.64  ? 99  PHE B CG    1 
ATOM   1796 C  CD1   . PHE B 1 82  ? 14.267  11.216 19.709 1.00 20.08  ? 99  PHE B CD1   1 
ATOM   1797 C  CD2   . PHE B 1 82  ? 12.218  12.262 20.294 1.00 14.64  ? 99  PHE B CD2   1 
ATOM   1798 C  CE1   . PHE B 1 82  ? 14.893  11.860 20.780 1.00 21.35  ? 99  PHE B CE1   1 
ATOM   1799 C  CE2   . PHE B 1 82  ? 12.850  12.918 21.361 1.00 17.81  ? 99  PHE B CE2   1 
ATOM   1800 C  CZ    . PHE B 1 82  ? 14.170  12.700 21.604 1.00 17.39  ? 99  PHE B CZ    1 
ATOM   1801 N  N     . GLU B 1 83  ? 9.320   9.455  18.139 1.00 16.51  ? 100 GLU B N     1 
ATOM   1802 C  CA    . GLU B 1 83  ? 8.088   9.228  17.397 1.00 18.45  ? 100 GLU B CA    1 
ATOM   1803 C  C     . GLU B 1 83  ? 7.405   10.541 17.029 1.00 18.39  ? 100 GLU B C     1 
ATOM   1804 O  O     . GLU B 1 83  ? 7.265   11.435 17.861 1.00 16.87  ? 100 GLU B O     1 
ATOM   1805 C  CB    . GLU B 1 83  ? 7.130   8.377  18.241 1.00 18.48  ? 100 GLU B CB    1 
ATOM   1806 C  CG    . GLU B 1 83  ? 5.746   8.151  17.642 1.00 19.97  ? 100 GLU B CG    1 
ATOM   1807 C  CD    . GLU B 1 83  ? 4.863   7.355  18.590 1.00 22.31  ? 100 GLU B CD    1 
ATOM   1808 O  OE1   . GLU B 1 83  ? 4.969   6.104  18.591 1.00 25.80  ? 100 GLU B OE1   1 
ATOM   1809 O  OE2   . GLU B 1 83  ? 4.127   7.997  19.356 1.00 24.34  ? 100 GLU B OE2   1 
ATOM   1810 N  N     . GLY B 1 84  ? 6.943   10.636 15.784 1.00 15.80  ? 101 GLY B N     1 
ATOM   1811 C  CA    . GLY B 1 84  ? 6.183   11.794 15.349 1.00 16.45  ? 101 GLY B CA    1 
ATOM   1812 C  C     . GLY B 1 84  ? 5.771   11.639 13.901 1.00 16.38  ? 101 GLY B C     1 
ATOM   1813 O  O     . GLY B 1 84  ? 6.104   10.653 13.240 1.00 16.75  ? 101 GLY B O     1 
ATOM   1814 N  N     . VAL B 1 85  ? 5.006   12.622 13.441 1.00 14.60  ? 102 VAL B N     1 
ATOM   1815 C  CA    . VAL B 1 85  ? 4.599   12.684 12.040 1.00 16.46  ? 102 VAL B CA    1 
ATOM   1816 C  C     . VAL B 1 85  ? 5.845   12.861 11.188 1.00 15.63  ? 102 VAL B C     1 
ATOM   1817 O  O     . VAL B 1 85  ? 6.623   13.799 11.387 1.00 16.77  ? 102 VAL B O     1 
ATOM   1818 C  CB    . VAL B 1 85  ? 3.598   13.815 11.818 1.00 18.21  ? 102 VAL B CB    1 
ATOM   1819 C  CG1   . VAL B 1 85  ? 3.274   13.952 10.342 1.00 22.24  ? 102 VAL B CG1   1 
ATOM   1820 C  CG2   . VAL B 1 85  ? 2.312   13.540 12.573 1.00 19.72  ? 102 VAL B CG2   1 
ATOM   1821 N  N     . ASP B 1 86  ? 6.044   11.959 10.228 1.00 16.82  ? 103 ASP B N     1 
ATOM   1822 C  CA    . ASP B 1 86  ? 7.120   12.132 9.249  1.00 16.99  ? 103 ASP B CA    1 
ATOM   1823 C  C     . ASP B 1 86  ? 8.477   12.273 9.952  1.00 16.80  ? 103 ASP B C     1 
ATOM   1824 O  O     . ASP B 1 86  ? 9.383   12.937 9.450  1.00 15.97  ? 103 ASP B O     1 
ATOM   1825 C  CB    . ASP B 1 86  ? 6.815   13.348 8.358  1.00 17.20  ? 103 ASP B CB    1 
ATOM   1826 C  CG    . ASP B 1 86  ? 7.723   13.474 7.124  1.00 19.80  ? 103 ASP B CG    1 
ATOM   1827 O  OD1   . ASP B 1 86  ? 8.016   12.446 6.447  1.00 22.68  ? 103 ASP B OD1   1 
ATOM   1828 O  OD2   . ASP B 1 86  ? 8.066   14.640 6.773  1.00 19.56  ? 103 ASP B OD2   1 
ATOM   1829 N  N     . VAL B 1 87  ? 8.643   11.648 11.123 1.00 16.70  ? 104 VAL B N     1 
ATOM   1830 C  CA    . VAL B 1 87  ? 9.798   11.968 11.953 1.00 15.77  ? 104 VAL B CA    1 
ATOM   1831 C  C     . VAL B 1 87  ? 11.101  11.469 11.327 1.00 15.30  ? 104 VAL B C     1 
ATOM   1832 O  O     . VAL B 1 87  ? 12.169  12.027 11.594 1.00 15.92  ? 104 VAL B O     1 
ATOM   1833 C  CB    . VAL B 1 87  ? 9.607   11.431 13.388 1.00 14.58  ? 104 VAL B CB    1 
ATOM   1834 C  CG1   . VAL B 1 87  ? 9.785   9.909  13.483 1.00 18.63  ? 104 VAL B CG1   1 
ATOM   1835 C  CG2   . VAL B 1 87  ? 10.558  12.127 14.366 1.00 15.72  ? 104 VAL B CG2   1 
ATOM   1836 N  N     . ILE B 1 88  ? 11.065  10.434 10.497 1.00 14.05  ? 105 ILE B N     1 
ATOM   1837 C  CA    . ILE B 1 88  ? 12.302  9.981  9.874  1.00 15.06  ? 105 ILE B CA    1 
ATOM   1838 C  C     . ILE B 1 88  ? 12.889  11.090 9.003  1.00 16.24  ? 105 ILE B C     1 
ATOM   1839 O  O     . ILE B 1 88  ? 14.027  11.534 9.204  1.00 16.26  ? 105 ILE B O     1 
ATOM   1840 C  CB    . ILE B 1 88  ? 12.064  8.680  9.091  1.00 17.63  ? 105 ILE B CB    1 
ATOM   1841 C  CG1   . ILE B 1 88  ? 11.679  7.549  10.052 1.00 17.53  ? 105 ILE B CG1   1 
ATOM   1842 C  CG2   . ILE B 1 88  ? 13.311  8.314  8.282  1.00 18.70  ? 105 ILE B CG2   1 
ATOM   1843 C  CD1   . ILE B 1 88  ? 11.175  6.306  9.312  1.00 20.04  ? 105 ILE B CD1   1 
ATOM   1844 N  N     . ALA B 1 89  ? 12.107  11.586 8.046  1.00 16.97  ? 106 ALA B N     1 
ATOM   1845 C  CA    . ALA B 1 89  ? 12.584  12.656 7.186  1.00 16.96  ? 106 ALA B CA    1 
ATOM   1846 C  C     . ALA B 1 89  ? 12.812  13.940 7.963  1.00 14.09  ? 106 ALA B C     1 
ATOM   1847 O  O     . ALA B 1 89  ? 13.741  14.701 7.653  1.00 15.67  ? 106 ALA B O     1 
ATOM   1848 C  CB    . ALA B 1 89  ? 11.586  12.920 6.061  1.00 16.57  ? 106 ALA B CB    1 
ATOM   1849 N  N     . GLN B 1 90  ? 11.934  14.230 8.933  1.00 13.90  ? 107 GLN B N     1 
ATOM   1850 C  CA    . GLN B 1 90  ? 12.055  15.493 9.645  1.00 12.70  ? 107 GLN B CA    1 
ATOM   1851 C  C     . GLN B 1 90  ? 13.300  15.511 10.509 1.00 12.56  ? 107 GLN B C     1 
ATOM   1852 O  O     . GLN B 1 90  ? 13.983  16.543 10.595 1.00 13.67  ? 107 GLN B O     1 
ATOM   1853 C  CB    . GLN B 1 90  ? 10.818  15.767 10.493 1.00 15.55  ? 107 GLN B CB    1 
ATOM   1854 C  CG    . GLN B 1 90  ? 9.610   16.141 9.659  1.00 14.24  ? 107 GLN B CG    1 
ATOM   1855 C  CD    . GLN B 1 90  ? 9.800   17.429 8.904  1.00 14.09  ? 107 GLN B CD    1 
ATOM   1856 O  OE1   . GLN B 1 90  ? 10.104  18.462 9.476  1.00 13.56  ? 107 GLN B OE1   1 
ATOM   1857 N  NE2   . GLN B 1 90  ? 9.642   17.371 7.608  1.00 17.46  ? 107 GLN B NE2   1 
ATOM   1858 N  N     . ALA B 1 91  ? 13.617  14.383 11.151 1.00 13.56  ? 108 ALA B N     1 
ATOM   1859 C  CA    . ALA B 1 91  ? 14.824  14.348 11.965 1.00 14.20  ? 108 ALA B CA    1 
ATOM   1860 C  C     . ALA B 1 91  ? 16.052  14.546 11.100 1.00 13.96  ? 108 ALA B C     1 
ATOM   1861 O  O     . ALA B 1 91  ? 16.979  15.245 11.506 1.00 15.89  ? 108 ALA B O     1 
ATOM   1862 C  CB    . ALA B 1 91  ? 14.931  13.047 12.764 1.00 15.69  ? 108 ALA B CB    1 
ATOM   1863 N  N     . ARG B 1 92  ? 16.071  13.950 9.902  1.00 16.20  ? 109 ARG B N     1 
ATOM   1864 C  CA    . ARG B 1 92  ? 17.195  14.177 8.995  1.00 16.71  ? 109 ARG B CA    1 
ATOM   1865 C  C     . ARG B 1 92  ? 17.319  15.647 8.629  1.00 16.22  ? 109 ARG B C     1 
ATOM   1866 O  O     . ARG B 1 92  ? 18.429  16.192 8.545  1.00 17.32  ? 109 ARG B O     1 
ATOM   1867 C  CB    . ARG B 1 92  ? 17.036  13.334 7.725  1.00 19.39  ? 109 ARG B CB    1 
ATOM   1868 C  CG    . ARG B 1 92  ? 17.102  11.834 7.983  1.00 20.81  ? 109 ARG B CG    1 
ATOM   1869 C  CD    . ARG B 1 92  ? 18.508  11.342 8.186  1.00 24.79  ? 109 ARG B CD    1 
ATOM   1870 N  NE    . ARG B 1 92  ? 19.203  11.310 6.906  1.00 31.44  ? 109 ARG B NE    1 
ATOM   1871 C  CZ    . ARG B 1 92  ? 20.375  10.723 6.710  1.00 40.49  ? 109 ARG B CZ    1 
ATOM   1872 N  NH1   . ARG B 1 92  ? 20.987  10.066 7.682  1.00 32.98  ? 109 ARG B NH1   1 
ATOM   1873 N  NH2   . ARG B 1 92  ? 20.945  10.798 5.510  1.00 38.17  ? 109 ARG B NH2   1 
ATOM   1874 N  N     . LYS B 1 93  ? 16.189  16.297 8.371  1.00 13.62  ? 110 LYS B N     1 
ATOM   1875 C  CA    . LYS B 1 93  ? 16.197  17.716 8.053  1.00 12.70  ? 110 LYS B CA    1 
ATOM   1876 C  C     . LYS B 1 93  ? 16.734  18.531 9.228  1.00 13.27  ? 110 LYS B C     1 
ATOM   1877 O  O     . LYS B 1 93  ? 17.522  19.468 9.043  1.00 16.11  ? 110 LYS B O     1 
ATOM   1878 C  CB    . LYS B 1 93  ? 14.783  18.155 7.669  1.00 14.00  ? 110 LYS B CB    1 
ATOM   1879 C  CG    . LYS B 1 93  ? 14.677  19.600 7.358  1.00 13.73  ? 110 LYS B CG    1 
ATOM   1880 C  CD    . LYS B 1 93  ? 13.269  19.919 6.906  1.00 13.69  ? 110 LYS B CD    1 
ATOM   1881 C  CE    . LYS B 1 93  ? 13.072  21.389 6.655  1.00 20.92  ? 110 LYS B CE    1 
ATOM   1882 N  NZ    . LYS B 1 93  ? 11.639  21.632 6.243  1.00 20.58  ? 110 LYS B NZ    1 
ATOM   1883 N  N     . MET B 1 94  ? 16.326  18.180 10.446 1.00 13.14  ? 111 MET B N     1 
ATOM   1884 C  CA    . MET B 1 94  ? 16.790  18.911 11.621 1.00 13.96  ? 111 MET B CA    1 
ATOM   1885 C  C     . MET B 1 94  ? 18.288  18.721 11.865 1.00 16.04  ? 111 MET B C     1 
ATOM   1886 O  O     . MET B 1 94  ? 18.942  19.626 12.391 1.00 14.65  ? 111 MET B O     1 
ATOM   1887 C  CB    . MET B 1 94  ? 16.000  18.476 12.848 1.00 14.46  ? 111 MET B CB    1 
ATOM   1888 C  CG    . MET B 1 94  ? 14.535  18.828 12.750 1.00 14.34  ? 111 MET B CG    1 
ATOM   1889 S  SD    . MET B 1 94  ? 13.581  17.942 14.006 1.00 15.00  ? 111 MET B SD    1 
ATOM   1890 C  CE    . MET B 1 94  ? 14.033  18.764 15.540 1.00 19.29  ? 111 MET B CE    1 
ATOM   1891 N  N     . MET B 1 95  ? 18.828  17.521 11.577 1.00 12.54  ? 112 MET B N     1 
ATOM   1892 C  CA    . MET B 1 95  ? 20.256  17.259 11.726 1.00 14.04  ? 112 MET B CA    1 
ATOM   1893 C  C     . MET B 1 95  ? 21.067  18.069 10.735 1.00 14.68  ? 112 MET B C     1 
ATOM   1894 O  O     . MET B 1 95  ? 22.139  18.570 11.077 1.00 15.35  ? 112 MET B O     1 
ATOM   1895 C  CB    . MET B 1 95  ? 20.538  15.765 11.521 1.00 16.65  ? 112 MET B CB    1 
ATOM   1896 C  CG    . MET B 1 95  ? 20.062  14.915 12.628 1.00 16.66  ? 112 MET B CG    1 
ATOM   1897 S  SD    . MET B 1 95  ? 20.296  13.156 12.311 1.00 24.21  ? 112 MET B SD    1 
ATOM   1898 C  CE    . MET B 1 95  ? 21.679  13.076 11.234 1.00 34.40  ? 112 MET B CE    1 
ATOM   1899 N  N     . GLY B 1 96  ? 20.548  18.228 9.520  1.00 15.52  ? 113 GLY B N     1 
ATOM   1900 C  CA    . GLY B 1 96  ? 21.269  18.865 8.429  1.00 15.15  ? 113 GLY B CA    1 
ATOM   1901 C  C     . GLY B 1 96  ? 22.203  17.927 7.709  1.00 15.19  ? 113 GLY B C     1 
ATOM   1902 O  O     . GLY B 1 96  ? 22.402  16.761 8.073  1.00 15.92  ? 113 GLY B O     1 
ATOM   1903 N  N     . SER B 1 97  ? 22.789  18.480 6.639  1.00 15.70  ? 114 SER B N     1 
ATOM   1904 C  CA    . SER B 1 97  ? 23.746  17.751 5.812  1.00 20.34  ? 114 SER B CA    1 
ATOM   1905 C  C     . SER B 1 97  ? 24.822  17.051 6.633  1.00 17.72  ? 114 SER B C     1 
ATOM   1906 O  O     . SER B 1 97  ? 25.283  17.553 7.661  1.00 16.52  ? 114 SER B O     1 
ATOM   1907 C  CB    . SER B 1 97  ? 24.414  18.718 4.839  1.00 17.53  ? 114 SER B CB    1 
ATOM   1908 O  OG    . SER B 1 97  ? 23.437  19.466 4.158  1.00 30.16  ? 114 SER B OG    1 
ATOM   1909 N  N     . THR B 1 98  ? 25.272  15.899 6.116  1.00 16.37  ? 115 THR B N     1 
ATOM   1910 C  CA    . THR B 1 98  ? 26.378  15.158 6.718  1.00 16.08  ? 115 THR B CA    1 
ATOM   1911 C  C     . THR B 1 98  ? 27.571  16.054 6.962  1.00 14.55  ? 115 THR B C     1 
ATOM   1912 O  O     . THR B 1 98  ? 28.276  15.909 7.975  1.00 18.18  ? 115 THR B O     1 
ATOM   1913 C  CB    . THR B 1 98  ? 26.815  14.019 5.784  1.00 27.03  ? 115 THR B CB    1 
ATOM   1914 O  OG1   . THR B 1 98  ? 25.687  13.229 5.437  1.00 32.65  ? 115 THR B OG1   1 
ATOM   1915 C  CG2   . THR B 1 98  ? 27.865  13.136 6.452  1.00 30.51  ? 115 THR B CG2   1 
ATOM   1916 N  N     . ARG B 1 99  ? 27.896  16.878 5.970  1.00 18.78  ? 116 ARG B N     1 
ATOM   1917 C  CA    . ARG B 1 99  ? 28.990  17.820 6.069  1.00 17.69  ? 116 ARG B CA    1 
ATOM   1918 C  C     . ARG B 1 99  ? 28.471  19.089 6.724  1.00 15.45  ? 116 ARG B C     1 
ATOM   1919 O  O     . ARG B 1 99  ? 27.653  19.802 6.110  1.00 17.61  ? 116 ARG B O     1 
ATOM   1920 C  CB    . ARG B 1 99  ? 29.557  18.130 4.691  1.00 19.89  ? 116 ARG B CB    1 
ATOM   1921 C  CG    . ARG B 1 99  ? 30.342  16.959 4.092  1.00 25.01  ? 116 ARG B CG    1 
ATOM   1922 C  CD    . ARG B 1 99  ? 30.292  16.893 2.553  1.00 42.37  ? 116 ARG B CD    1 
ATOM   1923 N  NE    . ARG B 1 99  ? 29.056  16.267 2.085  1.00 59.63  ? 116 ARG B NE    1 
ATOM   1924 C  CZ    . ARG B 1 99  ? 28.832  14.956 2.071  1.00 58.46  ? 116 ARG B CZ    1 
ATOM   1925 N  NH1   . ARG B 1 99  ? 29.765  14.088 2.431  1.00 55.81  ? 116 ARG B NH1   1 
ATOM   1926 N  NH2   . ARG B 1 99  ? 27.643  14.504 1.684  1.00 59.20  ? 116 ARG B NH2   1 
ATOM   1927 N  N     . PRO B 1 100 ? 28.916  19.425 7.940  1.00 15.69  ? 117 PRO B N     1 
ATOM   1928 C  CA    . PRO B 1 100 ? 28.348  20.601 8.610  1.00 15.13  ? 117 PRO B CA    1 
ATOM   1929 C  C     . PRO B 1 100 ? 28.486  21.889 7.826  1.00 16.21  ? 117 PRO B C     1 
ATOM   1930 O  O     . PRO B 1 100 ? 27.600  22.754 7.920  1.00 17.95  ? 117 PRO B O     1 
ATOM   1931 C  CB    . PRO B 1 100 ? 29.137  20.649 9.930  1.00 16.00  ? 117 PRO B CB    1 
ATOM   1932 C  CG    . PRO B 1 100 ? 29.488  19.260 10.184 1.00 16.87  ? 117 PRO B CG    1 
ATOM   1933 C  CD    . PRO B 1 100 ? 29.854  18.716 8.819  1.00 15.86  ? 117 PRO B CD    1 
ATOM   1934 N  N     . GLY B 1 101 ? 29.571  22.053 7.061  1.00 18.52  ? 118 GLY B N     1 
ATOM   1935 C  CA    . GLY B 1 101 ? 29.748  23.272 6.283  1.00 18.34  ? 118 GLY B CA    1 
ATOM   1936 C  C     . GLY B 1 101 ? 28.693  23.474 5.224  1.00 17.33  ? 118 GLY B C     1 
ATOM   1937 O  O     . GLY B 1 101 ? 28.490  24.603 4.758  1.00 19.58  ? 118 GLY B O     1 
ATOM   1938 N  N     . GLU B 1 102 ? 28.020  22.402 4.820  1.00 18.09  ? 119 GLU B N     1 
ATOM   1939 C  CA    . GLU B 1 102 ? 26.954  22.467 3.836  1.00 17.03  ? 119 GLU B CA    1 
ATOM   1940 C  C     . GLU B 1 102 ? 25.575  22.492 4.473  1.00 17.87  ? 119 GLU B C     1 
ATOM   1941 O  O     . GLU B 1 102 ? 24.582  22.708 3.773  1.00 20.43  ? 119 GLU B O     1 
ATOM   1942 C  CB    . GLU B 1 102 ? 27.037  21.262 2.885  1.00 20.25  ? 119 GLU B CB    1 
ATOM   1943 C  CG    . GLU B 1 102 ? 28.278  21.257 1.970  1.00 28.60  ? 119 GLU B CG    1 
ATOM   1944 C  CD    . GLU B 1 102 ? 28.507  19.905 1.273  1.00 46.79  ? 119 GLU B CD    1 
ATOM   1945 O  OE1   . GLU B 1 102 ? 27.579  19.065 1.249  1.00 42.10  ? 119 GLU B OE1   1 
ATOM   1946 O  OE2   . GLU B 1 102 ? 29.625  19.676 0.755  1.00 46.78  ? 119 GLU B OE2   1 
ATOM   1947 N  N     . ALA B 1 103 ? 25.496  22.284 5.780  1.00 15.88  ? 120 ALA B N     1 
ATOM   1948 C  CA    . ALA B 1 103 ? 24.224  22.204 6.468  1.00 14.72  ? 120 ALA B CA    1 
ATOM   1949 C  C     . ALA B 1 103 ? 23.591  23.579 6.646  1.00 16.82  ? 120 ALA B C     1 
ATOM   1950 O  O     . ALA B 1 103 ? 24.275  24.607 6.761  1.00 18.33  ? 120 ALA B O     1 
ATOM   1951 C  CB    . ALA B 1 103 ? 24.410  21.535 7.835  1.00 16.72  ? 120 ALA B CB    1 
ATOM   1952 N  N     . ALA B 1 104 ? 22.261  23.587 6.628  1.00 17.14  ? 121 ALA B N     1 
ATOM   1953 C  CA    . ALA B 1 104 ? 21.531  24.845 6.706  1.00 21.03  ? 121 ALA B CA    1 
ATOM   1954 C  C     . ALA B 1 104 ? 21.644  25.470 8.093  1.00 21.04  ? 121 ALA B C     1 
ATOM   1955 O  O     . ALA B 1 104 ? 21.593  24.764 9.114  1.00 16.30  ? 121 ALA B O     1 
ATOM   1956 C  CB    . ALA B 1 104 ? 20.058  24.629 6.369  1.00 21.13  ? 121 ALA B CB    1 
ATOM   1957 N  N     . PRO B 1 105 ? 21.700  26.793 8.183  1.00 24.87  ? 122 PRO B N     1 
ATOM   1958 C  CA    . PRO B 1 105 ? 21.658  27.425 9.502  1.00 22.75  ? 122 PRO B CA    1 
ATOM   1959 C  C     . PRO B 1 105 ? 20.414  26.956 10.248 1.00 16.25  ? 122 PRO B C     1 
ATOM   1960 O  O     . PRO B 1 105 ? 19.358  26.755 9.650  1.00 21.20  ? 122 PRO B O     1 
ATOM   1961 C  CB    . PRO B 1 105 ? 21.589  28.923 9.180  1.00 32.14  ? 122 PRO B CB    1 
ATOM   1962 C  CG    . PRO B 1 105 ? 22.130  29.032 7.801  1.00 34.51  ? 122 PRO B CG    1 
ATOM   1963 C  CD    . PRO B 1 105 ? 21.662  27.793 7.096  1.00 28.08  ? 122 PRO B CD    1 
ATOM   1964 N  N     . GLY B 1 106 ? 20.549  26.746 11.549 1.00 16.62  ? 123 GLY B N     1 
ATOM   1965 C  CA    . GLY B 1 106 ? 19.442  26.261 12.335 1.00 16.75  ? 123 GLY B CA    1 
ATOM   1966 C  C     . GLY B 1 106 ? 19.374  24.755 12.490 1.00 14.94  ? 123 GLY B C     1 
ATOM   1967 O  O     . GLY B 1 106 ? 18.562  24.271 13.296 1.00 17.24  ? 123 GLY B O     1 
ATOM   1968 N  N     . THR B 1 107 ? 20.163  24.000 11.728 1.00 14.19  ? 124 THR B N     1 
ATOM   1969 C  CA    . THR B 1 107 ? 20.264  22.564 11.910 1.00 11.81  ? 124 THR B CA    1 
ATOM   1970 C  C     . THR B 1 107 ? 21.319  22.234 12.958 1.00 14.28  ? 124 THR B C     1 
ATOM   1971 O  O     . THR B 1 107 ? 22.176  23.049 13.308 1.00 14.28  ? 124 THR B O     1 
ATOM   1972 C  CB    . THR B 1 107 ? 20.605  21.852 10.593 1.00 11.76  ? 124 THR B CB    1 
ATOM   1973 O  OG1   . THR B 1 107 ? 21.907  22.253 10.104 1.00 14.05  ? 124 THR B OG1   1 
ATOM   1974 C  CG2   . THR B 1 107 ? 19.541  22.132 9.530  1.00 14.13  ? 124 THR B CG2   1 
ATOM   1975 N  N     . ILE B 1 108 ? 21.242  21.004 13.455 1.00 12.49  ? 125 ILE B N     1 
ATOM   1976 C  CA    . ILE B 1 108 ? 22.158  20.582 14.512 1.00 15.27  ? 125 ILE B CA    1 
ATOM   1977 C  C     . ILE B 1 108 ? 23.598  20.643 14.019 1.00 16.26  ? 125 ILE B C     1 
ATOM   1978 O  O     . ILE B 1 108 ? 24.479  21.181 14.694 1.00 13.33  ? 125 ILE B O     1 
ATOM   1979 C  CB    . ILE B 1 108 ? 21.795  19.173 15.012 1.00 13.77  ? 125 ILE B CB    1 
ATOM   1980 C  CG1   . ILE B 1 108 ? 20.464  19.189 15.776 1.00 15.02  ? 125 ILE B CG1   1 
ATOM   1981 C  CG2   . ILE B 1 108 ? 22.903  18.613 15.886 1.00 14.33  ? 125 ILE B CG2   1 
ATOM   1982 C  CD1   . ILE B 1 108 ? 19.861  17.836 16.074 1.00 18.97  ? 125 ILE B CD1   1 
ATOM   1983 N  N     . ARG B 1 109 ? 23.870  20.070 12.849 1.00 13.32  ? 126 ARG B N     1 
ATOM   1984 C  CA    . ARG B 1 109 ? 25.257  20.004 12.393 1.00 13.32  ? 126 ARG B CA    1 
ATOM   1985 C  C     . ARG B 1 109 ? 25.801  21.389 12.071 1.00 13.75  ? 126 ARG B C     1 
ATOM   1986 O  O     . ARG B 1 109 ? 26.976  21.668 12.341 1.00 15.57  ? 126 ARG B O     1 
ATOM   1987 C  CB    . ARG B 1 109 ? 25.360  19.042 11.211 1.00 15.74  ? 126 ARG B CB    1 
ATOM   1988 C  CG    . ARG B 1 109 ? 25.223  17.622 11.744 1.00 17.32  ? 126 ARG B CG    1 
ATOM   1989 C  CD    . ARG B 1 109 ? 24.944  16.656 10.670 1.00 21.82  ? 126 ARG B CD    1 
ATOM   1990 N  NE    . ARG B 1 109 ? 24.857  15.290 11.161 1.00 16.56  ? 126 ARG B NE    1 
ATOM   1991 C  CZ    . ARG B 1 109 ? 24.466  14.293 10.388 1.00 22.56  ? 126 ARG B CZ    1 
ATOM   1992 N  NH1   . ARG B 1 109 ? 23.949  14.522 9.193  1.00 24.20  ? 126 ARG B NH1   1 
ATOM   1993 N  NH2   . ARG B 1 109 ? 24.609  13.041 10.810 1.00 20.81  ? 126 ARG B NH2   1 
ATOM   1994 N  N     . ALA B 1 110 ? 24.967  22.280 11.505 1.00 14.03  ? 127 ALA B N     1 
ATOM   1995 C  CA    . ALA B 1 110 ? 25.432  23.639 11.232 1.00 13.09  ? 127 ALA B CA    1 
ATOM   1996 C  C     . ALA B 1 110 ? 25.688  24.411 12.518 1.00 16.06  ? 127 ALA B C     1 
ATOM   1997 O  O     . ALA B 1 110 ? 26.584  25.260 12.564 1.00 16.59  ? 127 ALA B O     1 
ATOM   1998 C  CB    . ALA B 1 110 ? 24.422  24.408 10.387 1.00 16.10  ? 127 ALA B CB    1 
ATOM   1999 N  N     . ASP B 1 111 ? 24.878  24.163 13.545 1.00 13.08  ? 128 ASP B N     1 
ATOM   2000 C  CA    . ASP B 1 111 ? 24.934  24.959 14.764 1.00 13.73  ? 128 ASP B CA    1 
ATOM   2001 C  C     . ASP B 1 111 ? 26.045  24.505 15.697 1.00 13.00  ? 128 ASP B C     1 
ATOM   2002 O  O     . ASP B 1 111 ? 26.559  25.317 16.476 1.00 14.86  ? 128 ASP B O     1 
ATOM   2003 C  CB    . ASP B 1 111 ? 23.590  24.896 15.504 1.00 13.40  ? 128 ASP B CB    1 
ATOM   2004 C  CG    . ASP B 1 111 ? 22.485  25.710 14.826 1.00 21.95  ? 128 ASP B CG    1 
ATOM   2005 O  OD1   . ASP B 1 111 ? 22.779  26.483 13.879 1.00 23.36  ? 128 ASP B OD1   1 
ATOM   2006 O  OD2   . ASP B 1 111 ? 21.301  25.550 15.246 1.00 20.73  ? 128 ASP B OD2   1 
ATOM   2007 N  N     . PHE B 1 112 ? 26.439  23.233 15.613 1.00 12.41  ? 129 PHE B N     1 
ATOM   2008 C  CA    . PHE B 1 112 ? 27.367  22.629 16.557 1.00 14.10  ? 129 PHE B CA    1 
ATOM   2009 C  C     . PHE B 1 112 ? 28.703  22.152 15.975 1.00 15.11  ? 129 PHE B C     1 
ATOM   2010 O  O     . PHE B 1 112 ? 29.652  21.972 16.747 1.00 13.74  ? 129 PHE B O     1 
ATOM   2011 C  CB    . PHE B 1 112 ? 26.730  21.396 17.232 1.00 13.62  ? 129 PHE B CB    1 
ATOM   2012 C  CG    . PHE B 1 112 ? 25.650  21.693 18.228 1.00 13.58  ? 129 PHE B CG    1 
ATOM   2013 C  CD1   . PHE B 1 112 ? 24.308  21.729 17.857 1.00 15.31  ? 129 PHE B CD1   1 
ATOM   2014 C  CD2   . PHE B 1 112 ? 25.981  21.835 19.549 1.00 16.02  ? 129 PHE B CD2   1 
ATOM   2015 C  CE1   . PHE B 1 112 ? 23.316  21.955 18.813 1.00 18.60  ? 129 PHE B CE1   1 
ATOM   2016 C  CE2   . PHE B 1 112 ? 24.996  22.049 20.500 1.00 13.67  ? 129 PHE B CE2   1 
ATOM   2017 C  CZ    . PHE B 1 112 ? 23.678  22.100 20.138 1.00 18.24  ? 129 PHE B CZ    1 
ATOM   2018 N  N     . CYS B 1 113 ? 28.827  21.932 14.662 1.00 14.43  ? 130 CYS B N     1 
ATOM   2019 C  CA    . CYS B 1 113 ? 29.912  21.093 14.144 1.00 13.95  ? 130 CYS B CA    1 
ATOM   2020 C  C     . CYS B 1 113 ? 30.677  21.766 13.014 1.00 15.63  ? 130 CYS B C     1 
ATOM   2021 O  O     . CYS B 1 113 ? 30.241  22.775 12.451 1.00 14.94  ? 130 CYS B O     1 
ATOM   2022 C  CB    . CYS B 1 113 ? 29.370  19.738 13.687 1.00 14.12  ? 130 CYS B CB    1 
ATOM   2023 S  SG    . CYS B 1 113 ? 28.590  18.825 15.041 1.00 17.20  ? 130 CYS B SG    1 
ATOM   2024 N  N     . GLN B 1 114 ? 31.822  21.141 12.662 1.00 14.83  ? 131 GLN B N     1 
ATOM   2025 C  CA    . GLN B 1 114 ? 32.718  21.641 11.619 1.00 15.35  ? 131 GLN B CA    1 
ATOM   2026 C  C     . GLN B 1 114 ? 32.956  20.644 10.509 1.00 17.41  ? 131 GLN B C     1 
ATOM   2027 O  O     . GLN B 1 114 ? 33.030  21.046 9.341  1.00 17.40  ? 131 GLN B O     1 
ATOM   2028 C  CB    . GLN B 1 114 ? 34.077  22.047 12.228 1.00 16.10  ? 131 GLN B CB    1 
ATOM   2029 C  CG    . GLN B 1 114 ? 33.973  23.238 13.156 1.00 14.56  ? 131 GLN B CG    1 
ATOM   2030 C  CD    . GLN B 1 114 ? 35.319  23.734 13.608 1.00 16.13  ? 131 GLN B CD    1 
ATOM   2031 O  OE1   . GLN B 1 114 ? 36.252  23.859 12.797 1.00 17.50  ? 131 GLN B OE1   1 
ATOM   2032 N  NE2   . GLN B 1 114 ? 35.467  23.958 14.912 1.00 15.18  ? 131 GLN B NE2   1 
ATOM   2033 N  N     . GLN B 1 115 ? 33.086  19.363 10.829 1.00 16.33  ? 132 GLN B N     1 
ATOM   2034 C  CA    . GLN B 1 115 ? 33.460  18.362 9.847  1.00 17.72  ? 132 GLN B CA    1 
ATOM   2035 C  C     . GLN B 1 115 ? 32.595  17.114 9.951  1.00 18.04  ? 132 GLN B C     1 
ATOM   2036 O  O     . GLN B 1 115 ? 32.101  16.763 11.021 1.00 19.37  ? 132 GLN B O     1 
ATOM   2037 C  CB    . GLN B 1 115 ? 34.922  17.972 10.006 1.00 20.74  ? 132 GLN B CB    1 
ATOM   2038 C  CG    . GLN B 1 115 ? 35.867  19.143 9.954  1.00 24.38  ? 132 GLN B CG    1 
ATOM   2039 C  CD    . GLN B 1 115 ? 37.303  18.702 9.856  1.00 23.08  ? 132 GLN B CD    1 
ATOM   2040 O  OE1   . GLN B 1 115 ? 37.920  18.343 10.851 1.00 23.83  ? 132 GLN B OE1   1 
ATOM   2041 N  NE2   . GLN B 1 115 ? 37.850  18.720 8.639  1.00 27.31  ? 132 GLN B NE2   1 
ATOM   2042 N  N     . ALA B 1 116 ? 32.479  16.410 8.815  1.00 18.37  ? 133 ALA B N     1 
ATOM   2043 C  CA    . ALA B 1 116 ? 31.601  15.242 8.752  1.00 18.47  ? 133 ALA B CA    1 
ATOM   2044 C  C     . ALA B 1 116 ? 32.003  14.148 9.744  1.00 20.71  ? 133 ALA B C     1 
ATOM   2045 O  O     . ALA B 1 116 ? 31.140  13.462 10.303 1.00 20.72  ? 133 ALA B O     1 
ATOM   2046 C  CB    . ALA B 1 116 ? 31.586  14.693 7.330  1.00 21.52  ? 133 ALA B CB    1 
ATOM   2047 N  N     . GLY B 1 117 ? 33.300  13.961 9.966  1.00 20.83  ? 134 GLY B N     1 
ATOM   2048 C  CA    . GLY B 1 117 ? 33.743  12.906 10.853 1.00 20.88  ? 134 GLY B CA    1 
ATOM   2049 C  C     . GLY B 1 117 ? 33.400  13.140 12.307 1.00 21.02  ? 134 GLY B C     1 
ATOM   2050 O  O     . GLY B 1 117 ? 33.474  12.202 13.108 1.00 23.30  ? 134 GLY B O     1 
ATOM   2051 N  N     . ARG B 1 118 ? 33.053  14.374 12.675 1.00 17.41  ? 135 ARG B N     1 
ATOM   2052 C  CA    . ARG B 1 118 ? 32.565  14.688 14.015 1.00 17.49  ? 135 ARG B CA    1 
ATOM   2053 C  C     . ARG B 1 118 ? 31.299  15.523 13.852 1.00 16.64  ? 135 ARG B C     1 
ATOM   2054 O  O     . ARG B 1 118 ? 31.306  16.740 14.068 1.00 18.15  ? 135 ARG B O     1 
ATOM   2055 C  CB    . ARG B 1 118 ? 33.629  15.429 14.832 1.00 16.67  ? 135 ARG B CB    1 
ATOM   2056 C  CG    . ARG B 1 118 ? 34.857  14.534 15.236 1.00 17.93  ? 135 ARG B CG    1 
ATOM   2057 C  CD    . ARG B 1 118 ? 34.409  13.389 16.096 1.00 20.38  ? 135 ARG B CD    1 
ATOM   2058 N  NE    . ARG B 1 118 ? 35.524  12.769 16.802 1.00 22.45  ? 135 ARG B NE    1 
ATOM   2059 C  CZ    . ARG B 1 118 ? 35.428  11.655 17.512 1.00 22.49  ? 135 ARG B CZ    1 
ATOM   2060 N  NH1   . ARG B 1 118 ? 34.286  10.999 17.621 1.00 24.30  ? 135 ARG B NH1   1 
ATOM   2061 N  NH2   . ARG B 1 118 ? 36.518  11.173 18.105 1.00 23.38  ? 135 ARG B NH2   1 
ATOM   2062 N  N     . ASN B 1 119 ? 30.186  14.863 13.543 1.00 16.37  ? 136 ASN B N     1 
ATOM   2063 C  CA    . ASN B 1 119 ? 28.958  15.574 13.204 1.00 14.25  ? 136 ASN B CA    1 
ATOM   2064 C  C     . ASN B 1 119 ? 27.811  15.212 14.144 1.00 15.72  ? 136 ASN B C     1 
ATOM   2065 O  O     . ASN B 1 119 ? 26.639  15.323 13.783 1.00 14.69  ? 136 ASN B O     1 
ATOM   2066 C  CB    . ASN B 1 119 ? 28.587  15.355 11.734 1.00 14.26  ? 136 ASN B CB    1 
ATOM   2067 C  CG    . ASN B 1 119 ? 28.243  13.923 11.409 1.00 18.14  ? 136 ASN B CG    1 
ATOM   2068 O  OD1   . ASN B 1 119 ? 28.242  13.041 12.276 1.00 17.02  ? 136 ASN B OD1   1 
ATOM   2069 N  ND2   . ASN B 1 119 ? 27.919  13.678 10.131 1.00 20.73  ? 136 ASN B ND2   1 
ATOM   2070 N  N     . LEU B 1 120 ? 28.172  14.789 15.363 1.00 15.00  ? 137 LEU B N     1 
ATOM   2071 C  CA    . LEU B 1 120 ? 27.394  14.807 16.599 1.00 13.32  ? 137 LEU B CA    1 
ATOM   2072 C  C     . LEU B 1 120 ? 26.278  13.783 16.742 1.00 14.55  ? 137 LEU B C     1 
ATOM   2073 O  O     . LEU B 1 120 ? 26.031  13.292 17.856 1.00 15.50  ? 137 LEU B O     1 
ATOM   2074 C  CB    . LEU B 1 120 ? 26.729  16.188 16.770 1.00 13.45  ? 137 LEU B CB    1 
ATOM   2075 C  CG    . LEU B 1 120 ? 26.671  16.748 18.204 1.00 13.63  ? 137 LEU B CG    1 
ATOM   2076 C  CD1   . LEU B 1 120 ? 28.083  17.154 18.645 1.00 16.97  ? 137 LEU B CD1   1 
ATOM   2077 C  CD2   . LEU B 1 120 ? 25.684  17.956 18.262 1.00 15.00  ? 137 LEU B CD2   1 
ATOM   2078 N  N     . ILE B 1 121 ? 25.674  13.358 15.636 1.00 17.65  ? 138 ILE B N     1 
ATOM   2079 C  CA    . ILE B 1 121 ? 24.412  12.645 15.716 1.00 13.09  ? 138 ILE B CA    1 
ATOM   2080 C  C     . ILE B 1 121 ? 24.223  11.854 14.436 1.00 16.98  ? 138 ILE B C     1 
ATOM   2081 O  O     . ILE B 1 121 ? 24.700  12.246 13.365 1.00 17.40  ? 138 ILE B O     1 
ATOM   2082 C  CB    . ILE B 1 121 ? 23.233  13.613 15.996 1.00 14.17  ? 138 ILE B CB    1 
ATOM   2083 C  CG1   . ILE B 1 121 ? 21.921  12.848 16.197 1.00 16.88  ? 138 ILE B CG1   1 
ATOM   2084 C  CG2   . ILE B 1 121 ? 23.133  14.656 14.878 1.00 17.01  ? 138 ILE B CG2   1 
ATOM   2085 C  CD1   . ILE B 1 121 ? 20.820  13.713 16.776 1.00 17.18  ? 138 ILE B CD1   1 
ATOM   2086 N  N     . HIS B 1 122 ? 23.541  10.723 14.565 1.00 17.28  ? 139 HIS B N     1 
ATOM   2087 C  CA    . HIS B 1 122 ? 23.073  9.884  13.470 1.00 18.59  ? 139 HIS B CA    1 
ATOM   2088 C  C     . HIS B 1 122 ? 21.557  9.810  13.511 1.00 15.42  ? 139 HIS B C     1 
ATOM   2089 O  O     . HIS B 1 122 ? 20.978  9.711  14.590 1.00 16.94  ? 139 HIS B O     1 
ATOM   2090 C  CB    . HIS B 1 122 ? 23.605  8.450  13.587 1.00 18.73  ? 139 HIS B CB    1 
ATOM   2091 C  CG    . HIS B 1 122 ? 22.807  7.452  12.805 1.00 19.35  ? 139 HIS B CG    1 
ATOM   2092 N  ND1   . HIS B 1 122 ? 23.099  7.124  11.498 1.00 27.26  ? 139 HIS B ND1   1 
ATOM   2093 C  CD2   . HIS B 1 122 ? 21.700  6.745  13.133 1.00 20.46  ? 139 HIS B CD2   1 
ATOM   2094 C  CE1   . HIS B 1 122 ? 22.208  6.253  11.056 1.00 22.43  ? 139 HIS B CE1   1 
ATOM   2095 N  NE2   . HIS B 1 122 ? 21.343  6.013  12.025 1.00 21.07  ? 139 HIS B NE2   1 
ATOM   2096 N  N     . GLY B 1 123 ? 20.922  9.789  12.337 1.00 16.57  ? 140 GLY B N     1 
ATOM   2097 C  CA    . GLY B 1 123 ? 19.505  9.486  12.241 1.00 16.79  ? 140 GLY B CA    1 
ATOM   2098 C  C     . GLY B 1 123 ? 19.233  8.572  11.062 1.00 17.37  ? 140 GLY B C     1 
ATOM   2099 O  O     . GLY B 1 123 ? 19.886  8.662  10.025 1.00 18.73  ? 140 GLY B O     1 
ATOM   2100 N  N     . SER B 1 124 ? 18.253  7.676  11.238 1.00 17.08  ? 141 SER B N     1 
ATOM   2101 C  CA    . SER B 1 124 ? 17.850  6.762  10.159 1.00 17.81  ? 141 SER B CA    1 
ATOM   2102 C  C     . SER B 1 124 ? 17.515  7.525  8.885  1.00 17.83  ? 141 SER B C     1 
ATOM   2103 O  O     . SER B 1 124 ? 16.879  8.579  8.921  1.00 18.37  ? 141 SER B O     1 
ATOM   2104 C  CB    . SER B 1 124 ? 16.619  5.954  10.563 1.00 19.09  ? 141 SER B CB    1 
ATOM   2105 O  OG    . SER B 1 124 ? 16.816  5.275  11.781 1.00 20.18  ? 141 SER B OG    1 
ATOM   2106 N  N     . ASP B 1 125 ? 17.931  6.978  7.742  1.00 19.49  ? 142 ASP B N     1 
ATOM   2107 C  CA    . ASP B 1 125 ? 17.666  7.650  6.474  1.00 19.32  ? 142 ASP B CA    1 
ATOM   2108 C  C     . ASP B 1 125 ? 16.400  7.178  5.762  1.00 20.71  ? 142 ASP B C     1 
ATOM   2109 O  O     . ASP B 1 125 ? 16.043  7.763  4.729  1.00 24.25  ? 142 ASP B O     1 
ATOM   2110 C  CB    . ASP B 1 125 ? 18.876  7.510  5.538  1.00 23.59  ? 142 ASP B CB    1 
ATOM   2111 C  CG    . ASP B 1 125 ? 19.120  6.107  5.059  1.00 27.77  ? 142 ASP B CG    1 
ATOM   2112 O  OD1   . ASP B 1 125 ? 18.318  5.195  5.314  1.00 27.45  ? 142 ASP B OD1   1 
ATOM   2113 O  OD2   . ASP B 1 125 ? 20.146  5.919  4.377  1.00 34.33  ? 142 ASP B OD2   1 
ATOM   2114 N  N     . SER B 1 126 ? 15.709  6.159  6.269  1.00 20.79  ? 143 SER B N     1 
ATOM   2115 C  CA    . SER B 1 126 ? 14.536  5.620  5.595  1.00 23.93  ? 143 SER B CA    1 
ATOM   2116 C  C     . SER B 1 126 ? 13.749  4.783  6.587  1.00 25.30  ? 143 SER B C     1 
ATOM   2117 O  O     . SER B 1 126 ? 14.246  4.426  7.652  1.00 21.05  ? 143 SER B O     1 
ATOM   2118 C  CB    . SER B 1 126 ? 14.932  4.763  4.384  1.00 22.63  ? 143 SER B CB    1 
ATOM   2119 O  OG    . SER B 1 126 ? 15.512  3.543  4.816  1.00 24.46  ? 143 SER B OG    1 
ATOM   2120 N  N     . ALA B 1 127 ? 12.533  4.415  6.188  1.00 26.39  ? 144 ALA B N     1 
ATOM   2121 C  CA    . ALA B 1 127 ? 11.743  3.499  7.007  1.00 29.05  ? 144 ALA B CA    1 
ATOM   2122 C  C     . ALA B 1 127 ? 12.465  2.174  7.199  1.00 25.68  ? 144 ALA B C     1 
ATOM   2123 O  O     . ALA B 1 127 ? 12.447  1.597  8.297  1.00 25.11  ? 144 ALA B O     1 
ATOM   2124 C  CB    . ALA B 1 127 ? 10.382  3.262  6.359  1.00 33.42  ? 144 ALA B CB    1 
ATOM   2125 N  N     . GLU B 1 128 ? 13.083  1.662  6.131  1.00 27.35  ? 145 GLU B N     1 
ATOM   2126 C  CA    . GLU B 1 128 ? 13.764  0.376  6.220  1.00 25.38  ? 145 GLU B CA    1 
ATOM   2127 C  C     . GLU B 1 128 ? 14.948  0.440  7.182  1.00 24.25  ? 145 GLU B C     1 
ATOM   2128 O  O     . GLU B 1 128 ? 15.149  -0.475 7.994  1.00 25.78  ? 145 GLU B O     1 
ATOM   2129 C  CB    . GLU B 1 128 ? 14.218  -0.079 4.829  1.00 26.58  ? 145 GLU B CB    1 
ATOM   2130 C  CG    . GLU B 1 128 ? 14.961  -1.421 4.859  1.00 47.60  ? 145 GLU B CG    1 
ATOM   2131 C  CD    . GLU B 1 128 ? 15.169  -2.028 3.478  1.00 76.59  ? 145 GLU B CD    1 
ATOM   2132 O  OE1   . GLU B 1 128 ? 14.633  -1.476 2.492  1.00 80.58  ? 145 GLU B OE1   1 
ATOM   2133 O  OE2   . GLU B 1 128 ? 15.867  -3.062 3.382  1.00 69.05  ? 145 GLU B OE2   1 
ATOM   2134 N  N     . SER B 1 129 ? 15.750  1.506  7.105  1.00 25.60  ? 146 SER B N     1 
ATOM   2135 C  CA    A SER B 1 129 ? 16.902  1.602  7.996  0.59 24.99  ? 146 SER B CA    1 
ATOM   2136 C  CA    B SER B 1 129 ? 16.902  1.652  7.992  0.41 25.01  ? 146 SER B CA    1 
ATOM   2137 C  C     . SER B 1 129 ? 16.480  1.878  9.434  1.00 24.98  ? 146 SER B C     1 
ATOM   2138 O  O     . SER B 1 129 ? 17.172  1.448  10.367 1.00 25.55  ? 146 SER B O     1 
ATOM   2139 C  CB    A SER B 1 129 ? 17.878  2.671  7.503  0.59 24.53  ? 146 SER B CB    1 
ATOM   2140 C  CB    B SER B 1 129 ? 17.773  2.816  7.531  0.41 23.98  ? 146 SER B CB    1 
ATOM   2141 O  OG    A SER B 1 129 ? 17.242  3.897  7.251  0.59 27.04  ? 146 SER B OG    1 
ATOM   2142 O  OG    B SER B 1 129 ? 18.290  2.554  6.246  0.41 21.34  ? 146 SER B OG    1 
ATOM   2143 N  N     . ALA B 1 130 ? 15.369  2.581  9.637  1.00 22.05  ? 147 ALA B N     1 
ATOM   2144 C  CA    . ALA B 1 130 ? 14.901  2.807  10.999 1.00 23.49  ? 147 ALA B CA    1 
ATOM   2145 C  C     . ALA B 1 130 ? 14.538  1.489  11.657 1.00 25.17  ? 147 ALA B C     1 
ATOM   2146 O  O     . ALA B 1 130 ? 14.910  1.231  12.804 1.00 26.03  ? 147 ALA B O     1 
ATOM   2147 C  CB    . ALA B 1 130 ? 13.706  3.769  11.006 1.00 23.79  ? 147 ALA B CB    1 
ATOM   2148 N  N     . LYS B 1 131 ? 13.833  0.623  10.930 1.00 23.71  ? 148 LYS B N     1 
ATOM   2149 C  CA    . LYS B 1 131 ? 13.473  -0.678 11.488 1.00 28.70  ? 148 LYS B CA    1 
ATOM   2150 C  C     . LYS B 1 131 ? 14.723  -1.496 11.794 1.00 26.78  ? 148 LYS B C     1 
ATOM   2151 O  O     . LYS B 1 131 ? 14.852  -2.080 12.879 1.00 30.62  ? 148 LYS B O     1 
ATOM   2152 C  CB    . LYS B 1 131 ? 12.546  -1.387 10.499 1.00 33.14  ? 148 LYS B CB    1 
ATOM   2153 C  CG    . LYS B 1 131 ? 12.260  -2.850 10.748 1.00 47.03  ? 148 LYS B CG    1 
ATOM   2154 C  CD    . LYS B 1 131 ? 11.321  -3.348 9.648  1.00 66.19  ? 148 LYS B CD    1 
ATOM   2155 C  CE    . LYS B 1 131 ? 10.895  -4.795 9.832  1.00 78.35  ? 148 LYS B CE    1 
ATOM   2156 N  NZ    . LYS B 1 131 ? 12.025  -5.741 9.641  1.00 86.91  ? 148 LYS B NZ    1 
ATOM   2157 N  N     . ARG B 1 132 ? 15.676  -1.507 10.860 1.00 25.02  ? 149 ARG B N     1 
ATOM   2158 C  CA    . ARG B 1 132 ? 16.912  -2.256 11.045 1.00 28.26  ? 149 ARG B CA    1 
ATOM   2159 C  C     . ARG B 1 132 ? 17.723  -1.721 12.225 1.00 27.59  ? 149 ARG B C     1 
ATOM   2160 O  O     . ARG B 1 132 ? 18.247  -2.497 13.039 1.00 26.23  ? 149 ARG B O     1 
ATOM   2161 C  CB    . ARG B 1 132 ? 17.728  -2.185 9.764  1.00 27.35  ? 149 ARG B CB    1 
ATOM   2162 C  CG    . ARG B 1 132 ? 18.940  -3.059 9.778  1.00 32.17  ? 149 ARG B CG    1 
ATOM   2163 C  CD    . ARG B 1 132 ? 19.691  -2.918 8.486  1.00 33.02  ? 149 ARG B CD    1 
ATOM   2164 N  NE    . ARG B 1 132 ? 20.536  -1.733 8.520  1.00 48.39  ? 149 ARG B NE    1 
ATOM   2165 C  CZ    . ARG B 1 132 ? 21.744  -1.703 9.065  1.00 52.60  ? 149 ARG B CZ    1 
ATOM   2166 N  NH1   . ARG B 1 132 ? 22.299  -2.792 9.585  1.00 48.83  ? 149 ARG B NH1   1 
ATOM   2167 N  NH2   . ARG B 1 132 ? 22.412  -0.556 9.092  1.00 45.28  ? 149 ARG B NH2   1 
ATOM   2168 N  N     . GLU B 1 133 ? 17.863  -0.390 12.317 1.00 25.70  ? 150 GLU B N     1 
ATOM   2169 C  CA    . GLU B 1 133 ? 18.704  0.198  13.356 1.00 22.47  ? 150 GLU B CA    1 
ATOM   2170 C  C     . GLU B 1 133 ? 18.061  0.074  14.733 1.00 26.60  ? 150 GLU B C     1 
ATOM   2171 O  O     . GLU B 1 133 ? 18.755  -0.173 15.728 1.00 25.61  ? 150 GLU B O     1 
ATOM   2172 C  CB    . GLU B 1 133 ? 18.996  1.666  13.023 1.00 22.14  ? 150 GLU B CB    1 
ATOM   2173 C  CG    . GLU B 1 133 ? 19.921  1.812  11.810 1.00 24.77  ? 150 GLU B CG    1 
ATOM   2174 C  CD    . GLU B 1 133 ? 19.996  3.219  11.243 1.00 28.52  ? 150 GLU B CD    1 
ATOM   2175 O  OE1   . GLU B 1 133 ? 19.412  4.166  11.824 1.00 24.31  ? 150 GLU B OE1   1 
ATOM   2176 O  OE2   . GLU B 1 133 ? 20.659  3.371  10.196 1.00 27.25  ? 150 GLU B OE2   1 
ATOM   2177 N  N     . ILE B 1 134 ? 16.747  0.266  14.830 1.00 25.32  ? 151 ILE B N     1 
ATOM   2178 C  CA    . ILE B 1 134 ? 16.104  0.089  16.126 1.00 25.67  ? 151 ILE B CA    1 
ATOM   2179 C  C     . ILE B 1 134 ? 16.290  -1.346 16.611 1.00 29.37  ? 151 ILE B C     1 
ATOM   2180 O  O     . ILE B 1 134 ? 16.560  -1.578 17.794 1.00 29.12  ? 151 ILE B O     1 
ATOM   2181 C  CB    . ILE B 1 134 ? 14.620  0.498  16.051 1.00 26.31  ? 151 ILE B CB    1 
ATOM   2182 C  CG1   . ILE B 1 134 ? 14.486  2.009  15.826 1.00 27.62  ? 151 ILE B CG1   1 
ATOM   2183 C  CG2   . ILE B 1 134 ? 13.890  0.116  17.329 1.00 28.88  ? 151 ILE B CG2   1 
ATOM   2184 C  CD1   . ILE B 1 134 ? 13.105  2.451  15.400 1.00 27.96  ? 151 ILE B CD1   1 
ATOM   2185 N  N     . SER B 1 135 ? 16.192  -2.328 15.701 1.00 27.77  ? 152 SER B N     1 
ATOM   2186 C  CA    . SER B 1 135 ? 16.364  -3.734 16.089 1.00 29.94  ? 152 SER B CA    1 
ATOM   2187 C  C     . SER B 1 135 ? 17.794  -4.026 16.523 1.00 33.44  ? 152 SER B C     1 
ATOM   2188 O  O     . SER B 1 135 ? 18.024  -4.869 17.397 1.00 37.47  ? 152 SER B O     1 
ATOM   2189 C  CB    . SER B 1 135 ? 15.990  -4.668 14.934 1.00 37.30  ? 152 SER B CB    1 
ATOM   2190 O  OG    . SER B 1 135 ? 14.627  -4.522 14.573 1.00 51.13  ? 152 SER B OG    1 
ATOM   2191 N  N     . LEU B 1 136 ? 18.765  -3.379 15.883 1.00 26.10  ? 153 LEU B N     1 
ATOM   2192 C  CA    . LEU B 1 136 ? 20.166  -3.611 16.201 1.00 26.67  ? 153 LEU B CA    1 
ATOM   2193 C  C     . LEU B 1 136 ? 20.524  -3.071 17.574 1.00 31.25  ? 153 LEU B C     1 
ATOM   2194 O  O     . LEU B 1 136 ? 21.213  -3.739 18.355 1.00 28.11  ? 153 LEU B O     1 
ATOM   2195 C  CB    . LEU B 1 136 ? 21.051  -2.970 15.128 1.00 28.31  ? 153 LEU B CB    1 
ATOM   2196 C  CG    . LEU B 1 136 ? 22.546  -2.980 15.412 1.00 30.97  ? 153 LEU B CG    1 
ATOM   2197 C  CD1   . LEU B 1 136 ? 23.085  -4.412 15.464 1.00 38.32  ? 153 LEU B CD1   1 
ATOM   2198 C  CD2   . LEU B 1 136 ? 23.277  -2.187 14.379 1.00 29.64  ? 153 LEU B CD2   1 
ATOM   2199 N  N     . TRP B 1 137 ? 20.078  -1.857 17.890 1.00 26.55  ? 154 TRP B N     1 
ATOM   2200 C  CA    . TRP B 1 137 ? 20.565  -1.202 19.087 1.00 27.80  ? 154 TRP B CA    1 
ATOM   2201 C  C     . TRP B 1 137 ? 19.657  -1.366 20.293 1.00 28.86  ? 154 TRP B C     1 
ATOM   2202 O  O     . TRP B 1 137 ? 20.106  -1.089 21.413 1.00 32.24  ? 154 TRP B O     1 
ATOM   2203 C  CB    . TRP B 1 137 ? 20.763  0.289  18.820 1.00 26.31  ? 154 TRP B CB    1 
ATOM   2204 C  CG    . TRP B 1 137 ? 21.870  0.635  17.846 1.00 24.61  ? 154 TRP B CG    1 
ATOM   2205 C  CD1   . TRP B 1 137 ? 21.747  0.822  16.525 1.00 23.92  ? 154 TRP B CD1   1 
ATOM   2206 C  CD2   . TRP B 1 137 ? 23.243  0.886  18.163 1.00 24.18  ? 154 TRP B CD2   1 
ATOM   2207 N  NE1   . TRP B 1 137 ? 22.956  1.166  15.973 1.00 25.33  ? 154 TRP B NE1   1 
ATOM   2208 C  CE2   . TRP B 1 137 ? 23.896  1.207  16.965 1.00 27.33  ? 154 TRP B CE2   1 
ATOM   2209 C  CE3   . TRP B 1 137 ? 23.985  0.854  19.350 1.00 27.55  ? 154 TRP B CE3   1 
ATOM   2210 C  CZ2   . TRP B 1 137 ? 25.249  1.517  16.912 1.00 29.04  ? 154 TRP B CZ2   1 
ATOM   2211 C  CZ3   . TRP B 1 137 ? 25.319  1.175  19.300 1.00 26.58  ? 154 TRP B CZ3   1 
ATOM   2212 C  CH2   . TRP B 1 137 ? 25.948  1.480  18.091 1.00 30.92  ? 154 TRP B CH2   1 
ATOM   2213 N  N     . PHE B 1 138 ? 18.402  -1.785 20.109 1.00 28.29  ? 155 PHE B N     1 
ATOM   2214 C  CA    . PHE B 1 138 ? 17.454  -1.905 21.214 1.00 31.45  ? 155 PHE B CA    1 
ATOM   2215 C  C     . PHE B 1 138 ? 16.835  -3.296 21.259 1.00 37.71  ? 155 PHE B C     1 
ATOM   2216 O  O     . PHE B 1 138 ? 16.569  -3.904 20.219 1.00 38.23  ? 155 PHE B O     1 
ATOM   2217 C  CB    . PHE B 1 138 ? 16.281  -0.907 21.105 1.00 30.54  ? 155 PHE B CB    1 
ATOM   2218 C  CG    . PHE B 1 138 ? 16.630  0.491  21.489 1.00 26.52  ? 155 PHE B CG    1 
ATOM   2219 C  CD1   . PHE B 1 138 ? 16.698  0.860  22.825 1.00 28.99  ? 155 PHE B CD1   1 
ATOM   2220 C  CD2   . PHE B 1 138 ? 16.860  1.449  20.528 1.00 23.26  ? 155 PHE B CD2   1 
ATOM   2221 C  CE1   . PHE B 1 138 ? 17.019  2.155  23.171 1.00 26.92  ? 155 PHE B CE1   1 
ATOM   2222 C  CE2   . PHE B 1 138 ? 17.172  2.739  20.878 1.00 23.23  ? 155 PHE B CE2   1 
ATOM   2223 C  CZ    . PHE B 1 138 ? 17.255  3.087  22.196 1.00 23.22  ? 155 PHE B CZ    1 
ATOM   2224 N  N     . LYS B 1 139 ? 16.545  -3.796 22.539 1.00 40.45  ? 156 LYS B N     1 
ATOM   2225 C  CA    . LYS B 1 139 ? 15.607  -4.899 22.697 1.00 32.98  ? 156 LYS B CA    1 
ATOM   2226 C  C     . LYS B 1 139 ? 14.186  -4.353 22.733 1.00 45.29  ? 156 LYS B C     1 
ATOM   2227 O  O     . LYS B 1 139 ? 13.969  -3.223 23.181 1.00 36.10  ? 156 LYS B O     1 
ATOM   2228 C  CB    . LYS B 1 139 ? 15.871  -5.668 23.985 1.00 48.66  ? 156 LYS B CB    1 
ATOM   2229 C  CG    . LYS B 1 139 ? 17.295  -5.596 24.489 1.00 46.81  ? 156 LYS B CG    1 
ATOM   2230 C  CD    . LYS B 1 139 ? 17.408  -6.196 25.872 1.00 58.44  ? 156 LYS B CD    1 
ATOM   2231 C  CE    . LYS B 1 139 ? 18.852  -6.227 26.323 1.00 64.66  ? 156 LYS B CE    1 
ATOM   2232 N  NZ    . LYS B 1 139 ? 19.705  -6.967 25.352 1.00 78.13  ? 156 LYS B NZ    1 
ATOM   2233 N  N     . PRO B 1 140 ? 13.198  -5.135 22.296 1.00 43.11  ? 157 PRO B N     1 
ATOM   2234 C  CA    . PRO B 1 140 ? 11.829  -4.596 22.213 1.00 52.11  ? 157 PRO B CA    1 
ATOM   2235 C  C     . PRO B 1 140 ? 11.252  -4.122 23.534 1.00 47.56  ? 157 PRO B C     1 
ATOM   2236 O  O     . PRO B 1 140 ? 10.363  -3.263 23.513 1.00 47.40  ? 157 PRO B O     1 
ATOM   2237 C  CB    . PRO B 1 140 ? 11.015  -5.767 21.632 1.00 47.56  ? 157 PRO B CB    1 
ATOM   2238 C  CG    . PRO B 1 140 ? 11.926  -6.939 21.609 1.00 53.41  ? 157 PRO B CG    1 
ATOM   2239 C  CD    . PRO B 1 140 ? 13.318  -6.408 21.566 1.00 52.27  ? 157 PRO B CD    1 
ATOM   2240 N  N     . GLU B 1 141 ? 11.690  -4.658 24.679 1.00 52.02  ? 158 GLU B N     1 
ATOM   2241 C  CA    . GLU B 1 141 ? 11.178  -4.146 25.949 1.00 59.42  ? 158 GLU B CA    1 
ATOM   2242 C  C     . GLU B 1 141 ? 11.633  -2.724 26.202 1.00 57.29  ? 158 GLU B C     1 
ATOM   2243 O  O     . GLU B 1 141 ? 11.025  -2.026 27.023 1.00 48.57  ? 158 GLU B O     1 
ATOM   2244 C  CB    . GLU B 1 141 ? 11.612  -5.021 27.137 1.00 70.57  ? 158 GLU B CB    1 
ATOM   2245 C  CG    . GLU B 1 141 ? 12.902  -4.627 27.864 1.00 64.81  ? 158 GLU B CG    1 
ATOM   2246 C  CD    . GLU B 1 141 ? 13.971  -5.693 27.771 1.00 68.54  ? 158 GLU B CD    1 
ATOM   2247 O  OE1   . GLU B 1 141 ? 13.952  -6.484 26.798 1.00 77.58  ? 158 GLU B OE1   1 
ATOM   2248 O  OE2   . GLU B 1 141 ? 14.830  -5.742 28.678 1.00 67.70  ? 158 GLU B OE2   1 
ATOM   2249 N  N     . GLU B 1 142 ? 12.720  -2.306 25.558 1.00 47.35  ? 159 GLU B N     1 
ATOM   2250 C  CA    . GLU B 1 142 ? 13.240  -0.966 25.755 1.00 36.81  ? 159 GLU B CA    1 
ATOM   2251 C  C     . GLU B 1 142 ? 12.441  0.087  24.999 1.00 30.18  ? 159 GLU B C     1 
ATOM   2252 O  O     . GLU B 1 142 ? 12.604  1.276  25.292 1.00 30.40  ? 159 GLU B O     1 
ATOM   2253 C  CB    . GLU B 1 142 ? 14.716  -0.937 25.356 1.00 34.46  ? 159 GLU B CB    1 
ATOM   2254 C  CG    . GLU B 1 142 ? 15.584  -1.831 26.247 1.00 45.16  ? 159 GLU B CG    1 
ATOM   2255 C  CD    . GLU B 1 142 ? 17.006  -1.965 25.746 1.00 51.31  ? 159 GLU B CD    1 
ATOM   2256 O  OE1   . GLU B 1 142 ? 17.188  -2.187 24.532 1.00 47.35  ? 159 GLU B OE1   1 
ATOM   2257 O  OE2   . GLU B 1 142 ? 17.945  -1.851 26.564 1.00 54.31  ? 159 GLU B OE2   1 
ATOM   2258 N  N     . ILE B 1 143 ? 11.576  -0.316 24.066 1.00 33.08  ? 160 ILE B N     1 
ATOM   2259 C  CA    . ILE B 1 143 ? 10.689  0.607  23.354 1.00 33.18  ? 160 ILE B CA    1 
ATOM   2260 C  C     . ILE B 1 143 ? 9.410   0.729  24.171 1.00 34.47  ? 160 ILE B C     1 
ATOM   2261 O  O     . ILE B 1 143 ? 8.727   -0.268 24.418 1.00 35.50  ? 160 ILE B O     1 
ATOM   2262 C  CB    . ILE B 1 143 ? 10.373  0.117  21.931 1.00 26.95  ? 160 ILE B CB    1 
ATOM   2263 C  CG1   . ILE B 1 143 ? 11.619  -0.423 21.227 1.00 37.55  ? 160 ILE B CG1   1 
ATOM   2264 C  CG2   . ILE B 1 143 ? 9.740   1.220  21.124 1.00 31.40  ? 160 ILE B CG2   1 
ATOM   2265 C  CD1   . ILE B 1 143 ? 12.778  0.495  21.240 1.00 39.59  ? 160 ILE B CD1   1 
ATOM   2266 N  N     . GLN B 1 144 ? 9.083   1.943  24.593 1.00 24.71  ? 161 GLN B N     1 
ATOM   2267 C  CA    . GLN B 1 144 ? 8.010   2.172  25.549 1.00 28.69  ? 161 GLN B CA    1 
ATOM   2268 C  C     . GLN B 1 144 ? 6.831   2.801  24.836 1.00 25.87  ? 161 GLN B C     1 
ATOM   2269 O  O     . GLN B 1 144 ? 7.010   3.724  24.040 1.00 28.21  ? 161 GLN B O     1 
ATOM   2270 C  CB    . GLN B 1 144 ? 8.477   3.079  26.686 1.00 29.00  ? 161 GLN B CB    1 
ATOM   2271 C  CG    . GLN B 1 144 ? 9.835   2.702  27.253 1.00 27.89  ? 161 GLN B CG    1 
ATOM   2272 C  CD    . GLN B 1 144 ? 9.833   1.328  27.867 1.00 29.35  ? 161 GLN B CD    1 
ATOM   2273 O  OE1   . GLN B 1 144 ? 8.792   0.829  28.275 1.00 33.16  ? 161 GLN B OE1   1 
ATOM   2274 N  NE2   . GLN B 1 144 ? 10.994  0.698  27.914 1.00 36.75  ? 161 GLN B NE2   1 
ATOM   2275 N  N     . SER B 1 145 ? 5.636   2.298  25.114 1.00 28.78  ? 162 SER B N     1 
ATOM   2276 C  CA    A SER B 1 145 ? 4.409   2.796  24.509 0.56 29.16  ? 162 SER B CA    1 
ATOM   2277 C  CA    B SER B 1 145 ? 4.405   2.788  24.511 0.44 29.18  ? 162 SER B CA    1 
ATOM   2278 C  C     . SER B 1 145 ? 3.640   3.617  25.535 1.00 31.20  ? 162 SER B C     1 
ATOM   2279 O  O     . SER B 1 145 ? 3.227   3.094  26.576 1.00 28.45  ? 162 SER B O     1 
ATOM   2280 C  CB    A SER B 1 145 ? 3.540   1.651  23.988 0.56 32.18  ? 162 SER B CB    1 
ATOM   2281 C  CB    B SER B 1 145 ? 3.550   1.622  24.015 0.44 32.14  ? 162 SER B CB    1 
ATOM   2282 O  OG    A SER B 1 145 ? 2.352   2.164  23.401 0.56 31.89  ? 162 SER B OG    1 
ATOM   2283 O  OG    B SER B 1 145 ? 4.319   0.738  23.221 0.44 34.28  ? 162 SER B OG    1 
ATOM   2284 N  N     . TYR B 1 146 ? 3.450   4.897  25.234 1.00 25.20  ? 163 TYR B N     1 
ATOM   2285 C  CA    . TYR B 1 146 ? 2.656   5.801  26.054 1.00 23.17  ? 163 TYR B CA    1 
ATOM   2286 C  C     . TYR B 1 146 ? 2.251   6.957  25.151 1.00 21.93  ? 163 TYR B C     1 
ATOM   2287 O  O     . TYR B 1 146 ? 2.768   7.104  24.043 1.00 22.03  ? 163 TYR B O     1 
ATOM   2288 C  CB    . TYR B 1 146 ? 3.412   6.271  27.313 1.00 23.31  ? 163 TYR B CB    1 
ATOM   2289 C  CG    . TYR B 1 146 ? 4.639   7.132  27.044 1.00 21.43  ? 163 TYR B CG    1 
ATOM   2290 C  CD1   . TYR B 1 146 ? 5.888   6.554  26.813 1.00 23.41  ? 163 TYR B CD1   1 
ATOM   2291 C  CD2   . TYR B 1 146 ? 4.545   8.512  26.999 1.00 20.43  ? 163 TYR B CD2   1 
ATOM   2292 C  CE1   . TYR B 1 146 ? 7.001   7.331  26.549 1.00 21.27  ? 163 TYR B CE1   1 
ATOM   2293 C  CE2   . TYR B 1 146 ? 5.651   9.295  26.733 1.00 20.97  ? 163 TYR B CE2   1 
ATOM   2294 C  CZ    . TYR B 1 146 ? 6.878   8.703  26.516 1.00 18.88  ? 163 TYR B CZ    1 
ATOM   2295 O  OH    . TYR B 1 146 ? 7.954   9.517  26.245 1.00 20.58  ? 163 TYR B OH    1 
ATOM   2296 N  N     . LYS B 1 147 ? 1.287   7.746  25.608 1.00 25.09  ? 164 LYS B N     1 
ATOM   2297 C  CA    . LYS B 1 147 ? 0.724   8.842  24.821 1.00 22.10  ? 164 LYS B CA    1 
ATOM   2298 C  C     . LYS B 1 147 ? 1.100   10.175 25.451 1.00 18.99  ? 164 LYS B C     1 
ATOM   2299 O  O     . LYS B 1 147 ? 1.070   10.312 26.670 1.00 22.26  ? 164 LYS B O     1 
ATOM   2300 C  CB    . LYS B 1 147 ? -0.802  8.705  24.746 1.00 26.48  ? 164 LYS B CB    1 
ATOM   2301 C  CG    . LYS B 1 147 ? -1.528  9.915  24.181 1.00 34.76  ? 164 LYS B CG    1 
ATOM   2302 C  CD    . LYS B 1 147 ? -3.047  9.732  24.187 1.00 47.82  ? 164 LYS B CD    1 
ATOM   2303 C  CE    . LYS B 1 147 ? -3.750  10.914 23.515 1.00 57.27  ? 164 LYS B CE    1 
ATOM   2304 N  NZ    . LYS B 1 147 ? -5.141  10.589 23.087 1.00 67.67  ? 164 LYS B NZ    1 
ATOM   2305 N  N     . LEU B 1 148 ? 1.458   11.162 24.629 1.00 22.59  ? 165 LEU B N     1 
ATOM   2306 C  CA    . LEU B 1 148 ? 1.762   12.485 25.155 1.00 20.67  ? 165 LEU B CA    1 
ATOM   2307 C  C     . LEU B 1 148 ? 0.480   13.211 25.511 1.00 21.44  ? 165 LEU B C     1 
ATOM   2308 O  O     . LEU B 1 148 ? -0.451  13.289 24.697 1.00 21.34  ? 165 LEU B O     1 
ATOM   2309 C  CB    . LEU B 1 148 ? 2.539   13.321 24.138 1.00 20.18  ? 165 LEU B CB    1 
ATOM   2310 C  CG    . LEU B 1 148 ? 3.983   12.928 23.880 1.00 21.09  ? 165 LEU B CG    1 
ATOM   2311 C  CD1   . LEU B 1 148 ? 4.487   13.746 22.692 1.00 20.97  ? 165 LEU B CD1   1 
ATOM   2312 C  CD2   . LEU B 1 148 ? 4.846   13.117 25.151 1.00 22.33  ? 165 LEU B CD2   1 
ATOM   2313 N  N     . ALA B 1 149 ? 0.458   13.785 26.707 1.00 20.29  ? 166 ALA B N     1 
ATOM   2314 C  CA    . ALA B 1 149 ? -0.708  14.499 27.195 1.00 22.55  ? 166 ALA B CA    1 
ATOM   2315 C  C     . ALA B 1 149 ? -1.059  15.718 26.352 1.00 22.97  ? 166 ALA B C     1 
ATOM   2316 O  O     . ALA B 1 149 ? -2.231  16.128 26.341 1.00 24.06  ? 166 ALA B O     1 
ATOM   2317 C  CB    . ALA B 1 149 ? -0.475  14.908 28.648 1.00 30.20  ? 166 ALA B CB    1 
ATOM   2318 N  N     . LEU B 1 150 ? -0.098  16.298 25.629 1.00 20.64  ? 167 LEU B N     1 
ATOM   2319 C  CA    . LEU B 1 150 ? -0.374  17.459 24.790 1.00 20.84  ? 167 LEU B CA    1 
ATOM   2320 C  C     . LEU B 1 150 ? -0.765  17.062 23.358 1.00 18.28  ? 167 LEU B C     1 
ATOM   2321 O  O     . LEU B 1 150 ? -0.789  17.922 22.482 1.00 18.46  ? 167 LEU B O     1 
ATOM   2322 C  CB    . LEU B 1 150 ? 0.834   18.416 24.783 1.00 21.58  ? 167 LEU B CB    1 
ATOM   2323 C  CG    . LEU B 1 150 ? 0.973   19.407 25.959 1.00 19.86  ? 167 LEU B CG    1 
ATOM   2324 C  CD1   . LEU B 1 150 ? 2.333   20.051 25.969 1.00 27.98  ? 167 LEU B CD1   1 
ATOM   2325 C  CD2   . LEU B 1 150 ? -0.091  20.458 25.922 1.00 31.32  ? 167 LEU B CD2   1 
ATOM   2326 N  N     . SER B 1 151 ? -1.122  15.792 23.130 1.00 18.55  ? 168 SER B N     1 
ATOM   2327 C  CA    A SER B 1 151 ? -1.412  15.299 21.784 0.25 19.48  ? 168 SER B CA    1 
ATOM   2328 C  CA    B SER B 1 151 ? -1.392  15.319 21.772 0.75 19.38  ? 168 SER B CA    1 
ATOM   2329 C  C     . SER B 1 151 ? -2.419  16.179 21.049 1.00 18.55  ? 168 SER B C     1 
ATOM   2330 O  O     . SER B 1 151 ? -2.256  16.460 19.858 1.00 21.05  ? 168 SER B O     1 
ATOM   2331 C  CB    A SER B 1 151 ? -1.936  13.861 21.878 0.25 21.68  ? 168 SER B CB    1 
ATOM   2332 C  CB    B SER B 1 151 ? -1.871  13.864 21.793 0.75 21.49  ? 168 SER B CB    1 
ATOM   2333 O  OG    A SER B 1 151 ? -2.236  13.311 20.609 0.25 21.30  ? 168 SER B OG    1 
ATOM   2334 O  OG    B SER B 1 151 ? -0.775  12.979 21.935 0.75 28.83  ? 168 SER B OG    1 
ATOM   2335 N  N     . ASP B 1 152 ? -3.470  16.633 21.747 1.00 20.28  ? 169 ASP B N     1 
ATOM   2336 C  CA    . ASP B 1 152 ? -4.515  17.400 21.062 1.00 23.67  ? 169 ASP B CA    1 
ATOM   2337 C  C     . ASP B 1 152 ? -4.008  18.725 20.489 1.00 21.34  ? 169 ASP B C     1 
ATOM   2338 O  O     . ASP B 1 152 ? -4.652  19.289 19.592 1.00 22.57  ? 169 ASP B O     1 
ATOM   2339 C  CB    . ASP B 1 152 ? -5.676  17.704 22.015 1.00 25.24  ? 169 ASP B CB    1 
ATOM   2340 C  CG    . ASP B 1 152 ? -6.463  16.472 22.416 1.00 38.26  ? 169 ASP B CG    1 
ATOM   2341 O  OD1   . ASP B 1 152 ? -6.467  15.466 21.675 1.00 32.86  ? 169 ASP B OD1   1 
ATOM   2342 O  OD2   . ASP B 1 152 ? -7.091  16.531 23.490 1.00 49.44  ? 169 ASP B OD2   1 
ATOM   2343 N  N     . TYR B 1 153 ? -2.896  19.250 21.001 1.00 16.25  ? 170 TYR B N     1 
ATOM   2344 C  CA    . TYR B 1 153 ? -2.338  20.514 20.548 1.00 15.19  ? 170 TYR B CA    1 
ATOM   2345 C  C     . TYR B 1 153 ? -1.104  20.310 19.685 1.00 16.79  ? 170 TYR B C     1 
ATOM   2346 O  O     . TYR B 1 153 ? -0.561  21.282 19.168 1.00 18.48  ? 170 TYR B O     1 
ATOM   2347 C  CB    . TYR B 1 153 ? -2.029  21.418 21.763 1.00 18.14  ? 170 TYR B CB    1 
ATOM   2348 C  CG    . TYR B 1 153 ? -3.318  21.756 22.462 1.00 18.10  ? 170 TYR B CG    1 
ATOM   2349 C  CD1   . TYR B 1 153 ? -4.165  22.732 21.959 1.00 19.48  ? 170 TYR B CD1   1 
ATOM   2350 C  CD2   . TYR B 1 153 ? -3.746  21.016 23.550 1.00 18.40  ? 170 TYR B CD2   1 
ATOM   2351 C  CE1   . TYR B 1 153 ? -5.391  23.002 22.565 1.00 20.63  ? 170 TYR B CE1   1 
ATOM   2352 C  CE2   . TYR B 1 153 ? -4.969  21.274 24.153 1.00 20.62  ? 170 TYR B CE2   1 
ATOM   2353 C  CZ    . TYR B 1 153 ? -5.771  22.263 23.665 1.00 21.23  ? 170 TYR B CZ    1 
ATOM   2354 O  OH    . TYR B 1 153 ? -6.973  22.498 24.289 1.00 26.08  ? 170 TYR B OH    1 
ATOM   2355 N  N     . ILE B 1 154 ? -0.655  19.071 19.517 1.00 18.25  ? 171 ILE B N     1 
ATOM   2356 C  CA    . ILE B 1 154 ? 0.470   18.759 18.637 1.00 17.66  ? 171 ILE B CA    1 
ATOM   2357 C  C     . ILE B 1 154 ? -0.009  18.234 17.288 1.00 17.97  ? 171 ILE B C     1 
ATOM   2358 O  O     . ILE B 1 154 ? 0.526   18.616 16.250 1.00 21.53  ? 171 ILE B O     1 
ATOM   2359 C  CB    . ILE B 1 154 ? 1.406   17.744 19.322 1.00 18.00  ? 171 ILE B CB    1 
ATOM   2360 C  CG1   . ILE B 1 154 ? 2.072   18.368 20.554 1.00 18.42  ? 171 ILE B CG1   1 
ATOM   2361 C  CG2   . ILE B 1 154 ? 2.450   17.201 18.316 1.00 20.76  ? 171 ILE B CG2   1 
ATOM   2362 C  CD1   . ILE B 1 154 ? 2.609   17.335 21.530 1.00 25.03  ? 171 ILE B CD1   1 
ATOM   2363 N  N     . PHE B 1 155 ? -1.028  17.359 17.281 1.00 17.18  ? 172 PHE B N     1 
ATOM   2364 C  CA    . PHE B 1 155 ? -1.533  16.727 16.077 1.00 20.16  ? 172 PHE B CA    1 
ATOM   2365 C  C     . PHE B 1 155 ? -2.874  17.323 15.667 1.00 20.26  ? 172 PHE B C     1 
ATOM   2366 O  O     . PHE B 1 155 ? -3.683  17.726 16.514 1.00 24.01  ? 172 PHE B O     1 
ATOM   2367 C  CB    . PHE B 1 155 ? -1.679  15.227 16.302 1.00 21.74  ? 172 PHE B CB    1 
ATOM   2368 C  CG    . PHE B 1 155 ? -0.441  14.583 16.840 1.00 18.88  ? 172 PHE B CG    1 
ATOM   2369 C  CD1   . PHE B 1 155 ? 0.675   14.464 16.045 1.00 20.70  ? 172 PHE B CD1   1 
ATOM   2370 C  CD2   . PHE B 1 155 ? -0.386  14.119 18.138 1.00 21.93  ? 172 PHE B CD2   1 
ATOM   2371 C  CE1   . PHE B 1 155 ? 1.820   13.882 16.526 1.00 21.95  ? 172 PHE B CE1   1 
ATOM   2372 C  CE2   . PHE B 1 155 ? 0.770   13.530 18.628 1.00 25.03  ? 172 PHE B CE2   1 
ATOM   2373 C  CZ    . PHE B 1 155 ? 1.869   13.414 17.817 1.00 23.08  ? 172 PHE B CZ    1 
ATOM   2374 N  N     . GLU B 1 156 ? -3.091  17.393 14.356 1.00 24.05  ? 173 GLU B N     1 
ATOM   2375 C  CA    . GLU B 1 156 ? -4.301  18.007 13.810 1.00 30.71  ? 173 GLU B CA    1 
ATOM   2376 C  C     . GLU B 1 156 ? -5.427  16.985 13.874 1.00 44.24  ? 173 GLU B C     1 
ATOM   2377 O  O     . GLU B 1 156 ? -6.605  17.338 13.811 1.00 46.22  ? 173 GLU B O     1 
ATOM   2378 C  CB    . GLU B 1 156 ? -4.070  18.527 12.369 1.00 32.51  ? 173 GLU B CB    1 
ATOM   2379 C  CG    . GLU B 1 156 ? -3.598  17.504 11.367 1.00 39.60  ? 173 GLU B CG    1 
ATOM   2380 C  CD    . GLU B 1 156 ? -3.327  18.091 9.974  1.00 43.70  ? 173 GLU B CD    1 
ATOM   2381 O  OE1   . GLU B 1 156 ? -2.833  19.241 9.850  1.00 24.52  ? 173 GLU B OE1   1 
ATOM   2382 O  OE2   . GLU B 1 156 ? -3.605  17.379 8.987  1.00 43.33  ? 173 GLU B OE2   1 
ATOM   2383 O  OXT   . GLU B 1 156 ? -5.180  15.787 14.037 1.00 40.05  ? 173 GLU B OXT   1 
ATOM   2384 N  N     . HIS C 1 8   ? 43.210  21.217 9.152  1.00 45.99  ? 25  HIS C N     1 
ATOM   2385 C  CA    . HIS C 1 8   ? 43.578  22.413 8.398  1.00 37.86  ? 25  HIS C CA    1 
ATOM   2386 C  C     . HIS C 1 8   ? 42.646  23.581 8.740  1.00 35.54  ? 25  HIS C C     1 
ATOM   2387 O  O     . HIS C 1 8   ? 41.582  23.739 8.138  1.00 35.27  ? 25  HIS C O     1 
ATOM   2388 C  CB    . HIS C 1 8   ? 43.535  22.135 6.900  1.00 43.39  ? 25  HIS C CB    1 
ATOM   2389 N  N     . VAL C 1 9   ? 43.041  24.414 9.697  1.00 28.98  ? 26  VAL C N     1 
ATOM   2390 C  CA    . VAL C 1 9   ? 42.187  25.498 10.148 1.00 23.02  ? 26  VAL C CA    1 
ATOM   2391 C  C     . VAL C 1 9   ? 42.658  26.816 9.548  1.00 24.97  ? 26  VAL C C     1 
ATOM   2392 O  O     . VAL C 1 9   ? 43.780  26.956 9.040  1.00 24.08  ? 26  VAL C O     1 
ATOM   2393 C  CB    . VAL C 1 9   ? 42.139  25.585 11.692 1.00 23.66  ? 26  VAL C CB    1 
ATOM   2394 C  CG1   . VAL C 1 9   ? 41.538  24.332 12.265 1.00 26.79  ? 26  VAL C CG1   1 
ATOM   2395 C  CG2   . VAL C 1 9   ? 43.514  25.837 12.268 1.00 24.69  ? 26  VAL C CG2   1 
ATOM   2396 N  N     . GLU C 1 10  ? 41.771  27.802 9.575  1.00 18.99  ? 27  GLU C N     1 
ATOM   2397 C  CA    . GLU C 1 10  ? 42.137  29.164 9.248  1.00 22.94  ? 27  GLU C CA    1 
ATOM   2398 C  C     . GLU C 1 10  ? 41.575  30.087 10.318 1.00 18.82  ? 27  GLU C C     1 
ATOM   2399 O  O     . GLU C 1 10  ? 40.898  29.647 11.257 1.00 19.31  ? 27  GLU C O     1 
ATOM   2400 C  CB    . GLU C 1 10  ? 41.643  29.538 7.848  1.00 26.32  ? 27  GLU C CB    1 
ATOM   2401 C  CG    . GLU C 1 10  ? 40.175  29.418 7.711  1.00 23.61  ? 27  GLU C CG    1 
ATOM   2402 C  CD    . GLU C 1 10  ? 39.687  29.552 6.266  1.00 25.42  ? 27  GLU C CD    1 
ATOM   2403 O  OE1   . GLU C 1 10  ? 40.452  29.387 5.289  1.00 36.49  ? 27  GLU C OE1   1 
ATOM   2404 O  OE2   . GLU C 1 10  ? 38.510  29.849 6.127  1.00 19.99  ? 27  GLU C OE2   1 
ATOM   2405 N  N     . GLN C 1 11  ? 41.895  31.368 10.184 1.00 20.45  ? 28  GLN C N     1 
ATOM   2406 C  CA    . GLN C 1 11  ? 41.475  32.409 11.108 1.00 18.64  ? 28  GLN C CA    1 
ATOM   2407 C  C     . GLN C 1 11  ? 40.728  33.493 10.357 1.00 17.46  ? 28  GLN C C     1 
ATOM   2408 O  O     . GLN C 1 11  ? 41.134  33.887 9.258  1.00 18.25  ? 28  GLN C O     1 
ATOM   2409 C  CB    . GLN C 1 11  ? 42.671  33.006 11.836 1.00 20.72  ? 28  GLN C CB    1 
ATOM   2410 C  CG    . GLN C 1 11  ? 43.329  31.985 12.727 1.00 23.07  ? 28  GLN C CG    1 
ATOM   2411 C  CD    . GLN C 1 11  ? 44.322  32.576 13.712 1.00 25.52  ? 28  GLN C CD    1 
ATOM   2412 O  OE1   . GLN C 1 11  ? 44.727  33.736 13.604 1.00 29.89  ? 28  GLN C OE1   1 
ATOM   2413 N  NE2   . GLN C 1 11  ? 44.746  31.760 14.662 1.00 24.92  ? 28  GLN C NE2   1 
ATOM   2414 N  N     . THR C 1 12  ? 39.637  33.968 10.947 1.00 18.50  ? 29  THR C N     1 
ATOM   2415 C  CA    . THR C 1 12  ? 38.880  35.069 10.382 1.00 14.69  ? 29  THR C CA    1 
ATOM   2416 C  C     . THR C 1 12  ? 38.775  36.210 11.378 1.00 18.45  ? 29  THR C C     1 
ATOM   2417 O  O     . THR C 1 12  ? 38.871  36.000 12.592 1.00 17.67  ? 29  THR C O     1 
ATOM   2418 C  CB    . THR C 1 12  ? 37.481  34.625 9.936  1.00 16.13  ? 29  THR C CB    1 
ATOM   2419 O  OG1   . THR C 1 12  ? 36.928  35.654 9.115  1.00 18.05  ? 29  THR C OG1   1 
ATOM   2420 C  CG2   . THR C 1 12  ? 36.564  34.361 11.139 1.00 16.50  ? 29  THR C CG2   1 
ATOM   2421 N  N     . TYR C 1 13  ? 38.609  37.431 10.855 1.00 15.98  ? 30  TYR C N     1 
ATOM   2422 C  CA    . TYR C 1 13  ? 38.378  38.614 11.680 1.00 14.68  ? 30  TYR C CA    1 
ATOM   2423 C  C     . TYR C 1 13  ? 36.874  38.859 11.782 1.00 15.93  ? 30  TYR C C     1 
ATOM   2424 O  O     . TYR C 1 13  ? 36.187  39.000 10.767 1.00 16.01  ? 30  TYR C O     1 
ATOM   2425 C  CB    . TYR C 1 13  ? 39.084  39.853 11.111 1.00 16.27  ? 30  TYR C CB    1 
ATOM   2426 C  CG    . TYR C 1 13  ? 38.817  41.087 11.945 1.00 15.64  ? 30  TYR C CG    1 
ATOM   2427 C  CD1   . TYR C 1 13  ? 39.339  41.202 13.229 1.00 17.76  ? 30  TYR C CD1   1 
ATOM   2428 C  CD2   . TYR C 1 13  ? 38.021  42.115 11.471 1.00 16.80  ? 30  TYR C CD2   1 
ATOM   2429 C  CE1   . TYR C 1 13  ? 39.068  42.311 14.028 1.00 18.75  ? 30  TYR C CE1   1 
ATOM   2430 C  CE2   . TYR C 1 13  ? 37.737  43.241 12.277 1.00 19.72  ? 30  TYR C CE2   1 
ATOM   2431 C  CZ    . TYR C 1 13  ? 38.270  43.316 13.555 1.00 19.90  ? 30  TYR C CZ    1 
ATOM   2432 O  OH    . TYR C 1 13  ? 38.005  44.391 14.371 1.00 20.71  ? 30  TYR C OH    1 
ATOM   2433 N  N     . LEU C 1 14  ? 36.360  38.866 13.007 1.00 15.34  ? 31  LEU C N     1 
ATOM   2434 C  CA    . LEU C 1 14  ? 34.972  39.195 13.293 1.00 14.95  ? 31  LEU C CA    1 
ATOM   2435 C  C     . LEU C 1 14  ? 34.934  40.395 14.217 1.00 16.35  ? 31  LEU C C     1 
ATOM   2436 O  O     . LEU C 1 14  ? 35.710  40.471 15.179 1.00 17.95  ? 31  LEU C O     1 
ATOM   2437 C  CB    . LEU C 1 14  ? 34.249  38.013 13.921 1.00 15.48  ? 31  LEU C CB    1 
ATOM   2438 C  CG    . LEU C 1 14  ? 34.025  36.840 12.968 1.00 18.40  ? 31  LEU C CG    1 
ATOM   2439 C  CD1   . LEU C 1 14  ? 33.817  35.530 13.688 1.00 23.51  ? 31  LEU C CD1   1 
ATOM   2440 C  CD2   . LEU C 1 14  ? 32.809  37.172 12.114 1.00 23.89  ? 31  LEU C CD2   1 
ATOM   2441 N  N     . MET C 1 15  ? 34.009  41.316 13.961 1.00 15.10  ? 32  MET C N     1 
ATOM   2442 C  CA    . MET C 1 15  ? 33.919  42.533 14.751 1.00 17.42  ? 32  MET C CA    1 
ATOM   2443 C  C     . MET C 1 15  ? 32.470  42.800 15.124 1.00 16.76  ? 32  MET C C     1 
ATOM   2444 O  O     . MET C 1 15  ? 31.617  42.974 14.248 1.00 17.81  ? 32  MET C O     1 
ATOM   2445 C  CB    . MET C 1 15  ? 34.493  43.728 13.977 1.00 20.02  ? 32  MET C CB    1 
ATOM   2446 C  CG    . MET C 1 15  ? 34.502  45.009 14.766 1.00 17.57  ? 32  MET C CG    1 
ATOM   2447 S  SD    . MET C 1 15  ? 35.520  46.323 13.985 1.00 22.49  ? 32  MET C SD    1 
ATOM   2448 C  CE    . MET C 1 15  ? 34.879  46.327 12.318 1.00 25.67  ? 32  MET C CE    1 
ATOM   2449 N  N     . ILE C 1 16  ? 32.196  42.860 16.416 1.00 14.01  ? 33  ILE C N     1 
ATOM   2450 C  CA    . ILE C 1 16  ? 30.878  43.277 16.867 1.00 14.43  ? 33  ILE C CA    1 
ATOM   2451 C  C     . ILE C 1 16  ? 30.799  44.797 16.766 1.00 15.61  ? 33  ILE C C     1 
ATOM   2452 O  O     . ILE C 1 16  ? 31.632  45.519 17.323 1.00 16.09  ? 33  ILE C O     1 
ATOM   2453 C  CB    . ILE C 1 16  ? 30.603  42.789 18.294 1.00 13.05  ? 33  ILE C CB    1 
ATOM   2454 C  CG1   . ILE C 1 16  ? 30.756  41.268 18.360 1.00 15.62  ? 33  ILE C CG1   1 
ATOM   2455 C  CG2   . ILE C 1 16  ? 29.194  43.186 18.735 1.00 14.94  ? 33  ILE C CG2   1 
ATOM   2456 C  CD1   . ILE C 1 16  ? 30.462  40.677 19.746 1.00 19.78  ? 33  ILE C CD1   1 
ATOM   2457 N  N     . LYS C 1 17  ? 29.818  45.275 16.015 1.00 15.25  ? 34  LYS C N     1 
ATOM   2458 C  CA    . LYS C 1 17  ? 29.635  46.694 15.756 1.00 17.11  ? 34  LYS C CA    1 
ATOM   2459 C  C     . LYS C 1 17  ? 29.001  47.372 16.960 1.00 16.35  ? 34  LYS C C     1 
ATOM   2460 O  O     . LYS C 1 17  ? 28.572  46.713 17.923 1.00 16.04  ? 34  LYS C O     1 
ATOM   2461 C  CB    . LYS C 1 17  ? 28.782  46.862 14.506 1.00 15.22  ? 34  LYS C CB    1 
ATOM   2462 C  CG    . LYS C 1 17  ? 29.410  46.214 13.264 1.00 15.63  ? 34  LYS C CG    1 
ATOM   2463 C  CD    . LYS C 1 17  ? 28.525  46.381 11.997 1.00 16.64  ? 34  LYS C CD    1 
ATOM   2464 C  CE    . LYS C 1 17  ? 29.250  45.932 10.754 1.00 17.26  ? 34  LYS C CE    1 
ATOM   2465 N  NZ    . LYS C 1 17  ? 28.398  46.072 9.567  1.00 18.74  ? 34  LYS C NZ    1 
ATOM   2466 N  N     . PRO C 1 18  ? 28.966  48.706 16.967 1.00 15.27  ? 35  PRO C N     1 
ATOM   2467 C  CA    . PRO C 1 18  ? 28.433  49.403 18.144 1.00 16.90  ? 35  PRO C CA    1 
ATOM   2468 C  C     . PRO C 1 18  ? 27.030  48.996 18.514 1.00 15.72  ? 35  PRO C C     1 
ATOM   2469 O  O     . PRO C 1 18  ? 26.717  49.004 19.714 1.00 16.20  ? 35  PRO C O     1 
ATOM   2470 C  CB    . PRO C 1 18  ? 28.516  50.885 17.743 1.00 17.39  ? 35  PRO C CB    1 
ATOM   2471 C  CG    . PRO C 1 18  ? 29.706  50.925 16.847 1.00 18.47  ? 35  PRO C CG    1 
ATOM   2472 C  CD    . PRO C 1 18  ? 29.599  49.649 16.019 1.00 16.60  ? 35  PRO C CD    1 
ATOM   2473 N  N     . ASP C 1 19  ? 26.176  48.639 17.547 1.00 14.99  ? 36  ASP C N     1 
ATOM   2474 C  CA    . ASP C 1 19  ? 24.829  48.189 17.879 1.00 16.06  ? 36  ASP C CA    1 
ATOM   2475 C  C     . ASP C 1 19  ? 24.844  46.859 18.633 1.00 14.50  ? 36  ASP C C     1 
ATOM   2476 O  O     . ASP C 1 19  ? 23.995  46.637 19.502 1.00 15.71  ? 36  ASP C O     1 
ATOM   2477 C  CB    . ASP C 1 19  ? 23.941  48.126 16.622 1.00 15.70  ? 36  ASP C CB    1 
ATOM   2478 C  CG    . ASP C 1 19  ? 24.549  47.346 15.453 1.00 16.84  ? 36  ASP C CG    1 
ATOM   2479 O  OD1   . ASP C 1 19  ? 25.768  47.421 15.229 1.00 19.91  ? 36  ASP C OD1   1 
ATOM   2480 O  OD2   . ASP C 1 19  ? 23.765  46.691 14.719 1.00 16.48  ? 36  ASP C OD2   1 
ATOM   2481 N  N     . GLY C 1 20  ? 25.802  45.973 18.351 1.00 16.21  ? 37  GLY C N     1 
ATOM   2482 C  CA    . GLY C 1 20  ? 25.908  44.760 19.152 1.00 16.93  ? 37  GLY C CA    1 
ATOM   2483 C  C     . GLY C 1 20  ? 26.322  45.048 20.586 1.00 13.78  ? 37  GLY C C     1 
ATOM   2484 O  O     . GLY C 1 20  ? 25.825  44.416 21.533 1.00 15.22  ? 37  GLY C O     1 
ATOM   2485 N  N     . ILE C 1 21  ? 27.233  46.008 20.765 1.00 14.51  ? 38  ILE C N     1 
ATOM   2486 C  CA    . ILE C 1 21  ? 27.635  46.421 22.115 1.00 14.40  ? 38  ILE C CA    1 
ATOM   2487 C  C     . ILE C 1 21  ? 26.464  47.054 22.857 1.00 13.69  ? 38  ILE C C     1 
ATOM   2488 O  O     . ILE C 1 21  ? 26.149  46.686 24.001 1.00 14.26  ? 38  ILE C O     1 
ATOM   2489 C  CB    . ILE C 1 21  ? 28.821  47.397 22.049 1.00 16.49  ? 38  ILE C CB    1 
ATOM   2490 C  CG1   . ILE C 1 21  ? 29.994  46.846 21.226 1.00 19.64  ? 38  ILE C CG1   1 
ATOM   2491 C  CG2   . ILE C 1 21  ? 29.245  47.782 23.455 1.00 18.18  ? 38  ILE C CG2   1 
ATOM   2492 C  CD1   . ILE C 1 21  ? 30.504  45.545 21.677 1.00 18.29  ? 38  ILE C CD1   1 
ATOM   2493 N  N     . GLN C 1 22  ? 25.805  48.024 22.213 1.00 15.69  ? 39  GLN C N     1 
ATOM   2494 C  CA    . GLN C 1 22  ? 24.771  48.816 22.882 1.00 16.74  ? 39  GLN C CA    1 
ATOM   2495 C  C     . GLN C 1 22  ? 23.513  47.999 23.161 1.00 13.66  ? 39  GLN C C     1 
ATOM   2496 O  O     . GLN C 1 22  ? 22.827  48.246 24.149 1.00 16.38  ? 39  GLN C O     1 
ATOM   2497 C  CB    . GLN C 1 22  ? 24.449  50.059 22.035 1.00 15.79  ? 39  GLN C CB    1 
ATOM   2498 C  CG    . GLN C 1 22  ? 25.520  51.120 22.068 1.00 15.99  ? 39  GLN C CG    1 
ATOM   2499 C  CD    . GLN C 1 22  ? 25.558  51.861 23.363 1.00 20.31  ? 39  GLN C CD    1 
ATOM   2500 O  OE1   . GLN C 1 22  ? 24.735  51.611 24.245 1.00 21.22  ? 39  GLN C OE1   1 
ATOM   2501 N  NE2   . GLN C 1 22  ? 26.491  52.807 23.486 1.00 22.65  ? 39  GLN C NE2   1 
ATOM   2502 N  N     . ARG C 1 23  ? 23.176  47.039 22.293 1.00 13.66  ? 40  ARG C N     1 
ATOM   2503 C  CA    . ARG C 1 23  ? 22.040  46.161 22.525 1.00 12.93  ? 40  ARG C CA    1 
ATOM   2504 C  C     . ARG C 1 23  ? 22.386  45.037 23.490 1.00 15.16  ? 40  ARG C C     1 
ATOM   2505 O  O     . ARG C 1 23  ? 21.493  44.277 23.878 1.00 16.62  ? 40  ARG C O     1 
ATOM   2506 C  CB    . ARG C 1 23  ? 21.527  45.622 21.177 1.00 14.57  ? 40  ARG C CB    1 
ATOM   2507 C  CG    . ARG C 1 23  ? 20.932  46.735 20.304 1.00 14.01  ? 40  ARG C CG    1 
ATOM   2508 C  CD    . ARG C 1 23  ? 20.528  46.229 18.937 1.00 16.03  ? 40  ARG C CD    1 
ATOM   2509 N  NE    . ARG C 1 23  ? 19.358  45.370 19.018 1.00 15.21  ? 40  ARG C NE    1 
ATOM   2510 C  CZ    . ARG C 1 23  ? 18.994  44.504 18.087 1.00 16.54  ? 40  ARG C CZ    1 
ATOM   2511 N  NH1   . ARG C 1 23  ? 19.667  44.386 16.954 1.00 15.67  ? 40  ARG C NH1   1 
ATOM   2512 N  NH2   . ARG C 1 23  ? 17.971  43.688 18.330 1.00 16.23  ? 40  ARG C NH2   1 
ATOM   2513 N  N     . GLN C 1 24  ? 23.656  44.945 23.886 1.00 12.63  ? 41  GLN C N     1 
ATOM   2514 C  CA    . GLN C 1 24  ? 24.126  44.063 24.950 1.00 14.42  ? 41  GLN C CA    1 
ATOM   2515 C  C     . GLN C 1 24  ? 23.879  42.597 24.613 1.00 12.75  ? 41  GLN C C     1 
ATOM   2516 O  O     . GLN C 1 24  ? 23.404  41.810 25.444 1.00 15.37  ? 41  GLN C O     1 
ATOM   2517 C  CB    . GLN C 1 24  ? 23.524  44.470 26.293 1.00 17.01  ? 41  GLN C CB    1 
ATOM   2518 C  CG    . GLN C 1 24  ? 23.943  45.897 26.650 1.00 16.95  ? 41  GLN C CG    1 
ATOM   2519 C  CD    . GLN C 1 24  ? 24.289  46.070 28.111 1.00 20.37  ? 41  GLN C CD    1 
ATOM   2520 O  OE1   . GLN C 1 24  ? 23.419  46.399 28.897 1.00 19.20  ? 41  GLN C OE1   1 
ATOM   2521 N  NE2   . GLN C 1 24  ? 25.557  45.868 28.473 1.00 18.08  ? 41  GLN C NE2   1 
ATOM   2522 N  N     . VAL C 1 25  ? 24.277  42.231 23.386 1.00 13.04  ? 42  VAL C N     1 
ATOM   2523 C  CA    . VAL C 1 25  ? 24.198  40.861 22.889 1.00 13.36  ? 42  VAL C CA    1 
ATOM   2524 C  C     . VAL C 1 25  ? 25.588  40.303 22.564 1.00 14.49  ? 42  VAL C C     1 
ATOM   2525 O  O     . VAL C 1 25  ? 25.722  39.317 21.832 1.00 14.39  ? 42  VAL C O     1 
ATOM   2526 C  CB    . VAL C 1 25  ? 23.247  40.759 21.679 1.00 12.81  ? 42  VAL C CB    1 
ATOM   2527 C  CG1   . VAL C 1 25  ? 21.822  41.123 22.079 1.00 14.70  ? 42  VAL C CG1   1 
ATOM   2528 C  CG2   . VAL C 1 25  ? 23.708  41.638 20.556 1.00 15.38  ? 42  VAL C CG2   1 
ATOM   2529 N  N     . VAL C 1 26  ? 26.635  40.895 23.144 1.00 14.20  ? 43  VAL C N     1 
ATOM   2530 C  CA    . VAL C 1 26  ? 27.993  40.411 22.900 1.00 12.06  ? 43  VAL C CA    1 
ATOM   2531 C  C     . VAL C 1 26  ? 28.117  38.929 23.261 1.00 15.01  ? 43  VAL C C     1 
ATOM   2532 O  O     . VAL C 1 26  ? 28.694  38.135 22.510 1.00 14.35  ? 43  VAL C O     1 
ATOM   2533 C  CB    . VAL C 1 26  ? 29.013  41.263 23.688 1.00 13.25  ? 43  VAL C CB    1 
ATOM   2534 C  CG1   . VAL C 1 26  ? 30.388  40.627 23.674 1.00 13.95  ? 43  VAL C CG1   1 
ATOM   2535 C  CG2   . VAL C 1 26  ? 29.071  42.671 23.132 1.00 15.04  ? 43  VAL C CG2   1 
ATOM   2536 N  N     . GLY C 1 27  ? 27.653  38.544 24.447 1.00 12.29  ? 44  GLY C N     1 
ATOM   2537 C  CA    . GLY C 1 27  ? 27.821  37.160 24.864 1.00 13.31  ? 44  GLY C CA    1 
ATOM   2538 C  C     . GLY C 1 27  ? 27.059  36.189 23.985 1.00 13.08  ? 44  GLY C C     1 
ATOM   2539 O  O     . GLY C 1 27  ? 27.548  35.098 23.680 1.00 12.92  ? 44  GLY C O     1 
ATOM   2540 N  N     . GLU C 1 28  ? 25.861  36.585 23.545 1.00 12.73  ? 45  GLU C N     1 
ATOM   2541 C  CA    . GLU C 1 28  ? 25.083  35.729 22.660 1.00 12.12  ? 45  GLU C CA    1 
ATOM   2542 C  C     . GLU C 1 28  ? 25.812  35.523 21.339 1.00 12.46  ? 45  GLU C C     1 
ATOM   2543 O  O     . GLU C 1 28  ? 25.818  34.414 20.795 1.00 13.22  ? 45  GLU C O     1 
ATOM   2544 C  CB    . GLU C 1 28  ? 23.702  36.330 22.399 1.00 15.01  ? 45  GLU C CB    1 
ATOM   2545 C  CG    . GLU C 1 28  ? 22.725  36.277 23.527 1.00 15.62  ? 45  GLU C CG    1 
ATOM   2546 C  CD    . GLU C 1 28  ? 21.363  36.651 22.968 1.00 26.31  ? 45  GLU C CD    1 
ATOM   2547 O  OE1   . GLU C 1 28  ? 20.783  35.827 22.218 1.00 29.83  ? 45  GLU C OE1   1 
ATOM   2548 O  OE2   . GLU C 1 28  ? 20.936  37.787 23.196 1.00 29.62  ? 45  GLU C OE2   1 
ATOM   2549 N  N     . ILE C 1 29  ? 26.432  36.584 20.810 1.00 12.41  ? 46  ILE C N     1 
ATOM   2550 C  CA    . ILE C 1 29  ? 27.189  36.458 19.570 1.00 12.66  ? 46  ILE C CA    1 
ATOM   2551 C  C     . ILE C 1 29  ? 28.357  35.512 19.757 1.00 12.55  ? 46  ILE C C     1 
ATOM   2552 O  O     . ILE C 1 29  ? 28.559  34.589 18.962 1.00 12.40  ? 46  ILE C O     1 
ATOM   2553 C  CB    . ILE C 1 29  ? 27.649  37.836 19.076 1.00 12.85  ? 46  ILE C CB    1 
ATOM   2554 C  CG1   . ILE C 1 29  ? 26.437  38.661 18.647 1.00 15.85  ? 46  ILE C CG1   1 
ATOM   2555 C  CG2   . ILE C 1 29  ? 28.681  37.692 17.940 1.00 16.08  ? 46  ILE C CG2   1 
ATOM   2556 C  CD1   . ILE C 1 29  ? 26.760  40.126 18.406 1.00 17.00  ? 46  ILE C CD1   1 
ATOM   2557 N  N     . ILE C 1 30  ? 29.147  35.706 20.820 1.00 13.30  ? 47  ILE C N     1 
ATOM   2558 C  CA    . ILE C 1 30  ? 30.302  34.846 21.040 1.00 14.92  ? 47  ILE C CA    1 
ATOM   2559 C  C     . ILE C 1 30  ? 29.866  33.393 21.188 1.00 12.93  ? 47  ILE C C     1 
ATOM   2560 O  O     . ILE C 1 30  ? 30.506  32.481 20.655 1.00 14.13  ? 47  ILE C O     1 
ATOM   2561 C  CB    . ILE C 1 30  ? 31.087  35.339 22.271 1.00 12.92  ? 47  ILE C CB    1 
ATOM   2562 C  CG1   . ILE C 1 30  ? 31.758  36.673 21.967 1.00 14.61  ? 47  ILE C CG1   1 
ATOM   2563 C  CG2   . ILE C 1 30  ? 32.111  34.311 22.728 1.00 15.17  ? 47  ILE C CG2   1 
ATOM   2564 C  CD1   . ILE C 1 30  ? 32.203  37.383 23.183 1.00 16.83  ? 47  ILE C CD1   1 
ATOM   2565 N  N     . SER C 1 31  ? 28.780  33.148 21.929 1.00 13.66  ? 48  SER C N     1 
ATOM   2566 C  CA    . SER C 1 31  ? 28.326  31.781 22.146 1.00 14.53  ? 48  SER C CA    1 
ATOM   2567 C  C     . SER C 1 31  ? 27.998  31.062 20.844 1.00 13.77  ? 48  SER C C     1 
ATOM   2568 O  O     . SER C 1 31  ? 28.182  29.840 20.765 1.00 15.17  ? 48  SER C O     1 
ATOM   2569 C  CB    . SER C 1 31  ? 27.088  31.763 23.055 1.00 13.91  ? 48  SER C CB    1 
ATOM   2570 O  OG    . SER C 1 31  ? 27.398  32.114 24.402 1.00 14.08  ? 48  SER C OG    1 
ATOM   2571 N  N     . ARG C 1 32  ? 27.479  31.782 19.827 1.00 13.31  ? 49  ARG C N     1 
ATOM   2572 C  CA    . ARG C 1 32  ? 27.174  31.127 18.559 1.00 13.23  ? 49  ARG C CA    1 
ATOM   2573 C  C     . ARG C 1 32  ? 28.424  30.543 17.911 1.00 14.07  ? 49  ARG C C     1 
ATOM   2574 O  O     . ARG C 1 32  ? 28.380  29.462 17.299 1.00 14.06  ? 49  ARG C O     1 
ATOM   2575 C  CB    . ARG C 1 32  ? 26.512  32.093 17.590 1.00 14.31  ? 49  ARG C CB    1 
ATOM   2576 C  CG    . ARG C 1 32  ? 25.114  32.450 18.020 1.00 12.91  ? 49  ARG C CG    1 
ATOM   2577 C  CD    . ARG C 1 32  ? 24.375  32.995 16.857 1.00 21.39  ? 49  ARG C CD    1 
ATOM   2578 N  NE    . ARG C 1 32  ? 23.017  33.329 17.232 1.00 20.44  ? 49  ARG C NE    1 
ATOM   2579 C  CZ    . ARG C 1 32  ? 22.000  33.335 16.392 1.00 19.50  ? 49  ARG C CZ    1 
ATOM   2580 N  NH1   . ARG C 1 32  ? 22.164  33.035 15.109 1.00 19.88  ? 49  ARG C NH1   1 
ATOM   2581 N  NH2   . ARG C 1 32  ? 20.796  33.650 16.850 1.00 18.34  ? 49  ARG C NH2   1 
ATOM   2582 N  N     . PHE C 1 33  ? 29.546  31.252 18.008 1.00 12.70  ? 50  PHE C N     1 
ATOM   2583 C  CA    . PHE C 1 33  ? 30.777  30.750 17.416 1.00 12.52  ? 50  PHE C CA    1 
ATOM   2584 C  C     . PHE C 1 33  ? 31.441  29.691 18.286 1.00 12.98  ? 50  PHE C C     1 
ATOM   2585 O  O     . PHE C 1 33  ? 31.934  28.682 17.762 1.00 14.93  ? 50  PHE C O     1 
ATOM   2586 C  CB    . PHE C 1 33  ? 31.723  31.918 17.119 1.00 12.86  ? 50  PHE C CB    1 
ATOM   2587 C  CG    . PHE C 1 33  ? 31.163  32.881 16.100 1.00 12.91  ? 50  PHE C CG    1 
ATOM   2588 C  CD1   . PHE C 1 33  ? 31.042  32.505 14.779 1.00 16.58  ? 50  PHE C CD1   1 
ATOM   2589 C  CD2   . PHE C 1 33  ? 30.684  34.124 16.468 1.00 17.45  ? 50  PHE C CD2   1 
ATOM   2590 C  CE1   . PHE C 1 33  ? 30.492  33.357 13.840 1.00 14.32  ? 50  PHE C CE1   1 
ATOM   2591 C  CE2   . PHE C 1 33  ? 30.138  34.992 15.514 1.00 17.47  ? 50  PHE C CE2   1 
ATOM   2592 C  CZ    . PHE C 1 33  ? 30.043  34.590 14.199 1.00 14.71  ? 50  PHE C CZ    1 
ATOM   2593 N  N     . GLU C 1 34  ? 31.435  29.878 19.611 1.00 14.16  ? 51  GLU C N     1 
ATOM   2594 C  CA    . GLU C 1 34  ? 31.944  28.843 20.502 1.00 15.11  ? 51  GLU C CA    1 
ATOM   2595 C  C     . GLU C 1 34  ? 31.201  27.539 20.313 1.00 13.32  ? 51  GLU C C     1 
ATOM   2596 O  O     . GLU C 1 34  ? 31.777  26.461 20.503 1.00 15.43  ? 51  GLU C O     1 
ATOM   2597 C  CB    . GLU C 1 34  ? 31.788  29.270 21.956 1.00 15.33  ? 51  GLU C CB    1 
ATOM   2598 C  CG    . GLU C 1 34  ? 32.776  30.285 22.422 1.00 14.74  ? 51  GLU C CG    1 
ATOM   2599 C  CD    . GLU C 1 34  ? 32.595  30.586 23.922 1.00 15.27  ? 51  GLU C CD    1 
ATOM   2600 O  OE1   . GLU C 1 34  ? 31.509  31.094 24.293 1.00 15.30  ? 51  GLU C OE1   1 
ATOM   2601 O  OE2   . GLU C 1 34  ? 33.528  30.262 24.714 1.00 16.25  ? 51  GLU C OE2   1 
ATOM   2602 N  N     . LYS C 1 35  ? 29.916  27.624 19.970 1.00 13.66  ? 52  LYS C N     1 
ATOM   2603 C  CA    . LYS C 1 35  ? 29.066  26.445 19.888 1.00 15.57  ? 52  LYS C CA    1 
ATOM   2604 C  C     . LYS C 1 35  ? 29.554  25.468 18.839 1.00 16.08  ? 52  LYS C C     1 
ATOM   2605 O  O     . LYS C 1 35  ? 29.285  24.275 18.948 1.00 15.21  ? 52  LYS C O     1 
ATOM   2606 C  CB    . LYS C 1 35  ? 27.637  26.871 19.588 1.00 15.14  ? 52  LYS C CB    1 
ATOM   2607 C  CG    . LYS C 1 35  ? 26.613  25.795 19.832 1.00 17.75  ? 52  LYS C CG    1 
ATOM   2608 C  CD    . LYS C 1 35  ? 25.213  26.329 19.544 1.00 21.75  ? 52  LYS C CD    1 
ATOM   2609 C  CE    . LYS C 1 35  ? 24.168  25.571 20.323 1.00 33.33  ? 52  LYS C CE    1 
ATOM   2610 N  NZ    . LYS C 1 35  ? 24.323  25.857 21.777 1.00 32.08  ? 52  LYS C NZ    1 
ATOM   2611 N  N     . ARG C 1 36  ? 30.208  25.956 17.792 1.00 12.77  ? 53  ARG C N     1 
ATOM   2612 C  CA    . ARG C 1 36  ? 30.759  25.083 16.760 1.00 13.49  ? 53  ARG C CA    1 
ATOM   2613 C  C     . ARG C 1 36  ? 32.168  24.602 17.067 1.00 15.58  ? 53  ARG C C     1 
ATOM   2614 O  O     . ARG C 1 36  ? 32.787  23.939 16.229 1.00 14.05  ? 53  ARG C O     1 
ATOM   2615 C  CB    . ARG C 1 36  ? 30.730  25.787 15.399 1.00 14.63  ? 53  ARG C CB    1 
ATOM   2616 C  CG    . ARG C 1 36  ? 29.309  26.051 14.900 1.00 15.38  ? 53  ARG C CG    1 
ATOM   2617 C  CD    . ARG C 1 36  ? 29.302  26.609 13.503 1.00 16.87  ? 53  ARG C CD    1 
ATOM   2618 N  NE    . ARG C 1 36  ? 29.614  25.580 12.522 1.00 13.50  ? 53  ARG C NE    1 
ATOM   2619 C  CZ    . ARG C 1 36  ? 29.546  25.784 11.212 1.00 14.98  ? 53  ARG C CZ    1 
ATOM   2620 N  NH1   . ARG C 1 36  ? 29.224  26.966 10.730 1.00 16.44  ? 53  ARG C NH1   1 
ATOM   2621 N  NH2   . ARG C 1 36  ? 29.780  24.774 10.378 1.00 19.46  ? 53  ARG C NH2   1 
ATOM   2622 N  N     . GLY C 1 37  ? 32.713  24.921 18.234 1.00 13.06  ? 54  GLY C N     1 
ATOM   2623 C  CA    . GLY C 1 37  ? 34.085  24.588 18.505 1.00 14.55  ? 54  GLY C CA    1 
ATOM   2624 C  C     . GLY C 1 37  ? 35.093  25.513 17.877 1.00 14.00  ? 54  GLY C C     1 
ATOM   2625 O  O     . GLY C 1 37  ? 36.263  25.137 17.737 1.00 18.59  ? 54  GLY C O     1 
ATOM   2626 N  N     . TYR C 1 38  ? 34.681  26.722 17.499 1.00 14.20  ? 55  TYR C N     1 
ATOM   2627 C  CA    . TYR C 1 38  ? 35.643  27.688 17.006 1.00 15.58  ? 55  TYR C CA    1 
ATOM   2628 C  C     . TYR C 1 38  ? 36.414  28.249 18.187 1.00 16.01  ? 55  TYR C C     1 
ATOM   2629 O  O     . TYR C 1 38  ? 35.856  28.467 19.267 1.00 15.64  ? 55  TYR C O     1 
ATOM   2630 C  CB    . TYR C 1 38  ? 34.962  28.807 16.224 1.00 16.27  ? 55  TYR C CB    1 
ATOM   2631 C  CG    . TYR C 1 38  ? 34.300  28.388 14.912 1.00 15.43  ? 55  TYR C CG    1 
ATOM   2632 C  CD1   . TYR C 1 38  ? 34.812  27.365 14.122 1.00 14.37  ? 55  TYR C CD1   1 
ATOM   2633 C  CD2   . TYR C 1 38  ? 33.142  29.001 14.501 1.00 16.52  ? 55  TYR C CD2   1 
ATOM   2634 C  CE1   . TYR C 1 38  ? 34.209  27.002 12.933 1.00 15.43  ? 55  TYR C CE1   1 
ATOM   2635 C  CE2   . TYR C 1 38  ? 32.525  28.654 13.283 1.00 15.56  ? 55  TYR C CE2   1 
ATOM   2636 C  CZ    . TYR C 1 38  ? 33.047  27.655 12.522 1.00 15.14  ? 55  TYR C CZ    1 
ATOM   2637 O  OH    . TYR C 1 38  ? 32.418  27.310 11.362 1.00 16.48  ? 55  TYR C OH    1 
ATOM   2638 N  N     . ARG C 1 39  ? 37.702  28.462 17.972 1.00 16.59  ? 56  ARG C N     1 
ATOM   2639 C  CA    . ARG C 1 39  ? 38.620  28.856 19.025 1.00 15.50  ? 56  ARG C CA    1 
ATOM   2640 C  C     . ARG C 1 39  ? 38.806  30.362 19.009 1.00 16.69  ? 56  ARG C C     1 
ATOM   2641 O  O     . ARG C 1 39  ? 39.110  30.946 17.962 1.00 17.48  ? 56  ARG C O     1 
ATOM   2642 C  CB    . ARG C 1 39  ? 39.965  28.151 18.854 1.00 17.09  ? 56  ARG C CB    1 
ATOM   2643 C  CG    . ARG C 1 39  ? 40.929  28.441 19.992 1.00 15.35  ? 56  ARG C CG    1 
ATOM   2644 C  CD    . ARG C 1 39  ? 42.218  27.653 19.794 1.00 17.35  ? 56  ARG C CD    1 
ATOM   2645 N  NE    . ARG C 1 39  ? 43.015  28.150 18.685 1.00 17.64  ? 56  ARG C NE    1 
ATOM   2646 C  CZ    . ARG C 1 39  ? 43.853  29.174 18.757 1.00 18.50  ? 56  ARG C CZ    1 
ATOM   2647 N  NH1   . ARG C 1 39  ? 43.974  29.888 19.861 1.00 18.64  ? 56  ARG C NH1   1 
ATOM   2648 N  NH2   . ARG C 1 39  ? 44.584  29.495 17.688 1.00 24.71  ? 56  ARG C NH2   1 
ATOM   2649 N  N     . ILE C 1 40  ? 38.638  30.987 20.176 1.00 15.42  ? 57  ILE C N     1 
ATOM   2650 C  CA    . ILE C 1 40  ? 38.931  32.410 20.309 1.00 17.57  ? 57  ILE C CA    1 
ATOM   2651 C  C     . ILE C 1 40  ? 40.446  32.572 20.289 1.00 15.50  ? 57  ILE C C     1 
ATOM   2652 O  O     . ILE C 1 40  ? 41.139  32.157 21.225 1.00 17.72  ? 57  ILE C O     1 
ATOM   2653 C  CB    . ILE C 1 40  ? 38.353  33.012 21.589 1.00 16.06  ? 57  ILE C CB    1 
ATOM   2654 C  CG1   . ILE C 1 40  ? 36.841  32.762 21.700 1.00 15.34  ? 57  ILE C CG1   1 
ATOM   2655 C  CG2   . ILE C 1 40  ? 38.671  34.498 21.569 1.00 17.69  ? 57  ILE C CG2   1 
ATOM   2656 C  CD1   . ILE C 1 40  ? 36.280  33.058 23.084 1.00 17.27  ? 57  ILE C CD1   1 
ATOM   2657 N  N     . ALA C 1 41  ? 40.960  33.169 19.219 1.00 16.80  ? 58  ALA C N     1 
ATOM   2658 C  CA    . ALA C 1 41  ? 42.396  33.404 19.108 1.00 18.19  ? 58  ALA C CA    1 
ATOM   2659 C  C     . ALA C 1 41  ? 42.795  34.820 19.489 1.00 17.61  ? 58  ALA C C     1 
ATOM   2660 O  O     . ALA C 1 41  ? 43.966  35.068 19.793 1.00 20.64  ? 58  ALA C O     1 
ATOM   2661 C  CB    . ALA C 1 41  ? 42.886  33.111 17.689 1.00 19.10  ? 58  ALA C CB    1 
ATOM   2662 N  N     . ALA C 1 42  ? 41.863  35.756 19.478 1.00 17.13  ? 59  ALA C N     1 
ATOM   2663 C  CA    . ALA C 1 42  ? 42.154  37.122 19.868 1.00 16.07  ? 59  ALA C CA    1 
ATOM   2664 C  C     . ALA C 1 42  ? 40.839  37.808 20.184 1.00 17.08  ? 59  ALA C C     1 
ATOM   2665 O  O     . ALA C 1 42  ? 39.800  37.465 19.622 1.00 18.16  ? 59  ALA C O     1 
ATOM   2666 C  CB    . ALA C 1 42  ? 42.917  37.880 18.771 1.00 19.19  ? 59  ALA C CB    1 
ATOM   2667 N  N     . MET C 1 43  ? 40.898  38.782 21.081 1.00 16.93  ? 60  MET C N     1 
ATOM   2668 C  CA    . MET C 1 43  ? 39.703  39.523 21.449 1.00 18.18  ? 60  MET C CA    1 
ATOM   2669 C  C     . MET C 1 43  ? 40.129  40.824 22.113 1.00 23.14  ? 60  MET C C     1 
ATOM   2670 O  O     . MET C 1 43  ? 41.043  40.834 22.945 1.00 23.77  ? 60  MET C O     1 
ATOM   2671 C  CB    . MET C 1 43  ? 38.817  38.681 22.382 1.00 17.33  ? 60  MET C CB    1 
ATOM   2672 C  CG    . MET C 1 43  ? 37.481  39.284 22.699 1.00 20.63  ? 60  MET C CG    1 
ATOM   2673 S  SD    . MET C 1 43  ? 36.297  38.094 23.417 1.00 20.61  ? 60  MET C SD    1 
ATOM   2674 C  CE    . MET C 1 43  ? 35.682  37.204 21.991 1.00 20.54  ? 60  MET C CE    1 
ATOM   2675 N  N     . LYS C 1 44  ? 39.489  41.920 21.721 1.00 19.51  ? 61  LYS C N     1 
ATOM   2676 C  CA    . LYS C 1 44  ? 39.832  43.233 22.256 1.00 21.95  ? 61  LYS C CA    1 
ATOM   2677 C  C     . LYS C 1 44  ? 38.662  44.196 22.077 1.00 23.72  ? 61  LYS C C     1 
ATOM   2678 O  O     . LYS C 1 44  ? 38.154  44.355 20.959 1.00 21.43  ? 61  LYS C O     1 
ATOM   2679 C  CB    . LYS C 1 44  ? 41.090  43.764 21.542 1.00 23.22  ? 61  LYS C CB    1 
ATOM   2680 C  CG    . LYS C 1 44  ? 41.263  45.260 21.533 1.00 34.88  ? 61  LYS C CG    1 
ATOM   2681 C  CD    . LYS C 1 44  ? 42.659  45.644 21.042 1.00 32.36  ? 61  LYS C CD    1 
ATOM   2682 C  CE    . LYS C 1 44  ? 42.860  45.323 19.603 1.00 29.75  ? 61  LYS C CE    1 
ATOM   2683 N  NZ    . LYS C 1 44  ? 44.237  45.766 19.147 1.00 30.08  ? 61  LYS C NZ    1 
ATOM   2684 N  N     . LEU C 1 45  ? 38.251  44.852 23.164 1.00 20.51  ? 62  LEU C N     1 
ATOM   2685 C  CA    . LEU C 1 45  ? 37.299  45.952 23.085 1.00 18.64  ? 62  LEU C CA    1 
ATOM   2686 C  C     . LEU C 1 45  ? 38.055  47.249 22.828 1.00 19.28  ? 62  LEU C C     1 
ATOM   2687 O  O     . LEU C 1 45  ? 39.071  47.535 23.480 1.00 21.37  ? 62  LEU C O     1 
ATOM   2688 C  CB    . LEU C 1 45  ? 36.466  46.091 24.367 1.00 17.98  ? 62  LEU C CB    1 
ATOM   2689 C  CG    . LEU C 1 45  ? 35.327  47.114 24.260 1.00 21.47  ? 62  LEU C CG    1 
ATOM   2690 C  CD1   . LEU C 1 45  ? 34.122  46.500 23.568 1.00 24.17  ? 62  LEU C CD1   1 
ATOM   2691 C  CD2   . LEU C 1 45  ? 34.933  47.663 25.628 1.00 25.61  ? 62  LEU C CD2   1 
ATOM   2692 N  N     . THR C 1 46  ? 37.589  48.008 21.854 1.00 20.03  ? 63  THR C N     1 
ATOM   2693 C  CA    . THR C 1 46  ? 38.183  49.300 21.569 1.00 21.79  ? 63  THR C CA    1 
ATOM   2694 C  C     . THR C 1 46  ? 37.085  50.241 21.098 1.00 23.40  ? 63  THR C C     1 
ATOM   2695 O  O     . THR C 1 46  ? 35.927  49.849 20.946 1.00 23.15  ? 63  THR C O     1 
ATOM   2696 C  CB    . THR C 1 46  ? 39.316  49.157 20.549 1.00 27.40  ? 63  THR C CB    1 
ATOM   2697 O  OG1   . THR C 1 46  ? 40.083  50.366 20.523 1.00 27.01  ? 63  THR C OG1   1 
ATOM   2698 C  CG2   . THR C 1 46  ? 38.770  48.872 19.160 1.00 25.68  ? 63  THR C CG2   1 
ATOM   2699 N  N     . ILE C 1 47  ? 37.439  51.507 20.908 1.00 23.14  ? 64  ILE C N     1 
ATOM   2700 C  CA    . ILE C 1 47  ? 36.531  52.464 20.304 1.00 22.70  ? 64  ILE C CA    1 
ATOM   2701 C  C     . ILE C 1 47  ? 37.089  52.769 18.922 1.00 26.06  ? 64  ILE C C     1 
ATOM   2702 O  O     . ILE C 1 47  ? 38.189  53.312 18.784 1.00 27.70  ? 64  ILE C O     1 
ATOM   2703 C  CB    . ILE C 1 47  ? 36.349  53.731 21.145 1.00 26.41  ? 64  ILE C CB    1 
ATOM   2704 C  CG1   . ILE C 1 47  ? 35.636  53.385 22.459 1.00 29.96  ? 64  ILE C CG1   1 
ATOM   2705 C  CG2   . ILE C 1 47  ? 35.532  54.754 20.344 1.00 26.67  ? 64  ILE C CG2   1 
ATOM   2706 C  CD1   . ILE C 1 47  ? 35.448  54.546 23.373 1.00 39.15  ? 64  ILE C CD1   1 
ATOM   2707 N  N     . ALA C 1 48  ? 36.350  52.372 17.895 1.00 22.63  ? 65  ALA C N     1 
ATOM   2708 C  CA    . ALA C 1 48  ? 36.831  52.531 16.529 1.00 22.34  ? 65  ALA C CA    1 
ATOM   2709 C  C     . ALA C 1 48  ? 36.927  54.010 16.180 1.00 28.97  ? 65  ALA C C     1 
ATOM   2710 O  O     . ALA C 1 48  ? 36.081  54.811 16.577 1.00 29.48  ? 65  ALA C O     1 
ATOM   2711 C  CB    . ALA C 1 48  ? 35.891  51.815 15.564 1.00 25.75  ? 65  ALA C CB    1 
ATOM   2712 N  N     . THR C 1 49  ? 37.975  54.376 15.447 1.00 27.83  ? 66  THR C N     1 
ATOM   2713 C  CA    . THR C 1 49  ? 38.170  55.744 14.994 1.00 35.05  ? 66  THR C CA    1 
ATOM   2714 C  C     . THR C 1 49  ? 37.957  55.852 13.492 1.00 33.38  ? 66  THR C C     1 
ATOM   2715 O  O     . THR C 1 49  ? 38.083  54.860 12.765 1.00 28.68  ? 66  THR C O     1 
ATOM   2716 C  CB    . THR C 1 49  ? 39.586  56.212 15.341 1.00 33.67  ? 66  THR C CB    1 
ATOM   2717 O  OG1   . THR C 1 49  ? 40.539  55.329 14.729 1.00 35.50  ? 66  THR C OG1   1 
ATOM   2718 C  CG2   . THR C 1 49  ? 39.774  56.200 16.835 1.00 36.07  ? 66  THR C CG2   1 
ATOM   2719 N  N     . PRO C 1 50  ? 37.626  57.047 12.983 1.00 34.30  ? 67  PRO C N     1 
ATOM   2720 C  CA    . PRO C 1 50  ? 37.506  57.189 11.526 1.00 33.52  ? 67  PRO C CA    1 
ATOM   2721 C  C     . PRO C 1 50  ? 38.762  56.777 10.785 1.00 32.87  ? 67  PRO C C     1 
ATOM   2722 O  O     . PRO C 1 50  ? 38.659  56.158 9.726  1.00 35.18  ? 67  PRO C O     1 
ATOM   2723 C  CB    . PRO C 1 50  ? 37.192  58.682 11.346 1.00 36.66  ? 67  PRO C CB    1 
ATOM   2724 C  CG    . PRO C 1 50  ? 36.510  59.063 12.600 1.00 38.25  ? 67  PRO C CG    1 
ATOM   2725 C  CD    . PRO C 1 50  ? 37.191  58.265 13.684 1.00 34.55  ? 67  PRO C CD    1 
ATOM   2726 N  N     . ALA C 1 51  ? 39.950  57.057 11.326 1.00 35.03  ? 68  ALA C N     1 
ATOM   2727 C  CA    . ALA C 1 51  ? 41.170  56.725 10.590 1.00 39.18  ? 68  ALA C CA    1 
ATOM   2728 C  C     . ALA C 1 51  ? 41.285  55.222 10.361 1.00 42.34  ? 68  ALA C C     1 
ATOM   2729 O  O     . ALA C 1 51  ? 41.585  54.775 9.248  1.00 38.97  ? 68  ALA C O     1 
ATOM   2730 C  CB    . ALA C 1 51  ? 42.402  57.237 11.331 1.00 40.58  ? 68  ALA C CB    1 
ATOM   2731 N  N     . ILE C 1 52  ? 41.058  54.420 11.407 1.00 37.50  ? 69  ILE C N     1 
ATOM   2732 C  CA    . ILE C 1 52  ? 41.180  52.979 11.216 1.00 31.44  ? 69  ILE C CA    1 
ATOM   2733 C  C     . ILE C 1 52  ? 40.000  52.453 10.403 1.00 28.37  ? 69  ILE C C     1 
ATOM   2734 O  O     . ILE C 1 52  ? 40.152  51.517 9.610  1.00 26.31  ? 69  ILE C O     1 
ATOM   2735 C  CB    . ILE C 1 52  ? 41.324  52.244 12.558 1.00 28.33  ? 69  ILE C CB    1 
ATOM   2736 C  CG1   . ILE C 1 52  ? 41.742  50.797 12.283 1.00 31.06  ? 69  ILE C CG1   1 
ATOM   2737 C  CG2   . ILE C 1 52  ? 40.012  52.274 13.367 1.00 29.64  ? 69  ILE C CG2   1 
ATOM   2738 C  CD1   . ILE C 1 52  ? 42.130  50.033 13.507 1.00 38.53  ? 69  ILE C CD1   1 
ATOM   2739 N  N     . LEU C 1 53  ? 38.819  53.058 10.561 1.00 26.56  ? 70  LEU C N     1 
ATOM   2740 C  CA    . LEU C 1 53  ? 37.660  52.629 9.785  1.00 26.53  ? 70  LEU C CA    1 
ATOM   2741 C  C     . LEU C 1 53  ? 37.841  52.915 8.304  1.00 26.10  ? 70  LEU C C     1 
ATOM   2742 O  O     . LEU C 1 53  ? 37.387  52.131 7.460  1.00 27.46  ? 70  LEU C O     1 
ATOM   2743 C  CB    . LEU C 1 53  ? 36.402  53.310 10.311 1.00 25.51  ? 70  LEU C CB    1 
ATOM   2744 C  CG    . LEU C 1 53  ? 35.951  52.835 11.692 1.00 24.32  ? 70  LEU C CG    1 
ATOM   2745 C  CD1   . LEU C 1 53  ? 34.848  53.737 12.228 1.00 22.29  ? 70  LEU C CD1   1 
ATOM   2746 C  CD2   . LEU C 1 53  ? 35.489  51.359 11.656 1.00 25.39  ? 70  LEU C CD2   1 
ATOM   2747 N  N     . GLU C 1 54  ? 38.490  54.029 7.966  1.00 27.27  ? 71  GLU C N     1 
ATOM   2748 C  CA    . GLU C 1 54  ? 38.802  54.298 6.564  1.00 31.19  ? 71  GLU C CA    1 
ATOM   2749 C  C     . GLU C 1 54  ? 39.647  53.184 5.964  1.00 26.73  ? 71  GLU C C     1 
ATOM   2750 O  O     . GLU C 1 54  ? 39.437  52.795 4.810  1.00 32.02  ? 71  GLU C O     1 
ATOM   2751 C  CB    . GLU C 1 54  ? 39.532  55.633 6.441  1.00 36.83  ? 71  GLU C CB    1 
ATOM   2752 C  CG    . GLU C 1 54  ? 38.641  56.842 6.651  1.00 56.94  ? 71  GLU C CG    1 
ATOM   2753 C  CD    . GLU C 1 54  ? 39.423  58.116 6.936  1.00 68.17  ? 71  GLU C CD    1 
ATOM   2754 O  OE1   . GLU C 1 54  ? 40.653  58.139 6.697  1.00 59.77  ? 71  GLU C OE1   1 
ATOM   2755 O  OE2   . GLU C 1 54  ? 38.801  59.094 7.409  1.00 72.26  ? 71  GLU C OE2   1 
ATOM   2756 N  N     . GLU C 1 55  ? 40.649  52.711 6.707  1.00 28.04  ? 72  GLU C N     1 
ATOM   2757 C  CA    A GLU C 1 55  ? 41.472  51.616 6.206  0.59 27.70  ? 72  GLU C CA    1 
ATOM   2758 C  CA    B GLU C 1 55  ? 41.484  51.607 6.237  0.41 27.74  ? 72  GLU C CA    1 
ATOM   2759 C  C     . GLU C 1 55  ? 40.702  50.301 6.204  1.00 27.98  ? 72  GLU C C     1 
ATOM   2760 O  O     . GLU C 1 55  ? 40.849  49.496 5.279  1.00 27.68  ? 72  GLU C O     1 
ATOM   2761 C  CB    A GLU C 1 55  ? 42.743  51.481 7.034  0.59 33.50  ? 72  GLU C CB    1 
ATOM   2762 C  CB    B GLU C 1 55  ? 42.705  51.445 7.140  0.41 33.47  ? 72  GLU C CB    1 
ATOM   2763 C  CG    A GLU C 1 55  ? 43.775  50.554 6.405  0.59 34.31  ? 72  GLU C CG    1 
ATOM   2764 C  CG    B GLU C 1 55  ? 43.492  52.716 7.411  0.41 36.26  ? 72  GLU C CG    1 
ATOM   2765 C  CD    A GLU C 1 55  ? 45.165  50.776 6.954  0.59 38.53  ? 72  GLU C CD    1 
ATOM   2766 C  CD    B GLU C 1 55  ? 44.603  52.483 8.414  0.41 43.36  ? 72  GLU C CD    1 
ATOM   2767 O  OE1   A GLU C 1 55  ? 45.356  51.778 7.670  0.59 45.16  ? 72  GLU C OE1   1 
ATOM   2768 O  OE1   B GLU C 1 55  ? 45.508  51.677 8.112  0.41 46.59  ? 72  GLU C OE1   1 
ATOM   2769 O  OE2   A GLU C 1 55  ? 46.067  49.960 6.662  0.59 32.17  ? 72  GLU C OE2   1 
ATOM   2770 O  OE2   B GLU C 1 55  ? 44.561  53.079 9.514  0.41 45.16  ? 72  GLU C OE2   1 
ATOM   2771 N  N     . HIS C 1 56  ? 39.876  50.071 7.216  1.00 25.83  ? 73  HIS C N     1 
ATOM   2772 C  CA    . HIS C 1 56  ? 39.098  48.840 7.270  1.00 25.67  ? 73  HIS C CA    1 
ATOM   2773 C  C     . HIS C 1 56  ? 38.189  48.732 6.067  1.00 26.57  ? 73  HIS C C     1 
ATOM   2774 O  O     . HIS C 1 56  ? 38.082  47.671 5.446  1.00 24.96  ? 73  HIS C O     1 
ATOM   2775 C  CB    . HIS C 1 56  ? 38.263  48.817 8.540  1.00 21.25  ? 73  HIS C CB    1 
ATOM   2776 C  CG    . HIS C 1 56  ? 37.428  47.587 8.686  1.00 24.23  ? 73  HIS C CG    1 
ATOM   2777 N  ND1   . HIS C 1 56  ? 37.953  46.375 9.077  1.00 22.43  ? 73  HIS C ND1   1 
ATOM   2778 C  CD2   . HIS C 1 56  ? 36.103  47.384 8.500  1.00 25.46  ? 73  HIS C CD2   1 
ATOM   2779 C  CE1   . HIS C 1 56  ? 36.986  45.474 9.122  1.00 23.74  ? 73  HIS C CE1   1 
ATOM   2780 N  NE2   . HIS C 1 56  ? 35.852  46.062 8.780  1.00 24.88  ? 73  HIS C NE2   1 
ATOM   2781 N  N     . TYR C 1 57  ? 37.520  49.829 5.735  1.00 30.82  ? 74  TYR C N     1 
ATOM   2782 C  CA    . TYR C 1 57  ? 36.562  49.876 4.641  1.00 29.41  ? 74  TYR C CA    1 
ATOM   2783 C  C     . TYR C 1 57  ? 37.161  50.517 3.390  1.00 37.83  ? 74  TYR C C     1 
ATOM   2784 O  O     . TYR C 1 57  ? 36.447  51.138 2.600  1.00 37.17  ? 74  TYR C O     1 
ATOM   2785 C  CB    . TYR C 1 57  ? 35.300  50.606 5.104  1.00 32.44  ? 74  TYR C CB    1 
ATOM   2786 C  CG    . TYR C 1 57  ? 34.400  49.807 6.045  1.00 31.54  ? 74  TYR C CG    1 
ATOM   2787 C  CD1   . TYR C 1 57  ? 33.955  48.530 5.709  1.00 35.61  ? 74  TYR C CD1   1 
ATOM   2788 C  CD2   . TYR C 1 57  ? 33.978  50.341 7.261  1.00 37.59  ? 74  TYR C CD2   1 
ATOM   2789 C  CE1   . TYR C 1 57  ? 33.118  47.808 6.551  1.00 34.20  ? 74  TYR C CE1   1 
ATOM   2790 C  CE2   . TYR C 1 57  ? 33.149  49.624 8.107  1.00 35.31  ? 74  TYR C CE2   1 
ATOM   2791 C  CZ    . TYR C 1 57  ? 32.720  48.360 7.749  1.00 37.05  ? 74  TYR C CZ    1 
ATOM   2792 O  OH    . TYR C 1 57  ? 31.897  47.634 8.594  1.00 45.48  ? 74  TYR C OH    1 
ATOM   2793 N  N     . ALA C 1 58  ? 38.469  50.338 3.183  1.00 32.74  ? 75  ALA C N     1 
ATOM   2794 C  CA    . ALA C 1 58  ? 39.138  50.916 2.019  1.00 35.99  ? 75  ALA C CA    1 
ATOM   2795 C  C     . ALA C 1 58  ? 38.471  50.516 0.710  1.00 36.29  ? 75  ALA C C     1 
ATOM   2796 O  O     . ALA C 1 58  ? 38.477  51.296 -0.249 1.00 38.19  ? 75  ALA C O     1 
ATOM   2797 C  CB    . ALA C 1 58  ? 40.608  50.492 2.005  1.00 36.54  ? 75  ALA C CB    1 
ATOM   2798 N  N     . GLU C 1 59  ? 37.894  49.311 0.636  1.00 38.76  ? 76  GLU C N     1 
ATOM   2799 C  CA    . GLU C 1 59  ? 37.272  48.868 -0.611 1.00 38.39  ? 76  GLU C CA    1 
ATOM   2800 C  C     . GLU C 1 59  ? 36.083  49.739 -1.005 1.00 45.10  ? 76  GLU C C     1 
ATOM   2801 O  O     . GLU C 1 59  ? 35.625  49.658 -2.152 1.00 42.38  ? 76  GLU C O     1 
ATOM   2802 C  CB    . GLU C 1 59  ? 36.828  47.404 -0.504 1.00 39.11  ? 76  GLU C CB    1 
ATOM   2803 C  CG    . GLU C 1 59  ? 35.636  47.172 0.430  1.00 49.23  ? 76  GLU C CG    1 
ATOM   2804 C  CD    . GLU C 1 59  ? 35.408  45.703 0.775  1.00 58.01  ? 76  GLU C CD    1 
ATOM   2805 O  OE1   . GLU C 1 59  ? 36.131  45.164 1.646  1.00 55.40  ? 76  GLU C OE1   1 
ATOM   2806 O  OE2   . GLU C 1 59  ? 34.496  45.087 0.177  1.00 56.81  ? 76  GLU C OE2   1 
ATOM   2807 N  N     . HIS C 1 60  ? 35.568  50.554 -0.088 1.00 37.19  ? 77  HIS C N     1 
ATOM   2808 C  CA    . HIS C 1 60  ? 34.468  51.469 -0.360 1.00 43.86  ? 77  HIS C CA    1 
ATOM   2809 C  C     . HIS C 1 60  ? 34.929  52.918 -0.524 1.00 43.12  ? 77  HIS C C     1 
ATOM   2810 O  O     . HIS C 1 60  ? 34.091  53.822 -0.553 1.00 46.37  ? 77  HIS C O     1 
ATOM   2811 C  CB    . HIS C 1 60  ? 33.427  51.376 0.764  1.00 41.72  ? 77  HIS C CB    1 
ATOM   2812 C  CG    . HIS C 1 60  ? 32.919  49.988 1.010  1.00 38.20  ? 77  HIS C CG    1 
ATOM   2813 N  ND1   . HIS C 1 60  ? 32.387  49.201 0.012  1.00 45.08  ? 77  HIS C ND1   1 
ATOM   2814 C  CD2   . HIS C 1 60  ? 32.850  49.250 2.146  1.00 46.42  ? 77  HIS C CD2   1 
ATOM   2815 C  CE1   . HIS C 1 60  ? 32.018  48.038 0.520  1.00 44.95  ? 77  HIS C CE1   1 
ATOM   2816 N  NE2   . HIS C 1 60  ? 32.292  48.040 1.811  1.00 43.80  ? 77  HIS C NE2   1 
ATOM   2817 N  N     . LYS C 1 61  ? 36.235  53.160 -0.622 1.00 53.59  ? 78  LYS C N     1 
ATOM   2818 C  CA    . LYS C 1 61  ? 36.748  54.523 -0.713 1.00 61.88  ? 78  LYS C CA    1 
ATOM   2819 C  C     . LYS C 1 61  ? 36.125  55.265 -1.889 1.00 65.42  ? 78  LYS C C     1 
ATOM   2820 O  O     . LYS C 1 61  ? 35.865  54.685 -2.948 1.00 55.16  ? 78  LYS C O     1 
ATOM   2821 C  CB    . LYS C 1 61  ? 38.272  54.510 -0.862 1.00 68.30  ? 78  LYS C CB    1 
ATOM   2822 C  CG    . LYS C 1 61  ? 38.896  55.881 -1.123 1.00 84.22  ? 78  LYS C CG    1 
ATOM   2823 C  CD    . LYS C 1 61  ? 40.419  55.798 -1.142 1.00 104.11 ? 78  LYS C CD    1 
ATOM   2824 C  CE    . LYS C 1 61  ? 41.065  57.122 -1.534 1.00 103.85 ? 78  LYS C CE    1 
ATOM   2825 N  NZ    . LYS C 1 61  ? 42.482  56.935 -1.970 1.00 116.90 ? 78  LYS C NZ    1 
ATOM   2826 N  N     . GLY C 1 62  ? 35.880  56.562 -1.688 1.00 65.78  ? 79  GLY C N     1 
ATOM   2827 C  CA    . GLY C 1 62  ? 35.267  57.404 -2.691 1.00 61.13  ? 79  GLY C CA    1 
ATOM   2828 C  C     . GLY C 1 62  ? 33.768  57.249 -2.841 1.00 68.69  ? 79  GLY C C     1 
ATOM   2829 O  O     . GLY C 1 62  ? 33.128  58.129 -3.427 1.00 59.68  ? 79  GLY C O     1 
ATOM   2830 N  N     . LYS C 1 63  ? 33.180  56.168 -2.329 1.00 68.24  ? 80  LYS C N     1 
ATOM   2831 C  CA    . LYS C 1 63  ? 31.753  55.944 -2.502 1.00 64.17  ? 80  LYS C CA    1 
ATOM   2832 C  C     . LYS C 1 63  ? 30.941  56.881 -1.610 1.00 64.65  ? 80  LYS C C     1 
ATOM   2833 O  O     . LYS C 1 63  ? 31.446  57.399 -0.610 1.00 58.30  ? 80  LYS C O     1 
ATOM   2834 C  CB    . LYS C 1 63  ? 31.395  54.495 -2.191 1.00 52.49  ? 80  LYS C CB    1 
ATOM   2835 C  CG    . LYS C 1 63  ? 32.161  53.491 -3.031 1.00 68.37  ? 80  LYS C CG    1 
ATOM   2836 C  CD    . LYS C 1 63  ? 31.708  52.073 -2.739 1.00 67.09  ? 80  LYS C CD    1 
ATOM   2837 C  CE    . LYS C 1 63  ? 32.487  51.058 -3.564 1.00 66.44  ? 80  LYS C CE    1 
ATOM   2838 N  NZ    . LYS C 1 63  ? 32.064  49.664 -3.239 1.00 55.81  ? 80  LYS C NZ    1 
ATOM   2839 N  N     . PRO C 1 64  ? 29.666  57.108 -1.951 1.00 67.60  ? 81  PRO C N     1 
ATOM   2840 C  CA    . PRO C 1 64  ? 28.882  58.114 -1.219 1.00 68.35  ? 81  PRO C CA    1 
ATOM   2841 C  C     . PRO C 1 64  ? 28.326  57.631 0.108  1.00 55.61  ? 81  PRO C C     1 
ATOM   2842 O  O     . PRO C 1 64  ? 28.001  58.475 0.952  1.00 51.74  ? 81  PRO C O     1 
ATOM   2843 C  CB    . PRO C 1 64  ? 27.738  58.456 -2.195 1.00 63.02  ? 81  PRO C CB    1 
ATOM   2844 C  CG    . PRO C 1 64  ? 28.070  57.742 -3.486 1.00 67.23  ? 81  PRO C CG    1 
ATOM   2845 C  CD    . PRO C 1 64  ? 28.908  56.573 -3.092 1.00 77.69  ? 81  PRO C CD    1 
ATOM   2846 N  N     . PHE C 1 65  ? 28.187  56.320 0.319  1.00 46.82  ? 82  PHE C N     1 
ATOM   2847 C  CA    . PHE C 1 65  ? 27.711  55.812 1.603  1.00 63.21  ? 82  PHE C CA    1 
ATOM   2848 C  C     . PHE C 1 65  ? 28.821  55.659 2.636  1.00 52.95  ? 82  PHE C C     1 
ATOM   2849 O  O     . PHE C 1 65  ? 28.519  55.392 3.806  1.00 43.14  ? 82  PHE C O     1 
ATOM   2850 C  CB    . PHE C 1 65  ? 27.012  54.460 1.424  1.00 58.44  ? 82  PHE C CB    1 
ATOM   2851 C  CG    . PHE C 1 65  ? 27.922  53.361 0.937  1.00 75.89  ? 82  PHE C CG    1 
ATOM   2852 C  CD1   . PHE C 1 65  ? 28.174  53.201 -0.416 1.00 74.10  ? 82  PHE C CD1   1 
ATOM   2853 C  CD2   . PHE C 1 65  ? 28.519  52.483 1.831  1.00 72.33  ? 82  PHE C CD2   1 
ATOM   2854 C  CE1   . PHE C 1 65  ? 29.004  52.196 -0.865 1.00 68.15  ? 82  PHE C CE1   1 
ATOM   2855 C  CE2   . PHE C 1 65  ? 29.350  51.472 1.383  1.00 61.76  ? 82  PHE C CE2   1 
ATOM   2856 C  CZ    . PHE C 1 65  ? 29.592  51.330 0.035  1.00 61.73  ? 82  PHE C CZ    1 
ATOM   2857 N  N     . LEU C 1 66  ? 30.086  55.828 2.248  1.00 46.57  ? 83  LEU C N     1 
ATOM   2858 C  CA    . LEU C 1 66  ? 31.172  55.595 3.196  1.00 46.42  ? 83  LEU C CA    1 
ATOM   2859 C  C     . LEU C 1 66  ? 31.112  56.543 4.385  1.00 41.93  ? 83  LEU C C     1 
ATOM   2860 O  O     . LEU C 1 66  ? 31.237  56.070 5.527  1.00 36.44  ? 83  LEU C O     1 
ATOM   2861 C  CB    . LEU C 1 66  ? 32.525  55.684 2.485  1.00 40.17  ? 83  LEU C CB    1 
ATOM   2862 C  CG    . LEU C 1 66  ? 33.713  55.335 3.389  1.00 45.45  ? 83  LEU C CG    1 
ATOM   2863 C  CD1   . LEU C 1 66  ? 33.529  53.951 4.005  1.00 35.43  ? 83  LEU C CD1   1 
ATOM   2864 C  CD2   . LEU C 1 66  ? 35.015  55.414 2.606  1.00 55.71  ? 83  LEU C CD2   1 
ATOM   2865 N  N     . PRO C 1 67  ? 30.914  57.852 4.216  1.00 39.72  ? 84  PRO C N     1 
ATOM   2866 C  CA    . PRO C 1 67  ? 30.890  58.725 5.398  1.00 39.97  ? 84  PRO C CA    1 
ATOM   2867 C  C     . PRO C 1 67  ? 29.874  58.282 6.444  1.00 41.53  ? 84  PRO C C     1 
ATOM   2868 O  O     . PRO C 1 67  ? 30.175  58.315 7.640  1.00 39.23  ? 84  PRO C O     1 
ATOM   2869 C  CB    . PRO C 1 67  ? 30.556  60.103 4.806  1.00 43.10  ? 84  PRO C CB    1 
ATOM   2870 C  CG    . PRO C 1 67  ? 31.028  60.034 3.401  1.00 43.87  ? 84  PRO C CG    1 
ATOM   2871 C  CD    . PRO C 1 67  ? 30.770  58.621 2.963  1.00 48.62  ? 84  PRO C CD    1 
ATOM   2872 N  N     . GLY C 1 68  ? 28.688  57.834 6.024  1.00 36.41  ? 85  GLY C N     1 
ATOM   2873 C  CA    . GLY C 1 68  ? 27.691  57.399 6.985  1.00 35.46  ? 85  GLY C CA    1 
ATOM   2874 C  C     . GLY C 1 68  ? 28.027  56.068 7.622  1.00 38.10  ? 85  GLY C C     1 
ATOM   2875 O  O     . GLY C 1 68  ? 27.724  55.844 8.798  1.00 34.29  ? 85  GLY C O     1 
ATOM   2876 N  N     . LEU C 1 69  ? 28.642  55.164 6.860  1.00 29.71  ? 86  LEU C N     1 
ATOM   2877 C  CA    . LEU C 1 69  ? 29.118  53.915 7.439  1.00 36.45  ? 86  LEU C CA    1 
ATOM   2878 C  C     . LEU C 1 69  ? 30.157  54.183 8.521  1.00 30.08  ? 86  LEU C C     1 
ATOM   2879 O  O     . LEU C 1 69  ? 30.104  53.596 9.610  1.00 25.21  ? 86  LEU C O     1 
ATOM   2880 C  CB    . LEU C 1 69  ? 29.692  53.027 6.337  1.00 34.74  ? 86  LEU C CB    1 
ATOM   2881 C  CG    . LEU C 1 69  ? 30.387  51.738 6.767  1.00 34.02  ? 86  LEU C CG    1 
ATOM   2882 C  CD1   . LEU C 1 69  ? 29.487  50.883 7.660  1.00 35.99  ? 86  LEU C CD1   1 
ATOM   2883 C  CD2   . LEU C 1 69  ? 30.813  50.969 5.524  1.00 37.57  ? 86  LEU C CD2   1 
ATOM   2884 N  N     . ILE C 1 70  ? 31.116  55.068 8.237  1.00 31.27  ? 87  ILE C N     1 
ATOM   2885 C  CA    A ILE C 1 70  ? 32.135  55.388 9.232  0.59 27.53  ? 87  ILE C CA    1 
ATOM   2886 C  CA    B ILE C 1 70  ? 32.136  55.395 9.229  0.41 27.59  ? 87  ILE C CA    1 
ATOM   2887 C  C     . ILE C 1 70  ? 31.488  56.007 10.464 1.00 29.75  ? 87  ILE C C     1 
ATOM   2888 O  O     . ILE C 1 70  ? 31.887  55.720 11.597 1.00 29.20  ? 87  ILE C O     1 
ATOM   2889 C  CB    A ILE C 1 70  ? 33.225  56.298 8.629  0.59 30.23  ? 87  ILE C CB    1 
ATOM   2890 C  CB    B ILE C 1 70  ? 33.203  56.331 8.626  0.41 30.23  ? 87  ILE C CB    1 
ATOM   2891 C  CG1   A ILE C 1 70  ? 34.091  55.492 7.647  0.59 32.74  ? 87  ILE C CG1   1 
ATOM   2892 C  CG1   B ILE C 1 70  ? 33.803  55.732 7.345  0.41 32.41  ? 87  ILE C CG1   1 
ATOM   2893 C  CG2   A ILE C 1 70  ? 34.097  56.891 9.729  0.59 31.66  ? 87  ILE C CG2   1 
ATOM   2894 C  CG2   B ILE C 1 70  ? 34.318  56.580 9.627  0.41 31.54  ? 87  ILE C CG2   1 
ATOM   2895 C  CD1   A ILE C 1 70  ? 35.083  56.308 6.831  0.59 31.68  ? 87  ILE C CD1   1 
ATOM   2896 C  CD1   B ILE C 1 70  ? 34.560  54.434 7.552  0.41 28.97  ? 87  ILE C CD1   1 
ATOM   2897 N  N     . GLU C 1 71  ? 30.473  56.853 10.270 1.00 29.62  ? 88  GLU C N     1 
ATOM   2898 C  CA    . GLU C 1 71  ? 29.814  57.474 11.420 1.00 36.97  ? 88  GLU C CA    1 
ATOM   2899 C  C     . GLU C 1 71  ? 29.094  56.437 12.275 1.00 32.07  ? 88  GLU C C     1 
ATOM   2900 O  O     . GLU C 1 71  ? 29.241  56.426 13.504 1.00 32.06  ? 88  GLU C O     1 
ATOM   2901 C  CB    . GLU C 1 71  ? 28.848  58.563 10.950 1.00 44.94  ? 88  GLU C CB    1 
ATOM   2902 C  CG    . GLU C 1 71  ? 29.556  59.896 10.713 1.00 79.13  ? 88  GLU C CG    1 
ATOM   2903 C  CD    . GLU C 1 71  ? 28.692  60.927 10.003 1.00 105.29 ? 88  GLU C CD    1 
ATOM   2904 O  OE1   . GLU C 1 71  ? 27.449  60.814 10.064 1.00 103.29 ? 88  GLU C OE1   1 
ATOM   2905 O  OE2   . GLU C 1 71  ? 29.262  61.851 9.380  1.00 101.72 ? 88  GLU C OE2   1 
ATOM   2906 N  N     . LYS C 1 72  ? 28.331  55.537 11.645 1.00 30.90  ? 89  LYS C N     1 
ATOM   2907 C  CA    . LYS C 1 72  ? 27.645  54.494 12.406 1.00 28.55  ? 89  LYS C CA    1 
ATOM   2908 C  C     . LYS C 1 72  ? 28.638  53.649 13.192 1.00 22.43  ? 89  LYS C C     1 
ATOM   2909 O  O     . LYS C 1 72  ? 28.306  53.121 14.266 1.00 25.50  ? 89  LYS C O     1 
ATOM   2910 C  CB    . LYS C 1 72  ? 26.845  53.568 11.486 1.00 35.53  ? 89  LYS C CB    1 
ATOM   2911 C  CG    . LYS C 1 72  ? 25.802  54.227 10.598 1.00 55.99  ? 89  LYS C CG    1 
ATOM   2912 C  CD    . LYS C 1 72  ? 24.490  54.439 11.309 1.00 49.76  ? 89  LYS C CD    1 
ATOM   2913 C  CE    . LYS C 1 72  ? 23.588  55.383 10.512 1.00 62.02  ? 89  LYS C CE    1 
ATOM   2914 N  NZ    . LYS C 1 72  ? 22.800  56.284 11.405 1.00 82.38  ? 89  LYS C NZ    1 
ATOM   2915 N  N     . MET C 1 73  ? 29.856  53.509 12.665 1.00 26.12  ? 90  MET C N     1 
ATOM   2916 C  CA    . MET C 1 73  ? 30.850  52.596 13.211 1.00 25.86  ? 90  MET C CA    1 
ATOM   2917 C  C     . MET C 1 73  ? 31.799  53.259 14.198 1.00 23.71  ? 90  MET C C     1 
ATOM   2918 O  O     . MET C 1 73  ? 32.608  52.561 14.816 1.00 23.82  ? 90  MET C O     1 
ATOM   2919 C  CB    . MET C 1 73  ? 31.661  51.965 12.072 1.00 24.52  ? 90  MET C CB    1 
ATOM   2920 C  CG    . MET C 1 73  ? 30.927  50.890 11.289 1.00 24.51  ? 90  MET C CG    1 
ATOM   2921 S  SD    . MET C 1 73  ? 30.595  49.469 12.325 1.00 26.70  ? 90  MET C SD    1 
ATOM   2922 C  CE    . MET C 1 73  ? 32.236  48.783 12.502 1.00 28.14  ? 90  MET C CE    1 
ATOM   2923 N  N     . THR C 1 74  ? 31.727  54.579 14.355 1.00 26.51  ? 91  THR C N     1 
ATOM   2924 C  CA    . THR C 1 74  ? 32.554  55.285 15.328 1.00 26.64  ? 91  THR C CA    1 
ATOM   2925 C  C     . THR C 1 74  ? 31.909  55.111 16.693 1.00 25.29  ? 91  THR C C     1 
ATOM   2926 O  O     . THR C 1 74  ? 30.960  55.811 17.048 1.00 32.54  ? 91  THR C O     1 
ATOM   2927 C  CB    . THR C 1 74  ? 32.699  56.751 14.942 1.00 34.14  ? 91  THR C CB    1 
ATOM   2928 O  OG1   . THR C 1 74  ? 33.270  56.826 13.634 1.00 32.64  ? 91  THR C OG1   1 
ATOM   2929 C  CG2   . THR C 1 74  ? 33.620  57.457 15.886 1.00 31.20  ? 91  THR C CG2   1 
ATOM   2930 N  N     . GLY C 1 75  ? 32.436  54.174 17.458 1.00 23.51  ? 92  GLY C N     1 
ATOM   2931 C  CA    . GLY C 1 75  ? 31.897  53.809 18.743 1.00 22.84  ? 92  GLY C CA    1 
ATOM   2932 C  C     . GLY C 1 75  ? 32.576  52.539 19.203 1.00 25.36  ? 92  GLY C C     1 
ATOM   2933 O  O     . GLY C 1 75  ? 33.517  52.052 18.564 1.00 20.93  ? 92  GLY C O     1 
ATOM   2934 N  N     . PRO C 1 76  ? 32.135  52.000 20.339 1.00 19.73  ? 93  PRO C N     1 
ATOM   2935 C  CA    . PRO C 1 76  ? 32.737  50.768 20.865 1.00 20.03  ? 93  PRO C CA    1 
ATOM   2936 C  C     . PRO C 1 76  ? 32.509  49.610 19.909 1.00 19.40  ? 93  PRO C C     1 
ATOM   2937 O  O     . PRO C 1 76  ? 31.424  49.461 19.355 1.00 18.12  ? 93  PRO C O     1 
ATOM   2938 C  CB    . PRO C 1 76  ? 31.999  50.554 22.193 1.00 21.04  ? 93  PRO C CB    1 
ATOM   2939 C  CG    . PRO C 1 76  ? 30.692  51.246 22.023 1.00 20.94  ? 93  PRO C CG    1 
ATOM   2940 C  CD    . PRO C 1 76  ? 31.025  52.472 21.184 1.00 22.24  ? 93  PRO C CD    1 
ATOM   2941 N  N     . VAL C 1 77  ? 33.564  48.820 19.691 1.00 19.05  ? 94  VAL C N     1 
ATOM   2942 C  CA    . VAL C 1 77  ? 33.490  47.589 18.914 1.00 16.83  ? 94  VAL C CA    1 
ATOM   2943 C  C     . VAL C 1 77  ? 34.255  46.506 19.655 1.00 18.80  ? 94  VAL C C     1 
ATOM   2944 O  O     . VAL C 1 77  ? 35.175  46.790 20.430 1.00 19.11  ? 94  VAL C O     1 
ATOM   2945 C  CB    . VAL C 1 77  ? 34.067  47.749 17.486 1.00 16.94  ? 94  VAL C CB    1 
ATOM   2946 C  CG1   . VAL C 1 77  ? 33.284  48.780 16.692 1.00 21.51  ? 94  VAL C CG1   1 
ATOM   2947 C  CG2   . VAL C 1 77  ? 35.547  48.086 17.509 1.00 19.60  ? 94  VAL C CG2   1 
ATOM   2948 N  N     . LEU C 1 78  ? 33.881  45.251 19.412 1.00 17.29  ? 95  LEU C N     1 
ATOM   2949 C  CA    . LEU C 1 78  ? 34.646  44.111 19.925 1.00 17.84  ? 95  LEU C CA    1 
ATOM   2950 C  C     . LEU C 1 78  ? 35.358  43.449 18.757 1.00 17.86  ? 95  LEU C C     1 
ATOM   2951 O  O     . LEU C 1 78  ? 34.719  42.820 17.907 1.00 17.96  ? 95  LEU C O     1 
ATOM   2952 C  CB    . LEU C 1 78  ? 33.781  43.091 20.664 1.00 14.88  ? 95  LEU C CB    1 
ATOM   2953 C  CG    . LEU C 1 78  ? 34.610  42.066 21.457 1.00 17.69  ? 95  LEU C CG    1 
ATOM   2954 C  CD1   . LEU C 1 78  ? 35.332  42.677 22.662 1.00 18.69  ? 95  LEU C CD1   1 
ATOM   2955 C  CD2   . LEU C 1 78  ? 33.729  40.923 21.955 1.00 17.40  ? 95  LEU C CD2   1 
ATOM   2956 N  N     . CYS C 1 79  ? 36.677  43.598 18.729 1.00 17.16  ? 96  CYS C N     1 
ATOM   2957 C  CA    . CYS C 1 79  ? 37.523  42.952 17.730 1.00 16.60  ? 96  CYS C CA    1 
ATOM   2958 C  C     . CYS C 1 79  ? 37.738  41.498 18.126 1.00 19.36  ? 96  CYS C C     1 
ATOM   2959 O  O     . CYS C 1 79  ? 38.093  41.219 19.274 1.00 17.67  ? 96  CYS C O     1 
ATOM   2960 C  CB    . CYS C 1 79  ? 38.885  43.660 17.657 1.00 19.91  ? 96  CYS C CB    1 
ATOM   2961 S  SG    . CYS C 1 79  ? 38.770  45.453 17.489 1.00 21.49  ? 96  CYS C SG    1 
ATOM   2962 N  N     . MET C 1 80  ? 37.600  40.573 17.178 1.00 17.47  ? 97  MET C N     1 
ATOM   2963 C  CA    . MET C 1 80  ? 37.712  39.155 17.500 1.00 17.28  ? 97  MET C CA    1 
ATOM   2964 C  C     . MET C 1 80  ? 38.431  38.435 16.370 1.00 18.19  ? 97  MET C C     1 
ATOM   2965 O  O     . MET C 1 80  ? 38.297  38.794 15.192 1.00 18.14  ? 97  MET C O     1 
ATOM   2966 C  CB    . MET C 1 80  ? 36.356  38.486 17.742 1.00 18.98  ? 97  MET C CB    1 
ATOM   2967 C  CG    . MET C 1 80  ? 35.388  39.332 18.547 1.00 17.92  ? 97  MET C CG    1 
ATOM   2968 S  SD    . MET C 1 80  ? 33.844  38.467 18.951 1.00 17.24  ? 97  MET C SD    1 
ATOM   2969 C  CE    . MET C 1 80  ? 33.026  38.447 17.352 1.00 17.89  ? 97  MET C CE    1 
ATOM   2970 N  N     . VAL C 1 81  ? 39.187  37.406 16.738 1.00 15.76  ? 98  VAL C N     1 
ATOM   2971 C  CA    . VAL C 1 81  ? 39.725  36.436 15.782 1.00 16.13  ? 98  VAL C CA    1 
ATOM   2972 C  C     . VAL C 1 81  ? 39.266  35.067 16.228 1.00 15.73  ? 98  VAL C C     1 
ATOM   2973 O  O     . VAL C 1 81  ? 39.507  34.674 17.372 1.00 16.65  ? 98  VAL C O     1 
ATOM   2974 C  CB    . VAL C 1 81  ? 41.252  36.482 15.677 1.00 18.77  ? 98  VAL C CB    1 
ATOM   2975 C  CG1   . VAL C 1 81  ? 41.733  35.397 14.708 1.00 18.27  ? 98  VAL C CG1   1 
ATOM   2976 C  CG2   . VAL C 1 81  ? 41.700  37.847 15.199 1.00 20.88  ? 98  VAL C CG2   1 
ATOM   2977 N  N     . PHE C 1 82  ? 38.584  34.353 15.341 1.00 16.69  ? 99  PHE C N     1 
ATOM   2978 C  CA    . PHE C 1 82  ? 38.156  32.986 15.580 1.00 15.51  ? 99  PHE C CA    1 
ATOM   2979 C  C     . PHE C 1 82  ? 38.842  32.045 14.597 1.00 15.59  ? 99  PHE C C     1 
ATOM   2980 O  O     . PHE C 1 82  ? 39.070  32.387 13.426 1.00 17.02  ? 99  PHE C O     1 
ATOM   2981 C  CB    . PHE C 1 82  ? 36.630  32.821 15.434 1.00 16.23  ? 99  PHE C CB    1 
ATOM   2982 C  CG    . PHE C 1 82  ? 35.857  33.182 16.657 1.00 16.59  ? 99  PHE C CG    1 
ATOM   2983 C  CD1   . PHE C 1 82  ? 35.609  32.228 17.642 1.00 18.54  ? 99  PHE C CD1   1 
ATOM   2984 C  CD2   . PHE C 1 82  ? 35.397  34.459 16.848 1.00 17.87  ? 99  PHE C CD2   1 
ATOM   2985 C  CE1   . PHE C 1 82  ? 34.906  32.556 18.768 1.00 16.60  ? 99  PHE C CE1   1 
ATOM   2986 C  CE2   . PHE C 1 82  ? 34.682  34.788 17.997 1.00 17.80  ? 99  PHE C CE2   1 
ATOM   2987 C  CZ    . PHE C 1 82  ? 34.463  33.826 18.957 1.00 17.33  ? 99  PHE C CZ    1 
ATOM   2988 N  N     . GLU C 1 83  ? 39.147  30.848 15.081 1.00 14.83  ? 100 GLU C N     1 
ATOM   2989 C  CA    . GLU C 1 83  ? 39.841  29.819 14.322 1.00 14.93  ? 100 GLU C CA    1 
ATOM   2990 C  C     . GLU C 1 83  ? 38.981  28.574 14.168 1.00 18.58  ? 100 GLU C C     1 
ATOM   2991 O  O     . GLU C 1 83  ? 38.370  28.101 15.136 1.00 17.71  ? 100 GLU C O     1 
ATOM   2992 C  CB    . GLU C 1 83  ? 41.137  29.451 15.042 1.00 16.98  ? 100 GLU C CB    1 
ATOM   2993 C  CG    . GLU C 1 83  ? 41.907  28.324 14.379 1.00 19.02  ? 100 GLU C CG    1 
ATOM   2994 C  CD    . GLU C 1 83  ? 43.165  27.999 15.166 1.00 23.37  ? 100 GLU C CD    1 
ATOM   2995 O  OE1   . GLU C 1 83  ? 44.186  28.707 14.980 1.00 24.40  ? 100 GLU C OE1   1 
ATOM   2996 O  OE2   . GLU C 1 83  ? 43.100  27.074 15.988 1.00 22.97  ? 100 GLU C OE2   1 
ATOM   2997 N  N     . GLY C 1 84  ? 38.977  28.013 12.964 1.00 17.91  ? 101 GLY C N     1 
ATOM   2998 C  CA    . GLY C 1 84  ? 38.271  26.768 12.709 1.00 17.54  ? 101 GLY C CA    1 
ATOM   2999 C  C     . GLY C 1 84  ? 38.426  26.369 11.253 1.00 16.13  ? 101 GLY C C     1 
ATOM   3000 O  O     . GLY C 1 84  ? 38.967  27.111 10.433 1.00 18.62  ? 101 GLY C O     1 
ATOM   3001 N  N     . VAL C 1 85  ? 37.895  25.189 10.940 1.00 16.81  ? 102 VAL C N     1 
ATOM   3002 C  CA    . VAL C 1 85  ? 37.875  24.704 9.565  1.00 18.51  ? 102 VAL C CA    1 
ATOM   3003 C  C     . VAL C 1 85  ? 36.970  25.613 8.741  1.00 16.78  ? 102 VAL C C     1 
ATOM   3004 O  O     . VAL C 1 85  ? 35.796  25.816 9.077  1.00 18.17  ? 102 VAL C O     1 
ATOM   3005 C  CB    . VAL C 1 85  ? 37.392  23.244 9.526  1.00 19.48  ? 102 VAL C CB    1 
ATOM   3006 C  CG1   . VAL C 1 85  ? 37.193  22.749 8.088  1.00 22.34  ? 102 VAL C CG1   1 
ATOM   3007 C  CG2   . VAL C 1 85  ? 38.374  22.332 10.260 1.00 21.20  ? 102 VAL C CG2   1 
ATOM   3008 N  N     . ASP C 1 86  ? 37.507  26.163 7.640  1.00 17.37  ? 103 ASP C N     1 
ATOM   3009 C  CA    . ASP C 1 86  ? 36.702  26.946 6.704  1.00 16.70  ? 103 ASP C CA    1 
ATOM   3010 C  C     . ASP C 1 86  ? 36.000  28.105 7.419  1.00 16.43  ? 103 ASP C C     1 
ATOM   3011 O  O     . ASP C 1 86  ? 34.917  28.530 7.012  1.00 15.33  ? 103 ASP C O     1 
ATOM   3012 C  CB    . ASP C 1 86  ? 35.690  26.027 6.009  1.00 18.27  ? 103 ASP C CB    1 
ATOM   3013 C  CG    . ASP C 1 86  ? 35.011  26.645 4.793  1.00 23.86  ? 103 ASP C CG    1 
ATOM   3014 O  OD1   . ASP C 1 86  ? 35.660  27.396 4.008  1.00 24.50  ? 103 ASP C OD1   1 
ATOM   3015 O  OD2   . ASP C 1 86  ? 33.807  26.310 4.595  1.00 22.71  ? 103 ASP C OD2   1 
ATOM   3016 N  N     . VAL C 1 87  ? 36.604  28.623 8.496  1.00 14.38  ? 104 VAL C N     1 
ATOM   3017 C  CA    . VAL C 1 87  ? 35.862  29.539 9.358  1.00 15.43  ? 104 VAL C CA    1 
ATOM   3018 C  C     . VAL C 1 87  ? 35.565  30.862 8.676  1.00 15.60  ? 104 VAL C C     1 
ATOM   3019 O  O     . VAL C 1 87  ? 34.595  31.526 9.039  1.00 15.11  ? 104 VAL C O     1 
ATOM   3020 C  CB    . VAL C 1 87  ? 36.592  29.778 10.695 1.00 18.09  ? 104 VAL C CB    1 
ATOM   3021 C  CG1   . VAL C 1 87  ? 37.862  30.617 10.535 1.00 17.70  ? 104 VAL C CG1   1 
ATOM   3022 C  CG2   . VAL C 1 87  ? 35.612  30.399 11.725 1.00 17.82  ? 104 VAL C CG2   1 
ATOM   3023 N  N     . ILE C 1 88  ? 36.346  31.273 7.684  1.00 16.53  ? 105 ILE C N     1 
ATOM   3024 C  CA    . ILE C 1 88  ? 36.035  32.520 7.000  1.00 17.49  ? 105 ILE C CA    1 
ATOM   3025 C  C     . ILE C 1 88  ? 34.671  32.426 6.318  1.00 15.85  ? 105 ILE C C     1 
ATOM   3026 O  O     . ILE C 1 88  ? 33.755  33.206 6.612  1.00 15.59  ? 105 ILE C O     1 
ATOM   3027 C  CB    . ILE C 1 88  ? 37.144  32.880 6.003  1.00 17.57  ? 105 ILE C CB    1 
ATOM   3028 C  CG1   . ILE C 1 88  ? 38.456  33.135 6.758  1.00 16.88  ? 105 ILE C CG1   1 
ATOM   3029 C  CG2   . ILE C 1 88  ? 36.712  34.108 5.277  1.00 16.49  ? 105 ILE C CG2   1 
ATOM   3030 C  CD1   . ILE C 1 88  ? 39.657  33.252 5.832  1.00 18.59  ? 105 ILE C CD1   1 
ATOM   3031 N  N     . ALA C 1 89  ? 34.497  31.438 5.429  1.00 15.89  ? 106 ALA C N     1 
ATOM   3032 C  CA    . ALA C 1 89  ? 33.214  31.287 4.745  1.00 15.45  ? 106 ALA C CA    1 
ATOM   3033 C  C     . ALA C 1 89  ? 32.105  30.895 5.707  1.00 14.04  ? 106 ALA C C     1 
ATOM   3034 O  O     . ALA C 1 89  ? 30.960  31.321 5.552  1.00 15.34  ? 106 ALA C O     1 
ATOM   3035 C  CB    . ALA C 1 89  ? 33.334  30.253 3.625  1.00 18.63  ? 106 ALA C CB    1 
ATOM   3036 N  N     . GLN C 1 90  ? 32.422  30.066 6.695  1.00 15.85  ? 107 GLN C N     1 
ATOM   3037 C  CA    . GLN C 1 90  ? 31.381  29.609 7.607  1.00 15.21  ? 107 GLN C CA    1 
ATOM   3038 C  C     . GLN C 1 90  ? 30.876  30.740 8.491  1.00 13.62  ? 107 GLN C C     1 
ATOM   3039 O  O     . GLN C 1 90  ? 29.674  30.842 8.745  1.00 13.06  ? 107 GLN C O     1 
ATOM   3040 C  CB    . GLN C 1 90  ? 31.898  28.451 8.451  1.00 14.70  ? 107 GLN C CB    1 
ATOM   3041 C  CG    . GLN C 1 90  ? 32.081  27.178 7.662  1.00 17.05  ? 107 GLN C CG    1 
ATOM   3042 C  CD    . GLN C 1 90  ? 30.786  26.637 7.097  1.00 18.18  ? 107 GLN C CD    1 
ATOM   3043 O  OE1   . GLN C 1 90  ? 29.801  26.452 7.816  1.00 16.82  ? 107 GLN C OE1   1 
ATOM   3044 N  NE2   . GLN C 1 90  ? 30.765  26.402 5.779  1.00 20.82  ? 107 GLN C NE2   1 
ATOM   3045 N  N     . ALA C 1 91  ? 31.764  31.605 8.967  1.00 13.89  ? 108 ALA C N     1 
ATOM   3046 C  CA    . ALA C 1 91  ? 31.288  32.728 9.777  1.00 15.72  ? 108 ALA C CA    1 
ATOM   3047 C  C     . ALA C 1 91  ? 30.414  33.660 8.948  1.00 15.02  ? 108 ALA C C     1 
ATOM   3048 O  O     . ALA C 1 91  ? 29.434  34.211 9.466  1.00 15.28  ? 108 ALA C O     1 
ATOM   3049 C  CB    . ALA C 1 91  ? 32.455  33.503 10.413 1.00 14.33  ? 108 ALA C CB    1 
ATOM   3050 N  N     . ARG C 1 92  ? 30.759  33.857 7.671  1.00 15.35  ? 109 ARG C N     1 
ATOM   3051 C  CA    . ARG C 1 92  ? 29.913  34.653 6.786  1.00 15.74  ? 109 ARG C CA    1 
ATOM   3052 C  C     . ARG C 1 92  ? 28.536  34.017 6.652  1.00 14.52  ? 109 ARG C C     1 
ATOM   3053 O  O     . ARG C 1 92  ? 27.519  34.714 6.675  1.00 16.01  ? 109 ARG C O     1 
ATOM   3054 C  CB    . ARG C 1 92  ? 30.573  34.819 5.411  1.00 16.47  ? 109 ARG C CB    1 
ATOM   3055 C  CG    . ARG C 1 92  ? 31.812  35.689 5.418  1.00 18.80  ? 109 ARG C CG    1 
ATOM   3056 C  CD    . ARG C 1 92  ? 31.493  37.159 5.603  1.00 23.66  ? 109 ARG C CD    1 
ATOM   3057 N  NE    . ARG C 1 92  ? 30.970  37.728 4.365  1.00 31.61  ? 109 ARG C NE    1 
ATOM   3058 C  CZ    . ARG C 1 92  ? 30.834  39.025 4.120  1.00 42.76  ? 109 ARG C CZ    1 
ATOM   3059 N  NH1   . ARG C 1 92  ? 31.137  39.939 5.031  1.00 32.55  ? 109 ARG C NH1   1 
ATOM   3060 N  NH2   . ARG C 1 92  ? 30.394  39.417 2.926  1.00 48.37  ? 109 ARG C NH2   1 
ATOM   3061 N  N     . LYS C 1 93  ? 28.484  32.687 6.521  1.00 13.64  ? 110 LYS C N     1 
ATOM   3062 C  CA    . LYS C 1 93  ? 27.206  31.993 6.437  1.00 13.13  ? 110 LYS C CA    1 
ATOM   3063 C  C     . LYS C 1 93  ? 26.392  32.175 7.719  1.00 16.74  ? 110 LYS C C     1 
ATOM   3064 O  O     . LYS C 1 93  ? 25.172  32.389 7.676  1.00 18.34  ? 110 LYS C O     1 
ATOM   3065 C  CB    . LYS C 1 93  ? 27.456  30.524 6.157  1.00 15.14  ? 110 LYS C CB    1 
ATOM   3066 C  CG    . LYS C 1 93  ? 26.233  29.677 6.038  1.00 18.82  ? 110 LYS C CG    1 
ATOM   3067 C  CD    . LYS C 1 93  ? 26.651  28.295 5.541  1.00 25.60  ? 110 LYS C CD    1 
ATOM   3068 C  CE    . LYS C 1 93  ? 25.491  27.335 5.455  1.00 27.08  ? 110 LYS C CE    1 
ATOM   3069 N  NZ    . LYS C 1 93  ? 25.951  26.008 4.940  1.00 23.86  ? 110 LYS C NZ    1 
ATOM   3070 N  N     . MET C 1 94  ? 27.054  32.090 8.864  1.00 14.48  ? 111 MET C N     1 
ATOM   3071 C  CA    . MET C 1 94  ? 26.381  32.251 10.150 1.00 13.91  ? 111 MET C CA    1 
ATOM   3072 C  C     . MET C 1 94  ? 25.878  33.675 10.354 1.00 15.83  ? 111 MET C C     1 
ATOM   3073 O  O     . MET C 1 94  ? 24.865  33.880 11.044 1.00 15.00  ? 111 MET C O     1 
ATOM   3074 C  CB    . MET C 1 94  ? 27.352  31.859 11.276 1.00 13.85  ? 111 MET C CB    1 
ATOM   3075 C  CG    . MET C 1 94  ? 27.694  30.395 11.290 1.00 13.42  ? 111 MET C CG    1 
ATOM   3076 S  SD    . MET C 1 94  ? 29.138  30.066 12.292 1.00 15.76  ? 111 MET C SD    1 
ATOM   3077 C  CE    . MET C 1 94  ? 28.417  30.171 13.924 1.00 19.55  ? 111 MET C CE    1 
ATOM   3078 N  N     . MET C 1 95  ? 26.609  34.665 9.823  1.00 14.99  ? 112 MET C N     1 
ATOM   3079 C  CA    . MET C 1 95  ? 26.184  36.060 9.918  1.00 14.87  ? 112 MET C CA    1 
ATOM   3080 C  C     . MET C 1 95  ? 24.934  36.316 9.096  1.00 16.45  ? 112 MET C C     1 
ATOM   3081 O  O     . MET C 1 95  ? 24.051  37.063 9.527  1.00 14.59  ? 112 MET C O     1 
ATOM   3082 C  CB    . MET C 1 95  ? 27.308  36.980 9.446  1.00 16.05  ? 112 MET C CB    1 
ATOM   3083 C  CG    . MET C 1 95  ? 28.419  37.135 10.438 1.00 19.40  ? 112 MET C CG    1 
ATOM   3084 S  SD    . MET C 1 95  ? 29.790  38.031 9.690  1.00 23.69  ? 112 MET C SD    1 
ATOM   3085 C  CE    . MET C 1 95  ? 29.005  39.328 8.760  1.00 28.44  ? 112 MET C CE    1 
ATOM   3086 N  N     . GLY C 1 96  ? 24.859  35.728 7.910  1.00 14.81  ? 113 GLY C N     1 
ATOM   3087 C  CA    . GLY C 1 96  ? 23.775  35.968 6.986  1.00 15.82  ? 113 GLY C CA    1 
ATOM   3088 C  C     . GLY C 1 96  ? 24.033  37.167 6.093  1.00 15.15  ? 113 GLY C C     1 
ATOM   3089 O  O     . GLY C 1 96  ? 24.991  37.929 6.262  1.00 16.98  ? 113 GLY C O     1 
ATOM   3090 N  N     . SER C 1 97  ? 23.137  37.325 5.114  1.00 17.35  ? 114 SER C N     1 
ATOM   3091 C  CA    . SER C 1 97  ? 23.215  38.414 4.148  1.00 20.29  ? 114 SER C CA    1 
ATOM   3092 C  C     . SER C 1 97  ? 23.334  39.775 4.813  1.00 16.72  ? 114 SER C C     1 
ATOM   3093 O  O     . SER C 1 97  ? 22.828  39.999 5.922  1.00 16.92  ? 114 SER C O     1 
ATOM   3094 C  CB    . SER C 1 97  ? 21.961  38.425 3.267  1.00 19.62  ? 114 SER C CB    1 
ATOM   3095 O  OG    . SER C 1 97  ? 21.662  37.122 2.788  1.00 28.77  ? 114 SER C OG    1 
ATOM   3096 N  N     . THR C 1 98  ? 23.963  40.692 4.075  1.00 15.70  ? 115 THR C N     1 
ATOM   3097 C  CA    . THR C 1 98  ? 24.165  42.074 4.518  1.00 20.12  ? 115 THR C CA    1 
ATOM   3098 C  C     . THR C 1 98  ? 22.861  42.708 4.975  1.00 16.83  ? 115 THR C C     1 
ATOM   3099 O  O     . THR C 1 98  ? 22.806  43.389 6.005  1.00 17.69  ? 115 THR C O     1 
ATOM   3100 C  CB    . THR C 1 98  ? 24.753  42.902 3.360  1.00 23.59  ? 115 THR C CB    1 
ATOM   3101 O  OG1   . THR C 1 98  ? 25.943  42.269 2.871  1.00 25.80  ? 115 THR C OG1   1 
ATOM   3102 C  CG2   . THR C 1 98  ? 25.081  44.325 3.805  1.00 26.03  ? 115 THR C CG2   1 
ATOM   3103 N  N     . ARG C 1 99  ? 21.804  42.526 4.180  1.00 16.71  ? 116 ARG C N     1 
ATOM   3104 C  CA    . ARG C 1 99  ? 20.482  43.048 4.492  1.00 17.09  ? 116 ARG C CA    1 
ATOM   3105 C  C     . ARG C 1 99  ? 19.764  42.019 5.355  1.00 17.04  ? 116 ARG C C     1 
ATOM   3106 O  O     . ARG C 1 99  ? 19.459  40.924 4.867  1.00 16.21  ? 116 ARG C O     1 
ATOM   3107 C  CB    . ARG C 1 99  ? 19.707  43.312 3.212  1.00 19.06  ? 116 ARG C CB    1 
ATOM   3108 C  CG    . ARG C 1 99  ? 20.387  44.377 2.342  1.00 21.90  ? 116 ARG C CG    1 
ATOM   3109 C  CD    . ARG C 1 99  ? 19.724  44.512 0.982  1.00 32.22  ? 116 ARG C CD    1 
ATOM   3110 N  NE    . ARG C 1 99  ? 19.972  45.837 0.427  1.00 46.61  ? 116 ARG C NE    1 
ATOM   3111 C  CZ    . ARG C 1 99  ? 19.413  46.310 -0.677 1.00 89.94  ? 116 ARG C CZ    1 
ATOM   3112 N  NH1   . ARG C 1 99  ? 18.612  45.564 -1.423 1.00 98.52  ? 116 ARG C NH1   1 
ATOM   3113 N  NH2   . ARG C 1 99  ? 19.661  47.567 -1.041 1.00 89.90  ? 116 ARG C NH2   1 
ATOM   3114 N  N     . PRO C 1 100 ? 19.477  42.314 6.628  1.00 15.65  ? 117 PRO C N     1 
ATOM   3115 C  CA    . PRO C 1 100 ? 18.832  41.318 7.496  1.00 15.26  ? 117 PRO C CA    1 
ATOM   3116 C  C     . PRO C 1 100 ? 17.562  40.728 6.911  1.00 13.70  ? 117 PRO C C     1 
ATOM   3117 O  O     . PRO C 1 100 ? 17.273  39.540 7.137  1.00 14.16  ? 117 PRO C O     1 
ATOM   3118 C  CB    . PRO C 1 100 ? 18.570  42.123 8.786  1.00 14.05  ? 117 PRO C CB    1 
ATOM   3119 C  CG    . PRO C 1 100 ? 19.639  43.115 8.830  1.00 13.28  ? 117 PRO C CG    1 
ATOM   3120 C  CD    . PRO C 1 100 ? 19.797  43.546 7.361  1.00 15.43  ? 117 PRO C CD    1 
ATOM   3121 N  N     . GLY C 1 101 ? 16.790  41.512 6.154  1.00 14.88  ? 118 GLY C N     1 
ATOM   3122 C  CA    . GLY C 1 101 ? 15.548  40.998 5.600  1.00 18.53  ? 118 GLY C CA    1 
ATOM   3123 C  C     . GLY C 1 101 ? 15.748  39.901 4.570  1.00 17.47  ? 118 GLY C C     1 
ATOM   3124 O  O     . GLY C 1 101 ? 14.817  39.140 4.305  1.00 18.04  ? 118 GLY C O     1 
ATOM   3125 N  N     . GLU C 1 102 ? 16.939  39.829 3.969  1.00 14.12  ? 119 GLU C N     1 
ATOM   3126 C  CA    . GLU C 1 102 ? 17.293  38.804 3.008  1.00 15.99  ? 119 GLU C CA    1 
ATOM   3127 C  C     . GLU C 1 102 ? 18.056  37.646 3.620  1.00 19.94  ? 119 GLU C C     1 
ATOM   3128 O  O     . GLU C 1 102 ? 18.237  36.627 2.945  1.00 18.39  ? 119 GLU C O     1 
ATOM   3129 C  CB    . GLU C 1 102 ? 18.147  39.414 1.883  1.00 18.71  ? 119 GLU C CB    1 
ATOM   3130 C  CG    . GLU C 1 102 ? 17.405  40.486 1.108  1.00 21.65  ? 119 GLU C CG    1 
ATOM   3131 C  CD    . GLU C 1 102 ? 18.252  41.165 0.030  1.00 29.66  ? 119 GLU C CD    1 
ATOM   3132 O  OE1   . GLU C 1 102 ? 19.486  41.002 0.003  1.00 30.27  ? 119 GLU C OE1   1 
ATOM   3133 O  OE2   . GLU C 1 102 ? 17.663  41.885 -0.790 1.00 33.16  ? 119 GLU C OE2   1 
ATOM   3134 N  N     . ALA C 1 103 ? 18.506  37.787 4.867  1.00 16.49  ? 120 ALA C N     1 
ATOM   3135 C  CA    . ALA C 1 103 ? 19.297  36.761 5.513  1.00 14.70  ? 120 ALA C CA    1 
ATOM   3136 C  C     . ALA C 1 103 ? 18.441  35.566 5.903  1.00 15.51  ? 120 ALA C C     1 
ATOM   3137 O  O     . ALA C 1 103 ? 17.250  35.681 6.192  1.00 17.38  ? 120 ALA C O     1 
ATOM   3138 C  CB    . ALA C 1 103 ? 19.980  37.340 6.742  1.00 15.61  ? 120 ALA C CB    1 
ATOM   3139 N  N     . ALA C 1 104 ? 19.069  34.406 5.909  1.00 17.02  ? 121 ALA C N     1 
ATOM   3140 C  CA    . ALA C 1 104 ? 18.337  33.182 6.173  1.00 22.28  ? 121 ALA C CA    1 
ATOM   3141 C  C     . ALA C 1 104 ? 17.947  33.084 7.644  1.00 21.43  ? 121 ALA C C     1 
ATOM   3142 O  O     . ALA C 1 104 ? 18.715  33.468 8.532  1.00 16.67  ? 121 ALA C O     1 
ATOM   3143 C  CB    . ALA C 1 104 ? 19.185  31.973 5.788  1.00 23.84  ? 121 ALA C CB    1 
ATOM   3144 N  N     . PRO C 1 105 ? 16.793  32.501 7.946  1.00 22.50  ? 122 PRO C N     1 
ATOM   3145 C  CA    . PRO C 1 105 ? 16.455  32.264 9.348  1.00 24.08  ? 122 PRO C CA    1 
ATOM   3146 C  C     . PRO C 1 105 ? 17.541  31.443 10.022 1.00 15.22  ? 122 PRO C C     1 
ATOM   3147 O  O     . PRO C 1 105 ? 18.133  30.543 9.423  1.00 19.41  ? 122 PRO C O     1 
ATOM   3148 C  CB    . PRO C 1 105 ? 15.128  31.497 9.273  1.00 33.43  ? 122 PRO C CB    1 
ATOM   3149 C  CG    . PRO C 1 105 ? 14.558  31.892 7.941  1.00 29.84  ? 122 PRO C CG    1 
ATOM   3150 C  CD    . PRO C 1 105 ? 15.738  32.019 7.034  1.00 29.64  ? 122 PRO C CD    1 
ATOM   3151 N  N     . GLY C 1 106 ? 17.833  31.793 11.259 1.00 17.02  ? 123 GLY C N     1 
ATOM   3152 C  CA    . GLY C 1 106 ? 18.872  31.148 12.013 1.00 18.24  ? 123 GLY C CA    1 
ATOM   3153 C  C     . GLY C 1 106 ? 20.235  31.790 11.898 1.00 17.28  ? 123 GLY C C     1 
ATOM   3154 O  O     . GLY C 1 106 ? 21.170  31.344 12.577 1.00 18.86  ? 123 GLY C O     1 
ATOM   3155 N  N     . THR C 1 107 ? 20.397  32.776 11.018 1.00 14.43  ? 124 THR C N     1 
ATOM   3156 C  CA    . THR C 1 107 ? 21.620  33.556 10.995 1.00 11.63  ? 124 THR C CA    1 
ATOM   3157 C  C     . THR C 1 107 ? 21.547  34.724 11.979 1.00 11.38  ? 124 THR C C     1 
ATOM   3158 O  O     . THR C 1 107 ? 20.468  35.129 12.421 1.00 13.22  ? 124 THR C O     1 
ATOM   3159 C  CB    . THR C 1 107 ? 21.887  34.103 9.606  1.00 12.47  ? 124 THR C CB    1 
ATOM   3160 O  OG1   . THR C 1 107 ? 20.823  34.997 9.235  1.00 13.78  ? 124 THR C OG1   1 
ATOM   3161 C  CG2   . THR C 1 107 ? 21.991  32.978 8.574  1.00 14.96  ? 124 THR C CG2   1 
ATOM   3162 N  N     . ILE C 1 108 ? 22.717  35.273 12.308 1.00 13.17  ? 125 ILE C N     1 
ATOM   3163 C  CA    . ILE C 1 108 ? 22.767  36.389 13.255 1.00 13.56  ? 125 ILE C CA    1 
ATOM   3164 C  C     . ILE C 1 108 ? 21.939  37.571 12.745 1.00 15.11  ? 125 ILE C C     1 
ATOM   3165 O  O     . ILE C 1 108 ? 21.129  38.158 13.483 1.00 14.39  ? 125 ILE C O     1 
ATOM   3166 C  CB    . ILE C 1 108 ? 24.220  36.806 13.526 1.00 12.57  ? 125 ILE C CB    1 
ATOM   3167 C  CG1   . ILE C 1 108 ? 24.955  35.705 14.273 1.00 13.77  ? 125 ILE C CG1   1 
ATOM   3168 C  CG2   . ILE C 1 108 ? 24.269  38.081 14.340 1.00 14.06  ? 125 ILE C CG2   1 
ATOM   3169 C  CD1   . ILE C 1 108 ? 26.463  35.922 14.272 1.00 14.96  ? 125 ILE C CD1   1 
ATOM   3170 N  N     . ARG C 1 109 ? 22.161  37.980 11.497 1.00 12.38  ? 126 ARG C N     1 
ATOM   3171 C  CA    . ARG C 1 109 ? 21.477  39.175 11.025 1.00 13.22  ? 126 ARG C CA    1 
ATOM   3172 C  C     . ARG C 1 109 ? 19.970  38.960 10.949 1.00 12.57  ? 126 ARG C C     1 
ATOM   3173 O  O     . ARG C 1 109 ? 19.204  39.849 11.321 1.00 12.82  ? 126 ARG C O     1 
ATOM   3174 C  CB    . ARG C 1 109 ? 22.086  39.624 9.698  1.00 13.93  ? 126 ARG C CB    1 
ATOM   3175 C  CG    . ARG C 1 109 ? 23.476  40.216 9.964  1.00 17.45  ? 126 ARG C CG    1 
ATOM   3176 C  CD    . ARG C 1 109 ? 24.262  40.415 8.731  1.00 20.19  ? 126 ARG C CD    1 
ATOM   3177 N  NE    . ARG C 1 109 ? 25.543  41.060 9.000  1.00 17.64  ? 126 ARG C NE    1 
ATOM   3178 C  CZ    . ARG C 1 109 ? 26.433  41.256 8.044  1.00 20.06  ? 126 ARG C CZ    1 
ATOM   3179 N  NH1   . ARG C 1 109 ? 26.260  40.737 6.831  1.00 22.92  ? 126 ARG C NH1   1 
ATOM   3180 N  NH2   . ARG C 1 109 ? 27.489  42.019 8.286  1.00 21.45  ? 126 ARG C NH2   1 
ATOM   3181 N  N     . ALA C 1 110 ? 19.521  37.788 10.492 1.00 12.89  ? 127 ALA C N     1 
ATOM   3182 C  CA    . ALA C 1 110 ? 18.085  37.498 10.474 1.00 12.96  ? 127 ALA C CA    1 
ATOM   3183 C  C     . ALA C 1 110 ? 17.497  37.424 11.877 1.00 13.61  ? 127 ALA C C     1 
ATOM   3184 O  O     . ALA C 1 110 ? 16.337  37.800 12.084 1.00 15.65  ? 127 ALA C O     1 
ATOM   3185 C  CB    . ALA C 1 110 ? 17.801  36.190 9.749  1.00 15.57  ? 127 ALA C CB    1 
ATOM   3186 N  N     . ASP C 1 111 ? 18.242  36.905 12.833 1.00 11.99  ? 128 ASP C N     1 
ATOM   3187 C  CA    . ASP C 1 111 ? 17.654  36.683 14.145 1.00 11.56  ? 128 ASP C CA    1 
ATOM   3188 C  C     . ASP C 1 111 ? 17.639  37.932 15.016 1.00 14.77  ? 128 ASP C C     1 
ATOM   3189 O  O     . ASP C 1 111 ? 16.813  38.002 15.934 1.00 13.38  ? 128 ASP C O     1 
ATOM   3190 C  CB    . ASP C 1 111 ? 18.414  35.591 14.916 1.00 14.13  ? 128 ASP C CB    1 
ATOM   3191 C  CG    . ASP C 1 111 ? 18.233  34.191 14.341 1.00 21.44  ? 128 ASP C CG    1 
ATOM   3192 O  OD1   . ASP C 1 111 ? 17.295  33.959 13.541 1.00 22.52  ? 128 ASP C OD1   1 
ATOM   3193 O  OD2   . ASP C 1 111 ? 19.050  33.304 14.718 1.00 20.62  ? 128 ASP C OD2   1 
ATOM   3194 N  N     . PHE C 1 112 ? 18.522  38.910 14.744 1.00 11.37  ? 129 PHE C N     1 
ATOM   3195 C  CA    . PHE C 1 112 ? 18.700  40.083 15.594 1.00 12.55  ? 129 PHE C CA    1 
ATOM   3196 C  C     . PHE C 1 112 ? 18.354  41.424 14.953 1.00 13.36  ? 129 PHE C C     1 
ATOM   3197 O  O     . PHE C 1 112 ? 18.212  42.403 15.689 1.00 13.01  ? 129 PHE C O     1 
ATOM   3198 C  CB    . PHE C 1 112 ? 20.150  40.219 16.061 1.00 12.18  ? 129 PHE C CB    1 
ATOM   3199 C  CG    . PHE C 1 112 ? 20.588  39.215 17.102 1.00 13.01  ? 129 PHE C CG    1 
ATOM   3200 C  CD1   . PHE C 1 112 ? 21.151  38.008 16.712 1.00 14.06  ? 129 PHE C CD1   1 
ATOM   3201 C  CD2   . PHE C 1 112 ? 20.512  39.511 18.442 1.00 16.23  ? 129 PHE C CD2   1 
ATOM   3202 C  CE1   . PHE C 1 112 ? 21.627  37.099 17.641 1.00 17.02  ? 129 PHE C CE1   1 
ATOM   3203 C  CE2   . PHE C 1 112 ? 20.974  38.595 19.389 1.00 17.09  ? 129 PHE C CE2   1 
ATOM   3204 C  CZ    . PHE C 1 112 ? 21.531  37.394 18.985 1.00 16.94  ? 129 PHE C CZ    1 
ATOM   3205 N  N     . CYS C 1 113 ? 18.317  41.535 13.620 1.00 12.96  ? 130 CYS C N     1 
ATOM   3206 C  CA    . CYS C 1 113 ? 18.389  42.843 12.986 1.00 13.11  ? 130 CYS C CA    1 
ATOM   3207 C  C     . CYS C 1 113 ? 17.281  43.066 11.960 1.00 13.19  ? 130 CYS C C     1 
ATOM   3208 O  O     . CYS C 1 113 ? 16.544  42.157 11.576 1.00 13.81  ? 130 CYS C O     1 
ATOM   3209 C  CB    . CYS C 1 113 ? 19.758  43.034 12.326 1.00 12.75  ? 130 CYS C CB    1 
ATOM   3210 S  SG    . CYS C 1 113 ? 21.146  42.893 13.516 1.00 14.83  ? 130 CYS C SG    1 
ATOM   3211 N  N     . GLN C 1 114 ? 17.204  44.325 11.509 1.00 14.33  ? 131 GLN C N     1 
ATOM   3212 C  CA    . GLN C 1 114 ? 16.207  44.781 10.559 1.00 14.39  ? 131 GLN C CA    1 
ATOM   3213 C  C     . GLN C 1 114 ? 16.800  45.396 9.310  1.00 13.21  ? 131 GLN C C     1 
ATOM   3214 O  O     . GLN C 1 114 ? 16.261  45.174 8.220  1.00 16.84  ? 131 GLN C O     1 
ATOM   3215 C  CB    . GLN C 1 114 ? 15.280  45.817 11.212 1.00 15.17  ? 131 GLN C CB    1 
ATOM   3216 C  CG    . GLN C 1 114 ? 14.434  45.245 12.354 1.00 13.66  ? 131 GLN C CG    1 
ATOM   3217 C  CD    . GLN C 1 114 ? 13.421  46.222 12.890 1.00 14.80  ? 131 GLN C CD    1 
ATOM   3218 O  OE1   . GLN C 1 114 ? 12.710  46.908 12.137 1.00 14.91  ? 131 GLN C OE1   1 
ATOM   3219 N  NE2   . GLN C 1 114 ? 13.313  46.279 14.221 1.00 13.60  ? 131 GLN C NE2   1 
ATOM   3220 N  N     . GLN C 1 115 ? 17.866  46.185 9.440  1.00 16.80  ? 132 GLN C N     1 
ATOM   3221 C  CA    . GLN C 1 115 ? 18.394  46.962 8.331  1.00 15.79  ? 132 GLN C CA    1 
ATOM   3222 C  C     . GLN C 1 115 ? 19.902  46.789 8.220  1.00 14.08  ? 132 GLN C C     1 
ATOM   3223 O  O     . GLN C 1 115 ? 20.607  46.606 9.216  1.00 16.87  ? 132 GLN C O     1 
ATOM   3224 C  CB    . GLN C 1 115 ? 18.059  48.457 8.476  1.00 19.35  ? 132 GLN C CB    1 
ATOM   3225 C  CG    . GLN C 1 115 ? 16.553  48.720 8.528  1.00 21.41  ? 132 GLN C CG    1 
ATOM   3226 C  CD    . GLN C 1 115 ? 16.201  50.193 8.438  1.00 20.09  ? 132 GLN C CD    1 
ATOM   3227 O  OE1   . GLN C 1 115 ? 16.416  50.950 9.372  1.00 22.83  ? 132 GLN C OE1   1 
ATOM   3228 N  NE2   . GLN C 1 115 ? 15.667  50.608 7.286  1.00 26.78  ? 132 GLN C NE2   1 
ATOM   3229 N  N     . ALA C 1 116 ? 20.391  46.897 6.979  1.00 19.10  ? 133 ALA C N     1 
ATOM   3230 C  CA    . ALA C 1 116 ? 21.812  46.722 6.710  1.00 19.45  ? 133 ALA C CA    1 
ATOM   3231 C  C     . ALA C 1 116 ? 22.679  47.692 7.499  1.00 18.65  ? 133 ALA C C     1 
ATOM   3232 O  O     . ALA C 1 116 ? 23.766  47.320 7.961  1.00 20.61  ? 133 ALA C O     1 
ATOM   3233 C  CB    . ALA C 1 116 ? 22.089  46.898 5.220  1.00 17.98  ? 133 ALA C CB    1 
ATOM   3234 N  N     . GLY C 1 117 ? 22.222  48.937 7.667  1.00 21.04  ? 134 GLY C N     1 
ATOM   3235 C  CA    . GLY C 1 117 ? 23.034  49.916 8.374  1.00 22.98  ? 134 GLY C CA    1 
ATOM   3236 C  C     . GLY C 1 117 ? 23.212  49.614 9.850  1.00 20.25  ? 134 GLY C C     1 
ATOM   3237 O  O     . GLY C 1 117 ? 24.092  50.206 10.494 1.00 20.69  ? 134 GLY C O     1 
ATOM   3238 N  N     . ARG C 1 118 ? 22.382  48.732 10.411 1.00 17.54  ? 135 ARG C N     1 
ATOM   3239 C  CA    . ARG C 1 118 ? 22.551  48.265 11.789 1.00 15.74  ? 135 ARG C CA    1 
ATOM   3240 C  C     . ARG C 1 118 ? 22.452  46.731 11.789 1.00 16.06  ? 135 ARG C C     1 
ATOM   3241 O  O     . ARG C 1 118 ? 21.450  46.166 12.238 1.00 15.28  ? 135 ARG C O     1 
ATOM   3242 C  CB    . ARG C 1 118 ? 21.493  48.898 12.718 1.00 17.49  ? 135 ARG C CB    1 
ATOM   3243 C  CG    . ARG C 1 118 ? 21.678  50.400 12.972 1.00 17.89  ? 135 ARG C CG    1 
ATOM   3244 C  CD    . ARG C 1 118 ? 23.006  50.667 13.626 1.00 17.94  ? 135 ARG C CD    1 
ATOM   3245 N  NE    . ARG C 1 118 ? 23.103  52.006 14.198 1.00 20.74  ? 135 ARG C NE    1 
ATOM   3246 C  CZ    . ARG C 1 118 ? 24.222  52.511 14.703 1.00 22.71  ? 135 ARG C CZ    1 
ATOM   3247 N  NH1   . ARG C 1 118 ? 25.364  51.853 14.650 1.00 23.01  ? 135 ARG C NH1   1 
ATOM   3248 N  NH2   . ARG C 1 118 ? 24.200  53.724 15.242 1.00 24.95  ? 135 ARG C NH2   1 
ATOM   3249 N  N     . ASN C 1 119 ? 23.518  46.068 11.364 1.00 15.94  ? 136 ASN C N     1 
ATOM   3250 C  CA    . ASN C 1 119 ? 23.485  44.623 11.153 1.00 12.90  ? 136 ASN C CA    1 
ATOM   3251 C  C     . ASN C 1 119 ? 24.513  43.889 12.004 1.00 15.48  ? 136 ASN C C     1 
ATOM   3252 O  O     . ASN C 1 119 ? 24.954  42.794 11.657 1.00 14.85  ? 136 ASN C O     1 
ATOM   3253 C  CB    . ASN C 1 119 ? 23.632  44.274 9.672  1.00 13.04  ? 136 ASN C CB    1 
ATOM   3254 C  CG    . ASN C 1 119 ? 24.946  44.666 9.085  1.00 17.23  ? 136 ASN C CG    1 
ATOM   3255 O  OD1   . ASN C 1 119 ? 25.831  45.169 9.767  1.00 16.10  ? 136 ASN C OD1   1 
ATOM   3256 N  ND2   . ASN C 1 119 ? 25.106  44.394 7.790  1.00 19.09  ? 136 ASN C ND2   1 
ATOM   3257 N  N     . LEU C 1 120 ? 24.875  44.505 13.142 1.00 13.37  ? 137 LEU C N     1 
ATOM   3258 C  CA    . LEU C 1 120 ? 25.438  43.911 14.352 1.00 14.36  ? 137 LEU C CA    1 
ATOM   3259 C  C     . LEU C 1 120 ? 26.884  43.436 14.321 1.00 14.14  ? 137 LEU C C     1 
ATOM   3260 O  O     . LEU C 1 120 ? 27.595  43.556 15.335 1.00 16.97  ? 137 LEU C O     1 
ATOM   3261 C  CB    . LEU C 1 120 ? 24.642  42.659 14.745 1.00 15.57  ? 137 LEU C CB    1 
ATOM   3262 C  CG    . LEU C 1 120 ? 24.391  42.453 16.235 1.00 15.18  ? 137 LEU C CG    1 
ATOM   3263 C  CD1   . LEU C 1 120 ? 23.349  43.471 16.683 1.00 14.83  ? 137 LEU C CD1   1 
ATOM   3264 C  CD2   . LEU C 1 120 ? 23.909  41.016 16.550 1.00 16.63  ? 137 LEU C CD2   1 
ATOM   3265 N  N     . ILE C 1 121 ? 27.383  43.019 13.162 1.00 13.81  ? 138 ILE C N     1 
ATOM   3266 C  CA    . ILE C 1 121 ? 28.644  42.282 13.118 1.00 15.63  ? 138 ILE C CA    1 
ATOM   3267 C  C     . ILE C 1 121 ? 29.235  42.380 11.722 1.00 16.34  ? 138 ILE C C     1 
ATOM   3268 O  O     . ILE C 1 121 ? 28.513  42.460 10.719 1.00 15.82  ? 138 ILE C O     1 
ATOM   3269 C  CB    . ILE C 1 121 ? 28.433  40.809 13.553 1.00 14.08  ? 138 ILE C CB    1 
ATOM   3270 C  CG1   . ILE C 1 121 ? 29.769  40.052 13.620 1.00 18.54  ? 138 ILE C CG1   1 
ATOM   3271 C  CG2   . ILE C 1 121 ? 27.442  40.105 12.621 1.00 18.14  ? 138 ILE C CG2   1 
ATOM   3272 C  CD1   . ILE C 1 121 ? 29.642  38.733 14.354 1.00 18.12  ? 138 ILE C CD1   1 
ATOM   3273 N  N     . HIS C 1 122 ? 30.563  42.432 11.674 1.00 15.32  ? 139 HIS C N     1 
ATOM   3274 C  CA    . HIS C 1 122 ? 31.365  42.334 10.470 1.00 17.09  ? 139 HIS C CA    1 
ATOM   3275 C  C     . HIS C 1 122 ? 32.164  41.036 10.500 1.00 16.67  ? 139 HIS C C     1 
ATOM   3276 O  O     . HIS C 1 122 ? 32.656  40.633 11.557 1.00 15.77  ? 139 HIS C O     1 
ATOM   3277 C  CB    . HIS C 1 122 ? 32.359  43.496 10.376 1.00 18.26  ? 139 HIS C CB    1 
ATOM   3278 C  CG    . HIS C 1 122 ? 33.485  43.197 9.447  1.00 18.19  ? 139 HIS C CG    1 
ATOM   3279 N  ND1   . HIS C 1 122 ? 33.412  43.470 8.100  1.00 24.74  ? 139 HIS C ND1   1 
ATOM   3280 C  CD2   . HIS C 1 122 ? 34.674  42.581 9.651  1.00 19.55  ? 139 HIS C CD2   1 
ATOM   3281 C  CE1   . HIS C 1 122 ? 34.520  43.052 7.512  1.00 21.91  ? 139 HIS C CE1   1 
ATOM   3282 N  NE2   . HIS C 1 122 ? 35.300  42.504 8.428  1.00 20.26  ? 139 HIS C NE2   1 
ATOM   3283 N  N     . GLY C 1 123 ? 32.313  40.393 9.345  1.00 17.92  ? 140 GLY C N     1 
ATOM   3284 C  CA    . GLY C 1 123 ? 33.268  39.303 9.208  1.00 16.75  ? 140 GLY C CA    1 
ATOM   3285 C  C     . GLY C 1 123 ? 34.018  39.383 7.891  1.00 16.62  ? 140 GLY C C     1 
ATOM   3286 O  O     . GLY C 1 123 ? 33.468  39.778 6.858  1.00 16.89  ? 140 GLY C O     1 
ATOM   3287 N  N     . SER C 1 124 ? 35.273  38.949 7.932  1.00 16.10  ? 141 SER C N     1 
ATOM   3288 C  CA    . SER C 1 124 ? 36.104  38.908 6.730  1.00 15.25  ? 141 SER C CA    1 
ATOM   3289 C  C     . SER C 1 124 ? 35.421  38.082 5.647  1.00 14.78  ? 141 SER C C     1 
ATOM   3290 O  O     . SER C 1 124 ? 34.795  37.057 5.933  1.00 18.09  ? 141 SER C O     1 
ATOM   3291 C  CB    . SER C 1 124 ? 37.465  38.293 7.050  1.00 16.64  ? 141 SER C CB    1 
ATOM   3292 O  OG    . SER C 1 124 ? 38.106  38.932 8.119  1.00 18.09  ? 141 SER C OG    1 
ATOM   3293 N  N     . ASP C 1 125 ? 35.532  38.515 4.380  1.00 16.81  ? 142 ASP C N     1 
ATOM   3294 C  CA    . ASP C 1 125 ? 34.839  37.791 3.321  1.00 19.05  ? 142 ASP C CA    1 
ATOM   3295 C  C     . ASP C 1 125 ? 35.739  36.891 2.468  1.00 17.89  ? 142 ASP C C     1 
ATOM   3296 O  O     . ASP C 1 125 ? 35.223  36.197 1.576  1.00 20.84  ? 142 ASP C O     1 
ATOM   3297 C  CB    . ASP C 1 125 ? 34.022  38.762 2.437  1.00 27.66  ? 142 ASP C CB    1 
ATOM   3298 C  CG    . ASP C 1 125 ? 34.847  39.814 1.725  1.00 29.05  ? 142 ASP C CG    1 
ATOM   3299 O  OD1   . ASP C 1 125 ? 36.081  39.714 1.642  1.00 24.48  ? 142 ASP C OD1   1 
ATOM   3300 O  OD2   . ASP C 1 125 ? 34.215  40.758 1.169  1.00 33.39  ? 142 ASP C OD2   1 
ATOM   3301 N  N     . SER C 1 126 ? 37.036  36.830 2.748  1.00 17.47  ? 143 SER C N     1 
ATOM   3302 C  CA    . SER C 1 126 ? 37.964  36.029 1.963  1.00 16.52  ? 143 SER C CA    1 
ATOM   3303 C  C     . SER C 1 126 ? 39.250  35.827 2.750  1.00 17.10  ? 143 SER C C     1 
ATOM   3304 O  O     . SER C 1 126 ? 39.517  36.503 3.740  1.00 17.64  ? 143 SER C O     1 
ATOM   3305 C  CB    . SER C 1 126 ? 38.284  36.699 0.617  1.00 19.51  ? 143 SER C CB    1 
ATOM   3306 O  OG    . SER C 1 126 ? 39.156  37.804 0.832  1.00 18.96  ? 143 SER C OG    1 
ATOM   3307 N  N     . ALA C 1 127 ? 40.093  34.927 2.244  1.00 17.62  ? 144 ALA C N     1 
ATOM   3308 C  CA    . ALA C 1 127 ? 41.378  34.703 2.879  1.00 17.17  ? 144 ALA C CA    1 
ATOM   3309 C  C     . ALA C 1 127 ? 42.230  35.968 2.872  1.00 19.50  ? 144 ALA C C     1 
ATOM   3310 O  O     . ALA C 1 127 ? 42.867  36.297 3.875  1.00 18.88  ? 144 ALA C O     1 
ATOM   3311 C  CB    . ALA C 1 127 ? 42.112  33.564 2.178  1.00 21.75  ? 144 ALA C CB    1 
ATOM   3312 N  N     . GLU C 1 128 ? 42.240  36.698 1.749  1.00 18.06  ? 145 GLU C N     1 
ATOM   3313 C  CA    . GLU C 1 128 ? 43.048  37.906 1.680  1.00 18.92  ? 145 GLU C CA    1 
ATOM   3314 C  C     . GLU C 1 128 ? 42.532  38.962 2.643  1.00 18.16  ? 145 GLU C C     1 
ATOM   3315 O  O     . GLU C 1 128 ? 43.326  39.616 3.335  1.00 18.82  ? 145 GLU C O     1 
ATOM   3316 C  CB    . GLU C 1 128 ? 43.063  38.460 0.257  1.00 20.81  ? 145 GLU C CB    1 
ATOM   3317 C  CG    . GLU C 1 128 ? 43.975  39.694 0.151  1.00 24.12  ? 145 GLU C CG    1 
ATOM   3318 C  CD    . GLU C 1 128 ? 44.086  40.248 -1.247 1.00 28.56  ? 145 GLU C CD    1 
ATOM   3319 O  OE1   . GLU C 1 128 ? 44.627  39.541 -2.118 1.00 27.01  ? 145 GLU C OE1   1 
ATOM   3320 O  OE2   . GLU C 1 128 ? 43.642  41.395 -1.473 1.00 31.15  ? 145 GLU C OE2   1 
ATOM   3321 N  N     . SER C 1 129 ? 41.210  39.166 2.679  1.00 16.52  ? 146 SER C N     1 
ATOM   3322 C  CA    A SER C 1 129 ? 40.675  40.182 3.574  0.60 16.22  ? 146 SER C CA    1 
ATOM   3323 C  CA    B SER C 1 129 ? 40.635  40.164 3.573  0.40 16.25  ? 146 SER C CA    1 
ATOM   3324 C  C     . SER C 1 129 ? 40.862  39.784 5.030  1.00 18.22  ? 146 SER C C     1 
ATOM   3325 O  O     . SER C 1 129 ? 41.086  40.652 5.884  1.00 19.81  ? 146 SER C O     1 
ATOM   3326 C  CB    A SER C 1 129 ? 39.205  40.452 3.273  0.60 20.28  ? 146 SER C CB    1 
ATOM   3327 C  CB    B SER C 1 129 ? 39.142  40.330 3.288  0.40 20.22  ? 146 SER C CB    1 
ATOM   3328 O  OG    A SER C 1 129 ? 38.445  39.267 3.274  0.60 18.52  ? 146 SER C OG    1 
ATOM   3329 O  OG    B SER C 1 129 ? 38.921  40.986 2.046  0.40 23.17  ? 146 SER C OG    1 
ATOM   3330 N  N     . ALA C 1 130 ? 40.788  38.487 5.343  1.00 16.10  ? 147 ALA C N     1 
ATOM   3331 C  CA    . ALA C 1 130 ? 40.996  38.095 6.736  1.00 16.93  ? 147 ALA C CA    1 
ATOM   3332 C  C     . ALA C 1 130 ? 42.418  38.411 7.182  1.00 20.12  ? 147 ALA C C     1 
ATOM   3333 O  O     . ALA C 1 130 ? 42.631  38.976 8.261  1.00 20.17  ? 147 ALA C O     1 
ATOM   3334 C  CB    . ALA C 1 130 ? 40.700  36.611 6.924  1.00 17.78  ? 147 ALA C CB    1 
ATOM   3335 N  N     . LYS C 1 131 ? 43.401  38.088 6.353  1.00 19.96  ? 148 LYS C N     1 
ATOM   3336 C  CA    . LYS C 1 131 ? 44.776  38.387 6.723  1.00 19.74  ? 148 LYS C CA    1 
ATOM   3337 C  C     . LYS C 1 131 ? 44.964  39.891 6.913  1.00 16.92  ? 148 LYS C C     1 
ATOM   3338 O  O     . LYS C 1 131 ? 45.572  40.323 7.896  1.00 19.53  ? 148 LYS C O     1 
ATOM   3339 C  CB    . LYS C 1 131 ? 45.724  37.817 5.662  1.00 19.58  ? 148 LYS C CB    1 
ATOM   3340 C  CG    . LYS C 1 131 ? 47.192  37.822 6.034  1.00 37.60  ? 148 LYS C CG    1 
ATOM   3341 C  CD    . LYS C 1 131 ? 48.012  37.132 4.939  1.00 50.92  ? 148 LYS C CD    1 
ATOM   3342 C  CE    . LYS C 1 131 ? 49.481  36.994 5.322  1.00 60.03  ? 148 LYS C CE    1 
ATOM   3343 N  NZ    . LYS C 1 131 ? 50.097  38.313 5.614  1.00 47.09  ? 148 LYS C NZ    1 
ATOM   3344 N  N     . ARG C 1 132 ? 44.406  40.705 6.001  1.00 18.56  ? 149 ARG C N     1 
ATOM   3345 C  CA    . ARG C 1 132 ? 44.574  42.155 6.075  1.00 20.48  ? 149 ARG C CA    1 
ATOM   3346 C  C     . ARG C 1 132 ? 43.908  42.718 7.318  1.00 21.73  ? 149 ARG C C     1 
ATOM   3347 O  O     . ARG C 1 132 ? 44.484  43.560 8.021  1.00 20.24  ? 149 ARG C O     1 
ATOM   3348 C  CB    . ARG C 1 132 ? 43.982  42.819 4.821  1.00 21.59  ? 149 ARG C CB    1 
ATOM   3349 C  CG    . ARG C 1 132 ? 44.246  44.304 4.752  1.00 23.31  ? 149 ARG C CG    1 
ATOM   3350 C  CD    . ARG C 1 132 ? 43.628  44.951 3.522  1.00 25.37  ? 149 ARG C CD    1 
ATOM   3351 N  NE    . ARG C 1 132 ? 42.220  45.231 3.728  1.00 31.34  ? 149 ARG C NE    1 
ATOM   3352 C  CZ    . ARG C 1 132 ? 41.751  46.349 4.274  1.00 42.10  ? 149 ARG C CZ    1 
ATOM   3353 N  NH1   . ARG C 1 132 ? 42.553  47.346 4.618  1.00 41.66  ? 149 ARG C NH1   1 
ATOM   3354 N  NH2   . ARG C 1 132 ? 40.445  46.474 4.473  1.00 35.50  ? 149 ARG C NH2   1 
ATOM   3355 N  N     . GLU C 1 133 ? 42.697  42.254 7.603  1.00 19.23  ? 150 GLU C N     1 
ATOM   3356 C  CA    . GLU C 1 133 ? 41.917  42.813 8.696  1.00 17.08  ? 150 GLU C CA    1 
ATOM   3357 C  C     . GLU C 1 133 ? 42.487  42.411 10.050 1.00 17.01  ? 150 GLU C C     1 
ATOM   3358 O  O     . GLU C 1 133 ? 42.519  43.222 10.985 1.00 20.14  ? 150 GLU C O     1 
ATOM   3359 C  CB    . GLU C 1 133 ? 40.457  42.360 8.560  1.00 17.84  ? 150 GLU C CB    1 
ATOM   3360 C  CG    . GLU C 1 133 ? 39.739  43.046 7.406  1.00 17.88  ? 150 GLU C CG    1 
ATOM   3361 C  CD    . GLU C 1 133 ? 38.352  42.478 7.096  1.00 20.84  ? 150 GLU C CD    1 
ATOM   3362 O  OE1   . GLU C 1 133 ? 37.861  41.596 7.837  1.00 21.01  ? 150 GLU C OE1   1 
ATOM   3363 O  OE2   . GLU C 1 133 ? 37.764  42.926 6.089  1.00 23.11  ? 150 GLU C OE2   1 
ATOM   3364 N  N     . ILE C 1 134 ? 42.891  41.148 10.203 1.00 18.62  ? 151 ILE C N     1 
ATOM   3365 C  CA    . ILE C 1 134 ? 43.520  40.737 11.459 1.00 16.56  ? 151 ILE C CA    1 
ATOM   3366 C  C     . ILE C 1 134 ? 44.747  41.614 11.739 1.00 21.23  ? 151 ILE C C     1 
ATOM   3367 O  O     . ILE C 1 134 ? 44.936  42.106 12.857 1.00 22.38  ? 151 ILE C O     1 
ATOM   3368 C  CB    . ILE C 1 134 ? 43.888  39.241 11.421 1.00 18.37  ? 151 ILE C CB    1 
ATOM   3369 C  CG1   . ILE C 1 134 ? 42.641  38.370 11.413 1.00 19.34  ? 151 ILE C CG1   1 
ATOM   3370 C  CG2   . ILE C 1 134 ? 44.748  38.842 12.629 1.00 19.67  ? 151 ILE C CG2   1 
ATOM   3371 C  CD1   . ILE C 1 134 ? 42.915  36.934 11.111 1.00 19.95  ? 151 ILE C CD1   1 
ATOM   3372 N  N     . SER C 1 135 ? 45.585  41.825 10.728 1.00 19.95  ? 152 SER C N     1 
ATOM   3373 C  CA    . SER C 1 135 ? 46.786  42.651 10.892 1.00 22.70  ? 152 SER C CA    1 
ATOM   3374 C  C     . SER C 1 135 ? 46.454  44.107 11.184 1.00 20.63  ? 152 SER C C     1 
ATOM   3375 O  O     . SER C 1 135 ? 47.227  44.793 11.873 1.00 26.91  ? 152 SER C O     1 
ATOM   3376 C  CB    . SER C 1 135 ? 47.655  42.577 9.633  1.00 26.90  ? 152 SER C CB    1 
ATOM   3377 O  OG    . SER C 1 135 ? 48.198  41.285 9.494  1.00 33.04  ? 152 SER C OG    1 
ATOM   3378 N  N     . LEU C 1 136 ? 45.357  44.613 10.623 1.00 22.43  ? 153 LEU C N     1 
ATOM   3379 C  CA    . LEU C 1 136 ? 44.955  45.994 10.859 1.00 21.93  ? 153 LEU C CA    1 
ATOM   3380 C  C     . LEU C 1 136 ? 44.567  46.235 12.308 1.00 23.11  ? 153 LEU C C     1 
ATOM   3381 O  O     . LEU C 1 136 ? 44.927  47.265 12.883 1.00 24.40  ? 153 LEU C O     1 
ATOM   3382 C  CB    . LEU C 1 136 ? 43.769  46.352 9.965  1.00 21.55  ? 153 LEU C CB    1 
ATOM   3383 C  CG    . LEU C 1 136 ? 43.268  47.787 10.110 1.00 23.59  ? 153 LEU C CG    1 
ATOM   3384 C  CD1   . LEU C 1 136 ? 44.369  48.767 9.718  1.00 29.88  ? 153 LEU C CD1   1 
ATOM   3385 C  CD2   . LEU C 1 136 ? 42.030  48.007 9.233  1.00 24.66  ? 153 LEU C CD2   1 
ATOM   3386 N  N     . TRP C 1 137 ? 43.773  45.332 12.894 1.00 20.14  ? 154 TRP C N     1 
ATOM   3387 C  CA    . TRP C 1 137 ? 43.191  45.543 14.213 1.00 19.06  ? 154 TRP C CA    1 
ATOM   3388 C  C     . TRP C 1 137 ? 43.978  44.914 15.355 1.00 23.09  ? 154 TRP C C     1 
ATOM   3389 O  O     . TRP C 1 137 ? 43.730  45.264 16.520 1.00 23.88  ? 154 TRP C O     1 
ATOM   3390 C  CB    . TRP C 1 137 ? 41.767  44.979 14.243 1.00 18.77  ? 154 TRP C CB    1 
ATOM   3391 C  CG    . TRP C 1 137 ? 40.805  45.717 13.367 1.00 20.27  ? 154 TRP C CG    1 
ATOM   3392 C  CD1   . TRP C 1 137 ? 40.490  45.417 12.087 1.00 20.92  ? 154 TRP C CD1   1 
ATOM   3393 C  CD2   . TRP C 1 137 ? 40.006  46.856 13.726 1.00 18.31  ? 154 TRP C CD2   1 
ATOM   3394 N  NE1   . TRP C 1 137 ? 39.552  46.300 11.605 1.00 19.91  ? 154 TRP C NE1   1 
ATOM   3395 C  CE2   . TRP C 1 137 ? 39.237  47.193 12.595 1.00 18.60  ? 154 TRP C CE2   1 
ATOM   3396 C  CE3   . TRP C 1 137 ? 39.872  47.621 14.889 1.00 22.83  ? 154 TRP C CE3   1 
ATOM   3397 C  CZ2   . TRP C 1 137 ? 38.345  48.255 12.589 1.00 21.26  ? 154 TRP C CZ2   1 
ATOM   3398 C  CZ3   . TRP C 1 137 ? 38.983  48.668 14.891 1.00 22.35  ? 154 TRP C CZ3   1 
ATOM   3399 C  CH2   . TRP C 1 137 ? 38.235  48.986 13.744 1.00 21.06  ? 154 TRP C CH2   1 
ATOM   3400 N  N     . PHE C 1 138 ? 44.881  43.982 15.060 1.00 20.54  ? 155 PHE C N     1 
ATOM   3401 C  CA    . PHE C 1 138 ? 45.658  43.284 16.074 1.00 19.29  ? 155 PHE C CA    1 
ATOM   3402 C  C     . PHE C 1 138 ? 47.148  43.301 15.756 1.00 22.40  ? 155 PHE C C     1 
ATOM   3403 O  O     . PHE C 1 138 ? 47.553  43.086 14.611 1.00 23.63  ? 155 PHE C O     1 
ATOM   3404 C  CB    . PHE C 1 138 ? 45.215  41.826 16.211 1.00 18.90  ? 155 PHE C CB    1 
ATOM   3405 C  CG    . PHE C 1 138 ? 43.870  41.652 16.869 1.00 18.54  ? 155 PHE C CG    1 
ATOM   3406 C  CD1   . PHE C 1 138 ? 43.734  41.745 18.247 1.00 20.86  ? 155 PHE C CD1   1 
ATOM   3407 C  CD2   . PHE C 1 138 ? 42.750  41.356 16.113 1.00 21.57  ? 155 PHE C CD2   1 
ATOM   3408 C  CE1   . PHE C 1 138 ? 42.498  41.584 18.851 1.00 21.81  ? 155 PHE C CE1   1 
ATOM   3409 C  CE2   . PHE C 1 138 ? 41.521  41.186 16.708 1.00 19.25  ? 155 PHE C CE2   1 
ATOM   3410 C  CZ    . PHE C 1 138 ? 41.390  41.282 18.077 1.00 22.79  ? 155 PHE C CZ    1 
ATOM   3411 N  N     . LYS C 1 139 ? 47.973  43.515 16.798 1.00 23.65  ? 156 LYS C N     1 
ATOM   3412 C  CA    . LYS C 1 139 ? 49.397  43.227 16.688 1.00 26.53  ? 156 LYS C CA    1 
ATOM   3413 C  C     . LYS C 1 139 ? 49.637  41.724 16.802 1.00 21.52  ? 156 LYS C C     1 
ATOM   3414 O  O     . LYS C 1 139 ? 48.846  41.016 17.419 1.00 22.90  ? 156 LYS C O     1 
ATOM   3415 C  CB    . LYS C 1 139 ? 50.177  43.925 17.794 1.00 30.64  ? 156 LYS C CB    1 
ATOM   3416 C  CG    . LYS C 1 139 ? 49.843  45.389 18.000 1.00 42.83  ? 156 LYS C CG    1 
ATOM   3417 C  CD    . LYS C 1 139 ? 50.443  45.878 19.320 1.00 54.24  ? 156 LYS C CD    1 
ATOM   3418 C  CE    . LYS C 1 139 ? 49.769  47.143 19.825 1.00 73.24  ? 156 LYS C CE    1 
ATOM   3419 N  NZ    . LYS C 1 139 ? 49.969  48.284 18.892 1.00 85.53  ? 156 LYS C NZ    1 
ATOM   3420 N  N     . PRO C 1 140 ? 50.728  41.206 16.235 1.00 24.05  ? 157 PRO C N     1 
ATOM   3421 C  CA    . PRO C 1 140 ? 50.953  39.748 16.319 1.00 23.81  ? 157 PRO C CA    1 
ATOM   3422 C  C     . PRO C 1 140 ? 51.001  39.225 17.742 1.00 23.31  ? 157 PRO C C     1 
ATOM   3423 O  O     . PRO C 1 140 ? 50.592  38.081 17.983 1.00 25.38  ? 157 PRO C O     1 
ATOM   3424 C  CB    . PRO C 1 140 ? 52.299  39.557 15.597 1.00 27.83  ? 157 PRO C CB    1 
ATOM   3425 C  CG    . PRO C 1 140 ? 52.386  40.723 14.679 1.00 30.75  ? 157 PRO C CG    1 
ATOM   3426 C  CD    . PRO C 1 140 ? 51.715  41.866 15.351 1.00 27.18  ? 157 PRO C CD    1 
ATOM   3427 N  N     . GLU C 1 141 ? 51.475  40.043 18.691 1.00 23.73  ? 158 GLU C N     1 
ATOM   3428 C  CA    . GLU C 1 141 ? 51.579  39.654 20.092 1.00 27.48  ? 158 GLU C CA    1 
ATOM   3429 C  C     . GLU C 1 141 ? 50.214  39.417 20.730 1.00 23.11  ? 158 GLU C C     1 
ATOM   3430 O  O     . GLU C 1 141 ? 50.130  38.799 21.801 1.00 26.58  ? 158 GLU C O     1 
ATOM   3431 C  CB    . GLU C 1 141 ? 52.325  40.747 20.865 1.00 29.56  ? 158 GLU C CB    1 
ATOM   3432 C  CG    . GLU C 1 141 ? 51.472  42.002 21.083 1.00 40.68  ? 158 GLU C CG    1 
ATOM   3433 C  CD    . GLU C 1 141 ? 52.280  43.280 21.274 1.00 61.73  ? 158 GLU C CD    1 
ATOM   3434 O  OE1   . GLU C 1 141 ? 53.204  43.534 20.472 1.00 60.04  ? 158 GLU C OE1   1 
ATOM   3435 O  OE2   . GLU C 1 141 ? 51.974  44.039 22.220 1.00 79.38  ? 158 GLU C OE2   1 
ATOM   3436 N  N     . GLU C 1 142 ? 49.144  39.904 20.109 1.00 22.47  ? 159 GLU C N     1 
ATOM   3437 C  CA    . GLU C 1 142 ? 47.801  39.786 20.661 1.00 21.97  ? 159 GLU C CA    1 
ATOM   3438 C  C     . GLU C 1 142 ? 47.079  38.526 20.194 1.00 21.66  ? 159 GLU C C     1 
ATOM   3439 O  O     . GLU C 1 142 ? 45.989  38.218 20.710 1.00 22.83  ? 159 GLU C O     1 
ATOM   3440 C  CB    . GLU C 1 142 ? 47.011  41.034 20.278 1.00 22.77  ? 159 GLU C CB    1 
ATOM   3441 C  CG    . GLU C 1 142 ? 47.592  42.290 20.927 1.00 28.80  ? 159 GLU C CG    1 
ATOM   3442 C  CD    . GLU C 1 142 ? 46.878  43.569 20.540 1.00 34.56  ? 159 GLU C CD    1 
ATOM   3443 O  OE1   . GLU C 1 142 ? 46.752  43.858 19.340 1.00 32.66  ? 159 GLU C OE1   1 
ATOM   3444 O  OE2   . GLU C 1 142 ? 46.464  44.313 21.446 1.00 51.20  ? 159 GLU C OE2   1 
ATOM   3445 N  N     . ILE C 1 143 ? 47.667  37.794 19.256 1.00 21.88  ? 160 ILE C N     1 
ATOM   3446 C  CA    . ILE C 1 143 ? 47.088  36.567 18.728 1.00 20.91  ? 160 ILE C CA    1 
ATOM   3447 C  C     . ILE C 1 143 ? 47.619  35.409 19.560 1.00 23.80  ? 160 ILE C C     1 
ATOM   3448 O  O     . ILE C 1 143 ? 48.833  35.205 19.672 1.00 22.98  ? 160 ILE C O     1 
ATOM   3449 C  CB    . ILE C 1 143 ? 47.412  36.382 17.239 1.00 21.19  ? 160 ILE C CB    1 
ATOM   3450 C  CG1   . ILE C 1 143 ? 47.113  37.655 16.444 1.00 23.69  ? 160 ILE C CG1   1 
ATOM   3451 C  CG2   . ILE C 1 143 ? 46.663  35.212 16.699 1.00 24.06  ? 160 ILE C CG2   1 
ATOM   3452 C  CD1   . ILE C 1 143 ? 45.692  38.080 16.392 1.00 26.28  ? 160 ILE C CD1   1 
ATOM   3453 N  N     . GLN C 1 144 ? 46.708  34.662 20.158 1.00 19.77  ? 161 GLN C N     1 
ATOM   3454 C  CA    . GLN C 1 144 ? 47.041  33.660 21.154 1.00 22.08  ? 161 GLN C CA    1 
ATOM   3455 C  C     . GLN C 1 144 ? 46.907  32.264 20.570 1.00 22.78  ? 161 GLN C C     1 
ATOM   3456 O  O     . GLN C 1 144 ? 45.868  31.912 19.995 1.00 26.11  ? 161 GLN C O     1 
ATOM   3457 C  CB    . GLN C 1 144 ? 46.136  33.801 22.376 1.00 21.08  ? 161 GLN C CB    1 
ATOM   3458 C  CG    . GLN C 1 144 ? 46.000  35.216 22.878 1.00 19.23  ? 161 GLN C CG    1 
ATOM   3459 C  CD    . GLN C 1 144 ? 47.313  35.757 23.395 1.00 22.39  ? 161 GLN C CD    1 
ATOM   3460 O  OE1   . GLN C 1 144 ? 48.115  35.023 23.962 1.00 24.92  ? 161 GLN C OE1   1 
ATOM   3461 N  NE2   . GLN C 1 144 ? 47.536  37.042 23.197 1.00 23.79  ? 161 GLN C NE2   1 
ATOM   3462 N  N     . SER C 1 145 ? 47.958  31.470 20.736 1.00 19.18  ? 162 SER C N     1 
ATOM   3463 C  CA    A SER C 1 145 ? 47.992  30.103 20.245 0.58 20.81  ? 162 SER C CA    1 
ATOM   3464 C  CA    B SER C 1 145 ? 47.993  30.100 20.248 0.42 20.86  ? 162 SER C CA    1 
ATOM   3465 C  C     . SER C 1 145 ? 47.825  29.140 21.415 1.00 22.06  ? 162 SER C C     1 
ATOM   3466 O  O     . SER C 1 145 ? 48.654  29.118 22.334 1.00 24.15  ? 162 SER C O     1 
ATOM   3467 C  CB    A SER C 1 145 ? 49.302  29.829 19.501 0.58 24.06  ? 162 SER C CB    1 
ATOM   3468 C  CB    B SER C 1 145 ? 49.305  29.803 19.520 0.42 24.06  ? 162 SER C CB    1 
ATOM   3469 O  OG    A SER C 1 145 ? 49.450  28.448 19.240 0.58 24.56  ? 162 SER C OG    1 
ATOM   3470 O  OG    B SER C 1 145 ? 49.395  30.560 18.338 0.42 20.69  ? 162 SER C OG    1 
ATOM   3471 N  N     . TYR C 1 146 ? 46.765  28.342 21.364 1.00 20.97  ? 163 TYR C N     1 
ATOM   3472 C  CA    . TYR C 1 146 ? 46.531  27.269 22.308 1.00 20.18  ? 163 TYR C CA    1 
ATOM   3473 C  C     . TYR C 1 146 ? 45.619  26.269 21.620 1.00 19.97  ? 163 TYR C C     1 
ATOM   3474 O  O     . TYR C 1 146 ? 45.016  26.560 20.576 1.00 20.72  ? 163 TYR C O     1 
ATOM   3475 C  CB    . TYR C 1 146 ? 45.939  27.795 23.629 1.00 20.54  ? 163 TYR C CB    1 
ATOM   3476 C  CG    . TYR C 1 146 ? 44.594  28.475 23.472 1.00 17.30  ? 163 TYR C CG    1 
ATOM   3477 C  CD1   . TYR C 1 146 ? 44.499  29.832 23.198 1.00 15.76  ? 163 TYR C CD1   1 
ATOM   3478 C  CD2   . TYR C 1 146 ? 43.430  27.749 23.615 1.00 17.96  ? 163 TYR C CD2   1 
ATOM   3479 C  CE1   . TYR C 1 146 ? 43.248  30.452 23.037 1.00 18.06  ? 163 TYR C CE1   1 
ATOM   3480 C  CE2   . TYR C 1 146 ? 42.175  28.354 23.457 1.00 17.60  ? 163 TYR C CE2   1 
ATOM   3481 C  CZ    . TYR C 1 146 ? 42.093  29.700 23.182 1.00 17.81  ? 163 TYR C CZ    1 
ATOM   3482 O  OH    . TYR C 1 146 ? 40.847  30.285 23.026 1.00 16.63  ? 163 TYR C OH    1 
ATOM   3483 N  N     . LYS C 1 147 ? 45.569  25.071 22.178 1.00 21.11  ? 164 LYS C N     1 
ATOM   3484 C  CA    . LYS C 1 147 ? 44.796  23.979 21.606 1.00 20.38  ? 164 LYS C CA    1 
ATOM   3485 C  C     . LYS C 1 147 ? 43.562  23.724 22.462 1.00 18.97  ? 164 LYS C C     1 
ATOM   3486 O  O     . LYS C 1 147 ? 43.664  23.635 23.687 1.00 19.37  ? 164 LYS C O     1 
ATOM   3487 C  CB    . LYS C 1 147 ? 45.632  22.709 21.513 1.00 23.52  ? 164 LYS C CB    1 
ATOM   3488 C  CG    . LYS C 1 147 ? 44.837  21.499 21.091 1.00 28.62  ? 164 LYS C CG    1 
ATOM   3489 C  CD    . LYS C 1 147 ? 45.726  20.274 20.949 1.00 40.92  ? 164 LYS C CD    1 
ATOM   3490 C  CE    . LYS C 1 147 ? 44.889  19.006 20.834 1.00 55.33  ? 164 LYS C CE    1 
ATOM   3491 N  NZ    . LYS C 1 147 ? 45.654  17.855 20.280 1.00 63.33  ? 164 LYS C NZ    1 
ATOM   3492 N  N     . LEU C 1 148 ? 42.406  23.589 21.805 1.00 21.10  ? 165 LEU C N     1 
ATOM   3493 C  CA    . LEU C 1 148 ? 41.185  23.239 22.518 1.00 17.60  ? 165 LEU C CA    1 
ATOM   3494 C  C     . LEU C 1 148 ? 41.254  21.800 23.024 1.00 17.87  ? 165 LEU C C     1 
ATOM   3495 O  O     . LEU C 1 148 ? 41.570  20.870 22.277 1.00 18.62  ? 165 LEU C O     1 
ATOM   3496 C  CB    . LEU C 1 148 ? 39.968  23.424 21.611 1.00 18.94  ? 165 LEU C CB    1 
ATOM   3497 C  CG    . LEU C 1 148 ? 39.542  24.862 21.306 1.00 17.85  ? 165 LEU C CG    1 
ATOM   3498 C  CD1   . LEU C 1 148 ? 38.405  24.882 20.252 1.00 22.02  ? 165 LEU C CD1   1 
ATOM   3499 C  CD2   . LEU C 1 148 ? 39.154  25.626 22.568 1.00 19.31  ? 165 LEU C CD2   1 
ATOM   3500 N  N     . ALA C 1 149 ? 40.905  21.617 24.292 1.00 21.08  ? 166 ALA C N     1 
ATOM   3501 C  CA    . ALA C 1 149 ? 40.956  20.292 24.889 1.00 20.85  ? 166 ALA C CA    1 
ATOM   3502 C  C     . ALA C 1 149 ? 39.984  19.319 24.239 1.00 20.12  ? 166 ALA C C     1 
ATOM   3503 O  O     . ALA C 1 149 ? 40.232  18.108 24.271 1.00 24.29  ? 166 ALA C O     1 
ATOM   3504 C  CB    . ALA C 1 149 ? 40.666  20.403 26.393 1.00 27.42  ? 166 ALA C CB    1 
ATOM   3505 N  N     . LEU C 1 150 ? 38.910  19.811 23.618 1.00 18.98  ? 167 LEU C N     1 
ATOM   3506 C  CA    . LEU C 1 150 ? 37.951  18.972 22.906 1.00 17.10  ? 167 LEU C CA    1 
ATOM   3507 C  C     . LEU C 1 150 ? 38.310  18.742 21.423 1.00 16.59  ? 167 LEU C C     1 
ATOM   3508 O  O     . LEU C 1 150 ? 37.469  18.218 20.683 1.00 19.12  ? 167 LEU C O     1 
ATOM   3509 C  CB    . LEU C 1 150 ? 36.546  19.586 23.030 1.00 19.04  ? 167 LEU C CB    1 
ATOM   3510 C  CG    . LEU C 1 150 ? 35.856  19.353 24.382 1.00 19.03  ? 167 LEU C CG    1 
ATOM   3511 C  CD1   . LEU C 1 150 ? 34.634  20.247 24.552 1.00 25.92  ? 167 LEU C CD1   1 
ATOM   3512 C  CD2   . LEU C 1 150 ? 35.452  17.891 24.467 1.00 24.82  ? 167 LEU C CD2   1 
ATOM   3513 N  N     . SER C 1 151 ? 39.542  19.089 20.997 1.00 18.12  ? 168 SER C N     1 
ATOM   3514 C  CA    A SER C 1 151 ? 39.931  18.990 19.585 0.45 19.36  ? 168 SER C CA    1 
ATOM   3515 C  CA    B SER C 1 151 ? 39.918  18.991 19.584 0.55 19.35  ? 168 SER C CA    1 
ATOM   3516 C  C     . SER C 1 151 ? 39.637  17.613 18.998 1.00 19.43  ? 168 SER C C     1 
ATOM   3517 O  O     . SER C 1 151 ? 39.203  17.501 17.839 1.00 21.57  ? 168 SER C O     1 
ATOM   3518 C  CB    A SER C 1 151 ? 41.423  19.319 19.440 0.45 22.30  ? 168 SER C CB    1 
ATOM   3519 C  CB    B SER C 1 151 ? 41.397  19.339 19.429 0.55 22.29  ? 168 SER C CB    1 
ATOM   3520 O  OG    A SER C 1 151 ? 41.903  19.041 18.130 0.45 29.67  ? 168 SER C OG    1 
ATOM   3521 O  OG    B SER C 1 151 ? 41.579  20.731 19.559 0.55 21.12  ? 168 SER C OG    1 
ATOM   3522 N  N     . ASP C 1 152 ? 39.882  16.542 19.763 1.00 21.07  ? 169 ASP C N     1 
ATOM   3523 C  CA    . ASP C 1 152 ? 39.651  15.212 19.206 1.00 23.86  ? 169 ASP C CA    1 
ATOM   3524 C  C     . ASP C 1 152 ? 38.191  14.972 18.859 1.00 24.53  ? 169 ASP C C     1 
ATOM   3525 O  O     . ASP C 1 152 ? 37.898  14.081 18.057 1.00 24.30  ? 169 ASP C O     1 
ATOM   3526 C  CB    . ASP C 1 152 ? 40.096  14.108 20.172 1.00 27.95  ? 169 ASP C CB    1 
ATOM   3527 C  CG    . ASP C 1 152 ? 41.607  14.013 20.327 1.00 40.79  ? 169 ASP C CG    1 
ATOM   3528 O  OD1   . ASP C 1 152 ? 42.363  14.523 19.468 1.00 37.81  ? 169 ASP C OD1   1 
ATOM   3529 O  OD2   . ASP C 1 152 ? 42.031  13.405 21.328 1.00 39.05  ? 169 ASP C OD2   1 
ATOM   3530 N  N     . TYR C 1 153 ? 37.268  15.740 19.441 1.00 17.39  ? 170 TYR C N     1 
ATOM   3531 C  CA    . TYR C 1 153 ? 35.848  15.558 19.229 1.00 14.95  ? 170 TYR C CA    1 
ATOM   3532 C  C     . TYR C 1 153 ? 35.271  16.627 18.328 1.00 15.86  ? 170 TYR C C     1 
ATOM   3533 O  O     . TYR C 1 153 ? 34.080  16.588 18.024 1.00 20.91  ? 170 TYR C O     1 
ATOM   3534 C  CB    . TYR C 1 153 ? 35.114  15.527 20.581 1.00 18.05  ? 170 TYR C CB    1 
ATOM   3535 C  CG    . TYR C 1 153 ? 35.552  14.297 21.333 1.00 18.75  ? 170 TYR C CG    1 
ATOM   3536 C  CD1   . TYR C 1 153 ? 35.029  13.061 21.004 1.00 19.72  ? 170 TYR C CD1   1 
ATOM   3537 C  CD2   . TYR C 1 153 ? 36.553  14.356 22.292 1.00 18.77  ? 170 TYR C CD2   1 
ATOM   3538 C  CE1   . TYR C 1 153 ? 35.466  11.905 21.642 1.00 19.20  ? 170 TYR C CE1   1 
ATOM   3539 C  CE2   . TYR C 1 153 ? 36.994  13.208 22.919 1.00 21.37  ? 170 TYR C CE2   1 
ATOM   3540 C  CZ    . TYR C 1 153 ? 36.431  11.997 22.592 1.00 22.59  ? 170 TYR C CZ    1 
ATOM   3541 O  OH    . TYR C 1 153 ? 36.848  10.851 23.219 1.00 26.51  ? 170 TYR C OH    1 
ATOM   3542 N  N     . ILE C 1 154 ? 36.093  17.567 17.885 1.00 17.42  ? 171 ILE C N     1 
ATOM   3543 C  CA    . ILE C 1 154 ? 35.664  18.629 16.983 1.00 17.88  ? 171 ILE C CA    1 
ATOM   3544 C  C     . ILE C 1 154 ? 36.173  18.379 15.573 1.00 22.77  ? 171 ILE C C     1 
ATOM   3545 O  O     . ILE C 1 154 ? 35.443  18.567 14.595 1.00 22.41  ? 171 ILE C O     1 
ATOM   3546 C  CB    . ILE C 1 154 ? 36.152  20.001 17.504 1.00 19.30  ? 171 ILE C CB    1 
ATOM   3547 C  CG1   . ILE C 1 154 ? 35.496  20.365 18.847 1.00 17.97  ? 171 ILE C CG1   1 
ATOM   3548 C  CG2   . ILE C 1 154 ? 35.883  21.102 16.470 1.00 20.00  ? 171 ILE C CG2   1 
ATOM   3549 C  CD1   . ILE C 1 154 ? 36.233  21.485 19.623 1.00 22.24  ? 171 ILE C CD1   1 
ATOM   3550 N  N     . PHE C 1 155 ? 37.430  17.948 15.451 1.00 20.84  ? 172 PHE C N     1 
ATOM   3551 C  CA    . PHE C 1 155 ? 38.075  17.766 14.164 1.00 22.48  ? 172 PHE C CA    1 
ATOM   3552 C  C     . PHE C 1 155 ? 38.163  16.288 13.821 1.00 28.73  ? 172 PHE C C     1 
ATOM   3553 O  O     . PHE C 1 155 ? 38.354  15.445 14.701 1.00 26.47  ? 172 PHE C O     1 
ATOM   3554 C  CB    . PHE C 1 155 ? 39.468  18.396 14.191 1.00 21.89  ? 172 PHE C CB    1 
ATOM   3555 C  CG    . PHE C 1 155 ? 39.459  19.833 14.623 1.00 25.98  ? 172 PHE C CG    1 
ATOM   3556 C  CD1   . PHE C 1 155 ? 38.915  20.797 13.807 1.00 22.16  ? 172 PHE C CD1   1 
ATOM   3557 C  CD2   . PHE C 1 155 ? 39.979  20.217 15.850 1.00 23.31  ? 172 PHE C CD2   1 
ATOM   3558 C  CE1   . PHE C 1 155 ? 38.880  22.108 14.194 1.00 22.91  ? 172 PHE C CE1   1 
ATOM   3559 C  CE2   . PHE C 1 155 ? 39.955  21.534 16.234 1.00 27.86  ? 172 PHE C CE2   1 
ATOM   3560 C  CZ    . PHE C 1 155 ? 39.412  22.480 15.407 1.00 24.14  ? 172 PHE C CZ    1 
ATOM   3561 N  N     . GLU C 1 156 ? 37.993  15.975 12.540 1.00 27.90  ? 173 GLU C N     1 
ATOM   3562 C  CA    . GLU C 1 156 ? 38.038  14.587 12.112 1.00 39.34  ? 173 GLU C CA    1 
ATOM   3563 C  C     . GLU C 1 156 ? 39.528  14.229 12.055 1.00 50.59  ? 173 GLU C C     1 
ATOM   3564 O  O     . GLU C 1 156 ? 39.930  13.079 12.254 1.00 54.69  ? 173 GLU C O     1 
ATOM   3565 C  CB    . GLU C 1 156 ? 37.305  14.365 10.766 1.00 40.19  ? 173 GLU C CB    1 
ATOM   3566 C  CG    . GLU C 1 156 ? 37.859  15.122 9.578  1.00 37.45  ? 173 GLU C CG    1 
ATOM   3567 C  CD    . GLU C 1 156 ? 36.934  15.104 8.346  1.00 45.72  ? 173 GLU C CD    1 
ATOM   3568 O  OE1   . GLU C 1 156 ? 35.731  14.762 8.458  1.00 25.40  ? 173 GLU C OE1   1 
ATOM   3569 O  OE2   . GLU C 1 156 ? 37.420  15.443 7.246  1.00 51.36  ? 173 GLU C OE2   1 
ATOM   3570 O  OXT   . GLU C 1 156 ? 40.378  15.106 11.871 1.00 45.41  ? 173 GLU C OXT   1 
HETATM 3571 N  N1    A CTP D 2 .   ? -4.734  24.900 7.428  0.52 33.03  ? 201 CTP A N1    1 
HETATM 3572 C  C2    A CTP D 2 .   ? -4.946  23.541 7.562  0.52 35.20  ? 201 CTP A C2    1 
HETATM 3573 N  N3    A CTP D 2 .   ? -5.154  22.755 6.444  0.52 38.91  ? 201 CTP A N3    1 
HETATM 3574 C  C4    A CTP D 2 .   ? -5.192  23.338 5.192  0.52 43.40  ? 201 CTP A C4    1 
HETATM 3575 C  C5    A CTP D 2 .   ? -5.097  24.723 5.072  0.52 36.83  ? 201 CTP A C5    1 
HETATM 3576 C  C6    A CTP D 2 .   ? -4.759  25.480 6.190  0.52 37.42  ? 201 CTP A C6    1 
HETATM 3577 O  O2    A CTP D 2 .   ? -4.948  23.033 8.682  0.52 31.83  ? 201 CTP A O2    1 
HETATM 3578 N  N4    A CTP D 2 .   ? -5.309  22.574 4.108  0.52 44.79  ? 201 CTP A N4    1 
HETATM 3579 C  "C1'" A CTP D 2 .   ? -4.813  25.749 8.629  0.52 31.53  ? 201 CTP A "C1'" 1 
HETATM 3580 C  "C2'" A CTP D 2 .   ? -3.411  26.132 9.082  0.52 24.07  ? 201 CTP A "C2'" 1 
HETATM 3581 O  "O2'" A CTP D 2 .   ? -3.396  26.116 10.489 0.52 27.15  ? 201 CTP A "O2'" 1 
HETATM 3582 C  "C3'" A CTP D 2 .   ? -3.230  27.539 8.560  0.52 27.45  ? 201 CTP A "C3'" 1 
HETATM 3583 C  "C4'" A CTP D 2 .   ? -4.660  28.067 8.637  0.52 26.83  ? 201 CTP A "C4'" 1 
HETATM 3584 O  "O4'" A CTP D 2 .   ? -5.492  26.954 8.338  0.52 28.85  ? 201 CTP A "O4'" 1 
HETATM 3585 O  "O3'" A CTP D 2 .   ? -2.296  28.289 9.304  0.52 24.35  ? 201 CTP A "O3'" 1 
HETATM 3586 C  "C5'" A CTP D 2 .   ? -4.940  29.187 7.658  0.52 25.98  ? 201 CTP A "C5'" 1 
HETATM 3587 O  "O5'" A CTP D 2 .   ? -4.648  28.737 6.364  0.52 24.90  ? 201 CTP A "O5'" 1 
HETATM 3588 P  PA    A CTP D 2 .   ? -3.658  29.618 5.466  0.52 24.98  ? 201 CTP A PA    1 
HETATM 3589 O  O1A   A CTP D 2 .   ? -4.074  31.062 5.556  0.52 22.54  ? 201 CTP A O1A   1 
HETATM 3590 O  O2A   A CTP D 2 .   ? -3.634  29.097 4.042  0.52 24.12  ? 201 CTP A O2A   1 
HETATM 3591 O  O3A   A CTP D 2 .   ? -2.172  29.396 6.055  0.52 24.74  ? 201 CTP A O3A   1 
HETATM 3592 P  PB    A CTP D 2 .   ? -1.320  30.430 6.942  0.52 24.43  ? 201 CTP A PB    1 
HETATM 3593 O  O1B   A CTP D 2 .   ? -1.375  31.842 6.404  0.52 24.26  ? 201 CTP A O1B   1 
HETATM 3594 O  O2B   A CTP D 2 .   ? 0.092   29.878 7.004  0.52 22.16  ? 201 CTP A O2B   1 
HETATM 3595 O  O3B   A CTP D 2 .   ? -2.063  30.292 8.372  0.52 26.68  ? 201 CTP A O3B   1 
HETATM 3596 P  PG    A CTP D 2 .   ? -2.405  31.590 9.254  0.52 32.18  ? 201 CTP A PG    1 
HETATM 3597 O  O1G   A CTP D 2 .   ? -3.240  32.565 8.448  0.52 29.05  ? 201 CTP A O1G   1 
HETATM 3598 O  O2G   A CTP D 2 .   ? -3.210  31.166 10.446 0.52 17.84  ? 201 CTP A O2G   1 
HETATM 3599 O  O3G   A CTP D 2 .   ? -1.088  32.252 9.610  0.52 24.31  ? 201 CTP A O3G   1 
HETATM 3600 P  PB    B ADP E 3 .   ? -1.147  30.662 6.867  0.48 22.57  ? 202 ADP A PB    1 
HETATM 3601 O  O1B   B ADP E 3 .   ? -1.556  30.794 8.325  0.48 27.19  ? 202 ADP A O1B   1 
HETATM 3602 O  O2B   B ADP E 3 .   ? -1.322  31.909 6.028  0.48 23.87  ? 202 ADP A O2B   1 
HETATM 3603 O  O3B   B ADP E 3 .   ? 0.196   29.978 6.668  0.48 21.44  ? 202 ADP A O3B   1 
HETATM 3604 P  PA    B ADP E 3 .   ? -3.623  29.806 5.559  0.48 23.32  ? 202 ADP A PA    1 
HETATM 3605 O  O1A   B ADP E 3 .   ? -4.155  31.186 5.857  0.48 24.60  ? 202 ADP A O1A   1 
HETATM 3606 O  O2A   B ADP E 3 .   ? -3.540  29.310 4.124  0.48 24.50  ? 202 ADP A O2A   1 
HETATM 3607 O  O3A   B ADP E 3 .   ? -2.178  29.563 6.262  0.48 23.79  ? 202 ADP A O3A   1 
HETATM 3608 O  "O5'" B ADP E 3 .   ? -4.524  28.783 6.402  0.48 24.71  ? 202 ADP A "O5'" 1 
HETATM 3609 C  "C5'" B ADP E 3 .   ? -4.953  29.220 7.681  0.48 26.00  ? 202 ADP A "C5'" 1 
HETATM 3610 C  "C4'" B ADP E 3 .   ? -4.731  28.095 8.676  0.48 26.81  ? 202 ADP A "C4'" 1 
HETATM 3611 O  "O4'" B ADP E 3 .   ? -5.538  26.957 8.340  0.48 28.88  ? 202 ADP A "O4'" 1 
HETATM 3612 C  "C3'" B ADP E 3 .   ? -3.291  27.586 8.689  0.48 27.61  ? 202 ADP A "C3'" 1 
HETATM 3613 O  "O3'" B ADP E 3 .   ? -2.427  28.353 9.536  0.48 25.34  ? 202 ADP A "O3'" 1 
HETATM 3614 C  "C2'" B ADP E 3 .   ? -3.463  26.163 9.174  0.48 24.21  ? 202 ADP A "C2'" 1 
HETATM 3615 O  "O2'" B ADP E 3 .   ? -3.460  26.124 10.604 0.48 27.02  ? 202 ADP A "O2'" 1 
HETATM 3616 C  "C1'" B ADP E 3 .   ? -4.846  25.754 8.684  0.48 31.48  ? 202 ADP A "C1'" 1 
HETATM 3617 N  N9    B ADP E 3 .   ? -4.731  24.900 7.479  0.48 33.06  ? 202 ADP A N9    1 
HETATM 3618 C  C8    B ADP E 3 .   ? -4.650  25.369 6.219  0.48 37.38  ? 202 ADP A C8    1 
HETATM 3619 N  N7    B ADP E 3 .   ? -4.559  24.344 5.332  0.48 36.75  ? 202 ADP A N7    1 
HETATM 3620 C  C5    B ADP E 3 .   ? -4.583  23.192 6.034  0.48 38.44  ? 202 ADP A C5    1 
HETATM 3621 C  C6    B ADP E 3 .   ? -4.522  21.747 5.716  0.48 40.09  ? 202 ADP A C6    1 
HETATM 3622 N  N6    B ADP E 3 .   ? -4.419  21.327 4.430  0.48 40.29  ? 202 ADP A N6    1 
HETATM 3623 N  N1    B ADP E 3 .   ? -4.577  20.868 6.741  0.48 34.13  ? 202 ADP A N1    1 
HETATM 3624 C  C2    B ADP E 3 .   ? -4.684  21.268 8.021  0.48 29.69  ? 202 ADP A C2    1 
HETATM 3625 N  N3    B ADP E 3 .   ? -4.744  22.569 8.379  0.48 34.81  ? 202 ADP A N3    1 
HETATM 3626 C  C4    B ADP E 3 .   ? -4.699  23.562 7.453  0.48 35.45  ? 202 ADP A C4    1 
HETATM 3627 MG MG    . MG  F 4 .   ? -3.364  33.092 6.188  1.00 26.74  2 203 MG  A MG    1 
HETATM 3628 N  N1    A CTP G 2 .   ? 31.726  10.049 7.022  0.49 56.22  ? 201 CTP B N1    1 
HETATM 3629 C  C2    A CTP G 2 .   ? 33.018  10.545 7.008  0.49 55.64  ? 201 CTP B C2    1 
HETATM 3630 N  N3    A CTP G 2 .   ? 33.707  10.665 5.814  0.49 58.93  ? 201 CTP B N3    1 
HETATM 3631 C  C4    A CTP G 2 .   ? 33.150  10.180 4.646  0.49 57.04  ? 201 CTP B C4    1 
HETATM 3632 C  C5    A CTP G 2 .   ? 31.905  9.560  4.689  0.49 55.30  ? 201 CTP B C5    1 
HETATM 3633 C  C6    A CTP G 2 .   ? 31.141  9.650  5.850  0.49 56.81  ? 201 CTP B C6    1 
HETATM 3634 O  O2    A CTP G 2 .   ? 33.559  10.882 8.061  0.49 45.04  ? 201 CTP B O2    1 
HETATM 3635 N  N4    A CTP G 2 .   ? 33.801  10.321 3.493  0.49 55.14  ? 201 CTP B N4    1 
HETATM 3636 C  "C1'" A CTP G 2 .   ? 31.072  9.756  8.316  0.49 57.47  ? 201 CTP B "C1'" 1 
HETATM 3637 C  "C2'" A CTP G 2 .   ? 30.079  10.858 8.671  0.49 49.86  ? 201 CTP B "C2'" 1 
HETATM 3638 O  "O2'" A CTP G 2 .   ? 30.282  11.262 10.004 0.49 46.66  ? 201 CTP B "O2'" 1 
HETATM 3639 C  "C3'" A CTP G 2 .   ? 28.707  10.228 8.496  0.49 54.35  ? 201 CTP B "C3'" 1 
HETATM 3640 C  "C4'" A CTP G 2 .   ? 28.989  8.731  8.629  0.49 57.67  ? 201 CTP B "C4'" 1 
HETATM 3641 O  "O4'" A CTP G 2 .   ? 30.344  8.540  8.250  0.49 58.21  ? 201 CTP B "O4'" 1 
HETATM 3642 O  "O3'" A CTP G 2 .   ? 27.761  10.717 9.430  0.49 43.20  ? 201 CTP B "O3'" 1 
HETATM 3643 C  "C5'" A CTP G 2 .   ? 28.108  7.839  7.764  0.49 58.10  ? 201 CTP B "C5'" 1 
HETATM 3644 O  "O5'" A CTP G 2 .   ? 28.127  8.264  6.418  0.49 59.64  ? 201 CTP B "O5'" 1 
HETATM 3645 P  PA    A CTP G 2 .   ? 26.762  8.695  5.675  0.49 62.06  ? 201 CTP B PA    1 
HETATM 3646 O  O1A   A CTP G 2 .   ? 25.719  7.628  5.916  0.49 58.40  ? 201 CTP B O1A   1 
HETATM 3647 O  O2A   A CTP G 2 .   ? 27.005  8.898  4.196  0.49 57.73  ? 201 CTP B O2A   1 
HETATM 3648 O  O3A   A CTP G 2 .   ? 26.308  10.089 6.363  0.49 57.82  ? 201 CTP B O3A   1 
HETATM 3649 P  PB    A CTP G 2 .   ? 25.213  10.188 7.545  0.49 56.06  ? 201 CTP B PB    1 
HETATM 3650 O  O1B   A CTP G 2 .   ? 24.047  9.277  7.239  0.49 51.44  ? 201 CTP B O1B   1 
HETATM 3651 O  O2B   A CTP G 2 .   ? 24.749  11.619 7.702  0.49 46.82  ? 201 CTP B O2B   1 
HETATM 3652 O  O3B   A CTP G 2 .   ? 25.988  9.702  8.879  0.49 52.11  ? 201 CTP B O3B   1 
HETATM 3653 P  PG    A CTP G 2 .   ? 25.211  8.849  10.004 0.49 51.08  ? 201 CTP B PG    1 
HETATM 3654 O  O1G   A CTP G 2 .   ? 24.658  7.600  9.354  0.49 44.00  ? 201 CTP B O1G   1 
HETATM 3655 O  O2G   A CTP G 2 .   ? 26.117  8.430  11.130 0.49 33.26  ? 201 CTP B O2G   1 
HETATM 3656 O  O3G   A CTP G 2 .   ? 24.073  9.705  10.496 0.49 39.97  ? 201 CTP B O3G   1 
HETATM 3657 P  PB    B ADP H 3 .   ? 24.859  10.409 7.276  0.51 49.41  ? 202 ADP B PB    1 
HETATM 3658 O  O1B   B ADP H 3 .   ? 25.395  9.993  8.631  0.51 54.48  ? 202 ADP B O1B   1 
HETATM 3659 O  O2B   B ADP H 3 .   ? 23.721  9.567  6.749  0.51 48.27  ? 202 ADP B O2B   1 
HETATM 3660 O  O3B   B ADP H 3 .   ? 24.638  11.899 7.156  0.51 44.48  ? 202 ADP B O3B   1 
HETATM 3661 P  PA    B ADP H 3 .   ? 26.474  8.618  5.773  0.51 61.18  ? 202 ADP B PA    1 
HETATM 3662 O  O1A   B ADP H 3 .   ? 25.509  7.630  6.388  0.51 58.20  ? 202 ADP B O1A   1 
HETATM 3663 O  O2A   B ADP H 3 .   ? 26.667  8.616  4.272  0.51 59.29  ? 202 ADP B O2A   1 
HETATM 3664 O  O3A   B ADP H 3 .   ? 26.075  10.111 6.255  0.51 57.83  ? 202 ADP B O3A   1 
HETATM 3665 O  "O5'" B ADP H 3 .   ? 27.904  8.427  6.486  0.51 59.73  ? 202 ADP B "O5'" 1 
HETATM 3666 C  "C5'" B ADP H 3 .   ? 27.966  7.868  7.797  0.51 58.10  ? 202 ADP B "C5'" 1 
HETATM 3667 C  "C4'" B ADP H 3 .   ? 28.921  8.700  8.642  0.51 57.69  ? 202 ADP B "C4'" 1 
HETATM 3668 O  "O4'" B ADP H 3 .   ? 30.266  8.532  8.174  0.51 58.24  ? 202 ADP B "O4'" 1 
HETATM 3669 C  "C3'" B ADP H 3 .   ? 28.631  10.200 8.570  0.51 54.41  ? 202 ADP B "C3'" 1 
HETATM 3670 O  "O3'" B ADP H 3 .   ? 27.663  10.652 9.532  0.51 42.96  ? 202 ADP B "O3'" 1 
HETATM 3671 C  "C2'" B ADP H 3 .   ? 30.006  10.822 8.760  0.51 49.84  ? 202 ADP B "C2'" 1 
HETATM 3672 O  "O2'" B ADP H 3 .   ? 30.260  11.097 10.141 0.51 46.24  ? 202 ADP B "O2'" 1 
HETATM 3673 C  "C1'" B ADP H 3 .   ? 30.995  9.765  8.275  0.51 57.51  ? 202 ADP B "C1'" 1 
HETATM 3674 N  N9    B ADP H 3 .   ? 31.580  10.123 6.951  0.51 56.16  ? 202 ADP B N9    1 
HETATM 3675 C  C8    B ADP H 3 .   ? 31.068  9.771  5.753  0.51 56.81  ? 202 ADP B C8    1 
HETATM 3676 N  N7    B ADP H 3 .   ? 31.841  10.244 4.740  0.51 56.53  ? 202 ADP B N7    1 
HETATM 3677 C  C5    B ADP H 3 .   ? 32.874  10.917 5.285  0.51 57.77  ? 202 ADP B C5    1 
HETATM 3678 C  C6    B ADP H 3 .   ? 34.057  11.663 4.782  0.51 52.61  ? 202 ADP B C6    1 
HETATM 3679 N  N6    B ADP H 3 .   ? 34.297  11.792 3.453  0.51 48.75  ? 202 ADP B N6    1 
HETATM 3680 N  N1    B ADP H 3 .   ? 34.891  12.214 5.694  0.51 48.05  ? 202 ADP B N1    1 
HETATM 3681 C  C2    B ADP H 3 .   ? 34.677  12.098 7.019  0.51 45.97  ? 202 ADP B C2    1 
HETATM 3682 N  N3    B ADP H 3 .   ? 33.624  11.432 7.539  0.51 48.87  ? 202 ADP B N3    1 
HETATM 3683 C  C4    B ADP H 3 .   ? 32.700  10.831 6.745  0.51 55.54  ? 202 ADP B C4    1 
HETATM 3684 MG MG    . MG  I 4 .   ? 23.170  7.041  7.187  1.00 56.86  2 203 MG  B MG    1 
HETATM 3685 N  N1    A CTP J 2 .   ? 25.982  49.021 4.046  0.49 46.42  ? 201 CTP C N1    1 
HETATM 3686 C  C2    A CTP J 2 .   ? 24.817  49.774 4.051  0.49 47.06  ? 201 CTP C C2    1 
HETATM 3687 N  N3    A CTP J 2 .   ? 24.145  49.984 2.860  0.49 48.31  ? 201 CTP C N3    1 
HETATM 3688 C  C4    A CTP J 2 .   ? 24.833  49.848 1.668  0.49 54.23  ? 201 CTP C C4    1 
HETATM 3689 C  C5    A CTP J 2 .   ? 26.139  49.371 1.687  0.49 52.17  ? 201 CTP C C5    1 
HETATM 3690 C  C6    A CTP J 2 .   ? 26.622  48.786 2.855  0.49 50.21  ? 201 CTP C C6    1 
HETATM 3691 O  O2    A CTP J 2 .   ? 24.380  50.260 5.098  0.49 39.01  ? 201 CTP C O2    1 
HETATM 3692 N  N4    A CTP J 2 .   ? 24.249  50.163 0.515  0.49 49.48  ? 201 CTP C N4    1 
HETATM 3693 C  "C1'" A CTP J 2 .   ? 26.727  48.822 5.304  0.49 45.80  ? 201 CTP C "C1'" 1 
HETATM 3694 C  "C2'" A CTP J 2 .   ? 26.339  47.499 5.952  0.49 39.74  ? 201 CTP C "C2'" 1 
HETATM 3695 O  "O2'" A CTP J 2 .   ? 26.203  47.697 7.342  0.49 35.80  ? 201 CTP C "O2'" 1 
HETATM 3696 C  "C3'" A CTP J 2 .   ? 27.499  46.571 5.645  0.49 41.06  ? 201 CTP C "C3'" 1 
HETATM 3697 C  "C4'" A CTP J 2 .   ? 28.671  47.543 5.517  0.49 43.47  ? 201 CTP C "C4'" 1 
HETATM 3698 O  "O4'" A CTP J 2 .   ? 28.122  48.763 5.042  0.49 43.43  ? 201 CTP C "O4'" 1 
HETATM 3699 O  "O3'" A CTP J 2 .   ? 27.675  45.583 6.635  0.49 31.93  ? 201 CTP C "O3'" 1 
HETATM 3700 C  "C5'" A CTP J 2 .   ? 29.752  47.064 4.565  0.49 40.53  ? 201 CTP C "C5'" 1 
HETATM 3701 O  "O5'" A CTP J 2 .   ? 29.172  46.793 3.315  0.49 40.23  ? 201 CTP C "O5'" 1 
HETATM 3702 P  PA    A CTP J 2 .   ? 29.437  45.373 2.613  0.49 36.57  ? 201 CTP C PA    1 
HETATM 3703 O  O1A   A CTP J 2 .   ? 30.903  45.050 2.794  0.49 37.15  ? 201 CTP C O1A   1 
HETATM 3704 O  O2A   A CTP J 2 .   ? 29.023  45.454 1.157  0.49 35.47  ? 201 CTP C O2A   1 
HETATM 3705 O  O3A   A CTP J 2 .   ? 28.501  44.296 3.383  0.49 34.90  ? 201 CTP C O3A   1 
HETATM 3706 P  PB    A CTP J 2 .   ? 29.031  43.250 4.493  0.49 35.59  ? 201 CTP C PB    1 
HETATM 3707 O  O1B   A CTP J 2 .   ? 30.315  42.597 4.037  0.49 31.07  ? 201 CTP C O1B   1 
HETATM 3708 O  O2B   A CTP J 2 .   ? 27.965  42.206 4.722  0.49 32.19  ? 201 CTP C O2B   1 
HETATM 3709 O  O3B   A CTP J 2 .   ? 29.274  44.176 5.793  0.49 34.00  ? 201 CTP C O3B   1 
HETATM 3710 P  PG    A CTP J 2 .   ? 30.563  43.940 6.729  0.49 35.95  ? 201 CTP C PG    1 
HETATM 3711 O  O1G   A CTP J 2 .   ? 31.811  44.137 5.898  0.49 30.95  ? 201 CTP C O1G   1 
HETATM 3712 O  O2G   A CTP J 2 .   ? 30.594  44.951 7.845  0.49 23.40  ? 201 CTP C O2G   1 
HETATM 3713 O  O3G   A CTP J 2 .   ? 30.528  42.514 7.240  0.49 28.12  ? 201 CTP C O3G   1 
HETATM 3714 P  PB    B ADP K 3 .   ? 28.928  43.017 4.474  0.51 32.62  ? 202 ADP C PB    1 
HETATM 3715 O  O1B   B ADP K 3 .   ? 29.163  43.762 5.774  0.51 34.00  ? 202 ADP C O1B   1 
HETATM 3716 O  O2B   B ADP K 3 .   ? 30.145  42.369 3.854  0.51 30.79  ? 202 ADP C O2B   1 
HETATM 3717 O  O3B   B ADP K 3 .   ? 27.713  42.119 4.492  0.51 30.02  ? 202 ADP C O3B   1 
HETATM 3718 P  PA    B ADP K 3 .   ? 29.530  45.211 2.696  0.51 36.07  ? 202 ADP C PA    1 
HETATM 3719 O  O1A   B ADP K 3 .   ? 30.966  44.928 3.075  0.51 37.63  ? 202 ADP C O1A   1 
HETATM 3720 O  O2A   B ADP K 3 .   ? 29.144  45.293 1.232  0.51 36.41  ? 202 ADP C O2A   1 
HETATM 3721 O  O3A   B ADP K 3 .   ? 28.508  44.185 3.431  0.51 34.83  ? 202 ADP C O3A   1 
HETATM 3722 O  "O5'" B ADP K 3 .   ? 29.145  46.604 3.394  0.51 40.22  ? 202 ADP C "O5'" 1 
HETATM 3723 C  "C5'" B ADP K 3 .   ? 29.841  47.006 4.569  0.51 40.56  ? 202 ADP C "C5'" 1 
HETATM 3724 C  "C4'" B ADP K 3 .   ? 28.808  47.540 5.547  0.51 43.46  ? 202 ADP C "C4'" 1 
HETATM 3725 O  "O4'" B ADP K 3 .   ? 28.209  48.731 5.026  0.51 43.44  ? 202 ADP C "O4'" 1 
HETATM 3726 C  "C3'" B ADP K 3 .   ? 27.660  46.558 5.784  0.51 41.15  ? 202 ADP C "C3'" 1 
HETATM 3727 O  "O3'" B ADP K 3 .   ? 27.918  45.619 6.833  0.51 33.45  ? 202 ADP C "O3'" 1 
HETATM 3728 C  "C2'" B ADP K 3 .   ? 26.477  47.464 6.078  0.51 39.64  ? 202 ADP C "C2'" 1 
HETATM 3729 O  "O2'" B ADP K 3 .   ? 26.339  47.728 7.480  0.51 35.35  ? 202 ADP C "O2'" 1 
HETATM 3730 C  "C1'" B ADP K 3 .   ? 26.812  48.761 5.351  0.51 45.83  ? 202 ADP C "C1'" 1 
HETATM 3731 N  N9    B ADP K 3 .   ? 26.010  48.853 4.107  0.51 46.16  ? 202 ADP C N9    1 
HETATM 3732 C  C8    B ADP K 3 .   ? 26.405  48.416 2.891  0.51 49.24  ? 202 ADP C C8    1 
HETATM 3733 N  N7    B ADP K 3 .   ? 25.441  48.650 1.961  0.51 51.41  ? 202 ADP C N7    1 
HETATM 3734 C  C5    B ADP K 3 .   ? 24.408  49.248 2.588  0.51 51.74  ? 202 ADP C C5    1 
HETATM 3735 C  C6    B ADP K 3 .   ? 23.075  49.763 2.197  0.51 49.53  ? 202 ADP C C6    1 
HETATM 3736 N  N6    B ADP K 3 .   ? 22.650  49.679 0.913  0.51 46.29  ? 202 ADP C N6    1 
HETATM 3737 N  N1    B ADP K 3 .   ? 22.304  50.317 3.163  0.51 41.21  ? 202 ADP C N1    1 
HETATM 3738 C  C2    B ADP K 3 .   ? 22.714  50.412 4.443  0.51 35.59  ? 202 ADP C C2    1 
HETATM 3739 N  N3    B ADP K 3 .   ? 23.912  49.963 4.863  0.51 40.73  ? 202 ADP C N3    1 
HETATM 3740 C  C4    B ADP K 3 .   ? 24.787  49.381 4.003  0.51 46.83  ? 202 ADP C C4    1 
HETATM 3741 MG MG    . MG  L 4 .   ? 32.230  43.524 3.685  1.00 33.18  2 203 MG  C MG    1 
HETATM 3742 O  O     . HOH M 5 .   ? -5.268  37.047 4.401  1.00 30.06  ? 301 HOH A O     1 
HETATM 3743 O  O     . HOH M 5 .   ? 8.528   49.059 6.489  1.00 26.22  ? 302 HOH A O     1 
HETATM 3744 O  O     . HOH M 5 .   ? 15.942  27.827 16.033 1.00 34.91  ? 303 HOH A O     1 
HETATM 3745 O  O     . HOH M 5 .   ? 6.229   43.700 4.707  1.00 18.38  ? 304 HOH A O     1 
HETATM 3746 O  O     . HOH M 5 .   ? -3.549  31.189 2.414  1.00 37.16  ? 305 HOH A O     1 
HETATM 3747 O  O     . HOH M 5 .   ? -11.487 48.165 15.808 1.00 35.44  ? 306 HOH A O     1 
HETATM 3748 O  O     . HOH M 5 .   ? 5.090   22.446 26.125 1.00 34.34  ? 307 HOH A O     1 
HETATM 3749 O  O     . HOH M 5 .   ? -2.136  49.917 13.422 1.00 35.07  ? 308 HOH A O     1 
HETATM 3750 O  O     . HOH M 5 .   ? 21.167  54.567 13.035 1.00 39.30  ? 309 HOH A O     1 
HETATM 3751 O  O     . HOH M 5 .   ? -0.814  31.743 3.469  1.00 34.78  ? 310 HOH A O     1 
HETATM 3752 O  O     . HOH M 5 .   ? -4.698  54.559 23.882 1.00 27.90  ? 311 HOH A O     1 
HETATM 3753 O  O     . HOH M 5 .   ? 4.149   57.169 24.500 1.00 27.38  ? 312 HOH A O     1 
HETATM 3754 O  O     . HOH M 5 .   ? 18.952  54.683 20.687 1.00 30.98  ? 313 HOH A O     1 
HETATM 3755 O  O     . HOH M 5 .   ? 18.772  46.576 12.215 1.00 14.89  ? 314 HOH A O     1 
HETATM 3756 O  O     . HOH M 5 .   ? 8.538   27.762 26.760 1.00 27.82  ? 315 HOH A O     1 
HETATM 3757 O  O     . HOH M 5 .   ? -7.528  39.239 6.542  1.00 30.91  ? 316 HOH A O     1 
HETATM 3758 O  O     . HOH M 5 .   ? 12.379  38.573 25.641 1.00 16.50  ? 317 HOH A O     1 
HETATM 3759 O  O     B HOH M 5 .   ? -0.597  33.131 9.171  0.48 16.58  ? 318 HOH A O     1 
HETATM 3760 O  O     . HOH M 5 .   ? -1.346  54.961 19.297 1.00 22.61  ? 319 HOH A O     1 
HETATM 3761 O  O     . HOH M 5 .   ? -6.636  36.012 8.420  1.00 23.10  ? 320 HOH A O     1 
HETATM 3762 O  O     . HOH M 5 .   ? -7.571  46.408 4.618  1.00 30.68  ? 321 HOH A O     1 
HETATM 3763 O  O     . HOH M 5 .   ? 12.687  43.710 9.786  1.00 15.39  ? 322 HOH A O     1 
HETATM 3764 O  O     . HOH M 5 .   ? -11.494 44.801 10.234 1.00 29.88  ? 323 HOH A O     1 
HETATM 3765 O  O     . HOH M 5 .   ? 10.844  40.955 2.690  1.00 33.02  ? 324 HOH A O     1 
HETATM 3766 O  O     . HOH M 5 .   ? -14.393 43.080 16.153 1.00 34.92  ? 325 HOH A O     1 
HETATM 3767 O  O     . HOH M 5 .   ? 8.466   43.093 1.491  1.00 35.68  ? 326 HOH A O     1 
HETATM 3768 O  O     . HOH M 5 .   ? -2.204  54.950 24.309 1.00 26.17  ? 327 HOH A O     1 
HETATM 3769 O  O     . HOH M 5 .   ? 1.796   23.214 30.654 1.00 25.90  ? 328 HOH A O     1 
HETATM 3770 O  O     . HOH M 5 .   ? -14.205 35.450 24.415 1.00 29.80  ? 329 HOH A O     1 
HETATM 3771 O  O     . HOH M 5 .   ? -15.831 26.205 17.724 1.00 31.73  ? 330 HOH A O     1 
HETATM 3772 O  O     . HOH M 5 .   ? -3.070  25.631 13.827 1.00 33.83  ? 331 HOH A O     1 
HETATM 3773 O  O     . HOH M 5 .   ? 4.510   51.890 6.630  1.00 43.47  ? 332 HOH A O     1 
HETATM 3774 O  O     . HOH M 5 .   ? -13.246 21.307 8.124  1.00 36.25  ? 333 HOH A O     1 
HETATM 3775 O  O     . HOH M 5 .   ? 16.153  43.249 21.108 1.00 27.83  ? 334 HOH A O     1 
HETATM 3776 O  O     . HOH M 5 .   ? -1.105  28.447 3.139  1.00 26.71  ? 335 HOH A O     1 
HETATM 3777 O  O     . HOH M 5 .   ? -3.629  37.532 6.540  1.00 18.06  ? 336 HOH A O     1 
HETATM 3778 O  O     . HOH M 5 .   ? 12.643  32.534 21.876 1.00 16.26  ? 337 HOH A O     1 
HETATM 3779 O  O     . HOH M 5 .   ? 4.421   32.168 7.115  1.00 24.94  ? 338 HOH A O     1 
HETATM 3780 O  O     . HOH M 5 .   ? 10.554  48.278 15.876 1.00 17.48  ? 339 HOH A O     1 
HETATM 3781 O  O     . HOH M 5 .   ? 3.343   24.834 3.526  1.00 18.71  ? 340 HOH A O     1 
HETATM 3782 O  O     . HOH M 5 .   ? 13.143  21.941 12.971 1.00 28.23  ? 341 HOH A O     1 
HETATM 3783 O  O     . HOH M 5 .   ? 2.959   39.209 9.302  1.00 15.33  ? 342 HOH A O     1 
HETATM 3784 O  O     . HOH M 5 .   ? 13.261  22.231 17.479 1.00 16.15  ? 343 HOH A O     1 
HETATM 3785 O  O     . HOH M 5 .   ? 14.621  36.392 16.284 1.00 16.51  ? 344 HOH A O     1 
HETATM 3786 O  O     . HOH M 5 .   ? -6.995  23.084 10.504 1.00 34.14  ? 345 HOH A O     1 
HETATM 3787 O  O     . HOH M 5 .   ? 9.547   44.860 24.289 1.00 16.60  ? 346 HOH A O     1 
HETATM 3788 O  O     . HOH M 5 .   ? 24.013  56.323 22.171 1.00 31.82  ? 347 HOH A O     1 
HETATM 3789 O  O     . HOH M 5 .   ? 9.559   50.822 16.558 1.00 24.10  ? 348 HOH A O     1 
HETATM 3790 O  O     . HOH M 5 .   ? 13.307  43.638 5.124  1.00 20.75  ? 349 HOH A O     1 
HETATM 3791 O  O     . HOH M 5 .   ? -6.079  24.582 12.670 1.00 32.54  ? 350 HOH A O     1 
HETATM 3792 O  O     . HOH M 5 .   ? 7.611   36.766 3.691  1.00 25.25  ? 351 HOH A O     1 
HETATM 3793 O  O     . HOH M 5 .   ? 15.628  31.604 14.474 1.00 29.25  ? 352 HOH A O     1 
HETATM 3794 O  O     . HOH M 5 .   ? 9.900   24.856 23.976 1.00 23.39  ? 353 HOH A O     1 
HETATM 3795 O  O     . HOH M 5 .   ? 6.413   17.835 10.070 1.00 15.50  ? 354 HOH A O     1 
HETATM 3796 O  O     . HOH M 5 .   ? -0.777  47.718 9.380  1.00 22.80  ? 355 HOH A O     1 
HETATM 3797 O  O     . HOH M 5 .   ? -16.550 24.906 13.006 1.00 33.98  ? 356 HOH A O     1 
HETATM 3798 O  O     . HOH M 5 .   ? -0.832  47.776 6.631  1.00 27.25  ? 357 HOH A O     1 
HETATM 3799 O  O     . HOH M 5 .   ? 10.635  21.176 8.953  1.00 16.42  ? 358 HOH A O     1 
HETATM 3800 O  O     . HOH M 5 .   ? -5.447  45.632 24.687 1.00 25.09  ? 359 HOH A O     1 
HETATM 3801 O  O     . HOH M 5 .   ? -8.252  24.013 20.244 1.00 31.75  ? 360 HOH A O     1 
HETATM 3802 O  O     . HOH M 5 .   ? 27.748  53.889 20.960 1.00 32.42  ? 361 HOH A O     1 
HETATM 3803 O  O     . HOH M 5 .   ? -2.791  46.480 23.720 1.00 16.91  ? 362 HOH A O     1 
HETATM 3804 O  O     . HOH M 5 .   ? 15.039  37.703 7.281  1.00 18.76  ? 363 HOH A O     1 
HETATM 3805 O  O     . HOH M 5 .   ? 12.411  56.326 23.833 1.00 32.04  ? 364 HOH A O     1 
HETATM 3806 O  O     . HOH M 5 .   ? 11.932  54.708 16.407 1.00 29.22  ? 365 HOH A O     1 
HETATM 3807 O  O     . HOH M 5 .   ? 10.487  31.101 6.019  1.00 16.66  ? 366 HOH A O     1 
HETATM 3808 O  O     . HOH M 5 .   ? -0.687  22.731 29.397 1.00 22.02  ? 367 HOH A O     1 
HETATM 3809 O  O     . HOH M 5 .   ? -19.181 36.600 11.981 1.00 31.95  ? 368 HOH A O     1 
HETATM 3810 O  O     . HOH M 5 .   ? 8.324   46.577 22.613 1.00 15.14  ? 369 HOH A O     1 
HETATM 3811 O  O     . HOH M 5 .   ? -9.355  36.132 5.691  1.00 23.29  ? 370 HOH A O     1 
HETATM 3812 O  O     . HOH M 5 .   ? -9.397  40.445 26.812 1.00 22.70  ? 371 HOH A O     1 
HETATM 3813 O  O     . HOH M 5 .   ? -7.715  49.369 15.773 1.00 32.29  ? 372 HOH A O     1 
HETATM 3814 O  O     . HOH M 5 .   ? -3.484  33.911 3.768  1.00 27.67  ? 373 HOH A O     1 
HETATM 3815 O  O     . HOH M 5 .   ? -5.576  33.954 6.745  1.00 28.53  ? 374 HOH A O     1 
HETATM 3816 O  O     . HOH M 5 .   ? 6.550   24.988 0.848  1.00 18.30  ? 375 HOH A O     1 
HETATM 3817 O  O     . HOH M 5 .   ? -4.070  25.663 16.476 1.00 26.23  ? 376 HOH A O     1 
HETATM 3818 O  O     . HOH M 5 .   ? 14.640  38.452 22.700 1.00 24.38  ? 377 HOH A O     1 
HETATM 3819 O  O     . HOH M 5 .   ? 13.953  36.770 2.066  1.00 38.32  ? 378 HOH A O     1 
HETATM 3820 O  O     . HOH M 5 .   ? -0.544  55.651 22.134 1.00 21.40  ? 379 HOH A O     1 
HETATM 3821 O  O     . HOH M 5 .   ? 6.927   26.763 29.527 1.00 24.38  ? 380 HOH A O     1 
HETATM 3822 O  O     . HOH M 5 .   ? 11.572  33.636 26.308 0.50 12.89  ? 381 HOH A O     1 
HETATM 3823 O  O     . HOH M 5 .   ? 1.834   44.016 1.508  1.00 37.70  ? 382 HOH A O     1 
HETATM 3824 O  O     . HOH M 5 .   ? -12.857 37.000 21.492 1.00 43.61  ? 383 HOH A O     1 
HETATM 3825 O  O     . HOH M 5 .   ? 3.842   19.597 8.155  1.00 18.46  ? 384 HOH A O     1 
HETATM 3826 O  O     . HOH M 5 .   ? 8.384   56.987 23.786 1.00 26.33  ? 385 HOH A O     1 
HETATM 3827 O  O     . HOH M 5 .   ? -11.609 40.059 25.134 1.00 43.05  ? 386 HOH A O     1 
HETATM 3828 O  O     . HOH M 5 .   ? 4.874   20.842 23.856 1.00 29.02  ? 387 HOH A O     1 
HETATM 3829 O  O     . HOH M 5 .   ? -5.747  48.843 11.385 1.00 29.00  ? 388 HOH A O     1 
HETATM 3830 O  O     . HOH M 5 .   ? -2.339  35.178 6.837  1.00 22.41  ? 389 HOH A O     1 
HETATM 3831 O  O     . HOH M 5 .   ? 0.530   19.249 7.730  1.00 27.38  ? 390 HOH A O     1 
HETATM 3832 O  O     . HOH M 5 .   ? 1.544   52.247 17.693 1.00 28.51  ? 391 HOH A O     1 
HETATM 3833 O  O     . HOH M 5 .   ? 10.701  52.728 18.152 1.00 21.55  ? 392 HOH A O     1 
HETATM 3834 O  O     . HOH M 5 .   ? 9.709   28.407 5.826  1.00 15.96  ? 393 HOH A O     1 
HETATM 3835 O  O     . HOH M 5 .   ? 11.703  32.814 14.284 1.00 21.96  ? 394 HOH A O     1 
HETATM 3836 O  O     . HOH M 5 .   ? 1.362   49.639 9.098  1.00 26.88  ? 395 HOH A O     1 
HETATM 3837 O  O     . HOH M 5 .   ? 3.098   36.229 3.203  1.00 40.42  ? 396 HOH A O     1 
HETATM 3838 O  O     . HOH M 5 .   ? 7.879   46.775 3.334  1.00 42.94  ? 397 HOH A O     1 
HETATM 3839 O  O     . HOH M 5 .   ? 13.221  32.781 11.796 1.00 30.31  ? 398 HOH A O     1 
HETATM 3840 O  O     . HOH M 5 .   ? -8.879  25.178 22.250 1.00 37.70  ? 399 HOH A O     1 
HETATM 3841 O  O     . HOH M 5 .   ? -14.912 30.437 22.631 1.00 28.58  ? 400 HOH A O     1 
HETATM 3842 O  O     . HOH M 5 .   ? 18.311  41.213 20.727 1.00 24.11  ? 401 HOH A O     1 
HETATM 3843 O  O     . HOH M 5 .   ? 10.317  26.935 3.605  1.00 30.03  ? 402 HOH A O     1 
HETATM 3844 O  O     . HOH M 5 .   ? 12.577  23.853 4.161  1.00 32.73  ? 403 HOH A O     1 
HETATM 3845 O  O     . HOH M 5 .   ? 3.148   28.952 3.494  1.00 27.18  ? 404 HOH A O     1 
HETATM 3846 O  O     . HOH M 5 .   ? 12.496  29.955 20.731 1.00 20.74  ? 405 HOH A O     1 
HETATM 3847 O  O     . HOH M 5 .   ? -0.851  19.319 5.287  1.00 37.00  ? 406 HOH A O     1 
HETATM 3848 O  O     . HOH M 5 .   ? 5.921   57.836 19.791 1.00 47.91  ? 407 HOH A O     1 
HETATM 3849 O  O     . HOH M 5 .   ? 18.018  55.735 13.640 1.00 37.17  ? 408 HOH A O     1 
HETATM 3850 O  O     . HOH M 5 .   ? -7.857  41.122 4.068  1.00 42.79  ? 409 HOH A O     1 
HETATM 3851 O  O     . HOH M 5 .   ? 2.947   59.326 20.654 1.00 41.37  ? 410 HOH A O     1 
HETATM 3852 O  O     . HOH M 5 .   ? -4.336  53.019 26.456 1.00 40.39  ? 411 HOH A O     1 
HETATM 3853 O  O     . HOH M 5 .   ? -9.145  47.679 6.707  1.00 43.13  ? 412 HOH A O     1 
HETATM 3854 O  O     . HOH M 5 .   ? -18.071 29.625 5.267  1.00 40.89  ? 413 HOH A O     1 
HETATM 3855 O  O     . HOH M 5 .   ? -13.134 45.922 12.019 1.00 43.11  ? 414 HOH A O     1 
HETATM 3856 O  O     . HOH M 5 .   ? 1.734   48.538 5.576  1.00 34.90  ? 415 HOH A O     1 
HETATM 3857 O  O     . HOH M 5 .   ? 13.754  35.988 9.210  1.00 33.45  ? 416 HOH A O     1 
HETATM 3858 O  O     . HOH M 5 .   ? -23.718 34.148 4.266  1.00 44.98  ? 417 HOH A O     1 
HETATM 3859 O  O     . HOH M 5 .   ? 14.978  22.351 15.188 1.00 28.27  ? 418 HOH A O     1 
HETATM 3860 O  O     . HOH M 5 .   ? 7.322   34.160 3.834  1.00 38.87  ? 419 HOH A O     1 
HETATM 3861 O  O     . HOH M 5 .   ? -13.276 27.770 24.037 1.00 39.62  ? 420 HOH A O     1 
HETATM 3862 O  O     . HOH M 5 .   ? 15.625  30.243 19.305 1.00 33.52  ? 421 HOH A O     1 
HETATM 3863 O  O     . HOH M 5 .   ? 5.842   18.268 5.168  1.00 31.03  ? 422 HOH A O     1 
HETATM 3864 O  O     . HOH M 5 .   ? 14.609  34.204 20.809 1.00 19.09  ? 423 HOH A O     1 
HETATM 3865 O  O     . HOH M 5 .   ? 2.537   26.776 1.898  1.00 27.74  ? 424 HOH A O     1 
HETATM 3866 O  O     . HOH M 5 .   ? 0.687   58.517 22.256 1.00 35.07  ? 425 HOH A O     1 
HETATM 3867 O  O     . HOH M 5 .   ? 4.342   42.768 2.800  1.00 31.43  ? 426 HOH A O     1 
HETATM 3868 O  O     . HOH M 5 .   ? 13.360  32.407 24.530 1.00 20.47  ? 427 HOH A O     1 
HETATM 3869 O  O     . HOH M 5 .   ? -11.210 27.775 25.781 1.00 31.72  ? 428 HOH A O     1 
HETATM 3870 O  O     . HOH M 5 .   ? 1.468   58.150 25.239 1.00 38.91  ? 429 HOH A O     1 
HETATM 3871 O  O     . HOH M 5 .   ? 15.546  34.501 24.842 1.00 33.85  ? 430 HOH A O     1 
HETATM 3872 O  O     . HOH M 5 .   ? -1.624  56.631 26.219 1.00 39.44  ? 431 HOH A O     1 
HETATM 3873 O  O     . HOH M 5 .   ? -9.840  25.703 26.151 1.00 30.37  ? 432 HOH A O     1 
HETATM 3874 O  O     . HOH M 5 .   ? 16.719  25.549 4.967  1.00 40.35  ? 433 HOH A O     1 
HETATM 3875 O  O     . HOH M 5 .   ? 5.342   37.864 2.508  1.00 35.16  ? 434 HOH A O     1 
HETATM 3876 O  O     . HOH M 5 .   ? -15.645 37.457 23.280 1.00 34.78  ? 435 HOH A O     1 
HETATM 3877 O  O     . HOH M 5 .   ? 9.015   32.335 3.925  1.00 34.19  ? 436 HOH A O     1 
HETATM 3878 O  O     . HOH M 5 .   ? 1.977   50.720 6.818  1.00 37.59  ? 437 HOH A O     1 
HETATM 3879 O  O     . HOH M 5 .   ? -13.003 49.770 16.848 1.00 40.83  ? 438 HOH A O     1 
HETATM 3880 O  O     . HOH M 5 .   ? -2.773  49.208 10.659 1.00 34.03  ? 439 HOH A O     1 
HETATM 3881 O  O     . HOH M 5 .   ? 15.377  34.095 18.155 1.00 29.69  ? 440 HOH A O     1 
HETATM 3882 O  O     . HOH M 5 .   ? 12.976  31.219 4.642  1.00 33.24  ? 441 HOH A O     1 
HETATM 3883 O  O     . HOH N 5 .   ? 22.589  12.814 7.731  1.00 43.58  ? 301 HOH B O     1 
HETATM 3884 O  O     . HOH N 5 .   ? 20.802  0.803  7.917  1.00 45.16  ? 302 HOH B O     1 
HETATM 3885 O  O     . HOH N 5 .   ? 26.938  16.809 3.141  1.00 30.15  ? 303 HOH B O     1 
HETATM 3886 O  O     . HOH N 5 .   ? 19.905  27.565 15.789 1.00 30.70  ? 304 HOH B O     1 
HETATM 3887 O  O     . HOH N 5 .   ? 9.631   10.352 7.120  1.00 18.02  ? 305 HOH B O     1 
HETATM 3888 O  O     . HOH N 5 .   ? 35.616  8.623  19.697 1.00 36.31  ? 306 HOH B O     1 
HETATM 3889 O  O     . HOH N 5 .   ? 7.065   19.971 23.253 1.00 29.34  ? 307 HOH B O     1 
HETATM 3890 O  O     . HOH N 5 .   ? 26.350  24.321 23.234 1.00 25.12  ? 308 HOH B O     1 
HETATM 3891 O  O     . HOH N 5 .   ? 8.667   12.143 3.921  1.00 28.77  ? 309 HOH B O     1 
HETATM 3892 O  O     . HOH N 5 .   ? 1.963   20.449 15.032 1.00 15.00  ? 310 HOH B O     1 
HETATM 3893 O  O     . HOH N 5 .   ? -3.920  17.363 24.719 1.00 37.26  ? 311 HOH B O     1 
HETATM 3894 O  O     . HOH N 5 .   ? 1.858   3.312  28.842 1.00 35.26  ? 312 HOH B O     1 
HETATM 3895 O  O     . HOH N 5 .   ? 23.197  2.907  9.546  1.00 36.55  ? 313 HOH B O     1 
HETATM 3896 O  O     . HOH N 5 .   ? 31.553  17.460 17.298 1.00 16.58  ? 314 HOH B O     1 
HETATM 3897 O  O     . HOH N 5 .   ? 20.358  5.043  8.139  1.00 21.37  ? 315 HOH B O     1 
HETATM 3898 O  O     . HOH N 5 .   ? 30.625  -5.920 21.146 1.00 28.34  ? 316 HOH B O     1 
HETATM 3899 O  O     . HOH N 5 .   ? 7.092   16.348 12.218 1.00 15.57  ? 317 HOH B O     1 
HETATM 3900 O  O     . HOH N 5 .   ? -7.481  20.794 26.295 1.00 34.02  ? 318 HOH B O     1 
HETATM 3901 O  O     . HOH N 5 .   ? 17.418  26.949 7.809  1.00 39.46  ? 319 HOH B O     1 
HETATM 3902 O  O     . HOH N 5 .   ? 31.709  11.361 16.353 1.00 26.31  ? 320 HOH B O     1 
HETATM 3903 O  O     . HOH N 5 .   ? 14.398  2.874  26.495 1.00 23.92  ? 321 HOH B O     1 
HETATM 3904 O  O     . HOH N 5 .   ? 9.623   14.222 26.675 1.00 18.24  ? 322 HOH B O     1 
HETATM 3905 O  O     . HOH N 5 .   ? 18.921  -5.098 12.907 1.00 33.89  ? 323 HOH B O     1 
HETATM 3906 O  O     . HOH N 5 .   ? 31.326  21.691 25.043 1.00 31.72  ? 324 HOH B O     1 
HETATM 3907 O  O     . HOH N 5 .   ? 3.424   10.593 19.603 1.00 26.64  ? 325 HOH B O     1 
HETATM 3908 O  O     . HOH N 5 .   ? 14.557  14.975 5.090  1.00 27.04  ? 326 HOH B O     1 
HETATM 3909 O  O     . HOH N 5 .   ? 24.943  22.115 26.484 1.00 31.42  ? 327 HOH B O     1 
HETATM 3910 O  O     . HOH N 5 .   ? 29.438  -1.693 25.454 1.00 30.14  ? 328 HOH B O     1 
HETATM 3911 O  O     . HOH N 5 .   ? -4.949  13.750 20.216 1.00 44.69  ? 329 HOH B O     1 
HETATM 3912 O  O     . HOH N 5 .   ? 15.808  10.057 10.954 1.00 16.59  ? 330 HOH B O     1 
HETATM 3913 O  O     . HOH N 5 .   ? 13.723  19.907 27.052 1.00 15.70  ? 331 HOH B O     1 
HETATM 3914 O  O     . HOH N 5 .   ? 1.398   22.933 18.207 1.00 15.49  ? 332 HOH B O     1 
HETATM 3915 O  O     . HOH N 5 .   ? 14.767  -3.163 7.646  1.00 41.09  ? 333 HOH B O     1 
HETATM 3916 O  O     . HOH N 5 .   ? 9.576   15.723 4.763  1.00 26.40  ? 334 HOH B O     1 
HETATM 3917 O  O     . HOH N 5 .   ? 4.123   9.879  9.770  1.00 27.99  ? 335 HOH B O     1 
HETATM 3918 O  O     . HOH N 5 .   ? 6.348   10.288 6.086  1.00 36.49  ? 336 HOH B O     1 
HETATM 3919 O  O     . HOH N 5 .   ? -6.154  18.618 17.382 1.00 40.04  ? 337 HOH B O     1 
HETATM 3920 O  O     . HOH N 5 .   ? 18.219  22.791 22.382 1.00 17.10  ? 338 HOH B O     1 
HETATM 3921 O  O     . HOH N 5 .   ? 8.615   12.023 25.290 1.00 16.49  ? 339 HOH B O     1 
HETATM 3922 O  O     . HOH N 5 .   ? 16.586  25.228 14.973 1.00 31.10  ? 340 HOH B O     1 
HETATM 3923 O  O     . HOH N 5 .   ? 34.320  16.426 28.288 1.00 23.71  ? 341 HOH B O     1 
HETATM 3924 O  O     . HOH N 5 .   ? 6.223   16.556 7.542  1.00 18.45  ? 342 HOH B O     1 
HETATM 3925 O  O     . HOH N 5 .   ? -0.913  10.616 20.498 1.00 32.24  ? 343 HOH B O     1 
HETATM 3926 O  O     . HOH N 5 .   ? 18.428  21.641 26.936 1.00 14.70  ? 344 HOH B O     1 
HETATM 3927 O  O     . HOH N 5 .   ? -7.605  25.179 24.670 1.00 29.95  ? 345 HOH B O     1 
HETATM 3928 O  O     . HOH N 5 .   ? 14.054  24.100 23.549 1.00 31.16  ? 346 HOH B O     1 
HETATM 3929 O  O     . HOH N 5 .   ? 27.130  21.324 29.024 1.00 26.27  ? 347 HOH B O     1 
HETATM 3930 O  O     . HOH N 5 .   ? 4.938   12.736 18.790 1.00 18.62  ? 348 HOH B O     1 
HETATM 3931 O  O     . HOH N 5 .   ? 12.418  21.668 24.150 1.00 25.83  ? 349 HOH B O     1 
HETATM 3932 O  O     . HOH N 5 .   ? 32.161  23.535 8.416  1.00 18.37  ? 350 HOH B O     1 
HETATM 3933 O  O     . HOH N 5 .   ? 18.372  20.417 6.537  1.00 17.49  ? 351 HOH B O     1 
HETATM 3934 O  O     . HOH N 5 .   ? 4.493   7.588  8.012  1.00 47.52  ? 352 HOH B O     1 
HETATM 3935 O  O     . HOH N 5 .   ? 22.275  -6.352 18.435 1.00 33.82  ? 353 HOH B O     1 
HETATM 3936 O  O     . HOH N 5 .   ? 23.176  0.213  28.653 1.00 27.86  ? 354 HOH B O     1 
HETATM 3937 O  O     . HOH N 5 .   ? 20.622  14.618 7.579  1.00 26.61  ? 355 HOH B O     1 
HETATM 3938 O  O     . HOH N 5 .   ? 37.693  1.029  17.982 1.00 32.16  ? 356 HOH B O     1 
HETATM 3939 O  O     . HOH N 5 .   ? 7.889   3.715  12.148 1.00 33.96  ? 357 HOH B O     1 
HETATM 3940 O  O     . HOH N 5 .   ? 10.460  2.612  12.330 1.00 34.42  ? 358 HOH B O     1 
HETATM 3941 O  O     . HOH N 5 .   ? 24.616  23.925 1.179  1.00 35.89  ? 359 HOH B O     1 
HETATM 3942 O  O     . HOH N 5 .   ? -4.398  16.502 28.182 1.00 41.41  ? 360 HOH B O     1 
HETATM 3943 O  O     . HOH N 5 .   ? 31.820  20.340 6.578  1.00 25.64  ? 361 HOH B O     1 
HETATM 3944 O  O     . HOH N 5 .   ? 6.035   2.849  20.941 1.00 28.29  ? 362 HOH B O     1 
HETATM 3945 O  O     . HOH N 5 .   ? 24.543  0.489  6.939  1.00 37.64  ? 363 HOH B O     1 
HETATM 3946 O  O     . HOH N 5 .   ? -0.078  7.050  28.059 1.00 27.68  ? 364 HOH B O     1 
HETATM 3947 O  O     . HOH N 5 .   ? 32.528  21.991 22.482 1.00 24.65  ? 365 HOH B O     1 
HETATM 3948 O  O     . HOH N 5 .   ? 36.125  19.497 6.418  1.00 33.22  ? 366 HOH B O     1 
HETATM 3949 O  O     . HOH N 5 .   ? 1.510   10.563 21.766 1.00 26.58  ? 367 HOH B O     1 
HETATM 3950 O  O     . HOH N 5 .   ? 12.460  2.452  3.383  1.00 30.66  ? 368 HOH B O     1 
HETATM 3951 O  O     . HOH N 5 .   ? 18.081  12.196 4.351  1.00 42.37  ? 369 HOH B O     1 
HETATM 3952 O  O     . HOH N 5 .   ? 23.308  14.520 4.303  1.00 35.64  ? 370 HOH B O     1 
HETATM 3953 O  O     . HOH N 5 .   ? 5.503   -0.177 26.689 1.00 37.04  ? 371 HOH B O     1 
HETATM 3954 O  O     . HOH N 5 .   ? 21.045  21.005 5.896  1.00 18.65  ? 372 HOH B O     1 
HETATM 3955 O  O     . HOH N 5 .   ? -6.226  18.211 25.751 1.00 35.73  ? 373 HOH B O     1 
HETATM 3956 O  O     . HOH N 5 .   ? 33.834  -0.008 23.072 1.00 29.32  ? 374 HOH B O     1 
HETATM 3957 O  O     . HOH N 5 .   ? 17.468  21.204 14.933 1.00 22.39  ? 375 HOH B O     1 
HETATM 3958 O  O     . HOH N 5 .   ? 7.769   23.258 22.629 1.00 20.80  ? 376 HOH B O     1 
HETATM 3959 O  O     . HOH N 5 .   ? 33.268  17.780 6.303  1.00 27.53  ? 377 HOH B O     1 
HETATM 3960 O  O     B HOH N 5 .   ? 22.820  10.346 10.096 0.51 18.84  ? 378 HOH B O     1 
HETATM 3961 O  O     . HOH N 5 .   ? 25.125  27.779 11.900 1.00 39.90  ? 379 HOH B O     1 
HETATM 3962 O  O     . HOH N 5 .   ? -5.402  15.596 17.797 1.00 42.94  ? 380 HOH B O     1 
HETATM 3963 O  O     . HOH N 5 .   ? 20.363  23.919 20.840 1.00 23.83  ? 381 HOH B O     1 
HETATM 3964 O  O     . HOH N 5 .   ? 21.630  21.809 3.360  1.00 30.95  ? 382 HOH B O     1 
HETATM 3965 O  O     . HOH N 5 .   ? 13.964  10.099 4.946  1.00 32.47  ? 383 HOH B O     1 
HETATM 3966 O  O     . HOH N 5 .   ? 21.812  27.066 18.388 1.00 34.33  ? 384 HOH B O     1 
HETATM 3967 O  O     . HOH N 5 .   ? -1.795  11.024 28.000 1.00 33.96  ? 385 HOH B O     1 
HETATM 3968 O  O     . HOH N 5 .   ? 16.407  1.083  27.446 1.00 33.04  ? 386 HOH B O     1 
HETATM 3969 O  O     . HOH N 5 .   ? 24.896  29.201 14.146 1.00 31.82  ? 387 HOH B O     1 
HETATM 3970 O  O     . HOH N 5 .   ? 13.167  21.098 10.324 1.00 36.21  ? 388 HOH B O     1 
HETATM 3971 O  O     . HOH N 5 .   ? 17.472  15.841 4.963  1.00 41.62  ? 389 HOH B O     1 
HETATM 3972 O  O     . HOH N 5 .   ? 15.679  23.524 21.626 1.00 19.45  ? 390 HOH B O     1 
HETATM 3973 O  O     . HOH N 5 .   ? 21.892  -7.827 16.037 1.00 43.91  ? 391 HOH B O     1 
HETATM 3974 O  O     . HOH N 5 .   ? 11.012  9.125  5.106  1.00 34.76  ? 392 HOH B O     1 
HETATM 3975 O  O     . HOH N 5 .   ? 0.734   9.985  18.349 1.00 33.29  ? 393 HOH B O     1 
HETATM 3976 O  O     . HOH N 5 .   ? 18.436  23.734 24.972 1.00 21.57  ? 394 HOH B O     1 
HETATM 3977 O  O     . HOH N 5 .   ? 15.550  24.500 25.758 1.00 38.20  ? 395 HOH B O     1 
HETATM 3978 O  O     . HOH N 5 .   ? 28.801  -3.808 24.561 1.00 39.12  ? 396 HOH B O     1 
HETATM 3979 O  O     . HOH N 5 .   ? 34.826  4.721  25.682 1.00 30.31  ? 397 HOH B O     1 
HETATM 3980 O  O     . HOH N 5 .   ? 19.864  28.814 4.780  1.00 36.90  ? 398 HOH B O     1 
HETATM 3981 O  O     . HOH N 5 .   ? 18.055  18.392 4.708  1.00 32.27  ? 399 HOH B O     1 
HETATM 3982 O  O     . HOH N 5 .   ? 35.979  6.875  25.683 1.00 35.01  ? 400 HOH B O     1 
HETATM 3983 O  O     . HOH N 5 .   ? 15.087  24.045 18.985 1.00 26.57  ? 401 HOH B O     1 
HETATM 3984 O  O     . HOH N 5 .   ? 10.275  14.038 2.718  1.00 32.05  ? 402 HOH B O     1 
HETATM 3985 O  O     . HOH N 5 .   ? 16.749  22.399 5.403  1.00 31.74  ? 403 HOH B O     1 
HETATM 3986 O  O     . HOH O 5 .   ? 18.987  44.450 23.757 1.00 25.00  ? 301 HOH C O     1 
HETATM 3987 O  O     . HOH O 5 .   ? 32.965  42.921 1.472  1.00 32.32  ? 302 HOH C O     1 
HETATM 3988 O  O     . HOH O 5 .   ? 39.898  54.567 20.174 1.00 36.53  ? 303 HOH C O     1 
HETATM 3989 O  O     . HOH O 5 .   ? 45.575  37.164 -1.928 1.00 32.43  ? 304 HOH C O     1 
HETATM 3990 O  O     . HOH O 5 .   ? 40.144  16.172 22.572 1.00 34.32  ? 305 HOH C O     1 
HETATM 3991 O  O     . HOH O 5 .   ? 49.461  28.057 24.552 1.00 26.96  ? 306 HOH C O     1 
HETATM 3992 O  O     . HOH O 5 .   ? 25.752  48.256 10.884 1.00 36.36  ? 307 HOH C O     1 
HETATM 3993 O  O     B HOH O 5 .   ? 30.827  41.564 7.027  0.51 22.95  ? 308 HOH C O     1 
HETATM 3994 O  O     . HOH O 5 .   ? 46.388  40.306 -3.869 1.00 23.50  ? 309 HOH C O     1 
HETATM 3995 O  O     . HOH O 5 .   ? 40.170  30.192 2.824  1.00 35.43  ? 310 HOH C O     1 
HETATM 3996 O  O     . HOH O 5 .   ? 32.983  18.804 13.741 1.00 17.41  ? 311 HOH C O     1 
HETATM 3997 O  O     . HOH O 5 .   ? 49.505  44.025 12.903 1.00 38.21  ? 312 HOH C O     1 
HETATM 3998 O  O     . HOH O 5 .   ? 18.004  31.113 15.691 1.00 28.85  ? 313 HOH C O     1 
HETATM 3999 O  O     . HOH O 5 .   ? 18.724  38.926 22.389 1.00 25.22  ? 314 HOH C O     1 
HETATM 4000 O  O     . HOH O 5 .   ? 21.338  47.694 27.974 1.00 34.90  ? 315 HOH C O     1 
HETATM 4001 O  O     . HOH O 5 .   ? 43.527  42.219 -3.958 1.00 24.62  ? 316 HOH C O     1 
HETATM 4002 O  O     . HOH O 5 .   ? 44.632  27.440 6.608  1.00 35.49  ? 317 HOH C O     1 
HETATM 4003 O  O     . HOH O 5 .   ? 31.407  24.219 21.817 1.00 28.65  ? 318 HOH C O     1 
HETATM 4004 O  O     . HOH O 5 .   ? 36.647  29.873 4.260  1.00 19.64  ? 319 HOH C O     1 
HETATM 4005 O  O     . HOH O 5 .   ? 36.784  42.533 1.801  1.00 30.47  ? 320 HOH C O     1 
HETATM 4006 O  O     . HOH O 5 .   ? 35.017  27.715 1.455  1.00 29.81  ? 321 HOH C O     1 
HETATM 4007 O  O     . HOH O 5 .   ? 24.945  28.233 22.794 1.00 33.45  ? 322 HOH C O     1 
HETATM 4008 O  O     . HOH O 5 .   ? 51.604  36.720 22.568 1.00 31.09  ? 323 HOH C O     1 
HETATM 4009 O  O     . HOH O 5 .   ? 31.962  26.820 2.743  1.00 34.06  ? 324 HOH C O     1 
HETATM 4010 O  O     . HOH O 5 .   ? 33.539  25.065 10.280 1.00 16.62  ? 325 HOH C O     1 
HETATM 4011 O  O     . HOH O 5 .   ? 40.124  25.459 6.716  1.00 26.46  ? 326 HOH C O     1 
HETATM 4012 O  O     . HOH O 5 .   ? 26.616  26.127 2.358  1.00 34.35  ? 327 HOH C O     1 
HETATM 4013 O  O     . HOH O 5 .   ? 53.464  42.087 18.238 1.00 30.43  ? 328 HOH C O     1 
HETATM 4014 O  O     . HOH O 5 .   ? 37.740  47.118 2.532  1.00 30.53  ? 329 HOH C O     1 
HETATM 4015 O  O     . HOH O 5 .   ? 26.896  54.095 16.330 1.00 35.18  ? 330 HOH C O     1 
HETATM 4016 O  O     . HOH O 5 .   ? 51.358  36.141 19.749 1.00 28.06  ? 331 HOH C O     1 
HETATM 4017 O  O     . HOH O 5 .   ? 29.207  30.350 25.483 1.00 15.41  ? 332 HOH C O     1 
HETATM 4018 O  O     . HOH O 5 .   ? 43.969  43.352 0.360  1.00 30.47  ? 333 HOH C O     1 
HETATM 4019 O  O     . HOH O 5 .   ? 21.208  46.262 15.483 1.00 16.28  ? 334 HOH C O     1 
HETATM 4020 O  O     . HOH O 5 .   ? 38.616  25.659 16.275 1.00 18.53  ? 335 HOH C O     1 
HETATM 4021 O  O     . HOH O 5 .   ? 21.888  39.061 25.386 1.00 28.37  ? 336 HOH C O     1 
HETATM 4022 O  O     . HOH O 5 .   ? 41.287  25.304 16.943 1.00 24.37  ? 337 HOH C O     1 
HETATM 4023 O  O     . HOH O 5 .   ? 29.884  31.736 3.085  1.00 21.88  ? 338 HOH C O     1 
HETATM 4024 O  O     . HOH O 5 .   ? 50.707  34.461 23.332 1.00 27.66  ? 339 HOH C O     1 
HETATM 4025 O  O     . HOH O 5 .   ? 26.385  49.429 13.489 1.00 26.80  ? 340 HOH C O     1 
HETATM 4026 O  O     . HOH O 5 .   ? 46.465  45.305 7.320  1.00 27.25  ? 341 HOH C O     1 
HETATM 4027 O  O     . HOH O 5 .   ? 36.027  29.305 24.158 1.00 18.40  ? 342 HOH C O     1 
HETATM 4028 O  O     . HOH O 5 .   ? 34.367  35.522 8.161  1.00 16.25  ? 343 HOH C O     1 
HETATM 4029 O  O     . HOH O 5 .   ? 41.762  47.937 23.779 1.00 30.53  ? 344 HOH C O     1 
HETATM 4030 O  O     . HOH O 5 .   ? 36.151  41.553 4.352  1.00 22.17  ? 345 HOH C O     1 
HETATM 4031 O  O     . HOH O 5 .   ? 21.316  29.311 14.410 1.00 32.29  ? 346 HOH C O     1 
HETATM 4032 O  O     . HOH O 5 .   ? 23.894  32.552 21.388 1.00 17.12  ? 347 HOH C O     1 
HETATM 4033 O  O     . HOH O 5 .   ? 38.252  29.509 22.515 1.00 16.77  ? 348 HOH C O     1 
HETATM 4034 O  O     . HOH O 5 .   ? 27.589  37.348 5.544  1.00 28.60  ? 349 HOH C O     1 
HETATM 4035 O  O     . HOH O 5 .   ? 43.600  34.479 8.172  1.00 22.66  ? 350 HOH C O     1 
HETATM 4036 O  O     . HOH O 5 .   ? 27.173  25.622 7.681  1.00 19.52  ? 351 HOH C O     1 
HETATM 4037 O  O     . HOH O 5 .   ? 50.367  33.141 18.252 1.00 23.54  ? 352 HOH C O     1 
HETATM 4038 O  O     . HOH O 5 .   ? 14.339  43.256 7.723  1.00 17.11  ? 353 HOH C O     1 
HETATM 4039 O  O     . HOH O 5 .   ? 43.395  21.270 17.475 1.00 27.35  ? 354 HOH C O     1 
HETATM 4040 O  O     . HOH O 5 .   ? 34.509  33.557 2.021  1.00 32.97  ? 355 HOH C O     1 
HETATM 4041 O  O     . HOH O 5 .   ? 27.960  28.056 22.875 1.00 22.85  ? 356 HOH C O     1 
HETATM 4042 O  O     . HOH O 5 .   ? 22.298  49.992 26.242 1.00 23.93  ? 357 HOH C O     1 
HETATM 4043 O  O     . HOH O 5 .   ? 15.081  34.601 11.983 1.00 32.61  ? 358 HOH C O     1 
HETATM 4044 O  O     . HOH O 5 .   ? 27.000  43.465 0.592  1.00 34.99  ? 359 HOH C O     1 
HETATM 4045 O  O     . HOH O 5 .   ? 39.282  33.303 0.135  1.00 38.25  ? 360 HOH C O     1 
HETATM 4046 O  O     . HOH O 5 .   ? 45.402  47.495 5.554  1.00 36.05  ? 361 HOH C O     1 
HETATM 4047 O  O     . HOH O 5 .   ? 26.139  28.077 16.397 1.00 16.46  ? 362 HOH C O     1 
HETATM 4048 O  O     . HOH O 5 .   ? 43.710  39.096 22.056 1.00 21.71  ? 363 HOH C O     1 
HETATM 4049 O  O     . HOH O 5 .   ? 23.658  32.461 5.333  1.00 19.01  ? 364 HOH C O     1 
HETATM 4050 O  O     . HOH O 5 .   ? 33.076  23.875 5.752  1.00 22.47  ? 365 HOH C O     1 
HETATM 4051 O  O     . HOH O 5 .   ? 21.750  41.495 27.679 1.00 27.16  ? 366 HOH C O     1 
HETATM 4052 O  O     . HOH O 5 .   ? 27.381  58.708 3.681  1.00 43.12  ? 367 HOH C O     1 
HETATM 4053 O  O     . HOH O 5 .   ? 39.354  44.003 3.698  1.00 37.13  ? 368 HOH C O     1 
HETATM 4054 O  O     . HOH O 5 .   ? 21.887  41.365 1.419  1.00 20.48  ? 369 HOH C O     1 
HETATM 4055 O  O     . HOH O 5 .   ? 34.995  8.971  24.189 1.00 27.82  ? 370 HOH C O     1 
HETATM 4056 O  O     . HOH O 5 .   ? 43.629  34.165 5.547  1.00 25.96  ? 371 HOH C O     1 
HETATM 4057 O  O     . HOH O 5 .   ? 17.685  45.420 21.294 1.00 25.64  ? 372 HOH C O     1 
HETATM 4058 O  O     . HOH O 5 .   ? 48.553  28.850 16.244 1.00 32.95  ? 373 HOH C O     1 
HETATM 4059 O  O     . HOH O 5 .   ? 38.958  11.361 25.048 1.00 33.78  ? 374 HOH C O     1 
HETATM 4060 O  O     . HOH O 5 .   ? 41.363  43.152 1.982  1.00 32.47  ? 375 HOH C O     1 
HETATM 4061 O  O     . HOH O 5 .   ? 50.503  32.500 21.491 1.00 25.10  ? 376 HOH C O     1 
HETATM 4062 O  O     . HOH O 5 .   ? 46.113  40.102 2.934  1.00 22.13  ? 377 HOH C O     1 
HETATM 4063 O  O     . HOH O 5 .   ? 38.351  26.752 3.280  1.00 36.00  ? 378 HOH C O     1 
HETATM 4064 O  O     . HOH O 5 .   ? 44.597  21.289 25.046 1.00 33.96  ? 379 HOH C O     1 
HETATM 4065 O  O     . HOH O 5 .   ? 42.316  23.549 18.939 1.00 23.04  ? 380 HOH C O     1 
HETATM 4066 O  O     . HOH O 5 .   ? 23.686  30.371 11.577 1.00 30.54  ? 381 HOH C O     1 
HETATM 4067 O  O     . HOH O 5 .   ? 36.269  45.433 5.604  1.00 28.40  ? 382 HOH C O     1 
HETATM 4068 O  O     . HOH O 5 .   ? 32.955  59.585 12.844 1.00 39.13  ? 383 HOH C O     1 
HETATM 4069 O  O     . HOH O 5 .   ? 46.445  31.643 17.127 1.00 31.04  ? 384 HOH C O     1 
HETATM 4070 O  O     . HOH O 5 .   ? 17.054  44.320 5.458  1.00 21.80  ? 385 HOH C O     1 
HETATM 4071 O  O     . HOH O 5 .   ? 52.805  38.469 6.677  1.00 40.75  ? 386 HOH C O     1 
HETATM 4072 O  O     . HOH O 5 .   ? 49.122  25.696 20.172 1.00 46.78  ? 387 HOH C O     1 
HETATM 4073 O  O     . HOH O 5 .   ? 20.285  34.566 2.384  1.00 36.17  ? 388 HOH C O     1 
HETATM 4074 O  O     . HOH O 5 .   ? 18.502  46.895 4.720  1.00 26.55  ? 389 HOH C O     1 
HETATM 4075 O  O     . HOH O 5 .   ? 21.768  34.478 4.725  1.00 16.86  ? 390 HOH C O     1 
HETATM 4076 O  O     . HOH O 5 .   ? 34.167  45.015 3.842  1.00 35.43  ? 391 HOH C O     1 
HETATM 4077 O  O     . HOH O 5 .   ? 47.364  24.496 24.452 1.00 25.59  ? 392 HOH C O     1 
HETATM 4078 O  O     . HOH O 5 .   ? 48.591  40.464 13.722 1.00 29.37  ? 393 HOH C O     1 
HETATM 4079 O  O     . HOH O 5 .   ? 28.506  23.234 21.605 1.00 22.31  ? 394 HOH C O     1 
HETATM 4080 O  O     . HOH O 5 .   ? 23.692  35.239 1.709  1.00 36.87  ? 395 HOH C O     1 
HETATM 4081 O  O     . HOH O 5 .   ? 24.553  32.016 13.664 1.00 22.52  ? 396 HOH C O     1 
HETATM 4082 O  O     . HOH O 5 .   ? 33.481  41.830 4.700  1.00 25.21  ? 397 HOH C O     1 
HETATM 4083 O  O     . HOH O 5 .   ? 24.811  39.625 1.420  1.00 36.78  ? 398 HOH C O     1 
HETATM 4084 O  O     . HOH O 5 .   ? 44.336  31.969 8.562  1.00 26.77  ? 399 HOH C O     1 
HETATM 4085 O  O     . HOH O 5 .   ? 50.304  41.238 11.657 1.00 39.63  ? 400 HOH C O     1 
HETATM 4086 O  O     . HOH O 5 .   ? 47.183  38.437 9.666  1.00 27.20  ? 401 HOH C O     1 
HETATM 4087 O  O     . HOH O 5 .   ? 15.739  48.524 5.057  1.00 36.63  ? 402 HOH C O     1 
HETATM 4088 O  O     . HOH O 5 .   ? 21.750  33.710 19.999 1.00 22.74  ? 403 HOH C O     1 
HETATM 4089 O  O     . HOH O 5 .   ? 25.726  52.478 6.783  1.00 42.39  ? 404 HOH C O     1 
HETATM 4090 O  O     . HOH O 5 .   ? 40.488  13.669 24.027 1.00 37.62  ? 405 HOH C O     1 
HETATM 4091 O  O     . HOH O 5 .   ? 28.423  54.399 18.282 1.00 40.24  ? 406 HOH C O     1 
HETATM 4092 O  O     . HOH O 5 .   ? 23.127  26.175 3.535  1.00 39.30  ? 407 HOH C O     1 
HETATM 4093 O  O     . HOH O 5 .   ? 42.954  31.291 4.855  1.00 30.01  ? 408 HOH C O     1 
HETATM 4094 O  O     . HOH O 5 .   ? 44.236  41.714 22.741 1.00 30.17  ? 409 HOH C O     1 
HETATM 4095 O  O     . HOH O 5 .   ? 14.027  34.508 14.374 1.00 32.25  ? 410 HOH C O     1 
HETATM 4096 O  O     . HOH O 5 .   ? 26.267  27.995 9.297  1.00 35.28  ? 411 HOH C O     1 
HETATM 4097 O  O     . HOH O 5 .   ? 48.194  46.651 8.984  1.00 39.02  ? 412 HOH C O     1 
HETATM 4098 O  O     . HOH O 5 .   ? 47.721  41.511 4.714  1.00 34.45  ? 413 HOH C O     1 
HETATM 4099 O  O     . HOH O 5 .   ? 24.306  29.878 20.710 1.00 21.12  ? 414 HOH C O     1 
HETATM 4100 O  O     . HOH O 5 .   ? 14.930  42.878 2.803  1.00 41.11  ? 415 HOH C O     1 
HETATM 4101 O  O     . HOH O 5 .   ? 52.502  29.933 21.675 1.00 36.93  ? 416 HOH C O     1 
HETATM 4102 O  O     . HOH O 5 .   ? 36.746  31.562 2.087  1.00 28.76  ? 417 HOH C O     1 
HETATM 4103 O  O     . HOH O 5 .   ? 23.368  32.394 24.048 1.00 21.65  ? 418 HOH C O     1 
HETATM 4104 O  O     . HOH O 5 .   ? 24.056  29.773 24.814 1.00 36.20  ? 419 HOH C O     1 
HETATM 4105 O  O     . HOH O 5 .   ? 46.215  42.508 1.568  1.00 41.38  ? 420 HOH C O     1 
HETATM 4106 O  O     . HOH O 5 .   ? 31.920  55.994 21.694 1.00 33.70  ? 421 HOH C O     1 
HETATM 4107 O  O     . HOH O 5 .   ? 29.266  55.865 22.055 1.00 32.71  ? 422 HOH C O     1 
HETATM 4108 O  O     . HOH O 5 .   ? 23.805  28.788 18.265 1.00 26.47  ? 423 HOH C O     1 
HETATM 4109 O  O     . HOH O 5 .   ? 45.839  35.667 9.468  1.00 29.96  ? 424 HOH C O     1 
HETATM 4110 O  O     . HOH O 5 .   ? 45.148  30.642 6.554  1.00 32.54  ? 425 HOH C O     1 
HETATM 4111 O  O     . HOH O 5 .   ? 44.626  45.808 -0.216 1.00 33.58  ? 426 HOH C O     1 
HETATM 4112 O  O     . HOH O 5 .   ? 48.182  37.582 12.512 1.00 30.71  ? 427 HOH C O     1 
HETATM 4113 O  O     . HOH O 5 .   ? 22.528  30.080 4.414  1.00 35.19  ? 428 HOH C O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . HIS A 8   ? 0.6583 0.6012 0.6796 0.0631  -0.0388 0.0202  25  HIS A N   
2    C CA  . HIS A 8   ? 0.5591 0.5072 0.5823 0.0660  -0.0402 0.0160  25  HIS A CA  
3    C C   . HIS A 8   ? 0.4767 0.4313 0.5039 0.0663  -0.0384 0.0143  25  HIS A C   
4    O O   . HIS A 8   ? 0.4828 0.4397 0.5105 0.0644  -0.0360 0.0154  25  HIS A O   
5    C CB  . HIS A 8   ? 0.5759 0.5244 0.5969 0.0684  -0.0422 0.0144  25  HIS A CB  
6    N N   . VAL A 9   ? 0.4539 0.4126 0.4836 0.0673  -0.0387 0.0115  26  VAL A N   
7    C CA  . VAL A 9   ? 0.3049 0.2715 0.3381 0.0660  -0.0358 0.0096  26  VAL A CA  
8    C C   . VAL A 9   ? 0.2749 0.2474 0.3086 0.0685  -0.0366 0.0061  26  VAL A C   
9    O O   . VAL A 9   ? 0.3041 0.2748 0.3359 0.0718  -0.0397 0.0046  26  VAL A O   
10   C CB  . VAL A 9   ? 0.3180 0.2869 0.3538 0.0653  -0.0353 0.0083  26  VAL A CB  
11   C CG1 . VAL A 9   ? 0.3667 0.3298 0.4020 0.0628  -0.0345 0.0118  26  VAL A CG1 
12   C CG2 . VAL A 9   ? 0.3616 0.3312 0.3975 0.0690  -0.0385 0.0050  26  VAL A CG2 
13   N N   . GLU A 10  ? 0.2172 0.1967 0.2534 0.0669  -0.0339 0.0049  27  GLU A N   
14   C CA  . GLU A 10  ? 0.2371 0.2233 0.2743 0.0689  -0.0342 0.0013  27  GLU A CA  
15   C C   . GLU A 10  ? 0.1882 0.1819 0.2289 0.0675  -0.0322 -0.0010 27  GLU A C   
16   O O   . GLU A 10  ? 0.1917 0.1847 0.2338 0.0651  -0.0305 0.0003  27  GLU A O   
17   C CB  . GLU A 10  ? 0.3335 0.3207 0.3694 0.0682  -0.0331 0.0023  27  GLU A CB  
18   C CG  . GLU A 10  ? 0.2496 0.2389 0.2869 0.0644  -0.0293 0.0043  27  GLU A CG  
19   C CD  . GLU A 10  ? 0.3534 0.3415 0.3890 0.0635  -0.0283 0.0063  27  GLU A CD  
20   O OE1 . GLU A 10  ? 0.4987 0.4833 0.5316 0.0657  -0.0306 0.0065  27  GLU A OE1 
21   O OE2 . GLU A 10  ? 0.2548 0.2453 0.2914 0.0606  -0.0252 0.0075  27  GLU A OE2 
22   N N   . GLN A 11  ? 0.1873 0.1879 0.2292 0.0691  -0.0324 -0.0046 28  GLN A N   
23   C CA  . GLN A 11  ? 0.1814 0.1897 0.2265 0.0679  -0.0306 -0.0072 28  GLN A CA  
24   C C   . GLN A 11  ? 0.1757 0.1902 0.2216 0.0666  -0.0284 -0.0080 28  GLN A C   
25   O O   . GLN A 11  ? 0.2136 0.2287 0.2581 0.0684  -0.0294 -0.0087 28  GLN A O   
26   C CB  . GLN A 11  ? 0.1776 0.1897 0.2237 0.0712  -0.0331 -0.0112 28  GLN A CB  
27   C CG  . GLN A 11  ? 0.2290 0.2357 0.2747 0.0722  -0.0351 -0.0106 28  GLN A CG  
28   C CD  . GLN A 11  ? 0.3092 0.3199 0.3563 0.0750  -0.0372 -0.0145 28  GLN A CD  
29   O OE1 . GLN A 11  ? 0.2921 0.3093 0.3402 0.0768  -0.0377 -0.0180 28  GLN A OE1 
30   N NE2 . GLN A 11  ? 0.3020 0.3085 0.3490 0.0754  -0.0385 -0.0141 28  GLN A NE2 
31   N N   . THR A 12  ? 0.1574 0.1762 0.2056 0.0634  -0.0254 -0.0078 29  THR A N   
32   C CA  . THR A 12  ? 0.1577 0.1826 0.2068 0.0619  -0.0233 -0.0088 29  THR A CA  
33   C C   . THR A 12  ? 0.1551 0.1882 0.2070 0.0612  -0.0223 -0.0120 29  THR A C   
34   O O   . THR A 12  ? 0.1640 0.1974 0.2173 0.0608  -0.0224 -0.0126 29  THR A O   
35   C CB  . THR A 12  ? 0.1789 0.2015 0.2278 0.0582  -0.0203 -0.0052 29  THR A CB  
36   O OG1 . THR A 12  ? 0.1822 0.2098 0.2312 0.0574  -0.0188 -0.0061 29  THR A OG1 
37   C CG2 . THR A 12  ? 0.1445 0.1674 0.1953 0.0550  -0.0181 -0.0039 29  THR A CG2 
38   N N   . TYR A 13  ? 0.1460 0.1856 0.1985 0.0611  -0.0215 -0.0141 30  TYR A N   
39   C CA  . TYR A 13  ? 0.1184 0.1662 0.1733 0.0600  -0.0203 -0.0171 30  TYR A CA  
40   C C   . TYR A 13  ? 0.1504 0.2001 0.2064 0.0557  -0.0169 -0.0152 30  TYR A C   
41   O O   . TYR A 13  ? 0.1517 0.2006 0.2067 0.0545  -0.0155 -0.0136 30  TYR A O   
42   C CB  . TYR A 13  ? 0.1375 0.1919 0.1926 0.0624  -0.0215 -0.0208 30  TYR A CB  
43   C CG  . TYR A 13  ? 0.1490 0.2122 0.2065 0.0610  -0.0202 -0.0238 30  TYR A CG  
44   C CD1 . TYR A 13  ? 0.1498 0.2160 0.2091 0.0617  -0.0211 -0.0261 30  TYR A CD1 
45   C CD2 . TYR A 13  ? 0.1316 0.2003 0.1897 0.0587  -0.0180 -0.0242 30  TYR A CD2 
46   C CE1 . TYR A 13  ? 0.1451 0.2194 0.2065 0.0602  -0.0199 -0.0287 30  TYR A CE1 
47   C CE2 . TYR A 13  ? 0.1261 0.2029 0.1862 0.0571  -0.0168 -0.0269 30  TYR A CE2 
48   C CZ  . TYR A 13  ? 0.1380 0.2176 0.1998 0.0578  -0.0178 -0.0291 30  TYR A CZ  
49   O OH  . TYR A 13  ? 0.1570 0.2447 0.2208 0.0560  -0.0166 -0.0317 30  TYR A OH  
50   N N   . LEU A 14  ? 0.1283 0.1797 0.1862 0.0535  -0.0156 -0.0152 31  LEU A N   
51   C CA  . LEU A 14  ? 0.1267 0.1802 0.1857 0.0494  -0.0125 -0.0137 31  LEU A CA  
52   C C   . LEU A 14  ? 0.1531 0.2147 0.2142 0.0483  -0.0118 -0.0169 31  LEU A C   
53   O O   . LEU A 14  ? 0.1787 0.2424 0.2409 0.0498  -0.0133 -0.0191 31  LEU A O   
54   C CB  . LEU A 14  ? 0.1374 0.1846 0.1965 0.0471  -0.0114 -0.0103 31  LEU A CB  
55   C CG  . LEU A 14  ? 0.1621 0.2016 0.2191 0.0472  -0.0114 -0.0066 31  LEU A CG  
56   C CD1 . LEU A 14  ? 0.1878 0.2210 0.2447 0.0464  -0.0115 -0.0040 31  LEU A CD1 
57   C CD2 . LEU A 14  ? 0.2183 0.2582 0.2749 0.0445  -0.0089 -0.0047 31  LEU A CD2 
58   N N   . MET A 15  ? 0.1234 0.1900 0.1851 0.0458  -0.0098 -0.0173 32  MET A N   
59   C CA  . MET A 15  ? 0.1171 0.1919 0.1807 0.0446  -0.0091 -0.0204 32  MET A CA  
60   C C   . MET A 15  ? 0.1193 0.1952 0.1836 0.0401  -0.0062 -0.0186 32  MET A C   
61   O O   . MET A 15  ? 0.1315 0.2063 0.1950 0.0384  -0.0047 -0.0168 32  MET A O   
62   C CB  . MET A 15  ? 0.1413 0.2225 0.2046 0.0463  -0.0098 -0.0235 32  MET A CB  
63   C CG  . MET A 15  ? 0.1634 0.2534 0.2285 0.0449  -0.0091 -0.0267 32  MET A CG  
64   S SD  . MET A 15  ? 0.1904 0.2880 0.2553 0.0480  -0.0108 -0.0309 32  MET A SD  
65   C CE  . MET A 15  ? 0.1952 0.2895 0.2580 0.0477  -0.0100 -0.0287 32  MET A CE  
66   N N   . ILE A 16  ? 0.1133 0.1913 0.1794 0.0383  -0.0056 -0.0191 33  ILE A N   
67   C CA  . ILE A 16  ? 0.1244 0.2042 0.1913 0.0341  -0.0030 -0.0179 33  ILE A CA  
68   C C   . ILE A 16  ? 0.1196 0.2080 0.1871 0.0330  -0.0024 -0.0208 33  ILE A C   
69   O O   . ILE A 16  ? 0.1269 0.2211 0.1953 0.0344  -0.0036 -0.0242 33  ILE A O   
70   C CB  . ILE A 16  ? 0.0983 0.1771 0.1666 0.0323  -0.0026 -0.0172 33  ILE A CB  
71   C CG1 . ILE A 16  ? 0.1305 0.2008 0.1982 0.0334  -0.0033 -0.0143 33  ILE A CG1 
72   C CG2 . ILE A 16  ? 0.1098 0.1904 0.1787 0.0279  0.0000  -0.0159 33  ILE A CG2 
73   C CD1 . ILE A 16  ? 0.1337 0.2023 0.2027 0.0319  -0.0029 -0.0134 33  ILE A CD1 
74   N N   . LYS A 17  ? 0.1203 0.2094 0.1870 0.0307  -0.0007 -0.0197 34  LYS A N   
75   C CA  . LYS A 17  ? 0.1295 0.2261 0.1963 0.0295  0.0000  -0.0221 34  LYS A CA  
76   C C   . LYS A 17  ? 0.1185 0.2200 0.1868 0.0261  0.0013  -0.0231 34  LYS A C   
77   O O   . LYS A 17  ? 0.1062 0.2048 0.1753 0.0245  0.0019  -0.0215 34  LYS A O   
78   C CB  . LYS A 17  ? 0.1406 0.2355 0.2060 0.0283  0.0013  -0.0203 34  LYS A CB  
79   C CG  . LYS A 17  ? 0.1440 0.2343 0.2077 0.0314  0.0001  -0.0193 34  LYS A CG  
80   C CD  . LYS A 17  ? 0.1462 0.2347 0.2085 0.0300  0.0016  -0.0174 34  LYS A CD  
81   C CE  . LYS A 17  ? 0.1710 0.2559 0.2317 0.0332  0.0002  -0.0168 34  LYS A CE  
82   N NZ  . LYS A 17  ? 0.1931 0.2772 0.2524 0.0317  0.0017  -0.0154 34  LYS A NZ  
83   N N   . PRO A 18  ? 0.1121 0.2213 0.1807 0.0249  0.0017  -0.0257 35  PRO A N   
84   C CA  . PRO A 18  ? 0.1177 0.2320 0.1876 0.0216  0.0028  -0.0268 35  PRO A CA  
85   C C   . PRO A 18  ? 0.1192 0.2295 0.1890 0.0177  0.0048  -0.0236 35  PRO A C   
86   O O   . PRO A 18  ? 0.1198 0.2313 0.1907 0.0156  0.0053  -0.0236 35  PRO A O   
87   C CB  . PRO A 18  ? 0.1371 0.2598 0.2069 0.0210  0.0029  -0.0298 35  PRO A CB  
88   C CG  . PRO A 18  ? 0.1367 0.2600 0.2059 0.0253  0.0011  -0.0315 35  PRO A CG  
89   C CD  . PRO A 18  ? 0.1331 0.2473 0.2010 0.0267  0.0010  -0.0282 35  PRO A CD  
90   N N   . ASP A 19  ? 0.1243 0.2298 0.1928 0.0168  0.0059  -0.0209 36  ASP A N   
91   C CA  . ASP A 19  ? 0.1405 0.2420 0.2089 0.0134  0.0077  -0.0179 36  ASP A CA  
92   C C   . ASP A 19  ? 0.1166 0.2119 0.1857 0.0139  0.0074  -0.0158 36  ASP A C   
93   O O   . ASP A 19  ? 0.1407 0.2347 0.2104 0.0110  0.0085  -0.0143 36  ASP A O   
94   C CB  . ASP A 19  ? 0.1519 0.2499 0.2187 0.0125  0.0088  -0.0157 36  ASP A CB  
95   C CG  . ASP A 19  ? 0.1680 0.2612 0.2337 0.0158  0.0079  -0.0146 36  ASP A CG  
96   O OD1 . ASP A 19  ? 0.1931 0.2881 0.2588 0.0192  0.0061  -0.0166 36  ASP A OD1 
97   O OD2 . ASP A 19  ? 0.1553 0.2432 0.2199 0.0151  0.0089  -0.0118 36  ASP A OD2 
98   N N   . GLY A 20  ? 0.1093 0.2008 0.1782 0.0174  0.0059  -0.0155 37  GLY A N   
99   C CA  . GLY A 20  ? 0.1222 0.2083 0.1917 0.0179  0.0055  -0.0137 37  GLY A CA  
100  C C   . GLY A 20  ? 0.1105 0.2006 0.1818 0.0173  0.0049  -0.0157 37  GLY A C   
101  O O   . GLY A 20  ? 0.1344 0.2216 0.2065 0.0156  0.0055  -0.0141 37  GLY A O   
102  N N   . ILE A 21  ? 0.1055 0.2024 0.1773 0.0187  0.0038  -0.0193 38  ILE A N   
103  C CA  . ILE A 21  ? 0.0973 0.1990 0.1707 0.0180  0.0034  -0.0215 38  ILE A CA  
104  C C   . ILE A 21  ? 0.1022 0.2068 0.1761 0.0135  0.0053  -0.0210 38  ILE A C   
105  O O   . ILE A 21  ? 0.1102 0.2139 0.1852 0.0117  0.0057  -0.0203 38  ILE A O   
106  C CB  . ILE A 21  ? 0.1326 0.2415 0.2064 0.0205  0.0019  -0.0256 38  ILE A CB  
107  C CG1 . ILE A 21  ? 0.1636 0.2697 0.2367 0.0252  -0.0002 -0.0263 38  ILE A CG1 
108  C CG2 . ILE A 21  ? 0.1451 0.2592 0.2207 0.0198  0.0014  -0.0280 38  ILE A CG2 
109  C CD1 . ILE A 21  ? 0.2126 0.3127 0.2861 0.0273  -0.0015 -0.0251 38  ILE A CD1 
110  N N   . GLN A 22  ? 0.1123 0.2204 0.1855 0.0115  0.0064  -0.0214 39  GLN A N   
111  C CA  . GLN A 22  ? 0.1229 0.2347 0.1963 0.0071  0.0079  -0.0214 39  GLN A CA  
112  C C   . GLN A 22  ? 0.1290 0.2345 0.2022 0.0044  0.0094  -0.0177 39  GLN A C   
113  O O   . GLN A 22  ? 0.1603 0.2673 0.2341 0.0012  0.0103  -0.0174 39  GLN A O   
114  C CB  . GLN A 22  ? 0.1254 0.2425 0.1978 0.0059  0.0086  -0.0228 39  GLN A CB  
115  C CG  . GLN A 22  ? 0.1544 0.2796 0.2274 0.0076  0.0074  -0.0268 39  GLN A CG  
116  C CD  . GLN A 22  ? 0.1758 0.3074 0.2499 0.0050  0.0076  -0.0289 39  GLN A CD  
117  O OE1 . GLN A 22  ? 0.2048 0.3344 0.2793 0.0022  0.0086  -0.0272 39  GLN A OE1 
118  N NE2 . GLN A 22  ? 0.1868 0.3263 0.2614 0.0060  0.0068  -0.0325 39  GLN A NE2 
119  N N   . ARG A 23  ? 0.1047 0.2032 0.1770 0.0055  0.0096  -0.0150 40  ARG A N   
120  C CA  . ARG A 23  ? 0.1165 0.2088 0.1886 0.0032  0.0109  -0.0115 40  ARG A CA  
121  C C   . ARG A 23  ? 0.1294 0.2176 0.2027 0.0042  0.0103  -0.0104 40  ARG A C   
122  O O   . ARG A 23  ? 0.1344 0.2176 0.2078 0.0024  0.0113  -0.0077 40  ARG A O   
123  C CB  . ARG A 23  ? 0.1380 0.2251 0.2087 0.0039  0.0115  -0.0091 40  ARG A CB  
124  C CG  . ARG A 23  ? 0.1490 0.2400 0.2186 0.0023  0.0124  -0.0100 40  ARG A CG  
125  C CD  . ARG A 23  ? 0.1482 0.2345 0.2164 0.0032  0.0129  -0.0079 40  ARG A CD  
126  N NE  . ARG A 23  ? 0.1606 0.2408 0.2286 0.0013  0.0141  -0.0046 40  ARG A NE  
127  C CZ  . ARG A 23  ? 0.1297 0.2041 0.1968 0.0022  0.0145  -0.0022 40  ARG A CZ  
128  N NH1 . ARG A 23  ? 0.1599 0.2335 0.2260 0.0050  0.0138  -0.0025 40  ARG A NH1 
129  N NH2 . ARG A 23  ? 0.1598 0.2292 0.2269 0.0003  0.0156  0.0006  40  ARG A NH2 
130  N N   . GLN A 24  ? 0.1209 0.2112 0.1949 0.0070  0.0087  -0.0126 41  GLN A N   
131  C CA  . GLN A 24  ? 0.1541 0.2416 0.2293 0.0080  0.0079  -0.0122 41  GLN A CA  
132  C C   . GLN A 24  ? 0.1238 0.2027 0.1984 0.0090  0.0079  -0.0088 41  GLN A C   
133  O O   . GLN A 24  ? 0.1278 0.2030 0.2030 0.0075  0.0085  -0.0068 41  GLN A O   
134  C CB  . GLN A 24  ? 0.1585 0.2490 0.2349 0.0047  0.0087  -0.0125 41  GLN A CB  
135  C CG  . GLN A 24  ? 0.1667 0.2661 0.2435 0.0038  0.0085  -0.0160 41  GLN A CG  
136  C CD  . GLN A 24  ? 0.1799 0.2829 0.2583 0.0027  0.0081  -0.0176 41  GLN A CD  
137  O OE1 . GLN A 24  ? 0.1777 0.2821 0.2564 -0.0009 0.0093  -0.0170 41  GLN A OE1 
138  N NE2 . GLN A 24  ? 0.1583 0.2628 0.2375 0.0058  0.0065  -0.0197 41  GLN A NE2 
139  N N   . VAL A 25  ? 0.1029 0.1789 0.1764 0.0115  0.0073  -0.0082 42  VAL A N   
140  C CA  . VAL A 25  ? 0.0925 0.1606 0.1651 0.0129  0.0072  -0.0052 42  VAL A CA  
141  C C   . VAL A 25  ? 0.0887 0.1551 0.1610 0.0170  0.0050  -0.0062 42  VAL A C   
142  O O   . VAL A 25  ? 0.1108 0.1712 0.1820 0.0185  0.0046  -0.0040 42  VAL A O   
143  C CB  . VAL A 25  ? 0.1100 0.1751 0.1813 0.0118  0.0085  -0.0029 42  VAL A CB  
144  C CG1 . VAL A 25  ? 0.1479 0.2138 0.2195 0.0078  0.0104  -0.0017 42  VAL A CG1 
145  C CG2 . VAL A 25  ? 0.1376 0.2062 0.2079 0.0134  0.0080  -0.0047 42  VAL A CG2 
146  N N   . VAL A 26  ? 0.1074 0.1786 0.1805 0.0186  0.0036  -0.0093 43  VAL A N   
147  C CA  . VAL A 26  ? 0.1005 0.1701 0.1732 0.0226  0.0014  -0.0105 43  VAL A CA  
148  C C   . VAL A 26  ? 0.1047 0.1669 0.1773 0.0235  0.0008  -0.0080 43  VAL A C   
149  O O   . VAL A 26  ? 0.1068 0.1640 0.1781 0.0259  -0.0004 -0.0068 43  VAL A O   
150  C CB  . VAL A 26  ? 0.1093 0.1857 0.1832 0.0240  0.0000  -0.0144 43  VAL A CB  
151  C CG1 . VAL A 26  ? 0.1210 0.1950 0.1946 0.0281  -0.0024 -0.0155 43  VAL A CG1 
152  C CG2 . VAL A 26  ? 0.1310 0.2147 0.2048 0.0235  0.0004  -0.0171 43  VAL A CG2 
153  N N   . GLY A 27  ? 0.0898 0.1512 0.1635 0.0214  0.0014  -0.0071 44  GLY A N   
154  C CA  . GLY A 27  ? 0.0991 0.1539 0.1728 0.0220  0.0009  -0.0048 44  GLY A CA  
155  C C   . GLY A 27  ? 0.0904 0.1386 0.1628 0.0215  0.0018  -0.0012 44  GLY A C   
156  O O   . GLY A 27  ? 0.0952 0.1377 0.1667 0.0234  0.0007  0.0004  44  GLY A O   
157  N N   . GLU A 28  ? 0.1025 0.1512 0.1747 0.0188  0.0038  0.0002  45  GLU A N   
158  C CA  . GLU A 28  ? 0.1074 0.1503 0.1784 0.0181  0.0048  0.0035  45  GLU A CA  
159  C C   . GLU A 28  ? 0.1057 0.1465 0.1751 0.0211  0.0035  0.0035  45  GLU A C   
160  O O   . GLU A 28  ? 0.1292 0.1639 0.1974 0.0218  0.0033  0.0061  45  GLU A O   
161  C CB  . GLU A 28  ? 0.1571 0.2016 0.2282 0.0149  0.0069  0.0045  45  GLU A CB  
162  C CG  . GLU A 28  ? 0.1535 0.1980 0.2259 0.0117  0.0084  0.0057  45  GLU A CG  
163  C CD  . GLU A 28  ? 0.2628 0.3077 0.3348 0.0090  0.0103  0.0070  45  GLU A CD  
164  O OE1 . GLU A 28  ? 0.3052 0.3452 0.3763 0.0088  0.0110  0.0096  45  GLU A OE1 
165  O OE2 . GLU A 28  ? 0.3057 0.3558 0.3781 0.0072  0.0110  0.0053  45  GLU A OE2 
166  N N   . ILE A 29  ? 0.1126 0.1583 0.1816 0.0226  0.0028  0.0008  46  ILE A N   
167  C CA  . ILE A 29  ? 0.1107 0.1548 0.1781 0.0254  0.0015  0.0006  46  ILE A CA  
168  C C   . ILE A 29  ? 0.0938 0.1337 0.1606 0.0284  -0.0007 0.0006  46  ILE A C   
169  O O   . ILE A 29  ? 0.1311 0.1654 0.1963 0.0297  -0.0014 0.0027  46  ILE A O   
170  C CB  . ILE A 29  ? 0.1033 0.1540 0.1706 0.0264  0.0011  -0.0026 46  ILE A CB  
171  C CG1 . ILE A 29  ? 0.1366 0.1905 0.2039 0.0234  0.0033  -0.0023 46  ILE A CG1 
172  C CG2 . ILE A 29  ? 0.1393 0.1884 0.2049 0.0298  -0.0007 -0.0033 46  ILE A CG2 
173  C CD1 . ILE A 29  ? 0.1532 0.2147 0.2208 0.0237  0.0031  -0.0056 46  ILE A CD1 
174  N N   . ILE A 30  ? 0.1042 0.1468 0.1721 0.0295  -0.0020 -0.0017 47  ILE A N   
175  C CA  . ILE A 30  ? 0.1051 0.1438 0.1725 0.0324  -0.0043 -0.0018 47  ILE A CA  
176  C C   . ILE A 30  ? 0.1105 0.1418 0.1774 0.0315  -0.0039 0.0018  47  ILE A C   
177  O O   . ILE A 30  ? 0.1275 0.1534 0.1928 0.0336  -0.0054 0.0031  47  ILE A O   
178  C CB  . ILE A 30  ? 0.1016 0.1448 0.1706 0.0332  -0.0054 -0.0049 47  ILE A CB  
179  C CG1 . ILE A 30  ? 0.0998 0.1501 0.1691 0.0348  -0.0062 -0.0086 47  ILE A CG1 
180  C CG2 . ILE A 30  ? 0.1063 0.1448 0.1749 0.0358  -0.0077 -0.0047 47  ILE A CG2 
181  C CD1 . ILE A 30  ? 0.1283 0.1845 0.1994 0.0349  -0.0068 -0.0118 47  ILE A CD1 
182  N N   . SER A 31  ? 0.1015 0.1323 0.1695 0.0283  -0.0020 0.0035  48  SER A N   
183  C CA  . SER A 31  ? 0.0947 0.1188 0.1623 0.0272  -0.0015 0.0069  48  SER A CA  
184  C C   . SER A 31  ? 0.1225 0.1417 0.1882 0.0276  -0.0012 0.0096  48  SER A C   
185  O O   . SER A 31  ? 0.1410 0.1541 0.2057 0.0281  -0.0019 0.0118  48  SER A O   
186  C CB  . SER A 31  ? 0.1226 0.1475 0.1918 0.0236  0.0006  0.0083  48  SER A CB  
187  O OG  . SER A 31  ? 0.1245 0.1523 0.1953 0.0233  0.0002  0.0065  48  SER A OG  
188  N N   . ARG A 32  ? 0.1098 0.1314 0.1749 0.0270  -0.0002 0.0094  49  ARG A N   
189  C CA  . ARG A 32  ? 0.1154 0.1325 0.1787 0.0272  0.0002  0.0119  49  ARG A CA  
190  C C   . ARG A 32  ? 0.1552 0.1687 0.2167 0.0305  -0.0022 0.0117  49  ARG A C   
191  O O   . ARG A 32  ? 0.1401 0.1479 0.2000 0.0307  -0.0025 0.0144  49  ARG A O   
192  C CB  . ARG A 32  ? 0.1414 0.1620 0.2044 0.0262  0.0016  0.0114  49  ARG A CB  
193  C CG  . ARG A 32  ? 0.1404 0.1629 0.2047 0.0228  0.0040  0.0122  49  ARG A CG  
194  C CD  . ARG A 32  ? 0.2775 0.3015 0.3410 0.0219  0.0053  0.0126  49  ARG A CD  
195  N NE  . ARG A 32  ? 0.2408 0.2663 0.3052 0.0186  0.0075  0.0135  49  ARG A NE  
196  C CZ  . ARG A 32  ? 0.2184 0.2431 0.2822 0.0172  0.0091  0.0151  49  ARG A CZ  
197  N NH1 . ARG A 32  ? 0.1968 0.2191 0.2589 0.0185  0.0088  0.0160  49  ARG A NH1 
198  N NH2 . ARG A 32  ? 0.2448 0.2709 0.3095 0.0143  0.0109  0.0156  49  ARG A NH2 
199  N N   . PHE A 33  ? 0.1439 0.1607 0.2054 0.0330  -0.0041 0.0087  50  PHE A N   
200  C CA  . PHE A 33  ? 0.1257 0.1392 0.1854 0.0363  -0.0066 0.0083  50  PHE A CA  
201  C C   . PHE A 33  ? 0.1293 0.1381 0.1889 0.0373  -0.0082 0.0091  50  PHE A C   
202  O O   . PHE A 33  ? 0.1485 0.1514 0.2062 0.0386  -0.0096 0.0110  50  PHE A O   
203  C CB  . PHE A 33  ? 0.1306 0.1495 0.1904 0.0388  -0.0081 0.0047  50  PHE A CB  
204  C CG  . PHE A 33  ? 0.1423 0.1650 0.2017 0.0381  -0.0068 0.0041  50  PHE A CG  
205  C CD1 . PHE A 33  ? 0.1597 0.1790 0.2172 0.0388  -0.0069 0.0058  50  PHE A CD1 
206  C CD2 . PHE A 33  ? 0.1868 0.2163 0.2478 0.0367  -0.0055 0.0019  50  PHE A CD2 
207  C CE1 . PHE A 33  ? 0.1608 0.1834 0.2178 0.0381  -0.0056 0.0053  50  PHE A CE1 
208  C CE2 . PHE A 33  ? 0.1905 0.2234 0.2511 0.0359  -0.0043 0.0015  50  PHE A CE2 
209  C CZ  . PHE A 33  ? 0.1556 0.1850 0.2143 0.0366  -0.0043 0.0032  50  PHE A CZ  
210  N N   . GLU A 34  ? 0.1348 0.1460 0.1963 0.0364  -0.0080 0.0080  51  GLU A N   
211  C CA  . GLU A 34  ? 0.1414 0.1481 0.2028 0.0370  -0.0093 0.0089  51  GLU A CA  
212  C C   . GLU A 34  ? 0.1398 0.1401 0.2004 0.0351  -0.0083 0.0129  51  GLU A C   
213  O O   . GLU A 34  ? 0.1583 0.1531 0.2177 0.0361  -0.0098 0.0143  51  GLU A O   
214  C CB  . GLU A 34  ? 0.1405 0.1510 0.2043 0.0358  -0.0088 0.0073  51  GLU A CB  
215  C CG  . GLU A 34  ? 0.1536 0.1696 0.2182 0.0381  -0.0105 0.0033  51  GLU A CG  
216  C CD  . GLU A 34  ? 0.1420 0.1617 0.2090 0.0365  -0.0098 0.0019  51  GLU A CD  
217  O OE1 . GLU A 34  ? 0.1682 0.1909 0.2365 0.0335  -0.0075 0.0024  51  GLU A OE1 
218  O OE2 . GLU A 34  ? 0.1531 0.1722 0.2204 0.0384  -0.0117 0.0005  51  GLU A OE2 
219  N N   . LYS A 35  ? 0.1271 0.1282 0.1883 0.0323  -0.0057 0.0147  52  LYS A N   
220  C CA  . LYS A 35  ? 0.1291 0.1248 0.1896 0.0303  -0.0045 0.0184  52  LYS A CA  
221  C C   . LYS A 35  ? 0.1470 0.1370 0.2050 0.0318  -0.0058 0.0203  52  LYS A C   
222  O O   . LYS A 35  ? 0.1567 0.1415 0.2140 0.0309  -0.0057 0.0231  52  LYS A O   
223  C CB  . LYS A 35  ? 0.1376 0.1357 0.1991 0.0274  -0.0017 0.0195  52  LYS A CB  
224  C CG  . LYS A 35  ? 0.1819 0.1758 0.2436 0.0249  -0.0001 0.0228  52  LYS A CG  
225  C CD  . LYS A 35  ? 0.2622 0.2590 0.3249 0.0223  0.0025  0.0234  52  LYS A CD  
226  C CE  . LYS A 35  ? 0.3988 0.3931 0.4625 0.0195  0.0042  0.0260  52  LYS A CE  
227  N NZ  . LYS A 35  ? 0.3611 0.3574 0.4267 0.0186  0.0042  0.0249  52  LYS A NZ  
228  N N   . ARG A 36  ? 0.1448 0.1356 0.2013 0.0340  -0.0071 0.0190  53  ARG A N   
229  C CA  . ARG A 36  ? 0.1398 0.1251 0.1936 0.0355  -0.0085 0.0208  53  ARG A CA  
230  C C   . ARG A 36  ? 0.1386 0.1207 0.1911 0.0383  -0.0116 0.0199  53  ARG A C   
231  O O   . ARG A 36  ? 0.1682 0.1458 0.2183 0.0399  -0.0132 0.0211  53  ARG A O   
232  C CB  . ARG A 36  ? 0.1316 0.1190 0.1842 0.0364  -0.0083 0.0202  53  ARG A CB  
233  C CG  . ARG A 36  ? 0.1496 0.1392 0.2030 0.0337  -0.0054 0.0215  53  ARG A CG  
234  C CD  . ARG A 36  ? 0.1641 0.1549 0.2161 0.0344  -0.0052 0.0212  53  ARG A CD  
235  N NE  . ARG A 36  ? 0.1491 0.1343 0.1985 0.0353  -0.0062 0.0236  53  ARG A NE  
236  C CZ  . ARG A 36  ? 0.1687 0.1539 0.2165 0.0358  -0.0061 0.0240  53  ARG A CZ  
237  N NH1 . ARG A 36  ? 0.1849 0.1752 0.2334 0.0358  -0.0052 0.0220  53  ARG A NH1 
238  N NH2 . ARG A 36  ? 0.1842 0.1640 0.2296 0.0362  -0.0069 0.0263  53  ARG A NH2 
239  N N   . GLY A 37  ? 0.1557 0.1400 0.2098 0.0391  -0.0125 0.0178  54  GLY A N   
240  C CA  . GLY A 37  ? 0.1543 0.1358 0.2072 0.0421  -0.0156 0.0166  54  GLY A CA  
241  C C   . GLY A 37  ? 0.1349 0.1194 0.1870 0.0452  -0.0175 0.0135  54  GLY A C   
242  O O   . GLY A 37  ? 0.1746 0.1557 0.2250 0.0479  -0.0203 0.0129  54  GLY A O   
243  N N   . TYR A 38  ? 0.1395 0.1300 0.1926 0.0449  -0.0162 0.0117  55  TYR A N   
244  C CA  . TYR A 38  ? 0.1580 0.1523 0.2108 0.0478  -0.0180 0.0085  55  TYR A CA  
245  C C   . TYR A 38  ? 0.1678 0.1659 0.2223 0.0493  -0.0193 0.0052  55  TYR A C   
246  O O   . TYR A 38  ? 0.1695 0.1705 0.2261 0.0473  -0.0178 0.0049  55  TYR A O   
247  C CB  . TYR A 38  ? 0.1498 0.1496 0.2032 0.0468  -0.0161 0.0075  55  TYR A CB  
248  C CG  . TYR A 38  ? 0.1237 0.1203 0.1753 0.0457  -0.0149 0.0103  55  TYR A CG  
249  C CD1 . TYR A 38  ? 0.1992 0.1893 0.2483 0.0470  -0.0165 0.0124  55  TYR A CD1 
250  C CD2 . TYR A 38  ? 0.1398 0.1402 0.1923 0.0435  -0.0123 0.0106  55  TYR A CD2 
251  C CE1 . TYR A 38  ? 0.1680 0.1556 0.2155 0.0459  -0.0154 0.0149  55  TYR A CE1 
252  C CE2 . TYR A 38  ? 0.1675 0.1654 0.2184 0.0425  -0.0113 0.0130  55  TYR A CE2 
253  C CZ  . TYR A 38  ? 0.1466 0.1382 0.1951 0.0437  -0.0128 0.0151  55  TYR A CZ  
254  O OH  . TYR A 38  ? 0.1780 0.1674 0.2250 0.0427  -0.0117 0.0173  55  TYR A OH  
255  N N   . ARG A 39  ? 0.1380 0.1361 0.1915 0.0528  -0.0222 0.0029  56  ARG A N   
256  C CA  . ARG A 39  ? 0.1599 0.1609 0.2147 0.0548  -0.0239 -0.0003 56  ARG A CA  
257  C C   . ARG A 39  ? 0.1699 0.1793 0.2262 0.0558  -0.0237 -0.0041 56  ARG A C   
258  O O   . ARG A 39  ? 0.1596 0.1706 0.2148 0.0574  -0.0243 -0.0051 56  ARG A O   
259  C CB  . ARG A 39  ? 0.1703 0.1658 0.2229 0.0582  -0.0274 -0.0006 56  ARG A CB  
260  C CG  . ARG A 39  ? 0.1843 0.1818 0.2380 0.0604  -0.0295 -0.0037 56  ARG A CG  
261  C CD  . ARG A 39  ? 0.1846 0.1759 0.2358 0.0638  -0.0331 -0.0038 56  ARG A CD  
262  N NE  . ARG A 39  ? 0.1656 0.1576 0.2151 0.0669  -0.0351 -0.0056 56  ARG A NE  
263  C CZ  . ARG A 39  ? 0.1903 0.1878 0.2407 0.0698  -0.0367 -0.0096 56  ARG A CZ  
264  N NH1 . ARG A 39  ? 0.2186 0.2220 0.2716 0.0699  -0.0365 -0.0125 56  ARG A NH1 
265  N NH2 . ARG A 39  ? 0.2598 0.2571 0.3084 0.0726  -0.0387 -0.0108 56  ARG A NH2 
266  N N   . ILE A 40  ? 0.1334 0.1482 0.1921 0.0548  -0.0228 -0.0062 57  ILE A N   
267  C CA  . ILE A 40  ? 0.1108 0.1339 0.1711 0.0559  -0.0229 -0.0102 57  ILE A CA  
268  C C   . ILE A 40  ? 0.1431 0.1663 0.2026 0.0603  -0.0264 -0.0132 57  ILE A C   
269  O O   . ILE A 40  ? 0.1621 0.1839 0.2220 0.0616  -0.0280 -0.0142 57  ILE A O   
270  C CB  . ILE A 40  ? 0.1130 0.1417 0.1760 0.0535  -0.0211 -0.0115 57  ILE A CB  
271  C CG1 . ILE A 40  ? 0.1507 0.1784 0.2144 0.0493  -0.0179 -0.0083 57  ILE A CG1 
272  C CG2 . ILE A 40  ? 0.1885 0.2262 0.2530 0.0543  -0.0210 -0.0154 57  ILE A CG2 
273  C CD1 . ILE A 40  ? 0.2008 0.2328 0.2670 0.0466  -0.0163 -0.0091 57  ILE A CD1 
274  N N   . ALA A 41  ? 0.1451 0.1702 0.2035 0.0626  -0.0276 -0.0148 58  ALA A N   
275  C CA  . ALA A 41  ? 0.1498 0.1755 0.2074 0.0669  -0.0309 -0.0179 58  ALA A CA  
276  C C   . ALA A 41  ? 0.1760 0.2110 0.2356 0.0681  -0.0310 -0.0223 58  ALA A C   
277  O O   . ALA A 41  ? 0.2009 0.2374 0.2606 0.0714  -0.0337 -0.0254 58  ALA A O   
278  C CB  . ALA A 41  ? 0.1812 0.2026 0.2360 0.0691  -0.0326 -0.0169 58  ALA A CB  
279  N N   . ALA A 42  ? 0.1451 0.1865 0.2063 0.0654  -0.0283 -0.0228 59  ALA A N   
280  C CA  . ALA A 42  ? 0.1369 0.1876 0.2001 0.0660  -0.0282 -0.0270 59  ALA A CA  
281  C C   . ALA A 42  ? 0.1576 0.2133 0.2225 0.0617  -0.0248 -0.0262 59  ALA A C   
282  O O   . ALA A 42  ? 0.1407 0.1932 0.2049 0.0591  -0.0227 -0.0230 59  ALA A O   
283  C CB  . ALA A 42  ? 0.1813 0.2350 0.2434 0.0692  -0.0299 -0.0295 59  ALA A CB  
284  N N   . MET A 43  ? 0.1371 0.2005 0.2042 0.0611  -0.0242 -0.0293 60  MET A N   
285  C CA  . MET A 43  ? 0.1403 0.2088 0.2089 0.0570  -0.0211 -0.0290 60  MET A CA  
286  C C   . MET A 43  ? 0.1786 0.2569 0.2492 0.0574  -0.0213 -0.0333 60  MET A C   
287  O O   . MET A 43  ? 0.1858 0.2659 0.2573 0.0594  -0.0230 -0.0358 60  MET A O   
288  C CB  . MET A 43  ? 0.1637 0.2282 0.2331 0.0538  -0.0194 -0.0260 60  MET A CB  
289  C CG  . MET A 43  ? 0.2165 0.2847 0.2872 0.0493  -0.0163 -0.0249 60  MET A CG  
290  S SD  . MET A 43  ? 0.1995 0.2607 0.2703 0.0459  -0.0144 -0.0204 60  MET A SD  
291  C CE  . MET A 43  ? 0.1664 0.2205 0.2349 0.0453  -0.0135 -0.0163 60  MET A CE  
292  N N   . LYS A 44  ? 0.1345 0.2191 0.2056 0.0555  -0.0196 -0.0344 61  LYS A N   
293  C CA  . LYS A 44  ? 0.1502 0.2446 0.2230 0.0557  -0.0196 -0.0386 61  LYS A CA  
294  C C   . LYS A 44  ? 0.1738 0.2734 0.2472 0.0517  -0.0168 -0.0382 61  LYS A C   
295  O O   . LYS A 44  ? 0.1530 0.2515 0.2252 0.0510  -0.0158 -0.0367 61  LYS A O   
296  C CB  . LYS A 44  ? 0.1940 0.2914 0.2661 0.0600  -0.0221 -0.0418 61  LYS A CB  
297  C CG  . LYS A 44  ? 0.2820 0.3899 0.3555 0.0599  -0.0218 -0.0458 61  LYS A CG  
298  C CD  . LYS A 44  ? 0.2817 0.3918 0.3545 0.0646  -0.0247 -0.0493 61  LYS A CD  
299  C CE  . LYS A 44  ? 0.2431 0.3485 0.3140 0.0670  -0.0258 -0.0479 61  LYS A CE  
300  N NZ  . LYS A 44  ? 0.2288 0.3347 0.2972 0.0701  -0.0284 -0.0509 61  LYS A NZ  
301  N N   . LEU A 45  ? 0.1571 0.2627 0.2324 0.0491  -0.0155 -0.0396 62  LEU A N   
302  C CA  . LEU A 45  ? 0.1261 0.2380 0.2020 0.0456  -0.0132 -0.0401 62  LEU A CA  
303  C C   . LEU A 45  ? 0.1314 0.2521 0.2077 0.0474  -0.0142 -0.0444 62  LEU A C   
304  O O   . LEU A 45  ? 0.1322 0.2572 0.2096 0.0498  -0.0159 -0.0477 62  LEU A O   
305  C CB  . LEU A 45  ? 0.1084 0.2229 0.1858 0.0418  -0.0114 -0.0397 62  LEU A CB  
306  C CG  . LEU A 45  ? 0.1627 0.2825 0.2404 0.0376  -0.0089 -0.0395 62  LEU A CG  
307  C CD1 . LEU A 45  ? 0.1613 0.2744 0.2378 0.0349  -0.0070 -0.0351 62  LEU A CD1 
308  C CD2 . LEU A 45  ? 0.1567 0.2825 0.2362 0.0348  -0.0080 -0.0411 62  LEU A CD2 
309  N N   . THR A 46  ? 0.1397 0.2632 0.2153 0.0464  -0.0131 -0.0444 63  THR A N   
310  C CA  . THR A 46  ? 0.1372 0.2698 0.2133 0.0475  -0.0137 -0.0483 63  THR A CA  
311  C C   . THR A 46  ? 0.1535 0.2901 0.2293 0.0436  -0.0112 -0.0476 63  THR A C   
312  O O   . THR A 46  ? 0.1637 0.2959 0.2390 0.0403  -0.0092 -0.0442 63  THR A O   
313  C CB  . THR A 46  ? 0.1334 0.2646 0.2084 0.0523  -0.0161 -0.0498 63  THR A CB  
314  O OG1 . THR A 46  ? 0.1792 0.3177 0.2534 0.0529  -0.0168 -0.0537 63  THR A OG1 
315  C CG2 . THR A 46  ? 0.1499 0.2753 0.2229 0.0523  -0.0156 -0.0469 63  THR A CG2 
316  N N   . ILE A 47  ? 0.1576 0.3028 0.2339 0.0438  -0.0113 -0.0510 64  ILE A N   
317  C CA  . ILE A 47  ? 0.1605 0.3096 0.2362 0.0406  -0.0093 -0.0505 64  ILE A CA  
318  C C   . ILE A 47  ? 0.1640 0.3131 0.2382 0.0434  -0.0104 -0.0514 64  ILE A C   
319  O O   . ILE A 47  ? 0.1910 0.3425 0.2637 0.0457  -0.0121 -0.0543 64  ILE A O   
320  C CB  . ILE A 47  ? 0.2039 0.3598 0.2790 0.0370  -0.0083 -0.0527 64  ILE A CB  
321  C CG1 . ILE A 47  ? 0.2232 0.3784 0.2998 0.0338  -0.0069 -0.0512 64  ILE A CG1 
322  C CG2 . ILE A 47  ? 0.2646 0.4242 0.3384 0.0343  -0.0067 -0.0526 64  ILE A CG2 
323  C CD1 . ILE A 47  ? 0.2128 0.3737 0.2886 0.0305  -0.0061 -0.0532 64  ILE A CD1 
324  N N   . ALA A 48  ? 0.1392 0.2831 0.2121 0.0425  -0.0094 -0.0483 65  ALA A N   
325  C CA  . ALA A 48  ? 0.1271 0.2705 0.1986 0.0450  -0.0102 -0.0487 65  ALA A CA  
326  C C   . ALA A 48  ? 0.1625 0.3149 0.2340 0.0437  -0.0096 -0.0515 65  ALA A C   
327  O O   . ALA A 48  ? 0.2197 0.3760 0.2913 0.0396  -0.0076 -0.0514 65  ALA A O   
328  C CB  . ALA A 48  ? 0.1721 0.3074 0.2418 0.0436  -0.0089 -0.0444 65  ALA A CB  
329  N N   . THR A 49  ? 0.1351 0.3759 0.2513 0.0163  -0.0006 -0.0520 66  THR A N   
330  C CA  . THR A 49  ? 0.1146 0.3599 0.2319 0.0147  0.0014  -0.0565 66  THR A CA  
331  C C   . THR A 49  ? 0.1120 0.3586 0.2302 0.0148  0.0006  -0.0565 66  THR A C   
332  O O   . THR A 49  ? 0.1267 0.3717 0.2457 0.0167  -0.0025 -0.0538 66  THR A O   
333  C CB  . THR A 49  ? 0.1484 0.3986 0.2695 0.0158  -0.0007 -0.0610 66  THR A CB  
334  O OG1 . THR A 49  ? 0.1947 0.4462 0.3188 0.0184  -0.0053 -0.0608 66  THR A OG1 
335  C CG2 . THR A 49  ? 0.2303 0.4791 0.3508 0.0160  -0.0005 -0.0608 66  THR A CG2 
336  N N   . PRO A 50  ? 0.1389 0.3883 0.2569 0.0127  0.0034  -0.0596 67  PRO A N   
337  C CA  . PRO A 50  ? 0.1556 0.4062 0.2741 0.0126  0.0029  -0.0596 67  PRO A CA  
338  C C   . PRO A 50  ? 0.1637 0.4173 0.2862 0.0153  -0.0018 -0.0605 67  PRO A C   
339  O O   . PRO A 50  ? 0.1724 0.4247 0.2949 0.0163  -0.0035 -0.0581 67  PRO A O   
340  C CB  . PRO A 50  ? 0.1824 0.4366 0.3006 0.0098  0.0065  -0.0637 67  PRO A CB  
341  C CG  . PRO A 50  ? 0.1753 0.4270 0.2905 0.0079  0.0103  -0.0634 67  PRO A CG  
342  C CD  . PRO A 50  ? 0.1613 0.4123 0.2779 0.0100  0.0076  -0.0626 67  PRO A CD  
343  N N   . ALA A 51  ? 0.1491 0.4067 0.2749 0.0166  -0.0041 -0.0637 68  ALA A N   
344  C CA  . ALA A 51  ? 0.1760 0.4367 0.3055 0.0192  -0.0084 -0.0649 68  ALA A CA  
345  C C   . ALA A 51  ? 0.1554 0.4119 0.2847 0.0217  -0.0119 -0.0604 68  ALA A C   
346  O O   . ALA A 51  ? 0.2192 0.4762 0.3499 0.0232  -0.0145 -0.0593 68  ALA A O   
347  C CB  . ALA A 51  ? 0.2334 0.4989 0.3662 0.0203  -0.0100 -0.0691 68  ALA A CB  
348  N N   . ILE A 52  ? 0.1420 0.3946 0.2697 0.0222  -0.0121 -0.0578 69  ILE A N   
349  C CA  . ILE A 52  ? 0.1122 0.3608 0.2397 0.0244  -0.0153 -0.0535 69  ILE A CA  
350  C C   . ILE A 52  ? 0.1106 0.3553 0.2353 0.0236  -0.0140 -0.0493 69  ILE A C   
351  O O   . ILE A 52  ? 0.1392 0.3823 0.2644 0.0253  -0.0168 -0.0465 69  ILE A O   
352  C CB  . ILE A 52  ? 0.1343 0.3802 0.2611 0.0251  -0.0161 -0.0519 69  ILE A CB  
353  C CG1 . ILE A 52  ? 0.1916 0.4339 0.3186 0.0275  -0.0200 -0.0478 69  ILE A CG1 
354  C CG2 . ILE A 52  ? 0.1968 0.4392 0.3198 0.0228  -0.0121 -0.0499 69  ILE A CG2 
355  C CD1 . ILE A 52  ? 0.2918 0.5328 0.4193 0.0288  -0.0220 -0.0475 69  ILE A CD1 
356  N N   . LEU A 53  ? 0.1211 0.3641 0.2425 0.0210  -0.0096 -0.0487 70  LEU A N   
357  C CA  . LEU A 53  ? 0.1331 0.3722 0.2514 0.0202  -0.0080 -0.0448 70  LEU A CA  
358  C C   . LEU A 53  ? 0.1319 0.3734 0.2517 0.0205  -0.0090 -0.0457 70  LEU A C   
359  O O   . LEU A 53  ? 0.1450 0.3837 0.2636 0.0212  -0.0099 -0.0421 70  LEU A O   
360  C CB  . LEU A 53  ? 0.1180 0.3551 0.2326 0.0174  -0.0030 -0.0445 70  LEU A CB  
361  C CG  . LEU A 53  ? 0.1288 0.3624 0.2411 0.0170  -0.0016 -0.0422 70  LEU A CG  
362  C CD1 . LEU A 53  ? 0.1617 0.3946 0.2709 0.0141  0.0036  -0.0433 70  LEU A CD1 
363  C CD2 . LEU A 53  ? 0.1260 0.3545 0.2363 0.0184  -0.0031 -0.0365 70  LEU A CD2 
364  N N   . GLU A 54  ? 0.1358 0.3827 0.2581 0.0199  -0.0088 -0.0505 71  GLU A N   
365  C CA  . GLU A 54  ? 0.1123 0.3619 0.2361 0.0203  -0.0100 -0.0516 71  GLU A CA  
366  C C   . GLU A 54  ? 0.1898 0.4393 0.3161 0.0234  -0.0148 -0.0497 71  GLU A C   
367  O O   . GLU A 54  ? 0.2076 0.4561 0.3337 0.0240  -0.0158 -0.0476 71  GLU A O   
368  C CB  . GLU A 54  ? 0.2427 0.4984 0.3690 0.0191  -0.0090 -0.0571 71  GLU A CB  
369  C CG  . GLU A 54  ? 0.4927 0.7485 0.6162 0.0158  -0.0041 -0.0587 71  GLU A CG  
370  C CD  . GLU A 54  ? 0.8192 1.0813 0.9450 0.0145  -0.0030 -0.0642 71  GLU A CD  
371  O OE1 . GLU A 54  ? 0.6673 0.9339 0.7967 0.0160  -0.0060 -0.0666 71  GLU A OE1 
372  O OE2 . GLU A 54  ? 0.6345 0.8970 0.7585 0.0119  0.0007  -0.0662 71  GLU A OE2 
373  N N   . GLU A 55  ? 0.1069 0.3570 0.2355 0.0254  -0.0178 -0.0502 72  GLU A N   
374  C CA  . GLU A 55  ? 0.1673 0.4167 0.2980 0.0283  -0.0224 -0.0481 72  GLU A CA  
375  C C   . GLU A 55  ? 0.1677 0.4111 0.2956 0.0289  -0.0229 -0.0425 72  GLU A C   
376  O O   . GLU A 55  ? 0.1743 0.4166 0.3028 0.0304  -0.0253 -0.0399 72  GLU A O   
377  C CB  . GLU A 55  ? 0.1700 0.4203 0.3028 0.0301  -0.0252 -0.0500 72  GLU A CB  
378  C CG  . GLU A 55  ? 0.4042 0.6580 0.5383 0.0295  -0.0246 -0.0550 72  GLU A CG  
379  C CD  . GLU A 55  ? 0.6484 0.9005 0.7832 0.0317  -0.0281 -0.0558 72  GLU A CD  
380  O OE1 . GLU A 55  ? 0.6030 0.8516 0.7378 0.0336  -0.0310 -0.0541 72  GLU A OE1 
381  O OE2 . GLU A 55  ? 0.7551 1.0093 0.8904 0.0313  -0.0279 -0.0579 72  GLU A OE2 
382  N N   . HIS A 56  ? 0.1277 0.3676 0.2528 0.0276  -0.0206 -0.0404 73  HIS A N   
383  C CA  . HIS A 56  ? 0.1106 0.3450 0.2330 0.0281  -0.0209 -0.0349 73  HIS A CA  
384  C C   . HIS A 56  ? 0.1324 0.3651 0.2528 0.0274  -0.0195 -0.0325 73  HIS A C   
385  O O   . HIS A 56  ? 0.1549 0.3849 0.2749 0.0288  -0.0217 -0.0286 73  HIS A O   
386  C CB  . HIS A 56  ? 0.1065 0.3379 0.2260 0.0265  -0.0179 -0.0336 73  HIS A CB  
387  C CG  . HIS A 56  ? 0.1288 0.3549 0.2453 0.0268  -0.0179 -0.0281 73  HIS A CG  
388  N ND1 . HIS A 56  ? 0.1098 0.3337 0.2270 0.0289  -0.0214 -0.0252 73  HIS A ND1 
389  C CD2 . HIS A 56  ? 0.1431 0.3657 0.2559 0.0254  -0.0149 -0.0248 73  HIS A CD2 
390  C CE1 . HIS A 56  ? 0.1281 0.3475 0.2423 0.0287  -0.0205 -0.0203 73  HIS A CE1 
391  N NE2 . HIS A 56  ? 0.1395 0.3581 0.2510 0.0267  -0.0166 -0.0200 73  HIS A NE2 
392  N N   . TYR A 57  ? 0.3391 0.3878 0.1718 -0.1173 0.0321  -0.0257 74  TYR A N   
393  C CA  . TYR A 57  ? 0.3444 0.3866 0.1696 -0.1211 0.0409  -0.0223 74  TYR A CA  
394  C C   . TYR A 57  ? 0.3750 0.4185 0.1987 -0.1266 0.0398  -0.0267 74  TYR A C   
395  O O   . TYR A 57  ? 0.3975 0.4366 0.2135 -0.1301 0.0484  -0.0279 74  TYR A O   
396  C CB  . TYR A 57  ? 0.3622 0.3985 0.1787 -0.1209 0.0528  -0.0224 74  TYR A CB  
397  C CG  . TYR A 57  ? 0.3681 0.4012 0.1847 -0.1161 0.0558  -0.0160 74  TYR A CG  
398  C CD1 . TYR A 57  ? 0.3897 0.4206 0.2084 -0.1144 0.0548  -0.0088 74  TYR A CD1 
399  C CD2 . TYR A 57  ? 0.3976 0.4308 0.2123 -0.1133 0.0595  -0.0169 74  TYR A CD2 
400  C CE1 . TYR A 57  ? 0.4098 0.4376 0.2287 -0.1100 0.0575  -0.0030 74  TYR A CE1 
401  C CE2 . TYR A 57  ? 0.4090 0.4392 0.2239 -0.1089 0.0622  -0.0109 74  TYR A CE2 
402  C CZ  . TYR A 57  ? 0.5190 0.5461 0.3360 -0.1072 0.0611  -0.0042 74  TYR A CZ  
403  O OH  . TYR A 57  ? 0.4746 0.4987 0.2919 -0.1028 0.0636  0.0018  74  TYR A OH  
404  N N   . ALA A 58  ? 0.3478 0.3973 0.1794 -0.1273 0.0289  -0.0289 75  ALA A N   
405  C CA  . ALA A 58  ? 0.4160 0.4675 0.2469 -0.1325 0.0268  -0.0332 75  ALA A CA  
406  C C   . ALA A 58  ? 0.4180 0.4664 0.2442 -0.1361 0.0317  -0.0284 75  ALA A C   
407  O O   . ALA A 58  ? 0.4574 0.5050 0.2784 -0.1405 0.0359  -0.0324 75  ALA A O   
408  C CB  . ALA A 58  ? 0.3925 0.4508 0.2345 -0.1320 0.0128  -0.0352 75  ALA A CB  
409  N N   . GLU A 59  ? 0.3745 0.4224 0.2030 -0.1341 0.0311  -0.0201 76  GLU A N   
410  C CA  . GLU A 59  ? 0.3921 0.4393 0.2160 -0.1371 0.0359  -0.0158 76  GLU A CA  
411  C C   . GLU A 59  ? 0.3791 0.4201 0.1922 -0.1385 0.0487  -0.0188 76  GLU A C   
412  O O   . GLU A 59  ? 0.4391 0.4803 0.2476 -0.1416 0.0529  -0.0184 76  GLU A O   
413  C CB  . GLU A 59  ? 0.3728 0.4212 0.2004 -0.1343 0.0341  -0.0062 76  GLU A CB  
414  C CG  . GLU A 59  ? 0.3815 0.4240 0.2053 -0.1298 0.0416  -0.0035 76  GLU A CG  
415  C CD  . GLU A 59  ? 0.5621 0.6063 0.3902 -0.1268 0.0393  0.0060  76  GLU A CD  
416  O OE1 . GLU A 59  ? 0.6040 0.6500 0.4293 -0.1286 0.0427  0.0105  76  GLU A OE1 
417  O OE2 . GLU A 59  ? 0.6784 0.7228 0.5128 -0.1227 0.0339  0.0087  76  GLU A OE2 
418  N N   . HIS A 60  ? 0.3877 0.4236 0.1971 -0.1362 0.0547  -0.0215 77  HIS A N   
419  C CA  . HIS A 60  ? 0.4920 0.5212 0.2925 -0.1374 0.0662  -0.0239 77  HIS A CA  
420  C C   . HIS A 60  ? 0.5680 0.5962 0.3648 -0.1413 0.0687  -0.0320 77  HIS A C   
421  O O   . HIS A 60  ? 0.5251 0.5474 0.3155 -0.1424 0.0775  -0.0346 77  HIS A O   
422  C CB  . HIS A 60  ? 0.4458 0.4699 0.2448 -0.1331 0.0713  -0.0210 77  HIS A CB  
423  C CG  . HIS A 60  ? 0.4154 0.4395 0.2171 -0.1293 0.0703  -0.0130 77  HIS A CG  
424  N ND1 . HIS A 60  ? 0.4384 0.4636 0.2390 -0.1302 0.0716  -0.0088 77  HIS A ND1 
425  C CD2 . HIS A 60  ? 0.4256 0.4495 0.2312 -0.1247 0.0680  -0.0084 77  HIS A CD2 
426  C CE1 . HIS A 60  ? 0.4509 0.4766 0.2547 -0.1263 0.0701  -0.0017 77  HIS A CE1 
427  N NE2 . HIS A 60  ? 0.4105 0.4348 0.2175 -0.1229 0.0678  -0.0014 77  HIS A NE2 
428  N N   . LYS A 61  ? 0.4820 0.5160 0.2832 -0.1433 0.0609  -0.0362 78  LYS A N   
429  C CA  . LYS A 61  ? 0.5498 0.5838 0.3479 -0.1470 0.0627  -0.0440 78  LYS A CA  
430  C C   . LYS A 61  ? 0.6713 0.7007 0.4621 -0.1508 0.0707  -0.0461 78  LYS A C   
431  O O   . LYS A 61  ? 0.6311 0.6615 0.4211 -0.1518 0.0707  -0.0431 78  LYS A O   
432  C CB  . LYS A 61  ? 0.6335 0.6748 0.4381 -0.1486 0.0522  -0.0476 78  LYS A CB  
433  C CG  . LYS A 61  ? 0.7876 0.8300 0.5896 -0.1526 0.0531  -0.0558 78  LYS A CG  
434  C CD  . LYS A 61  ? 0.9062 0.9561 0.7160 -0.1532 0.0417  -0.0595 78  LYS A CD  
435  C CE  . LYS A 61  ? 0.9967 1.0491 0.8052 -0.1553 0.0420  -0.0681 78  LYS A CE  
436  N NZ  . LYS A 61  ? 0.8933 0.9510 0.7064 -0.1584 0.0336  -0.0727 78  LYS A NZ  
437  N N   . GLY A 62  ? 0.7904 0.8150 0.5805 -0.1512 0.0759  -0.0504 79  GLY A N   
438  C CA  . GLY A 62  ? 0.6362 0.6552 0.4254 -0.1525 0.0811  -0.0528 79  GLY A CA  
439  C C   . GLY A 62  ? 0.8033 0.8146 0.5910 -0.1491 0.0880  -0.0492 79  GLY A C   
440  O O   . GLY A 62  ? 0.9587 0.9641 0.7453 -0.1499 0.0930  -0.0522 79  GLY A O   
441  N N   . LYS A 63  ? 0.7187 0.7300 0.5064 -0.1456 0.0882  -0.0431 80  LYS A N   
442  C CA  . LYS A 63  ? 0.7911 0.7959 0.5777 -0.1422 0.0942  -0.0399 80  LYS A CA  
443  C C   . LYS A 63  ? 0.9065 0.9038 0.6927 -0.1411 0.0995  -0.0411 80  LYS A C   
444  O O   . LYS A 63  ? 0.8269 0.8255 0.6142 -0.1412 0.0982  -0.0416 80  LYS A O   
445  C CB  . LYS A 63  ? 0.6872 0.6942 0.4746 -0.1386 0.0927  -0.0327 80  LYS A CB  
446  C CG  . LYS A 63  ? 0.6443 0.6593 0.4321 -0.1403 0.0877  -0.0301 80  LYS A CG  
447  C CD  . LYS A 63  ? 0.6632 0.6807 0.4522 -0.1371 0.0864  -0.0223 80  LYS A CD  
448  C CE  . LYS A 63  ? 0.5107 0.5377 0.3006 -0.1401 0.0801  -0.0188 80  LYS A CE  
449  N NZ  . LYS A 63  ? 0.5606 0.5911 0.3537 -0.1373 0.0767  -0.0104 80  LYS A NZ  
450  N N   . PRO A 64  ? 1.0312 1.0213 0.8155 -0.1403 0.1055  -0.0416 81  PRO A N   
451  C CA  . PRO A 64  ? 1.0651 1.0479 0.8486 -0.1405 0.1105  -0.0426 81  PRO A CA  
452  C C   . PRO A 64  ? 0.8657 0.8475 0.6505 -0.1371 0.1110  -0.0374 81  PRO A C   
453  O O   . PRO A 64  ? 0.7121 0.6916 0.4972 -0.1381 0.1130  -0.0378 81  PRO A O   
454  C CB  . PRO A 64  ? 1.0314 1.0071 0.8121 -0.1402 0.1164  -0.0440 81  PRO A CB  
455  C CG  . PRO A 64  ? 1.0608 1.0408 0.8416 -0.1373 0.1148  -0.0409 81  PRO A CG  
456  C CD  . PRO A 64  ? 1.0317 1.0209 0.8144 -0.1390 0.1079  -0.0410 81  PRO A CD  
457  N N   . PHE A 65  ? 0.7099 0.6939 0.4956 -0.1332 0.1094  -0.0321 82  PHE A N   
458  C CA  . PHE A 65  ? 0.7150 0.6977 0.5021 -0.1296 0.1102  -0.0269 82  PHE A CA  
459  C C   . PHE A 65  ? 0.5307 0.5208 0.3196 -0.1295 0.1051  -0.0266 82  PHE A C   
460  O O   . PHE A 65  ? 0.5274 0.5176 0.3173 -0.1267 0.1056  -0.0229 82  PHE A O   
461  C CB  . PHE A 65  ? 0.6973 0.6789 0.4846 -0.1253 0.1109  -0.0213 82  PHE A CB  
462  C CG  . PHE A 65  ? 0.7099 0.6993 0.4984 -0.1248 0.1052  -0.0190 82  PHE A CG  
463  C CD1 . PHE A 65  ? 0.6337 0.6279 0.4239 -0.1231 0.1009  -0.0154 82  PHE A CD1 
464  C CD2 . PHE A 65  ? 0.8419 0.8342 0.6297 -0.1262 0.1042  -0.0201 82  PHE A CD2 
465  C CE1 . PHE A 65  ? 0.6251 0.6262 0.4163 -0.1236 0.0954  -0.0127 82  PHE A CE1 
466  C CE2 . PHE A 65  ? 0.5918 0.5917 0.3808 -0.1265 0.0987  -0.0169 82  PHE A CE2 
467  C CZ  . PHE A 65  ? 0.6567 0.6606 0.4474 -0.1255 0.0942  -0.0130 82  PHE A CZ  
468  N N   . LEU A 66  ? 0.3772 0.5122 0.3946 -0.0750 0.0425  -0.0562 83  LEU A N   
469  C CA  . LEU A 66  ? 0.4373 0.5789 0.4605 -0.0729 0.0355  -0.0561 83  LEU A CA  
470  C C   . LEU A 66  ? 0.4291 0.5731 0.4520 -0.0725 0.0333  -0.0581 83  LEU A C   
471  O O   . LEU A 66  ? 0.2663 0.4137 0.2964 -0.0695 0.0296  -0.0569 83  LEU A O   
472  C CB  . LEU A 66  ? 0.3513 0.4970 0.3723 -0.0748 0.0313  -0.0574 83  LEU A CB  
473  C CG  . LEU A 66  ? 0.3813 0.5341 0.4078 -0.0729 0.0239  -0.0576 83  LEU A CG  
474  C CD1 . LEU A 66  ? 0.2794 0.4336 0.3158 -0.0689 0.0219  -0.0543 83  LEU A CD1 
475  C CD2 . LEU A 66  ? 0.3250 0.4815 0.3486 -0.0750 0.0203  -0.0590 83  LEU A CD2 
476  N N   . PRO A 67  ? 0.3029 0.4456 0.3181 -0.0754 0.0351  -0.0611 84  PRO A N   
477  C CA  . PRO A 67  ? 0.3129 0.4583 0.3284 -0.0747 0.0327  -0.0628 84  PRO A CA  
478  C C   . PRO A 67  ? 0.3391 0.4823 0.3598 -0.0718 0.0347  -0.0609 84  PRO A C   
479  O O   . PRO A 67  ? 0.3038 0.4508 0.3295 -0.0695 0.0307  -0.0609 84  PRO A O   
480  C CB  . PRO A 67  ? 0.3287 0.4717 0.3342 -0.0785 0.0357  -0.0661 84  PRO A CB  
481  C CG  . PRO A 67  ? 0.3935 0.5352 0.3941 -0.0812 0.0371  -0.0665 84  PRO A CG  
482  C CD  . PRO A 67  ? 0.4540 0.5931 0.4599 -0.0792 0.0392  -0.0630 84  PRO A CD  
483  N N   . GLY A 68  ? 0.3909 0.5282 0.4110 -0.0716 0.0407  -0.0593 85  GLY A N   
484  C CA  . GLY A 68  ? 0.3389 0.4741 0.3644 -0.0687 0.0426  -0.0574 85  GLY A CA  
485  C C   . GLY A 68  ? 0.3839 0.5220 0.4192 -0.0650 0.0390  -0.0544 85  GLY A C   
486  O O   . GLY A 68  ? 0.3154 0.4548 0.3565 -0.0622 0.0375  -0.0533 85  GLY A O   
487  N N   . LEU A 69  ? 0.2815 0.4207 0.3189 -0.0649 0.0376  -0.0529 86  LEU A N   
488  C CA  . LEU A 69  ? 0.2579 0.4004 0.3046 -0.0615 0.0337  -0.0502 86  LEU A CA  
489  C C   . LEU A 69  ? 0.2471 0.3963 0.2977 -0.0600 0.0268  -0.0512 86  LEU A C   
490  O O   . LEU A 69  ? 0.2448 0.3962 0.3029 -0.0567 0.0243  -0.0495 86  LEU A O   
491  C CB  . LEU A 69  ? 0.2784 0.4211 0.3256 -0.0621 0.0333  -0.0488 86  LEU A CB  
492  C CG  . LEU A 69  ? 0.2532 0.3999 0.3094 -0.0589 0.0286  -0.0463 86  LEU A CG  
493  C CD1 . LEU A 69  ? 0.2912 0.4361 0.3550 -0.0553 0.0301  -0.0433 86  LEU A CD1 
494  C CD2 . LEU A 69  ? 0.2662 0.4124 0.3212 -0.0602 0.0289  -0.0454 86  LEU A CD2 
495  N N   . ILE A 70  ? 0.2312 0.3839 0.2769 -0.0624 0.0237  -0.0540 87  ILE A N   
496  C CA  A ILE A 70  ? 0.2264 0.3856 0.2756 -0.0612 0.0170  -0.0551 87  ILE A CA  
497  C CA  B ILE A 70  ? 0.2275 0.3867 0.2765 -0.0612 0.0170  -0.0551 87  ILE A CA  
498  C C   . ILE A 70  ? 0.2582 0.4174 0.3088 -0.0597 0.0171  -0.0557 87  ILE A C   
499  O O   . ILE A 70  ? 0.2466 0.4099 0.3039 -0.0569 0.0128  -0.0549 87  ILE A O   
500  C CB  A ILE A 70  ? 0.2436 0.4061 0.2865 -0.0643 0.0140  -0.0581 87  ILE A CB  
501  C CB  B ILE A 70  ? 0.2444 0.4067 0.2868 -0.0644 0.0143  -0.0583 87  ILE A CB  
502  C CG1 A ILE A 70  ? 0.2814 0.4454 0.3252 -0.0648 0.0123  -0.0571 87  ILE A CG1 
503  C CG1 B ILE A 70  ? 0.3013 0.4637 0.3422 -0.0659 0.0140  -0.0577 87  ILE A CG1 
504  C CG2 A ILE A 70  ? 0.2616 0.4302 0.3068 -0.0633 0.0079  -0.0598 87  ILE A CG2 
505  C CG2 B ILE A 70  ? 0.2589 0.4280 0.3046 -0.0632 0.0075  -0.0595 87  ILE A CG2 
506  C CD1 A ILE A 70  ? 0.3082 0.4751 0.3458 -0.0679 0.0096  -0.0598 87  ILE A CD1 
507  C CD1 B ILE A 70  ? 0.2084 0.3745 0.2577 -0.0631 0.0096  -0.0551 87  ILE A CD1 
508  N N   . GLU A 71  ? 0.2745 0.4292 0.3190 -0.0616 0.0222  -0.0572 88  GLU A N   
509  C CA  . GLU A 71  ? 0.3081 0.4624 0.3536 -0.0603 0.0228  -0.0578 88  GLU A CA  
510  C C   . GLU A 71  ? 0.3022 0.4552 0.3559 -0.0566 0.0235  -0.0546 88  GLU A C   
511  O O   . GLU A 71  ? 0.2775 0.4337 0.3364 -0.0541 0.0203  -0.0543 88  GLU A O   
512  C CB  . GLU A 71  ? 0.4152 0.5643 0.4523 -0.0631 0.0286  -0.0597 88  GLU A CB  
513  C CG  . GLU A 71  ? 0.6746 0.8253 0.7036 -0.0667 0.0274  -0.0633 88  GLU A CG  
514  C CD  . GLU A 71  ? 0.9913 1.1364 1.0118 -0.0696 0.0336  -0.0651 88  GLU A CD  
515  O OE1 . GLU A 71  ? 0.7940 0.9341 0.8151 -0.0688 0.0386  -0.0636 88  GLU A OE1 
516  O OE2 . GLU A 71  ? 1.0906 1.2364 1.1039 -0.0727 0.0333  -0.0679 88  GLU A OE2 
517  N N   . LYS A 72  ? 0.2537 0.4023 0.3088 -0.0560 0.0278  -0.0522 89  LYS A N   
518  C CA  . LYS A 72  ? 0.2805 0.4276 0.3432 -0.0525 0.0289  -0.0492 89  LYS A CA  
519  C C   . LYS A 72  ? 0.2183 0.3710 0.2897 -0.0495 0.0227  -0.0474 89  LYS A C   
520  O O   . LYS A 72  ? 0.2430 0.3965 0.3213 -0.0463 0.0216  -0.0456 89  LYS A O   
521  C CB  . LYS A 72  ? 0.3286 0.4698 0.3906 -0.0528 0.0347  -0.0470 89  LYS A CB  
522  C CG  . LYS A 72  ? 0.5074 0.6430 0.5610 -0.0557 0.0409  -0.0487 89  LYS A CG  
523  C CD  . LYS A 72  ? 0.5731 0.7050 0.6279 -0.0543 0.0447  -0.0480 89  LYS A CD  
524  C CE  . LYS A 72  ? 0.5300 0.6551 0.5823 -0.0550 0.0516  -0.0466 89  LYS A CE  
525  N NZ  . LYS A 72  ? 0.6482 0.7728 0.7047 -0.0539 0.0516  -0.0439 89  LYS A NZ  
526  N N   . MET A 73  ? 0.2401 0.3966 0.3113 -0.0504 0.0187  -0.0479 90  MET A N   
527  C CA  . MET A 73  ? 0.1936 0.3554 0.2728 -0.0477 0.0128  -0.0462 90  MET A CA  
528  C C   . MET A 73  ? 0.1793 0.3472 0.2603 -0.0469 0.0068  -0.0480 90  MET A C   
529  O O   . MET A 73  ? 0.1734 0.3460 0.2614 -0.0445 0.0016  -0.0467 90  MET A O   
530  C CB  . MET A 73  ? 0.2207 0.3838 0.2992 -0.0489 0.0114  -0.0457 90  MET A CB  
531  C CG  . MET A 73  ? 0.2268 0.3850 0.3066 -0.0485 0.0161  -0.0431 90  MET A CG  
532  S SD  . MET A 73  ? 0.2029 0.3616 0.2939 -0.0438 0.0150  -0.0391 90  MET A SD  
533  C CE  . MET A 73  ? 0.2719 0.4382 0.3690 -0.0421 0.0068  -0.0387 90  MET A CE  
534  N N   . THR A 74  ? 0.2000 0.3681 0.2748 -0.0491 0.0072  -0.0510 91  THR A N   
535  C CA  . THR A 74  ? 0.1757 0.3493 0.2517 -0.0485 0.0017  -0.0529 91  THR A CA  
536  C C   . THR A 74  ? 0.1915 0.3652 0.2736 -0.0453 0.0014  -0.0515 91  THR A C   
537  O O   . THR A 74  ? 0.2609 0.4312 0.3402 -0.0456 0.0051  -0.0523 91  THR A O   
538  C CB  . THR A 74  ? 0.1788 0.3521 0.2459 -0.0520 0.0025  -0.0565 91  THR A CB  
539  O OG1 . THR A 74  ? 0.2348 0.4085 0.2967 -0.0548 0.0023  -0.0577 91  THR A OG1 
540  C CG2 . THR A 74  ? 0.1992 0.3781 0.2677 -0.0513 -0.0029 -0.0583 91  THR A CG2 
541  N N   . GLY A 75  ? 0.1434 0.2598 0.2385 0.0176  -0.0130 -0.0304 92  GLY A N   
542  C CA  . GLY A 75  ? 0.1539 0.2669 0.2489 0.0156  -0.0114 -0.0291 92  GLY A CA  
543  C C   . GLY A 75  ? 0.1190 0.2284 0.2138 0.0187  -0.0115 -0.0274 92  GLY A C   
544  O O   . GLY A 75  ? 0.1371 0.2468 0.2318 0.0222  -0.0128 -0.0273 92  GLY A O   
545  N N   . PRO A 76  ? 0.1287 0.2347 0.2235 0.0173  -0.0101 -0.0260 93  PRO A N   
546  C CA  . PRO A 76  ? 0.1427 0.2449 0.2372 0.0200  -0.0101 -0.0243 93  PRO A CA  
547  C C   . PRO A 76  ? 0.1255 0.2220 0.2172 0.0223  -0.0106 -0.0221 93  PRO A C   
548  O O   . PRO A 76  ? 0.1254 0.2183 0.2150 0.0208  -0.0101 -0.0212 93  PRO A O   
549  C CB  . PRO A 76  ? 0.1312 0.2305 0.2258 0.0173  -0.0084 -0.0232 93  PRO A CB  
550  C CG  . PRO A 76  ? 0.1450 0.2436 0.2386 0.0135  -0.0076 -0.0234 93  PRO A CG  
551  C CD  . PRO A 76  ? 0.1562 0.2610 0.2508 0.0131  -0.0086 -0.0258 93  PRO A CD  
552  N N   . VAL A 77  ? 0.1372 0.2328 0.2289 0.0258  -0.0116 -0.0215 94  VAL A N   
553  C CA  . VAL A 77  ? 0.1437 0.2338 0.2327 0.0282  -0.0121 -0.0193 94  VAL A CA  
554  C C   . VAL A 77  ? 0.1481 0.2352 0.2372 0.0306  -0.0121 -0.0178 94  VAL A C   
555  O O   . VAL A 77  ? 0.1296 0.2202 0.2210 0.0315  -0.0125 -0.0189 94  VAL A O   
556  C CB  . VAL A 77  ? 0.1153 0.2073 0.2034 0.0306  -0.0139 -0.0201 94  VAL A CB  
557  C CG1 . VAL A 77  ? 0.1368 0.2313 0.2246 0.0283  -0.0138 -0.0215 94  VAL A CG1 
558  C CG2 . VAL A 77  ? 0.1128 0.2099 0.2030 0.0332  -0.0155 -0.0219 94  VAL A CG2 
559  N N   . LEU A 78  ? 0.1176 0.1984 0.2042 0.0316  -0.0118 -0.0154 95  LEU A N   
560  C CA  . LEU A 78  ? 0.1060 0.1835 0.1923 0.0342  -0.0120 -0.0138 95  LEU A CA  
561  C C   . LEU A 78  ? 0.1108 0.1868 0.1951 0.0374  -0.0137 -0.0131 95  LEU A C   
562  O O   . LEU A 78  ? 0.1388 0.2109 0.2204 0.0374  -0.0135 -0.0117 95  LEU A O   
563  C CB  . LEU A 78  ? 0.1125 0.1840 0.1976 0.0329  -0.0103 -0.0115 95  LEU A CB  
564  C CG  . LEU A 78  ? 0.1143 0.1832 0.1997 0.0353  -0.0105 -0.0101 95  LEU A CG  
565  C CD1 . LEU A 78  ? 0.1396 0.2127 0.2280 0.0352  -0.0105 -0.0116 95  LEU A CD1 
566  C CD2 . LEU A 78  ? 0.1114 0.1738 0.1951 0.0343  -0.0090 -0.0077 95  LEU A CD2 
567  N N   . CYS A 79  ? 0.1104 0.1897 0.1960 0.0401  -0.0153 -0.0142 96  CYS A N   
568  C CA  . CYS A 79  ? 0.1029 0.1806 0.1866 0.0434  -0.0171 -0.0135 96  CYS A CA  
569  C C   . CYS A 79  ? 0.1328 0.2044 0.2148 0.0450  -0.0169 -0.0109 96  CYS A C   
570  O O   . CYS A 79  ? 0.1470 0.2182 0.2305 0.0451  -0.0163 -0.0105 96  CYS A O   
571  C CB  . CYS A 79  ? 0.1254 0.2085 0.2112 0.0458  -0.0191 -0.0157 96  CYS A CB  
572  S SG  . CYS A 79  ? 0.1607 0.2520 0.2493 0.0438  -0.0193 -0.0191 96  CYS A SG  
573  N N   . MET A 80  ? 0.1268 0.1939 0.2056 0.0462  -0.0173 -0.0091 97  MET A N   
574  C CA  . MET A 80  ? 0.1234 0.1847 0.2004 0.0475  -0.0170 -0.0066 97  MET A CA  
575  C C   . MET A 80  ? 0.1448 0.2037 0.2189 0.0503  -0.0189 -0.0056 97  MET A C   
576  O O   . MET A 80  ? 0.1503 0.2103 0.2230 0.0505  -0.0197 -0.0062 97  MET A O   
577  C CB  . MET A 80  ? 0.1347 0.1911 0.2102 0.0451  -0.0149 -0.0047 97  MET A CB  
578  C CG  . MET A 80  ? 0.1542 0.2128 0.2318 0.0419  -0.0132 -0.0058 97  MET A CG  
579  S SD  . MET A 80  ? 0.1458 0.1985 0.2218 0.0392  -0.0109 -0.0038 97  MET A SD  
580  C CE  . MET A 80  ? 0.1846 0.2357 0.2577 0.0388  -0.0111 -0.0035 97  MET A CE  
581  N N   . VAL A 81  ? 0.1316 0.1871 0.2048 0.0524  -0.0195 -0.0040 98  VAL A N   
582  C CA  . VAL A 81  ? 0.1383 0.1899 0.2082 0.0547  -0.0209 -0.0024 98  VAL A CA  
583  C C   . VAL A 81  ? 0.1474 0.1928 0.2153 0.0543  -0.0196 0.0004  98  VAL A C   
584  O O   . VAL A 81  ? 0.1522 0.1965 0.2216 0.0545  -0.0190 0.0009  98  VAL A O   
585  C CB  . VAL A 81  ? 0.1488 0.2021 0.2190 0.0580  -0.0235 -0.0031 98  VAL A CB  
586  C CG1 . VAL A 81  ? 0.1726 0.2211 0.2388 0.0600  -0.0249 -0.0011 98  VAL A CG1 
587  C CG2 . VAL A 81  ? 0.1660 0.2257 0.2383 0.0583  -0.0248 -0.0060 98  VAL A CG2 
588  N N   . PHE A 82  ? 0.1093 0.1508 0.1741 0.0537  -0.0190 0.0019  99  PHE A N   
589  C CA  . PHE A 82  ? 0.1388 0.1743 0.2014 0.0534  -0.0179 0.0045  99  PHE A CA  
590  C C   . PHE A 82  ? 0.1541 0.1863 0.2131 0.0557  -0.0195 0.0060  99  PHE A C   
591  O O   . PHE A 82  ? 0.1479 0.1814 0.2053 0.0565  -0.0209 0.0053  99  PHE A O   
592  C CB  . PHE A 82  ? 0.1580 0.1916 0.2198 0.0506  -0.0157 0.0051  99  PHE A CB  
593  C CG  . PHE A 82  ? 0.1341 0.1685 0.1986 0.0484  -0.0138 0.0046  99  PHE A CG  
594  C CD1 . PHE A 82  ? 0.1253 0.1557 0.1899 0.0481  -0.0125 0.0063  99  PHE A CD1 
595  C CD2 . PHE A 82  ? 0.1783 0.2172 0.2453 0.0466  -0.0133 0.0025  99  PHE A CD2 
596  C CE1 . PHE A 82  ? 0.1668 0.1977 0.2338 0.0460  -0.0109 0.0059  99  PHE A CE1 
597  C CE2 . PHE A 82  ? 0.1903 0.2296 0.2596 0.0444  -0.0116 0.0022  99  PHE A CE2 
598  C CZ  . PHE A 82  ? 0.1404 0.1757 0.2096 0.0442  -0.0105 0.0039  99  PHE A CZ  
599  N N   . GLU A 83  ? 0.1423 0.1699 0.1999 0.0566  -0.0193 0.0081  100 GLU A N   
600  C CA  . GLU A 83  ? 0.1625 0.1862 0.2165 0.0585  -0.0208 0.0099  100 GLU A CA  
601  C C   . GLU A 83  ? 0.1755 0.1938 0.2268 0.0572  -0.0191 0.0122  100 GLU A C   
602  O O   . GLU A 83  ? 0.1792 0.1956 0.2317 0.0559  -0.0172 0.0130  100 GLU A O   
603  C CB  . GLU A 83  ? 0.1631 0.1860 0.2178 0.0610  -0.0224 0.0103  100 GLU A CB  
604  C CG  . GLU A 83  ? 0.1917 0.2102 0.2426 0.0630  -0.0241 0.0122  100 GLU A CG  
605  C CD  . GLU A 83  ? 0.2196 0.2373 0.2714 0.0654  -0.0257 0.0125  100 GLU A CD  
606  O OE1 . GLU A 83  ? 0.2365 0.2574 0.2893 0.0674  -0.0280 0.0109  100 GLU A OE1 
607  O OE2 . GLU A 83  ? 0.2702 0.2843 0.3218 0.0651  -0.0246 0.0142  100 GLU A OE2 
608  N N   . GLY A 84  ? 0.1512 0.1672 0.1989 0.0576  -0.0198 0.0133  101 GLY A N   
609  C CA  . GLY A 84  ? 0.1776 0.1888 0.2225 0.0565  -0.0183 0.0154  101 GLY A CA  
610  C C   . GLY A 84  ? 0.1600 0.1694 0.2008 0.0571  -0.0194 0.0162  101 GLY A C   
611  O O   . GLY A 84  ? 0.1810 0.1930 0.2213 0.0584  -0.0213 0.0150  101 GLY A O   
612  N N   . VAL A 85  ? 0.1767 0.1818 0.2147 0.0563  -0.0183 0.0182  102 VAL A N   
613  C CA  . VAL A 85  ? 0.1821 0.1852 0.2159 0.0565  -0.0191 0.0191  102 VAL A CA  
614  C C   . VAL A 85  ? 0.1552 0.1615 0.1893 0.0551  -0.0184 0.0174  102 VAL A C   
615  O O   . VAL A 85  ? 0.1852 0.1923 0.2211 0.0530  -0.0164 0.0168  102 VAL A O   
616  C CB  . VAL A 85  ? 0.2111 0.2092 0.2420 0.0556  -0.0177 0.0214  102 VAL A CB  
617  C CG1 . VAL A 85  ? 0.2299 0.2263 0.2566 0.0554  -0.0181 0.0222  102 VAL A CG1 
618  C CG2 . VAL A 85  ? 0.2191 0.2139 0.2494 0.0572  -0.0186 0.0231  102 VAL A CG2 
619  N N   . ASP A 86  ? 0.1688 0.1769 0.2014 0.0562  -0.0203 0.0165  103 ASP A N   
620  C CA  . ASP A 86  ? 0.1807 0.1915 0.2131 0.0549  -0.0199 0.0151  103 ASP A CA  
621  C C   . ASP A 86  ? 0.1764 0.1914 0.2130 0.0535  -0.0188 0.0131  103 ASP A C   
622  O O   . ASP A 86  ? 0.1749 0.1912 0.2118 0.0517  -0.0175 0.0122  103 ASP A O   
623  C CB  . ASP A 86  ? 0.2085 0.2161 0.2379 0.0533  -0.0183 0.0165  103 ASP A CB  
624  C CG  . ASP A 86  ? 0.2889 0.2987 0.3171 0.0523  -0.0183 0.0153  103 ASP A CG  
625  O OD1 . ASP A 86  ? 0.2839 0.2959 0.3113 0.0536  -0.0203 0.0143  103 ASP A OD1 
626  O OD2 . ASP A 86  ? 0.2657 0.2745 0.2934 0.0504  -0.0163 0.0154  103 ASP A OD2 
627  N N   . VAL A 87  ? 0.1715 0.1887 0.2114 0.0543  -0.0192 0.0122  104 VAL A N   
628  C CA  . VAL A 87  ? 0.1587 0.1790 0.2025 0.0525  -0.0177 0.0107  104 VAL A CA  
629  C C   . VAL A 87  ? 0.1343 0.1592 0.1792 0.0519  -0.0183 0.0084  104 VAL A C   
630  O O   . VAL A 87  ? 0.1569 0.1840 0.2041 0.0499  -0.0169 0.0072  104 VAL A O   
631  C CB  . VAL A 87  ? 0.1596 0.1810 0.2064 0.0534  -0.0180 0.0103  104 VAL A CB  
632  C CG1 . VAL A 87  ? 0.1588 0.1837 0.2067 0.0556  -0.0204 0.0089  104 VAL A CG1 
633  C CG2 . VAL A 87  ? 0.1413 0.1649 0.1917 0.0511  -0.0161 0.0092  104 VAL A CG2 
634  N N   . ILE A 88  ? 0.1424 0.1690 0.1859 0.0536  -0.0204 0.0077  105 ILE A N   
635  C CA  . ILE A 88  ? 0.1619 0.1931 0.2065 0.0529  -0.0209 0.0055  105 ILE A CA  
636  C C   . ILE A 88  ? 0.1588 0.1890 0.2020 0.0507  -0.0193 0.0056  105 ILE A C   
637  O O   . ILE A 88  ? 0.1665 0.1991 0.2119 0.0488  -0.0181 0.0043  105 ILE A O   
638  C CB  . ILE A 88  ? 0.1736 0.2064 0.2167 0.0552  -0.0236 0.0048  105 ILE A CB  
639  C CG1 . ILE A 88  ? 0.1540 0.1885 0.1990 0.0574  -0.0253 0.0042  105 ILE A CG1 
640  C CG2 . ILE A 88  ? 0.1704 0.2077 0.2145 0.0544  -0.0240 0.0026  105 ILE A CG2 
641  C CD1 . ILE A 88  ? 0.1998 0.2345 0.2427 0.0601  -0.0282 0.0040  105 ILE A CD1 
642  N N   . ALA A 89  ? 0.1591 0.1856 0.1985 0.0510  -0.0193 0.0072  106 ALA A N   
643  C CA  . ALA A 89  ? 0.1735 0.1990 0.2114 0.0490  -0.0178 0.0073  106 ALA A CA  
644  C C   . ALA A 89  ? 0.1445 0.1682 0.1840 0.0470  -0.0154 0.0078  106 ALA A C   
645  O O   . ALA A 89  ? 0.1649 0.1896 0.2051 0.0450  -0.0142 0.0069  106 ALA A O   
646  C CB  . ALA A 89  ? 0.1856 0.2075 0.2191 0.0497  -0.0183 0.0090  106 ALA A CB  
647  N N   . GLN A 90  ? 0.1596 0.1805 0.1995 0.0474  -0.0148 0.0093  107 GLN A N   
648  C CA  . GLN A 90  ? 0.1434 0.1623 0.1846 0.0455  -0.0126 0.0098  107 GLN A CA  
649  C C   . GLN A 90  ? 0.1478 0.1701 0.1929 0.0440  -0.0119 0.0081  107 GLN A C   
650  O O   . GLN A 90  ? 0.1467 0.1685 0.1926 0.0420  -0.0103 0.0076  107 GLN A O   
651  C CB  . GLN A 90  ? 0.1615 0.1767 0.2023 0.0463  -0.0122 0.0118  107 GLN A CB  
652  C CG  . GLN A 90  ? 0.1774 0.1886 0.2143 0.0470  -0.0123 0.0137  107 GLN A CG  
653  C CD  . GLN A 90  ? 0.1829 0.1923 0.2182 0.0452  -0.0106 0.0140  107 GLN A CD  
654  O OE1 . GLN A 90  ? 0.1815 0.1900 0.2183 0.0436  -0.0088 0.0140  107 GLN A OE1 
655  N NE2 . GLN A 90  ? 0.1950 0.2041 0.2271 0.0454  -0.0112 0.0142  107 GLN A NE2 
656  N N   . ALA A 91  ? 0.1322 0.1578 0.1795 0.0451  -0.0131 0.0069  108 ALA A N   
657  C CA  . ALA A 91  ? 0.1395 0.1684 0.1903 0.0435  -0.0125 0.0052  108 ALA A CA  
658  C C   . ALA A 91  ? 0.1403 0.1718 0.1911 0.0419  -0.0123 0.0036  108 ALA A C   
659  O O   . ALA A 91  ? 0.1467 0.1791 0.1992 0.0398  -0.0111 0.0027  108 ALA A O   
660  C CB  . ALA A 91  ? 0.1517 0.1842 0.2049 0.0449  -0.0138 0.0041  108 ALA A CB  
661  N N   . ARG A 92  ? 0.1611 0.1938 0.2099 0.0430  -0.0137 0.0032  109 ARG A N   
662  C CA  . ARG A 92  ? 0.1638 0.1987 0.2123 0.0416  -0.0136 0.0018  109 ARG A CA  
663  C C   . ARG A 92  ? 0.1412 0.1730 0.1884 0.0397  -0.0118 0.0024  109 ARG A C   
664  O O   . ARG A 92  ? 0.1656 0.1988 0.2140 0.0377  -0.0111 0.0012  109 ARG A O   
665  C CB  . ARG A 92  ? 0.1662 0.2025 0.2125 0.0432  -0.0154 0.0014  109 ARG A CB  
666  C CG  . ARG A 92  ? 0.1895 0.2296 0.2373 0.0450  -0.0173 0.0002  109 ARG A CG  
667  C CD  . ARG A 92  ? 0.2459 0.2909 0.2965 0.0437  -0.0175 -0.0022 109 ARG A CD  
668  N NE  . ARG A 92  ? 0.3370 0.3832 0.3859 0.0433  -0.0181 -0.0030 109 ARG A NE  
669  C CZ  . ARG A 92  ? 0.4469 0.4974 0.4974 0.0423  -0.0185 -0.0051 109 ARG A CZ  
670  N NH1 . ARG A 92  ? 0.3803 0.4342 0.4342 0.0413  -0.0182 -0.0065 109 ARG A NH1 
671  N NH2 . ARG A 92  ? 0.4310 0.4824 0.4797 0.0423  -0.0191 -0.0058 109 ARG A NH2 
672  N N   . LYS A 93  ? 0.1382 0.1658 0.1831 0.0402  -0.0112 0.0044  110 LYS A N   
673  C CA  . LYS A 93  ? 0.1441 0.1686 0.1879 0.0386  -0.0095 0.0050  110 LYS A CA  
674  C C   . LYS A 93  ? 0.1387 0.1627 0.1852 0.0367  -0.0080 0.0047  110 LYS A C   
675  O O   . LYS A 93  ? 0.1645 0.1879 0.2112 0.0349  -0.0070 0.0041  110 LYS A O   
676  C CB  . LYS A 93  ? 0.1793 0.1997 0.2202 0.0396  -0.0092 0.0071  110 LYS A CB  
677  C CG  . LYS A 93  ? 0.1714 0.1887 0.2110 0.0381  -0.0075 0.0077  110 LYS A CG  
678  C CD  . LYS A 93  ? 0.2240 0.2378 0.2604 0.0392  -0.0075 0.0097  110 LYS A CD  
679  C CE  . LYS A 93  ? 0.3077 0.3186 0.3431 0.0378  -0.0057 0.0103  110 LYS A CE  
680  N NZ  . LYS A 93  ? 0.2700 0.2777 0.3022 0.0387  -0.0055 0.0122  110 LYS A NZ  
681  N N   . MET A 94  ? 0.1481 0.1721 0.1965 0.0373  -0.0080 0.0051  111 MET A N   
682  C CA  . MET A 94  ? 0.1472 0.1705 0.1981 0.0356  -0.0067 0.0050  111 MET A CA  
683  C C   . MET A 94  ? 0.1390 0.1659 0.1922 0.0339  -0.0068 0.0029  111 MET A C   
684  O O   . MET A 94  ? 0.1326 0.1586 0.1870 0.0319  -0.0056 0.0025  111 MET A O   
685  C CB  . MET A 94  ? 0.1552 0.1778 0.2075 0.0368  -0.0068 0.0059  111 MET A CB  
686  C CG  . MET A 94  ? 0.1549 0.1733 0.2051 0.0381  -0.0065 0.0080  111 MET A CG  
687  S SD  . MET A 94  ? 0.1658 0.1839 0.2172 0.0401  -0.0072 0.0090  111 MET A SD  
688  C CE  . MET A 94  ? 0.1933 0.2105 0.2478 0.0382  -0.0055 0.0089  111 MET A CE  
689  N N   . MET A 95  ? 0.1227 0.1537 0.1765 0.0347  -0.0082 0.0016  112 MET A N   
690  C CA  . MET A 95  ? 0.1091 0.1440 0.1649 0.0330  -0.0084 -0.0004 112 MET A CA  
691  C C   . MET A 95  ? 0.1517 0.1861 0.2063 0.0313  -0.0079 -0.0011 112 MET A C   
692  O O   . MET A 95  ? 0.1308 0.1659 0.1868 0.0291  -0.0073 -0.0021 112 MET A O   
693  C CB  . MET A 95  ? 0.1485 0.1879 0.2050 0.0344  -0.0101 -0.0017 112 MET A CB  
694  C CG  . MET A 95  ? 0.1593 0.2002 0.2178 0.0357  -0.0106 -0.0016 112 MET A CG  
695  S SD  . MET A 95  ? 0.2250 0.2709 0.2840 0.0378  -0.0129 -0.0031 112 MET A SD  
696  C CE  . MET A 95  ? 0.2395 0.2893 0.2989 0.0360  -0.0131 -0.0052 112 MET A CE  
697  N N   . GLY A 96  ? 0.1289 0.1620 0.1808 0.0323  -0.0083 -0.0006 113 GLY A N   
698  C CA  . GLY A 96  ? 0.1456 0.1785 0.1961 0.0310  -0.0081 -0.0013 113 GLY A CA  
699  C C   . GLY A 96  ? 0.1370 0.1742 0.1878 0.0310  -0.0094 -0.0030 113 GLY A C   
700  O O   . GLY A 96  ? 0.1651 0.2057 0.2173 0.0318  -0.0104 -0.0039 113 GLY A O   
701  N N   . SER A 97  ? 0.1453 0.1823 0.1946 0.0300  -0.0093 -0.0037 114 SER A N   
702  C CA  A SER A 97  ? 0.1540 0.1946 0.2032 0.0299  -0.0105 -0.0053 114 SER A CA  
703  C CA  B SER A 97  ? 0.1555 0.1962 0.2047 0.0301  -0.0105 -0.0053 114 SER A CA  
704  C C   . SER A 97  ? 0.1298 0.1744 0.1819 0.0287  -0.0109 -0.0070 114 SER A C   
705  O O   . SER A 97  ? 0.1566 0.2007 0.2106 0.0270  -0.0099 -0.0072 114 SER A O   
706  C CB  A SER A 97  ? 0.1745 0.2139 0.2221 0.0286  -0.0100 -0.0059 114 SER A CB  
707  C CB  B SER A 97  ? 0.1880 0.2276 0.2353 0.0291  -0.0103 -0.0057 114 SER A CB  
708  O OG  A SER A 97  ? 0.2038 0.2393 0.2491 0.0291  -0.0092 -0.0044 114 SER A OG  
709  O OG  B SER A 97  ? 0.1306 0.1686 0.1789 0.0268  -0.0091 -0.0061 114 SER A OG  
710  N N   . THR A 98  ? 0.1557 0.2043 0.2081 0.0294  -0.0123 -0.0083 115 THR A N   
711  C CA  . THR A 98  ? 0.1510 0.2041 0.2061 0.0282  -0.0128 -0.0102 115 THR A CA  
712  C C   . THR A 98  ? 0.1539 0.2067 0.2100 0.0252  -0.0118 -0.0110 115 THR A C   
713  O O   . THR A 98  ? 0.1617 0.2160 0.2201 0.0237  -0.0114 -0.0116 115 THR A O   
714  C CB  . THR A 98  ? 0.1842 0.2412 0.2388 0.0292  -0.0144 -0.0115 115 THR A CB  
715  O OG1 . THR A 98  ? 0.1982 0.2549 0.2514 0.0320  -0.0154 -0.0107 115 THR A OG1 
716  C CG2 . THR A 98  ? 0.2302 0.2922 0.2876 0.0281  -0.0150 -0.0135 115 THR A CG2 
717  N N   . ARG A 99  ? 0.1317 0.1824 0.1860 0.0243  -0.0115 -0.0110 116 ARG A N   
718  C CA  . ARG A 99  ? 0.1470 0.1966 0.2018 0.0216  -0.0107 -0.0117 116 ARG A CA  
719  C C   . ARG A 99  ? 0.1524 0.1974 0.2071 0.0211  -0.0093 -0.0103 116 ARG A C   
720  O O   . ARG A 99  ? 0.1634 0.2050 0.2161 0.0221  -0.0088 -0.0091 116 ARG A O   
721  C CB  . ARG A 99  ? 0.1688 0.2180 0.2218 0.0211  -0.0111 -0.0125 116 ARG A CB  
722  C CG  . ARG A 99  ? 0.1943 0.2480 0.2476 0.0211  -0.0124 -0.0141 116 ARG A CG  
723  C CD  . ARG A 99  ? 0.2204 0.2733 0.2715 0.0211  -0.0127 -0.0145 116 ARG A CD  
724  N NE  . ARG A 99  ? 0.2984 0.3553 0.3499 0.0205  -0.0139 -0.0163 116 ARG A NE  
725  C CZ  . ARG A 99  ? 0.3833 0.4406 0.4329 0.0210  -0.0146 -0.0168 116 ARG A CZ  
726  N NH1 . ARG A 99  ? 0.2911 0.3452 0.3382 0.0221  -0.0142 -0.0158 116 ARG A NH1 
727  N NH2 . ARG A 99  ? 0.2994 0.3605 0.3497 0.0203  -0.0156 -0.0185 116 ARG A NH2 
728  N N   . PRO A 100 ? 0.1233 0.1680 0.1800 0.0194  -0.0086 -0.0104 117 PRO A N   
729  C CA  . PRO A 100 ? 0.1279 0.1681 0.1845 0.0188  -0.0074 -0.0091 117 PRO A CA  
730  C C   . PRO A 100 ? 0.1425 0.1792 0.1972 0.0180  -0.0069 -0.0089 117 PRO A C   
731  O O   . PRO A 100 ? 0.1566 0.1894 0.2104 0.0185  -0.0060 -0.0077 117 PRO A O   
732  C CB  . PRO A 100 ? 0.1328 0.1739 0.1916 0.0166  -0.0070 -0.0097 117 PRO A CB  
733  C CG  . PRO A 100 ? 0.1285 0.1749 0.1889 0.0171  -0.0080 -0.0109 117 PRO A CG  
734  C CD  . PRO A 100 ? 0.1178 0.1664 0.1769 0.0180  -0.0090 -0.0117 117 PRO A CD  
735  N N   . GLY A 101 ? 0.1260 0.1640 0.1802 0.0167  -0.0074 -0.0103 118 GLY A N   
736  C CA  . GLY A 101 ? 0.1488 0.1838 0.2015 0.0159  -0.0071 -0.0104 118 GLY A CA  
737  C C   . GLY A 101 ? 0.1568 0.1902 0.2072 0.0180  -0.0070 -0.0096 118 GLY A C   
738  O O   . GLY A 101 ? 0.1604 0.1908 0.2094 0.0176  -0.0064 -0.0094 118 GLY A O   
739  N N   . GLU A 102 ? 0.1260 0.1615 0.1757 0.0200  -0.0076 -0.0091 119 GLU A N   
740  C CA  . GLU A 102 ? 0.1494 0.1835 0.1966 0.0219  -0.0076 -0.0081 119 GLU A CA  
741  C C   . GLU A 102 ? 0.1850 0.2167 0.2320 0.0235  -0.0069 -0.0063 119 GLU A C   
742  O O   . GLU A 102 ? 0.1791 0.2089 0.2239 0.0248  -0.0067 -0.0052 119 GLU A O   
743  C CB  . GLU A 102 ? 0.1684 0.2060 0.2147 0.0233  -0.0089 -0.0088 119 GLU A CB  
744  C CG  . GLU A 102 ? 0.1357 0.1758 0.1820 0.0220  -0.0097 -0.0106 119 GLU A CG  
745  C CD  . GLU A 102 ? 0.1661 0.2095 0.2114 0.0234  -0.0111 -0.0112 119 GLU A CD  
746  O OE1 . GLU A 102 ? 0.2167 0.2611 0.2619 0.0253  -0.0116 -0.0104 119 GLU A OE1 
747  O OE2 . GLU A 102 ? 0.2256 0.2707 0.2704 0.0227  -0.0117 -0.0126 119 GLU A OE2 
748  N N   . ALA A 103 ? 0.1626 0.1946 0.2117 0.0232  -0.0066 -0.0059 120 ALA A N   
749  C CA  . ALA A 103 ? 0.1363 0.1663 0.1853 0.0248  -0.0061 -0.0042 120 ALA A CA  
750  C C   . ALA A 103 ? 0.1710 0.1965 0.2191 0.0244  -0.0048 -0.0030 120 ALA A C   
751  O O   . ALA A 103 ? 0.1700 0.1939 0.2186 0.0226  -0.0042 -0.0037 120 ALA A O   
752  C CB  . ALA A 103 ? 0.1587 0.1904 0.2103 0.0245  -0.0062 -0.0042 120 ALA A CB  
753  N N   . ALA A 104 ? 0.1759 0.1994 0.2228 0.0260  -0.0044 -0.0014 121 ALA A N   
754  C CA  . ALA A 104 ? 0.2075 0.2270 0.2535 0.0258  -0.0032 -0.0003 121 ALA A CA  
755  C C   . ALA A 104 ? 0.1913 0.2088 0.2394 0.0246  -0.0023 0.0000  121 ALA A C   
756  O O   . ALA A 104 ? 0.1469 0.1656 0.1968 0.0249  -0.0025 0.0002  121 ALA A O   
757  C CB  . ALA A 104 ? 0.1985 0.2164 0.2424 0.0278  -0.0031 0.0014  121 ALA A CB  
758  N N   . PRO A 105 ? 0.2286 0.2432 0.2767 0.0235  -0.0013 -0.0001 122 PRO A N   
759  C CA  . PRO A 105 ? 0.2235 0.2359 0.2734 0.0225  -0.0004 0.0004  122 PRO A CA  
760  C C   . PRO A 105 ? 0.1690 0.1802 0.2190 0.0241  -0.0001 0.0021  122 PRO A C   
761  O O   . PRO A 105 ? 0.2090 0.2195 0.2572 0.0257  -0.0001 0.0032  122 PRO A O   
762  C CB  . PRO A 105 ? 0.3051 0.3141 0.3542 0.0215  0.0005  0.0002  122 PRO A CB  
763  C CG  . PRO A 105 ? 0.3613 0.3718 0.4090 0.0213  -0.0001 -0.0010 122 PRO A CG  
764  C CD  . PRO A 105 ? 0.3279 0.3411 0.3743 0.0230  -0.0009 -0.0006 122 PRO A CD  
765  N N   . GLY A 106 ? 0.1790 0.1902 0.2312 0.0236  0.0001  0.0023  123 GLY A N   
766  C CA  . GLY A 106 ? 0.1878 0.1983 0.2403 0.0251  0.0003  0.0038  123 GLY A CA  
767  C C   . GLY A 106 ? 0.1675 0.1814 0.2206 0.0264  -0.0009 0.0037  123 GLY A C   
768  O O   . GLY A 106 ? 0.1888 0.2023 0.2425 0.0276  -0.0009 0.0048  123 GLY A O   
769  N N   . THR A 107 ? 0.1528 0.1701 0.2057 0.0263  -0.0019 0.0024  124 THR A N   
770  C CA  . THR A 107 ? 0.1398 0.1608 0.1935 0.0274  -0.0031 0.0020  124 THR A CA  
771  C C   . THR A 107 ? 0.1298 0.1532 0.1862 0.0259  -0.0031 0.0008  124 THR A C   
772  O O   . THR A 107 ? 0.1451 0.1677 0.2024 0.0237  -0.0025 0.0000  124 THR A O   
773  C CB  . THR A 107 ? 0.1379 0.1617 0.1902 0.0281  -0.0042 0.0010  124 THR A CB  
774  O OG1 . THR A 107 ? 0.1459 0.1710 0.1985 0.0262  -0.0043 -0.0005 124 THR A OG1 
775  C CG2 . THR A 107 ? 0.1525 0.1740 0.2018 0.0296  -0.0042 0.0023  124 THR A CG2 
776  N N   . ILE A 108 ? 0.1157 0.1422 0.1735 0.0269  -0.0040 0.0005  125 ILE A N   
777  C CA  . ILE A 108 ? 0.1067 0.1360 0.1670 0.0255  -0.0040 -0.0007 125 ILE A CA  
778  C C   . ILE A 108 ? 0.1520 0.1838 0.2127 0.0235  -0.0043 -0.0025 125 ILE A C   
779  O O   . ILE A 108 ? 0.1285 0.1600 0.1905 0.0212  -0.0038 -0.0032 125 ILE A O   
780  C CB  . ILE A 108 ? 0.1433 0.1759 0.2049 0.0272  -0.0050 -0.0009 125 ILE A CB  
781  C CG1 . ILE A 108 ? 0.1446 0.1742 0.2061 0.0289  -0.0046 0.0009  125 ILE A CG1 
782  C CG2 . ILE A 108 ? 0.1656 0.2020 0.2299 0.0257  -0.0051 -0.0025 125 ILE A CG2 
783  C CD1 . ILE A 108 ? 0.1491 0.1813 0.2113 0.0311  -0.0058 0.0009  125 ILE A CD1 
784  N N   . ARG A 109 ? 0.1211 0.1552 0.1806 0.0242  -0.0053 -0.0033 126 ARG A N   
785  C CA  . ARG A 109 ? 0.1200 0.1568 0.1800 0.0223  -0.0057 -0.0050 126 ARG A CA  
786  C C   . ARG A 109 ? 0.1376 0.1711 0.1967 0.0204  -0.0049 -0.0051 126 ARG A C   
787  O O   . ARG A 109 ? 0.1352 0.1696 0.1953 0.0181  -0.0048 -0.0063 126 ARG A O   
788  C CB  . ARG A 109 ? 0.1279 0.1678 0.1868 0.0237  -0.0070 -0.0058 126 ARG A CB  
789  C CG  . ARG A 109 ? 0.1190 0.1628 0.1795 0.0252  -0.0080 -0.0063 126 ARG A CG  
790  C CD  . ARG A 109 ? 0.1304 0.1767 0.1896 0.0271  -0.0094 -0.0068 126 ARG A CD  
791  N NE  . ARG A 109 ? 0.1588 0.2092 0.2197 0.0285  -0.0105 -0.0077 126 ARG A NE  
792  C CZ  . ARG A 109 ? 0.1710 0.2237 0.2310 0.0304  -0.0120 -0.0081 126 ARG A CZ  
793  N NH1 . ARG A 109 ? 0.1800 0.2310 0.2374 0.0313  -0.0124 -0.0076 126 ARG A NH1 
794  N NH2 . ARG A 109 ? 0.1722 0.2291 0.2340 0.0315  -0.0131 -0.0092 126 ARG A NH2 
795  N N   . ALA A 110 ? 0.1101 0.1398 0.1672 0.0212  -0.0043 -0.0039 127 ALA A N   
796  C CA  . ALA A 110 ? 0.1574 0.1841 0.2138 0.0194  -0.0036 -0.0041 127 ALA A CA  
797  C C   . ALA A 110 ? 0.1640 0.1883 0.2219 0.0177  -0.0027 -0.0039 127 ALA A C   
798  O O   . ALA A 110 ? 0.1588 0.1818 0.2169 0.0156  -0.0025 -0.0047 127 ALA A O   
799  C CB  . ALA A 110 ? 0.1454 0.1688 0.1996 0.0208  -0.0031 -0.0030 127 ALA A CB  
800  N N   . ASP A 111 ? 0.1274 0.1509 0.1863 0.0187  -0.0023 -0.0027 128 ASP A N   
801  C CA  . ASP A 111 ? 0.1184 0.1391 0.1785 0.0172  -0.0014 -0.0023 128 ASP A CA  
802  C C   . ASP A 111 ? 0.1273 0.1505 0.1893 0.0152  -0.0016 -0.0034 128 ASP A C   
803  O O   . ASP A 111 ? 0.1315 0.1524 0.1942 0.0133  -0.0010 -0.0035 128 ASP A O   
804  C CB  . ASP A 111 ? 0.1408 0.1595 0.2012 0.0189  -0.0007 -0.0006 128 ASP A CB  
805  C CG  . ASP A 111 ? 0.2056 0.2207 0.2640 0.0203  -0.0002 0.0007  128 ASP A CG  
806  O OD1 . ASP A 111 ? 0.2645 0.2782 0.3215 0.0198  -0.0001 0.0003  128 ASP A OD1 
807  O OD2 . ASP A 111 ? 0.2432 0.2569 0.3015 0.0220  0.0002  0.0022  128 ASP A OD2 
808  N N   . PHE A 112 ? 0.1292 0.1571 0.1922 0.0156  -0.0024 -0.0044 129 PHE A N   
809  C CA  . PHE A 112 ? 0.1287 0.1596 0.1936 0.0137  -0.0026 -0.0055 129 PHE A CA  
810  C C   . PHE A 112 ? 0.1290 0.1634 0.1941 0.0121  -0.0035 -0.0073 129 PHE A C   
811  O O   . PHE A 112 ? 0.1293 0.1656 0.1957 0.0100  -0.0035 -0.0082 129 PHE A O   
812  C CB  . PHE A 112 ? 0.1204 0.1545 0.1869 0.0153  -0.0029 -0.0053 129 PHE A CB  
813  C CG  . PHE A 112 ? 0.1204 0.1516 0.1874 0.0165  -0.0021 -0.0037 129 PHE A CG  
814  C CD1 . PHE A 112 ? 0.1609 0.1902 0.2268 0.0191  -0.0021 -0.0023 129 PHE A CD1 
815  C CD2 . PHE A 112 ? 0.1424 0.1733 0.2111 0.0149  -0.0015 -0.0037 129 PHE A CD2 
816  C CE1 . PHE A 112 ? 0.2112 0.2379 0.2775 0.0201  -0.0014 -0.0008 129 PHE A CE1 
817  C CE2 . PHE A 112 ? 0.1681 0.1966 0.2373 0.0161  -0.0008 -0.0023 129 PHE A CE2 
818  C CZ  . PHE A 112 ? 0.1612 0.1877 0.2293 0.0186  -0.0008 -0.0009 129 PHE A CZ  
819  N N   . CYS A 113 ? 0.1244 0.1600 0.1881 0.0130  -0.0042 -0.0078 130 CYS A N   
820  C CA  . CYS A 113 ? 0.1105 0.1505 0.1746 0.0120  -0.0051 -0.0095 130 CYS A CA  
821  C C   . CYS A 113 ? 0.1331 0.1721 0.1956 0.0110  -0.0055 -0.0103 130 CYS A C   
822  O O   . CYS A 113 ? 0.1442 0.1794 0.2052 0.0114  -0.0051 -0.0095 130 CYS A O   
823  C CB  . CYS A 113 ? 0.1033 0.1474 0.1678 0.0144  -0.0060 -0.0098 130 CYS A CB  
824  S SG  . CYS A 113 ? 0.1456 0.1916 0.2123 0.0157  -0.0058 -0.0093 130 CYS A SG  
825  N N   . GLN A 114 ? 0.1102 0.1529 0.1733 0.0095  -0.0063 -0.0119 131 GLN A N   
826  C CA  . GLN A 114 ? 0.1256 0.1679 0.1873 0.0083  -0.0068 -0.0129 131 GLN A CA  
827  C C   . GLN A 114 ? 0.1405 0.1868 0.2017 0.0095  -0.0079 -0.0139 131 GLN A C   
828  O O   . GLN A 114 ? 0.1756 0.2208 0.2351 0.0100  -0.0082 -0.0140 131 GLN A O   
829  C CB  . GLN A 114 ? 0.1480 0.1904 0.2104 0.0050  -0.0069 -0.0140 131 GLN A CB  
830  C CG  . GLN A 114 ? 0.1422 0.1798 0.2046 0.0035  -0.0060 -0.0131 131 GLN A CG  
831  C CD  . GLN A 114 ? 0.1851 0.2222 0.2476 0.0001  -0.0062 -0.0141 131 GLN A CD  
832  O OE1 . GLN A 114 ? 0.1744 0.2121 0.2361 -0.0011 -0.0070 -0.0152 131 GLN A OE1 
833  N NE2 . GLN A 114 ? 0.1512 0.1870 0.2148 -0.0015 -0.0057 -0.0137 131 GLN A NE2 
834  N N   . GLN A 115 ? 0.1329 0.1839 0.1957 0.0099  -0.0084 -0.0147 132 GLN A N   
835  C CA  . GLN A 115 ? 0.1595 0.2148 0.2221 0.0107  -0.0096 -0.0160 132 GLN A CA  
836  C C   . GLN A 115 ? 0.1495 0.2078 0.2129 0.0134  -0.0101 -0.0158 132 GLN A C   
837  O O   . GLN A 115 ? 0.1451 0.2039 0.2100 0.0140  -0.0097 -0.0153 132 GLN A O   
838  C CB  . GLN A 115 ? 0.1674 0.2262 0.2312 0.0081  -0.0101 -0.0178 132 GLN A CB  
839  C CG  . GLN A 115 ? 0.1866 0.2424 0.2495 0.0054  -0.0098 -0.0181 132 GLN A CG  
840  C CD  . GLN A 115 ? 0.2635 0.3229 0.3272 0.0028  -0.0105 -0.0199 132 GLN A CD  
841  O OE1 . GLN A 115 ? 0.2458 0.3072 0.3112 0.0008  -0.0103 -0.0205 132 GLN A OE1 
842  N NE2 . GLN A 115 ? 0.2674 0.3279 0.3300 0.0028  -0.0114 -0.0208 132 GLN A NE2 
843  N N   . ALA A 116 ? 0.1619 0.2223 0.2243 0.0151  -0.0111 -0.0163 133 ALA A N   
844  C CA  . ALA A 116 ? 0.1650 0.2278 0.2277 0.0179  -0.0119 -0.0161 133 ALA A CA  
845  C C   . ALA A 116 ? 0.1713 0.2388 0.2367 0.0176  -0.0123 -0.0172 133 ALA A C   
846  O O   . ALA A 116 ? 0.1877 0.2562 0.2539 0.0196  -0.0125 -0.0168 133 ALA A O   
847  C CB  . ALA A 116 ? 0.1930 0.2574 0.2541 0.0194  -0.0131 -0.0167 133 ALA A CB  
848  N N   . GLY A 117 ? 0.1644 0.2350 0.2312 0.0151  -0.0124 -0.0189 134 GLY A N   
849  C CA  . GLY A 117 ? 0.1973 0.2729 0.2667 0.0146  -0.0127 -0.0202 134 GLY A CA  
850  C C   . GLY A 117 ? 0.1888 0.2634 0.2597 0.0139  -0.0117 -0.0195 134 GLY A C   
851  O O   . GLY A 117 ? 0.1917 0.2704 0.2648 0.0140  -0.0119 -0.0205 134 GLY A O   
852  N N   . ARG A 118 ? 0.1331 0.2025 0.2030 0.0132  -0.0106 -0.0179 135 ARG A N   
853  C CA  . ARG A 118 ? 0.1514 0.2191 0.2225 0.0128  -0.0096 -0.0170 135 ARG A CA  
854  C C   . ARG A 118 ? 0.1328 0.1950 0.2022 0.0147  -0.0090 -0.0148 135 ARG A C   
855  O O   . ARG A 118 ? 0.1349 0.1927 0.2034 0.0133  -0.0080 -0.0138 135 ARG A O   
856  C CB  . ARG A 118 ? 0.1293 0.1962 0.2010 0.0092  -0.0088 -0.0174 135 ARG A CB  
857  C CG  . ARG A 118 ? 0.1395 0.2120 0.2131 0.0071  -0.0092 -0.0195 135 ARG A CG  
858  C CD  . ARG A 118 ? 0.1662 0.2428 0.2421 0.0083  -0.0093 -0.0201 135 ARG A CD  
859  N NE  . ARG A 118 ? 0.2270 0.3085 0.3049 0.0058  -0.0093 -0.0219 135 ARG A NE  
860  C CZ  . ARG A 118 ? 0.2364 0.3229 0.3166 0.0066  -0.0096 -0.0230 135 ARG A CZ  
861  N NH1 . ARG A 118 ? 0.2384 0.3252 0.3191 0.0099  -0.0099 -0.0224 135 ARG A NH1 
862  N NH2 . ARG A 118 ? 0.2650 0.3562 0.3470 0.0040  -0.0095 -0.0247 135 ARG A NH2 
863  N N   . ASN A 119 ? 0.1235 0.1859 0.1924 0.0178  -0.0096 -0.0141 136 ASN A N   
864  C CA  . ASN A 119 ? 0.1038 0.1614 0.1708 0.0196  -0.0091 -0.0121 136 ASN A CA  
865  C C   . ASN A 119 ? 0.1314 0.1884 0.1994 0.0215  -0.0089 -0.0110 136 ASN A C   
866  O O   . ASN A 119 ? 0.1125 0.1666 0.1790 0.0237  -0.0090 -0.0096 136 ASN A O   
867  C CB  . ASN A 119 ? 0.1199 0.1771 0.1847 0.0214  -0.0100 -0.0120 136 ASN A CB  
868  C CG  . ASN A 119 ? 0.1509 0.2121 0.2161 0.0238  -0.0114 -0.0127 136 ASN A CG  
869  O OD1 . ASN A 119 ? 0.1348 0.1994 0.2022 0.0241  -0.0118 -0.0135 136 ASN A OD1 
870  N ND2 . ASN A 119 ? 0.1543 0.2151 0.2175 0.0254  -0.0123 -0.0125 136 ASN A ND2 
871  N N   . LEU A 120 ? 0.1424 0.2019 0.2128 0.0205  -0.0087 -0.0118 137 LEU A N   
872  C CA  . LEU A 120 ? 0.1002 0.1584 0.1718 0.0211  -0.0080 -0.0107 137 LEU A CA  
873  C C   . LEU A 120 ? 0.1109 0.1704 0.1829 0.0243  -0.0089 -0.0103 137 LEU A C   
874  O O   . LEU A 120 ? 0.1133 0.1745 0.1873 0.0246  -0.0088 -0.0105 137 LEU A O   
875  C CB  . LEU A 120 ? 0.1306 0.1825 0.2006 0.0209  -0.0068 -0.0088 137 LEU A CB  
876  C CG  . LEU A 120 ? 0.1296 0.1796 0.2010 0.0195  -0.0057 -0.0081 137 LEU A CG  
877  C CD1 . LEU A 120 ? 0.1619 0.2131 0.2342 0.0161  -0.0052 -0.0094 137 LEU A CD1 
878  C CD2 . LEU A 120 ? 0.1445 0.1885 0.2143 0.0201  -0.0047 -0.0060 137 LEU A CD2 
879  N N   . ILE A 121 ? 0.1274 0.1867 0.1977 0.0266  -0.0099 -0.0100 138 ILE A N   
880  C CA  . ILE A 121 ? 0.1151 0.1738 0.1850 0.0297  -0.0108 -0.0090 138 ILE A CA  
881  C C   . ILE A 121 ? 0.1403 0.2007 0.2087 0.0318  -0.0123 -0.0095 138 ILE A C   
882  O O   . ILE A 121 ? 0.1432 0.2029 0.2099 0.0311  -0.0124 -0.0097 138 ILE A O   
883  C CB  . ILE A 121 ? 0.1322 0.1851 0.2006 0.0305  -0.0098 -0.0067 138 ILE A CB  
884  C CG1 . ILE A 121 ? 0.1463 0.1986 0.2145 0.0335  -0.0107 -0.0057 138 ILE A CG1 
885  C CG2 . ILE A 121 ? 0.1406 0.1896 0.2062 0.0300  -0.0094 -0.0057 138 ILE A CG2 
886  C CD1 . ILE A 121 ? 0.1511 0.1982 0.2184 0.0340  -0.0097 -0.0035 138 ILE A CD1 
887  N N   . HIS A 122 ? 0.1272 0.1902 0.1965 0.0342  -0.0137 -0.0100 139 HIS A N   
888  C CA  . HIS A 122 ? 0.1352 0.1992 0.2029 0.0367  -0.0154 -0.0102 139 HIS A CA  
889  C C   . HIS A 122 ? 0.1271 0.1872 0.1931 0.0393  -0.0159 -0.0082 139 HIS A C   
890  O O   . HIS A 122 ? 0.1426 0.2020 0.2099 0.0399  -0.0156 -0.0076 139 HIS A O   
891  C CB  . HIS A 122 ? 0.1407 0.2109 0.2107 0.0376  -0.0169 -0.0124 139 HIS A CB  
892  C CG  . HIS A 122 ? 0.1401 0.2109 0.2087 0.0408  -0.0189 -0.0124 139 HIS A CG  
893  N ND1 . HIS A 122 ? 0.1690 0.2408 0.2359 0.0413  -0.0200 -0.0131 139 HIS A ND1 
894  C CD2 . HIS A 122 ? 0.1466 0.2166 0.2151 0.0435  -0.0201 -0.0118 139 HIS A CD2 
895  C CE1 . HIS A 122 ? 0.1757 0.2474 0.2414 0.0442  -0.0218 -0.0129 139 HIS A CE1 
896  N NE2 . HIS A 122 ? 0.1875 0.2581 0.2541 0.0457  -0.0220 -0.0121 139 HIS A NE2 
897  N N   . GLY A 123 ? 0.1518 0.2098 0.2149 0.0409  -0.0168 -0.0073 140 GLY A N   
898  C CA  . GLY A 123 ? 0.1242 0.1791 0.1855 0.0435  -0.0177 -0.0057 140 GLY A CA  
899  C C   . GLY A 123 ? 0.1414 0.1974 0.2007 0.0457  -0.0197 -0.0060 140 GLY A C   
900  O O   . GLY A 123 ? 0.1494 0.2061 0.2073 0.0450  -0.0200 -0.0067 140 GLY A O   
901  N N   . SER A 124 ? 0.1391 0.1945 0.1979 0.0484  -0.0213 -0.0055 141 SER A N   
902  C CA  . SER A 124 ? 0.1451 0.2009 0.2017 0.0507  -0.0235 -0.0057 141 SER A CA  
903  C C   . SER A 124 ? 0.1566 0.2084 0.2093 0.0503  -0.0231 -0.0041 141 SER A C   
904  O O   . SER A 124 ? 0.1689 0.2162 0.2200 0.0496  -0.0217 -0.0022 141 SER A O   
905  C CB  . SER A 124 ? 0.1698 0.2242 0.2259 0.0535  -0.0251 -0.0048 141 SER A CB  
906  O OG  . SER A 124 ? 0.1755 0.2335 0.2351 0.0540  -0.0254 -0.0062 141 SER A OG  
907  N N   . ASP A 125 ? 0.1661 0.2195 0.2173 0.0510  -0.0244 -0.0050 142 ASP A N   
908  C CA  . ASP A 125 ? 0.1963 0.2465 0.2439 0.0505  -0.0241 -0.0038 142 ASP A CA  
909  C C   . ASP A 125 ? 0.2293 0.2763 0.2733 0.0529  -0.0258 -0.0023 142 ASP A C   
910  O O   . ASP A 125 ? 0.2442 0.2882 0.2848 0.0526  -0.0255 -0.0012 142 ASP A O   
911  C CB  . ASP A 125 ? 0.2089 0.2624 0.2567 0.0493  -0.0243 -0.0056 142 ASP A CB  
912  C CG  . ASP A 125 ? 0.2794 0.3366 0.3272 0.0511  -0.0267 -0.0072 142 ASP A CG  
913  O OD1 . ASP A 125 ? 0.2987 0.3559 0.3463 0.0536  -0.0284 -0.0071 142 ASP A OD1 
914  O OD2 . ASP A 125 ? 0.3626 0.4226 0.4106 0.0502  -0.0269 -0.0087 142 ASP A OD2 
915  N N   . SER A 126 ? 0.1926 0.2401 0.2371 0.0553  -0.0276 -0.0024 143 SER A N   
916  C CA  . SER A 126 ? 0.2064 0.2508 0.2474 0.0576  -0.0295 -0.0010 143 SER A CA  
917  C C   . SER A 126 ? 0.1787 0.2230 0.2209 0.0598  -0.0310 -0.0008 143 SER A C   
918  O O   . SER A 126 ? 0.1919 0.2395 0.2378 0.0598  -0.0307 -0.0022 143 SER A O   
919  C CB  . SER A 126 ? 0.2321 0.2787 0.2715 0.0587  -0.0315 -0.0023 143 SER A CB  
920  O OG  . SER A 126 ? 0.2576 0.3092 0.3000 0.0600  -0.0332 -0.0046 143 SER A OG  
921  N N   . ALA A 127 ? 0.2764 0.2660 0.2907 0.0997  -0.0602 0.0210  144 ALA A N   
922  C CA  . ALA A 127 ? 0.2768 0.2682 0.2961 0.0988  -0.0644 0.0180  144 ALA A CA  
923  C C   . ALA A 127 ? 0.2423 0.2381 0.2658 0.1002  -0.0686 0.0094  144 ALA A C   
924  O O   . ALA A 127 ? 0.2674 0.2691 0.2977 0.0994  -0.0700 0.0053  144 ALA A O   
925  C CB  . ALA A 127 ? 0.3315 0.3152 0.3460 0.0981  -0.0668 0.0219  144 ALA A CB  
926  N N   . GLU A 128 ? 0.2647 0.2577 0.2842 0.1022  -0.0704 0.0064  145 GLU A N   
927  C CA  . GLU A 128 ? 0.2643 0.2611 0.2875 0.1034  -0.0743 -0.0018 145 GLU A CA  
928  C C   . GLU A 128 ? 0.2490 0.2553 0.2793 0.1031  -0.0720 -0.0064 145 GLU A C   
929  O O   . GLU A 128 ? 0.2695 0.2811 0.3058 0.1026  -0.0744 -0.0124 145 GLU A O   
930  C CB  . GLU A 128 ? 0.3916 0.3833 0.4086 0.1056  -0.0765 -0.0035 145 GLU A CB  
931  C CG  . GLU A 128 ? 0.6307 0.6135 0.6413 0.1057  -0.0792 0.0000  145 GLU A CG  
932  C CD  . GLU A 128 ? 0.6864 0.6630 0.6908 0.1047  -0.0753 0.0085  145 GLU A CD  
933  O OE1 . GLU A 128 ? 0.4371 0.4153 0.4409 0.1043  -0.0705 0.0120  145 GLU A OE1 
934  O OE2 . GLU A 128 ? 0.7500 0.7201 0.7500 0.1043  -0.0770 0.0118  145 GLU A OE2 
935  N N   . SER A 129 ? 0.2437 0.2521 0.2731 0.1034  -0.0671 -0.0039 146 SER A N   
936  C CA  A SER A 129 ? 0.2177 0.2355 0.2540 0.1026  -0.0641 -0.0083 146 SER A CA  
937  C CA  B SER A 129 ? 0.2172 0.2350 0.2534 0.1025  -0.0639 -0.0080 146 SER A CA  
938  C C   . SER A 129 ? 0.2301 0.2537 0.2733 0.1006  -0.0629 -0.0077 146 SER A C   
939  O O   . SER A 129 ? 0.2252 0.2565 0.2753 0.0995  -0.0629 -0.0133 146 SER A O   
940  C CB  A SER A 129 ? 0.2390 0.2573 0.2716 0.1007  -0.0571 -0.0054 146 SER A CB  
941  C CB  B SER A 129 ? 0.2390 0.2569 0.2713 0.1005  -0.0566 -0.0045 146 SER A CB  
942  O OG  A SER A 129 ? 0.2438 0.2589 0.2729 0.0989  -0.0524 0.0026  146 SER A OG  
943  O OG  B SER A 129 ? 0.2419 0.2557 0.2686 0.1020  -0.0575 -0.0062 146 SER A OG  
944  N N   . ALA A 130 ? 0.1993 0.2192 0.2404 0.0995  -0.0617 -0.0011 147 ALA A N   
945  C CA  . ALA A 130 ? 0.2045 0.2295 0.2519 0.0973  -0.0607 -0.0005 147 ALA A CA  
946  C C   . ALA A 130 ? 0.2359 0.2626 0.2876 0.0965  -0.0656 -0.0062 147 ALA A C   
947  O O   . ALA A 130 ? 0.2254 0.2594 0.2840 0.0950  -0.0650 -0.0101 147 ALA A O   
948  C CB  . ALA A 130 ? 0.2004 0.2205 0.2443 0.0962  -0.0589 0.0078  147 ALA A CB  
949  N N   . LYS A 131 ? 0.2208 0.2409 0.2682 0.0975  -0.0701 -0.0068 148 LYS A N   
950  C CA  . LYS A 131 ? 0.2427 0.2640 0.2936 0.0970  -0.0746 -0.0121 148 LYS A CA  
951  C C   . LYS A 131 ? 0.2185 0.2464 0.2741 0.0972  -0.0752 -0.0199 148 LYS A C   
952  O O   . LYS A 131 ? 0.2665 0.2998 0.3280 0.0958  -0.0758 -0.0240 148 LYS A O   
953  C CB  . LYS A 131 ? 0.2592 0.2723 0.3041 0.0984  -0.0789 -0.0114 148 LYS A CB  
954  C CG  . LYS A 131 ? 0.5170 0.5301 0.5646 0.0980  -0.0833 -0.0158 148 LYS A CG  
955  C CD  . LYS A 131 ? 0.6620 0.6668 0.7035 0.0993  -0.0872 -0.0145 148 LYS A CD  
956  C CE  . LYS A 131 ? 0.8464 0.8511 0.8904 0.0993  -0.0915 -0.0192 148 LYS A CE  
957  N NZ  . LYS A 131 ? 0.9323 0.9419 0.9801 0.0999  -0.0933 -0.0269 148 LYS A NZ  
958  N N   . ARG A 132 ? 0.2158 0.2434 0.2689 0.0989  -0.0748 -0.0219 149 ARG A N   
959  C CA  . ARG A 132 ? 0.2505 0.2840 0.3077 0.0990  -0.0755 -0.0294 149 ARG A CA  
960  C C   . ARG A 132 ? 0.2495 0.2920 0.3135 0.0970  -0.0711 -0.0311 149 ARG A C   
961  O O   . ARG A 132 ? 0.2160 0.2640 0.2852 0.0957  -0.0718 -0.0369 149 ARG A O   
962  C CB  . ARG A 132 ? 0.2731 0.3043 0.3258 0.1012  -0.0756 -0.0306 149 ARG A CB  
963  C CG  . ARG A 132 ? 0.2822 0.3189 0.3385 0.1014  -0.0766 -0.0382 149 ARG A CG  
964  C CD  . ARG A 132 ? 0.3735 0.4072 0.4248 0.1038  -0.0772 -0.0391 149 ARG A CD  
965  N NE  . ARG A 132 ? 0.4565 0.4940 0.5084 0.1037  -0.0718 -0.0375 149 ARG A NE  
966  C CZ  . ARG A 132 ? 0.4546 0.4998 0.5116 0.1028  -0.0692 -0.0423 149 ARG A CZ  
967  N NH1 . ARG A 132 ? 0.4515 0.5009 0.5128 0.1020  -0.0719 -0.0492 149 ARG A NH1 
968  N NH2 . ARG A 132 ? 0.3607 0.4093 0.4183 0.1020  -0.0633 -0.0400 149 ARG A NH2 
969  N N   . GLU A 133 ? 0.1923 0.2361 0.2559 0.0965  -0.0662 -0.0261 150 GLU A N   
970  C CA  . GLU A 133 ? 0.1697 0.2222 0.2395 0.0945  -0.0614 -0.0274 150 GLU A CA  
971  C C   . GLU A 133 ? 0.2021 0.2579 0.2770 0.0920  -0.0616 -0.0275 150 GLU A C   
972  O O   . GLU A 133 ? 0.1774 0.2402 0.2581 0.0900  -0.0600 -0.0318 150 GLU A O   
973  C CB  . GLU A 133 ? 0.1856 0.2382 0.2530 0.0950  -0.0560 -0.0216 150 GLU A CB  
974  C CG  . GLU A 133 ? 0.2073 0.2575 0.2696 0.0961  -0.0543 -0.0222 150 GLU A CG  
975  C CD  . GLU A 133 ? 0.1981 0.2450 0.2546 0.0942  -0.0475 -0.0150 150 GLU A CD  
976  O OE1 . GLU A 133 ? 0.2134 0.2611 0.2707 0.0922  -0.0439 -0.0097 150 GLU A OE1 
977  O OE2 . GLU A 133 ? 0.2339 0.2776 0.2851 0.0947  -0.0459 -0.0150 150 GLU A OE2 
978  N N   . ILE A 134 ? 0.2148 0.2658 0.2876 0.0920  -0.0632 -0.0226 151 ILE A N   
979  C CA  . ILE A 134 ? 0.2430 0.2969 0.3204 0.0897  -0.0636 -0.0228 151 ILE A CA  
980  C C   . ILE A 134 ? 0.2473 0.3029 0.3277 0.0892  -0.0674 -0.0300 151 ILE A C   
981  O O   . ILE A 134 ? 0.2460 0.3073 0.3317 0.0871  -0.0663 -0.0330 151 ILE A O   
982  C CB  . ILE A 134 ? 0.1783 0.2259 0.2522 0.0899  -0.0652 -0.0165 151 ILE A CB  
983  C CG1 . ILE A 134 ? 0.1947 0.2415 0.2664 0.0898  -0.0607 -0.0091 151 ILE A CG1 
984  C CG2 . ILE A 134 ? 0.2138 0.2638 0.2922 0.0878  -0.0664 -0.0174 151 ILE A CG2 
985  C CD1 . ILE A 134 ? 0.2354 0.2752 0.3027 0.0899  -0.0618 -0.0023 151 ILE A CD1 
986  N N   . SER A 135 ? 0.2120 0.2628 0.2888 0.0912  -0.0718 -0.0328 152 SER A N   
987  C CA  . SER A 135 ? 0.2394 0.2913 0.3185 0.0910  -0.0754 -0.0395 152 SER A CA  
988  C C   . SER A 135 ? 0.2532 0.3120 0.3363 0.0901  -0.0734 -0.0454 152 SER A C   
989  O O   . SER A 135 ? 0.2763 0.3382 0.3631 0.0889  -0.0747 -0.0505 152 SER A O   
990  C CB  . SER A 135 ? 0.2976 0.3425 0.3716 0.0934  -0.0804 -0.0406 152 SER A CB  
991  O OG  . SER A 135 ? 0.3891 0.4278 0.4598 0.0937  -0.0822 -0.0357 152 SER A OG  
992  N N   . LEU A 136 ? 0.2079 0.2687 0.2901 0.0907  -0.0703 -0.0449 153 LEU A N   
993  C CA  . LEU A 136 ? 0.1552 0.2224 0.2409 0.0896  -0.0681 -0.0503 153 LEU A CA  
994  C C   . LEU A 136 ? 0.1946 0.2686 0.2859 0.0864  -0.0641 -0.0509 153 LEU A C   
995  O O   . LEU A 136 ? 0.2044 0.2826 0.2992 0.0849  -0.0641 -0.0564 153 LEU A O   
996  C CB  . LEU A 136 ? 0.2060 0.2734 0.2890 0.0910  -0.0654 -0.0492 153 LEU A CB  
997  C CG  . LEU A 136 ? 0.2110 0.2850 0.2972 0.0898  -0.0621 -0.0539 153 LEU A CG  
998  C CD1 . LEU A 136 ? 0.2654 0.3401 0.3526 0.0900  -0.0661 -0.0612 153 LEU A CD1 
999  C CD2 . LEU A 136 ? 0.2229 0.2964 0.3059 0.0914  -0.0592 -0.0519 153 LEU A CD2 
1000 N N   . TRP A 137 ? 0.1824 0.2574 0.2744 0.0854  -0.0605 -0.0452 154 TRP A N   
1001 C CA  . TRP A 137 ? 0.1504 0.2320 0.2473 0.0824  -0.0558 -0.0449 154 TRP A CA  
1002 C C   . TRP A 137 ? 0.1549 0.2368 0.2545 0.0806  -0.0571 -0.0441 154 TRP A C   
1003 O O   . TRP A 137 ? 0.2081 0.2954 0.3118 0.0779  -0.0540 -0.0453 154 TRP A O   
1004 C CB  . TRP A 137 ? 0.1664 0.2495 0.2626 0.0822  -0.0506 -0.0390 154 TRP A CB  
1005 C CG  . TRP A 137 ? 0.1650 0.2490 0.2592 0.0834  -0.0479 -0.0397 154 TRP A CG  
1006 C CD1 . TRP A 137 ? 0.1866 0.2655 0.2757 0.0863  -0.0490 -0.0373 154 TRP A CD1 
1007 C CD2 . TRP A 137 ? 0.1456 0.2356 0.2425 0.0815  -0.0435 -0.0429 154 TRP A CD2 
1008 N NE1 . TRP A 137 ? 0.1671 0.2488 0.2557 0.0866  -0.0455 -0.0389 154 TRP A NE1 
1009 C CE2 . TRP A 137 ? 0.1521 0.2407 0.2455 0.0836  -0.0421 -0.0425 154 TRP A CE2 
1010 C CE3 . TRP A 137 ? 0.1412 0.2372 0.2426 0.0781  -0.0407 -0.0461 154 TRP A CE3 
1011 C CZ2 . TRP A 137 ? 0.1947 0.2879 0.2892 0.0823  -0.0376 -0.0449 154 TRP A CZ2 
1012 C CZ3 . TRP A 137 ? 0.1702 0.2704 0.2724 0.0767  -0.0363 -0.0483 154 TRP A CZ3 
1013 C CH2 . TRP A 137 ? 0.1866 0.2855 0.2856 0.0788  -0.0348 -0.0479 154 TRP A CH2 
1014 N N   . PHE A 138 ? 0.2052 0.2230 0.2737 0.0909  -0.0327 -0.0272 155 PHE A N   
1015 C CA  . PHE A 138 ? 0.2434 0.2565 0.3103 0.0920  -0.0338 -0.0276 155 PHE A CA  
1016 C C   . PHE A 138 ? 0.2659 0.2729 0.3284 0.0960  -0.0385 -0.0289 155 PHE A C   
1017 O O   . PHE A 138 ? 0.2899 0.2924 0.3488 0.0983  -0.0417 -0.0290 155 PHE A O   
1018 C CB  . PHE A 138 ? 0.2095 0.2174 0.2755 0.0910  -0.0331 -0.0259 155 PHE A CB  
1019 C CG  . PHE A 138 ? 0.1752 0.1885 0.2454 0.0869  -0.0282 -0.0244 155 PHE A CG  
1020 C CD1 . PHE A 138 ? 0.1795 0.1956 0.2517 0.0855  -0.0265 -0.0253 155 PHE A CD1 
1021 C CD2 . PHE A 138 ? 0.1955 0.2109 0.2670 0.0850  -0.0261 -0.0231 155 PHE A CD2 
1022 C CE1 . PHE A 138 ? 0.1956 0.2162 0.2710 0.0821  -0.0227 -0.0246 155 PHE A CE1 
1023 C CE2 . PHE A 138 ? 0.1779 0.1980 0.2528 0.0813  -0.0216 -0.0217 155 PHE A CE2 
1024 C CZ  . PHE A 138 ? 0.1939 0.2164 0.2705 0.0799  -0.0201 -0.0226 155 PHE A CZ  
1025 N N   . LYS A 139 ? 0.2395 0.2461 0.3013 0.0975  -0.0401 -0.0310 156 LYS A N   
1026 C CA  . LYS A 139 ? 0.3255 0.3247 0.3824 0.1011  -0.0445 -0.0319 156 LYS A CA  
1027 C C   . LYS A 139 ? 0.2564 0.2465 0.3097 0.1018  -0.0467 -0.0312 156 LYS A C   
1028 O O   . LYS A 139 ? 0.2473 0.2382 0.3030 0.0992  -0.0438 -0.0299 156 LYS A O   
1029 C CB  . LYS A 139 ? 0.3605 0.3624 0.4174 0.1031  -0.0463 -0.0352 156 LYS A CB  
1030 C CG  . LYS A 139 ? 0.4551 0.4662 0.5149 0.1032  -0.0456 -0.0376 156 LYS A CG  
1031 C CD  . LYS A 139 ? 0.6110 0.6260 0.6722 0.1036  -0.0457 -0.0402 156 LYS A CD  
1032 C CE  . LYS A 139 ? 0.6673 0.6889 0.7292 0.1054  -0.0471 -0.0432 156 LYS A CE  
1033 N NZ  . LYS A 139 ? 0.8368 0.8657 0.9021 0.1030  -0.0444 -0.0429 156 LYS A NZ  
1034 N N   . PRO A 140 ? 0.2651 0.2461 0.3123 0.1052  -0.0519 -0.0319 157 PRO A N   
1035 C CA  . PRO A 140 ? 0.2786 0.2494 0.3214 0.1057  -0.0545 -0.0308 157 PRO A CA  
1036 C C   . PRO A 140 ? 0.2957 0.2659 0.3399 0.1046  -0.0533 -0.0311 157 PRO A C   
1037 O O   . PRO A 140 ? 0.2884 0.2541 0.3319 0.1031  -0.0529 -0.0295 157 PRO A O   
1038 C CB  . PRO A 140 ? 0.4245 0.3859 0.4601 0.1097  -0.0606 -0.0318 157 PRO A CB  
1039 C CG  . PRO A 140 ? 0.3386 0.3052 0.3751 0.1107  -0.0606 -0.0325 157 PRO A CG  
1040 C CD  . PRO A 140 ? 0.3260 0.3047 0.3695 0.1085  -0.0557 -0.0332 157 PRO A CD  
1041 N N   . GLU A 141 ? 0.2828 0.2576 0.3288 0.1053  -0.0528 -0.0329 158 GLU A N   
1042 C CA  . GLU A 141 ? 0.3173 0.2921 0.3647 0.1043  -0.0516 -0.0332 158 GLU A CA  
1043 C C   . GLU A 141 ? 0.3013 0.2830 0.3545 0.1001  -0.0459 -0.0316 158 GLU A C   
1044 O O   . GLU A 141 ? 0.2903 0.2711 0.3444 0.0989  -0.0447 -0.0314 158 GLU A O   
1045 C CB  . GLU A 141 ? 0.3832 0.3620 0.4312 0.1060  -0.0523 -0.0355 158 GLU A CB  
1046 C CG  . GLU A 141 ? 0.5191 0.5079 0.5708 0.1059  -0.0506 -0.0372 158 GLU A CG  
1047 C CD  . GLU A 141 ? 0.6909 0.6782 0.7392 0.1093  -0.0543 -0.0387 158 GLU A CD  
1048 O OE1 . GLU A 141 ? 0.4610 0.4422 0.5059 0.1103  -0.0562 -0.0372 158 GLU A OE1 
1049 O OE2 . GLU A 141 ? 0.7319 0.7243 0.7806 0.1114  -0.0557 -0.0418 158 GLU A OE2 
1050 N N   . GLU A 142 ? 0.2466 0.2349 0.3034 0.0978  -0.0424 -0.0304 159 GLU A N   
1051 C CA  A GLU A 142 ? 0.2286 0.2231 0.2904 0.0937  -0.0370 -0.0288 159 GLU A CA  
1052 C CA  B GLU A 142 ? 0.2282 0.2228 0.2901 0.0937  -0.0370 -0.0288 159 GLU A CA  
1053 C C   . GLU A 142 ? 0.2070 0.1969 0.2680 0.0926  -0.0367 -0.0271 159 GLU A C   
1054 O O   . GLU A 142 ? 0.2247 0.2186 0.2892 0.0893  -0.0326 -0.0259 159 GLU A O   
1055 C CB  A GLU A 142 ? 0.2242 0.2281 0.2899 0.0922  -0.0345 -0.0294 159 GLU A CB  
1056 C CB  B GLU A 142 ? 0.2213 0.2249 0.2868 0.0921  -0.0344 -0.0291 159 GLU A CB  
1057 C CG  A GLU A 142 ? 0.2436 0.2529 0.3102 0.0938  -0.0360 -0.0328 159 GLU A CG  
1058 C CG  B GLU A 142 ? 0.2548 0.2640 0.3211 0.0939  -0.0361 -0.0325 159 GLU A CG  
1059 C CD  A GLU A 142 ? 0.2925 0.3099 0.3617 0.0929  -0.0348 -0.0340 159 GLU A CD  
1060 C CD  B GLU A 142 ? 0.2552 0.2724 0.3245 0.0924  -0.0343 -0.0331 159 GLU A CD  
1061 O OE1 A GLU A 142 ? 0.3089 0.3269 0.3784 0.0922  -0.0340 -0.0325 159 GLU A OE1 
1062 O OE1 B GLU A 142 ? 0.2544 0.2771 0.3272 0.0892  -0.0309 -0.0327 159 GLU A OE1 
1063 O OE2 A GLU A 142 ? 0.3629 0.3861 0.4339 0.0931  -0.0349 -0.0364 159 GLU A OE2 
1064 O OE2 B GLU A 142 ? 0.2637 0.2814 0.3317 0.0943  -0.0362 -0.0337 159 GLU A OE2 
1065 N N   . ILE A 143 ? 0.1859 0.1668 0.2418 0.0950  -0.0411 -0.0269 160 ILE A N   
1066 C CA  . ILE A 143 ? 0.2214 0.1968 0.2756 0.0941  -0.0414 -0.0251 160 ILE A CA  
1067 C C   . ILE A 143 ? 0.2136 0.1805 0.2647 0.0945  -0.0437 -0.0249 160 ILE A C   
1068 O O   . ILE A 143 ? 0.2674 0.2265 0.3134 0.0971  -0.0484 -0.0257 160 ILE A O   
1069 C CB  . ILE A 143 ? 0.2609 0.2303 0.3105 0.0962  -0.0453 -0.0245 160 ILE A CB  
1070 C CG1 . ILE A 143 ? 0.2432 0.2207 0.2955 0.0962  -0.0435 -0.0250 160 ILE A CG1 
1071 C CG2 . ILE A 143 ? 0.2731 0.2367 0.3208 0.0952  -0.0457 -0.0222 160 ILE A CG2 
1072 C CD1 . ILE A 143 ? 0.2936 0.2804 0.3517 0.0929  -0.0382 -0.0240 160 ILE A CD1 
1073 N N   . GLN A 144 ? 0.2091 0.1772 0.2629 0.0918  -0.0406 -0.0237 161 GLN A N   
1074 C CA  . GLN A 144 ? 0.2405 0.2021 0.2924 0.0915  -0.0419 -0.0234 161 GLN A CA  
1075 C C   . GLN A 144 ? 0.2161 0.1673 0.2636 0.0912  -0.0447 -0.0214 161 GLN A C   
1076 O O   . GLN A 144 ? 0.2589 0.2125 0.3084 0.0895  -0.0424 -0.0199 161 GLN A O   
1077 C CB  . GLN A 144 ? 0.2094 0.1796 0.2673 0.0884  -0.0363 -0.0235 161 GLN A CB  
1078 C CG  . GLN A 144 ? 0.2237 0.2044 0.2858 0.0877  -0.0330 -0.0246 161 GLN A CG  
1079 C CD  . GLN A 144 ? 0.2315 0.2099 0.2911 0.0904  -0.0363 -0.0265 161 GLN A CD  
1080 O OE1 . GLN A 144 ? 0.2605 0.2313 0.3166 0.0919  -0.0395 -0.0270 161 GLN A OE1 
1081 N NE2 . GLN A 144 ? 0.2302 0.2147 0.2913 0.0911  -0.0357 -0.0275 161 GLN A NE2 
1082 N N   . SER A 145 ? 0.2419 0.1813 0.2829 0.0927  -0.0497 -0.0210 162 SER A N   
1083 C CA  A SER A 145 ? 0.2403 0.1674 0.2754 0.0919  -0.0532 -0.0183 162 SER A CA  
1084 C CA  B SER A 145 ? 0.2410 0.1680 0.2761 0.0919  -0.0532 -0.0183 162 SER A CA  
1085 C C   . SER A 145 ? 0.2748 0.1982 0.3103 0.0898  -0.0524 -0.0177 162 SER A C   
1086 O O   . SER A 145 ? 0.2806 0.2015 0.3147 0.0907  -0.0539 -0.0190 162 SER A O   
1087 C CB  A SER A 145 ? 0.2912 0.2055 0.3171 0.0942  -0.0600 -0.0177 162 SER A CB  
1088 C CB  B SER A 145 ? 0.2917 0.2060 0.3175 0.0942  -0.0600 -0.0177 162 SER A CB  
1089 O OG  A SER A 145 ? 0.3444 0.2452 0.3633 0.0925  -0.0637 -0.0145 162 SER A OG  
1090 O OG  B SER A 145 ? 0.2888 0.2057 0.3139 0.0959  -0.0608 -0.0180 162 SER A OG  
1091 N N   . TYR A 146 ? 0.2704 0.1934 0.3077 0.0871  -0.0502 -0.0157 163 TYR A N   
1092 C CA  . TYR A 146 ? 0.2381 0.1557 0.2748 0.0848  -0.0500 -0.0144 163 TYR A CA  
1093 C C   . TYR A 146 ? 0.2624 0.1747 0.2977 0.0822  -0.0503 -0.0112 163 TYR A C   
1094 O O   . TYR A 146 ? 0.2631 0.1791 0.2995 0.0825  -0.0494 -0.0105 163 TYR A O   
1095 C CB  . TYR A 146 ? 0.2235 0.1530 0.2684 0.0835  -0.0443 -0.0165 163 TYR A CB  
1096 C CG  . TYR A 146 ? 0.1863 0.1296 0.2390 0.0820  -0.0381 -0.0171 163 TYR A CG  
1097 C CD1 . TYR A 146 ? 0.2050 0.1584 0.2610 0.0830  -0.0358 -0.0187 163 TYR A CD1 
1098 C CD2 . TYR A 146 ? 0.1853 0.1312 0.2418 0.0791  -0.0348 -0.0159 163 TYR A CD2 
1099 C CE1 . TYR A 146 ? 0.1965 0.1617 0.2586 0.0810  -0.0303 -0.0188 163 TYR A CE1 
1100 C CE2 . TYR A 146 ? 0.1807 0.1393 0.2438 0.0775  -0.0292 -0.0165 163 TYR A CE2 
1101 C CZ  . TYR A 146 ? 0.1604 0.1283 0.2258 0.0783  -0.0270 -0.0178 163 TYR A CZ  
1102 O OH  . TYR A 146 ? 0.1915 0.1707 0.2620 0.0762  -0.0218 -0.0178 163 TYR A OH  
1103 N N   . LYS A 147 ? 0.2579 0.1612 0.2901 0.0796  -0.0517 -0.0089 164 LYS A N   
1104 C CA  . LYS A 147 ? 0.2681 0.1663 0.2974 0.0749  -0.0514 -0.0048 164 LYS A CA  
1105 C C   . LYS A 147 ? 0.2643 0.1734 0.3015 0.0708  -0.0445 -0.0051 164 LYS A C   
1106 O O   . LYS A 147 ? 0.2679 0.1768 0.3087 0.0718  -0.0440 -0.0069 164 LYS A O   
1107 C CB  . LYS A 147 ? 0.3309 0.2130 0.3486 0.0710  -0.0563 -0.0007 164 LYS A CB  
1108 C CG  . LYS A 147 ? 0.4055 0.2867 0.4178 0.0623  -0.0535 0.0046  164 LYS A CG  
1109 C CD  . LYS A 147 ? 0.5095 0.3754 0.5114 0.0581  -0.0582 0.0087  164 LYS A CD  
1110 C CE  . LYS A 147 ? 0.5492 0.4142 0.5450 0.0494  -0.0561 0.0142  164 LYS A CE  
1111 N NZ  . LYS A 147 ? 0.7936 0.6444 0.7797 0.0446  -0.0602 0.0184  164 LYS A NZ  
1112 N N   . LEU A 148 ? 0.2507 0.1688 0.2900 0.0662  -0.0394 -0.0034 165 LEU A N   
1113 C CA  . LEU A 148 ? 0.1903 0.1185 0.2364 0.0619  -0.0329 -0.0034 165 LEU A CA  
1114 C C   . LEU A 148 ? 0.2478 0.1680 0.2881 0.0557  -0.0330 0.0004  165 LEU A C   
1115 O O   . LEU A 148 ? 0.2501 0.1611 0.2809 0.0514  -0.0357 0.0047  165 LEU A O   
1116 C CB  . LEU A 148 ? 0.2317 0.1709 0.2808 0.0588  -0.0278 -0.0024 165 LEU A CB  
1117 C CG  . LEU A 148 ? 0.2453 0.1958 0.3026 0.0641  -0.0260 -0.0064 165 LEU A CG  
1118 C CD1 . LEU A 148 ? 0.2427 0.2017 0.3007 0.0604  -0.0218 -0.0048 165 LEU A CD1 
1119 C CD2 . LEU A 148 ? 0.2619 0.2215 0.3298 0.0671  -0.0230 -0.0106 165 LEU A CD2 
1120 N N   . ALA A 149 ? 0.2602 0.1843 0.3064 0.0550  -0.0302 -0.0011 166 ALA A N   
1121 C CA  . ALA A 149 ? 0.2789 0.1960 0.3204 0.0492  -0.0301 0.0022  166 ALA A CA  
1122 C C   . ALA A 149 ? 0.2344 0.1544 0.2722 0.0412  -0.0264 0.0067  166 ALA A C   
1123 O O   . ALA A 149 ? 0.2769 0.1881 0.3070 0.0358  -0.0281 0.0108  166 ALA A O   
1124 C CB  . ALA A 149 ? 0.3441 0.2672 0.3940 0.0502  -0.0268 -0.0007 166 ALA A CB  
1125 N N   . LEU A 150 ? 0.2153 0.1473 0.2580 0.0404  -0.0217 0.0061  167 LEU A N   
1126 C CA  . LEU A 150 ? 0.2128 0.1488 0.2523 0.0333  -0.0180 0.0101  167 LEU A CA  
1127 C C   . LEU A 150 ? 0.2186 0.1496 0.2497 0.0318  -0.0208 0.0132  167 LEU A C   
1128 O O   . LEU A 150 ? 0.2276 0.1642 0.2569 0.0269  -0.0175 0.0159  167 LEU A O   
1129 C CB  . LEU A 150 ? 0.2302 0.1820 0.2794 0.0328  -0.0110 0.0077  167 LEU A CB  
1130 C CG  . LEU A 150 ? 0.2496 0.2071 0.3051 0.0303  -0.0067 0.0068  167 LEU A CG  
1131 C CD1 . LEU A 150 ? 0.3265 0.2991 0.3924 0.0317  -0.0008 0.0035  167 LEU A CD1 
1132 C CD2 . LEU A 150 ? 0.3907 0.3452 0.4404 0.0225  -0.0052 0.0115  167 LEU A CD2 
1133 N N   . SER A 151 ? 0.2500 0.1702 0.2754 0.0358  -0.0271 0.0131  168 SER A N   
1134 C CA  A SER A 151 ? 0.2514 0.1668 0.2691 0.0352  -0.0302 0.0156  168 SER A CA  
1135 C CA  B SER A 151 ? 0.2504 0.1659 0.2681 0.0352  -0.0301 0.0156  168 SER A CA  
1136 C C   . SER A 151 ? 0.2651 0.1771 0.2746 0.0270  -0.0295 0.0214  168 SER A C   
1137 O O   . SER A 151 ? 0.2687 0.1847 0.2755 0.0248  -0.0281 0.0233  168 SER A O   
1138 C CB  A SER A 151 ? 0.2914 0.1935 0.3032 0.0402  -0.0376 0.0149  168 SER A CB  
1139 C CB  B SER A 151 ? 0.2908 0.1933 0.3028 0.0403  -0.0375 0.0149  168 SER A CB  
1140 O OG  A SER A 151 ? 0.3146 0.2105 0.3181 0.0393  -0.0411 0.0178  168 SER A OG  
1141 O OG  B SER A 151 ? 0.3586 0.2661 0.3772 0.0480  -0.0381 0.0100  168 SER A OG  
1142 N N   . ASP A 152 ? 0.2755 0.1804 0.2807 0.0225  -0.0305 0.0241  169 ASP A N   
1143 C CA  . ASP A 152 ? 0.2959 0.1972 0.2928 0.0144  -0.0303 0.0299  169 ASP A CA  
1144 C C   . ASP A 152 ? 0.2636 0.1790 0.2647 0.0100  -0.0233 0.0308  169 ASP A C   
1145 O O   . ASP A 152 ? 0.3039 0.2191 0.2984 0.0041  -0.0228 0.0353  169 ASP A O   
1146 C CB  . ASP A 152 ? 0.3509 0.2430 0.3435 0.0102  -0.0323 0.0325  169 ASP A CB  
1147 C CG  . ASP A 152 ? 0.4801 0.3560 0.4658 0.0134  -0.0401 0.0327  169 ASP A CG  
1148 O OD1 . ASP A 152 ? 0.4867 0.3564 0.4675 0.0166  -0.0445 0.0327  169 ASP A OD1 
1149 O OD2 . ASP A 152 ? 0.6197 0.4888 0.6046 0.0128  -0.0419 0.0327  169 ASP A OD2 
1150 N N   . TYR A 153 ? 0.2202 0.1479 0.2319 0.0125  -0.0181 0.0268  170 TYR A N   
1151 C CA  . TYR A 153 ? 0.2034 0.1448 0.2197 0.0090  -0.0115 0.0271  170 TYR A CA  
1152 C C   . TYR A 153 ? 0.1986 0.1494 0.2196 0.0130  -0.0095 0.0244  170 TYR A C   
1153 O O   . TYR A 153 ? 0.2328 0.1948 0.2573 0.0106  -0.0044 0.0243  170 TYR A O   
1154 C CB  . TYR A 153 ? 0.2070 0.1556 0.2317 0.0083  -0.0069 0.0248  170 TYR A CB  
1155 C CG  . TYR A 153 ? 0.2413 0.1813 0.2607 0.0032  -0.0085 0.0282  170 TYR A CG  
1156 C CD1 . TYR A 153 ? 0.2333 0.1746 0.2474 -0.0044 -0.0065 0.0329  170 TYR A CD1 
1157 C CD2 . TYR A 153 ? 0.2358 0.1659 0.2548 0.0061  -0.0126 0.0269  170 TYR A CD2 
1158 C CE1 . TYR A 153 ? 0.3089 0.2420 0.3177 -0.0094 -0.0082 0.0364  170 TYR A CE1 
1159 C CE2 . TYR A 153 ? 0.2713 0.1928 0.2849 0.0013  -0.0145 0.0301  170 TYR A CE2 
1160 C CZ  . TYR A 153 ? 0.3207 0.2438 0.3293 -0.0065 -0.0122 0.0349  170 TYR A CZ  
1161 O OH  . TYR A 153 ? 0.3518 0.2669 0.3551 -0.0117 -0.0140 0.0384  170 TYR A OH  
1162 N N   . ILE A 154 ? 0.2299 0.1761 0.2506 0.0190  -0.0135 0.0220  171 ILE A N   
1163 C CA  . ILE A 154 ? 0.2223 0.1763 0.2468 0.0230  -0.0124 0.0196  171 ILE A CA  
1164 C C   . ILE A 154 ? 0.2412 0.1890 0.2565 0.0219  -0.0159 0.0228  171 ILE A C   
1165 O O   . ILE A 154 ? 0.2883 0.2435 0.3038 0.0211  -0.0135 0.0232  171 ILE A O   
1166 C CB  . ILE A 154 ? 0.2636 0.2182 0.2951 0.0309  -0.0142 0.0144  171 ILE A CB  
1167 C CG1 . ILE A 154 ? 0.2239 0.1868 0.2653 0.0321  -0.0100 0.0110  171 ILE A CG1 
1168 C CG2 . ILE A 154 ? 0.2583 0.2188 0.2922 0.0353  -0.0142 0.0122  171 ILE A CG2 
1169 C CD1 . ILE A 154 ? 0.2898 0.2511 0.3367 0.0391  -0.0126 0.0066  171 ILE A CD1 
1170 N N   . PHE A 155 ? 0.2569 0.1908 0.2640 0.0218  -0.0218 0.0251  172 PHE A N   
1171 C CA  . PHE A 155 ? 0.2550 0.1814 0.2530 0.0211  -0.0260 0.0281  172 PHE A CA  
1172 C C   . PHE A 155 ? 0.3472 0.2674 0.3357 0.0133  -0.0269 0.0340  172 PHE A C   
1173 O O   . PHE A 155 ? 0.3693 0.2847 0.3561 0.0098  -0.0273 0.0357  172 PHE A O   
1174 C CB  . PHE A 155 ? 0.2736 0.1885 0.2686 0.0270  -0.0326 0.0264  172 PHE A CB  
1175 C CG  . PHE A 155 ? 0.2725 0.1937 0.2769 0.0346  -0.0320 0.0207  172 PHE A CG  
1176 C CD1 . PHE A 155 ? 0.2569 0.1872 0.2656 0.0376  -0.0298 0.0185  172 PHE A CD1 
1177 C CD2 . PHE A 155 ? 0.3088 0.2274 0.3179 0.0385  -0.0333 0.0175  172 PHE A CD2 
1178 C CE1 . PHE A 155 ? 0.2683 0.2049 0.2857 0.0443  -0.0292 0.0134  172 PHE A CE1 
1179 C CE2 . PHE A 155 ? 0.3225 0.2477 0.3402 0.0453  -0.0326 0.0124  172 PHE A CE2 
1180 C CZ  . PHE A 155 ? 0.2823 0.2165 0.3042 0.0481  -0.0306 0.0105  172 PHE A CZ  
1181 N N   . GLU A 156 ? 0.3974 0.3182 0.3798 0.0104  -0.0272 0.0371  173 GLU A N   
1182 C CA  . GLU A 156 ? 0.4741 0.3898 0.4473 0.0026  -0.0281 0.0430  173 GLU A CA  
1183 C C   . GLU A 156 ? 0.6084 0.5072 0.5723 0.0027  -0.0355 0.0455  173 GLU A C   
1184 O O   . GLU A 156 ? 0.6597 0.5510 0.6157 -0.0035 -0.0375 0.0503  173 GLU A O   
1185 C CB  . GLU A 156 ? 0.4672 0.3904 0.4371 -0.0007 -0.0255 0.0456  173 GLU A CB  
1186 C CG  . GLU A 156 ? 0.4890 0.4103 0.4567 0.0038  -0.0285 0.0445  173 GLU A CG  
1187 C CD  . GLU A 156 ? 0.5385 0.4682 0.5037 0.0007  -0.0256 0.0468  173 GLU A CD  
1188 O OE1 . GLU A 156 ? 0.3475 0.2901 0.3178 -0.0014 -0.0197 0.0461  173 GLU A OE1 
1189 O OE2 . GLU A 156 ? 0.5128 0.4361 0.4706 0.0007  -0.0295 0.0490  173 GLU A OE2 
1190 O OXT . GLU A 156 ? 0.5733 0.4653 0.5372 0.0089  -0.0399 0.0428  173 GLU A OXT 
1191 N N   . HIS B 8   ? 0.6104 0.4787 0.5822 -0.0575 0.0050  0.0297  25  HIS B N   
1192 C CA  . HIS B 8   ? 0.5937 0.4431 0.5435 -0.0533 0.0053  0.0295  25  HIS B CA  
1193 C C   . HIS B 8   ? 0.4498 0.2977 0.3970 -0.0464 0.0051  0.0288  25  HIS B C   
1194 O O   . HIS B 8   ? 0.4925 0.3549 0.4530 -0.0450 0.0031  0.0283  25  HIS B O   
1195 C CB  . HIS B 8   ? 0.6122 0.4583 0.5562 -0.0549 0.0039  0.0296  25  HIS B CB  
1196 N N   . VAL B 9   ? 0.5554 0.3951 0.4907 -0.0392 0.0070  0.0275  26  VAL B N   
1197 C CA  . VAL B 9   ? 0.4479 0.2950 0.3846 -0.0288 0.0070  0.0254  26  VAL B CA  
1198 C C   . VAL B 9   ? 0.4099 0.2426 0.3269 -0.0218 0.0074  0.0246  26  VAL B C   
1199 O O   . VAL B 9   ? 0.4386 0.2540 0.3395 -0.0243 0.0083  0.0254  26  VAL B O   
1200 C CB  . VAL B 9   ? 0.3374 0.1885 0.2774 -0.0251 0.0087  0.0245  26  VAL B CB  
1201 C CG1 . VAL B 9   ? 0.3897 0.2566 0.3503 -0.0312 0.0082  0.0250  26  VAL B CG1 
1202 C CG2 . VAL B 9   ? 0.4063 0.2393 0.3287 -0.0255 0.0111  0.0251  26  VAL B CG2 
1203 N N   . GLU B 10  ? 0.3445 0.1846 0.2630 -0.0130 0.0068  0.0229  27  GLU B N   
1204 C CA  . GLU B 10  ? 0.3874 0.2151 0.2879 -0.0049 0.0075  0.0219  27  GLU B CA  
1205 C C   . GLU B 10  ? 0.3366 0.1695 0.2367 0.0051  0.0084  0.0203  27  GLU B C   
1206 O O   . GLU B 10  ? 0.3149 0.1610 0.2287 0.0054  0.0083  0.0199  27  GLU B O   
1207 C CB  . GLU B 10  ? 0.4463 0.2764 0.3466 -0.0039 0.0056  0.0216  27  GLU B CB  
1208 C CG  . GLU B 10  ? 0.3994 0.2504 0.3189 -0.0028 0.0035  0.0211  27  GLU B CG  
1209 C CD  . GLU B 10  ? 0.4365 0.2911 0.3579 -0.0041 0.0015  0.0212  27  GLU B CD  
1210 O OE1 . GLU B 10  ? 0.5973 0.4413 0.5108 -0.0099 0.0013  0.0222  27  GLU B OE1 
1211 O OE2 . GLU B 10  ? 0.3471 0.2158 0.2783 0.0007  0.0000  0.0202  27  GLU B OE2 
1212 N N   . GLN B 11  ? 0.3727 0.1946 0.2565 0.0133  0.0092  0.0194  28  GLN B N   
1213 C CA  . GLN B 11  ? 0.3465 0.1720 0.2278 0.0234  0.0100  0.0180  28  GLN B CA  
1214 C C   . GLN B 11  ? 0.3530 0.1824 0.2316 0.0315  0.0089  0.0168  28  GLN B C   
1215 O O   . GLN B 11  ? 0.3697 0.1898 0.2383 0.0313  0.0086  0.0169  28  GLN B O   
1216 C CB  . GLN B 11  ? 0.3894 0.1975 0.2528 0.0268  0.0124  0.0182  28  GLN B CB  
1217 C CG  . GLN B 11  ? 0.4132 0.2193 0.2802 0.0196  0.0136  0.0193  28  GLN B CG  
1218 C CD  . GLN B 11  ? 0.4314 0.2219 0.2820 0.0228  0.0158  0.0195  28  GLN B CD  
1219 O OE1 . GLN B 11  ? 0.5241 0.3024 0.3585 0.0298  0.0166  0.0191  28  GLN B OE1 
1220 N NE2 . GLN B 11  ? 0.4370 0.2283 0.2920 0.0179  0.0170  0.0202  28  GLN B NE2 
1221 N N   . THR B 12  ? 0.3279 0.1721 0.2162 0.0381  0.0083  0.0157  29  THR B N   
1222 C CA  . THR B 12  ? 0.3039 0.1527 0.1896 0.0466  0.0074  0.0145  29  THR B CA  
1223 C C   . THR B 12  ? 0.3233 0.1711 0.2017 0.0568  0.0086  0.0136  29  THR B C   
1224 O O   . THR B 12  ? 0.3248 0.1746 0.2062 0.0571  0.0097  0.0136  29  THR B O   
1225 C CB  . THR B 12  ? 0.2895 0.1589 0.1947 0.0451  0.0049  0.0142  29  THR B CB  
1226 O OG1 . THR B 12  ? 0.3133 0.1843 0.2134 0.0520  0.0041  0.0134  29  THR B OG1 
1227 C CG2 . THR B 12  ? 0.3071 0.1932 0.2279 0.0469  0.0046  0.0136  29  THR B CG2 
1228 N N   . TYR B 13  ? 0.3245 0.1686 0.1927 0.0653  0.0086  0.0128  30  TYR B N   
1229 C CA  . TYR B 13  ? 0.3183 0.1637 0.1809 0.0758  0.0095  0.0119  30  TYR B CA  
1230 C C   . TYR B 13  ? 0.2953 0.1621 0.1738 0.0799  0.0077  0.0110  30  TYR B C   
1231 O O   . TYR B 13  ? 0.3176 0.1916 0.2011 0.0801  0.0061  0.0108  30  TYR B O   
1232 C CB  . TYR B 13  ? 0.3462 0.1760 0.1888 0.0833  0.0105  0.0116  30  TYR B CB  
1233 C CG  . TYR B 13  ? 0.3395 0.1711 0.1764 0.0944  0.0113  0.0109  30  TYR B CG  
1234 C CD1 . TYR B 13  ? 0.3483 0.1749 0.1807 0.0962  0.0129  0.0112  30  TYR B CD1 
1235 C CD2 . TYR B 13  ? 0.3577 0.1971 0.1945 0.1029  0.0105  0.0100  30  TYR B CD2 
1236 C CE1 . TYR B 13  ? 0.3707 0.1993 0.1982 0.1060  0.0135  0.0107  30  TYR B CE1 
1237 C CE2 . TYR B 13  ? 0.3783 0.2211 0.2109 0.1121  0.0112  0.0094  30  TYR B CE2 
1238 C CZ  . TYR B 13  ? 0.3669 0.2061 0.1959 0.1124  0.0126  0.0097  30  TYR B CZ  
1239 O OH  . TYR B 13  ? 0.4021 0.2487 0.2289 0.1181  0.0130  0.0091  30  TYR B OH  
1240 N N   . LEU B 14  ? 0.3121 0.1890 0.1986 0.0828  0.0079  0.0106  31  LEU B N   
1241 C CA  . LEU B 14  ? 0.2853 0.1820 0.1860 0.0872  0.0063  0.0098  31  LEU B CA  
1242 C C   . LEU B 14  ? 0.3020 0.1977 0.1945 0.0975  0.0074  0.0092  31  LEU B C   
1243 O O   . LEU B 14  ? 0.3295 0.2153 0.2132 0.0985  0.0092  0.0094  31  LEU B O   
1244 C CB  . LEU B 14  ? 0.2984 0.2102 0.2189 0.0803  0.0053  0.0098  31  LEU B CB  
1245 C CG  . LEU B 14  ? 0.3000 0.2172 0.2323 0.0708  0.0037  0.0104  31  LEU B CG  
1246 C CD1 . LEU B 14  ? 0.3439 0.2699 0.2915 0.0632  0.0035  0.0107  31  LEU B CD1 
1247 C CD2 . LEU B 14  ? 0.3179 0.2495 0.2600 0.0731  0.0013  0.0100  31  LEU B CD2 
1248 N N   . MET B 15  ? 0.2692 0.1751 0.1639 0.1051  0.0063  0.0085  32  MET B N   
1249 C CA  . MET B 15  ? 0.2862 0.1940 0.1741 0.1127  0.0071  0.0079  32  MET B CA  
1250 C C   . MET B 15  ? 0.2604 0.1911 0.1642 0.1131  0.0053  0.0070  32  MET B C   
1251 O O   . MET B 15  ? 0.2679 0.2090 0.1792 0.1126  0.0036  0.0066  32  MET B O   
1252 C CB  . MET B 15  ? 0.2964 0.1933 0.1675 0.1171  0.0079  0.0077  32  MET B CB  
1253 C CG  . MET B 15  ? 0.3297 0.2308 0.1948 0.1221  0.0086  0.0072  32  MET B CG  
1254 S SD  . MET B 15  ? 0.3964 0.2818 0.2399 0.1274  0.0099  0.0073  32  MET B SD  
1255 C CE  . MET B 15  ? 0.4468 0.3372 0.2948 0.1268  0.0083  0.0068  32  MET B CE  
1256 N N   . ILE B 16  ? 0.2449 0.1830 0.1539 0.1131  0.0056  0.0066  33  ILE B N   
1257 C CA  . ILE B 16  ? 0.2585 0.2160 0.1796 0.1129  0.0041  0.0057  33  ILE B CA  
1258 C C   . ILE B 16  ? 0.2445 0.2015 0.1546 0.1180  0.0044  0.0055  33  ILE B C   
1259 O O   . ILE B 16  ? 0.2662 0.2127 0.1629 0.1217  0.0060  0.0058  33  ILE B O   
1260 C CB  . ILE B 16  ? 0.2507 0.2154 0.1806 0.1109  0.0044  0.0054  33  ILE B CB  
1261 C CG1 . ILE B 16  ? 0.2657 0.2303 0.2062 0.1061  0.0043  0.0057  33  ILE B CG1 
1262 C CG2 . ILE B 16  ? 0.2280 0.2109 0.1696 0.1095  0.0027  0.0045  33  ILE B CG2 
1263 C CD1 . ILE B 16  ? 0.2553 0.2272 0.2053 0.1038  0.0047  0.0052  33  ILE B CD1 
1264 N N   . LYS B 17  ? 0.2570 0.2249 0.1725 0.1180  0.0030  0.0050  34  LYS B N   
1265 C CA  . LYS B 17  ? 0.2671 0.2355 0.1733 0.1227  0.0031  0.0048  34  LYS B CA  
1266 C C   . LYS B 17  ? 0.2349 0.2130 0.1440 0.1235  0.0029  0.0045  34  LYS B C   
1267 O O   . LYS B 17  ? 0.2337 0.2195 0.1537 0.1199  0.0025  0.0042  34  LYS B O   
1268 C CB  . LYS B 17  ? 0.2321 0.2086 0.1438 0.1217  0.0017  0.0044  34  LYS B CB  
1269 C CG  . LYS B 17  ? 0.2625 0.2303 0.1722 0.1206  0.0016  0.0047  34  LYS B CG  
1270 C CD  . LYS B 17  ? 0.2645 0.2410 0.1793 0.1200  0.0001  0.0043  34  LYS B CD  
1271 C CE  . LYS B 17  ? 0.3166 0.2810 0.2245 0.1205  0.0003  0.0048  34  LYS B CE  
1272 N NZ  . LYS B 17  ? 0.3403 0.3133 0.2539 0.1197  -0.0013 0.0045  34  LYS B NZ  
1273 N N   . PRO B 18  ? 0.2445 0.2221 0.1440 0.1282  0.0033  0.0045  35  PRO B N   
1274 C CA  . PRO B 18  ? 0.2748 0.2600 0.1754 0.1293  0.0033  0.0044  35  PRO B CA  
1275 C C   . PRO B 18  ? 0.2625 0.2641 0.1796 0.1242  0.0016  0.0036  35  PRO B C   
1276 O O   . PRO B 18  ? 0.2619 0.2690 0.1830 0.1232  0.0015  0.0034  35  PRO B O   
1277 C CB  . PRO B 18  ? 0.3099 0.2921 0.1978 0.1351  0.0038  0.0046  35  PRO B CB  
1278 C CG  . PRO B 18  ? 0.2998 0.2673 0.1757 0.1378  0.0048  0.0050  35  PRO B CG  
1279 C CD  . PRO B 18  ? 0.2545 0.2238 0.1407 0.1329  0.0040  0.0047  35  PRO B CD  
1280 N N   . ASP B 19  ? 0.2385 0.2475 0.1649 0.1207  0.0003  0.0032  36  ASP B N   
1281 C CA  . ASP B 19  ? 0.2485 0.2713 0.1902 0.1150  -0.0012 0.0025  36  ASP B CA  
1282 C C   . ASP B 19  ? 0.2122 0.2370 0.1647 0.1102  -0.0015 0.0024  36  ASP B C   
1283 O O   . ASP B 19  ? 0.2198 0.2532 0.1815 0.1067  -0.0021 0.0019  36  ASP B O   
1284 C CB  . ASP B 19  ? 0.2559 0.2860 0.2051 0.1120  -0.0025 0.0022  36  ASP B CB  
1285 C CG  . ASP B 19  ? 0.2582 0.2824 0.2075 0.1114  -0.0027 0.0025  36  ASP B CG  
1286 O OD1 . ASP B 19  ? 0.2880 0.2998 0.2261 0.1153  -0.0014 0.0030  36  ASP B OD1 
1287 O OD2 . ASP B 19  ? 0.2497 0.2814 0.2101 0.1067  -0.0040 0.0024  36  ASP B OD2 
1288 N N   . GLY B 20  ? 0.2140 0.2306 0.1654 0.1099  -0.0009 0.0028  37  GLY B N   
1289 C CA  . GLY B 20  ? 0.1989 0.2169 0.1598 0.1058  -0.0008 0.0027  37  GLY B CA  
1290 C C   . GLY B 20  ? 0.2022 0.2179 0.1582 0.1080  0.0003  0.0027  37  GLY B C   
1291 O O   . GLY B 20  ? 0.2000 0.2223 0.1660 0.1043  -0.0001 0.0022  37  GLY B O   
1292 N N   . ILE B 21  ? 0.2362 0.2419 0.1766 0.1140  0.0017  0.0033  38  ILE B N   
1293 C CA  . ILE B 21  ? 0.2114 0.2146 0.1460 0.1165  0.0027  0.0034  38  ILE B CA  
1294 C C   . ILE B 21  ? 0.1980 0.2133 0.1383 0.1156  0.0017  0.0028  38  ILE B C   
1295 O O   . ILE B 21  ? 0.2248 0.2450 0.1711 0.1135  0.0016  0.0024  38  ILE B O   
1296 C CB  . ILE B 21  ? 0.2440 0.2334 0.1600 0.1230  0.0044  0.0043  38  ILE B CB  
1297 C CG1 . ILE B 21  ? 0.3033 0.2780 0.2114 0.1238  0.0055  0.0050  38  ILE B CG1 
1298 C CG2 . ILE B 21  ? 0.2798 0.2666 0.1898 0.1256  0.0054  0.0047  38  ILE B CG2 
1299 C CD1 . ILE B 21  ? 0.3277 0.2977 0.2407 0.1205  0.0063  0.0051  38  ILE B CD1 
1300 N N   . GLN B 22  ? 0.2280 0.2477 0.1659 0.1170  0.0010  0.0027  39  GLN B N   
1301 C CA  . GLN B 22  ? 0.2278 0.2569 0.1684 0.1168  0.0002  0.0023  39  GLN B CA  
1302 C C   . GLN B 22  ? 0.2152 0.2556 0.1719 0.1099  -0.0012 0.0015  39  GLN B C   
1303 O O   . GLN B 22  ? 0.2188 0.2653 0.1790 0.1086  -0.0016 0.0011  39  GLN B O   
1304 C CB  . GLN B 22  ? 0.2408 0.2708 0.1740 0.1203  0.0001  0.0025  39  GLN B CB  
1305 C CG  . GLN B 22  ? 0.2788 0.2985 0.1956 0.1273  0.0015  0.0033  39  GLN B CG  
1306 C CD  . GLN B 22  ? 0.2799 0.3006 0.1911 0.1304  0.0020  0.0036  39  GLN B CD  
1307 O OE1 . GLN B 22  ? 0.2975 0.3261 0.2170 0.1273  0.0014  0.0031  39  GLN B OE1 
1308 N NE2 . GLN B 22  ? 0.2922 0.3042 0.1889 0.1366  0.0032  0.0044  39  GLN B NE2 
1309 N N   . ARG B 23  ? 0.2079 0.2505 0.1743 0.1053  -0.0020 0.0012  40  ARG B N   
1310 C CA  . ARG B 23  ? 0.1879 0.2396 0.1696 0.0983  -0.0033 0.0006  40  ARG B CA  
1311 C C   . ARG B 23  ? 0.2139 0.2650 0.2023 0.0955  -0.0029 0.0003  40  ARG B C   
1312 O O   . ARG B 23  ? 0.2028 0.2605 0.2036 0.0896  -0.0038 -0.0002 40  ARG B O   
1313 C CB  . ARG B 23  ? 0.1868 0.2415 0.1763 0.0943  -0.0044 0.0006  40  ARG B CB  
1314 C CG  . ARG B 23  ? 0.1823 0.2387 0.1660 0.0969  -0.0047 0.0007  40  ARG B CG  
1315 C CD  . ARG B 23  ? 0.2163 0.2749 0.2065 0.0935  -0.0057 0.0008  40  ARG B CD  
1316 N NE  . ARG B 23  ? 0.1945 0.2614 0.1966 0.0880  -0.0069 0.0004  40  ARG B NE  
1317 C CZ  . ARG B 23  ? 0.2060 0.2751 0.2167 0.0836  -0.0079 0.0007  40  ARG B CZ  
1318 N NH1 . ARG B 23  ? 0.2040 0.2683 0.2132 0.0840  -0.0079 0.0013  40  ARG B NH1 
1319 N NH2 . ARG B 23  ? 0.1800 0.2557 0.2010 0.0786  -0.0089 0.0004  40  ARG B NH2 
1320 N N   . GLN B 24  ? 0.1883 0.2308 0.1682 0.0995  -0.0015 0.0007  41  GLN B N   
1321 C CA  . GLN B 24  ? 0.1733 0.2145 0.1570 0.0980  -0.0007 0.0005  41  GLN B CA  
1322 C C   . GLN B 24  ? 0.1692 0.2137 0.1668 0.0919  -0.0013 0.0001  41  GLN B C   
1323 O O   . GLN B 24  ? 0.1807 0.2305 0.1887 0.0876  -0.0016 -0.0006 41  GLN B O   
1324 C CB  . GLN B 24  ? 0.2070 0.2539 0.1925 0.0976  -0.0008 -0.0001 41  GLN B CB  
1325 C CG  . GLN B 24  ? 0.2184 0.2621 0.1900 0.1039  -0.0002 0.0005  41  GLN B CG  
1326 C CD  . GLN B 24  ? 0.2562 0.2988 0.2239 0.1061  0.0007  0.0004  41  GLN B CD  
1327 O OE1 . GLN B 24  ? 0.2509 0.3003 0.2220 0.1048  0.0000  -0.0001 41  GLN B OE1 
1328 N NE2 . GLN B 24  ? 0.2457 0.2791 0.2058 0.1092  0.0022  0.0010  41  GLN B NE2 
1329 N N   . VAL B 25  ? 0.1731 0.2138 0.1702 0.0919  -0.0015 0.0006  42  VAL B N   
1330 C CA  . VAL B 25  ? 0.1519 0.1947 0.1609 0.0868  -0.0020 0.0006  42  VAL B CA  
1331 C C   . VAL B 25  ? 0.1920 0.2242 0.1943 0.0896  -0.0006 0.0013  42  VAL B C   
1332 O O   . VAL B 25  ? 0.1672 0.1993 0.1765 0.0867  -0.0010 0.0016  42  VAL B O   
1333 C CB  . VAL B 25  ? 0.1741 0.2226 0.1905 0.0830  -0.0037 0.0008  42  VAL B CB  
1334 C CG1 . VAL B 25  ? 0.1901 0.2475 0.2142 0.0790  -0.0049 0.0002  42  VAL B CG1 
1335 C CG2 . VAL B 25  ? 0.1977 0.2406 0.2026 0.0879  -0.0036 0.0014  42  VAL B CG2 
1336 N N   . VAL B 26  ? 0.1838 0.2060 0.1725 0.0951  0.0012  0.0016  43  VAL B N   
1337 C CA  . VAL B 26  ? 0.1856 0.1942 0.1652 0.0977  0.0029  0.0025  43  VAL B CA  
1338 C C   . VAL B 26  ? 0.1683 0.1785 0.1591 0.0935  0.0034  0.0023  43  VAL B C   
1339 O O   . VAL B 26  ? 0.1774 0.1820 0.1694 0.0923  0.0036  0.0030  43  VAL B O   
1340 C CB  . VAL B 26  ? 0.1988 0.1962 0.1622 0.1033  0.0049  0.0029  43  VAL B CB  
1341 C CG1 . VAL B 26  ? 0.2479 0.2295 0.2020 0.1047  0.0070  0.0038  43  VAL B CG1 
1342 C CG2 . VAL B 26  ? 0.2178 0.2120 0.1690 0.1079  0.0046  0.0034  43  VAL B CG2 
1343 N N   . GLY B 27  ? 0.1544 0.1720 0.1532 0.0911  0.0036  0.0013  44  GLY B N   
1344 C CA  . GLY B 27  ? 0.1451 0.1652 0.1550 0.0872  0.0042  0.0009  44  GLY B CA  
1345 C C   . GLY B 27  ? 0.1252 0.1543 0.1504 0.0813  0.0023  0.0009  44  GLY B C   
1346 O O   . GLY B 27  ? 0.1539 0.1809 0.1844 0.0794  0.0029  0.0015  44  GLY B O   
1347 N N   . GLU B 28  ? 0.1487 0.1876 0.1813 0.0781  0.0002  0.0005  45  GLU B N   
1348 C CA  . GLU B 28  ? 0.1300 0.1765 0.1765 0.0721  -0.0017 0.0008  45  GLU B CA  
1349 C C   . GLU B 28  ? 0.1427 0.1827 0.1845 0.0740  -0.0019 0.0020  45  GLU B C   
1350 O O   . GLU B 28  ? 0.1308 0.1739 0.1828 0.0700  -0.0026 0.0026  45  GLU B O   
1351 C CB  . GLU B 28  ? 0.1710 0.2250 0.2222 0.0690  -0.0035 0.0005  45  GLU B CB  
1352 C CG  . GLU B 28  ? 0.2273 0.2877 0.2869 0.0647  -0.0037 -0.0002 45  GLU B CG  
1353 C CD  . GLU B 28  ? 0.3515 0.4168 0.4166 0.0607  -0.0054 0.0002  45  GLU B CD  
1354 O OE1 . GLU B 28  ? 0.3416 0.4095 0.4169 0.0552  -0.0064 0.0012  45  GLU B OE1 
1355 O OE2 . GLU B 28  ? 0.3476 0.4134 0.4059 0.0633  -0.0056 -0.0001 45  GLU B OE2 
1356 N N   . ILE B 29  ? 0.1618 0.1922 0.1880 0.0800  -0.0012 0.0026  46  ILE B N   
1357 C CA  . ILE B 29  ? 0.1679 0.1895 0.1876 0.0820  -0.0013 0.0040  46  ILE B CA  
1358 C C   . ILE B 29  ? 0.1739 0.1834 0.1896 0.0782  0.0006  0.0048  46  ILE B C   
1359 O O   . ILE B 29  ? 0.1624 0.1705 0.1836 0.0707  0.0000  0.0055  46  ILE B O   
1360 C CB  . ILE B 29  ? 0.1748 0.1867 0.1773 0.0879  -0.0007 0.0043  46  ILE B CB  
1361 C CG1 . ILE B 29  ? 0.1968 0.2198 0.2035 0.0867  -0.0025 0.0036  46  ILE B CG1 
1362 C CG2 . ILE B 29  ? 0.2071 0.2048 0.1994 0.0899  -0.0001 0.0056  46  ILE B CG2 
1363 C CD1 . ILE B 29  ? 0.2135 0.2293 0.2038 0.0929  -0.0017 0.0036  46  ILE B CD1 
1364 N N   . ILE B 30  ? 0.1571 0.1576 0.1631 0.0802  0.0029  0.0045  47  ILE B N   
1365 C CA  . ILE B 30  ? 0.1938 0.1821 0.1951 0.0735  0.0048  0.0052  47  ILE B CA  
1366 C C   . ILE B 30  ? 0.1652 0.1634 0.1843 0.0647  0.0041  0.0050  47  ILE B C   
1367 O O   . ILE B 30  ? 0.1538 0.1453 0.1736 0.0572  0.0045  0.0060  47  ILE B O   
1368 C CB  . ILE B 30  ? 0.2086 0.1881 0.1983 0.0775  0.0071  0.0049  47  ILE B CB  
1369 C CG1 . ILE B 30  ? 0.1841 0.1510 0.1547 0.0854  0.0079  0.0054  47  ILE B CG1 
1370 C CG2 . ILE B 30  ? 0.2219 0.1920 0.2099 0.0699  0.0090  0.0054  47  ILE B CG2 
1371 C CD1 . ILE B 30  ? 0.2265 0.1879 0.1868 0.0912  0.0098  0.0051  47  ILE B CD1 
1372 N N   . SER B 31  ? 0.1471 0.1609 0.1806 0.0655  0.0031  0.0038  48  SER B N   
1373 C CA  . SER B 31  ? 0.1328 0.1564 0.1836 0.0577  0.0025  0.0034  48  SER B CA  
1374 C C   . SER B 31  ? 0.1239 0.1509 0.1835 0.0516  0.0005  0.0045  48  SER B C   
1375 O O   . SER B 31  ? 0.1392 0.1673 0.2079 0.0437  0.0006  0.0050  48  SER B O   
1376 C CB  . SER B 31  ? 0.1378 0.1780 0.2025 0.0601  0.0015  0.0018  48  SER B CB  
1377 O OG  . SER B 31  ? 0.1519 0.1897 0.2111 0.0635  0.0035  0.0008  48  SER B OG  
1378 N N   . ARG B 32  ? 0.1296 0.1589 0.1870 0.0552  -0.0012 0.0049  49  ARG B N   
1379 C CA  . ARG B 32  ? 0.1392 0.1724 0.2053 0.0493  -0.0032 0.0060  49  ARG B CA  
1380 C C   . ARG B 32  ? 0.1328 0.1512 0.1902 0.0431  -0.0020 0.0075  49  ARG B C   
1381 O O   . ARG B 32  ? 0.1506 0.1718 0.2178 0.0353  -0.0030 0.0084  49  ARG B O   
1382 C CB  . ARG B 32  ? 0.1502 0.1879 0.2139 0.0547  -0.0052 0.0062  49  ARG B CB  
1383 C CG  . ARG B 32  ? 0.1532 0.2082 0.2294 0.0588  -0.0070 0.0051  49  ARG B CG  
1384 C CD  . ARG B 32  ? 0.3312 0.3890 0.4075 0.0576  -0.0090 0.0054  49  ARG B CD  
1385 N NE  . ARG B 32  ? 0.2068 0.2707 0.2895 0.0531  -0.0097 0.0048  49  ARG B NE  
1386 C CZ  . ARG B 32  ? 0.1974 0.2652 0.2862 0.0485  -0.0113 0.0056  49  ARG B CZ  
1387 N NH1 . ARG B 32  ? 0.2053 0.2736 0.2955 0.0475  -0.0128 0.0065  49  ARG B NH1 
1388 N NH2 . ARG B 32  ? 0.2205 0.2905 0.3126 0.0450  -0.0113 0.0057  49  ARG B NH2 
1389 N N   . PHE B 33  ? 0.1513 0.1537 0.1900 0.0465  0.0000  0.0078  50  PHE B N   
1390 C CA  . PHE B 33  ? 0.1687 0.1559 0.1977 0.0407  0.0012  0.0092  50  PHE B CA  
1391 C C   . PHE B 33  ? 0.1659 0.1497 0.1983 0.0343  0.0030  0.0094  50  PHE B C   
1392 O O   . PHE B 33  ? 0.1691 0.1490 0.2046 0.0263  0.0030  0.0106  50  PHE B O   
1393 C CB  . PHE B 33  ? 0.1855 0.1566 0.1930 0.0468  0.0026  0.0094  50  PHE B CB  
1394 C CG  . PHE B 33  ? 0.1768 0.1503 0.1807 0.0522  0.0009  0.0094  50  PHE B CG  
1395 C CD1 . PHE B 33  ? 0.1915 0.1646 0.1979 0.0475  -0.0006 0.0103  50  PHE B CD1 
1396 C CD2 . PHE B 33  ? 0.2142 0.1911 0.2129 0.0617  0.0008  0.0084  50  PHE B CD2 
1397 C CE1 . PHE B 33  ? 0.2006 0.1765 0.2040 0.0522  -0.0021 0.0102  50  PHE B CE1 
1398 C CE2 . PHE B 33  ? 0.2481 0.2279 0.2439 0.0665  -0.0007 0.0084  50  PHE B CE2 
1399 C CZ  . PHE B 33  ? 0.1985 0.1781 0.1972 0.0615  -0.0021 0.0093  50  PHE B CZ  
1400 N N   . GLU B 34  ? 0.1572 0.1430 0.1893 0.0377  0.0045  0.0082  51  GLU B N   
1401 C CA  . GLU B 34  ? 0.1637 0.1484 0.2007 0.0318  0.0061  0.0082  51  GLU B CA  
1402 C C   . GLU B 34  ? 0.1411 0.1391 0.1984 0.0244  0.0047  0.0083  51  GLU B C   
1403 O O   . GLU B 34  ? 0.1632 0.1583 0.2244 0.0172  0.0057  0.0090  51  GLU B O   
1404 C CB  . GLU B 34  ? 0.1818 0.1692 0.2171 0.0371  0.0076  0.0067  51  GLU B CB  
1405 C CG  . GLU B 34  ? 0.2117 0.1841 0.2273 0.0423  0.0097  0.0069  51  GLU B CG  
1406 C CD  . GLU B 34  ? 0.1939 0.1711 0.2101 0.0469  0.0111  0.0055  51  GLU B CD  
1407 O OE1 . GLU B 34  ? 0.1920 0.1820 0.2159 0.0521  0.0098  0.0042  51  GLU B OE1 
1408 O OE2 . GLU B 34  ? 0.2080 0.1766 0.2176 0.0446  0.0133  0.0057  51  GLU B OE2 
1409 N N   . LYS B 35  ? 0.1318 0.1446 0.2022 0.0262  0.0023  0.0076  52  LYS B N   
1410 C CA  . LYS B 35  ? 0.1329 0.1592 0.2232 0.0199  0.0008  0.0076  52  LYS B CA  
1411 C C   . LYS B 35  ? 0.1305 0.1524 0.2236 0.0115  0.0002  0.0096  52  LYS B C   
1412 O O   . LYS B 35  ? 0.1285 0.1574 0.2357 0.0048  -0.0002 0.0099  52  LYS B O   
1413 C CB  . LYS B 35  ? 0.1358 0.1774 0.2377 0.0237  -0.0018 0.0068  52  LYS B CB  
1414 C CG  . LYS B 35  ? 0.1284 0.1857 0.2518 0.0187  -0.0034 0.0064  52  LYS B CG  
1415 C CD  . LYS B 35  ? 0.2057 0.2731 0.3293 0.0222  -0.0056 0.0052  52  LYS B CD  
1416 C CE  . LYS B 35  ? 0.3709 0.4432 0.4913 0.0181  -0.0055 0.0033  52  LYS B CE  
1417 N NZ  . LYS B 35  ? 0.3962 0.4692 0.5161 0.0212  -0.0037 0.0020  52  LYS B NZ  
1418 N N   . ARG B 36  ? 0.1477 0.1587 0.2282 0.0119  -0.0001 0.0108  53  ARG B N   
1419 C CA  . ARG B 36  ? 0.1373 0.1433 0.2191 0.0038  -0.0007 0.0127  53  ARG B CA  
1420 C C   . ARG B 36  ? 0.1610 0.1523 0.2320 -0.0008 0.0017  0.0137  53  ARG B C   
1421 O O   . ARG B 36  ? 0.1515 0.1365 0.2211 -0.0075 0.0014  0.0155  53  ARG B O   
1422 C CB  . ARG B 36  ? 0.1282 0.1301 0.2022 0.0058  -0.0024 0.0136  53  ARG B CB  
1423 C CG  . ARG B 36  ? 0.1440 0.1614 0.2304 0.0086  -0.0051 0.0130  53  ARG B CG  
1424 C CD  . ARG B 36  ? 0.1736 0.1877 0.2536 0.0096  -0.0067 0.0139  53  ARG B CD  
1425 N NE  . ARG B 36  ? 0.1432 0.1550 0.2275 0.0008  -0.0076 0.0158  53  ARG B NE  
1426 C CZ  . ARG B 36  ? 0.1601 0.1699 0.2411 -0.0006 -0.0092 0.0168  53  ARG B CZ  
1427 N NH1 . ARG B 36  ? 0.1786 0.1872 0.2507 0.0065  -0.0098 0.0161  53  ARG B NH1 
1428 N NH2 . ARG B 36  ? 0.1646 0.1742 0.2516 -0.0091 -0.0102 0.0186  53  ARG B NH2 
1429 N N   . GLY B 37  ? 0.1547 0.1400 0.2175 0.0025  0.0041  0.0128  54  GLY B N   
1430 C CA  . GLY B 37  ? 0.1553 0.1262 0.2069 -0.0016 0.0064  0.0138  54  GLY B CA  
1431 C C   . GLY B 37  ? 0.1723 0.1258 0.2030 0.0011  0.0071  0.0146  54  GLY B C   
1432 O O   . GLY B 37  ? 0.2121 0.1529 0.2336 -0.0039 0.0085  0.0159  54  GLY B O   
1433 N N   . TYR B 38  ? 0.1947 0.1475 0.2181 0.0086  0.0063  0.0139  55  TYR B N   
1434 C CA  . TYR B 38  ? 0.2017 0.1376 0.2044 0.0123  0.0072  0.0144  55  TYR B CA  
1435 C C   . TYR B 38  ? 0.2336 0.1598 0.2238 0.0166  0.0097  0.0138  55  TYR B C   
1436 O O   . TYR B 38  ? 0.2123 0.1470 0.2079 0.0210  0.0102  0.0125  55  TYR B O   
1437 C CB  . TYR B 38  ? 0.1871 0.1258 0.1860 0.0196  0.0056  0.0138  55  TYR B CB  
1438 C CG  . TYR B 38  ? 0.1907 0.1372 0.1994 0.0156  0.0031  0.0145  55  TYR B CG  
1439 C CD1 . TYR B 38  ? 0.1970 0.1392 0.2081 0.0066  0.0027  0.0161  55  TYR B CD1 
1440 C CD2 . TYR B 38  ? 0.1821 0.1399 0.1970 0.0209  0.0011  0.0137  55  TYR B CD2 
1441 C CE1 . TYR B 38  ? 0.1854 0.1350 0.2055 0.0029  0.0003  0.0169  55  TYR B CE1 
1442 C CE2 . TYR B 38  ? 0.1956 0.1606 0.2192 0.0173  -0.0012 0.0144  55  TYR B CE2 
1443 C CZ  . TYR B 38  ? 0.1595 0.1204 0.1857 0.0084  -0.0016 0.0160  55  TYR B CZ  
1444 O OH  . TYR B 38  ? 0.1782 0.1462 0.2126 0.0049  -0.0040 0.0168  55  TYR B OH  
1445 N N   . ARG B 39  ? 0.2300 0.1386 0.2035 0.0151  0.0113  0.0149  56  ARG B N   
1446 C CA  . ARG B 39  ? 0.2488 0.1462 0.2092 0.0180  0.0137  0.0148  56  ARG B CA  
1447 C C   . ARG B 39  ? 0.2638 0.1530 0.2085 0.0279  0.0140  0.0142  56  ARG B C   
1448 O O   . ARG B 39  ? 0.2764 0.1575 0.2115 0.0297  0.0133  0.0146  56  ARG B O   
1449 C CB  . ARG B 39  ? 0.2854 0.1677 0.2361 0.0107  0.0151  0.0165  56  ARG B CB  
1450 C CG  . ARG B 39  ? 0.2795 0.1507 0.2178 0.0124  0.0177  0.0166  56  ARG B CG  
1451 C CD  . ARG B 39  ? 0.3373 0.1940 0.2666 0.0044  0.0189  0.0185  56  ARG B CD  
1452 N NE  . ARG B 39  ? 0.3225 0.1635 0.2359 0.0045  0.0186  0.0195  56  ARG B NE  
1453 C CZ  . ARG B 39  ? 0.3680 0.1934 0.2623 0.0098  0.0198  0.0197  56  ARG B CZ  
1454 N NH1 . ARG B 39  ? 0.3890 0.2123 0.2770 0.0159  0.0212  0.0190  56  ARG B NH1 
1455 N NH2 . ARG B 39  ? 0.4189 0.2300 0.2995 0.0089  0.0195  0.0206  56  ARG B NH2 
1456 N N   . ILE B 40  ? 0.2566 0.1476 0.1984 0.0341  0.0152  0.0132  57  ILE B N   
1457 C CA  . ILE B 40  ? 0.2425 0.1246 0.1684 0.0435  0.0158  0.0128  57  ILE B CA  
1458 C C   . ILE B 40  ? 0.2782 0.1395 0.1852 0.0419  0.0177  0.0141  57  ILE B C   
1459 O O   . ILE B 40  ? 0.3242 0.1806 0.2280 0.0394  0.0195  0.0145  57  ILE B O   
1460 C CB  . ILE B 40  ? 0.2741 0.1651 0.2031 0.0504  0.0164  0.0114  57  ILE B CB  
1461 C CG1 . ILE B 40  ? 0.2977 0.2097 0.2463 0.0513  0.0145  0.0101  57  ILE B CG1 
1462 C CG2 . ILE B 40  ? 0.3049 0.1868 0.2174 0.0603  0.0169  0.0113  57  ILE B CG2 
1463 C CD1 . ILE B 40  ? 0.2679 0.1900 0.2222 0.0560  0.0152  0.0088  57  ILE B CD1 
1464 N N   . ALA B 41  ? 0.3065 0.1555 0.2008 0.0430  0.0174  0.0148  58  ALA B N   
1465 C CA  . ALA B 41  ? 0.3364 0.1648 0.2117 0.0420  0.0191  0.0160  58  ALA B CA  
1466 C C   . ALA B 41  ? 0.3813 0.1996 0.2401 0.0519  0.0201  0.0157  58  ALA B C   
1467 O O   . ALA B 41  ? 0.4179 0.2201 0.2614 0.0518  0.0217  0.0166  58  ALA B O   
1468 C CB  . ALA B 41  ? 0.3988 0.2174 0.2683 0.0368  0.0183  0.0170  58  ALA B CB  
1469 N N   . ALA B 42  ? 0.3670 0.1945 0.2285 0.0603  0.0191  0.0145  59  ALA B N   
1470 C CA  . ALA B 42  ? 0.3770 0.1967 0.2240 0.0704  0.0199  0.0142  59  ALA B CA  
1471 C C   . ALA B 42  ? 0.3582 0.1950 0.2155 0.0779  0.0187  0.0129  59  ALA B C   
1472 O O   . ALA B 42  ? 0.3426 0.1934 0.2138 0.0765  0.0169  0.0122  59  ALA B O   
1473 C CB  . ALA B 42  ? 0.3823 0.1859 0.2126 0.0733  0.0199  0.0148  59  ALA B CB  
1474 N N   . MET B 43  ? 0.3685 0.2042 0.2189 0.0857  0.0196  0.0126  60  MET B N   
1475 C CA  . MET B 43  ? 0.3609 0.2121 0.2196 0.0932  0.0185  0.0114  60  MET B CA  
1476 C C   . MET B 43  ? 0.4159 0.2587 0.2596 0.1026  0.0197  0.0116  60  MET B C   
1477 O O   . MET B 43  ? 0.4471 0.2803 0.2824 0.1018  0.0214  0.0123  60  MET B O   
1478 C CB  . MET B 43  ? 0.3493 0.2180 0.2266 0.0893  0.0181  0.0106  60  MET B CB  
1479 C CG  . MET B 43  ? 0.3709 0.2576 0.2593 0.0958  0.0167  0.0093  60  MET B CG  
1480 S SD  . MET B 43  ? 0.3492 0.2570 0.2620 0.0893  0.0157  0.0081  60  MET B SD  
1481 C CE  . MET B 43  ? 0.2937 0.2083 0.2179 0.0834  0.0135  0.0082  60  MET B CE  
1482 N N   . LYS B 44  ? 0.3721 0.2181 0.2122 0.1111  0.0189  0.0112  61  LYS B N   
1483 C CA  . LYS B 44  ? 0.3762 0.2198 0.2047 0.1168  0.0195  0.0113  61  LYS B CA  
1484 C C   . LYS B 44  ? 0.3926 0.2530 0.2277 0.1216  0.0178  0.0103  61  LYS B C   
1485 O O   . LYS B 44  ? 0.4038 0.2689 0.2426 0.1216  0.0165  0.0099  61  LYS B O   
1486 C CB  . LYS B 44  ? 0.5114 0.3354 0.3212 0.1169  0.0206  0.0121  61  LYS B CB  
1487 C CG  . LYS B 44  ? 0.5910 0.4139 0.3894 0.1235  0.0208  0.0120  61  LYS B CG  
1488 C CD  . LYS B 44  ? 0.6012 0.4039 0.3813 0.1230  0.0221  0.0127  61  LYS B CD  
1489 C CE  . LYS B 44  ? 0.5831 0.3806 0.3607 0.1211  0.0214  0.0124  61  LYS B CE  
1490 N NZ  . LYS B 44  ? 0.7042 0.4819 0.4636 0.1202  0.0228  0.0129  61  LYS B NZ  
1491 N N   . LEU B 45  ? 0.3418 0.2110 0.1781 0.1254  0.0178  0.0102  62  LEU B N   
1492 C CA  . LEU B 45  ? 0.3204 0.2031 0.1597 0.1296  0.0163  0.0096  62  LEU B CA  
1493 C C   . LEU B 45  ? 0.3340 0.2056 0.1561 0.1345  0.0171  0.0103  62  LEU B C   
1494 O O   . LEU B 45  ? 0.3715 0.2309 0.1812 0.1361  0.0187  0.0111  62  LEU B O   
1495 C CB  . LEU B 45  ? 0.3403 0.2372 0.1885 0.1308  0.0158  0.0092  62  LEU B CB  
1496 C CG  . LEU B 45  ? 0.3421 0.2537 0.1946 0.1340  0.0142  0.0088  62  LEU B CG  
1497 C CD1 . LEU B 45  ? 0.3490 0.2758 0.2179 0.1306  0.0122  0.0077  62  LEU B CD1 
1498 C CD2 . LEU B 45  ? 0.3669 0.2859 0.2203 0.1363  0.0142  0.0089  62  LEU B CD2 
1499 N N   . THR B 46  ? 0.3382 0.2138 0.1591 0.1368  0.0161  0.0099  63  THR B N   
1500 C CA  . THR B 46  ? 0.3999 0.2674 0.2057 0.1420  0.0167  0.0104  63  THR B CA  
1501 C C   . THR B 46  ? 0.3930 0.2752 0.2042 0.1452  0.0151  0.0098  63  THR B C   
1502 O O   . THR B 46  ? 0.3930 0.2910 0.2193 0.1429  0.0136  0.0091  63  THR B O   
1503 C CB  . THR B 46  ? 0.4033 0.2524 0.1959 0.1411  0.0178  0.0107  63  THR B CB  
1504 O OG1 . THR B 46  ? 0.4457 0.2853 0.2224 0.1463  0.0188  0.0112  63  THR B OG1 
1505 C CG2 . THR B 46  ? 0.4147 0.2671 0.2131 0.1391  0.0166  0.0100  63  THR B CG2 
1506 N N   . ILE B 47  ? 0.3747 0.2519 0.1738 0.1502  0.0156  0.0102  64  ILE B N   
1507 C CA  . ILE B 47  ? 0.3770 0.2657 0.1793 0.1531  0.0143  0.0097  64  ILE B CA  
1508 C C   . ILE B 47  ? 0.4152 0.2937 0.2080 0.1544  0.0146  0.0096  64  ILE B C   
1509 O O   . ILE B 47  ? 0.4436 0.3067 0.2211 0.1571  0.0160  0.0102  64  ILE B O   
1510 C CB  . ILE B 47  ? 0.3811 0.2748 0.1783 0.1582  0.0144  0.0102  64  ILE B CB  
1511 C CG1 . ILE B 47  ? 0.4088 0.3151 0.2176 0.1562  0.0138  0.0100  64  ILE B CG1 
1512 C CG2 . ILE B 47  ? 0.4487 0.3511 0.2462 0.1614  0.0134  0.0098  64  ILE B CG2 
1513 C CD1 . ILE B 47  ? 0.4888 0.3994 0.2929 0.1606  0.0140  0.0105  64  ILE B CD1 
1514 N N   . ALA B 48  ? 0.3718 0.2582 0.1737 0.1522  0.0133  0.0089  65  ALA B N   
1515 C CA  . ALA B 48  ? 0.3894 0.2669 0.1833 0.1532  0.0135  0.0087  65  ALA B CA  
1516 C C   . ALA B 48  ? 0.4090 0.2865 0.1929 0.1594  0.0136  0.0089  65  ALA B C   
1517 O O   . ALA B 48  ? 0.4208 0.3116 0.2100 0.1617  0.0128  0.0088  65  ALA B O   
1518 C CB  . ALA B 48  ? 0.3894 0.2768 0.1963 0.1496  0.0120  0.0078  65  ALA B CB  
1519 N N   . THR B 49  ? 0.4022 0.2704 0.1769 0.1817  -0.0274 -0.0150 66  THR B N   
1520 C CA  . THR B 49  ? 0.4133 0.2823 0.1870 0.1833  -0.0242 -0.0148 66  THR B CA  
1521 C C   . THR B 49  ? 0.4506 0.3122 0.2122 0.1876  -0.0258 -0.0169 66  THR B C   
1522 O O   . THR B 49  ? 0.4577 0.3142 0.2141 0.1889  -0.0298 -0.0188 66  THR B O   
1523 C CB  . THR B 49  ? 0.4084 0.2842 0.1961 0.1810  -0.0237 -0.0151 66  THR B CB  
1524 O OG1 . THR B 49  ? 0.4784 0.3520 0.2674 0.1818  -0.0278 -0.0177 66  THR B OG1 
1525 C CG2 . THR B 49  ? 0.4784 0.3619 0.2782 0.1770  -0.0225 -0.0131 66  THR B CG2 
1526 N N   . PRO B 50  ? 0.4568 0.3177 0.2137 0.1898  -0.0228 -0.0166 67  PRO B N   
1527 C CA  . PRO B 50  ? 0.4765 0.3310 0.2219 0.1941  -0.0241 -0.0188 67  PRO B CA  
1528 C C   . PRO B 50  ? 0.4542 0.3077 0.2032 0.1948  -0.0280 -0.0221 67  PRO B C   
1529 O O   . PRO B 50  ? 0.4896 0.3365 0.2285 0.1978  -0.0310 -0.0239 67  PRO B O   
1530 C CB  . PRO B 50  ? 0.4990 0.3562 0.2443 0.1952  -0.0197 -0.0182 67  PRO B CB  
1531 C CG  . PRO B 50  ? 0.4741 0.3351 0.2225 0.1927  -0.0162 -0.0147 67  PRO B CG  
1532 C CD  . PRO B 50  ? 0.4521 0.3176 0.2120 0.1887  -0.0179 -0.0142 67  PRO B CD  
1533 N N   . ALA B 51  ? 0.4591 0.3188 0.2221 0.1921  -0.0281 -0.0228 68  ALA B N   
1534 C CA  . ALA B 51  ? 0.4641 0.3228 0.2308 0.1928  -0.0317 -0.0259 68  ALA B CA  
1535 C C   . ALA B 51  ? 0.4254 0.2801 0.1889 0.1926  -0.0362 -0.0266 68  ALA B C   
1536 O O   . ALA B 51  ? 0.4849 0.3345 0.2422 0.1951  -0.0396 -0.0292 68  ALA B O   
1537 C CB  . ALA B 51  ? 0.4968 0.3626 0.2794 0.1897  -0.0310 -0.0260 68  ALA B CB  
1538 N N   . ILE B 52  ? 0.4584 0.3157 0.2267 0.1896  -0.0365 -0.0246 69  ILE B N   
1539 C CA  . ILE B 52  ? 0.4364 0.2903 0.2023 0.1892  -0.0407 -0.0256 69  ILE B CA  
1540 C C   . ILE B 52  ? 0.4258 0.2712 0.1759 0.1923  -0.0421 -0.0260 69  ILE B C   
1541 O O   . ILE B 52  ? 0.4470 0.2871 0.1913 0.1938  -0.0461 -0.0280 69  ILE B O   
1542 C CB  . ILE B 52  ? 0.5004 0.3602 0.2766 0.1852  -0.0407 -0.0238 69  ILE B CB  
1543 C CG1 . ILE B 52  ? 0.5670 0.4239 0.3421 0.1847  -0.0452 -0.0252 69  ILE B CG1 
1544 C CG2 . ILE B 52  ? 0.5395 0.4004 0.3131 0.1842  -0.0375 -0.0212 69  ILE B CG2 
1545 C CD1 . ILE B 52  ? 0.6203 0.4842 0.4093 0.1813  -0.0464 -0.0248 69  ILE B CD1 
1546 N N   . LEU B 53  ? 0.4493 0.2932 0.1923 0.1933  -0.0389 -0.0241 70  LEU B N   
1547 C CA  . LEU B 53  ? 0.5352 0.3705 0.2629 0.1963  -0.0401 -0.0243 70  LEU B CA  
1548 C C   . LEU B 53  ? 0.5317 0.3611 0.2489 0.2008  -0.0417 -0.0265 70  LEU B C   
1549 O O   . LEU B 53  ? 0.5360 0.3576 0.2417 0.2032  -0.0446 -0.0277 70  LEU B O   
1550 C CB  . LEU B 53  ? 0.4667 0.3017 0.1893 0.1965  -0.0361 -0.0216 70  LEU B CB  
1551 C CG  . LEU B 53  ? 0.4470 0.2868 0.1783 0.1923  -0.0350 -0.0196 70  LEU B CG  
1552 C CD1 . LEU B 53  ? 0.4403 0.2816 0.1692 0.1922  -0.0305 -0.0170 70  LEU B CD1 
1553 C CD2 . LEU B 53  ? 0.5002 0.3348 0.2279 0.1915  -0.0390 -0.0204 70  LEU B CD2 
1554 N N   . GLU B 54  ? 0.4903 0.3233 0.2117 0.2019  -0.0399 -0.0275 71  GLU B N   
1555 C CA  . GLU B 54  ? 0.5162 0.3449 0.2299 0.2059  -0.0416 -0.0303 71  GLU B CA  
1556 C C   . GLU B 54  ? 0.5061 0.3318 0.2204 0.2060  -0.0468 -0.0329 71  GLU B C   
1557 O O   . GLU B 54  ? 0.5737 0.3926 0.2767 0.2095  -0.0496 -0.0347 71  GLU B O   
1558 C CB  . GLU B 54  ? 0.5443 0.3789 0.2657 0.2060  -0.0386 -0.0317 71  GLU B CB  
1559 C CG  . GLU B 54  ? 0.6775 0.5134 0.3945 0.2071  -0.0338 -0.0301 71  GLU B CG  
1560 C CD  . GLU B 54  ? 1.0740 0.9167 0.8008 0.2062  -0.0307 -0.0319 71  GLU B CD  
1561 O OE1 . GLU B 54  ? 1.0251 0.8682 0.7549 0.2072  -0.0327 -0.0357 71  GLU B OE1 
1562 O OE2 . GLU B 54  ? 1.0027 0.8502 0.7345 0.2044  -0.0265 -0.0298 71  GLU B OE2 
1563 N N   . GLU B 55  ? 0.5139 0.3447 0.2413 0.2024  -0.0481 -0.0331 72  GLU B N   
1564 C CA  A GLU B 55  ? 0.5439 0.3722 0.2725 0.2021  -0.0529 -0.0353 72  GLU B CA  
1565 C CA  B GLU B 55  ? 0.5430 0.3711 0.2712 0.2022  -0.0529 -0.0353 72  GLU B CA  
1566 C C   . GLU B 55  ? 0.5617 0.3837 0.2813 0.2023  -0.0556 -0.0348 72  GLU B C   
1567 O O   . GLU B 55  ? 0.5963 0.4122 0.3082 0.2044  -0.0595 -0.0369 72  GLU B O   
1568 C CB  A GLU B 55  ? 0.5688 0.4043 0.3136 0.1981  -0.0534 -0.0351 72  GLU B CB  
1569 C CB  B GLU B 55  ? 0.5681 0.4033 0.3126 0.1983  -0.0535 -0.0354 72  GLU B CB  
1570 C CG  A GLU B 55  ? 0.6536 0.4948 0.4089 0.1974  -0.0514 -0.0359 72  GLU B CG  
1571 C CG  B GLU B 55  ? 0.6619 0.5023 0.4161 0.1980  -0.0516 -0.0363 72  GLU B CG  
1572 C CD  A GLU B 55  ? 0.6474 0.4890 0.4093 0.1972  -0.0550 -0.0386 72  GLU B CD  
1573 C CD  B GLU B 55  ? 0.6537 0.4907 0.4037 0.2013  -0.0538 -0.0400 72  GLU B CD  
1574 O OE1 A GLU B 55  ? 0.6977 0.5334 0.4511 0.2000  -0.0583 -0.0410 72  GLU B OE1 
1575 O OE1 B GLU B 55  ? 0.6449 0.4755 0.3846 0.2039  -0.0572 -0.0416 72  GLU B OE1 
1576 O OE2 A GLU B 55  ? 0.6879 0.5354 0.4633 0.1944  -0.0546 -0.0381 72  GLU B OE2 
1577 O OE2 B GLU B 55  ? 0.7578 0.5985 0.5150 0.2014  -0.0523 -0.0414 72  GLU B OE2 
1578 N N   . HIS B 56  ? 0.5092 0.3329 0.2305 0.1998  -0.0537 -0.0323 73  HIS B N   
1579 C CA  . HIS B 56  ? 0.4941 0.3123 0.2090 0.1993  -0.0562 -0.0322 73  HIS B CA  
1580 C C   . HIS B 56  ? 0.5310 0.3396 0.2295 0.2034  -0.0572 -0.0331 73  HIS B C   
1581 O O   . HIS B 56  ? 0.5717 0.3739 0.2642 0.2041  -0.0609 -0.0347 73  HIS B O   
1582 C CB  . HIS B 56  ? 0.4883 0.3104 0.2085 0.1961  -0.0534 -0.0295 73  HIS B CB  
1583 C CG  . HIS B 56  ? 0.5077 0.3248 0.2234 0.1950  -0.0557 -0.0293 73  HIS B CG  
1584 N ND1 . HIS B 56  ? 0.5364 0.3542 0.2578 0.1928  -0.0593 -0.0303 73  HIS B ND1 
1585 C CD2 . HIS B 56  ? 0.6170 0.4285 0.3243 0.1956  -0.0549 -0.0280 73  HIS B CD2 
1586 C CE1 . HIS B 56  ? 0.5385 0.3514 0.2552 0.1921  -0.0609 -0.0299 73  HIS B CE1 
1587 N NE2 . HIS B 56  ? 0.5870 0.3959 0.2956 0.1935  -0.0583 -0.0283 73  HIS B NE2 
1588 N N   . TYR B 57  ? 0.5245 0.3320 0.2158 0.2061  -0.0538 -0.0321 74  TYR B N   
1589 C CA  . TYR B 57  ? 0.5333 0.3319 0.2096 0.2103  -0.0538 -0.0328 74  TYR B CA  
1590 C C   . TYR B 57  ? 0.6456 0.4426 0.3154 0.2147  -0.0551 -0.0350 74  TYR B C   
1591 O O   . TYR B 57  ? 0.6843 0.4789 0.3490 0.2180  -0.0532 -0.0338 74  TYR B O   
1592 C CB  . TYR B 57  ? 0.6482 0.4471 0.3222 0.2103  -0.0491 -0.0298 74  TYR B CB  
1593 C CG  . TYR B 57  ? 0.6658 0.4651 0.3444 0.2056  -0.0489 -0.0270 74  TYR B CG  
1594 C CD1 . TYR B 57  ? 0.6479 0.4422 0.3250 0.2034  -0.0529 -0.0267 74  TYR B CD1 
1595 C CD2 . TYR B 57  ? 0.6483 0.4534 0.3333 0.2033  -0.0450 -0.0247 74  TYR B CD2 
1596 C CE1 . TYR B 57  ? 0.7080 0.5029 0.3895 0.1993  -0.0533 -0.0244 74  TYR B CE1 
1597 C CE2 . TYR B 57  ? 0.6648 0.4705 0.3543 0.1993  -0.0452 -0.0225 74  TYR B CE2 
1598 C CZ  . TYR B 57  ? 0.7147 0.5153 0.4023 0.1975  -0.0495 -0.0224 74  TYR B CZ  
1599 O OH  . TYR B 57  ? 0.7975 0.5987 0.4894 0.1937  -0.0503 -0.0205 74  TYR B OH  
1600 N N   . ALA B 58  ? 0.5804 0.3803 0.2568 0.2142  -0.0584 -0.0370 75  ALA B N   
1601 C CA  . ALA B 58  ? 0.6401 0.4404 0.3156 0.2174  -0.0593 -0.0393 75  ALA B CA  
1602 C C   . ALA B 58  ? 0.6996 0.4917 0.3621 0.2213  -0.0615 -0.0401 75  ALA B C   
1603 O O   . ALA B 58  ? 0.7256 0.5210 0.3866 0.2208  -0.0586 -0.0426 75  ALA B O   
1604 C CB  . ALA B 58  ? 0.6168 0.4209 0.3039 0.2152  -0.0621 -0.0418 75  ALA B CB  
1605 N N   . GLU B 59  ? 0.7072 0.4919 0.3655 0.2210  -0.0638 -0.0399 76  GLU B N   
1606 C CA  . GLU B 59  ? 0.7189 0.5014 0.3686 0.2183  -0.0649 -0.0400 76  GLU B CA  
1607 C C   . GLU B 59  ? 0.8441 0.6317 0.4892 0.2144  -0.0599 -0.0379 76  GLU B C   
1608 O O   . GLU B 59  ? 0.8693 0.6590 0.5084 0.2124  -0.0593 -0.0392 76  GLU B O   
1609 C CB  . GLU B 59  ? 0.7519 0.5284 0.4000 0.2156  -0.0684 -0.0386 76  GLU B CB  
1610 C CG  . GLU B 59  ? 0.8411 0.6177 0.4917 0.2115  -0.0666 -0.0349 76  GLU B CG  
1611 C CD  . GLU B 59  ? 1.0759 0.8476 0.7271 0.2084  -0.0707 -0.0343 76  GLU B CD  
1612 O OE1 . GLU B 59  ? 0.8178 0.5859 0.4623 0.2066  -0.0733 -0.0337 76  GLU B OE1 
1613 O OE2 . GLU B 59  ? 0.8544 0.6271 0.5131 0.2071  -0.0711 -0.0347 76  GLU B OE2 
1614 N N   . HIS B 60  ? 0.8203 0.6108 0.4685 0.2132  -0.0561 -0.0350 77  HIS B N   
1615 C CA  . HIS B 60  ? 0.7681 0.5635 0.4124 0.2090  -0.0514 -0.0326 77  HIS B CA  
1616 C C   . HIS B 60  ? 0.7427 0.5454 0.3903 0.2103  -0.0467 -0.0348 77  HIS B C   
1617 O O   . HIS B 60  ? 0.7600 0.5677 0.4065 0.2073  -0.0422 -0.0328 77  HIS B O   
1618 C CB  . HIS B 60  ? 0.8124 0.6069 0.4585 0.2060  -0.0499 -0.0280 77  HIS B CB  
1619 C CG  . HIS B 60  ? 0.8683 0.6565 0.5140 0.2041  -0.0543 -0.0264 77  HIS B CG  
1620 N ND1 . HIS B 60  ? 0.8018 0.5867 0.4407 0.2012  -0.0575 -0.0261 77  HIS B ND1 
1621 C CD2 . HIS B 60  ? 0.7917 0.5773 0.4437 0.2039  -0.0558 -0.0255 77  HIS B CD2 
1622 C CE1 . HIS B 60  ? 0.8770 0.6568 0.5181 0.1997  -0.0610 -0.0248 77  HIS B CE1 
1623 N NE2 . HIS B 60  ? 0.9672 0.7479 0.6165 0.2011  -0.0600 -0.0247 77  HIS B NE2 
1624 N N   . LYS B 61  ? 0.6792 0.4833 0.3323 0.2142  -0.0478 -0.0388 78  LYS B N   
1625 C CA  . LYS B 61  ? 0.7122 0.5239 0.3711 0.2146  -0.0435 -0.0412 78  LYS B CA  
1626 C C   . LYS B 61  ? 0.8974 0.7143 0.5500 0.2113  -0.0402 -0.0424 78  LYS B C   
1627 O O   . LYS B 61  ? 0.8790 0.6943 0.5242 0.2099  -0.0424 -0.0435 78  LYS B O   
1628 C CB  . LYS B 61  ? 0.8577 0.6705 0.5248 0.2175  -0.0460 -0.0454 78  LYS B CB  
1629 C CG  . LYS B 61  ? 0.8618 0.6829 0.5379 0.2172  -0.0421 -0.0480 78  LYS B CG  
1630 C CD  . LYS B 61  ? 1.0648 0.8876 0.7503 0.2187  -0.0451 -0.0520 78  LYS B CD  
1631 C CE  . LYS B 61  ? 1.1166 0.9431 0.7999 0.2191  -0.0444 -0.0572 78  LYS B CE  
1632 N NZ  . LYS B 61  ? 1.0823 0.9087 0.7727 0.2207  -0.0486 -0.0613 78  LYS B NZ  
1633 N N   . GLY B 62  ? 0.9355 0.7592 0.5911 0.2098  -0.0350 -0.0419 79  GLY B N   
1634 C CA  . GLY B 62  ? 1.0401 0.8705 0.6912 0.2067  -0.0315 -0.0435 79  GLY B CA  
1635 C C   . GLY B 62  ? 1.0017 0.8325 0.6442 0.2017  -0.0301 -0.0391 79  GLY B C   
1636 O O   . GLY B 62  ? 0.9701 0.8080 0.6098 0.1985  -0.0263 -0.0395 79  GLY B O   
1637 N N   . LYS B 63  ? 0.8229 0.6468 0.4619 0.2006  -0.0330 -0.0351 80  LYS B N   
1638 C CA  . LYS B 63  ? 0.7748 0.5989 0.4069 0.1951  -0.0322 -0.0306 80  LYS B CA  
1639 C C   . LYS B 63  ? 0.9664 0.7949 0.6015 0.1926  -0.0274 -0.0272 80  LYS B C   
1640 O O   . LYS B 63  ? 0.9187 0.7479 0.5614 0.1956  -0.0255 -0.0274 80  LYS B O   
1641 C CB  . LYS B 63  ? 0.8004 0.6159 0.4297 0.1943  -0.0372 -0.0276 80  LYS B CB  
1642 C CG  . LYS B 63  ? 0.8377 0.6487 0.4642 0.1967  -0.0421 -0.0309 80  LYS B CG  
1643 C CD  . LYS B 63  ? 0.8294 0.6321 0.4540 0.1958  -0.0472 -0.0283 80  LYS B CD  
1644 C CE  . LYS B 63  ? 0.9076 0.7063 0.5303 0.1985  -0.0518 -0.0320 80  LYS B CE  
1645 N NZ  . LYS B 63  ? 1.0065 0.7971 0.6291 0.1984  -0.0570 -0.0302 80  LYS B NZ  
1646 N N   . PRO B 64  ? 1.2749 1.1068 0.9044 0.1870  -0.0255 -0.0240 81  PRO B N   
1647 C CA  . PRO B 64  ? 1.2007 1.0375 0.8331 0.1844  -0.0207 -0.0210 81  PRO B CA  
1648 C C   . PRO B 64  ? 0.9728 0.8045 0.6090 0.1842  -0.0214 -0.0165 81  PRO B C   
1649 O O   . PRO B 64  ? 0.9341 0.7693 0.5750 0.1836  -0.0175 -0.0147 81  PRO B O   
1650 C CB  . PRO B 64  ? 1.2683 1.1104 0.8930 0.1781  -0.0192 -0.0190 81  PRO B CB  
1651 C CG  . PRO B 64  ? 1.2507 1.0872 0.8685 0.1766  -0.0243 -0.0183 81  PRO B CG  
1652 C CD  . PRO B 64  ? 1.2003 1.0322 0.8207 0.1825  -0.0276 -0.0229 81  PRO B CD  
1653 N N   . PHE B 65  ? 0.8431 0.6670 0.4777 0.1844  -0.0263 -0.0149 82  PHE B N   
1654 C CA  . PHE B 65  ? 0.9244 0.7440 0.5633 0.1840  -0.0272 -0.0112 82  PHE B CA  
1655 C C   . PHE B 65  ? 0.9627 0.7797 0.6097 0.1897  -0.0279 -0.0131 82  PHE B C   
1656 O O   . PHE B 65  ? 0.8171 0.6322 0.4692 0.1898  -0.0278 -0.0106 82  PHE B O   
1657 C CB  . PHE B 65  ? 0.8817 0.6948 0.5162 0.1809  -0.0323 -0.0087 82  PHE B CB  
1658 C CG  . PHE B 65  ? 1.0219 0.8290 0.6560 0.1843  -0.0373 -0.0115 82  PHE B CG  
1659 C CD1 . PHE B 65  ? 1.0763 0.8837 0.7044 0.1845  -0.0390 -0.0143 82  PHE B CD1 
1660 C CD2 . PHE B 65  ? 0.9842 0.7858 0.6242 0.1871  -0.0404 -0.0117 82  PHE B CD2 
1661 C CE1 . PHE B 65  ? 0.9975 0.7992 0.6253 0.1876  -0.0437 -0.0168 82  PHE B CE1 
1662 C CE2 . PHE B 65  ? 1.0472 0.8436 0.6872 0.1899  -0.0451 -0.0143 82  PHE B CE2 
1663 C CZ  . PHE B 65  ? 1.1046 0.9008 0.7384 0.1903  -0.0468 -0.0168 82  PHE B CZ  
1664 N N   . LEU B 66  ? 0.7999 0.7408 0.6063 0.1930  0.0533  -0.0105 83  LEU B N   
1665 C CA  . LEU B 66  ? 0.7411 0.6838 0.5532 0.1923  0.0514  -0.0108 83  LEU B CA  
1666 C C   . LEU B 66  ? 0.6736 0.6185 0.4913 0.1907  0.0523  -0.0104 83  LEU B C   
1667 O O   . LEU B 66  ? 0.5364 0.4815 0.3574 0.1903  0.0509  -0.0098 83  LEU B O   
1668 C CB  . LEU B 66  ? 0.6486 0.5930 0.4623 0.1921  0.0505  -0.0125 83  LEU B CB  
1669 C CG  . LEU B 66  ? 0.6386 0.5846 0.4576 0.1915  0.0484  -0.0130 83  LEU B CG  
1670 C CD1 . LEU B 66  ? 0.5607 0.5047 0.3783 0.1927  0.0463  -0.0123 83  LEU B CD1 
1671 C CD2 . LEU B 66  ? 0.6544 0.6022 0.4751 0.1911  0.0477  -0.0146 83  LEU B CD2 
1672 N N   . PRO B 67  ? 0.5890 0.5354 0.4081 0.1896  0.0543  -0.0105 84  PRO B N   
1673 C CA  . PRO B 67  ? 0.5169 0.4654 0.3415 0.1881  0.0549  -0.0100 84  PRO B CA  
1674 C C   . PRO B 67  ? 0.5973 0.5445 0.4217 0.1882  0.0549  -0.0085 84  PRO B C   
1675 O O   . PRO B 67  ? 0.5476 0.4960 0.3764 0.1873  0.0540  -0.0082 84  PRO B O   
1676 C CB  . PRO B 67  ? 0.6754 0.6251 0.5000 0.1873  0.0575  -0.0103 84  PRO B CB  
1677 C CG  . PRO B 67  ? 0.5748 0.5240 0.3960 0.1879  0.0576  -0.0116 84  PRO B CG  
1678 C CD  . PRO B 67  ? 0.7238 0.6704 0.5400 0.1895  0.0562  -0.0113 84  PRO B CD  
1679 N N   . GLY B 68  ? 0.6230 0.5676 0.4422 0.1892  0.0558  -0.0076 85  GLY B N   
1680 C CA  . GLY B 68  ? 0.6314 0.5747 0.4504 0.1893  0.0558  -0.0062 85  GLY B CA  
1681 C C   . GLY B 68  ? 0.5606 0.5025 0.3798 0.1901  0.0535  -0.0060 85  GLY B C   
1682 O O   . GLY B 68  ? 0.5281 0.4700 0.3497 0.1896  0.0530  -0.0052 85  GLY B O   
1683 N N   . LEU B 69  ? 0.5658 0.5067 0.3825 0.1913  0.0520  -0.0067 86  LEU B N   
1684 C CA  . LEU B 69  ? 0.5124 0.4524 0.3300 0.1919  0.0496  -0.0068 86  LEU B CA  
1685 C C   . LEU B 69  ? 0.4829 0.4255 0.3069 0.1903  0.0485  -0.0073 86  LEU B C   
1686 O O   . LEU B 69  ? 0.4570 0.3994 0.2832 0.1900  0.0474  -0.0068 86  LEU B O   
1687 C CB  . LEU B 69  ? 0.6158 0.5546 0.4300 0.1934  0.0484  -0.0077 86  LEU B CB  
1688 C CG  . LEU B 69  ? 0.5668 0.5051 0.3824 0.1939  0.0457  -0.0080 86  LEU B CG  
1689 C CD1 . LEU B 69  ? 0.6714 0.6076 0.4864 0.1945  0.0451  -0.0067 86  LEU B CD1 
1690 C CD2 . LEU B 69  ? 0.7597 0.6968 0.5713 0.1955  0.0448  -0.0088 86  LEU B CD2 
1691 N N   . ILE B 70  ? 0.4772 0.4224 0.3041 0.1893  0.0487  -0.0083 87  ILE B N   
1692 C CA  A ILE B 70  ? 0.4434 0.3911 0.2761 0.1878  0.0477  -0.0088 87  ILE B CA  
1693 C CA  B ILE B 70  ? 0.4443 0.3921 0.2771 0.1878  0.0477  -0.0088 87  ILE B CA  
1694 C C   . ILE B 70  ? 0.4613 0.4098 0.2971 0.1866  0.0486  -0.0078 87  ILE B C   
1695 O O   . ILE B 70  ? 0.4004 0.3496 0.2396 0.1858  0.0474  -0.0077 87  ILE B O   
1696 C CB  A ILE B 70  ? 0.4609 0.4110 0.2961 0.1871  0.0480  -0.0101 87  ILE B CB  
1697 C CB  B ILE B 70  ? 0.4610 0.4112 0.2963 0.1870  0.0481  -0.0101 87  ILE B CB  
1698 C CG1 A ILE B 70  ? 0.4929 0.4423 0.3255 0.1882  0.0466  -0.0112 87  ILE B CG1 
1699 C CG1 B ILE B 70  ? 0.5055 0.4549 0.3377 0.1882  0.0471  -0.0112 87  ILE B CG1 
1700 C CG2 A ILE B 70  ? 0.4558 0.4087 0.2972 0.1854  0.0473  -0.0104 87  ILE B CG2 
1701 C CG2 B ILE B 70  ? 0.4563 0.4091 0.2976 0.1855  0.0471  -0.0105 87  ILE B CG2 
1702 C CD1 A ILE B 70  ? 0.4916 0.4432 0.3265 0.1876  0.0468  -0.0126 87  ILE B CD1 
1703 C CD1 B ILE B 70  ? 0.4249 0.3738 0.2576 0.1887  0.0446  -0.0116 87  ILE B CD1 
1704 N N   . GLU B 71  ? 0.4199 0.3682 0.2543 0.1865  0.0508  -0.0071 88  GLU B N   
1705 C CA  . GLU B 71  ? 0.4761 0.4251 0.3131 0.1854  0.0517  -0.0061 88  GLU B CA  
1706 C C   . GLU B 71  ? 0.5156 0.4627 0.3517 0.1858  0.0508  -0.0052 88  GLU B C   
1707 O O   . GLU B 71  ? 0.4900 0.4381 0.3297 0.1847  0.0503  -0.0049 88  GLU B O   
1708 C CB  . GLU B 71  ? 0.5264 0.4753 0.3615 0.1853  0.0543  -0.0054 88  GLU B CB  
1709 C CG  . GLU B 71  ? 0.7663 0.7179 0.6046 0.1842  0.0556  -0.0060 88  GLU B CG  
1710 C CD  . GLU B 71  ? 1.0742 1.0255 0.9102 0.1842  0.0581  -0.0053 88  GLU B CD  
1711 O OE1 . GLU B 71  ? 0.9017 0.8520 0.7368 0.1841  0.0591  -0.0041 88  GLU B OE1 
1712 O OE2 . GLU B 71  ? 1.0884 1.0403 0.9235 0.1843  0.0591  -0.0061 88  GLU B OE2 
1713 N N   . LYS B 72  ? 0.4719 0.4161 0.3031 0.1873  0.0507  -0.0047 89  LYS B N   
1714 C CA  A LYS B 72  ? 0.4540 0.3962 0.2843 0.1878  0.0500  -0.0039 89  LYS B CA  
1715 C CA  B LYS B 72  ? 0.4548 0.3969 0.2850 0.1878  0.0500  -0.0039 89  LYS B CA  
1716 C C   . LYS B 72  ? 0.4704 0.4130 0.3036 0.1874  0.0476  -0.0045 89  LYS B C   
1717 O O   . LYS B 72  ? 0.4230 0.3652 0.2580 0.1869  0.0470  -0.0040 89  LYS B O   
1718 C CB  A LYS B 72  ? 0.4774 0.4163 0.3018 0.1896  0.0504  -0.0032 89  LYS B CB  
1719 C CB  B LYS B 72  ? 0.4782 0.4170 0.3025 0.1897  0.0502  -0.0033 89  LYS B CB  
1720 C CG  A LYS B 72  ? 0.6043 0.5427 0.4258 0.1897  0.0529  -0.0025 89  LYS B CG  
1721 C CG  B LYS B 72  ? 0.6020 0.5400 0.4227 0.1900  0.0526  -0.0026 89  LYS B CG  
1722 C CD  A LYS B 72  ? 0.5996 0.5346 0.4152 0.1914  0.0535  -0.0017 89  LYS B CD  
1723 C CD  B LYS B 72  ? 0.5876 0.5226 0.4044 0.1912  0.0532  -0.0014 89  LYS B CD  
1724 C CE  A LYS B 72  ? 0.6475 0.5825 0.4604 0.1909  0.0559  -0.0011 89  LYS B CE  
1725 C CE  B LYS B 72  ? 0.6637 0.5974 0.4757 0.1914  0.0547  -0.0008 89  LYS B CE  
1726 N NZ  A LYS B 72  ? 0.7460 0.6826 0.5621 0.1897  0.0575  -0.0005 89  LYS B NZ  
1727 N NZ  B LYS B 72  ? 0.7527 0.6853 0.5611 0.1924  0.0535  -0.0014 89  LYS B NZ  
1728 N N   . MET B 73  ? 0.4043 0.3479 0.2382 0.1876  0.0462  -0.0057 90  MET B N   
1729 C CA  . MET B 73  ? 0.3664 0.3105 0.2030 0.1873  0.0440  -0.0064 90  MET B CA  
1730 C C   . MET B 73  ? 0.3610 0.3081 0.2032 0.1853  0.0436  -0.0069 90  MET B C   
1731 O O   . MET B 73  ? 0.3587 0.3063 0.2035 0.1848  0.0418  -0.0074 90  MET B O   
1732 C CB  . MET B 73  ? 0.4324 0.3761 0.2670 0.1884  0.0426  -0.0074 90  MET B CB  
1733 C CG  . MET B 73  ? 0.4655 0.4060 0.2948 0.1905  0.0422  -0.0069 90  MET B CG  
1734 S SD  . MET B 73  ? 0.4295 0.3680 0.2595 0.1908  0.0405  -0.0064 90  MET B SD  
1735 C CE  . MET B 73  ? 0.5002 0.4409 0.3348 0.1896  0.0381  -0.0077 90  MET B CE  
1736 N N   . THR B 74  ? 0.3719 0.3210 0.2162 0.1843  0.0452  -0.0068 91  THR B N   
1737 C CA  . THR B 74  ? 0.3696 0.3215 0.2192 0.1826  0.0449  -0.0072 91  THR B CA  
1738 C C   . THR B 74  ? 0.3792 0.3309 0.2306 0.1817  0.0451  -0.0063 91  THR B C   
1739 O O   . THR B 74  ? 0.4622 0.4138 0.3132 0.1814  0.0468  -0.0054 91  THR B O   
1740 C CB  . THR B 74  ? 0.3707 0.3247 0.2220 0.1819  0.0466  -0.0073 91  THR B CB  
1741 O OG1 . THR B 74  ? 0.4004 0.3544 0.2498 0.1827  0.0465  -0.0082 91  THR B OG1 
1742 C CG2 . THR B 74  ? 0.3696 0.3266 0.2265 0.1802  0.0461  -0.0078 91  THR B CG2 
1743 N N   . GLY B 75  ? 0.3163 0.2692 0.2205 0.1321  0.0080  -0.0110 92  GLY B N   
1744 C CA  . GLY B 75  ? 0.3120 0.2726 0.2257 0.1291  0.0075  -0.0103 92  GLY B CA  
1745 C C   . GLY B 75  ? 0.2718 0.2240 0.1855 0.1256  0.0071  -0.0096 92  GLY B C   
1746 O O   . GLY B 75  ? 0.2817 0.2223 0.1882 0.1253  0.0072  -0.0096 92  GLY B O   
1747 N N   . PRO B 76  ? 0.2616 0.2190 0.1833 0.1227  0.0066  -0.0089 93  PRO B N   
1748 C CA  . PRO B 76  ? 0.2691 0.2193 0.1920 0.1189  0.0062  -0.0081 93  PRO B CA  
1749 C C   . PRO B 76  ? 0.2419 0.1906 0.1678 0.1162  0.0060  -0.0078 93  PRO B C   
1750 O O   . PRO B 76  ? 0.2848 0.2429 0.2173 0.1158  0.0062  -0.0079 93  PRO B O   
1751 C CB  . PRO B 76  ? 0.2790 0.2383 0.2117 0.1166  0.0058  -0.0075 93  PRO B CB  
1752 C CG  . PRO B 76  ? 0.2625 0.2354 0.2018 0.1176  0.0061  -0.0080 93  PRO B CG  
1753 C CD  . PRO B 76  ? 0.3123 0.2829 0.2429 0.1223  0.0066  -0.0088 93  PRO B CD  
1754 N N   . VAL B 77  ? 0.2791 0.2156 0.1997 0.1142  0.0057  -0.0075 94  VAL B N   
1755 C CA  . VAL B 77  ? 0.2639 0.1971 0.1868 0.1111  0.0053  -0.0070 94  VAL B CA  
1756 C C   . VAL B 77  ? 0.3095 0.2344 0.2329 0.1069  0.0046  -0.0062 94  VAL B C   
1757 O O   . VAL B 77  ? 0.3027 0.2208 0.2211 0.1070  0.0046  -0.0062 94  VAL B O   
1758 C CB  . VAL B 77  ? 0.2697 0.1943 0.1832 0.1130  0.0057  -0.0078 94  VAL B CB  
1759 C CG1 . VAL B 77  ? 0.2828 0.2162 0.1966 0.1167  0.0064  -0.0087 94  VAL B CG1 
1760 C CG2 . VAL B 77  ? 0.3441 0.2546 0.2454 0.1140  0.0059  -0.0083 94  VAL B CG2 
1761 N N   . LEU B 78  ? 0.2764 0.2022 0.2064 0.1032  0.0039  -0.0053 95  LEU B N   
1762 C CA  . LEU B 78  ? 0.2726 0.1892 0.2025 0.0987  0.0032  -0.0044 95  LEU B CA  
1763 C C   . LEU B 78  ? 0.2931 0.1983 0.2159 0.0971  0.0028  -0.0045 95  LEU B C   
1764 O O   . LEU B 78  ? 0.3002 0.2102 0.2275 0.0942  0.0024  -0.0039 95  LEU B O   
1765 C CB  . LEU B 78  ? 0.2424 0.1674 0.1850 0.0950  0.0025  -0.0031 95  LEU B CB  
1766 C CG  . LEU B 78  ? 0.2513 0.1676 0.1941 0.0903  0.0018  -0.0023 95  LEU B CG  
1767 C CD1 . LEU B 78  ? 0.2960 0.2098 0.2354 0.0912  0.0021  -0.0028 95  LEU B CD1 
1768 C CD2 . LEU B 78  ? 0.2499 0.1743 0.2054 0.0853  0.0010  -0.0008 95  LEU B CD2 
1769 N N   . CYS B 79  ? 0.3072 0.1996 0.2198 0.0966  0.0029  -0.0051 96  CYS B N   
1770 C CA  . CYS B 79  ? 0.3119 0.1920 0.2170 0.0941  0.0026  -0.0053 96  CYS B CA  
1771 C C   . CYS B 79  ? 0.3123 0.1890 0.2227 0.0873  0.0014  -0.0040 96  CYS B C   
1772 O O   . CYS B 79  ? 0.3188 0.1941 0.2317 0.0854  0.0013  -0.0036 96  CYS B O   
1773 C CB  . CYS B 79  ? 0.3309 0.2001 0.2240 0.0954  0.0034  -0.0064 96  CYS B CB  
1774 S SG  . CYS B 79  ? 0.3671 0.2412 0.2546 0.1026  0.0046  -0.0075 96  CYS B SG  
1775 N N   . MET B 80  ? 0.2914 0.1692 0.2047 0.0815  0.0006  -0.0033 97  MET B N   
1776 C CA  . MET B 80  ? 0.2906 0.1672 0.2102 0.0738  -0.0007 -0.0020 97  MET B CA  
1777 C C   . MET B 80  ? 0.3097 0.1777 0.2236 0.0692  -0.0013 -0.0021 97  MET B C   
1778 O O   . MET B 80  ? 0.2921 0.1603 0.2017 0.0705  -0.0011 -0.0027 97  MET B O   
1779 C CB  . MET B 80  ? 0.2497 0.1413 0.1837 0.0703  -0.0014 -0.0004 97  MET B CB  
1780 C CG  . MET B 80  ? 0.2994 0.2017 0.2396 0.0750  -0.0006 -0.0005 97  MET B CG  
1781 S SD  . MET B 80  ? 0.2767 0.1963 0.2339 0.0707  -0.0011 0.0012  97  MET B SD  
1782 C CE  . MET B 80  ? 0.2903 0.2157 0.2479 0.0698  -0.0013 0.0014  97  MET B CE  
1783 N N   . VAL B 81  ? 0.3009 0.1614 0.2149 0.0637  -0.0021 -0.0016 98  VAL B N   
1784 C CA  . VAL B 81  ? 0.3085 0.1635 0.2204 0.0577  -0.0031 -0.0014 98  VAL B CA  
1785 C C   . VAL B 81  ? 0.2807 0.1420 0.2044 0.0507  -0.0045 0.0005  98  VAL B C   
1786 O O   . VAL B 81  ? 0.2868 0.1463 0.2140 0.0489  -0.0046 0.0009  98  VAL B O   
1787 C CB  . VAL B 81  ? 0.3194 0.1578 0.2189 0.0574  -0.0027 -0.0027 98  VAL B CB  
1788 C CG1 . VAL B 81  ? 0.3388 0.1728 0.2376 0.0506  -0.0039 -0.0024 98  VAL B CG1 
1789 C CG2 . VAL B 81  ? 0.3553 0.1870 0.2428 0.0644  -0.0013 -0.0045 98  VAL B CG2 
1790 N N   . PHE B 82  ? 0.2666 0.1354 0.1964 0.0466  -0.0054 0.0016  99  PHE B N   
1791 C CA  . PHE B 82  ? 0.2604 0.1343 0.2008 0.0396  -0.0068 0.0033  99  PHE B CA  
1792 C C   . PHE B 82  ? 0.2893 0.1561 0.2261 0.0339  -0.0079 0.0035  99  PHE B C   
1793 O O   . PHE B 82  ? 0.2887 0.1521 0.2182 0.0348  -0.0078 0.0027  99  PHE B O   
1794 C CB  . PHE B 82  ? 0.2883 0.1780 0.2407 0.0389  -0.0070 0.0049  99  PHE B CB  
1795 C CG  . PHE B 82  ? 0.2451 0.1434 0.2057 0.0415  -0.0064 0.0053  99  PHE B CG  
1796 C CD1 . PHE B 82  ? 0.3007 0.2032 0.2591 0.0483  -0.0051 0.0043  99  PHE B CD1 
1797 C CD2 . PHE B 82  ? 0.2280 0.1300 0.1984 0.0370  -0.0069 0.0066  99  PHE B CD2 
1798 C CE1 . PHE B 82  ? 0.3116 0.2223 0.2774 0.0506  -0.0045 0.0046  99  PHE B CE1 
1799 C CE2 . PHE B 82  ? 0.2628 0.1730 0.2408 0.0392  -0.0063 0.0069  99  PHE B CE2 
1800 C CZ  . PHE B 82  ? 0.2570 0.1713 0.2324 0.0460  -0.0051 0.0058  99  PHE B CZ  
1801 N N   . GLU B 83  ? 0.2731 0.1386 0.2156 0.0278  -0.0089 0.0045  100 GLU B N   
1802 C CA  . GLU B 83  ? 0.3007 0.1597 0.2408 0.0219  -0.0102 0.0047  100 GLU B CA  
1803 C C   . GLU B 83  ? 0.2924 0.1614 0.2449 0.0157  -0.0116 0.0069  100 GLU B C   
1804 O O   . GLU B 83  ? 0.2676 0.1432 0.2302 0.0140  -0.0118 0.0081  100 GLU B O   
1805 C CB  . GLU B 83  ? 0.3072 0.1534 0.2414 0.0198  -0.0101 0.0037  100 GLU B CB  
1806 C CG  . GLU B 83  ? 0.3290 0.1684 0.2614 0.0132  -0.0113 0.0038  100 GLU B CG  
1807 C CD  . GLU B 83  ? 0.3644 0.1916 0.2915 0.0114  -0.0111 0.0028  100 GLU B CD  
1808 O OE1 . GLU B 83  ? 0.4149 0.2340 0.3315 0.0140  -0.0098 0.0009  100 GLU B OE1 
1809 O OE2 . GLU B 83  ? 0.3850 0.2179 0.3219 0.0072  -0.0114 0.0038  100 GLU B OE2 
1810 N N   . GLY B 84  ? 0.2598 0.1292 0.2114 0.0123  -0.0127 0.0073  101 GLY B N   
1811 C CA  . GLY B 84  ? 0.2617 0.1393 0.2241 0.0063  -0.0141 0.0095  101 GLY B CA  
1812 C C   . GLY B 84  ? 0.2624 0.1389 0.2210 0.0034  -0.0152 0.0096  101 GLY B C   
1813 O O   . GLY B 84  ? 0.2730 0.1427 0.2208 0.0061  -0.0147 0.0080  101 GLY B O   
1814 N N   . VAL B 85  ? 0.2346 0.1178 0.2023 -0.0022 -0.0167 0.0116  102 VAL B N   
1815 C CA  . VAL B 85  ? 0.2584 0.1426 0.2243 -0.0053 -0.0179 0.0122  102 VAL B CA  
1816 C C   . VAL B 85  ? 0.2460 0.1373 0.2105 -0.0008 -0.0171 0.0122  102 VAL B C   
1817 O O   . VAL B 85  ? 0.2541 0.1561 0.2268 0.0011  -0.0166 0.0134  102 VAL B O   
1818 C CB  . VAL B 85  ? 0.2746 0.1657 0.2516 -0.0118 -0.0195 0.0146  102 VAL B CB  
1819 C CG1 . VAL B 85  ? 0.3254 0.2187 0.3009 -0.0147 -0.0208 0.0154  102 VAL B CG1 
1820 C CG2 . VAL B 85  ? 0.2961 0.1795 0.2737 -0.0164 -0.0203 0.0144  102 VAL B CG2 
1821 N N   . ASP B 86  ? 0.2666 0.1518 0.2205 0.0007  -0.0169 0.0107  103 ASP B N   
1822 C CA  . ASP B 86  ? 0.2671 0.1589 0.2194 0.0043  -0.0163 0.0107  103 ASP B CA  
1823 C C   . ASP B 86  ? 0.2625 0.1595 0.2163 0.0107  -0.0146 0.0102  103 ASP B C   
1824 O O   . ASP B 86  ? 0.2473 0.1541 0.2053 0.0130  -0.0141 0.0109  103 ASP B O   
1825 C CB  . ASP B 86  ? 0.2631 0.1656 0.2249 0.0000  -0.0177 0.0132  103 ASP B CB  
1826 C CG  . ASP B 86  ? 0.2949 0.2032 0.2541 0.0025  -0.0173 0.0132  103 ASP B CG  
1827 O OD1 . ASP B 86  ? 0.3376 0.2388 0.2855 0.0049  -0.0168 0.0114  103 ASP B OD1 
1828 O OD2 . ASP B 86  ? 0.2848 0.2048 0.2535 0.0016  -0.0175 0.0152  103 ASP B OD2 
1829 N N   . VAL B 87  ? 0.2645 0.1552 0.2150 0.0137  -0.0136 0.0089  104 VAL B N   
1830 C CA  . VAL B 87  ? 0.2494 0.1464 0.2035 0.0191  -0.0122 0.0087  104 VAL B CA  
1831 C C   . VAL B 87  ? 0.2453 0.1437 0.1925 0.0253  -0.0109 0.0073  104 VAL B C   
1832 O O   . VAL B 87  ? 0.2484 0.1559 0.2006 0.0292  -0.0099 0.0075  104 VAL B O   
1833 C CB  . VAL B 87  ? 0.2373 0.1272 0.1895 0.0207  -0.0116 0.0077  104 VAL B CB  
1834 C CG1 . VAL B 87  ? 0.2977 0.1743 0.2357 0.0246  -0.0106 0.0053  104 VAL B CG1 
1835 C CG2 . VAL B 87  ? 0.2461 0.1451 0.2060 0.0245  -0.0106 0.0082  104 VAL B CG2 
1836 N N   . ILE B 88  ? 0.2360 0.1259 0.1720 0.0263  -0.0107 0.0058  105 ILE B N   
1837 C CA  . ILE B 88  ? 0.2504 0.1417 0.1801 0.0321  -0.0094 0.0044  105 ILE B CA  
1838 C C   . ILE B 88  ? 0.2583 0.1629 0.1959 0.0316  -0.0096 0.0059  105 ILE B C   
1839 O O   . ILE B 88  ? 0.2545 0.1675 0.1959 0.0360  -0.0085 0.0059  105 ILE B O   
1840 C CB  . ILE B 88  ? 0.2914 0.1708 0.2076 0.0328  -0.0092 0.0025  105 ILE B CB  
1841 C CG1 . ILE B 88  ? 0.2972 0.1636 0.2053 0.0344  -0.0085 0.0009  105 ILE B CG1 
1842 C CG2 . ILE B 88  ? 0.3060 0.1880 0.2165 0.0383  -0.0079 0.0013  105 ILE B CG2 
1843 C CD1 . ILE B 88  ? 0.3375 0.1912 0.2329 0.0336  -0.0084 -0.0009 105 ILE B CD1 
1844 N N   . ALA B 89  ? 0.2658 0.1727 0.2063 0.0261  -0.0110 0.0073  106 ALA B N   
1845 C CA  . ALA B 89  ? 0.2592 0.1782 0.2071 0.0252  -0.0113 0.0089  106 ALA B CA  
1846 C C   . ALA B 89  ? 0.2146 0.1449 0.1758 0.0245  -0.0112 0.0107  106 ALA B C   
1847 O O   . ALA B 89  ? 0.2293 0.1701 0.1960 0.0266  -0.0105 0.0113  106 ALA B O   
1848 C CB  . ALA B 89  ? 0.2541 0.1728 0.2025 0.0191  -0.0129 0.0102  106 ALA B CB  
1849 N N   . GLN B 90  ? 0.2110 0.1394 0.1777 0.0211  -0.0120 0.0116  107 GLN B N   
1850 C CA  . GLN B 90  ? 0.1879 0.1270 0.1675 0.0198  -0.0119 0.0134  107 GLN B CA  
1851 C C   . GLN B 90  ? 0.1843 0.1278 0.1651 0.0259  -0.0102 0.0123  107 GLN B C   
1852 O O   . GLN B 90  ? 0.1915 0.1466 0.1814 0.0267  -0.0096 0.0133  107 GLN B O   
1853 C CB  . GLN B 90  ? 0.2234 0.1591 0.2084 0.0147  -0.0130 0.0144  107 GLN B CB  
1854 C CG  . GLN B 90  ? 0.2062 0.1412 0.1937 0.0081  -0.0148 0.0161  107 GLN B CG  
1855 C CD  . GLN B 90  ? 0.1969 0.1443 0.1942 0.0058  -0.0152 0.0183  107 GLN B CD  
1856 O OE1 . GLN B 90  ? 0.1836 0.1402 0.1913 0.0056  -0.0148 0.0196  107 GLN B OE1 
1857 N NE2 . GLN B 90  ? 0.2406 0.1883 0.2344 0.0041  -0.0160 0.0188  107 GLN B NE2 
1858 N N   . ALA B 91  ? 0.2030 0.1376 0.1748 0.0302  -0.0094 0.0102  108 ALA B N   
1859 C CA  . ALA B 91  ? 0.2095 0.1483 0.1819 0.0363  -0.0078 0.0091  108 ALA B CA  
1860 C C   . ALA B 91  ? 0.2041 0.1507 0.1758 0.0404  -0.0068 0.0086  108 ALA B C   
1861 O O   . ALA B 91  ? 0.2230 0.1795 0.2014 0.0432  -0.0058 0.0088  108 ALA B O   
1862 C CB  . ALA B 91  ? 0.2355 0.1628 0.1977 0.0405  -0.0071 0.0071  108 ALA B CB  
1863 N N   . ARG B 92  ? 0.2366 0.1789 0.2002 0.0406  -0.0069 0.0080  109 ARG B N   
1864 C CA  . ARG B 92  ? 0.2406 0.1905 0.2037 0.0440  -0.0060 0.0076  109 ARG B CA  
1865 C C   . ARG B 92  ? 0.2259 0.1892 0.2012 0.0409  -0.0062 0.0097  109 ARG B C   
1866 O O   . ARG B 92  ? 0.2352 0.2081 0.2147 0.0443  -0.0050 0.0095  109 ARG B O   
1867 C CB  . ARG B 92  ? 0.2804 0.2232 0.2331 0.0437  -0.0062 0.0066  109 ARG B CB  
1868 C CG  . ARG B 92  ? 0.3070 0.2368 0.2468 0.0476  -0.0056 0.0043  109 ARG B CG  
1869 C CD  . ARG B 92  ? 0.3584 0.2899 0.2937 0.0551  -0.0038 0.0024  109 ARG B CD  
1870 N NE  . ARG B 92  ? 0.4425 0.3777 0.3743 0.0568  -0.0032 0.0019  109 ARG B NE  
1871 C CZ  . ARG B 92  ? 0.5591 0.4946 0.4849 0.0631  -0.0017 0.0000  109 ARG B CZ  
1872 N NH1 . ARG B 92  ? 0.4664 0.3982 0.3883 0.0685  -0.0006 -0.0014 109 ARG B NH1 
1873 N NH2 . ARG B 92  ? 0.5290 0.4686 0.4526 0.0639  -0.0012 -0.0003 109 ARG B NH2 
1874 N N   . LYS B 93  ? 0.1907 0.1548 0.1719 0.0344  -0.0077 0.0117  110 LYS B N   
1875 C CA  . LYS B 93  ? 0.1711 0.1472 0.1641 0.0311  -0.0080 0.0140  110 LYS B CA  
1876 C C   . LYS B 93  ? 0.1723 0.1568 0.1751 0.0327  -0.0070 0.0143  110 LYS B C   
1877 O O   . LYS B 93  ? 0.2020 0.1978 0.2122 0.0336  -0.0061 0.0150  110 LYS B O   
1878 C CB  . LYS B 93  ? 0.1870 0.1611 0.1839 0.0239  -0.0098 0.0160  110 LYS B CB  
1879 C CG  . LYS B 93  ? 0.1757 0.1614 0.1847 0.0202  -0.0101 0.0185  110 LYS B CG  
1880 C CD  . LYS B 93  ? 0.1751 0.1581 0.1869 0.0135  -0.0121 0.0205  110 LYS B CD  
1881 C CE  . LYS B 93  ? 0.2588 0.2529 0.2831 0.0096  -0.0124 0.0232  110 LYS B CE  
1882 N NZ  . LYS B 93  ? 0.2548 0.2456 0.2814 0.0031  -0.0144 0.0251  110 LYS B NZ  
1883 N N   . MET B 94  ? 0.1725 0.1516 0.1753 0.0329  -0.0071 0.0138  111 MET B N   
1884 C CA  . MET B 94  ? 0.1774 0.1639 0.1891 0.0342  -0.0062 0.0140  111 MET B CA  
1885 C C   . MET B 94  ? 0.2026 0.1944 0.2123 0.0411  -0.0045 0.0123  111 MET B C   
1886 O O   . MET B 94  ? 0.1786 0.1807 0.1973 0.0421  -0.0036 0.0127  111 MET B O   
1887 C CB  . MET B 94  ? 0.1866 0.1654 0.1976 0.0330  -0.0068 0.0137  111 MET B CB  
1888 C CG  . MET B 94  ? 0.1849 0.1601 0.1998 0.0260  -0.0084 0.0155  111 MET B CG  
1889 S SD  . MET B 94  ? 0.1990 0.1617 0.2093 0.0250  -0.0090 0.0146  111 MET B SD  
1890 C CE  . MET B 94  ? 0.2471 0.2179 0.2678 0.0263  -0.0080 0.0149  111 MET B CE  
1891 N N   . MET B 95  ? 0.1647 0.1491 0.1628 0.0459  -0.0040 0.0103  112 MET B N   
1892 C CA  . MET B 95  ? 0.1830 0.1719 0.1784 0.0527  -0.0023 0.0085  112 MET B CA  
1893 C C   . MET B 95  ? 0.1859 0.1859 0.1860 0.0532  -0.0016 0.0090  112 MET B C   
1894 O O   . MET B 95  ? 0.1896 0.1990 0.1946 0.0567  -0.0003 0.0085  112 MET B O   
1895 C CB  . MET B 95  ? 0.2244 0.2021 0.2060 0.0573  -0.0020 0.0064  112 MET B CB  
1896 C CG  . MET B 95  ? 0.2297 0.1973 0.2061 0.0585  -0.0022 0.0055  112 MET B CG  
1897 S SD  . MET B 95  ? 0.3355 0.2890 0.2954 0.0635  -0.0017 0.0031  112 MET B SD  
1898 C CE  . MET B 95  ? 0.4635 0.4236 0.4200 0.0686  -0.0004 0.0019  112 MET B CE  
1899 N N   . GLY B 96  ? 0.1972 0.1965 0.1961 0.0494  -0.0024 0.0101  113 GLY B N   
1900 C CA  . GLY B 96  ? 0.1885 0.1969 0.1902 0.0498  -0.0017 0.0105  113 GLY B CA  
1901 C C   . GLY B 96  ? 0.1935 0.1988 0.1848 0.0551  -0.0008 0.0084  113 GLY B C   
1902 O O   . GLY B 96  ? 0.2088 0.2053 0.1908 0.0591  -0.0005 0.0065  113 GLY B O   
1903 N N   . SER B 97  ? 0.1967 0.2098 0.1901 0.0550  -0.0002 0.0088  114 SER B N   
1904 C CA  . SER B 97  ? 0.2587 0.2707 0.2435 0.0598  0.0009  0.0069  114 SER B CA  
1905 C C   . SER B 97  ? 0.2271 0.2384 0.2076 0.0669  0.0023  0.0045  114 SER B C   
1906 O O   . SER B 97  ? 0.2076 0.2252 0.1949 0.0687  0.0030  0.0045  114 SER B O   
1907 C CB  . SER B 97  ? 0.2174 0.2408 0.2079 0.0591  0.0017  0.0078  114 SER B CB  
1908 O OG  . SER B 97  ? 0.3752 0.4001 0.3705 0.0526  0.0004  0.0102  114 SER B OG  
1909 N N   . THR B 98  ? 0.2162 0.2203 0.1854 0.0711  0.0029  0.0026  115 THR B N   
1910 C CA  . THR B 98  ? 0.2145 0.2178 0.1786 0.0783  0.0043  0.0002  115 THR B CA  
1911 C C   . THR B 98  ? 0.1878 0.2048 0.1602 0.0813  0.0057  0.0000  115 THR B C   
1912 O O   . THR B 98  ? 0.2326 0.2521 0.2062 0.0859  0.0065  -0.0012 115 THR B O   
1913 C CB  . THR B 98  ? 0.3597 0.3557 0.3116 0.0820  0.0049  -0.0017 115 THR B CB  
1914 O OG1 . THR B 98  ? 0.4376 0.4212 0.3817 0.0787  0.0037  -0.0015 115 THR B OG1 
1915 C CG2 . THR B 98  ? 0.4066 0.4003 0.3524 0.0896  0.0063  -0.0040 115 THR B CG2 
1916 N N   . ARG B 99  ? 0.2369 0.2626 0.2141 0.0793  0.0061  0.0008  116 ARG B N   
1917 C CA  . ARG B 99  ? 0.2158 0.2551 0.2014 0.0815  0.0075  0.0006  116 ARG B CA  
1918 C C   . ARG B 99  ? 0.1807 0.2276 0.1788 0.0767  0.0070  0.0027  116 ARG B C   
1919 O O   . ARG B 99  ? 0.2060 0.2543 0.2087 0.0709  0.0061  0.0048  116 ARG B O   
1920 C CB  . ARG B 99  ? 0.2421 0.2870 0.2268 0.0813  0.0083  0.0005  116 ARG B CB  
1921 C CG  . ARG B 99  ? 0.3126 0.3520 0.2858 0.0869  0.0093  -0.0020 116 ARG B CG  
1922 C CD  . ARG B 99  ? 0.5341 0.5728 0.5028 0.0849  0.0093  -0.0018 116 ARG B CD  
1923 N NE  . ARG B 99  ? 0.7589 0.7860 0.7208 0.0808  0.0077  -0.0009 116 ARG B NE  
1924 C CZ  . ARG B 99  ? 0.7518 0.7669 0.7025 0.0833  0.0075  -0.0025 116 ARG B CZ  
1925 N NH1 . ARG B 99  ? 0.7212 0.7337 0.6655 0.0899  0.0087  -0.0049 116 ARG B NH1 
1926 N NH2 . ARG B 99  ? 0.7661 0.7714 0.7118 0.0789  0.0060  -0.0016 116 ARG B NH2 
1927 N N   . PRO B 100 ? 0.1800 0.2321 0.1841 0.0790  0.0077  0.0022  117 PRO B N   
1928 C CA  . PRO B 100 ? 0.1669 0.2254 0.1827 0.0743  0.0072  0.0042  117 PRO B CA  
1929 C C   . PRO B 100 ? 0.1738 0.2433 0.1987 0.0705  0.0078  0.0058  117 PRO B C   
1930 O O   . PRO B 100 ? 0.1927 0.2642 0.2253 0.0648  0.0069  0.0081  117 PRO B O   
1931 C CB  . PRO B 100 ? 0.1750 0.2384 0.1944 0.0787  0.0082  0.0028  117 PRO B CB  
1932 C CG  . PRO B 100 ? 0.1929 0.2471 0.2010 0.0843  0.0083  0.0008  117 PRO B CG  
1933 C CD  . PRO B 100 ? 0.1837 0.2352 0.1838 0.0858  0.0086  0.0000  117 PRO B CD  
1934 N N   . GLY B 101 ? 0.2009 0.2775 0.2252 0.0735  0.0092  0.0048  118 GLY B N   
1935 C CA  . GLY B 101 ? 0.1924 0.2793 0.2251 0.0701  0.0099  0.0063  118 GLY B CA  
1936 C C   . GLY B 101 ? 0.1815 0.2641 0.2130 0.0643  0.0085  0.0085  118 GLY B C   
1937 O O   . GLY B 101 ? 0.2047 0.2948 0.2445 0.0601  0.0087  0.0104  118 GLY B O   
1938 N N   . GLU B 102 ? 0.1984 0.2691 0.2198 0.0641  0.0072  0.0082  119 GLU B N   
1939 C CA  . GLU B 102 ? 0.1873 0.2531 0.2067 0.0588  0.0057  0.0101  119 GLU B CA  
1940 C C   . GLU B 102 ? 0.1995 0.2585 0.2211 0.0540  0.0039  0.0117  119 GLU B C   
1941 O O   . GLU B 102 ? 0.2329 0.2889 0.2546 0.0489  0.0025  0.0136  119 GLU B O   
1942 C CB  . GLU B 102 ? 0.2353 0.2922 0.2419 0.0611  0.0055  0.0086  119 GLU B CB  
1943 C CG  . GLU B 102 ? 0.3398 0.4030 0.3437 0.0649  0.0071  0.0072  119 GLU B CG  
1944 C CD  . GLU B 102 ? 0.5778 0.6316 0.5683 0.0683  0.0072  0.0051  119 GLU B CD  
1945 O OE1 . GLU B 102 ? 0.5246 0.5671 0.5080 0.0667  0.0058  0.0052  119 GLU B OE1 
1946 O OE2 . GLU B 102 ? 0.5776 0.6352 0.5647 0.0727  0.0087  0.0034  119 GLU B OE2 
1947 N N   . ALA B 103 ? 0.1743 0.2313 0.1977 0.0556  0.0039  0.0111  120 ALA B N   
1948 C CA  . ALA B 103 ? 0.1615 0.2114 0.1863 0.0515  0.0022  0.0123  120 ALA B CA  
1949 C C   . ALA B 103 ? 0.1814 0.2389 0.2187 0.0459  0.0018  0.0150  120 ALA B C   
1950 O O   . ALA B 103 ? 0.1938 0.2626 0.2400 0.0461  0.0031  0.0154  120 ALA B O   
1951 C CB  . ALA B 103 ? 0.1890 0.2345 0.2116 0.0553  0.0025  0.0107  120 ALA B CB  
1952 N N   . ALA B 104 ? 0.1875 0.2386 0.2252 0.0407  0.0001  0.0167  121 ALA B N   
1953 C CA  . ALA B 104 ? 0.2308 0.2882 0.2800 0.0350  -0.0005 0.0194  121 ALA B CA  
1954 C C   . ALA B 104 ? 0.2264 0.2887 0.2845 0.0352  0.0003  0.0194  121 ALA B C   
1955 O O   . ALA B 104 ? 0.1693 0.2259 0.2240 0.0375  0.0001  0.0180  121 ALA B O   
1956 C CB  . ALA B 104 ? 0.2356 0.2846 0.2827 0.0296  -0.0026 0.0210  121 ALA B CB  
1957 N N   . PRO B 105 ? 0.2675 0.3401 0.3373 0.0323  0.0010  0.0211  122 PRO B N   
1958 C CA  . PRO B 105 ? 0.2362 0.3132 0.3149 0.0316  0.0015  0.0213  122 PRO B CA  
1959 C C   . PRO B 105 ? 0.1576 0.2251 0.2349 0.0287  -0.0001 0.0218  122 PRO B C   
1960 O O   . PRO B 105 ? 0.2233 0.2843 0.2978 0.0247  -0.0018 0.0232  122 PRO B O   
1961 C CB  . PRO B 105 ? 0.3476 0.4353 0.4384 0.0275  0.0022  0.0236  122 PRO B CB  
1962 C CG  . PRO B 105 ? 0.3775 0.4686 0.4651 0.0282  0.0027  0.0239  122 PRO B CG  
1963 C CD  . PRO B 105 ? 0.3039 0.3838 0.3793 0.0289  0.0012  0.0232  122 PRO B CD  
1964 N N   . GLY B 106 ? 0.1622 0.2286 0.2408 0.0307  0.0003  0.0206  123 GLY B N   
1965 C CA  . GLY B 106 ? 0.1674 0.2246 0.2444 0.0282  -0.0011 0.0208  123 GLY B CA  
1966 C C   . GLY B 106 ? 0.1527 0.1980 0.2168 0.0317  -0.0018 0.0189  123 GLY B C   
1967 O O   . GLY B 106 ? 0.1852 0.2226 0.2474 0.0303  -0.0027 0.0188  123 GLY B O   
1968 N N   . THR B 107 ? 0.1468 0.1902 0.2021 0.0360  -0.0013 0.0174  124 THR B N   
1969 C CA  . THR B 107 ? 0.1245 0.1569 0.1675 0.0400  -0.0016 0.0153  124 THR B CA  
1970 C C   . THR B 107 ? 0.1552 0.1901 0.1973 0.0459  -0.0002 0.0133  124 THR B C   
1971 O O   . THR B 107 ? 0.1491 0.1947 0.1988 0.0476  0.0011  0.0131  124 THR B O   
1972 C CB  . THR B 107 ? 0.1283 0.1570 0.1617 0.0420  -0.0017 0.0146  124 THR B CB  
1973 O OG1 . THR B 107 ? 0.1534 0.1917 0.1886 0.0457  -0.0001 0.0138  124 THR B OG1 
1974 C CG2 . THR B 107 ? 0.1590 0.1852 0.1928 0.0361  -0.0032 0.0166  124 THR B CG2 
1975 N N   . ILE B 108 ? 0.1393 0.1637 0.1716 0.0491  -0.0005 0.0117  125 ILE B N   
1976 C CA  . ILE B 108 ? 0.1747 0.2002 0.2052 0.0549  0.0006  0.0098  125 ILE B CA  
1977 C C   . ILE B 108 ? 0.1849 0.2184 0.2144 0.0602  0.0021  0.0084  125 ILE B C   
1978 O O   . ILE B 108 ? 0.1427 0.1854 0.1783 0.0630  0.0033  0.0078  125 ILE B O   
1979 C CB  . ILE B 108 ? 0.1640 0.1759 0.1832 0.0574  0.0000  0.0084  125 ILE B CB  
1980 C CG1 . ILE B 108 ? 0.1814 0.1864 0.2028 0.0525  -0.0012 0.0096  125 ILE B CG1 
1981 C CG2 . ILE B 108 ? 0.1720 0.1849 0.1876 0.0644  0.0013  0.0064  125 ILE B CG2 
1982 C CD1 . ILE B 108 ? 0.2401 0.2305 0.2501 0.0537  -0.0019 0.0085  125 ILE B CD1 
1983 N N   . ARG B 109 ? 0.1513 0.1816 0.1731 0.0617  0.0021  0.0078  126 ARG B N   
1984 C CA  . ARG B 109 ? 0.1497 0.1869 0.1696 0.0672  0.0036  0.0063  126 ARG B CA  
1985 C C   . ARG B 109 ? 0.1467 0.1980 0.1779 0.0654  0.0046  0.0073  126 ARG B C   
1986 O O   . ARG B 109 ? 0.1658 0.2258 0.1999 0.0696  0.0061  0.0061  126 ARG B O   
1987 C CB  . ARG B 109 ? 0.1865 0.2164 0.1953 0.0690  0.0035  0.0054  126 ARG B CB  
1988 C CG  . ARG B 109 ? 0.2145 0.2317 0.2119 0.0727  0.0032  0.0038  126 ARG B CG  
1989 C CD  . ARG B 109 ? 0.2782 0.2860 0.2648 0.0729  0.0028  0.0031  126 ARG B CD  
1990 N NE  . ARG B 109 ? 0.2194 0.2149 0.1949 0.0767  0.0027  0.0015  126 ARG B NE  
1991 C CZ  . ARG B 109 ? 0.3023 0.2874 0.2674 0.0767  0.0023  0.0008  126 ARG B CZ  
1992 N NH1 . ARG B 109 ? 0.3234 0.3081 0.2878 0.0725  0.0016  0.0018  126 ARG B NH1 
1993 N NH2 . ARG B 109 ? 0.2870 0.2618 0.2418 0.0811  0.0027  -0.0009 126 ARG B NH2 
1994 N N   . ALA B 110 ? 0.1470 0.2011 0.1848 0.0591  0.0038  0.0096  127 ALA B N   
1995 C CA  . ALA B 110 ? 0.1271 0.1943 0.1760 0.0571  0.0048  0.0107  127 ALA B CA  
1996 C C   . ALA B 110 ? 0.1589 0.2337 0.2175 0.0572  0.0056  0.0107  127 ALA B C   
1997 O O   . ALA B 110 ? 0.1594 0.2457 0.2254 0.0584  0.0071  0.0104  127 ALA B O   
1998 C CB  . ALA B 110 ? 0.1634 0.2313 0.2172 0.0504  0.0038  0.0133  127 ALA B CB  
1999 N N   . ASP B 111 ? 0.1230 0.1917 0.1822 0.0555  0.0047  0.0110  128 ASP B N   
2000 C CA  . ASP B 111 ? 0.1258 0.2011 0.1947 0.0546  0.0053  0.0113  128 ASP B CA  
2001 C C   . ASP B 111 ? 0.1164 0.1944 0.1831 0.0609  0.0065  0.0089  128 ASP B C   
2002 O O   . ASP B 111 ? 0.1345 0.2209 0.2093 0.0605  0.0074  0.0085  128 ASP B O   
2003 C CB  . ASP B 111 ? 0.1237 0.1913 0.1941 0.0501  0.0039  0.0125  128 ASP B CB  
2004 C CG  . ASP B 111 ? 0.2298 0.2979 0.3063 0.0431  0.0029  0.0151  128 ASP B CG  
2005 O OD1 . ASP B 111 ? 0.2437 0.3192 0.3246 0.0415  0.0034  0.0162  128 ASP B OD1 
2006 O OD2 . ASP B 111 ? 0.2167 0.2775 0.2933 0.0392  0.0015  0.0162  128 ASP B OD2 
2007 N N   . PHE B 112 ? 0.1153 0.1855 0.1706 0.0660  0.0063  0.0072  129 PHE B N   
2008 C CA  . PHE B 112 ? 0.1377 0.2085 0.1896 0.0723  0.0071  0.0050  129 PHE B CA  
2009 C C   . PHE B 112 ? 0.1514 0.2254 0.1974 0.0781  0.0083  0.0030  129 PHE B C   
2010 O O   . PHE B 112 ? 0.1343 0.2090 0.1786 0.0791  0.0088  0.0013  129 PHE B O   
2011 C CB  . PHE B 112 ? 0.1392 0.1965 0.1817 0.0738  0.0060  0.0044  129 PHE B CB  
2012 C CG  . PHE B 112 ? 0.1383 0.1919 0.1856 0.0694  0.0051  0.0057  129 PHE B CG  
2013 C CD1 . PHE B 112 ? 0.1627 0.2091 0.2099 0.0634  0.0037  0.0074  129 PHE B CD1 
2014 C CD2 . PHE B 112 ? 0.1668 0.2238 0.2179 0.0714  0.0056  0.0049  129 PHE B CD2 
2015 C CE1 . PHE B 112 ? 0.2042 0.2470 0.2556 0.0595  0.0029  0.0084  129 PHE B CE1 
2016 C CE2 . PHE B 112 ? 0.1370 0.1903 0.1921 0.0675  0.0048  0.0059  129 PHE B CE2 
2017 C CZ  . PHE B 112 ? 0.1973 0.2434 0.2525 0.0616  0.0035  0.0076  129 PHE B CZ  
2018 N N   . CYS B 113 ? 0.1445 0.2176 0.1860 0.0785  0.0083  0.0031  130 CYS B N   
2019 C CA  . CYS B 113 ? 0.1415 0.2140 0.1745 0.0849  0.0092  0.0010  130 CYS B CA  
2020 C C   . CYS B 113 ? 0.1586 0.2405 0.1949 0.0848  0.0103  0.0010  130 CYS B C   
2021 O O   . CYS B 113 ? 0.1454 0.2328 0.1893 0.0796  0.0103  0.0028  130 CYS B O   
2022 C CB  . CYS B 113 ? 0.1528 0.2108 0.1729 0.0861  0.0082  0.0006  130 CYS B CB  
2023 S SG  . CYS B 113 ? 0.1974 0.2436 0.2124 0.0869  0.0071  0.0003  130 CYS B SG  
2024 N N   . GLN B 114 ? 0.1508 0.2326 0.1802 0.0889  0.0112  -0.0011 131 GLN B N   
2025 C CA  . GLN B 114 ? 0.1545 0.2437 0.1852 0.0887  0.0122  -0.0015 131 GLN B CA  
2026 C C   . GLN B 114 ? 0.1852 0.2703 0.2061 0.0942  0.0127  -0.0026 131 GLN B C   
2027 O O   . GLN B 114 ? 0.1836 0.2723 0.2053 0.0926  0.0131  -0.0020 131 GLN B O   
2028 C CB  . GLN B 114 ? 0.1615 0.2560 0.1943 0.0878  0.0130  -0.0030 131 GLN B CB  
2029 C CG  . GLN B 114 ? 0.1370 0.2362 0.1799 0.0818  0.0129  -0.0021 131 GLN B CG  
2030 C CD  . GLN B 114 ? 0.1546 0.2588 0.1996 0.0808  0.0136  -0.0035 131 GLN B CD  
2031 O OE1 . GLN B 114 ? 0.1711 0.2794 0.2146 0.0819  0.0144  -0.0043 131 GLN B OE1 
2032 N NE2 . GLN B 114 ? 0.1418 0.2452 0.1897 0.0789  0.0133  -0.0038 131 GLN B NE2 
2033 N N   . GLN B 115 ? 0.1779 0.2537 0.1887 0.0992  0.0124  -0.0041 132 GLN B N   
2034 C CA  . GLN B 115 ? 0.2012 0.2709 0.2013 0.1029  0.0128  -0.0055 132 GLN B CA  
2035 C C   . GLN B 115 ? 0.2140 0.2682 0.2033 0.1031  0.0115  -0.0056 132 GLN B C   
2036 O O   . GLN B 115 ? 0.2329 0.2814 0.2215 0.1033  0.0108  -0.0054 132 GLN B O   
2037 C CB  . GLN B 115 ? 0.2395 0.3125 0.2361 0.1069  0.0137  -0.0076 132 GLN B CB  
2038 C CG  . GLN B 115 ? 0.2788 0.3636 0.2841 0.1034  0.0144  -0.0075 132 GLN B CG  
2039 C CD  . GLN B 115 ? 0.2632 0.3500 0.2638 0.1064  0.0150  -0.0093 132 GLN B CD  
2040 O OE1 . GLN B 115 ? 0.2736 0.3590 0.2727 0.1075  0.0147  -0.0101 132 GLN B OE1 
2041 N NE2 . GLN B 115 ? 0.3163 0.4064 0.3148 0.1079  0.0160  -0.0100 132 GLN B NE2 
2042 N N   . ALA B 116 ? 0.2234 0.2706 0.2039 0.1033  0.0114  -0.0061 133 ALA B N   
2043 C CA  . ALA B 116 ? 0.2332 0.2654 0.2032 0.1029  0.0104  -0.0062 133 ALA B CA  
2044 C C   . ALA B 116 ? 0.2662 0.2915 0.2290 0.1090  0.0107  -0.0079 133 ALA B C   
2045 O O   . ALA B 116 ? 0.2717 0.2861 0.2296 0.1079  0.0097  -0.0076 133 ALA B O   
2046 C CB  . ALA B 116 ? 0.2761 0.3035 0.2381 0.1025  0.0105  -0.0067 133 ALA B CB  
2047 N N   . GLY B 117 ? 0.2660 0.2973 0.2281 0.1155  0.0121  -0.0097 134 GLY B N   
2048 C CA  . GLY B 117 ? 0.2712 0.2961 0.2262 0.1215  0.0124  -0.0113 134 GLY B CA  
2049 C C   . GLY B 117 ? 0.2713 0.2961 0.2312 0.1191  0.0115  -0.0103 134 GLY B C   
2050 O O   . GLY B 117 ? 0.3050 0.3219 0.2584 0.1210  0.0111  -0.0109 134 GLY B O   
2051 N N   . ARG B 118 ? 0.2189 0.2524 0.1902 0.1147  0.0111  -0.0089 135 ARG B N   
2052 C CA  . ARG B 118 ? 0.2183 0.2514 0.1948 0.1118  0.0103  -0.0079 135 ARG B CA  
2053 C C   . ARG B 118 ? 0.2050 0.2388 0.1886 0.1069  0.0095  -0.0059 135 ARG B C   
2054 O O   . ARG B 118 ? 0.2169 0.2612 0.2117 0.1035  0.0096  -0.0048 135 ARG B O   
2055 C CB  . ARG B 118 ? 0.2018 0.2458 0.1858 0.1099  0.0106  -0.0081 135 ARG B CB  
2056 C CG  . ARG B 118 ? 0.2205 0.2631 0.1975 0.1138  0.0108  -0.0096 135 ARG B CG  
2057 C CD  . ARG B 118 ? 0.2581 0.2893 0.2271 0.1161  0.0102  -0.0099 135 ARG B CD  
2058 N NE  . ARG B 118 ? 0.2854 0.3171 0.2504 0.1189  0.0102  -0.0108 135 ARG B NE  
2059 C CZ  . ARG B 118 ? 0.2917 0.3142 0.2487 0.1215  0.0098  -0.0112 135 ARG B CZ  
2060 N NH1 . ARG B 118 ? 0.3201 0.3314 0.2717 0.1216  0.0094  -0.0107 135 ARG B NH1 
2061 N NH2 . ARG B 118 ? 0.3033 0.3278 0.2574 0.1241  0.0098  -0.0119 135 ARG B NH2 
2062 N N   . ASN B 119 ? 0.2079 0.2293 0.1848 0.1036  0.0084  -0.0052 136 ASN B N   
2063 C CA  . ASN B 119 ? 0.1796 0.2000 0.1620 0.0959  0.0071  -0.0030 136 ASN B CA  
2064 C C   . ASN B 119 ? 0.2018 0.2125 0.1828 0.0930  0.0059  -0.0022 136 ASN B C   
2065 O O   . ASN B 119 ? 0.1906 0.1958 0.1719 0.0872  0.0047  -0.0007 136 ASN B O   
2066 C CB  . ASN B 119 ? 0.1827 0.1990 0.1600 0.0932  0.0068  -0.0026 136 ASN B CB  
2067 C CG  . ASN B 119 ? 0.2411 0.2431 0.2050 0.0953  0.0065  -0.0038 136 ASN B CG  
2068 O OD1 . ASN B 119 ? 0.2315 0.2257 0.1893 0.0988  0.0065  -0.0048 136 ASN B OD1 
2069 N ND2 . ASN B 119 ? 0.2769 0.2750 0.2358 0.0931  0.0062  -0.0036 136 ASN B ND2 
2070 N N   . LEU B 120 ? 0.1937 0.2029 0.1734 0.0971  0.0062  -0.0031 137 LEU B N   
2071 C CA  . LEU B 120 ? 0.1730 0.1779 0.1552 0.0950  0.0055  -0.0023 137 LEU B CA  
2072 C C   . LEU B 120 ? 0.1968 0.1862 0.1700 0.0931  0.0044  -0.0022 137 LEU B C   
2073 O O   . LEU B 120 ? 0.2115 0.1951 0.1824 0.0946  0.0043  -0.0025 137 LEU B O   
2074 C CB  . LEU B 120 ? 0.1677 0.1808 0.1627 0.0883  0.0049  -0.0003 137 LEU B CB  
2075 C CG  . LEU B 120 ? 0.1658 0.1835 0.1685 0.0878  0.0049  0.0000  137 LEU B CG  
2076 C CD1 . LEU B 120 ? 0.2027 0.2322 0.2099 0.0932  0.0063  -0.0013 137 LEU B CD1 
2077 C CD2 . LEU B 120 ? 0.1779 0.2003 0.1917 0.0802  0.0041  0.0022  137 LEU B CD2 
2078 N N   . ILE B 121 ? 0.2404 0.2227 0.2077 0.0904  0.0039  -0.0019 138 ILE B N   
2079 C CA  . ILE B 121 ? 0.1891 0.1581 0.1502 0.0868  0.0028  -0.0014 138 ILE B CA  
2080 C C   . ILE B 121 ? 0.2442 0.2054 0.1957 0.0867  0.0027  -0.0021 138 ILE B C   
2081 O O   . ILE B 121 ? 0.2469 0.2144 0.1998 0.0865  0.0030  -0.0020 138 ILE B O   
2082 C CB  . ILE B 121 ? 0.1989 0.1701 0.1695 0.0792  0.0016  0.0007  138 ILE B CB  
2083 C CG1 . ILE B 121 ? 0.2400 0.1973 0.2042 0.0756  0.0005  0.0010  138 ILE B CG1 
2084 C CG2 . ILE B 121 ? 0.2294 0.2095 0.2073 0.0749  0.0013  0.0020  138 ILE B CG2 
2085 C CD1 . ILE B 121 ? 0.2401 0.1992 0.2136 0.0690  -0.0006 0.0028  138 ILE B CD1 
2086 N N   . HIS B 122 ? 0.2560 0.2032 0.1975 0.0868  0.0023  -0.0027 139 HIS B N   
2087 C CA  . HIS B 122 ? 0.2789 0.2165 0.2108 0.0855  0.0021  -0.0033 139 HIS B CA  
2088 C C   . HIS B 122 ? 0.2418 0.1708 0.1733 0.0788  0.0007  -0.0021 139 HIS B C   
2089 O O   . HIS B 122 ? 0.2621 0.1867 0.1949 0.0777  0.0003  -0.0018 139 HIS B O   
2090 C CB  . HIS B 122 ? 0.2886 0.2156 0.2076 0.0919  0.0032  -0.0054 139 HIS B CB  
2091 C CG  . HIS B 122 ? 0.3043 0.2182 0.2128 0.0898  0.0029  -0.0060 139 HIS B CG  
2092 N ND1 . HIS B 122 ? 0.4066 0.3196 0.3096 0.0903  0.0033  -0.0068 139 HIS B ND1 
2093 C CD2 . HIS B 122 ? 0.3244 0.2258 0.2271 0.0868  0.0022  -0.0060 139 HIS B CD2 
2094 C CE1 . HIS B 122 ? 0.3524 0.2530 0.2467 0.0877  0.0029  -0.0072 139 HIS B CE1 
2095 N NE2 . HIS B 122 ? 0.3377 0.2311 0.2317 0.0855  0.0022  -0.0068 139 HIS B NE2 
2096 N N   . GLY B 123 ? 0.2581 0.1843 0.1872 0.0746  0.0000  -0.0017 140 GLY B N   
2097 C CA  . GLY B 123 ? 0.2649 0.1815 0.1915 0.0687  -0.0013 -0.0010 140 GLY B CA  
2098 C C   . GLY B 123 ? 0.2787 0.1865 0.1947 0.0682  -0.0013 -0.0020 140 GLY B C   
2099 O O   . GLY B 123 ? 0.2950 0.2073 0.2095 0.0698  -0.0008 -0.0025 140 GLY B O   
2100 N N   . SER B 124 ? 0.2819 0.1766 0.1904 0.0660  -0.0018 -0.0026 141 SER B N   
2101 C CA  . SER B 124 ? 0.2978 0.1831 0.1959 0.0649  -0.0018 -0.0037 141 SER B CA  
2102 C C   . SER B 124 ? 0.2943 0.1862 0.1969 0.0600  -0.0028 -0.0025 141 SER B C   
2103 O O   . SER B 124 ? 0.2955 0.1943 0.2080 0.0548  -0.0041 -0.0005 141 SER B O   
2104 C CB  . SER B 124 ? 0.3206 0.1923 0.2125 0.0614  -0.0024 -0.0041 141 SER B CB  
2105 O OG  . SER B 124 ? 0.3380 0.2030 0.2258 0.0654  -0.0015 -0.0050 141 SER B OG  
2106 N N   . ASP B 125 ? 0.3187 0.2083 0.2137 0.0617  -0.0022 -0.0037 142 ASP B N   
2107 C CA  . ASP B 125 ? 0.3133 0.2091 0.2118 0.0574  -0.0032 -0.0025 142 ASP B CA  
2108 C C   . ASP B 125 ? 0.3356 0.2224 0.2288 0.0516  -0.0044 -0.0025 142 ASP B C   
2109 O O   . ASP B 125 ? 0.3777 0.2695 0.2740 0.0475  -0.0054 -0.0014 142 ASP B O   
2110 C CB  . ASP B 125 ? 0.3669 0.2676 0.2617 0.0620  -0.0019 -0.0037 142 ASP B CB  
2111 C CG  . ASP B 125 ? 0.4282 0.3175 0.3093 0.0655  -0.0008 -0.0061 142 ASP B CG  
2112 O OD1 . ASP B 125 ? 0.4308 0.3079 0.3044 0.0642  -0.0009 -0.0069 142 ASP B OD1 
2113 O OD2 . ASP B 125 ? 0.5113 0.4040 0.3889 0.0698  0.0005  -0.0072 142 ASP B OD2 
2114 N N   . SER B 126 ? 0.3435 0.2175 0.2288 0.0512  -0.0043 -0.0037 143 SER B N   
2115 C CA  . SER B 126 ? 0.3883 0.2532 0.2677 0.0460  -0.0053 -0.0040 143 SER B CA  
2116 C C   . SER B 126 ? 0.4114 0.2642 0.2857 0.0453  -0.0053 -0.0048 143 SER B C   
2117 O O   . SER B 126 ? 0.3589 0.2090 0.2318 0.0497  -0.0042 -0.0055 143 SER B O   
2118 C CB  . SER B 126 ? 0.3771 0.2370 0.2459 0.0479  -0.0045 -0.0058 143 SER B CB  
2119 O OG  . SER B 126 ? 0.4069 0.2572 0.2653 0.0537  -0.0027 -0.0081 143 SER B OG  
2120 N N   . ALA B 127 ? 0.5035 0.2047 0.2946 0.0450  0.0126  -0.0409 144 ALA B N   
2121 C CA  . ALA B 127 ? 0.5400 0.2370 0.3267 0.0448  0.0135  -0.0400 144 ALA B CA  
2122 C C   . ALA B 127 ? 0.4989 0.1924 0.2846 0.0463  0.0138  -0.0404 144 ALA B C   
2123 O O   . ALA B 127 ? 0.4940 0.1838 0.2762 0.0473  0.0136  -0.0395 144 ALA B O   
2124 C CB  . ALA B 127 ? 0.5957 0.2927 0.3815 0.0426  0.0153  -0.0399 144 ALA B CB  
2125 N N   . GLU B 128 ? 0.5186 0.2132 0.3074 0.0464  0.0143  -0.0417 145 GLU B N   
2126 C CA  . GLU B 128 ? 0.4950 0.1864 0.2830 0.0477  0.0146  -0.0422 145 GLU B CA  
2127 C C   . GLU B 128 ? 0.4812 0.1713 0.2688 0.0501  0.0130  -0.0419 145 GLU B C   
2128 O O   . GLU B 128 ? 0.5028 0.1891 0.2876 0.0512  0.0130  -0.0414 145 GLU B O   
2129 C CB  . GLU B 128 ? 0.5084 0.2016 0.3001 0.0474  0.0154  -0.0438 145 GLU B CB  
2130 C CG  . GLU B 128 ? 0.7758 0.4658 0.5671 0.0488  0.0157  -0.0445 145 GLU B CG  
2131 C CD  . GLU B 128 ? 1.1415 0.8328 0.9358 0.0482  0.0168  -0.0460 145 GLU B CD  
2132 O OE1 . GLU B 128 ? 1.1902 0.8847 0.9867 0.0466  0.0174  -0.0466 145 GLU B OE1 
2133 O OE2 . GLU B 128 ? 1.0466 0.7358 0.8411 0.0494  0.0170  -0.0467 145 GLU B OE2 
2134 N N   . SER B 129 ? 0.4963 0.1897 0.2866 0.0508  0.0115  -0.0421 146 SER B N   
2135 C CA  A SER B 129 ? 0.4891 0.1815 0.2790 0.0530  0.0099  -0.0417 146 SER B CA  
2136 C CA  B SER B 129 ? 0.4892 0.1817 0.2792 0.0529  0.0099  -0.0417 146 SER B CA  
2137 C C   . SER B 129 ? 0.4911 0.1812 0.2770 0.0535  0.0092  -0.0402 146 SER B C   
2138 O O   . SER B 129 ? 0.4997 0.1872 0.2839 0.0552  0.0083  -0.0398 146 SER B O   
2139 C CB  A SER B 129 ? 0.4805 0.1770 0.2745 0.0536  0.0086  -0.0423 146 SER B CB  
2140 C CB  B SER B 129 ? 0.4735 0.1703 0.2674 0.0534  0.0086  -0.0423 146 SER B CB  
2141 O OG  A SER B 129 ? 0.5108 0.2106 0.3059 0.0522  0.0083  -0.0421 146 SER B OG  
2142 O OG  B SER B 129 ? 0.4381 0.1370 0.2357 0.0531  0.0092  -0.0437 146 SER B OG  
2143 N N   . ALA B 130 ? 0.4541 0.1451 0.2386 0.0520  0.0094  -0.0395 147 ALA B N   
2144 C CA  . ALA B 130 ? 0.4744 0.1632 0.2550 0.0524  0.0088  -0.0381 147 ALA B CA  
2145 C C   . ALA B 130 ? 0.4985 0.1825 0.2753 0.0528  0.0097  -0.0376 147 ALA B C   
2146 O O   . ALA B 130 ? 0.5112 0.1925 0.2853 0.0543  0.0089  -0.0368 147 ALA B O   
2147 C CB  . ALA B 130 ? 0.4779 0.1685 0.2577 0.0506  0.0091  -0.0374 147 ALA B CB  
2148 N N   . LYS B 131 ? 0.4805 0.1634 0.2571 0.0515  0.0115  -0.0381 148 LYS B N   
2149 C CA  . LYS B 131 ? 0.5463 0.2247 0.3195 0.0518  0.0124  -0.0377 148 LYS B CA  
2150 C C   . LYS B 131 ? 0.5226 0.1988 0.2960 0.0539  0.0117  -0.0381 148 LYS B C   
2151 O O   . LYS B 131 ? 0.5735 0.2461 0.3437 0.0551  0.0114  -0.0373 148 LYS B O   
2152 C CB  . LYS B 131 ? 0.6026 0.2806 0.3760 0.0500  0.0143  -0.0383 148 LYS B CB  
2153 C CG  . LYS B 131 ? 0.7809 0.4545 0.5515 0.0502  0.0155  -0.0382 148 LYS B CG  
2154 C CD  . LYS B 131 ? 1.0232 0.6972 0.7946 0.0482  0.0173  -0.0388 148 LYS B CD  
2155 C CE  . LYS B 131 ? 1.1796 0.8492 0.9483 0.0481  0.0186  -0.0388 148 LYS B CE  
2156 N NZ  . LYS B 131 ? 1.2880 0.9561 1.0581 0.0498  0.0184  -0.0397 148 LYS B NZ  
2157 N N   . ARG B 132 ? 0.4983 0.1767 0.2756 0.0545  0.0115  -0.0393 149 ARG B N   
2158 C CA  . ARG B 132 ? 0.5397 0.2164 0.3177 0.0565  0.0109  -0.0398 149 ARG B CA  
2159 C C   . ARG B 132 ? 0.5318 0.2079 0.3086 0.0583  0.0090  -0.0390 149 ARG B C   
2160 O O   . ARG B 132 ? 0.5163 0.1891 0.2911 0.0598  0.0086  -0.0387 149 ARG B O   
2161 C CB  . ARG B 132 ? 0.5256 0.2053 0.3082 0.0565  0.0109  -0.0413 149 ARG B CB  
2162 C CG  . ARG B 132 ? 0.5869 0.2649 0.3705 0.0584  0.0105  -0.0420 149 ARG B CG  
2163 C CD  . ARG B 132 ? 0.5951 0.2763 0.3833 0.0584  0.0106  -0.0435 149 ARG B CD  
2164 N NE  . ARG B 132 ? 0.7878 0.4723 0.5785 0.0592  0.0091  -0.0435 149 ARG B NE  
2165 C CZ  . ARG B 132 ? 0.8411 0.5252 0.6324 0.0612  0.0077  -0.0434 149 ARG B CZ  
2166 N NH1 . ARG B 132 ? 0.7950 0.4756 0.5847 0.0627  0.0077  -0.0434 149 ARG B NH1 
2167 N NH2 . ARG B 132 ? 0.7465 0.4338 0.5400 0.0618  0.0063  -0.0434 149 ARG B NH2 
2168 N N   . GLU B 133 ? 0.5062 0.1856 0.2845 0.0582  0.0079  -0.0387 150 GLU B N   
2169 C CA  . GLU B 133 ? 0.4656 0.1449 0.2432 0.0600  0.0060  -0.0381 150 GLU B CA  
2170 C C   . GLU B 133 ? 0.5206 0.1967 0.2934 0.0603  0.0058  -0.0367 150 GLU B C   
2171 O O   . GLU B 133 ? 0.5094 0.1833 0.2805 0.0620  0.0047  -0.0362 150 GLU B O   
2172 C CB  . GLU B 133 ? 0.4591 0.1428 0.2395 0.0597  0.0048  -0.0382 150 GLU B CB  
2173 C CG  . GLU B 133 ? 0.4898 0.1766 0.2749 0.0599  0.0047  -0.0395 150 GLU B CG  
2174 C CD  . GLU B 133 ? 0.5346 0.2261 0.3229 0.0591  0.0039  -0.0398 150 GLU B CD  
2175 O OE1 . GLU B 133 ? 0.4813 0.1739 0.2683 0.0586  0.0033  -0.0389 150 GLU B OE1 
2176 O OE2 . GLU B 133 ? 0.5163 0.2106 0.3085 0.0591  0.0039  -0.0409 150 GLU B OE2 
2177 N N   . ILE B 134 ? 0.5052 0.1810 0.2760 0.0586  0.0067  -0.0361 151 ILE B N   
2178 C CA  . ILE B 134 ? 0.5122 0.1848 0.2784 0.0588  0.0066  -0.0348 151 ILE B CA  
2179 C C   . ILE B 134 ? 0.5614 0.2295 0.3250 0.0598  0.0072  -0.0347 151 ILE B C   
2180 O O   . ILE B 134 ? 0.5600 0.2255 0.3208 0.0612  0.0064  -0.0339 151 ILE B O   
2181 C CB  . ILE B 134 ? 0.5206 0.1938 0.2851 0.0568  0.0076  -0.0342 151 ILE B CB  
2182 C CG1 . ILE B 134 ? 0.5352 0.2126 0.3017 0.0560  0.0067  -0.0341 151 ILE B CG1 
2183 C CG2 . ILE B 134 ? 0.5561 0.2255 0.3156 0.0570  0.0078  -0.0330 151 ILE B CG2 
2184 C CD1 . ILE B 134 ? 0.5392 0.2179 0.3051 0.0538  0.0079  -0.0338 151 ILE B CD1 
2185 N N   . SER B 135 ? 0.5410 0.2083 0.3059 0.0592  0.0086  -0.0356 152 SER B N   
2186 C CA  . SER B 135 ? 0.5705 0.2336 0.3333 0.0601  0.0093  -0.0355 152 SER B CA  
2187 C C   . SER B 135 ? 0.6150 0.2771 0.3786 0.0624  0.0080  -0.0358 152 SER B C   
2188 O O   . SER B 135 ? 0.6681 0.3265 0.4291 0.0636  0.0078  -0.0353 152 SER B O   
2189 C CB  . SER B 135 ? 0.6635 0.3261 0.4277 0.0589  0.0110  -0.0365 152 SER B CB  
2190 O OG  . SER B 135 ? 0.8389 0.5019 0.6020 0.0568  0.0123  -0.0362 152 SER B OG  
2191 N N   . LEU B 136 ? 0.5195 0.1850 0.2870 0.0630  0.0070  -0.0366 153 LEU B N   
2192 C CA  . LEU B 136 ? 0.5266 0.1915 0.2952 0.0651  0.0058  -0.0369 153 LEU B CA  
2193 C C   . LEU B 136 ? 0.5858 0.2497 0.3520 0.0665  0.0042  -0.0357 153 LEU B C   
2194 O O   . LEU B 136 ? 0.5475 0.2086 0.3121 0.0682  0.0036  -0.0354 153 LEU B O   
2195 C CB  . LEU B 136 ? 0.5444 0.2134 0.3178 0.0653  0.0052  -0.0380 153 LEU B CB  
2196 C CG  . LEU B 136 ? 0.5775 0.2466 0.3525 0.0675  0.0038  -0.0383 153 LEU B CG  
2197 C CD1 . LEU B 136 ? 0.6720 0.3376 0.4464 0.0686  0.0044  -0.0387 153 LEU B CD1 
2198 C CD2 . LEU B 136 ? 0.5577 0.2311 0.3374 0.0674  0.0033  -0.0393 153 LEU B CD2 
2199 N N   . TRP B 137 ? 0.5256 0.1918 0.2914 0.0659  0.0034  -0.0351 154 TRP B N   
2200 C CA  . TRP B 137 ? 0.5421 0.2080 0.3062 0.0673  0.0017  -0.0342 154 TRP B CA  
2201 C C   . TRP B 137 ? 0.5582 0.2210 0.3175 0.0671  0.0018  -0.0330 154 TRP B C   
2202 O O   . TRP B 137 ? 0.6020 0.2637 0.3594 0.0685  0.0005  -0.0323 154 TRP B O   
2203 C CB  . TRP B 137 ? 0.5209 0.1911 0.2875 0.0670  0.0005  -0.0343 154 TRP B CB  
2204 C CG  . TRP B 137 ? 0.4967 0.1702 0.2680 0.0675  -0.0001 -0.0354 154 TRP B CG  
2205 C CD1 . TRP B 137 ? 0.4860 0.1623 0.2607 0.0663  0.0008  -0.0364 154 TRP B CD1 
2206 C CD2 . TRP B 137 ? 0.4907 0.1648 0.2634 0.0695  -0.0017 -0.0355 154 TRP B CD2 
2207 N NE1 . TRP B 137 ? 0.5017 0.1805 0.2801 0.0673  -0.0002 -0.0372 154 TRP B NE1 
2208 C CE2 . TRP B 137 ? 0.5279 0.2054 0.3052 0.0693  -0.0017 -0.0367 154 TRP B CE2 
2209 C CE3 . TRP B 137 ? 0.5346 0.2068 0.3054 0.0714  -0.0032 -0.0348 154 TRP B CE3 
2210 C CZ2 . TRP B 137 ? 0.5482 0.2272 0.3281 0.0709  -0.0031 -0.0371 154 TRP B CZ2 
2211 C CZ3 . TRP B 137 ? 0.5210 0.1947 0.2943 0.0729  -0.0046 -0.0352 154 TRP B CZ3 
2212 C CH2 . TRP B 137 ? 0.5734 0.2504 0.3512 0.0727  -0.0045 -0.0363 154 TRP B CH2 
2213 N N   . PHE B 138 ? 0.4861 0.2781 0.3107 -0.0058 0.0005  0.0526  155 PHE B N   
2214 C CA  . PHE B 138 ? 0.5299 0.3175 0.3477 -0.0118 0.0020  0.0517  155 PHE B CA  
2215 C C   . PHE B 138 ? 0.6196 0.3919 0.4213 -0.0176 0.0036  0.0493  155 PHE B C   
2216 O O   . PHE B 138 ? 0.6294 0.3972 0.4261 -0.0182 0.0043  0.0484  155 PHE B O   
2217 C CB  . PHE B 138 ? 0.5172 0.3085 0.3346 -0.0144 0.0033  0.0513  155 PHE B CB  
2218 C CG  . PHE B 138 ? 0.4574 0.2620 0.2882 -0.0106 0.0021  0.0532  155 PHE B CG  
2219 C CD1 . PHE B 138 ? 0.4881 0.2936 0.3198 -0.0121 0.0022  0.0535  155 PHE B CD1 
2220 C CD2 . PHE B 138 ? 0.4084 0.2246 0.2506 -0.0057 0.0009  0.0547  155 PHE B CD2 
2221 C CE1 . PHE B 138 ? 0.4546 0.2710 0.2972 -0.0087 0.0011  0.0551  155 PHE B CE1 
2222 C CE2 . PHE B 138 ? 0.4000 0.2283 0.2543 -0.0024 -0.0002 0.0564  155 PHE B CE2 
2223 C CZ  . PHE B 138 ? 0.4006 0.2278 0.2538 -0.0039 -0.0001 0.0564  155 PHE B CZ  
2224 N N   . LYS B 139 ? 0.6600 0.4241 0.4527 -0.0227 0.0043  0.0482  156 LYS B N   
2225 C CA  . LYS B 139 ? 0.5753 0.3257 0.3519 -0.0301 0.0065  0.0454  156 LYS B CA  
2226 C C   . LYS B 139 ? 0.7332 0.4831 0.5044 -0.0363 0.0091  0.0436  156 LYS B C   
2227 O O   . LYS B 139 ? 0.6120 0.3698 0.3898 -0.0358 0.0092  0.0444  156 LYS B O   
2228 C CB  . LYS B 139 ? 0.7793 0.5213 0.5483 -0.0334 0.0061  0.0447  156 LYS B CB  
2229 C CG  . LYS B 139 ? 0.7514 0.4978 0.5293 -0.0274 0.0033  0.0470  156 LYS B CG  
2230 C CD  . LYS B 139 ? 0.9057 0.6418 0.6731 -0.0315 0.0028  0.0461  156 LYS B CD  
2231 C CE  . LYS B 139 ? 0.9852 0.7183 0.7534 -0.0266 -0.0003 0.0474  156 LYS B CE  
2232 N NZ  . LYS B 139 ? 1.1566 0.8867 0.9252 -0.0225 -0.0016 0.0479  156 LYS B NZ  
2233 N N   . PRO B 140 ? 0.7125 0.4534 0.4719 -0.0427 0.0116  0.0409  157 PRO B N   
2234 C CA  . PRO B 140 ? 0.8276 0.5693 0.5830 -0.0492 0.0145  0.0389  157 PRO B CA  
2235 C C   . PRO B 140 ? 0.7709 0.5125 0.5236 -0.0546 0.0160  0.0377  157 PRO B C   
2236 O O   . PRO B 140 ? 0.7666 0.5133 0.5212 -0.0581 0.0180  0.0368  157 PRO B O   
2237 C CB  . PRO B 140 ? 0.7777 0.5089 0.5203 -0.0557 0.0169  0.0360  157 PRO B CB  
2238 C CG  . PRO B 140 ? 0.8556 0.5794 0.5942 -0.0529 0.0152  0.0364  157 PRO B CG  
2239 C CD  . PRO B 140 ? 0.8342 0.5663 0.5857 -0.0435 0.0118  0.0399  157 PRO B CD  
2240 N N   . GLU B 141 ? 0.8308 0.5667 0.5789 -0.0559 0.0154  0.0373  158 GLU B N   
2241 C CA  . GLU B 141 ? 0.9252 0.6614 0.6710 -0.0610 0.0169  0.0361  158 GLU B CA  
2242 C C   . GLU B 141 ? 0.8897 0.6381 0.6490 -0.0554 0.0153  0.0388  158 GLU B C   
2243 O O   . GLU B 141 ? 0.7785 0.5293 0.5376 -0.0596 0.0170  0.0377  158 GLU B O   
2244 C CB  . GLU B 141 ? 1.0722 0.7993 0.8098 -0.0633 0.0162  0.0354  158 GLU B CB  
2245 C CG  . GLU B 141 ? 0.9948 0.7266 0.7411 -0.0564 0.0127  0.0385  158 GLU B CG  
2246 C CD  . GLU B 141 ? 1.0445 0.7706 0.7891 -0.0525 0.0102  0.0397  158 GLU B CD  
2247 O OE1 . GLU B 141 ? 1.1616 0.8835 0.9026 -0.0521 0.0103  0.0392  158 GLU B OE1 
2248 O OE2 . GLU B 141 ? 1.0332 0.7591 0.7800 -0.0501 0.0080  0.0411  158 GLU B OE2 
2249 N N   . GLU B 142 ? 0.7572 0.5134 0.5283 -0.0462 0.0122  0.0421  159 GLU B N   
2250 C CA  . GLU B 142 ? 0.6151 0.3838 0.3999 -0.0404 0.0105  0.0447  159 GLU B CA  
2251 C C   . GLU B 142 ? 0.5267 0.3032 0.3167 -0.0407 0.0116  0.0448  159 GLU B C   
2252 O O   . GLU B 142 ? 0.5229 0.3092 0.3228 -0.0375 0.0108  0.0466  159 GLU B O   
2253 C CB  . GLU B 142 ? 0.5793 0.3546 0.3755 -0.0313 0.0072  0.0477  159 GLU B CB  
2254 C CG  . GLU B 142 ? 0.7182 0.4870 0.5107 -0.0310 0.0058  0.0478  159 GLU B CG  
2255 C CD  . GLU B 142 ? 0.7920 0.5647 0.5929 -0.0235 0.0030  0.0499  159 GLU B CD  
2256 O OE1 . GLU B 142 ? 0.7399 0.5149 0.5441 -0.0204 0.0027  0.0503  159 GLU B OE1 
2257 O OE2 . GLU B 142 ? 0.8313 0.6011 0.6313 -0.0213 0.0011  0.0505  159 GLU B OE2 
2258 N N   . ILE B 143 ? 0.5668 0.3394 0.3505 -0.0446 0.0135  0.0431  160 ILE B N   
2259 C CA  . ILE B 143 ? 0.5649 0.3439 0.3520 -0.0462 0.0148  0.0429  160 ILE B CA  
2260 C C   . ILE B 143 ? 0.5848 0.3606 0.3642 -0.0565 0.0187  0.0396  160 ILE B C   
2261 O O   . ILE B 143 ? 0.6049 0.3713 0.3727 -0.0642 0.0215  0.0362  160 ILE B O   
2262 C CB  . ILE B 143 ? 0.4876 0.2645 0.2719 -0.0461 0.0150  0.0425  160 ILE B CB  
2263 C CG1 . ILE B 143 ? 0.6202 0.3974 0.4090 -0.0380 0.0120  0.0446  160 ILE B CG1 
2264 C CG2 . ILE B 143 ? 0.5390 0.3246 0.3294 -0.0456 0.0151  0.0433  160 ILE B CG2 
2265 C CD1 . ILE B 143 ? 0.6374 0.4260 0.4409 -0.0289 0.0088  0.0478  160 ILE B CD1 
2266 N N   . GLN B 144 ? 0.4561 0.2402 0.2424 -0.0569 0.0192  0.0402  161 GLN B N   
2267 C CA  . GLN B 144 ? 0.5086 0.2916 0.2898 -0.0665 0.0232  0.0367  161 GLN B CA  
2268 C C   . GLN B 144 ? 0.4703 0.2591 0.2534 -0.0722 0.0261  0.0349  161 GLN B C   
2269 O O   . GLN B 144 ? 0.4942 0.2914 0.2862 -0.0668 0.0240  0.0377  161 GLN B O   
2270 C CB  . GLN B 144 ? 0.5086 0.2970 0.2963 -0.0639 0.0222  0.0383  161 GLN B CB  
2271 C CG  . GLN B 144 ? 0.4945 0.2807 0.2844 -0.0567 0.0186  0.0409  161 GLN B CG  
2272 C CD  . GLN B 144 ? 0.5213 0.2951 0.2987 -0.0616 0.0196  0.0385  161 GLN B CD  
2273 O OE1 . GLN B 144 ? 0.5751 0.3425 0.3423 -0.0710 0.0233  0.0346  161 GLN B OE1 
2274 N NE2 . GLN B 144 ? 0.6157 0.3866 0.3941 -0.0555 0.0165  0.0406  161 GLN B NE2 
2275 N N   . SER B 145 ? 0.5111 0.2961 0.2864 -0.0834 0.0309  0.0298  162 SER B N   
2276 C CA  A SER B 145 ? 0.5126 0.3046 0.2909 -0.0909 0.0345  0.0267  162 SER B CA  
2277 C CA  B SER B 145 ? 0.5129 0.3048 0.2911 -0.0910 0.0345  0.0267  162 SER B CA  
2278 C C   . SER B 145 ? 0.5345 0.3336 0.3173 -0.0982 0.0382  0.0233  162 SER B C   
2279 O O   . SER B 145 ? 0.5033 0.2978 0.2798 -0.1048 0.0412  0.0194  162 SER B O   
2280 C CB  A SER B 145 ? 0.5560 0.3415 0.3252 -0.0991 0.0378  0.0222  162 SER B CB  
2281 C CB  B SER B 145 ? 0.5557 0.3409 0.3246 -0.0991 0.0378  0.0222  162 SER B CB  
2282 O OG  A SER B 145 ? 0.5447 0.3433 0.3235 -0.1045 0.0402  0.0170  162 SER B OG  
2283 O OG  B SER B 145 ? 0.5871 0.3645 0.3509 -0.0927 0.0346  0.0250  162 SER B OG  
2284 N N   . TYR B 146 ? 0.4488 0.2627 0.2460 -0.0952 0.0370  0.0235  163 TYR B N   
2285 C CA  . TYR B 146 ? 0.4152 0.2420 0.2230 -0.1002 0.0396  0.0186  163 TYR B CA  
2286 C C   . TYR B 146 ? 0.3852 0.2339 0.2143 -0.0942 0.0363  0.0161  163 TYR B C   
2287 O O   . TYR B 146 ? 0.3838 0.2356 0.2175 -0.0858 0.0318  0.0194  163 TYR B O   
2288 C CB  . TYR B 146 ? 0.4209 0.2408 0.2238 -0.0994 0.0399  0.0231  163 TYR B CB  
2289 C CG  . TYR B 146 ? 0.3940 0.2169 0.2035 -0.0870 0.0343  0.0304  163 TYR B CG  
2290 C CD1 . TYR B 146 ? 0.4224 0.2383 0.2287 -0.0769 0.0294  0.0349  163 TYR B CD1 
2291 C CD2 . TYR B 146 ? 0.3697 0.2100 0.1964 -0.0823 0.0323  0.0298  163 TYR B CD2 
2292 C CE1 . TYR B 146 ? 0.3904 0.2118 0.2058 -0.0654 0.0244  0.0403  163 TYR B CE1 
2293 C CE2 . TYR B 146 ? 0.3739 0.2166 0.2063 -0.0714 0.0274  0.0365  163 TYR B CE2 
2294 C CZ  . TYR B 146 ? 0.3532 0.1853 0.1788 -0.0634 0.0237  0.0420  163 TYR B CZ  
2295 O OH  . TYR B 146 ? 0.3692 0.2079 0.2047 -0.0519 0.0188  0.0470  163 TYR B OH  
2296 N N   . LYS B 147 ? 0.4160 0.2794 0.2579 -0.0989 0.0386  0.0099  164 LYS B N   
2297 C CA  . LYS B 147 ? 0.3640 0.2488 0.2269 -0.0946 0.0356  0.0064  164 LYS B CA  
2298 C C   . LYS B 147 ? 0.3174 0.2122 0.1918 -0.0898 0.0338  0.0084  164 LYS B C   
2299 O O   . LYS B 147 ? 0.3615 0.2525 0.2317 -0.0949 0.0373  0.0078  164 LYS B O   
2300 C CB  . LYS B 147 ? 0.4132 0.3087 0.2841 -0.1039 0.0393  -0.0034 164 LYS B CB  
2301 C CG  . LYS B 147 ? 0.5030 0.4212 0.3967 -0.1010 0.0366  -0.0081 164 LYS B CG  
2302 C CD  . LYS B 147 ? 0.6624 0.5904 0.5640 -0.1107 0.0405  -0.0182 164 LYS B CD  
2303 C CE  . LYS B 147 ? 0.7669 0.7172 0.6919 -0.1072 0.0369  -0.0227 164 LYS B CE  
2304 N NZ  . LYS B 147 ? 0.8930 0.8523 0.8259 -0.1148 0.0391  -0.0319 164 LYS B NZ  
2305 N N   . LEU B 148 ? 0.3540 0.2616 0.2426 -0.0803 0.0285  0.0109  165 LEU B N   
2306 C CA  . LEU B 148 ? 0.3220 0.2405 0.2228 -0.0756 0.0266  0.0125  165 LEU B CA  
2307 C C   . LEU B 148 ? 0.3209 0.2564 0.2374 -0.0819 0.0291  0.0040  165 LEU B C   
2308 O O   . LEU B 148 ? 0.3120 0.2593 0.2395 -0.0835 0.0283  -0.0017 165 LEU B O   
2309 C CB  . LEU B 148 ? 0.3096 0.2363 0.2207 -0.0636 0.0199  0.0178  165 LEU B CB  
2310 C CG  . LEU B 148 ? 0.3301 0.2422 0.2290 -0.0557 0.0170  0.0267  165 LEU B CG  
2311 C CD1 . LEU B 148 ? 0.3212 0.2438 0.2318 -0.0451 0.0109  0.0301  165 LEU B CD1 
2312 C CD2 . LEU B 148 ? 0.3518 0.2540 0.2426 -0.0550 0.0183  0.0317  165 LEU B CD2 
2313 N N   . ALA B 149 ? 0.3051 0.2424 0.2236 -0.0850 0.0318  0.0032  166 ALA B N   
2314 C CA  . ALA B 149 ? 0.3235 0.2764 0.2569 -0.0913 0.0347  -0.0050 166 ALA B CA  
2315 C C   . ALA B 149 ? 0.3145 0.2882 0.2702 -0.0847 0.0297  -0.0071 166 ALA B C   
2316 O O   . ALA B 149 ? 0.3187 0.3067 0.2886 -0.0899 0.0314  -0.0153 166 ALA B O   
2317 C CB  . ALA B 149 ? 0.4228 0.3721 0.3526 -0.0951 0.0383  -0.0044 166 ALA B CB  
2318 N N   . LEU B 150 ? 0.2829 0.2588 0.2425 -0.0736 0.0237  -0.0003 167 LEU B N   
2319 C CA  . LEU B 150 ? 0.2723 0.2671 0.2523 -0.0671 0.0184  -0.0018 167 LEU B CA  
2320 C C   . LEU B 150 ? 0.2377 0.2361 0.2209 -0.0650 0.0149  -0.0034 167 LEU B C   
2321 O O   . LEU B 150 ? 0.2309 0.2422 0.2284 -0.0583 0.0095  -0.0030 167 LEU B O   
2322 C CB  . LEU B 150 ? 0.2800 0.2763 0.2636 -0.0564 0.0136  0.0062  167 LEU B CB  
2323 C CG  . LEU B 150 ? 0.2539 0.2561 0.2445 -0.0566 0.0151  0.0062  167 LEU B CG  
2324 C CD1 . LEU B 150 ? 0.3583 0.3573 0.3475 -0.0462 0.0109  0.0151  167 LEU B CD1 
2325 C CD2 . LEU B 150 ? 0.3850 0.4079 0.3972 -0.0584 0.0145  -0.0011 167 LEU B CD2 
2326 N N   . SER B 151 ? 0.2489 0.2364 0.2194 -0.0711 0.0180  -0.0054 168 SER B N   
2327 C CA  A SER B 151 ? 0.2601 0.2489 0.2313 -0.0693 0.0149  -0.0064 168 SER B CA  
2328 C CA  B SER B 151 ? 0.2587 0.2476 0.2300 -0.0690 0.0148  -0.0063 168 SER B CA  
2329 C C   . SER B 151 ? 0.2345 0.2435 0.2268 -0.0687 0.0115  -0.0126 168 SER B C   
2330 O O   . SER B 151 ? 0.2624 0.2768 0.2606 -0.0622 0.0059  -0.0106 168 SER B O   
2331 C CB  A SER B 151 ? 0.2970 0.2733 0.2534 -0.0782 0.0200  -0.0098 168 SER B CB  
2332 C CB  B SER B 151 ? 0.2947 0.2708 0.2510 -0.0775 0.0195  -0.0094 168 SER B CB  
2333 O OG  A SER B 151 ? 0.2922 0.2688 0.2482 -0.0771 0.0174  -0.0109 168 SER B OG  
2334 O OG  B SER B 151 ? 0.4005 0.3574 0.3374 -0.0753 0.0203  -0.0023 168 SER B OG  
2335 N N   . ASP B 152 ? 0.2488 0.2689 0.2528 -0.0755 0.0147  -0.0202 169 ASP B N   
2336 C CA  . ASP B 152 ? 0.2786 0.3175 0.3032 -0.0756 0.0113  -0.0268 169 ASP B CA  
2337 C C   . ASP B 152 ? 0.2401 0.2913 0.2793 -0.0654 0.0043  -0.0230 169 ASP B C   
2338 O O   . ASP B 152 ? 0.2462 0.3109 0.3005 -0.0633 -0.0004 -0.0265 169 ASP B O   
2339 C CB  . ASP B 152 ? 0.2916 0.3405 0.3270 -0.0848 0.0163  -0.0359 169 ASP B CB  
2340 C CG  . ASP B 152 ? 0.4631 0.5032 0.4875 -0.0958 0.0230  -0.0417 169 ASP B CG  
2341 O OD1 . ASP B 152 ? 0.4013 0.4323 0.4148 -0.0968 0.0227  -0.0408 169 ASP B OD1 
2342 O OD2 . ASP B 152 ? 0.6031 0.6455 0.6299 -0.1038 0.0286  -0.0473 169 ASP B OD2 
2343 N N   . TYR B 153 ? 0.1783 0.2253 0.2137 -0.0592 0.0032  -0.0159 170 TYR B N   
2344 C CA  . TYR B 153 ? 0.1571 0.2148 0.2053 -0.0495 -0.0031 -0.0118 170 TYR B CA  
2345 C C   . TYR B 153 ? 0.1839 0.2320 0.2219 -0.0404 -0.0075 -0.0029 170 TYR B C   
2346 O O   . TYR B 153 ? 0.1997 0.2555 0.2468 -0.0320 -0.0131 0.0010  170 TYR B O   
2347 C CB  . TYR B 153 ? 0.1910 0.2531 0.2450 -0.0488 -0.0013 -0.0109 170 TYR B CB  
2348 C CG  . TYR B 153 ? 0.1822 0.2562 0.2493 -0.0573 0.0025  -0.0204 170 TYR B CG  
2349 C CD1 . TYR B 153 ? 0.1862 0.2790 0.2749 -0.0561 -0.0015 -0.0259 170 TYR B CD1 
2350 C CD2 . TYR B 153 ? 0.1918 0.2579 0.2494 -0.0670 0.0100  -0.0244 170 TYR B CD2 
2351 C CE1 . TYR B 153 ? 0.1928 0.2968 0.2944 -0.0642 0.0021  -0.0354 170 TYR B CE1 
2352 C CE2 . TYR B 153 ? 0.2122 0.2892 0.2819 -0.0754 0.0139  -0.0338 170 TYR B CE2 
2353 C CZ  . TYR B 153 ? 0.2062 0.3022 0.2981 -0.0738 0.0101  -0.0393 170 TYR B CZ  
2354 O OH  . TYR B 153 ? 0.2600 0.3666 0.3642 -0.0822 0.0142  -0.0489 170 TYR B OH  
2355 N N   . ILE B 154 ? 0.2141 0.2458 0.2337 -0.0421 -0.0051 0.0001  171 ILE B N   
2356 C CA  . ILE B 154 ? 0.2131 0.2351 0.2227 -0.0342 -0.0088 0.0078  171 ILE B CA  
2357 C C   . ILE B 154 ? 0.2166 0.2398 0.2262 -0.0343 -0.0116 0.0056  171 ILE B C   
2358 O O   . ILE B 154 ? 0.2600 0.2856 0.2724 -0.0268 -0.0171 0.0097  171 ILE B O   
2359 C CB  . ILE B 154 ? 0.2310 0.2331 0.2199 -0.0352 -0.0047 0.0131  171 ILE B CB  
2360 C CG1 . ILE B 154 ? 0.2370 0.2373 0.2255 -0.0335 -0.0030 0.0165  171 ILE B CG1 
2361 C CG2 . ILE B 154 ? 0.2732 0.2643 0.2512 -0.0282 -0.0079 0.0199  171 ILE B CG2 
2362 C CD1 . ILE B 154 ? 0.3332 0.3150 0.3027 -0.0379 0.0021  0.0193  171 ILE B CD1 
2363 N N   . PHE B 155 ? 0.2082 0.2297 0.2148 -0.0431 -0.0080 -0.0008 172 PHE B N   
2364 C CA  . PHE B 155 ? 0.2466 0.2678 0.2517 -0.0443 -0.0100 -0.0032 172 PHE B CA  
2365 C C   . PHE B 155 ? 0.2359 0.2744 0.2593 -0.0479 -0.0122 -0.0113 172 PHE B C   
2366 O O   . PHE B 155 ? 0.2772 0.3245 0.3105 -0.0534 -0.0094 -0.0172 172 PHE B O   
2367 C CB  . PHE B 155 ? 0.2775 0.2833 0.2651 -0.0514 -0.0045 -0.0045 172 PHE B CB  
2368 C CG  . PHE B 155 ? 0.2531 0.2413 0.2229 -0.0489 -0.0021 0.0028  172 PHE B CG  
2369 C CD1 . PHE B 155 ? 0.2811 0.2617 0.2437 -0.0408 -0.0057 0.0099  172 PHE B CD1 
2370 C CD2 . PHE B 155 ? 0.2979 0.2770 0.2584 -0.0547 0.0037  0.0023  172 PHE B CD2 
2371 C CE1 . PHE B 155 ? 0.3074 0.2720 0.2546 -0.0382 -0.0038 0.0164  172 PHE B CE1 
2372 C CE2 . PHE B 155 ? 0.3481 0.3105 0.2924 -0.0522 0.0053  0.0091  172 PHE B CE2 
2373 C CZ  . PHE B 155 ? 0.3278 0.2833 0.2660 -0.0438 0.0015  0.0160  172 PHE B CZ  
2374 N N   . GLU B 156 ? 0.2808 0.3242 0.3089 -0.0447 -0.0174 -0.0115 173 GLU B N   
2375 C CA  . GLU B 156 ? 0.3536 0.4134 0.3997 -0.0470 -0.0209 -0.0187 173 GLU B CA  
2376 C C   . GLU B 156 ? 0.5268 0.5844 0.5697 -0.0569 -0.0164 -0.0261 173 GLU B C   
2377 O O   . GLU B 156 ? 0.5428 0.6131 0.6003 -0.0615 -0.0171 -0.0338 173 GLU B O   
2378 C CB  . GLU B 156 ? 0.3726 0.4380 0.4247 -0.0397 -0.0288 -0.0157 173 GLU B CB  
2379 C CG  . GLU B 156 ? 0.4718 0.5245 0.5085 -0.0384 -0.0295 -0.0121 173 GLU B CG  
2380 C CD  . GLU B 156 ? 0.5201 0.5782 0.5622 -0.0313 -0.0373 -0.0091 173 GLU B CD  
2381 O OE1 . GLU B 156 ? 0.2713 0.3373 0.3230 -0.0243 -0.0420 -0.0056 173 GLU B OE1 
2382 O OE2 . GLU B 156 ? 0.5187 0.5726 0.5550 -0.0329 -0.0387 -0.0101 173 GLU B OE2 
2383 O OXT . GLU B 156 ? 0.4843 0.5272 0.5101 -0.0607 -0.0119 -0.0248 173 GLU B OXT 
2384 N N   . HIS C 8   ? 0.4936 0.7055 0.5483 0.0637  0.0062  0.0101  25  HIS C N   
2385 C CA  . HIS C 8   ? 0.3878 0.6079 0.4428 0.0605  0.0063  0.0108  25  HIS C CA  
2386 C C   . HIS C 8   ? 0.3585 0.5754 0.4166 0.0574  0.0063  0.0109  25  HIS C C   
2387 O O   . HIS C 8   ? 0.3571 0.5661 0.4168 0.0581  0.0061  0.0102  25  HIS C O   
2388 C CB  . HIS C 8   ? 0.4586 0.6777 0.5124 0.0623  0.0060  0.0105  25  HIS C CB  
2389 N N   . VAL C 9   ? 0.2730 0.4963 0.3317 0.0540  0.0066  0.0116  26  VAL C N   
2390 C CA  . VAL C 9   ? 0.1976 0.4181 0.2591 0.0509  0.0068  0.0118  26  VAL C CA  
2391 C C   . VAL C 9   ? 0.2191 0.4492 0.2806 0.0463  0.0072  0.0127  26  VAL C C   
2392 O O   . VAL C 9   ? 0.2051 0.4452 0.2646 0.0448  0.0074  0.0133  26  VAL C O   
2393 C CB  . VAL C 9   ? 0.2056 0.4255 0.2680 0.0498  0.0070  0.0119  26  VAL C CB  
2394 C CG1 . VAL C 9   ? 0.2486 0.4581 0.3112 0.0540  0.0068  0.0110  26  VAL C CG1 
2395 C CG2 . VAL C 9   ? 0.2152 0.4473 0.2756 0.0472  0.0072  0.0127  26  VAL C CG2 
2396 N N   . GLU C 10  ? 0.1435 0.3705 0.2075 0.0438  0.0074  0.0128  27  GLU C N   
2397 C CA  . GLU C 10  ? 0.1906 0.4263 0.2548 0.0383  0.0082  0.0138  27  GLU C CA  
2398 C C   . GLU C 10  ? 0.1382 0.3726 0.2044 0.0344  0.0087  0.0142  27  GLU C C   
2399 O O   . GLU C 10  ? 0.1464 0.3732 0.2140 0.0366  0.0083  0.0137  27  GLU C O   
2400 C CB  . GLU C 10  ? 0.2339 0.4678 0.2983 0.0388  0.0082  0.0138  27  GLU C CB  
2401 C CG  . GLU C 10  ? 0.2029 0.4248 0.2695 0.0418  0.0078  0.0131  27  GLU C CG  
2402 C CD  . GLU C 10  ? 0.2267 0.4461 0.2931 0.0435  0.0076  0.0129  27  GLU C CD  
2403 O OE1 . GLU C 10  ? 0.3656 0.5909 0.4300 0.0438  0.0076  0.0131  27  GLU C OE1 
2404 O OE2 . GLU C 10  ? 0.1600 0.3714 0.2282 0.0446  0.0074  0.0125  27  GLU C OE2 
2405 N N   . GLN C 11  ? 0.1564 0.3981 0.2226 0.0283  0.0096  0.0151  28  GLN C N   
2406 C CA  . GLN C 11  ? 0.1331 0.3745 0.2006 0.0233  0.0105  0.0156  28  GLN C CA  
2407 C C   . GLN C 11  ? 0.1235 0.3531 0.1868 0.0192  0.0107  0.0158  28  GLN C C   
2408 O O   . GLN C 11  ? 0.1333 0.3659 0.1944 0.0174  0.0111  0.0161  28  GLN C O   
2409 C CB  . GLN C 11  ? 0.1567 0.4084 0.2222 0.0173  0.0111  0.0161  28  GLN C CB  
2410 C CG  . GLN C 11  ? 0.1863 0.4394 0.2509 0.0206  0.0102  0.0156  28  GLN C CG  
2411 C CD  . GLN C 11  ? 0.2149 0.4766 0.2780 0.0151  0.0106  0.0159  28  GLN C CD  
2412 O OE1 . GLN C 11  ? 0.2688 0.5362 0.3306 0.0081  0.0116  0.0164  28  GLN C OE1 
2413 N NE2 . GLN C 11  ? 0.2074 0.4697 0.2699 0.0181  0.0099  0.0155  28  GLN C NE2 
2414 N N   . THR C 12  ? 0.1416 0.3577 0.2038 0.0180  0.0105  0.0156  29  THR C N   
2415 C CA  . THR C 12  ? 0.0987 0.3028 0.1565 0.0140  0.0108  0.0158  29  THR C CA  
2416 C C   . THR C 12  ? 0.1494 0.3480 0.2038 0.0073  0.0115  0.0163  29  THR C C   
2417 O O   . THR C 12  ? 0.1383 0.3387 0.1945 0.0070  0.0114  0.0161  29  THR C O   
2418 C CB  . THR C 12  ? 0.1208 0.3120 0.1799 0.0194  0.0099  0.0151  29  THR C CB  
2419 O OG1 . THR C 12  ? 0.1498 0.3317 0.2043 0.0161  0.0103  0.0154  29  THR C OG1 
2420 C CG2 . THR C 12  ? 0.1277 0.3104 0.1890 0.0212  0.0095  0.0146  29  THR C CG2 
2421 N N   . TYR C 13  ? 0.1221 0.3140 0.1712 0.0017  0.0123  0.0168  30  TYR C N   
2422 C CA  . TYR C 13  ? 0.1095 0.2939 0.1545 -0.0049 0.0131  0.0172  30  TYR C CA  
2423 C C   . TYR C 13  ? 0.1312 0.2989 0.1751 -0.0029 0.0126  0.0170  30  TYR C C   
2424 O O   . TYR C 13  ? 0.1353 0.2954 0.1775 -0.0010 0.0125  0.0169  30  TYR C O   
2425 C CB  . TYR C 13  ? 0.1309 0.3170 0.1701 -0.0124 0.0146  0.0180  30  TYR C CB  
2426 C CG  . TYR C 13  ? 0.1274 0.3049 0.1619 -0.0193 0.0155  0.0183  30  TYR C CG  
2427 C CD1 . TYR C 13  ? 0.1523 0.3349 0.1875 -0.0225 0.0157  0.0182  30  TYR C CD1 
2428 C CD2 . TYR C 13  ? 0.1484 0.3124 0.1774 -0.0222 0.0162  0.0188  30  TYR C CD2 
2429 C CE1 . TYR C 13  ? 0.1691 0.3434 0.1999 -0.0286 0.0165  0.0185  30  TYR C CE1 
2430 C CE2 . TYR C 13  ? 0.1900 0.3451 0.2142 -0.0282 0.0171  0.0191  30  TYR C CE2 
2431 C CZ  . TYR C 13  ? 0.1901 0.3506 0.2154 -0.0315 0.0172  0.0189  30  TYR C CZ  
2432 O OH  . TYR C 13  ? 0.2048 0.3568 0.2254 -0.0373 0.0181  0.0192  30  TYR C OH  
2433 N N   . LEU C 14  ? 0.1252 0.2875 0.1701 -0.0031 0.0124  0.0168  31  LEU C N   
2434 C CA  . LEU C 14  ? 0.1259 0.2727 0.1696 -0.0019 0.0120  0.0166  31  LEU C CA  
2435 C C   . LEU C 14  ? 0.1471 0.2879 0.1862 -0.0088 0.0130  0.0171  31  LEU C C   
2436 O O   . LEU C 14  ? 0.1648 0.3129 0.2044 -0.0119 0.0133  0.0172  31  LEU C O   
2437 C CB  . LEU C 14  ? 0.1314 0.2760 0.1808 0.0049  0.0109  0.0158  31  LEU C CB  
2438 C CG  . LEU C 14  ? 0.1660 0.3136 0.2195 0.0120  0.0100  0.0150  31  LEU C CG  
2439 C CD1 . LEU C 14  ? 0.2277 0.3782 0.2872 0.0181  0.0092  0.0143  31  LEU C CD1 
2440 C CD2 . LEU C 14  ? 0.2404 0.3752 0.2920 0.0137  0.0096  0.0147  31  LEU C CD2 
2441 N N   . MET C 15  ? 0.1374 0.2646 0.1718 -0.0108 0.0134  0.0174  32  MET C N   
2442 C CA  . MET C 15  ? 0.1709 0.2910 0.2001 -0.0174 0.0144  0.0180  32  MET C CA  
2443 C C   . MET C 15  ? 0.1680 0.2727 0.1962 -0.0154 0.0140  0.0179  32  MET C C   
2444 O O   . MET C 15  ? 0.1848 0.2807 0.2112 -0.0130 0.0138  0.0179  32  MET C O   
2445 C CB  . MET C 15  ? 0.2062 0.3258 0.2288 -0.0240 0.0158  0.0188  32  MET C CB  
2446 C CG  . MET C 15  ? 0.1794 0.2920 0.1961 -0.0312 0.0171  0.0193  32  MET C CG  
2447 S SD  . MET C 15  ? 0.2434 0.3587 0.2526 -0.0398 0.0192  0.0201  32  MET C SD  
2448 C CE  . MET C 15  ? 0.2864 0.3953 0.2937 -0.0359 0.0191  0.0204  32  MET C CE  
2449 N N   . ILE C 16  ? 0.1341 0.2354 0.1630 -0.0163 0.0139  0.0178  33  ILE C N   
2450 C CA  . ILE C 16  ? 0.1449 0.2315 0.1720 -0.0153 0.0138  0.0179  33  ILE C CA  
2451 C C   . ILE C 16  ? 0.1655 0.2432 0.1845 -0.0221 0.0151  0.0187  33  ILE C C   
2452 O O   . ILE C 16  ? 0.1714 0.2528 0.1870 -0.0284 0.0162  0.0191  33  ILE C O   
2453 C CB  . ILE C 16  ? 0.1264 0.2124 0.1570 -0.0137 0.0132  0.0175  33  ILE C CB  
2454 C CG1 . ILE C 16  ? 0.1534 0.2484 0.1916 -0.0070 0.0121  0.0168  33  ILE C CG1 
2455 C CG2 . ILE C 16  ? 0.1560 0.2267 0.1849 -0.0124 0.0131  0.0176  33  ILE C CG2 
2456 C CD1 . ILE C 16  ? 0.2051 0.2995 0.2470 -0.0047 0.0117  0.0164  33  ILE C CD1 
2457 N N   . LYS C 17  ? 0.1658 0.2321 0.1815 -0.0208 0.0152  0.0189  34  LYS C N   
2458 C CA  . LYS C 17  ? 0.1954 0.2519 0.2028 -0.0264 0.0167  0.0198  34  LYS C CA  
2459 C C   . LYS C 17  ? 0.1901 0.2364 0.1946 -0.0289 0.0171  0.0201  34  LYS C C   
2460 O O   . LYS C 17  ? 0.1847 0.2308 0.1938 -0.0258 0.0161  0.0196  34  LYS C O   
2461 C CB  . LYS C 17  ? 0.1749 0.2233 0.1802 -0.0230 0.0165  0.0199  34  LYS C CB  
2462 C CG  . LYS C 17  ? 0.1760 0.2342 0.1838 -0.0205 0.0161  0.0196  34  LYS C CG  
2463 C CD  . LYS C 17  ? 0.1923 0.2423 0.1977 -0.0169 0.0159  0.0197  34  LYS C CD  
2464 C CE  . LYS C 17  ? 0.1965 0.2559 0.2033 -0.0154 0.0158  0.0196  34  LYS C CE  
2465 N NZ  . LYS C 17  ? 0.2185 0.2703 0.2231 -0.0118 0.0155  0.0195  34  LYS C NZ  
2466 N N   . PRO C 18  ? 0.1819 0.2197 0.1785 -0.0348 0.0186  0.0209  35  PRO C N   
2467 C CA  . PRO C 18  ? 0.2068 0.2351 0.2001 -0.0377 0.0191  0.0212  35  PRO C CA  
2468 C C   . PRO C 18  ? 0.1943 0.2126 0.1902 -0.0318 0.0180  0.0209  35  PRO C C   
2469 O O   . PRO C 18  ? 0.2013 0.2163 0.1981 -0.0322 0.0178  0.0208  35  PRO C O   
2470 C CB  . PRO C 18  ? 0.2193 0.2387 0.2029 -0.0441 0.0210  0.0221  35  PRO C CB  
2471 C CG  . PRO C 18  ? 0.2296 0.2598 0.2125 -0.0471 0.0217  0.0222  35  PRO C CG  
2472 C CD  . PRO C 18  ? 0.2009 0.2387 0.1910 -0.0399 0.0201  0.0216  35  PRO C CD  
2473 N N   . ASP C 19  ? 0.1862 0.1999 0.1834 -0.0265 0.0172  0.0207  36  ASP C N   
2474 C CA  . ASP C 19  ? 0.2016 0.2067 0.2018 -0.0208 0.0162  0.0203  36  ASP C CA  
2475 C C   . ASP C 19  ? 0.1765 0.1892 0.1854 -0.0163 0.0148  0.0193  36  ASP C C   
2476 O O   . ASP C 19  ? 0.1931 0.1996 0.2041 -0.0138 0.0143  0.0191  36  ASP C O   
2477 C CB  . ASP C 19  ? 0.1993 0.1983 0.1989 -0.0163 0.0157  0.0201  36  ASP C CB  
2478 C CG  . ASP C 19  ? 0.2090 0.2184 0.2123 -0.0136 0.0150  0.0196  36  ASP C CG  
2479 O OD1 . ASP C 19  ? 0.2450 0.2640 0.2475 -0.0173 0.0157  0.0198  36  ASP C OD1 
2480 O OD2 . ASP C 19  ? 0.2040 0.2116 0.2106 -0.0077 0.0139  0.0189  36  ASP C OD2 
2481 N N   . GLY C 20  ? 0.1921 0.2181 0.2058 -0.0150 0.0143  0.0188  37  GLY C N   
2482 C CA  . GLY C 20  ? 0.1962 0.2295 0.2174 -0.0110 0.0133  0.0181  37  GLY C CA  
2483 C C   . GLY C 20  ? 0.1562 0.1906 0.1767 -0.0148 0.0138  0.0184  37  GLY C C   
2484 O O   . GLY C 20  ? 0.1736 0.2065 0.1982 -0.0116 0.0132  0.0180  37  GLY C O   
2485 N N   . ILE C 21  ? 0.1664 0.2033 0.1816 -0.0217 0.0149  0.0190  38  ILE C N   
2486 C CA  . ILE C 21  ? 0.1652 0.2028 0.1790 -0.0260 0.0154  0.0192  38  ILE C CA  
2487 C C   . ILE C 21  ? 0.1622 0.1853 0.1728 -0.0261 0.0157  0.0196  38  ILE C C   
2488 O O   . ILE C 21  ? 0.1689 0.1907 0.1822 -0.0246 0.0153  0.0194  38  ILE C O   
2489 C CB  . ILE C 21  ? 0.1918 0.2346 0.2000 -0.0338 0.0167  0.0197  38  ILE C CB  
2490 C CG1 . ILE C 21  ? 0.2261 0.2833 0.2370 -0.0339 0.0166  0.0194  38  ILE C CG1 
2491 C CG2 . ILE C 21  ? 0.2133 0.2572 0.2202 -0.0381 0.0172  0.0197  38  ILE C CG2 
2492 C CD1 . ILE C 21  ? 0.2024 0.2717 0.2208 -0.0296 0.0155  0.0187  38  ILE C CD1 
2493 N N   . GLN C 22  ? 0.1933 0.2052 0.1977 -0.0278 0.0164  0.0201  39  GLN C N   
2494 C CA  . GLN C 22  ? 0.2127 0.2105 0.2128 -0.0287 0.0169  0.0206  39  GLN C CA  
2495 C C   . GLN C 22  ? 0.1739 0.1660 0.1793 -0.0217 0.0157  0.0201  39  GLN C C   
2496 O O   . GLN C 22  ? 0.2112 0.1955 0.2157 -0.0216 0.0158  0.0203  39  GLN C O   
2497 C CB  . GLN C 22  ? 0.2068 0.1946 0.1986 -0.0321 0.0181  0.0214  39  GLN C CB  
2498 C CG  . GLN C 22  ? 0.2109 0.2008 0.1959 -0.0401 0.0197  0.0220  39  GLN C CG  
2499 C CD  . GLN C 22  ? 0.2686 0.2533 0.2498 -0.0448 0.0204  0.0223  39  GLN C CD  
2500 O OE1 . GLN C 22  ? 0.2814 0.2602 0.2647 -0.0418 0.0198  0.0222  39  GLN C OE1 
2501 N NE2 . GLN C 22  ? 0.2997 0.2860 0.2749 -0.0523 0.0219  0.0226  39  GLN C NE2 
2502 N N   . ARG C 23  ? 0.1709 0.1665 0.1815 -0.0159 0.0146  0.0195  40  ARG C N   
2503 C CA  . ARG C 23  ? 0.1612 0.1525 0.1774 -0.0093 0.0135  0.0188  40  ARG C CA  
2504 C C   . ARG C 23  ? 0.1845 0.1841 0.2076 -0.0067 0.0129  0.0182  40  ARG C C   
2505 O O   . ARG C 23  ? 0.2024 0.1986 0.2303 -0.0016 0.0122  0.0176  40  ARG C O   
2506 C CB  . ARG C 23  ? 0.1811 0.1726 0.1998 -0.0045 0.0127  0.0182  40  ARG C CB  
2507 C CG  . ARG C 23  ? 0.1798 0.1610 0.1914 -0.0062 0.0134  0.0188  40  ARG C CG  
2508 C CD  . ARG C 23  ? 0.2043 0.1867 0.2181 -0.0016 0.0126  0.0181  40  ARG C CD  
2509 N NE  . ARG C 23  ? 0.1933 0.1718 0.2127 0.0048  0.0114  0.0171  40  ARG C NE  
2510 C CZ  . ARG C 23  ? 0.2076 0.1892 0.2316 0.0099  0.0104  0.0161  40  ARG C CZ  
2511 N NH1 . ARG C 23  ? 0.1946 0.1828 0.2181 0.0098  0.0103  0.0160  40  ARG C NH1 
2512 N NH2 . ARG C 23  ? 0.2029 0.1815 0.2324 0.0152  0.0094  0.0150  40  ARG C NH2 
2513 N N   . GLN C 24  ? 0.1488 0.1589 0.1723 -0.0101 0.0132  0.0183  41  GLN C N   
2514 C CA  . GLN C 24  ? 0.1671 0.1851 0.1958 -0.0084 0.0128  0.0179  41  GLN C CA  
2515 C C   . GLN C 24  ? 0.1415 0.1651 0.1779 -0.0013 0.0118  0.0170  41  GLN C C   
2516 O O   . GLN C 24  ? 0.1734 0.1962 0.2144 0.0025  0.0114  0.0166  41  GLN C O   
2517 C CB  . GLN C 24  ? 0.2031 0.2129 0.2303 -0.0095 0.0131  0.0182  41  GLN C CB  
2518 C CG  . GLN C 24  ? 0.2064 0.2119 0.2258 -0.0170 0.0143  0.0191  41  GLN C CG  
2519 C CD  . GLN C 24  ? 0.2495 0.2561 0.2684 -0.0197 0.0146  0.0192  41  GLN C CD  
2520 O OE1 . GLN C 24  ? 0.2385 0.2352 0.2559 -0.0192 0.0147  0.0195  41  GLN C OE1 
2521 N NE2 . GLN C 24  ? 0.2161 0.2348 0.2361 -0.0225 0.0147  0.0191  41  GLN C NE2 
2522 N N   . VAL C 25  ? 0.1427 0.1724 0.1804 0.0001  0.0115  0.0166  42  VAL C N   
2523 C CA  . VAL C 25  ? 0.1425 0.1784 0.1869 0.0065  0.0106  0.0157  42  VAL C CA  
2524 C C   . VAL C 25  ? 0.1512 0.2017 0.1976 0.0059  0.0105  0.0156  42  VAL C C   
2525 O O   . VAL C 25  ? 0.1465 0.2030 0.1971 0.0104  0.0099  0.0149  42  VAL C O   
2526 C CB  . VAL C 25  ? 0.1376 0.1670 0.1822 0.0100  0.0100  0.0152  42  VAL C CB  
2527 C CG1 . VAL C 25  ? 0.1663 0.1823 0.2100 0.0115  0.0100  0.0151  42  VAL C CG1 
2528 C CG2 . VAL C 25  ? 0.1717 0.2016 0.2111 0.0063  0.0104  0.0157  42  VAL C CG2 
2529 N N   . VAL C 26  ? 0.1465 0.2031 0.1899 0.0005  0.0112  0.0162  43  VAL C N   
2530 C CA  . VAL C 26  ? 0.1139 0.1851 0.1592 -0.0002 0.0112  0.0162  43  VAL C CA  
2531 C C   . VAL C 26  ? 0.1465 0.2251 0.1987 0.0061  0.0106  0.0155  43  VAL C C   
2532 O O   . VAL C 26  ? 0.1342 0.2218 0.1894 0.0090  0.0102  0.0151  43  VAL C O   
2533 C CB  . VAL C 26  ? 0.1286 0.2049 0.1699 -0.0070 0.0120  0.0167  43  VAL C CB  
2534 C CG1 . VAL C 26  ? 0.1312 0.2236 0.1754 -0.0072 0.0119  0.0166  43  VAL C CG1 
2535 C CG2 . VAL C 26  ? 0.1557 0.2260 0.1899 -0.0134 0.0129  0.0174  43  VAL C CG2 
2536 N N   . GLY C 27  ? 0.1124 0.1876 0.1670 0.0081  0.0105  0.0154  44  GLY C N   
2537 C CA  . GLY C 27  ? 0.1211 0.2030 0.1816 0.0139  0.0101  0.0148  44  GLY C CA  
2538 C C   . GLY C 27  ? 0.1177 0.1970 0.1824 0.0202  0.0096  0.0140  44  GLY C C   
2539 O O   . GLY C 27  ? 0.1115 0.1993 0.1802 0.0244  0.0093  0.0135  44  GLY C O   
2540 N N   . GLU C 28  ? 0.1176 0.1850 0.1811 0.0209  0.0094  0.0138  45  GLU C N   
2541 C CA  . GLU C 28  ? 0.1096 0.1742 0.1768 0.0265  0.0087  0.0128  45  GLU C CA  
2542 C C   . GLU C 28  ? 0.1112 0.1838 0.1783 0.0269  0.0085  0.0126  45  GLU C C   
2543 O O   . GLU C 28  ? 0.1180 0.1950 0.1894 0.0320  0.0080  0.0118  45  GLU C O   
2544 C CB  . GLU C 28  ? 0.1514 0.2023 0.2168 0.0267  0.0086  0.0126  45  GLU C CB  
2545 C CG  . GLU C 28  ? 0.1616 0.2037 0.2283 0.0280  0.0087  0.0125  45  GLU C CG  
2546 C CD  . GLU C 28  ? 0.3012 0.3316 0.3670 0.0294  0.0084  0.0121  45  GLU C CD  
2547 O OE1 . GLU C 28  ? 0.3447 0.3744 0.4143 0.0342  0.0078  0.0110  45  GLU C OE1 
2548 O OE2 . GLU C 28  ? 0.3473 0.3697 0.4083 0.0257  0.0087  0.0128  45  GLU C OE2 
2549 N N   . ILE C 29  ? 0.1117 0.1862 0.1738 0.0215  0.0088  0.0133  46  ILE C N   
2550 C CA  . ILE C 29  ? 0.1123 0.1948 0.1740 0.0215  0.0086  0.0132  46  ILE C CA  
2551 C C   . ILE C 29  ? 0.1052 0.2014 0.1703 0.0234  0.0086  0.0131  46  ILE C C   
2552 O O   . ILE C 29  ? 0.1003 0.2022 0.1686 0.0278  0.0082  0.0125  46  ILE C O   
2553 C CB  . ILE C 29  ? 0.1172 0.1986 0.1724 0.0149  0.0092  0.0141  46  ILE C CB  
2554 C CG1 . ILE C 29  ? 0.1609 0.2286 0.2126 0.0142  0.0092  0.0142  46  ILE C CG1 
2555 C CG2 . ILE C 29  ? 0.1547 0.2467 0.2096 0.0144  0.0092  0.0142  46  ILE C CG2 
2556 C CD1 . ILE C 29  ? 0.1791 0.2433 0.2237 0.0074  0.0101  0.0152  46  ILE C CD1 
2557 N N   . ILE C 30  ? 0.1129 0.2150 0.1773 0.0204  0.0091  0.0137  47  ILE C N   
2558 C CA  . ILE C 30  ? 0.1278 0.2437 0.1953 0.0223  0.0091  0.0137  47  ILE C CA  
2559 C C   . ILE C 30  ? 0.1006 0.2171 0.1737 0.0298  0.0087  0.0129  47  ILE C C   
2560 O O   . ILE C 30  ? 0.1119 0.2375 0.1876 0.0334  0.0086  0.0125  47  ILE C O   
2561 C CB  . ILE C 30  ? 0.1014 0.2224 0.1671 0.0179  0.0096  0.0143  47  ILE C CB  
2562 C CG1 . ILE C 30  ? 0.1241 0.2469 0.1843 0.0103  0.0102  0.0150  47  ILE C CG1 
2563 C CG2 . ILE C 30  ? 0.1242 0.2586 0.1935 0.0209  0.0096  0.0142  47  ILE C CG2 
2564 C CD1 . ILE C 30  ? 0.1526 0.2767 0.2103 0.0052  0.0107  0.0154  47  ILE C CD1 
2565 N N   . SER C 31  ? 0.1125 0.2192 0.1873 0.0322  0.0087  0.0125  48  SER C N   
2566 C CA  . SER C 31  ? 0.1219 0.2283 0.2019 0.0391  0.0086  0.0117  48  SER C CA  
2567 C C   . SER C 31  ? 0.1115 0.2179 0.1937 0.0434  0.0081  0.0108  48  SER C C   
2568 O O   . SER C 31  ? 0.1264 0.2376 0.2124 0.0488  0.0081  0.0102  48  SER C O   
2569 C CB  . SER C 31  ? 0.1177 0.2122 0.1987 0.0405  0.0087  0.0115  48  SER C CB  
2570 O OG  . SER C 31  ? 0.1199 0.2152 0.1999 0.0379  0.0092  0.0122  48  SER C OG  
2571 N N   . ARG C 32  ? 0.1085 0.2090 0.1882 0.0415  0.0077  0.0106  49  ARG C N   
2572 C CA  . ARG C 32  ? 0.1068 0.2075 0.1884 0.0456  0.0071  0.0097  49  ARG C CA  
2573 C C   . ARG C 32  ? 0.1128 0.2266 0.1953 0.0468  0.0071  0.0098  49  ARG C C   
2574 O O   . ARG C 32  ? 0.1106 0.2273 0.1963 0.0521  0.0068  0.0089  49  ARG C O   
2575 C CB  . ARG C 32  ? 0.1242 0.2172 0.2024 0.0430  0.0067  0.0096  49  ARG C CB  
2576 C CG  . ARG C 32  ? 0.1109 0.1907 0.1890 0.0433  0.0066  0.0092  49  ARG C CG  
2577 C CD  . ARG C 32  ? 0.2212 0.2943 0.2972 0.0431  0.0060  0.0088  49  ARG C CD  
2578 N NE  . ARG C 32  ? 0.2133 0.2742 0.2892 0.0436  0.0059  0.0084  49  ARG C NE  
2579 C CZ  . ARG C 32  ? 0.2036 0.2575 0.2798 0.0460  0.0052  0.0074  49  ARG C CZ  
2580 N NH1 . ARG C 32  ? 0.2071 0.2646 0.2837 0.0479  0.0047  0.0068  49  ARG C NH1 
2581 N NH2 . ARG C 32  ? 0.1923 0.2358 0.2686 0.0464  0.0052  0.0071  49  ARG C NH2 
2582 N N   . PHE C 33  ? 0.0937 0.2157 0.1731 0.0420  0.0075  0.0108  50  PHE C N   
2583 C CA  . PHE C 33  ? 0.0869 0.2220 0.1669 0.0430  0.0075  0.0110  50  PHE C CA  
2584 C C   . PHE C 33  ? 0.0887 0.2324 0.1721 0.0466  0.0078  0.0110  50  PHE C C   
2585 O O   . PHE C 33  ? 0.1127 0.2587 0.1959 0.0494  0.0075  0.0102  50  PHE C O   
2586 C CB  . PHE C 33  ? 0.0907 0.2316 0.1662 0.0363  0.0079  0.0120  50  PHE C CB  
2587 C CG  . PHE C 33  ? 0.0951 0.2283 0.1670 0.0334  0.0077  0.0121  50  PHE C CG  
2588 C CD1 . PHE C 33  ? 0.1411 0.2751 0.2136 0.0363  0.0072  0.0115  50  PHE C CD1 
2589 C CD2 . PHE C 33  ? 0.1570 0.2814 0.2247 0.0281  0.0080  0.0126  50  PHE C CD2 
2590 C CE1 . PHE C 33  ? 0.1161 0.2428 0.1851 0.0341  0.0071  0.0116  50  PHE C CE1 
2591 C CE2 . PHE C 33  ? 0.1610 0.2779 0.2250 0.0258  0.0080  0.0127  50  PHE C CE2 
2592 C CZ  . PHE C 33  ? 0.1254 0.2436 0.1901 0.0289  0.0075  0.0122  50  PHE C CZ  
2593 N N   . GLU C 34  ? 0.1042 0.2465 0.1875 0.0451  0.0082  0.0114  51  GLU C N   
2594 C CA  . GLU C 34  ? 0.1148 0.2603 0.1992 0.0478  0.0084  0.0111  51  GLU C CA  
2595 C C   . GLU C 34  ? 0.0962 0.2294 0.1804 0.0517  0.0079  0.0094  51  GLU C C   
2596 O O   . GLU C 34  ? 0.1233 0.2567 0.2062 0.0532  0.0078  0.0087  51  GLU C O   
2597 C CB  . GLU C 34  ? 0.1172 0.2626 0.2025 0.0465  0.0090  0.0119  51  GLU C CB  
2598 C CG  . GLU C 34  ? 0.1083 0.2613 0.1905 0.0402  0.0092  0.0128  51  GLU C CG  
2599 C CD  . GLU C 34  ? 0.1163 0.2660 0.1980 0.0384  0.0096  0.0132  51  GLU C CD  
2600 O OE1 . GLU C 34  ? 0.1211 0.2584 0.2019 0.0372  0.0096  0.0131  51  GLU C OE1 
2601 O OE2 . GLU C 34  ? 0.1251 0.2847 0.2075 0.0387  0.0099  0.0136  51  GLU C OE2 
2602 N N   . LYS C 35  ? 0.1037 0.2261 0.1891 0.0528  0.0075  0.0086  52  LYS C N   
2603 C CA  . LYS C 35  ? 0.1318 0.2421 0.2176 0.0551  0.0070  0.0067  52  LYS C CA  
2604 C C   . LYS C 35  ? 0.1384 0.2498 0.2229 0.0564  0.0066  0.0058  52  LYS C C   
2605 O O   . LYS C 35  ? 0.1295 0.2343 0.2142 0.0578  0.0065  0.0046  52  LYS C O   
2606 C CB  . LYS C 35  ? 0.1295 0.2292 0.2166 0.0553  0.0067  0.0059  52  LYS C CB  
2607 C CG  . LYS C 35  ? 0.1663 0.2536 0.2544 0.0562  0.0061  0.0038  52  LYS C CG  
2608 C CD  . LYS C 35  ? 0.2199 0.2976 0.3090 0.0560  0.0055  0.0027  52  LYS C CD  
2609 C CE  . LYS C 35  ? 0.3696 0.4367 0.4599 0.0557  0.0049  0.0005  52  LYS C CE  
2610 N NZ  . LYS C 35  ? 0.3538 0.4216 0.4435 0.0554  0.0055  0.0013  52  LYS C NZ  
2611 N N   . ARG C 36  ? 0.0941 0.2135 0.1777 0.0559  0.0065  0.0064  53  ARG C N   
2612 C CA  . ARG C 36  ? 0.1030 0.2243 0.1852 0.0573  0.0061  0.0058  53  ARG C CA  
2613 C C   . ARG C 36  ? 0.1270 0.2579 0.2072 0.0574  0.0065  0.0065  53  ARG C C   
2614 O O   . ARG C 36  ? 0.1072 0.2410 0.1857 0.0585  0.0063  0.0062  53  ARG C O   
2615 C CB  . ARG C 36  ? 0.1165 0.2410 0.1984 0.0569  0.0058  0.0060  53  ARG C CB  
2616 C CG  . ARG C 36  ? 0.1290 0.2429 0.2123 0.0574  0.0052  0.0050  53  ARG C CG  
2617 C CD  . ARG C 36  ? 0.1472 0.2640 0.2298 0.0575  0.0048  0.0051  53  ARG C CD  
2618 N NE  . ARG C 36  ? 0.1051 0.2213 0.1866 0.0591  0.0044  0.0041  53  ARG C NE  
2619 C CZ  . ARG C 36  ? 0.1238 0.2409 0.2045 0.0596  0.0040  0.0039  53  ARG C CZ  
2620 N NH1 . ARG C 36  ? 0.1416 0.2608 0.2224 0.0589  0.0039  0.0045  53  ARG C NH1 
2621 N NH2 . ARG C 36  ? 0.1812 0.2972 0.2610 0.0611  0.0036  0.0030  53  ARG C NH2 
2622 N N   . GLY C 37  ? 0.0934 0.2294 0.1733 0.0562  0.0070  0.0074  54  GLY C N   
2623 C CA  . GLY C 37  ? 0.1097 0.2558 0.1875 0.0560  0.0072  0.0082  54  GLY C CA  
2624 C C   . GLY C 37  ? 0.0989 0.2576 0.1756 0.0535  0.0073  0.0092  54  GLY C C   
2625 O O   . GLY C 37  ? 0.1550 0.3220 0.2295 0.0536  0.0073  0.0096  54  GLY C O   
2626 N N   . TYR C 38  ? 0.1002 0.2609 0.1783 0.0511  0.0073  0.0098  55  TYR C N   
2627 C CA  . TYR C 38  ? 0.1138 0.2871 0.1911 0.0476  0.0076  0.0109  55  TYR C CA  
2628 C C   . TYR C 38  ? 0.1164 0.2983 0.1935 0.0444  0.0081  0.0118  55  TYR C C   
2629 O O   . TYR C 38  ? 0.1127 0.2904 0.1912 0.0440  0.0083  0.0120  55  TYR C O   
2630 C CB  . TYR C 38  ? 0.1220 0.2951 0.2009 0.0456  0.0076  0.0113  55  TYR C CB  
2631 C CG  . TYR C 38  ? 0.1138 0.2800 0.1925 0.0485  0.0071  0.0104  55  TYR C CG  
2632 C CD1 . TYR C 38  ? 0.1010 0.2671 0.1779 0.0510  0.0066  0.0096  55  TYR C CD1 
2633 C CD2 . TYR C 38  ? 0.1293 0.2887 0.2096 0.0488  0.0069  0.0103  55  TYR C CD2 
2634 C CE1 . TYR C 38  ? 0.1165 0.2765 0.1932 0.0532  0.0061  0.0087  55  TYR C CE1 
2635 C CE2 . TYR C 38  ? 0.1194 0.2724 0.1994 0.0513  0.0063  0.0093  55  TYR C CE2 
2636 C CZ  . TYR C 38  ? 0.1145 0.2679 0.1928 0.0533  0.0059  0.0085  55  TYR C CZ  
2637 O OH  . TYR C 38  ? 0.1337 0.2808 0.2118 0.0554  0.0052  0.0074  55  TYR C OH  
2638 N N   . ARG C 39  ? 0.1206 0.3141 0.1957 0.0419  0.0082  0.0124  56  ARG C N   
2639 C CA  . ARG C 39  ? 0.1041 0.3064 0.1783 0.0387  0.0085  0.0130  56  ARG C CA  
2640 C C   . ARG C 39  ? 0.1164 0.3265 0.1913 0.0323  0.0092  0.0139  56  ARG C C   
2641 O O   . ARG C 39  ? 0.1249 0.3401 0.1992 0.0297  0.0094  0.0143  56  ARG C O   
2642 C CB  . ARG C 39  ? 0.1226 0.3329 0.1938 0.0397  0.0083  0.0130  56  ARG C CB  
2643 C CG  . ARG C 39  ? 0.0980 0.3171 0.1680 0.0368  0.0085  0.0135  56  ARG C CG  
2644 C CD  . ARG C 39  ? 0.1220 0.3486 0.1888 0.0385  0.0082  0.0134  56  ARG C CD  
2645 N NE  . ARG C 39  ? 0.1232 0.3585 0.1886 0.0358  0.0083  0.0137  56  ARG C NE  
2646 C CZ  . ARG C 39  ? 0.1309 0.3767 0.1953 0.0301  0.0085  0.0142  56  ARG C CZ  
2647 N NH1 . ARG C 39  ? 0.1315 0.3804 0.1962 0.0261  0.0088  0.0144  56  ARG C NH1 
2648 N NH2 . ARG C 39  ? 0.2077 0.4607 0.2706 0.0280  0.0086  0.0145  56  ARG C NH2 
2649 N N   . ILE C 40  ? 0.0997 0.3106 0.1756 0.0293  0.0096  0.0144  57  ILE C N   
2650 C CA  . ILE C 40  ? 0.1272 0.3401 0.2003 0.0213  0.0101  0.0149  57  ILE C CA  
2651 C C   . ILE C 40  ? 0.0956 0.3252 0.1680 0.0181  0.0104  0.0152  57  ILE C C   
2652 O O   . ILE C 40  ? 0.1227 0.3565 0.1942 0.0187  0.0102  0.0151  57  ILE C O   
2653 C CB  . ILE C 40  ? 0.1113 0.3159 0.1831 0.0183  0.0102  0.0150  57  ILE C CB  
2654 C CG1 . ILE C 40  ? 0.1071 0.2958 0.1800 0.0219  0.0099  0.0147  57  ILE C CG1 
2655 C CG2 . ILE C 40  ? 0.1340 0.3373 0.2009 0.0095  0.0107  0.0154  57  ILE C CG2 
2656 C CD1 . ILE C 40  ? 0.1341 0.3156 0.2066 0.0206  0.0101  0.0147  57  ILE C CD1 
2657 N N   . ALA C 41  ? 0.1115 0.3451 0.1817 0.0144  0.0107  0.0155  58  ALA C N   
2658 C CA  . ALA C 41  ? 0.1252 0.3725 0.1935 0.0107  0.0110  0.0156  58  ALA C CA  
2659 C C   . ALA C 41  ? 0.1182 0.3677 0.1833 0.0016  0.0118  0.0159  58  ALA C C   
2660 O O   . ALA C 41  ? 0.1529 0.4143 0.2169 -0.0021 0.0120  0.0159  58  ALA C O   
2661 C CB  . ALA C 41  ? 0.1360 0.3868 0.2031 0.0122  0.0108  0.0156  58  ALA C CB  
2662 N N   . ALA C 42  ? 0.1179 0.3531 0.1797 -0.0023 0.0120  0.0160  59  ALA C N   
2663 C CA  . ALA C 42  ? 0.1066 0.3401 0.1638 -0.0110 0.0128  0.0162  59  ALA C CA  
2664 C C   . ALA C 42  ? 0.1263 0.3418 0.1809 -0.0126 0.0128  0.0163  59  ALA C C   
2665 O O   . ALA C 42  ? 0.1432 0.3482 0.1987 -0.0082 0.0124  0.0162  59  ALA C O   
2666 C CB  . ALA C 42  ? 0.1454 0.3845 0.1994 -0.0164 0.0136  0.0165  59  ALA C CB  
2667 N N   . MET C 43  ? 0.1266 0.3389 0.1779 -0.0189 0.0133  0.0163  60  MET C N   
2668 C CA  . MET C 43  ? 0.1490 0.3445 0.1973 -0.0207 0.0134  0.0164  60  MET C CA  
2669 C C   . MET C 43  ? 0.2138 0.4084 0.2571 -0.0295 0.0143  0.0165  60  MET C C   
2670 O O   . MET C 43  ? 0.2180 0.4233 0.2619 -0.0322 0.0144  0.0162  60  MET C O   
2671 C CB  . MET C 43  ? 0.1391 0.3282 0.1910 -0.0146 0.0126  0.0162  60  MET C CB  
2672 C CG  . MET C 43  ? 0.1875 0.3592 0.2370 -0.0153 0.0127  0.0163  60  MET C CG  
2673 S SD  . MET C 43  ? 0.1883 0.3521 0.2428 -0.0067 0.0118  0.0160  60  MET C SD  
2674 C CE  . MET C 43  ? 0.1874 0.3483 0.2448 0.0000  0.0112  0.0157  60  MET C CE  
2675 N N   . LYS C 44  ? 0.1737 0.3557 0.2118 -0.0340 0.0151  0.0168  61  LYS C N   
2676 C CA  . LYS C 44  ? 0.2073 0.3869 0.2399 -0.0427 0.0161  0.0169  61  LYS C CA  
2677 C C   . LYS C 44  ? 0.2375 0.3988 0.2651 -0.0450 0.0167  0.0173  61  LYS C C   
2678 O O   . LYS C 44  ? 0.2112 0.3658 0.2371 -0.0437 0.0169  0.0177  61  LYS C O   
2679 C CB  . LYS C 44  ? 0.2203 0.4115 0.2506 -0.0485 0.0171  0.0169  61  LYS C CB  
2680 C CG  . LYS C 44  ? 0.3723 0.5575 0.3956 -0.0577 0.0186  0.0171  61  LYS C CG  
2681 C CD  . LYS C 44  ? 0.3361 0.5354 0.3580 -0.0635 0.0196  0.0169  61  LYS C CD  
2682 C CE  . LYS C 44  ? 0.3017 0.5045 0.3243 -0.0610 0.0198  0.0173  61  LYS C CE  
2683 N NZ  . LYS C 44  ? 0.3017 0.5184 0.3227 -0.0671 0.0209  0.0172  61  LYS C NZ  
2684 N N   . LEU C 45  ? 0.2004 0.3537 0.2251 -0.0483 0.0170  0.0173  62  LEU C N   
2685 C CA  . LEU C 45  ? 0.1842 0.3209 0.2030 -0.0518 0.0178  0.0177  62  LEU C CA  
2686 C C   . LEU C 45  ? 0.1942 0.3318 0.2065 -0.0609 0.0194  0.0179  62  LEU C C   
2687 O O   . LEU C 45  ? 0.2176 0.3652 0.2293 -0.0660 0.0198  0.0174  62  LEU C O   
2688 C CB  . LEU C 45  ? 0.1792 0.3062 0.1977 -0.0511 0.0174  0.0177  62  LEU C CB  
2689 C CG  . LEU C 45  ? 0.2314 0.3403 0.2440 -0.0533 0.0181  0.0182  62  LEU C CG  
2690 C CD1 . LEU C 45  ? 0.2678 0.3675 0.2829 -0.0461 0.0173  0.0185  62  LEU C CD1 
2691 C CD2 . LEU C 45  ? 0.2871 0.3886 0.2974 -0.0561 0.0183  0.0182  62  LEU C CD2 
2692 N N   . THR C 46  ? 0.2087 0.3364 0.2160 -0.0629 0.0203  0.0185  63  THR C N   
2693 C CA  . THR C 46  ? 0.2338 0.3601 0.2341 -0.0716 0.0221  0.0187  63  THR C CA  
2694 C C   . THR C 46  ? 0.2623 0.3705 0.2563 -0.0728 0.0230  0.0194  63  THR C C   
2695 O O   . THR C 46  ? 0.2619 0.3602 0.2574 -0.0668 0.0221  0.0197  63  THR C O   
2696 C CB  . THR C 46  ? 0.3001 0.4397 0.3012 -0.0734 0.0227  0.0187  63  THR C CB  
2697 O OG1 . THR C 46  ? 0.2971 0.4375 0.2918 -0.0827 0.0245  0.0187  63  THR C OG1 
2698 C CG2 . THR C 46  ? 0.2799 0.4147 0.2811 -0.0688 0.0225  0.0192  63  THR C CG2 
2699 N N   . ILE C 47  ? 0.2631 0.3667 0.2496 -0.0807 0.0249  0.0197  64  ILE C N   
2700 C CA  . ILE C 47  ? 0.2653 0.3524 0.2449 -0.0821 0.0260  0.0205  64  ILE C CA  
2701 C C   . ILE C 47  ? 0.3075 0.3981 0.2844 -0.0841 0.0272  0.0210  64  ILE C C   
2702 O O   . ILE C 47  ? 0.3266 0.4252 0.3008 -0.0908 0.0286  0.0208  64  ILE C O   
2703 C CB  . ILE C 47  ? 0.3183 0.3947 0.2905 -0.0891 0.0275  0.0207  64  ILE C CB  
2704 C CG1 . ILE C 47  ? 0.3640 0.4356 0.3389 -0.0861 0.0263  0.0203  64  ILE C CG1 
2705 C CG2 . ILE C 47  ? 0.3297 0.3898 0.2940 -0.0907 0.0290  0.0216  64  ILE C CG2 
2706 C CD1 . ILE C 47  ? 0.4860 0.5474 0.4541 -0.0925 0.0275  0.0204  64  ILE C CD1 
2707 N N   . ALA C 48  ? 0.2655 0.3508 0.2434 -0.0783 0.0266  0.0215  65  ALA C N   
2708 C CA  . ALA C 48  ? 0.2614 0.3503 0.2373 -0.0791 0.0276  0.0219  65  ALA C CA  
2709 C C   . ALA C 48  ? 0.3518 0.4311 0.3180 -0.0868 0.0300  0.0226  65  ALA C C   
2710 O O   . ALA C 48  ? 0.3649 0.4295 0.3256 -0.0883 0.0308  0.0230  65  ALA C O   
2711 C CB  . ALA C 48  ? 0.3052 0.3892 0.2840 -0.0709 0.0263  0.0222  65  ALA C CB  
2712 N N   . THR C 49  ? 0.3354 0.4228 0.2992 -0.0916 0.0315  0.0227  66  THR C N   
2713 C CA  . THR C 49  ? 0.4328 0.5117 0.3872 -0.0990 0.0341  0.0234  66  THR C CA  
2714 C C   . THR C 49  ? 0.4138 0.4891 0.3655 -0.0966 0.0349  0.0242  66  THR C C   
2715 O O   . THR C 49  ? 0.3493 0.4333 0.3070 -0.0908 0.0335  0.0241  66  THR C O   
2716 C CB  . THR C 49  ? 0.4118 0.5027 0.3648 -0.1075 0.0356  0.0228  66  THR C CB  
2717 O OG1 . THR C 49  ? 0.4273 0.5351 0.3864 -0.1055 0.0349  0.0225  66  THR C OG1 
2718 C CG2 . THR C 49  ? 0.4406 0.5343 0.3955 -0.1102 0.0350  0.0219  66  THR C CG2 
2719 N N   . PRO C 50  ? 0.4328 0.4950 0.3754 -0.1008 0.0371  0.0251  67  PRO C N   
2720 C CA  . PRO C 50  ? 0.4249 0.4842 0.3645 -0.0988 0.0380  0.0259  67  PRO C CA  
2721 C C   . PRO C 50  ? 0.4102 0.4857 0.3529 -0.1005 0.0384  0.0257  67  PRO C C   
2722 O O   . PRO C 50  ? 0.4375 0.5163 0.3829 -0.0951 0.0376  0.0260  67  PRO C O   
2723 C CB  . PRO C 50  ? 0.4736 0.5173 0.4019 -0.1049 0.0408  0.0269  67  PRO C CB  
2724 C CG  . PRO C 50  ? 0.4976 0.5316 0.4241 -0.1060 0.0405  0.0266  67  PRO C CG  
2725 C CD  . PRO C 50  ? 0.4435 0.4915 0.3779 -0.1065 0.0388  0.0254  67  PRO C CD  
2726 N N   . ALA C 51  ? 0.4340 0.5201 0.3767 -0.1076 0.0394  0.0252  68  ALA C N   
2727 C CA  . ALA C 51  ? 0.4806 0.5822 0.4258 -0.1095 0.0400  0.0250  68  ALA C CA  
2728 C C   . ALA C 51  ? 0.5130 0.6276 0.4682 -0.1014 0.0373  0.0245  68  ALA C C   
2729 O O   . ALA C 51  ? 0.4677 0.5884 0.4246 -0.0983 0.0372  0.0249  68  ALA C O   
2730 C CB  . ALA C 51  ? 0.4953 0.6070 0.4394 -0.1185 0.0414  0.0243  68  ALA C CB  
2731 N N   . ILE C 52  ? 0.4482 0.5670 0.4098 -0.0977 0.0352  0.0237  69  ILE C N   
2732 C CA  . ILE C 52  ? 0.3645 0.4951 0.3351 -0.0899 0.0328  0.0233  69  ILE C CA  
2733 C C   . ILE C 52  ? 0.3283 0.4496 0.3002 -0.0816 0.0315  0.0237  69  ILE C C   
2734 O O   . ILE C 52  ? 0.2979 0.4271 0.2746 -0.0759 0.0304  0.0236  69  ILE C O   
2735 C CB  . ILE C 52  ? 0.3204 0.4586 0.2973 -0.0882 0.0311  0.0223  69  ILE C CB  
2736 C CG1 . ILE C 52  ? 0.3472 0.5000 0.3328 -0.0812 0.0291  0.0218  69  ILE C CG1 
2737 C CG2 . ILE C 52  ? 0.3420 0.4658 0.3185 -0.0849 0.0300  0.0223  69  ILE C CG2 
2738 C CD1 . ILE C 52  ? 0.4364 0.5993 0.4281 -0.0798 0.0277  0.0210  69  ILE C CD1 
2739 N N   . LEU C 53  ? 0.3125 0.4169 0.2798 -0.0808 0.0318  0.0241  70  LEU C N   
2740 C CA  . LEU C 53  ? 0.3149 0.4101 0.2831 -0.0731 0.0306  0.0244  70  LEU C CA  
2741 C C   . LEU C 53  ? 0.3109 0.4054 0.2753 -0.0729 0.0317  0.0252  70  LEU C C   
2742 O O   . LEU C 53  ? 0.3267 0.4221 0.2947 -0.0659 0.0304  0.0251  70  LEU C O   
2743 C CB  . LEU C 53  ? 0.3094 0.3870 0.2729 -0.0728 0.0307  0.0247  70  LEU C CB  
2744 C CG  . LEU C 53  ? 0.2931 0.3699 0.2611 -0.0709 0.0292  0.0240  70  LEU C CG  
2745 C CD1 . LEU C 53  ? 0.2752 0.3345 0.2372 -0.0722 0.0298  0.0245  70  LEU C CD1 
2746 C CD2 . LEU C 53  ? 0.3017 0.3843 0.2788 -0.0619 0.0266  0.0233  70  LEU C CD2 
2747 N N   . GLU C 54  ? 0.3287 0.4215 0.2859 -0.0805 0.0343  0.0258  71  GLU C N   
2748 C CA  . GLU C 54  ? 0.3793 0.4728 0.3329 -0.0807 0.0356  0.0266  71  GLU C CA  
2749 C C   . GLU C 54  ? 0.3148 0.4252 0.2756 -0.0770 0.0344  0.0261  71  GLU C C   
2750 O O   . GLU C 54  ? 0.3815 0.4922 0.3430 -0.0722 0.0341  0.0265  71  GLU C O   
2751 C CB  . GLU C 54  ? 0.4545 0.5452 0.3996 -0.0902 0.0388  0.0272  71  GLU C CB  
2752 C CG  . GLU C 54  ? 0.7185 0.7904 0.6546 -0.0933 0.0404  0.0280  71  GLU C CG  
2753 C CD  . GLU C 54  ? 0.8641 0.9338 0.7924 -0.1036 0.0435  0.0283  71  GLU C CD  
2754 O OE1 . GLU C 54  ? 0.7532 0.8355 0.6823 -0.1084 0.0446  0.0281  71  GLU C OE1 
2755 O OE2 . GLU C 54  ? 0.9231 0.9782 0.8443 -0.1069 0.0448  0.0287  71  GLU C OE2 
2756 N N   . GLU C 55  ? 0.3250 0.4497 0.2908 -0.0795 0.0340  0.0254  72  GLU C N   
2757 C CA  A GLU C 55  ? 0.3128 0.4541 0.2854 -0.0757 0.0329  0.0250  72  GLU C CA  
2758 C CA  B GLU C 55  ? 0.3133 0.4548 0.2860 -0.0758 0.0328  0.0250  72  GLU C CA  
2759 C C   . GLU C 55  ? 0.3137 0.4558 0.2937 -0.0660 0.0301  0.0244  72  GLU C C   
2760 O O   . GLU C 55  ? 0.3064 0.4552 0.2900 -0.0607 0.0292  0.0244  72  GLU C O   
2761 C CB  A GLU C 55  ? 0.3802 0.5367 0.3559 -0.0808 0.0332  0.0244  72  GLU C CB  
2762 C CB  B GLU C 55  ? 0.3798 0.5362 0.3558 -0.0807 0.0330  0.0243  72  GLU C CB  
2763 C CG  A GLU C 55  ? 0.3827 0.5569 0.3640 -0.0782 0.0326  0.0242  72  GLU C CG  
2764 C CG  B GLU C 55  ? 0.4173 0.5736 0.3867 -0.0910 0.0357  0.0246  72  GLU C CG  
2765 C CD  A GLU C 55  ? 0.4310 0.6198 0.4131 -0.0852 0.0337  0.0238  72  GLU C CD  
2766 C CD  B GLU C 55  ? 0.5010 0.6723 0.4743 -0.0953 0.0355  0.0237  72  GLU C CD  
2767 O OE1 A GLU C 55  ? 0.5179 0.7025 0.4953 -0.0927 0.0352  0.0237  72  GLU C OE1 
2768 O OE1 B GLU C 55  ? 0.5347 0.7221 0.5135 -0.0934 0.0349  0.0234  72  GLU C OE1 
2769 O OE2 A GLU C 55  ? 0.3434 0.5481 0.3307 -0.0830 0.0330  0.0235  72  GLU C OE2 
2770 O OE2 B GLU C 55  ? 0.5258 0.6930 0.4969 -0.1002 0.0360  0.0233  72  GLU C OE2 
2771 N N   . HIS C 56  ? 0.2879 0.4233 0.2701 -0.0636 0.0288  0.0239  73  HIS C N   
2772 C CA  . HIS C 56  ? 0.2836 0.4190 0.2726 -0.0546 0.0263  0.0233  73  HIS C CA  
2773 C C   . HIS C 56  ? 0.2985 0.4250 0.2860 -0.0492 0.0259  0.0236  73  HIS C C   
2774 O O   . HIS C 56  ? 0.2745 0.4066 0.2672 -0.0425 0.0244  0.0232  73  HIS C O   
2775 C CB  . HIS C 56  ? 0.2300 0.3572 0.2203 -0.0537 0.0253  0.0228  73  HIS C CB  
2776 C CG  . HIS C 56  ? 0.2657 0.3922 0.2628 -0.0450 0.0230  0.0221  73  HIS C CG  
2777 N ND1 . HIS C 56  ? 0.2361 0.3754 0.2406 -0.0410 0.0216  0.0214  73  HIS C ND1 
2778 C CD2 . HIS C 56  ? 0.2851 0.3997 0.2826 -0.0396 0.0219  0.0220  73  HIS C CD2 
2779 C CE1 . HIS C 56  ? 0.2527 0.3875 0.2618 -0.0336 0.0198  0.0208  73  HIS C CE1 
2780 N NE2 . HIS C 56  ? 0.2734 0.3935 0.2785 -0.0327 0.0200  0.0211  73  HIS C NE2 
2781 N N   . TYR C 57  ? 0.4089 0.5533 0.2090 0.1378  0.0317  0.1036  74  TYR C N   
2782 C CA  . TYR C 57  ? 0.3914 0.5366 0.1896 0.1386  0.0310  0.1029  74  TYR C CA  
2783 C C   . TYR C 57  ? 0.4996 0.6417 0.2960 0.1390  0.0308  0.1033  74  TYR C C   
2784 O O   . TYR C 57  ? 0.4918 0.6341 0.2865 0.1400  0.0298  0.1028  74  TYR C O   
2785 C CB  . TYR C 57  ? 0.4287 0.5768 0.2270 0.1399  0.0298  0.1019  74  TYR C CB  
2786 C CG  . TYR C 57  ? 0.4157 0.5673 0.2153 0.1397  0.0299  0.1012  74  TYR C CG  
2787 C CD1 . TYR C 57  ? 0.4668 0.6200 0.2662 0.1390  0.0305  0.1008  74  TYR C CD1 
2788 C CD2 . TYR C 57  ? 0.4912 0.6448 0.2923 0.1402  0.0294  0.1010  74  TYR C CD2 
2789 C CE1 . TYR C 57  ? 0.4474 0.6039 0.2481 0.1388  0.0306  0.1002  74  TYR C CE1 
2790 C CE2 . TYR C 57  ? 0.4607 0.6177 0.2632 0.1400  0.0295  0.1003  74  TYR C CE2 
2791 C CZ  . TYR C 57  ? 0.4824 0.6407 0.2845 0.1393  0.0301  0.0999  74  TYR C CZ  
2792 O OH  . TYR C 57  ? 0.5876 0.7493 0.3910 0.1390  0.0302  0.0993  74  TYR C OH  
2793 N N   . ALA C 58  ? 0.4361 0.5752 0.2326 0.1380  0.0317  0.1043  75  ALA C N   
2794 C CA  . ALA C 58  ? 0.4789 0.6148 0.2737 0.1383  0.0316  0.1048  75  ALA C CA  
2795 C C   . ALA C 58  ? 0.4833 0.6195 0.2761 0.1386  0.0313  0.1042  75  ALA C C   
2796 O O   . ALA C 58  ? 0.5085 0.6430 0.2996 0.1394  0.0306  0.1042  75  ALA C O   
2797 C CB  . ALA C 58  ? 0.4866 0.6196 0.2821 0.1370  0.0327  0.1059  75  ALA C CB  
2798 N N   . GLU C 59  ? 0.5139 0.6520 0.3067 0.1380  0.0318  0.1037  76  GLU C N   
2799 C CA  . GLU C 59  ? 0.5098 0.6482 0.3008 0.1382  0.0316  0.1032  76  GLU C CA  
2800 C C   . GLU C 59  ? 0.5947 0.7346 0.3843 0.1397  0.0302  0.1023  76  GLU C C   
2801 O O   . GLU C 59  ? 0.5609 0.7006 0.3488 0.1401  0.0298  0.1019  76  GLU C O   
2802 C CB  . GLU C 59  ? 0.5180 0.6585 0.3094 0.1373  0.0323  0.1028  76  GLU C CB  
2803 C CG  . GLU C 59  ? 0.6445 0.7889 0.4370 0.1377  0.0319  0.1019  76  GLU C CG  
2804 C CD  . GLU C 59  ? 0.7549 0.9011 0.5483 0.1365  0.0328  0.1017  76  GLU C CD  
2805 O OE1 . GLU C 59  ? 0.7212 0.8672 0.5164 0.1355  0.0337  0.1023  76  GLU C OE1 
2806 O OE2 . GLU C 59  ? 0.7394 0.8874 0.5319 0.1367  0.0326  0.1009  76  GLU C OE2 
2807 N N   . HIS C 60  ? 0.4936 0.6352 0.2842 0.1406  0.0294  0.1020  77  HIS C N   
2808 C CA  . HIS C 60  ? 0.5779 0.7209 0.3675 0.1420  0.0280  0.1011  77  HIS C CA  
2809 C C   . HIS C 60  ? 0.5695 0.7103 0.3586 0.1429  0.0272  0.1015  77  HIS C C   
2810 O O   . HIS C 60  ? 0.6105 0.7524 0.3990 0.1442  0.0261  0.1008  77  HIS C O   
2811 C CB  . HIS C 60  ? 0.5492 0.6959 0.3402 0.1424  0.0275  0.1003  77  HIS C CB  
2812 C CG  . HIS C 60  ? 0.5036 0.6527 0.2953 0.1416  0.0282  0.0999  77  HIS C CG  
2813 N ND1 . HIS C 60  ? 0.5910 0.7406 0.3813 0.1414  0.0283  0.0994  77  HIS C ND1 
2814 C CD2 . HIS C 60  ? 0.6064 0.7575 0.4000 0.1408  0.0288  0.0998  77  HIS C CD2 
2815 C CE1 . HIS C 60  ? 0.5883 0.7401 0.3796 0.1406  0.0290  0.0991  77  HIS C CE1 
2816 N NE2 . HIS C 60  ? 0.5727 0.7255 0.3660 0.1402  0.0293  0.0993  77  HIS C NE2 
2817 N N   . LYS C 61  ? 0.7031 0.8408 0.4923 0.1423  0.0279  0.1025  78  LYS C N   
2818 C CA  . LYS C 61  ? 0.8089 0.9444 0.5978 0.1431  0.0273  0.1029  78  LYS C CA  
2819 C C   . LYS C 61  ? 0.8547 0.9897 0.6414 0.1442  0.0262  0.1024  78  LYS C C   
2820 O O   . LYS C 61  ? 0.7253 0.8600 0.5105 0.1441  0.0263  0.1022  78  LYS C O   
2821 C CB  . LYS C 61  ? 0.8913 1.0233 0.6804 0.1421  0.0282  0.1041  78  LYS C CB  
2822 C CG  . LYS C 61  ? 1.0940 1.2235 0.8826 0.1428  0.0276  0.1046  78  LYS C CG  
2823 C CD  . LYS C 61  ? 1.3468 1.4731 1.1359 0.1418  0.0286  0.1057  78  LYS C CD  
2824 C CE  . LYS C 61  ? 1.3446 1.4681 1.1330 0.1424  0.0281  0.1062  78  LYS C CE  
2825 N NZ  . LYS C 61  ? 1.5111 1.6312 1.2994 0.1415  0.0290  0.1072  78  LYS C NZ  
2826 N N   . GLY C 62  ? 0.8593 0.9941 0.6459 0.1453  0.0252  0.1022  79  GLY C N   
2827 C CA  . GLY C 62  ? 0.8013 0.9356 0.5859 0.1465  0.0241  0.1017  79  GLY C CA  
2828 C C   . GLY C 62  ? 0.8961 1.0336 0.6801 0.1474  0.0232  0.1005  79  GLY C C   
2829 O O   . GLY C 62  ? 0.7825 0.9200 0.5652 0.1485  0.0221  0.1000  79  GLY C O   
2830 N N   . LYS C 63  ? 0.8893 1.0294 0.6742 0.1468  0.0236  0.1001  80  LYS C N   
2831 C CA  . LYS C 63  ? 0.8369 0.9801 0.6212 0.1476  0.0228  0.0989  80  LYS C CA  
2832 C C   . LYS C 63  ? 0.8420 0.9873 0.6272 0.1486  0.0218  0.0983  80  LYS C C   
2833 O O   . LYS C 63  ? 0.7612 0.9062 0.5479 0.1485  0.0219  0.0987  80  LYS C O   
2834 C CB  . LYS C 63  ? 0.6880 0.8334 0.4731 0.1466  0.0237  0.0986  80  LYS C CB  
2835 C CG  . LYS C 63  ? 0.8900 1.0335 0.6743 0.1455  0.0248  0.0992  80  LYS C CG  
2836 C CD  . LYS C 63  ? 0.8727 1.0186 0.6578 0.1446  0.0255  0.0988  80  LYS C CD  
2837 C CE  . LYS C 63  ? 0.8654 1.0093 0.6497 0.1435  0.0266  0.0994  80  LYS C CE  
2838 N NZ  . LYS C 63  ? 0.7297 0.8760 0.5149 0.1425  0.0274  0.0990  80  LYS C NZ  
2839 N N   . PRO C 64  ? 0.8789 1.0264 0.6632 0.1496  0.0207  0.0972  81  PRO C N   
2840 C CA  . PRO C 64  ? 0.8875 1.0368 0.6725 0.1508  0.0196  0.0966  81  PRO C CA  
2841 C C   . PRO C 64  ? 0.7246 0.8770 0.5115 0.1505  0.0197  0.0961  81  PRO C C   
2842 O O   . PRO C 64  ? 0.6749 0.8283 0.4627 0.1512  0.0190  0.0959  81  PRO C O   
2843 C CB  . PRO C 64  ? 0.8204 0.9707 0.6035 0.1519  0.0185  0.0956  81  PRO C CB  
2844 C CG  . PRO C 64  ? 0.8748 1.0235 0.6563 0.1514  0.0190  0.0958  81  PRO C CG  
2845 C CD  . PRO C 64  ? 1.0070 1.1552 0.7896 0.1499  0.0204  0.0965  81  PRO C CD  
2846 N N   . PHE C 65  ? 0.6124 0.7665 0.4000 0.1496  0.0206  0.0960  82  PHE C N   
2847 C CA  . PHE C 65  ? 0.8184 0.9753 0.6079 0.1493  0.0208  0.0957  82  PHE C CA  
2848 C C   . PHE C 65  ? 0.6882 0.8440 0.4796 0.1483  0.0218  0.0967  82  PHE C C   
2849 O O   . PHE C 65  ? 0.5627 0.7207 0.3558 0.1481  0.0219  0.0965  82  PHE C O   
2850 C CB  . PHE C 65  ? 0.7572 0.9165 0.5467 0.1487  0.0213  0.0951  82  PHE C CB  
2851 C CG  . PHE C 65  ? 0.9789 1.1365 0.7682 0.1473  0.0226  0.0958  82  PHE C CG  
2852 C CD1 . PHE C 65  ? 0.9575 1.1131 0.7449 0.1473  0.0227  0.0960  82  PHE C CD1 
2853 C CD2 . PHE C 65  ? 0.9331 1.0911 0.7241 0.1461  0.0237  0.0963  82  PHE C CD2 
2854 C CE1 . PHE C 65  ? 0.8828 1.0367 0.6699 0.1461  0.0239  0.0966  82  PHE C CE1 
2855 C CE2 . PHE C 65  ? 0.7998 0.9561 0.5906 0.1449  0.0249  0.0970  82  PHE C CE2 
2856 C CZ  . PHE C 65  ? 0.8007 0.9550 0.5896 0.1449  0.0250  0.0971  82  PHE C CZ  
2857 N N   . LEU C 66  ? 0.6286 0.6249 0.5160 0.0623  0.0419  0.0981  83  LEU C N   
2858 C CA  . LEU C 66  ? 0.6282 0.6187 0.5168 0.0577  0.0413  0.0965  83  LEU C CA  
2859 C C   . LEU C 66  ? 0.5736 0.5587 0.4609 0.0560  0.0451  0.0980  83  LEU C C   
2860 O O   . LEU C 66  ? 0.5042 0.4871 0.3934 0.0516  0.0433  0.0969  83  LEU C O   
2861 C CB  . LEU C 66  ? 0.5505 0.5376 0.4383 0.0583  0.0422  0.0953  83  LEU C CB  
2862 C CG  . LEU C 66  ? 0.6188 0.6001 0.5080 0.0535  0.0413  0.0934  83  LEU C CG  
2863 C CD1 . LEU C 66  ? 0.4899 0.4737 0.3827 0.0494  0.0357  0.0912  83  LEU C CD1 
2864 C CD2 . LEU C 66  ? 0.7500 0.7284 0.6385 0.0543  0.0421  0.0923  83  LEU C CD2 
2865 N N   . PRO C 67  ? 0.5472 0.5303 0.4315 0.0591  0.0502  0.1004  84  PRO C N   
2866 C CA  . PRO C 67  ? 0.5526 0.5304 0.4357 0.0573  0.0537  0.1017  84  PRO C CA  
2867 C C   . PRO C 67  ? 0.5711 0.5510 0.4560 0.0547  0.0516  0.1019  84  PRO C C   
2868 O O   . PRO C 67  ? 0.5430 0.5186 0.4288 0.0508  0.0519  0.1015  84  PRO C O   
2869 C CB  . PRO C 67  ? 0.5936 0.5707 0.4732 0.0620  0.0591  0.1045  84  PRO C CB  
2870 C CG  . PRO C 67  ? 0.6030 0.5823 0.4817 0.0654  0.0589  0.1041  84  PRO C CG  
2871 C CD  . PRO C 67  ? 0.6603 0.6452 0.5419 0.0644  0.0532  0.1020  84  PRO C CD  
2872 N N   . GLY C 68  ? 0.5037 0.4902 0.3894 0.0566  0.0494  0.1024  85  GLY C N   
2873 C CA  . GLY C 68  ? 0.4904 0.4792 0.3779 0.0542  0.0473  0.1026  85  GLY C CA  
2874 C C   . GLY C 68  ? 0.5225 0.5117 0.4134 0.0495  0.0421  0.0999  85  GLY C C   
2875 O O   . GLY C 68  ? 0.4743 0.4620 0.3665 0.0460  0.0411  0.0997  85  GLY C O   
2876 N N   . LEU C 69  ? 0.4151 0.4063 0.3075 0.0493  0.0388  0.0979  86  LEU C N   
2877 C CA  . LEU C 69  ? 0.4994 0.4904 0.3950 0.0447  0.0340  0.0952  86  LEU C CA  
2878 C C   . LEU C 69  ? 0.4211 0.4049 0.3169 0.0407  0.0354  0.0944  86  LEU C C   
2879 O O   . LEU C 69  ? 0.3591 0.3417 0.2570 0.0365  0.0331  0.0934  86  LEU C O   
2880 C CB  . LEU C 69  ? 0.4763 0.4704 0.3731 0.0456  0.0306  0.0933  86  LEU C CB  
2881 C CG  . LEU C 69  ? 0.4664 0.4600 0.3663 0.0411  0.0258  0.0903  86  LEU C CG  
2882 C CD1 . LEU C 69  ? 0.4894 0.4861 0.3920 0.0380  0.0220  0.0897  86  LEU C CD1 
2883 C CD2 . LEU C 69  ? 0.5098 0.5070 0.4105 0.0428  0.0228  0.0887  86  LEU C CD2 
2884 N N   . ILE C 70  ? 0.4386 0.4173 0.3321 0.0419  0.0393  0.0950  87  ILE C N   
2885 C CA  A ILE C 70  ? 0.3937 0.3653 0.2872 0.0383  0.0410  0.0944  87  ILE C CA  
2886 C CA  B ILE C 70  ? 0.3944 0.3660 0.2879 0.0383  0.0410  0.0944  87  ILE C CA  
2887 C C   . ILE C 70  ? 0.4227 0.3919 0.3157 0.0366  0.0432  0.0959  87  ILE C C   
2888 O O   . ILE C 70  ? 0.4165 0.3819 0.3110 0.0323  0.0422  0.0949  87  ILE C O   
2889 C CB  A ILE C 70  ? 0.4302 0.3971 0.3212 0.0404  0.0450  0.0948  87  ILE C CB  
2890 C CB  B ILE C 70  ? 0.4303 0.3972 0.3212 0.0405  0.0451  0.0949  87  ILE C CB  
2891 C CG1 A ILE C 70  ? 0.4611 0.4295 0.3532 0.0407  0.0421  0.0927  87  ILE C CG1 
2892 C CG1 B ILE C 70  ? 0.4568 0.4264 0.3481 0.0424  0.0429  0.0935  87  ILE C CG1 
2893 C CG2 A ILE C 70  ? 0.4511 0.4105 0.3415 0.0371  0.0477  0.0948  87  ILE C CG2 
2894 C CG2 B ILE C 70  ? 0.4492 0.4088 0.3402 0.0366  0.0465  0.0941  87  ILE C CG2 
2895 C CD1 A ILE C 70  ? 0.4498 0.4146 0.3393 0.0434  0.0457  0.0932  87  ILE C CD1 
2896 C CD1 B ILE C 70  ? 0.4123 0.3819 0.3067 0.0385  0.0381  0.0905  87  ILE C CD1 
2897 N N   . GLU C 71  ? 0.4211 0.3924 0.3121 0.0400  0.0462  0.0984  88  GLU C N   
2898 C CA  . GLU C 71  ? 0.5151 0.4842 0.4055 0.0386  0.0484  0.1000  88  GLU C CA  
2899 C C   . GLU C 71  ? 0.4509 0.4231 0.3444 0.0351  0.0441  0.0989  88  GLU C C   
2900 O O   . GLU C 71  ? 0.4518 0.4201 0.3461 0.0313  0.0441  0.0985  88  GLU C O   
2901 C CB  . GLU C 71  ? 0.6163 0.5874 0.5039 0.0432  0.0524  0.1028  88  GLU C CB  
2902 C CG  . GLU C 71  ? 1.0521 1.0179 0.9365 0.0455  0.0580  0.1044  88  GLU C CG  
2903 C CD  . GLU C 71  ? 1.3836 1.3518 1.2652 0.0506  0.0617  0.1071  88  GLU C CD  
2904 O OE1 . GLU C 71  ? 1.3566 1.3295 1.2385 0.0518  0.0608  0.1082  88  GLU C OE1 
2905 O OE2 . GLU C 71  ? 1.3402 1.3055 1.2192 0.0534  0.0656  0.1081  88  GLU C OE2 
2906 N N   . LYS C 72  ? 0.4334 0.4122 0.3284 0.0363  0.0402  0.0982  89  LYS C N   
2907 C CA  . LYS C 72  ? 0.4016 0.3836 0.2997 0.0330  0.0358  0.0971  89  LYS C CA  
2908 C C   . LYS C 72  ? 0.3244 0.3028 0.2249 0.0279  0.0328  0.0945  89  LYS C C   
2909 O O   . LYS C 72  ? 0.3627 0.3409 0.2652 0.0242  0.0306  0.0939  89  LYS C O   
2910 C CB  . LYS C 72  ? 0.4869 0.4766 0.3864 0.0350  0.0318  0.0965  89  LYS C CB  
2911 C CG  . LYS C 72  ? 0.7453 0.7395 0.6426 0.0401  0.0340  0.0988  89  LYS C CG  
2912 C CD  . LYS C 72  ? 0.6655 0.6621 0.5629 0.0401  0.0344  0.1004  89  LYS C CD  
2913 C CE  . LYS C 72  ? 0.8207 0.8204 0.7154 0.0453  0.0378  0.1030  89  LYS C CE  
2914 N NZ  . LYS C 72  ? 1.0796 1.0776 0.9730 0.0454  0.0411  0.1053  89  LYS C NZ  
2915 N N   . MET C 73  ? 0.3721 0.3478 0.2725 0.0276  0.0327  0.0931  90  MET C N   
2916 C CA  . MET C 73  ? 0.3690 0.3419 0.2718 0.0231  0.0294  0.0905  90  MET C CA  
2917 C C   . MET C 73  ? 0.3445 0.3097 0.2466 0.0202  0.0324  0.0905  90  MET C C   
2918 O O   . MET C 73  ? 0.3462 0.3085 0.2502 0.0161  0.0300  0.0884  90  MET C O   
2919 C CB  . MET C 73  ? 0.3513 0.3258 0.2547 0.0243  0.0272  0.0887  90  MET C CB  
2920 C CG  . MET C 73  ? 0.3480 0.3299 0.2532 0.0255  0.0227  0.0878  90  MET C CG  
2921 S SD  . MET C 73  ? 0.3738 0.3578 0.2830 0.0203  0.0169  0.0856  90  MET C SD  
2922 C CE  . MET C 73  ? 0.3930 0.3723 0.3039 0.0164  0.0148  0.0827  90  MET C CE  
2923 N N   . THR C 74  ? 0.3821 0.3438 0.2813 0.0222  0.0377  0.0928  91  THR C N   
2924 C CA  . THR C 74  ? 0.3866 0.3409 0.2848 0.0196  0.0408  0.0930  91  THR C CA  
2925 C C   . THR C 74  ? 0.3693 0.3228 0.2689 0.0161  0.0399  0.0932  91  THR C C   
2926 O O   . THR C 74  ? 0.4612 0.4155 0.3595 0.0175  0.0423  0.0953  91  THR C O   
2927 C CB  . THR C 74  ? 0.4838 0.4349 0.3784 0.0233  0.0467  0.0953  91  THR C CB  
2928 O OG1 . THR C 74  ? 0.4649 0.4171 0.3583 0.0265  0.0472  0.0950  91  THR C OG1 
2929 C CG2 . THR C 74  ? 0.4495 0.3929 0.3431 0.0206  0.0498  0.0955  91  THR C CG2 
2930 N N   . GLY C 75  ? 0.3464 0.2983 0.2487 0.0114  0.0364  0.0910  92  GLY C N   
2931 C CA  . GLY C 75  ? 0.3374 0.2889 0.2415 0.0077  0.0347  0.0907  92  GLY C CA  
2932 C C   . GLY C 75  ? 0.3683 0.3194 0.2757 0.0031  0.0299  0.0879  92  GLY C C   
2933 O O   . GLY C 75  ? 0.3123 0.2628 0.2202 0.0029  0.0283  0.0862  92  GLY C O   
2934 N N   . PRO C 76  ? 0.2124 0.3101 0.2270 -0.0586 0.0132  0.0397  93  PRO C N   
2935 C CA  . PRO C 76  ? 0.2112 0.3185 0.2313 -0.0546 0.0135  0.0387  93  PRO C CA  
2936 C C   . PRO C 76  ? 0.2018 0.3111 0.2244 -0.0492 0.0132  0.0376  93  PRO C C   
2937 O O   . PRO C 76  ? 0.1884 0.2892 0.2107 -0.0465 0.0121  0.0374  93  PRO C O   
2938 C CB  . PRO C 76  ? 0.2246 0.3268 0.2480 -0.0525 0.0129  0.0386  93  PRO C CB  
2939 C CG  . PRO C 76  ? 0.2288 0.3176 0.2494 -0.0530 0.0117  0.0391  93  PRO C CG  
2940 C CD  . PRO C 76  ? 0.2480 0.3348 0.2623 -0.0586 0.0122  0.0401  93  PRO C CD  
2941 N N   . VAL C 77  ? 0.1927 0.3136 0.2177 -0.0477 0.0141  0.0370  94  VAL C N   
2942 C CA  . VAL C 77  ? 0.1624 0.2867 0.1903 -0.0422 0.0138  0.0359  94  VAL C CA  
2943 C C   . VAL C 77  ? 0.1822 0.3168 0.2153 -0.0390 0.0146  0.0352  94  VAL C C   
2944 O O   . VAL C 77  ? 0.1837 0.3254 0.2171 -0.0418 0.0155  0.0356  94  VAL C O   
2945 C CB  . VAL C 77  ? 0.1636 0.2919 0.1881 -0.0435 0.0143  0.0360  94  VAL C CB  
2946 C CG1 . VAL C 77  ? 0.2266 0.3446 0.2459 -0.0462 0.0136  0.0367  94  VAL C CG1 
2947 C CG2 . VAL C 77  ? 0.1939 0.3337 0.2172 -0.0475 0.0158  0.0365  94  VAL C CG2 
2948 N N   . LEU C 78  ? 0.1616 0.2969 0.1986 -0.0330 0.0142  0.0341  95  LEU C N   
2949 C CA  . LEU C 78  ? 0.1636 0.3090 0.2052 -0.0294 0.0151  0.0333  95  LEU C CA  
2950 C C   . LEU C 78  ? 0.1613 0.3146 0.2027 -0.0275 0.0156  0.0327  95  LEU C C   
2951 O O   . LEU C 78  ? 0.1636 0.3131 0.2057 -0.0238 0.0149  0.0319  95  LEU C O   
2952 C CB  . LEU C 78  ? 0.1258 0.2670 0.1724 -0.0238 0.0145  0.0325  95  LEU C CB  
2953 C CG  . LEU C 78  ? 0.1567 0.3080 0.2076 -0.0205 0.0156  0.0320  95  LEU C CG  
2954 C CD1 . LEU C 78  ? 0.1678 0.3238 0.2185 -0.0241 0.0163  0.0328  95  LEU C CD1 
2955 C CD2 . LEU C 78  ? 0.1528 0.2997 0.2087 -0.0144 0.0152  0.0311  95  LEU C CD2 
2956 N N   . CYS C 79  ? 0.1491 0.3133 0.1895 -0.0301 0.0168  0.0330  96  CYS C N   
2957 C CA  . CYS C 79  ? 0.1390 0.3122 0.1794 -0.0284 0.0175  0.0325  96  CYS C CA  
2958 C C   . CYS C 79  ? 0.1702 0.3496 0.2159 -0.0224 0.0178  0.0315  96  CYS C C   
2959 O O   . CYS C 79  ? 0.1464 0.3300 0.1948 -0.0217 0.0184  0.0315  96  CYS C O   
2960 C CB  . CYS C 79  ? 0.1785 0.3616 0.2163 -0.0336 0.0188  0.0333  96  CYS C CB  
2961 S SG  . CYS C 79  ? 0.2027 0.3792 0.2346 -0.0413 0.0187  0.0347  96  CYS C SG  
2962 N N   . MET C 80  ? 0.1455 0.3259 0.1922 -0.0180 0.0176  0.0305  97  MET C N   
2963 C CA  . MET C 80  ? 0.1400 0.3252 0.1915 -0.0120 0.0180  0.0295  97  MET C CA  
2964 C C   . MET C 80  ? 0.1489 0.3421 0.2001 -0.0097 0.0185  0.0288  97  MET C C   
2965 O O   . MET C 80  ? 0.1501 0.3409 0.1981 -0.0109 0.0181  0.0289  97  MET C O   
2966 C CB  . MET C 80  ? 0.1638 0.3390 0.2184 -0.0074 0.0169  0.0286  97  MET C CB  
2967 C CG  . MET C 80  ? 0.1540 0.3188 0.2081 -0.0099 0.0161  0.0293  97  MET C CG  
2968 S SD  . MET C 80  ? 0.1475 0.3014 0.2060 -0.0043 0.0151  0.0283  97  MET C SD  
2969 C CE  . MET C 80  ? 0.1588 0.3059 0.2151 -0.0030 0.0138  0.0274  97  MET C CE  
2970 N N   . VAL C 81  ? 0.1140 0.3164 0.1685 -0.0061 0.0195  0.0283  98  VAL C N   
2971 C CA  . VAL C 81  ? 0.1162 0.3255 0.1713 -0.0023 0.0200  0.0275  98  VAL C CA  
2972 C C   . VAL C 81  ? 0.1097 0.3181 0.1697 0.0042  0.0200  0.0263  98  VAL C C   
2973 O O   . VAL C 81  ? 0.1193 0.3310 0.1823 0.0057  0.0207  0.0264  98  VAL C O   
2974 C CB  . VAL C 81  ? 0.1454 0.3683 0.1995 -0.0043 0.0214  0.0280  98  VAL C CB  
2975 C CG1 . VAL C 81  ? 0.1367 0.3661 0.1915 0.0002  0.0218  0.0271  98  VAL C CG1 
2976 C CG2 . VAL C 81  ? 0.1735 0.3970 0.2228 -0.0109 0.0215  0.0291  98  VAL C CG2 
2977 N N   . PHE C 82  ? 0.1232 0.3270 0.1840 0.0082  0.0192  0.0252  99  PHE C N   
2978 C CA  . PHE C 82  ? 0.1071 0.3100 0.1723 0.0146  0.0193  0.0240  99  PHE C CA  
2979 C C   . PHE C 82  ? 0.1054 0.3161 0.1708 0.0182  0.0199  0.0231  99  PHE C C   
2980 O O   . PHE C 82  ? 0.1243 0.3361 0.1864 0.0166  0.0195  0.0231  99  PHE C O   
2981 C CB  . PHE C 82  ? 0.1199 0.3100 0.1867 0.0169  0.0179  0.0231  99  PHE C CB  
2982 C CG  . PHE C 82  ? 0.1264 0.3091 0.1950 0.0160  0.0176  0.0236  99  PHE C CG  
2983 C CD1 . PHE C 82  ? 0.1496 0.3321 0.2228 0.0204  0.0183  0.0231  99  PHE C CD1 
2984 C CD2 . PHE C 82  ? 0.1457 0.3219 0.2114 0.0110  0.0169  0.0246  99  PHE C CD2 
2985 C CE1 . PHE C 82  ? 0.1266 0.3026 0.2016 0.0197  0.0181  0.0236  99  PHE C CE1 
2986 C CE2 . PHE C 82  ? 0.1465 0.3160 0.2139 0.0104  0.0166  0.0251  99  PHE C CE2 
2987 C CZ  . PHE C 82  ? 0.1389 0.3086 0.2110 0.0147  0.0172  0.0246  99  PHE C CZ  
2988 N N   . GLU C 83  ? 0.0929 0.3084 0.1620 0.0231  0.0208  0.0224  100 GLU C N   
2989 C CA  . GLU C 83  ? 0.0939 0.3123 0.1612 0.0265  0.0208  0.0212  100 GLU C CA  
2990 C C   . GLU C 83  ? 0.1417 0.3525 0.2117 0.0322  0.0203  0.0195  100 GLU C C   
2991 O O   . GLU C 83  ? 0.1322 0.3361 0.2045 0.0342  0.0202  0.0190  100 GLU C O   
2992 C CB  . GLU C 83  ? 0.1192 0.3421 0.1840 0.0261  0.0213  0.0213  100 GLU C CB  
2993 C CG  . GLU C 83  ? 0.1447 0.3705 0.2076 0.0297  0.0214  0.0202  100 GLU C CG  
2994 C CD  . GLU C 83  ? 0.1990 0.4292 0.2596 0.0294  0.0218  0.0204  100 GLU C CD  
2995 O OE1 . GLU C 83  ? 0.2105 0.4483 0.2684 0.0258  0.0220  0.0213  100 GLU C OE1 
2996 O OE2 . GLU C 83  ? 0.1950 0.4210 0.2567 0.0326  0.0218  0.0197  100 GLU C OE2 
2997 N N   . GLY C 84  ? 0.1332 0.3450 0.2024 0.0348  0.0199  0.0185  101 GLY C N   
2998 C CA  . GLY C 84  ? 0.1303 0.3347 0.2013 0.0399  0.0194  0.0167  101 GLY C CA  
2999 C C   . GLY C 84  ? 0.1120 0.3193 0.1816 0.0419  0.0190  0.0158  101 GLY C C   
3000 O O   . GLY C 84  ? 0.1418 0.3564 0.2091 0.0394  0.0191  0.0166  101 GLY C O   
3001 N N   . VAL C 85  ? 0.1223 0.3232 0.1931 0.0463  0.0185  0.0140  102 VAL C N   
3002 C CA  . VAL C 85  ? 0.1438 0.3459 0.2135 0.0488  0.0179  0.0128  102 VAL C CA  
3003 C C   . VAL C 85  ? 0.1217 0.3234 0.1926 0.0479  0.0170  0.0129  102 VAL C C   
3004 O O   . VAL C 85  ? 0.1406 0.3351 0.2147 0.0484  0.0162  0.0125  102 VAL C O   
3005 C CB  . VAL C 85  ? 0.1584 0.3524 0.2294 0.0533  0.0175  0.0107  102 VAL C CB  
3006 C CG1 . VAL C 85  ? 0.1949 0.3890 0.2650 0.0560  0.0167  0.0093  102 VAL C CG1 
3007 C CG2 . VAL C 85  ? 0.1802 0.3756 0.2496 0.0542  0.0185  0.0108  102 VAL C CG2 
3008 N N   . ASP C 86  ? 0.1277 0.3365 0.1959 0.0464  0.0170  0.0134  103 ASP C N   
3009 C CA  . ASP C 86  ? 0.1228 0.3238 0.1879 0.0442  0.0153  0.0131  103 ASP C CA  
3010 C C   . ASP C 86  ? 0.1222 0.3154 0.1865 0.0397  0.0146  0.0142  103 ASP C C   
3011 O O   . ASP C 86  ? 0.1117 0.2954 0.1753 0.0391  0.0130  0.0136  103 ASP C O   
3012 C CB  . ASP C 86  ? 0.1442 0.3383 0.2116 0.0491  0.0140  0.0108  103 ASP C CB  
3013 C CG  . ASP C 86  ? 0.2183 0.4061 0.2821 0.0479  0.0122  0.0102  103 ASP C CG  
3014 O OD1 . ASP C 86  ? 0.2266 0.4185 0.2857 0.0449  0.0123  0.0112  103 ASP C OD1 
3015 O OD2 . ASP C 86  ? 0.2061 0.3848 0.2721 0.0503  0.0108  0.0086  103 ASP C OD2 
3016 N N   . VAL C 87  ? 0.0949 0.2922 0.1594 0.0365  0.0157  0.0158  104 VAL C N   
3017 C CA  . VAL C 87  ? 0.1107 0.3003 0.1754 0.0330  0.0152  0.0167  104 VAL C CA  
3018 C C   . VAL C 87  ? 0.1161 0.3008 0.1759 0.0281  0.0141  0.0176  104 VAL C C   
3019 O O   . VAL C 87  ? 0.1130 0.2884 0.1726 0.0262  0.0131  0.0178  104 VAL C O   
3020 C CB  . VAL C 87  ? 0.1420 0.3372 0.2080 0.0309  0.0166  0.0181  104 VAL C CB  
3021 C CG1 . VAL C 87  ? 0.1353 0.3398 0.1974 0.0262  0.0176  0.0197  104 VAL C CG1 
3022 C CG2 . VAL C 87  ? 0.1412 0.3271 0.2086 0.0288  0.0159  0.0186  104 VAL C CG2 
3023 N N   . ILE C 88  ? 0.1274 0.3177 0.1830 0.0261  0.0144  0.0181  105 ILE C N   
3024 C CA  . ILE C 88  ? 0.1429 0.3281 0.1936 0.0217  0.0135  0.0190  105 ILE C CA  
3025 C C   . ILE C 88  ? 0.1258 0.3000 0.1766 0.0240  0.0116  0.0176  105 ILE C C   
3026 O O   . ILE C 88  ? 0.1257 0.2909 0.1757 0.0216  0.0107  0.0179  105 ILE C O   
3027 C CB  . ILE C 88  ? 0.1425 0.3360 0.1889 0.0197  0.0143  0.0198  105 ILE C CB  
3028 C CG1 . ILE C 88  ? 0.1304 0.3344 0.1767 0.0167  0.0161  0.0212  105 ILE C CG1 
3029 C CG2 . ILE C 88  ? 0.1326 0.3198 0.1740 0.0156  0.0135  0.0206  105 ILE C CG2 
3030 C CD1 . ILE C 88  ? 0.1499 0.3637 0.1929 0.0155  0.0172  0.0219  105 ILE C CD1 
3031 N N   . ALA C 89  ? 0.1257 0.3006 0.1776 0.0287  0.0111  0.0158  106 ALA C N   
3032 C CA  . ALA C 89  ? 0.1233 0.2884 0.1755 0.0311  0.0092  0.0142  106 ALA C CA  
3033 C C   . ALA C 89  ? 0.1065 0.2636 0.1635 0.0331  0.0085  0.0134  106 ALA C C   
3034 O O   . ALA C 89  ? 0.1263 0.2737 0.1830 0.0327  0.0071  0.0128  106 ALA C O   
3035 C CB  . ALA C 89  ? 0.1623 0.3305 0.2149 0.0359  0.0088  0.0124  106 ALA C CB  
3036 N N   . GLN C 90  ? 0.1265 0.2876 0.1880 0.0354  0.0097  0.0132  107 GLN C N   
3037 C CA  . GLN C 90  ? 0.1194 0.2730 0.1857 0.0376  0.0092  0.0124  107 GLN C CA  
3038 C C   . GLN C 90  ? 0.1016 0.2490 0.1669 0.0332  0.0090  0.0138  107 GLN C C   
3039 O O   . GLN C 90  ? 0.0971 0.2349 0.1642 0.0338  0.0078  0.0132  107 GLN C O   
3040 C CB  . GLN C 90  ? 0.1094 0.2689 0.1803 0.0412  0.0107  0.0120  107 GLN C CB  
3041 C CG  . GLN C 90  ? 0.1373 0.3005 0.2100 0.0465  0.0108  0.0101  107 GLN C CG  
3042 C CD  . GLN C 90  ? 0.1539 0.3080 0.2290 0.0499  0.0092  0.0079  107 GLN C CD  
3043 O OE1 . GLN C 90  ? 0.1379 0.2845 0.2167 0.0510  0.0088  0.0073  107 GLN C OE1 
3044 N NE2 . GLN C 90  ? 0.1879 0.3425 0.2608 0.0516  0.0082  0.0066  107 GLN C NE2 
3045 N N   . ALA C 91  ? 0.1042 0.2568 0.1667 0.0287  0.0100  0.0158  108 ALA C N   
3046 C CA  . ALA C 91  ? 0.1299 0.2763 0.1911 0.0244  0.0097  0.0172  108 ALA C CA  
3047 C C   . ALA C 91  ? 0.1252 0.2629 0.1826 0.0221  0.0081  0.0172  108 ALA C C   
3048 O O   . ALA C 91  ? 0.1313 0.2601 0.1891 0.0208  0.0072  0.0174  108 ALA C O   
3049 C CB  . ALA C 91  ? 0.1106 0.2646 0.1694 0.0198  0.0111  0.0192  108 ALA C CB  
3050 N N   . ARG C 92  ? 0.1299 0.2700 0.1833 0.0217  0.0077  0.0170  109 ARG C N   
3051 C CA  . ARG C 92  ? 0.1387 0.2707 0.1885 0.0202  0.0062  0.0168  109 ARG C CA  
3052 C C   . ARG C 92  ? 0.1252 0.2482 0.1784 0.0243  0.0046  0.0148  109 ARG C C   
3053 O O   . ARG C 92  ? 0.1475 0.2613 0.1995 0.0228  0.0033  0.0149  109 ARG C O   
3054 C CB  . ARG C 92  ? 0.1479 0.2847 0.1931 0.0198  0.0062  0.0168  109 ARG C CB  
3055 C CG  . ARG C 92  ? 0.1764 0.3206 0.2174 0.0150  0.0077  0.0189  109 ARG C CG  
3056 C CD  . ARG C 92  ? 0.2414 0.3795 0.2782 0.0095  0.0074  0.0205  109 ARG C CD  
3057 N NE  . ARG C 92  ? 0.3454 0.4781 0.3776 0.0091  0.0063  0.0203  109 ARG C NE  
3058 C CZ  . ARG C 92  ? 0.4899 0.6180 0.5169 0.0045  0.0062  0.0218  109 ARG C CZ  
3059 N NH1 . ARG C 92  ? 0.3611 0.4889 0.3869 -0.0002 0.0071  0.0235  109 ARG C NH1 
3060 N NH2 . ARG C 92  ? 0.5637 0.6875 0.5866 0.0048  0.0053  0.0214  109 ARG C NH2 
3061 N N   . LYS C 93  ? 0.1117 0.2373 0.1693 0.0294  0.0046  0.0130  110 LYS C N   
3062 C CA  . LYS C 93  ? 0.1065 0.2241 0.1681 0.0334  0.0032  0.0110  110 LYS C CA  
3063 C C   . LYS C 93  ? 0.1535 0.2643 0.2184 0.0327  0.0032  0.0114  110 LYS C C   
3064 O O   . LYS C 93  ? 0.1765 0.2781 0.2424 0.0332  0.0017  0.0106  110 LYS C O   
3065 C CB  . LYS C 93  ? 0.1291 0.2516 0.1947 0.0387  0.0036  0.0091  110 LYS C CB  
3066 C CG  . LYS C 93  ? 0.1766 0.2917 0.2467 0.0430  0.0023  0.0067  110 LYS C CG  
3067 C CD  . LYS C 93  ? 0.2596 0.3805 0.3326 0.0480  0.0028  0.0049  110 LYS C CD  
3068 C CE  . LYS C 93  ? 0.2789 0.3931 0.3570 0.0525  0.0017  0.0024  110 LYS C CE  
3069 N NZ  . LYS C 93  ? 0.2354 0.3552 0.3159 0.0573  0.0022  0.0006  110 LYS C NZ  
3070 N N   . MET C 94  ? 0.1226 0.2382 0.1895 0.0316  0.0047  0.0127  111 MET C N   
3071 C CA  . MET C 94  ? 0.1163 0.2261 0.1863 0.0311  0.0049  0.0132  111 MET C CA  
3072 C C   . MET C 94  ? 0.1441 0.2471 0.2102 0.0262  0.0041  0.0147  111 MET C C   
3073 O O   . MET C 94  ? 0.1356 0.2305 0.2038 0.0262  0.0035  0.0147  111 MET C O   
3074 C CB  . MET C 94  ? 0.1121 0.2296 0.1844 0.0310  0.0068  0.0143  111 MET C CB  
3075 C CG  . MET C 94  ? 0.1034 0.2263 0.1801 0.0362  0.0077  0.0129  111 MET C CG  
3076 S SD  . MET C 94  ? 0.1289 0.2632 0.2066 0.0359  0.0100  0.0143  111 MET C SD  
3077 C CE  . MET C 94  ? 0.1777 0.3058 0.2593 0.0357  0.0105  0.0150  111 MET C CE  
3078 N N   . MET C 95  ? 0.1342 0.2407 0.1947 0.0220  0.0043  0.0161  112 MET C N   
3079 C CA  . MET C 95  ? 0.1363 0.2363 0.1925 0.0173  0.0037  0.0176  112 MET C CA  
3080 C C   . MET C 95  ? 0.1598 0.2503 0.2148 0.0184  0.0017  0.0164  112 MET C C   
3081 O O   . MET C 95  ? 0.1393 0.2214 0.1935 0.0165  0.0009  0.0170  112 MET C O   
3082 C CB  . MET C 95  ? 0.1511 0.2573 0.2016 0.0128  0.0045  0.0192  112 MET C CB  
3083 C CG  . MET C 95  ? 0.1907 0.3047 0.2416 0.0102  0.0063  0.0207  112 MET C CG  
3084 S SD  . MET C 95  ? 0.2443 0.3667 0.2890 0.0055  0.0073  0.0223  112 MET C SD  
3085 C CE  . MET C 95  ? 0.3097 0.4226 0.3483 0.0022  0.0060  0.0229  112 MET C CE  
3086 N N   . GLY C 96  ? 0.1388 0.2305 0.1934 0.0214  0.0010  0.0148  113 GLY C N   
3087 C CA  . GLY C 96  ? 0.1547 0.2385 0.2077 0.0225  -0.0009 0.0136  113 GLY C CA  
3088 C C   . GLY C 96  ? 0.1490 0.2319 0.1949 0.0187  -0.0013 0.0148  113 GLY C C   
3089 O O   . GLY C 96  ? 0.1718 0.2594 0.2140 0.0146  0.0000  0.0168  113 GLY C O   
3090 N N   . SER C 97  ? 0.1795 0.2561 0.2236 0.0202  -0.0030 0.0136  114 SER C N   
3091 C CA  . SER C 97  ? 0.2197 0.2942 0.2569 0.0172  -0.0034 0.0146  114 SER C CA  
3092 C C   . SER C 97  ? 0.1769 0.2482 0.2101 0.0117  -0.0028 0.0171  114 SER C C   
3093 O O   . SER C 97  ? 0.1801 0.2470 0.2158 0.0106  -0.0027 0.0176  114 SER C O   
3094 C CB  . SER C 97  ? 0.2142 0.2805 0.2508 0.0198  -0.0056 0.0129  114 SER C CB  
3095 O OG  . SER C 97  ? 0.3280 0.3960 0.3691 0.0251  -0.0064 0.0103  114 SER C OG  
3096 N N   . THR C 98  ? 0.1655 0.2388 0.1924 0.0083  -0.0022 0.0185  115 THR C N   
3097 C CA  . THR C 98  ? 0.2240 0.2944 0.2462 0.0028  -0.0015 0.0208  115 THR C CA  
3098 C C   . THR C 98  ? 0.1861 0.2454 0.2081 0.0021  -0.0028 0.0209  115 THR C C   
3099 O O   . THR C 98  ? 0.1980 0.2545 0.2198 -0.0012 -0.0022 0.0224  115 THR C O   
3100 C CB  . THR C 98  ? 0.2696 0.3418 0.2848 0.0002  -0.0010 0.0219  115 THR C CB  
3101 O OG1 . THR C 98  ? 0.2940 0.3767 0.3095 0.0011  0.0001  0.0217  115 THR C OG1 
3102 C CG2 . THR C 98  ? 0.3030 0.3729 0.3133 -0.0058 0.0000  0.0244  115 THR C CG2 
3103 N N   . ARG C 99  ? 0.1867 0.2396 0.2085 0.0052  -0.0046 0.0193  116 ARG C N   
3104 C CA  . ARG C 99  ? 0.1951 0.2374 0.2169 0.0052  -0.0060 0.0192  116 ARG C CA  
3105 C C   . ARG C 99  ? 0.1926 0.2330 0.2219 0.0088  -0.0066 0.0176  116 ARG C C   
3106 O O   . ARG C 99  ? 0.1803 0.2222 0.2135 0.0134  -0.0074 0.0154  116 ARG C O   
3107 C CB  . ARG C 99  ? 0.2230 0.2599 0.2412 0.0070  -0.0076 0.0181  116 ARG C CB  
3108 C CG  . ARG C 99  ? 0.2612 0.2994 0.2716 0.0034  -0.0069 0.0198  116 ARG C CG  
3109 C CD  . ARG C 99  ? 0.3946 0.4285 0.4013 0.0058  -0.0084 0.0186  116 ARG C CD  
3110 N NE  . ARG C 99  ? 0.5803 0.6115 0.5792 0.0019  -0.0078 0.0206  116 ARG C NE  
3111 C CZ  . ARG C 99  ? 1.1323 1.1586 1.1263 0.0029  -0.0089 0.0202  116 ARG C CZ  
3112 N NH1 . ARG C 99  ? 1.2410 1.2652 1.2371 0.0078  -0.0108 0.0178  116 ARG C NH1 
3113 N NH2 . ARG C 99  ? 1.1352 1.1587 1.1220 -0.0010 -0.0081 0.0223  116 ARG C NH2 
3114 N N   . PRO C 100 ? 0.1754 0.2124 0.2069 0.0070  -0.0062 0.0186  117 PRO C N   
3115 C CA  . PRO C 100 ? 0.1685 0.2040 0.2073 0.0105  -0.0065 0.0172  117 PRO C CA  
3116 C C   . PRO C 100 ? 0.1500 0.1791 0.1916 0.0148  -0.0084 0.0149  117 PRO C C   
3117 O O   . PRO C 100 ? 0.1533 0.1838 0.2011 0.0188  -0.0087 0.0131  117 PRO C O   
3118 C CB  . PRO C 100 ? 0.1548 0.1855 0.1934 0.0071  -0.0060 0.0191  117 PRO C CB  
3119 C CG  . PRO C 100 ? 0.1455 0.1803 0.1786 0.0022  -0.0046 0.0213  117 PRO C CG  
3120 C CD  . PRO C 100 ? 0.1746 0.2097 0.2021 0.0018  -0.0052 0.0211  117 PRO C CD  
3121 N N   . GLY C 101 ? 0.1685 0.1908 0.2059 0.0141  -0.0099 0.0148  118 GLY C N   
3122 C CA  . GLY C 101 ? 0.2159 0.2323 0.2560 0.0182  -0.0118 0.0124  118 GLY C CA  
3123 C C   . GLY C 101 ? 0.2001 0.2215 0.2423 0.0223  -0.0124 0.0101  118 GLY C C   
3124 O O   . GLY C 101 ? 0.2070 0.2249 0.2535 0.0263  -0.0138 0.0077  118 GLY C O   
3125 N N   . GLU C 102 ? 0.1560 0.1853 0.1952 0.0215  -0.0114 0.0107  119 GLU C N   
3126 C CA  . GLU C 102 ? 0.1772 0.2122 0.2180 0.0253  -0.0117 0.0086  119 GLU C CA  
3127 C C   . GLU C 102 ? 0.2230 0.2656 0.2692 0.0272  -0.0104 0.0081  119 GLU C C   
3128 O O   . GLU C 102 ? 0.2010 0.2479 0.2497 0.0310  -0.0107 0.0062  119 GLU C O   
3129 C CB  . GLU C 102 ? 0.2126 0.2518 0.2465 0.0234  -0.0114 0.0096  119 GLU C CB  
3130 C CG  . GLU C 102 ? 0.2542 0.2861 0.2824 0.0221  -0.0127 0.0099  119 GLU C CG  
3131 C CD  . GLU C 102 ? 0.3568 0.3925 0.3777 0.0201  -0.0121 0.0111  119 GLU C CD  
3132 O OE1 . GLU C 102 ? 0.3620 0.4060 0.3820 0.0188  -0.0105 0.0121  119 GLU C OE1 
3133 O OE2 . GLU C 102 ? 0.4046 0.4348 0.4207 0.0199  -0.0133 0.0111  119 GLU C OE2 
3134 N N   . ALA C 103 ? 0.1780 0.2224 0.2260 0.0249  -0.0088 0.0098  120 ALA C N   
3135 C CA  . ALA C 103 ? 0.1513 0.2032 0.2041 0.0266  -0.0074 0.0096  120 ALA C CA  
3136 C C   . ALA C 103 ? 0.1601 0.2092 0.2201 0.0313  -0.0080 0.0073  120 ALA C C   
3137 O O   . ALA C 103 ? 0.1857 0.2267 0.2479 0.0321  -0.0092 0.0066  120 ALA C O   
3138 C CB  . ALA C 103 ? 0.1621 0.2165 0.2144 0.0228  -0.0057 0.0120  120 ALA C CB  
3139 N N   . ALA C 104 ? 0.1757 0.2316 0.2395 0.0343  -0.0071 0.0062  121 ALA C N   
3140 C CA  . ALA C 104 ? 0.2407 0.2945 0.3114 0.0389  -0.0075 0.0039  121 ALA C CA  
3141 C C   . ALA C 104 ? 0.2296 0.2801 0.3047 0.0385  -0.0066 0.0048  121 ALA C C   
3142 O O   . ALA C 104 ? 0.1683 0.2225 0.2425 0.0358  -0.0050 0.0069  121 ALA C O   
3143 C CB  . ALA C 104 ? 0.2569 0.3190 0.3300 0.0422  -0.0066 0.0027  121 ALA C CB  
3144 N N   . PRO C 105 ? 0.2435 0.2876 0.3238 0.0414  -0.0074 0.0031  122 PRO C N   
3145 C CA  . PRO C 105 ? 0.2628 0.3042 0.3478 0.0416  -0.0064 0.0038  122 PRO C CA  
3146 C C   . PRO C 105 ? 0.1470 0.1967 0.2346 0.0428  -0.0043 0.0044  122 PRO C C   
3147 O O   . PRO C 105 ? 0.1977 0.2534 0.2865 0.0455  -0.0038 0.0031  122 PRO C O   
3148 C CB  . PRO C 105 ? 0.3816 0.4162 0.4722 0.0454  -0.0076 0.0013  122 PRO C CB  
3149 C CG  . PRO C 105 ? 0.3384 0.3696 0.4257 0.0456  -0.0097 -0.0001 122 PRO C CG  
3150 C CD  . PRO C 105 ? 0.3350 0.3740 0.4173 0.0447  -0.0094 0.0004  122 PRO C CD  
3151 N N   . GLY C 106 ? 0.1694 0.2196 0.2577 0.0407  -0.0029 0.0064  123 GLY C N   
3152 C CA  . GLY C 106 ? 0.1817 0.2395 0.2720 0.0415  -0.0009 0.0072  123 GLY C CA  
3153 C C   . GLY C 106 ? 0.1685 0.2345 0.2537 0.0380  0.0001  0.0091  123 GLY C C   
3154 O O   . GLY C 106 ? 0.1857 0.2587 0.2722 0.0384  0.0018  0.0099  123 GLY C O   
3155 N N   . THR C 107 ? 0.1345 0.2001 0.2138 0.0349  -0.0009 0.0097  124 THR C N   
3156 C CA  . THR C 107 ? 0.0984 0.1709 0.1727 0.0309  0.0001  0.0117  124 THR C CA  
3157 C C   . THR C 107 ? 0.0971 0.1660 0.1691 0.0264  0.0005  0.0139  124 THR C C   
3158 O O   . THR C 107 ? 0.1230 0.1833 0.1960 0.0260  -0.0004 0.0140  124 THR C O   
3159 C CB  . THR C 107 ? 0.1104 0.1842 0.1792 0.0295  -0.0008 0.0115  124 THR C CB  
3160 O OG1 . THR C 107 ? 0.1310 0.1955 0.1971 0.0278  -0.0025 0.0115  124 THR C OG1 
3161 C CG2 . THR C 107 ? 0.1401 0.2175 0.2108 0.0339  -0.0013 0.0093  124 THR C CG2 
3162 N N   . ILE C 108 ? 0.1186 0.1944 0.1874 0.0230  0.0018  0.0157  125 ILE C N   
3163 C CA  . ILE C 108 ? 0.1252 0.1984 0.1916 0.0185  0.0022  0.0178  125 ILE C CA  
3164 C C   . ILE C 108 ? 0.1492 0.2138 0.2111 0.0156  0.0007  0.0183  125 ILE C C   
3165 O O   . ILE C 108 ? 0.1425 0.1996 0.2047 0.0142  0.0002  0.0190  125 ILE C O   
3166 C CB  . ILE C 108 ? 0.1105 0.1932 0.1739 0.0152  0.0037  0.0195  125 ILE C CB  
3167 C CG1 . ILE C 108 ? 0.1216 0.2120 0.1896 0.0181  0.0052  0.0192  125 ILE C CG1 
3168 C CG2 . ILE C 108 ? 0.1315 0.2111 0.1917 0.0101  0.0040  0.0215  125 ILE C CG2 
3169 C CD1 . ILE C 108 ? 0.1340 0.2352 0.1993 0.0156  0.0066  0.0203  125 ILE C CD1 
3170 N N   . ARG C 109 ? 0.1157 0.1814 0.1731 0.0145  0.0000  0.0181  126 ARG C N   
3171 C CA  . ARG C 109 ? 0.1306 0.1885 0.1831 0.0114  -0.0012 0.0188  126 ARG C CA  
3172 C C   . ARG C 109 ? 0.1248 0.1729 0.1799 0.0142  -0.0028 0.0174  126 ARG C C   
3173 O O   . ARG C 109 ? 0.1312 0.1715 0.1845 0.0120  -0.0035 0.0183  126 ARG C O   
3174 C CB  . ARG C 109 ? 0.1403 0.2017 0.1872 0.0099  -0.0014 0.0190  126 ARG C CB  
3175 C CG  . ARG C 109 ? 0.1833 0.2528 0.2269 0.0057  0.0003  0.0209  126 ARG C CG  
3176 C CD  . ARG C 109 ? 0.2177 0.2926 0.2568 0.0048  0.0006  0.0210  126 ARG C CD  
3177 N NE  . ARG C 109 ? 0.1840 0.2663 0.2199 0.0004  0.0022  0.0228  126 ARG C NE  
3178 C CZ  . ARG C 109 ? 0.2139 0.3023 0.2459 -0.0009 0.0028  0.0232  126 ARG C CZ  
3179 N NH1 . ARG C 109 ? 0.2502 0.3391 0.2816 0.0022  0.0020  0.0218  126 ARG C NH1 
3180 N NH2 . ARG C 109 ? 0.2308 0.3247 0.2596 -0.0055 0.0043  0.0250  126 ARG C NH2 
3181 N N   . ALA C 110 ? 0.1273 0.1756 0.1870 0.0191  -0.0035 0.0152  127 ALA C N   
3182 C CA  . ALA C 110 ? 0.1300 0.1695 0.1930 0.0219  -0.0050 0.0136  127 ALA C CA  
3183 C C   . ALA C 110 ? 0.1383 0.1733 0.2055 0.0221  -0.0045 0.0142  127 ALA C C   
3184 O O   . ALA C 110 ? 0.1668 0.1930 0.2347 0.0222  -0.0057 0.0140  127 ALA C O   
3185 C CB  . ALA C 110 ? 0.1610 0.2022 0.2283 0.0271  -0.0057 0.0110  127 ALA C CB  
3186 N N   . ASP C 111 ? 0.1149 0.1556 0.1851 0.0224  -0.0029 0.0149  128 ASP C N   
3187 C CA  . ASP C 111 ? 0.1093 0.1458 0.1840 0.0233  -0.0024 0.0153  128 ASP C CA  
3188 C C   . ASP C 111 ? 0.1523 0.1852 0.2236 0.0187  -0.0021 0.0176  128 ASP C C   
3189 O O   . ASP C 111 ? 0.1358 0.1625 0.2099 0.0192  -0.0022 0.0179  128 ASP C O   
3190 C CB  . ASP C 111 ? 0.1379 0.1817 0.2173 0.0258  -0.0006 0.0152  128 ASP C CB  
3191 C CG  . ASP C 111 ? 0.2282 0.2742 0.3124 0.0309  -0.0007 0.0128  128 ASP C CG  
3192 O OD1 . ASP C 111 ? 0.2432 0.2839 0.3284 0.0330  -0.0022 0.0110  128 ASP C OD1 
3193 O OD2 . ASP C 111 ? 0.2145 0.2677 0.3014 0.0330  0.0008  0.0126  128 ASP C OD2 
3194 N N   . PHE C 112 ? 0.1101 0.1466 0.1754 0.0144  -0.0017 0.0192  129 PHE C N   
3195 C CA  . PHE C 112 ? 0.1269 0.1611 0.1887 0.0098  -0.0012 0.0214  129 PHE C CA  
3196 C C   . PHE C 112 ? 0.1413 0.1698 0.1967 0.0059  -0.0022 0.0224  129 PHE C C   
3197 O O   . PHE C 112 ? 0.1391 0.1634 0.1919 0.0025  -0.0021 0.0240  129 PHE C O   
3198 C CB  . PHE C 112 ? 0.1195 0.1633 0.1798 0.0072  0.0005  0.0227  129 PHE C CB  
3199 C CG  . PHE C 112 ? 0.1265 0.1756 0.1922 0.0099  0.0019  0.0226  129 PHE C CG  
3200 C CD1 . PHE C 112 ? 0.1363 0.1927 0.2054 0.0136  0.0025  0.0212  129 PHE C CD1 
3201 C CD2 . PHE C 112 ? 0.1675 0.2147 0.2346 0.0086  0.0026  0.0238  129 PHE C CD2 
3202 C CE1 . PHE C 112 ? 0.1705 0.2321 0.2442 0.0161  0.0039  0.0211  129 PHE C CE1 
3203 C CE2 . PHE C 112 ? 0.1750 0.2275 0.2469 0.0112  0.0039  0.0237  129 PHE C CE2 
3204 C CZ  . PHE C 112 ? 0.1696 0.2293 0.2447 0.0149  0.0046  0.0224  129 PHE C CZ  
3205 N N   . CYS C 113 ? 0.1372 0.1657 0.1894 0.0062  -0.0031 0.0215  130 CYS C N   
3206 C CA  . CYS C 113 ? 0.1425 0.1680 0.1876 0.0021  -0.0036 0.0228  130 CYS C CA  
3207 C C   . CYS C 113 ? 0.1467 0.1646 0.1900 0.0036  -0.0054 0.0217  130 CYS C C   
3208 O O   . CYS C 113 ? 0.1538 0.1697 0.2013 0.0080  -0.0064 0.0196  130 CYS C O   
3209 C CB  . CYS C 113 ? 0.1362 0.1707 0.1775 -0.0003 -0.0025 0.0235  130 CYS C CB  
3210 S SG  . CYS C 113 ? 0.1588 0.2029 0.2017 -0.0025 -0.0003 0.0249  130 CYS C SG  
3211 N N   . GLN C 114 ? 0.1646 0.1783 0.2014 -0.0001 -0.0058 0.0230  131 GLN C N   
3212 C CA  . GLN C 114 ? 0.1690 0.1752 0.2027 0.0007  -0.0074 0.0223  131 GLN C CA  
3213 C C   . GLN C 114 ? 0.1553 0.1639 0.1826 -0.0012 -0.0074 0.0227  131 GLN C C   
3214 O O   . GLN C 114 ? 0.2024 0.2087 0.2286 0.0014  -0.0087 0.0213  131 GLN C O   
3215 C CB  . GLN C 114 ? 0.1828 0.1793 0.2143 -0.0016 -0.0080 0.0235  131 GLN C CB  
3216 C CG  . GLN C 114 ? 0.1630 0.1553 0.2007 0.0008  -0.0083 0.0230  131 GLN C CG  
3217 C CD  . GLN C 114 ? 0.1815 0.1639 0.2171 -0.0010 -0.0091 0.0240  131 GLN C CD  
3218 O OE1 . GLN C 114 ? 0.1863 0.1624 0.2178 -0.0014 -0.0103 0.0240  131 GLN C OE1 
3219 N NE2 . GLN C 114 ? 0.1658 0.1467 0.2042 -0.0019 -0.0083 0.0250  131 GLN C NE2 
3220 N N   . GLN C 115 ? 0.2009 0.2138 0.2237 -0.0057 -0.0060 0.0247  132 GLN C N   
3221 C CA  . GLN C 115 ? 0.1900 0.2041 0.2060 -0.0082 -0.0057 0.0255  132 GLN C CA  
3222 C C   . GLN C 115 ? 0.1650 0.1897 0.1801 -0.0101 -0.0040 0.0262  132 GLN C C   
3223 O O   . GLN C 115 ? 0.1978 0.2276 0.2155 -0.0116 -0.0027 0.0269  132 GLN C O   
3224 C CB  . GLN C 115 ? 0.2397 0.2462 0.2494 -0.0126 -0.0057 0.0274  132 GLN C CB  
3225 C CG  . GLN C 115 ? 0.2692 0.2650 0.2792 -0.0108 -0.0074 0.0268  132 GLN C CG  
3226 C CD  . GLN C 115 ? 0.2574 0.2456 0.2604 -0.0148 -0.0074 0.0286  132 GLN C CD  
3227 O OE1 . GLN C 115 ? 0.2932 0.2795 0.2946 -0.0185 -0.0065 0.0304  132 GLN C OE1 
3228 N NE2 . GLN C 115 ? 0.3452 0.3288 0.3436 -0.0138 -0.0085 0.0282  132 GLN C NE2 
3229 N N   . ALA C 116 ? 0.2288 0.2569 0.2399 -0.0101 -0.0039 0.0260  133 ALA C N   
3230 C CA  . ALA C 116 ? 0.2302 0.2686 0.2402 -0.0117 -0.0023 0.0266  133 ALA C CA  
3231 C C   . ALA C 116 ? 0.2203 0.2611 0.2273 -0.0173 -0.0006 0.0289  133 ALA C C   
3232 O O   . ALA C 116 ? 0.2414 0.2911 0.2505 -0.0184 0.0008  0.0293  133 ALA C O   
3233 C CB  . ALA C 116 ? 0.2127 0.2527 0.2178 -0.0112 -0.0024 0.0264  133 ALA C CB  
3234 N N   . GLY C 117 ? 0.2547 0.2878 0.2569 -0.0210 -0.0007 0.0304  134 GLY C N   
3235 C CA  . GLY C 117 ? 0.2796 0.3146 0.2788 -0.0266 0.0009  0.0324  134 GLY C CA  
3236 C C   . GLY C 117 ? 0.2427 0.2799 0.2467 -0.0272 0.0015  0.0327  134 GLY C C   
3237 O O   . GLY C 117 ? 0.2475 0.2886 0.2500 -0.0315 0.0029  0.0341  134 GLY C O   
3238 N N   . ARG C 118 ? 0.2075 0.2419 0.2172 -0.0230 0.0004  0.0313  135 ARG C N   
3239 C CA  . ARG C 118 ? 0.1820 0.2190 0.1969 -0.0228 0.0009  0.0314  135 ARG C CA  
3240 C C   . ARG C 118 ? 0.1823 0.2239 0.2039 -0.0171 0.0005  0.0294  135 ARG C C   
3241 O O   . ARG C 118 ? 0.1728 0.2091 0.1987 -0.0138 -0.0005 0.0284  135 ARG C O   
3242 C CB  . ARG C 118 ? 0.2076 0.2346 0.2225 -0.0238 0.0002  0.0320  135 ARG C CB  
3243 C CG  . ARG C 118 ? 0.2160 0.2389 0.2247 -0.0296 0.0008  0.0341  135 ARG C CG  
3244 C CD  . ARG C 118 ? 0.2141 0.2453 0.2224 -0.0334 0.0026  0.0352  135 ARG C CD  
3245 N NE  . ARG C 118 ? 0.2526 0.2794 0.2561 -0.0388 0.0032  0.0370  135 ARG C NE  
3246 C CZ  . ARG C 118 ? 0.2760 0.3090 0.2780 -0.0432 0.0047  0.0381  135 ARG C CZ  
3247 N NH1 . ARG C 118 ? 0.2752 0.3193 0.2796 -0.0429 0.0057  0.0377  135 ARG C NH1 
3248 N NH2 . ARG C 118 ? 0.3074 0.3354 0.3053 -0.0479 0.0051  0.0396  135 ARG C NH2 
3249 N N   . ASN C 119 ? 0.1771 0.2287 0.1998 -0.0163 0.0015  0.0290  136 ASN C N   
3250 C CA  . ASN C 119 ? 0.1353 0.1914 0.1636 -0.0109 0.0011  0.0271  136 ASN C CA  
3251 C C   . ASN C 119 ? 0.1634 0.2291 0.1957 -0.0104 0.0026  0.0272  136 ASN C C   
3252 O O   . ASN C 119 ? 0.1522 0.2245 0.1877 -0.0068 0.0029  0.0259  136 ASN C O   
3253 C CB  . ASN C 119 ? 0.1369 0.1954 0.1631 -0.0088 0.0006  0.0260  136 ASN C CB  
3254 C CG  . ASN C 119 ? 0.1885 0.2554 0.2107 -0.0118 0.0020  0.0270  136 ASN C CG  
3255 O OD1 . ASN C 119 ? 0.1730 0.2446 0.1940 -0.0156 0.0034  0.0285  136 ASN C OD1 
3256 N ND2 . ASN C 119 ? 0.2121 0.2812 0.2321 -0.0100 0.0016  0.0262  136 ASN C ND2 
3257 N N   . LEU C 120 ? 0.1366 0.2028 0.1687 -0.0139 0.0035  0.0286  137 LEU C N   
3258 C CA  . LEU C 120 ? 0.1457 0.2177 0.1822 -0.0132 0.0045  0.0287  137 LEU C CA  
3259 C C   . LEU C 120 ? 0.1385 0.2229 0.1757 -0.0136 0.0060  0.0288  137 LEU C C   
3260 O O   . LEU C 120 ? 0.1723 0.2617 0.2106 -0.0155 0.0071  0.0297  137 LEU C O   
3261 C CB  . LEU C 120 ? 0.1597 0.2294 0.2026 -0.0075 0.0039  0.0271  137 LEU C CB  
3262 C CG  . LEU C 120 ? 0.1538 0.2220 0.2008 -0.0069 0.0044  0.0275  137 LEU C CG  
3263 C CD1 . LEU C 120 ? 0.1538 0.2112 0.1986 -0.0093 0.0034  0.0284  137 LEU C CD1 
3264 C CD2 . LEU C 120 ? 0.1698 0.2384 0.2235 -0.0010 0.0043  0.0259  137 LEU C CD2 
3265 N N   . ILE C 121 ? 0.1331 0.2226 0.1690 -0.0122 0.0061  0.0281  138 ILE C N   
3266 C CA  . ILE C 121 ? 0.1515 0.2530 0.1892 -0.0112 0.0074  0.0279  138 ILE C CA  
3267 C C   . ILE C 121 ? 0.1604 0.2662 0.1944 -0.0117 0.0076  0.0278  138 ILE C C   
3268 O O   . ILE C 121 ? 0.1564 0.2565 0.1883 -0.0104 0.0064  0.0271  138 ILE C O   
3269 C CB  . ILE C 121 ? 0.1289 0.2329 0.1731 -0.0054 0.0074  0.0264  138 ILE C CB  
3270 C CG1 . ILE C 121 ? 0.1807 0.2972 0.2267 -0.0043 0.0089  0.0262  138 ILE C CG1 
3271 C CG2 . ILE C 121 ? 0.1817 0.2801 0.2274 -0.0009 0.0060  0.0246  138 ILE C CG2 
3272 C CD1 . ILE C 121 ? 0.1724 0.2913 0.2247 0.0008  0.0092  0.0251  138 ILE C CD1 
3273 N N   . HIS C 122 ? 0.1445 0.2605 0.1772 -0.0139 0.0090  0.0284  139 HIS C N   
3274 C CA  . HIS C 122 ? 0.1656 0.2882 0.1956 -0.0140 0.0095  0.0284  139 HIS C CA  
3275 C C   . HIS C 122 ? 0.1555 0.2883 0.1897 -0.0100 0.0103  0.0273  139 HIS C C   
3276 O O   . HIS C 122 ? 0.1413 0.2792 0.1788 -0.0097 0.0112  0.0275  139 HIS C O   
3277 C CB  . HIS C 122 ? 0.1806 0.3076 0.2056 -0.0201 0.0108  0.0301  139 HIS C CB  
3278 C CG  . HIS C 122 ? 0.1770 0.3138 0.2004 -0.0200 0.0118  0.0301  139 HIS C CG  
3279 N ND1 . HIS C 122 ? 0.2618 0.3970 0.2811 -0.0200 0.0115  0.0301  139 HIS C ND1 
3280 C CD2 . HIS C 122 ? 0.1896 0.3380 0.2151 -0.0194 0.0132  0.0300  139 HIS C CD2 
3281 C CE1 . HIS C 122 ? 0.2227 0.3680 0.2416 -0.0196 0.0126  0.0300  139 HIS C CE1 
3282 N NE2 . HIS C 122 ? 0.1979 0.3514 0.2206 -0.0193 0.0136  0.0300  139 HIS C NE2 
3283 N N   . GLY C 123 ? 0.1705 0.3063 0.2042 -0.0070 0.0101  0.0263  140 GLY C N   
3284 C CA  . GLY C 123 ? 0.1512 0.2976 0.1877 -0.0038 0.0111  0.0256  140 GLY C CA  
3285 C C   . GLY C 123 ? 0.1489 0.3010 0.1816 -0.0043 0.0115  0.0257  140 GLY C C   
3286 O O   . GLY C 123 ? 0.1554 0.3019 0.1846 -0.0044 0.0106  0.0255  140 GLY C O   
3287 N N   . SER C 124 ? 0.1383 0.3018 0.1717 -0.0043 0.0129  0.0260  141 SER C N   
3288 C CA  . SER C 124 ? 0.1263 0.2965 0.1565 -0.0044 0.0136  0.0261  141 SER C CA  
3289 C C   . SER C 124 ? 0.1214 0.2881 0.1521 0.0007  0.0123  0.0244  141 SER C C   
3290 O O   . SER C 124 ? 0.1626 0.3270 0.1977 0.0054  0.0116  0.0229  141 SER C O   
3291 C CB  . SER C 124 ? 0.1389 0.3221 0.1711 -0.0039 0.0152  0.0263  141 SER C CB  
3292 O OG  . SER C 124 ? 0.1559 0.3430 0.1884 -0.0082 0.0163  0.0276  141 SER C OG  
3293 N N   . ASP C 125 ? 0.1487 0.3151 0.1748 -0.0002 0.0121  0.0246  142 ASP C N   
3294 C CA  . ASP C 125 ? 0.1783 0.3410 0.2046 0.0046  0.0108  0.0229  142 ASP C CA  
3295 C C   . ASP C 125 ? 0.1603 0.3325 0.1868 0.0078  0.0115  0.0222  142 ASP C C   
3296 O O   . ASP C 125 ? 0.1984 0.3682 0.2251 0.0122  0.0104  0.0206  142 ASP C O   
3297 C CB  . ASP C 125 ? 0.2921 0.4456 0.3134 0.0028  0.0096  0.0233  142 ASP C CB  
3298 C CG  . ASP C 125 ? 0.3105 0.4675 0.3258 -0.0018 0.0108  0.0250  142 ASP C CG  
3299 O OD1 . ASP C 125 ? 0.2494 0.4165 0.2642 -0.0031 0.0124  0.0258  142 ASP C OD1 
3300 O OD2 . ASP C 125 ? 0.3695 0.5187 0.3804 -0.0040 0.0101  0.0256  142 ASP C OD2 
3301 N N   . SER C 126 ? 0.1515 0.3344 0.1780 0.0061  0.0132  0.0232  143 SER C N   
3302 C CA  . SER C 126 ? 0.1363 0.3287 0.1627 0.0090  0.0140  0.0227  143 SER C CA  
3303 C C   . SER C 126 ? 0.1393 0.3430 0.1676 0.0075  0.0159  0.0237  143 SER C C   
3304 O O   . SER C 126 ? 0.1457 0.3501 0.1743 0.0034  0.0166  0.0249  143 SER C O   
3305 C CB  . SER C 126 ? 0.1759 0.3689 0.1965 0.0072  0.0142  0.0235  143 SER C CB  
3306 O OG  . SER C 126 ? 0.1686 0.3659 0.1859 0.0012  0.0157  0.0255  143 SER C OG  
3307 N N   . ALA C 127 ? 0.1257 0.3507 0.1932 -0.0081 0.0205  0.0069  144 ALA C N   
3308 C CA  . ALA C 127 ? 0.1156 0.3521 0.1845 -0.0058 0.0204  0.0052  144 ALA C CA  
3309 C C   . ALA C 127 ? 0.1430 0.3872 0.2107 -0.0113 0.0201  0.0045  144 ALA C C   
3310 O O   . ALA C 127 ? 0.1332 0.3827 0.2014 -0.0111 0.0192  0.0042  144 ALA C O   
3311 C CB  . ALA C 127 ? 0.1708 0.4145 0.2410 -0.0016 0.0220  0.0031  144 ALA C CB  
3312 N N   . GLU C 128 ? 0.1252 0.3700 0.1911 -0.0163 0.0207  0.0044  145 GLU C N   
3313 C CA  . GLU C 128 ? 0.1341 0.3861 0.1985 -0.0217 0.0204  0.0038  145 GLU C CA  
3314 C C   . GLU C 128 ? 0.1270 0.3730 0.1899 -0.0248 0.0186  0.0055  145 GLU C C   
3315 O O   . GLU C 128 ? 0.1333 0.3859 0.1959 -0.0265 0.0180  0.0049  145 GLU C O   
3316 C CB  . GLU C 128 ? 0.1586 0.4112 0.2209 -0.0265 0.0213  0.0035  145 GLU C CB  
3317 C CG  . GLU C 128 ? 0.1986 0.4591 0.2589 -0.0322 0.0209  0.0027  145 GLU C CG  
3318 C CD  . GLU C 128 ? 0.2551 0.5170 0.3131 -0.0370 0.0217  0.0022  145 GLU C CD  
3319 O OE1 . GLU C 128 ? 0.2330 0.5012 0.2921 -0.0354 0.0233  0.0006  145 GLU C OE1 
3320 O OE2 . GLU C 128 ? 0.2907 0.5474 0.3455 -0.0425 0.0208  0.0034  145 GLU C OE2 
3321 N N   . SER C 129 ? 0.1108 0.3442 0.1726 -0.0257 0.0179  0.0076  146 SER C N   
3322 C CA  A SER C 129 ? 0.1096 0.3368 0.1697 -0.0285 0.0163  0.0092  146 SER C CA  
3323 C CA  B SER C 129 ? 0.1102 0.3370 0.1703 -0.0284 0.0163  0.0093  146 SER C CA  
3324 C C   . SER C 129 ? 0.1339 0.3624 0.1960 -0.0245 0.0155  0.0093  146 SER C C   
3325 O O   . SER C 129 ? 0.1540 0.3834 0.2151 -0.0268 0.0145  0.0097  146 SER C O   
3326 C CB  A SER C 129 ? 0.1662 0.3797 0.2247 -0.0301 0.0157  0.0114  146 SER C CB  
3327 C CB  B SER C 129 ? 0.1655 0.3784 0.2242 -0.0295 0.0157  0.0114  146 SER C CB  
3328 O OG  A SER C 129 ? 0.1453 0.3527 0.2057 -0.0252 0.0161  0.0119  146 SER C OG  
3329 O OG  B SER C 129 ? 0.2044 0.4154 0.2606 -0.0342 0.0161  0.0116  146 SER C OG  
3330 N N   . ALA C 130 ? 0.1064 0.3347 0.1708 -0.0186 0.0160  0.0089  147 ALA C N   
3331 C CA  . ALA C 130 ? 0.1160 0.3455 0.1819 -0.0148 0.0152  0.0090  147 ALA C CA  
3332 C C   . ALA C 130 ? 0.1518 0.3942 0.2183 -0.0153 0.0152  0.0072  147 ALA C C   
3333 O O   . ALA C 130 ? 0.1522 0.3957 0.2185 -0.0161 0.0142  0.0076  147 ALA C O   
3334 C CB  . ALA C 130 ? 0.1268 0.3539 0.1947 -0.0082 0.0156  0.0088  147 ALA C CB  
3335 N N   . LYS C 131 ? 0.1464 0.3986 0.2135 -0.0151 0.0164  0.0053  148 LYS C N   
3336 C CA  . LYS C 131 ? 0.1391 0.4040 0.2068 -0.0157 0.0164  0.0035  148 LYS C CA  
3337 C C   . LYS C 131 ? 0.1039 0.3698 0.1693 -0.0220 0.0156  0.0040  148 LYS C C   
3338 O O   . LYS C 131 ? 0.1352 0.4060 0.2007 -0.0224 0.0149  0.0037  148 LYS C O   
3339 C CB  . LYS C 131 ? 0.1335 0.4084 0.2022 -0.0147 0.0179  0.0014  148 LYS C CB  
3340 C CG  . LYS C 131 ? 0.3567 0.6455 0.4266 -0.0140 0.0181  -0.0006 148 LYS C CG  
3341 C CD  . LYS C 131 ? 0.5220 0.8196 0.5930 -0.0124 0.0196  -0.0027 148 LYS C CD  
3342 C CE  . LYS C 131 ? 0.6321 0.9439 0.7047 -0.0109 0.0198  -0.0049 148 LYS C CE  
3343 N NZ  . LYS C 131 ? 0.4670 0.7842 0.5381 -0.0166 0.0192  -0.0050 148 LYS C NZ  
3344 N N   . ARG C 132 ? 0.1272 0.3878 0.1903 -0.0270 0.0157  0.0049  149 ARG C N   
3345 C CA  . ARG C 132 ? 0.1522 0.4133 0.2125 -0.0332 0.0149  0.0053  149 ARG C CA  
3346 C C   . ARG C 132 ? 0.1708 0.4244 0.2304 -0.0335 0.0135  0.0070  149 ARG C C   
3347 O O   . ARG C 132 ? 0.1509 0.4088 0.2095 -0.0361 0.0128  0.0068  149 ARG C O   
3348 C CB  . ARG C 132 ? 0.1691 0.4246 0.2267 -0.0379 0.0152  0.0060  149 ARG C CB  
3349 C CG  . ARG C 132 ? 0.1916 0.4481 0.2458 -0.0444 0.0144  0.0062  149 ARG C CG  
3350 C CD  . ARG C 132 ? 0.2208 0.4712 0.2719 -0.0490 0.0146  0.0070  149 ARG C CD  
3351 N NE  . ARG C 132 ? 0.3015 0.5381 0.3512 -0.0493 0.0135  0.0093  149 ARG C NE  
3352 C CZ  . ARG C 132 ? 0.4407 0.6712 0.4877 -0.0528 0.0122  0.0106  149 ARG C CZ  
3353 N NH1 . ARG C 132 ? 0.4336 0.6703 0.4789 -0.0565 0.0117  0.0100  149 ARG C NH1 
3354 N NH2 . ARG C 132 ? 0.3615 0.5795 0.4077 -0.0524 0.0113  0.0126  149 ARG C NH2 
3355 N N   . GLU C 133 ? 0.1427 0.3851 0.2028 -0.0310 0.0130  0.0087  150 GLU C N   
3356 C CA  . GLU C 133 ? 0.1186 0.3526 0.1778 -0.0315 0.0117  0.0104  150 GLU C CA  
3357 C C   . GLU C 133 ? 0.1154 0.3544 0.1766 -0.0280 0.0112  0.0099  150 GLU C C   
3358 O O   . GLU C 133 ? 0.1556 0.3937 0.2158 -0.0299 0.0103  0.0105  150 GLU C O   
3359 C CB  . GLU C 133 ? 0.1325 0.3534 0.1918 -0.0297 0.0114  0.0122  150 GLU C CB  
3360 C CG  . GLU C 133 ? 0.1362 0.3503 0.1929 -0.0341 0.0114  0.0132  150 GLU C CG  
3361 C CD  . GLU C 133 ? 0.1776 0.3796 0.2345 -0.0321 0.0113  0.0148  150 GLU C CD  
3362 O OE1 . GLU C 133 ? 0.1804 0.3784 0.2393 -0.0274 0.0112  0.0153  150 GLU C OE1 
3363 O OE2 . GLU C 133 ? 0.2089 0.4055 0.2637 -0.0352 0.0114  0.0155  150 GLU C OE2 
3364 N N   . ILE C 134 ? 0.1333 0.3769 0.1971 -0.0225 0.0119  0.0088  151 ILE C N   
3365 C CA  . ILE C 134 ? 0.1049 0.3539 0.1703 -0.0190 0.0114  0.0082  151 ILE C CA  
3366 C C   . ILE C 134 ? 0.1606 0.4205 0.2254 -0.0224 0.0113  0.0069  151 ILE C C   
3367 O O   . ILE C 134 ? 0.1751 0.4358 0.2396 -0.0229 0.0104  0.0073  151 ILE C O   
3368 C CB  . ILE C 134 ? 0.1256 0.3787 0.1935 -0.0127 0.0121  0.0071  151 ILE C CB  
3369 C CG1 . ILE C 134 ? 0.1417 0.3833 0.2100 -0.0090 0.0121  0.0085  151 ILE C CG1 
3370 C CG2 . ILE C 134 ? 0.1392 0.3997 0.2085 -0.0092 0.0117  0.0062  151 ILE C CG2 
3371 C CD1 . ILE C 134 ? 0.1477 0.3924 0.2178 -0.0033 0.0129  0.0074  151 ILE C CD1 
3372 N N   . SER C 135 ? 0.1418 0.4101 0.2062 -0.0248 0.0122  0.0054  152 SER C N   
3373 C CA  . SER C 135 ? 0.1732 0.4524 0.2368 -0.0282 0.0121  0.0041  152 SER C CA  
3374 C C   . SER C 135 ? 0.1494 0.4242 0.2102 -0.0340 0.0112  0.0053  152 SER C C   
3375 O O   . SER C 135 ? 0.2270 0.5083 0.2873 -0.0361 0.0107  0.0047  152 SER C O   
3376 C CB  . SER C 135 ? 0.2233 0.5118 0.2870 -0.0298 0.0133  0.0023  152 SER C CB  
3377 O OG  . SER C 135 ? 0.2981 0.5927 0.3645 -0.0243 0.0141  0.0009  152 SER C OG  
3378 N N   . LEU C 136 ? 0.1764 0.4405 0.2352 -0.0368 0.0109  0.0069  153 LEU C N   
3379 C CA  . LEU C 136 ? 0.1730 0.4317 0.2286 -0.0421 0.0100  0.0081  153 LEU C CA  
3380 C C   . LEU C 136 ? 0.1894 0.4435 0.2453 -0.0409 0.0089  0.0092  153 LEU C C   
3381 O O   . LEU C 136 ? 0.2055 0.4617 0.2597 -0.0444 0.0082  0.0092  153 LEU C O   
3382 C CB  . LEU C 136 ? 0.1726 0.4200 0.2261 -0.0445 0.0098  0.0096  153 LEU C CB  
3383 C CG  . LEU C 136 ? 0.2019 0.4428 0.2517 -0.0499 0.0088  0.0109  153 LEU C CG  
3384 C CD1 . LEU C 136 ? 0.2791 0.5294 0.3267 -0.0549 0.0090  0.0096  153 LEU C CD1 
3385 C CD2 . LEU C 136 ? 0.2200 0.4493 0.2678 -0.0515 0.0085  0.0125  153 LEU C CD2 
3386 N N   . TRP C 137 ? 0.1534 0.4007 0.2113 -0.0361 0.0086  0.0101  154 TRP C N   
3387 C CA  . TRP C 137 ? 0.1418 0.3828 0.1997 -0.0349 0.0076  0.0114  154 TRP C CA  
3388 C C   . TRP C 137 ? 0.1895 0.4380 0.2498 -0.0310 0.0075  0.0105  154 TRP C C   
3389 O O   . TRP C 137 ? 0.2006 0.4459 0.2607 -0.0308 0.0066  0.0113  154 TRP C O   
3390 C CB  . TRP C 137 ? 0.1422 0.3703 0.2005 -0.0323 0.0073  0.0132  154 TRP C CB  
3391 C CG  . TRP C 137 ? 0.1652 0.3840 0.2210 -0.0361 0.0070  0.0145  154 TRP C CG  
3392 C CD1 . TRP C 137 ? 0.1742 0.3909 0.2296 -0.0367 0.0077  0.0145  154 TRP C CD1 
3393 C CD2 . TRP C 137 ? 0.1441 0.3543 0.1974 -0.0397 0.0060  0.0161  154 TRP C CD2 
3394 N NE1 . TRP C 137 ? 0.1654 0.3728 0.2181 -0.0404 0.0071  0.0159  154 TRP C NE1 
3395 C CE2 . TRP C 137 ? 0.1508 0.3539 0.2020 -0.0423 0.0060  0.0169  154 TRP C CE2 
3396 C CE3 . TRP C 137 ? 0.2025 0.4102 0.2549 -0.0410 0.0050  0.0168  154 TRP C CE3 
3397 C CZ2 . TRP C 137 ? 0.1885 0.3822 0.2369 -0.0458 0.0050  0.0185  154 TRP C CZ2 
3398 C CZ3 . TRP C 137 ? 0.2004 0.3988 0.2500 -0.0444 0.0040  0.0183  154 TRP C CZ3 
3399 C CH2 . TRP C 137 ? 0.1871 0.3785 0.2346 -0.0467 0.0040  0.0191  154 TRP C CH2 
3400 N N   . PHE C 138 ? 0.1534 0.4112 0.2157 -0.0277 0.0083  0.0088  155 PHE C N   
3401 C CA  . PHE C 138 ? 0.1344 0.3996 0.1988 -0.0235 0.0082  0.0078  155 PHE C CA  
3402 C C   . PHE C 138 ? 0.1688 0.4484 0.2339 -0.0242 0.0088  0.0056  155 PHE C C   
3403 O O   . PHE C 138 ? 0.1828 0.4671 0.2480 -0.0249 0.0097  0.0045  155 PHE C O   
3404 C CB  . PHE C 138 ? 0.1300 0.3917 0.1965 -0.0172 0.0084  0.0079  155 PHE C CB  
3405 C CG  . PHE C 138 ? 0.1298 0.3786 0.1961 -0.0155 0.0077  0.0100  155 PHE C CG  
3406 C CD1 . PHE C 138 ? 0.1598 0.4065 0.2263 -0.0141 0.0068  0.0106  155 PHE C CD1 
3407 C CD2 . PHE C 138 ? 0.1717 0.4105 0.2375 -0.0152 0.0079  0.0111  155 PHE C CD2 
3408 C CE1 . PHE C 138 ? 0.1759 0.4108 0.2421 -0.0127 0.0062  0.0124  155 PHE C CE1 
3409 C CE2 . PHE C 138 ? 0.1461 0.3733 0.2119 -0.0137 0.0073  0.0130  155 PHE C CE2 
3410 C CZ  . PHE C 138 ? 0.1916 0.4167 0.2575 -0.0124 0.0064  0.0136  155 PHE C CZ  
3411 N N   . LYS C 139 ? 0.1820 0.4689 0.2476 -0.0238 0.0083  0.0049  156 LYS C N   
3412 C CA  . LYS C 139 ? 0.2133 0.5143 0.2803 -0.0229 0.0089  0.0027  156 LYS C CA  
3413 C C   . LYS C 139 ? 0.1480 0.4520 0.2176 -0.0161 0.0093  0.0019  156 LYS C C   
3414 O O   . LYS C 139 ? 0.1679 0.4640 0.2381 -0.0121 0.0088  0.0030  156 LYS C O   
3415 C CB  . LYS C 139 ? 0.2633 0.5709 0.3301 -0.0245 0.0082  0.0023  156 LYS C CB  
3416 C CG  . LYS C 139 ? 0.4200 0.7233 0.4840 -0.0306 0.0076  0.0034  156 LYS C CG  
3417 C CD  . LYS C 139 ? 0.5629 0.8710 0.6270 -0.0312 0.0068  0.0032  156 LYS C CD  
3418 C CE  . LYS C 139 ? 0.8070 1.1073 0.8685 -0.0358 0.0060  0.0047  156 LYS C CE  
3419 N NZ  . LYS C 139 ? 0.9631 1.2647 1.0219 -0.0420 0.0063  0.0045  156 LYS C NZ  
3420 N N   . PRO C 140 ? 0.1759 0.4911 0.2468 -0.0145 0.0100  -0.0001 157 PRO C N   
3421 C CA  . PRO C 140 ? 0.1712 0.4889 0.2444 -0.0078 0.0104  -0.0009 157 PRO C CA  
3422 C C   . PRO C 140 ? 0.1648 0.4820 0.2389 -0.0036 0.0095  -0.0006 157 PRO C C   
3423 O O   . PRO C 140 ? 0.1920 0.5051 0.2672 0.0018  0.0094  -0.0003 157 PRO C O   
3424 C CB  . PRO C 140 ? 0.2171 0.5487 0.2915 -0.0078 0.0113  -0.0032 157 PRO C CB  
3425 C CG  . PRO C 140 ? 0.2544 0.5872 0.3269 -0.0144 0.0117  -0.0033 157 PRO C CG  
3426 C CD  . PRO C 140 ? 0.2124 0.5377 0.2828 -0.0187 0.0108  -0.0016 157 PRO C CD  
3427 N N   . GLU C 141 ? 0.1689 0.4901 0.2426 -0.0061 0.0088  -0.0005 158 GLU C N   
3428 C CA  . GLU C 141 ? 0.2161 0.5375 0.2906 -0.0025 0.0079  -0.0003 158 GLU C CA  
3429 C C   . GLU C 141 ? 0.1655 0.4731 0.2393 -0.0008 0.0072  0.0018  158 GLU C C   
3430 O O   . GLU C 141 ? 0.2098 0.5159 0.2843 0.0032  0.0066  0.0022  158 GLU C O   
3431 C CB  . GLU C 141 ? 0.2403 0.5685 0.3142 -0.0065 0.0073  -0.0006 158 GLU C CB  
3432 C CG  . GLU C 141 ? 0.3848 0.7042 0.4565 -0.0119 0.0068  0.0011  158 GLU C CG  
3433 C CD  . GLU C 141 ? 0.6494 0.9762 0.7199 -0.0174 0.0066  0.0004  158 GLU C CD  
3434 O OE1 . GLU C 141 ? 0.6248 0.9611 0.6953 -0.0196 0.0073  -0.0011 158 GLU C OE1 
3435 O OE2 . GLU C 141 ? 0.8746 1.1976 0.9440 -0.0196 0.0058  0.0015  158 GLU C OE2 
3436 N N   . GLU C 142 ? 0.1612 0.4588 0.2336 -0.0038 0.0073  0.0032  159 GLU C N   
3437 C CA  . GLU C 142 ? 0.1596 0.4439 0.2314 -0.0028 0.0067  0.0053  159 GLU C CA  
3438 C C   . GLU C 142 ? 0.1576 0.4353 0.2301 0.0020  0.0071  0.0057  159 GLU C C   
3439 O O   . GLU C 142 ? 0.1762 0.4431 0.2482 0.0038  0.0066  0.0072  159 GLU C O   
3440 C CB  . GLU C 142 ? 0.1728 0.4496 0.2426 -0.0087 0.0065  0.0066  159 GLU C CB  
3441 C CG  . GLU C 142 ? 0.2480 0.5296 0.3166 -0.0132 0.0060  0.0064  159 GLU C CG  
3442 C CD  . GLU C 142 ? 0.3242 0.5986 0.3905 -0.0191 0.0057  0.0077  159 GLU C CD  
3443 O OE1 . GLU C 142 ? 0.3006 0.5743 0.3660 -0.0218 0.0063  0.0076  159 GLU C OE1 
3444 O OE2 . GLU C 142 ? 0.5368 0.8065 0.6021 -0.0211 0.0049  0.0088  159 GLU C OE2 
3445 N N   . ILE C 143 ? 0.1581 0.4419 0.2315 0.0042  0.0080  0.0042  160 ILE C N   
3446 C CA  . ILE C 143 ? 0.1474 0.4258 0.2214 0.0088  0.0084  0.0044  160 ILE C CA  
3447 C C   . ILE C 143 ? 0.1822 0.4647 0.2574 0.0149  0.0081  0.0036  160 ILE C C   
3448 O O   . ILE C 143 ? 0.1677 0.4617 0.2439 0.0163  0.0083  0.0019  160 ILE C O   
3449 C CB  . ILE C 143 ? 0.1494 0.4320 0.2237 0.0079  0.0096  0.0033  160 ILE C CB  
3450 C CG1 . ILE C 143 ? 0.1822 0.4627 0.2551 0.0013  0.0099  0.0039  160 ILE C CG1 
3451 C CG2 . ILE C 143 ? 0.1880 0.4635 0.2626 0.0122  0.0100  0.0037  160 ILE C CG2 
3452 C CD1 . ILE C 143 ? 0.2200 0.4870 0.2916 -0.0009 0.0095  0.0060  160 ILE C CD1 
3453 N N   . GLN C 144 ? 0.1344 0.4074 0.2092 0.0186  0.0076  0.0049  161 GLN C N   
3454 C CA  . GLN C 144 ? 0.1629 0.4377 0.2382 0.0241  0.0071  0.0045  161 GLN C CA  
3455 C C   . GLN C 144 ? 0.1723 0.4453 0.2479 0.0294  0.0076  0.0040  161 GLN C C   
3456 O O   . GLN C 144 ? 0.2180 0.4813 0.2929 0.0299  0.0079  0.0051  161 GLN C O   
3457 C CB  . GLN C 144 ? 0.1537 0.4191 0.2281 0.0245  0.0061  0.0063  161 GLN C CB  
3458 C CG  . GLN C 144 ? 0.1308 0.3954 0.2046 0.0189  0.0056  0.0071  161 GLN C CG  
3459 C CD  . GLN C 144 ? 0.1664 0.4434 0.2409 0.0176  0.0054  0.0057  161 GLN C CD  
3460 O OE1 . GLN C 144 ? 0.1958 0.4798 0.2712 0.0216  0.0052  0.0046  161 GLN C OE1 
3461 N NE2 . GLN C 144 ? 0.1834 0.4632 0.2574 0.0119  0.0054  0.0057  161 GLN C NE2 
3462 N N   . SER C 145 ? 0.1234 0.4056 0.1999 0.0335  0.0077  0.0024  162 SER C N   
3463 C CA  A SER C 145 ? 0.1442 0.4258 0.2208 0.0389  0.0081  0.0016  162 SER C CA  
3464 C CA  B SER C 145 ? 0.1448 0.4264 0.2214 0.0390  0.0081  0.0016  162 SER C CA  
3465 C C   . SER C 145 ? 0.1614 0.4393 0.2373 0.0442  0.0073  0.0021  162 SER C C   
3466 O O   . SER C 145 ? 0.1853 0.4704 0.2618 0.0456  0.0067  0.0014  162 SER C O   
3467 C CB  A SER C 145 ? 0.1805 0.4751 0.2585 0.0401  0.0089  -0.0007 162 SER C CB  
3468 C CB  B SER C 145 ? 0.1805 0.4751 0.2586 0.0402  0.0089  -0.0007 162 SER C CB  
3469 O OG  A SER C 145 ? 0.1868 0.4815 0.2650 0.0460  0.0092  -0.0015 162 SER C OG  
3470 O OG  B SER C 145 ? 0.1368 0.4341 0.2152 0.0356  0.0098  -0.0011 162 SER C OG  
3471 N N   . TYR C 146 ? 0.1517 0.4186 0.2264 0.0469  0.0072  0.0033  163 TYR C N   
3472 C CA  . TYR C 146 ? 0.1436 0.4061 0.2172 0.0521  0.0065  0.0037  163 TYR C CA  
3473 C C   . TYR C 146 ? 0.1445 0.3975 0.2169 0.0550  0.0069  0.0043  163 TYR C C   
3474 O O   . TYR C 146 ? 0.1554 0.4040 0.2277 0.0524  0.0076  0.0047  163 TYR C O   
3475 C CB  . TYR C 146 ? 0.1504 0.4069 0.2232 0.0507  0.0055  0.0053  163 TYR C CB  
3476 C CG  . TYR C 146 ? 0.1135 0.3584 0.1855 0.0468  0.0055  0.0072  163 TYR C CG  
3477 C CD1 . TYR C 146 ? 0.0935 0.3393 0.1660 0.0410  0.0056  0.0076  163 TYR C CD1 
3478 C CD2 . TYR C 146 ? 0.1263 0.3593 0.1967 0.0490  0.0053  0.0086  163 TYR C CD2 
3479 C CE1 . TYR C 146 ? 0.1265 0.3615 0.1982 0.0376  0.0056  0.0094  163 TYR C CE1 
3480 C CE2 . TYR C 146 ? 0.1256 0.3479 0.1952 0.0456  0.0053  0.0103  163 TYR C CE2 
3481 C CZ  . TYR C 146 ? 0.1276 0.3510 0.1980 0.0400  0.0054  0.0107  163 TYR C CZ  
3482 O OH  . TYR C 146 ? 0.1164 0.3292 0.1862 0.0368  0.0053  0.0125  163 TYR C OH  
3483 N N   . LYS C 147 ? 0.1602 0.4104 0.2314 0.0603  0.0065  0.0042  164 LYS C N   
3484 C CA  . LYS C 147 ? 0.1543 0.3960 0.2240 0.0636  0.0068  0.0047  164 LYS C CA  
3485 C C   . LYS C 147 ? 0.1414 0.3704 0.2090 0.0642  0.0061  0.0066  164 LYS C C   
3486 O O   . LYS C 147 ? 0.1468 0.3755 0.2138 0.0655  0.0052  0.0070  164 LYS C O   
3487 C CB  . LYS C 147 ? 0.1922 0.4396 0.2617 0.0694  0.0068  0.0031  164 LYS C CB  
3488 C CG  . LYS C 147 ? 0.2606 0.4987 0.3280 0.0732  0.0070  0.0035  164 LYS C CG  
3489 C CD  . LYS C 147 ? 0.4144 0.6587 0.4817 0.0789  0.0071  0.0019  164 LYS C CD  
3490 C CE  . LYS C 147 ? 0.6012 0.8351 0.6659 0.0829  0.0070  0.0025  164 LYS C CE  
3491 N NZ  . LYS C 147 ? 0.7009 0.9401 0.7653 0.0880  0.0074  0.0008  164 LYS C NZ  
3492 N N   . LEU C 148 ? 0.1722 0.3908 0.2387 0.0631  0.0064  0.0078  165 LEU C N   
3493 C CA  . LEU C 148 ? 0.1327 0.3389 0.1971 0.0638  0.0058  0.0096  165 LEU C CA  
3494 C C   . LEU C 148 ? 0.1375 0.3414 0.2000 0.0696  0.0055  0.0093  165 LEU C C   
3495 O O   . LEU C 148 ? 0.1465 0.3522 0.2086 0.0730  0.0059  0.0083  165 LEU C O   
3496 C CB  . LEU C 148 ? 0.1532 0.3495 0.2170 0.0612  0.0063  0.0109  165 LEU C CB  
3497 C CG  . LEU C 148 ? 0.1394 0.3344 0.2045 0.0552  0.0065  0.0118  165 LEU C CG  
3498 C CD1 . LEU C 148 ? 0.1955 0.3812 0.2600 0.0533  0.0071  0.0128  165 LEU C CD1 
3499 C CD2 . LEU C 148 ? 0.1590 0.3507 0.2239 0.0529  0.0057  0.0130  165 LEU C CD2 
3500 N N   . ALA C 149 ? 0.1802 0.3796 0.2413 0.0707  0.0046  0.0102  166 ALA C N   
3501 C CA  . ALA C 149 ? 0.1787 0.3757 0.2378 0.0760  0.0042  0.0100  166 ALA C CA  
3502 C C   . ALA C 149 ? 0.1736 0.3605 0.2303 0.0779  0.0045  0.0107  166 ALA C C   
3503 O O   . ALA C 149 ? 0.2270 0.4137 0.2822 0.0826  0.0044  0.0100  166 ALA C O   
3504 C CB  . ALA C 149 ? 0.2634 0.4570 0.3215 0.0761  0.0033  0.0111  166 ALA C CB  
3505 N N   . LEU C 150 ? 0.1620 0.3407 0.2185 0.0744  0.0049  0.0119  167 LEU C N   
3506 C CA  . LEU C 150 ? 0.1421 0.3112 0.1965 0.0757  0.0053  0.0125  167 LEU C CA  
3507 C C   . LEU C 150 ? 0.1340 0.3069 0.1893 0.0762  0.0062  0.0113  167 LEU C C   
3508 O O   . LEU C 150 ? 0.1692 0.3343 0.2230 0.0765  0.0066  0.0119  167 LEU C O   
3509 C CB  . LEU C 150 ? 0.1706 0.3286 0.2242 0.0717  0.0053  0.0144  167 LEU C CB  
3510 C CG  . LEU C 150 ? 0.1735 0.3243 0.2252 0.0722  0.0045  0.0157  167 LEU C CG  
3511 C CD1 . LEU C 150 ? 0.2637 0.4057 0.3154 0.0676  0.0045  0.0174  167 LEU C CD1 
3512 C CD2 . LEU C 150 ? 0.2500 0.3946 0.2986 0.0764  0.0045  0.0157  167 LEU C CD2 
3513 N N   . SER C 151 ? 0.1486 0.3335 0.2062 0.0763  0.0066  0.0097  168 SER C N   
3514 C CA  A SER C 151 ? 0.1625 0.3518 0.2213 0.0763  0.0075  0.0085  168 SER C CA  
3515 C CA  B SER C 151 ? 0.1624 0.3516 0.2212 0.0763  0.0075  0.0085  168 SER C CA  
3516 C C   . SER C 151 ? 0.1658 0.3501 0.2223 0.0806  0.0078  0.0081  168 SER C C   
3517 O O   . SER C 151 ? 0.1939 0.3751 0.2504 0.0798  0.0085  0.0081  168 SER C O   
3518 C CB  A SER C 151 ? 0.1942 0.3978 0.2554 0.0768  0.0078  0.0066  168 SER C CB  
3519 C CB  B SER C 151 ? 0.1940 0.3975 0.2553 0.0767  0.0078  0.0066  168 SER C CB  
3520 O OG  A SER C 151 ? 0.2855 0.4941 0.3477 0.0775  0.0088  0.0052  168 SER C OG  
3521 O OG  B SER C 151 ? 0.1771 0.3849 0.2405 0.0717  0.0078  0.0069  168 SER C OG  
3522 N N   . ASP C 152 ? 0.1874 0.3711 0.2421 0.0853  0.0072  0.0078  169 ASP C N   
3523 C CA  . ASP C 152 ? 0.2251 0.4042 0.2774 0.0894  0.0074  0.0073  169 ASP C CA  
3524 C C   . ASP C 152 ? 0.2387 0.4046 0.2887 0.0879  0.0075  0.0090  169 ASP C C   
3525 O O   . ASP C 152 ? 0.2377 0.3996 0.2860 0.0902  0.0079  0.0086  169 ASP C O   
3526 C CB  . ASP C 152 ? 0.2773 0.4571 0.3277 0.0945  0.0066  0.0069  169 ASP C CB  
3527 C CG  . ASP C 152 ? 0.4348 0.6279 0.4871 0.0973  0.0066  0.0049  169 ASP C CG  
3528 O OD1 . ASP C 152 ? 0.3933 0.5952 0.4482 0.0960  0.0073  0.0036  169 ASP C OD1 
3529 O OD2 . ASP C 152 ? 0.4125 0.6073 0.4638 0.1006  0.0058  0.0047  169 ASP C OD2 
3530 N N   . TYR C 153 ? 0.1506 0.3096 0.2004 0.0841  0.0072  0.0107  170 TYR C N   
3531 C CA  . TYR C 153 ? 0.1246 0.2712 0.1723 0.0825  0.0072  0.0123  170 TYR C CA  
3532 C C   . TYR C 153 ? 0.1363 0.2807 0.1856 0.0776  0.0078  0.0130  170 TYR C C   
3533 O O   . TYR C 153 ? 0.2040 0.3385 0.2518 0.0757  0.0079  0.0143  170 TYR C O   
3534 C CB  . TYR C 153 ? 0.1669 0.3062 0.2127 0.0820  0.0064  0.0137  170 TYR C CB  
3535 C CG  . TYR C 153 ? 0.1762 0.3163 0.2198 0.0870  0.0059  0.0131  170 TYR C CG  
3536 C CD1 . TYR C 153 ? 0.1918 0.3251 0.2324 0.0900  0.0060  0.0131  170 TYR C CD1 
3537 C CD2 . TYR C 153 ? 0.1735 0.3216 0.2181 0.0889  0.0053  0.0123  170 TYR C CD2 
3538 C CE1 . TYR C 153 ? 0.1857 0.3198 0.2242 0.0948  0.0055  0.0124  170 TYR C CE1 
3539 C CE2 . TYR C 153 ? 0.2067 0.3558 0.2494 0.0938  0.0048  0.0117  170 TYR C CE2 
3540 C CZ  . TYR C 153 ? 0.2256 0.3675 0.2652 0.0966  0.0049  0.0118  170 TYR C CZ  
3541 O OH  . TYR C 153 ? 0.2757 0.4183 0.3132 0.1014  0.0044  0.0111  170 TYR C OH  
3542 N N   . ILE C 154 ? 0.1518 0.3056 0.2043 0.0753  0.0082  0.0121  171 ILE C N   
3543 C CA  . ILE C 154 ? 0.1573 0.3103 0.2116 0.0706  0.0088  0.0126  171 ILE C CA  
3544 C C   . ILE C 154 ? 0.2173 0.3754 0.2726 0.0714  0.0098  0.0112  171 ILE C C   
3545 O O   . ILE C 154 ? 0.2145 0.3674 0.2697 0.0692  0.0104  0.0117  171 ILE C O   
3546 C CB  . ILE C 154 ? 0.1724 0.3319 0.2292 0.0667  0.0086  0.0127  171 ILE C CB  
3547 C CG1 . ILE C 154 ? 0.1578 0.3112 0.2137 0.0654  0.0076  0.0143  171 ILE C CG1 
3548 C CG2 . ILE C 154 ? 0.1803 0.3404 0.2391 0.0619  0.0092  0.0130  171 ILE C CG2 
3549 C CD1 . ILE C 154 ? 0.2085 0.3698 0.2666 0.0629  0.0073  0.0141  171 ILE C CD1 
3550 N N   . PHE C 155 ? 0.1891 0.3574 0.2453 0.0745  0.0101  0.0093  172 PHE C N   
3551 C CA  . PHE C 155 ? 0.2072 0.3820 0.2648 0.0752  0.0111  0.0077  172 PHE C CA  
3552 C C   . PHE C 155 ? 0.2879 0.4605 0.3432 0.0805  0.0113  0.0069  172 PHE C C   
3553 O O   . PHE C 155 ? 0.2602 0.4319 0.3137 0.0844  0.0105  0.0068  172 PHE C O   
3554 C CB  . PHE C 155 ? 0.1942 0.3829 0.2546 0.0745  0.0114  0.0061  172 PHE C CB  
3555 C CG  . PHE C 155 ? 0.2446 0.4358 0.3069 0.0693  0.0112  0.0069  172 PHE C CG  
3556 C CD1 . PHE C 155 ? 0.1965 0.3854 0.2599 0.0645  0.0118  0.0076  172 PHE C CD1 
3557 C CD2 . PHE C 155 ? 0.2091 0.4046 0.2718 0.0693  0.0103  0.0070  172 PHE C CD2 
3558 C CE1 . PHE C 155 ? 0.2049 0.3957 0.2697 0.0597  0.0115  0.0083  172 PHE C CE1 
3559 C CE2 . PHE C 155 ? 0.2656 0.4631 0.3299 0.0645  0.0101  0.0077  172 PHE C CE2 
3560 C CZ  . PHE C 155 ? 0.2190 0.4140 0.2842 0.0597  0.0107  0.0084  172 PHE C CZ  
3561 N N   . GLU C 156 ? 0.2777 0.4493 0.3330 0.0807  0.0122  0.0062  173 GLU C N   
3562 C CA  . GLU C 156 ? 0.4242 0.5933 0.4772 0.0857  0.0124  0.0054  173 GLU C CA  
3563 C C   . GLU C 156 ? 0.5620 0.7437 0.6166 0.0890  0.0128  0.0031  173 GLU C C   
3564 O O   . GLU C 156 ? 0.6143 0.7966 0.6672 0.0940  0.0125  0.0022  173 GLU C O   
3565 C CB  . GLU C 156 ? 0.4372 0.6005 0.4895 0.0847  0.0134  0.0055  173 GLU C CB  
3566 C CG  . GLU C 156 ? 0.3989 0.5700 0.4541 0.0820  0.0147  0.0043  173 GLU C CG  
3567 C CD  . GLU C 156 ? 0.5062 0.6701 0.5607 0.0801  0.0156  0.0048  173 GLU C CD  
3568 O OE1 . GLU C 156 ? 0.2535 0.4059 0.3056 0.0798  0.0150  0.0064  173 GLU C OE1 
3569 O OE2 . GLU C 156 ? 0.5749 0.7452 0.6314 0.0787  0.0169  0.0035  173 GLU C OE2 
3570 O OXT . GLU C 156 ? 0.4920 0.6838 0.5496 0.0867  0.0133  0.0022  173 GLU C OXT 
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